ID A0A010Q330_9MICC Unreviewed; 541 AA. AC A0A010Q330; DT 11-JUN-2014, integrated into UniProtKB/TrEMBL. DT 11-JUN-2014, sequence version 1. DT 07-JUN-2017, entry version 21. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=BG28_14470 {ECO:0000313|EMBL:EXF25248.1}; OS Nesterenkonia sp. AN1. OC Bacteria; Actinobacteria; Micrococcales; Micrococcaceae; OC Nesterenkonia. OX NCBI_TaxID=652017 {ECO:0000313|EMBL:EXF25248.1, ECO:0000313|Proteomes:UP000022206}; RN [1] {ECO:0000313|EMBL:EXF25248.1, ECO:0000313|Proteomes:UP000022206} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=AN1 {ECO:0000313|EMBL:EXF25248.1, RC ECO:0000313|Proteomes:UP000022206}; RX PubMed=24675854; RA Aliyu H., De Maayer P., Rees J., Tuffin M., Cowan D.A.; RT "Draft Genome Sequence of the Antarctic Polyextremophile Nesterenkonia RT sp. Strain AN1."; RL Genome Announc. 2:e00197-14(2014). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EXF25248.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JEMO01000009; EXF25248.1; -; Genomic_DNA. DR RefSeq; WP_036475041.1; NZ_JEMO01000009.1. DR EnsemblBacteria; EXF25248; EXF25248; BG28_14470. DR PATRIC; fig|652017.6.peg.1370; -. DR Proteomes; UP000022206; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 2. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000022206}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000022206}. FT DOMAIN 316 481 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 541 AA; 59093 MW; 4A234B1119A97DBB CRC64; MTKQKHTPAP SGETPEDATT PTAEQSSVDA TIERILAADR AREDAPKRTT RFEADSSFKR RGILGEQARE IAGETAHSES DGEQFELMER RSLRRVDGLS TELEDVSEVE YRQLRLERVV LAGLWGEGTV AEAEYSLREL SALAETAGST VLDGFLQRRA KPDPGTFFGS GKAEEIRVAV ADLGADTVVV DSELAPSQRR GLEDIVKVKV IDRTGLILDI FAQHAKSREG KAQVELAQME YMLPRLRGWG ESLSRQAGGQ VGGASAGIGS RGPGETKIEL DRRRINARMA KLRKDIAAMK PARDAKRANR KRNAVPSVAI AGYTNAGKSS LLNRLTDAGV LVENALFATL DPTTRKAVTP DGIGYTLSDT VGFVRQLPTQ LIEAFRSTLE EVADADLILH VVDASHPEPE SQISAVRTVL AEVDAHEVDE VIVLNKADVA DWDVVERIRR REPHTIVVSA HSGEGIEELR ELISSSIPRP SVPLELMVPY AQGDIVSRLH AEDAEILSTE YQEEGTLLKV LVRRELVGDL AEFQVKAEPT P // ID A0A010S347_PSEFL Unreviewed; 433 AA. AC A0A010S347; DT 11-JUN-2014, integrated into UniProtKB/TrEMBL. DT 11-JUN-2014, sequence version 1. DT 30-AUG-2017, entry version 25. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=HK44_026365 {ECO:0000313|EMBL:EXF95169.1}; OS Pseudomonas fluorescens HK44. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=1042209 {ECO:0000313|EMBL:EXF95169.1, ECO:0000313|Proteomes:UP000022611}; RN [1] {ECO:0000313|EMBL:EXF95169.1, ECO:0000313|Proteomes:UP000022611} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=HK44 {ECO:0000313|EMBL:EXF95169.1, RC ECO:0000313|Proteomes:UP000022611}; RX PubMed=21742869; DOI=10.1128/JB.05530-11; RA Chauhan A., Layton A.C., Williams D.E., Smartt A.E., Ripp S., RA Karpinets T.V., Brown S.D., Sayler G.S.; RT "Draft genome sequence of the polycyclic aromatic hydrocarbon- RT degrading, genetically engineered bioluminescent bioreporter RT Pseudomonas fluorescens HK44."; RL J. Bacteriol. 193:5009-5010(2011). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EXF95169.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFOY02000008; EXF95169.1; -; Genomic_DNA. DR RefSeq; WP_019691506.1; NZ_AFOY02000008.1. DR EnsemblBacteria; EXF95169; EXF95169; HK44_026365. DR PATRIC; fig|1042209.11.peg.1837; -. DR Proteomes; UP000022611; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000022611}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000022611}. FT DOMAIN 199 366 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 433 AA; 48970 MW; 3D61785DB7CC09D9 CRC64; MFFERHGGGE RTILVHLDGQ DPEAREDPQE FQELAISAGA ETVAFVNVPR HRPTAKYLIG SGKVEELRDQ VKAEKVDLVI FNSVLTPSQE RNLERVFECR VIDRTGLILD IFAQRARTHE GKLQVELAQL EYMSTRLVRG WTHLERQKGG IGLRGPGETQ LETDRRLLRV RLRQIKGRLE KVRSQRDQAR RGRKRADIPS VSLVGYTNAG KSTLFNSVTD SDVFAANQLF ATLDPTLRRL ELADLGPIVL ADTVGFIRHL PHKLVEAFRA TLEESSNSDL LLHVIDAHEP ERMAQIEQVM VVLGEIGAQD LPILEVYNKL DLLEGVEPQI QRDADGKPQR VWLSARDGQG LDLLKQAIAE LLGNDLFVGT LRLPQRFARL RAQFFALGAV QKEEHDEEGI CLLAVRLPRV ELNRLVSREG MQPLEFIEQH TLQ // ID A0A011MBV7_9PROT Unreviewed; 392 AA. AC A0A011MBV7; DT 11-JUN-2014, integrated into UniProtKB/TrEMBL. DT 11-JUN-2014, sequence version 1. DT 07-JUN-2017, entry version 18. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:EXI67223.1}; GN ORFNames=AW07_04549 {ECO:0000313|EMBL:EXI67223.1}; OS Candidatus Accumulibacter sp. SK-11. OC Bacteria; Proteobacteria; Betaproteobacteria; OC Candidatus Accumulibacter. OX NCBI_TaxID=1454000 {ECO:0000313|EMBL:EXI67223.1, ECO:0000313|Proteomes:UP000020226}; RN [1] {ECO:0000313|EMBL:EXI67223.1, ECO:0000313|Proteomes:UP000020226} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SK-11 {ECO:0000313|Proteomes:UP000020226}; RA Skennerton C.T., Barr J.J., Slater F.R., Bond P.L., Tyson G.W.; RT "Expanding our view of genomic diversity in Candidatus Accumulibacter RT clades."; RL Submitted (FEB-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EXI67223.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JFAW01000057; EXI67223.1; -; Genomic_DNA. DR PATRIC; fig|1454000.3.peg.3676; -. DR Proteomes; UP000020226; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000020226}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000020226}. FT DOMAIN 200 366 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 392 AA; 42269 MW; AE7C6C928F6C0416 CRC64; MAGAEPHAAC ERAVIVQLDF GGDDLAEQIE EVRLLTRSAG AEVCAVVQGR RHSPDAATYA GKGKVEEIAA ELAAHDADLV IFNHELSAGQ ERNLERVLQC RVIDRTSLIL DIFAQRAKSS EGKLQVELAQ LEHLATRLVR GWTHLERQKG GIGLRGPGET QLETDRRLLG IRVRTLKGRL ARLERQRGVQ RKARARGEQL SVSLVGYTNA GKSTLFNALT HAGVYAADQL FATLDTTTRK LWLPEAGHIV LSDTVGFIRK LPHSLVAAFH ATLEATAEAD LLLHVVDSAS PARDDQVADV NQVLAEIGAS GVPQLLVLNK LDLTGLPPAV ERDEYDRISR VRVSAIGGQG LPLLRGALAE IALLKTGGTR RGSSSAAVLQ DVDWHLDSDG SP // ID A0A011NPI6_9PROT Unreviewed; 392 AA. AC A0A011NPI6; DT 11-JUN-2014, integrated into UniProtKB/TrEMBL. DT 11-JUN-2014, sequence version 1. DT 07-JUN-2017, entry version 21. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:EXI66507.1}; GN ORFNames=AW08_02621 {ECO:0000313|EMBL:EXI66507.1}; OS Candidatus Accumulibacter sp. SK-12. OC Bacteria; Proteobacteria; Betaproteobacteria; OC Candidatus Accumulibacter. OX NCBI_TaxID=1454001 {ECO:0000313|EMBL:EXI66507.1, ECO:0000313|Proteomes:UP000020218}; RN [1] {ECO:0000313|EMBL:EXI66507.1, ECO:0000313|Proteomes:UP000020218} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SK-12 {ECO:0000313|Proteomes:UP000020218}; RA Skennerton C.T., Barr J.J., Slater F.R., Bond P.L., Tyson G.W.; RT "Expanding our view of genomic diversity in Candidatus Accumulibacter RT clades."; RL Submitted (FEB-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EXI66507.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JFAX01000015; EXI66507.1; -; Genomic_DNA. DR PATRIC; fig|1454001.3.peg.2667; -. DR Proteomes; UP000020218; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000020218}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000020218}. FT DOMAIN 200 366 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 392 AA; 42325 MW; F5212D3B42F0944F CRC64; MAAAERRAGV ERAIIVQLDF GGDDLAEQIE EVCLLARSAG AEVCAVVQGR RHAPDAATYA GKGKVEEIAA ELAAHAAELV IFNHELSAAQ ERNLERALQC RVIDRTSLIL DIFAQRAKSS EGKLQVELAQ LEHLATRLVR GWTHLERQTG GIGLRGPGET QLETDRRLLG IRVRTLKGRL ARLERQRGVQ RKARARGELL SVSLVGYTNA GKSTLFNALT HAGVYAADQL FATLDTTTRK LWLPQAGHIV LSDTVGFIRK LPHSLVAAFH ATLEATAEAD LLLHVVDSAS PARDDQVADV NQVLVEIGAS RVPQLMVLNK LDLTGLPPSV ERDEYGRIRR VRVSAIGGQG LPLLRAALAE IALLKTGGTS RDASGAAVLQ AVDRHLDSDR SP // ID A0A011Q566_9PROT Unreviewed; 396 AA. AC A0A011Q566; DT 11-JUN-2014, integrated into UniProtKB/TrEMBL. DT 11-JUN-2014, sequence version 1. DT 07-JUN-2017, entry version 18. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:EXI84432.1}; GN ORFNames=AW12_02453 {ECO:0000313|EMBL:EXI84432.1}; OS Candidatus Accumulibacter sp. BA-94. OC Bacteria; Proteobacteria; Betaproteobacteria; OC Candidatus Accumulibacter. OX NCBI_TaxID=1454005 {ECO:0000313|EMBL:EXI84432.1, ECO:0000313|Proteomes:UP000020878}; RN [1] {ECO:0000313|EMBL:EXI84432.1, ECO:0000313|Proteomes:UP000020878} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BA-94 {ECO:0000313|Proteomes:UP000020878}; RA Skennerton C.T., Barr J.J., Slater F.R., Bond P.L., Tyson G.W.; RT "Expanding our view of genomic diversity in Candidatus Accumulibacter RT clades."; RL Submitted (FEB-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EXI84432.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JEMZ01000145; EXI84432.1; -; Genomic_DNA. DR PATRIC; fig|1454005.3.peg.2397; -. DR Proteomes; UP000020878; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000020878}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000020878}. FT DOMAIN 204 370 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 396 AA; 42512 MW; BB80ED703FBECB1B CRC64; MPGMMAGTER HAPAERAVIV QLDFGSDDLA EQIDEIRLLA RSAGAEVCTV VQGRRHAPDA ATYAGKGKVE EIAAELAAHA AELVIFNHEL SAGQERNLER ALQCRVIDRT SLILDIFAQR AKSSEGKLQV ELAQLEHLAT RLVRGWTHLE RQTGGIGLRG PGETQLETDR RLLGIRVRTL KGRLARVERQ RGVQRKARAR GEVLSVSLVG YTNAGKSTLF NALTHAGVFA ADQLFATLDT TTRKLWLPEA GHIVVSDTVG FIRKLPHSLV AAFHATLEAT AEADLLLHVV DSASPARDDQ VADVNQVLAE IGADGVPQLV VLNKLDLTGL PPAVERDEYG KISRVRVSAI GGQGLPLLRA ALAEIALLKT GGTRRGHSGA AVLQAVDRHL DSDGSP // ID A0A011QJM9_9PROT Unreviewed; 390 AA. AC A0A011QJM9; DT 11-JUN-2014, integrated into UniProtKB/TrEMBL. DT 11-JUN-2014, sequence version 1. DT 07-JUN-2017, entry version 20. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:EXI89250.1}; GN ORFNames=AW11_01573 {ECO:0000313|EMBL:EXI89250.1}; OS Candidatus Accumulibacter sp. BA-93. OC Bacteria; Proteobacteria; Betaproteobacteria; OC Candidatus Accumulibacter. OX NCBI_TaxID=1454004 {ECO:0000313|EMBL:EXI89250.1, ECO:0000313|Proteomes:UP000022141}; RN [1] {ECO:0000313|EMBL:EXI89250.1, ECO:0000313|Proteomes:UP000022141} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BA-93 {ECO:0000313|Proteomes:UP000022141}; RA Skennerton C.T., Barr J.J., Slater F.R., Bond P.L., Tyson G.W.; RT "Expanding our view of genomic diversity in Candidatus Accumulibacter RT clades."; RL Submitted (FEB-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EXI89250.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JEMY01000017; EXI89250.1; -; Genomic_DNA. DR PATRIC; fig|1454004.3.peg.1622; -. DR Proteomes; UP000022141; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000022141}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000022141}. FT DOMAIN 198 364 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 164 191 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 390 AA; 42428 MW; 99FF5C947072D483 CRC64; MHERPSVEER AVIVQLDFGH DDLAEQLEEV RLLALSAGAS ICAVVHGRRH SPDAATYAGK GKVGEVAAEV LAHEADLVIF NHELSAGQER NLEQALQCRV IDRTSLILDI FAQRAKSAEG KLQVELAQLE HLSTRLVRGW THLERQKGGI GLRGPGETQL ETDRRLLGIR VKSLKERLVK LERQRGVQRK ARGRGELLNV SLVGYTNAGK STLFNALTHA GVLAADRLFA TLDTTTRKLW LAEAGHIVLS DTVGFIRDLP HSLVAAFHAT LEATAEADLL LHVVDSASPA RDEQVGDVNK VLAEIGAAGV PQLMVLNKLD LTGLPPTVER DEYGTLLRVR VSARRGDGLS LLREALAEVA LAKNRNLRQQ SSGEADLQDI DMVFDSDGSA // ID A0A011SEP2_9LACT Unreviewed; 411 AA. AC A0A011SEP2; DT 11-JUN-2014, integrated into UniProtKB/TrEMBL. DT 11-JUN-2014, sequence version 1. DT 07-JUN-2017, entry version 20. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=ADIAL_1943 {ECO:0000313|EMBL:EXJ22357.1}; OS Alkalibacterium sp. AK22. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Carnobacteriaceae; OC Alkalibacterium. OX NCBI_TaxID=1229520 {ECO:0000313|EMBL:EXJ22357.1, ECO:0000313|Proteomes:UP000020164}; RN [1] {ECO:0000313|EMBL:EXJ22357.1, ECO:0000313|Proteomes:UP000020164} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=AK22 {ECO:0000313|Proteomes:UP000020164}; RA Singh A., Pinnaka A.K.; RL Submitted (JAN-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EXJ22357.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JANL01000042; EXJ22357.1; -; Genomic_DNA. DR RefSeq; WP_034302947.1; NZ_JANL01000042.1. DR EnsemblBacteria; EXJ22357; EXJ22357; ADIAL_1943. DR PATRIC; fig|1229520.3.peg.1885; -. DR Proteomes; UP000020164; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000020164}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000020164}. FT DOMAIN 199 360 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 411 AA; 47276 MW; D3DAE9C0C158BD78 CRC64; MEEKKTYERV IIVGIEKQNE ADAFRYSFDE LEQLVENAGG RVVARLSQKR EKIDHKTVIG KGKITELKNL AEELDAQTIV FNQELSPSHV RNIQEMVDTK VIDRIQVILD IFALRAQSKE GRLQVQLAQL SYILPRLAGQ GENMSRLGAG IGTRGPGETK LETDRRHIQR QMTDIKRELD KIAAHRQRSR QQRKDSNVFQ IGLIGYTNAG KSTLLNQLTE AETYEKDQLF ATLDPLTRQC ELPSGMQVTL TDTVGFIQEL PTQLIEAFKS TLEESKYVDM LLHVVDASSE NIKAHEETVM TLLDELGMRH IPILTIYNKR DLIDQPVRST LYPNYTISAR DPKDIDHLRE AIEKEMKKQM THYQLSIPSD RGDWLIDLRQ HTLLERQLFD EDEQAYCVEG YAKKGSRWVQ N // ID A0A011SXU7_9RHIZ Unreviewed; 467 AA. AC A0A011SXU7; DT 11-JUN-2014, integrated into UniProtKB/TrEMBL. DT 11-JUN-2014, sequence version 1. DT 07-JUN-2017, entry version 22. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=BG36_10435 {ECO:0000313|EMBL:EXL04059.1}; OS Aquamicrobium defluvii. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Phyllobacteriaceae; Aquamicrobium. OX NCBI_TaxID=69279 {ECO:0000313|EMBL:EXL04059.1, ECO:0000313|Proteomes:UP000019849}; RN [1] {ECO:0000313|EMBL:EXL04059.1, ECO:0000313|Proteomes:UP000019849} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=W13Z1 {ECO:0000313|EMBL:EXL04059.1, RC ECO:0000313|Proteomes:UP000019849}; RA Wang X.; RT "Aquamicrobium defluvii Genome sequencing."; RL Submitted (FEB-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EXL04059.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JENY01000022; EXL04059.1; -; Genomic_DNA. DR RefSeq; WP_035028642.1; NZ_KK073894.1. DR EnsemblBacteria; EXL04059; EXL04059; BG36_10435. DR PATRIC; fig|69279.3.peg.3179; -. DR Proteomes; UP000019849; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000019849}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000019849}. FT DOMAIN 230 403 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 189 223 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 467 AA; 51088 MW; 124026641E96CDFA CRC64; MARNRDATDE SGTQPARGAG EANTVRTRAV VVVPVLTRPL AADDTARPRL TRSPQARHEE AVGLARAIDL DPVHSLVVSV NDPRPGTLLG SGKVAEIAGL VKDSEAELVI VDHPLTPVQQ RNLEKEMNVK VLDRTGLILE IFGERARTKE GTLQVELAHL NYQKGRLVRS WTHLERQRGG AGFLGGPGET QIEADRRILQ DKIVKLKREL ETVRRTRDLH RAKRKKVPFP VVAIVGYTNA GKSTLFNRLT GAGVLAEDML FATLDPTLRR VRLPHGTPVI LSDTVGFISD LPTHLVAAFR ATLEEVVEAD LVLHLRDISD PDTAAQAEDV ERILRDLGVD ASDDRRVVEV WNKIDLLDGA NRERLLGEAR HDRRHGPVAI SAISGEGLDR LLAAIEEHVS GELAEMAVTL APGQLGHADW LYRNGDVISR TDNEDGSLTL VLRATESARE EIRNRLGGGS AKDAPRA // ID A0A014M869_9GAMM Unreviewed; 426 AA. AC A0A014M869; DT 11-JUN-2014, integrated into UniProtKB/TrEMBL. DT 11-JUN-2014, sequence version 1. DT 30-AUG-2017, entry version 22. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=BG55_18100 {ECO:0000313|EMBL:EXU74299.1}; OS Erwinia mallotivora. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; OC Erwiniaceae; Erwinia. OX NCBI_TaxID=69222 {ECO:0000313|EMBL:EXU74299.1, ECO:0000313|Proteomes:UP000019918}; RN [1] {ECO:0000313|EMBL:EXU74299.1, ECO:0000313|Proteomes:UP000019918} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BT-MARDI {ECO:0000313|EMBL:EXU74299.1, RC ECO:0000313|Proteomes:UP000019918}; RA Redzuan R., Abu Bakar N., Badrun R., Mohd Raih M.F., Rozano L., RA Mat Amin N.; RT "Draft genome of Erwinia mallotivora strain BT-MARDI, a papaya dieback RT pathogen."; RL Submitted (FEB-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EXU74299.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JFHN01000063; EXU74299.1; -; Genomic_DNA. DR RefSeq; WP_034939917.1; NZ_JFHN01000063.1. DR EnsemblBacteria; EXU74299; EXU74299; BG55_18100. DR PATRIC; fig|69222.5.peg.3690; -. DR Proteomes; UP000019918; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000019918}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000019918}. FT DOMAIN 198 365 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 426 AA; 47802 MW; 465DAFC80D83B88A CRC64; MFDRYDAGEQ AVLVHIYFSQ DKDMEDLQEF ETLVSSAGVD ALRVVTGSRK APHPKYFVGE GKAVEIAEAV KSSGASVVLF DHALSPAQER NLEALCECRV IDRTGLILDI FAQRARTHEG KLQVELAQLR HLATRLVRGW THLERQKGGI GLRGPGETQL ETDRRLLRNR ITLILSRLER VEKQRDQGRQ ARNKADVPTI SLVGYTNAGK STLFNCLTSA EVYAADQLFA TLDPTLRRID VADVGEVVLA DTVGFIRHLP HDLVAAFKAT LQETRQATLL LHVIDAADLR IDENIAAVED VLTEIESDEI PTLQIMNKID MLENFVPRID RNEENLPVRV WLSAQTGEGV PLLFQALTER LAGEIAEYAL RLPPEAGRLR SRFYQLQAIE KEWNEDDGSV GLAVRMPVVD WRRLCKQEPG LVNYIV // ID A0A014MB34_9BURK Unreviewed; 403 AA. AC A0A014MB34; DT 11-JUN-2014, integrated into UniProtKB/TrEMBL. DT 11-JUN-2014, sequence version 1. DT 07-JUN-2017, entry version 20. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=AX13_08685 {ECO:0000313|EMBL:EXU78996.1}; OS Comamonas aquatica DA1877. OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Comamonadaceae; Comamonas. OX NCBI_TaxID=1457173 {ECO:0000313|EMBL:EXU78996.1, ECO:0000313|Proteomes:UP000020766}; RN [1] {ECO:0000313|EMBL:EXU78996.1, ECO:0000313|Proteomes:UP000020766} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DA1877 {ECO:0000313|EMBL:EXU78996.1, RC ECO:0000313|Proteomes:UP000020766}; RA Watson E., Macneil L.T., Ritter A.D., Yilmaz L.S., Rosebrock A.P., RA Caudy A.A., Walhout A.J.; RT "Interspecies Systems Biology Uncovers Metabolites Affecting C. RT elegans Gene Expression and Life History Traits."; RL Submitted (JAN-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EXU78996.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JBOK01000022; EXU78996.1; -; Genomic_DNA. DR EnsemblBacteria; EXU78996; EXU78996; AX13_08685. DR PATRIC; fig|1457173.3.peg.3155; -. DR Proteomes; UP000020766; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000020766}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000020766}. FT DOMAIN 203 376 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 403 AA; 44598 MW; 4750999D35A44D17 CRC64; MSVNAASSPE DATPVVLVGV DFGLPHFDTE LEELGLLAQT AGLRPVARIT CKRKAPDAAL FVGSGKADEI RMLAQMHGAR EVLFDQALSP AQQRNLERHL EMPVNDRTLL ILEIFAQRAR SHEGKLQVEL ARLQYVATRL VRRWTHLERQ MGGIGGRGGP GEKQIELDRR MIADAIKRTK DKLQKVKKQR ATQRRQRERR DVFNISLVGY TNAGKSTLFN ALVKARAYAA DQLFATLDTT TRQLYLSEAG MSVSLSDTVG FIRDLPHGLV EAFQATLQEA VDADLLLHVV DASNETFPEQ MDQVRRVLGE IGALDIPQVL VFNKLDALPP ERMPAITQDT YEVDGVAVPR VFVSARTGEG LVQLRQLLAQ AALAARNASD EGEVQDGRDG QRSEPMSLDD YDD // ID A0A015L0C2_9BACL Unreviewed; 430 AA. AC A0A015L0C2; DT 11-JUN-2014, integrated into UniProtKB/TrEMBL. DT 11-JUN-2014, sequence version 1. DT 07-JUN-2017, entry version 22. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=BG52_14700 {ECO:0000313|EMBL:EXX89826.1}; OS Paenibacillus darwinianus. OC Bacteria; Firmicutes; Bacilli; Bacillales; Paenibacillaceae; OC Paenibacillus. OX NCBI_TaxID=1380763 {ECO:0000313|EMBL:EXX89826.1, ECO:0000313|Proteomes:UP000052954}; RN [1] {ECO:0000313|EMBL:EXX89826.1, ECO:0000313|Proteomes:UP000052954} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Br {ECO:0000313|EMBL:EXX89826.1, RC ECO:0000313|Proteomes:UP000052954}; RA Dsouza M., Taylor M.W., Turner S.J., Aislabie J.; RT "Genome sequence of Paenibacillus darwinianus reveals adaptive RT mechanisms for survival in Antarctic soils."; RL Submitted (FEB-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EXX89826.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JFHT01000080; EXX89826.1; -; Genomic_DNA. DR RefSeq; WP_036579646.1; NZ_KK082335.1. DR EnsemblBacteria; EXX89826; EXX89826; BG52_14700. DR Proteomes; UP000052954; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000052954}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000052954}. FT DOMAIN 208 372 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 167 201 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 430 AA; 47418 MW; E6726C76AB469F8B CRC64; MATSTYDTNN DVQDRAVLVS LVTDDVKRGS ADPEHSLAEL VSLAETAGVR VLTTITQNRE TPDSKWFIGK GKVEELRAAA SELGATTAIF DQELSGAQVR NLEEALDLKI IDRTQLILDI FAGRAKTREG IIQVELAQLS YLLPRLSGHG KNLSRLGGGI GTRGPGESKL ETDRRHIRNR IAELKRQLDE VVRHRKLHRE RRKKSGVIQV ALVGYTNAGK STLLRELTEA DVYVENQLFA TLDPTSRNWQ LPNGKEIVLT DTVGFIQNLP HDLVAAFRAT LEEVNEADLI LHVVDSSSPM RSEQMAVVAD ILTQLGAGDK QQLTVFNKKD LCTEESSHLL AGGKDALFVS AYSEPDLQQI REAVQQRLTG DTLTFGIPAD RGDLIALAYR SGEVLGQDVG DDDGLVSLTV RLNKQEYELN GHKLQPYIRL // ID A0A016RVE2_9BILA Unreviewed; 485 AA. AC A0A016RVE2; DT 11-JUN-2014, integrated into UniProtKB/TrEMBL. DT 11-JUN-2014, sequence version 1. DT 10-MAY-2017, entry version 9. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EYB82032.1}; GN Name=Acey_s0368.g56 {ECO:0000313|EMBL:EYB82032.1}; GN ORFNames=Y032_0368g56 {ECO:0000313|EMBL:EYB82032.1}; OS Ancylostoma ceylanicum. OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida; OC Strongylida; Ancylostomatoidea; Ancylostomatidae; Ancylostomatinae; OC Ancylostoma. OX NCBI_TaxID=53326 {ECO:0000313|EMBL:EYB82032.1, ECO:0000313|Proteomes:UP000024635}; RN [1] {ECO:0000313|Proteomes:UP000024635} RP NUCLEOTIDE SEQUENCE. RC STRAIN=HY135 {ECO:0000313|Proteomes:UP000024635}; RX PubMed=25730766; DOI=10.1038/ng.3237; RA Schwarz E.M., Hu Y., Antoshechkin I., Miller M.M., Sternberg P.W., RA Aroian R.V.; RT "The genome and transcriptome of the zoonotic hookworm Ancylostoma RT ceylanicum identify infection-specific gene families."; RL Nat. Genet. 47:416-422(2015). CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EYB82032.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JARK01001704; EYB82032.1; -; Genomic_DNA. DR Proteomes; UP000024635; Unassembled WGS sequence. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR CDD; cd01878; HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000024635}; KW Reference proteome {ECO:0000313|Proteomes:UP000024635}. FT DOMAIN 259 423 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 485 AA; 54735 MW; 4655E70E1A081333 CRC64; MTSVLIRRLL LPQWQLARSF CTPTTSSIDE RYDALISEAF SGDQTLPEHW GLRAAKEVSA HDFMVVHPKV RWGPSSASRL KDPQRQLDEA VTLVNTLPGF RVVESVVMGV DYNTKRKAVW GSGQIEALVR KKMQSRVTAL MVNVDMLTPF QQHELFSIFH VPIYDRYNIV LSIFKHYAKT QEARLQIQLA EIPYIRNRLH YLNKYRSDPL TLHVERQSER ASVDEFEVLR LREQSLRKKL QQVIEKNVGK ASEETRDAAM VAVVGYTNAG KTSLVKCLTG ASSLLPKDRL FATLDTTRHA ARLPSGRKVI FTDTIGFLSD LPMHLLAAFQ ATLSHVNLAD VIIHIRDMSN PDWAAQSEDV DKTLESIGLS QSRISDIIVA DNKVDVEGSA VSYTPGAIRI SCTTSEGVNE LIGRVDEMVL RATGCKPRRL RLKASSPAIP YLYKEGFVAK EPSHTETHLI FDVFMNDAEF ARFQKSTGTL RKRER // ID A0A017HDM6_9RHOB Unreviewed; 427 AA. AC A0A017HDM6; DT 11-JUN-2014, integrated into UniProtKB/TrEMBL. DT 11-JUN-2014, sequence version 1. DT 07-JUN-2017, entry version 17. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=Lokhon_01970 {ECO:0000313|EMBL:EYD71899.1}; OS Loktanella hongkongensis DSM 17492. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae; Loktanella. OX NCBI_TaxID=1122180 {ECO:0000313|EMBL:EYD71899.1, ECO:0000313|Proteomes:UP000025047}; RN [1] {ECO:0000313|EMBL:EYD71899.1, ECO:0000313|Proteomes:UP000025047} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 17492 {ECO:0000313|EMBL:EYD71899.1, RC ECO:0000313|Proteomes:UP000025047}; RA Fiebig A., Goeker M., Klenk H.-P.P.; RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EYD71899.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; APGJ01000006; EYD71899.1; -; Genomic_DNA. DR EnsemblBacteria; EYD71899; EYD71899; Lokhon_01970. DR PATRIC; fig|1122180.6.peg.1957; -. DR Proteomes; UP000025047; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000025047}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000025047}. FT DOMAIN 207 376 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 427 AA; 47360 MW; C96FCB273782375A CRC64; MTDYYIPEAP DTRTWVIHPE IKNDQDRREP VAALAEAVAL AEALPGLDIV GSEVVRLPKR HPGMLFGTGK IEELKQRLKS NETELVLIDG HLSPVQQRNL EKEWKVKILD RTGLILEIFG DRAATREGVL QVEMAALNYQ RGRLVRAWTH LERQRGGLGF VGGPGETQIE ADRRAIDEQL VRLRRQLDKV VKTRALHRAS RAKVPFPIVA LVGYTNAGKS TLFNRLTGAE VMAKDMLFAT LDPTMRRVVL PTGDEVILSD TVGFISDLPT ELVAAFRATL EEVLDADLVL HVRDIGHPQT AEQAREVESI LSSLGLPEDT PQIEVWNKID ALEPEGREAS LERAARTENV SAVSAITGEG MDALLTEVSR ALGGAKHAED LVVPFAAGRK RAWLFEQGLV EADVPTEDGH RMTVRWSATQ KARFDRL // ID A0A017HHF2_9RHOB Unreviewed; 424 AA. AC A0A017HHF2; DT 11-JUN-2014, integrated into UniProtKB/TrEMBL. DT 11-JUN-2014, sequence version 1. DT 05-JUL-2017, entry version 22. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=Rumeso_04669 {ECO:0000313|EMBL:EYD73548.1}; OS Rubellimicrobium mesophilum DSM 19309. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae; Rubellimicrobium. OX NCBI_TaxID=442562 {ECO:0000313|EMBL:EYD73548.1, ECO:0000313|Proteomes:UP000019666}; RN [1] {ECO:0000313|EMBL:EYD73548.1, ECO:0000313|Proteomes:UP000019666} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 19309 {ECO:0000313|EMBL:EYD73548.1, RC ECO:0000313|Proteomes:UP000019666}; RA Fiebig A., Goeker M., Klenk H.-P.P.; RL Submitted (FEB-2013) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EYD73548.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AOSK01000130; EYD73548.1; -; Genomic_DNA. DR EnsemblBacteria; EYD73548; EYD73548; Rumeso_04669. DR PATRIC; fig|442562.3.peg.4599; -. DR Proteomes; UP000019666; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000019666}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000019666}. FT DOMAIN 204 372 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 424 AA; 47397 MW; FEC7AF9905E0BF49 CRC64; MLDRREKVTR AWVLHPDIKG DRDARPSEPA LEEAVALAAA LPGLDVRGSE VVRLGRVHPG MLFGSGKIEE LKARFTEAEV ELVLVDGPVS PVQQRNLEKE WGVKLLDRTG LILEIFSDRA RTREGVLQVE MAALSYQRTR LVRAWTHLER QRGGFGFVGG PGETQIEADR RAIDEQLIKL KRQIDRVART RTLHRAARAK VPFPVVALVG YTNAGKSTIF NRLTGAEVLA KDMLFATLDP TMRRIVLPAG LQVILSDTVG FISDLPTELV AAFRATLEEV LDADLILHVR DISHPQTDAQ AHDVEAILGS LGVSEATPLI EVWNKIDLLT PEARETVQRQ GERAPAVFPV SALTGEGLDA LLAEVARRLD EPREEEEIVV PYAAGRQRAW LHENRLVVEE RDEEKGTRVR VRWTARQRDR FLTL // ID A0A017SW61_9DELT Unreviewed; 452 AA. AC A0A017SW61; DT 11-JUN-2014, integrated into UniProtKB/TrEMBL. DT 11-JUN-2014, sequence version 1. DT 12-APR-2017, entry version 19. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=CAP_8944 {ECO:0000313|EMBL:EYF00855.1}; OS Chondromyces apiculatus DSM 436. OC Bacteria; Proteobacteria; Deltaproteobacteria; Myxococcales; OC Sorangiineae; Polyangiaceae; Chondromyces. OX NCBI_TaxID=1192034 {ECO:0000313|EMBL:EYF00855.1, ECO:0000313|Proteomes:UP000019678}; RN [1] {ECO:0000313|EMBL:EYF00855.1, ECO:0000313|Proteomes:UP000019678} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 436 {ECO:0000313|EMBL:EYF00855.1, RC ECO:0000313|Proteomes:UP000019678}; RA Sharma G., Khatri I., Kaur C., Mayilraj S., Subramanian S.; RT "Genome assembly of Chondromyces apiculatus DSM 436."; RL Submitted (MAY-2013) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EYF00855.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ASRX01000096; EYF00855.1; -; Genomic_DNA. DR EnsemblBacteria; EYF00855; EYF00855; CAP_8944. DR Proteomes; UP000019678; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 2. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000019678}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000019678}. FT DOMAIN 233 398 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 194 221 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 452 AA; 49768 MW; A5D84B299442D9FC CRC64; MADLAELGRL VETLGYDVVA TISQRRAALG AAAVLGRGKL RELAAYTGGE GEIGSSAPQR KDKARLRWEA EQREAEEGGE GDLDEGEGEV DEGEAYEGEE GDEEGAEGVP VADRQATLVA IDHDVSPSQL RNLERATGTQ VLDRTGVIIE IFHRHARSRE AKLQVEIARL SYVAPRLRES PGTSERQRGK GAGESALELD RRRIRDRIAE LREELAAVQR DHSVRRTLRR DARRVALVGY TNAGKSSLMR ALTASEVLVA DKLFATLDTT VRALQPEAKP RILVSDTVGF IKKLPHDLVA SFRSTLDEAL EASLLLFVAD VSDPMYEEQL TVTRSVLGEI GAVDIPSLLL LNKVDRLTPL QREALQQEHP EAVMLSAKDP ADVAALRDRI VAFFEASMVE GELVLPYGKQ SLIGEIYENA RVMEETYDEQ GGKFRLRAHP TALDRLRSLL LK // ID A0A017SWJ6_9DELT Unreviewed; 635 AA. AC A0A017SWJ6; DT 11-JUN-2014, integrated into UniProtKB/TrEMBL. DT 11-JUN-2014, sequence version 1. DT 12-APR-2017, entry version 19. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=CAP_8386 {ECO:0000313|EMBL:EYF01344.1}; OS Chondromyces apiculatus DSM 436. OC Bacteria; Proteobacteria; Deltaproteobacteria; Myxococcales; OC Sorangiineae; Polyangiaceae; Chondromyces. OX NCBI_TaxID=1192034 {ECO:0000313|EMBL:EYF01344.1, ECO:0000313|Proteomes:UP000019678}; RN [1] {ECO:0000313|EMBL:EYF01344.1, ECO:0000313|Proteomes:UP000019678} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 436 {ECO:0000313|EMBL:EYF01344.1, RC ECO:0000313|Proteomes:UP000019678}; RA Sharma G., Khatri I., Kaur C., Mayilraj S., Subramanian S.; RT "Genome assembly of Chondromyces apiculatus DSM 436."; RL Submitted (MAY-2013) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EYF01344.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ASRX01000083; EYF01344.1; -; Genomic_DNA. DR EnsemblBacteria; EYF01344; EYF01344; CAP_8386. DR Proteomes; UP000019678; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000019678}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000019678}. FT DOMAIN 394 559 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 635 AA; 70607 MW; 1C20B44C805C6BAE CRC64; MPTLYGNTTG LSPNATKLLE RIYRRKVPLN VIATPELIKA LAEASHETGR QVGALVHRSG EIDYVIVGDA TRLMLPDIGR LRAAQGRFRA LRLVHTHLWN EELTRDDFVD LVRLRLDLVA AIQLTPGGEP RSLQYAYNTP PHEKIEKASD AESIEEHLPY ATVGPLLLGR VDVDFGQLIQ ALEDEFAKRS RTRKVTAKDG RALLVHVAEK TKHGALAHAE ESLRELSELA DTAGVEIADT VLQLRERIDP RHVMGKGKLD EVLLRAAELD AETLVFDRNL TPSQASAIAK HTDLKVIDRT QLILDIFAQR AESRDGKLQV ELAQLKYALP RLSQKDDSLS RLTGGIGGRG PGETKLEIGR RRAKERVSFL EDQLKRLFRQ REVRRRRRGR LGVPVVSIVG YTNAGKSTLL NTLTGADVLA ENKLFATLDP RSRRLRFPEE REIVLTDTVG FIRDLPPDLF AAFRATFEEA ADADLLLHVV DASDPARDQH IETTEALLTE LHLVEIPRIL VFNKIDRLDA DEARWLQQGH PDAILLSATE RETARPLLAR IAERLKSRWE ASALVPTYTV DEGGADDEPV DGEAPSLHRT AATDDGDGES LWNEAQDAQD AQGESASLTT LAELGARPRR SVLRI // ID A0A017SWW4_9DELT Unreviewed; 742 AA. AC A0A017SWW4; DT 11-JUN-2014, integrated into UniProtKB/TrEMBL. DT 11-JUN-2014, sequence version 1. DT 12-APR-2017, entry version 19. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=CAP_8773 {ECO:0000313|EMBL:EYF01060.1}; OS Chondromyces apiculatus DSM 436. OC Bacteria; Proteobacteria; Deltaproteobacteria; Myxococcales; OC Sorangiineae; Polyangiaceae; Chondromyces. OX NCBI_TaxID=1192034 {ECO:0000313|EMBL:EYF01060.1, ECO:0000313|Proteomes:UP000019678}; RN [1] {ECO:0000313|EMBL:EYF01060.1, ECO:0000313|Proteomes:UP000019678} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 436 {ECO:0000313|EMBL:EYF01060.1, RC ECO:0000313|Proteomes:UP000019678}; RA Sharma G., Khatri I., Kaur C., Mayilraj S., Subramanian S.; RT "Genome assembly of Chondromyces apiculatus DSM 436."; RL Submitted (MAY-2013) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EYF01060.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ASRX01000091; EYF01060.1; -; Genomic_DNA. DR EnsemblBacteria; EYF01060; EYF01060; CAP_8773. DR Proteomes; UP000019678; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR002575; Aminoglycoside_PTrfase. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR011009; Kinase-like_dom. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF01636; APH; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF56112; SSF56112; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000019678}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000019678}. FT DOMAIN 213 378 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 174 201 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 742 AA; 80931 MW; 236B426A00272BF1 CRC64; MSKGSKRSIS FHASHSPACA ILLARQHPER SDTQVQVSLD ELQNLLAGLG IRVAHTVVQR RAAAASSTVL GEGKQAEVAA LLAEARREHG EESVLVVVDE ALSPGKLRTL ENALEVEVID RTGVILRVFE QRARTQVAQL EVEMARLTYE APRVREDASL GDREGGGGRG GRGHSNVELK KQRIRERVAS LRRALDEQRA VEEKQRARRR DALRVALVGY TNAGKSSLMR ALTGSDVLVE DKLFATLGTT VRALSPETAP RILLSDTVGF IRDLPHELVA SFHSTLEEAR DAGLLLFVAD ASDPAFRDQL RVTRETLDAV GASGVPSRVL LTKIDRVDAS TRAALAAELP DAVQVCAHDP DDIRGLRDAL VAFFAQRMTE ETFVVPFGDG RLLGEIRAEA RVVTETYTDE GVVLSVRALP EAIGRWKRAL PEGPPIEAVA DLVEAARRHG LQLTTVAGDF DRTGLDFLVV HARDEEGVPW IVRTPRRPEV FASSCVEARA LRLVRPRLPV AVPDWRVHAR EVIAYPRLDG TPAITVDPSS GYSWNIIAPG ALPEAFLDSF ADTLAALQAI PPEEAADAGV PTKTIAEARQ ALAKAMEATR GVLAPSEVMW TRWHRWLEDD ALWPQHLALV HGDLHPGHLL LGADGRMQGV LDWTEAQVTD PSLDFAMFAG CFGREALDAL LTRFERAGGK TWPRLAEHAA ERWAAFPVLG AEWALRTNNT AVLEFTRAQL AATEATAAPT QR // ID A0A021VYN5_9CELL Unreviewed; 531 AA. AC A0A021VYN5; DT 11-JUN-2014, integrated into UniProtKB/TrEMBL. DT 11-JUN-2014, sequence version 1. DT 07-JUN-2017, entry version 20. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=N866_14385 {ECO:0000313|EMBL:EYR64182.1}; OS Actinotalea ferrariae CF5-4. OC Bacteria; Actinobacteria; Micrococcales; Cellulomonadaceae; OC Actinotalea. OX NCBI_TaxID=948458 {ECO:0000313|EMBL:EYR64182.1, ECO:0000313|Proteomes:UP000019753}; RN [1] {ECO:0000313|EMBL:EYR64182.1, ECO:0000313|Proteomes:UP000019753} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CF5-4 {ECO:0000313|EMBL:EYR64182.1, RC ECO:0000313|Proteomes:UP000019753}; RA Chen F., Li Y., Wang G.; RT "Actinotalea ferrariae CF5-4."; RL Submitted (JAN-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EYR64182.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AXCW01000042; EYR64182.1; -; Genomic_DNA. DR EnsemblBacteria; EYR64182; EYR64182; N866_14385. DR Proteomes; UP000019753; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 2. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000019753}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000019753}. FT DOMAIN 311 477 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 531 AA; 57169 MW; 1673136B2AD4150D CRC64; MTHPRTDAAT GDTQDPRDAA TAAQDEADRP GADADGTREH DGFGPARRLV PDDVVARVLA RAGTALDEGG TRWTDDDGEQ LDREERAALR RVGGLSTELA DVTEVEYRQL RLERVVLAGV WTSGTVEEAE LSLRELAALA ETAGSQVLDG MLQRRSHPDP STYFGSGKAA ELAEVVSAEG ADTVIVDADL APSQRRSLED IVKVKVIDRT ALILDIFAQH AKSKEGKAQV ELAQLEYLLP RLRGWGESMS RQAGGRVAGG EGIGSRGPGE TKIELDRRRI RARMAKLRRE IAAMAPSRET RRSSRRRHEV PSVAIVGYTN AGKSSLLNRL TGAGVLVENA LFATLDPTVR RARTPDGRTY TLSDTVGFVR SLPTQLVEAF RSTLEEVAEA DLLLHVVDVS HPDPEGQIAA VRTVLADIEG ADALPELVVL NKADVADPET VARLQRREPR SVVVSAHTGA GLEELVELVA EALPRPQETV DVVVPYARGD LVHRAHTEGE VDTEEHTAAG TVLRARVAAE LAAELRAVSV A // ID A0A021X479_9RHIZ Unreviewed; 440 AA. AC A0A021X479; DT 11-JUN-2014, integrated into UniProtKB/TrEMBL. DT 11-JUN-2014, sequence version 1. DT 30-AUG-2017, entry version 24. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:EYR80025.1}; GN ORFNames=SHLA_1c002050 {ECO:0000313|EMBL:EYR80025.1}; OS Shinella sp. DD12. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Rhizobiaceae; Shinella. OX NCBI_TaxID=1410620 {ECO:0000313|EMBL:EYR80025.1, ECO:0000313|Proteomes:UP000017832}; RN [1] {ECO:0000313|EMBL:EYR80025.1, ECO:0000313|Proteomes:UP000017832} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DD12 {ECO:0000313|EMBL:EYR80025.1, RC ECO:0000313|Proteomes:UP000017832}; RA Poehlein A., Freese H., Daniel R., Simeonova D.D.; RT "Draft Genome Sequence of Shinella sp. DD12."; RL Submitted (JAN-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EYR80025.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AYLZ02000159; EYR80025.1; -; Genomic_DNA. DR RefSeq; WP_023514953.1; NZ_AYLZ02000159.1. DR EnsemblBacteria; EYR80025; EYR80025; SHLA_1c002050. DR Proteomes; UP000017832; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000017832}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000017832}. FT DOMAIN 202 374 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 161 195 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 440 AA; 48715 MW; AE587455284E11AE CRC64; MRAVVIVPVL KAARGKPDPT VTMRSDEARL EEAVGLARAI DLTIASSAVV PVSQPKPGTL LGTGKIAEIK ALLDEHDAGL VIVDHPLTPV QQRNLEKEWG AKVIDRTGLI LEIFGRRAST KEGTLQVELA HLNYQKGRLV RSWTHLERQR GGAGFMGGPG ETQIEADRRL LQDKIVKLER ELEQVRRTRQ LHRSKRKKVP HPIVALVGYT NAGKSTLFNR ITGAGVLAED MLFATLDPTL RRMKLPQGRT VILSDTVGFI SDLPTHLVAA FRATLEEVLE ADLILHVRDM SDPDNGAQSS DVLRILADLG IDEKDGAERI LEVWNKIDRL EPEAREALVQ KAESQPTVIA VSAISGEGVD KLLSEINQRL SGVLVDRDVI LPVTQLQLLP WVYDHSIVDA REDLEDGNVR LELRLTETEA AELDRRLGIG GKRVVEDWER // ID A0A022KWK9_9MICO Unreviewed; 522 AA. AC A0A022KWK9; DT 11-JUN-2014, integrated into UniProtKB/TrEMBL. DT 11-JUN-2014, sequence version 1. DT 07-JUN-2017, entry version 24. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=D641_0105250 {ECO:0000313|EMBL:EYT50189.1}; OS Brachybacterium muris UCD-AY4. OC Bacteria; Actinobacteria; Micrococcales; Dermabacteraceae; OC Brachybacterium. OX NCBI_TaxID=1249481 {ECO:0000313|EMBL:EYT50189.1, ECO:0000313|Proteomes:UP000019754}; RN [1] {ECO:0000313|EMBL:EYT50189.1, ECO:0000313|Proteomes:UP000019754} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=UCD-AY4 {ECO:0000313|EMBL:EYT50189.1, RC ECO:0000313|Proteomes:UP000019754}; RX PubMed=23516213; RA Lo J.R., Lang J.M., Darling A.E., Eisen J.A., Coil D.A.; RT "Draft genome sequence of an Actinobacterium, Brachybacterium muris RT strain UCD-AY4."; RL Genome Announc. 1:E0008613-E0008613(2013). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EYT50189.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AORC01000005; EYT50189.1; -; Genomic_DNA. DR RefSeq; WP_017822754.1; NZ_AORC01000005.1. DR ProteinModelPortal; A0A022KWK9; -. DR EnsemblBacteria; EYT50189; EYT50189; D641_0105250. DR Proteomes; UP000019754; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000019754}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000019754}. FT DOMAIN 305 470 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 522 AA; 56388 MW; 409B32F4ABB67E37 CRC64; MPIAFHPNPA RDDDVTGSSA EEADAAHSPS TPEAAPEQEQ PARRRDPLTE RILARGDASV STITYESTTD GEQMDLADRQ ALRRVGGLST ELEDVTEVEY RQLRLERVVL AGLYTTGNLE DAENSLRELA ALAETAGSEV LDGVLQRRAH PDPATFLGKG KAAELAEVVA DVGADTVVVD GELGPGQRRA LEDVVKVKVI DRTALILDIF AQHAKSREGK AQVELAQLEY LLPRLRGWGD SMSRQAGGRV AAGGAGMGSR GPGETKIELD RRRIRDRMAK LRREIKAMAP GREAQRADRH RNQVPSVAIA GYTNAGKSSL LNRLTGAGVL VENALFATLD PTVRRSQTPD GREFTYADTV GFVRHLPTQL VEAFRSTLEE VGGADLLLHV VDAAHPDPEG QIRAVRTVLG ELEGFDVPEI VVLNKADIAE PETIARIRSL VEHSAVISAR TGEGIEELRE QIAEHLPRPA VEVDVVVPYS RGDLISRVHT TGEVISEGHL MEGTHLKARV DEALAAELHG AA // ID A0A022LNR5_9MICO Unreviewed; 513 AA. AC A0A022LNR5; DT 11-JUN-2014, integrated into UniProtKB/TrEMBL. DT 11-JUN-2014, sequence version 1. DT 07-JUN-2017, entry version 21. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=H489_0110280 {ECO:0000313|EMBL:EYT63807.1}; OS Curtobacterium flaccumfaciens UCD-AKU. OC Bacteria; Actinobacteria; Micrococcales; Microbacteriaceae; OC Curtobacterium. OX NCBI_TaxID=1292022 {ECO:0000313|EMBL:EYT63807.1, ECO:0000313|Proteomes:UP000019755}; RN [1] {ECO:0000313|EMBL:EYT63807.1, ECO:0000313|Proteomes:UP000019755} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=UCD-AKU {ECO:0000313|EMBL:EYT63807.1, RC ECO:0000313|Proteomes:UP000019755}; RX PubMed=23682147; RA Flanagan J.C., Lang J.M., Darling A.E., Eisen J.A., Coil D.A.; RT "Draft Genome Sequence of Curtobacterium flaccumfaciens Strain UCD-AKU RT (Phylum Actinobacteria)."; RL Genome Announc. 1:E00244-13(2013). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EYT63807.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; APJN01000048; EYT63807.1; -; Genomic_DNA. DR RefSeq; WP_017885908.1; NZ_KB714607.1. DR EnsemblBacteria; EYT63807; EYT63807; H489_0110280. DR GeneID; 31840811; -. DR Proteomes; UP000019755; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 2. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000019755}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}. FT DOMAIN 289 454 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 513 AA; 55915 MW; 7AC6B2A57FF31FD0 CRC64; MTDTHQQNHQ TNDDSADGVV ERVLRNADHR AASSIFAPAQ AIQTRSTDDR SWTGDGDQYD REDRAALRRV AGLSTELEDV TEVEYRQLRL EQVVLIGVYP QGDAQDAENS LRELAALAET AGAVVLDGLL QRRPNPDPAT YLGKGKAQEL AMVVKATGAD TVIADTELAP SQRRALEDVV KVKVIDRTAV ILDIFSQHAK TREGKAQVEL AQLQYLLPRL RGWGDSMSRQ AGGQVSGGAG MGSRGPGETK MELDRRKIHT RMAKLRRQIA GFTPAREAKR AERNRNEVPS VAIAGYTNAG KSSLLNRLTS AGVLVQNQLF ATLDATVRRT ESTKGREYTF ADTVGFVRNL PHQLVEAFRS TLEEVGDADV IVHVVDGSHP DPGAQLSTVR EVIGDVGAGD IPEVVVFNKA DLIDDAQRLV LIGLVPDAVF VSARTGEGIP ELLSVIEDRL PEPDVDLTIV VPYDRGDLVS SLHDTGSVES VDYVEDGTRL RVRVFQRQVT DLEPYVVTPV PTV // ID A0A022MLS8_9ACTN Unreviewed; 499 AA. AC A0A022MLS8; DT 11-JUN-2014, integrated into UniProtKB/TrEMBL. DT 11-JUN-2014, sequence version 1. DT 12-APR-2017, entry version 20. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=CF54_07040 {ECO:0000313|EMBL:EYT83492.1}; OS Streptomyces sp. Tu 6176. OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae; OC Streptomyces. OX NCBI_TaxID=1470557 {ECO:0000313|EMBL:EYT83492.1, ECO:0000313|Proteomes:UP000020060}; RN [1] {ECO:0000313|EMBL:EYT83492.1, ECO:0000313|Proteomes:UP000020060} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Tu 6176 {ECO:0000313|EMBL:EYT83492.1, RC ECO:0000313|Proteomes:UP000020060}; RA Olano C., Cano-Prieto C., Mendez C., Salas J.A.; RT "Draft genome sequence of Streptomyces sp. Tu 6176, producer of the RT cytotoxic benzoxazol nataxazol."; RL Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EYT83492.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JFJQ01000205; EYT83492.1; -; Genomic_DNA. DR EnsemblBacteria; EYT83492; EYT83492; CF54_07040. DR Proteomes; UP000020060; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000313|EMBL:EYT83492.1}; KW Complete proteome {ECO:0000313|Proteomes:UP000020060}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900, KW ECO:0000313|EMBL:EYT83492.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000020060}. FT DOMAIN 277 442 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 499 AA; 54178 MW; 3E94AB358FEEA25D CRC64; MTSSSGSSSS SQATKRLAHT HPDGLRADAL MEEDVAWSHE IDGERDGDQF DRSERAALRR VVGLSTELED VTEVEYRQLR LERVVLVGVW TSGTVHDAEN SLAELAALAE TAGAVVLDGV IQRRDKPDAA TYIGSGKAGE LRDIVLETGA DTVVCDGELS PGQLIHLEDV VKVKVIDRTA VILDIFAQHA KSREGKAQVA LAQMQYMLPR LRGWGQSLSR QMGGGSGGLA TRGPGETKIE TDRRRIREKM AKMRREIAAM KTGREIKRQE RRRHKVPSVA IAGYTNAGKS SLLNRLTGAG VLVENALFAT LDPTVRRAET PSGRLYTLAD TVGFVRHLPH HLVEAFRSTM EEVGDSDLIL HVVDGSHPDP EEQLAAVREV IREVGATDVP EIVVVNKADA ADPLVLQRLL RREKHSIAVS ARTGQGIDTL LAMIDAELPR PAVQVEALVP YTHGKLVARA HTEGEVISEE HTAEGTLLKA LVHEELAAEL APYAPVPAL // ID A0A022R8Y3_ERYGU Unreviewed; 552 AA. AC A0A022R8Y3; DT 11-JUN-2014, integrated into UniProtKB/TrEMBL. DT 11-JUN-2014, sequence version 1. DT 07-JUN-2017, entry version 15. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EYU36741.1}; GN ORFNames=MIMGU_mgv1a003953mg {ECO:0000313|EMBL:EYU36741.1}; OS Erythranthe guttata (Yellow monkey flower) (Mimulus guttatus). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae; OC Pentapetalae; asterids; lamiids; Lamiales; Phrymaceae; Erythranthe. OX NCBI_TaxID=4155 {ECO:0000313|EMBL:EYU36741.1, ECO:0000313|Proteomes:UP000030748}; RN [1] {ECO:0000313|EMBL:EYU36741.1, ECO:0000313|Proteomes:UP000030748} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=24225854; DOI=10.1073/pnas.1319032110; RA Hellsten U., Wright K.M., Jenkins J., Shu S., Yuan Y., Wessler S.R., RA Schmutz J., Willis J.H., Rokhsar D.S.; RT "Fine-scale variation in meiotic recombination in Mimulus inferred RT from population shotgun sequencing."; RL Proc. Natl. Acad. Sci. U.S.A. 110:19478-19482(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; KI630592; EYU36741.1; -; Genomic_DNA. DR RefSeq; XP_012839111.1; XM_012983657.1. DR GeneID; 105959537; -. DR Proteomes; UP000030748; Unassembled WGS sequence. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000030748}; KW Reference proteome {ECO:0000313|Proteomes:UP000030748}. FT DOMAIN 329 495 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 295 322 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 552 AA; 60885 MW; B6DFFEDFB810F7F8 CRC64; MSLCFCSILK PSLLNREHDF VSRWAPNPSI KPVQLFNLQT HGGCFRFKAV HTDGVGVIYP DDTVSERTGP IAGAEPEAEA HGVISEAAGT APEESQDAPS QIRSKRSEEK KGSVDESDRE SRFKLRNGRE VFEEKAYLVG VSRKGDTDGS FSIEDSLGEL EQLADTAGLS VVGSTCQRLA TPNSRTYIGS GKVAEIKSAI TAFGVETVIF DDELSPGQLR NLEKAFGGGV RVCDRTALIL DIFNQRAATR EASLQVSLAQ MEYQLPRLTK MWSHLERQSG GQVKGMGEKQ IEVDKRILRD QIGALKKEIE SVRKHRKQYR NRRFDIPIPV VSLVGYTNAG KSTLLNRLTG ADVLAEDKLF ATLDPTTRRV LTKNGKEFLL TDTVGFIQKL PTTLVAAFRA TLEEISESSL IVHVVDISHP LAEQQVDAVD KVLAELDTTS IPKLIVWNKV DNAKDPEKIK SEAENNADIV CISALTGEGL DDFCNSVQEK LKDMMVWVEA LIPFDKGELL STIHHVGMVE KIEYVENGAL VRAHVPLRFA RLLTPMRQTC AS // ID A0A022RZY1_ERYGU Unreviewed; 575 AA. AC A0A022RZY1; DT 11-JUN-2014, integrated into UniProtKB/TrEMBL. DT 11-JUN-2014, sequence version 1. DT 07-JUN-2017, entry version 17. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EYU44525.1}; GN ORFNames=MIMGU_mgv1a003595mg {ECO:0000313|EMBL:EYU44525.1}; OS Erythranthe guttata (Yellow monkey flower) (Mimulus guttatus). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae; OC Pentapetalae; asterids; lamiids; Lamiales; Phrymaceae; Erythranthe. OX NCBI_TaxID=4155 {ECO:0000313|EMBL:EYU44525.1, ECO:0000313|Proteomes:UP000030748}; RN [1] {ECO:0000313|EMBL:EYU44525.1, ECO:0000313|Proteomes:UP000030748} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=24225854; DOI=10.1073/pnas.1319032110; RA Hellsten U., Wright K.M., Jenkins J., Shu S., Yuan Y., Wessler S.R., RA Schmutz J., Willis J.H., Rokhsar D.S.; RT "Fine-scale variation in meiotic recombination in Mimulus inferred RT from population shotgun sequencing."; RL Proc. Natl. Acad. Sci. U.S.A. 110:19478-19482(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; KI630214; EYU44525.1; -; Genomic_DNA. DR RefSeq; XP_012854184.1; XM_012998730.1. DR GeneID; 105973694; -. DR Proteomes; UP000030748; Unassembled WGS sequence. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR CDD; cd01878; HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 4: Predicted; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000030748}; KW Reference proteome {ECO:0000313|Proteomes:UP000030748}. FT DOMAIN 297 550 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 75 102 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 575 AA; 63795 MW; 8D53D7FCAAE31C23 CRC64; MLGAILHLRS RLSLLNPINT SSSSIIPSQF PPLSAYFSNS PILQRKQLNP DNDEFNREPD CPPRLFVVQP RIRPETLLKA KLEEALNLAN SLEQQRDGLY HTEFSDKEMP PHLVVQNPAA RSTRADTYFG GGTVGNIKCH INNLESKDEV DAVFVNAILS GVQQRNLERT WDKPVLDRIS LIIEIFNAHA QTKEAKLQAE LAALMYKRSR LVRVRGLDGR YTFGGAGESE VVSARGRGSG GRGFISGAGE TELQLQRRRI LDRRKKLLSE IKEVRSTRAI QRAARRRQGS SPGQEIPTVA VVGYTNAGKS TLVSALSNTY LYCDDRLFAT VDPKLSSVVL PSGRKVLLSD TVGFISDLPV QLVEAFHATL EEVVEADLLV HVLDSSSPSI NEHREAVMQV LCKLGVSKEK LHNMIEVWNK VDLLEKQPDI DEVDDGDYDT SLSGDDDADV ASEQLTGQHD EDRDYPEEWL LSEDEEEQEE DSWVDYDGCS IGSNTVSDKP NELLVDSVKD SVKDAVSVAE SSCPVKASAV TGLGLQELLQ LIDDKLGQSR VVERTVFDSK WRPPRGQDND IAIEQ // ID A0A023BYK9_9FLAO Unreviewed; 402 AA. AC A0A023BYK9; DT 11-JUN-2014, integrated into UniProtKB/TrEMBL. DT 11-JUN-2014, sequence version 1. DT 07-JUN-2017, entry version 22. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=ATO12_10530 {ECO:0000313|EMBL:EZH75151.1}; OS Aquimarina atlantica. OC Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales; OC Flavobacteriaceae; Aquimarina. OX NCBI_TaxID=1317122 {ECO:0000313|EMBL:EZH75151.1, ECO:0000313|Proteomes:UP000023541}; RN [1] {ECO:0000313|EMBL:EZH75151.1, ECO:0000313|Proteomes:UP000023541} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=22II-S11-z7 {ECO:0000313|EMBL:EZH75151.1, RC ECO:0000313|Proteomes:UP000023541}; RA Lai Q.; RT "Aquimarina sp. 22II-S11-z7 Genome Sequencing."; RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EZH75151.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AQRA01000002; EZH75151.1; -; Genomic_DNA. DR RefSeq; WP_034240319.1; NZ_AQRA01000002.1. DR EnsemblBacteria; EZH75151; EZH75151; ATO12_10530. DR Proteomes; UP000023541; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000023541}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000023541}. FT DOMAIN 200 385 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 402 AA; 46666 MW; 7E1BB0B36A5E35BE CRC64; MLEREKIAYE KTVLIGIITK NQDEEKLEEF LDELEFLTYT AGGEVVKRFT QKMDMPNSKT FIGSGKMEDV RIYVEQHDIG TVIFDDELSP GQLRNIERIL KAKIIDRTNL ILDIFAQRAQ TSYARTQVEL AQYQYLLPRL TGLWTHLERQ RGGIGMRGPG ETEIETDRRI VRDRISLLKK KLLTIDKQMA TQRGNRGKLV RVALVGYTNV GKSTLMNVIA KSEVFAENKL FATLDTTVRK VVIGNLPFLL SDTVGFIRKL PTQLVESFKS TLDEVREADL LLHVVDISHP QFEDHIESVN RILKEIDCTD KPTIMVFNKI DAYQHETIDE DDLTTEKTKA HYTLEEWKQT WMSRIGDNAL FISAIKKENI DDFRKRVYKE TRNIHVTRFP YNNFLYPEIV EE // ID A0A023D4E1_ACIMT Unreviewed; 435 AA. AC A0A023D4E1; DT 11-JUN-2014, integrated into UniProtKB/TrEMBL. DT 11-JUN-2014, sequence version 1. DT 07-JUN-2017, entry version 23. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=Amme_040_011 {ECO:0000313|EMBL:GAJ28939.1}; OS Acidomonas methanolica NBRC 104435. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales; OC Acetobacteraceae; Acidomonas. OX NCBI_TaxID=1231351 {ECO:0000313|EMBL:GAJ28939.1, ECO:0000313|Proteomes:UP000019760}; RN [1] {ECO:0000313|EMBL:GAJ28939.1, ECO:0000313|Proteomes:UP000019760} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MB58 {ECO:0000313|EMBL:GAJ28939.1, RC ECO:0000313|Proteomes:UP000019760}; RA Higashiura N., Hadano H., Hirakawa H., Matsutani M., Takabe S., RA Matsushita K., Azuma Y.; RT "Draft genomic DNA sequence of the facultatively methylotrophic RT bacterium Acidomonas methanolica type strain MB58."; RL FEMS Microbiol. Lett. 351:9-13(2014). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:GAJ28939.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BAND01000040; GAJ28939.1; -; Genomic_DNA. DR RefSeq; WP_042058134.1; NZ_BAND01000040.1. DR EnsemblBacteria; GAJ28939; GAJ28939; Amme_040_011. DR Proteomes; UP000019760; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000019760}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000019760}. FT DOMAIN 207 375 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 435 AA; 47787 MW; 9A53DAB28C87B840 CRC64; MASNVTTPPA TRAAVILPWE RPTPSDEFRA AEARLEEAVG LSASIGLVVV RQAILALRAR RPATLFGSGQ VEQLAEMVRQ DEVAVLIVDS KLSPGQQRNL ERALDCKVVD RTGLILDIFG ARAATREGVL QVELAHLEYQ RSRLVRLWTH LERQRGGFGF LGGPGETQME ADRRMLDERL VRLRKDLEQV RRTRGLHRTA RRKVPFPVVA LVGYTNAGKS TLFNALTGAS VHAQDQLFAT LDPTMRGVTL PSGRRIILSD TVGFISDLPT ELVAAFRATL EEVAEADIIL HVRDIAHPDT AAQRADVINV LSGMTRDGML DAHWPDRCIE VLNKIDLLGA EEAPRAPGTV AISAITGQGL ANLFSALDGK MTAAMRLAHA ELAVTDGAAL AWLYEHGEVL ERLDRESGIS LDVRLFEQDR LRFGQLYPEC AIRID // ID A0A023DHX9_9BACI Unreviewed; 416 AA. AC A0A023DHX9; DT 11-JUN-2014, integrated into UniProtKB/TrEMBL. DT 11-JUN-2014, sequence version 1. DT 07-JUN-2017, entry version 23. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:GAJ40853.1}; GN ORFNames=GCA01S_052_00290 {ECO:0000313|EMBL:GAJ40853.1}; OS Parageobacillus caldoxylosilyticus NBRC 107762. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; OC Parageobacillus. OX NCBI_TaxID=1220594 {ECO:0000313|EMBL:GAJ40853.1, ECO:0000313|Proteomes:UP000023561}; RN [1] {ECO:0000313|EMBL:GAJ40853.1, ECO:0000313|Proteomes:UP000023561} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NBRC 107762 {ECO:0000313|EMBL:GAJ40853.1, RC ECO:0000313|Proteomes:UP000023561}; RA Hosoyama A., Hosoyama Y., Katano-Makiyama Y., Tsuchikane K., Ohji S., RA Ichikawa N., Yamazoe A., Fujita N.; RT "Whole genome shotgun sequence of Geobacillus caldoxylosilyticus NBRC RT 107762."; RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:GAJ40853.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BAWO01000052; GAJ40853.1; -; Genomic_DNA. DR RefSeq; WP_017435028.1; NZ_BAWO01000052.1. DR EnsemblBacteria; GAJ40853; GAJ40853; GCA01S_052_00290. DR Proteomes; UP000023561; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000023561}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}. FT DOMAIN 197 359 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 416 AA; 47541 MW; 479D55158C41778D CRC64; MSEREKAILV GCQLPHIDDE RFFYSMEELA SLVHTANGEV VATVTQKREA IHPATYIGKG KVEELVHLVE QTEADLVIFN DELSPSQNRN LARQLAVRII DRTQLILDIF AQRARSKEGK LQVELAQLQY LLPRLGGQGT ALSRLGGGIG TRGPGETKLE TDRRHIYRRI DEIKTQLKLV AEHRERYRER RKKNRAFQIS LVGYTNAGKS TLFNRLTAAD SFEENLLFAT LDPLTRRLIL PSGYTVLLTD TVGFIQDLPT TLVAAFRSTL EEVKEADLIL HIVDSSNPDY YHHEQTVYDL LDELGVASIP IVTIYNKQDI RHPHFVPSTE TEAMMVSAFC ADDIRRLRQF IEEMVKKQMV GYYVSIPDDE GKLLAQLKSE TILHELHYNE ESGMYECKGY VMPKHPLYGQ LRQFQK // ID A0A023NTZ0_9GAMM Unreviewed; 438 AA. AC A0A023NTZ0; DT 09-JUL-2014, integrated into UniProtKB/TrEMBL. DT 09-JUL-2014, sequence version 1. DT 07-JUN-2017, entry version 21. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=CH75_12345 {ECO:0000313|EMBL:AHX13898.1}; OS Dyella jiangningensis. OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales; OC Rhodanobacteraceae; Dyella. OX NCBI_TaxID=1379159 {ECO:0000313|EMBL:AHX13898.1, ECO:0000313|Proteomes:UP000024387}; RN [1] {ECO:0000313|EMBL:AHX13898.1, ECO:0000313|Proteomes:UP000024387} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SBZ 3-12 {ECO:0000313|EMBL:AHX13898.1, RC ECO:0000313|Proteomes:UP000024387}; RA Bao Y., Kwok A., Huang Z., Jiang J., He L., Xu Z., Sheng X., Leung F.; RT "Dyella jiangningensis sp. nov., a mineral-weathering bacterium RT isolated from the surface of potassium-bearing rock."; RL Submitted (FEB-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP007444; AHX13898.1; -; Genomic_DNA. DR RefSeq; WP_038619548.1; NZ_CP007444.1. DR EnsemblBacteria; AHX13898; AHX13898; CH75_12345. DR KEGG; dji:CH75_12345; -. DR KO; K03665; -. DR Proteomes; UP000024387; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000024387}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000024387}. FT DOMAIN 200 366 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 166 193 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 438 AA; 47666 MW; F39422C4A382B82A CRC64; MFDRQKKGER ALLVLPHSRG DGDAVRRAEE FAELTKSAGA EILGTISARV DVPNPRYYIG TGKADEIAEA ARALEADLVL VDHLLTPVQE RNLEKLLNIR VVDRAGLILD IFAQRARSHE GKLEVELAQL KHLATRLVRG WTHLDAQRGG AIGNRGPGET QLETDRRLLA ERVKMLTKRL EKVQTQRVQQ RRARLRNTVP RVALVGYTNA GKSTLFNGLT QGEVFAANLL FATLDPTVRK LDGLSCGPAV LADTVGFVRE LPHDLVAAFR GTLAEARDAD LLLHVSDAAD EERERLAKVV DSVLEEIDAG DLPQLRVMNK IDLAGLEPRI DRDAEGRPTT VWLSAATGVG VDLLKQALGE LLGGDRVQSE LRLPHSAGRL HARLKAAGAI TGEEVDEQGW RLSIDAPRSV IAPLSGGSAA EAALLREILG SVEEQESL // ID A0A023X301_9ACTN Unreviewed; 450 AA. AC A0A023X301; DT 09-JUL-2014, integrated into UniProtKB/TrEMBL. DT 09-JUL-2014, sequence version 1. DT 05-JUL-2017, entry version 20. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=RradSPS_1435 {ECO:0000313|EMBL:AHY46718.1}; OS Rubrobacter radiotolerans. OC Bacteria; Actinobacteria; Rubrobacteria; Rubrobacterales; OC Rubrobacteraceae; Rubrobacter. OX NCBI_TaxID=42256 {ECO:0000313|EMBL:AHY46718.1, ECO:0000313|Proteomes:UP000025229}; RN [1] {ECO:0000313|EMBL:AHY46718.1, ECO:0000313|Proteomes:UP000025229} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=RSPS-4 {ECO:0000313|EMBL:AHY46718.1, RC ECO:0000313|Proteomes:UP000025229}; RA Egas C.C., Barroso C.C., Froufe H.J.C., Pacheco J.J., RA Albuquerque L.L., da Costa M.M.S.; RT "Complete genome sequence of the Radio-Resistant Rubrobacter RT radiotolerans RSPS-4."; RL Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP007514; AHY46718.1; -; Genomic_DNA. DR EnsemblBacteria; AHY46718; AHY46718; RradSPS_1435. DR KEGG; rrd:RradSPS_1435; -. DR PATRIC; fig|42256.3.peg.1453; -. DR KO; K03665; -. DR Proteomes; UP000025229; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000025229}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000025229}. FT DOMAIN 217 329 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 176 203 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 450 AA; 49403 MW; C29A3AA83F1E4E6B CRC64; MPSTGQREYG VLPALDGALR GVVLVGAGEE RYLDELARLA QTLGLEVLGE MEQARRDNAG YIGSGKRKEL RELVREVGAG MVITDDELTA SQARTLENDC DAPVVDRTEL IIRIFHEHAR DAPSKLQVEL AELSYLLPRV RGMWRHLERL GGGAAGSAGS SGSSASGGRA TRGPGEQQLE YDRRQIRARM ERLKRRLAEE ERSRAVRRSR LNSTETPRIA LVGYTNAGKT TILNALSGAG RSTKDRLFET LETTTRLVEP TSGSYTTNGG DAGPREGAHR PAFTVTDTVG FIRKLPTQLV ESFSSTLEAA SDADILLLCA DASSPRLDEE VNTVRETLAS SSLSLNHIIQ VMNKKDLLSE GDLTRIKARF PEAVFTDMHE GYEELLGKIY EAISSMRKRM EVLIPHEEYA EVARLYGAAS IHSREERESG VLLDVSVPAS MAGRYSRYLA // ID A0A024FFH5_9FLAO Unreviewed; 403 AA. AC A0A024FFH5; DT 09-JUL-2014, integrated into UniProtKB/TrEMBL. DT 09-JUL-2014, sequence version 1. DT 07-JUN-2017, entry version 20. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=WPG_1197 {ECO:0000313|EMBL:BAO75427.1}; OS Winogradskyella sp. PG-2. OC Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales; OC Flavobacteriaceae; Winogradskyella. OX NCBI_TaxID=754409 {ECO:0000313|EMBL:BAO75427.1, ECO:0000313|Proteomes:UP000031636}; RN [1] {ECO:0000313|Proteomes:UP000031636} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=PG-2 {ECO:0000313|Proteomes:UP000031636}; RA Kumagai Y., Yoshizawa S., Oshima K., Hattori M., Iwasaki W., RA Kogure K.; RT "Complete Genome Sequence of Winogradskyella sp. Strain PG-2, a RT Proteorhodopsin-Containing Marine Flavobacterium."; RL Genome Announc.2:e00490-14(2014). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AP014583; BAO75427.1; -; Genomic_DNA. DR RefSeq; WP_045470354.1; NZ_AP014583.1. DR EnsemblBacteria; BAO75427; BAO75427; WPG_1197. DR KEGG; win:WPG_1197; -. DR KO; K03665; -. DR Proteomes; UP000031636; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000031636}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000031636}. FT DOMAIN 200 385 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 403 AA; 46374 MW; EB38591D49E34E00 CRC64; MIEKKDIALE KVVLIGVITQ DQNEETSTEY LDELEFLTYT AGGEVVKRYT QKMAMPNPKT FIGTGKMEDV RHYVEGNKVG TVIFDDELSP AQERNISKIL NCKILDRTNL ILDIFAQRAQ TSYARTQVEL AQCEYLLPRL KGMWTHLERQ KGGIGMRGPG ETEIETDRRI VRDKISLLKS KIKTIDKQMA VQRGNRGKMV RVALVGYTNV GKSTLMNVIS KSKVFAENKL FATLDTTVRK VVIGNLPFLV SDTVGFIRKL PTQLVESFKS TLDEVREADL LLHVVDISHS NFEEHIDSVN QILDEIESKD KPTIMVFNKI DAYEPEPFDE EDLIVERTKA NYSIEEWKNT WMARVGDNAL FISALNKENL DEFRKRVYKE VREIHVTRFP YNHFLYPDVE DIQ // ID A0A024HPX7_PSEKB Unreviewed; 433 AA. AC A0A024HPX7; DT 09-JUL-2014, integrated into UniProtKB/TrEMBL. DT 09-JUL-2014, sequence version 1. DT 30-AUG-2017, entry version 22. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:CDF86567.1}; GN ORFNames=PKB_5255 {ECO:0000313|EMBL:CDF86567.1}; OS Pseudomonas knackmussii (strain DSM 6978 / LMG 23759 / B13). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=1301098 {ECO:0000313|EMBL:CDF86567.1, ECO:0000313|Proteomes:UP000025241}; RN [1] {ECO:0000313|EMBL:CDF86567.1, ECO:0000313|Proteomes:UP000025241} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=B13 {ECO:0000313|EMBL:CDF86567.1, RC ECO:0000313|Proteomes:UP000025241}; RA Linke B.; RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:CDF86567.1, ECO:0000313|Proteomes:UP000025241} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=B13 {ECO:0000313|EMBL:CDF86567.1, RC ECO:0000313|Proteomes:UP000025241}; RA Miyazaki R., Bertelli C., Falquet L., Robinson-Rechavi M., Gharib W., RA Roy S., Van der Meer J.R.; RT "Genome sequence of the 3-chlorobenzoate degrading bacterium RT Pseudomonas knackmussii B13 shows multiple evidence for horizontal RT gene transfer."; RL Submitted (MAY-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; HG322950; CDF86567.1; -; Genomic_DNA. DR RefSeq; WP_043255747.1; NZ_HG322950.1. DR EnsemblBacteria; CDF86567; CDF86567; PKB_5255. DR GeneID; 29898739; -. DR KEGG; pkc:PKB_5255; -. DR PATRIC; fig|1301098.3.peg.5236; -. DR KO; K03665; -. DR Proteomes; UP000025241; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000025241}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000025241}. FT DOMAIN 199 366 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 165 192 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 433 AA; 48880 MW; 05A28500B87BC9D6 CRC64; MFFERPGGGE RAILVHLEGQ DPEAREDPQE FQELARSAGA ESVAFVSISR HQPSAKYLIG SGKVDELRDL VHAQKVELVI FNHTLTPSQE RNLERALECR VLDRTGLILD IFAQRARTHE GKLQVELAQL EHMSTRLVRG WTHLERQKGG IGLRGPGETQ LETDRRLLRG RIRQIKQRLE KVRSQREQAR RGRRRAEIPS VSLVGYTNAG KSTLFNALTT SEVYAANQLF ATLDPTLRRL ELDDVGPVVL ADTVGFIRHL PHKLVEAFRA TLEESSNADL LLHVIDAAEP ERTAQVEQVH AVLAEIGANE LPMLEVYNKI DLMPDFEAQI QRDEDGKPVR VWLSAREGRG LELLEKAVAE LLGDDMFVGT LCLPQRLGRL RAQLFQLGAV QSEEHDEQGR AVLQVRLPRV ELNRLVSREG WQPAEFIAQH TLQ // ID A0A024JXQ5_9MYCO Unreviewed; 479 AA. AC A0A024JXQ5; DT 09-JUL-2014, integrated into UniProtKB/TrEMBL. DT 09-JUL-2014, sequence version 1. DT 30-AUG-2017, entry version 23. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=BN973_02387 {ECO:0000313|EMBL:CDO88028.1}; OS Mycobacterium triplex. OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae; OC Mycobacterium. OX NCBI_TaxID=47839 {ECO:0000313|EMBL:CDO88028.1, ECO:0000313|Proteomes:UP000028880}; RN [1] {ECO:0000313|EMBL:CDO88028.1, ECO:0000313|Proteomes:UP000028880} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 44626 {ECO:0000313|EMBL:CDO88028.1, RC ECO:0000313|Proteomes:UP000028880}; RX PubMed=24874681; DOI=10.1128/genomeA.00499-14; RA Sassi M., Croce O., Robert C., Raoult D., Drancourt M.; RT "Draft Genome Sequence of Mycobacterium triplex DSM 44626."; RL Genome Announc. Announc.2:e00499-e00414(2014). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; HG964446; CDO88028.1; -; Genomic_DNA. DR RefSeq; WP_036468235.1; NZ_LQPY01000034.1. DR EnsemblBacteria; CDO88028; CDO88028; BN973_02387. DR Proteomes; UP000028880; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000028880}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000028880}. FT DOMAIN 256 425 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 215 249 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 479 AA; 51760 MW; 6BAD1C569016BC90 CRC64; MTHPETPFHD QPPDQLASEP SVGELALEDR SALRRVAGLS TELADISEVE YRQLRLERVV LVGVWTEGSA ADNRASLAEL AALAETAGSQ VLEGLIQRRD KPDPSTYIGS GKAQELREVV LATGADTVIC DGELSPAQLT ALEKAVKVKV IDRTALILDI FAQHATSREG KAQVSLAQME YMLPRLRGWG ESMSRQAGGR AGGSGGGVGL RGPGETKIET DRRRIRERMS KLRREIRDMK QARDTQRSRR LHSDMPSVAI VGYTNAGKSS LLNALTGAGV LVQDALFATL EPTTRRAEFD DGRPLVLTDT VGFVRHLPTQ LVEAFRSTLE EVVDADLLLH VVDGSDVNPF AQINAVRQVI SEVISDHNGE PPPELLVVNK IDAAGDLMLA KLRHGLPGAV FVSAHTGDGI DALRRRMAEL AAPTDAAVDV VIPYDRGDLV ARVHSDGRVQ QAEHNPEGTR IKARVPVALA ASLRQYAAD // ID A0A024P230_9BACI Unreviewed; 411 AA. AC A0A024P230; DT 09-JUL-2014, integrated into UniProtKB/TrEMBL. DT 09-JUL-2014, sequence version 1. DT 07-JUN-2017, entry version 25. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:CDQ22118.1}; GN ORFNames=BN983_00321 {ECO:0000313|EMBL:CDQ22118.1}; OS Halobacillus karajensis. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Halobacillus. OX NCBI_TaxID=195088 {ECO:0000313|EMBL:CDQ22118.1, ECO:0000313|Proteomes:UP000028868}; RN [1] {ECO:0000313|EMBL:CDQ22118.1, ECO:0000313|Proteomes:UP000028868} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=HD-03 {ECO:0000313|EMBL:CDQ22118.1, RC ECO:0000313|Proteomes:UP000028868}; RA Urmite Genomes U.; RL Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:CDQ22118.1, ECO:0000313|Proteomes:UP000028868} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=HD-03 {ECO:0000313|EMBL:CDQ22118.1, RC ECO:0000313|Proteomes:UP000028868}; RA Khelaifia S., Croce O., Lagier J.C., Raoult D.; RT "Draft genome sequence of Halobacillus karajensis HK-03."; RL Submitted (MAY-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:CDQ22118.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CCDI010000001; CDQ22118.1; -; Genomic_DNA. DR RefSeq; WP_035505193.1; NZ_FNWW01000004.1. DR EnsemblBacteria; CDQ22118; CDQ22118; BN983_00321. DR Proteomes; UP000028868; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000028868}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000028868}. FT DOMAIN 197 358 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 163 190 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 411 AA; 46882 MW; 931F1ED30E2D7151 CRC64; MKGKELVVLV ARKDPFEQED RFQSSLEELQ SLTETADGEV CKIITQKRDR VHPATYLGEG KLQEIKEAAE ETEAELVIFN DELSPGQLRN IRDKIGVRVI DRSQLILDIF AGRARTKEGK LQVELAQLQY LLPRLSGQGT ALSRLGGGIG TRGPGETKLE TDRRHIQRRI DDIKKRLDAV VKQREQYRKR RKENRAFQVA IVGYTNAGKS TFFNRVTDSQ SFEEDLLFAT LDPLTRQMSL PSGFLALISD TVGFIQDLPT TLIAAFRSTL EEVTEADFVL HMVDASHPDH LQQEKTVLNL LDELGASHLP VLTVYNKKDL LQEDFIPHSF PSLTVSVHDP IDRKRVLHKI EEVLKEEWDE YDVFVPASEG KRLQQFKAYS MITSVTFYEE KEGYALHGFL HPEHPLKHQL L // ID A0A024QCE5_9BACI Unreviewed; 411 AA. AC A0A024QCE5; DT 09-JUL-2014, integrated into UniProtKB/TrEMBL. DT 09-JUL-2014, sequence version 1. DT 05-JUL-2017, entry version 23. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:CDQ39937.1}; GN ORFNames=BN990_02254 {ECO:0000313|EMBL:CDQ39937.1}; OS Virgibacillus massiliensis. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Virgibacillus. OX NCBI_TaxID=1462526 {ECO:0000313|EMBL:CDQ39937.1, ECO:0000313|Proteomes:UP000028875}; RN [1] {ECO:0000313|EMBL:CDQ39937.1, ECO:0000313|Proteomes:UP000028875} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Vm-5 {ECO:0000313|EMBL:CDQ39937.1, RC ECO:0000313|Proteomes:UP000028875}; RA Urmite Genomes U.; RL Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Proteomes:UP000028875} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Vm-5 {ECO:0000313|Proteomes:UP000028875}; RA Khelaifia S., Croce O., Lagier J.C., Raoult D.; RT "Draft genome sequence of Virgibacillus massiliensis Vm-5."; RL Submitted (MAY-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:CDQ39937.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CCDP010000001; CDQ39937.1; -; Genomic_DNA. DR RefSeq; WP_038244040.1; NZ_CCDP010000001.1. DR EnsemblBacteria; CDQ39937; CDQ39937; BN990_02254. DR Proteomes; UP000028875; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000028875}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000028875}. FT DOMAIN 196 357 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 411 AA; 46922 MW; D278628EF64D4E1E CRC64; MTKEKIVIIA VRKADQDEER FTSSIEELKS LSNTAGGEVI EVMTQKRERI HPATYIGSGK VTEINTVIDE LDIDLVISND ELSPGQLRNL ASLFGIRIID RSQLILDIFA KRARTKEGKL QVELAQLEYM LPRLRGQGTE MSRLGAGIGT RGPGETKLET DQRHIRRRIY EIKQRLQTVV KQREQYRKRR KTNDVFQIAI VGYTNAGKST LFNRLTNSRS LEEDQLFATL DPLTRQIKLP SGLEILITDT VGFLQDLPTS LIAAFKSTLE EVTEADFLIH MVDGSDPDLH QQQDTVIKLL EELDADTIPM LTVYNKKDQM NTAMIPINHP NILISALQPN DIDRLLQKIE ALLKTEWGYY AVSINPDQGK LLLQLEQQTI IESKQFDETD QVYQIKGYMR KHIPLNRLIE E // ID A0A024VPS2_PLAFA Unreviewed; 698 AA. AC A0A024VPS2; DT 09-JUL-2014, integrated into UniProtKB/TrEMBL. DT 09-JUL-2014, sequence version 1. DT 10-MAY-2017, entry version 12. DE SubName: Full=GTP-binding protein HflX {ECO:0000313|EMBL:ETW30462.1}; GN ORFNames=PFFCH_02111 {ECO:0000313|EMBL:ETW30462.1}; OS Plasmodium falciparum FCH/4. OC Eukaryota; Alveolata; Apicomplexa; Aconoidasida; Haemosporida; OC Plasmodiidae; Plasmodium; Plasmodium (Laverania). OX NCBI_TaxID=1036724 {ECO:0000313|EMBL:ETW30462.1, ECO:0000313|Proteomes:UP000030656}; RN [1] {ECO:0000313|EMBL:ETW30462.1, ECO:0000313|Proteomes:UP000030656} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=FCH/4 {ECO:0000313|EMBL:ETW30462.1, RC ECO:0000313|Proteomes:UP000030656}; RG The Broad Institute Genome Sequencing Platform; RG The Broad Institute Genome Sequencing Center for Infectious Disease; RA Neafsey D., Hoffman S., Volkman S., Rosenthal P., Walker B., RA Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B., RA Abouelleil A., Allen A.W., Alvarado L., Arachchi H.M., Berlin A.M., RA Chapman S.B., Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., RA Hansen M., Howarth C., Imamovic A., Ireland A., Larimer J., RA McCowan C., Murphy C., Pearson M., Poon T.W., Priest M., Roberts A., RA Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C., RA Birren B.; RT "The Genome Annotation of Plasmodium falciparum FCH/4."; RL Submitted (FEB-2013) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:ETW30462.1, ECO:0000313|Proteomes:UP000030656} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=FCH/4 {ECO:0000313|EMBL:ETW30462.1, RC ECO:0000313|Proteomes:UP000030656}; RG The Broad Institute Genome Sequencing Platform; RG The Broad Institute Genome Sequencing Center for Infectious Disease; RA Neafsey D., Cheeseman I., Volkman S., Adams J., Walker B., Young S.K., RA Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., RA Alvarado L., Arachchi H.M., Berlin A.M., Chapman S.B., Dewar J., RA Goldberg J., Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., RA Larimer J., McCowan C., Murphy C., Neiman D., Pearson M., Priest M., RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., RA Nusbaum C., Birren B.; RT "The Genome Sequence of Plasmodium falciparum FCH/4."; RL Submitted (FEB-2013) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; KI927911; ETW30462.1; -; Genomic_DNA. DR ProteinModelPortal; A0A024VPS2; -. DR SMR; A0A024VPS2; -. DR EnsemblProtists; ETW30462; ETW30462; PFFCH_02111. DR Proteomes; UP000030656; Unassembled WGS sequence. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000030656}; KW Reference proteome {ECO:0000313|Proteomes:UP000030656}. FT DOMAIN 459 629 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 698 AA; 81678 MW; FD385C7811AB7D0C CRC64; MGRILFLLKN VNKIEKRYFT NKSNIYYHNE SQKKEIIVLH PILKRSKNNS NKLFQEIIYD AQEALGLAKS ANFQIAKGIS MPLGGWYLKN EKQKKKNDPK NDKIDEGQVP NKELSQNNEH HHVFEKSEKE IPNEMSFTTD KSSSKYINYD EIERKVAESI LIKVNHIDNK FYFSKGKLNE LSKYYLKNPT PCIFINTLLS PEQFRNLEFL FNSLLKSYQD ELILNNKRER DNSEMYERVS DVKFDNCDSD DIIIDNSSYC LDAYNNFLDK EDEQCDDVDL EQNMNVLNEH IGDTSCEQAN DIPYEQISDT QECSKNIPMY VELFDRYSMI LYILKSRAKN NLSKLQLELA RANFVLNTYS EDSKSRMKYI KYIENNVLGG SCIDYEEKYT KLNFFTVGKQ NKKSNVNFSG YTSNYIKSNE TYKEYEKRII NNLYSKLKNE LIKCKNNMIL QNNSRKHKAI IAIVGYTNVG KTKLINYLTK SNLKARNLLF QTLDNAYKNL NISTCYSTIF VDSIGFIQNI PYSLYESFKI SLEAIKTADV IIHVIDVSHP YKDKHKKCVL ETLNKIGISD EFIKNNVIEV WNKIDKLTDN ELYTLCKNKP KNALPISAKY GTNCNYLIQI IEHLINQIKD VHILNLQFPT SEAKERINFL MKNYKVVPHS ISYSDDGNTT FIKLVENKSN LKKYYEKFEI KETYKSDN // ID A0A024W789_PLAFA Unreviewed; 698 AA. AC A0A024W789; DT 09-JUL-2014, integrated into UniProtKB/TrEMBL. DT 09-JUL-2014, sequence version 1. DT 05-JUL-2017, entry version 11. DE SubName: Full=GTP-binding protein HflX {ECO:0000313|EMBL:ETW36041.1}; GN ORFNames=PFTANZ_03266 {ECO:0000313|EMBL:ETW36041.1}; OS Plasmodium falciparum Tanzania (2000708). OC Eukaryota; Alveolata; Apicomplexa; Aconoidasida; Haemosporida; OC Plasmodiidae; Plasmodium; Plasmodium (Laverania). OX NCBI_TaxID=1036725 {ECO:0000313|EMBL:ETW36041.1, ECO:0000313|Proteomes:UP000030708}; RN [1] {ECO:0000313|EMBL:ETW36041.1, ECO:0000313|Proteomes:UP000030708} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Tanzania {ECO:0000313|EMBL:ETW36041.1}; RG The Broad Institute Genome Sequencing Platform; RG The Broad Institute Genome Sequencing Center for Infectious Disease; RA Neafsey D., Hoffman S., Volkman S., Rosenthal P., Walker B., RA Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B., RA Abouelleil A., Allen A.W., Alvarado L., Arachchi H.M., Berlin A.M., RA Chapman S.B., Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., RA Hansen M., Howarth C., Imamovic A., Ireland A., Larimer J., RA McCowan C., Murphy C., Pearson M., Poon T.W., Priest M., Roberts A., RA Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C., RA Birren B.; RT "The Genome Annotation of Plasmodium falciparum Tanzania (2000708)."; RL Submitted (FEB-2013) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:ETW36041.1, ECO:0000313|Proteomes:UP000030708} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Tanzania (2000708) {ECO:0000313|Proteomes:UP000030708}; RG The Broad Institute Genome Sequencing Platform; RG The Broad Institute Genome Sequencing Center for Infectious Disease; RA Neafsey D., Cheeseman I., Volkman S., Adams J., Walker B., Young S.K., RA Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., RA Alvarado L., Arachchi H.M., Berlin A.M., Chapman S.B., Dewar J., RA Goldberg J., Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., RA Larimer J., McCowan C., Murphy C., Neiman D., Pearson M., Priest M., RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., RA Nusbaum C., Birren B.; RT "The Genome Sequence of Plasmodium falciparum Tanzania (2000708)."; RL Submitted (FEB-2013) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; KI926440; ETW36041.1; -; Genomic_DNA. DR STRING; 5833.PF11_0143; -. DR EnsemblProtists; ETW36041; ETW36041; PFTANZ_03266. DR Proteomes; UP000030708; Unassembled WGS sequence. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000030708}; KW Reference proteome {ECO:0000313|Proteomes:UP000030708}. FT DOMAIN 459 629 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 698 AA; 81761 MW; 306606B5C7EC6D07 CRC64; MGRILFLLKN VNKIEKRYFT NKSNIYYHNE SQKKEIIVLH PILKRSKNNS NKLFQEIIYD AQEALGLAKS ANFQIAKGIS MPLGGWYLKN EKQKKKNDPK NDKIDEGQVP NKELSQNNEH HHVFEKSEKE IPNEMSFTTD KSSSKYINYD EIERKVAESI LIKVNHIDNK FYFSKGKLNE LSKYYLKNPT PCIFINTLLS PEQFRNLEFL FNSLLKSYQD ELILNNKRER DNSEMYERVS DVKFDNWDSD DIIIDNSSYC LDAYNNFLDK EDEQCDDVDL EQNMNVLNEH IGDTSCEQAN DIPYEQISDT QECSKNIPMY VELFDRYSMI LYILKSRAKN NLSKLQLELA RANFVLNTYS EDSKSRMKYI KYIENNVLGG SCIDYEEKYT KLNFFTVGKQ NKKSNVNFSG YTSNYIKSNE TYKEYEKRII NNLYSKLKNE LIKCKNNMIL QNNSRKHKAI IAIVGYTNVG KTKLINYLTK SNLKARNLLF QTLDNAYKNL NISTCYSTIF VDSIGFIQNI PYSLYESFKI SLEAIKTADV IIHVIDVSHP YKDKHKKCVL ETLNKIGISD EFIKNNVIEV WNKIDKLTDN ELYTLCKNKP KNALPISAKY GTNCNYLIQI IEHLINQIKD VHILNLQFPT SEAKERINFL MKNYKVVPHS ISYSDDGNTT FIKLVENKSN LKKYYEKFEI KETYKSDN // ID A0A024WN60_PLAFA Unreviewed; 698 AA. AC A0A024WN60; DT 09-JUL-2014, integrated into UniProtKB/TrEMBL. DT 09-JUL-2014, sequence version 1. DT 10-MAY-2017, entry version 10. DE SubName: Full=GTP-binding protein HflX {ECO:0000313|EMBL:ETW48669.1}; GN ORFNames=PFMALIP_03208 {ECO:0000313|EMBL:ETW48669.1}; OS Plasmodium falciparum MaliPS096_E11. OC Eukaryota; Alveolata; Apicomplexa; Aconoidasida; Haemosporida; OC Plasmodiidae; Plasmodium; Plasmodium (Laverania). OX NCBI_TaxID=1036727 {ECO:0000313|EMBL:ETW48669.1, ECO:0000313|Proteomes:UP000030699}; RN [1] {ECO:0000313|EMBL:ETW48669.1, ECO:0000313|Proteomes:UP000030699} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MaliPS096_E11 {ECO:0000313|EMBL:ETW48669.1, RC ECO:0000313|Proteomes:UP000030699}; RG The Broad Institute Genome Sequencing Platform; RG The Broad Institute Genome Sequencing Center for Infectious Disease; RA Neafsey D., Hoffman S., Volkman S., Rosenthal P., Walker B., RA Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B., RA Abouelleil A., Allen A.W., Alvarado L., Arachchi H.M., Berlin A.M., RA Chapman S.B., Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., RA Hansen M., Howarth C., Imamovic A., Ireland A., Larimer J., RA McCowan C., Murphy C., Pearson M., Poon T.W., Priest M., Roberts A., RA Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C., RA Birren B.; RT "The Genome Annotation of Plasmodium falciparum MaliPS096_E11."; RL Submitted (FEB-2013) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:ETW48669.1, ECO:0000313|Proteomes:UP000030699} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MaliPS096_E11 {ECO:0000313|EMBL:ETW48669.1, RC ECO:0000313|Proteomes:UP000030699}; RG The Broad Institute Genome Sequencing Platform; RG The Broad Institute Genome Sequencing Center for Infectious Disease; RA Neafsey D., Cheeseman I., Volkman S., Adams J., Walker B., Young S.K., RA Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., RA Alvarado L., Arachchi H.M., Berlin A.M., Chapman S.B., Dewar J., RA Goldberg J., Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., RA Larimer J., McCowan C., Murphy C., Neiman D., Pearson M., Priest M., RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., RA Nusbaum C., Birren B.; RT "The Genome Sequence of Plasmodium falciparum MaliPS096_E11."; RL Submitted (FEB-2013) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; KI925567; ETW48669.1; -; Genomic_DNA. DR EnsemblProtists; ETW48669; ETW48669; PFMALIP_03208. DR Proteomes; UP000030699; Unassembled WGS sequence. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000030699}; KW Reference proteome {ECO:0000313|Proteomes:UP000030699}. FT DOMAIN 459 629 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 698 AA; 81678 MW; 1E8067FDC3A04BF4 CRC64; MGRILFLLKN VNKIEKRYFT NKSNIYYHNE SQKKEIIVLH PILKRSKNNS NKLFQEIIYD AQEALGLAKS ANFQIAKGIS MPLGGWYLKN EKKKKKNDPK NDKIDEGQVP NKELSQNNEH HHVFEKSEKE IPNEMSFTTD KSSSKYINYD EIERKVAESI LIKVNHIDNK FYFSKGKLNE LSKYYLKNPT PCIFINTLLS PEQFRNLEFL FNSLLKSYQD ELILNNKRER DNSEMYERVS DVKFDNCDSD DIIIDNSSYC LDAYNNFLDK EDEQCDDVDL EQNMNVLNEH IGDTSCEQAN DIPYEQISDT QECSKNIPMY VELFDRYSMI LYILKSRAKN NLSKLQLELA RANFVLNTYS EDSKSRMKYI KYIENNVLGG SCIDYEEKYT KLNFFTVGKQ NKKSNVNFSG YTSNYIKSNE TYKEYEKRII NNLYSKLKNE LIKCKNNMIL QNNSRKHKAI IAIVGYTNVG KTKLINYLTK SNLKARNLLF QTLDNAYKNL NISTCYSTIF VDSIGFIQNI PYSLYESFKI SLEAIKTADV IIHVIDVSHP YKDKHKKCVL ETLNKIGISD EFIKNNVIEV WNKIDKLTDN ELYTLCKNKP KNALPISAKY GTNCNYLIQI IEHLINQIKD VHILNLQFPT SEAKERINFL MKNYKVVPHS ISYSDDGNTT FIKLVENKSN LKKYYEKFEI KETYKSDN // ID A0A026WEB0_CERBI Unreviewed; 483 AA. AC A0A026WEB0; DT 09-JUL-2014, integrated into UniProtKB/TrEMBL. DT 09-JUL-2014, sequence version 1. DT 07-JUN-2017, entry version 15. DE SubName: Full=Putative GTP-binding protein {ECO:0000313|EMBL:EZA54402.1}; GN ORFNames=X777_05632 {ECO:0000313|EMBL:EZA54402.1}; OS Cerapachys biroi (Ant). OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; OC Pterygota; Neoptera; Holometabola; Hymenoptera; Apocrita; Aculeata; OC Vespoidea; Formicidae; Cerapachyinae; Cerapachyini; Cerapachys. OX NCBI_TaxID=443821 {ECO:0000313|EMBL:EZA54402.1, ECO:0000313|Proteomes:UP000053097}; RN [1] {ECO:0000313|EMBL:EZA54402.1, ECO:0000313|Proteomes:UP000053097} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=24508170; DOI=10.1016/j.cub.2014.01.018; RA Oxley P.R., Ji L., Fetter-Pruneda I., McKenzie S.K., Li C., Hu H., RA Zhang G., Kronauer D.J.; RT "The genome of the clonal raider ant Cerapachys biroi."; RL Curr. Biol. 24:451-458(2014). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; KK107250; EZA54402.1; -; Genomic_DNA. DR RefSeq; XP_011338694.1; XM_011340392.2. DR GeneID; 105280133; -. DR OMA; MDTVGFM; -. DR Proteomes; UP000053097; Unassembled WGS sequence. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR CDD; cd01878; HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000053097}; KW Reference proteome {ECO:0000313|Proteomes:UP000053097}. FT DOMAIN 265 425 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 483 AA; 54670 MW; F9C6BB81FE81E511 CRC64; MHCVRKILNI AQCNFQAYSK TEFADTVCKR SGILLQNVVC RFKHDSGEHQ SFEGEAEEHE YTELSNYCLG TATGGHRTFI LQPYIKWGRD KKRNTSPELQ LAEAVALINT LPNWCVVGTK YAPLLTLQRK TLLGTGSMND LKQQISQCGD VSAVFVSTNM LRFRQIAQLR EILGLPIYDR YSIVVHIFRR HAQSAEAKLQ VTLAEIPYIR KKLFETCVTK SGAINVTEKT KLLLDGREKR LRSELKRLQQ HRQLIRRSRK KNGFPTIAVI GYTNAGKTSL IRALTDDSSL RPKNKLFATL DTTAHQGILL NKLKVLYMDT IGFIQDVPES LIEPFIVTLE DAMIADVIVH VYDVSHPDVK AQYQHVQQTV KPMIDTERPI IDVANKCDLV TSDCIPKDVI AVSAKNLTGI DLLRLKIEKI LLAVTGLLRT RVRVESGSSA ASWLYKMTTV INAQPDPDNP QYMIFEVLAT SLDIQKFKQF LRQ // ID A0A031FL78_9MICO Unreviewed; 504 AA. AC A0A031FL78; DT 09-JUL-2014, integrated into UniProtKB/TrEMBL. DT 09-JUL-2014, sequence version 1. DT 07-JUN-2017, entry version 21. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:EZP25348.1}; GN ORFNames=BW34_02803 {ECO:0000313|EMBL:EZP25348.1}; OS Microbacterium oleivorans. OC Bacteria; Actinobacteria; Micrococcales; Microbacteriaceae; OC Microbacterium. OX NCBI_TaxID=273677 {ECO:0000313|EMBL:EZP25348.1, ECO:0000313|Proteomes:UP000024001}; RN [1] {ECO:0000313|EMBL:EZP25348.1, ECO:0000313|Proteomes:UP000024001} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=RIT293 {ECO:0000313|EMBL:EZP25348.1, RC ECO:0000313|Proteomes:UP000024001}; RA Gan H.Y., Gan H.M., Savka M.A., Hudson A.O.; RT "Draft Genome Sequences of 13 Willow Endophytes."; RL Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EZP25348.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JFYO01000011; EZP25348.1; -; Genomic_DNA. DR RefSeq; WP_036313729.1; NZ_JFYO01000011.1. DR EnsemblBacteria; EZP25348; EZP25348; BW34_02803. DR PATRIC; fig|273677.3.peg.2774; -. DR Proteomes; UP000024001; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000024001}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000024001}. FT DOMAIN 286 451 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 504 AA; 54550 MW; 54FEAB79ADA8E9FF CRC64; MTDTTTPAAT DEPVDPVDRV LAHAEARSGV RVFGAAQALQ DQSTVAYGDT DGDQWDREER AALRRVPGLS TELEDVTEVE YRQLRLENVV LVGVYPQGST EDAENSLREL AALAETAGAV VLDGVLQRRP TPDPATYIGR GKAAELRELV VAVGADTVIA DTELAPSQRR ALEDVVKVKV IDRTTVILDI FSQHAKSREG KAQVELAQLE YLLPRLRGWG DSMSRQAGGQ VGAGGAGMGS RGPGETKIEL DRRRIRTRMA MLRRQIRDYK PAREAKRAER RRNTIPSVAI AGYTNAGKSS LLNRLTSAGV LVENALFATL DATVRRAQAA DGRVYTLTDT VGFVRNLPHQ LVEAFRSTLE EVGDADVIVH VVDGSHPDPA AQLATVRDVM GDVGARSTNE IVVFNKADLI DPDTRLVLRG LEPKAHFVSS RTGEGVAELR ATIEEALPLP AVEVHALVPY DRGDLVNAVH ESGHILSTRH EEGGTAVHAH VSERLAAELA PYSR // ID A0A031LIC4_9GAMM Unreviewed; 443 AA. AC A0A031LIC4; DT 09-JUL-2014, integrated into UniProtKB/TrEMBL. DT 09-JUL-2014, sequence version 1. DT 30-AUG-2017, entry version 22. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=CL42_14630 {ECO:0000313|EMBL:EZQ01245.1}; OS Acinetobacter sp. Ver3. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Moraxellaceae; Acinetobacter. OX NCBI_TaxID=466088 {ECO:0000313|EMBL:EZQ01245.1, ECO:0000313|Proteomes:UP000023816}; RN [1] {ECO:0000313|EMBL:EZQ01245.1, ECO:0000313|Proteomes:UP000023816} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Ver3 {ECO:0000313|EMBL:EZQ01245.1, RC ECO:0000313|Proteomes:UP000023816}; RA Kurth D.G., Ordonez O.F., Albarracin V.H., Revale S., Farias M.E.; RT "Polyextremophylic features in the genome of Acinetobacter sp. Ver3 RT isolated from a high altitude andean lake."; RL Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EZQ01245.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JFYL01000080; EZQ01245.1; -; Genomic_DNA. DR RefSeq; WP_035270005.1; NZ_JFYL01000080.1. DR EnsemblBacteria; EZQ01245; EZQ01245; CL42_14630. DR Proteomes; UP000023816; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000023816}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000023816}. FT DOMAIN 199 364 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 443 AA; 49815 MW; A50A4EE245099B65 CRC64; MEVTGQNQAN ERAVLVSVNV QILEDLDQEE FRLLAKSAGA EILEHIQAQR IKPDPKFFIG SGKAEEIAEF VAAVEADIVI FDHSLTPSQE RNLERVIQCR VIDRTRLILD IFAQRARTHE GKLQVELAQL DHLASRLVGG RMGLDGQKGG IGLRGPGETQ LETDRRLLRH RITQLKDKLE KVRQTRIQGR AARQKASIPT VSLVGYTNAG KSTLFNILAE SDVYAADQLF ATLDPTLRRL NWDGIGTLVL ADTVGFVRNL AHSLVESFKA TLEETLEATL LLHVIDSNSP EKLEQIDAVE KVLKEIGAQV PILRVYNKID QTGEEPKIIY ASPNLPDRVY VSAHSSQGLD LLRQAVQECL MGQIQQFELT LRPEYGKLRN QLYELNVIQS EHYDDLGHLI LNIQIAPHKL EQLIKQAHLP IDQILGDKAQ QFKRPLEEFE IKS // ID A0A033V3X9_STAAU Unreviewed; 412 AA. AC A0A033V3X9; DT 09-JUL-2014, integrated into UniProtKB/TrEMBL. DT 09-JUL-2014, sequence version 1. DT 07-JUN-2017, entry version 21. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=V070_00360 {ECO:0000313|EMBL:EZX25862.1}; OS Staphylococcus aureus C0673. OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae; OC Staphylococcus. OX NCBI_TaxID=1413510 {ECO:0000313|EMBL:EZX25862.1, ECO:0000313|Proteomes:UP000024810}; RN [1] {ECO:0000313|EMBL:EZX25862.1, ECO:0000313|Proteomes:UP000024810} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C0673 {ECO:0000313|EMBL:EZX25862.1, RC ECO:0000313|Proteomes:UP000024810}; RG The Broad Institute Genomics Platform; RG The Broad Institute Genome Sequencing Center for Infectious Disease; RA Feldgarden M., Price L., Nordstrom L., Larsen J., Contente-Cuomo T., RA Andersen P., Young S., Zeng Q., Gargeya S., Abouelleil A., RA Alvarado L., Chapman S.B., Gainer-Dewar J., Goldberg J., Griggs A., RA Gujja S., Hansen M., Howarth C., Imamovic A., Larimer J., Murphy C., RA Naylor J., Pearson M., Poon T.W., Priest M., Roberts A., Saif S., RA Shea T., Sykes S., Wortman J., Nusbaum C., Birren B.; RT "The Genome Sequence of Staphylococcus aureus C0673."; RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EZX25862.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JIZS01000003; EZX25862.1; -; Genomic_DNA. DR RefSeq; WP_037587882.1; NZ_KK222745.1. DR EnsemblBacteria; EZX25862; EZX25862; V070_00360. DR PATRIC; fig|1413510.3.peg.352; -. DR Proteomes; UP000024810; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000024810}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000024810}. FT DOMAIN 207 368 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 412 AA; 47351 MW; D34924CBF2D0D006 CRC64; MKNDMKSTKQ ETEQVILLAI HDKKDDEATF KSTVQELESL AVTSQLEVME VFTQKRERPD QQYYFGKGKI EEVIEYIEMN DIKVNAVIAN DELTTAQSKH LDELFNTKII DRTQLILEIF AQRASSREGQ LQVELAQLDY LLPRLSGHGK SLSRLGGGIG TRGPGETKLE TDRRHIRTRM NEIKHQLETI VSHRSRYRER RQHNQAYQVA LIGYTNAGKS SWFNQLSNDE TFEQDLLFAT LDPKSRAITI NDGFNVILSD TVGFIQKLPT TLIAAFKSTL EEAKYAQLLV HVVDASHPHY MEQYETVMTL VNQLDMGHIP MLVVFNKKDL APSNHSAISG QSIFVSAKDS NDKAIFKEKL VDMIKETMDY YEMDIPSSDA DKLYWQKTHT LVEKMDFDEE TETYHIKGYK QK // ID A0A037ZDQ0_CLOTT Unreviewed; 594 AA. AC A0A037ZDQ0; DT 09-JUL-2014, integrated into UniProtKB/TrEMBL. DT 09-JUL-2014, sequence version 1. DT 07-JUN-2017, entry version 23. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=CTM_00290 {ECO:0000313|EMBL:KAJ53661.1}; OS Clostridium tetanomorphum DSM 665. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=1230342 {ECO:0000313|EMBL:KAJ53661.1, ECO:0000313|Proteomes:UP000025063}; RN [1] {ECO:0000313|Proteomes:UP000025063} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 665 {ECO:0000313|Proteomes:UP000025063}; RA Bao G., Dong H., Zhang Y., Li Y.; RT "Clostridium tetanomorphum DSM 665 genome sequence."; RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KAJ53661.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; APJS01000002; KAJ53661.1; -; Genomic_DNA. DR EnsemblBacteria; KAJ53661; KAJ53661; CTM_00290. DR PATRIC; fig|1230342.3.peg.58; -. DR Proteomes; UP000025063; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000025063}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000025063}. FT DOMAIN 362 539 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 594 AA; 67039 MW; 56FBE7DE7165BC3B CRC64; MISGNIEGIR DILLEKLEKI YDIKVPKDEV FNIELLNIIS EVTSNIGREV SVAIDRKGNV VDVALGDSTT VEVPIIDIKE KRLSAIRVIH THPNGNSRLS ALDVSALIKL KLDCIGAIGV DETGVTNVTL GFCGIENDLL VAEITKEMTI EETMRFNLLD KVRYAEESIK LNRVEEDNSE KAILVGVESE ESLEELEELA KACNVITVEK VLQKRYKVDS AFYVGKGKVE EIALLRQARK ANVVIFDDEL TASQVRNLED FIGVKVIDRT TLILEIFAKR AKSKDGKIQV ELAQLKYRLP RLSGLGTVLS RTGGGIGTRG PGEKKLETDK RHIRERIYDL TKELEKIKKT RETQRDNRND IPKVSLVGYT NAGKSTLRNV LYNMYPAKEG IQKENVFEAD MLFATLDTTT RAILLPNNRN ITLTDTVGFI RKLPHDLVEA FKSTLEEVIY SDVLLHVVDI SSDSYEEQIQ AVNEVLKELS CLDKPTILLL NKVDKINEEK LSDIREKFKT LDCIEISAKQ GRNLEKLLEE IINKLPYKLI KAEYLIPYSD GSTVAYLHRN GNINIEEYKE EGTYISAEVD EKAYNVCKKY MISE // ID A0A037ZMJ5_9RHOB Unreviewed; 424 AA. AC A0A037ZMJ5; DT 09-JUL-2014, integrated into UniProtKB/TrEMBL. DT 09-JUL-2014, sequence version 1. DT 07-JUN-2017, entry version 21. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=ACMU_07485 {ECO:0000313|EMBL:KAJ56772.1}; OS Actibacterium mucosum KCTC 23349. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae; Actibacterium. OX NCBI_TaxID=1454373 {ECO:0000313|EMBL:KAJ56772.1, ECO:0000313|Proteomes:UP000026249}; RN [1] {ECO:0000313|EMBL:KAJ56772.1, ECO:0000313|Proteomes:UP000026249} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=KCTC 23349 {ECO:0000313|EMBL:KAJ56772.1, RC ECO:0000313|Proteomes:UP000026249}; RA Arahal D.R., Shao Z., Lai Q., Pujalte M.J.; RT "Draft Genome Sequence of Actibacterium mucosum KCTC 23349, a Marine RT Alphaproteobacterium with Complex Ionic Requirements Isolated from RT Mediterranean Seawater at Malvarrosa Beach, Valencia, Spain."; RL Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KAJ56772.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JFKE01000002; KAJ56772.1; -; Genomic_DNA. DR RefSeq; WP_035257098.1; NZ_JFKE01000002.1. DR EnsemblBacteria; KAJ56772; KAJ56772; ACMU_07485. DR Proteomes; UP000026249; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000026249}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000026249}. FT DOMAIN 204 377 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 424 AA; 46990 MW; 9520DD76D4A7AC19 CRC64; MEEHSTRPTR AWVLHPDISS DRARRAAGPA LAEAVSLAAA LPHLEIAGAE VVPLPKVRPG LLFGSGKIEE LAAKFKANEV DLVLVDGPVT PVQQRNLEKE WKVKLLDRTG LILEIFADRA RTREGVLQVE LAALSYQRTR LVRAWTHLER QRGGLGFVGG PGETQIEADR RAIDEAITRI RRQLAKVVKT RDLHRAARKK VPFPIVALVG YTNAGKSTLF NRLTGAEVLA KDMLFATLDP TMRAVELPTG KKVILSDTVG FISDLPTQLV AAFRATLEEV LEADLICHVR DIAADETEEQ AADVETILTE LGVRENVPRI EVWNKTDLLP DDQREALSKR AERAEDIFAL SAYEGTGLTP WIEAVTAALD DARHDSTLNL PYADGRRRAW LYDQGVVRDE VQGEDGVTLQ VHWTARQEKA FRGL // ID A0A044U5S5_ONCVO Unreviewed; 494 AA. AC A0A044U5S5; DT 09-JUL-2014, integrated into UniProtKB/TrEMBL. DT 08-JUN-2016, sequence version 2. DT 07-JUN-2017, entry version 20. DE SubName: Full=Uncharacterized protein {ECO:0000313|EnsemblMetazoa:OVOC6270}; OS Onchocerca volvulus. OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Spirurida; OC Filarioidea; Onchocercidae; Onchocerca. OX NCBI_TaxID=6282 {ECO:0000313|EnsemblMetazoa:OVOC6270, ECO:0000313|Proteomes:UP000024404}; RN [1] {ECO:0000313|EnsemblMetazoa:OVOC6270, ECO:0000313|Proteomes:UP000024404} RP NUCLEOTIDE SEQUENCE. RA Cotton J., Tsai J., Stanley E., Tracey A., Holroyd N., Lustigman S., RA Berriman M.; RT "Genome sequencing of Onchocerca volvulus."; RL Submitted (OCT-2013) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EnsemblMetazoa:OVOC6270} RP IDENTIFICATION. RG EnsemblMetazoa; RL Submitted (MAY-2014) to UniProtKB. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CBVM010000170; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EnsemblMetazoa; OVOC6270; OVOC6270; WBGene00243079. DR OrthoDB; EOG091G0852; -. DR Proteomes; UP000024404; Unassembled WGS sequence. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR CDD; cd01878; HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000024404}; KW Reference proteome {ECO:0000313|Proteomes:UP000024404}. FT DOMAIN 251 414 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 494 AA; 56469 MW; 8E3F40E81C1604B1 CRC64; MLLSKNFAKI FTSLHFERCL CTKIPEGTIQ RNDEFNIISK SYGIQDITPG GHRILLIHPR LRRGRFFDLN PTKAKLQLEE AVALVNTLPK FKVIETTAIS TDRSTKKKRL WGKGRLERII ALYEKINATA LMIDVDILSP KQQAELTSIF RIPVYDRYST VLLIFKMFAK TKEAKLQIEL AEIPYIRQRL LSMYELRTNP STFHLDTSEK SKAEKLEVLR YREQHLRKCL KAAVEEKVNL RIGEAQKNIR IVVAVVGYTN AGKSSLIKRL TGRDLYVEDR LFATLDTSLH VFRLPSGLSI LFADTIGFIS NLPTQLLASF QATLNHVANA DLLLHVEDVS NPDYLSQRDV VMKTLSLLKI RSELLNSVIR VGNKIDKLNQ LPPGEPNTYF VSCADGRGFV ELMAAVDKRV LTISGITIRR LKLRPHSEAF SYLCKYSFLV GQPVPSEDNN YLLCNVIMDD NEFSRNLNER KELQYLPFMI PLVKVLEKIT ISIR // ID A0A045JG23_MYCTX Unreviewed; 495 AA. AC A0A045JG23; DT 09-JUL-2014, integrated into UniProtKB/TrEMBL. DT 09-JUL-2014, sequence version 1. DT 05-JUL-2017, entry version 33. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:CNM75678.1}; GN ORFNames=ERS023446_01182 {ECO:0000313|EMBL:CNM75678.1}, GN SAMEA2682864_02052 {ECO:0000313|EMBL:SGM24965.1}, GN SAMEA2683035_01675 {ECO:0000313|EMBL:SGH64896.1}; OS Mycobacterium tuberculosis. OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae; OC Mycobacterium; Mycobacterium tuberculosis complex. OX NCBI_TaxID=1773 {ECO:0000313|EMBL:CNM75678.1, ECO:0000313|Proteomes:UP000039953}; RN [1] {ECO:0000313|EMBL:CNM75678.1, ECO:0000313|Proteomes:UP000039953} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=A70144_2 {ECO:0000313|EMBL:CNM75678.1, RC ECO:0000313|Proteomes:UP000039953}; RA Murphy D.; RL Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:SGH64896.1, ECO:0000313|Proteomes:UP000182946, ECO:0000313|Proteomes:UP000183655} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=2926STDY5723616 {ECO:0000313|EMBL:SGM24965.1, RC ECO:0000313|Proteomes:UP000183655}, and RC 2926STDY5723788 {ECO:0000313|EMBL:SGH64896.1, RC ECO:0000313|Proteomes:UP000182946}; RG Pathogen Informatics; RL Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CQGE01000018; CNM75678.1; -; Genomic_DNA. DR EMBL; FPTZ01000009; SGH64896.1; -; Genomic_DNA. DR EMBL; FPXX01000011; SGM24965.1; -; Genomic_DNA. DR RefSeq; WP_003413984.1; NZ_NCKT01000009.1. DR EnsemblBacteria; AMC47177; AMC47177; RN05_2901. DR EnsemblBacteria; CNM75678; CNM75678; ERS023446_01182. DR EnsemblBacteria; CNY23755; CNY23755; ERS013471_00923. DR PATRIC; fig|1773.206.peg.2238; -. DR Proteomes; UP000039953; Unassembled WGS sequence. DR Proteomes; UP000182946; Unassembled WGS sequence. DR Proteomes; UP000183655; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000039953, KW ECO:0000313|Proteomes:UP000182946, ECO:0000313|Proteomes:UP000183655}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}. FT DOMAIN 271 440 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 495 AA; 53328 MW; F82BA93092945121 CRC64; MPANSDARPA ATCHHRVLAM TYPDPPQTGL SDFTPSLGEL ALEDRSALRR VAGLSTELAD VSEVEYRQLR LERVVLVGVW TEGSAADNRA SLAELAALAE TAGSQVLEGL IQRRDKPDPS TYIGSGKAAE LREVIVATGA DTVICDGELS PAQLTALEKA VQVKVIDRTA LILDIFAQHA TSREGKAQVS LAQMEYMLPR LRGWGESMSR QAGGRAGGSG GGVGLRGPGE TKIETDRRRI RERMAKLRRD IRAMKQVRDT QRSRRRHSDV PSIAIVGYTN AGKSSLLNAL TGAGVLVQDA LFATLEPTTR RAEFGDGRPV VLTDTVGFVR HLPTQLVEAF RSTLEEVVHA DLLVHVVDGS DGHPLAQIDA VRQVISEVIA DHDGDPPPEL LVVNKVDVAS DLMLAKLRHG LPGAVFVSAR TGDGIDALRR RMAELVVPAD TAVDVVIPYD RGDLVARVHA DGRIQQAEHK PEGTRIKARV PEALAATLRE FAPRA // ID A0A058ZRA8_9RHOB Unreviewed; 412 AA. AC A0A058ZRA8; DT 09-JUL-2014, integrated into UniProtKB/TrEMBL. DT 09-JUL-2014, sequence version 1. DT 07-JUN-2017, entry version 20. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=ATO10_03155 {ECO:0000313|EMBL:KCV83725.1}; OS Actibacterium atlanticum. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae; Actibacterium. OX NCBI_TaxID=1461693 {ECO:0000313|EMBL:KCV83725.1, ECO:0000313|Proteomes:UP000024836}; RN [1] {ECO:0000313|EMBL:KCV83725.1, ECO:0000313|Proteomes:UP000024836} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=22II-S11-Z10 {ECO:0000313|Proteomes:UP000024836}; RA Lai Q., Li G., Shao Z.; RT "Shimia sp. 22II-S11-Z10 Genome Sequencing."; RL Submitted (APR-2013) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KCV83725.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AQQY01000001; KCV83725.1; -; Genomic_DNA. DR EnsemblBacteria; KCV83725; KCV83725; ATO10_03155. DR PATRIC; fig|1461693.3.peg.652; -. DR Proteomes; UP000024836; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000024836}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000024836}. FT DOMAIN 192 361 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 412 AA; 45679 MW; A30E8624E1826E43 CRC64; MLHPDIHSDR ERRPAAPALE EAVSLALALP HLEVVGSDVV PLPKARPGLL FGPGKIEELA AKFKAHEVDL VLVDGPVTPV QQRNLEKEWK VKLLDRTGLI LEIFADRART REGVLQVELA ALSYQRTRLV RAWTHLERQR GGLGFVGGPG ETQVEADRRA IDEAIVRIKR QLSKVVKTRD LHRAARKKVP FPIVALVGYT NAGKSSLFNY LTGAEVMAKD MLFATLDPTM RAVTLPTGKE VILSDTVGFI SDLPTQLVAA FRATLEEVLE ADLILHVRDI AHPDSADQAT DVLAILNDLG VAEDTKQIEV WNKIDLLDPG DREGLQVKAD REEKIFTMSA ITGEGVDPLM QAVTDALDDE RFTAEVKLDF AQGKQRAWLF NEGIVEHEVQ DEEGYTLTVH WTARQEKAFK GL // ID A0A059B124_EUCGR Unreviewed; 597 AA. AC A0A059B124; DT 09-JUL-2014, integrated into UniProtKB/TrEMBL. DT 09-JUL-2014, sequence version 1. DT 07-JUN-2017, entry version 16. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:KCW59591.1}; GN ORFNames=EUGRSUZ_H02336 {ECO:0000313|EMBL:KCW59591.1}; OS Eucalyptus grandis (Flooded gum). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae; OC Pentapetalae; rosids; malvids; Myrtales; Myrtaceae; Myrtoideae; OC Eucalypteae; Eucalyptus. OX NCBI_TaxID=71139 {ECO:0000313|EMBL:KCW59591.1, ECO:0000313|Proteomes:UP000030711}; RN [1] {ECO:0000313|Proteomes:UP000030711} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=24919147; DOI=10.1038/nature13308; RA Myburg A.A., Grattapaglia D., Tuskan G.A., Hellsten U., Hayes R.D., RA Grimwood J., Jenkins J., Lindquist E., Tice H., Bauer D., RA Goodstein D.M., Dubchak I., Poliakov A., Mizrachi E., Kullan A.R., RA Hussey S.G., Pinard D., van der Merwe K., Singh P., van Jaarsveld I., RA Silva-Junior O.B., Togawa R.C., Pappas M.R., Faria D.A., RA Sansaloni C.P., Petroli C.D., Yang X., Ranjan P., Tschaplinski T.J., RA Ye C.Y., Li T., Sterck L., Vanneste K., Murat F., Soler M., RA Clemente H.S., Saidi N., Cassan-Wang H., Dunand C., Hefer C.A., RA Bornberg-Bauer E., Kersting A.R., Vining K., Amarasinghe V., Ranik M., RA Naithani S., Elser J., Boyd A.E., Liston A., Spatafora J.W., RA Dharmwardhana P., Raja R., Sullivan C., Romanel E., Alves-Ferreira M., RA Kulheim C., Foley W., Carocha V., Paiva J., Kudrna D., RA Brommonschenkel S.H., Pasquali G., Byrne M., Rigault P., Tibbits J., RA Spokevicius A., Jones R.C., Steane D.A., Vaillancourt R.E., RA Potts B.M., Joubert F., Barry K., Pappas G.J., Strauss S.H., RA Jaiswal P., Grima-Pettenati J., Salse J., Van de Peer Y., RA Rokhsar D.S., Schmutz J.; RT "The genome of Eucalyptus grandis."; RL Nature 509:356-362(2014). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; KK198760; KCW59591.1; -; Genomic_DNA. DR RefSeq; XP_010023336.1; XM_010025034.2. DR GeneID; 104414041; -. DR KEGG; egr:104414041; -. DR Proteomes; UP000030711; Unassembled WGS sequence. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR CDD; cd01878; HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000030711}; KW Reference proteome {ECO:0000313|Proteomes:UP000030711}. FT DOMAIN 305 564 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 597 AA; 65710 MW; 2771D513867A8588 CRC64; MLRTASSLCR RHLAPLPTPL RPPSPFQFLA RPFSRTWTRG GDGGGEDGGG GGGGGGGESL INRDPRSPPR LFVVQPRIRP DTLLRAKLDE ALCLANSLED QRDGFFDTDF LDKALPPHAL VQNPLVRSHR ARADTYFGPG TVDTIKIHLN EAETKGEVDA VFVNTNLSGI QLRNLERRWG KPVLDRVGLI IEIFNAHAFT KEAKLQAELA ALMYKKTRLV RVRGPDGRYA FGVGGEAEVV SARGRGSGGH GFLSGAGESE LHLQRRRILE RRRVLESQIE EVRRTRASQR AGRKRHKDSH ECSLATVAVV GYTNAGKSTL VGALSDTDLY SDDRLFATLD PRLRSVILPS GRKVLLSDTV GFISDLPVQL VKAFQATLEE VIEADLLVHV LDSSAPNLDE HRSSVLQVLE QIGVSEEKLQ NMIEVWNKID LQEDDGSHFD ANDGEGATCT DVIDEDVISD GGDDCGEGEE SIDRLSEGEL EEIIESEEDQ YSDTWLSQED GIKWGSSICG DTSNNEPNAS LGEWRTKIVS DSAQAGPHVK TSAMTGVGLQ ELLELIDEKL ELQNDRSKRE NVVERSIFYS KWRPPRAEED ANVAVEQ // ID A0A059BPS0_EUCGR Unreviewed; 458 AA. AC A0A059BPS0; DT 09-JUL-2014, integrated into UniProtKB/TrEMBL. DT 09-JUL-2014, sequence version 1. DT 07-JUN-2017, entry version 11. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:KCW68192.1}; GN ORFNames=EUGRSUZ_F01859 {ECO:0000313|EMBL:KCW68192.1}; OS Eucalyptus grandis (Flooded gum). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae; OC Pentapetalae; rosids; malvids; Myrtales; Myrtaceae; Myrtoideae; OC Eucalypteae; Eucalyptus. OX NCBI_TaxID=71139 {ECO:0000313|EMBL:KCW68192.1, ECO:0000313|Proteomes:UP000030711}; RN [1] {ECO:0000313|Proteomes:UP000030711} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=24919147; DOI=10.1038/nature13308; RA Myburg A.A., Grattapaglia D., Tuskan G.A., Hellsten U., Hayes R.D., RA Grimwood J., Jenkins J., Lindquist E., Tice H., Bauer D., RA Goodstein D.M., Dubchak I., Poliakov A., Mizrachi E., Kullan A.R., RA Hussey S.G., Pinard D., van der Merwe K., Singh P., van Jaarsveld I., RA Silva-Junior O.B., Togawa R.C., Pappas M.R., Faria D.A., RA Sansaloni C.P., Petroli C.D., Yang X., Ranjan P., Tschaplinski T.J., RA Ye C.Y., Li T., Sterck L., Vanneste K., Murat F., Soler M., RA Clemente H.S., Saidi N., Cassan-Wang H., Dunand C., Hefer C.A., RA Bornberg-Bauer E., Kersting A.R., Vining K., Amarasinghe V., Ranik M., RA Naithani S., Elser J., Boyd A.E., Liston A., Spatafora J.W., RA Dharmwardhana P., Raja R., Sullivan C., Romanel E., Alves-Ferreira M., RA Kulheim C., Foley W., Carocha V., Paiva J., Kudrna D., RA Brommonschenkel S.H., Pasquali G., Byrne M., Rigault P., Tibbits J., RA Spokevicius A., Jones R.C., Steane D.A., Vaillancourt R.E., RA Potts B.M., Joubert F., Barry K., Pappas G.J., Strauss S.H., RA Jaiswal P., Grima-Pettenati J., Salse J., Van de Peer Y., RA Rokhsar D.S., Schmutz J.; RT "The genome of Eucalyptus grandis."; RL Nature 509:356-362(2014). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; KK198758; KCW68192.1; -; Genomic_DNA. DR Proteomes; UP000030711; Unassembled WGS sequence. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000030711}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000030711}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 413 432 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 326 389 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 458 AA; 51089 MW; FE8AD38D18A673D8 CRC64; MMASCSSLTS RPSPLVHGPW SSNPTSNGNR PILLSLKIRH FDPLRLAKAV RHGLGVVSPD NTAVEVEAPA IETQEVNDEV GGSLNGVAET QLGDNSKDGT TSSTRVKKKR EDDDNLDNRF QVRNGREVFE EKAYLVGVER KGDREESFGI DESLKELAQL ADTAGLMVVG STYQKLSSPN PRTYIGSGKV SEIKSAIHAL DVETVIFDDE LSPGQLRNLE KAFGGDVRVC DRTALILDIF NQRAATHEAA LQVALALMEY QLPRLTRMWT HLERQAGGQV KGMGEKQIEV DKRILRTQIG VLKKELDSVR KHRKQYRNRR TSVPVPVVSL VGYTNAGKST LLNRLTGANV LAEDRLFATL DPTTRRVQIK NGKEFLLTDT VGFIQKLPTM LVRWFIVHFH NLVKFVIIRT DLLLIYGVII MKMLVWVFSI VLGDELQFIY SLTTFTGCCF QSNIRGDI // ID A0A059BQ16_EUCGR Unreviewed; 393 AA. AC A0A059BQ16; DT 09-JUL-2014, integrated into UniProtKB/TrEMBL. DT 09-JUL-2014, sequence version 1. DT 07-JUN-2017, entry version 16. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:KCW68193.1}; GN ORFNames=EUGRSUZ_F01859 {ECO:0000313|EMBL:KCW68193.1}; OS Eucalyptus grandis (Flooded gum). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae; OC Pentapetalae; rosids; malvids; Myrtales; Myrtaceae; Myrtoideae; OC Eucalypteae; Eucalyptus. OX NCBI_TaxID=71139 {ECO:0000313|EMBL:KCW68193.1, ECO:0000313|Proteomes:UP000030711}; RN [1] {ECO:0000313|Proteomes:UP000030711} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=24919147; DOI=10.1038/nature13308; RA Myburg A.A., Grattapaglia D., Tuskan G.A., Hellsten U., Hayes R.D., RA Grimwood J., Jenkins J., Lindquist E., Tice H., Bauer D., RA Goodstein D.M., Dubchak I., Poliakov A., Mizrachi E., Kullan A.R., RA Hussey S.G., Pinard D., van der Merwe K., Singh P., van Jaarsveld I., RA Silva-Junior O.B., Togawa R.C., Pappas M.R., Faria D.A., RA Sansaloni C.P., Petroli C.D., Yang X., Ranjan P., Tschaplinski T.J., RA Ye C.Y., Li T., Sterck L., Vanneste K., Murat F., Soler M., RA Clemente H.S., Saidi N., Cassan-Wang H., Dunand C., Hefer C.A., RA Bornberg-Bauer E., Kersting A.R., Vining K., Amarasinghe V., Ranik M., RA Naithani S., Elser J., Boyd A.E., Liston A., Spatafora J.W., RA Dharmwardhana P., Raja R., Sullivan C., Romanel E., Alves-Ferreira M., RA Kulheim C., Foley W., Carocha V., Paiva J., Kudrna D., RA Brommonschenkel S.H., Pasquali G., Byrne M., Rigault P., Tibbits J., RA Spokevicius A., Jones R.C., Steane D.A., Vaillancourt R.E., RA Potts B.M., Joubert F., Barry K., Pappas G.J., Strauss S.H., RA Jaiswal P., Grima-Pettenati J., Salse J., Van de Peer Y., RA Rokhsar D.S., Schmutz J.; RT "The genome of Eucalyptus grandis."; RL Nature 509:356-362(2014). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; KK198758; KCW68193.1; -; Genomic_DNA. DR RefSeq; XP_010061265.1; XM_010062963.1. DR GeneID; 104448986; -. DR Proteomes; UP000030711; Unassembled WGS sequence. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000030711}; KW Reference proteome {ECO:0000313|Proteomes:UP000030711}. FT DOMAIN 166 332 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 393 AA; 44105 MW; CEEB9ACA4B287859 CRC64; MTTWIIGSKC GMEERLSSPN PRTYIGSGKV SEIKSAIHAL DVETVIFDDE LSPGQLRNLE KAFGGDVRVC DRTALILDIF NQRAATHEAA LQVALALMEY QLPRLTRMWT HLERQAGGQV KGMGEKQIEV DKRILRTQIG VLKKELDSVR KHRKQYRNRR TSVPVPVVSL VGYTNAGKST LLNRLTGANV LAEDRLFATL DPTTRRVQIK NGKEFLLTDT VGFIQKLPTM LVAAFRATLE EISESSLLVH VVDISHPLAE QQIEAVDNVL SELDVSSIPK LMVWNKVDKA KDPQKIKLEV ERREDVVCIS ALTGEGLEEF CDAVQDKVKD SMVWVEALVP FNKGELLSTI HQVGMVEKTE YMENGTLVKA HVPLRFARML TPMRQLHISE PHP // ID A0A059BQL4_EUCGR Unreviewed; 525 AA. AC A0A059BQL4; DT 09-JUL-2014, integrated into UniProtKB/TrEMBL. DT 09-JUL-2014, sequence version 1. DT 07-JUN-2017, entry version 12. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:KCW68191.1}; GN ORFNames=EUGRSUZ_F01859 {ECO:0000313|EMBL:KCW68191.1}; OS Eucalyptus grandis (Flooded gum). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae; OC Pentapetalae; rosids; malvids; Myrtales; Myrtaceae; Myrtoideae; OC Eucalypteae; Eucalyptus. OX NCBI_TaxID=71139 {ECO:0000313|EMBL:KCW68191.1, ECO:0000313|Proteomes:UP000030711}; RN [1] {ECO:0000313|Proteomes:UP000030711} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=24919147; DOI=10.1038/nature13308; RA Myburg A.A., Grattapaglia D., Tuskan G.A., Hellsten U., Hayes R.D., RA Grimwood J., Jenkins J., Lindquist E., Tice H., Bauer D., RA Goodstein D.M., Dubchak I., Poliakov A., Mizrachi E., Kullan A.R., RA Hussey S.G., Pinard D., van der Merwe K., Singh P., van Jaarsveld I., RA Silva-Junior O.B., Togawa R.C., Pappas M.R., Faria D.A., RA Sansaloni C.P., Petroli C.D., Yang X., Ranjan P., Tschaplinski T.J., RA Ye C.Y., Li T., Sterck L., Vanneste K., Murat F., Soler M., RA Clemente H.S., Saidi N., Cassan-Wang H., Dunand C., Hefer C.A., RA Bornberg-Bauer E., Kersting A.R., Vining K., Amarasinghe V., Ranik M., RA Naithani S., Elser J., Boyd A.E., Liston A., Spatafora J.W., RA Dharmwardhana P., Raja R., Sullivan C., Romanel E., Alves-Ferreira M., RA Kulheim C., Foley W., Carocha V., Paiva J., Kudrna D., RA Brommonschenkel S.H., Pasquali G., Byrne M., Rigault P., Tibbits J., RA Spokevicius A., Jones R.C., Steane D.A., Vaillancourt R.E., RA Potts B.M., Joubert F., Barry K., Pappas G.J., Strauss S.H., RA Jaiswal P., Grima-Pettenati J., Salse J., Van de Peer Y., RA Rokhsar D.S., Schmutz J.; RT "The genome of Eucalyptus grandis."; RL Nature 509:356-362(2014). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; KK198758; KCW68191.1; -; Genomic_DNA. DR Proteomes; UP000030711; Unassembled WGS sequence. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000030711}; KW Reference proteome {ECO:0000313|Proteomes:UP000030711}. FT DOMAIN 298 464 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 525 AA; 58425 MW; 199D5A5CEFA5FF5A CRC64; MMASCSSLTS RPSPLVHGPW SSNPTSNGNR PILLSLKIRH FDPLRLAKAV RHGLGVVSPD NTAVEVEAPA IETQEVNDEV GGSLNGVAET QLGDNSKDGT TSSTRVKKKR EDDDNLDNRF QVRNGREVFE EKAYLVGVER KGSTYQKLSS PNPRTYIGSG KVSEIKSAIH ALDVETVIFD DELSPGQLRN LEKAFGGDVR VCDRTALILD IFNQRAATHE AALQVALALM EYQLPRLTRM WTHLERQAGG QVKGMGEKQI EVDKRILRTQ IGVLKKELDS VRKHRKQYRN RRTSVPVPVV SLVGYTNAGK STLLNRLTGA NVLAEDRLFA TLDPTTRRVQ IKNGKEFLLT DTVGFIQKLP TMLVAAFRAT LEEISESSLL VHVVDISHPL AEQQIEAVDN VLSELDVSSI PKLMVWNKVD KAKDPQKIKL EVERREDVVC ISALTGEGLE EFCDAVQDKV KDSMVWVEAL VPFNKGELLS TIHQVGMVEK TEYMENGTLV KAHVPLRFAR MLTPMRQLHI SEPHP // ID A0A059BR97_EUCGR Unreviewed; 553 AA. AC A0A059BR97; DT 09-JUL-2014, integrated into UniProtKB/TrEMBL. DT 09-JUL-2014, sequence version 1. DT 07-JUN-2017, entry version 16. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:KCW68190.1}; GN ORFNames=EUGRSUZ_F01859 {ECO:0000313|EMBL:KCW68190.1}; OS Eucalyptus grandis (Flooded gum). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae; OC Pentapetalae; rosids; malvids; Myrtales; Myrtaceae; Myrtoideae; OC Eucalypteae; Eucalyptus. OX NCBI_TaxID=71139 {ECO:0000313|EMBL:KCW68190.1, ECO:0000313|Proteomes:UP000030711}; RN [1] {ECO:0000313|Proteomes:UP000030711} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=24919147; DOI=10.1038/nature13308; RA Myburg A.A., Grattapaglia D., Tuskan G.A., Hellsten U., Hayes R.D., RA Grimwood J., Jenkins J., Lindquist E., Tice H., Bauer D., RA Goodstein D.M., Dubchak I., Poliakov A., Mizrachi E., Kullan A.R., RA Hussey S.G., Pinard D., van der Merwe K., Singh P., van Jaarsveld I., RA Silva-Junior O.B., Togawa R.C., Pappas M.R., Faria D.A., RA Sansaloni C.P., Petroli C.D., Yang X., Ranjan P., Tschaplinski T.J., RA Ye C.Y., Li T., Sterck L., Vanneste K., Murat F., Soler M., RA Clemente H.S., Saidi N., Cassan-Wang H., Dunand C., Hefer C.A., RA Bornberg-Bauer E., Kersting A.R., Vining K., Amarasinghe V., Ranik M., RA Naithani S., Elser J., Boyd A.E., Liston A., Spatafora J.W., RA Dharmwardhana P., Raja R., Sullivan C., Romanel E., Alves-Ferreira M., RA Kulheim C., Foley W., Carocha V., Paiva J., Kudrna D., RA Brommonschenkel S.H., Pasquali G., Byrne M., Rigault P., Tibbits J., RA Spokevicius A., Jones R.C., Steane D.A., Vaillancourt R.E., RA Potts B.M., Joubert F., Barry K., Pappas G.J., Strauss S.H., RA Jaiswal P., Grima-Pettenati J., Salse J., Van de Peer Y., RA Rokhsar D.S., Schmutz J.; RT "The genome of Eucalyptus grandis."; RL Nature 509:356-362(2014). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; KK198758; KCW68190.1; -; Genomic_DNA. DR RefSeq; XP_010061264.1; XM_010062962.2. DR GeneID; 104448986; -. DR KEGG; egr:104448986; -. DR KO; K03665; -. DR Proteomes; UP000030711; Unassembled WGS sequence. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000030711}; KW Reference proteome {ECO:0000313|Proteomes:UP000030711}. FT DOMAIN 326 492 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 553 AA; 61401 MW; E61A2AD697DD4AA2 CRC64; MMASCSSLTS RPSPLVHGPW SSNPTSNGNR PILLSLKIRH FDPLRLAKAV RHGLGVVSPD NTAVEVEAPA IETQEVNDEV GGSLNGVAET QLGDNSKDGT TSSTRVKKKR EDDDNLDNRF QVRNGREVFE EKAYLVGVER KGDREESFGI DESLKELAQL ADTAGLMVVG STYQKLSSPN PRTYIGSGKV SEIKSAIHAL DVETVIFDDE LSPGQLRNLE KAFGGDVRVC DRTALILDIF NQRAATHEAA LQVALALMEY QLPRLTRMWT HLERQAGGQV KGMGEKQIEV DKRILRTQIG VLKKELDSVR KHRKQYRNRR TSVPVPVVSL VGYTNAGKST LLNRLTGANV LAEDRLFATL DPTTRRVQIK NGKEFLLTDT VGFIQKLPTM LVAAFRATLE EISESSLLVH VVDISHPLAE QQIEAVDNVL SELDVSSIPK LMVWNKVDKA KDPQKIKLEV ERREDVVCIS ALTGEGLEEF CDAVQDKVKD SMVWVEALVP FNKGELLSTI HQVGMVEKTE YMENGTLVKA HVPLRFARML TPMRQLHISE PHP // ID A0A059IJ53_9RHOB Unreviewed; 428 AA. AC A0A059IJ53; DT 09-JUL-2014, integrated into UniProtKB/TrEMBL. DT 09-JUL-2014, sequence version 1. DT 12-APR-2017, entry version 18. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=U879_20405 {ECO:0000313|EMBL:KDB01847.1}; OS Defluviimonas sp. 20V17. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae; Defluviimonas. OX NCBI_TaxID=1417296 {ECO:0000313|EMBL:KDB01847.1, ECO:0000313|Proteomes:UP000026305}; RN [1] {ECO:0000313|EMBL:KDB01847.1, ECO:0000313|Proteomes:UP000026305} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=20V17 {ECO:0000313|EMBL:KDB01847.1, RC ECO:0000313|Proteomes:UP000026305}; RX PubMed=24903865; RA Jiang L., Long M., Shao Z.; RT "Draft Genome Sequence of Defluviimonas indica Strain 20V17T, Isolated RT from a Deep-Sea Hydrothermal Vent Environment in the Southwest Indian RT Ocean."; RL Genome Announc. 2:e00479-14(2014). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KDB01847.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AYXI01000225; KDB01847.1; -; Genomic_DNA. DR EnsemblBacteria; KDB01847; KDB01847; U879_20405. DR Proteomes; UP000026305; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000026305}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000026305}. FT DOMAIN 208 377 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 428 AA; 47214 MW; C9AAEBBD8C1A2E3F CRC64; MTQTQTETRA PLTRAYVLHP DITSERRRRP AARALEEATA LAAALPGLEL AGAEVVRLPK VAPGTLFGSG KVAELKAKLS AAEVDLVLVD GPVSPVQQRN LEREWKVKLL DRTGLILEIF ADRARTREGV LQVELAALSY QRTRLVRAWT HLERQRGGLG FVGGPGETQI EADRRAIDEQ VTRIRRQLSK VVKTRELHRA ARRKVPFPIV ALVGYTNAGK STLFNRMTGA EVMAKDMLFA TLDPTMRGIE LPGGQKAILS DTVGFISDLP TQLVAAFRAT LEEVLEADLI LHVRDISHPE TEEQAADVAD ILRGLGLDAQ VPLIEVWNKI DQLVAPAREA LEVQAARSDN VRAISALSGQ GMAALLAGIE TGLAEERIER VLELSFAEGK RRAWLHDQGV VVDEIETETG YRLTLRWTPR QEQAFRDL // ID A0A059KML7_9BURK Unreviewed; 396 AA. AC A0A059KML7; DT 09-JUL-2014, integrated into UniProtKB/TrEMBL. DT 09-JUL-2014, sequence version 1. DT 07-JUN-2017, entry version 19. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=X805_20590 {ECO:0000313|EMBL:KDB52444.1}; OS Sphaerotilus natans subsp. natans DSM 6575. OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Sphaerotilus. OX NCBI_TaxID=1286631 {ECO:0000313|EMBL:KDB52444.1, ECO:0000313|Proteomes:UP000026714}; RN [1] {ECO:0000313|EMBL:KDB52444.1, ECO:0000313|Proteomes:UP000026714} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 6575 {ECO:0000313|EMBL:KDB52444.1, RC ECO:0000313|Proteomes:UP000026714}; RX PubMed=24965827; DOI=10.1111/1574-6941.12372; RA Park S., Kim D.H., Lee J.H., Hur H.G.; RT "Sphaerotilus natans encrusted with nanoball-shaped Fe(III) oxide RT minerals formed by nitrate-reducing mixotrophic Fe(II) oxidation."; RL FEMS Microbiol. Ecol. 90:68-77(2014). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KDB52444.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AZRA01000050; KDB52444.1; -; Genomic_DNA. DR EnsemblBacteria; KDB52444; KDB52444; X805_20590. DR PATRIC; fig|1286631.3.peg.2025; -. DR Proteomes; UP000026714; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000026714}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000026714}. FT DOMAIN 185 359 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 396 AA; 44018 MW; 1351A71D5BD614E3 CRC64; MDLGPGSSFD PSLDELALLA ESAGDLPVAR IIARRKSPDP ALFVGSGKAE EIRLTVLEHR AQCVIFDQAL GPAQQRNLER VLGVEVLDRT GLILDIFAAR ARSHEGKLQV ELAKLQYLAT RLVRRWSHLE RQKGGHGLRG GPGETQIELD RRMIDTRIKS VKERLAKVKR QRGTQRRARE RRGTFRISLV GYTNAGKSTL FNAMVKARSY AADQLFATLD TTVRQLYLED AGCSVSLSDT VGFIRDLPHG LVEAFQATLQ EAADADLLLH VVDAASPNRL EQIEEVMRVL QEIDAAGIRQ MLVFNKLDAL EDDARPRVMI DQFEIEPGRS IERLHVSARS GEGLAQLRER LAAIVLEADE PSPPAEHDPR FDRDGTIAPD WRSDPEDHFQ PAPDAA // ID A0A059MS22_9NOCA Unreviewed; 482 AA. AC A0A059MS22; A0A0F6S893; DT 09-JUL-2014, integrated into UniProtKB/TrEMBL. DT 09-JUL-2014, sequence version 1. DT 07-JUN-2017, entry version 24. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=N505_0109080 {ECO:0000313|EMBL:KDE13970.1}; OS Rhodococcus aetherivorans. OC Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae; OC Rhodococcus. OX NCBI_TaxID=191292 {ECO:0000313|EMBL:KDE13970.1, ECO:0000313|Proteomes:UP000024941}; RN [1] {ECO:0000313|EMBL:KDE13970.1, ECO:0000313|Proteomes:UP000024941} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BCP1 {ECO:0000313|EMBL:KDE13970.1, RC ECO:0000313|Proteomes:UP000024941}; RX PubMed=24158549; RA Cappelletti M., Di Gennaro P., D'Ursi P., Orro A., Mezzelani A., RA Landini M., Fedi S., Frascari D., Presentato A., Zannoni D., RA Milanesi L.; RT "Genome Sequence of Rhodococcus sp. Strain BCP1, a Biodegrader of RT Alkanes and Chlorinated Compounds."; RL Genome Announc. 1:e00657-13(2013). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KDE13970.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AVAE01000005; KDE13970.1; -; Genomic_DNA. DR RefSeq; WP_006935077.1; NZ_CP011341.1. DR EnsemblBacteria; KDE13970; KDE13970; N505_0109080. DR GeneID; 29568911; -. DR KEGG; rav:AAT18_11990; -. DR PATRIC; fig|191292.16.peg.1860; -. DR KO; K03665; -. DR Proteomes; UP000024941; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 2. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000313|EMBL:KDE13970.1}; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000024941}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900, KW ECO:0000313|EMBL:KDE13970.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000024941}. FT DOMAIN 260 428 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 219 246 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 482 AA; 52445 MW; 2BC81621972BC5C4 CRC64; MTNTRRNESA TDDADRVAGW APADPSVGEM QLEDRSALRR VAGLSTELED ITEVEYRQLR LERVVLVGVW TGGTAAQAEA SLAELAALAE TAGSEVLEGL IQRRDRPDAA TYIGSGKAEE LRQVVLATGA DTVICDGELT PAQLTALEKI VKVKVIDRTA LILDIFAQHA TSREGKAQVS LAQMEYMLPR LRGWGESMSR QAGGRAGSNG GVGLRGPGET KIETDRRRIR ERMAKLRREI KAMKSVRDTK RTRRMRNRIP SVAIVGYTNA GKSSLLNKLT GSGVLVQNAL FATLDPTTRR AELPDGREYV LTDTVGFVRH LPTQLVEAFR STLEEVTDAD LLLHVVDGSD PLPTDQIKAV REVITDVLRE SDAPPPPELI VVNKVDAADP LTLTELRALL PDAVFVSARS GEGLDELREH LAALLEHPDV EVKVLLPYTR GDLLARIHSD GQVLNSAHEV DGTRVHARVP QALASALVEY AA // ID A0A059W976_STRA9 Unreviewed; 495 AA. AC A0A059W976; DT 03-SEP-2014, integrated into UniProtKB/TrEMBL. DT 03-SEP-2014, sequence version 1. DT 05-JUL-2017, entry version 23. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=DC74_5881 {ECO:0000313|EMBL:AIA06330.1}; OS Streptomyces albulus. OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae; OC Streptomyces. OX NCBI_TaxID=68570 {ECO:0000313|EMBL:AIA06330.1, ECO:0000313|Proteomes:UP000026918}; RN [1] {ECO:0000313|Proteomes:UP000026918} RP NUCLEOTIDE SEQUENCE. RC STRAIN=NK660 {ECO:0000313|Proteomes:UP000026918}; RA Gu Y., Yang C., Song C., Wang S., Wang X., Geng W., Sun Y., Feng J., RA Wang Y.; RT "Genome Sequence of the epsilon-Poly-L-Lysine-Producing Microorganism RT Streptomyces albulus NK660."; RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP007574; AIA06330.1; -; Genomic_DNA. DR RefSeq; WP_016572961.1; NZ_CP007574.1. DR EnsemblBacteria; AIA06330; AIA06330; DC74_5881. DR GeneID; 32393267; -. DR KEGG; salu:DC74_5881; -. DR PATRIC; fig|68570.5.peg.6268; -. DR KO; K03665; -. DR Proteomes; UP000026918; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000026918}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000026918}. FT DOMAIN 275 440 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 495 AA; 54085 MW; 40E2F4F94F30AA88 CRC64; MTSSSSLPQD RQRLPESLRA DALMEEDVAW SHEIDGERDG DQYDRSARAA LRRVAGLSTE LEDVTEVEYR QLRLERVVLV GVWTSGTVQE AENSLAELAA LAETAGAMVL DGVIQRRDKP DPATYIGSGK ALELRDIVLE SGADTVVCDG ELSPGQLIHL EDVVKVKVVD RTALILDIFA QHAKSREGKA QVSLAQMQYM LPRLRGWGQS LSRQMGGGGS GSAGGGMATR GPGETKIETD RRRIREKMAK MRREIAEMKT GRDVKRQERR RNKVPSVAIA GYTNAGKSSL LNRLTGAGVL VENALFATLD PTVRRAETPS GRLYTLADTV GFVRHLPHHL VEAFRSTMEE VADADLILHV VDGSHPVPEE QLAAVREVIR DVGATEVPEI VVVNKADAAD PLTLQRLLRQ EKRALVVSAR TGEGITELLT LLDEELPRPQ VEIEVLVPYT QGALVSRAHA EGEVLSEEHT ADGTVLKARV HEELAAEFRP FVPAA // ID A0A060BHL0_9GAMM Unreviewed; 436 AA. AC A0A060BHL0; DT 03-SEP-2014, integrated into UniProtKB/TrEMBL. DT 03-SEP-2014, sequence version 1. DT 30-AUG-2017, entry version 21. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=FF32_17790 {ECO:0000313|EMBL:AIA76626.1}; OS Halomonas campaniensis. OC Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales; OC Halomonadaceae; Halomonas. OX NCBI_TaxID=213554 {ECO:0000313|EMBL:AIA76626.1, ECO:0000313|Proteomes:UP000027249}; RN [1] {ECO:0000313|EMBL:AIA76626.1, ECO:0000313|Proteomes:UP000027249} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=LS21 {ECO:0000313|EMBL:AIA76626.1, RC ECO:0000313|Proteomes:UP000027249}; RA Haitao Y., Guo-Qiang C.; RT "A Seawater Based Open and Continuous Process for RT Polyhydroxyalkanoates Production by Recombinant Halomonas campaniensis RT LS21 Grown in Mixed Substrates."; RL Submitted (MAY-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP007757; AIA76626.1; -; Genomic_DNA. DR RefSeq; WP_038485605.1; NZ_CP007757.1. DR EnsemblBacteria; AIA76626; AIA76626; FF32_17790. DR GeneID; 32424244; -. DR KEGG; hcs:FF32_17790; -. DR KO; K03665; -. DR Proteomes; UP000027249; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000027249}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}. FT DOMAIN 199 365 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 436 AA; 49001 MW; D3AFEDFC091477D8 CRC64; MFFERPDAGE TAVLVHVDFH DEQAREDPGE FLELVRSAGA EPATLLTASR QRPDSRTFIG SGKLEELRAL LAAHQAELVI FNHSLSPSQE RNLEHELKCR VLDRTGLILD IFAQRARTHE GKLQVELAQL EYMSTRLVRG WTHLERQKGG IGLRGPGETQ LETDRRLLRG RIKSIHKRLD KVRSQRDQNR RARSRAEIHS VSLVGYTNAG KSTLFNALTN AEVYAADQLF ATLDPTLRRL EIADVGPVVM ADTVGFIRHL PHKLVEAFRA TLQEAAEASL LVHVIDAADP DRDANVEQVD RVLKEIGADS VPVLKVMNKI DRLDSAPRIE RDGHGVPEVV WLSAQQGQGL DLLHEALTER LANDVIGFSL TLSPEQGKLR AGLHELNAVR EEYFDEQGQS VLDVRLPRRD FNQLMAQLGE RANTYLPVAL REIDEW // ID A0A060HLY7_9ARCH Unreviewed; 375 AA. AC A0A060HLY7; DT 03-SEP-2014, integrated into UniProtKB/TrEMBL. DT 03-SEP-2014, sequence version 1. DT 12-APR-2017, entry version 20. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=NVIE_019560 {ECO:0000313|EMBL:AIC16215.1}; OS Nitrososphaera viennensis EN76. OC Archaea; Thaumarchaeota; Nitrososphaeria; Nitrososphaerales; OC Nitrososphaeraceae; Nitrososphaera. OX NCBI_TaxID=926571 {ECO:0000313|EMBL:AIC16215.1, ECO:0000313|Proteomes:UP000027093}; RN [1] {ECO:0000313|EMBL:AIC16215.1, ECO:0000313|Proteomes:UP000027093} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=EN76 {ECO:0000313|EMBL:AIC16215.1}; RX PubMed=24907263; DOI=10.1099/ijs.0.063172-0; RA Stieglmeier M., Klingl A., Alves R.J., Rittmann S.K., Melcher M., RA Leisch N., Schleper C.; RT "Nitrososphaera viennensis gen. nov., sp. nov., an aerobic and RT mesophilic, ammonia-oxidizing archaeon from soil and a member of the RT archaeal phylum Thaumarchaeota."; RL Int. J. Syst. Evol. Microbiol. 64:2738-2752(2014). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP007536; AIC16215.1; -; Genomic_DNA. DR EnsemblBacteria; AIC16215; AIC16215; NVIE_019560. DR KEGG; nvn:NVIE_019560; -. DR KO; K03665; -. DR OrthoDB; POG093Z07D6; -. DR Proteomes; UP000027093; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000027093}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000027093}. FT DOMAIN 199 370 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 375 AA; 41745 MW; 5E974433C3B5B435 CRC64; MSTLSSPSSS PTRKSMKPVV LVAYPDAFAI EEAKSLVDSA DRAIVGTFTQ KYLNHSRYGI GSGKAEEIKA FVKESKAEQV VIDEHLTPRQ IYNLEKLTGV QVIDRERLIL DIFYSRATST EAKLQIELAE IEYEMPRVRE NAKLTSSGER AGKGGMGEYI VDVRFRDLKR RISFIKEKLK NAQRKRELCH QQRIKTGMTV VSLVGYTSSG KTTLFNLLTG EHKQTSSSLF TTLSTTTRSL KVNNEQEVLL TDTVGFISRL PTYMIDAFKS TLEESLAADL ILLLIDASEG LQEIRIKYTA CRHVLEELKA DRSKVLVVFT KYDKLTNSEE VVKQIAADLG IPNPISISAK SGHGISKLGT MIGQHPRVLP VQASD // ID A0A060HSE7_9ARCH Unreviewed; 380 AA. AC A0A060HSE7; DT 03-SEP-2014, integrated into UniProtKB/TrEMBL. DT 03-SEP-2014, sequence version 1. DT 12-APR-2017, entry version 20. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=NVIE_018320 {ECO:0000313|EMBL:AIC16087.1}; OS Nitrososphaera viennensis EN76. OC Archaea; Thaumarchaeota; Nitrososphaeria; Nitrososphaerales; OC Nitrososphaeraceae; Nitrososphaera. OX NCBI_TaxID=926571 {ECO:0000313|EMBL:AIC16087.1, ECO:0000313|Proteomes:UP000027093}; RN [1] {ECO:0000313|EMBL:AIC16087.1, ECO:0000313|Proteomes:UP000027093} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=EN76 {ECO:0000313|EMBL:AIC16087.1}; RX PubMed=24907263; DOI=10.1099/ijs.0.063172-0; RA Stieglmeier M., Klingl A., Alves R.J., Rittmann S.K., Melcher M., RA Leisch N., Schleper C.; RT "Nitrososphaera viennensis gen. nov., sp. nov., an aerobic and RT mesophilic, ammonia-oxidizing archaeon from soil and a member of the RT archaeal phylum Thaumarchaeota."; RL Int. J. Syst. Evol. Microbiol. 64:2738-2752(2014). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP007536; AIC16087.1; -; Genomic_DNA. DR EnsemblBacteria; AIC16087; AIC16087; NVIE_018320. DR KEGG; nvn:NVIE_018320; -. DR KO; K03665; -. DR OrthoDB; POG093Z07D6; -. DR Proteomes; UP000027093; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000027093}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000027093}. FT DOMAIN 190 361 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 156 183 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 380 AA; 42369 MW; 681C02A40C590C4B CRC64; MLLAAAYRKA ILITYPYDEA ISEAVSLADA AGYRVEKIVT QKHITKSRYG IGRGKAEEVK AIAEEIQPEV IVFDEVLKPS QTYNLASVCK KEVIDRERLI LEIFERRAST TESKTQIKLA QLRYDMTRAR EAVRLAKAGE QPGFYGLGKY EADTYLLDIK NRAQALKKKL EKEVTKRQLH RNQRAKAGLM SVSLAGYTSA GKTTLFNALT GETKSTAASV FTTLSTFTRA IDLDGDKVLL LDTVGFISKL PAYMIDAFKS TLEELSYASL VFLVIDISEP VLEIRRKLAS SLEVIREFEV PETRIVYVLN KVDRTTVEDA FDKAGQLGLL ASRRVLPVSA KTGYNMDQLK SLARSLLFET ERVVQDDNEK TTGGSAQDRA // ID A0A060JFH2_9MICO Unreviewed; 508 AA. AC A0A060JFH2; DT 03-SEP-2014, integrated into UniProtKB/TrEMBL. DT 03-SEP-2014, sequence version 1. DT 07-JUN-2017, entry version 22. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=Rhola_00004830 {ECO:0000313|EMBL:AIC47302.1}; OS Rhodoluna lacicola. OC Bacteria; Actinobacteria; Micrococcales; Microbacteriaceae; OC Luna cluster; Luna-1 subcluster; Rhodoluna. OX NCBI_TaxID=529884 {ECO:0000313|EMBL:AIC47302.1, ECO:0000313|Proteomes:UP000067708}; RN [1] {ECO:0000313|EMBL:AIC47302.1, ECO:0000313|Proteomes:UP000067708} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MWH-Ta8 {ECO:0000313|EMBL:AIC47302.1, RC ECO:0000313|Proteomes:UP000067708}; RX PubMed=24984700; DOI=10.1099/ijs.0.065292-0; RA Hahn M., Schmidt J., Taipale S.J., Doolittle W.F., Koll U.; RT "Rhodoluna lacicola gen. nov., sp. nov., a planktonic freshwater RT bacterium with stream-lined genome."; RL Int. J. Syst. Evol. Microbiol. 64:3254-3263(2014). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP007490; AIC47302.1; -; Genomic_DNA. DR RefSeq; WP_051636208.1; NZ_CP007490.1. DR EnsemblBacteria; AIC47302; AIC47302; Rhola_00004830. DR KEGG; rla:Rhola_00004830; -. DR PATRIC; fig|529884.3.peg.465; -. DR KO; K03665; -. DR Proteomes; UP000067708; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000067708}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000067708}. FT DOMAIN 288 453 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 508 AA; 55555 MW; 5509CCB3BE62FDA8 CRC64; MKNKDNHEEF GEDDSPTFTH GSSRGDEVVE RILRRGERAA ALGAVETHGY SDTDGDQYDL EDRSALKRVA GLSTELQDIT DVEYRQLRLE KVILIGLWGN NTLLDAENSL RELAALAETA GATVLDGLLQ RRANPDPATF LGKGKAQELK QLVQAAGADT VIADTELAPS QRRALEDVIN IKVIDRTAVI LDIFAQHAKS REGKAQVELA QLEYLLPRLR GWGESMSRQA GGQAAGGVGM GSRGPGETKI ELDRRRINTR MAKLRKQISA MKPARETKRA NRERNAIPAV AIAGYTNAGK SSLLNRMTQA GVLVQNALFA TLDPTVRKAK TPDGRDYTLA DTVGFVRNLP HQLVEAFRST LEEIAGSDLI VHVVDASHPD PSGQIATVRN VIGEVSARDI PELIVFNKID LADETHRMAL RGMEPNSIGV SARTGEGIEE LMQIIASLLP EPNVEIAALI PYDRGDLVSR LHLNSRIMVL DYRENGTFVR AMVKPEMAAE LSAYRVVV // ID A0A060LX28_9BACI Unreviewed; 420 AA. AC A0A060LX28; DT 03-SEP-2014, integrated into UniProtKB/TrEMBL. DT 03-SEP-2014, sequence version 1. DT 07-JUN-2017, entry version 21. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=BleG1_3279 {ECO:0000313|EMBL:AIC95826.1}; OS Bacillus lehensis G1. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus. OX NCBI_TaxID=1246626 {ECO:0000313|EMBL:AIC95826.1, ECO:0000313|Proteomes:UP000027142}; RN [1] {ECO:0000313|EMBL:AIC95826.1, ECO:0000313|Proteomes:UP000027142} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=G1 {ECO:0000313|EMBL:AIC95826.1, RC ECO:0000313|Proteomes:UP000027142}; RX PubMed=24811681; DOI=10.1016/j.gene.2014.05.012; RA Noor Y.M., Samsulrizal N.H., Jema'on N.A., Low K.O., Ramli A.N., RA Alias N.I., Damis S.I., Fuzi S.F., Isa M.N., Murad A.M., Raih M.F., RA Bakar F.D., Najimudin N., Mahadi N.M., Illias R.M.; RT "A comparative genomic analysis of the alkalitolerant soil bacterium RT Bacillus lehensis G1."; RL Gene 545:253-261(2014). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP003923; AIC95826.1; -; Genomic_DNA. DR RefSeq; WP_038483180.1; NZ_CP003923.1. DR EnsemblBacteria; AIC95826; AIC95826; BleG1_3279. DR KEGG; ble:BleG1_3279; -. DR PATRIC; fig|1246626.3.peg.3256; -. DR KO; K03665; -. DR Proteomes; UP000027142; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000027142}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000027142}. FT DOMAIN 203 367 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 162 196 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 420 AA; 48041 MW; 544ADD493B882B9E CRC64; MHETVTRTIK DSIVVGVERQ GDTYFDYGME ELENLTRALD LNPVASLTQK LQTPNQATYL GSGKVTELSR LIASFDVDLV IFNDELTPSQ IRNLEKELEV TVYDRTMLIL DIFGERAKTN EAQLQVEIAR LKYLLPRLVG MRASLSRQGG SGSGLANRGA GETKLELDRR KIESRISALE KELEVVVERR QTQRQKRKTE GIPVVALVGY TNAGKSSLLN AFVTEKQEKK VFEKDMLFAT LDTSVRRVEM QKNMPFLLAD TVGFVSKLPT HLVKAFRSTL EEAREADLLL HVVDYSSSYY KEMMRTTENT LKELEIDQPL LSVYNKMDRV EAREWSTEKD EIFLSAKTGE GLDRLVESIQ ANVFTHYIKK ALHIPYEDSK AFAYVNEHTH ILEQLEEDTG WYVETMMHKK HASLVTQYEK // ID A0A060NHD4_9BURK Unreviewed; 395 AA. AC A0A060NHD4; DT 03-SEP-2014, integrated into UniProtKB/TrEMBL. DT 03-SEP-2014, sequence version 1. DT 12-APR-2017, entry version 20. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:BAO80502.1}; GN ORFNames=SRAA_0648 {ECO:0000313|EMBL:BAO80502.1}; OS Comamonadaceae bacterium A1. OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Comamonadaceae. OX NCBI_TaxID=1458425 {ECO:0000313|EMBL:BAO80502.1, ECO:0000313|Proteomes:UP000067461}; RN [1] {ECO:0000313|EMBL:BAO80502.1, ECO:0000313|Proteomes:UP000067461} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=A1 {ECO:0000313|EMBL:BAO80502.1, RC ECO:0000313|Proteomes:UP000067461}; RX PubMed=24845058; DOI=10.1038/ncomms4900; RA Suzuki S., Kuenen J.G., Schipper K., van der Velde S., Ishii S., RA Wu A., Sorokin D.Y., Tenney A., Meng X.Y., Morrill P.L., Kamagata Y., RA Muyzer G., Nealson K.H.; RT "Physiological and genomic features of highly alkaliphilic hydrogen- RT utilizing Betaproteobacteria from a continental serpentinizing site."; RL Nat. Commun. 5:3900-3900(2014). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AP014568; BAO80502.1; -; Genomic_DNA. DR EnsemblBacteria; BAO80502; BAO80502; SRAA_0648. DR KEGG; cbaa:SRAA_0648; -. DR KO; K03665; -. DR Proteomes; UP000067461; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000067461}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000067461}. FT DOMAIN 218 391 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 395 AA; 43546 MW; 6DF000222F4F3988 CRC64; MLPGPGVSQM GDSLGYPPAK IRPASALPGV ILVGVDMGLP HFDAELSELA ELARTAGYEV LDRVVCKRRA PDPALYLGSG KADEIKALAL AHGAQEILFD QALSPAQQRN LERHMERPVN DRVLLILEIF SQRARSHEGK LQVELARLQY LSTRLVRRWS HLERQSGGIG LRGGPGETQI ELDRRMIGDS IKRTRERLER VQRQRNTQRR RRERSGTFKV SLVGYTNAGK SSLFNALVKA RAYAADQLFA TLDTTTRQLY LSEAGRSLSL SDTVGFIRDL PHALVSAFAA TLQEACEADL LLHVVDCANP AHLEQIANVQ LVLREIGAEG IEQVLVFNKI DALAPERWPL QSVDSMELDG QSVARIFLSA QTGQGLDALR GLLAQRLQAA TQEMV // ID A0A060Q7Z5_9PROT Unreviewed; 440 AA. AC A0A060Q7Z5; DT 03-SEP-2014, integrated into UniProtKB/TrEMBL. DT 03-SEP-2014, sequence version 1. DT 07-JUN-2017, entry version 22. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=SACS_0211 {ECO:0000313|EMBL:CDG32949.1}; OS Saccharibacter sp. AM169. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales; OC Acetobacteraceae; Saccharibacter. OX NCBI_TaxID=1343158 {ECO:0000313|EMBL:CDG32949.1, ECO:0000313|Proteomes:UP000027590}; RN [1] {ECO:0000313|EMBL:CDG32949.1, ECO:0000313|Proteomes:UP000027590} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=AM169 {ECO:0000313|Proteomes:UP000027590}; RX PubMed=24682158; DOI=10.1093/gbe/evu062; RA Chouaia B., Gaiarsa S., Crotti E., Comandatore F., Degli Esposti M., RA Ricci I., Alma A., Favia G., Bandi C., Daffonchio D.; RT "Acetic acid bacteria genomes reveal functional traits for adaptation RT to life in insect guts."; RL Genome Biol. Evol. 6:912-920(2014). RN [2] {ECO:0000313|EMBL:CDG32949.1, ECO:0000313|Proteomes:UP000027590} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=AM169 {ECO:0000313|Proteomes:UP000027590}; RX PubMed=24804722; DOI=10.1371/journal.pone.0096566; RA Degli Esposti M., Chouaia B., Comandatore F., Crotti E., Sassera D., RA Lievens P.M., Daffonchio D., Bandi C.; RT "Evolution of mitochondria reconstructed from the energy metabolism of RT living bacteria."; RL PLoS ONE 9:e96566-e96566(2014). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:CDG32949.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CBLY010000002; CDG32949.1; -; Genomic_DNA. DR RefSeq; WP_043558020.1; NZ_CBLY010000002.1. DR EnsemblBacteria; CDG32949; CDG32949; SACS_0211. DR Proteomes; UP000027590; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000027590}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000027590}. FT DOMAIN 208 377 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 440 AA; 48694 MW; 7B22F0468DB05DC3 CRC64; MRRQPKETAR KPTLAAVILP AEKQAFAEGR AAEARLEEAV GLAASIGLEI VHTAIYPLRT KRPATLLGAG QLEELTEIVK AESVGVVVVD ARLSPAQQRN LEKEMGCKVV DRTGLILDIF GARAATREGV LQVELAHLEY QRSRLVRLWT HLERQRGGFG FLGGPGETQI EADRRMLDER LVKLRKELEQ VRRTRGLHRH ARRKVPFPVV ALVGYTNAGK STLFNRITGA GVHAQDQLFA TLDPTMRNLT LPSGRRVILS DTVGFISDLP TELIAAFRAT LEEVAEADII LHVRDVAHPD SASQREDVLS VLGDMTADGM LDEAWPERTI EVLNKADLLG GTEAVPRREG SVAVSALTGE GLPDLMEALD AFMTRSMKQF SVQIPVTDGA ALAWLHEHGE VMERLDDEER LHLRVRLFPA DQQRFVRQFP ALPLMPEQDG // ID A0A060QD28_9PROT Unreviewed; 436 AA. AC A0A060QD28; DT 03-SEP-2014, integrated into UniProtKB/TrEMBL. DT 03-SEP-2014, sequence version 1. DT 10-MAY-2017, entry version 22. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=ASAP_0780 {ECO:0000313|EMBL:CDG38825.1}; OS Asaia platycodi SF2.1. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales; OC Acetobacteraceae; Asaia. OX NCBI_TaxID=1382230 {ECO:0000313|EMBL:CDG38825.1, ECO:0000313|Proteomes:UP000027583}; RN [1] {ECO:0000313|EMBL:CDG38825.1, ECO:0000313|Proteomes:UP000027583} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SF2.1 {ECO:0000313|EMBL:CDG38825.1}; RX PubMed=24682158; DOI=10.1093/gbe/evu062; RA Chouaia B., Gaiarsa S., Crotti E., Comandatore F., Degli Esposti M., RA Ricci I., Alma A., Favia G., Bandi C., Daffonchio D.; RT "Acetic acid bacteria genomes reveal functional traits for adaptation RT to life in insect guts."; RL Genome Biol. Evol. 6:912-920(2014). RN [2] {ECO:0000313|EMBL:CDG38825.1, ECO:0000313|Proteomes:UP000027583} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SF2.1 {ECO:0000313|EMBL:CDG38825.1}; RX PubMed=24804722; DOI=10.1371/journal.pone.0096566; RA Degli Esposti M., Chouaia B., Comandatore F., Crotti E., Sassera D., RA Lievens P.M., Daffonchio D., Bandi C.; RT "Evolution of mitochondria reconstructed from the energy metabolism of RT living bacteria."; RL PLoS ONE 9:e96566-e96566(2014). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:CDG38825.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CBLX010000004; CDG38825.1; -; Genomic_DNA. DR EnsemblBacteria; CDG38825; CDG38825; ASAP_0780. DR Proteomes; UP000027583; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000027583}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000027583}. FT DOMAIN 208 377 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 436 AA; 48081 MW; ACB45B7352169D41 CRC64; MSVTTSTTPP ATRAAVILPW ARPTPNDEFR AAEARLEEAV GLTSSIGLVV VRQAVLAIRA VRPATLFGKG QVEQLAELVH ENDVKVMIVD AKLSPGQQRN LEKALDCKVL DRTGLILDIF GARAATREGV LQVELAHLEY QRSRLVRLWT HLERQRGGFG FLGGPGETQI EADRRMIDER LVRLRKDLDQ VRRTRGLHRS ARKKVPFPVV ALVGYTNAGK STLFNALTGS AVHAQDQLFA TLDPTMRGLR LPSGRRVILS DTVGFISELP TELVAAFRAT LEEVAEADII LHVRDIAHPD SAAQRADVIN VLDGMVRDGM LDENWPERTI EVLNKADLMG GIEAVPRHPG CVAISAMTGE GLPNLYSMLD QHMTASMSLT RVSLDISNGA ALAWLYEHGE VLERLDQETE ITLDVRLFEQ DRSRFGQLYP DCLVSA // ID A0A060R895_9BACT Unreviewed; 397 AA. AC A0A060R895; DT 03-SEP-2014, integrated into UniProtKB/TrEMBL. DT 03-SEP-2014, sequence version 1. DT 07-JUN-2017, entry version 22. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=BN938_1589 {ECO:0000313|EMBL:CDN31676.1}; OS Mucinivorans hirudinis. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Rikenellaceae; OC Mucinivorans. OX NCBI_TaxID=1433126 {ECO:0000313|EMBL:CDN31676.1, ECO:0000313|Proteomes:UP000027616}; RN [1] {ECO:0000313|EMBL:CDN31676.1, ECO:0000313|Proteomes:UP000027616} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=25657285; DOI=10.1128/genomeA.01530-14; RA Nelson M.C., Bomar L., Graf J.; RT "Complete Genome Sequence of the Novel Leech Symbiont Mucinivorans RT hirudinis M3T."; RL Genome Announc. 3:e01530-e01514(2015). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; HG934468; CDN31676.1; -; Genomic_DNA. DR RefSeq; WP_038654875.1; NZ_HG934468.1. DR EnsemblBacteria; CDN31676; CDN31676; BN938_1589. DR KEGG; rbc:BN938_1589; -. DR PATRIC; fig|1433126.3.peg.1574; -. DR KO; K03665; -. DR Proteomes; UP000027616; Chromosome I. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000027616}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000027616}. FT DOMAIN 203 386 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 397 AA; 45695 MW; A452D59583E643DF CRC64; MEKGKLTEKK TDRVVLVGII RDREQDRVVA EYLEELRFLA ETAGAQTINI FTQRLSQPHK RTFVGEGKLE EIRTYCEDNE IDAVIFDDEL SPSQLRNIEK ELAIRVLDRT ILILEIFTQR ATTAYAKTQV DLAHWQYMLP RLSGMWTHLE RQRGGIGTRG GAGEREIETD RRIVRGRITR LKEELTKIDR QMAVQRSNRG EFVRVALVGY TNVGKSTLMN TLSKSEVFAE NKLFATLDTT VRKVVLENLP FLLSDTVGFI RKLPHQLVES FKSTLDEVRE ADLLLHVVDI SHPGFEAQIE VVKKTLQEIG AGEKPVFYIF NKIDAYQYVV KEEDDLLPMT DENRSLEDLK KGYLSKTEAA IFISAKNGTG ISQMKEELYA MVRDIHKVRY PYNNFLY // ID A0A060UPB7_9PROT Unreviewed; 424 AA. AC A0A060UPB7; DT 03-SEP-2014, integrated into UniProtKB/TrEMBL. DT 03-SEP-2014, sequence version 1. DT 10-MAY-2017, entry version 20. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:CDQ10116.1}; GN ORFNames=AFERRI_40068 {ECO:0000313|EMBL:CDQ10116.1}; OS Acidithiobacillus ferrivorans. OC Bacteria; Proteobacteria; Acidithiobacillia; Acidithiobacillales; OC Acidithiobacillaceae; Acidithiobacillus. OX NCBI_TaxID=160808 {ECO:0000313|EMBL:CDQ10116.1, ECO:0000313|Proteomes:UP000029069}; RN [1] {ECO:0000313|EMBL:CDQ10116.1, ECO:0000313|Proteomes:UP000029069} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CF27 {ECO:0000313|EMBL:CDQ10116.1, RC ECO:0000313|Proteomes:UP000029069}; RA Genoscope - CEA; RL Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:CDQ10116.1, ECO:0000313|Proteomes:UP000029069} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CF27 {ECO:0000313|EMBL:CDQ10116.1, RC ECO:0000313|Proteomes:UP000029069}; RA Talla E., Hedrich S., Mangenot S., Ji B., Johnson D.B., Barbe V., RA Bonnefoy V.; RT "Initial genome analysis of the psychrotolerant acidophile RT Acidithiobacillus ferrivorans CF27: insights into iron and sulfur RT oxidation pathways and into biofilm formation."; RL Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:CDQ10116.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CCCS020000034; CDQ10116.1; -; Genomic_DNA. DR STRING; 743299.Acife_1422; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR Proteomes; UP000029069; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000029069}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}. FT DOMAIN 187 353 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 424 AA; 46493 MW; 5E9CBCB59F8FE1C1 CRC64; MLVHVVLHGE TDPDDGAEFS HLATDSGAEV LAFLSVQRDR PDPATFLGRG KVTELAGQVS DLSVDLVLFD RVLSPVQERN LERALQCRVV DRVGLILDIF ARRAHTHEGK LQVELAQLTR LRTRLIRGWT HLERQRGGIG LRGPGETQLE TDRRLIGERI RSLRGRLVKV AAHRATQRRA RQRAPLPTVA LVGYTNAGKS SLFNTLTESS SYAADRLFAT LDPAIRRLQV VGHEAILLAD TVGFLRDLPT DLIAAFRATL EEVNQAQLLL HVVDGSAPDR DAQIAAVDAV LTEIGADEIP RLLVLNKVDL TGDAPGNVYE GSGKLMAVRV SARSGTGIPE LLQAMTQRVG RSMLRAELTL TPEEGALRAR LHRVASIVEE SFDDQGMAHL IFDIDDLTWR RMRAQMRSSG CQAMDAPPTI PADG // ID A0A061AGK8_9MOLU Unreviewed; 421 AA. AC A0A061AGK8; DT 03-SEP-2014, integrated into UniProtKB/TrEMBL. DT 03-SEP-2014, sequence version 1. DT 05-JUL-2017, entry version 23. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:CDR30097.1}; GN ORFNames=Aocu_00240 {ECO:0000313|EMBL:CDR30097.1}; OS Acholeplasma oculi. OC Bacteria; Tenericutes; Mollicutes; Acholeplasmatales; OC Acholeplasmataceae; Acholeplasma. OX NCBI_TaxID=35623 {ECO:0000313|EMBL:CDR30097.1, ECO:0000313|Proteomes:UP000032434}; RN [1] {ECO:0000313|EMBL:CDR30097.1} RP NUCLEOTIDE SEQUENCE. RA Kube Michael; RL Submitted (MAY-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LK028559; CDR30097.1; -; Genomic_DNA. DR EnsemblBacteria; CDR30097; CDR30097; Aocu_00240. DR KEGG; aoc:Aocu_00240; -. DR PATRIC; fig|35623.3.peg.24; -. DR KO; K03665; -. DR Proteomes; UP000032434; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000032434}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000032434}. FT DOMAIN 197 362 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 156 183 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 421 AA; 47548 MW; 30E6BAFB7F7C0EFD CRC64; MQKIDRAILV ALNHQTPYDV TKASIDELEE LAKALEIKTV DKVIQTLSSI DPRYYIGSGK VQEIKGMVDV LNADMVIFDD TLSSSQIRNL EEILQVQILD RSFLILQIFA LRAQTRQAIL EVSLAQKLYL LPRLVGMGKS LSRQGGGSFN AKGPGETKLE LDRRKLNDEI IQLTKELEVI KKERMISRQK RVKNNIPIVA LVGYTNAGKS SLMNYLASHY GKDKTDVFEK DMLFATLDTK SKRIQKDNHQ AFILTDTVGF ISKLPPELVK SFESTLSDIT SADLILHMVD GKQFSLLQLS LTKQVLEGLG CKDTPRILVV TKKDLGLPAP MIQDDYIQIS SKTGEGIDDL YRMIDSMLYK DARIYKLLLP FDSGNLYQIL KSNHTVLETS YQSEGIYTRV VLNPKDLHLF EKYILTSKNV N // ID A0A061DHA7_THECC Unreviewed; 614 AA. AC A0A061DHA7; DT 03-SEP-2014, integrated into UniProtKB/TrEMBL. DT 03-SEP-2014, sequence version 1. DT 12-APR-2017, entry version 19. DE SubName: Full=GTP-binding protein hflx, putative {ECO:0000313|EMBL:EOX91775.1}; GN ORFNames=TCM_000854 {ECO:0000313|EMBL:EOX91775.1}; OS Theobroma cacao (Cacao) (Cocoa). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae; OC Pentapetalae; rosids; malvids; Malvales; Malvaceae; Byttnerioideae; OC Theobroma. OX NCBI_TaxID=3641 {ECO:0000313|EMBL:EOX91775.1, ECO:0000313|Proteomes:UP000026915}; RN [1] {ECO:0000313|EMBL:EOX91775.1, ECO:0000313|Proteomes:UP000026915} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=23731509; RA Motamayor J.C., Mockaitis K., Schmutz J., Haiminen N., Iii D.L., RA Cornejo O., Findley S.D., Zheng P., Utro F., Royaert S., Saski C., RA Jenkins J., Podicheti R., Zhao M., Scheffler B.E., Stack J.C., RA Feltus F.A., Mustiga G.M., Amores F., Phillips W., Marelli J.P., RA May G.D., Shapiro H., Ma J., Bustamante C.D., Schnell R.J., Main D., RA Gilbert D., Parida L., Kuhn D.N.; RT "The genome sequence of the most widely cultivated cacao type and its RT use to identify candidate genes regulating pod color."; RL Genome Biol. 14:R53-R53(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CM001879; EOX91775.1; -; Genomic_DNA. DR EnsemblPlants; EOX91775; EOX91775; TCM_000854. DR Gramene; EOX91775; EOX91775; TCM_000854. DR OMA; CNEDEVP; -. DR Proteomes; UP000026915; Chromosome 1. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR CDD; cd01878; HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 2. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000026915}; KW Reference proteome {ECO:0000313|Proteomes:UP000026915}. FT DOMAIN 300 429 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 614 AA; 68190 MW; 62E1D0C35DBBB6CE CRC64; MLRALSLTRT CLRSRCQFLS HRPSPSPLSI LSSPYSTSKQ QNRVTEDDQH TTVSVFNRDP TDPPRLFLVQ PRLRPATFLQ AKLNEALCLA NSLEEQRDGY FDTDFFDKEL PPHVVVQNPS LKSSKIRADT YFGPGTVHNI KCHLNAVESK DEVDAVFINT ILSGIQQRNL ERIWGKPVLD RVGLIIEIFN AHAHTKEAKL QAELAALMYK KSRLVRVRGA DGRYTFGVTG EAEVVSARGR GSGGRGFISG AGETELQLQR RRILERRSHL LTQIEEVRRT RAVQRAARKR RGGLDGQGLA TVAVVGYTNA GKSTLIGALS DSDLYSDARL FATLDARLKG VVLPSGRKVL LSDTVGFISD LPVQLVEAFH STLEEVVEAD LLVHVIDCTA PNLDEHRSTV LLVLRKIGVS EEKLQNMIEV WNKIDYEEEV GADVYIDDGD EDAEISNFSG AEDSKINSSS EVEDCNVASE PLDGKSVGNC VAGNADADGS DVFKPSPGDL QETMVDKQGD YSDGWLLSGD DFADDYWNTL NDQQTETSND WMVEKDSQSQ SQHVPHVKVS ALTGVGLQEL LEIIDDRLKV QDDKLKSQKV VESSFFDRKW RPPRKEDEQV AVEQ // ID A0A061FBZ5_THECC Unreviewed; 484 AA. AC A0A061FBZ5; DT 03-SEP-2014, integrated into UniProtKB/TrEMBL. DT 03-SEP-2014, sequence version 1. DT 07-JUN-2017, entry version 18. DE SubName: Full=GTP-binding protein isoform 2 {ECO:0000313|EMBL:EOY14860.1}; GN ORFNames=TCM_034115 {ECO:0000313|EMBL:EOY14860.1}; OS Theobroma cacao (Cacao) (Cocoa). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae; OC Pentapetalae; rosids; malvids; Malvales; Malvaceae; Byttnerioideae; OC Theobroma. OX NCBI_TaxID=3641 {ECO:0000313|EMBL:EOY14860.1, ECO:0000313|Proteomes:UP000026915}; RN [1] {ECO:0000313|EMBL:EOY14860.1, ECO:0000313|Proteomes:UP000026915} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=23731509; RA Motamayor J.C., Mockaitis K., Schmutz J., Haiminen N., Iii D.L., RA Cornejo O., Findley S.D., Zheng P., Utro F., Royaert S., Saski C., RA Jenkins J., Podicheti R., Zhao M., Scheffler B.E., Stack J.C., RA Feltus F.A., Mustiga G.M., Amores F., Phillips W., Marelli J.P., RA May G.D., Shapiro H., Ma J., Bustamante C.D., Schnell R.J., Main D., RA Gilbert D., Parida L., Kuhn D.N.; RT "The genome sequence of the most widely cultivated cacao type and its RT use to identify candidate genes regulating pod color."; RL Genome Biol. 14:R53-R53(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CM001886; EOY14860.1; -; Genomic_DNA. DR EnsemblPlants; EOY14860; EOY14860; TCM_034115. DR Gramene; EOY14860; EOY14860; TCM_034115. DR Proteomes; UP000026915; Chromosome 8. DR ExpressionAtlas; A0A061FBZ5; differential. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000026915}; KW Reference proteome {ECO:0000313|Proteomes:UP000026915}. FT DOMAIN 321 484 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 484 AA; 53914 MW; F69E8FBBB1E858BA CRC64; MSLCFCSLIR SSPLIYDSNF PWNLNLNRST YPISFSVHGN SRNLVARVVQ HGLEVNNISL PSPTIEAEEE KEVIRELGTG AAGAELVEHE PKPVRVRKKR AGDDDNDDES FEDRFKLRNG KEVFEEKAYL VGVERKGETL DSFGIEESLK ELAQLADTAG LMVVGSTYQK LSSPSPRTYI GSGKVAEIKS ATHAFGVETV IFDDELSPGQ LRNLEKAFGG DVRVCDRTAL ILDIFNQRAA THEAALQVAL AQMEYQLPRL TRMWTHLERQ AGGKVKGMGE KQIEVDKRIL RTQIGVLKKE LESVRKHRKQ YRNRRFSVPV PVVSLVGYTN AGKSTLLNQL TGANVLSEDR LFATLDPTTR RVQMKNGSEF LLTDTVGFIQ KLPTTLVAAF RATLEEISES SLLVHVVDIS HPLAEQQIDA VEKVLSELDV SAIPRLMVWN KVDRVSDPQR IKLEAERSED VVCASALTGD GLQEFCNAVQ EKLK // ID A0A061FCT1_THECC Unreviewed; 410 AA. AC A0A061FCT1; DT 03-SEP-2014, integrated into UniProtKB/TrEMBL. DT 03-SEP-2014, sequence version 1. DT 07-JUN-2017, entry version 17. DE SubName: Full=GTP-binding protein isoform 3 {ECO:0000313|EMBL:EOY14861.1}; GN ORFNames=TCM_034115 {ECO:0000313|EMBL:EOY14861.1}; OS Theobroma cacao (Cacao) (Cocoa). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae; OC Pentapetalae; rosids; malvids; Malvales; Malvaceae; Byttnerioideae; OC Theobroma. OX NCBI_TaxID=3641 {ECO:0000313|EMBL:EOY14861.1, ECO:0000313|Proteomes:UP000026915}; RN [1] {ECO:0000313|EMBL:EOY14861.1, ECO:0000313|Proteomes:UP000026915} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=23731509; RA Motamayor J.C., Mockaitis K., Schmutz J., Haiminen N., Iii D.L., RA Cornejo O., Findley S.D., Zheng P., Utro F., Royaert S., Saski C., RA Jenkins J., Podicheti R., Zhao M., Scheffler B.E., Stack J.C., RA Feltus F.A., Mustiga G.M., Amores F., Phillips W., Marelli J.P., RA May G.D., Shapiro H., Ma J., Bustamante C.D., Schnell R.J., Main D., RA Gilbert D., Parida L., Kuhn D.N.; RT "The genome sequence of the most widely cultivated cacao type and its RT use to identify candidate genes regulating pod color."; RL Genome Biol. 14:R53-R53(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CM001886; EOY14861.1; -; Genomic_DNA. DR EnsemblPlants; EOY14861; EOY14861; TCM_034115. DR Gramene; EOY14861; EOY14861; TCM_034115. DR Proteomes; UP000026915; Chromosome 8. DR ExpressionAtlas; A0A061FCT1; differential. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000026915}; KW Reference proteome {ECO:0000313|Proteomes:UP000026915}. FT DOMAIN 321 410 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 410 AA; 45741 MW; 3CBDEA31917D6D92 CRC64; MSLCFCSLIR SSPLIYDSNF PWNLNLNRST YPISFSVHGN SRNLVARVVQ HGLEVNNISL PSPTIEAEEE KEVIRELGTG AAGAELVEHE PKPVRVRKKR AGDDDNDDES FEDRFKLRNG KEVFEEKAYL VGVERKGETL DSFGIEESLK ELAQLADTAG LMVVGSTYQK LSSPSPRTYI GSGKVAEIKS ATHAFGVETV IFDDELSPGQ LRNLEKAFGG DVRVCDRTAL ILDIFNQRAA THEAALQVAL AQMEYQLPRL TRMWTHLERQ AGGKVKGMGE KQIEVDKRIL RTQIGVLKKE LESVRKHRKQ YRNRRFSVPV PVVSLVGYTN AGKSTLLNQL TGANVLSEDR LFATLDPTTR RVQMKNGSEF LLTDTVGFIQ KLPTTLVAAF RATLEEISES SLLVHVVDIR // ID A0A061FDR8_THECC Unreviewed; 414 AA. AC A0A061FDR8; DT 03-SEP-2014, integrated into UniProtKB/TrEMBL. DT 03-SEP-2014, sequence version 1. DT 07-JUN-2017, entry version 17. DE SubName: Full=GTP-binding protein isoform 4 {ECO:0000313|EMBL:EOY14862.1}; GN ORFNames=TCM_034115 {ECO:0000313|EMBL:EOY14862.1}; OS Theobroma cacao (Cacao) (Cocoa). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae; OC Pentapetalae; rosids; malvids; Malvales; Malvaceae; Byttnerioideae; OC Theobroma. OX NCBI_TaxID=3641 {ECO:0000313|EMBL:EOY14862.1, ECO:0000313|Proteomes:UP000026915}; RN [1] {ECO:0000313|EMBL:EOY14862.1, ECO:0000313|Proteomes:UP000026915} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=23731509; RA Motamayor J.C., Mockaitis K., Schmutz J., Haiminen N., Iii D.L., RA Cornejo O., Findley S.D., Zheng P., Utro F., Royaert S., Saski C., RA Jenkins J., Podicheti R., Zhao M., Scheffler B.E., Stack J.C., RA Feltus F.A., Mustiga G.M., Amores F., Phillips W., Marelli J.P., RA May G.D., Shapiro H., Ma J., Bustamante C.D., Schnell R.J., Main D., RA Gilbert D., Parida L., Kuhn D.N.; RT "The genome sequence of the most widely cultivated cacao type and its RT use to identify candidate genes regulating pod color."; RL Genome Biol. 14:R53-R53(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CM001886; EOY14862.1; -; Genomic_DNA. DR EnsemblPlants; EOY14862; EOY14862; TCM_034115. DR Gramene; EOY14862; EOY14862; TCM_034115. DR Proteomes; UP000026915; Chromosome 8. DR ExpressionAtlas; A0A061FDR8; differential. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000026915}; KW Reference proteome {ECO:0000313|Proteomes:UP000026915}. FT DOMAIN 321 414 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 414 AA; 46040 MW; B59BFDF58D0DEA31 CRC64; MSLCFCSLIR SSPLIYDSNF PWNLNLNRST YPISFSVHGN SRNLVARVVQ HGLEVNNISL PSPTIEAEEE KEVIRELGTG AAGAELVEHE PKPVRVRKKR AGDDDNDDES FEDRFKLRNG KEVFEEKAYL VGVERKGETL DSFGIEESLK ELAQLADTAG LMVVGSTYQK LSSPSPRTYI GSGKVAEIKS ATHAFGVETV IFDDELSPGQ LRNLEKAFGG DVRVCDRTAL ILDIFNQRAA THEAALQVAL AQMEYQLPRL TRMWTHLERQ AGGKVKGMGE KQIEVDKRIL RTQIGVLKKE LESVRKHRKQ YRNRRFSVPV PVVSLVGYTN AGKSTLLNQL TGANVLSEDR LFATLDPTTR RVQMKNGSEF LLTDTVGFIQ KLPTTLVAAF RATLEEISES SLLVHVVDIS SAIP // ID A0A061FK28_THECC Unreviewed; 544 AA. AC A0A061FK28; DT 03-SEP-2014, integrated into UniProtKB/TrEMBL. DT 03-SEP-2014, sequence version 1. DT 30-AUG-2017, entry version 25. DE SubName: Full=GTP-binding protein isoform 1 {ECO:0000313|EMBL:EOY14859.1}; GN ORFNames=TCM_034115 {ECO:0000313|EMBL:EOY14859.1}; OS Theobroma cacao (Cacao) (Cocoa). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae; OC Pentapetalae; rosids; malvids; Malvales; Malvaceae; Byttnerioideae; OC Theobroma. OX NCBI_TaxID=3641 {ECO:0000313|EMBL:EOY14859.1, ECO:0000313|Proteomes:UP000026915}; RN [1] {ECO:0000313|EMBL:EOY14859.1, ECO:0000313|Proteomes:UP000026915} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=23731509; RA Motamayor J.C., Mockaitis K., Schmutz J., Haiminen N., Iii D.L., RA Cornejo O., Findley S.D., Zheng P., Utro F., Royaert S., Saski C., RA Jenkins J., Podicheti R., Zhao M., Scheffler B.E., Stack J.C., RA Feltus F.A., Mustiga G.M., Amores F., Phillips W., Marelli J.P., RA May G.D., Shapiro H., Ma J., Bustamante C.D., Schnell R.J., Main D., RA Gilbert D., Parida L., Kuhn D.N.; RT "The genome sequence of the most widely cultivated cacao type and its RT use to identify candidate genes regulating pod color."; RL Genome Biol. 14:R53-R53(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CM001886; EOY14859.1; -; Genomic_DNA. DR EnsemblPlants; EOY14859; EOY14859; TCM_034115. DR Gramene; EOY14859; EOY14859; TCM_034115. DR OMA; VILEIFH; -. DR Proteomes; UP000026915; Chromosome 8. DR ExpressionAtlas; A0A061FK28; differential. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000026915}; KW Reference proteome {ECO:0000313|Proteomes:UP000026915}. FT DOMAIN 321 487 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 544 AA; 60685 MW; 958C24CE6F6D519E CRC64; MSLCFCSLIR SSPLIYDSNF PWNLNLNRST YPISFSVHGN SRNLVARVVQ HGLEVNNISL PSPTIEAEEE KEVIRELGTG AAGAELVEHE PKPVRVRKKR AGDDDNDDES FEDRFKLRNG KEVFEEKAYL VGVERKGETL DSFGIEESLK ELAQLADTAG LMVVGSTYQK LSSPSPRTYI GSGKVAEIKS ATHAFGVETV IFDDELSPGQ LRNLEKAFGG DVRVCDRTAL ILDIFNQRAA THEAALQVAL AQMEYQLPRL TRMWTHLERQ AGGKVKGMGE KQIEVDKRIL RTQIGVLKKE LESVRKHRKQ YRNRRFSVPV PVVSLVGYTN AGKSTLLNQL TGANVLSEDR LFATLDPTTR RVQMKNGSEF LLTDTVGFIQ KLPTTLVAAF RATLEEISES SLLVHVVDIS HPLAEQQIDA VEKVLSELDV SAIPRLMVWN KVDRVSDPQR IKLEAERSED VVCASALTGD GLQEFCNAVQ EKLKDSMVPV EALVPFDKGE LLNTIHQVGM VEKTEYTENG TLVKAFVPLR FARLLTPMRQ LCKL // ID A0A061LTU2_9MICO Unreviewed; 590 AA. AC A0A061LTU2; DT 03-SEP-2014, integrated into UniProtKB/TrEMBL. DT 03-SEP-2014, sequence version 1. DT 05-JUL-2017, entry version 24. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=H490_0110580 {ECO:0000313|EMBL:EYT53163.1}; OS Leucobacter sp. UCD-THU. OC Bacteria; Actinobacteria; Micrococcales; Microbacteriaceae; OC Leucobacter. OX NCBI_TaxID=1292023 {ECO:0000313|EMBL:EYT53163.1, ECO:0000313|Proteomes:UP000026917}; RN [1] {ECO:0000313|EMBL:EYT53163.1, ECO:0000313|Proteomes:UP000026917} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=UCD-THU {ECO:0000313|EMBL:EYT53163.1, RC ECO:0000313|Proteomes:UP000026917}; RX PubMed=23792744; DOI=10.1128/genomeA.00325-13; RA Holland-Moritz H.E., Bevans D.R., Lang J.M., Darling A.E., Eisen J.A., RA Coil D.A.; RT "Draft Genome Sequence of Leucobacter sp. Strain UCD-THU (Phylum RT Actinobacteria)."; RL Genome Announc. 1:S69-S82(2013). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EYT53163.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; APJM01000020; EYT53163.1; -; Genomic_DNA. DR EnsemblBacteria; EYT53163; EYT53163; H490_0110580. DR Proteomes; UP000026917; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000026917}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000026917}. FT DOMAIN 372 537 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 590 AA; 63201 MW; 4E02DEC00F6710A4 CRC64; MTERFTEESD LALDDVVVNG EAGRGAKSAQ RSDRADSANA ASQADASEAP AAGDEPGASA ARSGADSGTP DDDSHAADSA DPLERLLARA ARGGSATVIR DAAARSGGLG VDNLTGGAQA LGDEVHDRLA EDLELIRLER EERASLTRVA GLSTELEDVT EVEYRQLRLE NAVLIGVYTG SARHGLEEAE NSLRELAALA ETAGARVLDG LLQRRAHPDP ATYLGKGKAQ ELAELVAAVG ADTVVADTEL APSQRRALED VVKVKVIDRT AVILDIFSQH AKSREGKAQV ELAQLEYLLP RLRGWGESMS RQAGGQVGSG GAGMGSRGPG ETKMELDRRK IHTRMAKLRK QIAGFAPARD AKRANRKRGE VPSVAIAGYT NAGKSSLLNR LTGTQELVQN QLFATLDTAV RHAETADGRR FTYADTVGFV RNLPHQLVEA FRSTFEEVGE ADVILHVVDG SHPDPAAQLR TVRDVIAEVD AQGIPEIVAF NKADLLDESQ RLVLHGLAPD AVFVSARTGE GVEELRRRID AALPVPDREV TVVVPYDRGE LVAELHERNR VLSTEYVEQG TRVRAYVTGE MLAKLDPYLA // ID A0A061NY26_9BACL Unreviewed; 408 AA. AC A0A061NY26; DT 03-SEP-2014, integrated into UniProtKB/TrEMBL. DT 03-SEP-2014, sequence version 1. DT 07-JUN-2017, entry version 22. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=JCM19038_2761 {ECO:0000313|EMBL:GAK08959.1}; OS Geomicrobium sp. JCM 19038. OC Bacteria; Firmicutes; Bacilli; Bacillales; Geomicrobium. OX NCBI_TaxID=1460635 {ECO:0000313|EMBL:GAK08959.1, ECO:0000313|Proteomes:UP000027014}; RN [1] {ECO:0000313|EMBL:GAK08959.1, ECO:0000313|Proteomes:UP000027014} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=JCM 19038 {ECO:0000313|EMBL:GAK08959.1, RC ECO:0000313|Proteomes:UP000027014}; RA Kudo T., Nakahara T., Zhang X., Taniyama S., Arakawa O., Murase S., RA Nakata H., Oshima K., Suda W., Kitamura K., Iida T., Oshida Y., RA Inoue T., Hongoh Y., Hattori M., Ohkuma M.; RT "Draft Genome Sequences of Geomicrobium sp. Strains JCM 19037, JCM RT 19038, JCM 19039, and JCM 19055, Isolated from Aquatic Samples."; RL Genome Announc. 2:e00622-14(2014). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:GAK08959.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BAXA01000010; GAK08959.1; -; Genomic_DNA. DR RefSeq; WP_042418675.1; NZ_BAXA01000010.1. DR EnsemblBacteria; GAK08959; GAK08959; JCM19038_2761. DR Proteomes; UP000027014; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR Gene3D; 3.40.50.620; -; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR014729; Rossmann-like_a/b/a_fold. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000027014}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000027014}. FT DOMAIN 194 358 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 6 29 {ECO:0000256|SAM:Coils}. FT COILED 153 187 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 408 AA; 45775 MW; 2813CC3C12D3BA79 CRC64; MERVIVVAVI EENEKEEEAQ QSLEELKSLV HTAHGTVVHT ETQNRKTAHV TSYVGSGKME ELKELVEEHE ADVIIINGEL SPRQGYTLSA NTEAAVIDRT QLILDIFAER ARTKEGRIQV ELAQMTYLLP RLRGQGHSLS RLGGGIGTRG PGETKLETDR RHIQRRMDEL KRELKRIVKH RQLLKNNKHQ RLVPKVALVG YTNAGKTTLL NALTDEEAFA EDLLFATLDP LTREYRLPSG LHVAISDTVG FIRDLPTTLI AAFRSTLEEV SDSDLLLRVI DVTSPYMSEE QETIDTLLEE LGATGIPSIT VLNKYDRTNP IPNGVEQLKN PKVYISAKHK DNLHALNAQI EIALKEDMQA YTLTVGASEG KRLARLKTTT IVEYIEFDES DEVYTVTGFA NRSHPEIN // ID A0A061P8H2_9BACL Unreviewed; 411 AA. AC A0A061P8H2; DT 03-SEP-2014, integrated into UniProtKB/TrEMBL. DT 03-SEP-2014, sequence version 1. DT 12-APR-2017, entry version 19. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=JCM19039_673 {ECO:0000313|EMBL:GAK11005.1}; OS Geomicrobium sp. JCM 19039. OC Bacteria; Firmicutes; Bacilli; Bacillales; Geomicrobium. OX NCBI_TaxID=1460636 {ECO:0000313|EMBL:GAK11005.1, ECO:0000313|Proteomes:UP000027177}; RN [1] {ECO:0000313|EMBL:GAK11005.1, ECO:0000313|Proteomes:UP000027177} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=JCM 19039 {ECO:0000313|EMBL:GAK11005.1, RC ECO:0000313|Proteomes:UP000027177}; RA Kudo T., Nakahara T., Zhang X., Taniyama S., Arakawa O., Murase S., RA Nakata H., Oshima K., Suda W., Kitamura K., Iida T., Oshida Y., RA Inoue T., Hongoh Y., Hattori M., Ohkuma M.; RT "Draft Genome Sequences of Geomicrobium sp. Strains JCM 19037, JCM RT 19038, JCM 19039, and JCM 19055, Isolated from Aquatic Samples."; RL Genome Announc. 2:e00622-14(2014). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:GAK11005.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BAXB01000002; GAK11005.1; -; Genomic_DNA. DR EnsemblBacteria; GAK11005; GAK11005; JCM19039_673. DR Proteomes; UP000027177; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000027177}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000027177}. FT DOMAIN 194 358 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 411 AA; 46026 MW; A76B2CF0580A9BA9 CRC64; MERVIVVAVI NEKKDEALQY RSVEELKSLV TTAHGTVVHT SLQNRRTADV SRYVGSGKVD ELSELASELD VDLIVINDEL SPRQGQSLAE STGVAVIDRT QLILDIFAER ARTREGKIQV ELAQLTYLLP RLRGQGLSLS RLGGGIGTRV PGETKLETDR RHIHRRMDEL KRDLVRVQKH RNVRKHQKQQ GERLHITLVG YTNAGKTTLL NALTDEHAFA EDLLFATLDP LTRRLRLPSG LEVQVSDTVG FIRDLPTTLI ASFRSTLEEV TEADLLVHVV DASSEHADDE VKTVEALLQD LGASGIETIT VLNKQDEHHS NRETLVSGNA PRIEVSAKTG RNMTELLHLL EKQIISFMEP YEQVVPAGDG KQLSRLKSTT IVQKEDFDEQ TESYFVKGYA RSQNCYVNKD N // ID A0A061Q9G8_9PROT Unreviewed; 453 AA. AC A0A061Q9G8; DT 03-SEP-2014, integrated into UniProtKB/TrEMBL. DT 03-SEP-2014, sequence version 1. DT 12-APR-2017, entry version 18. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:GAK32880.1}; GN ORFNames=AQ1_00755 {ECO:0000313|EMBL:GAK32880.1}; OS alpha proteobacterium Q-1. OC Bacteria; Proteobacteria; Alphaproteobacteria. OX NCBI_TaxID=1492281 {ECO:0000313|EMBL:GAK32880.1, ECO:0000313|Proteomes:UP000027360}; RN [1] {ECO:0000313|EMBL:GAK32880.1, ECO:0000313|Proteomes:UP000027360} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Q-1 {ECO:0000313|EMBL:GAK32880.1, RC ECO:0000313|Proteomes:UP000027360}; RX PubMed=22447601; DOI=10.1128/AEM.00084-12; RA Suzuki M., Eda Y., Ohsawa S., Kanesaki Y., Yoshikawa H., Tanaka K., RA Muramatsu Y., Yoshikawa J., Sato I., Fujii T., Amachi S.; RT "Iodide oxidation by a novel multicopper oxidase from the RT alphaproteobacterium strain Q-1."; RL Appl. Environ. Microbiol. 78:3941-3949(2012). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:GAK32880.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BAYV01000009; GAK32880.1; -; Genomic_DNA. DR EnsemblBacteria; GAK32880; GAK32880; AQ1_00755. DR Proteomes; UP000027360; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000027360}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000027360}. FT DOMAIN 222 395 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 453 AA; 49986 MW; 154918CC7FA8E6F2 CRC64; MIHITDEHVG LRSPHDGEQP TRALVIHPWV KKNAHKTAYD DKARSPAARL EEAVGLAMAI NITVERAELV ALAPARPATL LGKGKVAEMG SYIAEHSIDL VIMDAELSPV QQRNLEREWK TKVIDRTGLI LEIFGERAAT KEGELQVELA HLNYQKSRLV RSWTHLERQR GGFGFIGGPG ETQIEADRRI ITDRIAQIKR QLETVTRTRE LHRTRRQKAP YPVVALVGYT NAGKSTLFNR LTHSDVLAAD MLFATLDPTM RSIDLVTGRK VILSDTVGFI SDLPTHLIAA FRATLEEVIS ADLIVHVRDV AHPDSEAQKA DVLHVLADLG VKPGEVAGPM MIEALNKIDL LPDDERDALV NLSQKSPHDV PVSALSGAGL DELMERIDQC VGADDSVHDL IIEPWRGGDL SWLHRHGEVL AQSADDEGRT HVKVRIDPVS HAKFLAQQGG DQS // ID A0A061SUH5_9RHOB Unreviewed; 425 AA. AC A0A061SUH5; DT 03-SEP-2014, integrated into UniProtKB/TrEMBL. DT 03-SEP-2014, sequence version 1. DT 12-APR-2017, entry version 19. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=PM02_08500 {ECO:0000313|EMBL:KAJ03383.1}; OS Sulfitobacter mediterraneus. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae; Sulfitobacter. OX NCBI_TaxID=83219 {ECO:0000313|EMBL:KAJ03383.1, ECO:0000313|Proteomes:UP000027337}; RN [1] {ECO:0000313|EMBL:KAJ03383.1, ECO:0000313|Proteomes:UP000027337} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=1FIGIMAR09 {ECO:0000313|EMBL:KAJ03383.1, RC ECO:0000313|Proteomes:UP000027337}; RX PubMed=24855294; RA Mas-Llado M., Pina-Villalonga J.M., Brunet-Galmes I., Nogales B., RA Bosch R.; RT "Draft Genome Sequences of Two Isolates of the Roseobacter Group, RT Sulfitobacter sp. Strains 3SOLIMAR09 and 1FIGIMAR09, from Harbors of RT Mallorca Island (Mediterranean Sea)."; RL Genome Announc. 2:e00350-14(2014). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KAJ03383.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JEMU01000006; KAJ03383.1; -; Genomic_DNA. DR EnsemblBacteria; KAJ03383; KAJ03383; PM02_08500. DR Proteomes; UP000027337; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000027337}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000027337}. FT DOMAIN 205 374 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 425 AA; 47022 MW; 8DD2DDBC7B2BA217 CRC64; MDDTDGPRVT RAWVLHPDIR SNPDRRDPKP ALEEAVSLAR ALPQLEVVGA DVVPLRSVSA GMLFGSGKIK EVHDLLEAAE VELVLVDGPV SPVQQRNLEK AWGVKLLDRT GLILEIFSDR AATREGVLQV EMAALNYQRT RLVRAWTHLE RQRGGLGFVG GPGETQIEAD RRAIDEQLVR LRRQLEKVVK TRALHRAARA KVPYPIVALV GYTNAGKSTL FNRLTGAEVM AKDMLFATLD PTMRSLVLPD GPEIILSDTV GFISDLPTEL VAAFRATLEE VLAADIICHV RDISHAETEE QARDVLEILT SLGVPEETRT FEIWNKIDQL TPEAADAMRQ RAERDENVLA ISAITGEGLE GLQAVVAEAL QGAVRDADLT LGFAEGKKRA WLFAQDVVQE ERQTDDGFEL TVRWSAQQEA QFQRL // ID A0A062TZ28_9RHOB Unreviewed; 438 AA. AC A0A062TZ28; DT 03-SEP-2014, integrated into UniProtKB/TrEMBL. DT 03-SEP-2014, sequence version 1. DT 07-JUN-2017, entry version 21. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=HY2_02475 {ECO:0000313|EMBL:KCZ50738.1}; OS Hyphomonas sp. T16B2. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Hyphomonadaceae; Hyphomonas. OX NCBI_TaxID=1280941 {ECO:0000313|EMBL:KCZ50738.1, ECO:0000313|Proteomes:UP000027006}; RN [1] {ECO:0000313|Proteomes:UP000027006} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=T16B2 {ECO:0000313|Proteomes:UP000027006}; RA Lai Q., Shao Z.; RT "Hyphomonas sp. T16B2 Genome Sequencing."; RL Submitted (APR-2013) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KCZ50738.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AWFA01000023; KCZ50738.1; -; Genomic_DNA. DR EnsemblBacteria; KCZ50738; KCZ50738; HY2_02475. DR PATRIC; fig|1280941.3.peg.1818; -. DR Proteomes; UP000027006; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000027006}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000027006}. FT DOMAIN 205 379 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 164 191 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 438 AA; 48735 MW; D06F7BAFBB2E3C7D CRC64; MNDKMIDRTP APEVAGAVIP WFTPANRPTE DRLQETAGLV EALGCELAFL RPEHVRKVNS SVLLSGGILD RLAEDLKVHE CTIAVIDGDL TPVQQRNLER RLEVKVIDRT GLILEIFGLR ARTKEGRLQV ELARLLYERS RLVRTWTHLE RQRGGGGFLS GPGESQLEAD RRMLDEKILR LRRDLEDVKR TRAVQRAGRK RSGKPVIALV GYTNAGKSTL FNRISGADVF ARDMPFATLD PTIRRFDLPT LGEAALIDTV GFITDLPTHL IDSFQATLEE AMQADLLVHV RDRSSPADLD QAHDVMLVLE RLQKETGLPL PPMIEAWNKS DALPPERAEA LSYAAHGDRE HSAVLVSALT GEGIEELLSE IEGALLRGAS ELMLDLAPAD GRARAWLHRN GDVISEEPTE SGHVELLVRL THDRLGQFFA EFPHMKAD // ID A0A062VQI6_9MICO Unreviewed; 501 AA. AC A0A062VQI6; DT 03-SEP-2014, integrated into UniProtKB/TrEMBL. DT 03-SEP-2014, sequence version 1. DT 07-JUN-2017, entry version 21. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=DC31_15505 {ECO:0000313|EMBL:KDA05794.1}; OS Microbacterium sp. CH12i. OC Bacteria; Actinobacteria; Micrococcales; Microbacteriaceae; OC Microbacterium. OX NCBI_TaxID=1479651 {ECO:0000313|EMBL:KDA05794.1, ECO:0000313|Proteomes:UP000027096}; RN [1] {ECO:0000313|EMBL:KDA05794.1, ECO:0000313|Proteomes:UP000027096} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CH12i {ECO:0000313|EMBL:KDA05794.1, RC ECO:0000313|Proteomes:UP000027096}; RA Ferreras E.R., DeMaayer P., Guerrero L.D., Aislabie J.M., Cowan D.A.; RT "Draft genome sequence of Microbacterium sp. strain CH12i, isolated RT from shallow groundwater in Cape Hallet, Antarctica."; RL Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KDA05794.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JHET01000007; KDA05794.1; -; Genomic_DNA. DR RefSeq; WP_036279628.1; NZ_JHET01000007.1. DR EnsemblBacteria; KDA05794; KDA05794; DC31_15505. DR Proteomes; UP000027096; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 2. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000027096}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000027096}. FT DOMAIN 283 448 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 501 AA; 54359 MW; 36BC4A54E928F7A5 CRC64; MTKATDETHS DEMLDRVLAN AETRTAARVF GGAQALQNSS TAAFGDHDGN QWDLEDRHAL RRVVGLSTEL EDVTEVEYRQ LRLENVVLVG VYPQGAQSDA ENSLRELAAL AETAGAVVLD AVLQRRPHPD PATYLGRGKA QELKDLVAAT GADTVIVDSE LAPSQRRALE DVVKVKVIDR TTVILDIFSQ HAKSREGKAQ VELAQLEYLL PRLRGWGDSM SRQAGGQVGA GGAGMGSRGP GETKIELDRR RIRTRMALLR RQIRDFTPAR DAKRAERKRN TIPSVAITGY TNAGKSSLLN ALTSAGVLVE NALFATLDAT VRRTATADGR VYTFTDTVGF VRNLPHQLVE AFRSTLEEVA DADIVLHIVD GAHPDPAGQL QTVRDVMGDV GARDIPEIVV FNKADLIPDD ERLVLQGLES HAHFVSSRTG EGIEELRLAI DEALPKPAVE VHARVPYDRG DLVAAVHETG VLLSAEHGED GTDIHAHVSE RLAAELAPFA R // ID A0A062X810_9LACO Unreviewed; 419 AA. AC A0A062X810; DT 03-SEP-2014, integrated into UniProtKB/TrEMBL. DT 03-SEP-2014, sequence version 1. DT 07-JUN-2017, entry version 22. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=Lani381_0102 {ECO:0000313|EMBL:KDA46888.1}; OS Lactobacillus animalis. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; OC Lactobacillus. OX NCBI_TaxID=1605 {ECO:0000313|EMBL:KDA46888.1, ECO:0000313|Proteomes:UP000027129}; RN [1] {ECO:0000313|EMBL:KDA46888.1, ECO:0000313|Proteomes:UP000027129} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=381-IL-28 {ECO:0000313|EMBL:KDA46888.1, RC ECO:0000313|Proteomes:UP000027129}; RA Sturino J.M., Rajendran M., Altermann E.; RT "Draft Genome Sequence of Lactobacillus animalis 381-IL-28."; RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KDA46888.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JMHU01000001; KDA46888.1; -; Genomic_DNA. DR RefSeq; WP_035446837.1; NZ_JMHU01000001.1. DR STRING; 930942.LaniK3_010100009228; -. DR EnsemblBacteria; KDA46888; KDA46888; Lani381_0102. DR PATRIC; fig|1605.9.peg.103; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR Proteomes; UP000027129; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000027129}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000027129}. FT DOMAIN 197 365 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 156 183 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 419 AA; 46775 MW; CFDAA286957031F9 CRC64; MTPVIIAGIE NEQENFDYTM AELASLAEAA NMEVTRQFKQ KLERPIAATY LGKGKAEEIK TAGAVTDSQI LILNDELTPT QIRNLENITE MRVLDRTALI LEIFAARAKT KEAKLQVQVA KLQYQLPRLH TGLTDKLDQQ TAGNAGGGYT NRGAGETKLE LNRRVIEKKI SALNKELKTI DKEHQTRRKQ RQRSGIKTAA LVGYTNAGKS TTLNGLLRLF GETENKEVFE KDMLFATLDT SVRRLRFDDN KEILLSDTVG FVSKLPHQLV KAFRTTLAEA ANADLLVQVV DLSDDHYQEM IETTEKTLAE IGVTDIPMLY VFNKADKLAV SYPSLAGREL TFSAQDDESL KALAELLKQE LFKDYQTHTY LIPYAKGNLV EELNQKATVL ETEYLADGTK LKAEVAPALA GRLSEHQLD // ID A0A063BE41_9BURK Unreviewed; 392 AA. AC A0A063BE41; DT 03-SEP-2014, integrated into UniProtKB/TrEMBL. DT 03-SEP-2014, sequence version 1. DT 07-JUN-2017, entry version 20. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=LIG30_3691 {ECO:0000313|EMBL:KDB07039.1}; OS Burkholderia sp. lig30. OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Burkholderia. OX NCBI_TaxID=1192124 {ECO:0000313|EMBL:KDB07039.1, ECO:0000313|Proteomes:UP000027020}; RN [1] {ECO:0000313|EMBL:KDB07039.1, ECO:0000313|Proteomes:UP000027020} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=LIG30 {ECO:0000313|Proteomes:UP000027020}; RA Woo H.L., Utturkar S.M., Klingeman D.M., Simmons B.A., DeAngelis K.M., RA Brown S.D., Hazen T.C.; RT "Draft Genome of the Lignin-degrading Burkholderia sp. Strain LIG30, RT Isolated from Wet Tropical Forest Soil."; RL Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KDB07039.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JGVW01000091; KDB07039.1; -; Genomic_DNA. DR EnsemblBacteria; KDB07039; KDB07039; LIG30_3691. DR PATRIC; fig|1192124.4.peg.3760; -. DR Proteomes; UP000027020; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000027020}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000027020}. FT DOMAIN 196 367 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 162 189 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 392 AA; 42886 MW; 6B908536CBA28FCD CRC64; MISDNLINAA LVGIDFGKTD FEASLEELSL LASSAGAHPA VTLTGRRSSP DAAMFVGSGK AEELRLACEA NDVEIVIFNH ALAPAQQRNL ERALDRRVVD RTSLILDIFA QRARSHEGKL QVELAQLQYL STRLIRAWTH LERQKGGIGL RGPGETQLET DRRLIGERIK MLKSRLDRLR RQHSTQRRQR ARSGTMSVSL VGYTNAGKST LFNALTKAQA YAADQLFATL DTTSRRVYLG GDVGQIVVSD TVGFIRELPH QLVAAFRATL EETIHADLLL HVVDASSAVR LEQIEQVNGV LHEIGADTIR QVLVFNKIDA VPELAARGDA VERDEYGNIS RVFLSARTGQ GLDALRAAIA EIATAEHLSG AMPLDGVPAE IHEDHTISEQ GR // ID A0A063Y741_9GAMM Unreviewed; 434 AA. AC A0A063Y741; DT 03-SEP-2014, integrated into UniProtKB/TrEMBL. DT 03-SEP-2014, sequence version 1. DT 07-JUN-2017, entry version 21. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=ADINL_1163 {ECO:0000313|EMBL:KDE40571.1}; OS Nitrincola lacisaponensis. OC Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales; OC Nitrincola. OX NCBI_TaxID=267850 {ECO:0000313|EMBL:KDE40571.1, ECO:0000313|Proteomes:UP000027318}; RN [1] {ECO:0000313|EMBL:KDE40571.1, ECO:0000313|Proteomes:UP000027318} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=4CA {ECO:0000313|EMBL:KDE40571.1, RC ECO:0000313|Proteomes:UP000027318}; RX PubMed=16280482; DOI=10.1099/ijs.0.63647-0; RA Dimitriu P.A., Shukla S.K., Conradt J., Marquez M.C., Ventosa A., RA Maglia A., Peyton B.M., Pinkart H.C., Mormile M.R.; RT "Nitrincola lacisaponensis gen. nov., sp. nov., a novel alkaliphilic RT bacterium isolated from an alkaline, saline lake."; RL Int. J. Syst. Evol. Microbiol. 55:2273-2278(2005). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KDE40571.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JMSZ01000016; KDE40571.1; -; Genomic_DNA. DR RefSeq; WP_036544794.1; NZ_JMSZ01000016.1. DR EnsemblBacteria; KDE40571; KDE40571; ADINL_1163. DR PATRIC; fig|267850.7.peg.1157; -. DR Proteomes; UP000027318; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000027318}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000027318}. FT DOMAIN 199 366 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 434 AA; 49181 MW; 60A484E3A09FE6C0 CRC64; MFFDRPESGE RAILVHIDLA SEAEAEDPRE LEELALSAGA DPICFMQGSR SDPSPRFFLG KGKVEELAEL VRMHEAELVI FNHSLSPAQE RNIEREIKCR VLDRTGLILD IFAQRARTHE GKLQVELAQL EHMSTRLVRG WTHLERQKGG IGLRGPGETQ LETDRRLLRA RIKAILKRLE KVRRQRDQGR RARVRAEIPT VSLVGYTNAG KSTLFNSLTS ANVYAADQLF ATLDPTLRKV QLPDAGPMIL ADTVGFIRHL PHKLVEAFRA TLQETAEADL LLHVIDCHDE ERDAHIEQVN DVLHEIGADD RPVLLVYNKI DLLPDFAPRV DRDEDGMPVR VWLSAQRGEG TDLLLAAVNE RLSGSMFEDT LHLSPAEGQF RSMLYARDAV LDERIDEDGR ISLKVRLQLK DFRQLLSRLQ IPAERYLSVV VDNE // ID A0A063YVQ8_9BACI Unreviewed; 415 AA. AC A0A063YVQ8; DT 03-SEP-2014, integrated into UniProtKB/TrEMBL. DT 03-SEP-2014, sequence version 1. DT 12-APR-2017, entry version 18. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=DI43_05430 {ECO:0000313|EMBL:KDE48387.1}; OS Geobacillus sp. CAMR12739. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus. OX NCBI_TaxID=1482738 {ECO:0000313|EMBL:KDE48387.1, ECO:0000313|Proteomes:UP000029104}; RN [1] {ECO:0000313|EMBL:KDE48387.1, ECO:0000313|Proteomes:UP000029104} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CAMR12739 {ECO:0000313|EMBL:KDE48387.1, RC ECO:0000313|Proteomes:UP000029104}; RA De Maayer P., Willliamson C.E., Vennard C.T., Danson M.J., Cowan D.A.; RT "The draft genomes of Geobacillus sp. CAMR5420 and CAMR12739."; RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KDE48387.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JHUR01000024; KDE48387.1; -; Genomic_DNA. DR EnsemblBacteria; KDE48387; KDE48387; DI43_05430. DR Proteomes; UP000029104; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000029104}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000029104}. FT DOMAIN 197 358 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 415 AA; 46282 MW; 807408B71B0A8CDC CRC64; MSREQAILVG CQLAGVDDER FRYSMEELAS LVATANGEVV AELTQKREAP HPATYIGKGK TEELAAIVKQ LEPDVVIFNS ELSPSQARNL TKMLGEVKVI DRTQLILDIF ARRARSKEGK LQVELAQLEY MLPRLSGQGE ALSRLGGGIG TRGPGETKLE TDRRHIRRRI DDIKSELVRI AEHRGRYRER RQKTQAFQVA LVGYTNAGKS TIFNRLTAAD SLEENLLFAT LDPLTRKCVL PCGYTVLVTD TVGFIQDLPT TLVAAFRSTL EEVTEADLLL HVVDSSHPDY VAHERTVSRL LAELGASSIP MVTVYNKSDQ KASEFIPTTT ASIMISALSA ADIDRLRYFL EEAVKQQMAR YDVSIPSGEG KLLARLKSDT ILHEWHYNEQ GGTYDCQGYV LPTHPLYGEL QSFQR // ID A0A066RIM4_9GAMM Unreviewed; 429 AA. AC A0A066RIM4; DT 03-SEP-2014, integrated into UniProtKB/TrEMBL. DT 03-SEP-2014, sequence version 1. DT 30-AUG-2017, entry version 23. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=EA58_17490 {ECO:0000313|EMBL:KDM90290.1}; OS Photobacterium galatheae. OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; OC Vibrionaceae; Photobacterium. OX NCBI_TaxID=1654360 {ECO:0000313|EMBL:KDM90290.1, ECO:0000313|Proteomes:UP000027192}; RN [1] {ECO:0000313|EMBL:KDM90290.1, ECO:0000313|Proteomes:UP000027192} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=S2753 {ECO:0000313|EMBL:KDM90290.1, RC ECO:0000313|Proteomes:UP000027192}; RA Machado H.R., Gram L.; RT "Draft genome sequence of Photobacterium halotolerans S2753: a RT solonamide, ngercheumicin and holomycin producer."; RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KDM90290.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JMIB01000034; KDM90290.1; -; Genomic_DNA. DR RefSeq; WP_036755398.1; NZ_JMIB01000034.1. DR EnsemblBacteria; KDM90290; KDM90290; EA58_17490. DR Proteomes; UP000027192; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000027192}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}. FT DOMAIN 198 365 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 429 AA; 48569 MW; 59B6E503CCB08FC7 CRC64; MFDRYEAGEQ AILVHINFTQ EGEWEDLSEF EMLVSSAGVN TLRVITGSRQ APHPKYYVGE GKAQEIADAV RAEGAEIVIF NHSLSPAQER NLERLCKCRV LDRTGLILDI FAQRARTHEG KLQVELAQLR HISTRLIRGW THLERQKGGI GLRGPGETQL ETDRRLLRER IKAILRRLDK VSKQRDQGRR ARSRADIPTI SLVGYTNAGK STLFNQVTNA EVYAADQLFA TLDPTLRKIE VEDVGTSILA DTVGFIRHLP HDLVAAFKAT LKETQEATLL LHVVDASDER YRENIDAVNA VLEEIEASDV PVLVVMNKID NLEDAEPRIE RDEDGIPRRV WVSARERLGI DLLFTALTER LAGTMVMHTL RLPPAVSGRI RSKFYQLGAI VREEYEQDGS LLLDVRLPMT DWARLQKREE QGLDDFILA // ID A0A066UKS2_9GAMM Unreviewed; 463 AA. AC A0A066UKS2; DT 03-SEP-2014, integrated into UniProtKB/TrEMBL. DT 03-SEP-2014, sequence version 1. DT 07-JUN-2017, entry version 22. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:KDN24749.1}; GN ORFNames=MBO_07278 {ECO:0000313|EMBL:KDN24749.1}; OS Moraxella bovoculi 237. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Moraxellaceae; Moraxella. OX NCBI_TaxID=743974 {ECO:0000313|EMBL:KDN24749.1, ECO:0000313|Proteomes:UP000035860}; RN [1] {ECO:0000313|EMBL:KDN24749.1, ECO:0000313|Proteomes:UP000035860} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=237 {ECO:0000313|EMBL:KDN24749.1, RC ECO:0000313|Proteomes:UP000035860}; RX PubMed=24970830; RA Calcutt M.J., Foecking M.F., Martin N.T., Mhlanga-Mutangadura T., RA Reilly T.J.; RT "Draft Genome Sequence of Moraxella bovoculi Strain 237T (ATCC BAA- RT 1259T) Isolated from a Calf with Infectious Bovine RT Keratoconjunctivitis."; RL Genome Announc. 2:e00612-14(2014). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KDN24749.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AOMT01000026; KDN24749.1; -; Genomic_DNA. DR RefSeq; WP_036366201.1; NZ_AOMT01000026.1. DR EnsemblBacteria; KDN24749; KDN24749; MBO_07278. DR Proteomes; UP000035860; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000035860}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000035860}. FT DOMAIN 200 365 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 159 193 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 463 AA; 52043 MW; E05D34F4AE4F4CAB CRC64; MQYFDRHDGG ENAILVHLDI REMIDPDDLE EFRLLVHSAG ANELDIITGG RNKPHAKYFV GTGKADEIAQ AVARHEADVV IFNHDLTPSQ ERNLEALIKC RVLDRTGLIL DIFAQRARTY EGKLQVELAQ LSHLATRLVR GWTHLERQKG GIGLRGPGET QLETDRRLLQ IRVNQLKNKL DKVKQTRSQG RAKRQKSDVP TVSLVGYTNA GKSTLFNRLA NDNIYAADQL FATLDATLRK VKWAGVGNVV LADTVGFVRH LPHELVESFH ATLEETLEAD LLLHVIDSSS PEMHEQIDAV NAVLDEIGVT APVLLVHNKI DRTDEMPTIH YKEQGVPHRV YVSARENLGM DELTQAVQEL LVGGLSDFTL TLPYHAGQFK NTLHELGVIT HSEFDDTGHE MLTVRLAKAK LKELLGKYHF NAFDVLPSHE ASQFLPELEE FEKVEVKAND DKDHNDDLDP FCL // ID A0A066WRR0_9FLAO Unreviewed; 410 AA. AC A0A066WRR0; DT 03-SEP-2014, integrated into UniProtKB/TrEMBL. DT 03-SEP-2014, sequence version 1. DT 07-JUN-2017, entry version 22. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=FEM21_18540 {ECO:0000313|EMBL:KDN55263.1}; OS Flavobacterium seoulense. OC Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales; OC Flavobacteriaceae; Flavobacterium. OX NCBI_TaxID=1492738 {ECO:0000313|EMBL:KDN55263.1, ECO:0000313|Proteomes:UP000027064}; RN [1] {ECO:0000313|EMBL:KDN55263.1, ECO:0000313|Proteomes:UP000027064} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=EM1321 {ECO:0000313|EMBL:KDN55263.1, RC ECO:0000313|Proteomes:UP000027064}; RA Shin S.-K., Yi H.; RT "Genome Sequence of Flavobacterium sp. EM1321."; RL Submitted (MAY-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KDN55263.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JNCA01000016; KDN55263.1; -; Genomic_DNA. DR RefSeq; WP_035659726.1; NZ_JNCA01000016.1. DR EnsemblBacteria; KDN55263; KDN55263; FEM21_18540. DR PATRIC; fig|1492738.3.peg.1843; -. DR Proteomes; UP000027064; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000027064}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000027064}. FT DOMAIN 200 386 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 410 AA; 47226 MW; E2BECA1E8179E695 CRC64; MLEKEVINFE KTAIVGIVTQ NQSEEKLNEY LDELEFLTFT AGGQVVKRFF QKVDKPNPKT FLGTGKIDEI HHYVKENGIS TIIFDDELTP SQQKNISKII DCKILDRTNL ILDIFAQRAE TSYARTQVEL AQCIYLLPRL SGLWTHLERQ KGGIGMRGPG ETEIETDRRI VRDRISLLKD KIKAIDKQMG TQRSNRGAMV RVALVGYTNV GKSTLMNAIG KSDVFVENKL FATLDTTVRK VVIKNLPFLL SDTVGFIRKL PTQLVDSFKS TLDEVREADL LLHVVDISHP DFEDHIASVN QILLDIKAGD KPVIMVFNKI DAYRHLTIDE DDLMTEKTTK HYTLEEWKST WMSRVGEQNA LFISATNKQN FEEFRERVYE AVRQIHITRF PYNKFLYPDY KEAIDKEENE // ID A0A066YN52_9ACTN Unreviewed; 1291 AA. AC A0A066YN52; DT 03-SEP-2014, integrated into UniProtKB/TrEMBL. DT 03-SEP-2014, sequence version 1. DT 05-JUL-2017, entry version 20. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=KCH_53760 {ECO:0000313|EMBL:KDN82903.1}; OS Kitasatospora cheerisanensis KCTC 2395. OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae; OC Kitasatospora. OX NCBI_TaxID=1348663 {ECO:0000313|EMBL:KDN82903.1, ECO:0000313|Proteomes:UP000027178}; RN [1] {ECO:0000313|EMBL:KDN82903.1, ECO:0000313|Proteomes:UP000027178} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=KCTC 2395 {ECO:0000313|EMBL:KDN82903.1, RC ECO:0000313|Proteomes:UP000027178}; RA Nam D.H.; RT "Draft Genome Sequence of Kitasatospora cheerisanensis KCTC 2395."; RL Submitted (MAY-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KDN82903.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JNBY01000099; KDN82903.1; -; Genomic_DNA. DR EnsemblBacteria; KDN82903; KDN82903; KCH_53760. DR PATRIC; fig|1348663.4.peg.5204; -. DR Proteomes; UP000027178; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW. DR GO; GO:0015969; P:guanosine tetraphosphate metabolic process; IEA:InterPro. DR CDD; cd01878; HflX; 1. DR CDD; cd05399; NT_Rel-Spo_like; 1. DR CDD; cd01668; TGS_RelA_SpoT; 1. DR Gene3D; 3.10.20.30; -; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR002912; ACT_dom. DR InterPro; IPR012675; Beta-grasp_dom. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR003607; HD/PDEase_dom. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR007685; RelA_SpoT. DR InterPro; IPR004095; TGS. DR InterPro; IPR012676; TGS-like. DR InterPro; IPR033655; TGS_RelA. DR Pfam; PF13291; ACT_4; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF13328; HD_4; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR Pfam; PF04607; RelA_SpoT; 1. DR Pfam; PF02824; TGS; 1. DR PRINTS; PR00326; GTP1OBG. DR SMART; SM00471; HDc; 1. DR SMART; SM00954; RelA_SpoT; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF81271; SSF81271; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51671; ACT; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000027178}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Kinase {ECO:0000313|EMBL:KDN82903.1}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000027178}; KW Transferase {ECO:0000313|EMBL:KDN82903.1}. FT DOMAIN 637 711 ACT. {ECO:0000259|PROSITE:PS51671}. FT DOMAIN 1070 1235 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 1029 1063 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 1291 AA; 139825 MW; 221E2C9B99696DCF CRC64; MLLPEVQMTI RSELAGSPSK QQAGRFSRAA LGRAGRAALL ATGRTPVPDA IEPIVQAHRV HHPQADLALL ARAYRVAEES HRGQTRKSGE PYITHPLAVT MILAQLGADT TTLVASLLHD TVEDTEVTLD QVAEDFGPEI AYLVDGVTKL EKVDFGAAAE PETFRKMLVA TGDDVRVMVI KLADRLHNMR TIRHMKPASQ VRIAKVTRDV LIPLAERLGI QVVKAELEDI VFATLHPDEY AYTDAVATAR AAAEDGVLAP FAAELGRQLG EAGIASAVTV RPRHLVSLHR VMIKRGAGPD GTGLRPADLG RLLVVVEENA DCYAVLGELH TCWTPLPGEF KDFVAAPKFN LYQSLHTAVA LPGGEVVEVL VRTRRMHEVA ETGVVALGDP RTDRQGAADD PEDRTDPARP GWLARLLEWQ QDTPDPDAFW SALTADLRDD REITAVTEDG TTLHLPAGAS CLDAAYLIGE ETGHRCIGAR INGRLTALST ELRDGDVLGL LTAPADDEDS GPDPEWLEYL RTPAARLAVE RRLAVRPAPA PAAARPPRPA PGARRAARAA RRRPADVPEL PGAAVRLARC CTPVPPDEVT GIVLRGGAVA VHRAGCPTGT RMLGGGRRPV AVRWLPGGAP QWGYRATLRA EALNRPRLLA DLTAAISGEG VSIHSAEVEP PRQLRVRHSY TLELADATAL PAVMRAMLRV SGVYDVYRPG GPEEVPGRAE AAAAPPAGGR SRPWRSRSRR RWRRRCRGRC PGPVRRLVKG MTRAQRACDH RGEFTAAPPC CPRARPDLSK DEMTSTFDSR TRSSESASRL TDLKAEALMD EDLAAFDEGL GNYDGEQYDR SERAALRRVA GLSTELQDVT EVEYRQLRLE RVVLVGVWTD GTLEEAENSM AELAALAETA GSEVLDGVIQ RRDKPDAATY IGSGKAQELR DLVASSGADT VVCDGELTPG QLIHLEDVVK VKVVDRTALI LDIFAQHAKS REGKAQVSLA QMQYMLPRLR GWGQSLSRQM GGGGSGTSGG GMATRGPGET KIETDRRRIR EKMAKLRKEI ADMKKGRDTK RQERRRHQVP SVAIAGYTNA GKSSLLNRLT GAGVLVENAL FATLDPTVRR AQTPSGRLYT LADTVGFVRH LPHHLVEAFR STMEEVAEAD LILHVVDGSH PEPETQLAAV REVIVSVEAQ NVPEIVVINK ADAADPAVLQ RLLRREPHAI VVSARSGHGI DELLALIDEE LPRPAVEIRA LVPYTRGDLV SRVHAEGELI ATEHTAEGTL LHAKVAAMLA GELERYAVVT A // ID A0A066ZRY6_HYDMR Unreviewed; 432 AA. AC A0A066ZRY6; DT 03-SEP-2014, integrated into UniProtKB/TrEMBL. DT 03-SEP-2014, sequence version 1. DT 07-JUN-2017, entry version 21. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=EI16_01665 {ECO:0000313|EMBL:KDN95044.1}; OS Hydrogenovibrio marinus. OC Bacteria; Proteobacteria; Gammaproteobacteria; Thiotrichales; OC Piscirickettsiaceae; Hydrogenovibrio. OX NCBI_TaxID=28885 {ECO:0000313|EMBL:KDN95044.1, ECO:0000313|Proteomes:UP000027341}; RN [1] {ECO:0000313|EMBL:KDN95044.1, ECO:0000313|Proteomes:UP000027341} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MH-110 {ECO:0000313|EMBL:KDN95044.1, RC ECO:0000313|Proteomes:UP000027341}; RA Cha H.J., Jo B.H., Hwang B.H.; RT "Draft genome sequence of Hydrogenovibrio marinus MH-110, a model RT organism for aerobic H2 metabolism."; RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KDN95044.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JMIU01000001; KDN95044.1; -; Genomic_DNA. DR RefSeq; WP_029908761.1; NZ_JMIU01000001.1. DR EnsemblBacteria; KDN95044; KDN95044; EI16_01665. DR Proteomes; UP000027341; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000027341}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000027341}. FT DOMAIN 201 369 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 432 AA; 48739 MW; D263FBFE3C3230C0 CRC64; MELFGRLEQR ELEKAVLVHV DFYQESDREI LEEFYELVDS AGAEVVELIT TKRQSPDPKY FVGKGKAEEI KNAVEVHEAD VVIVNHALSP AQERNLSKYL DCQVLDRVGL ILDIFAQRAR SHEGKLQVEL AQLKRMATRL VKGWSHLDRQ GGIGARGPGE TQLETDRRLI QGKIKQLETR IEKVRHQRQL GRRSRKKSDM PTVTIVGYTN AGKSTLFNQM TQAGVYAEDR LFATLDATLR KVRLPGAGSV IFADTVGFIR HIPHDLVAAF RSTLEETSEA NLLIHLVDAS DPHRDEKIAD VLDVIKEVGA EDVPQLLVFN KIDLLDPPVA PHVDLNDKQL PERVWISAQD EQGIELMLDA VASYFRGKFV TVKLTLDVTA GKRRAELYTL GTILDEGFDE QGNSQFTMCL TEQEWKAIQG WPEVKLAELQ DQ // ID A0A067GU40_CITSI Unreviewed; 237 AA. AC A0A067GU40; DT 03-SEP-2014, integrated into UniProtKB/TrEMBL. DT 03-SEP-2014, sequence version 1. DT 09-DEC-2015, entry version 8. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:KDO78846.1}; DE Flags: Fragment; GN ORFNames=CISIN_1g0075831mg {ECO:0000313|EMBL:KDO78846.1}; OS Citrus sinensis (Sweet orange) (Citrus aurantium var. sinensis). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae; OC Pentapetalae; rosids; malvids; Sapindales; Rutaceae; Aurantioideae; OC Citrus. OX NCBI_TaxID=2711 {ECO:0000313|EMBL:KDO78846.1, ECO:0000313|Proteomes:UP000027120}; RN [1] {ECO:0000313|EMBL:KDO78846.1, ECO:0000313|Proteomes:UP000027120} RP NUCLEOTIDE SEQUENCE. RG International Citrus Genome Consortium; RA Gmitter F., Chen C., Farmerie W., Harkins T., Desany B., Mohiuddin M., RA Kodira C., Borodovsky M., Lomsadze A., Burns P., Jenkins J., RA Prochnik S., Shu S., Chapman J., Pitluck S., Schmutz J., Rokhsar D.; RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; KK784878; KDO78846.1; -; Genomic_DNA. DR EMBL; KK784878; KDO78847.1; -; Genomic_DNA. DR Proteomes; UP000027120; Unassembled WGS sequence. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000027120}; KW Reference proteome {ECO:0000313|Proteomes:UP000027120}. FT DOMAIN 113 187 GTP-bdg_N. {ECO:0000259|Pfam:PF13167}. FT DOMAIN 190 221 GTP-bdg_M. {ECO:0000259|Pfam:PF16360}. FT NON_TER 237 237 {ECO:0000313|EMBL:KDO78846.1}. SQ SEQUENCE 237 AA; 26541 MW; 12D7270ADBFE884A CRC64; MLRAISVVKR TQLRSITQTL TFPISLHSYS YSSSKRQTKD NKDKDDLHDV VTLFNRDPDD PPRLFLVQPR LKPPTFLQAK LNEALCLANS LEEQRDGYFD TDFFDKELPP HVVVQNPSLK SGKARADTFF GPGTVETIKC HINGAESKGE LDAIFVNAIL SGIQQRNLER AWGKPVLDRV GLIIEIFNAH AHTKEAKLQA ELAALMYKKS RLVRVRGPDG RLTFGETGEA EVVSARG // ID A0A067HAJ9_CITSI Unreviewed; 248 AA. AC A0A067HAJ9; DT 03-SEP-2014, integrated into UniProtKB/TrEMBL. DT 03-SEP-2014, sequence version 1. DT 09-DEC-2015, entry version 8. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:KDO84666.1}; DE Flags: Fragment; GN ORFNames=CISIN_1g0093711mg {ECO:0000313|EMBL:KDO84666.1}; OS Citrus sinensis (Sweet orange) (Citrus aurantium var. sinensis). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae; OC Pentapetalae; rosids; malvids; Sapindales; Rutaceae; Aurantioideae; OC Citrus. OX NCBI_TaxID=2711 {ECO:0000313|EMBL:KDO84666.1, ECO:0000313|Proteomes:UP000027120}; RN [1] {ECO:0000313|EMBL:KDO84666.1, ECO:0000313|Proteomes:UP000027120} RP NUCLEOTIDE SEQUENCE. RG International Citrus Genome Consortium; RA Gmitter F., Chen C., Farmerie W., Harkins T., Desany B., Mohiuddin M., RA Kodira C., Borodovsky M., Lomsadze A., Burns P., Jenkins J., RA Prochnik S., Shu S., Chapman J., Pitluck S., Schmutz J., Rokhsar D.; RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; KK784874; KDO84666.1; -; Genomic_DNA. DR Proteomes; UP000027120; Unassembled WGS sequence. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF13167; GTP-bdg_N; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000027120}; KW Reference proteome {ECO:0000313|Proteomes:UP000027120}. FT DOMAIN 147 236 GTP-bdg_N. {ECO:0000259|Pfam:PF13167}. FT NON_TER 248 248 {ECO:0000313|EMBL:KDO84666.1}. SQ SEQUENCE 248 AA; 27531 MW; C26892D36173A19C CRC64; MSFSLCSLTR VSPQIHERNS QWSQNAKRSI FRLSLTNNSS RCICRVVEQG LEVEVASADT APQKQGPVID TKEEEEEQQE VFNGVATTES DNKALNSSYT AKKKKRDDDD SYENRFKLQN GREVFQEKSY LVGVERKGGA EYLFVIEESL KELAQLADTA GLMVVGSTHQ KLNSPNPRTY IGSGKVAEIK SAIHALGVET VIFDDELSAG QLRNLEKAFG GDVRVCDRTA LILDIFNQRA ATHEAALQ // ID A0A067KIM9_JATCU Unreviewed; 594 AA. AC A0A067KIM9; DT 03-SEP-2014, integrated into UniProtKB/TrEMBL. DT 03-SEP-2014, sequence version 1. DT 07-JUN-2017, entry version 12. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:KDP32120.1}; GN ORFNames=JCGZ_12581 {ECO:0000313|EMBL:KDP32120.1}; OS Jatropha curcas (Barbados nut). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae; OC Pentapetalae; rosids; fabids; Malpighiales; Euphorbiaceae; OC Crotonoideae; Jatropheae; Jatropha. OX NCBI_TaxID=180498 {ECO:0000313|EMBL:KDP32120.1, ECO:0000313|Proteomes:UP000027138}; RN [1] {ECO:0000313|EMBL:KDP32120.1, ECO:0000313|Proteomes:UP000027138} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC TISSUE=Young leaves {ECO:0000313|EMBL:KDP32120.1}; RX PubMed=24837971; RA Zhang L., Zhang C., Wu P., Chen Y., Li M., Jiang H., Wu G.; RT "Global Analysis of Gene Expression Profiles in Physic Nut (Jatropha RT curcas L.) Seedlings Exposed to Salt Stress."; RL PLoS ONE 9:E97878-E97878(2014). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; KK914593; KDP32120.1; -; Genomic_DNA. DR RefSeq; XP_012079461.1; XM_012224071.1. DR GeneID; 105639887; -. DR KEGG; jcu:105639887; -. DR Proteomes; UP000027138; Unassembled WGS sequence. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR CDD; cd01878; HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 2. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000027138}; KW Reference proteome {ECO:0000313|Proteomes:UP000027138}. FT DOMAIN 302 562 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 594 AA; 66022 MW; F9DC28E2EC1BC244 CRC64; MLALSSFKSR VKSLTQTLIA INQSQPESRI LPPISIISSP YSSKEEKDKD NYSVVSLYNR DPTSPPRLFV VQPRLRPDNF LQAKLNEALC LANSLEEQRD GFFDSDFFDK ALPPYIVVQN PILRSSRARA DTYFGPGTVD TIKCHINASE SKGEVDAVFV NSILSGIQQR NLERAWGKPV LDRVGLIIEI FNAHAHTKEA KLQSELAALM YKKSRLVRVR GPDGRYGFGT AGEAEVVSAR GRGSGGRGFI SGAGETELQL QRRRILERRN HLLSQIEEVR RTRALQRVAR KRHGGLDNKA LATVAVVGYT NAGKSTLVSA LSESDLYSDS RLFATLDPRL KSVILPSGRK VLLSDTVGFI SDLPVQLVKA FHATLEEVVE ADLLLHVIDC TAPNLDEHRT TVLQVLQQIG VSEEKLQSMI EVWNKIDYEE EEMGADESLD ASSWSTDEDD NASEISSEAK DDKANISSGV KDGEGDIEEI IDEDQGDYSD GWLLSENDQE MVNDQWLKSL DDQQGETLND SGIEKDLQPQ AQHGPHLKIS AITGVGLQEL LELIDERLKT QDETLKTQNV VERGFFDRKW RPSHTDDAGV AVQQ // ID A0A067L390_JATCU Unreviewed; 545 AA. AC A0A067L390; DT 03-SEP-2014, integrated into UniProtKB/TrEMBL. DT 03-SEP-2014, sequence version 1. DT 07-JUN-2017, entry version 13. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:KDP38559.1}; GN ORFNames=JCGZ_04484 {ECO:0000313|EMBL:KDP38559.1}; OS Jatropha curcas (Barbados nut). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae; OC Pentapetalae; rosids; fabids; Malpighiales; Euphorbiaceae; OC Crotonoideae; Jatropheae; Jatropha. OX NCBI_TaxID=180498 {ECO:0000313|EMBL:KDP38559.1, ECO:0000313|Proteomes:UP000027138}; RN [1] {ECO:0000313|EMBL:KDP38559.1, ECO:0000313|Proteomes:UP000027138} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC TISSUE=Young leaves {ECO:0000313|EMBL:KDP38559.1}; RX PubMed=24837971; RA Zhang L., Zhang C., Wu P., Chen Y., Li M., Jiang H., Wu G.; RT "Global Analysis of Gene Expression Profiles in Physic Nut (Jatropha RT curcas L.) Seedlings Exposed to Salt Stress."; RL PLoS ONE 9:E97878-E97878(2014). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; KK914362; KDP38559.1; -; Genomic_DNA. DR RefSeq; XP_012071935.1; XM_012216545.1. DR GeneID; 105633851; -. DR KEGG; jcu:105633851; -. DR KO; K03665; -. DR Proteomes; UP000027138; Unassembled WGS sequence. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000027138}; KW Reference proteome {ECO:0000313|Proteomes:UP000027138}. FT DOMAIN 322 488 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 545 AA; 60974 MW; 79BA2B582B04C10E CRC64; MIACHCSLIR PSPPINENYL LRSPNPNKLN FPFTFTFTTH STKSFRLITR VLQEGVEVVS PEDVSLPGPV IDTKEDKEEV HGLVNGVAGT VSEGTSVSST RVKKKKIQDE DTFEYRYKIQ NGKEVFEEKA YLVGVERKGE VDSFGIEESL KEVAQLADTA GLMVVGSTYQ KLASPNPRTY IGSGKVAEIK SAIHALDVET VIFDDELSPG QLRNLEKIFG RDVRVCDRTA LILDIFNQRA ATHEASLQVA LAQMEYQLPR LTKMWTHLER QAGGQVKGMG EKQIEVDKRI LRTQIGVLKK ELETVRKHRK QYRNRRTSVP VPVVSLVGYT NAGKSTLLNQ LTGADVLAED RLFATLDPTT RRVQMKNGSE FLLTDTVGFI QKLPTTLVAA FRATLEEIAE SSLLVHVVDI SHPLAEQQID AVDRVLSELD VSSIPKLMVW NKVDRVNDPS KIKLEVDKRQ DVVCISALNG DGLQEFCLSV QEKLKDSMVW VEALVPFEKG DLISTIHQVG MVERIEYMEN GTLVKAHVPL RFARLLTPMR QLCKA // ID A0A067QX51_ZOONE Unreviewed; 588 AA. AC A0A067QX51; DT 03-SEP-2014, integrated into UniProtKB/TrEMBL. DT 03-SEP-2014, sequence version 1. DT 07-JUN-2017, entry version 14. DE SubName: Full=Putative GTP-binding protein 6 {ECO:0000313|EMBL:KDR13950.1}; GN ORFNames=L798_11908 {ECO:0000313|EMBL:KDR13950.1}; OS Zootermopsis nevadensis (Dampwood termite). OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; OC Pterygota; Neoptera; Polyneoptera; Dictyoptera; Blattodea; Blattoidea; OC Termitoidae; Termopsidae; Zootermopsis. OX NCBI_TaxID=136037 {ECO:0000313|EMBL:KDR13950.1, ECO:0000313|Proteomes:UP000027135}; RN [1] {ECO:0000313|EMBL:KDR13950.1, ECO:0000313|Proteomes:UP000027135} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC TISSUE=Whole organism {ECO:0000313|EMBL:KDR13950.1}; RX PubMed=24845553; DOI=10.1038/ncomms4636; RA Terrapon N., Li C., Robertson H.M., Ji L., Meng X., Booth W., Chen Z., RA Childers C.P., Glastad K.M., Gokhale K., Gowin J., Gronenberg W., RA Hermansen R.A., Hu H., Hunt B.G., Huylmans A.K., Khalil S.M., RA Mitchell R.D., Munoz-Torres M.C., Mustard J.A., Pan H., Reese J.T., RA Scharf M.E., Sun F., Vogel H., Xiao J., Yang W., Yang Z., Yang Z., RA Zhou J., Zhu J., Brent C.S., Elsik C.G., Goodisman M.A., RA Liberles D.A., Roe R.M., Vargo E.L., Vilcinskas A., Wang J., RA Bornberg-Bauer E., Korb J., Zhang G., Liebig J.; RT "Molecular traces of alternative social organization in a termite RT genome."; RL Nat. Commun. 5:3636-3636(2014). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; KK852908; KDR13950.1; -; Genomic_DNA. DR EnsemblMetazoa; KDR13950; KDR13950; L798_11908. DR OMA; MDTVGFM; -. DR Proteomes; UP000027135; Unassembled WGS sequence. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR CDD; cd01878; HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000027135}; KW Reference proteome {ECO:0000313|Proteomes:UP000027135}. FT DOMAIN 363 529 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 588 AA; 66840 MW; FBF1C80E0BA6C1C9 CRC64; MKYLHNMITF SQNKCLNRSL SSFYKYGRYF STKNCYMRSK LDAVKYITCQ RNLNIVGLRR FTHLCSLTIV NLSFSENIYI SFVTSTKFPG QYKMSAINSS LPAVCMIKGS RSFFSGRQTW KYQSDINDPD NIDECEDKME DIDKEEYDDM VTRMLHLPDM GHQVLVVQPY VKWGSDKKRN TTPELQLAEA VALVDTLPKW KVVDKVKTAL HSLGRKTMFG TGNLEMLKER IRRDKQITAI FISTDVLRGL QHRELEEVFG VPVYDRYMVV IQIFKEHAVS KEAKLQIAMA EIPYLRMRLK GLIEGAVDHQ GAGMAAIGGA GETLFEVRKR ILNTREIKLK HMLEKLRNQR TLLRKKRHKL EYPVIAVVGY TNSGKTSLIK ALTGERDLEP KDHLFATLDV TAHGGELPSR LKVLYVDTVG FISDIPSHLI ESFVATLEDA MLADVIIHLC DISHPDCKAQ AETVTKTLKI LNPSSNLLDN ILVVGNKIDL LPERTQIQDL NCNVLVSAVT NQGLHDLIVQ LDKTILKATG RRSVVIRVKM GGEEVSWLYK YAAVTGVTTD SKNSNYLLMK VVISEAQLSR FQHIFIKR // ID A0A068NIC8_9BACT Unreviewed; 417 AA. AC A0A068NIC8; DT 01-OCT-2014, integrated into UniProtKB/TrEMBL. DT 01-OCT-2014, sequence version 1. DT 05-JUL-2017, entry version 21. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=OP10G_0005 {ECO:0000313|EMBL:AIE83373.1}; OS Fimbriimonas ginsengisoli Gsoil 348. OC Bacteria; Armatimonadetes; Fimbriimonadia; Fimbriimonadales; OC Fimbriimonadaceae; Fimbriimonas. OX NCBI_TaxID=661478 {ECO:0000313|EMBL:AIE83373.1, ECO:0000313|Proteomes:UP000027982}; RN [1] {ECO:0000313|EMBL:AIE83373.1, ECO:0000313|Proteomes:UP000027982} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Gsoil 348 {ECO:0000313|EMBL:AIE83373.1}; RX PubMed=24967843; RA Hu Z.Y., Wang Y.Z., Im W.T., Wang S.Y., Zhao G.P., Zheng H.J., RA Quan Z.X.; RT "The first complete genome sequence of the class fimbriimonadia in the RT phylum armatimonadetes."; RL PLoS ONE 9:E100794-E100794(2014). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP007139; AIE83373.1; -; Genomic_DNA. DR EnsemblBacteria; AIE83373; AIE83373; OP10G_0005. DR KEGG; fgi:OP10G_0005; -. DR KO; K03665; -. DR Proteomes; UP000027982; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000027982}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Hydrolase {ECO:0000313|EMBL:AIE83373.1}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Protease {ECO:0000313|EMBL:AIE83373.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000027982}. FT DOMAIN 198 364 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 417 AA; 47130 MW; 97C9A037821EF26E CRC64; MESLELLVER AVLVYLNEDE NEDRMVEAEL EGLCEAANVE PVASIRQRLD RPWKGTYVGK GKVLEISALA AEVDADLVLI DAELSGIQQR NLQDQIGRKV VDRTQLILDI FARRAKTREG MLQVELAQLT YMMPKLMSVY TKFERQKGGI GMRGPGETKL ESDRRLVKER IARLGDEIEE VKRVRAQQRA SRRKHPFPFA TIVGYTSAGK STLMNRFAGT ELLADAMPFA TLDPTTRKVD LEEGYAIFLT DTVGFIRNLP THLVAAFQST LEEVTFSDFA LHVVDVSTPS WEIQRDAVLE TLRILKADDK PIITVFNKID ALNDPTEARR LVAEFPNSVA ISATTGEGMD DLQNAIVRQV KDLLNSVQIL IPYDHQGVLQ ECYDFGRVRQ VEYREDGIYV EAELVNELRE RLRGYAI // ID A0A068QQL0_9GAMM Unreviewed; 426 AA. AC A0A068QQL0; DT 01-OCT-2014, integrated into UniProtKB/TrEMBL. DT 01-OCT-2014, sequence version 1. DT 30-AUG-2017, entry version 20. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:CDG16125.1}; GN ORFNames=XDD1_0422 {ECO:0000313|EMBL:CDG16125.1}; OS Xenorhabdus doucetiae. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; OC Morganellaceae; Xenorhabdus. OX NCBI_TaxID=351671 {ECO:0000313|EMBL:CDG16125.1, ECO:0000313|Proteomes:UP000032721}; RN [1] {ECO:0000313|EMBL:CDG16125.1, ECO:0000313|Proteomes:UP000032721} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=FRM16 / DSM 17909 {ECO:0000313|Proteomes:UP000032721}; RA Genoscope - CEA; RL Submitted (JUL-2013) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; FO704550; CDG16125.1; -; Genomic_DNA. DR RefSeq; WP_045968243.1; NZ_FO704550.1. DR EnsemblBacteria; CDG16125; CDG16125; XDD1_0422. DR KEGG; xdo:XDD1_0422; -. DR KO; K03665; -. DR Proteomes; UP000032721; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000032721}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000032721}. FT DOMAIN 198 365 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 426 AA; 48088 MW; 3271393AFBA59397 CRC64; MFDRYEGGEL AVLVHVFFSQ EKDTENLSEF ESLVTSAGVS PVQIVTGSRK APHPKYFVGE GKAEEIAEAV KNSGADVVLF DHALSPAQER NLERLCQCRV VDRTGVILDI FAQRARTHEG KLQVELAQLR HLSTRLVRGW THLERQKGGI GLRGPGETQL ESDRRMLRDK IKQILGRLGK VEKQREQGRQ ARNKADIPTV SLVGYTNAGK SSLFNTITSS EVYAADQLFA TLDPTLRRIE VDDVGTVVLA DTVGFIRHLP HDLVAAFKAT LQETRQARLL LHVVDAADTR VDENITAVDS VLEEIESHEI PSLMVMNKID MLEDFIPRID RDEENRPVRV WLSAQTGEGI PLLLQALTER LSGEIAHYKL HLPPEAGRLR SRFYQLQAIE REWMEENGEV GVEVRMPIVD WRRLCKQEPN LPDYVV // ID A0A068RA28_9GAMM Unreviewed; 426 AA. AC A0A068RA28; DT 01-OCT-2014, integrated into UniProtKB/TrEMBL. DT 01-OCT-2014, sequence version 1. DT 30-AUG-2017, entry version 24. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:CDG23070.1}; GN ORFNames=XPG1_3434 {ECO:0000313|EMBL:CDG23070.1}; OS Xenorhabdus poinarii G6. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; OC Morganellaceae; Xenorhabdus. OX NCBI_TaxID=1354304 {ECO:0000313|EMBL:CDG23070.1, ECO:0000313|Proteomes:UP000032735}; RN [1] {ECO:0000313|EMBL:CDG23070.1, ECO:0000313|Proteomes:UP000032735} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=G6 {ECO:0000313|EMBL:CDG23070.1, RC ECO:0000313|Proteomes:UP000032735}; RA Genoscope - CEA; RL Submitted (JUL-2013) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; FO704551; CDG23070.1; -; Genomic_DNA. DR RefSeq; WP_045960018.1; NZ_FO704551.1. DR EnsemblBacteria; CDG23070; CDG23070; XPG1_3434. DR KEGG; xpo:XPG1_3434; -. DR KO; K03665; -. DR Proteomes; UP000032735; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000032735}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000032735}. FT DOMAIN 198 365 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 426 AA; 48037 MW; B0A473AD08793967 CRC64; MFDRYEGGEL AVLVHVFFSQ EKDTENLSEF ESLVTSAGVS PVQIVTGSRK APHPKYFVGE GKAEEIADAV KNSGADVVLF NHPLSPAQER NLERLCQCRV VDRTGVILDI FAQRARTHEG KLQVELAQLR HLSTRLVRGW THLERQKGGI GLRGPGETQL ESDRRMLRDK IKQILGRLNK VEKQREQGRQ ARNKADIPTV SLVGYTNAGK SSLFNTITSS DVYAADQLFA TLDPTLRRIA VEDVGTVVLA DTVGFIRHLP HDLVAAFKAT LQETRQAKLL LHVVDAADNR LDQNIIAVDN VLEEIESHEI PALRVMNKID MLEDFIPRID RDEENRPVRV WLSAQTGEGI PLLLQALTER LSGEIAHYKL HLPPEAGRLR SRFYQLQAIE CEWMEENGQV GIEVRMPMVD WRRLCKKDPS LPGYIV // ID A0A068YQ90_9BURK Unreviewed; 383 AA. AC A0A068YQ90; DT 01-OCT-2014, integrated into UniProtKB/TrEMBL. DT 01-OCT-2014, sequence version 1. DT 07-JUN-2017, entry version 22. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; OS Polaromonas sp. CG9_12. OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Comamonadaceae; Polaromonas. OX NCBI_TaxID=1504672 {ECO:0000313|EMBL:CDS49088.1, ECO:0000313|Proteomes:UP000043372}; RN [1] {ECO:0000313|EMBL:CDS49088.1, ECO:0000313|Proteomes:UP000043372} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Smith H.J., Foreman C.M., Ramaraj T.; RT "Draft Genome Sequence of a Metabolically Diverse Antarctic RT Supraglacial Stream Organism, Polaromonas sp. Strain CG9_12, RT Determined Using Pacific Biosciences Single-Molecule Real-Time RT Sequencing Technology."; RL Genome Announc. 2:1-2(2014). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CCJP01000005; CDS49088.1; -; Genomic_DNA. DR RefSeq; WP_036804210.1; NZ_CCJP01000005.1. DR EnsemblBacteria; CDS49088; CDS49088; CDS49088. DR Proteomes; UP000043372; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000043372}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000043372}. FT DOMAIN 195 377 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 383 AA; 42463 MW; D727AC689067A1CD CRC64; MKTQALALLV GVDLGLPNFD TELLELGLLA QTAGLEPVAR VTCKRRAPDA ALFIGSGKAD EIKMLALDTG ATEVLFDQSL SPAQQRNLER HLEMPVNDRT LLILEIFAQR ARSHEGKLQV ELARLQYVST RLVRRWSHLE RQTGGAGVRG GPGEKQIELD KRMIGDAIKR TKERLTKVKK QRQTQRKQRE RRNSFSVSLV GYTNAGKSTL FNALVKATAY TADQLFATLD TTTRQLYLGE AGRFASLSDT VGFIRDLPHG LIDAFAATLK EAVDADLLLH VVDASNPDYL EQIEQVQRVL SEIGAEDVPQ ILVFNKLDAI ENSVLPLHLH DRFELRDAFE GASRSVERVF VSAMTGEGLN LLRELLAFQA SRLQSGNSPQ TPQ // ID A0A069CRQ1_9LACT Unreviewed; 427 AA. AC A0A069CRQ1; DT 01-OCT-2014, integrated into UniProtKB/TrEMBL. DT 01-OCT-2014, sequence version 1. DT 07-JUN-2017, entry version 20. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:GAK30052.1}; GN ORFNames=WOSG25_011420 {ECO:0000313|EMBL:GAK30052.1}; OS Weissella oryzae SG25. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Leuconostocaceae; OC Weissella. OX NCBI_TaxID=1329250 {ECO:0000313|EMBL:GAK30052.1, ECO:0000313|Proteomes:UP000030643}; RN [1] {ECO:0000313|EMBL:GAK30052.1, ECO:0000313|Proteomes:UP000030643} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SG25 {ECO:0000313|EMBL:GAK30052.1, RC ECO:0000313|Proteomes:UP000030643}; RA Tanizawa Y., Fujisawa T., Mochizuki T., Kaminuma E., Suzuki Y., RA Nakamura Y., Tohno M.; RT "Draft Genome Sequence of Weissella oryzae SG25T, Isolated from RT Fermented Rice Grains."; RL Genome Announc. 2:e00667-14(2014). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; DF820484; GAK30052.1; -; Genomic_DNA. DR RefSeq; WP_027698194.1; NZ_DF820484.1. DR EnsemblBacteria; GAK30052; GAK30052; WOSG25_011420. DR Proteomes; UP000030643; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000030643}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000030643}. FT DOMAIN 204 373 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 427 AA; 47400 MW; 92D34BFC9A7FDA45 CRC64; MYDNEQSPLQ PVVLVGLDRG NEQFDYQMIE LANLANANHM TVVDTVTQKL ERPNSATYFG KGKIEELNEL LKTLDVKMVV ANDELSPSQI RNIEQGTNAT VMDRTALILD IFASRAKTRL AKLQVQIAQL QYQLPRLRTS MNIRLDQQTG GGGSSFTSRG AGETKLETNR RLIEHQISAL RKELAEIQAD DDTRRAQRSK QNIKNVALIG YTNAGKSTIM NGLVSRYGEN QAKLVFQADM LFATLETSVR KINLPDKQNF ILSDTVGFVS QLPHNLVAAF RATLAEAAQA DLLVQVVDYA DPHYQEMMAT TQSTLNEIGV GDIPMITVYN KADLRADTVF PERTGDILTL SAVDEASLDL LVETVREHIF ADHVQVKLLI PFSEGQLVSD LNENATVHDL TYSEAGTELV VTLTPAQAGR YDNYIIK // ID A0A069CYT8_9BACE Unreviewed; 415 AA. AC A0A069CYT8; DT 01-OCT-2014, integrated into UniProtKB/TrEMBL. DT 01-OCT-2014, sequence version 1. DT 07-JUN-2017, entry version 20. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=JCM15093_897 {ECO:0000313|EMBL:GAK35773.1}; OS Bacteroides graminisolvens DSM 19988 = JCM 15093. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae; OC Bacteroides. OX NCBI_TaxID=1121097 {ECO:0000313|EMBL:GAK35773.1, ECO:0000313|Proteomes:UP000027601}; RN [1] {ECO:0000313|EMBL:GAK35773.1, ECO:0000313|Proteomes:UP000027601} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=JCM 15093 {ECO:0000313|EMBL:GAK35773.1, RC ECO:0000313|Proteomes:UP000027601}; RX PubMed=25736980; RA Inoue J., Oshima K., Suda W., Sakamoto M., Iino T., Noda S., RA Hongoh Y., Hattori M., Ohkuma M.; RT "Distribution and evolution of nitrogen fixation genes in the phylum RT bacteroidetes."; RL Microbes Environ. 30:44-50(2015). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:GAK35773.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BAJS01000003; GAK35773.1; -; Genomic_DNA. DR RefSeq; WP_024995847.1; NZ_BAJS01000003.1. DR EnsemblBacteria; GAK35773; GAK35773; JCM15093_897. DR Proteomes; UP000027601; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000027601}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000027601}. FT DOMAIN 210 394 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 415 AA; 46894 MW; 2A2576BCACB2559B CRC64; MKEFVISEAQ AETAVLVALI TQSQDERKTN EYLDELAFLA ETAGADVVKK FTQRLDMANS VTYVGKGKLQ EIKDYVTENE VGMVIFDDEL SAKQIRNIEG ELQVKILDRT SLILDIFAMR AQTAHAKTQV ELAQYKYMLP RLTRLWTHLE RQGGGSGGGK GGSVGLRGPG ETQLEMDRRI ILGRMSLLKG QLADIDKQKA TQRKNRGSMI RVALVGYTNV GKSTLMNLLS KSDVFAENKL FATLDTTVRK VIIENLPFLL SDTVGFIRKL PTDLVESFKS TLDEVREADL LLHVVDISHP GFEEQIEIVN KTLADIGGAG KPCILIFNKI DAYTYVEKAP DDLTPRTKDN LTLEELMNTW MAKMEDNCLF ISAREKVNME EFKSVVYNRV KALHVQRFPY NDFLYQTYDK DEEIE // ID A0A069D9S4_9BACL Unreviewed; 430 AA. AC A0A069D9S4; DT 01-OCT-2014, integrated into UniProtKB/TrEMBL. DT 01-OCT-2014, sequence version 1. DT 07-JUN-2017, entry version 20. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=TCA2_2021 {ECO:0000313|EMBL:GAK39533.1}; OS Paenibacillus sp. TCA20. OC Bacteria; Firmicutes; Bacilli; Bacillales; Paenibacillaceae; OC Paenibacillus. OX NCBI_TaxID=1499968 {ECO:0000313|EMBL:GAK39533.1, ECO:0000313|Proteomes:UP000028160}; RN [1] {ECO:0000313|EMBL:GAK39533.1, ECO:0000313|Proteomes:UP000028160} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=TCA20 {ECO:0000313|EMBL:GAK39533.1, RC ECO:0000313|Proteomes:UP000028160}; RA Fujinami S., Takeda-Yano K., Onodera T., Satoh K., Sano M., RA Takahashi Y., Narumi I., Ito M.; RT "Draft Genome Sequence of Calcium-Dependent Paenibacillus sp. Strain RT TCA20, Isolated from a Hot Spring Containing a High Concentration of RT Calcium Ions."; RL Genome Announc. 2:e00866-14(2014). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:GAK39533.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BBIW01000002; GAK39533.1; -; Genomic_DNA. DR RefSeq; WP_047910664.1; NZ_BBIW01000002.1. DR EnsemblBacteria; GAK39533; GAK39533; TCA2_2021. DR Proteomes; UP000028160; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000028160}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000028160}. FT DOMAIN 208 372 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 430 AA; 48145 MW; 9A8D621AA05F62EB CRC64; MSNSTHETST EIKDKAVLVS LVTDEVKRSG INPEYSLEEL VKLAETAGVE VLSVISQNRE TPDSKWFIGK GKVEELRAAA EELGATTAIF DQELSGAQVR NLEESLDLKI IDRTQLILDI FAQRAHTREG IIQVELAQHS YLLPRLSGHG KNLSRLGGGI GTRGPGESKL ETDRRHIRGR ITDLKRQLEE VTRHRTLHRE RRKKSGVIQV ALVGYTNAGK STLLKQLTSA DVYIENQLFA TLDPTSRTLE LPSGKEIVLT DTVGFIQNLP HELVAAFRAT LEEVNEADLI LHVVDASSTM REEQMNVVEK LLQELGASDK PQIVLFNKKD ACSPEQLQML PTGKGYRKIS AFDEQDLLSI RELIQEELTG DTVKFRIPAE RGDITSVVYR IGDVIETTYD ENDVIYEVQV QKGEYEKHGY LLKDFIDSSN // ID A0A069DA59_9BACL Unreviewed; 423 AA. AC A0A069DA59; DT 01-OCT-2014, integrated into UniProtKB/TrEMBL. DT 01-OCT-2014, sequence version 1. DT 07-JUN-2017, entry version 20. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=TCA2_1758 {ECO:0000313|EMBL:GAK39270.1}; OS Paenibacillus sp. TCA20. OC Bacteria; Firmicutes; Bacilli; Bacillales; Paenibacillaceae; OC Paenibacillus. OX NCBI_TaxID=1499968 {ECO:0000313|EMBL:GAK39270.1, ECO:0000313|Proteomes:UP000028160}; RN [1] {ECO:0000313|EMBL:GAK39270.1, ECO:0000313|Proteomes:UP000028160} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=TCA20 {ECO:0000313|EMBL:GAK39270.1, RC ECO:0000313|Proteomes:UP000028160}; RA Fujinami S., Takeda-Yano K., Onodera T., Satoh K., Sano M., RA Takahashi Y., Narumi I., Ito M.; RT "Draft Genome Sequence of Calcium-Dependent Paenibacillus sp. Strain RT TCA20, Isolated from a Hot Spring Containing a High Concentration of RT Calcium Ions."; RL Genome Announc. 2:e00866-14(2014). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:GAK39270.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BBIW01000002; GAK39270.1; -; Genomic_DNA. DR RefSeq; WP_047910454.1; NZ_BBIW01000002.1. DR EnsemblBacteria; GAK39270; GAK39270; TCA2_1758. DR Proteomes; UP000028160; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000028160}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000028160}. FT DOMAIN 199 369 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 158 192 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 423 AA; 47678 MW; 9183FDB5EFF806F0 CRC64; MTQPFKDKAV IIGLQMNGQE DFEHSMEELG NLANACDIEV AAVLTQKAER IHPAHYIGSG KIEELSDLLK MLETTIVIFN DELSPSQVRN LEKRLDAAVL DRTTLILNIF AERARSRESQ LQVELARLQY VLPRLSGISS SSGRQRGGVG TKNRGSGETK LELSQRRIEE KITELNRELE LLVSQRQTQR RRRQKTEMPV VSLVGYTNTG KSSLMNAMLD KYDAASDKAV LAKDMLFATL QTSVRQISLP DRKRFLLTDT VGFVSKLPHH LVKAFRSTLE EVLESDLLLH VVDASNSDAE QLIEVTNQTL KDLGADKIPV VYVYNKIDLS SELMKEIQVR RPAVFVSAKT GQGLDQLEDA IKEQLFGHYE RVALNIPYDQ GHLLSYFHEH ANVETVLYEE DGTKLTIEAS PVEVKKWSHL QAE // ID A0A069K0Z3_9ACTN Unreviewed; 506 AA. AC A0A069K0Z3; DT 01-OCT-2014, integrated into UniProtKB/TrEMBL. DT 01-OCT-2014, sequence version 1. DT 05-JUL-2017, entry version 24. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=DT87_22715 {ECO:0000313|EMBL:KDQ69900.1}; OS Streptomyces sp. NTK 937. OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae; OC Streptomyces. OX NCBI_TaxID=1487711 {ECO:0000313|EMBL:KDQ69900.1, ECO:0000313|Proteomes:UP000027475}; RN [1] {ECO:0000313|EMBL:KDQ69900.1, ECO:0000313|Proteomes:UP000027475} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NTK 937 {ECO:0000313|EMBL:KDQ69900.1, RC ECO:0000313|Proteomes:UP000027475}; RA Olano C., Cano-Prieto C., Losada A., Mendez C., Salas J.A.; RT "Draft genome sequence of marine actinomycete Streptomyces sp. NTK RT 937, producer of the benzoxazol antibiotic caboxamycin."; RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KDQ69900.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JJOB01000001; KDQ69900.1; -; Genomic_DNA. DR RefSeq; WP_028443693.1; NZ_JJOB01000001.1. DR EnsemblBacteria; KDQ69900; KDQ69900; DT87_22715. DR Proteomes; UP000027475; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 2. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000313|EMBL:KDQ69900.1}; KW Complete proteome {ECO:0000313|Proteomes:UP000027475}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900, KW ECO:0000313|EMBL:KDQ69900.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000027475}. FT DOMAIN 285 450 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 506 AA; 54865 MW; 001D94A1738BBDBA CRC64; MTSSSSLPQD AQDAQSATDT ASESLTESLR ADALMEEDVA WSHEIDTERD GEQLDRSERA ALRRVAGLST ELEDVTEVEY RQLRLERVVL VGVWTSGTVT DAQNSLAELA ALAETAGAMV LDAVFQRRDK PDPATYIGSG KALELRDIVL ESGADTVVCD GELSPGQLIH LEDVVKVKVV DRTALILDIF AQHAKSREGK AQVSLAQMQY MLPRLRGWGQ SLSRQMGGGG SSGGGGMATR GPGETKIETD RRRIREKMAK MRREIAEMKT GREIKRQERR RNKVPSVAIA GYTNAGKSSL LNRLTGAGVL VENALFATLD PTVRRAETPS GRLYTLADTV GFVRHLPHHL VEAFRSTMEE VGESDLILHV VDGAHPVPEE QLAAVREVIR DVGAVDVPEI VVINKADAAD PLVLQRLLRN EKHAIAVSAR TGAGIDELLA LIDAELPRPS VEIEALVPFT QGALVSRVHA EGEVVSEEHT PEGTLLKARV HEELAAELST FVPAAH // ID A0A069Q1Y2_9BURK Unreviewed; 414 AA. AC A0A069Q1Y2; DT 01-OCT-2014, integrated into UniProtKB/TrEMBL. DT 01-OCT-2014, sequence version 1. DT 07-JUN-2017, entry version 22. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=BG61_28755 {ECO:0000313|EMBL:KDR43771.1}, GN BGLT_04467 {ECO:0000313|EMBL:CDY75568.1}; OS Caballeronia glathei. OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Caballeronia. OX NCBI_TaxID=60547 {ECO:0000313|EMBL:KDR43771.1, ECO:0000313|Proteomes:UP000027466}; RN [1] {ECO:0000313|EMBL:KDR43771.1, ECO:0000313|Proteomes:UP000027466} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 50014 {ECO:0000313|EMBL:KDR43771.1, RC ECO:0000313|Proteomes:UP000027466}; RA Liu X.Y., Li C.X., Xu J.H.; RT "Draft Genome Sequences of Four Burkholderia Strains."; RL Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:CDY75568.1} RP NUCLEOTIDE SEQUENCE. RA Carlier L.Aurelien.; RL Submitted (AUG-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CCNS02000036; CDY75568.1; -; Genomic_DNA. DR EMBL; JFHC01000005; KDR43771.1; -; Genomic_DNA. DR RefSeq; WP_035930457.1; NZ_JFHC01000005.1. DR EnsemblBacteria; KDR43771; KDR43771; BG61_28755. DR Proteomes; UP000027466; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000027466}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000027466}. FT DOMAIN 191 362 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 157 184 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 414 AA; 45329 MW; A8128C5DB91260B5 CRC64; MINAALVGID FGKIDFEASL EELSLLAQSA GANPAVTLTG RRTSPDAKMF VGSGKVEELR LACEANDVEL VIFNHALAPA QQRNLEVALN RRVVDRTSLI LDIFAQRARS HEGKLQVELA QLQYLSTRLI RAWTHLERQK GGIGLRGPGE TQLETDRRLI GERIKALKAR LEKLRRQHGT QRRQRVRNRT MSVSLVGYTN AGKSTLFNAL TKAQAYAADQ LFATLDTTSR RVFLGEEAGH VVVSDTVGFI RELPHQLVAA FRATLEETIH ADLLLHVVDA SSAVRLDQID QVNEVLRGIG ADTIPQILVF NKIDAVPELA ARGDAVERDE YGNISRVFLS ARTGQGLDAL RAAIAEIAAS DSSGFNEPAE FAESEQSTES PESTQASPYD GTALPEDHRS ADESDDRKVP EHGL // ID A0A071M081_9ENTR Unreviewed; 426 AA. AC A0A071M081; DT 01-OCT-2014, integrated into UniProtKB/TrEMBL. DT 01-OCT-2014, sequence version 1. DT 30-AUG-2017, entry version 22. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=DT73_02100 {ECO:0000313|EMBL:KEA54193.1}; OS Mangrovibacter sp. MFB070. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; OC Enterobacteriaceae; Mangrovibacter. OX NCBI_TaxID=1224318 {ECO:0000313|EMBL:KEA54193.1, ECO:0000313|Proteomes:UP000027726}; RN [1] {ECO:0000313|EMBL:KEA54193.1, ECO:0000313|Proteomes:UP000027726} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MFB070 {ECO:0000313|EMBL:KEA54193.1, RC ECO:0000313|Proteomes:UP000027726}; RA Joseph T.C., Varghese A.M., Baby A., Reghunathan D., V M., RA Lalitha K.V.; RT "Draft Genome Sequence of Mangrovibacter spp. MFB070 a Nitrogen-fixing RT Bacterium Isolated from an Aquaculture Farm."; RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KEA54193.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JJMI01000005; KEA54193.1; -; Genomic_DNA. DR RefSeq; WP_036103133.1; NZ_JJMI01000005.1. DR EnsemblBacteria; KEA54193; KEA54193; DT73_02100. DR Proteomes; UP000027726; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000027726}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000027726}. FT DOMAIN 198 365 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 426 AA; 47837 MW; 3569E46E232A76BD CRC64; MFDRYDAGEQ AVLVHIYFSQ DKDMEDLQEF ESLVSSAGVD ALQVITGTRK APHPKYFVGE GKAEEIADAV KATGASVVLF DHALSPAQER NLERLCECRV IDRTGLILDI FAQRARTHEG KLQVELAQLR HLATRLVRGW THLERQKGGI GLRGPGETQL ETDRRLLRNR ISQILSRLER VEKQREQGRR ARTRADVPTV SLVGYTNAGK STLFNSLTTA EVYAADQLFA TLDPTLRRID VADVGETVLA DTVGFIRHLP HDLVAAFKAT LQETRQATLL LHVIDASDVR VQENIDAVNA VLDEIDALEI PTLLVMNKID CLDGFAPRID RDENNVPVRV WLSAQTGEGI PLLFQALTER LSGEIALHTL RLPPQAGRLR SRFYQLQAIE KEWMEDDGSM GLQVRLPVVD WRRLCKQEPA LVDYIT // ID A0A072N7X4_9DEIO Unreviewed; 569 AA. AC A0A072N7X4; DT 01-OCT-2014, integrated into UniProtKB/TrEMBL. DT 01-OCT-2014, sequence version 1. DT 05-JUL-2017, entry version 20. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=RDMS_12725 {ECO:0000313|EMBL:KEF33372.1}; OS Deinococcus sp. RL. OC Bacteria; Deinococcus-Thermus; Deinococci; Deinococcales; OC Deinococcaceae; Deinococcus. OX NCBI_TaxID=1489678 {ECO:0000313|EMBL:KEF33372.1, ECO:0000313|Proteomes:UP000027898}; RN [1] {ECO:0000313|EMBL:KEF33372.1, ECO:0000313|Proteomes:UP000027898} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=RL {ECO:0000313|EMBL:KEF33372.1, RC ECO:0000313|Proteomes:UP000027898}; RA Lal R., Mahato N.K., Tripathi C., Verma H., Kumari R., Singh N.; RT "Draft genome sequence of Deinococcus sp. strain RL isolated from RT sediments of hot springs located at Manikaran, India."; RL Submitted (MAY-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KEF33372.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JMQF01000058; KEF33372.1; -; Genomic_DNA. DR EnsemblBacteria; KEF33372; KEF33372; RDMS_12725. DR Proteomes; UP000027898; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000027898}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000027898}. FT DOMAIN 382 551 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 569 AA; 61749 MW; 137342FAC6F302B1 CRC64; MHGNTSGLKA AQLKALGNLY RRRIEPGRVG SPELARNLAE LSHDIRREIS VLIDRRGRVL SVSVADAKGA ELPGVRLGEN RLAGFHLLHT HPRGGALSKG DLSTLFLRRL DAVSAIEVRE GGQPGPVHTA HLTPPGTVGE EEDWRILAPV PSFQIDEFDL GAQVAALEEE IARAARTREA KRDRERAILV QIDGGEFDAE ERLEELSELA RTAGAEVVHR ELVYRRHLKA GTLVGAGKLE ELTSRAYHLD ADLLIFGQEL GPAQAREIEA ATGLKVLDRT QLILDIFALH AQGVESRLQV ELAQLRYMKP RLLGAGAQLS RIGGSAGGAA GGAIGTRGPG ETKLELDRRR INDRIAFLEK QLEGVAVRRE ERRKARARND VPVISIVGYT NAGKSTLLNT FTHAAEEPRR VLAENKLFAT LRPTSRQGYI EGIGPVVFTD TVGFIRDLPR DLARAFRATL EEIGDADVLL HVVDVAAPGA DTRLDAVNRI LEDLGLRELP TVVALNKAEA ADPDVLAREL ERTGGVPVSA LKSLGIGDLK DALADAVAGV QRRELALREE ARERAAAYP // ID A0A072UH10_MEDTR Unreviewed; 547 AA. AC A0A072UH10; DT 01-OCT-2014, integrated into UniProtKB/TrEMBL. DT 01-OCT-2014, sequence version 1. DT 07-JUN-2017, entry version 15. DE SubName: Full=GTP-binding protein HflX {ECO:0000313|EMBL:KEH28383.1}; GN OrderedLocusNames=MTR_5g089970 {ECO:0000313|EMBL:KEH28383.1}; OS Medicago truncatula (Barrel medic) (Medicago tribuloides). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae; OC Pentapetalae; rosids; fabids; Fabales; Fabaceae; Papilionoideae; OC Trifolieae; Medicago. OX NCBI_TaxID=3880 {ECO:0000313|EMBL:KEH28383.1, ECO:0000313|Proteomes:UP000002051}; RN [1] {ECO:0000313|EMBL:KEH28383.1, ECO:0000313|EnsemblPlants:KEH28383, ECO:0000313|Proteomes:UP000002051} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=A17 {ECO:0000313|EMBL:KEH28383.1}, and RC cv. Jemalong A17 {ECO:0000313|EnsemblPlants:KEH28383, RC ECO:0000313|Proteomes:UP000002051}; RX PubMed=22089132; DOI=10.1038/nature10625; RA Young N.D., Debelle F., Oldroyd G.E.D., Geurts R., Cannon S.B., RA Udvardi M.K., Benedito V.A., Mayer K.F.X., Gouzy J., Schoof H., RA Van de Peer Y., Proost S., Cook D.R., Meyers B.C., Spannagl M., RA Cheung F., De Mita S., Krishnakumar V., Gundlach H., Zhou S., RA Mudge J., Bharti A.K., Murray J.D., Naoumkina M.A., Rosen B., RA Silverstein K.A.T., Tang H., Rombauts S., Zhao P.X., Zhou P., RA Barbe V., Bardou P., Bechner M., Bellec A., Berger A., Berges H., RA Bidwell S., Bisseling T., Choisne N., Couloux A., Denny R., RA Deshpande S., Dai X., Doyle J.J., Dudez A.-M., Farmer A.D., RA Fouteau S., Franken C., Gibelin C., Gish J., Goldstein S., RA Gonzalez A.J., Green P.J., Hallab A., Hartog M., Hua A., RA Humphray S.J., Jeong D.-H., Jing Y., Jocker A., Kenton S.M., RA Kim D.-J., Klee K., Lai H., Lang C., Lin S., Macmil S.L., RA Magdelenat G., Matthews L., McCorrison J., Monaghan E.L., Mun J.-H., RA Najar F.Z., Nicholson C., Noirot C., O'Bleness M., Paule C.R., RA Poulain J., Prion F., Qin B., Qu C., Retzel E.F., Riddle C., RA Sallet E., Samain S., Samson N., Sanders I., Saurat O., Scarpelli C., RA Schiex T., Segurens B., Severin A.J., Sherrier D.J., Shi R., Sims S., RA Singer S.R., Sinharoy S., Sterck L., Viollet A., Wang B.-B., Wang K., RA Wang M., Wang X., Warfsmann J., Weissenbach J., White D.D., RA White J.D., Wiley G.B., Wincker P., Xing Y., Yang L., Yao Z., Ying F., RA Zhai J., Zhou L., Zuber A., Denarie J., Dixon R.A., May G.D., RA Schwartz D.C., Rogers J., Quetier F., Town C.D., Roe B.A.; RT "The Medicago genome provides insight into the evolution of rhizobial RT symbioses."; RL Nature 480:520-524(2011). RN [2] {ECO:0000313|EMBL:KEH28383.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=A17 {ECO:0000313|EMBL:KEH28383.1}; RX PubMed=24767513; DOI=10.1186/1471-2164-15-312; RA Tang H., Krishnakumar V., Bidwell S., Rosen B., Chan A., Zhou S., RA Gentzbittel L., Childs K.L., Yandell M., Gundlach H., Mayer K.F., RA Schwartz D.C., Town C.D.; RT "An improved genome release (version Mt4.0) for the model legume RT Medicago truncatula."; RL BMC Genomics 15:312-312(2014). RN [3] {ECO:0000313|EnsemblPlants:KEH28383} RP IDENTIFICATION. RC STRAIN=cv. Jemalong A17 {ECO:0000313|EnsemblPlants:KEH28383}; RG EnsemblPlants; RL Submitted (APR-2015) to UniProtKB. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CM001221; KEH28383.1; -; Genomic_DNA. DR RefSeq; XP_013454352.1; XM_013598898.1. DR EnsemblPlants; KEH28383; KEH28383; MTR_5g089970. DR GeneID; 11437034; -. DR Gramene; KEH28383; KEH28383; MTR_5g089970. DR Proteomes; UP000002051; Chromosome 5. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR CDD; cd01878; HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 2. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000002051}; KW Reference proteome {ECO:0000313|Proteomes:UP000002051}. FT DOMAIN 269 515 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 547 AA; 60631 MW; 144F189D3A67043D CRC64; MLRNLSATLE STKRKILTSS KCRIYPPPSP YSTAPVDDAP PKLLVVQPRL RSEKLLQAKL NEALCLANSL EDQRDGYFHT DFFDLPLPPH VIVQNPSLKG HKARAVDTIK CHLNAVESKG EVDAVFVNAI LSGIQIRNME RAWNKPVVDR VGLIIEIFNA HAFTKEAKLQ AELAALSYKK SRLVRVLGPN GRLTFGGSGE AEVVSARGRG SGGQGFMSGA GETELQLQRR RLLDRRNYLL TQIEEVRRTR AVQRAGRKRQ GGSSAQRLAT IAVVGYTNAG KSTLVSNLTD SDLYSDCRLF ATVDPRLRSA VLPSGRKVLF SDTVGFISDL PVKLVEAFHA TLEEVVEADL LVHVVDSTAP NLEEHRTTVF QVLQQIGVSQ EKLQNMIEVW NKIDAEEEFT DVDENVDEHL NEDEEADETS SIDGEEDVNI ETLTEEKEDY SDGWLYEEDT VLNEGDFCLP SSAADQQIES SNKDNSVENA GAMLPSSPHV KTSAITGVGL QELMELIDEK LSSQDEKLKG AQVVERNLFD RKWRPSHTQD SSIVVEN // ID A0A073CCQ1_PLAAG Unreviewed; 541 AA. AC A0A073CCQ1; DT 01-OCT-2014, integrated into UniProtKB/TrEMBL. DT 01-OCT-2014, sequence version 1. DT 07-JUN-2017, entry version 19. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:KEI65707.1}; GN ORFNames=A19Y_0503 {ECO:0000313|EMBL:KEI65707.1}; OS Planktothrix agardhii NIVA-CYA 126/8. OC Bacteria; Cyanobacteria; Oscillatoriophycideae; Oscillatoriales; OC Microcoleaceae; Planktothrix. OX NCBI_TaxID=388467 {ECO:0000313|EMBL:KEI65707.1, ECO:0000313|Proteomes:UP000027395}; RN [1] {ECO:0000313|EMBL:KEI65707.1, ECO:0000313|Proteomes:UP000027395} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NIVA-CYA 126/8 {ECO:0000313|EMBL:KEI65707.1, RC ECO:0000313|Proteomes:UP000027395}; RX PubMed=24907328; DOI=10.1128/AEM.01188-14; RA Christiansen G., Goesmann A., Kurmayer R.; RT "Elucidation of insertion elements encoded on plasmids and in vitro RT construction of shuttle vectors from the toxic cyanobacterium RT Planktothrix."; RL Appl. Environ. Microbiol. 80:4887-4897(2014). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CM002803; KEI65707.1; -; Genomic_DNA. DR EnsemblBacteria; KEI65707; KEI65707; A19Y_0503. DR PATRIC; fig|388467.6.peg.453; -. DR Proteomes; UP000027395; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000027395}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Hydrolase {ECO:0000313|EMBL:KEI65707.1}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000027395}. FT DOMAIN 368 538 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 327 361 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 541 AA; 59938 MW; 61396D8895DDB70F CRC64; MEFAQRLAAI STEIDQPLCA YINRRGQVMR VGVGTPRQTQ IPPLELPRYG NGRLSGIRCI TTQTSPEPPK EAALTAMAIQ RLDILVVLTL TGGGFQRRGG GETGYIKDTY MAHLVPEMDT TKNQQIDNGF SAIPYYLSLP MSLDALSQQD FLDLVNELET EFEREFVARE VDSSQDKVLL VGVKTDKISP QRFEDGLTEL VRLVDTAGGQ VLQTLRQKRS HPHPQTVVGE GKVQEIALVA QTIGANLIVF DRDLSPAQVR NLETQIGVRV VDRTEVILDI FAQRAQSGAG KLQVELAQLE YSLPRLTGRG LAMSRLGGGI GTRGPGETKL ETERRAIQRR ISRLQQEVNQ LQAHRSRLRQ NRQAQEVPTL ALVGYTNAGK STLLNVLTQS EVYTADQLFA TLDPTTRRLE IPDMITEEPL TIVITDTVGF IHELPPPLVN AFRATLEEVT DADALIHLVD LSHSAWESQI ESVMQILREM PVTPGPGLLV FNKIDQTDGE NLRSAQEKYP QAVYISASKA LGLETLRKRM AALVHYAISN R // ID A0A073IFU1_9RHOB Unreviewed; 432 AA. AC A0A073IFU1; DT 01-OCT-2014, integrated into UniProtKB/TrEMBL. DT 01-OCT-2014, sequence version 1. DT 07-JUN-2017, entry version 20. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=DSW25_15085 {ECO:0000313|EMBL:KEJ88420.1}; OS Sulfitobacter donghicola DSW-25 = KCTC 12864 = JCM 14565. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae; Sulfitobacter. OX NCBI_TaxID=1300350 {ECO:0000313|EMBL:KEJ88420.1, ECO:0000313|Proteomes:UP000027734}; RN [1] {ECO:0000313|EMBL:KEJ88420.1, ECO:0000313|Proteomes:UP000027734} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=JCM 14565 {ECO:0000313|EMBL:KEJ88420.1, RC ECO:0000313|Proteomes:UP000027734}; RA Lai Q., Hong Z.; RT "Sulfitobacter donghicola JCM 14565 Genome Sequencing."; RL Submitted (JAN-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KEJ88420.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JAMC01000006; KEJ88420.1; -; Genomic_DNA. DR RefSeq; WP_052033206.1; NZ_JASF01000005.1. DR EnsemblBacteria; KEJ88420; KEJ88420; DSW25_15085. DR Proteomes; UP000027734; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000027734}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000027734}. FT DOMAIN 212 381 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 432 AA; 47578 MW; 5C7619208AEAD95A CRC64; MSKAQFQIDE TDGPAQTRAW VLHPDIKSDN SRREPVAALG EAVALAEALP NLEVVGSDVV PLRAVSAGYL FGSGKIDEIS TLLHDNEVEL VLIDGPVTPV QQRNLEKAWN VKLLDRTGLI LEIFSDRAAT REGVLQVEMA ALNYQRTRLV RAWTHLERQR GGLGFVGGPG ETQIEADRRA IDEQLVRLRR QLEKVVKTRA LHRAARAKVP YPIVALVGYT NAGKSTLFNR LTGADVMVKD MLFATLDPTM RSLELLDGPE IILSDTVGFI SDLPTELVAA FRATLEEVLA ADIILHVRDV SHAETEAQAR NVRDIMTSLG VPEETRTFEV WNKLDLLSED AADAMRERAA RDETVLAISA ITGEGLDGLQ TTVAEALQGA LRTADLVLSF AEGRKRAWLF SQDVVVNEEQ TEEGFALTVR WSADVEAAYQ RL // ID A0A073IPM5_9BACT Unreviewed; 373 AA. AC A0A073IPM5; DT 01-OCT-2014, integrated into UniProtKB/TrEMBL. DT 01-OCT-2014, sequence version 1. DT 05-JUL-2017, entry version 21. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=EH55_09465 {ECO:0000313|EMBL:KEJ91426.1}; OS Synergistes jonesii. OC Bacteria; Synergistetes; Synergistia; Synergistales; Synergistaceae; OC Synergistes. OX NCBI_TaxID=2754 {ECO:0000313|EMBL:KEJ91426.1, ECO:0000313|Proteomes:UP000027665}; RN [1] {ECO:0000313|EMBL:KEJ91426.1, ECO:0000313|Proteomes:UP000027665} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=78-1 {ECO:0000313|EMBL:KEJ91426.1, RC ECO:0000313|Proteomes:UP000027665}; RA Coil D.A., Eisen J.A., Holland-Moritz H.E.; RT "Draft Genome Sequence of Synergistes jonesii."; RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KEJ91426.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JMKI01000047; KEJ91426.1; -; Genomic_DNA. DR EnsemblBacteria; KEJ91426; KEJ91426; EH55_09465. DR PATRIC; fig|2754.20.peg.2471; -. DR Proteomes; UP000027665; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000027665}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000027665}. FT DOMAIN 194 364 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 160 187 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 373 AA; 41123 MW; 612AB9980C0FAD46 CRC64; MKPKKAVIAA LSCGDADDVS LSLDELVMLL KNVEVPVAAR VVQKRKAPDP AYFLGAGKAL EIKEYAPPNE ITHLVVDDFL TPTQRSNLQR LTGLVVWDRA FVIMKIFERR AVTAEAKLQV ELAQYRYEIP SLKGLGRQMS RTGGGIGTRG PGETEFERHR RKLDRRIRGI EQNLEEVRRR RGERRERRKR GGVPVAALVG YTNSGKSTLL KALSKDSEIL AKDQLFSTLD TVARRVSYRD GSGSFLLSDT VGFIRKLPPE LVAAFRATLE EASNADLLLV VLDASRKNPC ETLDIVLDTL RGLGAGALPR IVVLNKIDKC GESALFTAAE IRSRGERVVS TCAIDGSGFE ELLGEIKKIF ADEVAAKVQK DIL // ID A0A073JAJ5_9RHOB Unreviewed; 412 AA. AC A0A073JAJ5; DT 01-OCT-2014, integrated into UniProtKB/TrEMBL. DT 01-OCT-2014, sequence version 1. DT 10-MAY-2017, entry version 19. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=SUH3_04825 {ECO:0000313|EMBL:KEJ94747.1}; OS Sulfitobacter pseudonitzschiae. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae; Sulfitobacter. OX NCBI_TaxID=1402135 {ECO:0000313|EMBL:KEJ94747.1, ECO:0000313|Proteomes:UP000027746}; RN [1] {ECO:0000313|EMBL:KEJ94747.1, ECO:0000313|Proteomes:UP000027746} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=H3 {ECO:0000313|EMBL:KEJ94747.1, RC ECO:0000313|Proteomes:UP000027746}; RA Lai Q., Hong Z.; RT "Sulfitobacter sp. H3 (MCCC 1A00686) Genome Sequencing."; RL Submitted (JAN-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KEJ94747.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JAMD01000010; KEJ94747.1; -; Genomic_DNA. DR EnsemblBacteria; KEJ94747; KEJ94747; SUH3_04825. DR Proteomes; UP000027746; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000027746}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000027746}. FT DOMAIN 192 361 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 412 AA; 45704 MW; 4F88AD078A3B2611 CRC64; MLHPDIKSDR NRRGAELALA EAVSLAHALR HLEVVGSQIV PLPKVHAGML FGKGKIEELR ARFEAEEIEL VLVDGPVTPV QQRNLEKAWG VKLLDRTGLI LEIFSDRAAT REGVLQVEMA ALNYQRTRLV RAWTHLERQR GGLGFVGGPG ETQIEADRRA IDLQLVRLRR QLDKVVKTRT LHRAARAKVP FPIVALVGYT NAGKSTLFNR LTGANVMAED MLFATLDPTM RRVELDNGPE IILSDTVGFI SDLPTELVAA FRATLEEVLA ADIICHVRDI SHPETEDQAA DVREILTTLG VGNERPMFEI WNKIDLLAQA EAEAAQARAA RDQDIIAISA LHGTGVESFM SIISEALQGR VSEEVLRLSF AQGKKRAWLF SEGVAVDEVQ DEDGFAVTVR WTPKQRAQFE QV // ID A0A073JTM6_9BACI Unreviewed; 413 AA. AC A0A073JTM6; DT 01-OCT-2014, integrated into UniProtKB/TrEMBL. DT 01-OCT-2014, sequence version 1. DT 07-JUN-2017, entry version 20. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=BAMA_12350 {ECO:0000313|EMBL:KEK17531.1}; OS Bacillus manliponensis. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=574376 {ECO:0000313|EMBL:KEK17531.1, ECO:0000313|Proteomes:UP000027822}; RN [1] {ECO:0000313|EMBL:KEK17531.1, ECO:0000313|Proteomes:UP000027822} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=JCM 15802 {ECO:0000313|EMBL:KEK17531.1, RC ECO:0000313|Proteomes:UP000027822}; RA Lai Q., Liu Y., Shao Z.; RT "Draft genome sequence of Bacillus manliponensis JCM 15802 (MCCC RT 1A00708)."; RL Submitted (JUN-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KEK17531.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JOTN01000026; KEK17531.1; -; Genomic_DNA. DR RefSeq; WP_034643031.1; NZ_JOTN01000026.1. DR EnsemblBacteria; KEK17531; KEK17531; BAMA_12350. DR Proteomes; UP000027822; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000027822}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000027822}. FT DOMAIN 198 360 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 413 AA; 47034 MW; 614445358AAE5DC4 CRC64; MLEKKEKAIL VGCQLSQDED KRFVHSMEEL ASLTKTARAD VLVSTTQKRP KFHPATYIGK GKLEELSSLV KELEPDVIIF NNELTPSQIR NLSAELDGRV IDRTQLILDI FAQRARSREG QLQVELAQLQ YALPRLVGQG TSLSRLGGGI GTRGPGETKL ETDRRHIRSR IDEIKRQLAV VVEHRKRYRE RRKQNQVFQV SIVGYTNAGK STLFNRLTEA NTFEENLLFA TLDPTTRKMQ LPCGYTVLLT DTVGFIQDLP TSLVAAFRST LEEVNEADLI LHVIDSSDSN YVNHEETVNE LLHELEVKHV PVITVYNKRD EQYDKFIPSP TSDSIMTSAF CIDDIEELKR KIETGVIEQM EPYEVTVPAH EGRLLMQLKT DSVLTDMVFR EEEQVYVCKG YIFAHSPLNG RMK // ID A0A073K062_9BACI Unreviewed; 419 AA. AC A0A073K062; DT 01-OCT-2014, integrated into UniProtKB/TrEMBL. DT 01-OCT-2014, sequence version 1. DT 07-JUN-2017, entry version 20. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=BAMA_18875 {ECO:0000313|EMBL:KEK19842.1}; OS Bacillus manliponensis. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=574376 {ECO:0000313|EMBL:KEK19842.1, ECO:0000313|Proteomes:UP000027822}; RN [1] {ECO:0000313|EMBL:KEK19842.1, ECO:0000313|Proteomes:UP000027822} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=JCM 15802 {ECO:0000313|EMBL:KEK19842.1, RC ECO:0000313|Proteomes:UP000027822}; RA Lai Q., Liu Y., Shao Z.; RT "Draft genome sequence of Bacillus manliponensis JCM 15802 (MCCC RT 1A00708)."; RL Submitted (JUN-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KEK19842.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JOTN01000005; KEK19842.1; -; Genomic_DNA. DR RefSeq; WP_034637954.1; NZ_JOTN01000005.1. DR EnsemblBacteria; KEK19842; KEK19842; BAMA_18875. DR Proteomes; UP000027822; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000027822}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000027822}. FT DOMAIN 198 366 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 157 191 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 419 AA; 47828 MW; 604AE0FC005930D2 CRC64; MEELVQKAIL VGVNLGGQGN FEYSMEELAN LTEACDVEVV GQVTQNLQRV NPSHYIGTGK IEEVSAFIKE ADANLVIFND ELSPSQIRNL EAELDCKVID RTILILDIFA QRAKTKEAQL QVEVAHLQYM MPRLIGLRES LGRQSGGVGT KNKGVGEKKL ELDRRKIEEQ ISALNKELEA LTHHRQTQRK QRKKKDMPVV ALVGYTNAGK STMMNAMLEM FNESIEKQVF EKDMLFATLE TSVRNIQLPD QKSFLLTDTV GFVSKLPHHL VKAFRSTLEE VAEADLLIHV VDYSNPNYEQ LIEITNETLR KIGVDNIQTI YAYNKSDMMD IEIPQVQEER VYMSAKKQVG VDELVQLIRT HIYTDYTQCD MLIPYDQGQL VSYFNEHAHV LETSYENEGT KITVECKNSD FEKYKCYVM // ID A0A074JSA7_9RHOB Unreviewed; 428 AA. AC A0A074JSA7; DT 01-OCT-2014, integrated into UniProtKB/TrEMBL. DT 01-OCT-2014, sequence version 1. DT 07-JUN-2017, entry version 19. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=DT23_04570 {ECO:0000313|EMBL:KEO59359.1}; OS Thioclava indica. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae; Thioclava. OX NCBI_TaxID=1353528 {ECO:0000313|EMBL:KEO59359.1, ECO:0000313|Proteomes:UP000027471}; RN [1] {ECO:0000313|EMBL:KEO59359.1, ECO:0000313|Proteomes:UP000027471} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DT23-4 {ECO:0000313|EMBL:KEO59359.1, RC ECO:0000313|Proteomes:UP000027471}; RX PubMed=25361528; DOI=10.1007/s10482-014-0320-3; RA Liu Y., Lai Q., Du J., Xu H., Jiang L., Shao Z.; RT "Thioclava indica sp. nov., isolated from surface seawater of the RT Indian Ocean."; RL Antonie Van Leeuwenhoek 107:297-304(2015). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KEO59359.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AUNB01000029; KEO59359.1; -; Genomic_DNA. DR RefSeq; WP_038131061.1; NZ_AUNB01000029.1. DR EnsemblBacteria; KEO59359; KEO59359; DT23_04570. DR Proteomes; UP000027471; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000027471}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000027471}. FT DOMAIN 208 377 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 428 AA; 47475 MW; B634B4FF8E790EF7 CRC64; MSDLHSSERA PTRAFVLHPD IPSREGPRHL PKFALAEAES LARALPGLEV IGGQIVRLPK PHPGHLFGTG KMAELKAQLE ADEIELVLVD GPVTPVQQRN LEKEWGVKLL DRTGLILEIF ADRARTREGV LQVELAALSY QRTRLVRAWT HLERQRGGLG FVGGPGETQI EADRRAIDDQ MVRLRRQLAR VVKTRELHRA ARRKIPFPIV ALVGYTNAGK STLFNTVTGA DVLAKDMLFA TLDPTMRGLT LPSGRKVIMS DTVGFISDLP HELVAAFRAT LEEVLEADLI LHVRDIAHPE TEEQAADVND ILATLGVDED VASLEVWNKI DALDPDQRAA LQMQASRDPD IQAVSALTGT GLADLLGAID ARLAEEKLFE TLDLGFDQGR KHAWLHEQNV VRAERQTKTG WRCDVEWSAA QRNRFRAL // ID A0A074KX27_9BACT Unreviewed; 421 AA. AC A0A074KX27; DT 01-OCT-2014, integrated into UniProtKB/TrEMBL. DT 01-OCT-2014, sequence version 1. DT 07-JUN-2017, entry version 20. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=EL17_19625 {ECO:0000313|EMBL:KEO72123.1}; OS Anditalea andensis. OC Bacteria; Bacteroidetes; Cytophagia; Cytophagales; Cytophagaceae; OC Anditalea. OX NCBI_TaxID=1048983 {ECO:0000313|EMBL:KEO72123.1, ECO:0000313|Proteomes:UP000027821}; RN [1] {ECO:0000313|EMBL:KEO72123.1, ECO:0000313|Proteomes:UP000027821} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=LY1 {ECO:0000313|EMBL:KEO72123.1, RC ECO:0000313|Proteomes:UP000027821}; RA Yang L., Wei S., Tay Q.X.M.; RT "Characterization and application of a salt tolerant electro-active RT bacterium."; RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KEO72123.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JMIH01000028; KEO72123.1; -; Genomic_DNA. DR RefSeq; WP_035078395.1; NZ_JMIH01000028.1. DR EnsemblBacteria; KEO72123; KEO72123; EL17_19625. DR Proteomes; UP000027821; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000027821}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000027821}. FT DOMAIN 210 399 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 171 198 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 421 AA; 48401 MW; C619B1CCF8928A6F CRC64; MSKYSRKLQK LHDTAPKPET AVLVAIIHQH QTEQQAQEYL DELAFLTETL GAKTVYRFTQ RLERPDVKSF VGSGKLEEIK AYVNHFEVNM VIFDDDLSAS QMRNLENELQ VKVYDRSLLI LDIFLSRAQT AQAKTQVELA RFQYLLPRLT RMWTHLERQR GGTTTRGGAG EKEIETDKRD IRNQITLLKE KLRKIEKQGQ TQRKSREGIV RVALVGYTNV GKSTLMRLMT KADVLAENKL FATVDSTVRK VVLENIPFLL SDTVGFIRKL PTHLIESFKS TLDEIREADI LVHIVDISHP NFEDHITVVN QTLTEIGASD KPTILVFNKI DLVPGMPSED ELQLMTEIEI GEANFLDFEK LKESYTKKVG IPPVFMAAED GTHIDELRYS LIDEVKKRHL QIYPNYLEDE TIDLSQFRDL E // ID A0A074LQT2_9BACL Unreviewed; 457 AA. AC A0A074LQT2; DT 01-OCT-2014, integrated into UniProtKB/TrEMBL. DT 01-OCT-2014, sequence version 1. DT 10-MAY-2017, entry version 18. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=EL26_09580 {ECO:0000313|EMBL:KEO83459.1}; OS Tumebacillus flagellatus. OC Bacteria; Firmicutes; Bacilli; Bacillales; Alicyclobacillaceae; OC Tumebacillus. OX NCBI_TaxID=1157490 {ECO:0000313|EMBL:KEO83459.1, ECO:0000313|Proteomes:UP000027931}; RN [1] {ECO:0000313|EMBL:KEO83459.1, ECO:0000313|Proteomes:UP000027931} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=GST4 {ECO:0000313|EMBL:KEO83459.1, RC ECO:0000313|Proteomes:UP000027931}; RX PubMed=23435245; DOI=10.1099/ijs.0.045351-0; RA Wang Q., Xie N., Qin Y., Shen N., Zhu J., Mi H., Huang R.; RT "Tumebacillus flagellatus sp. nov., an alpha-amylase/pullulanase- RT producing bacterium isolated from cassava wastewater."; RL Int. J. Syst. Evol. Microbiol. 63:3138-3142(2013). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KEO83459.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JMIR01000011; KEO83459.1; -; Genomic_DNA. DR EnsemblBacteria; KEO83459; KEO83459; EL26_09580. DR Proteomes; UP000027931; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000027931}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000027931}. FT DOMAIN 204 375 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 457 AA; 51320 MW; A6F1DA2D0D717C3A CRC64; MHELYDNQGR TERAVLVGLK LARHDDEIWQ MAFTELKGLV ETAGAEVVTE LIQNRDLPDP ATYIGKGKLA ELNAVIGELN IDVVVFDSEL SPKHVRNLEN ALSCRVLDRT QVILDIFAMR AKTREGKLQV ELAQLHYLMP RLTGQGAAMS RLGGGIGTRG PGETKLETDR RHIRGRILEL SRQLDEVRKH RDLHKKRRKK QEIPVIAFVG YTNAGKSTLM KAIVERYGNG NREVAEGRNR LFDTLDTTTR QVQLPDGKTA IFSDTVGFIQ QLPHSLIRAF RSTLEETAEA DLIVHVVDAS HPGFDVQMAT VYDVLQELKV LDRPILTVFN KIDLVPGAWI GNDPNSTETV RVSATLGDGL DTLMEKANDL AGVRHLLVTV EVPYKEAALT AQVHREGRIF EEEHRESGTY LKAEVPQRLA DELSVYFLQE AEEVVPPKEV KKLYFDFTTP ESDDVLH // ID A0A074MDB5_ERYLO Unreviewed; 432 AA. AC A0A074MDB5; DT 01-OCT-2014, integrated into UniProtKB/TrEMBL. DT 01-OCT-2014, sequence version 1. DT 07-JUN-2017, entry version 20. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=EH31_01960 {ECO:0000313|EMBL:KEO91454.1}; OS Erythrobacter longus. OC Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales; OC Erythrobacteraceae; Erythrobacter. OX NCBI_TaxID=1044 {ECO:0000313|EMBL:KEO91454.1, ECO:0000313|Proteomes:UP000027647}; RN [1] {ECO:0000313|EMBL:KEO91454.1, ECO:0000313|Proteomes:UP000027647} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 6997 {ECO:0000313|EMBL:KEO91454.1, RC ECO:0000313|Proteomes:UP000027647}; RA Zheng Q.; RT "A comprehensive comparison of genomes of Erythrobacter spp. RT strains."; RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KEO91454.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JMIW01000001; KEO91454.1; -; Genomic_DNA. DR RefSeq; WP_051698860.1; NZ_JMIW01000001.1. DR EnsemblBacteria; KEO91454; KEO91454; EH31_01960. DR Proteomes; UP000027647; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000027647}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000027647}. FT DOMAIN 202 376 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 168 195 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 432 AA; 47727 MW; 202E4C9E850AE60B CRC64; MDEVTRGARC LVLCPDIRSL SYDLDAKERL AEAEGLALAI GVIIAHSAVM PVRQMQPNTL FGSGQVENIA TICEQYECEL VIVDGALTPI QQRNLEDKLK RKVIDRTGLI LEIFGERAAT AEGRLQVELA HLDYQQSRLV RSWTHLERQR GGFGFLGGPG ETQIEADRRM IRQRMGRLRR ELEQVRKTRQ LHRARRGRAP WPVIALVGYT NAGKSTLFNH LTGADVMAED LLFATLDPTM RAVSLPGVEK AILSDTVGFI SDLPTQLVAA FRATLEEVTG ADIICHVRDM ANPAHAAQKK QVMEILSDLG VVDADSGHSE VPILEVWNKA DLLDEERAEE LREAAQSQDA VLVSAANGQG LEDLEARIAE ILTEKASEVT VTIPVSDGRR IAWLHAHGEV IVDEDAGEGE QGPMRRMTVR LNPKEMGQYT TL // ID A0A074N2A9_9SPHN Unreviewed; 434 AA. AC A0A074N2A9; DT 01-OCT-2014, integrated into UniProtKB/TrEMBL. DT 01-OCT-2014, sequence version 1. DT 07-JUN-2017, entry version 20. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=EH32_07810 {ECO:0000313|EMBL:KEO99000.1}; OS Erythrobacter litoralis. OC Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales; OC Erythrobacteraceae; Erythrobacter. OX NCBI_TaxID=39960 {ECO:0000313|EMBL:KEO99000.1, ECO:0000313|Proteomes:UP000027866}; RN [1] {ECO:0000313|EMBL:KEO99000.1, ECO:0000313|Proteomes:UP000027866} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 8509 {ECO:0000313|EMBL:KEO99000.1, RC ECO:0000313|Proteomes:UP000027866}; RA Zheng Q.; RT "A comprehensive comparison of genomes of Erythrobacter spp. RT Strains."; RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KEO99000.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JMIX01000003; KEO99000.1; -; Genomic_DNA. DR RefSeq; WP_051697647.1; NZ_JMIX01000003.1. DR EnsemblBacteria; KEO99000; KEO99000; EH32_07810. DR PATRIC; fig|39960.10.peg.1599; -. DR Proteomes; UP000027866; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000027866}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000027866}. FT DOMAIN 202 376 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 161 195 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 434 AA; 47807 MW; 46AD74F478C756D1 CRC64; MDEVTRGARA LVLCPDIRSF TYDLDARERL EEAEGLALAI GVVIAHSEIL PVRQMQPNTL FGSGQVQRIA DWCELYEAEL VIVDGALTPI QQRNLEEKLK RKVIDRTGLI LEIFGERAAT AEGRLQVELA HLDYQQSRLV RSWTHLERQR GGFGFLGGPG ETQIEADRRM INQRMARLRR ELEQVRKTRA LHRERRGRAP WPVVALVGYT NAGKSTLFNR LTGADVMAED LLFATLDPTM RAIALPGVEK AILSDTVGFI SDLPTQLVAA FRATLEEVTG ADLICHVRDI ANPAHAAQKK QVMEVLGDLG VVDPETGVGE IPILEVWNKA DLLPPERRGE LSEAAEAHEA VLLSAASGVG IEALEARIGA MLTARAKEVT VTLPVSDGRR MAWLHAHGDV LGEEDAGEGE NGPMKRVTVR LNPKELGQYE TLEN // ID A0A074U616_9MICO Unreviewed; 505 AA. AC A0A074U616; DT 01-OCT-2014, integrated into UniProtKB/TrEMBL. DT 01-OCT-2014, sequence version 1. DT 10-MAY-2017, entry version 18. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=HR12_11630 {ECO:0000313|EMBL:KEP76354.1}; OS Microbacterium sp. SUBG005. OC Bacteria; Actinobacteria; Micrococcales; Microbacteriaceae; OC Microbacterium. OX NCBI_TaxID=1504156 {ECO:0000313|EMBL:KEP76354.1, ECO:0000313|Proteomes:UP000032117}; RN [1] {ECO:0000313|EMBL:KEP76354.1, ECO:0000313|Proteomes:UP000032117} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SUBG005 {ECO:0000313|EMBL:KEP76354.1, RC ECO:0000313|Proteomes:UP000032117}; RA Rakhashiya P.M., Patel P., Thaker V.S.; RT "Genomic sequences of Microbacterium sp. SUBG005."; RL Submitted (JUN-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KEP76354.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JNNT01000002; KEP76354.1; -; Genomic_DNA. DR EnsemblBacteria; KEP76354; KEP76354; HR12_11630. DR Proteomes; UP000032117; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000032117}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000032117}. FT DOMAIN 287 452 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 505 AA; 54543 MW; 2A5D3ABA20C262D4 CRC64; MTEQTTPPST DASAVDPVDR VLARADAHRG VRVFGAAQAL QDNTTAYGGD SDGDQWDREE RAALRRVVGL STELEDVTEV EYRQLRLENV VLVGVHPQGE QTDAENSLRE LSALAETAGA VVLDGVLQRR PHPDPATYVG RGKAAELRDI VAAVGADTVI ADTELAPSQR RALEDVVKVK VIDRTTVILD IFSQHAKSRE GKAQVELAQL EYLLPRLRGW GDSMSRQAGG QVGAGGAGMG SRGPGETKIE LDRRRIRTRM AQLRKQLRDF APAREAKRAE RKRHTIPSVA IAGYTNAGKS SLLNRLTSAG VLVENALFAT LDATVRRSET SDGRVYTLTD TVGFVRNLPH QLVEAFRSTL EEVGDADVIL HVVDASHPDP AAQLMTVRDV MGDVDANFGQ EIVVFNKADL VSEDDRLVLR GLAPNAKFVS SRTGEGIDEL RAAIEDALPL PAVEVQAVVP YDRGDLVSAV HESGLIVAQE HRESGTFLHA HVGARLAAEL AAFEA // ID A0A074U9W0_9RHOB Unreviewed; 428 AA. AC A0A074U9W0; DT 01-OCT-2014, integrated into UniProtKB/TrEMBL. DT 01-OCT-2014, sequence version 1. DT 12-APR-2017, entry version 17. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=DL1_00150 {ECO:0000313|EMBL:KEP71477.1}; OS Thioclava dalianensis. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae; Thioclava. OX NCBI_TaxID=1185766 {ECO:0000313|EMBL:KEP71477.1, ECO:0000313|Proteomes:UP000027725}; RN [1] {ECO:0000313|EMBL:KEP71477.1, ECO:0000313|Proteomes:UP000027725} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DLFJ1-1 {ECO:0000313|EMBL:KEP71477.1, RC ECO:0000313|Proteomes:UP000027725}; RA Lai Q., Shao Z.; RT "The draft genome sequence of Thioclava dalianensis DLFJ1-1."; RL Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KEP71477.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JHEH01000001; KEP71477.1; -; Genomic_DNA. DR EnsemblBacteria; KEP71477; KEP71477; DL1_00150. DR Proteomes; UP000027725; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000027725}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000027725}. FT DOMAIN 208 377 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 428 AA; 47526 MW; 49E1C89EE0C9528B CRC64; MSELHVSERA PTRAYVLHPD IPSREGPRHL PKFALAEAEA LAHALPGLEV VGGQVVRLPK PHPGHLFGTG KMAELKTQLE ADEIELVLID GPVSPVQQRN LEKEWGVKLL DRTGLILEIF ADRARTREGV LQVELAALSY QRTRLVRAWT HLERQRGGLG FVGGPGETQI EADRRAIDDQ MVRLRRQLAR VVKTRELHRA ARRKIPFPIV ALVGYTNAGK STLFNKVTGA EVFAQDMLFA TLDPTMRGLT LPSGRKVILS DTVGFISDLP HELVAAFRAT LEEVLEADLI LHVRDISHPE TEEQAQDVND ILGTLGVDED VVLLEVWNKI DAMAEEPRAA LQVQAGREPD IEAVSALSGA GLDGLLSAID ARLAEEKLFE TLDVPFSEGR KHAWLHEQNV VRAEQQSETG WRCDVEWSAA QRNRFRAL // ID A0A075JKA9_9MICO Unreviewed; 508 AA. AC A0A075JKA9; DT 29-OCT-2014, integrated into UniProtKB/TrEMBL. DT 29-OCT-2014, sequence version 1. DT 07-JUN-2017, entry version 19. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=HX89_05740 {ECO:0000313|EMBL:AIF40523.1}; OS Dermacoccus nishinomiyaensis. OC Bacteria; Actinobacteria; Micrococcales; Dermacoccaceae; Dermacoccus. OX NCBI_TaxID=1274 {ECO:0000313|EMBL:AIF40523.1, ECO:0000313|Proteomes:UP000027986}; RN [1] {ECO:0000313|EMBL:AIF40523.1, ECO:0000313|Proteomes:UP000027986} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=M25 {ECO:0000313|EMBL:AIF40523.1, RC ECO:0000313|Proteomes:UP000027986}; RA Hong K.W., Chan K.G.; RT "Genome Sequencing of Dermacoccus nishinomiyaensis."; RL Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP008889; AIF40523.1; -; Genomic_DNA. DR EnsemblBacteria; AIF40523; AIF40523; HX89_05740. DR KEGG; dni:HX89_05740; -. DR KO; K03665; -. DR Proteomes; UP000027986; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 2. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000027986}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000027986}. FT DOMAIN 288 453 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 508 AA; 55956 MW; 5646C525206FEAA2 CRC64; MNRTATNDYL RREDPALNER NPADFLSRRA QALADSDDAT PTYDERGFVV DAYDGDQFER EERAALRRVH GLSTELEDVS EVEYRQLRLE KVVLAGVWSE GSAEDAENSL RELAALAETA GSEVLAGVVQ RRLRPDPGTW LGKGKAEELK EIVIAEGADT VITDGELAPS QRRALEDVVK VKVIDRTALI LDIFAQHAKS KEGKAQVELA QMQYLLPRLR GWGESMSRQA GGQAAGGQGM GSRGPGETKI ELDRRRINTR MAKLRREIAE MKTTRDTKRS GRRNNNVPSV AIAGYTNAGK SSILNRLTNA GVLVQNQLFA TLDPAVRRAE TADGRAYTLA DTVGFVRDLP HQLVEAFRST LEEVADADLL LHVVDGSHPD PESQISAVRE VLADVDASDV KEIIVINKAD VADPDVIDRL MRHEKYAIAV SARTGAGLPE LLQLIADELP KPERRVDVLL PYERGDLLSR LHADAEVLSI EHRGEGTYVH AKVMPELEGE LEAYLTNA // ID A0A075JUF8_9BACI Unreviewed; 411 AA. AC A0A075JUF8; DT 29-OCT-2014, integrated into UniProtKB/TrEMBL. DT 29-OCT-2014, sequence version 1. DT 07-JUN-2017, entry version 20. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=X953_11480 {ECO:0000313|EMBL:AIF43678.1}; OS Virgibacillus sp. SK37. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Virgibacillus. OX NCBI_TaxID=403957 {ECO:0000313|EMBL:AIF43678.1, ECO:0000313|Proteomes:UP000027985}; RN [1] {ECO:0000313|EMBL:AIF43678.1, ECO:0000313|Proteomes:UP000027985} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SK37 {ECO:0000313|EMBL:AIF43678.1, RC ECO:0000313|Proteomes:UP000027985}; RA Phrommao E., Yongsawatdigul J., Rodtong S., Steele J.L.; RT "Complete genome sequence of Virgibacillus sp. SK37, a moderately RT halophilic bacterium isolated from Thai fish sauce fermentation."; RL Submitted (FEB-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP007161; AIF43678.1; -; Genomic_DNA. DR RefSeq; WP_040955589.1; NZ_CP007161.1. DR EnsemblBacteria; AIF43678; AIF43678; X953_11480. DR KEGG; vir:X953_11480; -. DR KO; K03665; -. DR Proteomes; UP000027985; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000027985}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000027985}. FT DOMAIN 196 357 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 411 AA; 47415 MW; C97157662D39E576 CRC64; MTAEKILVIA VMRPRQNEER FQSSLKELIS LSHTAGGAVE KVMVQKRDRI HPANYIGTGK MEEIKQEIEE LDIELVISND ELSSGQLRNL GNEFGVRIID RSQLILDIFA QRARTKEGKL QVELAQLEYM LPRLRGQGVS MSRLGAGIGT RGPGETKLET DQRHIRRRIY DIKRRLSSVA QQREQYRKRR KANEVFQIAI VGYTNAGKST LFNRLTDSES MVEDKLFATL DPLTRQIKLP SGFQPLLTDT VGFIQDLPTS LIAAFKSTLE EVTEADFLLH VVDGSNPDLE QHQHTVRKLL EELHADTIPM LNIYNKKDLM EKEFIPSNHP YFIMSAYGDE DLSRLETKIE ETLIKEWKYY SLELRPDEGK IMNRLELESI VTEKYFNEEK NQYTVKGYMR KDHALESLLE E // ID A0A075KBY3_9FIRM Unreviewed; 599 AA. AC A0A075KBY3; DT 29-OCT-2014, integrated into UniProtKB/TrEMBL. DT 29-OCT-2014, sequence version 1. DT 07-JUN-2017, entry version 20. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=UFO1_2154 {ECO:0000313|EMBL:AIF51701.1}; OS Pelosinus sp. UFO1. OC Bacteria; Firmicutes; Negativicutes; Selenomonadales; Sporomusaceae; OC Pelosinus. OX NCBI_TaxID=484770 {ECO:0000313|EMBL:AIF51701.1, ECO:0000313|Proteomes:UP000027983}; RN [1] {ECO:0000313|EMBL:AIF51701.1, ECO:0000313|Proteomes:UP000027983} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=UFO1 {ECO:0000313|EMBL:AIF51701.1}; RX PubMed=25189589; RA Brown S.D., Utturkar S.M., Magnuson T.S., Ray A.E., Poole F.L., RA Lancaster W.A., Thorgersen M.P., Adams M.W., Elias D.A.; RT "Complete Genome Sequence of Pelosinus sp. Strain UFO1 Assembled Using RT Single-Molecule Real-Time DNA Sequencing Technology."; RL Genome Announc. 2:e00881-14(2014). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP008852; AIF51701.1; -; Genomic_DNA. DR RefSeq; WP_038670693.1; NZ_CP008852.1. DR EnsemblBacteria; AIF51701; AIF51701; UFO1_2154. DR KEGG; puf:UFO1_2154; -. DR KO; K03665; -. DR Proteomes; UP000027983; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000027983}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000027983}. FT DOMAIN 376 541 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 342 369 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 599 AA; 66881 MW; 2D879EB43D8BF272 CRC64; MSKIYGEIAG IRKSILNRLE ELYEFTIPFG QVITSELAQQ MVNLTTDLNR EIAIYISRRG QITCVAVGDI YTVVLPEIDG RRSSNRLSGI RCIHTHPSGD TELSGVDVAS LKEMRFDLMA ALGNKDGVIQ VGFGIITNIE KDNFNTQTVG PLSLEEFIEL DITYLTAQIE RQLDLNTKTS AIEETERAIL VGLEKQGKWA IVDSLKELAQ LAETAGAEVL GMTWQKRERP DSALFIGRGK VQELSLLRQE KNANLIIFDD ELSPAQQRNL EKALGIKVLD RTALILDIFA QRARSHEGKL QVELAQLRYN LPRLGGQGLV LSRLGGGIGT RGPGETKLEV DRRRIRDRVS DITQQIEQIK KQRNLHRKRR ENTRIPTVAL VGYTNAGKST LLNTLTASDV LAEDKLFATL DPTTRHITLP NGQQALLTDT VGFIQKLPHQ LIAAFRATLE EVIQADILLH VIDASHPQYQ EQSHAVYQVL RELKVDTKQL ITVFNKGDKL EDPSMKDQLL KKENSVIISA LSGTGTNTLL LLIENFIKEQ TVEMHLLIPY NDSGVIAKLY DIANVHSTEY REDGIYVVIS LPPDQISYFS TYAIGAELS // ID A0A075KFG2_9FIRM Unreviewed; 600 AA. AC A0A075KFG2; DT 29-OCT-2014, integrated into UniProtKB/TrEMBL. DT 29-OCT-2014, sequence version 1. DT 07-JUN-2017, entry version 21. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=UFO1_3381 {ECO:0000313|EMBL:AIF52924.1}; OS Pelosinus sp. UFO1. OC Bacteria; Firmicutes; Negativicutes; Selenomonadales; Sporomusaceae; OC Pelosinus. OX NCBI_TaxID=484770 {ECO:0000313|EMBL:AIF52924.1, ECO:0000313|Proteomes:UP000027983}; RN [1] {ECO:0000313|EMBL:AIF52924.1, ECO:0000313|Proteomes:UP000027983} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=UFO1 {ECO:0000313|EMBL:AIF52924.1}; RX PubMed=25189589; RA Brown S.D., Utturkar S.M., Magnuson T.S., Ray A.E., Poole F.L., RA Lancaster W.A., Thorgersen M.P., Adams M.W., Elias D.A.; RT "Complete Genome Sequence of Pelosinus sp. Strain UFO1 Assembled Using RT Single-Molecule Real-Time DNA Sequencing Technology."; RL Genome Announc. 2:e00881-14(2014). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP008852; AIF52924.1; -; Genomic_DNA. DR RefSeq; WP_038672723.1; NZ_CP008852.1. DR EnsemblBacteria; AIF52924; AIF52924; UFO1_3381. DR KEGG; puf:UFO1_3381; -. DR KO; K03665; -. DR Proteomes; UP000027983; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000027983}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000027983}. FT DOMAIN 376 541 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 600 AA; 66940 MW; B641C3D60D79C924 CRC64; MSTIHGEFDG IRKSFLTRLE QLYEFTVPFG QVITSELAKK MIEITEDLKR EIAVYINRRG QITAVAVGNS IAVVLPEIDG RRSANRLSGT RCIHTHPSGD TELSGVDIAS LKQVRFDLMA AIGQLDGMIQ VSFGIITDVK NDTFHTQTIG PLSLEEFIEL DLTYLASQIE RQLELNTRTS AISEPEKSIL VGLERQGKWE IQDSLKELEQ LAETAGAEVL GMTWQKRERP DPALFIGKGK VQELNLLKQE KGANLIIFDD ELSPAQQRNL EKQLNTKVLD RAALILDICA QRAHSHEAKL QVELAQLRYT LPRLGGQGLV LSRLGGGIGT RGPGESKIEV DRRRIRDRIG DIARQIENIE KQRNLHRKRR QSTRIPTVAL VGYTNAGKST LLNTLTDSDV FAEDKLFATL DPTTRHMTLP DGQTTLLTDT VGFIQKLPHH LIAAFRATLE EVIQADLLLH IIDVSHPQYQ EQSKTVYQVL GELNVDTRNL ITVFNKVDRI GNQGLLDQLL QQDNSIAISA LSGVGTEKLL GLISTFLKEQ TIEISLLIPY SDSSIIAQLY DVSTVHSTEY RDEGIYVLIS LPPDEINRFS TYTIGADVNE // ID A0A075LPP0_9BACI Unreviewed; 413 AA. AC A0A075LPP0; DT 29-OCT-2014, integrated into UniProtKB/TrEMBL. DT 29-OCT-2014, sequence version 1. DT 07-JUN-2017, entry version 20. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=GZ22_07300 {ECO:0000313|EMBL:AIF66458.1}; OS Terribacillus aidingensis. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Terribacillus. OX NCBI_TaxID=586416 {ECO:0000313|EMBL:AIF66458.1, ECO:0000313|Proteomes:UP000027980}; RN [1] {ECO:0000313|EMBL:AIF66458.1, ECO:0000313|Proteomes:UP000027980} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MP602 {ECO:0000313|EMBL:AIF66458.1, RC ECO:0000313|Proteomes:UP000027980}; RA Wang Y., Lu P., Zhang L.; RT "Complete genome sequence of a moderately halophilic bacterium RT Terribacillus aidingensis MP602, isolated from Cryptomeria fortunei in RT Tianmu mountain in China."; RL Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP008876; AIF66458.1; -; Genomic_DNA. DR RefSeq; WP_038560426.1; NZ_CP008876.1. DR EnsemblBacteria; AIF66458; AIF66458; GZ22_07300. DR KEGG; tap:GZ22_07300; -. DR KO; K03665; -. DR Proteomes; UP000027980; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000027980}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000027980}. FT DOMAIN 194 355 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 413 AA; 46768 MW; 43141653C7C4CF31 CRC64; MERVLLMAVH HQNQTLERFQ SSLDELEALT KTAGGEVAGI VTQKRERLHP GTYFGSGKLE ELAELVEEEE PLLVISNDEL SPGQLKNISN RVGVRVIDRS QLILDIFATR AHTREGKLQV ELAQMQYLLP RLYGQGTEMS RLGAGIGTRG PGETKLETDR RHIRRRIDEI KQQLKAVVSH RSRYRERRKA NQAFQVALVG YTNAGKSTIF NRVTGNDSLE QDQLFATLDP MTRRMRLPSG FQALLTDTVG FIQDLPTALI AAFRSTLEEV TEADFIIHMV NSAHPDHEQQ QNTVLKLLKE LGADQLPILT VYNKADLLTE DFIASAHPYV QISAFKEEDR RLVMEKVQEM IQETSEFYDT IVPASGGRLL DKLAQETILT KREYNEEMDA YEVSGYVLPN NPLFHQLKGK NEA // ID A0A075LTI5_9EURY Unreviewed; 433 AA. AC A0A075LTI5; DT 29-OCT-2014, integrated into UniProtKB/TrEMBL. DT 29-OCT-2014, sequence version 1. DT 12-APR-2017, entry version 19. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=PAP_04290 {ECO:0000313|EMBL:AIF69272.1}; OS Palaeococcus pacificus DY20341. OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae; OC Palaeococcus. OX NCBI_TaxID=1343739 {ECO:0000313|EMBL:AIF69272.1, ECO:0000313|Proteomes:UP000027981}; RN [1] {ECO:0000313|Proteomes:UP000027981} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DY20341 {ECO:0000313|Proteomes:UP000027981}; RA Zeng X., Shao Z.; RT "Complete Genome Sequence of Hyperthermophilic Palaeococcus pacificus RT DY20341T, Isolated from a Deep-Sea Hydrothermal Sediments."; RL Submitted (JUN-2013) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP006019; AIF69272.1; -; Genomic_DNA. DR EnsemblBacteria; AIF69272; AIF69272; PAP_04290. DR KEGG; ppac:PAP_04290; -. DR KO; K03665; -. DR OrthoDB; POG093Z07D6; -. DR Proteomes; UP000027981; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000027981}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000027981}. FT DOMAIN 187 363 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 433 AA; 49592 MW; 232510D05295DA00 CRC64; MMKVIGVIRH SQRKRVSREE FEELLSSAGY EVLDIIEQVR EESPRYNIGK GKVQEIKVKI EELKPDKVIF ANRLTPSQAY NLSKELGIEI IDKWQLVLEI FEKRARSKEA KLQVELANLQ YELPIVKEAI RRIKLGDKAG FKGMGQYQTQ QYLKHIRYRM GKIRKELERV KADRAVKRKR REEVGFILLA LAGYTNAGKS TLLNALTREE VAVKNQMFTT LGTITRAFKV SRKKVLVTDT VGFIDNLPPF IVEAFHSTLE EIVQADIILL VLDASEPWTE IKRKFLASIH VLRELKSLDK PIIAVLNKND LTTPEDIKDK KEEIKKLADS RGLVIFDVVS ISAKLNDLDE LFDALDRLIL TLPKFKLFEI IVGDIEKVPR VLSLLNSIGE IVEVKENEET RILAYIQMGM IKELTKLGVE LKQAGESKEL EDS // ID A0A075R4A8_BRELA Unreviewed; 429 AA. AC A0A075R4A8; DT 29-OCT-2014, integrated into UniProtKB/TrEMBL. DT 29-OCT-2014, sequence version 1. DT 07-JUN-2017, entry version 20. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:AIG27377.1}; GN ORFNames=BRLA_c030650 {ECO:0000313|EMBL:AIG27377.1}; OS Brevibacillus laterosporus LMG 15441. OC Bacteria; Firmicutes; Bacilli; Bacillales; Paenibacillaceae; OC Brevibacillus. OX NCBI_TaxID=1042163 {ECO:0000313|EMBL:AIG27377.1, ECO:0000313|Proteomes:UP000005850}; RN [1] {ECO:0000313|EMBL:AIG27377.1, ECO:0000313|Proteomes:UP000005850} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=LMG 15441 {ECO:0000313|EMBL:AIG27377.1, RC ECO:0000313|Proteomes:UP000005850}; RX PubMed=21914864; DOI=10.1128/JB.05696-11; RA Djukic M., Poehlein A., Thurmer A., Daniel R.; RT "Genome sequence of Brevibacillus laterosporus LMG 15441, a pathogen RT of invertebrates."; RL J. Bacteriol. 193:5535-5536(2011). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP007806; AIG27377.1; -; Genomic_DNA. DR RefSeq; WP_003335721.1; NZ_CP007806.1. DR ProteinModelPortal; A0A075R4A8; -. DR STRING; 1042163.BRLA_c21030; -. DR EnsemblBacteria; AIG27377; AIG27377; BRLA_c030650. DR KEGG; blr:BRLA_c030650; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR KO; K03665; -. DR Proteomes; UP000005850; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000005850}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000005850}. FT DOMAIN 200 362 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 159 193 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 429 AA; 48608 MW; 7652B0F14AC3FF5B CRC64; MSEWNKQQTA IVVGCLLDQR DEERMRLSLE ELGELARTAG VEVLEVITQN RERVDSAWYL GTGKIQEIAE LAVSLDVDVV IFNDELSASQ NRNLEALFEC RVIDRTQLIL DIFASRANSR EGKIQVELAQ YSYLLPRLAG QGNQMSRLGG GIGTRGPGET KLETDRRHIR RRISELKQQL DDIVRTRQLH RERRKKNHVY QIALVGYTNA GKSTLLNNLT KADTLQEDKL FATLDPTTRQ LALPSGKEVL LTDTVGFIQD LPTALIAAFR STLEGVQEAD LILHVVDCSH PDFEVHMEVV DQVLKDLEAE GIPRLVVYNK ADLLDTDKYL PHPEDSIQIS ALSEQDLQRL LNRVEGIVLT GYESVELIIP MERGDVISMM HRAGLEMEQE FSEDGTAYHI TIRIKPDEPM YGRLIPYMVN PPAINEEEW // ID A0A075U7M9_9LACT Unreviewed; 427 AA. AC A0A075U7M9; DT 29-OCT-2014, integrated into UniProtKB/TrEMBL. DT 29-OCT-2014, sequence version 1. DT 07-JUN-2017, entry version 23. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=WS74_1228 {ECO:0000313|EMBL:AIM63477.1}; OS Weissella ceti. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Leuconostocaceae; OC Weissella. OX NCBI_TaxID=759620 {ECO:0000313|EMBL:AIM63477.1, ECO:0000313|Proteomes:UP000029079}; RN [1] {ECO:0000313|Proteomes:UP000029079} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=WS74 {ECO:0000313|Proteomes:UP000029079}; RA Figueiredo H.C.P., Leal C.A.G., Pereira F.L., Soares S.C., RA Dorella F.A., Carvalho A.F., Azevedo V.A.C.; RT "Complete genome of Weissella ceti strain WS74 isolated from diseased RT rainbow trout in Brazil."; RL Submitted (AUG-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP009223; AIM63477.1; -; Genomic_DNA. DR RefSeq; WP_009765104.1; NZ_CP009224.1. DR EnsemblBacteria; AIM63477; AIM63477; WS74_1228. DR KEGG; wce:WS08_1159; -. DR KEGG; wci:WS105_1222; -. DR KEGG; wct:WS74_1228; -. DR PATRIC; fig|759620.7.peg.1184; -. DR KO; K03665; -. DR Proteomes; UP000029079; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000029079}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000029079}. FT DOMAIN 204 373 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 163 202 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 427 AA; 47638 MW; 057C46C02A4A3F20 CRC64; MIENEQNPRR KVILAGLERV DVDFTYQMEE LANLADANNM EVVGTLTQKM ERPHGGTYFG KGKVEELGEL VKALDAEMVV TNDELSPSQI RNLEAGTGVS MMDRTALILD IFATRAKTKV AKLQVAIAQL QYQLPRLRTS MNVRMDQQTG GGGGSFTSRG AGETKLELNR RHIEHQISEL RKELANIEAD DQTRRAHREK EEIKTVALVG YTNAGKSTIM NGLVKRFGEN QEKTVFQADM LFATLETAVR KINLPDKQSF LLSDTVGFVS KLPHGLVAAF KATLAEAAQA DLLIQVVDYS DPDYKAMMET TMKTLQEIGV RDVPMVIAFN KADRIEDQAY PERQEDELIM SAKSDESLDT LIEMVRAEIF SDHVQKELMI PFADGQVVAA LNDDATVHET EYTEEGTKLS VTLTPTQVAR YGKYIIE // ID A0A076K4J7_9RHOB Unreviewed; 434 AA. AC A0A076K4J7; DT 29-OCT-2014, integrated into UniProtKB/TrEMBL. DT 29-OCT-2014, sequence version 1. DT 07-JUN-2017, entry version 17. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:AII87118.1}; GN ORFNames=RCA23_c15810 {ECO:0000313|EMBL:AII87118.1}; OS Planktomarina temperata RCA23. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae; Planktomarina. OX NCBI_TaxID=666509 {ECO:0000313|EMBL:AII87118.1, ECO:0000313|Proteomes:UP000028680}; RN [1] {ECO:0000313|EMBL:AII87118.1, ECO:0000313|Proteomes:UP000028680} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=RCA23 {ECO:0000313|EMBL:AII87118.1}; RX PubMed=25083934; RA Voget S., Wemheuer B., Brinkhoff T., Vollmers J., Dietrich S., RA Giebel H.A., Beardsley C., Sardemann C., Bakenhus I., Billerbeck S., RA Daniel R., Simon M.; RT "Adaptation of an abundant Roseobacter RCA organism to pelagic systems RT revealed by genomic and transcriptomic analyses."; RL ISME J. 0:0-0(2014). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP003984; AII87118.1; -; Genomic_DNA. DR RefSeq; WP_044049883.1; NZ_CP003984.1. DR EnsemblBacteria; AII87118; AII87118; RCA23_c15810. DR KEGG; ptp:RCA23_c15810; -. DR KO; K03665; -. DR Proteomes; UP000028680; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000028680}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000028680}. FT DOMAIN 205 374 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 434 AA; 47801 MW; 1C437E8C8F235CBB CRC64; MGNTPDAHET HAWVLHPDIK TDYSARAATD ALAEAVSLAH ALPGLEVMGE TIVRLPRAHP GKLFGKGKIA ELAELFKAAE VELVLIDGHV SPVQQRNLEK DWGVKILDRT GLILEIFSDR ARTREGVLQV EMAALSYQRT RLVRAWTHLE RQRGGLGFVG GPGETQIESD RRAIDIQLVR LQKQLDKVVK TRELHRSARA KVPYPIVALV GYTNAGKSTL FNYMTGAKVL AKDMLFATLD PTMRAVKLPS GMDVILSDTV GFISDLPTEL VASFRATLEE VTAAQLVVHV RDIAHPETAE QAQDVNTILE TLGLDRDVPR IEMWNKSDIL DPSALEALQN AAERSDDVFI TSALTGAGVP EFLDAVSRRL TPDKTQSELV LGFDEGRARA WLFEQGLVRD EQQTQEGFSL SVSWTARQKK AFSDQFGPKL VSGS // ID A0A076MWD6_AMYME Unreviewed; 476 AA. AC A0A076MWD6; DT 29-OCT-2014, integrated into UniProtKB/TrEMBL. DT 29-OCT-2014, sequence version 1. DT 07-JUN-2017, entry version 22. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:AIJ25078.1}; GN ORFNames=AMETH_4986 {ECO:0000313|EMBL:AIJ25078.1}; OS Amycolatopsis methanolica 239. OC Bacteria; Actinobacteria; Pseudonocardiales; Pseudonocardiaceae; OC Amycolatopsis. OX NCBI_TaxID=1068978 {ECO:0000313|EMBL:AIJ25078.1, ECO:0000313|Proteomes:UP000062973}; RN [1] {ECO:0000313|EMBL:AIJ25078.1, ECO:0000313|Proteomes:UP000062973} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=239 {ECO:0000313|EMBL:AIJ25078.1, RC ECO:0000313|Proteomes:UP000062973}; RA Tang B.; RT "Whole Genome Sequence of the Amycolatopsis methanolica 239."; RL Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP009110; AIJ25078.1; -; Genomic_DNA. DR RefSeq; WP_017983915.1; NZ_CP009110.1. DR EnsemblBacteria; AIJ25078; AIJ25078; AMETH_4986. DR KEGG; amq:AMETH_4986; -. DR PATRIC; fig|1068978.7.peg.5361; -. DR KO; K03665; -. DR Proteomes; UP000062973; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000062973}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000062973}. FT DOMAIN 249 418 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 476 AA; 51370 MW; ECB9ADCD5C8F46C8 CRC64; MTELTYTDLV EDPSTGDLEL SERASLRRVA GLSTELSDIT EVEYRKLRLE RVVLVGVWTE GTAEQSEASL AELARLAETA GSEVLEGLVQ RRAKPDPATY IGSGKVRELF DIVVATGADT VICDGELSPG QLRQLEERLK VKVIDRTALI LDIFAQHARS REGKAQVELA QLQYLIPRLR GWGESLSRQA GGRAGGANGG VGLRGPGETK LETDRRRINK RVAKLRREIA AMDTIRATKR GRRVANEVPS VAIVGYTNAG KSSLLNAITG AGVLVENALF ATLDPTTRRA ATPDGRTFTL TDTVGFVRHL PHQLVDAFRS TLDETADADL LLHVVDGSDP APEEQVNAVR QVLAEITRSH ESPLPPELIV INKADAADEL SLVRLRHLLP GAIVVSAKTG EGVPELLDAL AERLPRPDVV VDALVPYTRG ELVARVHSEG EVLTEEHLAE GTRLSARVRP DVASALEAYA VNGSPA // ID A0A076NGX8_9CORY Unreviewed; 508 AA. AC A0A076NGX8; DT 29-OCT-2014, integrated into UniProtKB/TrEMBL. DT 29-OCT-2014, sequence version 1. DT 07-JUN-2017, entry version 20. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=CIMIT_07320 {ECO:0000313|EMBL:AIJ33734.1}; OS Corynebacterium imitans. OC Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae; OC Corynebacterium. OX NCBI_TaxID=156978 {ECO:0000313|EMBL:AIJ33734.1, ECO:0000313|Proteomes:UP000028780}; RN [1] {ECO:0000313|EMBL:AIJ33734.1, ECO:0000313|Proteomes:UP000028780} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 44264 {ECO:0000313|EMBL:AIJ33734.1, RC ECO:0000313|Proteomes:UP000028780}; RA Mollmann S., Albersmeier A., Ruckert C., Tauch A.; RT "Complete genome sequence of Corynebacterium imitans DSM 44264, RT isolated from a five-month-old boy with suspected pharyngeal RT diphtheria."; RL Submitted (AUG-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP009211; AIJ33734.1; -; Genomic_DNA. DR RefSeq; WP_051904867.1; NZ_CP009211.1. DR EnsemblBacteria; AIJ33734; AIJ33734; CIMIT_07320. DR KEGG; cii:CIMIT_07320; -. DR KO; K03665; -. DR Proteomes; UP000028780; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000028780}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000028780}. FT DOMAIN 280 460 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 239 266 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 508 AA; 55727 MW; 52CB28C08FF36EC2 CRC64; MTSTVNTHPE HDPQEAAHDA LLAEAFRHNA PQPPREGSGE PTTGSLDLEA RNALRRVGQR TEIRTDEAEE AYEVEYRKLR LEQVILVGAW LEGTTAEMEA NMRELEALTE TAGAEVIDML YQKRDKPDPG TYIGAGKVSE LRDVVEASGA DTVVFDGELS PSQIVALEEA LRVKVIDRTM LILDIFAQHA KSNEGKAQVS LAQMEYLFSR TRGWGGNLSR QAGGRAGSNG GVGLRGPGET RIEADRRRLR ADMARLRHEL KGMKTVREVK RARRNRSTTP QIAIAGYTNA GKSSLINAMT DAGVLVEDAL FATLDPATRR AQLADGRTVV LTDTVGFVRH LPTQLVEAFK STLEEVTNAD LVLHVVDGSD PFPLKQIEAV NEVLAEITRD SGEEIPPEIV VVNKIDQADP LVLAELRHAF DKSGRDVVFV SALTGEGIPE LEGKVEQFLN TLDAHVEMLV PYTRGDVVSH IHEAGTVRSE AYEEDGTRID VRLPHVLAEQ YAEFVVAK // ID A0A077DGS2_9BURK Unreviewed; 367 AA. AC A0A077DGS2; DT 29-OCT-2014, integrated into UniProtKB/TrEMBL. DT 29-OCT-2014, sequence version 1. DT 07-JUN-2017, entry version 18. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=IX83_04460 {ECO:0000313|EMBL:AIL32657.1}; OS Basilea psittacipulmonis DSM 24701. OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Alcaligenaceae; Basilea. OX NCBI_TaxID=1072685 {ECO:0000313|EMBL:AIL32657.1, ECO:0000313|Proteomes:UP000028945}; RN [1] {ECO:0000313|EMBL:AIL32657.1, ECO:0000313|Proteomes:UP000028945} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 24701 {ECO:0000313|EMBL:AIL32657.1}; RX PubMed=24581117; RA Whiteson K.L., Hernandez D., Lazarevic V., Gaia N., Farinelli L., RA Francois P., Pilo P., Frey J., Schrenzel J.; RT "A genomic perspective on a new bacterial genus and species from the RT Alcaligenaceae family, Basilea psittacipulmonis."; RL BMC Genomics 15:169-169(2014). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP009238; AIL32657.1; -; Genomic_DNA. DR RefSeq; WP_038501537.1; NZ_CP009238.1. DR EnsemblBacteria; AIL32657; AIL32657; IX83_04460. DR KEGG; bpsi:IX83_04460; -. DR KO; K03665; -. DR Proteomes; UP000028945; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000028945}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000028945}. FT DOMAIN 190 356 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 156 183 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 367 AA; 41400 MW; 1169FED851E3F5C6 CRC64; MRAYIISVNF GDPDYQAHAD EFMMLAKGAG AEVVGYLEAK RDKPDSALFI GSGKAEEALA QMSAVQADIV LFDQILTPAQ QRNLERLFKI RVIDRVALIL DIFALRARSY EGKLQVELAQ LQRLVTRLTR LWTHLERQRG GIGMRGPGES QLEMDKRMIG AKVKTLKERL DKVERQRHTQ RRSRYRSNIL TVSIVGYTNA GKSTLFNALT KADTYAADQL FATLDTTTRK LWIQECGNVI ISDTVGFIRD LPTTLIAAFK ATLEETVEAD LLLHVVDASS EQRDEQIRSV HQVLEEIGAN EIPAILVYNK IDQAGLEPKV ILDEEGMPKK VFVSALETKG LSELRHAIAE YARKLGKYEQ YTIKEYE // ID A0A077E8H5_9FLAO Unreviewed; 405 AA. AC A0A077E8H5; DT 29-OCT-2014, integrated into UniProtKB/TrEMBL. DT 29-OCT-2014, sequence version 1. DT 07-JUN-2017, entry version 19. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=BD94_0117 {ECO:0000313|EMBL:AIL43892.1}; OS Elizabethkingia anophelis NUHP1. OC Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales; OC Flavobacteriaceae; Elizabethkingia. OX NCBI_TaxID=1338011 {ECO:0000313|EMBL:AIL43892.1, ECO:0000313|Proteomes:UP000028933}; RN [1] {ECO:0000313|EMBL:AIL43892.1, ECO:0000313|Proteomes:UP000028933} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NUHP1 {ECO:0000313|EMBL:AIL43892.1}; RX PubMed=24012265; DOI=10.1016/S0140-6736(13)61858-9; RA Teo J., Tan S.Y., Tay M., Ding Y., Kjelleberg S., Givskov M., RA Lin R.T., Yang L.; RT "First case of E anophelis outbreak in an intensive-care unit."; RL Lancet 382:855-856(2013). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP007547; AIL43892.1; -; Genomic_DNA. DR RefSeq; WP_009086423.1; NZ_CP007547.1. DR EnsemblBacteria; AIL43892; AIL43892; BD94_0117. DR GeneID; 23371385; -. DR KEGG; eao:BD94_0117; -. DR KO; K03665; -. DR Proteomes; UP000028933; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000028933}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000028933}. FT DOMAIN 200 384 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 405 AA; 47181 MW; 0DB60A3347CC1F91 CRC64; MLEKKEHQYE KAVLVGLITK DQDEEKLKEY MDELEFLAYT AGATVEKRFT QKMSQPDSKT FVGKGKAEEI RDYVKENEIG TVIFDDELSP SQLKNLERDI EVKILDRTNL ILDIFAQRAQ TSYARTQVEL AQYEYLLPRL TRMWTHLERQ RGGIGMRGPG ETEIETDRRI IRDRISLLKD KLKTIDRQMA TQRNNRGKMV RVALVGYTNV GKSTLMNSLS KSEVFAENKL FATLDTTVRK VVIGNLPFLL TDTVGFIRKL PTQLVESFKS TLDEVREADL LIHVVDISHE SFEDHVNSVN EILQEIDAHK KPVLMVFNKI DDFSYEKKAE DDLTPATRKN ISLEEWKNTW MAKSKHPTVF ISALTKENFP EMKKMIYDEV LKIHISRFPY NDFLFEYYDD EEVVE // ID A0A077FKE1_9RICK Unreviewed; 411 AA. AC A0A077FKE1; DT 29-OCT-2014, integrated into UniProtKB/TrEMBL. DT 29-OCT-2014, sequence version 1. DT 12-APR-2017, entry version 15. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:AIL65987.1}; GN ORFNames=NOVO_08305 {ECO:0000313|EMBL:AIL65987.1}; OS Rickettsiales bacterium Ac37b. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales. OX NCBI_TaxID=1528098 {ECO:0000313|EMBL:AIL65987.1, ECO:0000313|Proteomes:UP000028936}; RN [1] {ECO:0000313|EMBL:AIL65987.1, ECO:0000313|Proteomes:UP000028936} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Ac37b {ECO:0000313|EMBL:AIL65987.1, RC ECO:0000313|Proteomes:UP000028936}; RA Felsheim R.F., Kurtti T.J., Johnson S., Labruna M.B., Munderloh U.G.; RT "Genome sequence of a novel Rickettsiales species cultured from RT Amblyomma cajennense."; RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP009217; AIL65987.1; -; Genomic_DNA. DR EnsemblBacteria; AIL65987; AIL65987; NOVO_08305. DR KEGG; rbt:NOVO_08305; -. DR KO; K03665; -. DR Proteomes; UP000028936; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000028936}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000028936}. FT DOMAIN 186 352 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 411 AA; 46922 MW; FE7E2CCA5B185882 CRC64; MKKDFVEYKA KDRLAEAVAL AKAINLEIVL EEIVILSKIS SASFIGSGKV SEYANIIKQL DVTLVIIDEK VSPIQQRNLE KAWKCKVIER TALIIEIFGD RAKTKEGKLQ VNLAHFQYQK SRLVRTWTHL ERQRGGHGFL AGPGEKQIEV DRRIITQQIT KIKRELEKIK LTRAEHRKSR QAVPYPIISL VGYTNTGKTT LFNRLTGAKL LAADMLFATL DPTMRIVTLP SRKKIILSDT VGFISDLPTE LIVSFRATLE EVKQADLILH VQDISSPNRL KQKEEVNKIL VSLGTEDKIY HHTIEVLNKM DLLEETKEIS NSVSDNVLYI SASTGINCDK LLEYIDHKLS MNDKVIKIEI ENLDGKVLAW IYSNSAVIER QEQEDKIYML LRISEKNYQK LLKNFTVKIL N // ID A0A077FKX0_9PSED Unreviewed; 433 AA. AC A0A077FKX0; DT 29-OCT-2014, integrated into UniProtKB/TrEMBL. DT 29-OCT-2014, sequence version 1. DT 30-AUG-2017, entry version 22. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=PSAKL28_47910 {ECO:0000313|EMBL:AIL63931.1}; OS Pseudomonas alkylphenolica. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=237609 {ECO:0000313|EMBL:AIL63931.1, ECO:0000313|Proteomes:UP000028931}; RN [1] {ECO:0000313|EMBL:AIL63931.1, ECO:0000313|Proteomes:UP000028931} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=KL28 {ECO:0000313|EMBL:AIL63931.1, RC ECO:0000313|Proteomes:UP000028931}; RA Lee K., Lim J.Y., Hwang I.; RL Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP009048; AIL63931.1; -; Genomic_DNA. DR RefSeq; WP_038615206.1; NZ_CP009048.1. DR EnsemblBacteria; AIL63931; AIL63931; PSAKL28_47910. DR GeneID; 29605797; -. DR KEGG; palk:PSAKL28_47910; -. DR KO; K03665; -. DR Proteomes; UP000028931; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000028931}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000028931}. FT DOMAIN 199 366 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 165 192 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 433 AA; 48750 MW; 4CC0011EF47CFD5D CRC64; MFFERHGGGE RAVLVHLEGQ NPEAREDPQE FRELALSAGA DIVAFANVAR HQPSAKYLIG SGKVEELRDL VSAEQVDLVI FNHTLTPSQE RNLERVFECR VLDRTGLILD IFAQRARTHE GKLQVELAQL EYMSTRLVRG WTHLERQKGG IGLRGPGETQ LETDRRLLRV RLRQIKARLE KVRSQREQAR RGRKRADIPS VSLVGYTNAG KSTLFNALTQ SEVYAADQLF ATLDPTLRRL ELDDVGPIVL ADTVGFIRHL PHKLVEAFRA TLEESSNSDL LLHVIDAHEP DRMEQIEQVM AVLGEIGAEG LPILEVYNKL DLLEGVEPQI QRDADGKPQR VWVSARDGRG LELVGQAVAE LLGDDLFIGT LRLEQRFARL RAQFFALGAV QGEEHDDEGS SLLAIRVSRV EFNRLVTREG LKPAEFIEQH TLQ // ID A0A077HKX4_9CORY Unreviewed; 493 AA. AC A0A077HKX4; DT 29-OCT-2014, integrated into UniProtKB/TrEMBL. DT 29-OCT-2014, sequence version 1. DT 05-JUL-2017, entry version 20. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=CUREI_07100 {ECO:0000313|EMBL:AIL97086.1}; OS Corynebacterium ureicelerivorans. OC Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae; OC Corynebacterium. OX NCBI_TaxID=401472 {ECO:0000313|EMBL:AIL97086.1, ECO:0000313|Proteomes:UP000028939}; RN [1] {ECO:0000313|EMBL:AIL97086.1, ECO:0000313|Proteomes:UP000028939} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=IMMIB RIV-2301 {ECO:0000313|EMBL:AIL97086.1, RC ECO:0000313|Proteomes:UP000028939}; RA Tippelt A., Albersmeier A., Brinkrolf K., Ruckert C., Tauch A.; RT "Complete genome sequence of Corynebacterium ureicelerivorans DSM RT 45051, a lipophilic and urea-splitting isolate from a blood culture of RT a septicaemia patient."; RL Submitted (AUG-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP009215; AIL97086.1; -; Genomic_DNA. DR EnsemblBacteria; AIL97086; AIL97086; CUREI_07100. DR KEGG; cuv:CUREI_07100; -. DR KO; K03665; -. DR Proteomes; UP000028939; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000028939}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000028939}. FT DOMAIN 266 439 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 225 252 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 493 AA; 54160 MW; 5481BC939257BA24 CRC64; MTPEQRTHDE LLRQAFRHNE PQPGAEPTVG ALDLAERNSF RSVTGATELR SEEQADGYEV EYRKLRIEQV LLVGAWTEGT VAEIEASMWE LAALAKTAGA EVLDMLYQKR DKPDPGTYIG SGKVAELRDI AQATGADTVI FDGELSPSQM IALEEALKIK VIDRTMLILD IFAQHAKSRE GKAQVSLAQM EYLYSRTRGW GGNLSRQAGG RAGSNGGVGL RGPGETRIEA DRRRLRTEMA KLRHQLRDMT TAREVKRAQR QRSTIPKIAI AGYTNAGKSS LINAMTGAGV LVEDALFATL DPSTRRAKLA DGRNVVLTDT VGFVRHLPTQ LVEAFKSTLE EVSGADLLLH VVDGSDAFPL KQIEAVNEVL AEVTRDSGED MPPEIVVVNK IDEADPLVLA ELRHAFEKTG RTAVFVSALT GEGIEELEVR IEQHLNSIDA HVTMVVPYTR GDVVSRVHDE GTVRSEEYEE AGTRIDVRLP RVLAEQYAEF VVG // ID A0A077J9Z5_9BACI Unreviewed; 418 AA. AC A0A077J9Z5; DT 29-OCT-2014, integrated into UniProtKB/TrEMBL. DT 29-OCT-2014, sequence version 1. DT 07-JUN-2017, entry version 22. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=HW35_17160 {ECO:0000313|EMBL:AIM17771.1}; OS Bacillus sp. X1(2014). OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus. OX NCBI_TaxID=1565991 {ECO:0000313|EMBL:AIM17771.1, ECO:0000313|Proteomes:UP000031100}; RN [1] {ECO:0000313|Proteomes:UP000031100} RP NUCLEOTIDE SEQUENCE. RC STRAIN=X1 {ECO:0000313|Proteomes:UP000031100}; RA Fomenkov A., Lunnen K.D., Zhu Z., Wilson G.G., Vincze T., RA Roberts R.J.; RT "Complete Genome Sequence and Methylome Analysis of Bacillus sp. RT X1(2014)."; RL Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP008855; AIM17771.1; -; Genomic_DNA. DR RefSeq; WP_038541333.1; NZ_CP008855.1. DR EnsemblBacteria; AIM17771; AIM17771; HW35_17160. DR KEGG; gst:HW35_17160; -. DR PATRIC; fig|1565991.4.peg.3399; -. DR KO; K03665; -. DR Proteomes; UP000031100; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000031100}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000031100}. FT DOMAIN 199 361 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 418 AA; 47626 MW; 2C07FBEFAE75422D CRC64; MEQREPKEKA ILVGCQIDDD DLRFHYSMEE LKSLTETAQG TVLATVSQKR DRLHPATYIG KGKVEEIKNL VEETEADLVI FNDELTPSQK RNLAAEIDAR IIDRTQLILD IFAQRARSKE GKLQVELAQL QYLLPRLGGQ GTALSRLGGG IGTRGPGETK LESDRRHIRR RIDDIKNQLS VITQHRNRYR ERRKKNKTFQ VAIVGYTNAG KSTLFNRLSE ADSYEENQLF ATLDPMTRKL ILPSGFHALI TDTVGFIQDL PTSLIAAFRS TLEEVKEADL LLHVVDMSNP DYFHHEKTVN KLLEELEVSD VPQLTVYNKR DIKHPDFVPT ANTPTVFISA LDEGDRQNLK LKIEQVMKGM MQPYEVVVPS SEGKLLSQLK NATILRELTF NEETQAYHCK GYTLQDHQIT GQLQKYQI // ID A0A077LGP6_9PSED Unreviewed; 433 AA. AC A0A077LGP6; DT 29-OCT-2014, integrated into UniProtKB/TrEMBL. DT 29-OCT-2014, sequence version 1. DT 30-AUG-2017, entry version 20. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=PSCI_2364 {ECO:0000313|EMBL:BAP43066.1}; OS Pseudomonas sp. StFLB209. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=1028989 {ECO:0000313|EMBL:BAP43066.1, ECO:0000313|Proteomes:UP000031652}; RN [1] {ECO:0000313|Proteomes:UP000031652} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=StFLB209 {ECO:0000313|Proteomes:UP000031652}; RA Morohoshi T., Kato T., Someya N., Ikeda T.; RT "Complete Genome Sequence of N-Acylhomoserine Lactone-Producing RT Pseudomonas sp. Strain StFLB209, Isolated from Potato Phyllosphere."; RL Genome Announc.2:e01037-14(2014). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AP014637; BAP43066.1; -; Genomic_DNA. DR RefSeq; WP_045486825.1; NZ_AP014637.1. DR EnsemblBacteria; BAP43066; BAP43066; PSCI_2364. DR KEGG; pses:PSCI_2364; -. DR KO; K03665; -. DR Proteomes; UP000031652; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000031652}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000031652}. FT DOMAIN 199 366 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 433 AA; 49076 MW; 23D5E2AF35E3E50F CRC64; MFFERHSGGE RALLVHLEGQ DPEAREDPQE FQELALSAGA DTVALVNVPR HRPSAKYLIG TGKVEELRDQ VRSGHVDLVI FNHTLTPSQE RNLERVFECR VLDRTGLILD IFAQRARTHE GKLQVELAQL EHMSTRLVRG WTHLERQKGG IGLRGPGETQ LETDRRLLRV RLRQIKGRLE KVRSQRDQAR RGRKRADIPS VSLVGYTNAG KSTLFNSVTD SEVYAADQLF ATLDPTLRRL QLDDLGPIVL ADTVGFIRHL PHKLVEAFRA TLEESSNSDL LLHVIDAHEP ERDAQIEQVM AVLVEIGAQD LPILEVYNKL DLLENVEPHI QRTPDGKPER VWLSARDGRG LDLLKQAIAE LLGEDLFVAT LRLPQRFARL RARFFEVGAV QSEVHDEEGA SLLAVRLPRV ELNRLVSREG LQPLEFIEQH TLQ // ID A0A077LXW0_9MICO Unreviewed; 484 AA. AC A0A077LXW0; DT 29-OCT-2014, integrated into UniProtKB/TrEMBL. DT 29-OCT-2014, sequence version 1. DT 07-JUN-2017, entry version 19. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=BN12_1450003 {ECO:0000313|EMBL:CCH76760.1}; OS Tetrasphaera japonica T1-X7. OC Bacteria; Actinobacteria; Micrococcales; Intrasporangiaceae; OC Tetrasphaera. OX NCBI_TaxID=1194083 {ECO:0000313|EMBL:CCH76760.1, ECO:0000313|Proteomes:UP000035721}; RN [1] {ECO:0000313|EMBL:CCH76760.1, ECO:0000313|Proteomes:UP000035721} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=T1-X7 {ECO:0000313|EMBL:CCH76760.1, RC ECO:0000313|Proteomes:UP000035721}; RX PubMed=23178666; DOI=10.1038/ismej.2012.136; RA Kristiansen R., Nguyen H.T.T., Saunders A.M., Nielsen J.L., Wimmer R., RA Le V.Q., McIlroy S.J., Petrovski S., Seviour R.J., Calteau A., RA Nielsen K.L., Nielsen P.H.; RT "A metabolic model for members of the genus Tetrasphaera involved in RT enhanced biological phosphorus removal."; RL ISME J. 7:543-554(2013). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:CCH76760.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CAJB01000052; CCH76760.1; -; Genomic_DNA. DR RefSeq; WP_048553565.1; NZ_HF570958.1. DR EnsemblBacteria; CCH76760; CCH76760; BN12_1450003. DR Proteomes; UP000035721; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 2. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000035721}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000035721}. FT DOMAIN 266 431 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 484 AA; 52587 MW; 7488A682760D000D CRC64; MTARHTDYFT EQAAALAAED AAWDPDTDLS RDGEQLDREE RAALRRVAGL STELQDVTEV EYRQLRLERV VLAAVWTEGT AEDAENSLRE LAALAETAGS TVLDGVVQRR SHPDPGTWLG SGKAEELRDI VIAEGADTVI CDSELAPSQR RALEDIVKVK VIDRTALILD IFAQHAKSKE GRAQVELAQL QYLLPRLRGW GESMSRQAGG RVAGGEGIGS RGPGETKIEL DRRRINSRIA KLRRDLKAMK TVRDTKRGGR RRGHVPSVAI AGYTNAGKSS LLNRLTGAGV LVENQLFATL DTTVRRAETP EGREYTLTDT VGFVRQLPTE LVEAFRSTLE EVGEADLLLH VVDGSHPDPE GQISAVRGVL ADVDAADVKE IVVVNKADVA DPEVVDRILR HEKHAVAVSA RTGEGIDALR QLVADELPQP SVEVDIVVPY HRGDLVSRVH ERGEVVTSDH LAGGTRLVAK VNPDLAAELA AYAS // ID A0A077MEN5_9MICO Unreviewed; 493 AA. AC A0A077MEN5; DT 29-OCT-2014, integrated into UniProtKB/TrEMBL. DT 29-OCT-2014, sequence version 1. DT 07-JUN-2017, entry version 19. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=BN13_710006 {ECO:0000313|EMBL:CCI54440.1}; OS Tetrasphaera jenkinsii Ben 74. OC Bacteria; Actinobacteria; Micrococcales; Intrasporangiaceae; OC Tetrasphaera. OX NCBI_TaxID=1193518 {ECO:0000313|EMBL:CCI54440.1, ECO:0000313|Proteomes:UP000035720}; RN [1] {ECO:0000313|EMBL:CCI54440.1, ECO:0000313|Proteomes:UP000035720} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Ben 74 {ECO:0000313|EMBL:CCI54440.1, RC ECO:0000313|Proteomes:UP000035720}; RX PubMed=23178666; DOI=10.1038/ismej.2012.136; RA Kristiansen R., Nguyen H.T.T., Saunders A.M., Nielsen J.L., Wimmer R., RA Le V.Q., McIlroy S.J., Petrovski S., Seviour R.J., Calteau A., RA Nielsen K.L., Nielsen P.H.; RT "A metabolic model for members of the genus Tetrasphaera involved in RT enhanced biological phosphorus removal."; RL ISME J. 7:543-554(2013). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:CCI54440.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CAJC01000185; CCI54440.1; -; Genomic_DNA. DR EnsemblBacteria; CCI54440; CCI54440; BN13_710006. DR Proteomes; UP000035720; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 2. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000035720}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000035720}. FT DOMAIN 275 440 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 493 AA; 53497 MW; 18499148BA863593 CRC64; MSDYAVETSD PRDLPGAAGD HLLRGRASAL AGAAYESSDR DGEQFEREER AALQRIGGLS TELEDVTEVE YRQLRLERVV LAGVWTEGTA EDAENSLREL AALAETAGSD VLAGMLQRRQ RPDPGTWLGS GKAQELRDVV IAEGADTVVC DSELAPSQRR ALEDIVKVKV IDRTALILDI FAQHAKSREG KAQVELAQLQ YLLPRLRGWG ESMSRQAGGR VAGGEGIGSR GPGETKIELD RRRINSRIAK LRREIRDMKT HRDTKRHSRK AHGVPSVAIA GYTNAGKSSL LNRLTDAGVL VENQLFATLD TTVRRAETPD GREFTLTDTV GFVRQLPHEL IDAFRSTLEE VADADLLLHV VDGSHPDPEG QISAVRAVLA DVEAADVKEI IVVNKSDIAD PDVVDRLLRH EKHAIAVSAH TGAGIAELIE LVAGELPRPG VRVAVLIPYD RGDLLSRIHE TGELLDSEHT EHGTRVEALV GPDLAAELAP FGA // ID A0A077Z9N5_TRITR Unreviewed; 462 AA. AC A0A077Z9N5; DT 29-OCT-2014, integrated into UniProtKB/TrEMBL. DT 29-OCT-2014, sequence version 1. DT 07-JUN-2017, entry version 10. DE SubName: Full=GTP binding protein 6 {ECO:0000313|EMBL:CDW57122.1}; GN ORFNames=TTRE_0000540901 {ECO:0000313|EMBL:CDW57122.1}; OS Trichuris trichiura (Whipworm) (Trichocephalus trichiurus). OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia; OC Trichocephalida; Trichuridae; Trichuris. OX NCBI_TaxID=36087 {ECO:0000313|EMBL:CDW57122.1, ECO:0000313|Proteomes:UP000030665}; RN [1] {ECO:0000313|EMBL:CDW57122.1, ECO:0000313|Proteomes:UP000030665} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Foth B.J., Tsai I.J., Reid A.J., Bancroft A.J., Nichol S., Tracey A., RA Holroyd N., Cotton J.A., Stanley E.J., Zarowiecki M., Liu J.Z., RA Huckvale T., Cooper P.J., Grencis R.K., Berriman M.; RT "The whipworm genome and dual-species transcriptomics of an intimate RT host-pathogen interaction."; RL Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; HG806122; CDW57122.1; -; Genomic_DNA. DR Proteomes; UP000030665; Unassembled WGS sequence. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 2. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000030665}; KW Reference proteome {ECO:0000313|Proteomes:UP000030665}. FT DOMAIN 225 391 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 462 AA; 52486 MW; 899B893303DC2E14 CRC64; MYSLRICACS KLVLVRIRNF RLRTRLRWSL LSGRTFSLES DEGSGLTDTG LYDDDEPLST RTDFRDLQNY LSLPQPSSRH RLYVIQPKLS TPELKRLATT NEDLQVEAVQ LVKSVPSWTV SGINESFVKV SPKTRFIFGS GKLEELKAIV RRSRDCSAIF LNIDRLTPLQ HRSLISVFGV PVFDRYALFL ALYAHQRQLK MKEKLKATVA QRNILRQNAQ RRRFPIVAVV GYTNCGKTSL IRCLSENANL SGEDRFFATL DVTVHSGKLP CKLSILYADT VGFFSNLPMD LMPCFNSTLE EITYADLVIH VIDRSNPNWQ FQRQSVIHTF DQLNAACNLH MSPLEVWNKS DKFHLETEDD KPTTVAVVSC LSGDGMAKLL TLIEDRILKT TMYKRFVLRI PITGGYLSSL YSIGSIVSTE TSQENDHMCV TLVSKRYHID KLLGMYPNVI EVMNESTTTT TA // ID A0A078ENN5_BRANA Unreviewed; 545 AA. AC A0A078ENN5; DT 29-OCT-2014, integrated into UniProtKB/TrEMBL. DT 29-OCT-2014, sequence version 1. DT 07-JUN-2017, entry version 15. DE SubName: Full=BnaC02g11080D protein {ECO:0000313|EMBL:CDY02781.1}; GN Name=BnaC02g11080D {ECO:0000313|EMBL:CDY02781.1}; GN ORFNames=GSBRNA2T00114953001 {ECO:0000313|EMBL:CDY02781.1}; OS Brassica napus (Rape). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae; OC Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Brassiceae; OC Brassica. OX NCBI_TaxID=3708 {ECO:0000313|EMBL:CDY02781.1, ECO:0000313|Proteomes:UP000028999}; RN [1] {ECO:0000313|EMBL:CDY02781.1, ECO:0000313|Proteomes:UP000028999} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Darmor-bzh {ECO:0000313|Proteomes:UP000028999}; RX PubMed=25146293; DOI=10.1126/science.1253435; RA Chalhoub B., Denoeud F., Liu S., Parkin I.A., Tang H., Wang X., RA Chiquet J., Belcram H., Tong C., Samans B., Correa M., Da Silva C., RA Just J., Falentin C., Koh C.S., Le Clainche I., Bernard M., Bento P., RA Noel B., Labadie K., Alberti A., Charles M., Arnaud D., Guo H., RA Daviaud C., Alamery S., Jabbari K., Zhao M., Edger P.P., Chelaifa H., RA Tack D., Lassalle G., Mestiri I., Schnel N., Le Paslier M.C., Fan G., RA Renault V., Bayer P.E., Golicz A.A., Manoli S., Lee T.H., Thi V.H., RA Chalabi S., Hu Q., Fan C., Tollenaere R., Lu Y., Battail C., Shen J., RA Sidebottom C.H., Wang X., Canaguier A., Chauveau A., Berard A., RA Deniot G., Guan M., Liu Z., Sun F., Lim Y.P., Lyons E., Town C.D., RA Bancroft I., Wang X., Meng J., Ma J., Pires J.C., King G.J., RA Brunel D., Delourme R., Renard M., Aury J.M., Adams K.L., Batley J., RA Snowdon R.J., Tost J., Edwards D., Zhou Y., Hua W., Sharpe A.G., RA Paterson A.H., Guan C., Wincker P.; RT "Plant genetics. Early allopolyploid evolution in the post-Neolithic RT Brassica napus oilseed genome."; RL Science 345:950-953(2014). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LK031937; CDY02781.1; -; Genomic_DNA. DR RefSeq; XP_013684064.1; XM_013828610.1. DR EnsemblPlants; CDY02781; CDY02781; GSBRNA2T00114953001. DR GeneID; 106388519; -. DR Gramene; CDY02781; CDY02781; GSBRNA2T00114953001. DR KEGG; bna:106388519; -. DR KO; K03665; -. DR OMA; VILEIFH; -. DR Proteomes; UP000028999; Unassembled WGS sequence. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000028999}; KW Reference proteome {ECO:0000313|Proteomes:UP000028999}. FT DOMAIN 311 477 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 545 AA; 61207 MW; 88FB8656B25C1710 CRC64; MSSFLFPSSS PIPKSHWRAN SIPKPNRPIT LSLLHGNSYS WRLSCKLSLD YFEESVEEDE IPQFLDFSAE GEEPDLEKET VSAPTMTLMQ RKKKKGDEES LEDRFKLRNG KEVFEEKAYL VGVERKGDGE CLFDIEESLE ELEQLADTAG LMVVGSTYQK LASPNPRTYI GSGKVSEIKS AINALDVETV IFDDELSPGQ LRNLEKAFGG DVRVCDRTAL ILDIFNQRAA THEAALQVAL AQMEYQLPRL TRMWTHLERQ SGGQVKGMGE KQIEVDKRIL RTQIGVLKKE LESVRKHRKQ YRTRRVAIPV PVVSLVGYTN AGKSTLLNQL TGANVLAENR LFATLDPTTR RVQMHNGKEF LLTDTVGFIQ KLPTTLVAAF RATLEEISES SLLVHVVDIS HPLANQQIEA VEKVMSELDV SSIPKLVVWN KVDRVDDPQK VKLEAEEHGD VICISALTGE GLDKFCNAVH EKLKDSMVWV EALLPFDKGD LLSTIHKVGM VKETEYTENG TLIRAHVPLR FAQLLKPMRH LVKEASYAKK GEIES // ID A0A078EXQ6_BRANA Unreviewed; 432 AA. AC A0A078EXQ6; DT 29-OCT-2014, integrated into UniProtKB/TrEMBL. DT 29-OCT-2014, sequence version 1. DT 07-JUN-2017, entry version 13. DE SubName: Full=BnaC08g21330D protein {ECO:0000313|EMBL:CDY05956.1}; GN Name=BnaC08g21330D {ECO:0000313|EMBL:CDY05956.1}; GN ORFNames=GSBRNA2T00121784001 {ECO:0000313|EMBL:CDY05956.1}; OS Brassica napus (Rape). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae; OC Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Brassiceae; OC Brassica. OX NCBI_TaxID=3708 {ECO:0000313|EMBL:CDY05956.1, ECO:0000313|Proteomes:UP000028999}; RN [1] {ECO:0000313|EMBL:CDY05956.1, ECO:0000313|Proteomes:UP000028999} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Darmor-bzh {ECO:0000313|Proteomes:UP000028999}; RX PubMed=25146293; DOI=10.1126/science.1253435; RA Chalhoub B., Denoeud F., Liu S., Parkin I.A., Tang H., Wang X., RA Chiquet J., Belcram H., Tong C., Samans B., Correa M., Da Silva C., RA Just J., Falentin C., Koh C.S., Le Clainche I., Bernard M., Bento P., RA Noel B., Labadie K., Alberti A., Charles M., Arnaud D., Guo H., RA Daviaud C., Alamery S., Jabbari K., Zhao M., Edger P.P., Chelaifa H., RA Tack D., Lassalle G., Mestiri I., Schnel N., Le Paslier M.C., Fan G., RA Renault V., Bayer P.E., Golicz A.A., Manoli S., Lee T.H., Thi V.H., RA Chalabi S., Hu Q., Fan C., Tollenaere R., Lu Y., Battail C., Shen J., RA Sidebottom C.H., Wang X., Canaguier A., Chauveau A., Berard A., RA Deniot G., Guan M., Liu Z., Sun F., Lim Y.P., Lyons E., Town C.D., RA Bancroft I., Wang X., Meng J., Ma J., Pires J.C., King G.J., RA Brunel D., Delourme R., Renard M., Aury J.M., Adams K.L., Batley J., RA Snowdon R.J., Tost J., Edwards D., Zhou Y., Hua W., Sharpe A.G., RA Paterson A.H., Guan C., Wincker P.; RT "Plant genetics. Early allopolyploid evolution in the post-Neolithic RT Brassica napus oilseed genome."; RL Science 345:950-953(2014). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LK031966; CDY05956.1; -; Genomic_DNA. DR EnsemblPlants; CDY05956; CDY05956; GSBRNA2T00121784001. DR Gramene; CDY05956; CDY05956; GSBRNA2T00121784001. DR OMA; CNEDEVP; -. DR Proteomes; UP000028999; Unassembled WGS sequence. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR CDD; cd01878; HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 2. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 2. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000028999}; KW Reference proteome {ECO:0000313|Proteomes:UP000028999}. FT DOMAIN 155 399 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 432 AA; 48478 MW; C063D7FAA4074FDA CRC64; MLAQEEVDAV FINAILSAIQ QRNLERIWGK PVLDRVGLII EIFNAHAHTK EAKLQAELAA LMYKKSRLVR VRGTDGRQTF GQFGEAEVVS ARGRAASKGT GFVGGAGETE LQLQRRRIAD RRLRLLSQIK EAQRTRLLQR AARKRQSGLE GKNLATIAVV GYTNAGKSTL TSALTRTALY CNERLFATLD PTLKNAILPS GRKVLFSDTV GFISDLPIQL VEAFQSTLEE VVEADLLLHV VDSTAPNIEE HRSTVFHVLN QIGVPEEKLK NMIEVWNKID YEEEEEEEEE DMHYLDDAKG EEEEVEAELS EDSIAEETSE ASSEATVDED QIQNQEDDSD EWLLSEDENV SDSEIWKVPE EAKVDAAQKS GPDVRVSALT GVGLKELMYL IDEKLSGEDE KRKSETIVER NDFQSRKWRP SFKDDEEFAA GQ // ID A0A078F491_BRANA Unreviewed; 581 AA. AC A0A078F491; DT 29-OCT-2014, integrated into UniProtKB/TrEMBL. DT 29-OCT-2014, sequence version 1. DT 07-JUN-2017, entry version 12. DE SubName: Full=BnaA06g15600D protein {ECO:0000313|EMBL:CDY08166.1}; GN Name=BnaA06g15600D {ECO:0000313|EMBL:CDY08166.1}; GN ORFNames=GSBRNA2T00125462001 {ECO:0000313|EMBL:CDY08166.1}; OS Brassica napus (Rape). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae; OC Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Brassiceae; OC Brassica. OX NCBI_TaxID=3708 {ECO:0000313|EMBL:CDY08166.1, ECO:0000313|Proteomes:UP000028999}; RN [1] {ECO:0000313|EMBL:CDY08166.1, ECO:0000313|Proteomes:UP000028999} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Darmor-bzh {ECO:0000313|Proteomes:UP000028999}; RX PubMed=25146293; DOI=10.1126/science.1253435; RA Chalhoub B., Denoeud F., Liu S., Parkin I.A., Tang H., Wang X., RA Chiquet J., Belcram H., Tong C., Samans B., Correa M., Da Silva C., RA Just J., Falentin C., Koh C.S., Le Clainche I., Bernard M., Bento P., RA Noel B., Labadie K., Alberti A., Charles M., Arnaud D., Guo H., RA Daviaud C., Alamery S., Jabbari K., Zhao M., Edger P.P., Chelaifa H., RA Tack D., Lassalle G., Mestiri I., Schnel N., Le Paslier M.C., Fan G., RA Renault V., Bayer P.E., Golicz A.A., Manoli S., Lee T.H., Thi V.H., RA Chalabi S., Hu Q., Fan C., Tollenaere R., Lu Y., Battail C., Shen J., RA Sidebottom C.H., Wang X., Canaguier A., Chauveau A., Berard A., RA Deniot G., Guan M., Liu Z., Sun F., Lim Y.P., Lyons E., Town C.D., RA Bancroft I., Wang X., Meng J., Ma J., Pires J.C., King G.J., RA Brunel D., Delourme R., Renard M., Aury J.M., Adams K.L., Batley J., RA Snowdon R.J., Tost J., Edwards D., Zhou Y., Hua W., Sharpe A.G., RA Paterson A.H., Guan C., Wincker P.; RT "Plant genetics. Early allopolyploid evolution in the post-Neolithic RT Brassica napus oilseed genome."; RL Science 345:950-953(2014). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LK031983; CDY08166.1; -; Genomic_DNA. DR EnsemblPlants; CDY08166; CDY08166; GSBRNA2T00125462001. DR Gramene; CDY08166; CDY08166; GSBRNA2T00125462001. DR OMA; NGPEAIS; -. DR Proteomes; UP000028999; Unassembled WGS sequence. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR CDD; cd01878; HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 2. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000028999}; KW Reference proteome {ECO:0000313|Proteomes:UP000028999}. FT DOMAIN 297 548 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 581 AA; 65030 MW; 177F655F407D5B5D CRC64; MLRTLSLARD HLRSKAQISS SPFSSPSTIR ALSSPFSSKR HAPKATEEEA PAALKESVLL YPKDPSSTPK LFLVQPRLTP PKFLQAKLNE ALCLANSLEE QRYGYFESDF FDKELPSHVV VQNPIARSSK PRVDTYFGRG TLNISIEEVD AVFINAILSA IQQRNLERIW GKPVLDRVGL IIEIFNAHAH TKEAKLQAEL AALMYKKSRL VRVRGTDGRQ TFGQFGEAEV VSARGRAASK GTGFVGGAGE TELQLQRRRI ADRRLRLLSQ IKEAQRTRLL QRAARKRQSG LAGKSLATIA VVGYTNAGKS TLTSALTRTA LYCNERLFAT LDPTLKNAIL PSGILILSLR RKVLFSDTVG FISDLPIQLV EAFQSTLEEV VEADLLLHVV DSTAPNIEEH RSTVFHVLNQ IGVPEEKLKN MIEVWNKIDY EEEEEEEEED MHYLDDAKGE EEEVEAELSE DSIAEETSEA SSEATVDEDQ IQNQEDDSDE WLLSEDENVS DSEIWKVPEE AKVDAAQKSG PDVRVSALTG VGLKELMYLI DEKLSGEDEK RKSETIVERN DFQSRKWRPS FKDDEEFAAG Q // ID A0A078H4G2_BRANA Unreviewed; 545 AA. AC A0A078H4G2; DT 29-OCT-2014, integrated into UniProtKB/TrEMBL. DT 29-OCT-2014, sequence version 1. DT 07-JUN-2017, entry version 12. DE SubName: Full=BnaA02g07980D protein {ECO:0000313|EMBL:CDY32736.1}; GN Name=BnaA02g07980D {ECO:0000313|EMBL:CDY32736.1}; GN ORFNames=GSBRNA2T00052789001 {ECO:0000313|EMBL:CDY32736.1}; OS Brassica napus (Rape). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae; OC Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Brassiceae; OC Brassica. OX NCBI_TaxID=3708 {ECO:0000313|EMBL:CDY32736.1, ECO:0000313|Proteomes:UP000028999}; RN [1] {ECO:0000313|EMBL:CDY32736.1, ECO:0000313|Proteomes:UP000028999} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Darmor-bzh {ECO:0000313|Proteomes:UP000028999}; RX PubMed=25146293; DOI=10.1126/science.1253435; RA Chalhoub B., Denoeud F., Liu S., Parkin I.A., Tang H., Wang X., RA Chiquet J., Belcram H., Tong C., Samans B., Correa M., Da Silva C., RA Just J., Falentin C., Koh C.S., Le Clainche I., Bernard M., Bento P., RA Noel B., Labadie K., Alberti A., Charles M., Arnaud D., Guo H., RA Daviaud C., Alamery S., Jabbari K., Zhao M., Edger P.P., Chelaifa H., RA Tack D., Lassalle G., Mestiri I., Schnel N., Le Paslier M.C., Fan G., RA Renault V., Bayer P.E., Golicz A.A., Manoli S., Lee T.H., Thi V.H., RA Chalabi S., Hu Q., Fan C., Tollenaere R., Lu Y., Battail C., Shen J., RA Sidebottom C.H., Wang X., Canaguier A., Chauveau A., Berard A., RA Deniot G., Guan M., Liu Z., Sun F., Lim Y.P., Lyons E., Town C.D., RA Bancroft I., Wang X., Meng J., Ma J., Pires J.C., King G.J., RA Brunel D., Delourme R., Renard M., Aury J.M., Adams K.L., Batley J., RA Snowdon R.J., Tost J., Edwards D., Zhou Y., Hua W., Sharpe A.G., RA Paterson A.H., Guan C., Wincker P.; RT "Plant genetics. Early allopolyploid evolution in the post-Neolithic RT Brassica napus oilseed genome."; RL Science 345:950-953(2014). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LK032298; CDY32736.1; -; Genomic_DNA. DR EnsemblPlants; CDY32736; CDY32736; GSBRNA2T00052789001. DR Gramene; CDY32736; CDY32736; GSBRNA2T00052789001. DR OMA; VYAKDQL; -. DR Proteomes; UP000028999; Unassembled WGS sequence. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000028999}; KW Reference proteome {ECO:0000313|Proteomes:UP000028999}. FT DOMAIN 311 477 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 545 AA; 61116 MW; 7D519D9EEE892C80 CRC64; MSSFLFPSSS PIPKSHWRAN SIPRPNRSIT LSPLHGNSYS WRLSCKLSLD FEESVEEDAI PQFLDFSAEE EEESSLEKET VSAPTTTLMQ RKKKKGDEES LEDRFKLRNG KEVFEEKAYL VGVERKGDGE CLFDIEESLE ELEQLADTAG LMVVGSTYQK LASPNPRTYI GSGKVSEIKS AINALDVETV IFDDELSPGQ LRNLEKAFGG DVRVCDRTAL ILDIFNQRAA THEAALQVAL AQMEYQLPRL TRMWTHLERQ SGGQVKGMGE KQIEVDKRIL RTQIGVLKKE LESVRKHRKQ YRSRRVAIPV PVVSLVGYTN AGKSTLLNQL TGANVLAENR LFATLDPTTR RVQMHNGKEF LLTDTVGFIQ KLPTTLVAAF RATLEEISES SLLVHVVDIS HPLANQQIEA VEKVMSELDV SSIPKLVVWN KVDRVDDPHK IKLEAEEHGD VICISALTGE GLDKFCNAVH EKLKDSMVWV EALLPFDKGD LLSTIHKVGM VKETEYTENG TLVRAHVPLR FAQLLKPMRH LVKEASYAKK GEIES // ID A0A078KI50_9FIRM Unreviewed; 418 AA. AC A0A078KI50; DT 29-OCT-2014, integrated into UniProtKB/TrEMBL. DT 29-OCT-2014, sequence version 1. DT 07-JUN-2017, entry version 17. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:CDZ23226.1}; GN ORFNames=CCDG5_0076 {ECO:0000313|EMBL:CDZ23226.1}; OS [Clostridium] cellulosi. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Ruminococcaceae; OC Ruminiclostridium. OX NCBI_TaxID=29343 {ECO:0000313|EMBL:CDZ23226.1, ECO:0000313|Proteomes:UP000032431}; RN [1] {ECO:0000313|EMBL:CDZ23226.1} RP NUCLEOTIDE SEQUENCE. RA Wibberg Daniel; RL Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LM995447; CDZ23226.1; -; Genomic_DNA. DR EnsemblBacteria; CDZ23226; CDZ23226; CCDG5_0076. DR KEGG; ccel:CCDG5_0076; -. DR PATRIC; fig|29343.3.peg.83; -. DR KO; K03665; -. DR Proteomes; UP000032431; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000032431}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000032431}. FT DOMAIN 193 361 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 152 186 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 418 AA; 47213 MW; 413C4CD2773DD025 CRC64; MQRAVLVGAN LGDPGFEKSM EELEGLAQAC DIEPVDTVVQ KLETLNAGYY IGMGKVKEIK ILVDMYGADT VIFNDELSPS QIRNLEEALG CTIMDRTGLI LEIFARRAKT REAKLQVETA NLQYMLPRLV GLRKSLEQQA GGVGTTNRGA GEKLLELNRR QIQNRISRLN AELDEISAQR NTQRKQRKKT GIPIVSLVGY TNAGKSTIMN ALLEETNSEQ DKKVFEKDML FATLETSVRR ITLPDKKAFL LTDTVGFIDK LPHNLVKAFR STLEEACEAD LIIHVVDCSD KDYRRQIEVT ERTLKEIGVW GIPIIYALNK ADKLDIKPAS ERPDSVYISA KYRTGLDTLL GLIKKRLFGN YVRCNMLIPY KDGDVVSYLN QNANIIRTEY DGDGTRLSLE LRESDFNRFK KFVVSRHK // ID A0A078KT71_9GAMM Unreviewed; 413 AA. AC A0A078KT71; DT 29-OCT-2014, integrated into UniProtKB/TrEMBL. DT 29-OCT-2014, sequence version 1. DT 07-JUN-2017, entry version 25. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:CDZ76157.1}; GN ORFNames=BN59_00423 {ECO:0000313|EMBL:CDZ76157.1}; OS Legionella massiliensis. OC Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales; OC Legionellaceae; Legionella. OX NCBI_TaxID=1034943 {ECO:0000313|EMBL:CDZ76157.1, ECO:0000313|Proteomes:UP000044071}; RN [1] {ECO:0000313|EMBL:CDZ76157.1, ECO:0000313|Proteomes:UP000044071} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Urmite Genomes Urmite Genomes; RL Submitted (JUN-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CCSB01000001; CDZ76157.1; -; Genomic_DNA. DR RefSeq; WP_043872752.1; NZ_CCVW01000001.1. DR EnsemblBacteria; CDZ76157; CDZ76157; BN59_00423. DR Proteomes; UP000044071; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000044071}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000044071}. FT DOMAIN 198 363 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 413 AA; 46282 MW; 745F549E8817FA57 CRC64; MFERPQGGER AILVQLALPG VDAEKALSEF KELALSAQAE IMACVVGARA TPEAKYYVGL GKAEEIQELV AAHNAELVLV NHELSPSQER NLERLFQCRV VDRSGLILDI FAQRARTFEG KLQVELAQLQ HISTRLIRGW THLERQKGGI GLRGPGETQL ETDRRLLRER IKSINKRLEK VRRSRDQNRR ARQKAALPTV SLVGYTNAGK STLFNALTGE QIYVADQLFA TLDPTMRKLD LPGAGSVILT DTVGFIRDLP HQLVEAFRAT LEETEEADLL LHVIDIADPF WRDTVIAVEQ VLSEIGVTEI PIIHVFNKID LQKDWLPKID WQEDSCKVWL SAKTGEGLDL LCEVIATQLE GAIIEEEIYV APSDAKLRAK LYQLAAIVSE RASDEGGWYL KIKLTQAQKA HLF // ID A0A078L9H5_9CHLA Unreviewed; 438 AA. AC A0A078L9H5; DT 29-OCT-2014, integrated into UniProtKB/TrEMBL. DT 29-OCT-2014, sequence version 1. DT 12-APR-2017, entry version 19. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:CDZ80523.1}; GN ORFNames=BN1013_01037 {ECO:0000313|EMBL:CDZ80523.1}; OS Candidatus Rubidus massiliensis. OC Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae; Candidatus Rubidus. OX NCBI_TaxID=1444712 {ECO:0000313|EMBL:CDZ80523.1, ECO:0000313|Proteomes:UP000039860}; RN [1] {ECO:0000313|EMBL:CDZ80523.1, ECO:0000313|Proteomes:UP000039860} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Urmite Genomes Urmite Genomes; RL Submitted (JUN-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CCSC01000001; CDZ80523.1; -; Genomic_DNA. DR EnsemblBacteria; CDZ80523; CDZ80523; BN1013_01037. DR Proteomes; UP000039860; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000039860}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000039860}. FT DOMAIN 218 384 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 177 211 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 438 AA; 49935 MW; 24EAAF9888A8F3B1 CRC64; MSENITNKNK TYETSPQEMK KAYLVSVYKG NQNADLAKEH LEELELLTKT YGVEIAGKQI CLVRRYDAAT FITEGKLEEV LNAAKNCNAN LLIFDDEIAP SQQRNLENLF KGPVMDRTGV ILEVFAQRAQ TKEAQLQIDL AKLKYQAPRL KRLWSHLSRQ HGSGGAGGGA YLKGEGEKQI EIDRRILKKE IDTLNKEIKE VRENREMQRS SRIRSELPIF AIIGYTNAGK STLLHALTDA KVLIEDKLFA TLDTTTRKFT LVNNQDILLI DTVGFIRKLP HLLVAAFKST LEEALHADIL LHVVDVSHPM AEEQAQTSYE VLKELNAENK PVITVLNKID QCQNPNIIQK MKVLYPKTVC ISAKEKIGFN ELQQIMIEEL SRRRKIVRFR IPQKDYAKVS ELMRVGNIIH QDYEENDVIL RVDLPTAAIG RLQQYIEE // ID A0A078LTG4_9PSED Unreviewed; 433 AA. AC A0A078LTG4; DT 29-OCT-2014, integrated into UniProtKB/TrEMBL. DT 29-OCT-2014, sequence version 1. DT 30-AUG-2017, entry version 22. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:CDZ94434.1}; GN ORFNames=BN1079_01755 {ECO:0000313|EMBL:CDZ94434.1}; OS Pseudomonas saudiphocaensis. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=1499686 {ECO:0000313|EMBL:CDZ94434.1, ECO:0000313|Proteomes:UP000053902}; RN [1] {ECO:0000313|EMBL:CDZ94434.1, ECO:0000313|Proteomes:UP000053902} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=20_BN {ECO:0000313|EMBL:CDZ94434.1, RC ECO:0000313|Proteomes:UP000053902}; RA Urmite Genomes Urmite Genomes; RL Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CCSF01000001; CDZ94434.1; -; Genomic_DNA. DR RefSeq; WP_037023689.1; NZ_CCSF01000001.1. DR EnsemblBacteria; CDZ94434; CDZ94434; BN1079_01755. DR Proteomes; UP000053902; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000053902}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000053902}. FT DOMAIN 199 366 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 165 192 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 433 AA; 48855 MW; E144084F8E21EC84 CRC64; MFFERPDGGE RAILVHLDGQ DPAAREDPQE FQELVRSAGA DTVGFVSVAR HQPSAKFLIG SGKVEELRDL VREGEVELVI FNHTLTPSQE RNLERALECR VLDRTGLILD IFAQRARTHE GKLQVELAQL EHMSTRLVRG WTHLERQKGG IGLRGPGETQ LETDRRLLRV RIRQIKQRLE KVRGQREQAR RGRRRADIQL VSLVGYTNAG KSTLFNALTQ SSVYAADQLF ATLDPTLRRL ELDDLGPVVL ADTVGFIRHL PHKLVESFRA TLEESSNADL LLHVIDAHEP ERDEQIEQVL AVLTEIGAHE LPILEVYNKV DLLEGIEPQI QRDADGVPQR VWISAQKGLG LDLLQQAIAE LLGNDLFVGR MRLPQSLGRL RAQLFGLGAV QSESHDEEGG SLLDVRVQRV ELHRLISREG FDTEQFLQQH TLQ // ID A0A078M342_9STAP Unreviewed; 409 AA. AC A0A078M342; DT 29-OCT-2014, integrated into UniProtKB/TrEMBL. DT 29-OCT-2014, sequence version 1. DT 07-JUN-2017, entry version 19. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:CDZ99632.1}; GN ORFNames=BN1048_00573 {ECO:0000313|EMBL:CDZ99632.1}; OS Jeotgalicoccus saudimassiliensis. OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae; OC Jeotgalicoccus. OX NCBI_TaxID=1461582 {ECO:0000313|EMBL:CDZ99632.1, ECO:0000313|Proteomes:UP000044136}; RN [1] {ECO:0000313|EMBL:CDZ99632.1, ECO:0000313|Proteomes:UP000044136} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=13MG44_air {ECO:0000313|EMBL:CDZ99632.1, RC ECO:0000313|Proteomes:UP000044136}; RA Urmite Genomes Urmite Genomes; RL Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CCSE01000001; CDZ99632.1; -; Genomic_DNA. DR RefSeq; WP_035808229.1; NZ_CCSE01000001.1. DR EnsemblBacteria; CDZ99632; CDZ99632; BN1048_00573. DR Proteomes; UP000044136; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000044136}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000044136}. FT DOMAIN 193 313 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 409 AA; 46416 MW; 48645063764C7CE8 CRC64; MEMTHTGIIL ATNTVQNKDV ESEARELKEL SESIGIEIIG THIQNRTMID RKSYVGSGFL EEVKMQYEDI DYAIVNDEIL ASQNRKIENI LDTSVIDRTQ VILDIFSLRA QSKAGKLQVE LAQLEYLVPR LKGQGINLSR LGAGIGTRGP GETKLETDRR HINSRISDIK KQLAVVEEHR LRYRDKRRSN QVTKVSLIGY TNAGKSTLFN KLTNAETMQE DKLFATLDPL TREMVLPSGF QCIISDTVGF IQKLPTTLIE SFKSTLEEAA DSDFIIHVID NNAPDIVSQY DTVLDLIDSL DMKDIPQLIL FNKTDLNDKK RLLPMKPHKF VNMNMPAQDI LMDIENFMTK TFDAYNTSIP LARQDKLYRL KRQTIVKDVE LDEASVNVSG YEPAGNFVER IVKKDDDSE // ID A0A080K511_9NEIS Unreviewed; 392 AA. AC A0A080K511; DT 29-OCT-2014, integrated into UniProtKB/TrEMBL. DT 29-OCT-2014, sequence version 1. DT 07-JUN-2017, entry version 19. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=SASC598P14_014160 {ECO:0000313|EMBL:KES13944.1}; OS Snodgrassella alvi SCGC AB-598-P14. OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Snodgrassella. OX NCBI_TaxID=1443104 {ECO:0000313|EMBL:KES13944.1, ECO:0000313|Proteomes:UP000028206}; RN [1] {ECO:0000313|Proteomes:UP000028206} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=25210772; DOI=10.1371/journal.pgen.1004596; RA Engel P., Stepanauskas R., Moran N.; RT "Hidden diversity in honey bee gut symbionts detected by single-cell RT genomics."; RL PLoS Genet. 10:e1004596-e1004596(2014). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KES13944.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JACG01000001; KES13944.1; -; Genomic_DNA. DR EnsemblBacteria; KES13944; KES13944; SASC598P14_014160. DR PATRIC; fig|1443104.3.peg.11; -. DR Proteomes; UP000028206; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000028206}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000028206}. FT DOMAIN 214 383 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 180 207 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 392 AA; 44175 MW; 9747752DA1D8A635 CRC64; MSRFDKTNLS EQQPERVLLV GVLLDKDFPV AAGRRTVLFE SALAEAEELV RATGADLMEV VPCKRQQPDS ALFVGKGKAE ELAQKVAETG IDLVVFNHAL TPTQERNLER LLQCRVLDRV GLILAIFARR AQSQEGRLQV ELAQLVHLSS RLVRGYGHLQ SQRGGIGLRG PGETRLETDR RLIRQKITRL RQQLQQVRRQ RATQRKSRYQ GTLPAFALVG YTNVGKSSLF NRLTKAQVMA EDQLFATLDN TVRRLYLNDQ TSVLLSDTVG FIRDLPHGLV AAFAATLEET SLADVLLHVV DITHPEFERQ IDAVNTVLQE IDAENIPQLI IYNKIDKLPA EQRMQGIVRD IHGRPQAVYI SVQDGRGLDD LRTAMIEMAG MKYVQHNKQD EY // ID A0A080LVT9_9PROT Unreviewed; 402 AA. AC A0A080LVT9; DT 29-OCT-2014, integrated into UniProtKB/TrEMBL. DT 29-OCT-2014, sequence version 1. DT 10-MAY-2017, entry version 17. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:KFB72812.1}; GN ORFNames=AW09_001966 {ECO:0000313|EMBL:KFB72812.1}; OS Candidatus Accumulibacter sp. BA-91. OC Bacteria; Proteobacteria; Betaproteobacteria; OC Candidatus Accumulibacter. OX NCBI_TaxID=1454002 {ECO:0000313|EMBL:KFB72812.1, ECO:0000313|Proteomes:UP000020077}; RN [1] {ECO:0000313|EMBL:KFB72812.1, ECO:0000313|Proteomes:UP000020077} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BA-91 {ECO:0000313|Proteomes:UP000020077}; RA Skennerton C.T., Barr J.J., Slater F.R., Bond P.L., Tyson G.W.; RT "Expanding our view of genomic diversity in Candidatus Accumulibacter RT clades."; RL Submitted (FEB-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KFB72812.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JDVG02000333; KFB72812.1; -; Genomic_DNA. DR Proteomes; UP000020077; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000020077}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000020077}. FT DOMAIN 198 364 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 164 191 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 402 AA; 43903 MW; 6AE42DBA8EE9923D CRC64; MVERAAAKER AVIVQLDFGR EDLAEQLAEV RLLTRSAGAA VCAIVQGSRH SPDAATYAGK GKVEEVAAEI NVHQADLVIF NHELSAGQER NLERRLQCRV IDRTSLILDI FAQRAQSSEG KLQVELAQLE HLSTRLVRGW THLERQKGGI GLRGPGETQL ETDRRLLGIR VKLLKERLAR LERQRGVQRK ARGRGELLNV SLVGYTNAGK STLFNALTHA GVFAADQLFA TLDTTTRKLW LGEAGHIVLS DTVGFIRDLP HSLVAAFHAT LEATAEADLL LHVVDSASPA RDDQIADVNK VLAEIGAADV PQLTVQNKLD LTGLPPAVER DEYGRISRVR LSAVSGDGLP LLREALSELA LAKTRDLQDL RDLQELRDSR ERAAGAATVQ NVDRILDSDG SP // ID A0A080M7H7_9PROT Unreviewed; 395 AA. AC A0A080M7H7; DT 29-OCT-2014, integrated into UniProtKB/TrEMBL. DT 29-OCT-2014, sequence version 1. DT 12-APR-2017, entry version 16. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:KFB76440.1}; GN ORFNames=AW06_002478 {ECO:0000313|EMBL:KFB76440.1}; OS Candidatus Accumulibacter sp. SK-02. OC Bacteria; Proteobacteria; Betaproteobacteria; OC Candidatus Accumulibacter. OX NCBI_TaxID=1453999 {ECO:0000313|EMBL:KFB76440.1, ECO:0000313|Proteomes:UP000021315}; RN [1] {ECO:0000313|EMBL:KFB76440.1, ECO:0000313|Proteomes:UP000021315} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SK-02 {ECO:0000313|Proteomes:UP000021315}; RA Skennerton C.T., Barr J.J., Slater F.R., Bond P.L., Tyson G.W.; RT "Expanding our view of genomic diversity in Candidatus Accumulibacter RT clades."; RL Submitted (FEB-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KFB76440.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JDST02000055; KFB76440.1; -; Genomic_DNA. DR Proteomes; UP000021315; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000021315}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000021315}. FT DOMAIN 198 364 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 164 191 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 395 AA; 43034 MW; CBE9EFF2C949D469 CRC64; MVERAIAEER AVIVQLDFGR EDLAEQLAEV RLLTRSAGAV VCAVVQGRRH SPDAATYAGK GKVEEVAAEV AAHAADLVIF NHELSAGQER NLERTLQCRV IDRTSLILDI FAQRAQSSEG KLQVELAQLE HLATRLVRGW THLERQKGGI GLRGPGETQL ETDRRLLGIR VKLLRERLAR LERQRGVQRK ARGRGELLNV SLVGYTNAGK STLFNALTHA GVFAADQLFA TLDTTTRKLW LAEAGHIVLS DTVGFIRDLP HSLVAAFHAT LEATAEADLL LHVVDSASPA RDDQIADVNK VLAEIGAADV PQLTVQNKLD LTGLPPAVER DEYGRIWRVR LSAVSGDGLP LLREALAELA LAKTRDLQEL RDSRARTAGA AAQDVDRILD SDGSS // ID A0A080N658_9BIFI Unreviewed; 496 AA. AC A0A080N658; DT 29-OCT-2014, integrated into UniProtKB/TrEMBL. DT 29-OCT-2014, sequence version 1. DT 12-APR-2017, entry version 18. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=BBOMB_0630 {ECO:0000313|EMBL:KFF31289.1}; OS Bifidobacterium bombi DSM 19703. OC Bacteria; Actinobacteria; Bifidobacteriales; Bifidobacteriaceae; OC Bifidobacterium. OX NCBI_TaxID=1341695 {ECO:0000313|EMBL:KFF31289.1, ECO:0000313|Proteomes:UP000028730}; RN [1] {ECO:0000313|EMBL:KFF31289.1, ECO:0000313|Proteomes:UP000028730} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 19703 {ECO:0000313|EMBL:KFF31289.1, RC ECO:0000313|Proteomes:UP000028730}; RX PubMed=25085493; DOI=10.1128/AEM.02308-14; RA Milani C., Lugli G.A., Duranti S., Turroni F., Bottacini F., RA Mangifesta M., Sanchez B., Viappiani A., Mancabelli L., Taminiau B., RA Delcenserie V., Barrangou R., Margolles A., van Sinderen D., RA Ventura M.; RT "Genomic encyclopedia of type strains of the genus Bifidobacterium."; RL Appl. Environ. Microbiol. 80:6290-6302(2014). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KFF31289.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ATLK01000001; KFF31289.1; -; Genomic_DNA. DR EnsemblBacteria; KFF31289; KFF31289; BBOMB_0630. DR Proteomes; UP000028730; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000028730}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000028730}. FT DOMAIN 276 442 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 496 AA; 54135 MW; DECC8DA4EB38AB8E CRC64; MSRDENGTTQ DDDVLASESD VLQDARTRPG SAAFAMDADD EQWQERQSRN ELRHVTGLGE LQDVSEVEYR QVRLERVVLV GVWSNRETTA GKAEESLREL AALAATAGAQ VCDGVLQHRL KPDAATYVGR GKAKEIAGIV AREEADTIIV DGDLAPSQRR ALEDATKVKV VDRTAVILDI FAQHATSREG KAQVELAQLE YMLPRLRGWG ASLSRQAGGQ AAGVNGGIGS RGPGETKIEM DRRVIRTRIS RLKRQIADMT PSREVKRGSR RRNDVPTVAV VGYTNAGKSS LTNRLTGAKE LVENALFATL DTAVRGAKAR DGRLYTYVDT VGFVRRLPTQ LVEAFKSTLE EVDQADVILH VVDASYPDPF AQIRAVDEVL ADIDGAERIP RVLAFNKADL VAPEVLERLQ SLMPEAFLVS AMTGEGLGDV RMAVESLLPQ PEVSVEVLLP YTEGSLISEV RRFGVVDDLR YLDDGVKVKA RVGSRLAAKL MNRAIG // ID A0A081BFA4_9RHIZ Unreviewed; 474 AA. AC A0A081BFA4; DT 29-OCT-2014, integrated into UniProtKB/TrEMBL. DT 29-OCT-2014, sequence version 1. DT 12-APR-2017, entry version 17. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=M2A_3221 {ECO:0000313|EMBL:GAK46722.1}; OS Tepidicaulis marinus. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Rhodobiaceae; Tepidicaulis. OX NCBI_TaxID=1333998 {ECO:0000313|EMBL:GAK46722.1, ECO:0000313|Proteomes:UP000028702}; RN [1] {ECO:0000313|EMBL:GAK46722.1, ECO:0000313|Proteomes:UP000028702} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MA2 {ECO:0000313|EMBL:GAK46722.1, RC ECO:0000313|Proteomes:UP000028702}; RA Takeuchi M., Yamagishi T., Kamagata Y., Oshima K., Hattori M., RA Katayama T., Hanada S., Tamaki H., Marumo K., Maeda H., Nedachi M., RA Iwasaki W., Suwa Y., Sakata S.; RT "Tepidicaulis marinum gen. nov., sp. nov., a novel marine bacterium RT denitrifying nitrate to nitrous oxide strictly under microaerobic RT conditions."; RL Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:GAK46722.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BBIO01000026; GAK46722.1; -; Genomic_DNA. DR EnsemblBacteria; GAK46722; GAK46722; M2A_3221. DR Proteomes; UP000028702; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000028702}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000028702}. FT DOMAIN 231 402 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 190 224 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 474 AA; 52438 MW; 9D4DD5094ABD6815 CRC64; MTDHRKLPPS QKKAAAGAPE KTRGPAEYQT GPKEPTRAFV IVPWFKAQKD ARRKPESRLE EAVGLAAAID LDVVGREIVM ITQARPATLI GTGKLEELGE LLSALQVELV VVDGTLTPGQ QRNLEKAWKV KVLDRTGLIL EIFGARAATR EGALQVELAH LTYQKSRLVR SWTHLERQRG GTGFLGGPGE TQIEADRRAI QDKINRLEKQ LDKVKRTREL HRKGRREAPY PVIALVGYTN AGKSTLFNRL TKSSVFAQDL LFATLDPTMR LVELPSGRKI VLSDTVGFIS DLPTHLVAAF RATLEEVLEA EIILHVRDIS HEETQAQRAD VLDVLKTLGI EQDGERPIIE VLNKADLMEP ERREALLNQT DRQKEVTLIS ALTGEGVDRL LANLDAFLAE QALVVEAELG PQEAEALAWL HQQGAVAAQE MGEDGTNRLV LKLDDVTLGR FRKRFADTAA RVLAGVPERQ PEEG // ID A0A081BI05_9LACO Unreviewed; 423 AA. AC A0A081BI05; DT 29-OCT-2014, integrated into UniProtKB/TrEMBL. DT 29-OCT-2014, sequence version 1. DT 07-JUN-2017, entry version 21. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=LOSG293_100380 {ECO:0000313|EMBL:GAK47673.1}; OS Lactobacillus oryzae JCM 18671. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; OC Lactobacillus. OX NCBI_TaxID=1291743 {ECO:0000313|EMBL:GAK47673.1, ECO:0000313|Proteomes:UP000028700}; RN [1] {ECO:0000313|EMBL:GAK47673.1, ECO:0000313|Proteomes:UP000028700} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SG293 {ECO:0000313|EMBL:GAK47673.1, RC ECO:0000313|Proteomes:UP000028700}; RA Tanizawa Y., Fujisawa T., Mochizuki T., Kaminuma E., Nakamura Y., RA Tohno M.; RT "Draft Genome Sequence of Lactobacillus oryzae Strain SG293T."; RL Genome Announc. 2:e00861-14(2014). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:GAK47673.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BBJM01000010; GAK47673.1; -; Genomic_DNA. DR RefSeq; WP_034527237.1; NZ_BBJM01000010.1. DR EnsemblBacteria; GAK47673; GAK47673; LOSG293_100380. DR Proteomes; UP000028700; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000028700}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000028700}. FT DOMAIN 202 370 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 423 AA; 47296 MW; A461E76A68C35F01 CRC64; MAETETIKAV AIGLNTGQRD FDYSMEELSA LAAANNIEIV ETVTQNLDRP VSGTYFGSGK VEELAQIVLD DEATMVIAND ELSPSQIRNL EKVVKEDVID RTGLILQIFA DRAQSREAKL QVQLAKLQYQ LPRLHTSASQ RLDQQTGTSS GGGFTNRGAG ESQIELNRRV VQRQINHVRH ELKEINKSEQ TKRQQRERKG LPMVALVGYT NAGKSTIMNA LVRQFGMNDD KQVFEKNMLF ATLDTSVRQL TFDDQKQLLL SDTVGFVDHL PTHLVEAFKS TLYEAANADL LIQVVDSADA NRDNMMATTM KTLSDIGVPD LPMITVYNKA DLTDRAFPSR EGDSLTMSAK DATSVDLLVD MVREKVFTNY VTAEFLIPFA NGDVVSYLND HANVLETEYV EDGTKVKVEL ERTDYDRLNQ YLI // ID A0A081BVG7_9BACT Unreviewed; 587 AA. AC A0A081BVG7; DT 29-OCT-2014, integrated into UniProtKB/TrEMBL. DT 29-OCT-2014, sequence version 1. DT 12-APR-2017, entry version 18. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=U27_03284 {ECO:0000313|EMBL:GAK56322.1}; OS Candidatus Vecturithrix granuli. OC Bacteria; Candidatus Vecturithrix. OX NCBI_TaxID=1499967 {ECO:0000313|EMBL:GAK56322.1, ECO:0000313|Proteomes:UP000030661}; RN [1] {ECO:0000313|EMBL:GAK56322.1, ECO:0000313|Proteomes:UP000030661} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Sekiguchi Y., Ohashi A., Parks D.H., Yamauchi T., Tyson G.W., RA Hugenholtz P.; RT "First genomic representation of candidate bacterial phylum KSB3 RT points to enhanced environmental sensing as a trigger of wastewater RT bulking."; RL PeerJ 3:e740-e740(2015). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; DF820464; GAK56322.1; -; Genomic_DNA. DR EnsemblBacteria; GAK56322; GAK56322; U27_03284. DR Proteomes; UP000030661; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000030661}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000030661}. FT DOMAIN 403 587 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 362 389 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 587 AA; 67499 MW; 217BBD2E6DCC46E1 CRC64; MHKPKNRVSS RNPVFTHLIR KEECAIRKVY GNLTGLKTNH IQRLERIYRR KIPANQVITQ ELANYLAELS LEINRQIGVL VARKGAIEYV IVGDQKQIHL PDIGRFRAGY LRLRGLRYLH THLADIPLNR DDFVDLAMLR FDLVGAIIVN DQGLPGKYYL AHLVPENPEE KRWEVLEAIL PGQLTLDFEE FIRALEEEFR RTQGPRDVDD QRERAVLVGV SNGKRLLAEE SFRELHELAQ SAGLFVMDTI MQHREKIDPK FLLGKGKLNE LIIRSYQVGA EVLVFDHDLT PAQARTIADM TELKIIDRTQ LILDIFAQRA HSRVGKVQVE LAQLKYQLPR LGTRDDALSR ITGGIGARGP GETKLEIDRR RARDRIRNLE KELSHLQKGR KQRRVKRQRN QIPVISIIGY TNAGKSTLLN ALTHSEVEVK DQMFATLDPT SRRLRFPRDI EVIITDTVGF LRDLPKDLVE AFRSTLEELE DADLLLHVVD LSNPDFEEHI TAVNRILEEL HLDQIPQLLV FNKEDRVEPQ LAETLCTRYN GVSIAAIHKP TLRKLVQRVQ EEILRLYPEQ EKYPQLKPAA LSVSLSV // ID A0A081CW40_9RHIZ Unreviewed; 442 AA. AC A0A081CW40; DT 29-OCT-2014, integrated into UniProtKB/TrEMBL. DT 29-OCT-2014, sequence version 1. DT 07-JUN-2017, entry version 21. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:GAK70886.1}; GN ORFNames=RRU01S_14_01070 {ECO:0000313|EMBL:GAK70886.1}; OS Rhizobium rubi NBRC 13261. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Rhizobiaceae; Rhizobium/Agrobacterium group; Agrobacterium. OX NCBI_TaxID=1220582 {ECO:0000313|EMBL:GAK70886.1, ECO:0000313|Proteomes:UP000028701}; RN [1] {ECO:0000313|EMBL:GAK70886.1, ECO:0000313|Proteomes:UP000028701} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NBRC 13261 {ECO:0000313|EMBL:GAK70886.1, RC ECO:0000313|Proteomes:UP000028701}; RA Katano-Makiyama Y., Hosoyama A., Hashimoto M., Hosoyama Y., RA Noguchi M., Tsuchikane K., Uohara A., Ohji S., Ichikawa N., Kimura A., RA Yamazoe A., Fujita N.; RT "Whole genome shotgun sequence of Rhizobium rubi NBRC 13261."; RL Submitted (AUG-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:GAK70886.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BBJU01000014; GAK70886.1; -; Genomic_DNA. DR RefSeq; WP_045230446.1; NZ_BBJU01000014.1. DR Proteomes; UP000028701; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000028701}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}. FT DOMAIN 204 376 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 163 197 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 442 AA; 48843 MW; 925DEB4EFFEDF58D CRC64; MRAVVIIPVL KQGRTPKEAS ATTPPRSMEA KLEEAKGLAL AIDLHVSQGL IVPVNQPRPA TLFGSGKIEE IGQLLDETDS GLVIIDHPLT PVQQRNLEKE WNAKVIDRTG LILEIFGRRA STKEGTLQVD LAHLNYQKGR LVRSWTHLER QRGGAGFMGG PGETQIEADR RLLQDRIVKL ERELEQVVRT RQLHRAKRRK VPHPIVALVG YTNAGKSTLF NRVTGAGVLA EDMLFATLDP TLRRMKLPHG RTVIMSDTVG FISDLPTHLV AAFRATLEEV LEADLILHVR DMSDPDNGAQ SADVLRILSD LGIDEKVADE RIIEVWNKVD RLDTETHDAM MHKAEGRANV RAVSAITGEG VDALMDEISQ RLSGVLVESS VVLDVDQLQL LSWVYSNAIV DGRQDNEDGS VTLDVRLSDA QALELDRRLG HPNKSVPEER GA // ID A0A081EPX0_STRFR Unreviewed; 501 AA. AC A0A081EPX0; DT 29-OCT-2014, integrated into UniProtKB/TrEMBL. DT 29-OCT-2014, sequence version 1. DT 07-JUN-2017, entry version 25. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=SFRA_04210 {ECO:0000313|EMBL:KDS89458.1}; OS Streptomyces fradiae (Streptomyces roseoflavus). OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae; OC Streptomyces. OX NCBI_TaxID=1906 {ECO:0000313|EMBL:KDS89458.1, ECO:0000313|Proteomes:UP000028058}; RN [1] {ECO:0000313|Proteomes:UP000028058} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 19609 {ECO:0000313|Proteomes:UP000028058}; RA Bekker O.B., Klimina K.M., Vatlin A.A., Zakharevich N.V., RA Danilenko V.N.; RT "Genome sequence of Streptomyces fradiae ATCC 19609."; RL Submitted (MAY-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KDS89458.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JNAD01000003; KDS89458.1; -; Genomic_DNA. DR RefSeq; WP_043460811.1; NZ_MCNU01000020.1. DR EnsemblBacteria; KDS89458; KDS89458; SFRA_04210. DR PATRIC; fig|1906.11.peg.2; -. DR Proteomes; UP000028058; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 2. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000313|EMBL:KDS89458.1}; KW Complete proteome {ECO:0000313|Proteomes:UP000028058}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900, KW ECO:0000313|EMBL:KDS89458.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000028058}. FT DOMAIN 279 444 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 501 AA; 54262 MW; 23F91CF9CBA668AE CRC64; MTPSSSPSQD TERLARTSSA SLRADALMEE DVAWGDEFDE LRDGEQYDRS DRAALRRIAG LSTELEDVTE VEYRQLRLER VVLVGVWTSG TAQDAENSLA ELAALAETAG ALVLDGVIQR RDKPDPATYI GSGKAVELRD IVLETGADTV VCDGELTPGQ LIHLEDVVKV KVVDRTALIL DIFAQHAKSR EGKAQVSLAQ MQYMLPRLRG WGQSLSRQMG GGGSGSSGGG MATRGPGETK IETDRRRIRE KMAKMRREIA EMKTGRDVKR QERKRNKVPS VAIAGYTNAG KSSLLNRLTG AGVLVENALF ATLDPTVRRA ETPSGRAYTL ADTVGFVRHL PHHLVEAFRS TMEEVGDADL ILHVVDGAHP VPEEQLAAVR EVIREVGAQD VPEIVVVNKA DAADPLVLQR LLRTEKGAIA VSARTGQGIV ELLALLDEKL PRPRVGIEAL VPYTQGGLIS RAHADGEVIS EEHTGEGTLL KARVHEELAA ELAPYALAGQ R // ID A0A081G247_9GAMM Unreviewed; 432 AA. AC A0A081G247; DT 29-OCT-2014, integrated into UniProtKB/TrEMBL. DT 29-OCT-2014, sequence version 1. DT 30-AUG-2017, entry version 21. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=ADIMK_1305 {ECO:0000313|EMBL:KEA64852.1}; OS Marinobacterium sp. AK27. OC Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales; OC Marinobacterium. OX NCBI_TaxID=1232683 {ECO:0000313|EMBL:KEA64852.1, ECO:0000313|Proteomes:UP000028252}; RN [1] {ECO:0000313|EMBL:KEA64852.1, ECO:0000313|Proteomes:UP000028252} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=AK27 {ECO:0000313|EMBL:KEA64852.1, RC ECO:0000313|Proteomes:UP000028252}; RA Singh A., Pinnaka A.K.; RT "Marinobacterium kochiensis sp. nov., isolated from sediment sample RT collected from Kochi backwaters in Kerala, India."; RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KEA64852.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JMQN01000015; KEA64852.1; -; Genomic_DNA. DR RefSeq; WP_036185113.1; NZ_JMQN01000015.1. DR EnsemblBacteria; KEA64852; KEA64852; ADIMK_1305. DR PATRIC; fig|1232683.4.peg.1295; -. DR Proteomes; UP000028252; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000028252}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000028252}. FT DOMAIN 199 366 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 165 192 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 432 AA; 48710 MW; ACD4D23D8A176C8A CRC64; MFFERPESGE TAILVHIELS SDENSEDPRE LEELALSAGA DPVVFLTGSR ADPSPKFFLG KGKVEELAGL VQQYQAELVI FNHALSPAQE RNLEREIKCR VLDRTGLILD IFAQRARTHE GKLQVELAQL EHMSTRLVRG WTHLERQKGG IGLRGPGETQ LETDRRLLRA RIKAIQKRLE KVRSQREQGR RARQRAEVPT VALVGYTNAG KSTLFNYMTD ASVYAADQLF ATLDPTLRRI ELDDVGPAIL ADTVGFIRHL PHKLVESFRA TLQETVEATL LLHVIDCYDE ERQDHIDQVH AVLREIGADE VPALQVYNKI DKLPGQAPRI DRDEDGVAQR VWLSAQTGEG VALLMDAVRE RLGSDMFHDT LCLTPDQGQL RAQLYAQGAV LTEQVDEQGH ISLEVRIPMR DIRQLLSRLS IPAERYLPEQ VH // ID A0A081K778_9GAMM Unreviewed; 430 AA. AC A0A081K778; DT 29-OCT-2014, integrated into UniProtKB/TrEMBL. DT 29-OCT-2014, sequence version 1. DT 30-AUG-2017, entry version 20. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=GV64_03910 {ECO:0000313|EMBL:KEI70004.1}; OS Endozoicomonas elysicola. OC Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales; OC Hahellaceae; Endozoicomonas. OX NCBI_TaxID=305900 {ECO:0000313|EMBL:KEI70004.1, ECO:0000313|Proteomes:UP000027997}; RN [1] {ECO:0000313|EMBL:KEI70004.1, ECO:0000313|Proteomes:UP000027997} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 22380 {ECO:0000313|EMBL:KEI70004.1, RC ECO:0000313|Proteomes:UP000027997}; RA Neave M.J., Apprill A., Voolstra C.R.; RT "Whole Genome Sequences of Three Symbiotic Endozoicomonas Bacteria."; RL Submitted (JUN-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KEI70004.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JOJP01000001; KEI70004.1; -; Genomic_DNA. DR RefSeq; WP_020584270.1; NZ_JOJP01000001.1. DR EnsemblBacteria; KEI70004; KEI70004; GV64_03910. DR Proteomes; UP000027997; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000027997}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000027997}. FT DOMAIN 199 366 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 165 192 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 430 AA; 48853 MW; 9CA0B3505EA0BF82 CRC64; MFFDRHEGGE TAVLVHLELN DEREREDPQE FMELVRSAGV ESAAFITAGC KHPTPRFFVG PGKVEEIRQL VVLHDVDVVL FNHALSPSQE RNLEKELQCR VIDRTGLILD IFAQRARTFE GKLQVELAQL QHMSTRLIRG WTHLERQKGG IGLRGPGETQ LETDRRLLRV RIKSITRRLE KVRRQREQGR RSRKRAEVPQ VSLVGYTNAG KSTLFNRVTE SVVYAADQLF ATLDPTLRRI DLPDIGPVVL ADTVGFIRHL PHKLVEAFRA TLEETRQADL LLHVIDSHDP ERLENMDQVH SVLKEINADE VPQLEVYNKI DLLQGVEPKI QRNDEGRPVR VWVSAVTGDG VELLQEAIKE LLSDDMLQGQ LTLKPAQGRI RARLYRLGAI QSEAYSESGD IVLDIRLPKP DFERLSKQEG LSDSCFSTSA // ID A0A081MB71_9RHIZ Unreviewed; 446 AA. AC A0A081MB71; DT 29-OCT-2014, integrated into UniProtKB/TrEMBL. DT 29-OCT-2014, sequence version 1. DT 07-JUN-2017, entry version 21. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=GV67_13665 {ECO:0000313|EMBL:KEQ03444.1}; OS Pseudorhizobium pelagicum. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Rhizobiaceae; Rhizobium/Agrobacterium group; Pseudorhizobium. OX NCBI_TaxID=1509405 {ECO:0000313|EMBL:KEQ03444.1, ECO:0000313|Proteomes:UP000052187}; RN [1] {ECO:0000313|EMBL:KEQ03444.1, ECO:0000313|Proteomes:UP000052187} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=R1-200B4 {ECO:0000313|Proteomes:UP000052187}; RA Kimes N.E., Lopez-Perez M.; RT "Rhizobium pelagicum/R1-200B2."; RL Submitted (JUN-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KEQ03444.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JOKI01000027; KEQ03444.1; -; Genomic_DNA. DR RefSeq; WP_037168808.1; NZ_JOKJ01000028.1. DR EnsemblBacteria; KEQ03444; KEQ03444; GV67_13665. DR Proteomes; UP000052187; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000052187}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000052187}. FT DOMAIN 208 380 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 167 201 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 446 AA; 49475 MW; 66EC349D4F42E3EB CRC64; MRAIVIVPVL KQGRTARSAQ ADSATPSPQR SDEARLEEAI GLARAIDLTI VQGLIVPVAQ PKPATLMGSG KIEEIKALLD EHHAGLVIID HPLTPVQQRN LEKEWNAKVI DRTGLILEIF GRRASTKEGT LQVDLAHLNY QKGRLVRSWT HLERQRGGAG FMGGPGETQI EADRRLLQDR IVKLERELEQ VVRTRQLHRA KRRKVPHPIV ALVGYTNAGK STLFNRITGA GVLAEDMLFA TLDPTLRRMK LPHGRTVILS DTVGFISNLP THLVAAFRAT LEEVLEADLI LHVRDMSDPD NAAQSGDVLR ILTDLGIDEK EREKRIIEVW NKIDRLDPEA HDALIERAHG RDDIMAVSAV SGEGVEPLME EISRRLSGVL TEATITIPAD KLALVSWVYE NAIVDGREDL EDGAVELDVR LSDGQAVELE RKLGIGQAPQ KEDWER // ID A0A081MZE5_9GAMM Unreviewed; 429 AA. AC A0A081MZE5; DT 29-OCT-2014, integrated into UniProtKB/TrEMBL. DT 29-OCT-2014, sequence version 1. DT 30-AUG-2017, entry version 19. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=GZ77_23890 {ECO:0000313|EMBL:KEQ11568.1}; OS Endozoicomonas montiporae. OC Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales; OC Hahellaceae; Endozoicomonas. OX NCBI_TaxID=1027273 {ECO:0000313|EMBL:KEQ11568.1, ECO:0000313|Proteomes:UP000028006}; RN [1] {ECO:0000313|EMBL:KEQ11568.1, ECO:0000313|Proteomes:UP000028006} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=LMG 24815 {ECO:0000313|EMBL:KEQ11568.1, RC ECO:0000313|Proteomes:UP000028006}; RA Neave M.J., Apprill A., Voolstra C.R.; RT "Whole Genome Sequences of Three Symbiotic Endozoicomonas Bacteria."; RL Submitted (JUN-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KEQ11568.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JOKG01000006; KEQ11568.1; -; Genomic_DNA. DR RefSeq; WP_034879338.1; NZ_JOKG01000006.1. DR EnsemblBacteria; KEQ11568; KEQ11568; GZ77_23890. DR Proteomes; UP000028006; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000028006}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000028006}. FT DOMAIN 199 366 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 429 AA; 49023 MW; 1E2C09D431A0793C CRC64; MFFERHEGGE NAILVHLDMT DDKEREDPHE FRELARSAGI SEIDFVTVSS NKPSPRYFIG QGKVEEIQQL VKLHEADVVL FNHALSPSQE RNLEKEFECK VVDRTGLILD IFAQRARTFE GKLQVELAQL QHLSTRLVRG WTHLERQKGG IGLRGPGETQ LETDRRLLRV RIKSITKRLD KVRKQRDQGR RYRKRAEVPL VSLVGYTNAG KSTLFNALTE SDVYAQDQLF ATLDPTLRRL DLPDVGESVL ADTVGFIRHL PHKLVEAFRA TLEETAQADL LLHVIDAHDP ERLDNIKQVH DVLEEIKADE VPRLQVYNKI DLLENVEPKI QRDDQGKPVR VWVSAMQGEG LELVLQAVAE LLGEDLVQGT LRLEPAQGKV RSRLYQLGAI QSEEYAETGE LLLDIRLPRH DFDRISKQEG LQKSCLVER // ID A0A081NIG3_9GAMM Unreviewed; 429 AA. AC A0A081NIG3; DT 29-OCT-2014, integrated into UniProtKB/TrEMBL. DT 29-OCT-2014, sequence version 1. DT 30-AUG-2017, entry version 20. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=GZ78_11950 {ECO:0000313|EMBL:KEQ18236.1}; OS Endozoicomonas numazuensis. OC Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales; OC Hahellaceae; Endozoicomonas. OX NCBI_TaxID=1137799 {ECO:0000313|EMBL:KEQ18236.1, ECO:0000313|Proteomes:UP000028073}; RN [1] {ECO:0000313|EMBL:KEQ18236.1, ECO:0000313|Proteomes:UP000028073} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 25634 {ECO:0000313|EMBL:KEQ18236.1, RC ECO:0000313|Proteomes:UP000028073}; RA Neave M.J., Apprill A., Voolstra C.R.; RT "Whole Genome Sequences of Three Symbiotic Endozoicomonas Bacteria."; RL Submitted (JUN-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KEQ18236.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JOKH01000002; KEQ18236.1; -; Genomic_DNA. DR RefSeq; WP_034835379.1; NZ_JOKH01000002.1. DR EnsemblBacteria; KEQ18236; KEQ18236; GZ78_11950. DR Proteomes; UP000028073; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000028073}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000028073}. FT DOMAIN 199 366 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 429 AA; 48780 MW; 33F1361DF1C7AF25 CRC64; MFFERHEGGE SAILVHPDMS EDKEREDPQE FMELVRSAGI ETLAFITVNV RSPSPRYFVG PGKVEEIRQS VLQHKAEVVL VNHALSPSQA RNLEKELECR VIDRTGLILD IFAQRARTFE GKLQVELAQL EYMSTRLIRG WTHLERQKGG IGLRGPGETQ LETDRRLLRA RIKSITRRLQ KVRKQREQGR RSRKRAEVPQ VSLVGYTNAG KSTLFNSMTQ SDVYAQDQLF ATLDPTLRRL DLADLGPVIL ADTVGFIRHL PHKLVEAFRA TLEETRQADL LLHVIDAHDP ERLENIKEVH EVLKEIDAND VPTLQIYNKI DLLAEVVPKI QRDDNGLPER VWVSAKTGAG LELIEQAITE LLGDDMVQGR LQLQAAQGKV RARLYRLGAI QSEEYSDNGE LLLDIRMPRS DFERVAKQEG LQADCLREG // ID A0A081P0X1_9BACL Unreviewed; 444 AA. AC A0A081P0X1; DT 29-OCT-2014, integrated into UniProtKB/TrEMBL. DT 29-OCT-2014, sequence version 1. DT 07-JUN-2017, entry version 20. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=ET33_08640 {ECO:0000313|EMBL:KEQ24344.1}; OS Paenibacillus tyrfis. OC Bacteria; Firmicutes; Bacilli; Bacillales; Paenibacillaceae; OC Paenibacillus. OX NCBI_TaxID=1501230 {ECO:0000313|EMBL:KEQ24344.1, ECO:0000313|Proteomes:UP000028123}; RN [1] {ECO:0000313|EMBL:KEQ24344.1, ECO:0000313|Proteomes:UP000028123} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MSt1 {ECO:0000313|EMBL:KEQ24344.1, RC ECO:0000313|Proteomes:UP000028123}; RA Aw Y.K., Ong K.S., Gan H.M., Lee S.M.; RT "Draft genome sequence of Paenibacillus sp. MSt1."; RL Submitted (JUN-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KEQ24344.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JNVM01000016; KEQ24344.1; -; Genomic_DNA. DR RefSeq; WP_036685439.1; NZ_JNVM01000016.1. DR EnsemblBacteria; KEQ24344; KEQ24344; ET33_08640. DR Proteomes; UP000028123; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000028123}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000028123}. FT DOMAIN 209 373 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 168 202 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 444 AA; 50100 MW; FB85DA724744D323 CRC64; MKKTIHEVTG EIQDRAVLVS LVTPQLKKQE LYDPDHSLAE LISLAETAQV EVLGTLTQNK EYTDSKWFIG KGKAEELKAM LEQTGGNTAI FDQELSGAQV RNLEQFLDVK IIDRTQLILD IFAQRAKTRE GIIQVELAQL SYLLPRLYGQ GKNLSRLGGG IGTRGPGETK LETDRRHIRE RIAELKRQLQ EVVRHRSLHR ERRKKTGVFQ VALVGYTNAG KSTLLRQLTH ADVYVENQLF ATLDLTSRSL ELPGGMEIVV TDTVGFIQNL PHDLVAAFRA TLEEACEADL ILQVVDSSSE MMAAQMKVVD QVLEELGAHG KERVTVFNKI DLCSPEQKEL LTTDGPFVRI SAYREEDLSL LVELIESRFM GTSRTYRIPA DKGDLISLVY RVGEVLENEV DGEDMRFKVR VNNKEYDKIG YLLAAYDEAR PTQEEPKGET WEDV // ID A0A081PM10_9SPHI Unreviewed; 397 AA. AC A0A081PM10; DT 29-OCT-2014, integrated into UniProtKB/TrEMBL. DT 29-OCT-2014, sequence version 1. DT 07-JUN-2017, entry version 21. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=N180_16845 {ECO:0000313|EMBL:KEQ31733.1}; OS Pedobacter antarcticus 4BY. OC Bacteria; Bacteroidetes; Sphingobacteriia; Sphingobacteriales; OC Sphingobacteriaceae; Pedobacter. OX NCBI_TaxID=1358423 {ECO:0000313|EMBL:KEQ31733.1, ECO:0000313|Proteomes:UP000028007}; RN [1] {ECO:0000313|EMBL:KEQ31733.1, ECO:0000313|Proteomes:UP000028007} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=4BY {ECO:0000313|EMBL:KEQ31733.1, RC ECO:0000313|Proteomes:UP000028007}; RA Shivaji S., Ray M.K., Rao N.S., Saiserr L., Jagannadham M.V., RA Kumar G.S., Reddy G., Bhargava P.M.; RT "Sphingobacterium antarcticus sp. nov. a Psychrotrophic Bacterium from RT the Soils of Schirmacher Oasis, Antarctica."; RL Int. J. Syst. Bacteriol. 42:102-106(1992). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KEQ31733.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JNFF01000004; KEQ31733.1; -; Genomic_DNA. DR RefSeq; WP_037437737.1; NZ_JNFF01000004.1. DR EnsemblBacteria; KEQ31733; KEQ31733; N180_16845. DR Proteomes; UP000028007; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000028007}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000028007}. FT DOMAIN 204 386 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 397 AA; 45439 MW; 7EBBE4CB1E654288 CRC64; MGKAKFYDTA LKQERAVLVG VIKPGEKPEQ TKEYLDELAF LVDTAGGVVD QIFTQKMQRP DRSTFVGTGK LEEIKGYVQS EEIDMVVFDD ELSPSQLRNI ERELQVKILD RSNLILDIFA GRAQTAQAKT QVELAQLQYL LPRLTRLWTH LERQKGGIGM RGPGETQIES DRRMILEKIS LLKERLKLID KQNETQRKNR AQLIRVALVG YTNVGKSTIM NMLAKSEVFA ENKLFATLDT TVRKVVIDNL PFLLSDTVGF IRKLPHHLVE CFKSTLDEVR EADILIHVVD VSHESFEDQI NVVNETLQEL GARDKDTIMV FNKIDAYVSP EGEEDENGER KTLTLEDFKK SWMAQHNAPA LFISALHKEN LEEFKQLLYD KVIAVHTARY PYDSLLY // ID A0A081SEV6_9CHLB Unreviewed; 426 AA. AC A0A081SEV6; DT 29-OCT-2014, integrated into UniProtKB/TrEMBL. DT 29-OCT-2014, sequence version 1. DT 07-JUN-2017, entry version 17. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=HY22_11690 {ECO:0000313|EMBL:KER09459.1}; OS Chlorobium sp. GBChlB. OC Bacteria; Chlorobi; Chlorobia; Chlorobiales; Chlorobiaceae; OC Chlorobium/Pelodictyon group; Chlorobium. OX NCBI_TaxID=1519464 {ECO:0000313|EMBL:KER09459.1, ECO:0000313|Proteomes:UP000028104}; RN [1] {ECO:0000313|EMBL:KER09459.1, ECO:0000313|Proteomes:UP000028104} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Stamps B.W., Stevenson B.S.; RT "Binning of Metagenomic Samples from Little Hot Creek."; RL Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KER09459.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JPGV01000031; KER09459.1; -; Genomic_DNA. DR EnsemblBacteria; KER09459; KER09459; HY22_11690. DR PATRIC; fig|1519464.4.peg.2358; -. DR Proteomes; UP000028104; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000028104}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000028104}. FT DOMAIN 198 365 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 426 AA; 48498 MW; 946747716F37C1AF CRC64; METVVREKAV LVGVSRPPEV LRRQVQDYLN ELELLADTAG AIVLQKWIQE RAHLDPVFYL GKGKVEELSD YVKEEAVDLV IFDEDLSPVQ VRNLERVLEC KILDRTALIL QIFATHAKSY QAKLQVELAQ LEYFLPRLSG LWTHLSKQKG GIGTKGPGET QIETDRRLVW QRISTLRRKL REISQQHDTQ TKWRENVLRI ALVGYTNAGK STLMNALCPK ANVKAENQLF ATLDTTTRRM TLKQNKHALV SDTVGFIRKL PHKLVESFKS TLKEVRDADM LIHVVDASHP SYAEQIDVVE QTLRDIQASD KTVLTVFNKV DLLDAEFDFA AVKERYPTAV FVSAHRGIGV GGLLDAISRV MDKEFQPRTA RIHISHYKFI SYLHDAAEIL NKTYDGEFVE VEFRAPKKIL EHIDAKVEQL RAHSAA // ID A0A084A342_9GAMM Unreviewed; 426 AA. AC A0A084A342; DT 29-OCT-2014, integrated into UniProtKB/TrEMBL. DT 29-OCT-2014, sequence version 1. DT 30-AUG-2017, entry version 22. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:KEY59721.1}; GN ORFNames=SRDD_12980 {ECO:0000313|EMBL:KEY59721.1}; OS Serratia sp. DD3. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; OC Yersiniaceae; Serratia. OX NCBI_TaxID=1410619 {ECO:0000313|EMBL:KEY59721.1, ECO:0000313|Proteomes:UP000017810}; RN [1] {ECO:0000313|EMBL:KEY59721.1, ECO:0000313|Proteomes:UP000017810} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DD3 {ECO:0000313|EMBL:KEY59721.1, RC ECO:0000313|Proteomes:UP000017810}; RX PubMed=25212623; RA Poehlein A., Freese H.M., Daniel R., Simeonova D.D.; RT "Draft Genome Sequence of Serratia sp. Strain DD3, Isolated from the RT Guts of Daphnia magna."; RL Genome Announc. 2:e00903-14(2014). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KEY59721.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AYKS02000041; KEY59721.1; -; Genomic_DNA. DR RefSeq; WP_023489454.1; NZ_AYKS02000041.1. DR EnsemblBacteria; KEY59721; KEY59721; SRDD_12980. DR Proteomes; UP000017810; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000017810}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000017810}. FT DOMAIN 198 365 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 426 AA; 48054 MW; 60119903780B1FB1 CRC64; MFDRYETGEQ AVLVHIYFSQ DKDSEDLSEF ESLVSSAGVE ALQVVTGSRK APHPKYFVGE GKAQEIAEAV KAAGASVVLF DHALSAAQER NLERLCECRV IDRTGLILDI FAQRARTHEG KLQVELAQLR HIATRLVRGW THLERQKGGI GLRGPGETQL ETDRRLLRDR ISLILRRLER VEKQREQGRR ARTRADVPTV SLVGYTNAGK STLFNRITSA DVYAADQLFA TLDPTLRRIE VADVGDTVLA DTVGFIRHLP HDLVAAFKAT LQETRQASLL LHVIDAADNR VDENIEAVNS VLAEIESDEI PTLLVMNKID MLDDFVPRID RNDENLPIRV WLSAASGEGI PLLFQALTER LSGQIVHHQL RLPPQAGRLR SRFYQLQAIE KEWNEEDGSI GVIIRMPIVE WRRLCKQEQD LINFIV // ID A0A084H429_9BACI Unreviewed; 423 AA. AC A0A084H429; DT 29-OCT-2014, integrated into UniProtKB/TrEMBL. DT 29-OCT-2014, sequence version 1. DT 07-JUN-2017, entry version 18. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=GS18_0205290 {ECO:0000313|EMBL:KEZ54341.1}; OS Bacillus indicus. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus. OX NCBI_TaxID=246786 {ECO:0000313|EMBL:KEZ54341.1, ECO:0000313|Proteomes:UP000028549}; RN [1] {ECO:0000313|EMBL:KEZ54341.1, ECO:0000313|Proteomes:UP000028549} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 16189 {ECO:0000313|EMBL:KEZ54341.1, RC ECO:0000313|Proteomes:UP000028549}; RX PubMed=15774653; DOI=10.1099/ijs.0.63208-0; RA Yoon J.H., Lee C.H., Oh T.K.; RT "Bacillus cibi sp. nov., isolated from jeotgal, a traditional Korean RT fermented seafood."; RL Int. J. Syst. Evol. Microbiol. 55:733-736(2005). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KEZ54341.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JNVC02000001; KEZ54341.1; -; Genomic_DNA. DR RefSeq; WP_029565658.1; NZ_JNVC02000001.1. DR EnsemblBacteria; KEZ54341; KEZ54341; GS18_0205290. DR Proteomes; UP000028549; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000028549}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000028549}. FT DOMAIN 198 360 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 423 AA; 47332 MW; 6D8DF953E8E1DBF0 CRC64; MNTGSEKVIL VGCQLPKTED EAFSYTMSEL ASLTKTANGE VLVQLSQKRE RIHPATYIGK GKVDELLALS EELEPDLIIF NDELSPSQQR NLSAALDVKI IDRTQLILDI FATRAKSKEG KLQVELAQLQ YLLPRLSGQG INLSRQGGGI GTRGPGETQL ETDRRHIRTR IHEIKMQLAA IVSHRNRYRE RRKKNQAFQV ALVGYTNAGK STLFNRITDA GTFEEDLLFA TLDPMTRKMT LPSGYQALLT DTVGFIQDLP TTLVAAFRST LEEVKEADLI LHVVDSSNED YVNHEKTVYK LLEELKVTTI PVLTVYNKQD KQSAGFVPSP KGEHVLISAF SDADIAKLKQ KIQSFSMELM EEYSIDVPAS EGKLLASLKT ETMVGHFAFN EEENHYEIQG HFLPGHAASG QIEMYKRKGN KHV // ID A0A084ILV2_9GAMM Unreviewed; 449 AA. AC A0A084ILV2; DT 29-OCT-2014, integrated into UniProtKB/TrEMBL. DT 29-OCT-2014, sequence version 1. DT 07-JUN-2017, entry version 18. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=C41B8_08875 {ECO:0000313|EMBL:KEZ77686.1}; OS Salinisphaera hydrothermalis C41B8. OC Bacteria; Proteobacteria; Gammaproteobacteria; Salinisphaerales; OC Salinisphaeraceae; Salinisphaera. OX NCBI_TaxID=1304275 {ECO:0000313|EMBL:KEZ77686.1, ECO:0000313|Proteomes:UP000028302}; RN [1] {ECO:0000313|EMBL:KEZ77686.1, ECO:0000313|Proteomes:UP000028302} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C41B8 {ECO:0000313|EMBL:KEZ77686.1, RC ECO:0000313|Proteomes:UP000028302}; RA Li C., Lai Q., Shao Z.; RT "Salinisphaera hydrothermalis C41B8 Genome Sequencing."; RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KEZ77686.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; APNK01000010; KEZ77686.1; -; Genomic_DNA. DR RefSeq; WP_051883313.1; NZ_APNK01000010.1. DR EnsemblBacteria; KEZ77686; KEZ77686; C41B8_08875. DR PATRIC; fig|1304275.5.peg.1809; -. DR Proteomes; UP000028302; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000028302}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000028302}. FT DOMAIN 198 365 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 449 AA; 49480 MW; 6AD90F7E8B937D83 CRC64; MFERPPTGQA AVIVHIAFGI DEYDEADQEF RELVESAGAD VLCHIGGSRR VPDPRFFIGG GKADEIAAAV AEHGAELVVF NHDLSPSQER NLEKRMNARV LDRAGLILDI FARRARSHEG KLQVELAQLQ HLATRLVRGW SHLERQKGGI GLRGPGETQL ETDRRLLNDR IKLLRSRLDK VLARRDQGRA SRRRARTPVV SLVGYTNAGK STLFNRLTGE EIYAADQLFA TLDPTLRRMD VPVGEPLIVA DTVGFIRDLP HELVAAFRAT LEETREADVL VHVIDAADNE RRAHAREVNG VLADIGAGEV PQLEVFNKVD LLDDESPRVE YDAHGRPVRV YVSAMTGEGL DELRHALAAF CYPDTVTGTL RVPPAAGWLR SQLYELGVVG AESYADNGDA LLSVTASQAD LERVVAQAGL KFGDVLIERR PVRPDVERLA AERAPRPPA // ID A0A084J936_9CLOT Unreviewed; 595 AA. AC A0A084J936; DT 29-OCT-2014, integrated into UniProtKB/TrEMBL. DT 29-OCT-2014, sequence version 1. DT 07-JUN-2017, entry version 18. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=IO99_14455 {ECO:0000313|EMBL:KEZ85470.1}; OS Clostridium sulfidigenes. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=318464 {ECO:0000313|EMBL:KEZ85470.1, ECO:0000313|Proteomes:UP000028542}; RN [1] {ECO:0000313|EMBL:KEZ85470.1, ECO:0000313|Proteomes:UP000028542} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=113A {ECO:0000313|EMBL:KEZ85470.1, RC ECO:0000313|Proteomes:UP000028542}; RA Honkalas V.S., Dabir A.P., Arora P., Dhakephalkar P.K.; RT "Draft genome of Clostridium sulfidigenes 113A isolated from sediments RT associated with methane hydrate from Krishna Godavari basin."; RL Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KEZ85470.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JPMD01000035; KEZ85470.1; -; Genomic_DNA. DR RefSeq; WP_035134428.1; NZ_JPMD01000035.1. DR EnsemblBacteria; KEZ85470; KEZ85470; IO99_14455. DR Proteomes; UP000028542; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000028542}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000028542}. FT DOMAIN 364 541 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 595 AA; 66894 MW; 2F75204FAEB6E985 CRC64; MINGNTDGVK NFILKKLDTI YDMRFQKSDI LTEELAELLR EVTLEIEREV SVAIDRKGSV VSVAIGDSST VEVPMIDTRE GRLSQVRVIH THPNGNPKLS ALDLSALLKL KLDCIVAIGV SEDKPLIYNM GFCDVKDNML IEEEVENLTI NKVLSYKFLD KVRYIEDVFK VDNIVEDNSE RAILVSIEDE ESLAELKELT KACDVEPVFE ILQKRNKIDS AYFIGSGKVE EIAYLRQSLR ANVVIFDEEL SGSQVRNLEQ AIGTKVIDRT TLILEIFARR ARSKESKIQV ELSQLKYRLS RLSGLGTMLS RTGGGIGTKG PGEKKLETDK RKIRDTIYDL NKELEKIKSI RATQRERRSK DNISKISLVG YTNAGKSTLR NALCEYSPVK SATVKEKVFE ADMLFATLDI TTRAMALPDN RVATVTDTVG FIRKLPHDLV EAFKSTLEEV VYSDLLLHVV DASSNAAEKQ ITVVEEVLKE LGAGDKPTLL VLNKIDNSND DILNSLKETF NNYSILEVSA KHKINFEELL NRCTDILPYK LKTFKVLIPY SDSSSVAYLH RNALVESEEY GEEGTILVVQ GDDEVYNKSS KYIIE // ID A0A084JAT2_9CLOT Unreviewed; 415 AA. AC A0A084JAT2; DT 29-OCT-2014, integrated into UniProtKB/TrEMBL. DT 29-OCT-2014, sequence version 1. DT 10-MAY-2017, entry version 18. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=IO99_11035 {ECO:0000313|EMBL:KEZ86066.1}; OS Clostridium sulfidigenes. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=318464 {ECO:0000313|EMBL:KEZ86066.1, ECO:0000313|Proteomes:UP000028542}; RN [1] {ECO:0000313|EMBL:KEZ86066.1, ECO:0000313|Proteomes:UP000028542} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=113A {ECO:0000313|EMBL:KEZ86066.1, RC ECO:0000313|Proteomes:UP000028542}; RA Honkalas V.S., Dabir A.P., Arora P., Dhakephalkar P.K.; RT "Draft genome of Clostridium sulfidigenes 113A isolated from sediments RT associated with methane hydrate from Krishna Godavari basin."; RL Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KEZ86066.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JPMD01000026; KEZ86066.1; -; Genomic_DNA. DR EnsemblBacteria; KEZ86066; KEZ86066; IO99_11035. DR Proteomes; UP000028542; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000028542}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000028542}. FT DOMAIN 195 361 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 154 191 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 415 AA; 47042 MW; A60EEB1F4416D830 CRC64; MERKGIVVGI NINNENGFEE SMVELKNLCM ACDIEAIGEL VQNSKQINKA HYIGSGKLDE LKSLVNSEEV DIVIFNNELS SSQLRNIEKA IECEVIDRTA LILSIFAERA KTREAKLQVE VARLQYLLPR LIGANENLGR QSGGVGTKNK GAGEKKLELD RRKIEAKIAA LNKELEELKH QRETQRNLRR KSSVPQIALV GYTNAGKSSI MNSMIDTFKD SEEKKVFEKD MLFATLETSI RSIKLDDNKK FLLSDTVGFV SNLPHNLIKA FRSTLEEVCE ADLLLHVVDI SNPDYKHHLK VTNETLKEIG AESVPMIYVY NKIDLVDDYL TEKNGVYISA KKNLGIDKLV ETISTKVFNN YINCNMFIPY DKGNLLSYLN DNARVIDRKY RNDGAELSIE CSNIDYEKYR EYVIG // ID A0A084TL59_9FLAO Unreviewed; 406 AA. AC A0A084TL59; DT 29-OCT-2014, integrated into UniProtKB/TrEMBL. DT 29-OCT-2014, sequence version 1. DT 07-JUN-2017, entry version 19. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=IA57_06345 {ECO:0000313|EMBL:KFB01445.1}; OS Mangrovimonas yunxiaonensis. OC Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales; OC Flavobacteriaceae; Mangrovimonas. OX NCBI_TaxID=1197477 {ECO:0000313|EMBL:KFB01445.1, ECO:0000313|Proteomes:UP000028521}; RN [1] {ECO:0000313|EMBL:KFB01445.1, ECO:0000313|Proteomes:UP000028521} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=LY01 {ECO:0000313|EMBL:KFB01445.1, RC ECO:0000313|Proteomes:UP000028521}; RA Li Y., Zheng T.; RT "Genome sequence of Mangrovimonas yunxiaonensis."; RL Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KFB01445.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JPFK01000005; KFB01445.1; -; Genomic_DNA. DR RefSeq; WP_036120663.1; NZ_JPFK01000005.1. DR EnsemblBacteria; KFB01445; KFB01445; IA57_06345. DR Proteomes; UP000028521; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000028521}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000028521}. FT DOMAIN 200 385 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 406 AA; 46802 MW; B7993204981BEADF CRC64; MLEKKNIALE SAVLIGVVTQ DQDEQKSKEY LDELEFLTYT AGGEVVKRFT QKLDTPNPKT FIGSGKLEDV KTFIKEHEVG TAIFDDELSP AQERNISRIL ECKVLDRTNL ILDIFAQRAT TSYARTQVEL AQCEYLLPRL KGMWTHLERQ KGGIGMRGPG ETEIETDRRI VRDKIALLKE KIKTIDKQMA VQRGNRGQLI RVALVGYTNV GKSTLMNVVS KSEVFAENKL FATLDTTVRK VVIKNLPFLM TDTVGFIRKL PTQLVESFKS TLDEVREADL LLHVVDISHP NFEEHIESVN KILDEINSAD KPIIMVFNKI DAYEAEPFDE TDLMTPRTPA NYSLKEWKRT WMNKMEGNVL FISALNKENL EAFRKKVYQE VRRIHVTRFP YNNFLYPDYD ENEQQE // ID A0A084UAL0_9RHIZ Unreviewed; 452 AA. AC A0A084UAL0; DT 29-OCT-2014, integrated into UniProtKB/TrEMBL. DT 29-OCT-2014, sequence version 1. DT 07-JUN-2017, entry version 19. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:KFB09996.1}; GN ORFNames=EL18_01023 {ECO:0000313|EMBL:KFB09996.1}; OS Nitratireductor basaltis. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Phyllobacteriaceae; Nitratireductor. OX NCBI_TaxID=472175 {ECO:0000313|EMBL:KFB09996.1, ECO:0000313|Proteomes:UP000053675}; RN [1] {ECO:0000313|EMBL:KFB09996.1, ECO:0000313|Proteomes:UP000053675} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=UMTGB225 {ECO:0000313|EMBL:KFB09996.1, RC ECO:0000313|Proteomes:UP000053675}; RA Gan H.Y.; RT "Draft Genome Sequence of Nitratireductor basaltis Strain UMTGB225, A RT Marine Bacterium Isolated from Green Barrel Tunicate."; RL Submitted (MAY-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KFB09996.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JMQM01000001; KFB09996.1; -; Genomic_DNA. DR RefSeq; WP_036480438.1; NZ_JMQM01000001.1. DR EnsemblBacteria; KFB09996; KFB09996; EL18_01023. DR PATRIC; fig|472175.3.peg.1031; -. DR Proteomes; UP000053675; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000053675}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000053675}. FT DOMAIN 228 397 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 452 AA; 49558 MW; F14FAD4AE42DE80D CRC64; MTDWESPSDG SFRTLPAENA SGATAIVLVP VLPRHFAKNS DEGNADTIPL TPDARLDEAV GLAAAIELEV AHAETAIVNA PRPGTLIGTG KVEEVAALVK ELEAELVVVD HQLSPVQQRN LEKAFRAKVL DRTGLILEIF GRRARTKEGR LQVDLAHLEY QRGRLVRSWT HLERQRGGGG FMGGPGETQI EADRRLLQER IVRIKRELET VRRTRDLHRA KRQKVPFPVV AIVGYTNAGK STLFNRLTGA TVMAEDMLFA TLDPTLRRVR FPHGTIAILS DTVGFISDLP THLVAAFRAT LEEVVEADFI IHVRDISDPN ASAHAANVQD VLKSLGVDVA DDKRIIEVLN KIDLLDEGAN AALAHAQNRS SIAISAVSGQ GIDALLQEIE RRVAGVLEEI TIEVSPAKMG TLDWIYRNSQ VLSRRDNDDG SLTLTLRATE MAREEIRGRL SA // ID A0A084WSX6_ANOSI Unreviewed; 661 AA. AC A0A084WSX6; DT 29-OCT-2014, integrated into UniProtKB/TrEMBL. DT 29-OCT-2014, sequence version 1. DT 12-APR-2017, entry version 11. DE SubName: Full=AGAP003969-PA-like protein {ECO:0000313|EMBL:KFB53320.1}; GN ORFNames=ZHAS_00021644 {ECO:0000313|EMBL:KFB53320.1}; OS Anopheles sinensis (Mosquito). OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; OC Pterygota; Neoptera; Holometabola; Diptera; Nematocera; Culicoidea; OC Culicidae; Anophelinae; Anopheles. OX NCBI_TaxID=74873 {ECO:0000313|EMBL:KFB53320.1, ECO:0000313|Proteomes:UP000030765}; RN [1] {ECO:0000313|EMBL:KFB53320.1, ECO:0000313|Proteomes:UP000030765, ECO:0000313|VectorBase:ASIC021644-PA} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=24438588; DOI=10.1186/1471-2164-15-42; RA Zhou D., Zhang D., Ding G., Shi L., Hou Q., Ye Y., Xu Y., Zhou H., RA Xiong C., Li S., Yu J., Hong S., Yu X., Zou P., Chen C., Chang X., RA Wang W., Lv Y., Sun Y., Ma L., Shen B., Zhu C.; RT "Genome sequence of Anopheles sinensis provides insight into genetics RT basis of mosquito competence for malaria parasites."; RL BMC Genomics 15:42-42(2014). RN [2] {ECO:0000313|VectorBase:ASIC021644-PA} RP IDENTIFICATION. RG VectorBase; RL Submitted (FEB-2017) to UniProtKB. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ATLV01026741; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; KE525419; KFB53320.1; -; Genomic_DNA. DR VectorBase; ASIC021644-RA; ASIC021644-PA; ASIC021644. DR Proteomes; UP000030765; Unassembled WGS sequence. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR CDD; cd01878; HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR026788; Tmem141. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR Pfam; PF15110; TMEM141; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000030765}; KW Reference proteome {ECO:0000313|Proteomes:UP000030765}. FT DOMAIN 421 598 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 661 AA; 74627 MW; 45DE06ED80C2677C CRC64; MNDIRLLKDQ QRDKHPGFDS YIECSTRSLF TGLATFSLGF AGVYFLQQVG QRYLPYTKKG NILVAAIVST VASYKVTSDR MRACQARWMA VEDKYSVLQE TLDTAAPEGV ASKEVGTIGM LFRAVDLRNG GETVRQHYIK TNPTDNLLKW QQLTQFCFYR RKYTDSSKYK GGKVAGQRHR AINNGPEDTD ESCSEESIER SELIDDREYD SVASSAMHVT KRIQNVQHVA IIQPYIKWGP RKSTTKPELL QQEAEALVRS LPKWNIELSL KIPVDTLDKR QLFGTGKLEE LKEMLRARQE AGTPLTCVFI SKGTLSYGQK HTLEQAFRLP VMDRYSIVVQ ILRLHAVSME AKLQVALAEL PYIWSQVKDQ EGSSKGSGRI FLSDSQRQML QLRERKLRHE LAMIRSHREL LRNRRRQKNF PVVAVVGYTN AGKTSLIKAL TEEASLQPRD QLFATLDVTA HAGRLPCKLE VLYMDTVGFM ADIPTGLIEC FVATLEDAML ADVIVHVQDL AHENCTEQKA HVERTLRTLM RNGERSLAPE RIINVGNKVD LVEDRQEVIT GAVSETPNGG RLHLVSSKTL HGIHELLLEV ERKVLQVTGR QRMVIKVPMG GQEVAWLYKN AAVTETAADP ANAERLLVSA VITEAKLQQF RHLFVRNRAT G // ID A0A085BPP1_9FLAO Unreviewed; 404 AA. AC A0A085BPP1; DT 29-OCT-2014, integrated into UniProtKB/TrEMBL. DT 29-OCT-2014, sequence version 1. DT 07-JUN-2017, entry version 20. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=IO90_03845 {ECO:0000313|EMBL:KFC24436.1}; OS Chryseobacterium sp. FH1. OC Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales; OC Flavobacteriaceae; Chryseobacterium. OX NCBI_TaxID=1233951 {ECO:0000313|EMBL:KFC24436.1, ECO:0000313|Proteomes:UP000028641}; RN [1] {ECO:0000313|EMBL:KFC24436.1, ECO:0000313|Proteomes:UP000028641} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=FH1 {ECO:0000313|EMBL:KFC24436.1, RC ECO:0000313|Proteomes:UP000028641}; RA Pipes S.E., Stropko S.J.; RT "Epilithonimonas sp. FH1 Genome."; RL Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KFC24436.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JPLZ01000002; KFC24436.1; -; Genomic_DNA. DR RefSeq; WP_034963991.1; NZ_JPLZ01000002.1. DR EnsemblBacteria; KFC24436; KFC24436; IO90_03845. DR Proteomes; UP000028641; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000028641}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000028641}. FT DOMAIN 200 384 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 404 AA; 47054 MW; 763E667A6E176A4A CRC64; MLEKKEHQYE KAVLVGLITQ NQSEDKLIEY MDELEFLAFT AGATVEKRFT QRLTQPDSKT FVGKGKMEEI RDYAKENGIG TVIFDDELSP SQLKNLEREM EVKILDRTNL ILDIFAQRAQ TSYARTQVEL AQYQYLLPRL TRMWTHLERQ KGGIGMRGPG ETEIETDRRI IRDRITLLKD KLKVIDKQMG TQRNNRGKMV RTALVGYTNV GKSTLMNALS KSDVFAENKL FATLDTTVRK VVIGNLPFLL TDTVGFIRKL PTQLVESFKS TLDEVREADL LIHVVDISHE SFEDHINSVN EILQEIDAHR KPMIMVFNKI DDFTYEKKDE DDLTPGSNKN ISLEEWQKTW MAKSKFPTVF ISALTKENFP EMKKMIYDEV HRIHISRFPY NDLLFEYFED EEEN // ID A0A085BUV6_9RHOB Unreviewed; 412 AA. AC A0A085BUV6; DT 29-OCT-2014, integrated into UniProtKB/TrEMBL. DT 29-OCT-2014, sequence version 1. DT 12-APR-2017, entry version 16. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=IV89_13495 {ECO:0000313|EMBL:KFC26251.1}; OS Sulfitobacter sp. CB2047. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae; Sulfitobacter. OX NCBI_TaxID=1525218 {ECO:0000313|EMBL:KFC26251.1, ECO:0000313|Proteomes:UP000028921}; RN [1] {ECO:0000313|EMBL:KFC26251.1, ECO:0000313|Proteomes:UP000028921} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CB2047 {ECO:0000313|EMBL:KFC26251.1, RC ECO:0000313|Proteomes:UP000028921}; RA Ankrah N.Y., Budinoff C., Hadden M., Lane T., Buchan A.; RT "Genome sequence of Sulfitobacter sp. CB2047."; RL Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KFC26251.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JPOY01000011; KFC26251.1; -; Genomic_DNA. DR EnsemblBacteria; KFC26251; KFC26251; IV89_13495. DR Proteomes; UP000028921; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000028921}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000028921}. FT DOMAIN 192 361 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 412 AA; 45607 MW; 39BD07670DACD9B7 CRC64; MIHPDIKSDN DRRIAEPALA EAVALARALP HLDVEGANIV PLRTVSAGML FGSGKIEELR LVFEEAEVEL VLVDGPVTPV QQRNLEKAWG VKLLDRTGLI LEIFSDRAAT REGVLQVEMA ALNYQRTRLV RAWTHLERQR GGLGFVGGPG ETQIESDRRA IDEQLVRLRR QLDKVVKTRA LHRAARAKVP FPIVALVGYT NAGKSTLFNR MTGADVMAKD MLFATLDPTM RSLVLPDGPE IILSDTVGFI SDLPTELVAA FRATLEEVLA ADIICHVRDI SHAETESQAR NVRDILTSLG VPKDTRSFEV WNKLDQLDED RAAAVRARAQ RDDSVLAISA ITGEGLDELQ AVIAEALQGA VREAELTLAF ADGKKRAWLF EQDVVIEETQ TEDGFNLIVR WSAQQEAQYQ RL // ID A0A085EL13_9FLAO Unreviewed; 410 AA. AC A0A085EL13; DT 29-OCT-2014, integrated into UniProtKB/TrEMBL. DT 29-OCT-2014, sequence version 1. DT 07-JUN-2017, entry version 19. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=FEM08_14190 {ECO:0000313|EMBL:KFC59908.1}; OS Flavobacterium gilvum. OC Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales; OC Flavobacteriaceae; Flavobacterium. OX NCBI_TaxID=1492737 {ECO:0000313|EMBL:KFC59908.1, ECO:0000313|Proteomes:UP000028636}; RN [1] {ECO:0000313|EMBL:KFC59908.1, ECO:0000313|Proteomes:UP000028636} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=EM1308 {ECO:0000313|EMBL:KFC59908.1, RC ECO:0000313|Proteomes:UP000028636}; RA Shin S.-K., Yi H.; RT "Genome Sequence of Flavobacterium sp. EM1308."; RL Submitted (MAY-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KFC59908.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JNCP01000036; KFC59908.1; -; Genomic_DNA. DR RefSeq; WP_035636092.1; NZ_JNCP01000036.1. DR EnsemblBacteria; KFC59908; KFC59908; FEM08_14190. DR PATRIC; fig|1492737.3.peg.1409; -. DR Proteomes; UP000028636; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000028636}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000028636}. FT DOMAIN 200 386 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 410 AA; 47501 MW; 06650390B3CBDDF0 CRC64; MLEKETINFE KTAIVGIITQ NQSEEKLNEY LDELEFLTFT AGGEVVKRFS QKMDRPNPKT FVGTGKLEEI CLFVKENNVS TLIFDDELSP SQQKNISRII DCKILDRTNL ILDIFAQRAE TSYARTQVEL AQCQYLLPRL SGMWTHLERQ KGGIGMRGPG ETEIETDRRI VRDRISLLKE KIKTIDRQMG VQRSNRGAMV RVALVGYTNV GKSTLMNAIG KSDVFVENKL FATLDTTVRK VVIKNLPFLL SDTVGFIRKL PTQLVDSFKS TLDEVREADL LLHIVDISHP EFEDHIESVN QILQDIKAHD KPVIMVFNKI DAYKHLTIDE DDLMTEKTPR HFTLEEWQQT WMHRLGESKA LFISASQKQN FEEFRECVYE AVRQIHITRF PYNKFLYPDY KDAVEKEENE // ID A0A085EQW3_9BRAD Unreviewed; 461 AA. AC A0A085EQW3; DT 29-OCT-2014, integrated into UniProtKB/TrEMBL. DT 29-OCT-2014, sequence version 1. DT 07-JUN-2017, entry version 17. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflx {ECO:0000313|EMBL:KFC61608.1}; GN Synonyms=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=FG93_06200 {ECO:0000313|EMBL:KFC61608.1}; OS Bosea sp. LC85. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Bradyrhizobiaceae; Bosea. OX NCBI_TaxID=1502851 {ECO:0000313|EMBL:KFC61608.1, ECO:0000313|Proteomes:UP000028622}; RN [1] {ECO:0000313|EMBL:KFC61608.1, ECO:0000313|Proteomes:UP000028622} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=LC85 {ECO:0000313|EMBL:KFC61608.1, RC ECO:0000313|Proteomes:UP000028622}; RA Gan H.M., Gan H.Y., Barton H.A., Savka M.A.; RT "Genome sequence of acyl-homoserine lactone-producing cave bacterial RT isolate."; RL Submitted (JUN-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KFC61608.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JPKG01000072; KFC61608.1; -; Genomic_DNA. DR EnsemblBacteria; KFC61608; KFC61608; FG93_06200. DR PATRIC; fig|1502851.3.peg.6272; -. DR Proteomes; UP000028622; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000028622}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000028622}. FT DOMAIN 227 401 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 461 AA; 50460 MW; 779FA4139FC13E52 CRC64; MAGRSGTDDV PAGVKPLDEI ERDIAANTRA FVIGPYLQRR GAAADANQRS FAARLDEAVG LAAAIDLSVV EPISALLTAL RPATYLGKGK VEEIAERITN EEIGLVVMDC ALSPVQQRNL EKAWGCKVID RTGLILEIFG RRARTKEGAL QVELAHLNYQ KSRLVRSWTH LERQRGGFGF LGGPGETQIE ADRRVIQERM TKIERDLDTV KRTRSLHRAS RKRVPYPVVA LVGYTNAGKS TLFNRLTSAD VLAQDMLFAT LDPTARAIKL PHGARIMLSD TVGFISDLPT QLIAAFRATL EDAIEADVLL HVRDLAHDDT QAQAADVQAI LRDLGIDPDD GQRVVEVWNK ADLLIGAEHD RQLALAELRP AASRPVLVSA LTGEGVDRLT DAIETRIARS RPVYRLTLEP GDGKSLAWLH TNGEVLSRED AEDGALALTV RLPPEREGAF GARFPRAERQ G // ID A0A085FAL4_9BURK Unreviewed; 401 AA. AC A0A085FAL4; DT 29-OCT-2014, integrated into UniProtKB/TrEMBL. DT 29-OCT-2014, sequence version 1. DT 30-AUG-2017, entry version 26. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:KFC68509.1}; GN ORFNames=FG94_02713 {ECO:0000313|EMBL:KFC68509.1}; OS Massilia sp. LC238. OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Oxalobacteraceae; Massilia. OX NCBI_TaxID=1502852 {ECO:0000313|EMBL:KFC68509.1, ECO:0000313|Proteomes:UP000028601}; RN [1] {ECO:0000313|EMBL:KFC68509.1, ECO:0000313|Proteomes:UP000028601} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=LC238 {ECO:0000313|EMBL:KFC68509.1, RC ECO:0000313|Proteomes:UP000028601}; RA Gan H.M., Gan H.Y., Barton H.A., Savka M.A.; RT "Genome sequence of acyl-homoserine lactone-producing cave bacterial RT isolate."; RL Submitted (JUN-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KFC68509.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JNNN01000050; KFC68509.1; -; Genomic_DNA. DR EnsemblBacteria; KFC68509; KFC68509; FG94_02713. DR PATRIC; fig|1502852.3.peg.2670; -. DR Proteomes; UP000028601; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000028601}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}. FT DOMAIN 199 366 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 401 AA; 43917 MW; 8350994CB801EAEC CRC64; MADAPGNTSM RAALVGIDFG SGDFTASLEE LSLLARSAGA EPITTITAKR SSPDPAHFVG SGKADEIKMA CKAEGIELVI FNHALSPAQQ RNLERRLEVR VVDRTSLILD IFAQRAQSHE GKLQVELAQL QHLATRLIRG WTHLERQKGG IGLRGPGETQ LETDRRLIGE RVKMLRTRLT KLRKQHETQR RQRGRNQTFS VSLVGYTNAG KSTLFNTLTK AGVYVANQLF ATLDTTSRRL YLGDEVGNVV ISDTVGFVRE LPHQLVAAFR ATLEETIHAD LLLHVVDGNS PVRMEQIEQV NEVLREIGAD HVPQILVWNK IDAAGLEPGV ERDEYDKISR VFISAHSGAG LDLLRDAIVE AALAARAEQE QSRNGEEPAV GGSLANSAEN NMTTSTHLGP H // ID A0A085FLQ0_9RHIZ Unreviewed; 459 AA. AC A0A085FLQ0; DT 29-OCT-2014, integrated into UniProtKB/TrEMBL. DT 29-OCT-2014, sequence version 1. DT 07-JUN-2017, entry version 19. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:KFC72395.1}; GN ORFNames=FF80_00150 {ECO:0000313|EMBL:KFC72395.1}; OS Devosia sp. LC5. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Hyphomicrobiaceae; Devosia. OX NCBI_TaxID=1502724 {ECO:0000313|EMBL:KFC72395.1, ECO:0000313|Proteomes:UP000028638}; RN [1] {ECO:0000313|EMBL:KFC72395.1, ECO:0000313|Proteomes:UP000028638} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=LC5 {ECO:0000313|EMBL:KFC72395.1, RC ECO:0000313|Proteomes:UP000028638}; RA Gan H.M., Gan H.Y., Barton H.A., Savka M.A.; RT "Genome sequence of acyl-homoserine lactone-producing cave bacterial RT isolate."; RL Submitted (JUN-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KFC72395.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JNNO01000001; KFC72395.1; -; Genomic_DNA. DR RefSeq; WP_035096783.1; NZ_JNNO01000001.1. DR EnsemblBacteria; KFC72395; KFC72395; FF80_00150. DR PATRIC; fig|1502724.3.peg.152; -. DR Proteomes; UP000028638; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000028638}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000028638}. FT DOMAIN 222 397 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 188 215 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 459 AA; 49828 MW; C2012A22AD94712B CRC64; MNDFHDDEAV QKGGPQAFID QRAQPTRAGL ICPDVRGAIS QHSIEARKAE FEGLAGAIRL EIAFSEIVKV REVKPATFIG GGHVETLAAR VKEDEIDLLL VDAALTPIQQ RNLEKETGTK VLDRTGLILE IFGERAATRE GVLQVELAHL NYQKSRLVRS WTHLERQRGS GGMGFMGGPG ETQIESDRRQ LTDRIVLLED RLEKVKKTRA QQRRQRDDTP FPIVALVGYT NAGKSSLFNT LTGAGVFAED LLFATLDTTV RKLELPHGRA VMLSDTVGFV ADLPTDLVAA FRATLEEVVD ADVILHARDV ANPDHLAQAL DVLKVLGDLG VSAETTPVIE VWNKIDLLGT VDGSTEEALT AISPAGRVAA VVPVSAKTGQ GLDTLKLAIE AALAEKSRTY HVHVPHSAGG DIGWLHSHAE IISRDEATEK GSGFVVRVEP RHKAAFLERF NGRIEGSDA // ID A0A085HF46_9GAMM Unreviewed; 427 AA. AC A0A085HF46; DT 29-OCT-2014, integrated into UniProtKB/TrEMBL. DT 29-OCT-2014, sequence version 1. DT 30-AUG-2017, entry version 22. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=GLGR_2708 {ECO:0000313|EMBL:KFC94591.1}; OS Leminorella grimontii ATCC 33999 = DSM 5078. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; OC Budviciaceae; Leminorella. OX NCBI_TaxID=1005999 {ECO:0000313|EMBL:KFC94591.1, ECO:0000313|Proteomes:UP000028624}; RN [1] {ECO:0000313|EMBL:KFC94591.1, ECO:0000313|Proteomes:UP000028624} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33999 {ECO:0000313|EMBL:KFC94591.1, RC ECO:0000313|Proteomes:UP000028624}; RA Plunkett G.III., Neeno-Eckwall E.C., Glasner J.D., Perna N.T.; RT "ATOL: Assembling a taxonomically balanced genome-scale reconstruction RT of the evolutionary history of the Enterobacteriaceae."; RL Submitted (MAY-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KFC94591.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JMPN01000019; KFC94591.1; -; Genomic_DNA. DR RefSeq; WP_027276115.1; NZ_KE392227.1. DR EnsemblBacteria; KFC94591; KFC94591; GLGR_2708. DR PATRIC; fig|1005999.4.peg.2699; -. DR Proteomes; UP000028624; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000028624}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000028624}. FT DOMAIN 198 365 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 164 191 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 427 AA; 48203 MW; 6B59AADB4A222083 CRC64; MFERYDAGEQ AVLVHIDFSQ EKEAEDLREF ESLVSSAGVE TLQVVTGSRK APQAKYFVGE GKAEEIAQAV SATEASVVLF NHSLTPAQER NLERLCQCRV IDRTGLILDI FAQRARTHEG KLQVELAQLR HLATRLVRGW THLERQKGGI GLRGPGETQL ETDRRLLRER IKQILSRLEK VEKQREQGRR ARVRAEIPTV SLVGYTNAGK STLFNQITTA GVYADDRLFA TLDPTLRRIE VEDVGATVLA DTVGFIRHLP HDLVAAFKAT LQETRQASLL LHVVDAADAR ISDNIAAVTD VLAEIEADEI PVLLVMNKID RLEDFAPRID RDENNVPVRV WLSAETGAGI DLLFRALTER LSGEIAQYTL KLPVQEGRLR SRFYQLQSIL KEWTEEDGSI GLVIRMPIAD WRRLCKQEQA LERYIVR // ID A0A085ICM3_9ENTR Unreviewed; 426 AA. AC A0A085ICM3; DT 29-OCT-2014, integrated into UniProtKB/TrEMBL. DT 29-OCT-2014, sequence version 1. DT 30-AUG-2017, entry version 23. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:KFD05969.1}; GN ORFNames=GKAS_01657 {ECO:0000313|EMBL:KFD05969.1}; OS Kluyvera ascorbata ATCC 33433. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; OC Enterobacteriaceae; Kluyvera. OX NCBI_TaxID=1006000 {ECO:0000313|EMBL:KFD05969.1, ECO:0000313|Proteomes:UP000028600}; RN [1] {ECO:0000313|EMBL:KFD05969.1, ECO:0000313|Proteomes:UP000028600} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33433 {ECO:0000313|EMBL:KFD05969.1, RC ECO:0000313|Proteomes:UP000028600}; RA Plunkett G.III., Neeno-Eckwall E.C., Glasner J.D., Perna N.T.; RT "ATOL: Assembling a taxonomically balanced genome-scale reconstruction RT of the evolutionary history of the Enterobacteriaceae."; RL Submitted (MAY-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KFD05969.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JMPL01000022; KFD05969.1; -; Genomic_DNA. DR RefSeq; WP_035893324.1; NZ_JMPL01000022.1. DR EnsemblBacteria; KFD05969; KFD05969; GKAS_01657. DR Proteomes; UP000028600; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000028600}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000028600}. FT DOMAIN 198 365 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 426 AA; 48141 MW; 9ED12C818FBA2F42 CRC64; MFDRYDAGEQ AVLVHIYFTQ DKDMEDLQEF ESLVSSAGVE AMQVITGSRK APHPKYFVGE GKAVEIAEAV KATGASVVLF DHALSPAQER NLEALCQCRV IDRTGLILDI FAQRARTHEG KLQVELAQLR HLATRLVRGW THLERQKGGI GLRGPGETQL ETDRRLLRNR IMQILSRIER VEKQREQGRR ARVKADVPTV SLVGYTNAGK STLFNHITQA EVYAADQLFA TLDPTLRRID VADVGETVLA DTVGFIRHLP HDLVAAFKAT LQETREATLL LHVIDAADVR VQENIDAVNT VLEEIDAHEI PTLLVMNKID MLDDFEPRID RDEENKPIRV WLSAQTGVGI PLLFQALTER LAGEVAQHTL RLPPQAGRLR SRFYQLQAIE KEWMEEDGCV NLQVRMPIVD WRRLCKQEPT LADYVV // ID A0A085JKT8_9GAMM Unreviewed; 426 AA. AC A0A085JKT8; DT 29-OCT-2014, integrated into UniProtKB/TrEMBL. DT 29-OCT-2014, sequence version 1. DT 30-AUG-2017, entry version 21. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:KFD21084.1}; GN ORFNames=GTPT_1026 {ECO:0000313|EMBL:KFD21084.1}; OS Tatumella ptyseos ATCC 33301. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; OC Erwiniaceae; Tatumella. OX NCBI_TaxID=1005995 {ECO:0000313|EMBL:KFD21084.1, ECO:0000313|Proteomes:UP000028602}; RN [1] {ECO:0000313|EMBL:KFD21084.1, ECO:0000313|Proteomes:UP000028602} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33301 {ECO:0000313|EMBL:KFD21084.1, RC ECO:0000313|Proteomes:UP000028602}; RA Plunkett G.III., Neeno-Eckwall E.C., Glasner J.D., Perna N.T.; RT "ATOL: Assembling a taxonomically balanced genome-scale reconstruction RT of the evolutionary history of the Enterobacteriaceae."; RL Submitted (MAY-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KFD21084.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JMPR01000018; KFD21084.1; -; Genomic_DNA. DR RefSeq; WP_025901084.1; NZ_JMPR01000018.1. DR EnsemblBacteria; KFD21084; KFD21084; GTPT_1026. DR Proteomes; UP000028602; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000028602}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000028602}. FT DOMAIN 198 365 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 426 AA; 47886 MW; 622D269FAAC6BEC4 CRC64; MFERYEAGEQ AVLVHIWFTQ DRDQEDLQEF ETLVSSAGVE ALQVVTGSRK APHPKYFVGE GKAQEIADAV KATGASVVLF DHALSPAQER NLEAICQCRV VDRTGLILDI FAQRARTHEG KLQVELAQLR HLATRLVRGW THLERQKGGI GLRGPGETQL ETDRRLLRNR ISLILSRLSR VEKQREQGRQ ARAKADIPTV SLVGYTNAGK STLFNKVTSA DVYAADQLFA TLDPTLRRLH IADVGDVVLA DTVGFIRHLP HDLVAAFKAT LQETREASLL MHVVDAADVR LDENIDAVDE VLAEIEADEI PALLVMNKID RLEGFEPRID RNEENMPVRV WLSAQSGAGI PLLWQALSER LAGEIAQYEL RLPPHAGKLR SRFYQLHAIE KEWNEDDGST GLHIRMPVVD WRRMCKQEPS VIDYIV // ID A0A085L0I8_9FLAO Unreviewed; 401 AA. AC A0A085L0I8; DT 29-OCT-2014, integrated into UniProtKB/TrEMBL. DT 29-OCT-2014, sequence version 1. DT 07-JUN-2017, entry version 20. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=AT05_09570 {ECO:0000313|EMBL:KFD38484.1}; OS Schleiferia thermophila str. Yellowstone. OC Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales; OC Schleiferiaceae; Schleiferia. OX NCBI_TaxID=1453500 {ECO:0000313|EMBL:KFD38484.1, ECO:0000313|Proteomes:UP000028720}; RN [1] {ECO:0000313|EMBL:KFD38484.1, ECO:0000313|Proteomes:UP000028720} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Yellowstone {ECO:0000313|EMBL:KFD38484.1, RC ECO:0000313|Proteomes:UP000028720}; RA Thiel V., Tomsho L.P., Burhans R., Gay S.E., Ramaley R.F., RA Schuster S.C., Steinke L.A., Bryant D.A.; RT "Draft genome sequence of the moderately thermophilic bacterium RT Schleiferia thermophila strain Yellowstone (Bacteroidetes)."; RL Submitted (JAN-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KFD38484.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JDSI01000011; KFD38484.1; -; Genomic_DNA. DR RefSeq; WP_037360255.1; NZ_JDSI01000011.1. DR EnsemblBacteria; KFD38484; KFD38484; AT05_09570. DR Proteomes; UP000028720; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000028720}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000028720}. FT DOMAIN 203 388 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 401 AA; 45679 MW; 611C0F0943DFF0AB CRC64; MIESKIKISQ EREKAVLVGV STPGQPEEKT REYLDELQFL ADTAGAEVVG TLTQKLQHPN PATYIGSGKL EELGEMVRTL EANLVIFDDE LSATQIRNLE KFLQVKILDR TNLILDIFAG RARTSYARAQ VELAQYEYLL PRLTRMWTHL ERQKGGIGLR GPGETQIETD RRIIQQKIAL LTEKLKKIDR QMATQRKHRG DMVRVALVGY TNVGKSTLMN LLSKANVFAE NKLFATLDTT VRKVVLQDVA FLLSDTVGFI RKLPTQLVES FKSTLDEVRE SDLLLHVVDI SHPAFEDHII AVNQTIQELL QGQEKKIVMV FNKIDLYQPA KRDPDDLSPL QKDQMTLDDW QQTWMAKAAG DCVFISAEKK INIDSLREVL YREVKKIRDA RYPYAGIKTD I // ID A0A085LFB7_9MICO Unreviewed; 519 AA. AC A0A085LFB7; DT 29-OCT-2014, integrated into UniProtKB/TrEMBL. DT 29-OCT-2014, sequence version 1. DT 05-JUL-2017, entry version 22. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=IU11_09660 {ECO:0000313|EMBL:KFD43663.1}; OS Cellulosimicrobium sp. MM. OC Bacteria; Actinobacteria; Micrococcales; Promicromonosporaceae; OC Cellulosimicrobium. OX NCBI_TaxID=1523621 {ECO:0000313|EMBL:KFD43663.1, ECO:0000313|Proteomes:UP000028634}; RN [1] {ECO:0000313|EMBL:KFD43663.1, ECO:0000313|Proteomes:UP000028634} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MM {ECO:0000313|EMBL:KFD43663.1, RC ECO:0000313|Proteomes:UP000028634}; RA Lal R., Sharma A., Sangwan N., Hira P.; RL Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:KFD43663.1, ECO:0000313|Proteomes:UP000028634} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MM {ECO:0000313|EMBL:KFD43663.1, RC ECO:0000313|Proteomes:UP000028634}; RA Khurana J.P.; RT "Draft genome sequence of Cellulosimicrobium sp. MM isolated from RT arsenic rich microbial mats of a himalayan hotspring."; RL Submitted (AUG-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KFD43663.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JPQW01000152; KFD43663.1; -; Genomic_DNA. DR RefSeq; WP_024840599.1; NZ_JPQW01000152.1. DR EnsemblBacteria; KFD43663; KFD43663; IU11_09660. DR GeneID; 32509485; -. DR Proteomes; UP000028634; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 2. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000028634}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000028634}. FT DOMAIN 298 464 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 519 AA; 55537 MW; 172580D2B7CB2851 CRC64; MSPTPANTPT NPTSAQDEPT GATRDIASDV VARVLARAGT ARAEGGTVHA EHDGEQLDLA ERSALRRVAG LSTELEDVTE VEYRQLRLEK VVLVGIWSPG SDPREDGAPS TAEEAEISLR ELAALAETAG SQVLDGVIQR RAKPDPGTYL GSGKAAELAD VVAASGADTV VVDGELAPSQ RRALEDIVKV KVIDRTALIL DIFAQHAKSR EGKAQVELAQ LEYLLPRLRG WGESMSRQAG GQVGGAGAGM GSRGPGETKI ELDRRRIRNR MAKLRREIQA MAPGRETKRA SRKRHAVPSV AIAGYTNAGK SSLLNAVTGA GVLVENALFA TLDPTVRRTR TEDGRVYTLA DTVGFVRALP HQLVEAFRST LEEVGDADLL LHVVDASHPD PEGQIAAVRH VLAGIPGVED VPEVIVLNKA DVADPETIAR IRLRERRTVV VSAHTGEGIE HLRELIAREL PRPDVEIDLV VPYSRGDLVH RVHTEGEIDH EEHTPEGTLL RGRVAQALAT ELVGAAAQA // ID A0A085N7I9_9BILA Unreviewed; 508 AA. AC A0A085N7I9; DT 29-OCT-2014, integrated into UniProtKB/TrEMBL. DT 29-OCT-2014, sequence version 1. DT 07-JUN-2017, entry version 11. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:KFD65435.1}; DE Flags: Fragment; GN ORFNames=M513_03823 {ECO:0000313|EMBL:KFD55182.1}, GN M514_03823 {ECO:0000313|EMBL:KFD65435.1}; OS Trichuris suis (pig whipworm). OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia; OC Trichocephalida; Trichuridae; Trichuris. OX NCBI_TaxID=68888 {ECO:0000313|EMBL:KFD65435.1, ECO:0000313|Proteomes:UP000030758}; RN [1] {ECO:0000313|EMBL:KFD65435.1, ECO:0000313|Proteomes:UP000030758, ECO:0000313|Proteomes:UP000030764} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DCEP-RM93F {ECO:0000313|EMBL:KFD65435.1}, and RC DCEP-RM93M {ECO:0000313|EMBL:KFD55182.1}; RX PubMed=24929829; DOI=10.1038/ng.3012; RA Jex A.R., Nejsum P., Schwarz E.M., Hu L., Young N.D., Hall R.S., RA Korhonen P.K., Liao S., Thamsborg S., Xia J., Xu P., Wang S., RA Scheerlinck J.P., Hofmann A., Sternberg P.W., Wang J., Gasser R.B.; RT "Genome and transcriptome of the porcine whipworm Trichuris suis."; RL Nat. Genet. 46:701-706(2014). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; KL363201; KFD55182.1; -; Genomic_DNA. DR EMBL; KL367538; KFD65435.1; -; Genomic_DNA. DR Proteomes; UP000030758; Unassembled WGS sequence. DR Proteomes; UP000030764; Unassembled WGS sequence. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR CDD; cd01878; HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000030758}; KW Reference proteome {ECO:0000313|Proteomes:UP000030758}. FT DOMAIN 279 445 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT NON_TER 508 508 {ECO:0000313|EMBL:KFD65435.1}. SQ SEQUENCE 508 AA; 57485 MW; 0C6161530D305659 CRC64; MHSVRICAYS KRLLVRIGGL RLQTKLCWSV LAKRTFSLNS GEGSSLTGTD LYDDDEPLSN RTDFRGLQSY LNLPQPGSSH RLFVIQPKLS TPELRRLATT NEDLLLEAVQ LVKSVPSWTV SSISDSFAKV SPRTRFIFGS GKLEELKSIV NRSRDCTDIF LNIDRLTPLQ HRSLISVFGV PVFDRFTVAL QIFKLYASSK EAKIQAALAE LEYMKVHVTS YAGGLMQKYF PRTLMPIGVD WKKREEIISR RQLRMKEKLK ATVAQRNVLR QNAQRRRFPM VAVVGYTNCG KTSLIRCLSE NANLSGEDRF FATLDVTVHA GKLPCKLPIL YADTVGFFSN LPMDLMPCFD STLEEITYAD LVIHVIDRSN PNWQFQRQSV MQTFDRLNAA SNLHMSPLEV WNKSDKFQLE TEDDKPTAVA IVSCLSGDGM PKLLTLIEDR ILTTTMYKRF VVRIPITGGY LSSLYSIGSI VATETPQTSD HMRVTLVTKQ HHIDKLLGMY PNVIEVVK // ID A0A085TX47_9RHOB Unreviewed; 413 AA. AC A0A085TX47; DT 29-OCT-2014, integrated into UniProtKB/TrEMBL. DT 29-OCT-2014, sequence version 1. DT 07-JUN-2017, entry version 18. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=DW2_07692 {ECO:0000313|EMBL:KFE35294.1}; OS Thioclava atlantica. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae; Thioclava. OX NCBI_TaxID=1317124 {ECO:0000313|EMBL:KFE35294.1, ECO:0000313|Proteomes:UP000028607}; RN [1] {ECO:0000313|Proteomes:UP000028607} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=13D2W-2 {ECO:0000313|Proteomes:UP000028607}; RA Lai Q., Li G., Shao Z.; RT "Thioclava sp. 13D2W-2 Genome Sequencing."; RL Submitted (APR-2013) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KFE35294.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AQRC01000005; KFE35294.1; -; Genomic_DNA. DR EnsemblBacteria; KFE35294; KFE35294; DW2_07692. DR PATRIC; fig|1317124.6.peg.1556; -. DR Proteomes; UP000028607; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000028607}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000028607}. FT DOMAIN 193 362 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 413 AA; 46029 MW; 4B45F18C496B4D69 CRC64; MIHPDIPSRE GQRHLPEFAL AEAVSLAGAL PHLQVVGSEI AKLRKPEPGH LFGSGKLAEI KDRLEAAEVD LVLVDGPVTP VQQRNLEKAW GVKLLDRTGL ILEIFADRAR TREGVLQVEL AALSYQRTRL VRAWTHLERQ RGGLGFVGGP GETQIEADRR AIDEQIVRLR RQLAKVVKTR ELHRAARRKV PFPIVALVGY TNAGKSTLFN RVTGAEVLAK DMLFATLDPT MRGLELPSGR KVILSDTVGF ISDLPTQLVA AFRATLEEVL EADLILHVRD ISHPETEEQA QDVNDILGKL GVAKDVPLIE VWNKMDLVPP EPRRALSVQE AREPDLQAIS ALTGEGVAAL LAAVDEKLAE ERFHEEIALP FAEGRKRAWL HEQNVVRAEH QTEEGWRFDV EWTGAQRSRF RNL // ID A0A085V9A7_PSESX Unreviewed; 433 AA. AC A0A085V9A7; DT 29-OCT-2014, integrated into UniProtKB/TrEMBL. DT 29-OCT-2014, sequence version 1. DT 30-AUG-2017, entry version 23. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=IV01_23155 {ECO:0000313|EMBL:KFE52020.1}; OS Pseudomonas syringae. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=317 {ECO:0000313|EMBL:KFE52020.1, ECO:0000313|Proteomes:UP000028631}; RN [1] {ECO:0000313|EMBL:KFE52020.1, ECO:0000313|Proteomes:UP000028631} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=GAW0119 {ECO:0000313|EMBL:KFE52020.1, RC ECO:0000313|Proteomes:UP000028631}; RA Baltrus D.A., Berge O., Morris C.; RT "Draft Genome Sequences of Environmental Pseudomonas syringae RT strains."; RL Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KFE52020.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JPQU01000078; KFE52020.1; -; Genomic_DNA. DR RefSeq; WP_032631227.1; NZ_JPQU01000078.1. DR EnsemblBacteria; KFE52020; KFE52020; IV01_23155. DR PATRIC; fig|317.175.peg.4828; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR Proteomes; UP000028631; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000028631}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000028631}. FT DOMAIN 199 366 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 433 AA; 48794 MW; F8E957F7B04BE1E3 CRC64; MFFERHSGGE RAILVHLDGQ DPEAREDPQE FQELAISAGA DTVAFVNVPR HRPSAKYLIG SGKVEELRDQ VKAEKADIVI FNHTLTPSQE RNLEKVFECR VLDRTGLILD IFAQRARTHE GKLQVELAQL EHMSTRLVRG WTHLERQGGG IGLRGPGETQ LETDRRLLRV RLRQIKGRLE KVRSQREQAR RGRKRADIPS VSLVGYTNAG KSTLFNAVTD SDVFAADQLF ATLDPTLRRL QLDDLGPVVL ADTVGFIRHL PHKLVEAFRS TLEESSNSDL LLHVIDSHEP ERMAQIEQVM VVLGEIGAEG LPILEVYNKL DLLEGVEPQI QRDADGKPQR VWLSARDGRG LDLLKQAIAE LLGDDLFIGT LHLPQRLARL RAQFFELGAV QSEEHDEDGA SLLAVRLPRV EFNRLVSREG LQPLEFIEQH TLQ // ID A0A085W038_9DELT Unreviewed; 550 AA. AC A0A085W038; DT 29-OCT-2014, integrated into UniProtKB/TrEMBL. DT 29-OCT-2014, sequence version 1. DT 07-JUN-2017, entry version 21. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=DB31_4486 {ECO:0000313|EMBL:KFE61051.1}; OS Hyalangium minutum. OC Bacteria; Proteobacteria; Deltaproteobacteria; Myxococcales; OC Cystobacterineae; Archangiaceae; Hyalangium. OX NCBI_TaxID=394096 {ECO:0000313|EMBL:KFE61051.1, ECO:0000313|Proteomes:UP000028725}; RN [1] {ECO:0000313|EMBL:KFE61051.1, ECO:0000313|Proteomes:UP000028725} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 14724 {ECO:0000313|EMBL:KFE61051.1, RC ECO:0000313|Proteomes:UP000028725}; RA Sharma G., Subramanian S.; RT "Genome assembly of Hyalangium minutum DSM 14724."; RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KFE61051.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JMCB01000025; KFE61051.1; -; Genomic_DNA. DR RefSeq; WP_044198402.1; NZ_JMCB01000025.1. DR EnsemblBacteria; KFE61051; KFE61051; DB31_4486. DR PATRIC; fig|394096.3.peg.8219; -. DR Proteomes; UP000028725; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000028725}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000028725}. FT DOMAIN 378 542 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 337 364 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 550 AA; 60808 MW; 5630B7CCCFBB11C2 CRC64; MKEIYGNTLG LKSSEQQRLR NTYRRRVDPH EIVSPELARH LTELSSETHR QIGVLINRKG DIEYVVVGNA HKLELPDIGR ARAGQVRLRG LRLVHTHLKS EPLTKDDLTD LALLRLDMVA AVGVGREGLP GVLHYAHLVP ENGANEFWRV STLPSVHTGQ PDLIDTMDAL EEELNRKAAA RAVGGREKAI LVAVCLDGNR GHAEASLAEL KELARTAGVE VIDSVLQMRR EADPRYLIGR GKLEDLNLRS MQSMVDLIIF DKDLTPSQGR HIAEATSLKV LDRTQLILDI FAQRAQSAEG KLQVELAQLK YRLPRLVQSD DSLSRLAGGI GGRGPGETKL EIDRRRVRER ITHLEKRIDT ISRERSVRRA QRNRRELPVI SIVGYTNAGK STLLNAITNA EVLAENKLFA TLDPTSRRLR FPQEREVIIT DTVGFIRDLP KDLVAAFRAT LEELADASLL LHVVDAADLA RDEQVEAVEG ILGSLGLMDK PRLMVWNKAD LLPAEDVEAL LRSRGGVAIS AQTREGLTSL LAKADTTLFA EGASEALGAL // ID A0A085WVP4_9DELT Unreviewed; 460 AA. AC A0A085WVP4; DT 29-OCT-2014, integrated into UniProtKB/TrEMBL. DT 29-OCT-2014, sequence version 1. DT 07-JUN-2017, entry version 21. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=DB31_0018 {ECO:0000313|EMBL:KFE71757.1}; OS Hyalangium minutum. OC Bacteria; Proteobacteria; Deltaproteobacteria; Myxococcales; OC Cystobacterineae; Archangiaceae; Hyalangium. OX NCBI_TaxID=394096 {ECO:0000313|EMBL:KFE71757.1, ECO:0000313|Proteomes:UP000028725}; RN [1] {ECO:0000313|EMBL:KFE71757.1, ECO:0000313|Proteomes:UP000028725} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 14724 {ECO:0000313|EMBL:KFE71757.1, RC ECO:0000313|Proteomes:UP000028725}; RA Sharma G., Subramanian S.; RT "Genome assembly of Hyalangium minutum DSM 14724."; RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KFE71757.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JMCB01000001; KFE71757.1; -; Genomic_DNA. DR RefSeq; WP_044180444.1; NZ_JMCB01000001.1. DR EnsemblBacteria; KFE71757; KFE71757; DB31_0018. DR PATRIC; fig|394096.3.peg.17; -. DR Proteomes; UP000028725; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 2. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000028725}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000028725}. FT DOMAIN 241 406 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 460 AA; 50107 MW; 88DF85C23CD7E43A CRC64; MPKTLSARPL AVLVGVQLPD VSDAEHAADL AELARLVKTL GYDAVATVSQ RREGLASGTV LGTGKLKELA QLTGGSGVIA SGAQERTSKA RERWESADAA HEEPGDEEAA PPAEDAPGEV AQRPTIVVVD HELSPSQLRN LEKATGAQVL DRTGVIVDIF HRHARSHEAR MQVEIARLNY LAPRLRESTG GRERQQGRGS GDSAVELDRR KIRDRLAELR EGLAAIQKDQ DQRRYARRDQ LRVALVGYTN AGKSSLMRAL TGSEVLVADQ LFATLDTTVR ALQPESRPRV LVSDTVGFIQ KLPHDLVASF RSTLDEALEA SLLLYVVDAS DPTWNTQLEV TRTVLREIGA DAVPSQLLFN KVDRLDAAAQ EALRSRHPEA MLLSAHRPED VGLLRERILS AFAASMVDAD LVIPYASQSR ISEVYEHTTV LSESFDESGR KLRVRGLPGA IARLTQSFGA // ID A0A086D7W7_9GAMM Unreviewed; 440 AA. AC A0A086D7W7; DT 29-OCT-2014, integrated into UniProtKB/TrEMBL. DT 29-OCT-2014, sequence version 1. DT 30-AUG-2017, entry version 20. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=GY26_01605 {ECO:0000313|EMBL:KFF50531.1}; OS Gammaproteobacteria bacterium MFB021. OC Bacteria; Proteobacteria; Gammaproteobacteria. OX NCBI_TaxID=1492922 {ECO:0000313|EMBL:KFF50531.1, ECO:0000313|Proteomes:UP000028732}; RN [1] {ECO:0000313|EMBL:KFF50531.1, ECO:0000313|Proteomes:UP000028732} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MFB021 {ECO:0000313|EMBL:KFF50531.1, RC ECO:0000313|Proteomes:UP000028732}; RA Joseph T.C., Baby A., Varghese A.M., Reghunathan D., Murugadas V., RA Lalitha K.V.; RT "Draft Genome sequence of a halophilic and highly halotolerant unknown RT Gammaproteobacteria strain MFB021."; RL Submitted (JUN-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KFF50531.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JNVT01000019; KFF50531.1; -; Genomic_DNA. DR RefSeq; WP_035469969.1; NZ_JNVT01000019.1. DR EnsemblBacteria; KFF50531; KFF50531; GY26_01605. DR Proteomes; UP000028732; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000028732}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000028732}. FT DOMAIN 199 365 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 440 AA; 49664 MW; 79DB5F7FDFF344FF CRC64; MFFERPDAGE TAILVHVDFQ DEQDREDPGE LLELVRSAGA VPATLIQGSR RRPDPRSFIG SGKLDEVKHA LTAHHAELVI FNHALSPSQE RNLERSLNCR VLDRTGLILD IFAQRARTHE GKLQVELAQL EYMSTRLVRG WTHLERQKGG IGLRGPGETQ LETDRRLLRA RIKSIHKRLE KVRKQRDQNR RARARAEVPS VSLVGYTNAG KSTLFNAITA AEVYAADQLF ATLDPTLRRL DVPDVGEVVL ADTVGFIRHL PHKLVEAFQA TLQEATEASL LVHVIDAADP DRELNVAQVD SVLAEIDADD VPRLLVMNKI DLMDTAPRIE RDGQGRPQVV WLSARDGQGL ELLREAIGEW LAEDILDTRL TLTPEQGRLR AALHELQAVR EESFAEDGRT ILQIRLPRRE FMQMMARLGE SADDYLPVHE QTPIDDWERV // ID A0A086MQ61_9RHIZ Unreviewed; 464 AA. AC A0A086MQ61; DT 29-OCT-2014, integrated into UniProtKB/TrEMBL. DT 29-OCT-2014, sequence version 1. DT 07-JUN-2017, entry version 20. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=JH26_00760 {ECO:0000313|EMBL:KFG71029.1}; OS Microvirga sp. BSC39. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Methylobacteriaceae; Microvirga. OX NCBI_TaxID=1549810 {ECO:0000313|EMBL:KFG71029.1, ECO:0000313|Proteomes:UP000028825}; RN [1] {ECO:0000313|EMBL:KFG71029.1, ECO:0000313|Proteomes:UP000028825} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BSC39 {ECO:0000313|EMBL:KFG71029.1, RC ECO:0000313|Proteomes:UP000028825}; RA Kellom M., Bailey A., Poret-Peterson A., Noonan K., Raymond J.; RT "Draft Genome of Microvirga aerilata BSC39, Isolated from Biological RT Soil Crust of Moab, Utah."; RL Submitted (AUG-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KFG71029.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JPUG01000005; KFG71029.1; -; Genomic_DNA. DR RefSeq; WP_036345673.1; NZ_JPUG01000005.1. DR EnsemblBacteria; KFG71029; KFG71029; JH26_00760. DR Proteomes; UP000028825; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000028825}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000028825}. FT DOMAIN 231 405 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 464 AA; 51429 MW; 4C985CA34B843EF7 CRC64; MTEPRTPGEE RLLQLAEPEK EVAAGTRTLV VGPYLTRKRR VSADAEGEGA NPRPPEARLD EITGLSLAID LTIVRSLTAP LSSPRPATFI GSGKVEELAG MVRAEEIGLV VMDCALSPVQ QRNLEKAWGA KVIDRTGLIL EIFGRRARTK EGTLQVELAH LSYQKGRLVR SWTHLERQRG GFGFLGGPGE TQIEADRRMI QERMNRIERD LESVVKTRSL HRTSRRRVPY PIIALVGYTN AGKSTLFNRM TQADVLAENM LFATLDPTSR AIDLPHGEKA ILSDTVGFIS DLPTMLVAAF RATLEDVVEA DVLLHVRDVS HGETEAQAGD VAVVLRELGI DPDDTRRIIE VWNKADLLSA EDRERLATTS QRTGEERRPI LISALTGDGI PELLATIEQH LALGRLTYEV DVAAEDGQGL AWLHENTEIL DRQTRENGHT VLQVRLVAGK EPRFLNRFPE ARVL // ID A0A086P9U2_SPHHM Unreviewed; 444 AA. AC A0A086P9U2; DT 29-OCT-2014, integrated into UniProtKB/TrEMBL. DT 29-OCT-2014, sequence version 1. DT 07-JUN-2017, entry version 20. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:KFG90160.1}; GN ORFNames=BV98_002105 {ECO:0000313|EMBL:KFG90160.1}; OS Sphingobium herbicidovorans (strain ATCC 700291 / DSM 11019 / NBRC OS 16415 / MH) (Sphingomonas herbicidovorans). OC Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales; OC Sphingomonadaceae; Sphingobium. OX NCBI_TaxID=1219045 {ECO:0000313|EMBL:KFG90160.1, ECO:0000313|Proteomes:UP000024284}; RN [1] {ECO:0000313|EMBL:KFG90160.1, ECO:0000313|Proteomes:UP000024284} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NBRC 16415 {ECO:0000313|EMBL:KFG90160.1, RC ECO:0000313|Proteomes:UP000024284}; RA Gan H.M., Gan H.Y., Savka M.A.; RT "Draft genome sequences of Sphingobium herbicidovorans."; RL Submitted (AUG-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KFG90160.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JFZA02000015; KFG90160.1; -; Genomic_DNA. DR RefSeq; WP_037465759.1; NZ_JFZA02000015.1. DR EnsemblBacteria; KFG90160; KFG90160; BV98_002105. DR PATRIC; fig|1219045.3.peg.2146; -. DR Proteomes; UP000024284; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0016810; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds; IEA:InterPro. DR CDD; cd01878; HflX; 1. DR Gene3D; 2.30.40.10; -; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR011059; Metal-dep_hydrolase_composite. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 2. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000024284}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}. FT DOMAIN 209 390 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 444 AA; 48553 MW; 63EC566F5BBEE078 CRC64; MAVFNRDSDD EVSRGARAVV VRAETHGMER RDSDARLEEA KGLALAIGID VRAAQAFRVR DRKPATLFGS GQVDQIATLA RAEQAELVIV DNALSPVQQS NLEKATEAKV IDRTGLILEI FGERAATNEG RLQVELAHLD YQAGRLVRSW THLERQRGGF GFLGGPGETQ IEADRRMIRD RMAKIRRELD QVTRTRSLHR ARRQRAPWPV IALVGYTNAG KSTLFNRMTG AHVMAEDLLF ATLDPTMRQI ALPGLDKAIL SDTVGFVSDL PTQLIAAFRA TLEEVLSADL IIHVRDIAHP DSDAQRDDVI DVLSELGLAG EGALEGGEDA VEPPPIIEAW NKLDLLDDDA AALVREMAAR RDDVVILSAL TGEGVDDLQR KISSRLTAGA QVHQLHVSLS DGAALAWLHE HGEVIGSHAA EGDMVVDVRL SESALARFRK RADD // ID A0A086XYX5_9RHOB Unreviewed; 427 AA. AC A0A086XYX5; DT 29-OCT-2014, integrated into UniProtKB/TrEMBL. DT 29-OCT-2014, sequence version 1. DT 07-JUN-2017, entry version 18. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=CG50_00320 {ECO:0000313|EMBL:KFI27225.1}; OS Paenirhodobacter enshiensis. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae; Paenirhodobacter. OX NCBI_TaxID=1105367 {ECO:0000313|EMBL:KFI27225.1, ECO:0000313|Proteomes:UP000028824}; RN [1] {ECO:0000313|EMBL:KFI27225.1, ECO:0000313|Proteomes:UP000028824} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DW2-9 {ECO:0000313|EMBL:KFI27225.1, RC ECO:0000313|Proteomes:UP000028824}; RA Wang D., Wang G.; RT "Genome of Paenirhodobacter enshiensis DW2-9."; RL Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KFI27225.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JFZB01000010; KFI27225.1; -; Genomic_DNA. DR RefSeq; WP_036636824.1; NZ_JFZB01000010.1. DR EnsemblBacteria; KFI27225; KFI27225; CG50_00320. DR Proteomes; UP000028824; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000028824}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000028824}. FT DOMAIN 207 376 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 427 AA; 47725 MW; D63B76B2EFCF4AD0 CRC64; MSAPVSSQAR PTRAYVLHPD LRSAEARREP ELRLAEAVSL AAALPDMEVV GHEVVRLPKP NAGHLFGSGK LEELKERLSA AEVDLVLVDG PVTPVQQRNL EKDWGVKLLD RTGLILEIFA DRARTREGVL QVELAALSYQ RTRLVRAWTH LERQRGGFGF VGGPGETQIE ADRRAIDEQV IRIRRQLSKV VKTRELHRAA RRKVPFPIVA LVGYTNAGKS TLFNRMTGAE VLAKDMLFAT LDPTMRGVTL ASGRKIILSD TVGFISDLPH ELVAAFRATL EEVLEADLIL HVRDISHPET EEQAEDVAEI LDSLGVDEDV PMIEVWNKID ALSQPMRDAL LVQDARKTTI QAVSALTGEG VPALVSAIEA QLAEERHREE LLVPFDEGRR RAWLHEHNVV RTERETKEGW VLDVEWTGTQ RARYRAL // ID A0A086YC58_9RHOB Unreviewed; 417 AA. AC A0A086YC58; DT 29-OCT-2014, integrated into UniProtKB/TrEMBL. DT 29-OCT-2014, sequence version 1. DT 12-APR-2017, entry version 16. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=CN97_05430 {ECO:0000313|EMBL:KFI31858.1}; OS Haematobacter massiliensis. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae; Haematobacter. OX NCBI_TaxID=195105 {ECO:0000313|EMBL:KFI31858.1, ECO:0000313|Proteomes:UP000028826}; RN [1] {ECO:0000313|EMBL:KFI31858.1, ECO:0000313|Proteomes:UP000028826} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CCUG 47968 {ECO:0000313|EMBL:KFI31858.1, RC ECO:0000313|Proteomes:UP000028826}; RA Wang D., Wang G.; RT "Genome of Haematobacter massiliensis CCUG 47968."; RL Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KFI31858.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JGYG01000001; KFI31858.1; -; Genomic_DNA. DR EnsemblBacteria; KFI31858; KFI31858; CN97_05430. DR Proteomes; UP000028826; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000028826}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000028826}. FT DOMAIN 197 366 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 417 AA; 45894 MW; 74805A0ACC34C777 CRC64; MVHPDIKGAA SGRDGGERLP EHRLAEAVAL AAALPGLEVI GADVVRLPKV APGKLFGSGK VEELAELFKA QEIGLVLIDG PVTPVQQRNL EKAWGVKLLD RTGLILEIFA DRARTREGVL QVELAALSYQ RTRLVRAWTH LERQRGGLGF VGGPGETQIE ADRRAIDEAV TRIRRQLAKV VKTRELHRAA RRKVPYPIVA LVGYTNAGKS TLFNRMTGAE VLAKDMLFAT LDPTMRGVTL PSGREVILSD TVGFISDLPT QLVAAFRATL EEVLEADLIL HVRDISHPET EAQKADVEGI LAELGVREET PMLEVWNKID QLLPEQREVV EVLAARTPNV FVASALTGEG LGPLLAAVSE RLSEERTVRD LVLPFEDGRR RAWLHEQNVV ESEAPGEEGW HITVLWTARQ RAQYDAL // ID A0A086YUY6_9FIRM Unreviewed; 424 AA. AC A0A086YUY6; DT 29-OCT-2014, integrated into UniProtKB/TrEMBL. DT 29-OCT-2014, sequence version 1. DT 10-MAY-2017, entry version 18. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=DK28_0214305 {ECO:0000313|EMBL:KFD42109.1}; OS Peptococcaceae bacterium SCADC1_2_3. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Peptococcaceae. OX NCBI_TaxID=1487582 {ECO:0000313|EMBL:KFD42109.1, ECO:0000313|Proteomes:UP000027084}; RN [1] {ECO:0000313|EMBL:KFD42109.1, ECO:0000313|Proteomes:UP000027084} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SCADC1_2_3 {ECO:0000313|EMBL:KFD42109.1}; RA Tan B.F., Charchuk R., Li C., Nesbo C., Abu-Laban N., Foght J.; RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:KFD42109.1, ECO:0000313|Proteomes:UP000027084} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SCADC1_2_3 {ECO:0000313|EMBL:KFD42109.1}; RA Tan B., Charchuk R., Li C., Nesbo C., Abu-Laban N., Foght J.; RT "Draft genome sequence of an unculturable Firmicutes affiliated with RT Peptococcaceae sorted using a microfluidic device from methanogenic RT alkane-degrading cultures."; RL Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KFD42109.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JJNX02000008; KFD42109.1; -; Genomic_DNA. DR EnsemblBacteria; KFD42109; KFD42109; DK28_0214305. DR Proteomes; UP000027084; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000027084}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000027084}. FT DOMAIN 199 371 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 165 195 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 424 AA; 47002 MW; C1612479E0DA966A CRC64; MMEMEEEKAF IVAVDLPAKD RWPVEESLAE LARLVVSAGA TVVGKAVQKQ IKPHPATFLG QGKVQEIAHL CRELKAELLI IGQELSPAQK KNLEEAMQVR VIDRVQLILD IFAQRARTSE GKIQVELAQL NYLLPRLTGL GTELSRLGGG IGTRGPGETK LEVDRRRIYR RIAILKRELK EVQRHRTLLR QARQKIPIPL VALVGYTNAG KSTLLNTLTA AGVLVEDKLF ATLDPTTRQV ILPNNETILL TDTVGFIHRL PLHLVAAFRA TLEEVVEADL ILHLVDAAAA ANNQAQIAVV EDILSSLGVQ DKPTILVYNK IDELNQEKSL PGIEDNLFTY KDVPTAAISA LTGQGIKTLL ELIAQVLAAK RVCITLFIPY HKSSILSLLH QKGQVLKEEY RADGTMVKVD LEEVWAKRVE AWLK // ID A0A086YZQ6_9BIFI Unreviewed; 509 AA. AC A0A086YZQ6; DT 29-OCT-2014, integrated into UniProtKB/TrEMBL. DT 29-OCT-2014, sequence version 1. DT 12-APR-2017, entry version 18. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=BACT_0456 {ECO:0000313|EMBL:KFI39756.1}; OS Bifidobacterium actinocoloniiforme DSM 22766. OC Bacteria; Actinobacteria; Bifidobacteriales; Bifidobacteriaceae; OC Bifidobacterium. OX NCBI_TaxID=1437605 {ECO:0000313|EMBL:KFI39756.1, ECO:0000313|Proteomes:UP000029015}; RN [1] {ECO:0000313|EMBL:KFI39756.1, ECO:0000313|Proteomes:UP000029015} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 22766 {ECO:0000313|EMBL:KFI39756.1, RC ECO:0000313|Proteomes:UP000029015}; RA Ventura M., Milani C., Lugli G.A.; RT "Genomics of Bifidobacteria."; RL Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KFI39756.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JGYK01000001; KFI39756.1; -; Genomic_DNA. DR EnsemblBacteria; KFI39756; KFI39756; BACT_0456. DR Proteomes; UP000029015; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000029015}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000029015}. FT DOMAIN 286 452 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 509 AA; 55587 MW; 0E561C45371C8E22 CRC64; MTQESEQSKA AQAFQTDGEW QDTRADAPLH GRSQVLLDQG QSGPEEGEAD EAWQERERRN QFKHVEGLGE LEDVSEVEYR KVRLERVVLV GVYSSASSSL ETAEESLREL AALAQTAGAE VLDGLLQQRD KPDPATYIGS GKARQLADVV ASQEADTIIV DDDLQPSQRR ALEDATKVKV VDRTALILDI FAQHASSREG KAQVELAQLE YMLPRLRGWG GSLSRQAGGQ AAGQSGGIGS RGPGETKIET DRRVIRHRIS RLKRQIKQMA PAREVKRGSR RRYELPTVAV VGYTNAGKSS LINRMTGSKE LVENALFATL DTAVRRARAR DGRLYALVDT VGFVRRLPTQ LVEAFKSTLE EVGQADVIVH VVDGSHPDPF SQIEAVDKVL ATIPGAEGIA RVLVFNKADL MDPSTRQRIG RLEPDAFLVS AGTGEGVEAL SERVEAMLPK PHVRVEARLP YASGSLLSRV RQYGKVLSVS YRGDGVDLVA DVDDRLAAQI MSQAIEPDG // ID A0A086ZGH3_9BIFI Unreviewed; 517 AA. AC A0A086ZGH3; DT 29-OCT-2014, integrated into UniProtKB/TrEMBL. DT 29-OCT-2014, sequence version 1. DT 12-APR-2017, entry version 18. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=BBOH_0964 {ECO:0000313|EMBL:KFI45623.1}; OS Bifidobacterium bohemicum DSM 22767. OC Bacteria; Actinobacteria; Bifidobacteriales; Bifidobacteriaceae; OC Bifidobacterium. OX NCBI_TaxID=1437606 {ECO:0000313|EMBL:KFI45623.1, ECO:0000313|Proteomes:UP000029096}; RN [1] {ECO:0000313|EMBL:KFI45623.1, ECO:0000313|Proteomes:UP000029096} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 22767 {ECO:0000313|EMBL:KFI45623.1, RC ECO:0000313|Proteomes:UP000029096}; RA Ventura M., Milani C., Lugli G.A.; RT "Genomics of Bifidobacteria."; RL Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KFI45623.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JGYP01000002; KFI45623.1; -; Genomic_DNA. DR EnsemblBacteria; KFI45623; KFI45623; BBOH_0964. DR Proteomes; UP000029096; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000029096}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000029096}. FT DOMAIN 297 463 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 517 AA; 55820 MW; 22E254E10B16108E CRC64; MVLCLPTATI HGGRARGKVD VLTNDDRLEA GNDEVLGRRS DILQDQGARS PADMDGFSAG AEQWSERESR NQLRRVVGLG EMQDEGDVEY RKVRLERVVL VGVWSRNETT LEKAEESLRE LAALANTAGA QVCDGVLQHR LKPDAATYVG RGKTKEIEGI VARHEADTII VDGDLAPSQR RALEDATKVK VVDRTAVILD IFAQHATSRE GKAQVELAQL EYMLPRLRGW GGSLSRQAGG QAAGVNGGIG SRGPGETQIE MDRRVIRTRI ARLKKQIRAM APARDVKRGS RRRLGLPTVA VVGYTNAGKS SLVNRLTGSG ELVENALFAT LDTAVRRAKA HDGRFYAYVD TVGFVRSLPT QLVEAFKSTL EEVAGADVIV HVVDASTADP FAQIEAVNRV LADIDGVEGI PRVLVFNKVD QVDASTVGRL ANMRPEALFV SAASGEGLDR LRDAVESLLP APEIHVSALL PYSAGGLLSE VREYGKVQKV EYRTEGVALE ADVDSRLAAR VLDSAVG // ID A0A087A567_9BIFI Unreviewed; 508 AA. AC A0A087A567; DT 29-OCT-2014, integrated into UniProtKB/TrEMBL. DT 29-OCT-2014, sequence version 1. DT 07-JUN-2017, entry version 20. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=BBIA_1265 {ECO:0000313|EMBL:KFI53917.1}; OS Bifidobacterium biavatii DSM 23969. OC Bacteria; Actinobacteria; Bifidobacteriales; Bifidobacteriaceae; OC Bifidobacterium. OX NCBI_TaxID=1437608 {ECO:0000313|EMBL:KFI53917.1, ECO:0000313|Proteomes:UP000029108}; RN [1] {ECO:0000313|EMBL:KFI53917.1, ECO:0000313|Proteomes:UP000029108} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 23969 {ECO:0000313|EMBL:KFI53917.1, RC ECO:0000313|Proteomes:UP000029108}; RA Ventura M., Milani C., Lugli G.A.; RT "Genomics of Bifidobacteria."; RL Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KFI53917.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JGYN01000001; KFI53917.1; -; Genomic_DNA. DR RefSeq; WP_033495109.1; NZ_JGYN01000001.1. DR EnsemblBacteria; KFI53917; KFI53917; BBIA_1265. DR Proteomes; UP000029108; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000029108}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000029108}. FT DOMAIN 288 454 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 508 AA; 55278 MW; D23EB1E8077E0EDD CRC64; MSEQSQQSAS EKTVVNQPIA EEGPALTGVL ADQSDVLLDA HDRGVASSEQ SNEAWEERES RNQLKHVAGL GELQDVTEVE YRKVRLERVV LVGVWSSATT TAAAAEESLR ELAALAETAG AVVCDGLLQH RYRPDAATYV GSGKAREIAD IVAREEADTI IVDDDLPPSQ RRALEDATKV KVVDRTAVIL DIFAQHATSR EGKAQVELAQ LEYMLPRLRG WGGSLSRQAG GRAAGADAGI GSRGPGETKI EMDRRVIRTR IARLRKQIRD MAPAREVKRG SRRRYGLPTV AVVGYTNAGK SSLTNRLTGS AELVENALFA TLDTAVRRAR AKDGRLYAYV DTVGFVRRLP TQLIEAFKST LEEVAEADLI VHVVDGSHPD PFSQIDAVND VLADIDGAAD IPRILVFNKA DRMDEATRER ILALEPDAYV VSAFSGEGID GLRDRIESML PVPNVHVQAL LPYSAGSLLS KIREYGHVIN VEYRDDGMMV EAEVGSRLAA QVVEQAID // ID A0A087A9N7_9BIFI Unreviewed; 502 AA. AC A0A087A9N7; DT 29-OCT-2014, integrated into UniProtKB/TrEMBL. DT 29-OCT-2014, sequence version 1. DT 12-APR-2017, entry version 18. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=BCAL_0745 {ECO:0000313|EMBL:KFI55487.1}; OS Bifidobacterium callitrichos DSM 23973. OC Bacteria; Actinobacteria; Bifidobacteriales; Bifidobacteriaceae; OC Bifidobacterium. OX NCBI_TaxID=1437609 {ECO:0000313|EMBL:KFI55487.1, ECO:0000313|Proteomes:UP000029072}; RN [1] {ECO:0000313|EMBL:KFI55487.1, ECO:0000313|Proteomes:UP000029072} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 23973 {ECO:0000313|EMBL:KFI55487.1, RC ECO:0000313|Proteomes:UP000029072}; RA Ventura M., Milani C., Lugli G.A.; RT "Genomics of Bifidobacteria."; RL Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KFI55487.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JGYS01000005; KFI55487.1; -; Genomic_DNA. DR EnsemblBacteria; KFI55487; KFI55487; BCAL_0745. DR Proteomes; UP000029072; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000029072}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000029072}. FT DOMAIN 282 448 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 502 AA; 54588 MW; 429AB70E80146210 CRC64; MTRDAESMGK YEDRTEGDEH GDVLAEASEV LIDEGGGSAP WAESHDEAWE ERESRNQLKH VAGLGELQDV TEVEYRKVRL ERVVLVGVWS SALTTQAKAE ESLRELAALA ETAGAVVCDG LLQHRIKPDA ATYVGSGKAK EIADIVAREE ADTIVVDDDL PPSQRRGLED AAKVKVVDRT AVILDIFAQH ATSREGKAQV ELAQLEYMLP RLRGWGGSLS RQAGGRAAGA DAGIGSRGPG ETKIEMDRRV IRTRIARLRR QIREMAPARE VKRGSRRRYG LPTIAVVGYT NAGKSSLTNR LTGSSELVEN ALFATLDTAV RRAKARDGRL YAYVDTVGFV RRLPTQLVEA FKSTLEEVGE ADVILHVVDG SHPDPFSQID AVNEVLADIE GAESIPRLLV FNKADRCDEA TLERLAALEP DAHIVSAYSG RGLDELRDAV EALLPTPGVH VEALLPYSAG SLLSQVREYG HVDSIEWLAE GVKVVADVDS RLAARLVERS VG // ID A0A087AR83_9BIFI Unreviewed; 510 AA. AC A0A087AR83; DT 29-OCT-2014, integrated into UniProtKB/TrEMBL. DT 29-OCT-2014, sequence version 1. DT 12-APR-2017, entry version 17. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=BIGA_0720 {ECO:0000313|EMBL:KFI61283.1}; OS Bifidobacterium gallinarum. OC Bacteria; Actinobacteria; Bifidobacteriales; Bifidobacteriaceae; OC Bifidobacterium. OX NCBI_TaxID=78344 {ECO:0000313|EMBL:KFI61283.1, ECO:0000313|Proteomes:UP000029046}; RN [1] {ECO:0000313|EMBL:KFI61283.1, ECO:0000313|Proteomes:UP000029046} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=LMG 11586 {ECO:0000313|EMBL:KFI61283.1, RC ECO:0000313|Proteomes:UP000029046}; RA Ventura M., Milani C., Lugli G.A.; RT "Genomics of Bifidobacteria."; RL Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KFI61283.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JGYX01000002; KFI61283.1; -; Genomic_DNA. DR EnsemblBacteria; KFI61283; KFI61283; BIGA_0720. DR Proteomes; UP000029046; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000029046}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000029046}. FT DOMAIN 290 456 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 510 AA; 55110 MW; A19E5AE93BD32BAA CRC64; MGGCLTELNE AMIDSGQASA EDGRPDARRD VLSEQSEVLL DDDRRGSGAA ADSDELWEER EGRNALRHVV GLGEMQDVTE VEYRKVRLER VVLVGVWSSA VTTQAQAEES LRELAALAET AGAEVCDGLL QHRYRPDAAT YVGSGKAKEI AGIVAREEAD TIIVDDDLPP SQRRALEDVT KVKVVDRTAV ILDIFAQHAT SREGKAQVEL AQLQYMLPRL RGWGASLSRQ AGGRAAGADG GIGSRGPGET KIEMDRRVIR NRIARLRKQI AQMAPTRDVK RGSRRRFGLP TVAVVGYTNA GKSSLTNRLT GSAELVENAL FATLDTAVRR ARAKDGRLYA YVDTVGFVRR LPTQLIEAFK STLEEVGEAD LILHVVDGSH PDPFSQIDAV NEVLSDIEGV GNIPVVIAFN KADMMDEAAR ERIAALAPEA HIVSAATGEG IEALRTQVES MLPTPNVHVS ALLPYTAGSL LSRVREYGKV ESVEYRGDGV MLEAEVDGVL AAQIVEQSIG // ID A0A087B3E7_9BIFI Unreviewed; 507 AA. AC A0A087B3E7; DT 29-OCT-2014, integrated into UniProtKB/TrEMBL. DT 29-OCT-2014, sequence version 1. DT 07-JUN-2017, entry version 20. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=BCUN_0040 {ECO:0000313|EMBL:KFI65547.1}; OS Bifidobacterium cuniculi. OC Bacteria; Actinobacteria; Bifidobacteriales; Bifidobacteriaceae; OC Bifidobacterium. OX NCBI_TaxID=1688 {ECO:0000313|EMBL:KFI65547.1, ECO:0000313|Proteomes:UP000029067}; RN [1] {ECO:0000313|EMBL:KFI65547.1, ECO:0000313|Proteomes:UP000029067} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=LMG 10738 {ECO:0000313|EMBL:KFI65547.1, RC ECO:0000313|Proteomes:UP000029067}; RA Ventura M., Milani C., Lugli G.A.; RT "Genomics of Bifidobacteria."; RL Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KFI65547.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JGYV01000001; KFI65547.1; -; Genomic_DNA. DR RefSeq; WP_051920381.1; NZ_JGYV01000001.1. DR EnsemblBacteria; KFI65547; KFI65547; BCUN_0040. DR Proteomes; UP000029067; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000029067}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000029067}. FT DOMAIN 287 454 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 507 AA; 55376 MW; 1B541B33F01E720B CRC64; MPLNQTATAM PNPRYLTHDE DPHGQPSDDA DVLAGQSQVL LEEADAADLR DEEWDERESR NQLKHVTGLG ELEDVTEVEY RKVRLERVVL VGVWSSRDSS QREAEESLRE LAALADTAGA QVCDAVLQHR SRPDAATYVG SGKAKEIAQL VEACDADTIV VDADLPPSQR RALEDVTRVK VVDRTAVILD IFAQHATSRE GKAQVELAQL QYMLPRLRGW GAALSRQAGG RAAGADGGIG SRGPGETQIE LDRRVIRTRI ARLRRQIAQM APTREVKRGS RRRNGVPSIA VVGYTNAGKS SLTNRLTGSD ELVENALFAT LDTAVRRARS ADGRRYTYVD TVGFVRRLPT QLVEAFKSTL EETADADIVL HVVDASHPDP FGQIEAVNTV LKDVEGADRL PTVTVFNKID LLDDTALARL RNLAPDAHFV SSATGEGLDR LRDALEAMLP VPAVHIEALM PYTAGSLLSK VRELGEVTSM EYRDDGVMLV ADVDEHLAAQ LMEHAIG // ID A0A087BDV7_9BIFI Unreviewed; 520 AA. AC A0A087BDV7; DT 29-OCT-2014, integrated into UniProtKB/TrEMBL. DT 29-OCT-2014, sequence version 1. DT 12-APR-2017, entry version 18. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=BMAGN_0972 {ECO:0000313|EMBL:KFI69207.1}; OS Bifidobacterium magnum. OC Bacteria; Actinobacteria; Bifidobacteriales; Bifidobacteriaceae; OC Bifidobacterium. OX NCBI_TaxID=1692 {ECO:0000313|EMBL:KFI69207.1, ECO:0000313|Proteomes:UP000029052}; RN [1] {ECO:0000313|EMBL:KFI69207.1, ECO:0000313|Proteomes:UP000029052} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=LMG 11591 {ECO:0000313|EMBL:KFI69207.1, RC ECO:0000313|Proteomes:UP000029052}; RA Ventura M., Milani C., Lugli G.A.; RT "Genomics of Bifidobacteria."; RL Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KFI69207.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JGZB01000002; KFI69207.1; -; Genomic_DNA. DR EnsemblBacteria; KFI69207; KFI69207; BMAGN_0972. DR Proteomes; UP000029052; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000029052}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000029052}. FT DOMAIN 300 466 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 520 AA; 57321 MW; B1A6685E2E56C1E3 CRC64; MSLQAMIIRH REFYILYKAI VRCLWGQLVS IERDDEVRGG GVLAGQSEVL LADRDDHDLF TPGNEQWEER ESRNELKHVT GLGELQDVTE VEYRKVRLER VVLVGVWSRR ETTQAEAEES LRELSALAQT AGAVVCDGVL QQRYRPDAAT YVGSGKAREI ANIVAANEAD TIIVDDDLAP SQRRALEDAA KVKVVDRTAV ILDIFAQHAS SKEGKAQVEL AQLQYMLPRL RGWGASLSRQ AGGRAAGADA GIGSRGPGET KIEMDRRVIR NRIAKLRRDI AHMEPSRAIK RGSRNRNGMP TVAVVGYTNA GKSSLTNRLT GSRELVENAL FATLDTAVRA ASTPEGRRYA YVDTVGFVRR LPIQLVEAFK STLEEVGEAD LIVHVVDMSY PDPFSQIDSV NETLQSIEHV GDIPSLLVMN KADLVDEETR ERLHRLAPDA FIVSSATGEG IDELKAAVEA MLPQPSVHVD ALLPYTAGSL VEKIRLDGRV LDIEYRDDGV RVQAFVDDHL SARIMESAIG // ID A0A087BPX5_9BIFI Unreviewed; 524 AA. AC A0A087BPX5; DT 29-OCT-2014, integrated into UniProtKB/TrEMBL. DT 29-OCT-2014, sequence version 1. DT 12-APR-2017, entry version 17. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=BMIN_0798 {ECO:0000313|EMBL:KFI73075.1}; OS Bifidobacterium minimum. OC Bacteria; Actinobacteria; Bifidobacteriales; Bifidobacteriaceae; OC Bifidobacterium. OX NCBI_TaxID=1693 {ECO:0000313|EMBL:KFI73075.1, ECO:0000313|Proteomes:UP000029014}; RN [1] {ECO:0000313|EMBL:KFI73075.1, ECO:0000313|Proteomes:UP000029014} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=LMG 11592 {ECO:0000313|EMBL:KFI73075.1, RC ECO:0000313|Proteomes:UP000029014}; RA Ventura M., Milani C., Lugli G.A.; RT "Genomics of Bifidobacteria."; RL Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KFI73075.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JGZD01000008; KFI73075.1; -; Genomic_DNA. DR EnsemblBacteria; KFI73075; KFI73075; BMIN_0798. DR Proteomes; UP000029014; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000029014}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000029014}. FT DOMAIN 304 471 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 524 AA; 57153 MW; 71FB4501E1F76EFA CRC64; MDHTFDNQRQ DFPSEGRGAM NDDDAVRGGP GDGGGVDRVD AAHEDVLSGR SQVLLDRSAT GARSDAGQEE WREREARNQF KHVEGLGELQ DVTEVEYRRL RLERVVLVGV WSSATGTLEQ AEESLRELAA LAQTAGAVVC DGLLQQRYRP DAATYVGSGK AKELAGIVAT NEADTIIVDD DMAPSQRRAL EDATKVKVVD RTAVILDIFA QHATSREAKA QVELAQLEYM LPRLRGWGGS LSRQAGGRAA GADAGIGSRG PGETKIEMDR RVIRTRIARL RRQIAQMAPA RDVKRGSRRR HDLPTVAVVG YTNAGKSSLT NRLTGSGELV ENALFATLDT AVRRADSHDG RAYAYVDTVG FVRRLPTQLV EAFKSTLEEV AEADIIIHVV DASHPDPLGQ IDAVNEVLED IEGVEEIPRV LVFNKIDMVD STVRTRLSSL KPEARLVSAY SGEGIDALRR EVEKILPVPD VHVGGLLPYA AGGLVAQARR FGRVDSVEYR DDGMWLEADV TPVLAARIVR ECRD // ID A0A087BUW6_9BIFI Unreviewed; 497 AA. AC A0A087BUW6; DT 29-OCT-2014, integrated into UniProtKB/TrEMBL. DT 29-OCT-2014, sequence version 1. DT 07-JUN-2017, entry version 20. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=BMON_1359 {ECO:0000313|EMBL:KFI74816.1}; OS Bifidobacterium mongoliense DSM 21395. OC Bacteria; Actinobacteria; Bifidobacteriales; Bifidobacteriaceae; OC Bifidobacterium. OX NCBI_TaxID=1437603 {ECO:0000313|EMBL:KFI74816.1, ECO:0000313|Proteomes:UP000029082}; RN [1] {ECO:0000313|EMBL:KFI74816.1, ECO:0000313|Proteomes:UP000029082} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 21395 {ECO:0000313|EMBL:KFI74816.1, RC ECO:0000313|Proteomes:UP000029082}; RA Ventura M., Milani C., Lugli G.A.; RT "Genomics of Bifidobacteria."; RL Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KFI74816.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JGZE01000021; KFI74816.1; -; Genomic_DNA. DR RefSeq; WP_033513144.1; NZ_JGZE01000021.1. DR EnsemblBacteria; KFI74816; KFI74816; BMON_1359. DR Proteomes; UP000029082; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000029082}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000029082}. FT DOMAIN 277 443 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 497 AA; 54218 MW; 2CBF035E7699A825 CRC64; MTQEFDTDHS HDEEANQGVL ADRSEVLLDQ SQGAAAGERS QEDWAERESR NALRHVVGLG EMQDVSEVEY RKVRLERVVL VGVWSSATGS LAQTEESLRE LAALAQTAGA DVCDGVLQQR YKPDAATYVG SGKAREIAGI VAQQSADTIV VDDDLAPSQR RALEDLTKVK VVDRTAVILD IFAQHATSRE GKAQVELAQL QYMLPRLRGW GASLSRQAGG RAAGADAGIG SRGPGETKIE MDRRVIRTRI ARLRRQIARM AAAREVKRGS RHRYGLPTVA VVGYTNAGKS SLINRLTGSS ELVENALFAT LDTAVRSAKT SQGRLYAYVD TVGFVRRLPT QLIEAFKSTL EEVVEADLIV HVVDASHAEP LAQIDAVNEV LAGIDGTDDI PRLLVLNKVD RIDDDRRARL ASLKPQAMLV SSRSGEGIDA LRADIEARLP APRVKVEATL PYDQGSLISR IREYGRPESI EYREDGIHIV AQVDDRLAAA VVEHSID // ID A0A087CE45_9BIFI Unreviewed; 524 AA. AC A0A087CE45; DT 29-OCT-2014, integrated into UniProtKB/TrEMBL. DT 29-OCT-2014, sequence version 1. DT 07-JUN-2017, entry version 19. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=BPSY_1954 {ECO:0000313|EMBL:KFI81545.1}; OS Bifidobacterium psychraerophilum. OC Bacteria; Actinobacteria; Bifidobacteriales; Bifidobacteriaceae; OC Bifidobacterium. OX NCBI_TaxID=218140 {ECO:0000313|EMBL:KFI81545.1, ECO:0000313|Proteomes:UP000029050}; RN [1] {ECO:0000313|EMBL:KFI81545.1, ECO:0000313|Proteomes:UP000029050} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=LMG 21775 {ECO:0000313|EMBL:KFI81545.1, RC ECO:0000313|Proteomes:UP000029050}; RA Ventura M., Milani C., Lugli G.A.; RT "Genomics of Bifidobacteria."; RL Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KFI81545.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JGZI01000010; KFI81545.1; -; Genomic_DNA. DR EnsemblBacteria; KFI81545; KFI81545; BPSY_1954. DR Proteomes; UP000029050; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000029050}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000029050}. FT DOMAIN 304 471 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 524 AA; 57224 MW; 3E5C66CFCE34A2E6 CRC64; MTQRLPADSF AQNHDHNTED GGAADHAVTA GVLRAGHDVE RRPQSEPLQE QSEVLLDGRR DDQDERSRQE WVERQQRNEL KHVAGLGELQ DVTEVEYRKL RLERVVLVGV WSSATSSLAQ AEESLRELSA LAQTAGAEVL DGLLQHRNVP DRATYVGSGK AYELAGIVAK LEADTIIVDD DLPPSQRRAL EDATKVKVVD RTAVILDIFA QHATSREGKA QVELAQLEYM LPRLRGWGAS LSRQAGGQAA GQAGGIGSRG PGETKIEMDR RVIRTRIAKL RRQIRQMAPA RDVKRGSRRR FGMPTIAVVG YTNAGKSSLT NRLTGSGELV ENALFATLDT AVRRAQTPDG RYYAYVDTVG FVRRLPTQLV EAFKSTLEEV AAADLIIHVV DGSHPDPFSQ IDAVNTVLTD IPGAESIPRI IVFNKADRIS EVQRERLKQL DAGSFVVSAQ SGYGLAALRE AVESKLPVPD VHVHALLPYT SGSLVSQIRE YGKVSSVEYT NDGILVDADV DSRTAALIVD QAAD // ID A0A087CSC6_9BIFI Unreviewed; 501 AA. AC A0A087CSC6; DT 29-OCT-2014, integrated into UniProtKB/TrEMBL. DT 29-OCT-2014, sequence version 1. DT 07-JUN-2017, entry version 20. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=BREU_1345 {ECO:0000313|EMBL:KFI86176.1}; OS Bifidobacterium reuteri DSM 23975. OC Bacteria; Actinobacteria; Bifidobacteriales; Bifidobacteriaceae; OC Bifidobacterium. OX NCBI_TaxID=1437610 {ECO:0000313|EMBL:KFI86176.1, ECO:0000313|Proteomes:UP000028984}; RN [1] {ECO:0000313|EMBL:KFI86176.1, ECO:0000313|Proteomes:UP000028984} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 23975 {ECO:0000313|EMBL:KFI86176.1, RC ECO:0000313|Proteomes:UP000028984}; RA Ventura M., Milani C., Lugli G.A.; RT "Genomics of Bifidobacteria."; RL Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KFI86176.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JGZK01000005; KFI86176.1; -; Genomic_DNA. DR RefSeq; WP_044088763.1; NZ_JGZK01000005.1. DR EnsemblBacteria; KFI86176; KFI86176; BREU_1345. DR Proteomes; UP000028984; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000028984}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000028984}. FT DOMAIN 281 447 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 501 AA; 54520 MW; 614A0D084F1679B6 CRC64; MSEHNQYTDI DHGSSSITSQ GVLSAQSDVL LDTTQQPSGW HEDANQEWEE REARNELKHV AGLGELEDVT EVEYRKVRLE RVVLVGVWSS AVTTQTKAEE SLRELAALAE TAGAVVCDGL LQHRLKPDAA TYVGSGKARE IADIVAREEA DTIIVDDDLA PSQRRALEDA AKVKVVDRTA VILDIFAQHA TSREGKAQVE LAQLEYMLPR LRGWGGSLSR QAGGRAAGAD AGIGSRGPGE TKIEMDRRVI RTRIARLRRQ IRDMAPAREI KRGSRRRYGL PTVAVVGYTN AGKSSLTNRL TGSTELVENA LFATLDTAVR RAKTHDGRLY AYVDTVGFVR RLPTQLVEAF KSTLEEVAES DVIVHVVDGS HPDPFSQIDA VNAVLADIEG TASIPRIVVF NKADQVDAVT RERLMALQPD AYIVSAYSGE GVDGLRAAVE ALLPVPHVHV NAVLPYSAGS LLSRVREYGK VGKVEYRDDG VLLEADVDSH LAARVIDASI D // ID A0A087DCL5_9BIFI Unreviewed; 506 AA. AC A0A087DCL5; DT 29-OCT-2014, integrated into UniProtKB/TrEMBL. DT 29-OCT-2014, sequence version 1. DT 12-APR-2017, entry version 16. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=BSCA_1780 {ECO:0000313|EMBL:KFI93265.1}; OS Bifidobacterium scardovii. OC Bacteria; Actinobacteria; Bifidobacteriales; Bifidobacteriaceae; OC Bifidobacterium. OX NCBI_TaxID=158787 {ECO:0000313|EMBL:KFI93265.1, ECO:0000313|Proteomes:UP000029033}; RN [1] {ECO:0000313|EMBL:KFI93265.1, ECO:0000313|Proteomes:UP000029033} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=LMG 21589 {ECO:0000313|EMBL:KFI93265.1, RC ECO:0000313|Proteomes:UP000029033}; RA Ventura M., Milani C., Lugli G.A.; RT "Genomics of Bifidobacteria."; RL Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KFI93265.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JGZO01000013; KFI93265.1; -; Genomic_DNA. DR EnsemblBacteria; KFI93265; KFI93265; BSCA_1780. DR Proteomes; UP000029033; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000029033}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000029033}. FT DOMAIN 285 451 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 506 AA; 55121 MW; EAA76166292C49C3 CRC64; MTQSDTRADD IRSMQDEPVL TGVLADQSEV LLDEHDRSGA PGVPGGPGDE VWEERESRNA LKHVAGLGEL QDVTEVEYRK VRLERVVLVG VWSSAVTTAS AAEESLRELA ALAETAGAVV CDGLLQHRLR PDAATYVGSG KAKEIADVVA REEADTIIVD DDLPPSQRRA LEDATKVKVV DRTAVILDIF AQHATSREGK AQVELAQLEY MLPRLRGWGG SLSRQAGGRA AGADAGIGSR GPGETKIEMD RRVIRTRIAR LRKQIREMAP AREVKRGSRR RYELPTVAVV GYTNAGKSSL TNRLTGSAEL VENALFATLD TAVRRARAKD GRLYAYVDTV GFVRRLPTQL VEAFKSTLEE VAEADLIVHV VDGSHPDPFS QIDAVNDVLA DIDGAADIPR ILVFNKADRI DGVTRERLAA LEPDAHIVSA FTGEGIDALR ERVESMLPVP HVHVRALLPY TAGALVSRIR EYGHVIEVEY RDDGMMVEAE VGSRLAAQVM EQSIDE // ID A0A087DQT7_9BIFI Unreviewed; 479 AA. AC A0A087DQT7; DT 29-OCT-2014, integrated into UniProtKB/TrEMBL. DT 29-OCT-2014, sequence version 1. DT 12-APR-2017, entry version 18. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=BSTEL_0698 {ECO:0000313|EMBL:KFI97887.1}; OS Bifidobacterium stellenboschense. OC Bacteria; Actinobacteria; Bifidobacteriales; Bifidobacteriaceae; OC Bifidobacterium. OX NCBI_TaxID=762211 {ECO:0000313|EMBL:KFI97887.1, ECO:0000313|Proteomes:UP000029004}; RN [1] {ECO:0000313|EMBL:KFI97887.1, ECO:0000313|Proteomes:UP000029004} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 23968 {ECO:0000313|EMBL:KFI97887.1, RC ECO:0000313|Proteomes:UP000029004}; RA Ventura M., Milani C., Lugli G.A.; RT "Genomics of Bifidobacteria."; RL Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KFI97887.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JGZP01000011; KFI97887.1; -; Genomic_DNA. DR EnsemblBacteria; KFI97887; KFI97887; BSTEL_0698. DR Proteomes; UP000029004; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000029004}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000029004}. FT DOMAIN 259 425 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 479 AA; 51976 MW; 1E585B08A1F20F4A CRC64; MLAESSEVLL DEGNGAGWAE RHDEAWEERE SRNQLKHVAG LGELKDVTEV EYRKVRLERV VLVGVWSSAK TTQAKAEESL RELAALAETA GAEVCDGLLQ HRLKPDAATY VGSGKAREIA DIVAREEADT IVVDDDLPPS QRRGLEDAAK VKVVDRTAVI LDIFAQHATS REGKAQVELA QLEYMLPRLR GWGGSLSRQA GGRAAGADGG IGSRGPGETK IEMDRRVIRT RIARLKRQIR EMAPAREVKR GSRRRYGLPT IAVVGYTNAG KSSLTNRLTG STELVENALF ATLDTAVRRA KARDGRLYAY VDTVGFVRRL PTQLVEAFKS TLEEVAEADV ILHVVDGSHP DPFSQIDAVN EVLSGIDGAE SIPRVIAFNK ADMCDEATLE RLAALEPDAH IVSAFDGRGV DALRDAVESL LPVPNVHVDA LLPYTAGALL SQVREYGHVG SVEWRDDGVR VVADVDAHLA ARIVAVAVD // ID A0A087DTZ3_9BIFI Unreviewed; 501 AA. AC A0A087DTZ3; DT 29-OCT-2014, integrated into UniProtKB/TrEMBL. DT 29-OCT-2014, sequence version 1. DT 07-JUN-2017, entry version 19. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=BISU_2194 {ECO:0000313|EMBL:KFI98993.1}; OS Bifidobacterium subtile. OC Bacteria; Actinobacteria; Bifidobacteriales; Bifidobacteriaceae; OC Bifidobacterium. OX NCBI_TaxID=77635 {ECO:0000313|EMBL:KFI98993.1, ECO:0000313|Proteomes:UP000029055}; RN [1] {ECO:0000313|EMBL:KFI98993.1, ECO:0000313|Proteomes:UP000029055} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=LMG 11597 {ECO:0000313|EMBL:KFI98993.1, RC ECO:0000313|Proteomes:UP000029055}; RA Ventura M., Milani C., Lugli G.A.; RT "Genomics of Bifidobacteria."; RL Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KFI98993.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JGZR01000016; KFI98993.1; -; Genomic_DNA. DR RefSeq; WP_024463601.1; NZ_JGZR01000016.1. DR EnsemblBacteria; KFI98993; KFI98993; BISU_2194. DR Proteomes; UP000029055; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000029055}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000029055}. FT DOMAIN 281 448 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 501 AA; 54684 MW; D49983E00BFD46A2 CRC64; MTQQFTQQFE SDSNNDVSKA TGVLADRSEV LLDRSYDIPD ADQGGEEWAE RESRNALKHV TGLGELEDIT EVEYRKVRLE RVVLVGVWSS ATGTQSQAEE SLRELAALAE TAGAEVCEGM LQHRLKPDPA TYIGSGKAKE LAGIVAQHEA DTIIVDDDLA PSQRRALEDV AKVKVVDRTA VILDIFAQHA TSREGKAQVE LAQLQYMLPR LRGWGAALSR QAGGQAAGAD GGIGSRGPGE TQIELDRRVI RTRIARLRRQ IARMAPAREV KRGSRRRYGL PTVAVVGYTN AGKSSLTNRL TGSSELVENA LFATLDTAVR SARTKDGRVY AYVDTVGFVR RLPTQLVEAF KSTLEEVAQS DLIVHVVDAS YGDPLAQIDA VNEVLADIAG AQDIPRIIVF NKADHIDEAT RRRLSSLYPQ AHIVSSLSGE GVDALREEIE ALLPVPDVRV EAVLPYAQGS LLSRVREYGR LDAAEYRNDG VRIEARVDSR LASQIVEASI D // ID A0A087EJU5_9BIFI Unreviewed; 540 AA. AC A0A087EJU5; DT 29-OCT-2014, integrated into UniProtKB/TrEMBL. DT 29-OCT-2014, sequence version 1. DT 07-JUN-2017, entry version 18. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=BITS_0359 {ECO:0000313|EMBL:KFJ08046.1}; OS Bifidobacterium tsurumiense. OC Bacteria; Actinobacteria; Bifidobacteriales; Bifidobacteriaceae; OC Bifidobacterium. OX NCBI_TaxID=356829 {ECO:0000313|EMBL:KFJ08046.1, ECO:0000313|Proteomes:UP000029080}; RN [1] {ECO:0000313|EMBL:KFJ08046.1, ECO:0000313|Proteomes:UP000029080} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=JCM 13495 {ECO:0000313|EMBL:KFJ08046.1, RC ECO:0000313|Proteomes:UP000029080}; RA Ventura M., Milani C., Lugli G.A.; RT "Genomics of Bifidobacteria."; RL Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KFJ08046.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JGZU01000003; KFJ08046.1; -; Genomic_DNA. DR EnsemblBacteria; KFJ08046; KFJ08046; BITS_0359. DR Proteomes; UP000029080; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000029080}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000029080}. FT DOMAIN 320 486 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 540 AA; 59095 MW; ACFC1DC113750A6B CRC64; MRCLSYKSMI IMLRVYKQVQ QWAKRLREVA LKQQYGAIHG DDGREADGMG EMAGADGTEH DQGVLSGHSQ VLLDDGQDAS WDAGGQWQER ESRNTLKHVT GLGELQDVTE VEYRKVRLER VVLVGVWSSA TSSQQQAEES LRELAALAQT AGAVVCDGVL QHRYRPDAAT YVGSGKAKEI ADIVALNEAD TIIADDDLAP SQRRALEDAT KVKVVDRTAV ILDIFAQHAT SREGKAQVEL AQLQYMLPRL RGWGAALSRQ AGGRAAGADG GIGSRGPGET QIELDRRVIR TRIARLRRQI AQMAPARDVK RGSRRRFGLP TVAVVGYTNA GKSSLTNRLT GSSELVENAL FATLDTAVRR ARAKDGRLYA YVDTVGFVRR LPTQLVEAFK STLEEVADAD LIVHVVDGSH PDPFAQIDAV NDVLADIDGA EDIPRIVVFN KADRIDEATR ERLEALMPDA YVVSAFTGEG VDEVRHVVEG MLPTPDVYVE ALLPYTAGSL VSRVREYGQV ENIEYRDDGV MVHAYVDDHL AAQVIDASID // ID A0A087EPF0_9LACO Unreviewed; 423 AA. AC A0A087EPF0; DT 29-OCT-2014, integrated into UniProtKB/TrEMBL. DT 29-OCT-2014, sequence version 1. DT 07-JUN-2017, entry version 19. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:KOY75706.1}; GN ORFNames=JI66_03355 {ECO:0000313|EMBL:KFJ15151.1}, GN RZ71_01240 {ECO:0000313|EMBL:KOY75706.1}; OS Lactobacillus kunkeei. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; OC Lactobacillus. OX NCBI_TaxID=148814 {ECO:0000313|EMBL:KFJ15151.1, ECO:0000313|Proteomes:UP000029013}; RN [1] {ECO:0000313|EMBL:KFJ15151.1, ECO:0000313|Proteomes:UP000029013} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MP2 {ECO:0000313|EMBL:KFJ15151.1, RC ECO:0000313|Proteomes:UP000029013}; RA Olmos A., Aldea P., Henriquez P., Sanchez C., Rojas-Herrera M., RA Maracaja-Coutinho V., Trombert A.; RT "Improved Draft Genome Sequence of Lactobacillus kunkeei strain MP2 RT isolated from Chilean Apis Mellifera gut."; RL Submitted (AUG-2014) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:KOY75706.1, ECO:0000313|Proteomes:UP000037778} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=LAko {ECO:0000313|EMBL:KOY75706.1, RC ECO:0000313|Proteomes:UP000037778}; RX PubMed=25953738; DOI=10.1093/gbe/evv079; RA Tamarit D., Ellegaard K.M., Wikander J., Olofsson T., Vasquez A., RA Andersson S.G.; RT "Functionally Structured Genomes in Lactobacillus kunkeei Colonizing RT the Honey Crop and Food Products of Honeybees and Stingless Bees."; RL Genome Biol. Evol. 7:1455-1473(2015). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KFJ15151.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JPUI01000033; KFJ15151.1; -; Genomic_DNA. DR EMBL; JXCY01000007; KOY75706.1; -; Genomic_DNA. DR RefSeq; WP_034531452.1; NZ_JXCY01000007.1. DR EnsemblBacteria; KFJ15151; KFJ15151; JI66_03355. DR EnsemblBacteria; KOY75706; KOY75706; RZ71_01240. DR GeneID; 31613799; -. DR KEGG; lku:APS55_04605; -. DR PATRIC; fig|148814.8.peg.1048; -. DR KO; K03665; -. DR Proteomes; UP000029013; Unassembled WGS sequence. DR Proteomes; UP000037778; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000037778}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000037778}. FT DOMAIN 200 368 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 423 AA; 47699 MW; B8ED7664D6EDA216 CRC64; MDTEQQTAVI IGLNLDNEQF EYSMTELAAL AEANNLEVVA RLVQKLDHPD KATYFGKGKV EELKMTVLDK DADMVIVNDE LSPSQIRNLE KQTETKIIDR TGLILEIFAN RARTHEAKLQ VQLAKLQYQL PRLHTSASQR LDQQTGSGGG GFTNRGSGES QLELNRRVIE KDISHIKQEL KDIQKSDLTQ RKQRDGKNIP TVALVGYTNA GKSTIMNQLV NRYGENQEKQ VMVKNMLFAT LDTSVRKLIF DDNKTMLLSD TVGFVSKLPH QLVKAFRSTL AEAANADLLV QVVDEADENK ELMMKTTEQT LKEIGVENIP MITVFNKADI LDEPRPQRAG DNLIMAALEE DSIDELVQII RENSYKDYVT EEFLIPFDKG DIVNYLNTKA NVLSTEYVAE GTKVKAELTA VDSERFKQYL INN // ID A0A087GBT1_ARAAL Unreviewed; 534 AA. AC A0A087GBT1; DT 29-OCT-2014, integrated into UniProtKB/TrEMBL. DT 29-OCT-2014, sequence version 1. DT 07-JUN-2017, entry version 11. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:KFK27333.1}; GN ORFNames=AALP_AA8G369300 {ECO:0000313|EMBL:KFK27333.1}; OS Arabis alpina (Alpine rock-cress). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae; OC Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Arabideae; OC Arabis. OX NCBI_TaxID=50452 {ECO:0000313|EMBL:KFK27333.1, ECO:0000313|Proteomes:UP000029120}; RN [1] {ECO:0000313|EMBL:KFK27333.1, ECO:0000313|Proteomes:UP000029120} RP NUCLEOTIDE SEQUENCE. RC STRAIN=cv. Pajares {ECO:0000313|Proteomes:UP000029120}; RC TISSUE=Leaf {ECO:0000313|EMBL:KFK27333.1}; RA Willing E.-M.; RT "The reference genome of Arabis alpina."; RL Submitted (JUN-2014) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CM002876; KFK27333.1; -; Genomic_DNA. DR Proteomes; UP000029120; Chromosome 8. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000029120}; KW Reference proteome {ECO:0000313|Proteomes:UP000029120}. FT DOMAIN 314 480 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 534 AA; 59922 MW; 09D68A4488AA1FAF CRC64; MSSFFFSSSS PISKLQWRAN RNPKPNLAIV PLRLSLLHGN CNSWRLSCNL TKHGLDFEET VVEEDEIPQI LDFSPEEEPS FVEETIPAPS RMLRKKKADE ESLDDRFKLR NGKEVFEEKA YLVGVERKGD GECLFNIEES LEELEQLADT AGLMVVGSTY QKLTSPNPRT YIGSGKVAEI KSAINALDVE TVIFDDELSP GQLRNLEKAF GGDVRVCDRT ALILDIFNQR AATHEAALQV ALAQMEYQLP RLTRMWTHLE RQSGSGQVKG MGEKQIEVDK RILRTQIGVL KKELESVRKH RKQYRSRRVA IPVPVVSLVG YTNAGKSTLL NQLTGANVLA ENRLFATLDP TTRRVQMHNG KEFLLTDTVG FIQKLPTTLV AAFRATLEEI SESSLLVHVV DISHPLANQQ IEAVEKVLSE LDVSSVPKLV VWNKVDRVDY PQKVKLEAEE SGDVICISAL TGEGLDDFCN AVHEKLKDSM VWVEALLPFD KGDLLSTIHK VGMVEEAEYT ENGTLIRAHV PLRFAQLLKP MRHL // ID A0A087GWI9_ARAAL Unreviewed; 565 AA. AC A0A087GWI9; DT 29-OCT-2014, integrated into UniProtKB/TrEMBL. DT 29-OCT-2014, sequence version 1. DT 12-APR-2017, entry version 10. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:KFK34241.1}; GN ORFNames=AALP_AA5G119600 {ECO:0000313|EMBL:KFK34241.1}; OS Arabis alpina (Alpine rock-cress). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae; OC Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Arabideae; OC Arabis. OX NCBI_TaxID=50452 {ECO:0000313|EMBL:KFK34241.1, ECO:0000313|Proteomes:UP000029120}; RN [1] {ECO:0000313|EMBL:KFK34241.1, ECO:0000313|Proteomes:UP000029120} RP NUCLEOTIDE SEQUENCE. RC STRAIN=cv. Pajares {ECO:0000313|Proteomes:UP000029120}; RC TISSUE=Leaf {ECO:0000313|EMBL:KFK34241.1}; RA Willing E.-M.; RT "The reference genome of Arabis alpina."; RL Submitted (JUN-2014) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CM002873; KFK34241.1; -; Genomic_DNA. DR Proteomes; UP000029120; Chromosome 5. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR CDD; cd01878; HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 2. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000029120}; KW Reference proteome {ECO:0000313|Proteomes:UP000029120}. FT DOMAIN 301 532 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 565 AA; 63386 MW; F24F49720E4855D9 CRC64; MLKTLSLARN SLRSKGKSSY SLTSRVLSSP FSSKRHAPKA SEEGEEPAPK DSVLLYPKDP SSTPNLFLVQ PRLAPPKFLQ AKLNEALCLA NSLEEQRYGY FESDFFDKEL PSHVVVQNPV ARSSKPRVDT YFGAGTVDNI KCHLNAEESK EEVDAVFVNA VLSAIQQRNL ERIWEKPVLD RVGLIIEIFN AHAHTKEAKL QAELAALMYS RSRLVRVRGT DGRQTFGQFG EAEVVSARGR AAGKGAGFIG GAGETELQLQ RRRISDRKLR LLSQIKDARR TRLSHRAARK RRGGLEGQSL ATIAVVGYTN AGKSTLTSAL TKTALYCNER LFATLDPTLK SAILPSGRKV LLSDTVGFIS DLPIQLVEAF QSTLEEVVEA DLLLHVVDST APNIEEHRST VFHVLNQIGV SEEKLKNMIE VWNKIDYEEE EEEEEEVEDI HYLDDGKEEE AELNDSSKAE ATVDEEQIQN QDDDWILSDD ENVSDTELWK VPEFGKLDPP QNNEPHIRVS ALTGVGLKEL MHLIDERLKG EDEKVKSQTI LERNELQSRK WRPPRKDDED LAVEQ // ID A0A087M6D0_9RHIZ Unreviewed; 455 AA. AC A0A087M6D0; DT 29-OCT-2014, integrated into UniProtKB/TrEMBL. DT 29-OCT-2014, sequence version 1. DT 07-JUN-2017, entry version 19. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=JP75_02435 {ECO:0000313|EMBL:KFL32433.1}; OS Devosia riboflavina. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Hyphomicrobiaceae; Devosia. OX NCBI_TaxID=46914 {ECO:0000313|EMBL:KFL32433.1, ECO:0000313|Proteomes:UP000028981}; RN [1] {ECO:0000313|EMBL:KFL32433.1, ECO:0000313|Proteomes:UP000028981} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=IFO13584 {ECO:0000313|EMBL:KFL32433.1, RC ECO:0000313|Proteomes:UP000028981}; RA Hassan Y.I., Lepp D., Zhou T.; RL Submitted (AUG-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KFL32433.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JQGC01000002; KFL32433.1; -; Genomic_DNA. DR RefSeq; WP_035078719.1; NZ_JQGC01000002.1. DR EnsemblBacteria; KFL32433; KFL32433; JP75_02435. DR Proteomes; UP000028981; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000028981}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000028981}. FT DOMAIN 222 393 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 188 215 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 455 AA; 50201 MW; 0334A32E024C2627 CRC64; MDDFDDEDGR LPGGPKPYID RQEQPTRVGL VCPDVRGKSS YHSLEARQAE FEGLAEAIRL DVIFSDVVKV REIRPATYLG AGHVEALAAK VKAENIELLL VDASLSPIQQ RNLERETHTK VLDRTALILE IFGERAATRE GVLQVELAHL NYQKGRLVRS WTHLERQRGS GGTGFMGGPG ETQIESDRRQ ITDRIVLLED RLDKVKRTRA QQRQQRIRAA IPVVALVGYT NAGKSTLFNR LTGAGVFAED LLFATLDTTV RKIELPHGRE VMLSDTVGFV ADLPHDLVAA FRATLEEVVD ADIILHVRDV ANPDHSAQAQ DVLTVLDELG VSSETTPIIE VWNKIDLLVE PGVTLGGAAP AGKVLASMPV SAHTGQGIED LLNLIERSLG EQSRTYHVHV PHSAGADIGW LHTNAEVISR DEPTERGQDY VVRVEPRHKT AFLERFNGRI ALSDL // ID A0A087MF08_9GAMM Unreviewed; 438 AA. AC A0A087MF08; DT 29-OCT-2014, integrated into UniProtKB/TrEMBL. DT 29-OCT-2014, sequence version 1. DT 07-JUN-2017, entry version 20. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=N788_08250 {ECO:0000313|EMBL:KFL35461.1}; OS Arenimonas donghaensis DSM 18148 = HO3-R19. OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales; OC Xanthomonadaceae; Arenimonas. OX NCBI_TaxID=1121014 {ECO:0000313|EMBL:KFL35461.1, ECO:0000313|Proteomes:UP000029085}; RN [1] {ECO:0000313|Proteomes:UP000029085} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=HO3-R19 {ECO:0000313|Proteomes:UP000029085}; RA Chen F., Wang G.; RT "Genome sequencing of Arenimonas donghaensis."; RL Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KFL35461.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AVCJ01000051; KFL35461.1; -; Genomic_DNA. DR RefSeq; WP_034225879.1; NZ_AVCJ01000051.1. DR EnsemblBacteria; KFL35461; KFL35461; N788_08250. DR PATRIC; fig|1121014.3.peg.2547; -. DR Proteomes; UP000029085; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000029085}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000029085}. FT DOMAIN 199 363 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 158 192 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 438 AA; 48343 MW; 1199A359691A3FEB CRC64; MFERARKGER ALLVQPHPPG QQDPSRLEEF TELAHSAGAT VVGTVPARVE RPNPAYYIGT GKLEEVKSAC EATEADLVLV NELLTPAQER NLERVLKRRV VDRTGLILDI FAQRAASHEG KLQVELAQLK HWATRLVRGW THLERQRGGA IGLRGPGETQ LELDKRMLQK KLESVRARLD KVEVQRTQMR RARLRNDIPR VALVGYTNAG KSTLFNILTN SGVYADDRLF ATLDPTTRRI EGVAPLVLSD TVGFVRDLPH ELVAAFRSTL SEARDADLLL HVVDAADELR DERIGQVDAV LGEIGAGDIP QVLVFNKIDR IEGAAPRRDP EVEGRERVWL SAKTGNGLDG LRELLTDRFL DRRVAGELAL GPGQGRLRAR LHEVGAVKTE SSDEDGWHLE IDLPRAVAER LSSEPGGESL AGLLLVAPAA PTYNPETN // ID A0A087N349_9BACI Unreviewed; 424 AA. AC A0A087N349; DT 29-OCT-2014, integrated into UniProtKB/TrEMBL. DT 29-OCT-2014, sequence version 1. DT 07-JUN-2017, entry version 19. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=CH76_06230 {ECO:0000313|EMBL:KFL43552.1}; OS Lysinibacillus sp. BF-4. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; OC Lysinibacillus. OX NCBI_TaxID=1473546 {ECO:0000313|EMBL:KFL43552.1, ECO:0000313|Proteomes:UP000029097}; RN [1] {ECO:0000313|EMBL:KFL43552.1, ECO:0000313|Proteomes:UP000029097} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BF-4 {ECO:0000313|EMBL:KFL43552.1, RC ECO:0000313|Proteomes:UP000029097}; RA Antwerpen M.H., Georgi E., Zimmermann P., Hoermansdorfer S., Meyer H., RA Grass G.; RT "Genome sequence of strain, BF-4, a Lysinibacillus-like bacillus RT isolated during an anthrax outbreak in Bavaria."; RL Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KFL43552.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JPUW01000012; KFL43552.1; -; Genomic_DNA. DR RefSeq; WP_036144246.1; NZ_JPUW01000012.1. DR EnsemblBacteria; KFL43552; KFL43552; CH76_06230. DR Proteomes; UP000029097; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000029097}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000029097}. FT DOMAIN 203 371 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 162 196 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 424 AA; 48148 MW; 4D08E373E5E1F9CE CRC64; MKEVDTLKEY AVLVGVQLQK DTHFDYGMQE LENLAHALNV EVVGTVTQNL ERINPGYYVG TGKIEEIKAF YEEREANVVI FNDELTPSQI RNLEQELACK VIDRTMLILD IFARRANTKE AQLQVQLAQL QYMLPRLIGL RASLGRQGGG TGGGFKNRGA GETKLELDRR KIEDQISKIK KELEHVKEQR DTQRKQRERN ALPVVSLVGY TNAGKSTVMN QLLEKSGQSE HKQVFEKDML FATLETSVRQ IELVDKKSFL LTDTVGFVSK LPHHLVKAFR STLEEARNAD LLLHVVDVSH EEYRYMMEVT DQTLQAVGVE GIPTIHVYNK CDITDKPYPV VSGDHIWLAA KEGVGLDELL AIISQHVFAN YVKCELLVPY DRGEVVAYLN ENAAIQSTDY EEDGTRILVE LNDMDAKRFS EYMQ // ID A0A087NB32_9SPHN Unreviewed; 444 AA. AC A0A087NB32; DT 29-OCT-2014, integrated into UniProtKB/TrEMBL. DT 29-OCT-2014, sequence version 1. DT 07-JUN-2017, entry version 19. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=IL54_1751 {ECO:0000313|EMBL:KFL46335.1}; OS Sphingobium sp. ba1. OC Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales; OC Sphingomonadaceae; Sphingobium. OX NCBI_TaxID=1522072 {ECO:0000313|EMBL:KFL46335.1, ECO:0000313|Proteomes:UP000029094}; RN [1] {ECO:0000313|EMBL:KFL46335.1, ECO:0000313|Proteomes:UP000029094} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ba1 {ECO:0000313|Proteomes:UP000029094}; RA Manzari C., Chiara M., Costanza A., Leoni C., Picardi E., Trotta M., RA Volpicella M., D'Erchia A.M., Horner D.S., Pesole G., Ceci L.R.; RT "Draft genome sequence of a Kanamycin and Nickel resistant bacterium RT Sphingobium species."; RL Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KFL46335.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JPPQ01000069; KFL46335.1; -; Genomic_DNA. DR RefSeq; WP_037474547.1; NZ_JPPQ01000069.1. DR EnsemblBacteria; KFL46335; KFL46335; IL54_1751. DR PATRIC; fig|1522072.3.peg.3558; -. DR Proteomes; UP000029094; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0016810; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds; IEA:InterPro. DR CDD; cd01878; HflX; 1. DR Gene3D; 2.30.40.10; -; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR011059; Metal-dep_hydrolase_composite. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 2. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000029094}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}. FT DOMAIN 209 390 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 444 AA; 48560 MW; 23C8177B954A73F8 CRC64; MAIFNRDSED EVARGARAVV VHAETHGGDR RDSDARLEEA RGLALAIGID VRAAQAFRVR DRKPATLFGS GQVDQIATLA RQEEADLIIV DNSLSPVQQS NLEKACEAKV IDRTGLILEI FGERAATNEG RLQVELAHLD YQAGRLVRSW THLERQRGGF GFLGGPGETQ IEADRRMIRD RMAKIRKELD QVTRTRGLHR ARRQRAPWPV IALVGYTNAG KSTLFNRMTG ADVMAQDLLF ATLDPTMRQI ALPGLDKAIL SDTVGFVSDL PTQLIAAFRA TLEEVLSADL IVHVRDIAHP DSDAQRDDVL DVLGELGVAG EAALERAEGE PPAPLIIEAW NKLDLLNADA AVLARETAAR RDDVAILSAL TGEGVDQLQR MISDHMTTGA KVYGLRIPVS DGAAMAWLHE HGEVLSTDVE EEESRVEVRL SDAAFARFGK RGEA // ID A0A087R603_APTFO Unreviewed; 405 AA. AC A0A087R603; DT 29-OCT-2014, integrated into UniProtKB/TrEMBL. DT 29-OCT-2014, sequence version 1. DT 10-MAY-2017, entry version 12. DE SubName: Full=Putative GTP-binding protein 6 {ECO:0000313|EMBL:KFM08907.1}; DE Flags: Fragment; GN ORFNames=AS27_05342 {ECO:0000313|EMBL:KFM08907.1}; OS Aptenodytes forsteri (Emperor penguin). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda; OC Coelurosauria; Aves; Neognathae; Sphenisciformes; Spheniscidae; OC Aptenodytes. OX NCBI_TaxID=9233 {ECO:0000313|EMBL:KFM08907.1, ECO:0000313|Proteomes:UP000053286}; RN [1] {ECO:0000313|EMBL:KFM08907.1, ECO:0000313|Proteomes:UP000053286} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BGI_AS27 {ECO:0000313|EMBL:KFM08907.1}; RA Zhang G., Li C.; RT "Genome evolution of avian class."; RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; KL226137; KFM08907.1; -; Genomic_DNA. DR Proteomes; UP000053286; Unassembled WGS sequence. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR CDD; cd01878; HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 4: Predicted; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000053286}; KW Reference proteome {ECO:0000313|Proteomes:UP000053286}. FT DOMAIN 180 344 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 142 169 {ECO:0000256|SAM:Coils}. FT NON_TER 1 1 {ECO:0000313|EMBL:KFM08907.1}. FT NON_TER 405 405 {ECO:0000313|EMBL:KFM08907.1}. SQ SEQUENCE 405 AA; 45857 MW; 090D42E776D6D387 CRC64; AELQIAEAVA LVDTIQNWTV LDKIIIPTKN PDKKFIFGKG NFQVLTEKIK KLPHVTAVFL NVERISSLTK KELEDAWGVK VFDRYTVVLH IFRCNARTKE AKLQIALAEI PLLRSNLKNE VSQLDQQRGG SRYIMGSGET FMETQNRILK EKELKIRNAL EKLRRKRSLL RTQRRKREFP IISVMGYTNC GKTTLIKALT GEAGLQPRDQ LFATLDITAH AGYLPSHMAV IYVDTIGFLT DLPHNLVESF SATLEEVAYS DLIVHVRDIT HPETILQKAT VLSVLKNLNL PSHLLDSMVE VHNKVDLIER YKPTEENALA VSALHGHGLE ELKEEIEKKI LTTTGKKILT VNVNLEGPQL SWLYKEATVQ EVEVMPEDGT ARVKVIISNS AFGRYKNLFP NSKIF // ID A0A087SIX2_AUXPR Unreviewed; 553 AA. AC A0A087SIX2; DT 29-OCT-2014, integrated into UniProtKB/TrEMBL. DT 29-OCT-2014, sequence version 1. DT 07-JUN-2017, entry version 12. DE SubName: Full=GTPase HflX {ECO:0000313|EMBL:KFM25676.1}; GN ORFNames=F751_2518 {ECO:0000313|EMBL:KFM25676.1}; OS Auxenochlorella protothecoides (Green microalga) (Chlorella OS protothecoides). OC Eukaryota; Viridiplantae; Chlorophyta; Trebouxiophyceae; Chlorellales; OC Chlorellaceae; Auxenochlorella. OX NCBI_TaxID=3075 {ECO:0000313|EMBL:KFM25676.1, ECO:0000313|Proteomes:UP000028924}; RN [1] {ECO:0000313|EMBL:KFM25676.1, ECO:0000313|Proteomes:UP000028924} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=0710 {ECO:0000313|EMBL:KFM25676.1}; RX PubMed=25012212; RA Gao C., Wang Y., Shen Y., Yan D., He X., Dai J., Wu Q.; RT "Oil accumulation mechanisms of the oleaginous microalga Chlorella RT protothecoides revealed through its genome, transcriptomes, and RT proteomes."; RL BMC Genomics 15:582-582(2014). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; KL662122; KFM25676.1; -; Genomic_DNA. DR RefSeq; XP_011398572.1; XM_011400270.1. DR GeneID; 23613909; -. DR KEGG; apro:F751_2518; -. DR KO; K03665; -. DR Proteomes; UP000028924; Unassembled WGS sequence. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000028924}; KW Reference proteome {ECO:0000313|Proteomes:UP000028924}. FT DOMAIN 302 479 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 553 AA; 59446 MW; 03411B9959E767A6 CRC64; MLGATQFAGG SLTLPARYCF VPQPAPRWRC RGPRRTCTTA IRHEDRVSGA GPDVVHVVPQ VEPVASPPAL PENELPPLSE SLSLDTARGR NTPAPVPVAG PDDRERCYLV AVARKSSPRS RAFSAPDSIL ELGRLAVTAG CQVVGHCIQA LEEPHPRTYV GSGKLAELAA AVEGASADTL VFDDELSPGQ LRNLDRAFGG AVRLCDRTAL ILDIFSQRAA TREGQLQVAL AQAEYQLPRL TRMWTHLERQ SGSGQVKGMG EKQIEVDKRL LRGRMARLRS DIEEVRTHRA AYRVRRAEAP IPVIALVGYT NAGKSTLLNT LTHAGVLAED KLFATLDPTT RRVELGQGQE VLLTDTVGFI QKLPTQLVAA FRATLEEIAE ASLLLHVVDV SHPTAAAQVE TVNDVLKELG VGGIPVLHVW NKARRHGEGG GPDVDACADP HAVRAVAALR PHSVCVSAMS GEGVEDLLEA VSYMLQQSMV DVEVLVPYSR GEFVDLIHRS GMVQSAEFTA TGTRIKAHVP QSLARKLAPM AVGGQGAAPP LQIGLQHRDW EGP // ID A0A087YCM0_POEFO Unreviewed; 399 AA. AC A0A087YCM0; DT 29-OCT-2014, integrated into UniProtKB/TrEMBL. DT 26-NOV-2014, sequence version 2. DT 30-AUG-2017, entry version 12. DE SubName: Full=GTP binding protein 6 (putative) {ECO:0000313|Ensembl:ENSPFOP00000015773}; OS Poecilia formosa (Amazon molly) (Limia formosa). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata; OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; OC Poeciliinae; Poecilia. OX NCBI_TaxID=48698 {ECO:0000313|Ensembl:ENSPFOP00000015773, ECO:0000313|Proteomes:UP000028760}; RN [1] {ECO:0000313|Ensembl:ENSPFOP00000015773, ECO:0000313|Proteomes:UP000028760} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=female {ECO:0000313|Ensembl:ENSPFOP00000015773}; RA Schartl M., Warren W.; RL Submitted (OCT-2013) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Ensembl:ENSPFOP00000015773} RP IDENTIFICATION. RG Ensembl; RL Submitted (SEP-2014) to UniProtKB. CC -!- CAUTION: The sequence shown here is derived from an Ensembl CC automatic analysis pipeline and should be considered as CC preliminary data. {ECO:0000313|Ensembl:ENSPFOP00000015773}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AYCK01012525; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR Ensembl; ENSPFOT00000015795; ENSPFOP00000015773; ENSPFOG00000015695. DR GeneTree; ENSGT00390000001397; -. DR Proteomes; UP000028760; Unassembled WGS sequence. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR CDD; cd01878; HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000028760}; KW Reference proteome {ECO:0000313|Proteomes:UP000028760}. FT DOMAIN 177 341 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 399 AA; 44820 MW; D7360CCB2630E187 CRC64; MMAEAEGLVN TLDNWTVVDK IILSTKTPEK KKIFGKGNFQ LLTGKIRGTP GVTAVFVNVD RLSSVSEREF EETWGVKVFD RYSVVLHIFR CNARTKEAKL QISLAEIPLL RSRLKNDMAD LDQQGGGARY IGGSGETLYE VQQRLLKERE TRIRSALEKL RRKRHLLRSQ RKHREFPTVS VLGYTNCGKT TLIKALTGDS GLQPRNQLFA TLDVTVHAGQ LPSHMTVLYV DTIGFLSQLP HQLIDSFSAT LEDIIHSDLL VHVRDVSHPE TVNQKANVLN VLRNLQIPHR LLDSMIEVHN KIDLLGSYES SEPCAVLISA LQQRGLDELK RAVEQEVVKS TGKQILDLRV NLSSPQLSWL YKEATVQDVQ VNAEEGSAVV KVIISAAAHG RYKKLFESR // ID A0A088ATJ0_APIME Unreviewed; 475 AA. AC A0A088ATJ0; DT 29-OCT-2014, integrated into UniProtKB/TrEMBL. DT 29-OCT-2014, sequence version 1. DT 05-JUL-2017, entry version 18. DE SubName: Full=Uncharacterized protein {ECO:0000313|EnsemblMetazoa:GB55017-PA}; GN Name=LOC410784 {ECO:0000313|EnsemblMetazoa:GB55017-PA}; OS Apis mellifera (Honeybee). OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; OC Pterygota; Neoptera; Holometabola; Hymenoptera; Apocrita; Aculeata; OC Apoidea; Apidae; Apis. OX NCBI_TaxID=7460 {ECO:0000313|EnsemblMetazoa:GB55017-PA, ECO:0000313|Proteomes:UP000005203}; RN [1] {ECO:0000313|EnsemblMetazoa:GB55017-PA} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DH4 {ECO:0000313|EnsemblMetazoa:GB55017-PA}; RA Wu J.L., Liu J.H., Yuan Y.N., Qiao L.Y., Liu W.Z.; RL Submitted (NOV-2010) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EnsemblMetazoa:GB55017-PA} RP IDENTIFICATION. RC STRAIN=DH4 {ECO:0000313|EnsemblMetazoa:GB55017-PA}; RG EnsemblMetazoa; RL Submitted (JAN-2017) to UniProtKB. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR RefSeq; XP_006571673.1; XM_006571610.2. DR STRING; 7460.GB16691-PA; -. DR PaxDb; A0A088ATJ0; -. DR EnsemblMetazoa; GB55017-RA; GB55017-PA; GB55017. DR GeneID; 410784; -. DR KEGG; ame:410784; -. DR eggNOG; KOG0410; Eukaryota. DR eggNOG; COG2262; LUCA. DR Proteomes; UP000005203; Unplaced. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR CDD; cd01878; HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 4: Predicted; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000005203}; KW Reference proteome {ECO:0000313|Proteomes:UP000005203}. FT DOMAIN 253 352 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 219 249 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 475 AA; 54665 MW; 78B39E223D99791C CRC64; MQCLKRLVVL NKLQYVKNKK KELLNYITYQ YRYKSDIIFD ETEEEKNIYS KLTKDYLGSI INGNRVFVIQ PYIKWGVQKK RNTTPQLQLA EAIALINTLP NWSVVGKKIV PLLSLQKHKL VGSGGLETLK KDITNCPNVT AIFISTNLLK FIQIAELQNI FHLPIYDRYS IIIHIFREHA KSPEAKLQVA IAEIPYVRKK MIDLTNYLIR QVKFDEKTKN LLQTREKKLR NALKKLKEHR QMIKRHRTSY GFPTIAIVGY TNAGKTSLIK ALTGDTSLQP ENKLFATLDT TVHQGLLPNN LKVLYIDTIG FIQDVPETLL EPFLVTLEDA INAHILIHVF DISHPDVKAQ IEHIQKTIQP MIDENKVIIN VANKCDMVDK NEIENLLPED AFTISATKLK GIDLLRSKIQ EEIIHAANLI QKRIKVGNGS AEASWLYKET TVLNVIPDSK NSQYLIMDVF MTTPIFYKFK RIFNV // ID A0A088F5K8_9SPHI Unreviewed; 395 AA. AC A0A088F5K8; DT 26-NOV-2014, integrated into UniProtKB/TrEMBL. DT 26-NOV-2014, sequence version 1. DT 07-JUN-2017, entry version 18. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=KO02_21055 {ECO:0000313|EMBL:AIM38912.1}; OS Sphingobacterium sp. ML3W. OC Bacteria; Bacteroidetes; Sphingobacteriia; Sphingobacteriales; OC Sphingobacteriaceae; Sphingobacterium. OX NCBI_TaxID=1538644 {ECO:0000313|EMBL:AIM38912.1, ECO:0000313|Proteomes:UP000028992}; RN [1] {ECO:0000313|EMBL:AIM38912.1, ECO:0000313|Proteomes:UP000028992} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ML3W {ECO:0000313|EMBL:AIM38912.1}; RX PubMed=25614576; RA Smith S.A., Krasucki S.P., McDowell J.V., Balke V.L.; RT "Complete Genome Sequence of Sphingobacterium sp. Strain ML3W, RT Isolated from Wings of Myotis lucifugus Infected with White Nose RT Syndrome."; RL Genome Announc. 3:0-0(2015). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP009278; AIM38912.1; -; Genomic_DNA. DR RefSeq; WP_038701255.1; NZ_CP009278.1. DR EnsemblBacteria; AIM38912; AIM38912; KO02_21055. DR KEGG; sht:KO02_21055; -. DR KO; K03665; -. DR Proteomes; UP000028992; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000028992}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000028992}. FT DOMAIN 204 384 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 395 AA; 44961 MW; 4E1F835C06D65100 CRC64; MAKIKIYDTE VKPETAILVS VIPQGVTETK AQEYLEELEF LVQTAGGITK GIFTQKLTYP DRATFVGSGK LEEIKAFIIA EEIDMVVFDD ELTPSQLRNV EKELKVKILD RSNLILDIFA SHAKSAQAKT QVELAQLQYL LPRLTRMWTH LERQRGGIGM RGPGESQIET DRRIILNKIT VFKDRLESID KQNETQRKNR GDMIRVALVG YTNVGKSTIM NMVSKSDVLI ENKLFATLDT TVRKVVIDNL PFLLSDTVGF IRKLPHHLVE CFKSTLDEVR EADVLIHVVD ISHPNFEDHI HAVNETLKEI GAQDKPVITV FNKIDAFIPT KEEGEEGEKI VTLADFENSW MAKNADPAIF ISATNKTNLE EFKQKLYEII VEMHNARYPY NNLLY // ID A0A088QEC4_9CORY Unreviewed; 517 AA. AC A0A088QEC4; DT 26-NOV-2014, integrated into UniProtKB/TrEMBL. DT 26-NOV-2014, sequence version 1. DT 10-MAY-2017, entry version 19. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:AIN81593.1}; GN ORFNames=DR71_2070 {ECO:0000313|EMBL:AIN81593.1}; OS Corynebacterium sp. ATCC 6931. OC Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae; OC Corynebacterium. OX NCBI_TaxID=1487956 {ECO:0000313|EMBL:AIN81593.1, ECO:0000313|Proteomes:UP000029247}; RN [1] {ECO:0000313|EMBL:AIN81593.1, ECO:0000313|Proteomes:UP000029247} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=6931 {ECO:0000313|Proteomes:UP000029247}; RA Bishop-Lilly K.A., Broomall S.M., Chain P.S., Chertkov O., Coyne S.R., RA Daligault H.E., Davenport K.W., Erkkila T., Frey K.G., Gibbons H.S., RA Gu W., Jaissle J., Johnson S.L., Koroleva G.I., Ladner J.T., Lo C.-C., RA Minogue T.D., Munk C., Palacios G.F., Redden C.L., Rosenzweig C.N., RA Scholz M.B., Teshima H., Xu Y.; RL Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP008913; AIN81593.1; -; Genomic_DNA. DR EnsemblBacteria; AIN81593; AIN81593; DR71_2070. DR KEGG; coa:DR71_2070; -. DR KO; K03665; -. DR Proteomes; UP000029247; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000029247}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000029247}. FT DOMAIN 293 462 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 252 279 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 517 AA; 56740 MW; 004A9056FCDC5290 CRC64; MTNFSNNFDE VSDAMSQQAS TSHEMDDFFI DANDADKNAD SASGDAFATN VGTQREPTVG DLDLEARSSL RRLTRSVAHT ESEEVMVEYR QLRLERVVLL GVWTSGTLQE AEVAMEELAA LAETAGSEVL EMVLQRRDKP DPGTYVGSGK LNELRDIVAS TGADTVICDG ELSPGQLVAL EDRLDAKVID RTMLILDIFA QHAKSKEGKA QVSLAQMQYL YTRLRGWGGN LSRQAGGRAG SNGGVGLRGP GETKIETDRQ RLRQDMARIR KELAGMKTAR EIKRARRKAG HLPRVAIVGY TNAGKSSLLN ALTGAGVLVE DALFATLDPT TRRTKLRDGR TVIMTDTVGF VRHLPTQLIE AFRSTLEEVL EADVIMHVVD SSDPFPLEQI KAVNKVINEI AEEENAEIPP ELLVVNKVDK ADGITLAQLR HQLDDAVFVS ARTGEGIGEL ETRLELALNE LESHVHMLIP YDKGNIVSML HEDATVLSET WTEQGTQMDV RLPTSLADEL SAYHIEP // ID A0A089IES9_9BACL Unreviewed; 421 AA. AC A0A089IES9; DT 26-NOV-2014, integrated into UniProtKB/TrEMBL. DT 26-NOV-2014, sequence version 1. DT 07-JUN-2017, entry version 19. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=H70737_01385 {ECO:0000313|EMBL:AIQ21625.1}; OS Paenibacillus sp. FSL H7-0737. OC Bacteria; Firmicutes; Bacilli; Bacillales; Paenibacillaceae; OC Paenibacillus. OX NCBI_TaxID=1536775 {ECO:0000313|EMBL:AIQ21625.1, ECO:0000313|Proteomes:UP000029519}; RN [1] {ECO:0000313|EMBL:AIQ21625.1, ECO:0000313|Proteomes:UP000029519} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=FSL H7-0737 {ECO:0000313|EMBL:AIQ21625.1, RC ECO:0000313|Proteomes:UP000029519}; RA den Bakker H.C., Tsai Y.-C., Martin N., Korlach J., Wiedmann M.; RT "Comparative genomics of the Paenibacillus odorifer group."; RL Submitted (AUG-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP009279; AIQ21625.1; -; Genomic_DNA. DR RefSeq; WP_042184155.1; NZ_CP009279.1. DR EnsemblBacteria; AIQ21625; AIQ21625; H70737_01385. DR KEGG; paej:H70737_01385; -. DR KO; K03665; -. DR Proteomes; UP000029519; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000029519}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000029519}. FT DOMAIN 198 366 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 157 184 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 421 AA; 47451 MW; FBFC9C7C263F045D CRC64; MEQLREKAII VGVQLQNETN FDYSMEELTN LAAACDLEVV GELSQKASRI NPSHYIGTGK IQELSALLEA HDAPIVIFND ELSPSQIRNL ESSLGRQVID RTILILNIFA ERAKTKEAQL QVEVAKLQYM LPRLTGLRES LGRQGGGAGL KNRGAGETKL ELDRRRIEER ISALQVELQQ QVARRQIQRK QRHKNEVPVV CLVGYTNTGK SSLMNVIVET YHPGSNKQVF AKDMLFATLE TSVRSIELPD HKTFLLTDTV GFVSQLPHHL VKAFRSTLEE VTEADLLIHV VDISDPQHQQ HMAVTDETLK ALGADQIPTV YAYNKADLTD LPYPHLEGDN VYLSAKQNSG IAELTDLIRS HVFTDYVQCE ILIPFDRGNV VSYFNEHAHV QSTSYEETGT RLALECRKSD FEKFRNDFVE L // ID A0A089IJ83_9BACL Unreviewed; 429 AA. AC A0A089IJ83; DT 26-NOV-2014, integrated into UniProtKB/TrEMBL. DT 26-NOV-2014, sequence version 1. DT 07-JUN-2017, entry version 19. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=H70737_16955 {ECO:0000313|EMBL:AIQ24386.1}; OS Paenibacillus sp. FSL H7-0737. OC Bacteria; Firmicutes; Bacilli; Bacillales; Paenibacillaceae; OC Paenibacillus. OX NCBI_TaxID=1536775 {ECO:0000313|EMBL:AIQ24386.1, ECO:0000313|Proteomes:UP000029519}; RN [1] {ECO:0000313|EMBL:AIQ24386.1, ECO:0000313|Proteomes:UP000029519} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=FSL H7-0737 {ECO:0000313|EMBL:AIQ24386.1, RC ECO:0000313|Proteomes:UP000029519}; RA den Bakker H.C., Tsai Y.-C., Martin N., Korlach J., Wiedmann M.; RT "Comparative genomics of the Paenibacillus odorifer group."; RL Submitted (AUG-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP009279; AIQ24386.1; -; Genomic_DNA. DR RefSeq; WP_042188885.1; NZ_CP009279.1. DR EnsemblBacteria; AIQ24386; AIQ24386; H70737_16955. DR KEGG; paej:H70737_16955; -. DR KO; K03665; -. DR Proteomes; UP000029519; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000029519}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000029519}. FT DOMAIN 208 372 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 167 201 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 429 AA; 47840 MW; 871D4BBFCF2C16BA CRC64; MAITTHDTET DVQDRAILVS LVTDKIKRTG IDPELSLQEL VQLAETAGVE VLDVLRQNKE TPDSRWFIGK GKVEELRMAA DALGANTAIF DQELSGAQVR NLEEALDLKI IDRTQLILDI FAGRAKTREG IIQVELAQLS YLLPRLSGQG KNLSRLGGGI GTRGPGESKL ETDRRHIRDR ITELKRQLDE VVKTRELHRE RRRKAGAVQV ALVGYTNAGK STLLKQLTDA DVYIENQLFA TLDPTSRVLE LAGGKEVVLT DTVGFIQNLP HDLVASFRAT LEEVNEANLV LHVVDASSPM REEQMEIVQS ILQDLGASGT PQIVLFNKID LCQPEQLEML PTGTGYLKIS AFNPEDLTRI TEMIADELAG DTLNFRIPGD RGDISSLLYR VGEVLETTYD ENDVLYNVRL NKEDYDKWGY MLADFVDQQ // ID A0A089KTK8_9BACL Unreviewed; 422 AA. AC A0A089KTK8; DT 26-NOV-2014, integrated into UniProtKB/TrEMBL. DT 26-NOV-2014, sequence version 1. DT 07-JUN-2017, entry version 21. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=R70331_01210 {ECO:0000313|EMBL:AIQ50293.1}; OS Paenibacillus sp. FSL R7-0331. OC Bacteria; Firmicutes; Bacilli; Bacillales; Paenibacillaceae; OC Paenibacillus. OX NCBI_TaxID=1536773 {ECO:0000313|EMBL:AIQ50293.1, ECO:0000313|Proteomes:UP000029487}; RN [1] {ECO:0000313|EMBL:AIQ50293.1, ECO:0000313|Proteomes:UP000029487} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=FSL R7-0331 {ECO:0000313|EMBL:AIQ50293.1, RC ECO:0000313|Proteomes:UP000029487}; RA den Bakker H.C., Tsai Y.-C., Martin N., Korlach J., Wiedmann M.; RT "Comparative genomics of the Paenibacillus odorifer group."; RL Submitted (AUG-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP009284; AIQ50293.1; -; Genomic_DNA. DR RefSeq; WP_042172134.1; NZ_CP009284.1. DR EnsemblBacteria; AIQ50293; AIQ50293; R70331_01210. DR KEGG; paee:R70331_01210; -. DR KO; K03665; -. DR Proteomes; UP000029487; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000029487}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000029487}. FT DOMAIN 197 365 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 156 183 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 422 AA; 47449 MW; 5191B358171AAFA8 CRC64; METTRQHAII VGVQLQNDTN FAYSMEELRN LAAACNITVI GELSQKASRI NPSHYLGTGK IQELSMLVED EDTLIIFNDE LAPSQIRNLE SSLDRQVIDR TILILNIFAD RAKTKEAQLQ VEVAQLQYML PRLNGMRESL GRQGGGSGLK NRGAGETKLE LDRRRIEERI TALETELQGQ VERRQIQRRQ RHKNEVPVVC LVGYTNAGKS SLLNAMVETY HPGSNKQVFA KNMLFATLET SVRSIRLPDH KTFLLTDTVG FVSQLPHHLV KAFRSTLEEV TEADLLIHVV DASDPQHEQH MAVTSETLKA LGADGIPTVY AYNKSDLTDR AYPAVEGGTI TISARQSSGI SELTGLIRSH VFNDYIQCEI LVPFDRGSIV SYFNEHAHVQ EVSYEEQGTR LRLECRAADY ERFRGDFVEL SH // ID A0A089LW42_9BACL Unreviewed; 426 AA. AC A0A089LW42; DT 26-NOV-2014, integrated into UniProtKB/TrEMBL. DT 26-NOV-2014, sequence version 1. DT 07-JUN-2017, entry version 19. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=PSTEL_10320 {ECO:0000313|EMBL:AIQ63418.1}; OS Paenibacillus stellifer. OC Bacteria; Firmicutes; Bacilli; Bacillales; Paenibacillaceae; OC Paenibacillus. OX NCBI_TaxID=169760 {ECO:0000313|EMBL:AIQ63418.1, ECO:0000313|Proteomes:UP000029507}; RN [1] {ECO:0000313|EMBL:AIQ63418.1, ECO:0000313|Proteomes:UP000029507} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 14472 {ECO:0000313|EMBL:AIQ63418.1, RC ECO:0000313|Proteomes:UP000029507}; RA den Bakker H.C., Tsai Y.-C., Martin N., Korlach J., Wiedmann M.; RT "Comparative genomics of the Paenibacillus odorifer group."; RL Submitted (AUG-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP009286; AIQ63418.1; -; Genomic_DNA. DR RefSeq; WP_038694939.1; NZ_CP009286.1. DR EnsemblBacteria; AIQ63418; AIQ63418; PSTEL_10320. DR KEGG; pste:PSTEL_10320; -. DR KO; K03665; -. DR Proteomes; UP000029507; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000029507}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000029507}. FT DOMAIN 198 366 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 164 191 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 426 AA; 47515 MW; 896A28CA56DF2B32 CRC64; MESMTTTAII VGVQLQQDED FAYSMEELSN LAAACGIETV GEVTQKAAKT NAAHYIGSGK LKELAALADQ LDVSAVIFDG ELSPSQIRNL ERKLGREVLD RTMLILHIFA ERAKTKEAQL QVEIARLQYM LTRLAGQRDS LGRQGGGSGL KNRGTGETKL ELDRRASLDR IASLQEELER LVARRQIQRK QRGKNEIPVV CLVGYTNAGK SSLLNAIMDY SGAGPDKHVL ARNMLFATLE TSVRRITLPD KKTFLLTDTV GFVSRLPHHL VKAFRSTLEE IAEADLLIHV ADYANPKYEQ QMEVTRETLS ELGVDDIPMI YAYNKADLTD SAYPFATDNG VIMSAAEGSG LDELMSLIRS RIFTDYVSCE VLIPFDRGNV VSYFNEHALV QAVSYEENGT RLELECRKAD FERFRDVYLP LQSHIE // ID A0A089M8S3_9BACL Unreviewed; 427 AA. AC A0A089M8S3; DT 26-NOV-2014, integrated into UniProtKB/TrEMBL. DT 26-NOV-2014, sequence version 1. DT 07-JUN-2017, entry version 22. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=R70331_17300 {ECO:0000313|EMBL:AIQ53109.1}; OS Paenibacillus sp. FSL R7-0331. OC Bacteria; Firmicutes; Bacilli; Bacillales; Paenibacillaceae; OC Paenibacillus. OX NCBI_TaxID=1536773 {ECO:0000313|EMBL:AIQ53109.1, ECO:0000313|Proteomes:UP000029487}; RN [1] {ECO:0000313|EMBL:AIQ53109.1, ECO:0000313|Proteomes:UP000029487} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=FSL R7-0331 {ECO:0000313|EMBL:AIQ53109.1, RC ECO:0000313|Proteomes:UP000029487}; RA den Bakker H.C., Tsai Y.-C., Martin N., Korlach J., Wiedmann M.; RT "Comparative genomics of the Paenibacillus odorifer group."; RL Submitted (AUG-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP009284; AIQ53109.1; -; Genomic_DNA. DR RefSeq; WP_042177330.1; NZ_CP009284.1. DR EnsemblBacteria; AIQ53109; AIQ53109; R70331_17300. DR KEGG; paee:R70331_17300; -. DR KO; K03665; -. DR Proteomes; UP000029487; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000029487}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000029487}. FT DOMAIN 207 371 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 427 AA; 47520 MW; 4F6DCED4BA28D70E CRC64; MSLTHDTQTD VQDRAILVSL VTDQIKRTGI DPELSLQELV QLAETAGVEV LDVLRQNKET PDSRWFIGKG KVEELRMAAD GLGANTAIFD QELSGAQVRN LEEALDMKII DRTQLILDIF AGRAKTREGI IQVELAQHSY LLPRLSGHGK NLSRLGGGIG TRGPGESKLE TDRRHIRGRI TELKRQLDEV VKTRELHRER RRKSGAVQVA LVGYTNAGKS TLLKQLTDAD VYIENQLFAT LDPTSRVLQL PAGKEVVLTD TVGFIQNLPH DLVASFRATL EEVNEANLVL HVVDASSPMR EEQMEVVDTI LQELGAAGKP RVVLFNKCDL CQPEQLEMLP AGPGYLKISA FNAEDLARVT DLIADELAGD TLVFRIPGDR GDLSSLLYRV GEVLETNYEE NDVLYSVRLN KEDYDKWGYK LEAFVVQ // ID A0A089WC08_9ENTR Unreviewed; 426 AA. AC A0A089WC08; A0A089VZ61; DT 26-NOV-2014, integrated into UniProtKB/TrEMBL. DT 26-NOV-2014, sequence version 1. DT 30-AUG-2017, entry version 20. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=LH23_07665 {ECO:0000313|EMBL:AIR60534.1}; OS Cedecea neteri. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; OC Enterobacteriaceae; Cedecea. OX NCBI_TaxID=158822 {ECO:0000313|EMBL:AIR60534.1, ECO:0000313|Proteomes:UP000029516}; RN [1] {ECO:0000313|EMBL:AIR60534.1, ECO:0000313|Proteomes:UP000029516} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=M006 {ECO:0000313|EMBL:AIR60534.1, RC ECO:0000313|Proteomes:UP000029516}; RA Chan K.-G.; RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP009458; AIR60534.1; -; Genomic_DNA. DR RefSeq; WP_008453606.1; NZ_CP009459.1. DR EnsemblBacteria; AIR60534; AIR60534; LH23_07665. DR KEGG; cem:LH23_07665; -. DR KEGG; cen:LH86_07550; -. DR KO; K03665; -. DR Proteomes; UP000029516; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000029516}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000029516}. FT DOMAIN 198 365 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 426 AA; 47855 MW; F93C05B703176A92 CRC64; MFDRYDAGEQ AVLVHIYFSQ DKDMEDLAEF ESLVSSAGVE ALQVVTGSRK SPHPKYFVGE GKAVEIAEAV KATGASVVLF DHALSPAQER NLEALCQCRV IDRTGLILDI FAQRARTHEG KLQVELAQLR HLATRLVRGW THLERQKGGI GLRGPGETQL ETDRRLLRNR IMLILSRLER VEKQREQGRR SRNKADVPTI SLVGYTNAGK STLFNRITAA DVYAADQLFA TLDPTLRRID VADVGETVLA DTVGFIRHLP HDLVAAFKAT LQETRQATLL LHVIDAADFR MQENIAAVDT VLEEIEANEI PTLLVMNKID ALDEFEPRID RNDENVPIRV WLSAQTGAGV PLLFQALTER LSGEIAQHTL RLPPQAGRLR SRFYQLQAIE KEWTEEDGCV GLEVRMPIVD WRRLCKQEPA LADYIV // ID A0A089XCI0_STRGA Unreviewed; 499 AA. AC A0A089XCI0; DT 26-NOV-2014, integrated into UniProtKB/TrEMBL. DT 26-NOV-2014, sequence version 1. DT 30-AUG-2017, entry version 21. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=SGLAU_24980 {ECO:0000313|EMBL:AIS00934.1}; OS Streptomyces glaucescens. OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae; OC Streptomyces. OX NCBI_TaxID=1907 {ECO:0000313|EMBL:AIS00934.1, ECO:0000313|Proteomes:UP000029482}; RN [1] {ECO:0000313|Proteomes:UP000029482} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=GLA.O {ECO:0000313|Proteomes:UP000029482}; RX PubMed=25499805; DOI=10.1016/j.jbiotec.2014.11.036; RA Ortseifen V., Winkler A., Albersmeier A., Wendler S., Puhler A., RA Kalinowski J., Ruckert C.; RT "Complete genome sequence of the actinobacterium Streptomyces RT glaucescens GLA.O (DSM 40922) consisting of a linear chromosome and RT one linear plasmid."; RL J. Biotechnol. 194:81-83(2015). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP009438; AIS00934.1; -; Genomic_DNA. DR RefSeq; WP_043504643.1; NZ_CP009438.1. DR EnsemblBacteria; AIS00934; AIS00934; SGLAU_24980. DR KEGG; sgu:SGLAU_24980; -. DR KO; K03665; -. DR Proteomes; UP000029482; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 2. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000029482}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000029482}. FT DOMAIN 277 442 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 499 AA; 54636 MW; 01BFB0E4EE9C07F2 CRC64; MTSSSSPSQD TQRKRLAHDY PEGLRADALM EEDVAWSLEI DGERDGDQFD RSERAALRRV AGLSTELEDV TEVEYRQLRL ERVVLVGVWT SGTVQDAENS LAELAALAET AGALVLDGVI QRRDKPDAAT YIGSGKAEEL RDIVLETGAD TVICDGELSP GQLIHLEDVV KVKVIDRTAL ILDIFAQHAK SREGKAQVAL AQMQYMLPRL RGWGQSLSRQ MGGGKGGGLA TRGPGETKIE TDRRRIREKM AKMRREIAEM KTGRDIKRQE RRRHKVPSVA IAGYTNAGKS SLLNRLTGAG VLVENALFAT LDPTVRRAET PSGRLYTLAD TVGFVRHLPH HLVEAFRSTM EEVADSDLIL HVVDGSHPVP EEQLAAVREV IRDVGATDVP EIVVINKADA ADPLVLQRLL RIEKRSIAVS ARTGRGLPEL LALIDNELPR PAVEVEALVP YTHGKLVARA HDEGEVISEE HTAEGTLLKV RVHEELAAEL TPYAPASAV // ID A0A089Y8Y0_9PSED Unreviewed; 433 AA. AC A0A089Y8Y0; DT 26-NOV-2014, integrated into UniProtKB/TrEMBL. DT 26-NOV-2014, sequence version 1. DT 30-AUG-2017, entry version 19. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=LK03_03200 {ECO:0000313|EMBL:AIR88303.1}; OS Pseudomonas cremoricolorata. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=157783 {ECO:0000313|EMBL:AIR88303.1, ECO:0000313|Proteomes:UP000029493}; RN [1] {ECO:0000313|EMBL:AIR88303.1, ECO:0000313|Proteomes:UP000029493} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ND07 {ECO:0000313|EMBL:AIR88303.1, RC ECO:0000313|Proteomes:UP000029493}; RA Chan K.-G.; RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP009455; AIR88303.1; -; Genomic_DNA. DR RefSeq; WP_038411027.1; NZ_CP009455.1. DR EnsemblBacteria; AIR88303; AIR88303; LK03_03200. DR KEGG; psw:LK03_03200; -. DR KO; K03665; -. DR Proteomes; UP000029493; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000029493}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000029493}. FT DOMAIN 199 366 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 165 192 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 433 AA; 48963 MW; 6D1AEEB38414AE0E CRC64; MFFERHGGGE RALLVHLEGQ NPEAREDPQE FQELALSAGA EIVQLATVSR HQPTAKFLIG SGKVEELRDL VKTEHVDLVI FNHTLTPSQE RNLERVFECR VLDRTGLILD IFAQRARTHE GKLQVELAQL EHMSTRLVRG WTHLERQKGG IGMRGPGETQ LETDRRLLRV RLRQIKSRLE KVRSQREQAR RGRRRADIPS VSLVGYTNAG KSTLFNALTQ SEVFAADQLF ATLDPTLRRL ELADLGPIVL ADTVGFIRHL PHKLVEAFRA TLEESSNSDL LLHVIDAHEP ERMEQIEQVL AVLGEIGAQG LPILEVYNKL DLLEEVEPQI QRDADGKPQR VWVSARDGRG LELVGQAIAE LLGDDLFVGT LRLEQQYARL RAQFFSLGAV RSEAHDEQGS SLLDVRLPRV ELNRLVSREG LEPQVFIEQH TLQ // ID A0A089YY88_9PSED Unreviewed; 433 AA. AC A0A089YY88; DT 26-NOV-2014, integrated into UniProtKB/TrEMBL. DT 26-NOV-2014, sequence version 1. DT 30-AUG-2017, entry version 19. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=LT40_14060 {ECO:0000313|EMBL:AIS18445.1}; OS Pseudomonas rhizosphaerae. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=216142 {ECO:0000313|EMBL:AIS18445.1, ECO:0000313|Proteomes:UP000029499}; RN [1] {ECO:0000313|EMBL:AIS18445.1, ECO:0000313|Proteomes:UP000029499} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 16299 {ECO:0000313|EMBL:AIS18445.1}; RX PubMed=25483321; DOI=10.1016/j.jbiotec.2014.11.031; RA Kwak Y., Jung B.K., Shin J.H.; RT "Complete genome sequence of Pseudomonas rhizosphaerae IH5T (=DSM RT 16299T), a phosphate-solubilizing rhizobacterium for bacterial RT biofertilizer."; RL J. Biotechnol. 193:137-138(2015). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP009533; AIS18445.1; -; Genomic_DNA. DR RefSeq; WP_043191142.1; NZ_CP009533.1. DR EnsemblBacteria; AIS18445; AIS18445; LT40_14060. DR KEGG; prh:LT40_14060; -. DR KO; K03665; -. DR Proteomes; UP000029499; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000029499}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000029499}. FT DOMAIN 199 366 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 165 192 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 433 AA; 48588 MW; 25C4F045C6727379 CRC64; MFFERHGGGE RAILVHLDGQ DPEAREDPQE FQELAISAGA ETVAFVNVAR HRPSAKFLIG SGKVEELRDQ VKTEHADLVI FNHTLTPSQE RNLEKVFECR VLDRTGLILD IFAQRARTHE GKLQVELAQL EHMSTRLVRG WTHLERQGGG IGLRGPGETQ LETDRRLLRV RLRQIKQRLE KVRSQREQAR RGRRRADIPS VSLVGYTNAG KSTLFNAVTR SEVYAADQLF ATLDPTLRRL ELNDLGPVIL ADTVGFIRHL PHKLVEAFRA TLEESSNSDL LLHVIDAHEP ERMAQIEQVM AVLTEIGAQG LPILEVYNKL DLLEGVEPQI QRDADGKPVR VWVSARDGRG LELIKQAVAE LLGEDLFVGT LQLGQNLGRL RAQLFSLGAV QSEAHDEQGG SLLAIRLPRA ELNRLVSREG MEPAEFIEQH TLQ // ID A0A089ZL07_9LACO Unreviewed; 426 AA. AC A0A089ZL07; DT 26-NOV-2014, integrated into UniProtKB/TrEMBL. DT 26-NOV-2014, sequence version 1. DT 07-JUN-2017, entry version 16. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=LACWKB8_1547 {ECO:0000313|EMBL:AIS09801.1}; OS Lactobacillus sp. wkB8. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; OC Lactobacillus. OX NCBI_TaxID=1545702 {ECO:0000313|EMBL:AIS09801.1, ECO:0000313|Proteomes:UP000029494}; RN [1] {ECO:0000313|EMBL:AIS09801.1, ECO:0000313|Proteomes:UP000029494} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=wkB8 {ECO:0000313|Proteomes:UP000029494}; RA Kwong W.K., Moran N.A.; RT "Genomes of Lactobacillus 'Firm-5' strains."; RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP009531; AIS09801.1; -; Genomic_DNA. DR RefSeq; WP_038524122.1; NZ_CP009531.1. DR EnsemblBacteria; AIS09801; AIS09801; LACWKB8_1547. DR KEGG; law:LACWKB8_1547; -. DR KO; K03665; -. DR Proteomes; UP000029494; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000029494}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000029494}. FT DOMAIN 205 337 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 426 AA; 48046 MW; 0DADB83C1B3274DB CRC64; MIENTPRKAK AFIAGVNLND SNFDYYMTEL ANLTEAANME VVGQARQNAE HVVAGTYFGL GKINEIKDMA RGLKAKVLIL NDELTPVQIR NLEKLTKLRV IDRTELILEI FSKRARTKQA KLQVQLARLQ YELPRLHPSE NNLDQQRGNG GSTGGGFANR GAGESKLELN RRTIGKQIAI IKNELKEISQ QEEIKAKRRN QNNIPKVALV GYTNAGKSTT MNGLLQEFSK HSDKQVFVKN MLFATLDTNV RRIELDNNFS FILSDTVGFI SKLPHNLVES FKATLQEVRD ADLLINVVDA SDPNMIQMIR TTQNVLNEIG IKNTPMITAY NKADKSERNY PQIEGSNILY SATDPKSITT LANLITKRIF VNYKRTRLLL PLSDGKTLSY LHENAQIISE NFQNDGIHVT VRLAPEQQNR FSNYIV // ID A0A090AF43_9GAMM Unreviewed; 433 AA. AC A0A090AF43; DT 26-NOV-2014, integrated into UniProtKB/TrEMBL. DT 26-NOV-2014, sequence version 1. DT 30-AUG-2017, entry version 19. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=THII_2391 {ECO:0000313|EMBL:BAP56688.1}; OS Thioploca ingrica. OC Bacteria; Proteobacteria; Gammaproteobacteria; Thiotrichales; OC Thiotrichaceae; Thioploca. OX NCBI_TaxID=40754 {ECO:0000313|EMBL:BAP56688.1, ECO:0000313|Proteomes:UP000031623}; RN [1] {ECO:0000313|EMBL:BAP56688.1, ECO:0000313|Proteomes:UP000031623} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Kojima H., Ogura Y., Yamamoto N., Togashi T., Mori H., Watanabe T., RA Nemoto F., Kurokawa K., Hayashi T., Fukui M.; RT "Ecophysiology of Thioploca ingrica as revealed by the complete genome RT sequence supplemented with proteomic evidence."; RL ISME J. 0:0-0(2014). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AP014633; BAP56688.1; -; Genomic_DNA. DR RefSeq; WP_045475816.1; NZ_AP014633.1. DR EnsemblBacteria; BAP56688; BAP56688; THII_2391. DR KEGG; tig:THII_2391; -. DR KO; K03665; -. DR Proteomes; UP000031623; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000031623}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000031623}. FT DOMAIN 198 364 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 433 AA; 48608 MW; 5A471303FD921CBB CRC64; MFERPRQGER AILVHINMIG MFEPATLSEF EKLARAAGAI TVGQITGTRQ SPDPGYFVGK GKLQEIIALV QAQTVEVVLF NHTLTPTQER NLEQSLGCRV VDRTGVILDI FAQRARSFEG KLQVELAQLN YLSTRLVRGW THLERQRGGI GLRGPGETQL ETDRRLIAER IKTINKRLEK VTQQRELGRR ARQRAQLPVV ALVGYTNAGK STLFNRLTTA KAYVADQLFA TLDATLRRIQ LPNKMSVILA DTVGFIQQLP HDLVAAFRAT LEETRQASLL LHVVDASDTD RQWRIEQVNQ VLADIDAAEV PQLIIYNKID KLPPGSVPDE SSHTQVSKIW LSASQGKGID LLYTELAKYF DKEMVHYWVK VPVQAGELRA RLFTLGMVLQ EQYTDNGDSL LEIQMSAVYF NQLIKAEPAL QLIQPLASVY QAS // ID A0A090E5H9_9RHIZ Unreviewed; 462 AA. AC A0A090E5H9; DT 26-NOV-2014, integrated into UniProtKB/TrEMBL. DT 26-NOV-2014, sequence version 1. DT 07-JUN-2017, entry version 20. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:CDX22491.1}; GN ORFNames=MPLSOD_100087 {ECO:0000313|EMBL:CDX22491.1}; OS Mesorhizobium sp. SOD10. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Phyllobacteriaceae; Mesorhizobium. OX NCBI_TaxID=1505946 {ECO:0000313|EMBL:CDX22491.1, ECO:0000313|Proteomes:UP000045063}; RN [1] {ECO:0000313|EMBL:CDX22491.1, ECO:0000313|Proteomes:UP000045063} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Moulin Lionel; RL Submitted (AUG-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CCNA01000002; CDX22491.1; -; Genomic_DNA. DR RefSeq; WP_040994735.1; NZ_CCNA01000002.1. DR EnsemblBacteria; CDX22491; CDX22491; MPLSOD_100087. DR Proteomes; UP000045063; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000045063}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000045063}. FT DOMAIN 231 403 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 462 AA; 50681 MW; 2FA50463B76ECA3D CRC64; MARDKDADRS VRGKQGHQLG PEAKDPTRAV VIVPVLTRQP RGDDESSRPR LSRSADARHD EAVGLASAID LNPVHTAVVT VADPRPATLL GSGKVAEFAD IVKERKAELV IVDHPLTPVQ QRNLEKELNA KVLDRTGLIL EIFGERARTK EGTLQVELAH LNYQKGRLVR SWTHLERQRG GAGFLGGPGE TQIESDRRIL QDKITKLKHE LETVRRTRDL HRAKRKKVPF PVVAIVGYTN AGKSTLFNRL TGAGVLAEDM LFATLDPTLR RVRLPHGTPI ILSDTVGFIS DLPTHLVAAF RATLEEVVEA DLVLHLRDIS DPDTAAQAED VERILGDLGV DAADTNRVIE VWNKIDLLDE GNRERLLAEG ASGRRPPIAI SAVTGEGLDT LKALIESRVS GELETMTVTL SAAQLGQVDW LYRNGDVISR TDNEDGSVTL SLTATHSARQ EIESRLHRKN GS // ID A0A090HWU0_9FIRM Unreviewed; 433 AA. AC A0A090HWU0; DT 26-NOV-2014, integrated into UniProtKB/TrEMBL. DT 26-NOV-2014, sequence version 1. DT 07-JUN-2017, entry version 19. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=ING2D1G_0473 {ECO:0000313|EMBL:CDZ74656.1}; OS Peptoniphilus sp. ING2-D1G. OC Bacteria; Firmicutes; Tissierellia; Tissierellales; Peptoniphilaceae; OC Peptoniphilus. OX NCBI_TaxID=1912856 {ECO:0000313|EMBL:CDZ74656.1, ECO:0000313|Proteomes:UP000032409}; RN [1] {ECO:0000313|EMBL:CDZ74656.1, ECO:0000313|Proteomes:UP000032409} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Peptoniphilus sp. ING2-D1G {ECO:0000313|Proteomes:UP000032409}; RA Evans L.H., Alamgir A., Owens N., Weber N.D., Virtaneva K., RA Barbian K., Babar A., Rosenke K.; RL Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LM997412; CDZ74656.1; -; Genomic_DNA. DR RefSeq; WP_045077709.1; NZ_LM997412.1. DR KEGG; ped:ING2D1G_0473; -. DR PATRIC; fig|875453.3.peg.460; -. DR KO; K03665; -. DR Proteomes; UP000032409; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000032409}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000032409}. FT DOMAIN 209 377 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 175 202 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 433 AA; 49538 MW; A10A8389F39C0FAD CRC64; MENIKDKEIE KAIIVATDLG ARPYSMHTSL EELEDLTVAA GAEVRGVVSQ SLEKFNPKYL IGTGKVKEIR DMLVNLDIDL VIFNDELSGI QVRNLEKNFN DGRDFFDKKV KVLDRTNLIL DIFAQRASTY EGKLQVELAQ LEYQLPRLLG IDGWSRTGGG IGTRGPGEQI IETDRRRLLR EIDSIKAKLK KLEKTRDVMR SNRTKSKIST VSLVGYTNAG KSTILNRIKE RDSKEVFVKD MLFATLDPNS RRAKLPNGMD FIISDTVGFV SKLPTKLIEA FKSTLEEIKY SDLILHVIDA SSEDIEIQYK ITTDILKDLG IKGKKIITVF NKMDKVDGKQ FPINPEYAQN RIYISAKKDE NLDELLYAIE ESLSDKFYEV ELLIGYDRSD VLSDILNNHK YKDLSYVEDG TKIRVVLRDD EYERYKEYVI NHV // ID A0A090ICX2_9GAMM Unreviewed; 429 AA. AC A0A090ICX2; DT 26-NOV-2014, integrated into UniProtKB/TrEMBL. DT 26-NOV-2014, sequence version 1. DT 30-AUG-2017, entry version 19. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:CED58432.1}; GN ORFNames=MVIS_0401 {ECO:0000313|EMBL:CED58432.1}; OS Moritella viscosa. OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales; OC Moritellaceae; Moritella. OX NCBI_TaxID=80854 {ECO:0000313|EMBL:CED58432.1, ECO:0000313|Proteomes:UP000032438}; RN [1] {ECO:0000313|EMBL:CED58432.1} RP NUCLEOTIDE SEQUENCE. RA Hjerde Erik; RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LN554852; CED58432.1; -; Genomic_DNA. DR RefSeq; WP_045108863.1; NZ_LN554852.1. DR EnsemblBacteria; CED58432; CED58432; MVIS_0401. DR GeneID; 31932602; -. DR KEGG; mvs:MVIS_0401; -. DR PATRIC; fig|80854.5.peg.427; -. DR KO; K03665; -. DR Proteomes; UP000032438; Chromosome complete sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000032438}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Hydrolase {ECO:0000313|EMBL:CED58432.1}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000032438}. FT DOMAIN 198 365 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 429 AA; 48590 MW; 002D4CA91BC6BCFB CRC64; MFDRHEAGER AILVHVNFND EGNREDLHEL EMLVSSAGVN ALSVVTGSRS RPHPKYFVGS GKAEEIAEAV KLHQADIVIF NHALAPRQER NLEALLECRV VDRTGLILDI FSQRARTHEG KLQVELAQLR HMSTRLIRGW THLERQKGGI GMRGPGETQL ETDRRLLRVR MDSILRRLDK VVTKRDQGRR SRKRREIPTI SLVGYTNAGK STLFNRLTDS KVYAADQLFA TLDPTLRRIA VADVGEVVLA DTVGFIRHLP HDLVAAFKAT LTETREADLL LHVIDCADEN MRGNITEVNS VLTEIDAGEV PVLMVYNKVD KLDDGRCRID YDDEGKPVSV WLSAMSGEGT AFLYQALTEL LASTMKVVRL QLPAMQGNVV SHLYNLDCIE HEAFSENGDW LLDIRMTMID WQRLKKHKCN NIEDFILQR // ID A0A090IE13_9GAMM Unreviewed; 451 AA. AC A0A090IE13; DT 26-NOV-2014, integrated into UniProtKB/TrEMBL. DT 26-NOV-2014, sequence version 1. DT 07-JUN-2017, entry version 18. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=MVIS_0900 {ECO:0000313|EMBL:CED58912.1}; OS Moritella viscosa. OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales; OC Moritellaceae; Moritella. OX NCBI_TaxID=80854 {ECO:0000313|EMBL:CED58912.1, ECO:0000313|Proteomes:UP000032438}; RN [1] {ECO:0000313|EMBL:CED58912.1} RP NUCLEOTIDE SEQUENCE. RA Hjerde Erik; RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LN554852; CED58912.1; -; Genomic_DNA. DR EnsemblBacteria; CED58912; CED58912; MVIS_0900. DR KEGG; mvs:MVIS_0900; -. DR PATRIC; fig|80854.5.peg.951; -. DR KO; K03665; -. DR Proteomes; UP000032438; Chromosome complete sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000032438}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000032438}. FT DOMAIN 229 398 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 451 AA; 50641 MW; 4A70AD4C1FADBB54 CRC64; MSTDMSITTT EHSVTRALLI SIRTPCTTQQ DVDESLSELG RLVHTLGFSV VGTKTQRQKS TKQLSVLGAG KLEELASLTG ESTFYEDEVQ IELDQDELSQ LLATTDVKCQ ANIVVFDCEL SPNQLSNVKA ALGVEVYDRT RVIIEIFSKH ARTRTAKLQV EIARLNYLTP RLRDESSGDR ERQKGRSISE TVFEINRRRV RTKIAELRRE LTKVQREMQG RSSGRIEQLT VALVGYTNAG KSSLMRALTG SEVLVEDKLF ATLDTTIRTL QPPTQPRILI SDTVGFIQKL PHDLVASFHS TLEEAKNADL LLYVVDASDE NFISQLAIVD HVLGQLNIDL NNKVLLLNKV DCLNEEQQLD LLERYPDALQ ISAHDKGDVA FVHQEIQNLL EKKMCPACFD IPYTASGVIG EIHSKMQVLE EEYHEKGIRI TLKASPVALE RLHKMLQLTT F // ID A0A090ITX9_9BACI Unreviewed; 421 AA. AC A0A090ITX9; DT 07-JAN-2015, integrated into UniProtKB/TrEMBL. DT 07-JAN-2015, sequence version 1. DT 05-JUL-2017, entry version 22. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:CEE01521.1}; GN ORFNames=B4166_0383 {ECO:0000313|EMBL:KIO70973.1}, GN B4167_0493 {ECO:0000313|EMBL:KIO74215.1}, GN BT1A1_1693 {ECO:0000313|EMBL:CEE01521.1}; OS Bacillus thermoamylovorans. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus. OX NCBI_TaxID=35841 {ECO:0000313|EMBL:CEE01521.1, ECO:0000313|Proteomes:UP000040576}; RN [1] {ECO:0000313|EMBL:CEE01521.1, ECO:0000313|Proteomes:UP000040576} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Wibberg Daniel; RL Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:KIO70973.1, ECO:0000313|Proteomes:UP000032076, ECO:0000313|Proteomes:UP000032097} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=B4166 {ECO:0000313|EMBL:KIO70973.1, RC ECO:0000313|Proteomes:UP000032097}, and RC B4167 {ECO:0000313|EMBL:KIO74215.1, RC ECO:0000313|Proteomes:UP000032076}; RA Krawcyk A.O., Berendsen E.M., Eijlander R.T., de Jong A., RA Wells-Bennik M., Kuipers O.P.; RT "Draft Genome Sequences of Four Bacillus thermoamylovorans Strains, RT Isolated From Food Products."; RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CCRF01000049; CEE01521.1; -; Genomic_DNA. DR EMBL; JXLT01000005; KIO70973.1; -; Genomic_DNA. DR EMBL; JXLU01000010; KIO74215.1; -; Genomic_DNA. DR RefSeq; WP_034769980.1; NZ_JXLU01000010.1. DR EnsemblBacteria; CEE01521; CEE01521; BT1A1_1693. DR EnsemblBacteria; KIO70973; KIO70973; B4166_0383. DR EnsemblBacteria; KIO74215; KIO74215; B4167_0493. DR PATRIC; fig|35841.7.peg.3435; -. DR Proteomes; UP000032076; Unassembled WGS sequence. DR Proteomes; UP000032097; Unassembled WGS sequence. DR Proteomes; UP000040576; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000040576}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000040576}. FT DOMAIN 198 360 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 421 AA; 48068 MW; 1F1916908CCCAD16 CRC64; MENAREKVIV VGCQLPEMDD FRFENSMEEL VSLTDTANGE VILRVTQKRD KPDSSTYLGK GKVEELRNLI EELEVDVVIF NSELTPSQLR NLSNQLQTKI IDRTQLILDI FARRAKSREG KLQVELAQLE YLLPRLVGQG TELSRLGGGI GTRGPGETKL ETDRRHIRNR INEIKNQLSV IVEHRKRYRS NRKKKNTYQI ALIGYTNAGK STLFNRLTVA ASYEENKLFA TLDPLTRKLV LHSGFTVLLS DTVGFIEDLP TTLVAAFRST LEEVAEADLL LHVIDASNPD YDQHEKTVNK ILKELHAEKI PQLVLYNKMD RVHNDFVPTA DGKVLQISAL NLADRERLKR KIEEMMIEEM VQYEVNLPST SGKLLARLKE ETILRELKFL ESDETYQCKG YIFAHSPLYG EIKKQNDGDG E // ID A0A090L3K9_STRRB Unreviewed; 1118 AA. AC A0A090L3K9; DT 26-NOV-2014, integrated into UniProtKB/TrEMBL. DT 26-NOV-2014, sequence version 1. DT 30-AUG-2017, entry version 17. DE SubName: Full=Putative GTP-binding protein 6 {ECO:0000313|EMBL:CEF64292.1, ECO:0000313|WBParaSite:SRAE_1000254700}; GN ORFNames=SRAE_1000254700 {ECO:0000313|EMBL:CEF64292.1, GN ECO:0000313|WormBase:SRAE_1000254700}; OS Strongyloides ratti (Parasitic roundworm). OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida; OC Panagrolaimoidea; Strongyloididae; Strongyloides. OX NCBI_TaxID=34506 {ECO:0000313|EMBL:CEF64292.1, ECO:0000313|Proteomes:UP000035682}; RN [1] {ECO:0000313|WBParaSite:SRAE_1000254700} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ED321 {ECO:0000313|WBParaSite:SRAE_1000254700}; RA Magalhaes I.L.F., Oliveira U., Santos F.R., Vidigal T.H.D.A., RA Brescovit A.D., Santos A.J.; RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:CEF64292.1, ECO:0000313|Proteomes:UP000035682} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ED321 {ECO:0000313|Proteomes:UP000035682}, and RC ED321 Heterogonic {ECO:0000313|EMBL:CEF64292.1}; RA Martin A.A.; RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases. RN [3] {ECO:0000313|WBParaSite:SRAE_1000254700} RP IDENTIFICATION. RG WormBaseParasite; RL Submitted (JAN-2017) to UniProtKB. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LN609528; CEF64292.1; -; Genomic_DNA. DR EnsemblMetazoa; SRAE_1000254700; SRAE_1000254700; WBGene00259162. DR WBParaSite; SRAE_1000254700; SRAE_1000254700; WBGene00259162. DR WormBase; SRAE_1000254700; SRP08833; WBGene00259162; -. DR Proteomes; UP000035682; Chromosome 1. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR006594; LisH. DR InterPro; IPR027417; P-loop_NTPase. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR PROSITE; PS51705; G_HFLX; 1. DR PROSITE; PS50896; LISH; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000035682}; KW Reference proteome {ECO:0000313|Proteomes:UP000035682}. FT DOMAIN 47 79 LisH. {ECO:0000259|PROSITE:PS50896}. FT DOMAIN 884 1056 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 1118 AA; 125850 MW; B1C1956A9896E21F CRC64; MKKNFHYFFD CNINANISLF AYTHTSVGLI IDKMAVPYLN RDYEKNIISE VESLFVDYLT RHKLSKTLDA FMQECICYKK NYSQTSDRSL IQNSHSTIED LVMNANFREN ANKKYLFSTC KSFVDAIAEN SHRLINLICE NSISANTKED LNDFKNRQHF SHPFISEGNL NNNRTFIYSQ GSVHNGSISH DSSGAMSYET PYSSRFVSNT CSSNIVPSNL PNVTLYPHNG QSFMYRSESF ALSSGEGNGF RPIDGSCLTS PGNRVNVNCD GSMDYGSYFV PNGSSTPRII GNDLGVKKGT HVVIQGGNLP TPNYFLNSNS NKFMHGSDDH ISPSQYGGHL HIENKNILND NRMQNFSGHS PNTPSGVTSN SSVEVKEKKS RANSSLKSTA KSRILKEGNR ASTVSKRKND SPGEGNGKKV QKLDNGDGYR SGVLDFQTTV SPSQFRKAAR DVDLEKEPHL AKQYSPISNQ VGKHFKPENL LNVSKFKNEK IQSISGRKEQ FVQISGRTLN SSLNISGFGK KNADKNKVTS SKDSVFKSPN QINSPKNDDN LMKDSSKVSS SQDQSSVNSN NFEDNVGDST GVDRHYNPYE LCQVDNSLEF NSECNFDLDS NVFYDPGRDL ELFDEIGSLF FPSKIVLRSR ILKCRNLCSD VKEEIDQSFL EMDINATSSA IDQHSFLVIH PKIRWGQNAT PPKERNDELQ LEEAISLIKS IPGFSVSQSA IVGTDYTLKK KLIWGKGRIE NLLQLKSSCR VSAMMVNVDC LTPLQQSELY NVFQIPIYDR YNIVLKIFRL YAKTKLAYYQ IQLAEIPYIK HRLHYLNNSS CNPDILHVSS ALNALSKSGL DQKEALRLRE QALRKKIKNC IEASKTEIVE KKNRQDKKNA YNSLTAAVIG YTNVGKTTFI KRLTGSSQLN PEDRLFATLD TTIHSFLLPS KNKIFIADTI GFMGSLPVGL FESFSATLMH AISADLLIHL YDLSHPDVLA QKKNVLKSLI DLNFPDELIK NMINVGNKID KISDNDKFEL TENGILNNND LVISCTTGYG IEELISKIDK TIMNMNNSRM RRFKLKPESK IISYFYENNL VTKEPVVSEC GKYLIFDVYL NDNQLNKLTK HMNLKKKQ // ID A0A090M260_OSTTA Unreviewed; 567 AA. AC A0A090M260; DT 26-NOV-2014, integrated into UniProtKB/TrEMBL. DT 26-NOV-2014, sequence version 1. DT 12-APR-2017, entry version 15. DE SubName: Full=p-loop containing nucleoside triphosphate hydrolase {ECO:0000313|EMBL:CEF98320.1}; DE Flags: Fragment; GN ORFNames=OT_ostta06g01810 {ECO:0000313|EMBL:CEF98320.1}; OS Ostreococcus tauri. OC Eukaryota; Viridiplantae; Chlorophyta; prasinophytes; Mamiellophyceae; OC Mamiellales; Bathycoccaceae; Ostreococcus. OX NCBI_TaxID=70448 {ECO:0000313|EMBL:CEF98320.1, ECO:0000313|Proteomes:UP000009170}; RN [1] {ECO:0000313|Proteomes:UP000009170} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=OTTH0595 {ECO:0000313|Proteomes:UP000009170}; RX PubMed=16868079; DOI=10.1073/pnas.0604795103; RA Derelle E., Ferraz C., Rombauts S., Rouze P., Worden A.Z., Robbens S., RA Partensky F., Degroeve S., Echeynie S., Cooke R., Saeys Y., Wuyts J., RA Jabbari K., Bowler C., Panaud O., Piegu B., Ball S.G., Ral J.-P., RA Bouget F.-Y., Piganeau G., De Baets B., Picard A., Delseny M., RA Demaille J., Van de Peer Y., Moreau H.; RT "Genome analysis of the smallest free-living eukaryote Ostreococcus RT tauri unveils many unique features."; RL Proc. Natl. Acad. Sci. U.S.A. 103:11647-11652(2006). CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:CEF98320.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CAID01000006; CEF98320.1; -; Genomic_DNA. DR STRING; 70448.Q017F5; -. DR eggNOG; KOG0410; Eukaryota. DR eggNOG; COG2262; LUCA. DR Proteomes; UP000009170; Chromosome 6. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 2. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000009170}; KW Hydrolase {ECO:0000313|EMBL:CEF98320.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000009170}. FT DOMAIN 335 503 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT NON_TER 1 1 {ECO:0000313|EMBL:CEF98320.1}. SQ SEQUENCE 567 AA; 63534 MW; A1696184945B9A9C CRC64; XXRARARAPS DGALDDAFER LIVDVDALPR VDVDDGALET MTWEEIIERA HGTAIERGDD ALRTRARDAR IREDMWGWAH EPERVVVCGV GAKDGRMTMR GEFELEDSLD ELERLAATAG CAVVGRMTQR LARGAVPATY LGRGKIGELR ELCGLPRALE DEAEEDDEEE WDDEDEDMDW GDEDDYEDPE PERRQDRRNG YNIDAASVDM VIFDDELSPK QARNLERRLG DKVRVCDRTA LILDIFSQRA QTAEGQLQVE LAQLEYQMPR LSKMWSHLER QVGGGKGNVK GMGEKQLEVD KRLLRERKSL LTAKIESVRT HREQYRQKRK AERIPIVSLA GYTNAGKSTL LNKLTKSDVL AEDKLFATLD PTTRRLGLPN GMSVLMTDTV GFIQKLPTQL VAAFRATLEE VLESSLILHV VDISSELAEV QMSAVNNVLD ELDASHIPQL LVWNKIDLVT DEEKMLEIEI AAEAAGAVLI STHTGEGLDA LQEKVSAIIM RSALTRCELL VPYERGALIG EMRRSGFIET EEFLENGTRV VAYLPVGMAR RRDVVGYLAR ASRADDS // ID A0A090P518_9VIBR Unreviewed; 429 AA. AC A0A090P518; DT 26-NOV-2014, integrated into UniProtKB/TrEMBL. DT 26-NOV-2014, sequence version 1. DT 30-AUG-2017, entry version 18. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=JCM19238_2418 {ECO:0000313|EMBL:GAK84840.1}; OS Vibrio ponticus. OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; OC Vibrionaceae; Vibrio. OX NCBI_TaxID=265668 {ECO:0000313|EMBL:GAK84840.1, ECO:0000313|Proteomes:UP000029122}; RN [1] {ECO:0000313|EMBL:GAK84840.1, ECO:0000313|Proteomes:UP000029122} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=JCM 19238 {ECO:0000313|EMBL:GAK84840.1, RC ECO:0000313|Proteomes:UP000029122}; RA Al-saari N., Meirelles P.M., Mino S., Suda W., Oshima K., Hattori M., RA Ohkuma M., Thompson F.L., Gomez-Gil B., Sawabe T., Sawabe T.; RT "Draft Genome Sequences of Two Vibrionaceae Species, Vibrio ponticus RT C121 and Photobacterium aphoticum C119, Isolated as Coral Reef RT Microbiota."; RL Genome Announc. 2:e01095-14(2014). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:GAK84840.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BBMI01000032; GAK84840.1; -; Genomic_DNA. DR EnsemblBacteria; GAK84840; GAK84840; JCM19238_2418. DR Proteomes; UP000029122; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000029122}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000029122}. FT DOMAIN 198 365 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 429 AA; 48706 MW; 2534E2C25B0F7241 CRC64; MFDRYEAGER AVLVHINFTQ EGEWEDLNEF EMLVSSAGVS SLHVVTGSRQ SPLPKYYVGE GKAQEIAQIV QSTDADIVIF NHALSPAQER NLEALCQCRV VDRTGLILDI FAQRARTHEG KLQVELAQLR HISTRLIRGW THLERQKGGI GLRGPGETQL ETDRRLLRER IKAILRRLER VAKQREQGRR ARSRAEIPTI SLVGYTNAGK STLFNRITQA GVYAADQLFA TLDPTLRKID LADVGTAILA DTVGFIRHLP HDLVAAFKAT LQETQEADIL LHVVDASDER FRENMQAVQE VLEEIDAHEV PALVVMNKID NLDGQEPRIE RDEEGIPRTV WVSAMEGKGI DLLFTALTER LASQMVQYQL CIPPQHQGRL RSTFFQMNCI QQEEYDQDGN LLINIRMQQV DWSRLEKREG AVLRDFIVT // ID A0A090QKX6_9FLAO Unreviewed; 402 AA. AC A0A090QKX6; DT 26-NOV-2014, integrated into UniProtKB/TrEMBL. DT 26-NOV-2014, sequence version 1. DT 07-JUN-2017, entry version 20. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=JCM19294_2958 {ECO:0000313|EMBL:GAK96176.1}; OS Nonlabens sediminis. OC Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales; OC Flavobacteriaceae; Nonlabens. OX NCBI_TaxID=319236 {ECO:0000313|EMBL:GAK96176.1, ECO:0000313|Proteomes:UP000029221}; RN [1] {ECO:0000313|EMBL:GAK96176.1, ECO:0000313|Proteomes:UP000029221} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=JCM19294 {ECO:0000313|Proteomes:UP000029221}; RA Nakanishi M., Meirelles P., Suzuki R., Takatani N., Mino S., Suda W., RA Oshima K., Hattori M., Ohkuma M., Hosokawa M., Miyashita K., RA Thompson F.L., Niwa A., Sawabe T., Sawabe T.; RT "Draft Genome Sequences of Marine Flavobacterium Nonlabens Strains RT NR17, NR24, NR27, NR32, NR33, and Ara13."; RL Genome Announc. 2:e01165-14(2014). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:GAK96176.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BBML01000001; GAK96176.1; -; Genomic_DNA. DR RefSeq; WP_042277191.1; NZ_BBML01000001.1. DR EnsemblBacteria; GAK96176; GAK96176; JCM19294_2958. DR Proteomes; UP000029221; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000029221}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000029221}. FT DOMAIN 200 383 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 402 AA; 46675 MW; 669F52088CC71026 CRC64; MLEQESHEYE NAVLIGIVTQ QQSEEKLTEY LDELEFLAYT AGASVKGRFT QKMQHPNPKT FIGTGKMEEV AQFVEANDIG TVIFDDELTP TQQRNIEKIL KAKIIDRTYL ILDIFAQRAQ TSYARTQVEL AQYEYLLPRL VGLWTHLERQ RGGIGMRGPG ETEIETDRRI VRDRISLLKK KLTTIDRQMK TQRGNRGKLV RVALVGYTNV GKSTLMNVVS KSDVFAENKL FATLDTTVRK VVVKNLPFLL TDTVGFIRKL PTQLVESFKS TLDEVRESDL LLHVVDISHE SFEDHIDSVN AILQDIEAID KPTIMVFNKI DQYQPEEYDD EFDERTTAHN TLEDWKRTWM NRAGDDVIFI SAIEKENMEQ FRKKVYDRVR EIHVSRFPYN AFLYPDYSEE EE // ID A0A090RK19_9VIBR Unreviewed; 79 AA. AC A0A090RK19; DT 26-NOV-2014, integrated into UniProtKB/TrEMBL. DT 26-NOV-2014, sequence version 1. DT 16-MAR-2016, entry version 6. DE SubName: Full=GTP-binding protein HflX {ECO:0000313|EMBL:GAL15805.1}; GN ORFNames=JCM19233_6827 {ECO:0000313|EMBL:GAL15805.1}; OS Vibrio sp. C7. OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; OC Vibrionaceae; Vibrio. OX NCBI_TaxID=1001886 {ECO:0000313|EMBL:GAL15805.1, ECO:0000313|Proteomes:UP000029225}; RN [1] {ECO:0000313|EMBL:GAL15805.1, ECO:0000313|Proteomes:UP000029225} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=JCM19233 {ECO:0000313|Proteomes:UP000029225}; RA Sawabe T., Meirelles P., Nakanishi M., Sayaka M., Hattori M., RA Ohkuma M.; RT "Vibrio sp. JCM 19233. (C7) whole genome shotgun sequence."; RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:GAL15805.1, ECO:0000313|Proteomes:UP000029225} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=JCM19233 {ECO:0000313|Proteomes:UP000029225}; RG NBRP consortium; RA Sawabe T., Meirelles P., Nakanishi M., Sayaka M., Hattori M., RA Ohkuma M.; RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:GAL15805.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BBMQ01000302; GAL15805.1; -; Genomic_DNA. DR EnsemblBacteria; GAL15805; GAL15805; JCM19233_6827. DR Proteomes; UP000029225; Unassembled WGS sequence. DR InterPro; IPR025121; GTPase_HflX_N. DR Pfam; PF13167; GTP-bdg_N; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000029225}; KW Reference proteome {ECO:0000313|Proteomes:UP000029225}. FT DOMAIN 25 65 GTP-bdg_N. {ECO:0000259|Pfam:PF13167}. SQ SEQUENCE 79 AA; 8922 MW; 0C069035E1E9141F CRC64; MFDRYEAGER AVLVHINFTQ EGEWEDLVEF EMLVSSSGVQ SLQVITGSRQ SPHPKYYVGE GKARKSLKQF SVKSGRGDL // ID A0A090STP0_9VIBR Unreviewed; 429 AA. AC A0A090STP0; DT 26-NOV-2014, integrated into UniProtKB/TrEMBL. DT 26-NOV-2014, sequence version 1. DT 30-AUG-2017, entry version 18. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=JCM19239_826 {ECO:0000313|EMBL:GAL29849.1}; OS Vibrio variabilis. OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; OC Vibrionaceae; Vibrio. OX NCBI_TaxID=990271 {ECO:0000313|EMBL:GAL29849.1, ECO:0000313|Proteomes:UP000029223}; RN [1] {ECO:0000313|EMBL:GAL29849.1, ECO:0000313|Proteomes:UP000029223} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=JCM 19239 {ECO:0000313|EMBL:GAL29849.1, RC ECO:0000313|Proteomes:UP000029223}; RA Sawabe T., Meirelles P., Nakanishi M., Sayaka M., Hattori M., RA Ohkuma M.; RT "Vibrio variabilis JCM 19239. (C206) whole genome shotgun sequence."; RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:GAL29849.1, ECO:0000313|Proteomes:UP000029223} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=JCM 19239 {ECO:0000313|EMBL:GAL29849.1, RC ECO:0000313|Proteomes:UP000029223}; RG NBRP consortium; RA Sawabe T., Meirelles P., Nakanishi M., Sayaka M., Hattori M., RA Ohkuma M.; RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:GAL29849.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BBMS01000075; GAL29849.1; -; Genomic_DNA. DR EnsemblBacteria; GAL29849; GAL29849; JCM19239_826. DR Proteomes; UP000029223; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000029223}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000029223}. FT DOMAIN 198 365 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 429 AA; 48707 MW; 9E92DCE0E684F828 CRC64; MFDRYESGEQ AVLVHINFTQ EGEWEDLSEF EMLVSSAGVN ALQTVTGSRQ SPHPKYYVGE GKAQEIAQTV QLTGADIVIF NHALSPAQER NLESLCKCRV LDRTGLILDI FAQRARTHEG KLQVELAQLR HISTRLIRGW THLERQKGGI GLRGPGETQL ETDRRLLRDR IKAILRRLEK VAKQREQGRR ARNRAEIPTI SLVGYTNAGK STLFNRITEA GVYAADQLFA TLDPTLRKIE LADVGSAILA DTVGFIRHLP HDLVAAFKAT LQETQEADIL LHVVDASDER FRENIQAVHD VLEEIDADEV PTLVVMNKID NLDGQRPRIE RDDEGIPRTV WVSAMEGQGI ELLFEALTER LASQMVQYQL RIPPQFQGRF RSTFFQMNCI QREEYDSEGN LLIDIRMQQV DWSRLEKREG AVLGDFIVT // ID A0A090TE27_9VIBR Unreviewed; 105 AA. AC A0A090TE27; DT 26-NOV-2014, integrated into UniProtKB/TrEMBL. DT 26-NOV-2014, sequence version 1. DT 16-MAR-2016, entry version 8. DE SubName: Full=GTP-binding protein HflX {ECO:0000313|EMBL:GAL38151.1}; GN ORFNames=JCM19240_3115 {ECO:0000313|EMBL:GAL38151.1}; OS Vibrio maritimus. OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; OC Vibrionaceae; Vibrio. OX NCBI_TaxID=990268 {ECO:0000313|EMBL:GAL38151.1, ECO:0000313|Proteomes:UP000029224}; RN [1] {ECO:0000313|EMBL:GAL38151.1, ECO:0000313|Proteomes:UP000029224} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=JCM 19240 {ECO:0000313|EMBL:GAL38151.1, RC ECO:0000313|Proteomes:UP000029224}; RA Sawabe T., Meirelles P., Nakanishi M., Sayaka M., Hattori M., RA Ohkuma M.; RT "Vibrio maritimus JCM 19240. (C210) whole genome shotgun sequence."; RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:GAL38151.1, ECO:0000313|Proteomes:UP000029224} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=JCM 19240 {ECO:0000313|EMBL:GAL38151.1, RC ECO:0000313|Proteomes:UP000029224}; RG NBRP consortium; RA Sawabe T., Meirelles P., Nakanishi M., Sayaka M., Hattori M., RA Ohkuma M.; RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:GAL38151.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BBMT01000028; GAL38151.1; -; Genomic_DNA. DR EnsemblBacteria; GAL38151; GAL38151; JCM19240_3115. DR Proteomes; UP000029224; Unassembled WGS sequence. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF13167; GTP-bdg_N; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000029224}; KW Reference proteome {ECO:0000313|Proteomes:UP000029224}. FT DOMAIN 25 99 GTP-bdg_N. {ECO:0000259|Pfam:PF13167}. SQ SEQUENCE 105 AA; 11600 MW; 6A94402E6C7761EA CRC64; MFDRYESGEQ AVLVHINFTQ EGEWEDLSEF EMLVSSAGVN ALQTVTGSRQ SPHPKYYVGE GKAQEIAQTV QLTGADIVIF NHALSPAKSV TLKVCVNVEC WIVQV // ID A0A090V0X5_ESCVU Unreviewed; 426 AA. AC A0A090V0X5; DT 26-NOV-2014, integrated into UniProtKB/TrEMBL. DT 26-NOV-2014, sequence version 1. DT 30-AUG-2017, entry version 21. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:GAL56929.1}; GN ORFNames=EV102420_02_05340 {ECO:0000313|EMBL:GAL56929.1}; OS Escherichia vulneris NBRC 102420. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=1115515 {ECO:0000313|EMBL:GAL56929.1, ECO:0000313|Proteomes:UP000029462}; RN [1] {ECO:0000313|EMBL:GAL56929.1, ECO:0000313|Proteomes:UP000029462} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NBRC 102420 {ECO:0000313|EMBL:GAL56929.1, RC ECO:0000313|Proteomes:UP000029462}; RA Yoshida Y., Hosoyama A., Tsuchikane K., Ohji S., Ichikawa N., RA Kimura A., Yamazoe A., Ezaki T., Fujita N.; RT "Whole genome shotgun sequence of Escherichia vulneris NBRC 102420."; RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:GAL56929.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BBMZ01000002; GAL56929.1; -; Genomic_DNA. DR RefSeq; WP_042388548.1; NZ_BBMZ01000002.1. DR EnsemblBacteria; GAL56929; GAL56929; EV102420_02_05340. DR Proteomes; UP000029462; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000029462}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000029462}. FT DOMAIN 198 365 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 426 AA; 48098 MW; D370144693CDB597 CRC64; MFDRYDAGEQ AVLVHIYFSQ DKDMEDLQEF ESLVSSAGVD AMQVITGSRK APHPKYFVGE GKAVEIADAV KASGASVVLF DHALTPAQER NLERLCECRV IDRTGLILDI FAQRARTHEG KLQVELAQLR HLATRLVRGW THLERQKGGI GLRGPGETQL ETDRRLLRNR ITLILSRLER VSKQREQGRR SRAKADIPTV SLVGYTNAGK STLFNQITEA QVYAADQLFA TLDPTLRRIN VADVGETVLA DTVGFIRHLP HDLVAAFKAT LQETREATLL LHVIDAADLR LQENIDAVNT VLEEIDAHEI PTLLVMNKID MLDEFEPRID RDDENRPIRV WLSAQTGAGV PLLFQALTER LSGEVAQHTL HLPPQEGRLR SRFYQLQAIE KEWMEEDGSL GLQVRMPIVD WRRLCKQEPA LVDYVV // ID A0A090VDA4_9FLAO Unreviewed; 405 AA. AC A0A090VDA4; DT 26-NOV-2014, integrated into UniProtKB/TrEMBL. DT 26-NOV-2014, sequence version 1. DT 07-JUN-2017, entry version 22. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=JCM19300_3319 {ECO:0000313|EMBL:GAL62751.1}, GN SAMN04489722_104162 {ECO:0000313|EMBL:SFC96082.1}; OS Algibacter lectus. OC Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales; OC Flavobacteriaceae; Algibacter. OX NCBI_TaxID=221126 {ECO:0000313|EMBL:GAL62751.1, ECO:0000313|Proteomes:UP000029644}; RN [1] {ECO:0000313|EMBL:GAL62751.1, ECO:0000313|Proteomes:UP000029644} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=JCM 19300 {ECO:0000313|EMBL:GAL62751.1, RC ECO:0000313|Proteomes:UP000029644}; RA Takatani N., Nakanishi M., Meirelles P., Mino S., Suda W., Oshima K., RA Hattori M., Ohkuma M., Hosokawa M., Miyashita K., Thompson F.L., RA Niwa A., Sawabe T., Sawabe T.; RT "Draft Genome Sequences of Marine Flavobacterium Algibacter lectus RT Strains SS8 and NR4."; RL Genome Announc. 2:e01168-14(2014). RN [2] {ECO:0000313|EMBL:SFC96082.1, ECO:0000313|Proteomes:UP000182021} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 15365 {ECO:0000313|EMBL:SFC96082.1, RC ECO:0000313|Proteomes:UP000182021}; RA de Groot N.N.; RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BBNQ01000008; GAL62751.1; -; Genomic_DNA. DR EMBL; FOLN01000004; SFC96082.1; -; Genomic_DNA. DR RefSeq; WP_042504644.1; NZ_FOLN01000004.1. DR EnsemblBacteria; GAL62751; GAL62751; JCM19300_3319. DR Proteomes; UP000029644; Unassembled WGS sequence. DR Proteomes; UP000182021; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000029644}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000029644}. FT DOMAIN 200 385 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 405 AA; 46690 MW; CF43776FDE48D24D CRC64; MIEEKDISLE RAVLIGVITK EQDEEKSKEY LDELEFLTYT AGGYAIKRFT QKMDMPNPKT FIGTGKIEDV RVFIEENDIT TAIFDDELSS AQERNISKIL NVKVLDRTNL ILDIFAQRAQ TSYARTQVEL AQCQYLLPRL RGMWTHLERQ KGGIGMRGPG ETEIETDRRI VRDKIALLKD RIKIIDKQMA VQRGNRGKMV RVALVGYTNV GKSTLMNVIS KSDVFAENKL FATLDTTVRK VVIQNLPFLL SDTVGFIRKL PTQLVDSFKS TLDEVREADL LLHVVDISHP NFEEHIASVE KILGEIKSGD KPTIMVFNKI DAYSAEHLDD DDLETERGAR HYSLDEWKST WMSKVGNNAL FISALNKKNL EDFKKRVYDE VREIHVTRFP YNQFLYPDYD YEDME // ID A0A090ZEE8_PAEMA Unreviewed; 440 AA. AC A0A090ZEE8; DT 26-NOV-2014, integrated into UniProtKB/TrEMBL. DT 26-NOV-2014, sequence version 1. DT 07-JUN-2017, entry version 19. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:KFN08818.1}; GN ORFNames=DJ90_5003 {ECO:0000313|EMBL:KFN08818.1}; OS Paenibacillus macerans (Bacillus macerans). OC Bacteria; Firmicutes; Bacilli; Bacillales; Paenibacillaceae; OC Paenibacillus. OX NCBI_TaxID=44252 {ECO:0000313|EMBL:KFN08818.1, ECO:0000313|Proteomes:UP000029278}; RN [1] {ECO:0000313|EMBL:KFN08818.1, ECO:0000313|Proteomes:UP000029278} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=8244 {ECO:0000313|EMBL:KFN08818.1, RC ECO:0000313|Proteomes:UP000029278}; RA Bishop-Lilly K.A., Broomall S.M., Chain P.S., Chertkov O., Coyne S.R., RA Daligault H.E., Davenport K.W., Erkkila T., Frey K.G., Gibbons H.S., RA Gu W., Jaissle J., Johnson S.L., Koroleva G.I., Ladner J.T., Lo C.-C., RA Minogue T.D., Munk C., Palacios G.F., Redden C.L., Rosenzweig C.N., RA Scholz M.B., Teshima H., Xu Y.; RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KFN08818.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JMQA01000026; KFN08818.1; -; Genomic_DNA. DR RefSeq; WP_051985452.1; NZ_KN125580.1. DR EnsemblBacteria; KFN08818; KFN08818; DJ90_5003. DR PATRIC; fig|44252.3.peg.2921; -. DR Proteomes; UP000029278; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000029278}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000029278}. FT DOMAIN 208 372 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 440 AA; 49091 MW; C220EE8A80B5B59E CRC64; MAKSLHETND KIQDIAVLVS LITPETKQSG IDPSYSLDEL VRLAETAGVE VAETAVQNRD KPDPRWLIGK GKVLELRELM DRLRANTAIF DQELSGAQVR NLEEMLDAKI IDRTQPILDI FAQRAKTREG IIQVELAQLT YLLPRLSGHG KNLSRLGGGI GTRGPGESKL EMDRRHIRRR IGELKRQLEE VTRHRRLHRA RRKETGVVQV ALVGYTNAGK STLLRQLTNA DVYVENQLFA TLDPTTRLLP LPGGKEVVLT DTVGFIQNLP HDLVAAFRAT LEEVNEADLI LHVVDASSPM RQEQMAVVGR ILTELGAGGK PQIVLFNKID LCRPDGLQML PSGEGYLKIS AYDERDLAAI REAVQRRLSG GTKSFRIPAE RGDLASVLYR IGDVVNQQMD EADMIYDVNV NQADFAKYGY QLAPFAVQKP DVHEETNESR // ID A0A090ZEN8_PAEMA Unreviewed; 425 AA. AC A0A090ZEN8; DT 26-NOV-2014, integrated into UniProtKB/TrEMBL. DT 26-NOV-2014, sequence version 1. DT 07-JUN-2017, entry version 19. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:KFN08685.1}; GN ORFNames=DJ90_5297 {ECO:0000313|EMBL:KFN08685.1}; OS Paenibacillus macerans (Bacillus macerans). OC Bacteria; Firmicutes; Bacilli; Bacillales; Paenibacillaceae; OC Paenibacillus. OX NCBI_TaxID=44252 {ECO:0000313|EMBL:KFN08685.1, ECO:0000313|Proteomes:UP000029278}; RN [1] {ECO:0000313|EMBL:KFN08685.1, ECO:0000313|Proteomes:UP000029278} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=8244 {ECO:0000313|EMBL:KFN08685.1, RC ECO:0000313|Proteomes:UP000029278}; RA Bishop-Lilly K.A., Broomall S.M., Chain P.S., Chertkov O., Coyne S.R., RA Daligault H.E., Davenport K.W., Erkkila T., Frey K.G., Gibbons H.S., RA Gu W., Jaissle J., Johnson S.L., Koroleva G.I., Ladner J.T., Lo C.-C., RA Minogue T.D., Munk C., Palacios G.F., Redden C.L., Rosenzweig C.N., RA Scholz M.B., Teshima H., Xu Y.; RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KFN08685.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JMQA01000027; KFN08685.1; -; Genomic_DNA. DR RefSeq; WP_036619672.1; NZ_KN125580.1. DR EnsemblBacteria; KFN08685; KFN08685; DJ90_5297. DR PATRIC; fig|44252.3.peg.2954; -. DR Proteomes; UP000029278; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000029278}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000029278}. FT DOMAIN 200 368 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 159 186 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 425 AA; 48187 MW; 46A4EE481B2728AB CRC64; MEQQQLEQKA ILVGVNLNHQ EDFEYSMEEL ANLAEACDIE VVGTLAQNLL KINTSHYIGT GKLTEVRALL EAHEGNLVIF NDELSPSQIR NLEADLDCKV IDRTVLILDI FAQRAKTREA QLQVEVAQLK YMLPRLVGLR ESLGRQSGGV GTKNRGAGET RLELDRRRIE EKITALSKEL ELLVAHRQTQ RKQRKKNELP VVSLVGYTNA GKSTIMNALM ELYNPSPEKL VLEKDMLFAT LETSVRSIPL QDNKAFLLTD TVGFVSKLPH HLIKAFRSTL EEVAEADLLI HVVDYSNPEY ERLIEITNRT LKEIGITDIP TVYAYNKSDL TDQAIPEVRG DIVYMAAKPR IGLQELVSEI RSRIFKDYVQ CQMMIPYDQG ALVSYFNEHA NVLETSYEPE GTKLSLECKL SDYGKYKEYV IEALK // ID A0A091APQ0_9GAMM Unreviewed; 428 AA. AC A0A091APQ0; DT 26-NOV-2014, integrated into UniProtKB/TrEMBL. DT 26-NOV-2014, sequence version 1. DT 07-JUN-2017, entry version 18. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=N789_05640 {ECO:0000313|EMBL:KFN41356.1}; OS Arenimonas oryziterrae DSM 21050 = YC6267. OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales; OC Xanthomonadaceae; Arenimonas. OX NCBI_TaxID=1121015 {ECO:0000313|EMBL:KFN41356.1, ECO:0000313|Proteomes:UP000029385}; RN [1] {ECO:0000313|EMBL:KFN41356.1, ECO:0000313|Proteomes:UP000029385} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=YC6267 {ECO:0000313|EMBL:KFN41356.1, RC ECO:0000313|Proteomes:UP000029385}; RA Chen F., Wang G.; RT "Genome sequencing of Arenimonas oryziterrae."; RL Submitted (SEP-2013) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KFN41356.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AVCI01000045; KFN41356.1; -; Genomic_DNA. DR EnsemblBacteria; KFN41356; KFN41356; N789_05640. DR PATRIC; fig|1121015.4.peg.2793; -. DR Proteomes; UP000029385; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000029385}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000029385}. FT DOMAIN 189 354 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 148 182 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 428 AA; 46680 MW; 426F802F32A5C7C2 CRC64; MLVQPYPLGP QDPGLIEEFS ELARSAGAVV VATIAARIER PSPSTYVGSG KVEEILAACE ATDADVVLFN HALSPSQERN LSKALNRRVV DRTGLILDIF AQRAVSHEGK LQVELAQLKH LSARLIQGSA ARLDSQRGGS IGLRGPGETH LETDRRLLQK RRDQLEARLD KVEVQRVQMR RARIRNAIPR VALVGYTNAG KSTLFNALTG SEVYAADKLF ATLDPTVRRM DGQGSSLVLS DTVGFVRDLP HELVAAFRST LAEAREADLL LHIVDAADEA REERIGQVDA VLEEIGAGDI PQILVYNKID RLEDVAPRHD PTISGRERLW LSAKTGAGFD LLKAALTLRF ADRRLIAELH LAPDQGRLRS RLHALDAVRG ESVDELGWRL SIDLPLATAE RLASEAGGHV LAPLLVTPAA PTYNPDND // ID A0A091C112_9GAMM Unreviewed; 447 AA. AC A0A091C112; DT 26-NOV-2014, integrated into UniProtKB/TrEMBL. DT 26-NOV-2014, sequence version 1. DT 07-JUN-2017, entry version 20. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=P873_06465 {ECO:0000313|EMBL:KFN50315.1}; OS Arenimonas composti TR7-09 = DSM 18010. OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales; OC Xanthomonadaceae; Arenimonas. OX NCBI_TaxID=1121013 {ECO:0000313|EMBL:KFN50315.1, ECO:0000313|Proteomes:UP000029391}; RN [1] {ECO:0000313|EMBL:KFN50315.1, ECO:0000313|Proteomes:UP000029391} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=TR7-09 {ECO:0000313|EMBL:KFN50315.1, RC ECO:0000313|Proteomes:UP000029391}; RA Chen F., Wang G.; RT "Genome sequencing of Arenimonas composti."; RL Submitted (SEP-2013) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KFN50315.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AWXU01000020; KFN50315.1; -; Genomic_DNA. DR RefSeq; WP_026817806.1; NZ_KE384525.1. DR EnsemblBacteria; KFN50315; KFN50315; P873_06465. DR Proteomes; UP000029391; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000029391}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000029391}. FT DOMAIN 207 371 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 166 200 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 447 AA; 48952 MW; 4C0257FFBA66BAB5 CRC64; MSTPQGSAAF ERARRGERAL LIQPYPPGQV DPALLEEFTE LARSAGATIV GTITARVERA NAATYIGSGK VEEVQSAVAA TGADLVLVNH ALSPAQERNL ERALKLRVVD RTGLILDIFA QRAATHEGKL QVELAQLKHW QTRLVRGWTH LERQRGGAIG LRGPGETQLE MDKRILQRKI ESLQSRLDKV EVQRTQMRRA RNRNAVPRVA LVGYTNAGKS TLFNALTGSG VYADDRLFAT LDPTVRRVEG VAPLVLSDTV GFVRDLPHEL VAAFRSTLAE AREADLLLHV VDAADELRDE RIRQVDAVLE EIGAGDIPQV LVFNKIDRIE GAEARVDAEV EGRARVWVSA RDRLGLDLLL DLLQRRFQEH RFTGELVLGP ADGRLRARLH DAGAVRAERV DAEGHSVLDI DLALAAAERL AAEAGGHPLQ ALLLVTPDAP TYNPDTD // ID A0A091CD92_9ENTE Unreviewed; 390 AA. AC A0A091CD92; DT 26-NOV-2014, integrated into UniProtKB/TrEMBL. DT 26-NOV-2014, sequence version 1. DT 07-JUN-2017, entry version 18. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=TMU3MR103_0912 {ECO:0000313|EMBL:KFN91678.1}; OS Tetragenococcus muriaticus 3MR10-3. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Enterococcaceae; OC Tetragenococcus. OX NCBI_TaxID=1302648 {ECO:0000313|EMBL:KFN91678.1, ECO:0000313|Proteomes:UP000029381}; RN [1] {ECO:0000313|EMBL:KFN91678.1, ECO:0000313|Proteomes:UP000029381} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=3MR10-3 {ECO:0000313|EMBL:KFN91678.1, RC ECO:0000313|Proteomes:UP000029381}; RA Chuea-nongthon C., Rodtong S., Yongsawatdigul J., Steele J.L., RA Liu X.-y., Speers J., Glasner J.D., Neeno-Eckwall E.C.; RT "Genome sequence of Tetragenococcus muriaticus."; RL Submitted (AUG-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KFN91678.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JPVT01000081; KFN91678.1; -; Genomic_DNA. DR EnsemblBacteria; KFN91678; KFN91678; TMU3MR103_0912. DR PATRIC; fig|1302648.3.peg.885; -. DR Proteomes; UP000029381; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000029381}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000029381}. FT DOMAIN 172 334 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 138 168 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 390 AA; 44461 MW; 377A75E53C92109B CRC64; MAELANLAKT AHGEVITTVE QNRDQVDHQT IIGKGKMEEL RQIIDKENID LVIFNRALTP RQGQIVENFL ETPTIDRIQL ILDIFAKRAR SKEGKLQVEL AQLEYSFPRI IGQGKTLSRL GGGIGTRGPG ETKLETDRRL IRKKMTSIRQ ELKEVEEHRR RTRQQRNEQE VYQIGLVGYT NAGKSTLLNL LTSANTYEKD QLFATLDPLT KKWRLPDGFE VTVTDTVGFI QDLPTQLVDA FHSTLEESQN MDLILHVIDA SAANRQQQEQ TVLQLMEDLN LRHVPVLAIY NKADIIDEKQ FVPTQYPHVL LSANDPDSKE KLTNAIQSIM KEKLQPYTLV LAPDEGRLLE KLKENTLVIT TDFDESTQQY VVKGFAKENS FAITKMNQKK // ID A0A091ECW0_CORBR Unreviewed; 437 AA. AC A0A091ECW0; DT 26-NOV-2014, integrated into UniProtKB/TrEMBL. DT 26-NOV-2014, sequence version 1. DT 07-JUN-2017, entry version 14. DE SubName: Full=Putative GTP-binding protein 6 {ECO:0000313|EMBL:KFO55828.1}; DE Flags: Fragment; GN ORFNames=N302_15885 {ECO:0000313|EMBL:KFO55828.1}; OS Corvus brachyrhynchos (American crow). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda; OC Coelurosauria; Aves; Neognathae; Passeriformes; Corvoidea; Corvidae; OC Corvus. OX NCBI_TaxID=85066 {ECO:0000313|EMBL:KFO55828.1, ECO:0000313|Proteomes:UP000052976}; RN [1] {ECO:0000313|EMBL:KFO55828.1, ECO:0000313|Proteomes:UP000052976} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BGI_N302 {ECO:0000313|EMBL:KFO55828.1}; RA Zhang G., Li C.; RT "Genome evolution of avian class."; RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; KK718333; KFO55828.1; -; Genomic_DNA. DR RefSeq; XP_008627585.1; XM_008629363.1. DR GeneID; 103611796; -. DR CTD; 8225; -. DR Proteomes; UP000052976; Unassembled WGS sequence. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR CDD; cd01878; HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 4: Predicted; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000052976}; KW Reference proteome {ECO:0000313|Proteomes:UP000052976}. FT DOMAIN 210 374 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 172 206 {ECO:0000256|SAM:Coils}. FT NON_TER 1 1 {ECO:0000313|EMBL:KFO55828.1}. FT NON_TER 437 437 {ECO:0000313|EMBL:KFO55828.1}. SQ SEQUENCE 437 AA; 49065 MW; AB3FB102ECEDFBEF CRC64; SPLAPRPGAQ RVAIVHPAVK WGPQKSPLTT AELQIAEAVA LVDTLQNWTV LDKIIIPTRN PNKKFVFGKG NFQVLTEKIK KLPHVTAVFL NVERISSLTK KELEGAWGVQ VFDRYTVVLH IFRCNAQTKE AKLQVALAEI PLLRSNLKSE VSQRDQQRGG SRYIMGSGET FLETQNRVLK DKELKIRNAL EKLRRKRALL RTQRRRCEFP MVSVMGYTNC GKTTLIKALT GEAGLQPRDQ LFATLDITAH AGYLPSHMAV IYVDTIGFLT DLPHNLVESF SATLEEVAYS DLIVHVRDIT HPETILQKAT VLSVLRNLNL PSHLLDSMVE VHNKVDLIER YKPTEENALA ISALHGHGLE ELKQEIEKKI LTATGKMILT VNINLEGPQL SWLYKEATVQ EVEVMPEDGT ARVKVIISSS AFGRYKNLFP NSQIFMS // ID A0A091F9C9_9DELT Unreviewed; 547 AA. AC A0A091F9C9; DT 26-NOV-2014, integrated into UniProtKB/TrEMBL. DT 26-NOV-2014, sequence version 1. DT 12-APR-2017, entry version 16. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=ER57_14710 {ECO:0000313|EMBL:KFO66853.1}; OS Smithella sp. SCADC. OC Bacteria; Proteobacteria; Deltaproteobacteria; Syntrophobacterales; OC Syntrophaceae; Smithella. OX NCBI_TaxID=1499107 {ECO:0000313|EMBL:KFO66853.1, ECO:0000313|Proteomes:UP000029283}; RN [1] {ECO:0000313|EMBL:KFO66853.1, ECO:0000313|Proteomes:UP000029283} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Tan B.F., Silva R., Rozycki T., Nesbo C., Foght J.; RT "Draft genomes of three Smithella spp. obtained from a methanogenic RT alkane-degrading culture and produced water of an oilfield."; RL Genome Announc. 2:e01085-14(2014). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KFO66853.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JQDQ01000201; KFO66853.1; -; Genomic_DNA. DR Proteomes; UP000029283; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000029283}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000029283}. FT DOMAIN 377 542 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 336 363 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 547 AA; 61230 MW; D792F80C664EA0D6 CRC64; MNKIFGNTTG LRAAQIKQIE RLGHKGIPPE NIITNDLARQ LSSISREINR QIGLLISRKG EISSVIVGDH KSILIPDLDG FRSSSLRFKG LRLIHTHLNG EELSDEDLTD LSHLRLDLIG ALEVKEDGSP GVMHRAHLIA ENPDGDYWLI MKPEEPHRLQ INFLSFIQAL EDEFARKQKA RKIDAAEKAI LLRVEKNPLA GAETSLAELA QLARTCGVEV FDSIVQYRPQ PDPKFMVGRG KLSAIDLRAS QIGANMLIFD HELTPAQARS ISNFTGLKII DRTQVILDIF ARRAHSREGK IQVELAQLRY RLPRLTHVDT SLSRLAGGIG GIGPGETKLE IDRRRIRERI HRLEKDLKAI TKSRRQRSSR REKTGLPIIS IVGYTNAGKS TLLNTLTQSS VLVEDKLFAT LDTKSARLRF PQDTEAIITD TVGFIRSLPG ELFTAFRATL DELLDADILL HVIDASSSQF EEQIAAVEKI LEDLEINGKP TIRVLNKSDR VADKEMLQNL CRRLDAVAVS ALDKRTLFVL MEKIESLLAG KHNFSPR // ID A0A091FFD9_9DELT Unreviewed; 547 AA. AC A0A091FFD9; DT 26-NOV-2014, integrated into UniProtKB/TrEMBL. DT 26-NOV-2014, sequence version 1. DT 12-APR-2017, entry version 16. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=ER57_09965 {ECO:0000313|EMBL:KFO67537.1}; OS Smithella sp. SCADC. OC Bacteria; Proteobacteria; Deltaproteobacteria; Syntrophobacterales; OC Syntrophaceae; Smithella. OX NCBI_TaxID=1499107 {ECO:0000313|EMBL:KFO67537.1, ECO:0000313|Proteomes:UP000029283}; RN [1] {ECO:0000313|EMBL:KFO67537.1, ECO:0000313|Proteomes:UP000029283} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Tan B.F., Silva R., Rozycki T., Nesbo C., Foght J.; RT "Draft genomes of three Smithella spp. obtained from a methanogenic RT alkane-degrading culture and produced water of an oilfield."; RL Genome Announc. 2:e01085-14(2014). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KFO67537.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JQDQ01000168; KFO67537.1; -; Genomic_DNA. DR Proteomes; UP000029283; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000029283}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000029283}. FT DOMAIN 377 542 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 336 363 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 547 AA; 61218 MW; 73FEF57B83F4C6BB CRC64; MNKIFGNTTG LRAAQIKQIE RLGHKGIPPE NIITNDLARQ LSSISREINR QIGLLISRKG EISSVIVGDH KSILIPNLDG FRSSSLRFKG LRLIHTHLNG EELSGEDLTD LSHLRLDLIG ALEVKEDGSP GVMHRAHLIA ENPEGNYWLI MKPEEPHRMQ INFLSFIQAL EDEFARKQKS RKIDAAEKAI LLRVEKNPLA GAETSLAELA QLARTCGVEV FDSIVQYRPQ PDPKFMVGRG KLSAIDLRAS QIGANMLIFD HELTPAQARS ISNFTGLKII DRTQVILDIF ARRAHSREGK IQVELAQLRY RLPRLTHVDT SLSRLAGGIG GIGPGETKLE IDRRRIRERI HRLEKDLKAI TKSRRQRSSR REKTGLPIIS IVGYTNAGKS TLLNTLTQSS VLVEDKLFAT LDTKSARLRF PQDTEAIITD TVGFIRSLPG ELFTAFRATL DELLDADILL HVIDASSSQF EEQIAAVEKI LEDLEINGKP TIRVLNKSDR VADKEMLQNL CRRLDAVAVS ALDKRTLFVL MEKIESLLAG KHNFSPR // ID A0A091GEY8_9AVES Unreviewed; 449 AA. AC A0A091GEY8; DT 26-NOV-2014, integrated into UniProtKB/TrEMBL. DT 26-NOV-2014, sequence version 1. DT 10-MAY-2017, entry version 12. DE SubName: Full=Putative GTP-binding protein 6 {ECO:0000313|EMBL:KFO79901.1}; DE Flags: Fragment; GN ORFNames=N303_15191 {ECO:0000313|EMBL:KFO79901.1}; OS Cuculus canorus (common cuckoo). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda; OC Coelurosauria; Aves; Neognathae; Cuculiformes; Cuculidae; Cuculus. OX NCBI_TaxID=55661 {ECO:0000313|EMBL:KFO79901.1, ECO:0000313|Proteomes:UP000053760}; RN [1] {ECO:0000313|EMBL:KFO79901.1, ECO:0000313|Proteomes:UP000053760} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BGI_N303 {ECO:0000313|EMBL:KFO79901.1}; RA Zhang G., Li C.; RT "Genome evolution of avian class."; RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; KL448073; KFO79901.1; -; Genomic_DNA. DR Proteomes; UP000053760; Unassembled WGS sequence. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR CDD; cd01878; HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 4: Predicted; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000053760}; KW Reference proteome {ECO:0000313|Proteomes:UP000053760}. FT DOMAIN 223 387 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 185 219 {ECO:0000256|SAM:Coils}. FT NON_TER 1 1 {ECO:0000313|EMBL:KFO79901.1}. FT NON_TER 449 449 {ECO:0000313|EMBL:KFO79901.1}. SQ SEQUENCE 449 AA; 50363 MW; FE67B65A159524CE CRC64; EDEDEDVEEL LGPSPVAVGP GAQRVAVVHP DVKWGPKKSP LTTAELQIAE AVALVETLHN WTVLDKIIIP TKNPDKKFIF GKGNFQVLTE KIKKLPHVTA VFLNVERISS LTKKELEDAW GVKVFDRYTV VLHIFRCNAQ TKEAKLQIAL AEIPLLRSNL KNEVSRLDQQ RGGSRYIMGS GETFMETQNR ILKEKELKIR NALEKLKRKR SLLRTQRRKR EFPTISVMGY TNCGKTTLIK ALTGEAGLQP RDQLFATLDI TAHAGYLPSH MAVIYVDTIG FLTDLPHNLV ESFSATLEEV AYSDLIVHVR DITHPETVLQ KATVLSVLKN LNLPSHLLDS MVEVHNKVDL IERYKPTEEN ALAISALHGL GLEELKEEIE KKILTATGKK ILTVNVNLEG PQLSWLYKEA TVQEVEVMPE DGTAKVKVII GNSAFGKYKN LFPNSKIFM // ID A0A091HB74_BUCRH Unreviewed; 406 AA. AC A0A091HB74; DT 26-NOV-2014, integrated into UniProtKB/TrEMBL. DT 26-NOV-2014, sequence version 1. DT 10-MAY-2017, entry version 12. DE SubName: Full=Putative GTP-binding protein 6 {ECO:0000313|EMBL:KFO92724.1}; DE Flags: Fragment; GN ORFNames=N320_11051 {ECO:0000313|EMBL:KFO92724.1}; OS Buceros rhinoceros silvestris. OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda; OC Coelurosauria; Aves; Neognathae; Bucerotiformes; Bucerotidae; Buceros. OX NCBI_TaxID=175836 {ECO:0000313|EMBL:KFO92724.1, ECO:0000313|Proteomes:UP000054064}; RN [1] {ECO:0000313|EMBL:KFO92724.1, ECO:0000313|Proteomes:UP000054064} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BGI_N320 {ECO:0000313|EMBL:KFO92724.1}; RA Zhang G., Li C.; RT "Genome evolution of avian class."; RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; KL530861; KFO92724.1; -; Genomic_DNA. DR Proteomes; UP000054064; Unassembled WGS sequence. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR CDD; cd01878; HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 4: Predicted; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000054064}; KW Reference proteome {ECO:0000313|Proteomes:UP000054064}. FT DOMAIN 180 344 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 142 169 {ECO:0000256|SAM:Coils}. FT NON_TER 1 1 {ECO:0000313|EMBL:KFO92724.1}. FT NON_TER 406 406 {ECO:0000313|EMBL:KFO92724.1}. SQ SEQUENCE 406 AA; 45999 MW; 8724E986E6738ADE CRC64; AELQIAEAVA LVDTLQNWTI LDKIVIPTKN PDKKFVFGKG NFQVLTEKIK KLPHVTAVFL NVERISSLTK KELEDAWGVK VFDRYTVVLH IFRCNARTKE AKLQIALAEI PLLRSNLKNE VSQLDQQRGG SRYIMGSGET FMETQTRILK EKELKIRNAL EKVRRKRSLL RTQRRKREFP IISVMGYTNC GKTTLIKALT GEAGLQPKDQ LFATLDITAH AGYLPSRMAV IYVDTIGFLT DLPHNLVESF SATLEEVAYS DLIVHVRDIT HPETVLQKAT VLSVLKNLNL PSHLLDSMVE VHNKVDLIER YEPTEENALA ISALHGHGLE ELKDEIEKKI FTATGRKILT VNINLEGPQL SWLYKEATVQ EVEVMPEDGT ARVRVIISNS AFGRYKNLFP NSKIFM // ID A0A091I9Q7_CALAN Unreviewed; 444 AA. AC A0A091I9Q7; DT 26-NOV-2014, integrated into UniProtKB/TrEMBL. DT 26-NOV-2014, sequence version 1. DT 10-MAY-2017, entry version 13. DE SubName: Full=Putative GTP-binding protein 6 {ECO:0000313|EMBL:KFP04213.1}; DE Flags: Fragment; GN ORFNames=N300_03220 {ECO:0000313|EMBL:KFP04213.1}; OS Calypte anna (Anna's hummingbird) (Archilochus anna). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda; OC Coelurosauria; Aves; Neognathae; Trochiliformes; Trochilidae; Calypte. OX NCBI_TaxID=9244 {ECO:0000313|EMBL:KFP04213.1, ECO:0000313|Proteomes:UP000054308}; RN [1] {ECO:0000313|EMBL:KFP04213.1, ECO:0000313|Proteomes:UP000054308} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BGI_N300 {ECO:0000313|EMBL:KFP04213.1}; RA Zhang G., Li C.; RT "Genome evolution of avian class."; RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; KL218306; KFP04213.1; -; Genomic_DNA. DR Proteomes; UP000054308; Unassembled WGS sequence. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR CDD; cd01878; HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000054308}; KW Reference proteome {ECO:0000313|Proteomes:UP000054308}. FT DOMAIN 219 383 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT NON_TER 1 1 {ECO:0000313|EMBL:KFP04213.1}. FT NON_TER 444 444 {ECO:0000313|EMBL:KFP04213.1}. SQ SEQUENCE 444 AA; 49925 MW; AB5A14455657068E CRC64; AELEELLGPS PLAVEPGAQR VAVVHPAVKW GPKKSPLTTA ELQVAEAVAL VNTLQNWTVL DKIIIPTKNP DKKFIFGKGN FQVLTEKLKK LPHMTAVFLN MERISSLTKK ELEDAWGVKV FDRYTVVLHI FRSNARTKEA KLQIALAEIP LLRSNVKNEA SQLDQQRGGS RYIMGSGETF LELQYRLLKE RELKIRNALE KLRRKRSLLR TRRKKREFPV VSVMGYTNCG KTTLIKALTG EAGLQPRDQL FATLDITAHA GYLPSHMVVI YVDTIGFLTD LPHNLIESFS ATLEEVAYSD LIVHVRDITH PETVLQKATV LSVLKNLNLP SHLLDSMVEV HNKVDLIERY KPTEENALAI SALHGHGLEE LREEIEKKIL VATGKKILTV NINLEGPQLS WLYKEATVQN IEVMAEDGTA RVKVIISNSA FGKYRTLFPN SKIL // ID A0A091IPI0_9AVES Unreviewed; 406 AA. AC A0A091IPI0; DT 26-NOV-2014, integrated into UniProtKB/TrEMBL. DT 26-NOV-2014, sequence version 1. DT 10-MAY-2017, entry version 13. DE SubName: Full=Putative GTP-binding protein 6 {ECO:0000313|EMBL:KFP09325.1}; DE Flags: Fragment; GN ORFNames=Z169_09031 {ECO:0000313|EMBL:KFP09325.1}; OS Egretta garzetta (little egret). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda; OC Coelurosauria; Aves; Neognathae; Pelecaniformes; Ardeidae; Egretta. OX NCBI_TaxID=188379 {ECO:0000313|EMBL:KFP09325.1, ECO:0000313|Proteomes:UP000053119}; RN [1] {ECO:0000313|EMBL:KFP09325.1, ECO:0000313|Proteomes:UP000053119} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BGI_Z169 {ECO:0000313|EMBL:KFP09325.1}; RA Zhang G., Li C.; RT "Genome evolution of avian class."; RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; KK500599; KFP09325.1; -; Genomic_DNA. DR Proteomes; UP000053119; Unassembled WGS sequence. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR CDD; cd01878; HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 4: Predicted; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000053119}; KW Reference proteome {ECO:0000313|Proteomes:UP000053119}. FT DOMAIN 180 344 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 146 169 {ECO:0000256|SAM:Coils}. FT NON_TER 1 1 {ECO:0000313|EMBL:KFP09325.1}. FT NON_TER 406 406 {ECO:0000313|EMBL:KFP09325.1}. SQ SEQUENCE 406 AA; 45983 MW; 6BA2898DE0C705E5 CRC64; AELQIAEAVA LVDTLQNWTV LDKIIIPTKN PDKKFIFGKG NFQVLTEKIK KLHHVTAVFL NVERISSLTK KELEDAWGVK VFDRYTVVLH IFRCNARTRE AKLQIALAEI PLLRSNLKNE VSQLDQQRGG SRYIMGSGET FMETQIRILK EKELKIRNAL EKLRRKRSLL RTQRRKREFP IISVMGYTNC GKTTLIKALT GEAGLQPRDQ LFATLDITAH AGYLPSHMAV IYVDTIGFLT DLPHNLVESF SATLEEVAYS DLIVHVRDIT HPETVLQKAT VLSVLKNLNL PSHLLDSMVE VHNKVDLTER YKPTEENALA ISALHGHGLE ELKEEIEKKI LTATGKKILT VNVNLEGPQL SWLYKEATVQ EVEVMPEDGT ARVKVIIGNS AFGRYKNLFP NSKIFM // ID A0A091KGQ3_9GRUI Unreviewed; 406 AA. AC A0A091KGQ3; DT 26-NOV-2014, integrated into UniProtKB/TrEMBL. DT 26-NOV-2014, sequence version 1. DT 10-MAY-2017, entry version 13. DE SubName: Full=Putative GTP-binding protein 6 {ECO:0000313|EMBL:KFP39292.1}; DE Flags: Fragment; GN ORFNames=N324_08096 {ECO:0000313|EMBL:KFP39292.1}; OS Chlamydotis macqueenii (Macqueen's bustard). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda; OC Coelurosauria; Aves; Neognathae; Gruiformes; Otididae; Chlamydotis. OX NCBI_TaxID=187382 {ECO:0000313|EMBL:KFP39292.1, ECO:0000313|Proteomes:UP000053330}; RN [1] {ECO:0000313|EMBL:KFP39292.1, ECO:0000313|Proteomes:UP000053330} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BGI_N324 {ECO:0000313|EMBL:KFP39292.1}; RA Zhang G., Li C.; RT "Genome evolution of avian class."; RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; KK742798; KFP39292.1; -; Genomic_DNA. DR Proteomes; UP000053330; Unassembled WGS sequence. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR CDD; cd01878; HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 4: Predicted; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000053330}; KW Reference proteome {ECO:0000313|Proteomes:UP000053330}. FT DOMAIN 180 344 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 142 169 {ECO:0000256|SAM:Coils}. FT NON_TER 1 1 {ECO:0000313|EMBL:KFP39292.1}. FT NON_TER 406 406 {ECO:0000313|EMBL:KFP39292.1}. SQ SEQUENCE 406 AA; 45909 MW; C679EC8D75762AE5 CRC64; AELQVAEAVA LVDTLQNWTI LDKIIIPTKN PDKKFIFGKG NFQVLTEKIK KLPHVTAVFL NVERISSLTK KELEDAWGVK VFDRYTVVLH IFRCNARTKE AKLQIALAEI PLLRSNLKNE VSQLDQQRGG SRYIMGSGET FMETQNRILK EKELKIRNAL EKLRRKRSLL RTQRRKREFP VISVMGYTNC GKTTLIKALT GEAGLQPRDQ LFATLDITAH AGYLPSHMAV IYVDTIGFLT DLPHSLVESF SATLEEVAYS DLIVHVRDIT HPETILQKAT VLSVLKNLNL PSHLLDSMIE VHNKVDLIER YKPTEENALA ISALRGHGLE ELKEEIEKKI LTATGKKILT VNVNLEGPQL SWLYKEATVQ EVEVMPEDGT ARVKVIISNS AFGKYKNLFP SSKIFM // ID A0A091L7L9_CATAU Unreviewed; 406 AA. AC A0A091L7L9; DT 26-NOV-2014, integrated into UniProtKB/TrEMBL. DT 26-NOV-2014, sequence version 1. DT 10-MAY-2017, entry version 12. DE SubName: Full=Putative GTP-binding protein 6 {ECO:0000313|EMBL:KFP52489.1}; DE Flags: Fragment; GN ORFNames=N323_12822 {ECO:0000313|EMBL:KFP52489.1}; OS Cathartes aura (Turkey vulture) (Vultur aura). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda; OC Coelurosauria; Aves; Neognathae; Ciconiiformes; Cathartidae; OC Cathartes. OX NCBI_TaxID=43455 {ECO:0000313|EMBL:KFP52489.1, ECO:0000313|Proteomes:UP000053745}; RN [1] {ECO:0000313|EMBL:KFP52489.1, ECO:0000313|Proteomes:UP000053745} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BGI_N323 {ECO:0000313|EMBL:KFP52489.1}; RA Zhang G., Li C.; RT "Genome evolution of avian class."; RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; KL307702; KFP52489.1; -; Genomic_DNA. DR Proteomes; UP000053745; Unassembled WGS sequence. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR CDD; cd01878; HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 4: Predicted; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000053745}; KW Reference proteome {ECO:0000313|Proteomes:UP000053745}. FT DOMAIN 180 344 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 142 169 {ECO:0000256|SAM:Coils}. FT NON_TER 1 1 {ECO:0000313|EMBL:KFP52489.1}. FT NON_TER 406 406 {ECO:0000313|EMBL:KFP52489.1}. SQ SEQUENCE 406 AA; 46008 MW; A284D32D8DD0758E CRC64; AELQIAEAVA LVDTLQNWTV LDKIIIPTKN PDKKFIFGKG NFQVLTEKIK KLPHVTAVFL NVERISSLTK KELEDAWGVK VFDRYTVVLH IFRCNARTKE AKLQIALAEI PLLRSNLKNE VSRLDQQRGG SRYIMGSGET FMETQNRILK EKELKIRHAL EKLRRKRSLL RTQRRKREFP IISVMGYTNC GKTTLIKALT GEAGLQPRDQ LFATLDITAH AGYLPSHMAV IYVDTIGFLT DLPHNLVESF SATLEEVAYS DLIVHVRDIT HPETILQKAT VLSVLKNLNL PSHLLDSMVE VHNKVDLIER YKPTEENAVA ISALHGHGLE ELKEEIEKKI LTATGKKILT VNVNLEGPQL SWLYKEATVQ EVEVMPEDGT ARVKVIIGNS AFGRYRNLFP NSKIFM // ID A0A091MQ19_CARIC Unreviewed; 406 AA. AC A0A091MQ19; DT 26-NOV-2014, integrated into UniProtKB/TrEMBL. DT 26-NOV-2014, sequence version 1. DT 10-MAY-2017, entry version 13. DE SubName: Full=Putative GTP-binding protein 6 {ECO:0000313|EMBL:KFP63650.1}; DE Flags: Fragment; GN ORFNames=N322_01834 {ECO:0000313|EMBL:KFP63650.1}; OS Cariama cristata (Red-legged seriema). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda; OC Coelurosauria; Aves; Neognathae; Cariamiformes; Cariamidae; Cariama. OX NCBI_TaxID=54380 {ECO:0000313|EMBL:KFP63650.1, ECO:0000313|Proteomes:UP000054116}; RN [1] {ECO:0000313|EMBL:KFP63650.1, ECO:0000313|Proteomes:UP000054116} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BGI_N322 {ECO:0000313|EMBL:KFP63650.1}; RA Zhang G., Li C.; RT "Genome evolution of avian class."; RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; KK512609; KFP63650.1; -; Genomic_DNA. DR Proteomes; UP000054116; Unassembled WGS sequence. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR CDD; cd01878; HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000054116}; KW Reference proteome {ECO:0000313|Proteomes:UP000054116}. FT DOMAIN 180 344 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT NON_TER 1 1 {ECO:0000313|EMBL:KFP63650.1}. FT NON_TER 406 406 {ECO:0000313|EMBL:KFP63650.1}. SQ SEQUENCE 406 AA; 45939 MW; AAC7DB786BBECB47 CRC64; AELQIAEAVA LVDSLQNWTV LDKIIIPTKN PDKKFIFGKG NFQVLTEKIK KLPHVTAVFL NVERISSLTK KELEDAWGVK VFDRYTVVLH IFRSNARTKE AKLQIALAEI PLLRSNLKNE VSRLDQQRGG SRYIMGSGET FMETQNRILR ERELKIRNAL EKLRRKRSLL RTQRRKREFP IISVMGYTNC GKTTLIKALT GEAGLQPRDE LFATLDITAH AGYLPSHMAV IYVDTIGFLT DLPHNLVESF SATLEEVAYS DLIVHVRDIT HPETILQKAT VLSVLKNLNL PSHLLDSMVE VHNKVDLIER YKATEENALA ISALHGHGLE ELKEEIEKKI LTATGKKILT VNVNLEGPQL SWLYKEATVQ EVEVVPEDGT ARVKVIIGNS AFGRYKNLFP NSKIFM // ID A0A091NBZ9_9PASS Unreviewed; 240 AA. AC A0A091NBZ9; DT 26-NOV-2014, integrated into UniProtKB/TrEMBL. DT 26-NOV-2014, sequence version 1. DT 08-JUN-2016, entry version 8. DE SubName: Full=Putative GTP-binding protein 6 {ECO:0000313|EMBL:KFP74700.1}; DE Flags: Fragment; GN ORFNames=N310_03267 {ECO:0000313|EMBL:KFP74700.1}; OS Acanthisitta chloris (rifleman). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda; OC Coelurosauria; Aves; Neognathae; Passeriformes; Acanthisittidae; OC Acanthisitta. OX NCBI_TaxID=57068 {ECO:0000313|EMBL:KFP74700.1, ECO:0000313|Proteomes:UP000053537}; RN [1] {ECO:0000313|EMBL:KFP74700.1, ECO:0000313|Proteomes:UP000053537} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BGI_N310 {ECO:0000313|EMBL:KFP74700.1}; RA Zhang G., Li C.; RT "Genome evolution of avian class."; RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; KK828628; KFP74700.1; -; Genomic_DNA. DR Proteomes; UP000053537; Unassembled WGS sequence. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000053537}; KW Reference proteome {ECO:0000313|Proteomes:UP000053537}. FT DOMAIN 47 135 GTP-bdg_N. {ECO:0000259|Pfam:PF13167}. FT DOMAIN 139 217 GTP-bdg_M. {ECO:0000259|Pfam:PF16360}. FT NON_TER 1 1 {ECO:0000313|EMBL:KFP74700.1}. FT NON_TER 240 240 {ECO:0000313|EMBL:KFP74700.1}. SQ SEQUENCE 240 AA; 27341 MW; 258E68FC1A927156 CRC64; EEEDAELEEL LGPSPLSLGP GAQRVAIVHP AVKWGPKKSP LTTAELQVAE AVALVDTLQN WTVLDKIIIP TKNPDKKFVF GKGNFQVLTE KIKKLPHLTA VFLNVERVSS VTKKELEDAW GVKIFDRYTT VLHIFRCNAR TKEAKLQIAL AEIPLLRSNL KNEVSQRDQQ RGGSRYIMGS GETFMEIQTR ILKERELKIR NALEKLRRKR SLLRTQRRKR EFPTVSVMGY TNCGKLNLLE // ID A0A091NE93_APAVI Unreviewed; 406 AA. AC A0A091NE93; DT 26-NOV-2014, integrated into UniProtKB/TrEMBL. DT 26-NOV-2014, sequence version 1. DT 10-MAY-2017, entry version 12. DE SubName: Full=Putative GTP-binding protein 6 {ECO:0000313|EMBL:KFP87402.1}; DE Flags: Fragment; GN ORFNames=N311_04207 {ECO:0000313|EMBL:KFP87402.1}; OS Apaloderma vittatum (Bar-tailed trogon). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda; OC Coelurosauria; Aves; Neognathae; Trogoniformes; Trogonidae; OC Apaloderma. OX NCBI_TaxID=57397 {ECO:0000313|EMBL:KFP87402.1, ECO:0000313|Proteomes:UP000054244}; RN [1] {ECO:0000313|EMBL:KFP87402.1, ECO:0000313|Proteomes:UP000054244} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BGI_N311 {ECO:0000313|EMBL:KFP87402.1}; RA Zhang G., Li C.; RT "Genome evolution of avian class."; RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; KL381187; KFP87402.1; -; Genomic_DNA. DR Proteomes; UP000054244; Unassembled WGS sequence. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR CDD; cd01878; HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 4: Predicted; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000054244}; KW Reference proteome {ECO:0000313|Proteomes:UP000054244}. FT DOMAIN 180 344 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 142 169 {ECO:0000256|SAM:Coils}. FT NON_TER 1 1 {ECO:0000313|EMBL:KFP87402.1}. FT NON_TER 406 406 {ECO:0000313|EMBL:KFP87402.1}. SQ SEQUENCE 406 AA; 45751 MW; E46A1F56B1180F64 CRC64; AELQIAEAVA LVDTLQNWTV LDKIIIPTKN PDKKFVFGKG NFEVLTEKIK KLPHVTAVFL NVERVSSVTK KELEDAWGVK VFDRYTVVLH IFRCNARTKE ARLQIALAEI PLLRSNLKTE VSQLDQQRGG SRYIMGSGET FMETQSRILK EKELKIRNAL EKLRRKRSLL RTQRRKRQFP IISVMGYTNC GKTTLIKALT GEAGLQPRDQ LFATLDITAH AGYLPSHMAV IYVDTIGFLT DLPHSLVESF SATLEEVAYS DLIVHVRDIT HPETILQKAT VLSVLKNLNL PSHLLDSVVE VHNKVDLIER YKPTEEGALA ISALHGHGLE ELKEKIEKKI LAATGKKILA LNINLEGPQL SWLYKEATVQ EVEVMPEDGT ARVKVIISNS AFGRYKNLFP NSKIFL // ID A0A091PD71_HALAL Unreviewed; 406 AA. AC A0A091PD71; DT 26-NOV-2014, integrated into UniProtKB/TrEMBL. DT 26-NOV-2014, sequence version 1. DT 10-MAY-2017, entry version 12. DE SubName: Full=Putative GTP-binding protein 6 {ECO:0000313|EMBL:KFQ05163.1}; DE Flags: Fragment; GN ORFNames=N329_05511 {ECO:0000313|EMBL:KFQ05163.1}; OS Haliaeetus albicilla (White-tailed sea-eagle). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda; OC Coelurosauria; Aves; Neognathae; Falconiformes; Accipitridae; OC Accipitrinae; Haliaeetus. OX NCBI_TaxID=8969 {ECO:0000313|EMBL:KFQ05163.1, ECO:0000313|Proteomes:UP000054379}; RN [1] {ECO:0000313|EMBL:KFQ05163.1, ECO:0000313|Proteomes:UP000054379} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BGI_N329 {ECO:0000313|EMBL:KFQ05163.1}; RA Zhang G., Li C.; RT "Genome evolution of avian class."; RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; KK656314; KFQ05163.1; -; Genomic_DNA. DR Proteomes; UP000054379; Unassembled WGS sequence. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR CDD; cd01878; HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 4: Predicted; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000054379}; KW Reference proteome {ECO:0000313|Proteomes:UP000054379}. FT DOMAIN 180 344 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 142 169 {ECO:0000256|SAM:Coils}. FT NON_TER 1 1 {ECO:0000313|EMBL:KFQ05163.1}. FT NON_TER 406 406 {ECO:0000313|EMBL:KFQ05163.1}. SQ SEQUENCE 406 AA; 46059 MW; 34EB622F18785EC1 CRC64; AELQIAEAVA LIDTLQNWTV LEKIIIPTKN PDKKFIFGKG NFQALTEKIK KLPHVTAVFL NVERISSLTK KELEDAWGVK VFDRYTVVLH IFRCNARTKE AKLQIALAEI PLLRSNLKND VSWLDQQRGG SRYIMGSGET FMETQNRILK EKELKIRNAL EKLRRKRSLL RTQRRKREFP IISVMGYTNC GKTTLIKALT GEAGLQPRDQ LFATLDITAH AGYLPSHMAV IYVDTIGFLT DLPHNLVESF SATLEEVAYS DLIVHVRDIT HPETILQKAT VLSVLKNLNL PSHLLDSMVE VHNKVDLIER YKPTEENALA ISALHGHGLE ELKEEIEKKI LTATGKKILT VNINLEGPQL SWLYKEATVQ EVEVMPEDGT ARVKVIISNS AFGRYRNLFP NSKIFM // ID A0A091RII9_9GRUI Unreviewed; 406 AA. AC A0A091RII9; DT 26-NOV-2014, integrated into UniProtKB/TrEMBL. DT 26-NOV-2014, sequence version 1. DT 10-MAY-2017, entry version 12. DE SubName: Full=Putative GTP-binding protein 6 {ECO:0000313|EMBL:KFQ39107.1}; DE Flags: Fragment; GN ORFNames=N332_03461 {ECO:0000313|EMBL:KFQ39107.1}; OS Mesitornis unicolor (brown roatelo). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda; OC Coelurosauria; Aves; Neognathae; Gruiformes; Mesitornithidae; OC Mesitornis. OX NCBI_TaxID=54374 {ECO:0000313|EMBL:KFQ39107.1, ECO:0000313|Proteomes:UP000053369}; RN [1] {ECO:0000313|EMBL:KFQ39107.1, ECO:0000313|Proteomes:UP000053369} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BGI_N332 {ECO:0000313|EMBL:KFQ39107.1}; RA Zhang G., Li C.; RT "Genome evolution of avian class."; RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; KK818348; KFQ39107.1; -; Genomic_DNA. DR Proteomes; UP000053369; Unassembled WGS sequence. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR CDD; cd01878; HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 4: Predicted; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000053369}; KW Reference proteome {ECO:0000313|Proteomes:UP000053369}. FT DOMAIN 180 344 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 142 169 {ECO:0000256|SAM:Coils}. FT NON_TER 1 1 {ECO:0000313|EMBL:KFQ39107.1}. FT NON_TER 406 406 {ECO:0000313|EMBL:KFQ39107.1}. SQ SEQUENCE 406 AA; 45900 MW; 61F8657B96E33B70 CRC64; AELQIAEAVA LVDTLQDWTV LDKIIIPTKN PDKKFIFGKG NFQVLTEKIK KLPNVTAVFM NVERLSSLTK KELEDAWGVK VFDRYTVVLH IFRCNARTKE AKLQIALAEI PLLRSNLKNE VSQLDQQRGG SRYIMGSGET FMETQNRVLR EKELKIRSAL EKLRRKRSLL RTQRRKREFP IISVMGYTNC GKTTLIKALT GEAGLQPRDQ LFATLDITAH AGYLPSHMTV IYVDTIGFLT DLPHNLVESF SATLEEVAYS DLIIHVRDIT HPETVLQKAT VLSVLKNLNI PSHLLDSMVE VHNKVDLIER YKPTEENALA ISALRGHGLE ELKEEIEKKV LTATGKKILT VHVNLEGPQL SWLYKEATVQ EVEVMPEDGT AKVKVIIGNS AFGKYKNLFP SSQIFM // ID A0A091SZM4_9AVES Unreviewed; 406 AA. AC A0A091SZM4; DT 26-NOV-2014, integrated into UniProtKB/TrEMBL. DT 26-NOV-2014, sequence version 1. DT 10-MAY-2017, entry version 12. DE SubName: Full=Putative GTP-binding protein 6 {ECO:0000313|EMBL:KFQ63410.1}; DE Flags: Fragment; GN ORFNames=N334_05266 {ECO:0000313|EMBL:KFQ63410.1}; OS Pelecanus crispus (Dalmatian pelican). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda; OC Coelurosauria; Aves; Neognathae; Pelecaniformes; Pelecanidae; OC Pelecanus. OX NCBI_TaxID=36300 {ECO:0000313|EMBL:KFQ63410.1, ECO:0000313|Proteomes:UP000054150}; RN [1] {ECO:0000313|EMBL:KFQ63410.1, ECO:0000313|Proteomes:UP000054150} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BGI_N334 {ECO:0000313|EMBL:KFQ63410.1}; RA Zhang G., Li C.; RT "Genome evolution of avian class."; RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; KK490752; KFQ63410.1; -; Genomic_DNA. DR Proteomes; UP000054150; Unassembled WGS sequence. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR CDD; cd01878; HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 4: Predicted; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000054150}; KW Reference proteome {ECO:0000313|Proteomes:UP000054150}. FT DOMAIN 180 344 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 142 169 {ECO:0000256|SAM:Coils}. FT NON_TER 1 1 {ECO:0000313|EMBL:KFQ63410.1}. FT NON_TER 406 406 {ECO:0000313|EMBL:KFQ63410.1}. SQ SEQUENCE 406 AA; 45859 MW; 13BA2F42FEAF4F1D CRC64; AELQIAEAVA LVDTLQNWTV LDKIIIPTKN PDKKFIFGKG NFQVLTEKIK KLPHVTAVFL NVERISSLTK KELEDAWGVK VFDRYTVVLH IFRCNARTKE AKLQIALAEI PLLRSNLKNE VSQLDQQKGG SRYIMGSGET FMETQNRVLK EKELKIRSAL EKLRRKRSLL RTQRRKREFP VISVMGYTNC GKTTLIKALT GEAGLQPRDQ LFATLDITAH AGYLPSHMAV IYVDTIGFLT DLPHNLVESF SATLEEVAYS DLIVHVRDIT HPETILQKAT VLSVLKNLNI PSHLLDSMVE VHNKVDLIER YKPTEENALA ISALHGHGLE LLKEEIEKKV LTATGKKILT VNINLEGPQL SWLYKEATVQ QVEVMPEDGT ARVKVIISSS AFGRYKKLFP NSKIFM // ID A0A091U2H0_PHORB Unreviewed; 406 AA. AC A0A091U2H0; DT 26-NOV-2014, integrated into UniProtKB/TrEMBL. DT 26-NOV-2014, sequence version 1. DT 10-MAY-2017, entry version 12. DE SubName: Full=Putative GTP-binding protein 6 {ECO:0000313|EMBL:KFQ84631.1}; DE Flags: Fragment; GN ORFNames=N337_04239 {ECO:0000313|EMBL:KFQ84631.1}; OS Phoenicopterus ruber ruber. OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda; OC Coelurosauria; Aves; Neognathae; Phoenicopteriformes; OC Phoenicopteridae; Phoenicopterus. OX NCBI_TaxID=9218 {ECO:0000313|EMBL:KFQ84631.1, ECO:0000313|Proteomes:UP000053700}; RN [1] {ECO:0000313|EMBL:KFQ84631.1, ECO:0000313|Proteomes:UP000053700} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BGI_N337 {ECO:0000313|EMBL:KFQ84631.1}; RA Zhang G., Li C.; RT "Genome evolution of avian class."; RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; KK413393; KFQ84631.1; -; Genomic_DNA. DR Proteomes; UP000053700; Unassembled WGS sequence. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR CDD; cd01878; HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 4: Predicted; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000053700}; KW Reference proteome {ECO:0000313|Proteomes:UP000053700}. FT DOMAIN 180 344 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 142 169 {ECO:0000256|SAM:Coils}. FT NON_TER 1 1 {ECO:0000313|EMBL:KFQ84631.1}. FT NON_TER 406 406 {ECO:0000313|EMBL:KFQ84631.1}. SQ SEQUENCE 406 AA; 45792 MW; 840354B7A9BC9931 CRC64; AELQIAEAVA LVDTLQNWTV LDKIIIPTKN PDKKFIFGKG NFQVLTEKIK KLPHVTAVFL NVERISSLTK KELEDAWGVK VFDRYTVVLH IFRCNAHTKE AKLQIALAEI PLLRSNLKSE VSQLDQQRGG SRYIMGSGET FMETQNRVLK EKELKIRSAL EKLRRKRSLL RTQRRKRELP IISVMGYTNC GKTTLIKALT GEAGLQPRDQ LFATLDITAH AGYLPSHMAV IYVDTIGFLT DLPHNLVESF SATLEEVAYS DLIVHVRDIT HPETTLQKAT VLSVLKNLNL PSHLLDSMVE VHNKVDLIER YKPPEENALA ISALHGHGLE ELKEEIEKKI LTATGKKILT VNINLEGPQL SWLYKEATVQ EVEVMPEDGT ARVKVIIGNS AFGKYRSLFP NSKIFM // ID A0A091WW33_NIPNI Unreviewed; 406 AA. AC A0A091WW33; DT 26-NOV-2014, integrated into UniProtKB/TrEMBL. DT 26-NOV-2014, sequence version 1. DT 10-MAY-2017, entry version 13. DE SubName: Full=Putative GTP-binding protein 6 {ECO:0000313|EMBL:KFR05616.1}; DE Flags: Fragment; GN ORFNames=Y956_02732 {ECO:0000313|EMBL:KFR05616.1}; OS Nipponia nippon (Crested ibis) (Ibis nippon). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda; OC Coelurosauria; Aves; Neognathae; Pelecaniformes; Threskiornithidae; OC Nipponia. OX NCBI_TaxID=128390 {ECO:0000313|EMBL:KFR05616.1, ECO:0000313|Proteomes:UP000053283}; RN [1] {ECO:0000313|EMBL:KFR05616.1, ECO:0000313|Proteomes:UP000053283} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BGI_Y956 {ECO:0000313|EMBL:KFR05616.1}; RA Zhang G., Li C.; RT "Genome evolution of avian class."; RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; KL411326; KFR05616.1; -; Genomic_DNA. DR Proteomes; UP000053283; Unassembled WGS sequence. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR CDD; cd01878; HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 4: Predicted; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000053283}; KW Reference proteome {ECO:0000313|Proteomes:UP000053283}. FT DOMAIN 180 344 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 142 169 {ECO:0000256|SAM:Coils}. FT NON_TER 1 1 {ECO:0000313|EMBL:KFR05616.1}. FT NON_TER 406 406 {ECO:0000313|EMBL:KFR05616.1}. SQ SEQUENCE 406 AA; 45903 MW; B88F1F4CBB04CCBF CRC64; AELQIAEAVA LVDTLQNWTV LDKIIIPTKN PDKKFIFGKG NFQVLTEKIK KLPHVTAVFL NVERISSLTK KELEDAWGVK VFDRYAVVLH IFRCNARTKE AKLQIALAEI PLLRSNLKNE VSQLDQQRGG SRYIMGSGET FMETQNRILK EKELKIRNAL EKLRRKRSLL RTQRRKREFP IISVMGYTNC GKTTLIKALT GEAGLQPRDQ LFATLDITAH AGYLPSQMAV IYVDTIGFLT DLPHNLVESF SATLEEVAYS DLIVHVRDVT HPETILQKAT VLSVLKNLNL PSHLLDSMVE VHNKVDLIER YKPTEENAIA ISALHGHGLE ELKEEIEKKI LAATGKKILT VNINLEGPQL SWLYKEATVQ EVEVMPEDGT ARVKVIISNS AFGRYKNLFP NSKIFM // ID A0A091WX71_OPIHO Unreviewed; 406 AA. AC A0A091WX71; DT 26-NOV-2014, integrated into UniProtKB/TrEMBL. DT 26-NOV-2014, sequence version 1. DT 10-MAY-2017, entry version 12. DE SubName: Full=Putative GTP-binding protein 6 {ECO:0000313|EMBL:KFR05956.1}; DE Flags: Fragment; GN ORFNames=N306_14230 {ECO:0000313|EMBL:KFR05956.1}; OS Opisthocomus hoazin (Hoatzin) (Phasianus hoazin). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda; OC Coelurosauria; Aves; Neognathae; Opisthocomiformes; Opisthocomidae; OC Opisthocomus. OX NCBI_TaxID=30419 {ECO:0000313|EMBL:KFR05956.1, ECO:0000313|Proteomes:UP000053605}; RN [1] {ECO:0000313|EMBL:KFR05956.1, ECO:0000313|Proteomes:UP000053605} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BGI_N306 {ECO:0000313|EMBL:KFR05956.1}; RA Zhang G., Li C.; RT "Genome evolution of avian class."; RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; KK734289; KFR05956.1; -; Genomic_DNA. DR PhylomeDB; A0A091WX71; -. DR Proteomes; UP000053605; Unassembled WGS sequence. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR CDD; cd01878; HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 4: Predicted; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000053605}; KW Reference proteome {ECO:0000313|Proteomes:UP000053605}. FT DOMAIN 180 344 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 142 169 {ECO:0000256|SAM:Coils}. FT NON_TER 1 1 {ECO:0000313|EMBL:KFR05956.1}. FT NON_TER 406 406 {ECO:0000313|EMBL:KFR05956.1}. SQ SEQUENCE 406 AA; 45879 MW; FDD9461D9447E313 CRC64; AGLQIAEAVA LVDTLQNWTV LDKIIIPTKN PDKKFVFGKG NFQVLTEKIK KLTHLTAVFL NVERISSLTK KELEDAWGVK VFDRYTVVLH IFRCNARTKE AKLQIALAEI PLLRSNLKNE VSQLDQQRGG SRYIMGSGET FMETQNRILK EKELKIRNAL EKLRRKRSLL RTQRRKREFP IISVMGYTNC GKTTLIKALT GDAGLQPRDQ LFATLDITAH AGYLPSNMTV IYVDTIGFLT DLPHNLVESF SATLEEVAYS DLIVHVRDIT HPETILQKAT VLSVLKNLNL PSHLFDSMVE VHNKVDMIER YTPTEENALA ISALHGHGLE ELKEEIEKKI LTATGKKILT VNVNLEGPQL SWLYKEATVQ EVEVMPEDGT ARVKVIIGNS AFGRYKNLFP TSKIFM // ID A0A093CCE2_TAUER Unreviewed; 404 AA. AC A0A093CCE2; DT 26-NOV-2014, integrated into UniProtKB/TrEMBL. DT 26-NOV-2014, sequence version 1. DT 10-MAY-2017, entry version 12. DE SubName: Full=Putative GTP-binding protein 6 {ECO:0000313|EMBL:KFV12068.1}; DE Flags: Fragment; GN ORFNames=N340_01738 {ECO:0000313|EMBL:KFV12068.1}; OS Tauraco erythrolophus (Red-crested turaco). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda; OC Coelurosauria; Aves; Neognathae; Musophagiformes; Musophagidae; OC Tauraco. OX NCBI_TaxID=121530 {ECO:0000313|EMBL:KFV12068.1, ECO:0000313|Proteomes:UP000053661}; RN [1] {ECO:0000313|EMBL:KFV12068.1, ECO:0000313|Proteomes:UP000053661} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BGI_N340 {ECO:0000313|EMBL:KFV12068.1}; RA Zhang G., Li C.; RT "Genome evolution of avian class."; RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; KL459986; KFV12068.1; -; Genomic_DNA. DR Proteomes; UP000053661; Unassembled WGS sequence. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR CDD; cd01878; HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 4: Predicted; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000053661}; KW Reference proteome {ECO:0000313|Proteomes:UP000053661}. FT DOMAIN 180 344 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 142 169 {ECO:0000256|SAM:Coils}. FT NON_TER 1 1 {ECO:0000313|EMBL:KFV12068.1}. FT NON_TER 404 404 {ECO:0000313|EMBL:KFV12068.1}. SQ SEQUENCE 404 AA; 45552 MW; F840DDE333E0122F CRC64; AELQVAEAVA LVDTLQNWTV LDKIIIPTKN PDKKFIFGKG NFQVLTEKIK KLPHVTAVFL NMERVSSLTK KELEDAWGVK VFDRYTVVLH IFRCNARTKE AKLQIALAEI PLLRSNLKNE VSQLAQQRGG SRYIMGSGET FMETQNRILK EKELKIRNAL EKLRRKRSLL RTQRRKREFP IISVMGYTNC GKTTLIKALT GEAGLQPRDQ LFATLDITAH AGYLPSRMAV IYVDTIGFLT DLPHNLVESF SATLEEVAYS DLIVHVRDIT HPETILQKAT VLSVLKNLNV PSHLLDSMIE VHNKVDLIER YKPTEENALA ISALCGHGLE ELKEEIEKKI LAATGKKILT VNVNLEGPQL SWLYKEATVQ EVEVMPEDGT ARVKVIIGSS AFGRYKNLFP NSKI // ID A0A093DPP0_9AVES Unreviewed; 406 AA. AC A0A093DPP0; DT 26-NOV-2014, integrated into UniProtKB/TrEMBL. DT 26-NOV-2014, sequence version 1. DT 10-MAY-2017, entry version 12. DE SubName: Full=Putative GTP-binding protein 6 {ECO:0000313|EMBL:KFV04076.1}; DE Flags: Fragment; GN ORFNames=N339_06450 {ECO:0000313|EMBL:KFV04076.1}; OS Pterocles gutturalis (yellow-throated sandgrouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda; OC Coelurosauria; Aves; Neognathae; Ciconiiformes; Pteroclidae; OC Pterocles. OX NCBI_TaxID=240206 {ECO:0000313|EMBL:KFV04076.1, ECO:0000313|Proteomes:UP000053149}; RN [1] {ECO:0000313|EMBL:KFV04076.1, ECO:0000313|Proteomes:UP000053149} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BGI_N339 {ECO:0000313|EMBL:KFV04076.1}; RA Zhang G., Li C.; RT "Genome evolution of avian class."; RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; KL228451; KFV04076.1; -; Genomic_DNA. DR Proteomes; UP000053149; Unassembled WGS sequence. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR CDD; cd01878; HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 4: Predicted; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000053149}; KW Reference proteome {ECO:0000313|Proteomes:UP000053149}. FT DOMAIN 180 344 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 142 169 {ECO:0000256|SAM:Coils}. FT NON_TER 1 1 {ECO:0000313|EMBL:KFV04076.1}. FT NON_TER 406 406 {ECO:0000313|EMBL:KFV04076.1}. SQ SEQUENCE 406 AA; 46024 MW; 98C1D5D625F45538 CRC64; AELQIAEAIA LIDTLQNWTV LDKIIVPTKN PDKKFIFGKG NFQVLTEKIK KMPHVTAVFL NVERISSLTK KELEDAWGVK VFDRYTVVLH IFRCNARTKE AKLQIALAEI PLLRSNLRNE VSHLDQQRGG SRYIMGSGET FMETQNRLLK EKELKIRNAL EKLRRKRSLL RTQRRKREFP IISVMGYTNC GKTTLIKALT GEAELQPRDQ LFATLDITAH AGYLPSHMAV IYVDTIGFLT DLPHNLVESF SATLEEVAYS DLLVHVRDIT HPDTILQKAT VLSVLKNLNL PSHLLDSMVE VHNKVDLIER YKPTEENALA ISALHGHGLE ELKEEIEKKI LTATGKKILT VTVNLEGPQL SWLYKEATVQ EVEVMPEDGT ARVKVIIGNS AFGRYKNLFP NSKIFV // ID A0A093ERK9_TYTAL Unreviewed; 406 AA. AC A0A093ERK9; DT 26-NOV-2014, integrated into UniProtKB/TrEMBL. DT 26-NOV-2014, sequence version 1. DT 10-MAY-2017, entry version 12. DE SubName: Full=Putative GTP-binding protein 6 {ECO:0000313|EMBL:KFV42755.1}; DE Flags: Fragment; GN ORFNames=N341_07745 {ECO:0000313|EMBL:KFV42755.1}; OS Tyto alba (Barn owl). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda; OC Coelurosauria; Aves; Neognathae; Strigiformes; Tytonidae; Tyto. OX NCBI_TaxID=56313 {ECO:0000313|EMBL:KFV42755.1, ECO:0000313|Proteomes:UP000054190}; RN [1] {ECO:0000313|EMBL:KFV42755.1, ECO:0000313|Proteomes:UP000054190} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BGI_N341 {ECO:0000313|EMBL:KFV42755.1}; RA Zhang G., Li C.; RT "Genome evolution of avian class."; RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; KK369416; KFV42755.1; -; Genomic_DNA. DR Proteomes; UP000054190; Unassembled WGS sequence. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR CDD; cd01878; HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 4: Predicted; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000054190}; KW Reference proteome {ECO:0000313|Proteomes:UP000054190}. FT DOMAIN 180 344 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 142 169 {ECO:0000256|SAM:Coils}. FT NON_TER 1 1 {ECO:0000313|EMBL:KFV42755.1}. FT NON_TER 406 406 {ECO:0000313|EMBL:KFV42755.1}. SQ SEQUENCE 406 AA; 45916 MW; B4AC18DA7296CAE2 CRC64; AELQIAEAVA LVDTLQNWTV LDKIIIPTKN PDKKFIFGKG NFQVLTEKIK KLPHVTAVFL NVERISSLTK KELEDAWGVK VFDRYTVVLH IFRCNARTRE AKLQIALAEI PLLRSNLKNE VSRLDQQKGG SRYIMGSGET FMETQNRILK EKELKIRNAL EKLRRKRSLL RTQRRKREFP IISVMGYTNC GKTTLIKALT GEAGLQPRDQ LFATLDITAH AGYLPSHMAV IYVDTIGFLT DLPHNLVESF SATLEEVVYS DLIIHVRDIT HPETILQKAT VLSVLKNLNL PSHLLDSMVE VHNKVDLIDR YKPTEENALA ISALHGHGLE ELKEEIEKKI LTATGKKILT VSVNLQGPQL SWLYKEATVQ EVEVMPEDGT ARVKVIIGNS AFGKYRNLFP SSTIFM // ID A0A093GPL0_PICPB Unreviewed; 449 AA. AC A0A093GPL0; DT 26-NOV-2014, integrated into UniProtKB/TrEMBL. DT 26-NOV-2014, sequence version 1. DT 10-MAY-2017, entry version 12. DE SubName: Full=Putative GTP-binding protein 6 {ECO:0000313|EMBL:KFV68947.1}; DE Flags: Fragment; GN ORFNames=N307_04506 {ECO:0000313|EMBL:KFV68947.1}; OS Picoides pubescens (Downy woodpecker) (Dryobates pubescens). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda; OC Coelurosauria; Aves; Neognathae; Piciformes; Picidae; Picoides. OX NCBI_TaxID=118200 {ECO:0000313|EMBL:KFV68947.1, ECO:0000313|Proteomes:UP000053875}; RN [1] {ECO:0000313|EMBL:KFV68947.1, ECO:0000313|Proteomes:UP000053875} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BGI_N307 {ECO:0000313|EMBL:KFV68947.1}; RA Zhang G., Li C.; RT "Genome evolution of avian class."; RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; KL216283; KFV68947.1; -; Genomic_DNA. DR Proteomes; UP000053875; Unassembled WGS sequence. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR CDD; cd01878; HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 4: Predicted; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000053875}; KW Reference proteome {ECO:0000313|Proteomes:UP000053875}. FT DOMAIN 223 387 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 185 212 {ECO:0000256|SAM:Coils}. FT NON_TER 1 1 {ECO:0000313|EMBL:KFV68947.1}. FT NON_TER 449 449 {ECO:0000313|EMBL:KFV68947.1}. SQ SEQUENCE 449 AA; 50534 MW; D101FE751E909AC7 CRC64; EDDESELEEL LGPSPLALGP GAQRVVIVHP DVKWGPKKSP LTKVELQIAE AVALVDTLQN WTVLDKIILP TKNPDKKFVF GKGNFQVLTE KIKELPHVTA VFLNMERLSS VTKRELEDAW GVKVFDRYTV VLHIFRCNAR TKEAKLQIAL AEIPLLRSNL KNEVSQLDQQ RGGSRYIMGS GETFMETQTR ILKEKELKLR NALEKLRRKR CLLRTQRKKR EFPIISVMGY TNCGKTTLIK ALTGEAELQP RDQLFATLDI TAHAGYLPSH MAVIYVDTIG FLTDLPHNLV ESFSATLEEV AYSDLIVHVR DITHPDTILQ KATVLSVLKN LNLPNHLLDS MVEVHNKVDL IEGYKPTEEN ALAISALHGH GLEELKEEIE KKILTVTGKK ILTVNINLEG PQLSWLYKEA TVQEVEVMPE DGTAQVKVII SNSAFGKYKN LFPNSKICI // ID A0A093HCC9_STRCA Unreviewed; 391 AA. AC A0A093HCC9; DT 26-NOV-2014, integrated into UniProtKB/TrEMBL. DT 26-NOV-2014, sequence version 1. DT 10-MAY-2017, entry version 12. DE SubName: Full=Putative GTP-binding protein 6 {ECO:0000313|EMBL:KFV76667.1}; DE Flags: Fragment; GN ORFNames=N308_07492 {ECO:0000313|EMBL:KFV76667.1}; OS Struthio camelus australis. OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda; OC Coelurosauria; Aves; Palaeognathae; Struthioniformes; Struthionidae; OC Struthio. OX NCBI_TaxID=441894 {ECO:0000313|EMBL:KFV76667.1, ECO:0000313|Proteomes:UP000053584}; RN [1] {ECO:0000313|EMBL:KFV76667.1, ECO:0000313|Proteomes:UP000053584} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BGI_N308 {ECO:0000313|EMBL:KFV76667.1}; RA Zhang G., Li C.; RT "Genome evolution of avian class."; RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; KL205917; KFV76667.1; -; Genomic_DNA. DR Proteomes; UP000053584; Unassembled WGS sequence. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR CDD; cd01878; HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 4: Predicted; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000053584}; KW Reference proteome {ECO:0000313|Proteomes:UP000053584}. FT DOMAIN 180 344 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 142 169 {ECO:0000256|SAM:Coils}. FT NON_TER 1 1 {ECO:0000313|EMBL:KFV76667.1}. FT NON_TER 391 391 {ECO:0000313|EMBL:KFV76667.1}. SQ SEQUENCE 391 AA; 43965 MW; F58C1F1459F13EEB CRC64; AELQMAEAVA LVDTLQNWTI LDKIIIPTKT PDKKFIFGKG NFQVLTEKIK KLPHLTAVFL NVERMSSLTK KELEDAWGVK VFDRYTVVLH IFRCNARTKE AKLQIALAEI PLLRSNLKNE VSQLDQQRGG SRYIMGSGET FMETQNRLLK EKELKVRNAL EKLRRKRSIL RSQRKRREFP IISVMGYTNC GKTTLIKALT GEAGLQPKDQ LFATLDITAH AGSLPSRMAV IYVDTIGFLS DLPHNLVESF SATLEEVAYS DLIVHVRDIT HPEAVLQKAS VLSVLKNLNL PSHLLESMVE VHNKVDLIER YKPTEESALA ISALHGHGLE ELKEEIEKRI LKATGKKILT VKINLEGPQL SWLYKEATVQ EVEVTPEDGT ASVKVIISNS A // ID A0A093QGJ3_9PASS Unreviewed; 407 AA. AC A0A093QGJ3; DT 26-NOV-2014, integrated into UniProtKB/TrEMBL. DT 26-NOV-2014, sequence version 1. DT 10-MAY-2017, entry version 12. DE SubName: Full=Putative GTP-binding protein 6 {ECO:0000313|EMBL:KFW87641.1}; DE Flags: Fragment; GN ORFNames=N305_08300 {ECO:0000313|EMBL:KFW87641.1}; OS Manacus vitellinus (golden-collared manakin). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda; OC Coelurosauria; Aves; Neognathae; Passeriformes; Pipridae; Manacus. OX NCBI_TaxID=328815 {ECO:0000313|EMBL:KFW87641.1, ECO:0000313|Proteomes:UP000053258}; RN [1] {ECO:0000313|EMBL:KFW87641.1, ECO:0000313|Proteomes:UP000053258} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BGI_N305 {ECO:0000313|EMBL:KFW87641.1}; RA Zhang G., Li C.; RT "Genome evolution of avian class."; RL Submitted (JUN-2014) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; KL672982; KFW87641.1; -; Genomic_DNA. DR Proteomes; UP000053258; Unassembled WGS sequence. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR CDD; cd01878; HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 4: Predicted; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000053258}; KW Reference proteome {ECO:0000313|Proteomes:UP000053258}. FT DOMAIN 180 344 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 142 166 {ECO:0000256|SAM:Coils}. FT NON_TER 1 1 {ECO:0000313|EMBL:KFW87641.1}. FT NON_TER 407 407 {ECO:0000313|EMBL:KFW87641.1}. SQ SEQUENCE 407 AA; 45988 MW; 91E3F9314A988810 CRC64; AELQIAEAVA LVDTLQNWTV LDKIIIPTKN PDKKFVFGKG NFQVLTEKIK KLPHLTAVFL NVERVSSLTK KELEGAWGVK VFDRYTIVLH IFRCNARTKE AKLQIALAEI PLLRSNLKNE VSQRDQQRGG SRYIMGSGET FLETQNRILK ERELKIRNAL EKLRRKRSLL RTQRRKREFP MISIMGYTNC GKTTLIKALT GEAGLQPRDQ LFATLDVTAH AGYLPSHMAV IYVDTIGFLT DLPHSLVESF SATLEEVAYT DLIVHVRDIT HPETILQKAT VLSVLKNLNL PSHLLDSIVE VHNKVDLIER YKPTEENALA VSALHGHGLE ELKQEIEKKI LTATGKKILT IDVNLEGPQL SWLHKEATVQ EVEVMPEDGT ARVKVIISSS AFGRYKNLFP NSKIFMS // ID A0A093R2C7_PHACA Unreviewed; 409 AA. AC A0A093R2C7; DT 26-NOV-2014, integrated into UniProtKB/TrEMBL. DT 26-NOV-2014, sequence version 1. DT 10-MAY-2017, entry version 13. DE SubName: Full=Putative GTP-binding protein 6 {ECO:0000313|EMBL:KFW94936.1}; DE Flags: Fragment; GN ORFNames=N336_06760 {ECO:0000313|EMBL:KFW94936.1}; OS Phalacrocorax carbo (Great cormorant) (Pelecanus carbo). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda; OC Coelurosauria; Aves; Neognathae; Pelecaniformes; Phalacrocoracidae; OC Phalacrocorax. OX NCBI_TaxID=9209 {ECO:0000313|EMBL:KFW94936.1, ECO:0000313|Proteomes:UP000053238}; RN [1] {ECO:0000313|EMBL:KFW94936.1, ECO:0000313|Proteomes:UP000053238} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BGI_N336 {ECO:0000313|EMBL:KFW94936.1}; RA Zhang G., Li C.; RT "Genome evolution of avian class."; RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; KL443969; KFW94936.1; -; Genomic_DNA. DR Proteomes; UP000053238; Unassembled WGS sequence. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR CDD; cd01878; HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000053238}; KW Reference proteome {ECO:0000313|Proteomes:UP000053238}. FT DOMAIN 183 347 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT NON_TER 1 1 {ECO:0000313|EMBL:KFW94936.1}. FT NON_TER 409 409 {ECO:0000313|EMBL:KFW94936.1}. SQ SEQUENCE 409 AA; 46332 MW; 184FAA3557EA5C6A CRC64; LPKAELQIAE AVALVDTLQN WTVLDKIILP TKNPDKKFIF GKGNFEVLTE KIKKLPHVTA VFLNVERISS LTKRELEDAW GVKVFDRYTV VLHIFRCNAR TKEAKLQIAL AEIPLRRSNL KNEVSQLDQQ RGGSRYIMGS GETFMETQNR ILKERELKIR NALEKLRRKR SLLRTQRRKC EFPTISVMGY TNCGKTTLIK ALTGEAGLQP RDQLFATLDI TAHGGYLPSR MAVIYVDTIG FLTDLPHNLI ESFFATLEEV AYSDLIVHVR DITHPETILQ KATVLSVLKN LNLPSHLLDS MVEVHNKVDL IERYKPTEEN ALAISALHGH GLEKLKEEIE KKILTATGKK ILTVNINLEG PQLSWLYKEA TVQEVEVMPE DGTARVKVII SSSAFGKYRS LFPNSKILL // ID A0A094IQ79_9GAMM Unreviewed; 431 AA. AC A0A094IQ79; DT 26-NOV-2014, integrated into UniProtKB/TrEMBL. DT 26-NOV-2014, sequence version 1. DT 30-AUG-2017, entry version 18. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=IDAT_12135 {ECO:0000313|EMBL:KFZ28009.1}; OS Idiomarina atlantica. OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales; OC Idiomarinaceae; Idiomarina. OX NCBI_TaxID=1517416 {ECO:0000313|EMBL:KFZ28009.1, ECO:0000313|Proteomes:UP000053718}; RN [1] {ECO:0000313|EMBL:KFZ28009.1, ECO:0000313|Proteomes:UP000053718} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MCCC 1A10513 {ECO:0000313|EMBL:KFZ28009.1, RC ECO:0000313|Proteomes:UP000053718}; RA Du J., Lai Q., Shao Z.; RT "Draft genome sequence of Idiomarina sp. MCCC 1A10513."; RL Submitted (JUN-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KFZ28009.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JPIN01000013; KFZ28009.1; -; Genomic_DNA. DR RefSeq; WP_034733995.1; NZ_JPIN01000013.1. DR EnsemblBacteria; KFZ28009; KFZ28009; IDAT_12135. DR Proteomes; UP000053718; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000053718}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000053718}. FT DOMAIN 198 365 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 431 AA; 48181 MW; 06B0A497D328A2C6 CRC64; MFDRFESGEQ AILVHVDFPA EIDREDLSEL KLLVTSAGVE TLAVVTAARS TPSSRYFVGS GKAEEIADAV KLHGANIVIF NHSLSPTQER NLEKLCQCRV LDRTGLILDI FAQRARTHEG KLQVELAQLR HISTRLVRGW THLERQKGGI GLRGPGETQL ETDRRLIRGR IKNILGRLDK VQKQRQQGRR ARQRAEVPTV SLVGYTNAGK STLFNRVTES EVYAADQLFA TLDPTLRKLE LPDVGAVILA DTVGFIRHLP HELVAAFKAT LQETQDADLL LHVIDISDDR QKENVEQVEA VLEEIGADEV PQLLICNKID KLDDGVARID YDDQQRPIRV WLSAQSGAGL ELLRQALVER LRPDMVDVSL RIPPSMGKLR GKLYALNSVT DEAVNEDGAL SLHVRMSSVD WRRLCKQVAD EYGDSLQGFV E // ID A0A094L397_9AVES Unreviewed; 406 AA. AC A0A094L397; DT 26-NOV-2014, integrated into UniProtKB/TrEMBL. DT 26-NOV-2014, sequence version 1. DT 10-MAY-2017, entry version 12. DE SubName: Full=Putative GTP-binding protein 6 {ECO:0000313|EMBL:KFZ65305.1}; DE Flags: Fragment; GN ORFNames=N338_07389 {ECO:0000313|EMBL:KFZ65305.1}; OS Podiceps cristatus (great crested grebe). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda; OC Coelurosauria; Aves; Neognathae; Podicipediformes; Podicipedidae; OC Podiceps. OX NCBI_TaxID=345573 {ECO:0000313|EMBL:KFZ65305.1, ECO:0000313|Proteomes:UP000053854}; RN [1] {ECO:0000313|EMBL:KFZ65305.1, ECO:0000313|Proteomes:UP000053854} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BGI_N338 {ECO:0000313|EMBL:KFZ65305.1}; RA Zhang G., Li C.; RT "Genome evolution of avian class."; RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; KL273688; KFZ65305.1; -; Genomic_DNA. DR Proteomes; UP000053854; Unassembled WGS sequence. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR CDD; cd01878; HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 4: Predicted; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000053854}; KW Reference proteome {ECO:0000313|Proteomes:UP000053854}. FT DOMAIN 180 344 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 142 169 {ECO:0000256|SAM:Coils}. FT NON_TER 1 1 {ECO:0000313|EMBL:KFZ65305.1}. FT NON_TER 406 406 {ECO:0000313|EMBL:KFZ65305.1}. SQ SEQUENCE 406 AA; 45968 MW; DC359E645E395B90 CRC64; AELQIAEAVA LVNTLQNWTV LDKIIIPTKN PDKKFIFGKG NFQVLTEKIK KMPHVTAVFL NVERISSLTK KELEDAWGVK VFDRYTIVLH IFRCNARTKE AKLQIALAEI PLLRSNLKNE VSQLDQQRGG SRYIMGSGET FMETQNRILK EKELKIRSAL EKLRRKRSLL RTQRRKREFP IISVMGYTNC GKTTLIKALT GEAGLQPRDQ LFATLDITAH AGYLPSHMAV IYVDTIGFLT DLPHNLVESF SATLEEVAYS DLIVHVRDIT HPETVLQKAT VLSVLKNLNL PRHLLDSMVE VHNKVDLIEG YKPTEENALA ISALHGRGLD ELKEEMEKKI LTATGKKILT LNINLEGPQL SWLYKEATVQ EIEVMPEDGT ARVKVIIGNS AFGRYKNLFP NSKIFM // ID A0A094L892_9GAMM Unreviewed; 431 AA. AC A0A094L892; DT 26-NOV-2014, integrated into UniProtKB/TrEMBL. DT 26-NOV-2014, sequence version 1. DT 30-AUG-2017, entry version 18. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=IDSA_05980 {ECO:0000313|EMBL:KFZ31028.1}; OS Idiomarina salinarum. OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales; OC Idiomarinaceae; Idiomarina. OX NCBI_TaxID=435908 {ECO:0000313|EMBL:KFZ31028.1, ECO:0000313|Proteomes:UP000054363}; RN [1] {ECO:0000313|EMBL:KFZ31028.1, ECO:0000313|Proteomes:UP000054363} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ISL-52 {ECO:0000313|EMBL:KFZ31028.1, RC ECO:0000313|Proteomes:UP000054363}; RA Du J., Shao Z.; RT "The draft genome sequence of Idiomarina salinarum ISL-52."; RL Submitted (JUN-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KFZ31028.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JPER01000002; KFZ31028.1; -; Genomic_DNA. DR RefSeq; WP_034775077.1; NZ_JPER01000002.1. DR EnsemblBacteria; KFZ31028; KFZ31028; IDSA_05980. DR Proteomes; UP000054363; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000054363}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000054363}. FT DOMAIN 198 365 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 431 AA; 48002 MW; 7B49A75637B094C2 CRC64; MFDRFESGEQ AVLVHVNFPT EIDREDLSEL KLLVSSAGVD TLGVVTAARS TPSSRYFVGS GKAEEVAEHV KAVGANLVIF NHSLSPTQER NLEKLCQCRV LDRTGLILDI FAQRARTHEG KLQVELAQLR HLSTRLVRGW THLERQKGGI GLRGPGETQL ETDRRLIRGR IRNIMARLAK VQKQREQGRR ARQRAEIPTV SLVGYTNAGK STLFNRITES NVFAADQLFA TLDPTLRKLE LPDVGSIILA DTVGFIRHLP HELVAAFKAT LQETQEADLL LHVVDISDDR QADNMHQVTE VLSEIGADEV PQLLVCNKID ALDDGEARID RDDLGMPIRV WLSARRGDGV ELLAKALTDR LRPRMVNVSL RIPPSMGKLR GKLYALNSVT GEQTCDDGQL ALQVRMSAVD WQRLCKQVAT EYGDSLQGFV E // ID A0A094LQS2_9GAMM Unreviewed; 437 AA. AC A0A094LQS2; DT 26-NOV-2014, integrated into UniProtKB/TrEMBL. DT 26-NOV-2014, sequence version 1. DT 30-AUG-2017, entry version 19. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=HR45_11000 {ECO:0000313|EMBL:KFZ37528.1}; OS Shewanella mangrovi. OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales; OC Shewanellaceae; Shewanella. OX NCBI_TaxID=1515746 {ECO:0000313|EMBL:KFZ37528.1, ECO:0000313|Proteomes:UP000029264}; RN [1] {ECO:0000313|EMBL:KFZ37528.1, ECO:0000313|Proteomes:UP000029264} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=YQH10 {ECO:0000313|EMBL:KFZ37528.1, RC ECO:0000313|Proteomes:UP000029264}; RA Liu Y., Zeng R.; RT "Shewanella sp. YQH10."; RL Submitted (JUN-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KFZ37528.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JPEO01000006; KFZ37528.1; -; Genomic_DNA. DR RefSeq; WP_037442754.1; NZ_JPEO01000006.1. DR EnsemblBacteria; KFZ37528; KFZ37528; HR45_11000. DR Proteomes; UP000029264; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000029264}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000029264}. FT DOMAIN 198 364 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 437 AA; 49027 MW; 751A702DBC3CA5FA CRC64; MFERYEAGET AVLVHLEFSD EDSREDLLEL QLLVESAGAH SVGVITGSRK APDRKYFVGT GKAEELAALV AATEANVVIF NHALTPAQER NLEALCHCRV LDRTTLILDI FAQRARTHEG KLQVELAQLR HMSTRLIRGW THLERQKGGI GLRGPGETQL ETDRRLLRGR IKYINRRLEK VDKQREQSRR ARQRSDMATV SLVGYTNAGK STLFNTLTSS TVYAADQLFA TLDPTLRKLD LEHHAVFLAD TVGFIRHLPH ELVAAFKATL QETRQADLLL HVVDCADDNM DDNFAQVQNV LADIDAGDIP QLIVCNKIDL LEEAQAKIDV DAEGKPFRVW ISAQQQLGLE LLRDAIEQLI GSHVVDLDLK LPASAGKYVS QFFRLEAIQQ QAYDDEGNCL LSVKMPEADW NRLVKQSEGE LESFIIEAEA ETDTVIR // ID A0A094P2T4_9ACTN Unreviewed; 499 AA. AC A0A094P2T4; DT 26-NOV-2014, integrated into UniProtKB/TrEMBL. DT 26-NOV-2014, sequence version 1. DT 30-AUG-2017, entry version 18. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=GM43_2510 {ECO:0000313|EMBL:KGA05665.1}; OS actinobacterium acMicro-4. OC Bacteria; Actinobacteria. OX NCBI_TaxID=1504317 {ECO:0000313|EMBL:KGA05665.1, ECO:0000313|Proteomes:UP000029304}; RN [1] {ECO:0000313|EMBL:KGA05665.1, ECO:0000313|Proteomes:UP000029304} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Ghai R., Mizuno C.M., Picazo A., Camacho A., Rodriguez-Valera F.; RT "Key roles for freshwater Actinobacteria revealed by deep metagenomic RT sequencing."; RL Submitted (MAY-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KGA05665.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JNSD01000004; KGA05665.1; -; Genomic_DNA. DR PATRIC; fig|1504317.4.peg.507; -. DR Proteomes; UP000029304; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR Gene3D; 1.10.3680.10; -; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR029024; TerB-like. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 2. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000029304}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000029304}. FT DOMAIN 279 444 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 499 AA; 54150 MW; 091DAF45E815E1EE CRC64; MTTDTSAHRD DVDRILSAAE EESAPVTVFR GTSGQSLSPL TGVTRGDMDL EERQALRRVA SLSTELDDVT EVEYRQLRLE KVVLIGVYSQ GTVVDAENSL RELAALCETA GAQVLDGLLQ RLPHPDAATY LGKGKAHDLK ELIAELGADT VVADTELAPS QRRALEDVVK VKVIDRTAVI LDIFSQHAKT REGKAQVELA QLQYLLPRLR GWGESMSRQA GGQVGGASAG MGSRGPGETK IELDRRRINT RMARLRKQIA SFGPSRETKR QQRKRTGIPN VAIAGYTNAG KSSLLNRITR AGVLVEDALF ATLDATVRKA TAPSGTHFTL TDTVGFVRQL PHQLVEAFRS TLEEVGQADV IVHVVDASHP DPGAQLATVR DVISDVGASD VPEIVVFNKA DLVDGGVSMQ LRGLAPNSLF VSAKTGEGID RLMARIDELL PHPTVPAHIM VPFNRGDLVA RLHDIAVIQE TSYTEHGTQM RVLVEPKMLE ELQQFALPN // ID A0A094PBA4_9ACTN Unreviewed; 236 AA. AC A0A094PBA4; DT 26-NOV-2014, integrated into UniProtKB/TrEMBL. DT 26-NOV-2014, sequence version 1. DT 16-MAR-2016, entry version 8. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:KGA06809.1}; DE Flags: Fragment; GN ORFNames=GM42_2800 {ECO:0000313|EMBL:KGA06809.1}; OS actinobacterium acMicro-1. OC Bacteria; Actinobacteria. OX NCBI_TaxID=1504316 {ECO:0000313|EMBL:KGA06809.1, ECO:0000313|Proteomes:UP000029316}; RN [1] {ECO:0000313|EMBL:KGA06809.1, ECO:0000313|Proteomes:UP000029316} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Ghai R., Mizuno C.M., Picazo A., Camacho A., Rodriguez-Valera F.; RT "Key roles for freshwater Actinobacteria revealed by deep metagenomic RT sequencing."; RL Submitted (MAY-2014) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KGA06809.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JNSC01000028; KGA06809.1; -; Genomic_DNA. DR Proteomes; UP000029316; Unassembled WGS sequence. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000029316}; KW Reference proteome {ECO:0000313|Proteomes:UP000029316}. FT DOMAIN 98 185 GTP-bdg_N. {ECO:0000259|Pfam:PF13167}. FT DOMAIN 188 231 GTP-bdg_M. {ECO:0000259|Pfam:PF16360}. FT NON_TER 236 236 {ECO:0000313|EMBL:KGA06809.1}. SQ SEQUENCE 236 AA; 25370 MW; 9AAC90B82F432C01 CRC64; MADYEHDDLI DRILSRAPSG GVVGGVVGRA AAITEDDTSR FPNSDGDQFD LADRQSLKRV AGLSTELEDV TEVEYRQLRL ERVVLIGVYP QGATTDAENS LRELAALCET AGAQVLDGVL QRRPNPDPAT YLGRGKVTEL RDLVLEVGAD TVVADTELAP SQRRALEDAV KVKVIDRTAV ILDIFSQHAK SREGKAQVEL AQLEYLLPRL RGWGDSMSRQ AGGQVGSAGA GMGSRG // ID A0A094PCB4_9ACTN Unreviewed; 457 AA. AC A0A094PCB4; DT 26-NOV-2014, integrated into UniProtKB/TrEMBL. DT 26-NOV-2014, sequence version 1. DT 07-JUN-2017, entry version 18. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=GM45_4805 {ECO:0000313|EMBL:KGA08577.1}; OS actinobacterium acAMD-5. OC Bacteria; Actinobacteria. OX NCBI_TaxID=1504319 {ECO:0000313|EMBL:KGA08577.1, ECO:0000313|Proteomes:UP000029322}; RN [1] {ECO:0000313|EMBL:KGA08577.1, ECO:0000313|Proteomes:UP000029322} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Ghai R., Mizuno C.M., Picazo A., Camacho A., Rodriguez-Valera F.; RT "Key roles for freshwater Actinobacteria revealed by deep metagenomic RT sequencing."; RL Submitted (MAY-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KGA08577.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JNSF01000008; KGA08577.1; -; Genomic_DNA. DR PATRIC; fig|1504319.4.peg.965; -. DR Proteomes; UP000029322; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000029322}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000029322}. FT DOMAIN 239 404 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 198 225 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 457 AA; 49862 MW; D195CC83DBD18383 CRC64; MTEFEEDLPE FTAGELDLQE RSALRRVVGL STELQDITEV EYRQVRLERV ILVGVWTSGT LDEAERSMQE LAALAETAGT QVLDGLIQRR DKPDAATYIG SGKALEIKRI VQSSGADSVI CDGELSPGQL RNLEDIIKVR VVDRTWLILD IFAQHAKSRE GKAQVSLAQM TYMLPRIRGW GEALSRQGAG VLARGPGETK IETDRRRIRD QMAKLRKELK AMGQTREIQR STRRKAAIPS VAIAGYTNAG KSSLLNRLTG AGVLVEDALF ATLDPTVRKV QTPSGRNITV TDTVGFVRHL PHELIEAFRS TLEEISQSDL LLHILDGSDP APEAQLAAVK EVLSEIGASS VTELVVINKI DIANLDTLMR LKTLLPEALL ISAQTGEGID KLLIAIDEEL SKLDLQIDLV LPYSAAALIA KTHNVGQVTL LEHTEIGTRI VASVPAKLAV ELKAASV // ID A0A094PL24_9ACTN Unreviewed; 453 AA. AC A0A094PL24; DT 26-NOV-2014, integrated into UniProtKB/TrEMBL. DT 26-NOV-2014, sequence version 1. DT 07-JUN-2017, entry version 17. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=GM46_1705 {ECO:0000313|EMBL:KGA12380.1}; OS actinobacterium acAcidi. OC Bacteria; Actinobacteria. OX NCBI_TaxID=1504320 {ECO:0000313|EMBL:KGA12380.1, ECO:0000313|Proteomes:UP000029305}; RN [1] {ECO:0000313|EMBL:KGA12380.1, ECO:0000313|Proteomes:UP000029305} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Ghai R., Mizuno C.M., Picazo A., Camacho A., Rodriguez-Valera F.; RT "Key roles for freshwater Actinobacteria revealed by deep metagenomic RT sequencing."; RL Submitted (MAY-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KGA12380.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JNSG01000013; KGA12380.1; -; Genomic_DNA. DR PATRIC; fig|1504320.4.peg.344; -. DR Proteomes; UP000029305; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000029305}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000029305}. FT DOMAIN 221 385 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 180 207 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 453 AA; 49369 MW; 4BE7F12ACCC0FE81 CRC64; MTNTNSNPNS PYNQALGQTL IERTIRERIV LVGVTLNGQT EEDTEASLDE LSLLIDTAGA DEAGRLTQKR DVPDHTWFVG KGKAEELRDL CLAVDADTVV FDNELSPGQQ YNLEKLLGRT ALDRTAVILD IFAQNAHTLE GKAQVELALL RYRLPRLRRG ADAKMSQQRG GVGSRFGSGE TKLEVDRRRI KNRISRLEQE LKDLGSTRDL QRKGRSRSGL ANVVIVGYTN AGKSTLLNRL TNAGVLVEDR LFATLDPTTR RLSFPGGEPV LVTDTVGFVR RLPHGLVESF KSTLEVAAQA DYLVHVVDGS SSDPDGQIDA VRTVLREIHA DEVPEFLVFN KSDLDPVGVA DVVAWHPGSV GISAHTGDGI DLFLQTLSDR LRSVSKVIEL VIPYERGDVL ASVHREGEVV STTHETNGVR VRARLAEASV GRLSEFVVSD GGIDPTPTGN MGV // ID A0A094PM54_9ACTN Unreviewed; 484 AA. AC A0A094PM54; DT 26-NOV-2014, integrated into UniProtKB/TrEMBL. DT 26-NOV-2014, sequence version 1. DT 07-JUN-2017, entry version 18. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=GM48_0905 {ECO:0000313|EMBL:KGA10664.1}; OS actinobacterium acIB-AMD-7. OC Bacteria; Actinobacteria. OX NCBI_TaxID=1504322 {ECO:0000313|EMBL:KGA10664.1, ECO:0000313|Proteomes:UP000029310}; RN [1] {ECO:0000313|EMBL:KGA10664.1, ECO:0000313|Proteomes:UP000029310} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Ghai R., Mizuno C.M., Picazo A., Camacho A., Rodriguez-Valera F.; RT "Key roles for freshwater Actinobacteria revealed by deep metagenomic RT sequencing."; RL Submitted (MAY-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KGA10664.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JNSI01000007; KGA10664.1; -; Genomic_DNA. DR PATRIC; fig|1504322.4.peg.183; -. DR Proteomes; UP000029310; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000313|EMBL:KGA10664.1}; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000029310}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900, KW ECO:0000313|EMBL:KGA10664.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000029310}. FT DOMAIN 264 429 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 230 257 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 484 AA; 53107 MW; DD05D79F56769341 CRC64; MSKNKFGEED GLEIDIDTLI RENAQAVADY ELQDSPESDN QDLQDRQALR RVSGLSTELQ DVSDAEYRQL RLEKVVLVGV WTEGSAKDAD NSIKELAALA ETAGSQVMEA LIQRRDKPDS ATFIGSGKVK EVRDAVVATG ADTVVCDGEL SPAQLRTLEQ KVKVKVIDRT ALILDIFAQH AKSREGKAQV ELAQMSYMLP RLRGWGESLS RQAGGIGGRG PGETKIETDR RRINDKMSKL RREIKEMKVS RDTKRNERRK NNIPSVAIAG YTNAGKSSLL NRLTGADVLV ENALFATLDP TVRKTQSSDG RIYTLVDTVG FVRHLPHQLV EAFKSTLEEV SQSDLIVHVV DGAHPDPTEQ LRAVREVITE IGGGEIMEII AINKADVAAP EVLMELLRKE SNAYAISART GYGIETLVKA IESALPKPKV EVNAVIPFNR GDLVSAVHEQ GEIISEEYLP EGTKLHAMVG GALARKIEML AEKI // ID A0A094PR64_9ACTN Unreviewed; 484 AA. AC A0A094PR64; DT 26-NOV-2014, integrated into UniProtKB/TrEMBL. DT 26-NOV-2014, sequence version 1. DT 07-JUN-2017, entry version 19. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=GM47_1665 {ECO:0000313|EMBL:KGA04441.1}; OS actinobacterium acIB-AMD-6. OC Bacteria; Actinobacteria. OX NCBI_TaxID=1504321 {ECO:0000313|EMBL:KGA04441.1, ECO:0000313|Proteomes:UP000029266}; RN [1] {ECO:0000313|EMBL:KGA04441.1, ECO:0000313|Proteomes:UP000029266} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Ghai R., Mizuno C.M., Picazo A., Camacho A., Rodriguez-Valera F.; RT "Key roles for freshwater Actinobacteria revealed by deep metagenomic RT sequencing."; RL Submitted (MAY-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KGA04441.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JNSH01000014; KGA04441.1; -; Genomic_DNA. DR PATRIC; fig|1504321.4.peg.339; -. DR Proteomes; UP000029266; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000313|EMBL:KGA04441.1}; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000029266}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900, KW ECO:0000313|EMBL:KGA04441.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000029266}. FT DOMAIN 264 429 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 223 257 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 484 AA; 53020 MW; 338FDF52B24A53AD CRC64; MSDKGIGNGD GLEIDIDTLI RENAQAVADY ELADSPQSSN QDLQDRQALR RVSGLSTELQ DVSDAEYRQL RLEKVVLVGV WTEGTSKDAD NSIKELAALA ETAGSQVMEA LIQRRDKPDA ATFIGSGKVA EVRQAVVATG ADTVVCDGEL SPAQLRTLEQ KVKVKVIDRT ALILDIFAQH AKSREGKAQV ELAQMSYMLP RLRGWGESLS RQAGGIGGRG PGETKIETDR RRINDKMAKL RREIKDMKTS RDTKRNERRR KNIPSVAIAG YTNAGKSSLL NRLTGSDVLV ENALFATLDP TVRKTQSEDG RIYTYTDTVG FVRHLPHQLV EAFKSTLEEV SQSDLIVHVV DGSHPDPFEQ IRAVREVINE IGGGEIMEII AVNKADIAAP EVLMELLRKE SNAYAISART GYGVPALTKA IESHLPKPKV EINAVIPFDR GDLVSLIHEQ GEIISEEYLP EGTKIHAMVG GALARKIEML VVNS // ID A0A094PTA6_9ACTN Unreviewed; 448 AA. AC A0A094PTA6; DT 26-NOV-2014, integrated into UniProtKB/TrEMBL. DT 26-NOV-2014, sequence version 1. DT 07-JUN-2017, entry version 17. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=GM46_0215 {ECO:0000313|EMBL:KGA12904.1}; OS actinobacterium acAcidi. OC Bacteria; Actinobacteria. OX NCBI_TaxID=1504320 {ECO:0000313|EMBL:KGA12904.1, ECO:0000313|Proteomes:UP000029305}; RN [1] {ECO:0000313|EMBL:KGA12904.1, ECO:0000313|Proteomes:UP000029305} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Ghai R., Mizuno C.M., Picazo A., Camacho A., Rodriguez-Valera F.; RT "Key roles for freshwater Actinobacteria revealed by deep metagenomic RT sequencing."; RL Submitted (MAY-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KGA12904.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JNSG01000002; KGA12904.1; -; Genomic_DNA. DR PATRIC; fig|1504320.4.peg.44; -. DR Proteomes; UP000029305; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000029305}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000029305}. FT DOMAIN 219 383 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 178 205 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 448 AA; 48848 MW; 06BB30F44138BD57 CRC64; MTNSSPNSPY NQALGQTLIE RSIRERIVLV GVTLNGKTEE ETEASLDELS LLIDTAGADE AGRLTQKRDV PDHTWFVGKG KAEELRDLCL AVDADTVVFD NELSPGQQYN LEKLLGRTAI DRTAVILDIF AQNAHTLEGK AQVELALLRY RLPRLRRGAD AKMSQQRGGV GSRFGSGETK LEVDRRRIKN RISRLEQELK ELGGTRDLQR KGRSRSGLAN VVIVGYTNAG KSTLLNRLTN AGVLVEDRLF ATLDPTTRRL SFPGGEPVLV TDTVGFVRRL PHGLVESFKS TLEVAARADY LVHVVDGSSS DPDGQIDAVR TVLREIHADE VPEFVVFNKS DLDPVGVADV VAWHPGSVGI SAHTGDGIDL FLQTLSDRLR SVSKVIELLI PYERGDILAA VHREGEVVST THETDGVRVR ARLAEASVGR LSEFVVSGGI DPTPTGNI // ID A0A094WFJ7_BACAO Unreviewed; 423 AA. AC A0A094WFJ7; DT 26-NOV-2014, integrated into UniProtKB/TrEMBL. DT 26-NOV-2014, sequence version 1. DT 07-JUN-2017, entry version 21. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=BALCAV_0215580 {ECO:0000313|EMBL:KGA96554.1}; OS Bacillus alcalophilus ATCC 27647 = CGMCC 1.3604. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus. OX NCBI_TaxID=1218173 {ECO:0000313|EMBL:KGA96554.1, ECO:0000313|Proteomes:UP000002754}; RN [1] {ECO:0000313|EMBL:KGA96554.1, ECO:0000313|Proteomes:UP000002754} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=AV1934 {ECO:0000313|EMBL:KGA96554.1, RC ECO:0000313|Proteomes:UP000002754}; RX PubMed=25395643; RA Attie O., Jayaprakash A., Shah H., Paulsen I.T., Morino M., RA Takahashi Y., Narumi I., Sachidanandam R., Satoh K., Ito M., RA Krulwich T.A.; RT "Draft Genome Sequence of Bacillus alcalophilus AV1934, a Classic RT Alkaliphile Isolated from Human Feces in 1934."; RL Genome Announc. 2:0-0(2014). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KGA96554.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ALPT02000056; KGA96554.1; -; Genomic_DNA. DR RefSeq; WP_003324170.1; NZ_ALPT02000056.1. DR EnsemblBacteria; KGA96554; KGA96554; BALCAV_0215580. DR Proteomes; UP000002754; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000002754}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000002754}. FT DOMAIN 198 367 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 423 AA; 48452 MW; 2AB38E375ACE1E06 CRC64; MQEEQQVAIL VGAELQQQSS HERSMDELEQ LAFACEVAVE AKVSQRLEKI NPSTYIGAGK LLEVKQVLSA TDANLVIFDD ELSPSQIRNT EQILECKVID RTILILDIFA QRAKTKEAKL QVELAKLQYM LPRLVGLRQS LGRQSGGVGT TNRGAGETKL ELDRRKIEEK MSILSKELER LVKQRQIQRG RRQKQEMPVV ALVGYTNAGK STLMNAFLQF GTNASDKKYV FEENMLFATL ETSVRKVTLP KNRSFLLTDT VGFVNKLPHH LVKAFRSTLE EVKEADLLLH VVDYSNPNYE QQIQVTNETL KEIGVENIPM IYLFNKSELV DDKFHINRED SLYVSAREKK GFEALLQTLE LSLFATDVKV EFLFPYTAGE HVHYFQNHAD VLEMEHQETG TYMKVICRLK DKQKYEQFMI KTV // ID A0A095AKU7_9SPHN Unreviewed; 430 AA. AC A0A095AKU7; DT 26-NOV-2014, integrated into UniProtKB/TrEMBL. DT 26-NOV-2014, sequence version 1. DT 07-JUN-2017, entry version 19. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:KGB51400.1}; GN ORFNames=FG95_03886 {ECO:0000313|EMBL:KGB51400.1}; OS Sphingopyxis sp. LC363. OC Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales; OC Sphingomonadaceae; Sphingopyxis. OX NCBI_TaxID=1120705 {ECO:0000313|EMBL:KGB51400.1, ECO:0000313|Proteomes:UP000029625}; RN [1] {ECO:0000313|EMBL:KGB51400.1, ECO:0000313|Proteomes:UP000029625} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=LC363 {ECO:0000313|EMBL:KGB51400.1, RC ECO:0000313|Proteomes:UP000029625}; RA Gan H.M., Gan H.Y., Barton H.A., Savka M.A.; RT "Genome sequence of acyl-homoserine lactone-producing cave bacterial RT isolate."; RL Submitted (MAY-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KGB51400.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JNFC01000073; KGB51400.1; -; Genomic_DNA. DR EnsemblBacteria; KGB51400; KGB51400; FG95_03886. DR PATRIC; fig|1120705.3.peg.3887; -. DR Proteomes; UP000029625; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 2. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000029625}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}. FT DOMAIN 189 369 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 430 AA; 47537 MW; 3F8D89E3766BA056 CRC64; MPEWHSQRLV RDLDARAEEA RGLALAIGLD VVAVHTLRLR QTRAATLLGV GQIDAIAPDI AAKGVQLVVV DAALTPIQQR NLETAFGTKV IDRTGLILEI FGERAATAEG RLQVELAHLD YQAGRLVRSW THLERQRGGF GFLGGPGETQ IEADRRMIRN RMARIRRSLE DARRTRQLQR SKRQRAPWPV IALVGYTNAG KSTFFNRLTG SDVMAEDMLF ATLDPTMREI RLPGIDKAIL SDTVGFVSDL PTELVAAFRA TLEEVTTADL IVHVRDIVHP DSEAQYDDVR AILNSLGANG PQDGGEGDTA EAIPQIEIWN KIDTADIDRR AIIEEMAARR PDVAVISAVT GEGVEDARIL MASQLTARHQ VQRIHLGYEQ GEAMAWLHAR GEVLADEPEG EGHVLTVRLD PADRARFERL WPNLRDAPTA // ID A0A095CQX3_9RHOB Unreviewed; 427 AA. AC A0A095CQX3; DT 26-NOV-2014, integrated into UniProtKB/TrEMBL. DT 26-NOV-2014, sequence version 1. DT 10-MAY-2017, entry version 17. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=JT55_07175 {ECO:0000313|EMBL:KGB82582.1}; OS Rhodovulum sp. NI22. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae; Rhodovulum. OX NCBI_TaxID=1469613 {ECO:0000313|EMBL:KGB82582.1, ECO:0000313|Proteomes:UP000029524}; RN [1] {ECO:0000313|EMBL:KGB82582.1, ECO:0000313|Proteomes:UP000029524} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NI22 {ECO:0000313|EMBL:KGB82582.1, RC ECO:0000313|Proteomes:UP000029524}; RA Ruiz O.N., Brown L.M., Smart C.E., Striebich R.C., Bowen L., Lee J.S., RA Little B.J., Mueller S.R., Gunasekera T.S.; RT "Effect of Conventional and Alternative Fuels on Marine Bacterial RT Community and the Isolation of a Novel Hydrocarbon Degrading RT Rhodovulum sp., (R. navalis)."; RL Submitted (AUG-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KGB82582.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JQFU01000012; KGB82582.1; -; Genomic_DNA. DR EnsemblBacteria; KGB82582; KGB82582; JT55_07175. DR Proteomes; UP000029524; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000029524}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000029524}. FT DOMAIN 207 376 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 427 AA; 47193 MW; 888BBD86CBBEBFC0 CRC64; MTGFEDHSPT PTRAWVLHPE ITSDRARRAS GPALEEAVAL AAALPGLEVV GAEVVRLPKA RPGLLFGTGK VDEIGAKLAA QEVGLVLVDG HVTPVQQRNL EREWKVKLLD RTGLILEIFA DRARTREGVL QVELAALSYQ RTRLVRAWTH LERQRGGLGF VGGPGETQIE ADRRAIDEAI TRIKRQLSKV AKTRELHRAA RKKVPFPVVA LVGYTNAGKS TLFNRLTGAE VMAKDMLFAT LDPTMRGVVL PSGRKIILSD TVGFISELPT QLVAAFRATL EEVLEADLIV HVRDISHADS DEQARDVASI LGELGVSETT PLIEVWNKID RLDEARRAAL AVKAEREPDI FSLSALTGEG VDTLLAAVSA ALDEERFELD LHLGFDEGKR RAWLFQQGVV ESEEQVEDGY RLHVRWTARQ ESRFREI // ID A0A095U295_9FLAO Unreviewed; 406 AA. AC A0A095U295; DT 26-NOV-2014, integrated into UniProtKB/TrEMBL. DT 26-NOV-2014, sequence version 1. DT 07-JUN-2017, entry version 20. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=LG45_03420 {ECO:0000313|EMBL:KGD68708.1}; OS Flavobacterium aquatile LMG 4008. OC Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales; OC Flavobacteriaceae; Flavobacterium. OX NCBI_TaxID=1453498 {ECO:0000313|EMBL:KGD68708.1, ECO:0000313|Proteomes:UP000029554}; RN [1] {ECO:0000313|EMBL:KGD68708.1, ECO:0000313|Proteomes:UP000029554} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=LMG 4008 {ECO:0000313|EMBL:KGD68708.1, RC ECO:0000313|Proteomes:UP000029554}; RA Gale A.N., Pipes S.E., Newman J.D.; RT "Whole Genome Shotgun of Flavobacterium aquatile LMG 4008."; RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KGD68708.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JRHH01000002; KGD68708.1; -; Genomic_DNA. DR RefSeq; WP_035124396.1; NZ_JRHH01000002.1. DR EnsemblBacteria; KGD68708; KGD68708; LG45_03420. DR Proteomes; UP000029554; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000029554}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000029554}. FT DOMAIN 200 386 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 406 AA; 46898 MW; 2A7E15DDA44D53A3 CRC64; MIEKEKINFE KTVVVGVVTQ NQSEEKLTEY LDELEFLTFT AGGEVVKRFW QKMDKPNPKT FLGTGKMDEI ALYCKENEIS TVIFDDELSP SQQKNISKVI DSKILDRTNL ILDIFAQRAE SSYARTQVEL AQCQYLLPRL SGMWTHLERQ KGGIGLRGPG ETEIETDRRI VRDRIALLKE KIKTIDRQMS VQRSNRGAMV RVALVGYTNV GKSTLMNVIS KSEVFVENKL FATLDTTVRK VVIGNLPFLL SDTVGFIRKL PTQLVESFKS TLDEVREADL LLHIVDISHP DFEDHIASVN QILMDIKSNN KPVIMVFNKI DAFKHLTIDE DDLITEKTSK HYTLEEWKQT WMSNVGAENA LFISAIEKEN FEEFRERIYE KVREIHVTRF PYNKFLYPDF KDIVVE // ID A0A095V099_9RHIZ Unreviewed; 450 AA. AC A0A095V099; DT 26-NOV-2014, integrated into UniProtKB/TrEMBL. DT 26-NOV-2014, sequence version 1. DT 07-JUN-2017, entry version 19. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=JL39_21405 {ECO:0000313|EMBL:KGD94422.1}; OS Rhizobium sp. YS-1r. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium. OX NCBI_TaxID=1532558 {ECO:0000313|EMBL:KGD94422.1, ECO:0000313|Proteomes:UP000029602}; RN [1] {ECO:0000313|EMBL:KGD94422.1, ECO:0000313|Proteomes:UP000029602} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=YS-1r {ECO:0000313|EMBL:KGD94422.1, RC ECO:0000313|Proteomes:UP000029602}; RA Prabhakaran M., Cougar B., Weirick T., Fathepure B.Z.; RT "Genome sequences of the lignin degrading proteobacteria."; RL Submitted (AUG-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KGD94422.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JPYQ01000032; KGD94422.1; -; Genomic_DNA. DR RefSeq; WP_037155115.1; NZ_JPYQ01000032.1. DR EnsemblBacteria; KGD94422; KGD94422; JL39_21405. DR Proteomes; UP000029602; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000029602}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000029602}. FT DOMAIN 212 384 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 171 205 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 450 AA; 49512 MW; 0B060A1C126773A3 CRC64; MRAVVVVPVL KQARPQAGHR AGQGDSPAAP VPQRSSEARL DEAIGLAKAI DLTVVEGLIV PVGQPRPATL IGTGKIEEIK ALLDAKNAGL VIVDHPLTPV QQRNLEKEWN AKVIDRTGLI LEIFGRRAST KEGTLQVDLA HLNYQKGRLV RSWTHLERQR GGAGFMGGPG ETQIEADRRL LQERIVRLER ELEQVVRTRQ LHRAKRRKVP HPIVALVGYT NAGKSTLFNR ITGAGVLAED MLFATLDPTL RRMKLPHGRT VILSDTVGFI SDLPTHLVAA FRATLEEVLE ADLILHVRDM SDPDNAAQAS DVLRILADLG IGEKEGAERI IEVWNKIDRL DPEAHEAIAE RAAGRKNVMA VSAITGEGID ALMEEIARRL SGVLTETTIT IPPDRLSLVS WVYGDAVVDD RKDNDDGSVT LDVRLTERQA ADLERRLGNA PKPVKEDWER // ID A0A095WVS8_9ACTO Unreviewed; 508 AA. AC A0A095WVS8; DT 26-NOV-2014, integrated into UniProtKB/TrEMBL. DT 26-NOV-2014, sequence version 1. DT 07-JUN-2017, entry version 20. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=HMPREF1628_03660 {ECO:0000313|EMBL:KGF01885.1}; OS Actinomyces sp. S4-C9. OC Bacteria; Actinobacteria; Actinomycetales; Actinomycetaceae; OC Actinomyces. OX NCBI_TaxID=1219581 {ECO:0000313|EMBL:KGF01885.1, ECO:0000313|Proteomes:UP000035029}; RN [1] {ECO:0000313|EMBL:KGF01885.1, ECO:0000313|Proteomes:UP000035029} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=S4-C9 {ECO:0000313|EMBL:KGF01885.1, RC ECO:0000313|Proteomes:UP000035029}; RA McCorrison J., Sanka R., Torralba M., Gillis M., Haft D.H., Methe B., RA Sutton G., Nelson K.E.; RL Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KGF01885.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JRMU01000007; KGF01885.1; -; Genomic_DNA. DR RefSeq; WP_034507987.1; NZ_JRMU01000007.1. DR EnsemblBacteria; KGF01885; KGF01885; HMPREF1628_03660. DR Proteomes; UP000035029; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 2. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000035029}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000035029}. FT DOMAIN 288 454 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 508 AA; 55413 MW; 0C6797F9ED6D543A CRC64; MKERDQDLDV QRAEDVVARV LARSKRRPEM QRVEGMSLAE RATSLQSTRG QTENSAGSLE REARAGTRRV ASLSTELEDV SEVEYRQLRL ERVVLIGIFD FDASEAENSL HELAALAQTA GSTVLDGVLQ RRANPDPATY LGSGKAKELA RIVESVGADT VIVDGELAPS QRRALEDVVK VKVVDRTALI LDIFAQHAKS REGKAQVELA QLEYLLPRLR GWGESMSRQA GGRVAGGEGI GSRGPGETKI ELDRRRIRTR MAKLRREIKE MKPSRETQRH SRRAGGVPSV AIVGYTNAGK STLLNRITGA DVMVQDALFA TLDPTVRQAI TPDNRVYTLV DTVGFVRNLP TQLVEAFRST LEEVAEADVI LHVVDAAHPD PIGQVHTVME VLSQIEGASD IPQVLALNKA DLASPEQVAV LRSKFANSVA VSAKTGAGIT KLEQLISATL PRPSKYVDVV VPYADGDLVN RFHEMGEIEK EEYLPGGTHL VGRVDADLAY ELSLVDVS // ID A0A095XE04_9FIRM Unreviewed; 406 AA. AC A0A095XE04; DT 26-NOV-2014, integrated into UniProtKB/TrEMBL. DT 26-NOV-2014, sequence version 1. DT 07-JUN-2017, entry version 19. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=HMPREF1634_02985 {ECO:0000313|EMBL:KGF07891.1}; OS Tissierellia bacterium S7-1-4. OC Bacteria; Firmicutes; Tissierellia. OX NCBI_TaxID=1284708 {ECO:0000313|EMBL:KGF07891.1, ECO:0000313|Proteomes:UP000029539}; RN [1] {ECO:0000313|EMBL:KGF07891.1, ECO:0000313|Proteomes:UP000029539} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=S7-1-4 {ECO:0000313|EMBL:KGF07891.1, RC ECO:0000313|Proteomes:UP000029539}; RA McCorrison J., Sanka R., Torralba M., Gillis M., Haft D.H., Methe B., RA Sutton G., Nelson K.E.; RL Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KGF07891.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JRMY01000006; KGF07891.1; -; Genomic_DNA. DR RefSeq; WP_034545967.1; NZ_JRMY01000006.1. DR EnsemblBacteria; KGF07891; KGF07891; HMPREF1634_02985. DR Proteomes; UP000029539; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000029539}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000029539}. FT DOMAIN 193 360 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 152 179 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 406 AA; 46197 MW; 483E3AA8043D2085 CRC64; MDFKDKKAVI IANDISEDSP RQKENIELVK SLGAEVISVL IQNIQRINPK YYFGSGKIEY FSNISKELKA DFIVVCEDLS PRQLQNVKDE FDMLVIDRNQ LILELFNQRA TTAFGKLQVE LATLSYMYPR LRGMRKDMDR QFGVMGMRGA GEQKLELDRR VLRKRIDKLK EDVKAAQVVL DTKSKMRSDS SIPIVSLIGY SNTGKSTLLN RIIELSGADE DKRVYADDRL FATLDTHARR IELPHGGDII LTDTVGLISN LPHQLIDAFR STLLEIKKAD LLVQVLDISN KHLDVEIETT ENLIKDLGLG DKKIIKVYNK ADKVVDKHIY ADADMVISAY NDGDVRSLLK AIELELYGEA VEDTKFFPYS EAKELSLFME NNQIISKKYS DEGTVVTYTK YLKRGL // ID A0A095XG20_9FIRM Unreviewed; 416 AA. AC A0A095XG20; DT 26-NOV-2014, integrated into UniProtKB/TrEMBL. DT 26-NOV-2014, sequence version 1. DT 10-MAY-2017, entry version 18. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=HMPREF1635_06245 {ECO:0000313|EMBL:KGF08788.1}; OS Clostridiales bacterium S5-A14a. OC Bacteria; Firmicutes; Clostridia; Clostridiales; OC Clostridiales Family XIII. Incertae Sedis. OX NCBI_TaxID=1230734 {ECO:0000313|EMBL:KGF08788.1, ECO:0000313|Proteomes:UP000029601}; RN [1] {ECO:0000313|EMBL:KGF08788.1, ECO:0000313|Proteomes:UP000029601} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=S5-A14a {ECO:0000313|EMBL:KGF08788.1, RC ECO:0000313|Proteomes:UP000029601}; RA McCorrison J., Sanka R., Torralba M., Gillis M., Haft D.H., Methe B., RA Sutton G., Nelson K.E.; RL Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KGF08788.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JRNA01000017; KGF08788.1; -; Genomic_DNA. DR EnsemblBacteria; KGF08788; KGF08788; HMPREF1635_06245. DR Proteomes; UP000029601; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000029601}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000029601}. FT DOMAIN 189 362 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 148 182 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 416 AA; 47487 MW; E2A25CE4BCF55CC4 CRC64; MLVGVSKNNY NYEIETSLDE LESLVESANG IVLGKMIQKL DKINTSTYIG KGKVVELAEY VANLEVDTVV FDDELSGIQI RNLEDQIGTK VIDRTILIMD IFAARANSKE GRLQVELAQL QYRLPRLVGF GKSLSKLGGG IGTRGPGEKQ IETDRRHIRR RIDDLKRDLA DIQKTRTLHR KKRKKSGIPI VALVGYTNVG KSAIMNYMLE NYGKEEKKVE EEDMLFATLD AKHRLIEFDN NRQFILVDTV GFVSKLSHNL VDAFKGTLQE AEYADLIIQV EDISHNRTDF QREVLNNVLD DLKLSEKKSI FVYNKIDKID NQIENSSIFE QNNDNRVFVS AKTGLNMDKL KNAIEKNVFE DEKELKLLIP FDKANLASKL CDNTNVLNIE YKDDGIHMLA RLNERDQELV KKYVTI // ID A0A095XKQ7_9FIRM Unreviewed; 408 AA. AC A0A095XKQ7; DT 26-NOV-2014, integrated into UniProtKB/TrEMBL. DT 26-NOV-2014, sequence version 1. DT 07-JUN-2017, entry version 19. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=HMPREF1633_10525 {ECO:0000313|EMBL:KGF10276.1}; OS Tissierellia bacterium S5-A11. OC Bacteria; Firmicutes; Tissierellia. OX NCBI_TaxID=1230730 {ECO:0000313|EMBL:KGF10276.1, ECO:0000313|Proteomes:UP000029576}; RN [1] {ECO:0000313|EMBL:KGF10276.1, ECO:0000313|Proteomes:UP000029576} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=S5-A11 {ECO:0000313|EMBL:KGF10276.1, RC ECO:0000313|Proteomes:UP000029576}; RA McCorrison J., Sanka R., Torralba M., Gillis M., Haft D.H., Methe B., RA Sutton G., Nelson K.E.; RL Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KGF10276.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JRMZ01000038; KGF10276.1; -; Genomic_DNA. DR RefSeq; WP_034439496.1; NZ_JRMZ01000038.1. DR EnsemblBacteria; KGF10276; KGF10276; HMPREF1633_10525. DR Proteomes; UP000029576; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0051087; F:chaperone binding; IEA:InterPro. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR Gene3D; 1.20.58.120; -; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR003103; BAG_domain. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000029576}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000029576}. FT DOMAIN 188 355 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 154 181 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 408 AA; 46106 MW; B0F69AD374C70B0D CRC64; MDQKEGVILL TTNLSPSSPE ETRALIQADN GCVLAELSQN LKEPGPYYIG KGKLEELKAL IQSLDPDLVL VNDDLKGFQL RNLERELDIQ VMDRTHLILD IFASRARTKQ AKLQVLLAQL TYGKSRLIGS YSLSKAGGGI GTRGPGEQKL ELDRRKIDRQ IHQIQSRLDE IKSQRQEQLK QRKKSQVPLV SFVGYTNAGK STMMNALLGQ ESDKRVFVKD MVFATLDTSL RSVKLLDKRP VILADTVGFI SDLPETLMEA FQSTLDELKN SSALVHVLDG QSESLQKDYM ETLKILKALD LMDIPRLTVF NKIDRPDMRP QVIQPRPDKL LFYSALNDPV EKLEEALVDL LGDQWVQGEI FFSFQDQGLL NRALKDYPQA QVSYNEKGSL LKGEFLREDM EKWTGGKQ // ID A0A095XZJ6_9GAMM Unreviewed; 421 AA. AC A0A095XZJ6; DT 26-NOV-2014, integrated into UniProtKB/TrEMBL. DT 26-NOV-2014, sequence version 1. DT 30-AUG-2017, entry version 21. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=HRUBRA_00195 {ECO:0000313|EMBL:KGE05186.1}; OS Pseudohaliea rubra DSM 19751. OC Bacteria; Proteobacteria; Gammaproteobacteria; Cellvibrionales; OC Halieaceae; Pseudohaliea. OX NCBI_TaxID=1265313 {ECO:0000313|EMBL:KGE05186.1, ECO:0000313|Proteomes:UP000029640}; RN [1] {ECO:0000313|EMBL:KGE05186.1, ECO:0000313|Proteomes:UP000029640} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 19751 {ECO:0000313|EMBL:KGE05186.1, RC ECO:0000313|Proteomes:UP000029640}; RX PubMed=25414506; RA Spring S., Fiebig A., Riedel T., Goker M., Klenk H.P.; RT "Genome Sequence of Gammaproteobacterial Pseudohaliea rubra Type RT Strain DSM 19751, Isolated from Coastal Seawater of the Mediterranean RT Sea."; RL Genome Announc. 2:e01208-14(2014). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KGE05186.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AUVB01000008; KGE05186.1; -; Genomic_DNA. DR RefSeq; WP_035518156.1; NZ_KN234806.1. DR EnsemblBacteria; KGE05186; KGE05186; HRUBRA_00195. DR PATRIC; fig|1265313.6.peg.195; -. DR Proteomes; UP000029640; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000029640}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000029640}. FT DOMAIN 199 365 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 421 AA; 46513 MW; DEA80D29C5A136E3 CRC64; MFFDRPASGE VAVLVHLAMG RECEADDPRE FEELVLSAGG DPVAYIMGRR DAPHPGTFVG SGKVEEIAAL VHEHDAQVVI FNHTLSPSQE RNLERALKCR VLDRTGLILD IFAQRARTHE GKLQVELAQL RHMSTRLVRG WTHLERQKGG IGLRGPGETQ LETDRRLLRA RIKAIVARLE KVRRQREQGR RSRRRAEVPT VALVGYTNAG KSTLFNGLTT AGVYAADQLF ATLDPTLRRL SLPEAGPVIL ADTVGFISHL PHRLVDAFKA TLEETRNADL LLHVVDAASE DRAEQAHQVR EVLREIGAED VPQLEVYNKI DLLALAPRID RDEAGRPLRA WVSARDGLGL EGLLGAIGEL VGDDMVARDL VLAPEQGRLR AALYRLGAVR DERYGSDGAA HVSVRLPRAD WERLVANEGA P // ID A0A095Y7D0_9BACT Unreviewed; 415 AA. AC A0A095Y7D0; DT 26-NOV-2014, integrated into UniProtKB/TrEMBL. DT 26-NOV-2014, sequence version 1. DT 07-JUN-2017, entry version 19. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=HMPREF1640_05505 {ECO:0000313|EMBL:KGF17981.1}; OS Prevotella sp. S7-1-8. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Prevotellaceae; OC Prevotella. OX NCBI_TaxID=1284775 {ECO:0000313|EMBL:KGF17981.1, ECO:0000313|Proteomes:UP000029597}; RN [1] {ECO:0000313|EMBL:KGF17981.1, ECO:0000313|Proteomes:UP000029597} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=S7-1-8 {ECO:0000313|EMBL:KGF17981.1, RC ECO:0000313|Proteomes:UP000029597}; RA McCorrison J., Sanka R., Torralba M., Gillis M., Haft D.H., Methe B., RA Sutton G., Nelson K.E.; RL Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KGF17981.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JRNC01000031; KGF17981.1; -; Genomic_DNA. DR RefSeq; WP_036892878.1; NZ_JRNC01000031.1. DR EnsemblBacteria; KGF17981; KGF17981; HMPREF1640_05505. DR Proteomes; UP000029597; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000029597}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000029597}. FT DOMAIN 216 400 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 415 AA; 47470 MW; FF35DE5316DC635F CRC64; MKEFVISEAK AETAILVGLI TPQQDEAKTN EYLDELDFLA DTAGAVTVKR YTQRVNGPNQ VTYVGKGKLE EIKTYIENEA DEDREVGMVI FDDELSAKQL RNIENALKVK ILDRTSLILD IFAMRAQTAN AKTQVELAQY RYMLPRLQRL WTHLERQRGG AGAGGGKGSV GLRGPGETQL EMDRRIILQR ITLLKQRLAD IEKQKNTQRK NRGRLIRVAL VGYTNVGKST IMNILAKSDV FAENKLFATL DTTVRKVVIE NLPFLLADTV GFIRKLPTDL VDSFKSTLDE VREADLLVHV IDISHPDFEE QVKVVKNTLK DLDCAEKPTI MVFNKIDNYH WVDKEPDDLT PETKENVTLD ELKKTWMARH DEDCIFVSAK LKENLDELRG TLYRKVRELH VQKYPYNDFL YPVDD // ID A0A095YFZ0_9ACTO Unreviewed; 490 AA. AC A0A095YFZ0; DT 26-NOV-2014, integrated into UniProtKB/TrEMBL. DT 26-NOV-2014, sequence version 1. DT 07-JUN-2017, entry version 19. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=HMPREF1631_06560 {ECO:0000313|EMBL:KGF05462.1}; OS Arcanobacterium sp. S3PF19. OC Bacteria; Actinobacteria; Actinomycetales; Actinomycetaceae; OC Arcanobacterium. OX NCBI_TaxID=1219585 {ECO:0000313|EMBL:KGF05462.1, ECO:0000313|Proteomes:UP000054502}; RN [1] {ECO:0000313|EMBL:KGF05462.1, ECO:0000313|Proteomes:UP000054502} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=S3PF19 {ECO:0000313|EMBL:KGF05462.1, RC ECO:0000313|Proteomes:UP000054502}; RA McCorrison J., Sanka R., Torralba M., Gillis M., Haft D.H., Methe B., RA Sutton G., Nelson K.E.; RL Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KGF05462.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JRMX01000015; KGF05462.1; -; Genomic_DNA. DR RefSeq; WP_034233601.1; NZ_JRMX01000015.1. DR EnsemblBacteria; KGF05462; KGF05462; HMPREF1631_06560. DR Proteomes; UP000054502; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000054502}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000054502}. FT DOMAIN 270 436 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 490 AA; 53949 MW; 121303B476865953 CRC64; MTFGEQRQEL REHRVEVHSR QGTALQADPN YRGDWAGDSL ERDVRSSLRR IPNLSSMREE QVDVEYRRLR LERVVLAGLW TQGTFAEAED SLRELAALAE TAGSQVLDGV IQRRQIPERT TFLGSGKARE LADIVHAAEA DTVIVDSELA PSQRRALEDI VKVKVIDRTA LILDIFARHA KSREGKAQVE LAQLEYLLPR LRGWGESMSR QAGGRVAAGA GIGSRGPGET KIELDRRRIR TRMAKLRRDL EKMHPARLAQ KNRRRKRKIP SAVVVGYTNA GKSSLLNVLT DSAVLVENAL FATLDPTVRR SKTADGRAFT LTDTVGFVRS LPTQLVEAFR STLEEAAEAD LLLHVVDASH HDPVGQVEAV HRVLRDVPGV SQVRELIVLS KADLADSVDL TVLRSKFPDS VAVSAVTGLG IEELKQKIAL LLPCPCERIE AVIPYAHGDI VARIHAEGEV LGESFSASGT RITALVEKDL AAAVRQCADK // ID A0A095ZFG0_9FIRM Unreviewed; 412 AA. AC A0A095ZFG0; DT 26-NOV-2014, integrated into UniProtKB/TrEMBL. DT 26-NOV-2014, sequence version 1. DT 12-APR-2017, entry version 18. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=HMPREF2134_07345 {ECO:0000313|EMBL:KGF33495.1}; OS Peptoniphilus lacrimalis DNF00528. OC Bacteria; Firmicutes; Tissierellia; Tissierellales; Peptoniphilaceae; OC Peptoniphilus. OX NCBI_TaxID=1401070 {ECO:0000313|EMBL:KGF33495.1, ECO:0000313|Proteomes:UP000029621}; RN [1] {ECO:0000313|EMBL:KGF33495.1, ECO:0000313|Proteomes:UP000029621} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DNF00528 {ECO:0000313|EMBL:KGF33495.1, RC ECO:0000313|Proteomes:UP000029621}; RA McCorrison J., Sanka R., Torralba M., Gillis M., Haft D.H., Methe B., RA Sutton G., Nelson K.E.; RL Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KGF33495.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JRNL01000072; KGF33495.1; -; Genomic_DNA. DR EnsemblBacteria; KGF33495; KGF33495; HMPREF2134_07345. DR Proteomes; UP000029621; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000029621}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000029621}. FT DOMAIN 199 359 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 158 192 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 412 AA; 46785 MW; 42706DC52A80A9AA CRC64; MIETEKKEER VLLIGVELQG MDNFDLSMEE LASLAKTAGA VVVDSYRQKR EKYDSKTFVG SGKLEEIAQM VDAEEITTVI VNNRLTPRQN VNLEEVLGVK VIDRMQLILD IFAMRARSHE GKLQVHLAQL KYLLPRLVGQ GIMLSRQAGG IGSRGPGESQ LELNRRSVRN QITDIERQLK VVEKNRATVR EKRLESSTFK IGLIGYTNAG KSTIMNTLTS KTQYEADELF ATLDATTKSI HLGGNLQVTL TDTVGFIQDL PTELVSSFKS TLEESKHVDL LVHVIDASNP YHEEHEKTVL SIMKDLDMED IPRLTLYNKA DLVEDFTPTQ TPYALISAKS KDSREQLQAL LLDKIKEIFE AFTLRVPFSK SYKIHDLESV AILEERDYQD DGEVIRGYIS EKNKWRLEEF YD // ID A0A095ZL06_9FIRM Unreviewed; 422 AA. AC A0A095ZL06; DT 26-NOV-2014, integrated into UniProtKB/TrEMBL. DT 26-NOV-2014, sequence version 1. DT 12-APR-2017, entry version 18. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=HMPREF2134_04165 {ECO:0000313|EMBL:KGF35440.1}; OS Peptoniphilus lacrimalis DNF00528. OC Bacteria; Firmicutes; Tissierellia; Tissierellales; Peptoniphilaceae; OC Peptoniphilus. OX NCBI_TaxID=1401070 {ECO:0000313|EMBL:KGF35440.1, ECO:0000313|Proteomes:UP000029621}; RN [1] {ECO:0000313|EMBL:KGF35440.1, ECO:0000313|Proteomes:UP000029621} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DNF00528 {ECO:0000313|EMBL:KGF35440.1, RC ECO:0000313|Proteomes:UP000029621}; RA McCorrison J., Sanka R., Torralba M., Gillis M., Haft D.H., Methe B., RA Sutton G., Nelson K.E.; RL Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KGF35440.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JRNL01000023; KGF35440.1; -; Genomic_DNA. DR EnsemblBacteria; KGF35440; KGF35440; HMPREF2134_04165. DR Proteomes; UP000029621; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000029621}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000029621}. FT DOMAIN 200 368 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 159 193 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 422 AA; 48200 MW; 614D5CF86316C2A1 CRC64; MEDVSSKKIE RVITVGTDIG AYPNSLETSM KELDELCYAD GAEVIGQMTQ NLEKFNPKYL IGKGKVKEIK EMAENLEADA IVFNDELTGI QLRNLEDTIK KKVVDRTNLI LDIFALRAST YEGKLQVELA QLEYQLPRLL GIKGWSRTGG GIGTRGPGEQ IIETDRRRLL REIDKIKEKL NKAKKTRDTT RSKRMNSKIP TVSLVGYTNA GKSTILNRIK EDDSKEVFVK DMLFATLDPN SRKARLLSGR EFIISDTVGF VSKLPTKLIE AFKSTLEEIK YSDLIVHVID ASSKDLEIAY DTTMNILQEI GIKDKKILTV FNKSDKIDLN STTIPLKIKS QKIYISAKND PDMNKLLKAI EENLPEQYIY TKLNFPYDDT DILYKLIERF DLKPIYKENF IEIELSLSKK EYNKLKRYVA NV // ID A0A096AU06_9BACT Unreviewed; 414 AA. AC A0A096AU06; DT 26-NOV-2014, integrated into UniProtKB/TrEMBL. DT 26-NOV-2014, sequence version 1. DT 07-JUN-2017, entry version 19. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=HMPREF2137_09180 {ECO:0000313|EMBL:KGF34102.1}; OS Prevotella buccalis DNF00853. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Prevotellaceae; OC Prevotella. OX NCBI_TaxID=1401074 {ECO:0000313|EMBL:KGF34102.1, ECO:0000313|Proteomes:UP000029556}; RN [1] {ECO:0000313|EMBL:KGF34102.1, ECO:0000313|Proteomes:UP000029556} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DNF00853 {ECO:0000313|EMBL:KGF34102.1, RC ECO:0000313|Proteomes:UP000029556}; RA McCorrison J., Sanka R., Torralba M., Gillis M., Haft D.H., Methe B., RA Sutton G., Nelson K.E.; RL Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KGF34102.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JRNN01000073; KGF34102.1; -; Genomic_DNA. DR RefSeq; WP_036873764.1; NZ_JRNN01000073.1. DR EnsemblBacteria; KGF34102; KGF34102; HMPREF2137_09180. DR Proteomes; UP000029556; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000029556}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}. FT DOMAIN 216 400 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 414 AA; 47443 MW; 843C811EB8CAC70C CRC64; MKEFVISEAK AETAILVGLI TQEQNEEKTN EYLDELEFLA DTAGAVTVKR FTQKLGGPNM VSYVGKGKLE EIKQYIENEK ENDRPVGMVI FDDELSAKQI RNIEKELQVK ILDRTSLILD IFAMRAQTAN AKTQVELAQY RYMLPRLQRL WTHLERQGGG SGSGGGKGSV GLRGPGETQL EMDRRIILQR ITLLKQRLIE IDKQKTTQRK NRGRLIRVAL VGYTNVGKST LMNLLSKSEV FAENKLFATL DTTVRKVVIE NLPFLLADTV GFIRKLPTDL VDSFKSTLDE VREADLLLHV VDISHPDFEE QIRVVDNTLK ELDAADKPTM IVFNKIDQYR WVEKAPDDLT PSTQENISLE ELKRTWMAKL NENCVFISAK QKQNIDEFRE TLYKAVRQLH VQKYPYNDFL YPTD // ID A0A096BFC2_9BURK Unreviewed; 363 AA. AC A0A096BFC2; DT 26-NOV-2014, integrated into UniProtKB/TrEMBL. DT 26-NOV-2014, sequence version 1. DT 07-JUN-2017, entry version 20. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=HMPREF2130_02290 {ECO:0000313|EMBL:KGF31859.1}; OS Oligella urethralis DNF00040. OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Alcaligenaceae; Oligella. OX NCBI_TaxID=1401065 {ECO:0000313|EMBL:KGF31859.1, ECO:0000313|Proteomes:UP000029629}; RN [1] {ECO:0000313|EMBL:KGF31859.1, ECO:0000313|Proteomes:UP000029629} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DNF00040 {ECO:0000313|EMBL:KGF31859.1, RC ECO:0000313|Proteomes:UP000029629}; RA McCorrison J., Sanka R., Torralba M., Gillis M., Haft D.H., Methe B., RA Sutton G., Nelson K.E.; RL Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KGF31859.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JRNI01000010; KGF31859.1; -; Genomic_DNA. DR RefSeq; WP_036557690.1; NZ_JRNI01000010.1. DR EnsemblBacteria; KGF31859; KGF31859; HMPREF2130_02290. DR Proteomes; UP000029629; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000029629}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000029629}. FT DOMAIN 191 357 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 363 AA; 40689 MW; 3A1812B5AAD3702C CRC64; MQAFIVDVNL YGDLDFQAHH EELIMLAKGA GATIVGTLVA NRERPDPAFF IGKGKVEEAV ALAKAASAEI VIFGQPLSPA QQRNLQEEFN CRVVDRVALI LDIFALRAQS HEGKIQVELA QLQYMRTRLS MIWSKFEQQQ GGIGTRGPGE TQLELDRRII GGRIKALGER LKKVRKQREN QRRQRMRSGT FMVSLVGYTN TGKSTLFNAM TRADAYAADQ LFATLDTTTR RVWIEGAGQI TLSDTVGFIR ELPTTLIEAF KATLEESLYA DVLLHVIDSS SPQKEEQIFE VNKVLQEIGA QHIPTILVYN KTDLTEQEPR LELDESGRVS RVFLSAAERS GLEFLREAIV LTKQQLEKTI DAK // ID A0A096BJ02_9CLOT Unreviewed; 428 AA. AC A0A096BJ02; DT 26-NOV-2014, integrated into UniProtKB/TrEMBL. DT 26-NOV-2014, sequence version 1. DT 12-APR-2017, entry version 17. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=Y919_01855 {ECO:0000313|EMBL:KGG81155.1}; OS Caloranaerobacter azorensis H53214. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Caloranaerobacter. OX NCBI_TaxID=1156417 {ECO:0000313|EMBL:KGG81155.1, ECO:0000313|Proteomes:UP000029622}; RN [1] {ECO:0000313|EMBL:KGG81155.1, ECO:0000313|Proteomes:UP000029622} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=H53214 {ECO:0000313|EMBL:KGG81155.1, RC ECO:0000313|Proteomes:UP000029622}; RA Jiang L.J., Shao Z.Z., Long M.N.; RT "Draft genome sequence of Caloranaerobacter sp. H53214."; RL Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KGG81155.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AZTB01000005; KGG81155.1; -; Genomic_DNA. DR EnsemblBacteria; KGG81155; KGG81155; Y919_01855. DR Proteomes; UP000029622; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000029622}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000029622}. FT DOMAIN 197 368 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 163 193 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 428 AA; 48887 MW; 1A6C034BDEBB97ED CRC64; MPEDERVLLV GVDLQKKSQI SIESSMKELE ELVKAAGGIP ISSIVQKRNK IDSSYFIGKG KVEEIRLYCD ELDIDTVVFN DELSGMQIRN IENIVERKII DRTTLILDIF ANRATTKEGK LQVELAQLKY RLPRLVGLGK SLSRTGAGIG TRGPGEKKLE IDRRHILRRI SEIERQLQEV KKVREVKRKC RDKSSLPIVA LIGYTNAGKS TLLNTILNIC GEDFENKEVF AYDMLFATLE TTLRKAKLPN GHDFLITDTV GFVSKLPTHL IEAFKGTLEE IKYADLLLHV VDCTNKDLDI QIKTTLDVIK DLKVSDKPII TVFNKVDKIR EEDLIYNISG PKLFISAKEG KNIDKLLSMI QEYFSKKYHK VSLLIPYSDL DIMSKFFNTS KVEEYIYQEN GVLIKTVLDE INYNKYSKYL IENRDDAI // ID A0A096M5X8_POEFO Unreviewed; 518 AA. AC A0A096M5X8; DT 26-NOV-2014, integrated into UniProtKB/TrEMBL. DT 26-NOV-2014, sequence version 1. DT 30-AUG-2017, entry version 15. DE SubName: Full=GTP binding protein 6 (putative) {ECO:0000313|Ensembl:ENSPFOP00000026819}; OS Poecilia formosa (Amazon molly) (Limia formosa). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata; OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; OC Poeciliinae; Poecilia. OX NCBI_TaxID=48698 {ECO:0000313|Ensembl:ENSPFOP00000026819, ECO:0000313|Proteomes:UP000028760}; RN [1] {ECO:0000313|Ensembl:ENSPFOP00000026819, ECO:0000313|Proteomes:UP000028760} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=female {ECO:0000313|Ensembl:ENSPFOP00000026819}; RA Schartl M., Warren W.; RL Submitted (OCT-2013) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Ensembl:ENSPFOP00000026819} RP IDENTIFICATION. RG Ensembl; RL Submitted (OCT-2014) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an Ensembl CC automatic analysis pipeline and should be considered as CC preliminary data. {ECO:0000313|Ensembl:ENSPFOP00000026819}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AYCK01012525; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR Ensembl; ENSPFOT00000028798; ENSPFOP00000026819; ENSPFOG00000015695. DR GeneTree; ENSGT00390000001397; -. DR OMA; MDTVGFM; -. DR OrthoDB; EOG091G0852; -. DR Proteomes; UP000028760; Unassembled WGS sequence. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR CDD; cd01878; HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000028760}; KW Reference proteome {ECO:0000313|Proteomes:UP000028760}. FT DOMAIN 296 456 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 518 AA; 58373 MW; E70292864F26A2C1 CRC64; MKTLRFVHSR LPLFPRSCQR PAVACRLLPT SHRGQPPVLQ SNRSLALSAS SLKNWKDLGS SSHTEEEEED GDLLEETEVE ELFQQHVPAG IGQGQHRVFI VHPDVKWGSR KQYLTTAELM MAEAEGLVNT LDNWTVVDKI ILSTKTPEKK KIFGKGNFQL LTGKIRGTPG VTAVFVNVDR LSSVSEREFE ETWGVKVFDR YSVVLHIFRC NARTKEAKLQ ISLAEIPLLR SRLKNDMADL DQQGGGARYI GGSGETLYEV QQRLLKERET RIRSALEKLR RKRHLLRSQR KHREFPTVSV LGYTNCGKTT LIKALTGDSG LQPRNQLFAT LDVTVHAGQL PSHMTVLYVD TIGFLSQLPH QLIDSFSATL EDIIHSDLLV HVRDVSHPET VNQKANVLNV LRNLQIPHRL LDSMIEVHNK IDLLGREPCA VLISALQQRG LDELKRAVEQ EVVKSTGKQI LDLRVNLSSP QLSWLYKEAT VQDVQVNAEE GSAVVKVIIS AAAHGRYKKL FEKLRTMK // ID A0A096MEI8_POEFO Unreviewed; 400 AA. AC A0A096MEI8; DT 26-NOV-2014, integrated into UniProtKB/TrEMBL. DT 26-NOV-2014, sequence version 1. DT 30-AUG-2017, entry version 12. DE SubName: Full=GTP binding protein 6 (putative) {ECO:0000313|Ensembl:ENSPFOP00000029829}; OS Poecilia formosa (Amazon molly) (Limia formosa). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata; OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; OC Poeciliinae; Poecilia. OX NCBI_TaxID=48698 {ECO:0000313|Ensembl:ENSPFOP00000029829, ECO:0000313|Proteomes:UP000028760}; RN [1] {ECO:0000313|Ensembl:ENSPFOP00000029829, ECO:0000313|Proteomes:UP000028760} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=female {ECO:0000313|Ensembl:ENSPFOP00000029829}; RA Schartl M., Warren W.; RL Submitted (OCT-2013) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Ensembl:ENSPFOP00000029829} RP IDENTIFICATION. RG Ensembl; RL Submitted (OCT-2014) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an Ensembl CC automatic analysis pipeline and should be considered as CC preliminary data. {ECO:0000313|Ensembl:ENSPFOP00000029829}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AYCK01012525; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR Ensembl; ENSPFOT00000027683; ENSPFOP00000029829; ENSPFOG00000015695. DR GeneTree; ENSGT00390000001397; -. DR Proteomes; UP000028760; Unassembled WGS sequence. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000028760}; KW Reference proteome {ECO:0000313|Proteomes:UP000028760}. FT DOMAIN 296 373 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 400 AA; 44873 MW; E85E7C1E01C7C16D CRC64; MKTLRFVHSR LPLFPRSCQR PAVACRLLPT SHRGQPPVLQ SNRSLALSAS SLKNWKDLGS SSHTEEEEED GDLLEETEVE ELFQQHVPAG IGQGQHRVFI VHPDVKWGSR KQYLTTAELM MAEAEGLVNT LDNWTVVDKI ILSTKTPEKK KIFGKGNFQL LTGKIRGTPG VTAVFVNVDR LSSVSEREFE ETWGVKVFDR YSVVLHIFRC NARTKEAKLQ ISLAEIPLLR SRLKNDMADL DQQGGGARYI GGSGETLYEV QQRLLKERET RIRSALEKLR RKRHLLRSQR KHREFPTVSV LGYTNCGKTT LIKALTGDSG LQPRNQLFAT LDVTVHAGQL PSHMTVLYVD TIGFLSQLPH QLIDSFSATL EDIIHSVGSP VSSSTPTGIR RAFISFIRLG // ID A0A096NSG3_PAPAN Unreviewed; 519 AA. AC A0A096NSG3; DT 26-NOV-2014, integrated into UniProtKB/TrEMBL. DT 26-NOV-2014, sequence version 1. DT 30-AUG-2017, entry version 18. DE SubName: Full=GTP binding protein 6 (putative) {ECO:0000313|Ensembl:ENSPANP00000015984}; GN Name=GTPBP6 {ECO:0000313|Ensembl:ENSPANP00000015984}; OS Papio anubis (Olive baboon). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Cercopithecidae; Cercopithecinae; Papio. OX NCBI_TaxID=9555 {ECO:0000313|Ensembl:ENSPANP00000015984, ECO:0000313|Proteomes:UP000028761}; RN [1] {ECO:0000313|Ensembl:ENSPANP00000015984} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Liu Y.L., Abraham K.A., Akbar H.A., Ali S.A., Anosike U.A., RA Aqrawi P.A., Arias F.A., Attaway T.A., Awwad R.A., Babu C.B., RA Bandaranaike D.B., Battles P.B., Bell A.B., Beltran B.B., RA Berhane-Mersha D.B., Bess C.B., Bickham C.B., Bolden T.B., RA Carter K.C., Chau D.C., Chavez A.C., Clerc-Blankenburg K.C., RA Coyle M.C., Dao M.D., Davila M.L.D., Davy-Carroll L.D., Denson S.D., RA Dinh H.D., Fernandez S.F., Fernando P.F., Forbes L.F., Francis C.F., RA Francisco L.F., Fu Q.F., Garcia-Iii R.G., Garrett T.G., Gross S.G., RA Gubbala S.G., Hirani K.H., Hogues M.H., Hollins B.H., Jackson L.J., RA Javaid M.J., Jhangiani S.J., Johnson A.J., Johnson B.J., Jones J.J., RA Joshi V.J., Kalu J.K., Khan N.K., Korchina V.K., Kovar C.K., RA Lago L.L., Lara F.L., Le T.-K.L., Lee S.L., Legall-Iii F.L., RA Lemon S.L., Liu J.L., Liu Y.-S.L., Liyanage D.L., Lopez J.L., RA Lorensuhewa L.L., Mata R.M., Mathew T.M., Mercado C.M., Mercado I.M., RA Morales K.M., Morgan M.M., Munidasa M.M., Ngo D.N., Nguyen L.N., RA Nguyen T.N., Nguyen N.N., Obregon M.O., Okwuonu G.O., Ongeri F.O., RA Onwere C.O., Osifeso I.O., Parra A.P., Patil S.P., Perez A.P., RA Perez Y.P., Pham C.P., Pu L.-L.P., Puazo M.P., Quiroz J.Q., RA Rouhana J.R., Ruiz M.R., Ruiz S.-J.R., Saada N.S., Santibanez J.S., RA Scheel M.S., Schneider B.S., Simmons D.S., Sisson I.S., Tang L.-Y.T., RA Thornton R.T., Tisius J.T., Toledanes G.T., Trejos Z.T., Usmani K.U., RA Varghese R.V., Vattathil S.V., Vee V.V., Walker D.W., RA Weissenberger G.W., White C.W., Williams A.W., Woodworth J.W., RA Wright R.W., Zhu Y.Z., Han Y.H., Newsham I.N., Nazareth L.N., RA Worley K.W., Muzny D.M., Rogers J.R., Gibbs R.G.; RT "Whole Genome Assembly of Papio anubis."; RL Submitted (MAR-2012) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Ensembl:ENSPANP00000015984} RP IDENTIFICATION. RG Ensembl; RL Submitted (OCT-2014) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an Ensembl CC automatic analysis pipeline and should be considered as CC preliminary data. {ECO:0000313|Ensembl:ENSPANP00000015984}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR Ensembl; ENSPANT00000026776; ENSPANP00000015984; ENSPANG00000011580. DR GeneTree; ENSGT00390000001397; -. DR OMA; MDTVGFM; -. DR OrthoDB; EOG091G0852; -. DR Proteomes; UP000028761; Unplaced. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR CDD; cd01878; HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 4: Predicted; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000028761}; KW Reference proteome {ECO:0000313|Proteomes:UP000028761}. FT DOMAIN 298 462 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 260 291 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 519 AA; 56630 MW; 2DD7F33117223CF9 CRC64; MWALRAAVRP GLRLSRVGRG LPAPKAAGPS CPARALAAVG RRGPGNLAGP WGGGRGLQAD GGRSRAEDDE EEPEDADENA EEELLQGEPL LPAGTQRVCL VHPDVKWGPG KPQMTRAEWQ VAEATALVHT LDGWSVVQTM VVSEDAEAAP VSRLTPGPGE IQNVLKKIRG SPDITCVFLN VERMAAPTKK ELEAAWGVEV FDRFTVVLHI FRCNARTKEA RLQVALAEIP LHRSNLKRDV AHLYRGAGSR YIMGSGESFM QVQQRLLREK EAKIRKALDR LRKKRHLLRQ QRTRREFPVV SVVGYTNCGK TTLIKALTGD AAIRPRDQLF ATLDVTVHAG ALPSRMTVLY VDTIGFLSQL PHGLIESFSA TLEDVAHSDL VVHVRDVSHP EAELQKRSVL STLRSLQLPA PLLDSMVEVH NKVDLVPGYS PTEPNAVPVS ALLGHGLQEL KAELDAAVLK ATGRQILTLR VRLAGAQLSW LYKEATVQDV DVIPEDGAAD VTVIISDSAY GKFRKLFPG // ID A0A096RL53_MAIZE Unreviewed; 588 AA. AC A0A096RL53; DT 26-NOV-2014, integrated into UniProtKB/TrEMBL. DT 26-NOV-2014, sequence version 1. DT 30-AUG-2017, entry version 26. DE SubName: Full=GTP-binding protein chloroplastic {ECO:0000313|EMBL:ONM08832.1}; GN ORFNames=ZEAMMB73_Zm00001d033866 {ECO:0000313|EMBL:ONM08832.1}; OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACMAD clade; Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; OC Zea. OX NCBI_TaxID=4577 {ECO:0000313|EMBL:ONM08832.1, ECO:0000313|Proteomes:UP000007305}; RN [1] {ECO:0000313|EMBL:ONM08832.1, ECO:0000313|Proteomes:UP000007305} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. B73 {ECO:0000313|Proteomes:UP000007305}; RC TISSUE=Seedling {ECO:0000313|EMBL:ONM08832.1}; RG Maize Genome Sequencing Project; RA Ware D.; RT "Update maize B73 reference genome by single molecule sequencing RT technologies."; RL Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EnsemblPlants:Zm00001d033866_P002} RP IDENTIFICATION. RC STRAIN=cv. B73 {ECO:0000313|EnsemblPlants:Zm00001d033866_P002}; RG EnsemblPlants; RL Submitted (MAY-2017) to UniProtKB. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CM007647; ONM08832.1; -; Genomic_DNA. DR STRING; 4577.GRMZM2G101460_P02; -. DR EnsemblPlants; Zm00001d033866_T002; Zm00001d033866_P002; Zm00001d033866. DR Gramene; Zm00001d033866_T002; Zm00001d033866_P002; Zm00001d033866. DR OMA; NGPEAIS; -. DR OrthoDB; EOG09360975; -. DR Proteomes; UP000007305; Chromosome 1. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR CDD; cd01878; HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000007305}; KW Reference proteome {ECO:0000313|Proteomes:UP000007305}. FT DOMAIN 301 561 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 588 AA; 64540 MW; A78C154EF4D26FB6 CRC64; MLRGAISRLG ARLRLHADPS PASPRLRVLS TRRGKRSSPT LSPADCDDEG PLRGLFVLSR DPECPPRLLV VQPRLRPGSL LESKLAEALN LANSLEERRD GFYHSEFGAK GAPPHLVVQN PASRGRSHAD TYFGPGTVDN VKCYLSATES EEDVDAVFVN AILSGIQQRN LEVAWGKSVL DRVGLIIEIF NAHAETKEAK LQSELAALMY MKTRLVRVRG PGGRLTFGPS GEAEVVSARG RGSGGRGFMS GAGETELQLQ RRRIQERRVS LLAQIEDVRR TRAIQRSSRK RHGGSFGQEL VTVAVVGYTN AGKSTLVSAL SEADLYSDDR LFATVDPRLR SVILPSGRKA LLSDTVGFIS DLPVQLVEAF HATLEEVVEA DMLVHVLDSS ASNLEEHRST VLQVLQQIGV SQEKINNMIE VWNKIDLVDE NVKSDGIDDE VFLTEGEQED DIFSEDDAPS EQTSFDSVDV DDGADSEYLS EENSEDSNEL PSKKSFAEPT EMGAMKELSS KECFGELRVL DTNGHTFPQP ASTCHVKTSA VTGTGLQELL ALIERKLTEQ QTVVQRSYGP FDRKWRPTSM DCEKAAEP // ID A0A097ED97_9SPHN Unreviewed; 428 AA. AC A0A097ED97; DT 07-JAN-2015, integrated into UniProtKB/TrEMBL. DT 07-JAN-2015, sequence version 1. DT 07-JUN-2017, entry version 19. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=MC45_03050 {ECO:0000313|EMBL:AIT05548.1}; OS Sphingomonas taxi. OC Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales; OC Sphingomonadaceae; Sphingomonas. OX NCBI_TaxID=1549858 {ECO:0000313|EMBL:AIT05548.1, ECO:0000313|Proteomes:UP000033200}; RN [1] {ECO:0000313|EMBL:AIT05548.1, ECO:0000313|Proteomes:UP000033200} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 55669 {ECO:0000313|EMBL:AIT05548.1, RC ECO:0000313|Proteomes:UP000033200}; RA Zhou Y., Ma T., Liu T.; RT "Using Illumina technology Improving SMRT sequencing Genome Assembly RT by RASTools."; RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP009571; AIT05548.1; -; Genomic_DNA. DR RefSeq; WP_038659357.1; NZ_CP009571.1. DR EnsemblBacteria; AIT05548; AIT05548; MC45_03050. DR KEGG; stax:MC45_03050; -. DR KO; K03665; -. DR Proteomes; UP000033200; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000033200}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000033200}. FT DOMAIN 208 377 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 428 AA; 47269 MW; 6D5B6C8685F2BB3A CRC64; MTNGFNRDRD DFARGGRTLI VLPDQGDAHR DADARLDETA GLAAAIGLVV TEKVAVRVRA PKAATLIGSG QVEQLAVQVR QNEADLVVFD ASLTPVQQRN LETALEAKVI DRTGLILEIF GERAATAEGR LQVELAHLDY QAGRLVRSWT HLERQRGGFG FLGGPGETQI EADRRLIRDR MARLRRELEQ VSRTRGLHRD RRQRAPWPII ALVGYTNAGK STLFNRLTGA HVMAEDLLFA TLDPTLRQIS LPGIDKAILS DTVGFVSDLP TQLVAAFQAT LEEVVSADLL IHVRDIAHPE SEAQRSDVEA VLAEIGVSEL TPRFEAWNKL DLLDPERHED VLVEAGHRDD VVAISALSGE GIDDLIEQVA AKLTAGHRRY WITLDAGDGA GAAWLHAHGE VLGQISEDLQ TQYEVRLAER DYERFLQR // ID A0A097IGP1_9CORY Unreviewed; 505 AA. AC A0A097IGP1; DT 07-JAN-2015, integrated into UniProtKB/TrEMBL. DT 07-JAN-2015, sequence version 1. DT 07-JUN-2017, entry version 18. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=CDOO_08495 {ECO:0000313|EMBL:AIT61290.1}; OS Corynebacterium doosanense CAU 212 = DSM 45436. OC Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae; OC Corynebacterium. OX NCBI_TaxID=558173 {ECO:0000313|EMBL:AIT61290.1, ECO:0000313|Proteomes:UP000029914}; RN [1] {ECO:0000313|EMBL:AIT61290.1, ECO:0000313|Proteomes:UP000029914} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CAU 212 {ECO:0000313|EMBL:AIT61290.1, RC ECO:0000313|Proteomes:UP000029914}; RA Schaffert L., Albersmeier A., Kalinowski J., Ruckert C.; RT "Complete genome sequence of Corynebacterium doosanense CAU 212(T) RT (=DSM 45436(T)), isolated from activated sludge."; RL Submitted (SEP-2013) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP006764; AIT61290.1; -; Genomic_DNA. DR RefSeq; WP_018021054.1; NZ_CP006764.1. DR EnsemblBacteria; AIT61290; AIT61290; CDOO_08495. DR KEGG; cdo:CDOO_08495; -. DR KO; K03665; -. DR Proteomes; UP000029914; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000029914}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000029914}. FT DOMAIN 281 452 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 240 267 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 505 AA; 55695 MW; BF123FE685D43C20 CRC64; MTEFPRETTP DHDDLLARAF RENAPQREAE DSGRDLSDLE SPTVGELELA ERNAFRRVTR DTDIRSEDTE DGYEVEYRKL RLEQVILVGV WTEGTTAEVE ANMAELAALA ETAGAEVHDL LYQKRDKPDP GTYIGSGKVD QLKTIVESTG ADTVVFDGEL SPGQLITLED RLKTKVIDRT MLILDIFAQH AKSKEGKAQV SLAQMEYLYT RVRGWGGNLS RQAGGRAGSN GGVGLRGPGE TRIEADRRRL RTDMAKLRKE LSAMKTAREI KRSQRRGSTT PQIAIAGYTN AGKSSLINAM TGAGVLVEDA LFATLDPTTR RAHLPDGRAI VFTDTVGFVR HLPTQLVEAF KSTLEEVLGA DLILHVVDGA DPFPLKQIEA VNKVIYDIVR ESGEDVPPEL IVVNKIDAAD PVTLAELRHT LDRDNVVYVS AATGEGIDEL TARIELFLNS LDAHVEMLVP FTRGDVVSRI HEVGTVLAEK YDEDGTRLDV RLPQRVAQEL DEFVV // ID A0A097QYC0_HAFAL Unreviewed; 426 AA. AC A0A097QYC0; DT 07-JAN-2015, integrated into UniProtKB/TrEMBL. DT 07-JAN-2015, sequence version 1. DT 30-AUG-2017, entry version 18. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=AT03_03195 {ECO:0000313|EMBL:AIU71491.1}; OS Hafnia alvei FB1. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; OC Hafniaceae; Hafnia. OX NCBI_TaxID=1453496 {ECO:0000313|EMBL:AIU71491.1, ECO:0000313|Proteomes:UP000029986}; RN [1] {ECO:0000313|EMBL:AIU71491.1, ECO:0000313|Proteomes:UP000029986} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=FB1 {ECO:0000313|EMBL:AIU71491.1, RC ECO:0000313|Proteomes:UP000029986}; RX PubMed=25075225; DOI=10.1186/1757-4749-6-29; RA Tan J.Y., Yin W.F., Chan K.G.; RT "Gene clusters of Hafnia alvei strain FB1 important in survival and RT pathogenesis: a draft genome perspective."; RL Gut Pathog 6:29-29(2014). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP009706; AIU71491.1; -; Genomic_DNA. DR RefSeq; WP_025798761.1; NZ_CP009706.1. DR EnsemblBacteria; AIU71491; AIU71491; AT03_03195. DR KEGG; hav:AT03_03195; -. DR PATRIC; fig|1453496.5.peg.631; -. DR KO; K03665; -. DR Proteomes; UP000029986; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000029986}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000029986}. FT DOMAIN 198 365 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 426 AA; 48254 MW; 6A5CA650BCEB78BE CRC64; MFDRYEAGEQ AVLVHVYFSQ ERDIEDLREF ESLVSSAGVE ALRVVTGSRK APHPKYFVGE GKAEEIAQAV QETGASVVLF DHALSAAQER NLEKLCQCRV IDRTGLILDI FAQRARTHEG KLQVELAQLR HLATRLVRGW THLERQKGGI GLRGPGETQL ETDRRLLRDR ISLILSRLER VEKQRDQGRR ARSRADVPTV SLVGYTNAGK STLFNHITKA DVYAADQLFA TLDPTLRRID VVDVGTTVLA DTVGFIRHLP HDLVAAFKAT LQETRQASLL LHIIDASDAR VDENIDAVNT VLAEIEADEI PVLLVMNKID MLDEFEPRID RNDENLPIRV WVSAQTGVGI DLLFQALTER LSGEIASYEL RLPPEAGRLR SRFYQLQAIE KEWIEEDGSI GLHIRLPIVE WHRLCKREQE LLKYII // ID A0A098BXB1_9PORP Unreviewed; 417 AA. AC A0A098BXB1; DT 07-JAN-2015, integrated into UniProtKB/TrEMBL. DT 07-JAN-2015, sequence version 1. DT 07-JUN-2017, entry version 18. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:CEA14639.1}; GN ORFNames=ING2E5B_0029 {ECO:0000313|EMBL:CEA14639.1}; OS Fermentimonas caenicola. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; OC Porphyromonadaceae; Fermentimonas. OX NCBI_TaxID=1562970 {ECO:0000313|EMBL:CEA14639.1, ECO:0000313|Proteomes:UP000032417}; RN [1] {ECO:0000313|EMBL:CEA14639.1} RP NUCLEOTIDE SEQUENCE. RA Wibberg Daniel; RL Submitted (AUG-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LN515532; CEA14639.1; -; Genomic_DNA. DR RefSeq; WP_045088775.1; NZ_LN515532.1. DR EnsemblBacteria; CEA14639; CEA14639; ING2E5B_0029. DR KEGG; pbt:ING2E5B_0029; -. DR PATRIC; fig|1562970.3.peg.28; -. DR KO; K03665; -. DR Proteomes; UP000032417; Chromosome : chrI. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000032417}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000032417}. FT DOMAIN 206 390 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 174 201 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 417 AA; 48384 MW; 2CFAF06795F116EA CRC64; MKDFITQEIK NENAVLVGLI TQDQNEDKVN EYLDELAFLA ETAGLRPTKR FLQKMNTPNT ATFVGKGKLQ EIGDFIKDED NEVGVVIFDD ELSARQLRNI EKEFKIRIMD RTSLILDIFA MRAQTSHAKA QVELAQYEYL LPRLTRMWTH LERQRGGGGT IMRGPGETQL ETDRRIILDK ISRLKQQLKD IDKQKTVQRK NRGKLVRVAL VGYTNVGKST LMTLLSKSEV FAENKLFATL DTTVRKVTVK NLPFLLTDTV GFIRKLPTHL VESFKSTLDE VREADILLHV VDISHPAFEE QIEVVEKTLF EIDKTEKPTI LVFNKIDAFS HTVKEEDDLT PKKRENYSLE ELEQTWFSKL KENCIFISAK EKKNIDELKE LIYDKVKEIH ITRFPYNDFL YQDYEEDMPD QGDDQAE // ID A0A098EQK9_9BACL Unreviewed; 423 AA. AC A0A098EQK9; DT 07-JAN-2015, integrated into UniProtKB/TrEMBL. DT 07-JAN-2015, sequence version 1. DT 07-JUN-2017, entry version 17. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:CEG24065.1}; GN ORFNames=BN1080_03084 {ECO:0000313|EMBL:CEG24065.1}; OS Planococcus massiliensis. OC Bacteria; Firmicutes; Bacilli; Bacillales; Planococcaceae; OC Planococcus. OX NCBI_TaxID=1499687 {ECO:0000313|EMBL:CEG24065.1, ECO:0000313|Proteomes:UP000043699}; RN [1] {ECO:0000313|EMBL:CEG24065.1, ECO:0000313|Proteomes:UP000043699} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ES2 {ECO:0000313|EMBL:CEG24065.1, RC ECO:0000313|Proteomes:UP000043699}; RA Urmite Genomes Urmite Genomes; RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CCXS01000001; CEG24065.1; -; Genomic_DNA. DR RefSeq; WP_052653289.1; NZ_CCXS01000001.1. DR EnsemblBacteria; CEG24065; CEG24065; BN1080_03084. DR Proteomes; UP000043699; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000043699}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000043699}. FT DOMAIN 200 368 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 159 193 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 423 AA; 48175 MW; 6DC66E623BBFE608 CRC64; MDELHEKAVL VGVQLQKDLH FEYEMEELRN LAEACNVEVM GEVHQNLERI NPSHYVGKGK VDEIKVFYEE TDANLVIFND ELSPSQIRNL EEDLECKVID RTMLILDIFS RRAKTREAQV QVELAQLQYM LPRLVGLRAS LGRQAGSSGG GLANRGAGET KLELDRRKIE EQLSKLHKEL EQIRAQRETQ RKQRKKTGSP VVSLVGYTNA GKSTIMNELL TKSGQQEEKQ VFEKDMLFAT LDTSVRQIRL EDNKNFLLTD TVGFVSKLPH HLVKAFRSTL EEARNADLLL HVVDVSNEEY RHMMNVTHAT LHEVGVEGVP TVYVYNKADL AGVPYPRVNG DSLWISAKEG RGLDELVEMI KQHLFSGHVT CRMVVPFERG DVVAYLNEHA TILDTQYEEE GTLLKVELGK VDYDRFEEFV IGK // ID A0A098EWZ7_9BACI Unreviewed; 425 AA. AC A0A098EWZ7; DT 07-JAN-2015, integrated into UniProtKB/TrEMBL. DT 07-JAN-2015, sequence version 1. DT 12-APR-2017, entry version 16. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=BN1002_01741 {ECO:0000313|EMBL:CEG26889.1}; OS Bacillus sp. B-jedd. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus. OX NCBI_TaxID=1476857 {ECO:0000313|EMBL:CEG26889.1, ECO:0000313|Proteomes:UP000042335}; RN [1] {ECO:0000313|EMBL:CEG26889.1, ECO:0000313|Proteomes:UP000042335} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=B-jedd {ECO:0000313|EMBL:CEG26889.1, RC ECO:0000313|Proteomes:UP000042335}; RA Urmite Genomes Urmite Genomes; RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CCXR01000001; CEG26889.1; -; Genomic_DNA. DR EnsemblBacteria; CEG26889; CEG26889; BN1002_01741. DR Proteomes; UP000042335; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000042335}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000042335}. FT DOMAIN 206 368 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 425 AA; 48585 MW; 98FAA6739D454052 CRC64; MKEVFHLEAK TIKEKAILVG CQTTEHDDLR FQYSMEELVS LTETAQGEVL ISVVQKRERI HPATYIGKGK VEELKALVDE LEADIVIFND ELSPSQKRNL GGDLDARIID RTQLILDIFA QRARSKEGKL QVELAQLQYI LPRLAGQGVE LSRLGGGIGT RGPGETKLES DRRHIRRRID EIKQQLAIIV QHRDRYRERR KKNKAFQIAI AGYTNAGKST LFNRLSEADS YEENQLFATL DPMTRKMILP SGFASLITDT VGFIQDLPTS LIAAFRSTLE EVREADLILH VVDMSNPDYF HHEKTVQRLL EELEVKEIPQ LTVYNKRDIK HPDFVPTADT PTAFISAFEK EDRDALKKKI EEMAIAMMEP YKVLIPANEG KLLSQLKNET ILRELSFQEQ EQVYRCKGYA PRDHQVAGQL QKFTV // ID A0A098G0L3_9GAMM Unreviewed; 420 AA. AC A0A098G0L3; DT 07-JAN-2015, integrated into UniProtKB/TrEMBL. DT 07-JAN-2015, sequence version 1. DT 30-AUG-2017, entry version 17. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:CEG55501.1}; GN ORFNames=LFA_0014 {ECO:0000313|EMBL:CEG55501.1}; OS Legionella fallonii LLAP-10. OC Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales; OC Legionellaceae; Legionella. OX NCBI_TaxID=1212491 {ECO:0000313|EMBL:CEG55501.1, ECO:0000313|Proteomes:UP000032430}; RN [1] {ECO:0000313|EMBL:CEG55501.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=LLAP-10 {ECO:0000313|EMBL:CEG55501.1}; RA GOMEZ-VALERO Laura; RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LN614827; CEG55501.1; -; Genomic_DNA. DR RefSeq; WP_045094379.1; NZ_LN614827.1. DR EnsemblBacteria; CEG55501; CEG55501; LFA_0014. DR KEGG; lfa:LFA_0014; -. DR KO; K03665; -. DR Proteomes; UP000032430; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000032430}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000032430}. FT DOMAIN 198 363 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 420 AA; 47047 MW; C227520DE3BB1C73 CRC64; MFERPQGGER AILVQLAVPG IDADEALTEF EELALSANAE VLDCVLGTRA TPDAKYYVGK GKAEEISQLV KAHNAELVLV NHELSPSQER NLERLFECRV VDRSGLILDI FAQRARTFEG KLQVELAQLQ HLSTRLIRGW THLERQKGGI GLRGPGETQL ETDRRLLRDR IRAINKRLEK VRSSRDQNRQ SRRKADLSTV SLVGYTNAGK STLFNSLTGE DIYVANQLFA TLDPTMRKLD LPGASAAILA DTVGFIRDLP HHLVEAFRAT LEETQQADLL LHVIDISDPY WRDMVLAVQK VLEELGVRDI PVIQVFNKID LQEGWQPKVD YTEGACKVWI SAASGLGLDL LKEAIAAQLH GTILTEEVLI KSSQAKLRSQ LYQLGSVLTE SITEEGDWLL KIRITKAQKQ RLFAMEAEQN // ID A0A098GA74_TATMI Unreviewed; 428 AA. AC A0A098GA74; DT 07-JAN-2015, integrated into UniProtKB/TrEMBL. DT 07-JAN-2015, sequence version 1. DT 07-JUN-2017, entry version 19. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:CEG59384.1}; GN ORFNames=LMI_0009 {ECO:0000313|EMBL:CEG59384.1}; OS Tatlockia micdadei (Legionella micdadei). OC Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales; OC Legionellaceae; Tatlockia. OX NCBI_TaxID=451 {ECO:0000313|EMBL:CEG59384.1, ECO:0000313|Proteomes:UP000032414}; RN [1] {ECO:0000313|EMBL:CEG59384.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC33218 {ECO:0000313|EMBL:CEG59384.1}; RA GOMEZ-VALERO Laura; RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LN614830; CEG59384.1; -; Genomic_DNA. DR EnsemblBacteria; CEG59384; CEG59384; LMI_0009. DR KEGG; tmc:LMI_0009; -. DR PATRIC; fig|451.8.peg.982; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR Proteomes; UP000032414; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000032414}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000032414}. FT DOMAIN 203 368 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 428 AA; 48024 MW; 7DA0397F9BBA5DDD CRC64; MENAVLFERP QSGERAILVQ LALPGVDAEK ALAEFKELAL SAQAEIVACV LGARATPEAK YYVGSGKAEE IQQLVSAHNA ELVLVNHELS PSQERNLEKL LQCRVVDRSG LILDIFAQRA RTFEGKLQVE LAQLQHISTR LIRGWTHLER QKGGIGLRGP GETQLETDRR LVRERIKSIN KRLEKVRRSR DQNRRARQKA ALPTVSLVGY TNAGKSTLFN ALTGEQIYVA DQLFATLDPT MRKIELPGAA AAILVDTVGF IRDLPHQLIE AFRATLEETK EADLLLHVID IADPHWREMA FSVQRVLTEI GVTDVPTIQV FNKIDLQEGW CPKIDCQEDT CKVWVSAKSN AGLDLLREAI VTQLQGKINV EEVFIKPSEA KLRAKLYQLD AVIEETPADE GGWHLKIKLT EVQRKRLFAE EKTESKEI // ID A0A098LL22_9BACT Unreviewed; 403 AA. AC A0A098LL22; DT 07-JAN-2015, integrated into UniProtKB/TrEMBL. DT 07-JAN-2015, sequence version 1. DT 12-APR-2017, entry version 16. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=MYP_4317 {ECO:0000313|EMBL:GAL87087.1}; OS Sporocytophaga myxococcoides. OC Bacteria; Bacteroidetes; Cytophagia; Cytophagales; Cytophagaceae; OC Sporocytophaga. OX NCBI_TaxID=153721 {ECO:0000313|EMBL:GAL87087.1, ECO:0000313|Proteomes:UP000030185}; RN [1] {ECO:0000313|EMBL:GAL87087.1, ECO:0000313|Proteomes:UP000030185} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=PG-01 {ECO:0000313|EMBL:GAL87087.1, RC ECO:0000313|Proteomes:UP000030185}; RA Liu L., Gao P.J., Chen G.J., Wang L.S.; RT "Sporocytophaga myxococcoides PG-01 genome sequencing."; RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:GAL87087.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BBLT01000011; GAL87087.1; -; Genomic_DNA. DR EnsemblBacteria; GAL87087; GAL87087; MYP_4317. DR Proteomes; UP000030185; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000030185}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000030185}. FT DOMAIN 205 393 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 403 AA; 46175 MW; D1EF985FB2C5010E CRC64; MKTNTGQETK KAVETAILVA LIHKRQPQDR AKEYLEELAF LASTAGVETL AWFTQKVDHP DRRTFIGKGK LEEIQAYVTA HSVNRVIFDD DLSPSQLKNL ENELKVRIYD RSLLILEIFM NRAQTAQART QVELARYQYL LPRLTRMWTH LERQRGGTGT RGGSGEKEIE TDKRVIRDQI TLLKEKLKKI DMQNATQRKS RTDIVRVALV GYTNVGKSTL MNLLSKSDVF AENKLFATVD ATVRKINYLN IPYLLSDTVG FIRKLPTTLI ESFKSTLDEV READILIHVV DISHPSFEEH IEVVNATLAD IKAADKPVIL VFNKIDQYHP EVEQSELDGE KISEAEVIKA SLEQLKSSYL NKNQFATVFI SATQRENIDE LREIIGQKVK EKHLMIYPNY LIY // ID A0A098LLN3_9FLAO Unreviewed; 404 AA. AC A0A098LLN3; DT 07-JAN-2015, integrated into UniProtKB/TrEMBL. DT 07-JAN-2015, sequence version 1. DT 07-JUN-2017, entry version 20. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=JCM19538_2253 {ECO:0000313|EMBL:GAL87890.1}; OS Jejuia pallidilutea. OC Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales; OC Flavobacteriaceae; Jejuia. OX NCBI_TaxID=504487 {ECO:0000313|EMBL:GAL87890.1, ECO:0000313|Proteomes:UP000030184}; RN [1] {ECO:0000313|EMBL:GAL87890.1, ECO:0000313|Proteomes:UP000030184} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=JCM 19538 {ECO:0000313|EMBL:GAL87890.1, RC ECO:0000313|Proteomes:UP000030184}; RA Takatani N., Nakanishi M., Meirelles P., Mino S., Suda W., Oshima K., RA Hattori M., Ohkuma M., Hosokawa M., Miyashita K., Thompson F.L., RA Niwa A., Sawabe T., Sawabe T.; RT "Draft Genome Sequence of Marine Flavobacterium Jejuia pallidilutea RT Strain 11shimoA1 and Pigmentation Mutants."; RL Genome Announc. 2:e01236-14(2014). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:GAL87890.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BBNY01000001; GAL87890.1; -; Genomic_DNA. DR RefSeq; WP_045370914.1; NZ_BBNY01000001.1. DR EnsemblBacteria; GAL87890; GAL87890; JCM19538_2253. DR Proteomes; UP000030184; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000030184}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000030184}. FT DOMAIN 200 385 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 404 AA; 46753 MW; 63A5B9915A897E6C CRC64; MIEKKDVDLE KAVLVGIITK DQDEEKLKEY LDELEFLTFT AGGYAIKRFT QKMDMPNPKT FIGSGKMEEV KHFVDENDIS TAIFDDELSA TQERNISKIL GCKVLDRTNL ILDIFAQRAQ TSYARTQVEL AQYEYLLPRL RGMWTHLERQ RGGIGMRGPG ETEIETDRRI VRDKIALLKD RIKTIDKQMA VQRGNRGKLV RVALVGYTNV GKSTLMNVIS KSDVFAENKL FATLDTTVRK VVIQNLPFLL SDTVGFIRKL PTQLVESFKS TLDEVREADL LLHVVDISHP NFEEHIASVN KILGEIESSD KPTIMVFNKI DAYEPEPFEE DELDEERTKK HYTLEEWKST WMSKIGNNAL FISAINKSNI DDFKKRVYDE VREIHVTRFP YNSFLYPDYN YEER // ID A0A098MDX0_9BACL Unreviewed; 421 AA. AC A0A098MDX0; DT 07-JAN-2015, integrated into UniProtKB/TrEMBL. DT 07-JAN-2015, sequence version 1. DT 07-JUN-2017, entry version 18. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=PWYN_10715 {ECO:0000313|EMBL:KGE19757.1}; OS Paenibacillus wynnii. OC Bacteria; Firmicutes; Bacilli; Bacillales; Paenibacillaceae; OC Paenibacillus. OX NCBI_TaxID=268407 {ECO:0000313|EMBL:KGE19757.1, ECO:0000313|Proteomes:UP000029734}; RN [1] {ECO:0000313|EMBL:KGE19757.1, ECO:0000313|Proteomes:UP000029734} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 18334 {ECO:0000313|EMBL:KGE19757.1, RC ECO:0000313|Proteomes:UP000029734}; RA den Bakker H.C.; RL Submitted (AUG-2014) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:KGE19757.1, ECO:0000313|Proteomes:UP000029734} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 18334 {ECO:0000313|EMBL:KGE19757.1, RC ECO:0000313|Proteomes:UP000029734}; RA Tsai Y.-C., Martin N., Korlach J., Wiedmann M.; RT "Comparative genomics of the Paenibacillus odorifer group."; RL Submitted (OCT-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KGE19757.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JQCR01000002; KGE19757.1; -; Genomic_DNA. DR RefSeq; WP_036651103.1; NZ_JQCR01000002.1. DR EnsemblBacteria; KGE19757; KGE19757; PWYN_10715. DR Proteomes; UP000029734; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000029734}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000029734}. FT DOMAIN 198 366 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 421 AA; 47599 MW; 92DFF82B31D9B67A CRC64; MESIQQKAVI VGVQLQNDTN FAYSMEELRN LAAACDLRIA GELSQKASRV NPSHYIGTGK IQELSALLEA EDAPIVIFND ELTPSQIRNL ESALDRQVID RTILILNIFA ERAKTKEAQL QVEVAQLQYM LPRLTGLRES LGRQGGGAGL KNKGAGETKL ELDRRRIEER ITALQVELQH QVSRRQIQRK QRRKNEVPVV CLVGYTNTGK SSLMNVMVET YHPGSHKQVF AKDMLFATLE TSVRSIMLPD HKTFLLTDTV GFVSQLPHHL VKAFRSTLEE VTEADLLIHV VDYADSEYKQ HMAVTDETLK ALGADQIPTI YAYNKADLTE QPYPLIQGDS VYLSAKEKSG AEELTQMIRS HVFNDYIQCE ILVPFDRGAV VSYFNEHAHV QSASYEEEGT RLTLECRVAD YERFRNDFIE I // ID A0A098R1X5_9SPIO Unreviewed; 425 AA. AC A0A098R1X5; DT 07-JAN-2015, integrated into UniProtKB/TrEMBL. DT 07-JAN-2015, sequence version 1. DT 07-JUN-2017, entry version 18. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=DC28_01540 {ECO:0000313|EMBL:KGE73668.1}; OS Spirochaeta lutea. OC Bacteria; Spirochaetes; Spirochaetales; Spirochaetaceae; Spirochaeta. OX NCBI_TaxID=1480694 {ECO:0000313|EMBL:KGE73668.1, ECO:0000313|Proteomes:UP000029692}; RN [1] {ECO:0000313|EMBL:KGE73668.1, ECO:0000313|Proteomes:UP000029692} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=JC230 {ECO:0000313|EMBL:KGE73668.1, RC ECO:0000313|Proteomes:UP000029692}; RA Shivani Y., Subhash Y., Tushar L., Sasikala C., Ramana C.V.; RT "De novo Genome Sequence of Spirocheata sp."; RL Submitted (MAY-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KGE73668.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JNUP01000004; KGE73668.1; -; Genomic_DNA. DR RefSeq; WP_037545200.1; NZ_JNUP01000004.1. DR EnsemblBacteria; KGE73668; KGE73668; DC28_01540. DR Proteomes; UP000029692; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000029692}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000029692}. FT DOMAIN 203 367 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 169 196 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 425 AA; 47039 MW; 5BE8C32983F0795E CRC64; MIEHTTLEPD RAFLVGIQDP GENPGQAKAH LEELIRLTET MGAQAVANLT AKISDPNPKL ILGTGKADEI IQAAEEAEAD ILIIDSDLSP SQQRNWERLS GLPVLDRQLV ILEIFAQRAQ TKEARLQVDL ARYEYALPRL TRAWTHLGRQ RGGTRGTRGE GEKQIEADRR IIEARIAKIK QDLQQVQKQR ATLRKGRESV PVPTAALVGY TNAGKSSLLK TLTQAEILVE DKLFATLDPT TRRFELGDGL AMLLTDTVGF IRKLPHGLVD AFRSTLEETT RADLLIHLAD ASNPEVIPHL TTTETVLQEI GATAPRLLVF NKIDAAPEAT LTALQSAYPE AVCISAITGQ GLDLLAQELK DFLRGRFQRF CVLLPFARED LVALAHRSGV VEEKKYQESG IHLQGTIPER LVSHFEPYKI SQDVI // ID A0A098RCU2_9GAMM Unreviewed; 438 AA. AC A0A098RCU2; DT 07-JAN-2015, integrated into UniProtKB/TrEMBL. DT 07-JAN-2015, sequence version 1. DT 30-AUG-2017, entry version 18. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=FP66_10555 {ECO:0000313|EMBL:KGE77373.1}; OS Halomonas salina. OC Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales; OC Halomonadaceae; Halomonas. OX NCBI_TaxID=42565 {ECO:0000313|EMBL:KGE77373.1, ECO:0000313|Proteomes:UP000029721}; RN [1] {ECO:0000313|EMBL:KGE77373.1, ECO:0000313|Proteomes:UP000029721} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CIFRI 1 {ECO:0000313|EMBL:KGE77373.1, RC ECO:0000313|Proteomes:UP000029721}; RA Behera B.D., Meena D.K., Das P., Maharana J., Paria P., Sharma A.P., RA Shamsudheen K.V., Rijit J., Dixit V., Verma A., Scaria V., RA Sivasubbu S.; RT "Draft genome sequence of an extremely salt tolerant bacteria RT Halomonas salina/CIFRI 1."; RL Submitted (JUN-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KGE77373.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JOKD01000041; KGE77373.1; -; Genomic_DNA. DR RefSeq; WP_035598046.1; NZ_JOKD01000041.1. DR EnsemblBacteria; KGE77373; KGE77373; FP66_10555. DR Proteomes; UP000029721; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000029721}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000029721}. FT DOMAIN 199 365 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 438 AA; 49350 MW; 8708B39818D4CCD8 CRC64; MFFERPDAGE TAVLVHVDFQ DEQEREDPGE FLELVRSAGA EPATLLTGSR NRPDPRSFIG SGKVEELREA LQVHKAELVI FNHALSPSQE RNLEQSLKCR VLDRTGLILD IFAQRARTHE GKLQVELAQL EYMSTRLVRG WTHLERQKGG IGLRGPGETQ LETDRRLLRG RIKAIHKRLD KVRSQRDQNR RARSRAEVPS VSLVGYTNAG KSTLFNAVTA SQVYAADQLF ATLDPTLRRL EIEDVGPVVL ADTVGFIRHL PHKLVEAFQA TLQEAAEASL LVHVIDAADA DRDLNVSQVE EVLDEIGALD VPTLKVMNKI DMFDSAPRIE RGADGMPETV WLSARDGKGL ELFEQALSEC LADDIIDFDV TLEPHQGKLR AGLHELGAVR EERFDEMGRT QLEIRLPRRD FLQLMARLGE RADDYLPEAL QDRPLWEQ // ID A0A098S6Z9_9BACT Unreviewed; 404 AA. AC A0A098S6Z9; DT 07-JAN-2015, integrated into UniProtKB/TrEMBL. DT 07-JAN-2015, sequence version 1. DT 07-JUN-2017, entry version 21. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=IX84_12100 {ECO:0000313|EMBL:KGE87866.1}; OS Phaeodactylibacter xiamenensis. OC Bacteria; Bacteroidetes; Saprospiria; Saprospirales; OC Haliscomenobacteraceae; Phaeodactylibacter. OX NCBI_TaxID=1524460 {ECO:0000313|EMBL:KGE87866.1, ECO:0000313|Proteomes:UP000029736}; RN [1] {ECO:0000313|EMBL:KGE87866.1, ECO:0000313|Proteomes:UP000029736} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=KD52 {ECO:0000313|EMBL:KGE87866.1, RC ECO:0000313|Proteomes:UP000029736}; RX PubMed=25052393; DOI=10.1099/ijs.0.063909-0; RA Chen Z.Jr., Lei X., Lai Q., Li Y., Zhang B., Zhang J., Zhang H., RA Yang L., Zheng W., Tian Y., Yu Z., Xu H.Jr., Zheng T.; RT "Phaeodactylibacter xiamenensis gen. nov., sp. nov., a member of the RT family Saprospiraceae isolated from the marine alga Phaeodactylum RT tricornutum."; RL Int. J. Syst. Evol. Microbiol. 64:3496-3502(2014). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KGE87866.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JPOS01000029; KGE87866.1; -; Genomic_DNA. DR RefSeq; WP_044220418.1; NZ_JPOS01000029.1. DR EnsemblBacteria; KGE87866; KGE87866; IX84_12100. DR Proteomes; UP000029736; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000029736}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000029736}. FT DOMAIN 211 393 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 179 206 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 404 AA; 47037 MW; B969A7D186389F59 CRC64; MAHDWTIGTK DKKGLKQNKE YAILVGVVRQ LQTEEEVEEY LDELEFLALT AGAKTRKRYI QKLSQPDKRT FVGKGKLEEI KEYIDAHEEV SMVIFDDDLS GKQVNILEEF LKLKIVDRST LILDIFASRA QTAQAKTQVE LAQLQYLLPR LRGLWTHLER QRGGIGMRGP GEKEIETDRR IVRDKISLLK KKLEKIDQQN QTQRKQRGEM IRVALVGYTN VGKSTLMNLL SKSEVFAENK LFATLDTTVR KVVIDRMPFL LSDTVGFIRK LPHHLVESFK STLDEVRESD ILLHVVDVAH PLHEDHIRTV NSTLKDLQAV DKPTLLVFNK IDLYRERNYD DLLTEEGKRE IEEGLLGNLR YMFDQECMFV SAATGEHIDE LRKKLQQMVH EQYMIRYPYR AKQW // ID A0A098SU77_9PSED Unreviewed; 433 AA. AC A0A098SU77; DT 07-JAN-2015, integrated into UniProtKB/TrEMBL. DT 07-JAN-2015, sequence version 1. DT 30-AUG-2017, entry version 19. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=LT42_18270 {ECO:0000313|EMBL:KGF63830.1}; OS Pseudomonas lutea. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=243924 {ECO:0000313|EMBL:KGF63830.1, ECO:0000313|Proteomes:UP000029719}; RN [1] {ECO:0000313|EMBL:KGF63830.1, ECO:0000313|Proteomes:UP000029719} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 17257 {ECO:0000313|EMBL:KGF63830.1, RC ECO:0000313|Proteomes:UP000029719}; RA Kwak Y., Shin J.-H.; RT "Genome sequence of Pseudomonas lutea strain DSM 17257T."; RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KGF63830.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JRMB01000002; KGF63830.1; -; Genomic_DNA. DR RefSeq; WP_037015730.1; NZ_JRMB01000002.1. DR EnsemblBacteria; KGF63830; KGF63830; LT42_18270. DR Proteomes; UP000029719; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000029719}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000029719}. FT DOMAIN 199 366 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 433 AA; 49052 MW; 530933C752DBB2F6 CRC64; MFFERHSGGE RAILVHLDGQ DPEAREDPQE FRELALSAGA DIVSFVNVPR HRPTAKYLVG SGKVEELRDL VKTEKSDIVI FNHVLTPSQE RNLERVFECR VLDRTGLILD IFAQRARTHE GKLQVELAQL EHMSTRLVRG WTHLERQGGG IGLRGPGETQ LETDRRLLRV RLRQIKGRLE KVRSQRDQAR RGRSRADIPT VSIVGYTNAG KSTLFNAVTD SDVYAADQLF ATLDPTLRRL EINDLGPIVL ADTVGFIRHL PHKLVEAFRA TLEESSNSDL LLHVIDSHEP ERLEQIEQVM VVLGEIGAQD LPMLEVYNKL DLLEGVEPQI QRDADGKPQR VWVSARDGRG LDLLKQAIAE VLGNDLFVGT LRLTQQFARL RAQFFKLGAV QSEEHDEEGQ SLLAVRLPRV EFNRLVSREG LQPLEFIEQH TLQ // ID A0A098T4C0_9RHIZ Unreviewed; 450 AA. AC A0A098T4C0; DT 07-JAN-2015, integrated into UniProtKB/TrEMBL. DT 07-JAN-2015, sequence version 1. DT 30-AUG-2017, entry version 20. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=LL06_24850 {ECO:0000313|EMBL:KGF66992.1}; OS Hoeflea sp. BAL378. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Phyllobacteriaceae; Hoeflea. OX NCBI_TaxID=1547437 {ECO:0000313|EMBL:KGF66992.1, ECO:0000313|Proteomes:UP000029706}; RN [1] {ECO:0000313|EMBL:KGF66992.1, ECO:0000313|Proteomes:UP000029706} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BAL378 {ECO:0000313|EMBL:KGF66992.1, RC ECO:0000313|Proteomes:UP000029706}; RA Bentzon-Tilia M., Riemann L., Gram L.; RT "Draft genome sequence of Hoeflea sp. BAL378, a potential producer of RT bioactive compounds."; RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KGF66992.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JRJG01000173; KGF66992.1; -; Genomic_DNA. DR EnsemblBacteria; KGF66992; KGF66992; LL06_24850. DR Proteomes; UP000029706; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000029706}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000029706}. FT DOMAIN 216 387 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 175 209 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 450 AA; 49246 MW; 368A0C074D628228 CRC64; MDADGKSGVT RAIVLIPALR TRNAAPGTAA DGGDVVKRPD AHRMGEAIGL AGAIDLKVAE ALIVPISAPR PSTLFGKGKM LEILALIEST GAELVIVDHP LTPVQQRNLE TEWKVKVIDR TGLILEIFGR RASTKEGVLQ VELAHLNYQK GRLVRSWTHL ERQRGGGGFM GGPGETQIEA DRRLLQERII KLERELEQVR RTRQLHRAKR KKVPHPIVAL VGYTNAGKST LFNRLTGSEV LAEDMLFATL DPTLRRMKLP HGATVILSDT VGFISNLPTH LVAAFRATLE EVIEADLILH VRDMSDPDRK SQAADVEAIL KSLGVGEGDG RKLIEVWNKI DLLDAEAAED LKLRAEKSDN AIALSSVTGE GVDTLLSVIE ARISGELATR TVTLTTRQLP IMSWIYDRGR VKSRIDHEDG SVEIIAEFTA SDSLDLDRQL GLGPKPDTDY // ID A0A098TLE8_9CYAN Unreviewed; 583 AA. AC A0A098TLE8; DT 07-JAN-2015, integrated into UniProtKB/TrEMBL. DT 07-JAN-2015, sequence version 1. DT 07-JUN-2017, entry version 19. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=DO97_06720 {ECO:0000313|EMBL:KGF72702.1}; OS Neosynechococcus sphagnicola sy1. OC Bacteria; Cyanobacteria; Synechococcales; Leptolyngbyaceae; OC Neosynechococcus. OX NCBI_TaxID=1497020 {ECO:0000313|EMBL:KGF72702.1, ECO:0000313|Proteomes:UP000030170}; RN [1] {ECO:0000313|EMBL:KGF72702.1, ECO:0000313|Proteomes:UP000030170} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CAUP A 1101 {ECO:0000313|EMBL:KGF72702.1, RC ECO:0000313|Proteomes:UP000030170}; RA Dvorak P., Casamatta D., Hasler P., Poulickova A., Ondrej V., RA Sanges R.; RT "Evolution of Synechococcus."; RL Mol. Ecol. 0:0-0(2014). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KGF72702.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JJML01000020; KGF72702.1; -; Genomic_DNA. DR RefSeq; WP_052128613.1; NZ_JJML01000020.1. DR EnsemblBacteria; KGF72702; KGF72702; DO97_06720. DR Proteomes; UP000030170; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000030170}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000030170}. FT DOMAIN 410 580 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 369 403 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 583 AA; 64648 MW; 889CF5B4957F723A CRC64; MGTPFRCARI EAVIETIYGN LQGLKASQLR QLQRLYHQRL PGDRLTTSEV AQRVAAISTD IDQPICVYVN RRGQVIRVGV GTVRQTQIPP LELPRYGAER LSGIRCLATQ FTEEPPGEAV LTAMALQRLD ALVTLVLSGQ GFERRGGGAS GYVTATYLAH LQPESGEPGA ERSPGTWLVS PLRSLEDVCQ EDFLDWVEGL ETAFRREFVA RQVDTDQDRV LLVGLKTDQM EMQRFQDGLA ELERLVDTAG GEVLQTLRQR RPRPHPQTVV GTGKVEEIAL AAQTVGANLV VFDRGLSPAQ VRNLEMQLGV RVIDRTELIL DIFAQRAQSG AGKLQVELAQ LEYRLPRLTG RGQAMSRLGG GIGTRGPGET KLESDRRAIQ RRIAHLQQEV NHLQAHRARM RQQRQHQQVP SVALVGYTNA GKSTLLNVLT QAEVYTADQL FATLDPTTRR FIVTDPMTRK PLTVLLTDTV GFIHELPAAL VDAFRATLEE VSEADALLHV VDLSHPAWLS QIRSVMQILS EMPITPGPAL IVFNKIDQVD GDNLSLAQEE YPQGVFISAS DRLGLETLRQ RLIQLVQYVT QDN // ID A0A098U226_9BURK Unreviewed; 378 AA. AC A0A098U226; DT 07-JAN-2015, integrated into UniProtKB/TrEMBL. DT 07-JAN-2015, sequence version 1. DT 07-JUN-2017, entry version 17. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=IA69_29630 {ECO:0000313|EMBL:KGF78559.1}; OS Massilia sp. JS1662. OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Oxalobacteraceae; Massilia. OX NCBI_TaxID=1519190 {ECO:0000313|EMBL:KGF78559.1, ECO:0000313|Proteomes:UP000029701}; RN [1] {ECO:0000313|EMBL:KGF78559.1, ECO:0000313|Proteomes:UP000029701} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=JS1662 {ECO:0000313|EMBL:KGF78559.1, RC ECO:0000313|Proteomes:UP000029701}; RA Fida T.T., Spain J.C.; RT "Identification of Arachidin-3 degrading bacteria in the peanut RT rhizosphere."; RL Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KGF78559.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JPQD01000055; KGF78559.1; -; Genomic_DNA. DR RefSeq; WP_036240093.1; NZ_JPQD01000055.1. DR EnsemblBacteria; KGF78559; KGF78559; IA69_29630. DR Proteomes; UP000029701; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000029701}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000029701}. FT DOMAIN 190 356 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 378 AA; 41497 MW; A257900B32256790 CRC64; MRAALVGIDF NAGDFKASLE ELALLARSAG AEPISTITAK RNSPDPAYFV GSGKADEIAQ AVLADKVEIV IFNHALSPAQ QRNLERRLNV RVVDRTSLIL DIFAQRAQSH EGKLQVELAQ LQHLATRLIR GWTHLERQKG GIGLRGPGET QLETDRRLIG ERVKMLRTRL TKLRKQHETQ RRSRGRNQTF SVSLVGYTNA GKSTLFNTLT KAGVYVANQL FATLDTTSRR LYLGPDTGNV VVSDTVGFVR ELPHQLVAAF RATLEETIHA DLLLHVVDGA SPVRMEQIEQ VNEVLREIGA DHIPQILVWN KIDAAGLEPE IERDEYGKIS RVFISARSGA GLDLLRDAIV EAAGSPAVVP GVDEHADLMP ATPHPGPH // ID A0A098YBQ8_9ACTN Unreviewed; 514 AA. AC A0A098YBQ8; DT 07-JAN-2015, integrated into UniProtKB/TrEMBL. DT 07-JAN-2015, sequence version 1. DT 12-APR-2017, entry version 16. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=IN07_05350 {ECO:0000313|EMBL:KGH47934.1}; OS Modestobacter caceresii. OC Bacteria; Actinobacteria; Geodermatophilales; Geodermatophilaceae; OC Modestobacter. OX NCBI_TaxID=1522368 {ECO:0000313|EMBL:KGH47934.1, ECO:0000313|Proteomes:UP000029713}; RN [1] {ECO:0000313|EMBL:KGH47934.1, ECO:0000313|Proteomes:UP000029713} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=KNN45-2b {ECO:0000313|EMBL:KGH47934.1, RC ECO:0000313|Proteomes:UP000029713}; RA Bukarasam K., Bull A., Girard G., van Wezel G., Goodfellow M.; RT "Biosystematic studies on Modestobacter strains isolated from extreme RT hyper-arid desert soil and from historic building."; RL Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KGH47934.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JPMX01000015; KGH47934.1; -; Genomic_DNA. DR EnsemblBacteria; KGH47934; KGH47934; IN07_05350. DR Proteomes; UP000029713; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000313|EMBL:KGH47934.1}; KW Complete proteome {ECO:0000313|Proteomes:UP000029713}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900, KW ECO:0000313|EMBL:KGH47934.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000029713}. FT DOMAIN 291 456 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 514 AA; 55282 MW; B3CABC4B703521AE CRC64; MTSRSPHEQG RATLETMTTA QNRAILDQAE ARADKARASM PDTKPAPAGQ WDADDETTGS YVKEERGALR RVAGLGTELT DVTEVEYRQL RLERVVLVGV WTEGTAADAQ RSLTELAALA ETAGSQVLDA LMQRRDKPDP ATYVGSGKAA ELREVVAATG ADTVICDGEL APGQLNQLEK VLKVKVVDRT ALILDIFAQH ATSREGKAQV ELAQMQYMLP RLRGWGESLS RQAGGRVAGG GGIGTRGPGE TKIETDRRRI RSRVSKLRKE IAGMATARTT QRNSRDRNAT PSVAIAGYTN AGKSSLLNQL TGAGVLVQDA LFATLDPTVR RAQTPEGREY TMTDTVGFVR HLPHQLVDAF RSTLEEVADA DLLVHVVDGS DSDPLGQIDA VHTVLNEIDA SAVPELIVVN KVDAMTEEDM LALRQALPGA MWVSARTGEG IEALRDVIAQ RLPHPHIDVE VLVPYDRGDL VARVHRDGEV VEEAHEAAGT RLTARVDAGL AAQLDGFAAP ATED // ID A0A099BUP1_9BACT Unreviewed; 416 AA. AC A0A099BUP1; DT 07-JAN-2015, integrated into UniProtKB/TrEMBL. DT 07-JAN-2015, sequence version 1. DT 07-JUN-2017, entry version 18. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=HMPREF0671_08490 {ECO:0000313|EMBL:KGI60001.1}; OS Prevotella sp. S7 MS 2. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Prevotellaceae; OC Prevotella. OX NCBI_TaxID=1287488 {ECO:0000313|EMBL:KGI60001.1, ECO:0000313|Proteomes:UP000029732}; RN [1] {ECO:0000313|EMBL:KGI60001.1, ECO:0000313|Proteomes:UP000029732} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=S7 MS 2 {ECO:0000313|EMBL:KGI60001.1, RC ECO:0000313|Proteomes:UP000029732}; RA McCorrison J., Sanka R., Torralba M., Gillis M., Haft D.H., Methe B., RA Sutton G., Nelson K.E.; RL Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KGI60001.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JRPT01000043; KGI60001.1; -; Genomic_DNA. DR RefSeq; WP_036899295.1; NZ_JRPT01000043.1. DR EnsemblBacteria; KGI60001; KGI60001; HMPREF0671_08490. DR Proteomes; UP000029732; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000029732}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000029732}. FT DOMAIN 216 400 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 416 AA; 47658 MW; DE173371A6AED6C5 CRC64; MKEFVISEVK AETTVLVGLI TQNQDEAKTK EYLDELEFLA DTAGAVTVKR FTQKVAGPSQ VTYVGKGKLE EIKQYIKDEE ENERPVGMVI FDDELSAKQI RNIEGELGVK ILDRTSLILD IFAMRAQTAN AKTQVELAQY RYMLPRLQRL WTHLERQGGG SGSGGGKGSV GLRGPGETQL EMDRRIILQR ITLLKQRLLE IDKQKTTQRK NRGRMIRVAL VGYTNVGKST LMNLMAKSEV FAENKLFATL DTTVRKVVVD NLPFLLADTV GFIRKLPTDL VDSFKSTLDE VREADLLLHV VDISHPDFEE QIQVVEKTLS ELGCAEKPCM IVFNKIDNYT WIEKEEDDLT PIRKENITLE ELKRTWMARL NDNCLFISAK QRENIDEFRS VLYKKVRELH VQKYPYNDFL YPQMEG // ID A0A099CU82_9GAMM Unreviewed; 436 AA. AC A0A099CU82; DT 07-JAN-2015, integrated into UniProtKB/TrEMBL. DT 07-JAN-2015, sequence version 1. DT 07-JUN-2017, entry version 21. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=LF63_0110770 {ECO:0000313|EMBL:KGI77354.1}; OS Oleiagrimonas soli. OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales; OC Rhodanobacteraceae; Oleiagrimonas. OX NCBI_TaxID=1543381 {ECO:0000313|EMBL:KGI77354.1, ECO:0000313|Proteomes:UP000029708}; RN [1] {ECO:0000313|EMBL:KGI77354.1, ECO:0000313|Proteomes:UP000029708} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=3.5X {ECO:0000313|EMBL:KGI77354.1, RC ECO:0000313|Proteomes:UP000029708}; RA Fang T., Wang H.; RT "Xanthomonadaceae 3.5X direct submission."; RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KGI77354.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JROI01000012; KGI77354.1; -; Genomic_DNA. DR RefSeq; WP_043101693.1; NZ_KN196470.1. DR EnsemblBacteria; KGI77354; KGI77354; LF63_0110770. DR Proteomes; UP000029708; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000029708}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000029708}. FT DOMAIN 200 366 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 436 AA; 47529 MW; 417C832461719D61 CRC64; MFEREKKGER AVVVLPHGRG DVDSASRADE FVELVRSAGA EVLARLEARV DRPNPKFYIG TGKADELAEV VRGVEADLVL VDHTLTPVQE RNLEAHLKAR VVDRAGLILD IFAQRARSHE GKLEVELAQL KHLATRLVRG WTHLDTQRGG AIGNRGPGET QLETDRRLLA ARVKMLTQRL AKVNTQREQQ RRARLRNTVP RVALVGYTNA GKSTLFNVIT TGGVYAADQL FATLDPTVRR IEDLSCGPAV IADTVGFIRE LPHDLVAAFR ATLSEARDAD LLLHVSDAAD DERELLARVV DEVLEEIGAG DVPQLRVMNK IDLTDGEPSI QRDSEGVPQQ VSLSAMTGQG LDLLRQALGE RLGGERIRAE LQLPLSAGRM HARLTALGAI AEEHVDADGW QLRIDAPRSV LAPLAGAGDE ASRALRALIA PPQEPA // ID A0A099D5K7_9ACTN Unreviewed; 468 AA. AC A0A099D5K7; DT 07-JAN-2015, integrated into UniProtKB/TrEMBL. DT 07-JAN-2015, sequence version 1. DT 05-JUL-2017, entry version 20. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=IL38_13730 {ECO:0000313|EMBL:KGI81087.1}; OS Actinopolyspora erythraea. OC Bacteria; Actinobacteria; Actinopolysporales; Actinopolysporaceae; OC Actinopolyspora. OX NCBI_TaxID=414996 {ECO:0000313|EMBL:KGI81087.1, ECO:0000313|Proteomes:UP000029737}; RN [1] {ECO:0000313|EMBL:KGI81087.1, ECO:0000313|Proteomes:UP000029737} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=YIM90600 {ECO:0000313|EMBL:KGI81087.1, RC ECO:0000313|Proteomes:UP000029737}; RX PubMed=25250723; RA Chen D., Feng J., Huang L., Zhang Q., Wu J., Zhu X., Duan Y., Xu Z.; RT "Identification and Characterization of a New Erythromycin RT Biosynthetic Gene Cluster in Actinopolyspora erythraea YIM90600, a RT Novel Erythronolide-Producing Halophilic Actinomycete Isolated from RT Salt Field."; RL PLoS ONE 9:E108129-E108129(2014). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KGI81087.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JPMV01000024; KGI81087.1; -; Genomic_DNA. DR EnsemblBacteria; KGI81087; KGI81087; IL38_13730. DR Proteomes; UP000029737; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000313|EMBL:KGI81087.1}; KW Complete proteome {ECO:0000313|Proteomes:UP000029737}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900, KW ECO:0000313|EMBL:KGI81087.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000029737}. FT DOMAIN 244 413 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 468 AA; 50861 MW; 98B9FF057F45674F CRC64; MGFDSREPSV GEMERAERAS LRRVSGLSTE LSDITEVEYR RLRLERVVLV GVWTEGTSAQ AEASLAELGR LAETAGSEVL DGVVQRRDRP DPATYVGSGK VRELRDIALA AGADTVICDG ELAPGQLRQL EEKLKIKVVD RTALILDIFA QHASSKEGKA QVELAQLQYY LPRLRGWGDK MSRQAGGRAG GGNGGVGTRG PGETKMETDR RRIHKRISKL RKELASMSTI RETKRSRRVA NAVPGVTIAG YTNAGKSSLL NALTGNGLLV EDSLFATLDP ATRSARTPDG RPYTLSDTVG FVRHLPHQLV EAFRSTLEEV TRADLLLHVV DGTDPAPQEQ VSAVREVVSE ISAEQGGSVP PELVVVNKAD SLDNTKVVEL RRLLPEAIFV SARSGEGIEE LKGALADWLP KPDVYVDALV PYTRGELVSR VHTEGELVER EHTAEGTRLR AKVRTDLANA LEPFVTTG // ID A0A099F2W5_9RHOB Unreviewed; 435 AA. AC A0A099F2W5; DT 07-JAN-2015, integrated into UniProtKB/TrEMBL. DT 07-JAN-2015, sequence version 1. DT 07-JUN-2017, entry version 18. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=IT41_09060 {ECO:0000313|EMBL:KGJ04799.1}, GN SAMN04487972_10892 {ECO:0000313|EMBL:SFA51266.1}; OS Paracoccus halophilus. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae; Paracoccus. OX NCBI_TaxID=376733 {ECO:0000313|EMBL:KGJ04799.1, ECO:0000313|Proteomes:UP000029846}; RN [1] {ECO:0000313|EMBL:KGJ04799.1, ECO:0000313|Proteomes:UP000029846} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=JCM 14014 {ECO:0000313|EMBL:KGJ04799.1, RC ECO:0000313|Proteomes:UP000029846}; RA McGinnis J.M., Wolfgang W.J.; RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:KGJ04799.1, ECO:0000313|Proteomes:UP000029846} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=JCM 14014 {ECO:0000313|EMBL:KGJ04799.1, RC ECO:0000313|Proteomes:UP000029846}; RA Mingle L.A., Cole J.A., Lapierre P., Musser K.A.; RT "Paracoccus sanguinis sp. nov., isolated from clinical specimens of RT New York State patients."; RL Submitted (OCT-2014) to the EMBL/GenBank/DDBJ databases. RN [3] {ECO:0000313|EMBL:SFA51266.1, ECO:0000313|Proteomes:UP000182312} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CGMCC 1.6117 {ECO:0000313|EMBL:SFA51266.1, RC ECO:0000313|Proteomes:UP000182312}; RA de Groot N.N.; RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JRKN01000009; KGJ04799.1; -; Genomic_DNA. DR EMBL; FOJO01000008; SFA51266.1; -; Genomic_DNA. DR RefSeq; WP_036740330.1; NZ_JRKN01000009.1. DR EnsemblBacteria; KGJ04799; KGJ04799; IT41_09060. DR Proteomes; UP000029846; Unassembled WGS sequence. DR Proteomes; UP000182312; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000029846}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000029846}. FT DOMAIN 211 380 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 435 AA; 48006 MW; B1F4240EDD45709A CRC64; MAEAFETRER PTRAYVIHPD LGNERTRRAP DLALEEAVAL AHALPAIEVT GAEVARLRKP DPGMLFSKGK REEVGRNIKA AAGGEGAELV LIDGPVTPVQ QRNLEQDWGV KILDRTGLIL EIFADRAQTR EGVLQVELAA LAYQRTRLVR AWTHLERQRG GLGFVGGPGE TQIEADRRAI DDQMVRLRRQ LERVVRTREL HRKARAKVPY PIVALVGYTN AGKSTLFNRL TGAEVMAKDQ LFATLDPTMR QLTLPGGRRA ILSDTVGFIS DLPHELVAAF RATLEEVLAA DLILHVRDIS HPETEEQAGD VGEILDSLGV DDDVPLIEVW NKIDALSPET RAALRRADAR TEGVQAISAL SGEGLEDLLA AIEAHLAAAL EEPRSEAELV LPHADGRRRA WLHGEGVVLG EEIAEDGVHM RLRWTERQKS RFEGL // ID A0A099JLG5_9MICO Unreviewed; 513 AA. AC A0A099JLG5; DT 07-JAN-2015, integrated into UniProtKB/TrEMBL. DT 07-JAN-2015, sequence version 1. DT 07-JUN-2017, entry version 18. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=GY21_06465 {ECO:0000313|EMBL:KGJ79026.1}; OS Cryobacterium roopkundense. OC Bacteria; Actinobacteria; Micrococcales; Microbacteriaceae; OC Cryobacterium. OX NCBI_TaxID=1001240 {ECO:0000313|EMBL:KGJ79026.1, ECO:0000313|Proteomes:UP000029864}; RN [1] {ECO:0000313|EMBL:KGJ79026.1, ECO:0000313|Proteomes:UP000029864} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=RuG17 {ECO:0000313|EMBL:KGJ79026.1, RC ECO:0000313|Proteomes:UP000029864}; RA Sisinthy S.; RL Submitted (AUG-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KGJ79026.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JPXF01000019; KGJ79026.1; -; Genomic_DNA. DR RefSeq; WP_035835897.1; NZ_JPXF01000019.1. DR EnsemblBacteria; KGJ79026; KGJ79026; GY21_06465. DR Proteomes; UP000029864; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 2. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000029864}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000029864}. FT DOMAIN 289 453 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 513 AA; 55645 MW; 6D94D28DAACA9FD0 CRC64; MVDPIVPHDE DDVVARVLAS AETRAAGYSL FRSGSAQALQ AESASGAPEY NEHDGEQTQR EDRNALRRVG GLSTELQDVT EVEYRQLRLE NVVLVGVYTH GTVDDAENSM RELAALAETA GATVLDGLLQ RRATPDPSTY LGKGKAQEVA DIVKAMGADT VIADTELAPS QRRALEDVVK VKVIDRTAVI LDIFSQHATS REGKAQVELA QLAYLLPRLR GWGDSMSRQA GGQVGGAGAG MGSRGPGETK IELDRRRIHT RMSRLRKQMI EMKPAREAKR ANRKRNAVPS VAIVGYTNAG KSSLLNRITR AGVLVENSLF ATLDATVRKS TTEDGRLYTL TDTVGFVRNL PHQLVEAFRS TLEEVADADV IVHVVDGSHP DPVAQLSTVR DVISEVGARH IPELVVFNKS DLISDDDRLV LRGLEPQATF VSARSGEGIE TVLAAISALL PTPQIELELL IPYERGDLIA LLHDEGRVVS TEYVETGTRV NAFVTPEIEP QFTPFLSLPA VTA // ID A0A099KCZ5_9GAMM Unreviewed; 428 AA. AC A0A099KCZ5; DT 07-JAN-2015, integrated into UniProtKB/TrEMBL. DT 07-JAN-2015, sequence version 1. DT 30-AUG-2017, entry version 19. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=ND16A_2728 {ECO:0000313|EMBL:KGJ88175.1}; OS Thalassotalea sp. ND16A. OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales; OC Colwelliaceae; Thalassotalea. OX NCBI_TaxID=1535422 {ECO:0000313|EMBL:KGJ88175.1, ECO:0000313|Proteomes:UP000029848}; RN [1] {ECO:0000313|EMBL:KGJ88175.1, ECO:0000313|Proteomes:UP000029848} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ND16A {ECO:0000313|EMBL:KGJ88175.1, RC ECO:0000313|Proteomes:UP000029848}; RA Stelling S.C., Techtmann S.M., Utturkar S.M., Alshibli N., Brown S.D., RA Hazen T.C.; RT "Draft Genome Sequence of Thalassotalea sp. strain ND16A Isolated from RT Eastern Mediterranean Deep Water."; RL Submitted (AUG-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KGJ88175.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JQDZ01000123; KGJ88175.1; -; Genomic_DNA. DR RefSeq; WP_033079300.1; NZ_JQDZ01000123.1. DR EnsemblBacteria; KGJ88175; KGJ88175; ND16A_2728. DR PATRIC; fig|1535422.3.peg.3857; -. DR Proteomes; UP000029848; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000029848}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000029848}. FT DOMAIN 198 365 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 428 AA; 48525 MW; 7C8089E2F02402E9 CRC64; MFDRHQAGEQ AVLVHIDFPQ ENAREDLQEF EMLVSSAGIN SLTVITGKRD TPHPKYFVGS GKAEEIREAV NLFDADVILF NHVLSPSQEK NLEALCQCRV VDRTTLILDI FAQRARTHEG KLQVELAQLR HMSTRLIRGW THLERQKGGI GLRGPGETQL ETDRRLLRER MHNIRGRLAK VEKQRHQGRR ARERAEIPTV SIVGYTNAGK STLFNRITDS DVYAADQLFA TLDPTLRKLH IEDVGKIILA DTVGFIRHLP HDLVAAFKAT LTETREAHLQ LHVVDISDER RADNIAQVDA VLKEIEANEI PQLLVCNKID NLHDVAPRID RDEQGKPIRV WLSARANIGL ELLSAALTEL LATELIEHRL KIPPSAGKLR GTLYQLNCIK EESYDEQGNC FLDVTLPLRE WNKLLKVGKT DLEGFIQH // ID A0A099PG56_9GAMM Unreviewed; 434 AA. AC A0A099PG56; DT 07-JAN-2015, integrated into UniProtKB/TrEMBL. DT 07-JAN-2015, sequence version 1. DT 30-AUG-2017, entry version 19. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=LH51_02780 {ECO:0000313|EMBL:KGK43046.1}; OS Nitrincola sp. A-D6. OC Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales; OC Nitrincola. OX NCBI_TaxID=1545442 {ECO:0000313|EMBL:KGK43046.1, ECO:0000313|Proteomes:UP000029924}; RN [1] {ECO:0000313|EMBL:KGK43046.1, ECO:0000313|Proteomes:UP000029924} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=A-D6 {ECO:0000313|EMBL:KGK43046.1, RC ECO:0000313|Proteomes:UP000029924}; RA Valdes N., Rivera-Araya J., Bijman J., Escudero G L., Demergasso C., RA Fernandez S., Ferrer A., Chavez R., Levican G.; RT "Draft Genome Sequence of the Arsenic-Resistant Bacterium Nitrincola RT sp. Strain A-D6 Isolated from a Salt Flat in Northern Chile."; RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KGK43046.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JRLB01000010; KGK43046.1; -; Genomic_DNA. DR RefSeq; WP_036519533.1; NZ_JRLB01000010.1. DR EnsemblBacteria; KGK43046; KGK43046; LH51_02780. DR Proteomes; UP000029924; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000029924}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000029924}. FT DOMAIN 199 366 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 434 AA; 48915 MW; D810D8C4486809F1 CRC64; MFFERPESGE CAILVHIDLA SEAEAEDPKE LEELALSAGA DPVCFMHGSR SDPSPRFFLG KGKVEELAEL VRLHEADLVI FNHALSPAQE RNLEREIKCR VLDRTGLILD IFAQRARTHE GKLQVELAQL EHMSTRLVRG WTHLERQKGG IGLRGPGETQ LETDRRLLRA RIKAILKRLD KVRRQRDQGR RARVRAEIAT VSLVGYTNAG KSTLFNRLTT ANVYVADQLF ATLDPTLRKV QLPDAGPIIL ADTVGFIRHL PHKLVEAFRA TLQETAEADL LLHVIDCHDD ERQAHIAQVN DVLAEIGADS RPVLLVYNKI DLLDDFPARI DRDEEGRPVR VWLSAQTGEG ADLLLQAVNE RLSGLMFEGV LQLSPSEGQL RSLLYTKDAV LNERIDEDGR ISLQVRIQQK DFRQLLSRLN IPAERYLAAM VDNE // ID A0A099S5Q7_9CLOT Unreviewed; 592 AA. AC A0A099S5Q7; DT 07-JAN-2015, integrated into UniProtKB/TrEMBL. DT 07-JAN-2015, sequence version 1. DT 07-JUN-2017, entry version 18. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=DP68_08050 {ECO:0000313|EMBL:KGK87889.1}; OS Clostridium sp. HMP27. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=1487921 {ECO:0000313|EMBL:KGK87889.1, ECO:0000313|Proteomes:UP000030009}; RN [1] {ECO:0000313|EMBL:KGK87889.1, ECO:0000313|Proteomes:UP000030009} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=HMP27 {ECO:0000313|EMBL:KGK87889.1, RC ECO:0000313|Proteomes:UP000030009}; RA Tan B.F., Foght J., Budwill K.; RT "Draft genome sequence of Clostridium sp. HMP27 isolated from a coal RT degrading methanogenic culture."; RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KGK87889.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JMFY01000017; KGK87889.1; -; Genomic_DNA. DR RefSeq; WP_035308263.1; NZ_JMFY01000017.1. DR EnsemblBacteria; KGK87889; KGK87889; DP68_08050. DR Proteomes; UP000030009; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000030009}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000030009}. FT DOMAIN 362 538 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 592 AA; 66759 MW; 0FD82ED0D0A061DA CRC64; MINGNIEGIK DSTLKRLEAI YDLKIPKDEV FTEELINIIV GVTLDVNREV SVAISRKGMI EGVAIGDSTS VEMPMIDIKE RKLSGVRIIH THPNGNSHLS ALDISALIKL KLDCIAAVGV DENDITDITL GFCNVKDNML VAETTKKLIL EEAINYPILD KVRYIEELIK TTSVEEETGE KAILVGVESE ESLDELEELA RACEVEVVDK MLQNRYKIDT AYYVGSGKVE EIALLRQAKR ANVVIFDDEL TASQVRNLED IIGVKVIDRT TLILEIFAKR AKSREGKIQV ELAQLKYRLP RLSGLGTVLS RTGGGIGTKG PGEKKLETDK RHIKERIYDL KSELEKTKQT RMTQRESRSE IPKVSLVGYT NAGKSTLRNT LCTIAAKETI KKESVLEADM LFATLDTTTR AIVLPDNRTI TLTDTVGFIR KLPHDLVEAF KSTLEEVIYS DLLLHVVDVS QENYLEQIEA VNKVLEELAA IDKPYVYVLN KIDKLSEEKL EEINELFKDK MNIKISARHN INLEELLNLI GSKLPNKLRK AEYLIPYDKQ SMVAYLHRNS NVISEEYRED GTYICAEVSE MVYNTCEEYM TK // ID A0A099SDU8_9CLOT Unreviewed; 422 AA. AC A0A099SDU8; DT 07-JAN-2015, integrated into UniProtKB/TrEMBL. DT 07-JAN-2015, sequence version 1. DT 07-JUN-2017, entry version 18. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=DP68_02255 {ECO:0000313|EMBL:KGK90256.1}; OS Clostridium sp. HMP27. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=1487921 {ECO:0000313|EMBL:KGK90256.1, ECO:0000313|Proteomes:UP000030009}; RN [1] {ECO:0000313|EMBL:KGK90256.1, ECO:0000313|Proteomes:UP000030009} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=HMP27 {ECO:0000313|EMBL:KGK90256.1, RC ECO:0000313|Proteomes:UP000030009}; RA Tan B.F., Foght J., Budwill K.; RT "Draft genome sequence of Clostridium sp. HMP27 isolated from a coal RT degrading methanogenic culture."; RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KGK90256.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JMFY01000002; KGK90256.1; -; Genomic_DNA. DR RefSeq; WP_035305444.1; NZ_JMFY01000002.1. DR EnsemblBacteria; KGK90256; KGK90256; DP68_02255. DR Proteomes; UP000030009; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000030009}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000030009}. FT DOMAIN 197 365 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 422 AA; 48017 MW; 7B6854C19E089E37 CRC64; MEQKQRAIIV GCNLKNDKEF LNMMKELSSL ADACDIEVVG EITQKLERVY SSHYLGKGKI QELFTLIHEK DVDMVIFNDE LSPSQIRNLD TALKCKVIDR TVLIFDILAK RAKSKEAQLQ VEIAKLQYIL PRVAGLEGSL GRQEGSVRFI SRGFGETKLE LNHRKIKDRI SGLNAELETL VVERKNQRKQ RKKSGMPAVA LVGYTNAGKS SIMNSMIDLY SSSIDKKVFE KDMLFATLET YVRNIKLPNN KSFLLSDTVG FISKLPHQLV NAFRSTLEEI TEADMLVHVV DYSNPNYKQH IEVTKNTLKE LGADNIPIIY AYNKTDLVDG EITKDEKDCI YISAKNKAGI DELVNEICKR VFPQHVCCQL LIPYEKGNIL SYFNDNANIK SNEYNSDGAL ISMECNKSDY ERYKQFESLV KI // ID A0A099TEJ3_9RHOB Unreviewed; 438 AA. AC A0A099TEJ3; DT 07-JAN-2015, integrated into UniProtKB/TrEMBL. DT 07-JAN-2015, sequence version 1. DT 07-JUN-2017, entry version 16. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=PM04_01275 {ECO:0000313|EMBL:KGL02647.1}; OS Thalassobacter sp. 16PALIMAR09. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae; Thalassobacter. OX NCBI_TaxID=1225651 {ECO:0000313|EMBL:KGL02647.1, ECO:0000313|Proteomes:UP000029829}; RN [1] {ECO:0000313|EMBL:KGL02647.1, ECO:0000313|Proteomes:UP000029829} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=16PALIMAR09 {ECO:0000313|EMBL:KGL02647.1, RC ECO:0000313|Proteomes:UP000029829}; RA Mas-Llado M., Nogales B., Bosch R.; RT "Draft genome sequence of Thalassobacter sp. 16PALIMAR09."; RL Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KGL02647.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JHAK01000001; KGL02647.1; -; Genomic_DNA. DR RefSeq; WP_052068260.1; NZ_JHAK01000001.1. DR EnsemblBacteria; KGL02647; KGL02647; PM04_01275. DR Proteomes; UP000029829; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000029829}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000029829}. FT DOMAIN 216 385 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 438 AA; 48137 MW; F34869380E7C4F06 CRC64; MMAKTALTDP VESGATEAPP TRTAVLHPDL GPDHTRRAPE HGLAEAVSLA HALPGLEVVR DQVVRLPKPH PGHLFGTGKL AELKQLLHDD EIDLVVIDGP VTPVQQRNLE KEWKVKLLDR TGLILEIFAD RAATREGVLQ VELAALSYQR TRLVRAWTHL ERQRGGLGFV GGPGETQIEA DRRAIDDAVN RIRKQLAKVV KTRALHRAAR AKVPYPIVAL VGYTNAGKST LFNYLTGADV FAKDMLFATL DPTMRAVTLP GGTDIILSDT VGFISDLPTQ LVAAFRATLE EVLDADLICH VRDISHPESD AQARDVNAIL AQLGVSDEIP KIELWNKIDA VDADTRASIE AIAARREDVF TLSAVTGEGR DPALAAIATR VTPATHDEEV FVPFADGRAR AWLHGEDIIQ QEAQEDEGFR FQVRWTTRQA EQFAKMRR // ID A0A099W450_9LIST Unreviewed; 423 AA. AC A0A099W450; DT 07-JAN-2015, integrated into UniProtKB/TrEMBL. DT 07-JAN-2015, sequence version 1. DT 07-JUN-2017, entry version 18. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=EP56_13070 {ECO:0000313|EMBL:KGL39491.1}; OS Listeriaceae bacterium FSL A5-0209. OC Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae. OX NCBI_TaxID=1497679 {ECO:0000313|EMBL:KGL39491.1, ECO:0000313|Proteomes:UP000029855}; RN [1] {ECO:0000313|EMBL:KGL39491.1, ECO:0000313|Proteomes:UP000029855} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=FSL A5-0209 {ECO:0000313|EMBL:KGL39491.1, RC ECO:0000313|Proteomes:UP000029855}; RA den Bakker H.C.; RT "Novel Listeriaceae from food processing plants."; RL Submitted (MAY-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KGL39491.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JNEZ01000044; KGL39491.1; -; Genomic_DNA. DR RefSeq; WP_036132833.1; NZ_JNEZ01000044.1. DR EnsemblBacteria; KGL39491; KGL39491; EP56_13070. DR Proteomes; UP000029855; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000029855}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000029855}. FT DOMAIN 194 363 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 153 187 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 423 AA; 47802 MW; 2AD70CACECB59B8A CRC64; MTRTAILVGI TMQQADFEYS MAELANLAEA NAIEPVGEIT QKLDRKNKAT YVGKGKVDEI KSLVDYEAVD LVIFNDELAP SQIRNLEELL EIEVMDRTRL ILDIFAERAK TREAQLQVQV ARLKYELPRV VGQGEGMDQQ SGKGGLKNRG AGETKLEMDR RRIKNQISQL NKELDGLVAE RQVQRRQRQK NEIPVVSLVG YTNAGKSTIM NAMVTAHSQT ANKQVFEKDM LFATLETSVR EIVLPDKKQF LLTDTVGFVS KLPHNLVKAF RSTLEEAAEA DVLIHVVDVS HEHFDAMIKT TEETLAELDI TDRPIIFAYN KADLATNVMF PRREGDSLYL SAREDTGLEL LIEMIKERVF NDYQTVTFVI PFDRGDVVSY LNENADVLET AYENEGTVLR VNAQESDRMK YAAFISEDTQ KEG // ID A0A099WWQ9_PORCN Unreviewed; 409 AA. AC A0A099WWQ9; DT 07-JAN-2015, integrated into UniProtKB/TrEMBL. DT 07-JAN-2015, sequence version 1. DT 07-JUN-2017, entry version 20. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=HQ35_10630 {ECO:0000313|EMBL:KGN78132.1}; OS Porphyromonas cangingivalis. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; OC Porphyromonadaceae; Porphyromonas. OX NCBI_TaxID=36874 {ECO:0000313|EMBL:KGN78132.1, ECO:0000313|Proteomes:UP000030125}; RN [1] {ECO:0000313|EMBL:KGN78132.1, ECO:0000313|Proteomes:UP000030125} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=COT-109 OH1386 {ECO:0000313|Proteomes:UP000030125}; RA Wallis C., Deusch O., O'Flynn C., Davis I., Jospin G., Darling A.E., RA Coil D.A., Alexiev A., Horsfall A., Kirkwood N., Harris S., RA Eisen J.A.; RT "Porphyromonas cangingivalis strain:COT-109_OH1386 Genome RT sequencing."; RL Submitted (AUG-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KGN78132.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JQJD01000065; KGN78132.1; -; Genomic_DNA. DR RefSeq; WP_036845971.1; NZ_KN265638.1. DR EnsemblBacteria; KGN78132; KGN78132; HQ35_10630. DR Proteomes; UP000030125; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000030125}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000030125}. FT DOMAIN 202 388 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 170 197 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 409 AA; 46755 MW; 9CA8E06931DEAF57 CRC64; MKDFIITDIG SEKAFLVGLI TQGQSEAEVS EYLDELAFLA DTAGVTAVRR FTQKLEHPQP ATFVGKGKLQ EIKEAIEDEE VGVVIFDDEL SPKQLRNIEN ELKVKILDRT RLILDIFASR AQTAHAKVQV ELALYNYMLP RLTGLWTHLE RQRGGVGMRG PGETQLETDR RIILDKIARL KEQLKAIDRQ MNVQRQNRGK MVRVALVGYT NVGKSTMMNL LSKSEVFAEN KLFATLDTTV RKVIIHNLPF LLSDTVGFIR KLPTQLIESF KSTLDEVREA DLLVHVVDVS HPSFEEQIEV VNSTLREILG DEEKPVILVF NKVDAFTYTP KAEDDLTPIT RENISLEELQ KTWMNHASQT DVRFVSAKTG DGINELKSLF YDRIKTIHMS RFPYNDFLFE TYEHLNEEE // ID A0A099XXJ7_9FLAO Unreviewed; 403 AA. AC A0A099XXJ7; DT 07-JAN-2015, integrated into UniProtKB/TrEMBL. DT 07-JAN-2015, sequence version 1. DT 07-JUN-2017, entry version 18. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=PHEL85_1621 {ECO:0000313|EMBL:KGL61836.1}; OS Polaribacter sp. Hel1_85. OC Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales; OC Flavobacteriaceae; Polaribacter. OX NCBI_TaxID=1250005 {ECO:0000313|EMBL:KGL61836.1, ECO:0000313|Proteomes:UP000029991}; RN [1] {ECO:0000313|EMBL:KGL61836.1, ECO:0000313|Proteomes:UP000029991} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Hel1_85 {ECO:0000313|EMBL:KGL61836.1, RC ECO:0000313|Proteomes:UP000029991}; RA Xing P., Hahnke R.L., Unfried F., Markert S., Huang S., Barbeyron T., RA Harder J., Becher D., Schweder T., Gloenk F.O., Amann R.I., RA Teeling H.; RT "Niches of two polysaccharide-degrading Polaribacter strains isolated RT from the North Sea during a spring diatom bloom."; RL ISME J. 0:0-0(2014). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KGL61836.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JPDS01000002; KGL61836.1; -; Genomic_DNA. DR RefSeq; WP_036823679.1; NZ_JPDS01000002.1. DR EnsemblBacteria; KGL61836; KGL61836; PHEL85_1621. DR Proteomes; UP000029991; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000029991}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000029991}. FT DOMAIN 200 385 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 403 AA; 46328 MW; AB6085A27431EE6A CRC64; MIDQKEAKSE KAVLIGIISQ QQDEIQSTEY LDELEFLTTT AGGVSVKRFV QKMERPNPKT FLGTGKLDEV KAYIESNNIG TAIFDDELSP AQLRNIEKIL DCKILDRTNL ILDIFAQRAH TSSAKTQVEL AQCQYLLPRL TRLWTHLDKQ KGGIGMRGPG ETEIETDRRI INDRIVLLKK KLKTIDKQMA VQRKNRGKMV RVALVGYTNV GKSTLMNVIS KSDVFAENKL FATLDTTVRK VVIKNIPFLM TDTVGFIRKL PTQLVESFKS TLDEVREADL LLHVVDISHP NFEDHIASVN TILADIKCAD KPTLMVFNKI DAYSHETIDE DDIVTEKGKE HYTLQDWQKT WMNDKEVESI FISALNKENL DDFKEKTYQE VKKIHIQRFP YNDFLYYEYK GEE // ID A0A099YRA0_TINGU Unreviewed; 406 AA. AC A0A099YRA0; DT 07-JAN-2015, integrated into UniProtKB/TrEMBL. DT 07-JAN-2015, sequence version 1. DT 10-MAY-2017, entry version 12. DE SubName: Full=Putative GTP-binding protein 6 {ECO:0000313|EMBL:KGL72829.1}; DE Flags: Fragment; GN ORFNames=N309_12452 {ECO:0000313|EMBL:KGL72829.1}; OS Tinamus guttatus (White-throated tinamou). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda; OC Coelurosauria; Aves; Palaeognathae; Tinamiformes; Tinamidae; Tinamus. OX NCBI_TaxID=94827 {ECO:0000313|EMBL:KGL72829.1, ECO:0000313|Proteomes:UP000053641}; RN [1] {ECO:0000313|EMBL:KGL72829.1, ECO:0000313|Proteomes:UP000053641} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BGI_N309 {ECO:0000313|EMBL:KGL72829.1}; RA Zhang G., Li C.; RT "Genome evolution of avian class."; RL Submitted (JUN-2014) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; KL885241; KGL72829.1; -; Genomic_DNA. DR Proteomes; UP000053641; Unassembled WGS sequence. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR CDD; cd01878; HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 4: Predicted; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000053641}; KW Reference proteome {ECO:0000313|Proteomes:UP000053641}. FT DOMAIN 180 344 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 142 176 {ECO:0000256|SAM:Coils}. FT NON_TER 1 1 {ECO:0000313|EMBL:KGL72829.1}. FT NON_TER 406 406 {ECO:0000313|EMBL:KGL72829.1}. SQ SEQUENCE 406 AA; 45993 MW; 78FB4882CC16662D CRC64; AELQIAEAVA LVDTLQNWTI LDKIIISTKT PDKKFIFGKG NFQALTEKIK KLPRLTAVFL NVERISSLTK KELEDAWGVK VFDRYTVVLH IFRCNARTKE AKLQIALAEI PLLRSNLKNE VSQLDQQRGG SRYIMGSGET FMETQNRLLR EKELKIRNAL EKLKRKRSIL RNQRKRQEFP IISVMGYTNC GKTTLIKALT GEAGLQPKDQ LFATLDITAH AGYLPSHMTV IYVDTIGFLS DLPHNLVESF SATLEEVAYS DLIVHVRDIT HPETVLQKAS VLSVLKNLNL PSHLLESMVE VHNKVDLIER YKSTEENALA ISALHGHGLE ELKEEIEKRI LKTTGKKILT VQINLEGPQL SWLYKQATVQ DIEVAPEDGT ARVKVIISNS AFGRYKKLFP NSRLFI // ID A0A0A0B472_9CELL Unreviewed; 516 AA. AC A0A0A0B472; DT 07-JAN-2015, integrated into UniProtKB/TrEMBL. DT 07-JAN-2015, sequence version 1. DT 07-JUN-2017, entry version 18. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=Q760_07455 {ECO:0000313|EMBL:KGM00594.1}; OS Cellulomonas cellasea DSM 20118. OC Bacteria; Actinobacteria; Micrococcales; Cellulomonadaceae; OC Cellulomonas. OX NCBI_TaxID=1408250 {ECO:0000313|EMBL:KGM00594.1, ECO:0000313|Proteomes:UP000029833}; RN [1] {ECO:0000313|EMBL:KGM00594.1, ECO:0000313|Proteomes:UP000029833} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 20118 {ECO:0000313|EMBL:KGM00594.1, RC ECO:0000313|Proteomes:UP000029833}; RA Wang G., Zhuang W.; RL Submitted (OCT-2013) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KGM00594.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AXNT01000188; KGM00594.1; -; Genomic_DNA. DR EnsemblBacteria; KGM00594; KGM00594; Q760_07455. DR Proteomes; UP000029833; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 2. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000313|EMBL:KGM00594.1}; KW Complete proteome {ECO:0000313|Proteomes:UP000029833}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900, KW ECO:0000313|EMBL:KGM00594.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000029833}. FT DOMAIN 294 460 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 516 AA; 55595 MW; 5FE00D757C421EEC CRC64; MDERHRVSDP QHPQTREETA DAAVDRRSAQ EVADDVVARV LARAGTALHE GGTVHSSYDG DQLDLEERTS LRRVGGLSTE LEDVTEVEYR QLRLERVVLV GLWGSGTAEQ AELSLRELAA LAETAGSQVL DGMLQRRRTP DPSTFLGSGK AAELAGVVAA VGADTVIVDA DLAPSQRRAL EDVVRVKVID RTALILDIFA QHAKSREGKA QVELAQLEYL LPRLRGWGES MSRQAGGQVG GAGAGMGSRG PGETKIELDR RRIRDRMAKL RREIAAMEPA RQTKRASRKR HAIPSVAIAG YTNAGKSSLL NRLTGAGVLV ENALFATLDP TVRRAEAADG RVYTLTDTVG FVRDLPHQLV EAFRSTLEEV ADADLVLHVV DASHPDPEGQ ISAVRHVFAD IPGAMDVPEV IVLNKADLAE PEALARLRSR EPGSIVVSAH TGEGIEALQA LIADQLPRPS VTVDVVIPYD RGDLVHRVHL HGEIDSEEHT EAGTALRARV DETLASELSA AAVRSA // ID A0A0A0BR32_9CELL Unreviewed; 495 AA. AC A0A0A0BR32; DT 07-JAN-2015, integrated into UniProtKB/TrEMBL. DT 07-JAN-2015, sequence version 1. DT 07-JUN-2017, entry version 17. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=N869_06690 {ECO:0000313|EMBL:KGM09559.1}; OS Cellulomonas bogoriensis 69B4 = DSM 16987. OC Bacteria; Actinobacteria; Micrococcales; Cellulomonadaceae; OC Cellulomonas. OX NCBI_TaxID=1386082 {ECO:0000313|EMBL:KGM09559.1, ECO:0000313|Proteomes:UP000054314}; RN [1] {ECO:0000313|EMBL:KGM09559.1, ECO:0000313|Proteomes:UP000054314} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=69B4 {ECO:0000313|EMBL:KGM09559.1, RC ECO:0000313|Proteomes:UP000054314}; RA Chen F., Li Y., Wang G.; RT "Genome sequencing of Cellulomonas bogoriensis 69B4."; RL Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KGM09559.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AXCZ01000182; KGM09559.1; -; Genomic_DNA. DR RefSeq; WP_035062234.1; NZ_AXCZ01000182.1. DR EnsemblBacteria; KGM09559; KGM09559; N869_06690. DR Proteomes; UP000054314; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 2. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000054314}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000054314}. FT DOMAIN 274 440 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 495 AA; 53416 MW; 6B74C1CEA2EB5788 CRC64; MTEPTDQQRA RELADSVVAR VLARAGTALD EGTTQVRDTD GDQLDREERA ALRRVGGLST ELQDVTEVEY RELRLEKVVL AGLWSGGAVE EAEVSLRELA ALAETAGSTV LDGVLQRRAT PDPGTYLGSG KAAELAEIVA ATGADTVVVD ADLAPSQRRG LEDIVRVKVI DRTALILDIF AQHAKSREGK AQVELAQLEY LLPRLRGWGE SMSRQAGGRV AAGAGIGSRG PGETKIELDR RRIRTRMAKL RREIAAMKPA RATQRAARRR GHVPAVAIVG YTNAGKSSLL NRLTGAGVLV ENALFATLDP TVRRATTPDG RQYTIADTVG FVRSLPTQLV EAFRSTLEEV GESDLLLHVV DASHADPEGQ IAAVRSVLAE IEGVEDVPEL VVLNKADKAD PDTLARLRRR EPRTVVVSAH TGAGLDELLA RVADELPRPS VQVSVVVPYQ RGDLVNRVHL EGEIDSEEHT GQGTRLQARV DPELAAELQE VAVRE // ID A0A0A0BW35_9CELL Unreviewed; 518 AA. AC A0A0A0BW35; DT 07-JAN-2015, integrated into UniProtKB/TrEMBL. DT 07-JAN-2015, sequence version 1. DT 07-JUN-2017, entry version 18. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=N868_01820 {ECO:0000313|EMBL:KGM12136.1}; OS Cellulomonas carbonis T26. OC Bacteria; Actinobacteria; Micrococcales; Cellulomonadaceae; OC Cellulomonas. OX NCBI_TaxID=947969 {ECO:0000313|EMBL:KGM12136.1, ECO:0000313|Proteomes:UP000029839}; RN [1] {ECO:0000313|EMBL:KGM12136.1, ECO:0000313|Proteomes:UP000029839} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=T26 {ECO:0000313|EMBL:KGM12136.1, RC ECO:0000313|Proteomes:UP000029839}; RA Chen F., Li Y., Wang G.; RT "Genome sequencing of Cellulomonas carbonis T26."; RL Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KGM12136.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AXCY01000008; KGM12136.1; -; Genomic_DNA. DR EnsemblBacteria; KGM12136; KGM12136; N868_01820. DR Proteomes; UP000029839; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 2. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000029839}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000029839}. FT DOMAIN 298 464 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 518 AA; 56089 MW; 38C0F74CAB76DCA4 CRC64; MTHPTTPAGD GADATIPERN PEPTATAPAE TAAPTLRPDD VVARVLARAG TALDEGDTRW TDDDGDQLDR EERAALRRVG GLSTELEDVT EVEYRSLRLE RVVLAGVWSS GTVEDAELSL RELAALAETA GSEVLDGLLQ RRQNPDPGTY FGSGKAAELA DVVRATGADT VVVDADLSPS QRRGLEDIVK VKVIDRTALI LDIFAQHAKS KEGKAQVELA QLEYLLPRLR GWGESMSRQA GGRVAGGEGI GSRGPGETKI ELDRRRIRTR MAKLRREIAH MRPARETRRA SRRRHQVPAV AIVGYTNAGK SSLLNRLTGA GVLVENALFA TLDPTVRRAR TPDGRTYTLA DTVGFVRSLP TQLVEAFRST LEEVAEADVL LHVVDVSHPD PEGQIAAVRT VLGEIEGVDD IVEVVVLNKA DVADPETVAR LRRREPRSVV VSAHTGEGLE ELQRVVAEHL PRPHEVVDVV VPYDRGDLVH RVHSEGEVDD EQHTADGTVL RARVGADLAA ELRAVSVA // ID A0A0A0C5M4_9CELL Unreviewed; 497 AA. AC A0A0A0C5M4; DT 07-JAN-2015, integrated into UniProtKB/TrEMBL. DT 07-JAN-2015, sequence version 1. DT 07-JUN-2017, entry version 18. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=N867_08195 {ECO:0000313|EMBL:KGM15476.1}; OS Actinotalea fermentans ATCC 43279 = JCM 9966 = DSM 3133. OC Bacteria; Actinobacteria; Micrococcales; Cellulomonadaceae; OC Actinotalea. OX NCBI_TaxID=862422 {ECO:0000313|EMBL:KGM15476.1, ECO:0000313|Proteomes:UP000029877}; RN [1] {ECO:0000313|Proteomes:UP000029877} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 3133 {ECO:0000313|Proteomes:UP000029877}; RA Chen F., Li Y., Wang G.; RT "Actinotalea ferrariae CF5-4."; RL Submitted (JAN-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KGM15476.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AXCX01000262; KGM15476.1; -; Genomic_DNA. DR EnsemblBacteria; KGM15476; KGM15476; N867_08195. DR Proteomes; UP000029877; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 2. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000029877}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000029877}. FT DOMAIN 277 443 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 497 AA; 53599 MW; 20FE82E93DE245BE CRC64; MTTPNHPAAS DGDPIALADD VVARVLARAG RSLDAAPESW EDADGDQLDR ADRAALRRVA GLSTELDDVT EVEYRQLRLE RVVLAGLYSR SAHEAEVSLR ELAALAETAG SQVLDGVLQR RPHPDPGTFL GSGKAGELAD LVRDSGADTV IVDGDLAPSQ RRALEDIVKV KVIDRTALIL DIFAQHARSK EGKAQVELAQ LEYLLPRLRG WGESMSRQAG GRVAGGEGIG SRGPGETKIE LDRRRIRARM AKLRREIAEM SPARSTRRAS RRRHGVPGVA VVGYTNAGKS SLLNRLTGAG VLVENALFAT LDPTVRRTQT PDGRTYTLTD TVGFVRALPT QLVEAFRSTL EEVAESDLLL HVVDASHPDP EGQIATVRGV VREIDGAERI PELLVLNKVD VADPDVVDRV LRREPRAVVI SARTGAGLEE LAERVAAALP RPHELVDLVV PYARGDLVSR VHDDGEIERE VHTAEGTALV ARVDPALAAE LRAAARP // ID A0A0A0DAH8_9PROT Unreviewed; 433 AA. AC A0A0A0DAH8; DT 07-JAN-2015, integrated into UniProtKB/TrEMBL. DT 07-JAN-2015, sequence version 1. DT 07-JUN-2017, entry version 17. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=P409_06235 {ECO:0000313|EMBL:KGM35134.1}; OS Inquilinus limosus MP06. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales; OC Rhodospirillaceae; Inquilinus. OX NCBI_TaxID=1398085 {ECO:0000313|EMBL:KGM35134.1, ECO:0000313|Proteomes:UP000029995}; RN [1] {ECO:0000313|EMBL:KGM35134.1, ECO:0000313|Proteomes:UP000029995} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MP06 {ECO:0000313|EMBL:KGM35134.1, RC ECO:0000313|Proteomes:UP000029995}; RA Pino M., Di Conza J., Gutkind G.; RT "Genome sequence determination for a cystic fibrosis isolate, RT Inquilinus limosus."; RL Submitted (JAN-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KGM35134.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JANX01000046; KGM35134.1; -; Genomic_DNA. DR RefSeq; WP_034833073.1; NZ_JANX01000046.1. DR EnsemblBacteria; KGM35134; KGM35134; P409_06235. DR Proteomes; UP000029995; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000029995}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000029995}. FT DOMAIN 203 375 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 433 AA; 47844 MW; CD99A43B91AFCDEA CRC64; MDGASSGRAI VIHPVLPGAR NDAGRTAEAS LEEAVGLSRA ISLDIAEARC VRVSRPQPST LIGEGALEEL SSVVAATEAG LVVVDATLSP VQQRNLERRW KTKVIDRTGL ILEIFGERAR TREGQLQVEL AHLSYQRSRL VRSWTHLERQ RGGAGFLGGP GETQIELDRR QIDDRIIQIK RQLDDVRRTR SLHRDARARV PYPVVALVGY TNAGKSTLFN RLTRATVLAK DMLFATLDPT MRAIEAGQGR RIILSDTVGF ISDLPTHLVA AFRATLEEVQ AADLILHVRD IAHPDTEAQR EDVEAVLRDL DIDIDSDGRV IEVLNKADLL PEAERETLST AVRRRGHDAA VISALTGEGC DGLMELIARR INADRETMTV KLDIADGRTL AWLHEHGEVL EARDDGAHLF VRVRLHPNDA ARLHRQLGIA TRH // ID A0A0A0DIB1_9STRE Unreviewed; 412 AA. AC A0A0A0DIB1; DT 07-JAN-2015, integrated into UniProtKB/TrEMBL. DT 07-JAN-2015, sequence version 1. DT 05-JUL-2017, entry version 19. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=SSIN_0574 {ECO:0000313|EMBL:KGM37633.1}; OS Streptococcus sinensis. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=176090 {ECO:0000313|EMBL:KGM37633.1, ECO:0000313|Proteomes:UP000030019}; RN [1] {ECO:0000313|EMBL:KGM37633.1, ECO:0000313|Proteomes:UP000030019} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=HKU4 {ECO:0000313|EMBL:KGM37633.1, RC ECO:0000313|Proteomes:UP000030019}; RA Teng J.L., Huang Y., Tse H., Lau S.K., Woo P.C.; RL Submitted (JUN-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KGM37633.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JPEN01000042; KGM37633.1; -; Genomic_DNA. DR RefSeq; WP_037615452.1; NZ_JPEN01000042.1. DR EnsemblBacteria; KGM37633; KGM37633; SSIN_0574. DR PATRIC; fig|176090.4.peg.569; -. DR Proteomes; UP000030019; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000030019}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}. FT DOMAIN 199 359 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 158 192 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 412 AA; 46593 MW; 39C9236619DAB341 CRC64; MIETEKKIER VFLVGVELPD TENFDLSMEE LQSLAKTAGA EVVGSYSQKR EKYDSKTFVG SGKLEEIRQM VDAEEISTVI VNNRLTPRQN VNLEESLGVK VIDRMQLILD IFAMRARSHE GKLQVHLAQL KYLLPRLVGQ GIMLSRQAGG IGSRGPGESQ LELNRRSVRN QIHDIERQLK AVEKNRATVR EKRLESSIFK IGLIGYTNAG KSTIMNCLTS KSQYEADELF ATLDATTKNI NLSGQLNVTL TDTVGFIQDL PTELVSSFKS TLEESKNVDL LVHVIDASDP HHEEHEKTVL DIMKELDMLD IPRLTLYNKA DKAEDFTPTL TPYSLISAKA DNSRAVLQQV LLERMKELFL PFTIKVAPAK AYKIYDLEKV AIIGSREYLD DVETISGWIA EKNKWKLEEF YD // ID A0A0A0DLZ3_9BURK Unreviewed; 410 AA. AC A0A0A0DLZ3; DT 07-JAN-2015, integrated into UniProtKB/TrEMBL. DT 07-JAN-2015, sequence version 1. DT 10-MAY-2017, entry version 16. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=JY96_02225 {ECO:0000313|EMBL:KGM39239.1}; OS Aquabacterium sp. NJ1. OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Aquabacterium. OX NCBI_TaxID=1538295 {ECO:0000313|EMBL:KGM39239.1, ECO:0000313|Proteomes:UP000029993}; RN [1] {ECO:0000313|EMBL:KGM39239.1, ECO:0000313|Proteomes:UP000029993} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NJ1 {ECO:0000313|EMBL:KGM39239.1, RC ECO:0000313|Proteomes:UP000029993}; RA Masuda H.; RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:KGM39239.1, ECO:0000313|Proteomes:UP000029993} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NJ1 {ECO:0000313|EMBL:KGM39239.1, RC ECO:0000313|Proteomes:UP000029993}; RA Shiwa Y., Yoshikawa H., Zylstra G.J.; RT "The draft genome sequence of a soil bacterium, Aquabacterium sp. RT strain NJ1, capable of utilizing both liquid and solid n-alkanes."; RL Submitted (OCT-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KGM39239.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JRKM01000001; KGM39239.1; -; Genomic_DNA. DR EnsemblBacteria; KGM39239; KGM39239; JY96_02225. DR Proteomes; UP000029993; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000029993}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000029993}. FT DOMAIN 199 373 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 410 AA; 45138 MW; 3094BAD22E8E9276 CRC64; MLNASQDPRV VLVGVDLGPG SSFDPTLDEL ALLAESAGDM PVAKVTAKRK APDARLFVGS GKADEIKSIV DLYQAHGVIF DQALSPAQQR NLERHLGVEV LDRTGLILEI FGARARSHEG KLQVELARLQ YLSTRLVRRW SHLERQRGGV GHRGGPGETQ LELDRRMIET KIKSLKDSLI KVKRQRNTQR RSRERTGTFR VSLVGYTNAG KSTLFNALTK AGTYAANQLF ATLDTTTRQL FLAEAQRSVT LSDTVGFIRD LPHSLVESFE ATLQEAAEAD LLLHVVDAAS PVLHEQIDEV LRVLDSIGAG QLPQVLVFNK SDCLPEHQQP RHERDLYELP SGRRCIRVFV SALKGEGLDV LRAVLAEAAL HGLGDAPNDN TPSDPRFGMH NPIDAEAPSP ERPDFPTVRT // ID A0A0A0E830_9BACI Unreviewed; 422 AA. AC A0A0A0E830; DT 07-JAN-2015, integrated into UniProtKB/TrEMBL. DT 07-JAN-2015, sequence version 1. DT 12-APR-2017, entry version 17. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=NP83_00780 {ECO:0000313|EMBL:KGM46325.1}; OS Bacillus niacini. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus. OX NCBI_TaxID=86668 {ECO:0000313|EMBL:KGM46325.1, ECO:0000313|Proteomes:UP000031376}; RN [1] {ECO:0000313|EMBL:KGM46325.1, ECO:0000313|Proteomes:UP000031376} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 2923 {ECO:0000313|EMBL:KGM46325.1, RC ECO:0000313|Proteomes:UP000031376}; RA Harvey Z.H., Snider M.J.; RT "Draft Genome of the Nicotinate-Metabolizing Soil Bacterium Bacillus RT niacini (DSM 2923)."; RL Submitted (OCT-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KGM46325.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JRYQ01000014; KGM46325.1; -; Genomic_DNA. DR EnsemblBacteria; KGM46325; KGM46325; NP83_00780. DR Proteomes; UP000031376; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000031376}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000031376}. FT DOMAIN 200 362 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 422 AA; 48326 MW; 9BCE4FCF1FC4260E CRC64; MEQEVSLEKA ILVGCQTQTL DDSRFHYSME ELASLTETAK GEVLMSVSQK RERIHPALYI GKGKVEELKT LVDEVEADLV IFNDELSPSQ KRNLASELNA RIIDRTQLIL DIFAQRARSK EGKLQVELAQ LQYLLPRLAG QGTALSRLGA GIGTRGPGET KLESDRRHIR RRIDDIKSQL SVIVQHRDRY RERRKKNKTF QIAIVGYTNA GKSTLFNRLS EADSYEENQL FATLDPMTRK LVLPSGYQTL ITDTVGFIQD LPTALIAAFR STLEEVKEAD LLLHVVDMAN ADYFQHEKTV NKLLEDLEVK DIPQITVYNK RDIKHPDFVP TANTPLIFIS AYDKEDRNEL KRKIEKAIIE MMDQYQVSIP STEGKLLAQL KNETIVRELV FDEEKELYQC RGFSLPDHQI SGQLEKYKTR ME // ID A0A0A0EE04_9RHOB Unreviewed; 424 AA. AC A0A0A0EE04; DT 07-JAN-2015, integrated into UniProtKB/TrEMBL. DT 07-JAN-2015, sequence version 1. DT 07-JUN-2017, entry version 19. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=ATO9_18620 {ECO:0000313|EMBL:KGM47412.1}; OS Pseudooceanicola atlanticus. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae; Pseudooceanicola. OX NCBI_TaxID=1461694 {ECO:0000313|EMBL:KGM47412.1, ECO:0000313|Proteomes:UP000030004}; RN [1] {ECO:0000313|EMBL:KGM47412.1, ECO:0000313|Proteomes:UP000030004} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=22II-s11g {ECO:0000313|EMBL:KGM47412.1, RC ECO:0000313|Proteomes:UP000030004}; RX PubMed=25663028; DOI=10.1007/s10482-015-0398-2; RA Lai Q., Li G., Liu X., Du Y., Sun F., Shao Z.; RT "Pseudooceanicola atlanticus gen. nov. sp. nov., isolated from surface RT seawater of the Atlantic Ocean and reclassification of Oceanicola RT batsensis, Oceanicola marinus, Oceanicola nitratireducens, Oceanicola RT nanhaiensis, Oceanicola antarcticus and Oceanicola flagellatus, as RT Pseudooceanicola batsensis comb. nov., Pseudooceanicola marinus comb. RT nov., Pseudooceanicola nitratireducens comb. nov., Pseudooceanicola RT nanhaiensis comb. nov., Pseudooceanicola antarcticus comb. nov., and RT Pseudooceanicola flagellatus comb. nov."; RL Antonie Van Leeuwenhoek 107:1065-1074(2015). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KGM47412.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AQQX01000011; KGM47412.1; -; Genomic_DNA. DR RefSeq; WP_043752950.1; NZ_AQQX01000011.1. DR EnsemblBacteria; KGM47412; KGM47412; ATO9_18620. DR Proteomes; UP000030004; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000030004}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000030004}. FT DOMAIN 203 373 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 424 AA; 47099 MW; 6B15F991674D09B6 CRC64; MPHDKPLTRA WVLHPELKGE DTRHAPEYAL EEAVSLAHAL PDLEVIGSGI VRLAKAIPAT LFGTGKIEEL GALLKENEVE LVLVDGPVSP KQQRNLEKKW GVKLLDRTGL ILEIFSDRAR TREGVLQVEM AALGYQRTRL VRAWTHLERQ RGGLGFVGGP GETQIEADRR AIDEQLTRLR RQLERVVKTR ELHRKARAKV PFPIVALVGY TNAGKSTLFN RLTGADVLAK DMLFATLDPT MRRVRLPDNG PEVILSDTVG FISDLPTQLV AAFRATLEEV LEADLVLHVR DISHPETEEQ AQDVLDILSD LGLAEGVPVL EVWNKVDRLG EEEGPALIAR AEREEDTYPI SAITGFGLEN LLRAVEQGLE TGHVTETISL PFDAGKSRAW LFEQGVVLEE VQTETGFDLT LRWTAKQKAQ FATL // ID A0A0A0ETM7_9GAMM Unreviewed; 435 AA. AC A0A0A0ETM7; DT 07-JAN-2015, integrated into UniProtKB/TrEMBL. DT 07-JAN-2015, sequence version 1. DT 07-JUN-2017, entry version 18. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=N792_05475 {ECO:0000313|EMBL:KGM52517.1}; OS Lysobacter concretionis Ko07 = DSM 16239. OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales; OC Xanthomonadaceae; Lysobacter. OX NCBI_TaxID=1122185 {ECO:0000313|EMBL:KGM52517.1, ECO:0000313|Proteomes:UP000030017}; RN [1] {ECO:0000313|EMBL:KGM52517.1, ECO:0000313|Proteomes:UP000030017} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Ko07 {ECO:0000313|EMBL:KGM52517.1, RC ECO:0000313|Proteomes:UP000030017}; RA Zhang S., Wang G.; RT "Genome sequencing of Lysobacter."; RL Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KGM52517.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AVPS01000003; KGM52517.1; -; Genomic_DNA. DR RefSeq; WP_036192750.1; NZ_AVPS01000003.1. DR EnsemblBacteria; KGM52517; KGM52517; N792_05475. DR Proteomes; UP000030017; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000030017}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000030017}. FT DOMAIN 199 364 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 158 192 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 435 AA; 47932 MW; 9805FCA52549BD3D CRC64; MFERSRKGES ALLIQPHAGG PPDEGQVEEF AELARSAGAT VVAVLKARID HPNAAILIGS GKLEEVQAAV AATGADLVLV NHPLSPVQER NLERILECRV VDRTGLILDI FAQRARSHEG KLQVELAQLR HMSTRLIRGW THLERQRGGS IGLRGPGETQ LETDRRLLQK RLEQLQKKLD KVEVQRDQMR RARVRSELPR IALVGYTNAG KSTLFNALTG AQAYAADQLF ATLDPTVRRI ELGGHGVVLA DTVGFVRDLP HELVAAFRST LSEAREADLL LHLVDAADPL REERIAQVDE VLAEIGAGEI PQLLVYNKID QLEQSRPRID RPAEGHPRVW LSARDGQGLE LLPEILGEML DLRRVSGTIH LPSRAGKLRA RLHELGAVRS EEPAEHGWQL QVDLSHADAE RLHAQPHGDA LHALLPPADP DHDAG // ID A0A0A0EZD2_9GAMM Unreviewed; 433 AA. AC A0A0A0EZD2; DT 07-JAN-2015, integrated into UniProtKB/TrEMBL. DT 07-JAN-2015, sequence version 1. DT 07-JUN-2017, entry version 18. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=N800_13765 {ECO:0000313|EMBL:KGM55398.1}; OS Lysobacter daejeonensis GH1-9. OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales; OC Xanthomonadaceae; Lysobacter. OX NCBI_TaxID=1385517 {ECO:0000313|EMBL:KGM55398.1, ECO:0000313|Proteomes:UP000029998}; RN [1] {ECO:0000313|EMBL:KGM55398.1, ECO:0000313|Proteomes:UP000029998} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=GH1-9 {ECO:0000313|EMBL:KGM55398.1, RC ECO:0000313|Proteomes:UP000029998}; RA Zhang S., Wang G.; RT "Genome sequencing of Lysobacter."; RL Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KGM55398.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AVPU01000005; KGM55398.1; -; Genomic_DNA. DR RefSeq; WP_036135242.1; NZ_AVPU01000005.1. DR EnsemblBacteria; KGM55398; KGM55398; N800_13765. DR Proteomes; UP000029998; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000029998}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000029998}. FT DOMAIN 200 365 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 159 193 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 433 AA; 47435 MW; 25AE88144084D510 CRC64; MFFERSRKGE HALLIQPHAG GPPDEGLLEE FTDLARSAGA TIAAVVTARI DRPNAATLIG SGKLEEIKAA VEATGADLIL VNFTLTPTQE RNLERALQRR VVDRTGLILD IFAQRAHSHE GKLQVELAQL RHMSTRLVRG WTHLERQRGG AIGLRGPGET QLELDRRMLQ ARLESLQRRL AKVEVQRTQM RRARLRSEMP RVALVGYTNA GKSTLFNALT GAEAYAADQL FATLDPTVRR IDLSGGSVTL ADTVGFVRDL PHALVAAFRS TLSESREADL LLHVIDAADP LRDERIAQVN SVLAEIGAGD IPQVLVFNKI DRIEGATPRL DQPGEGPVRV WLSARDGVGL DLLQTAMAEA LELRHVQGEV RIPPQAARLR ARLHELGAVR SEQGDEHGWR LQVDIALADA QRLFAQSHGE PLRPLLEAAG APT // ID A0A0A0J0I6_9MICO Unreviewed; 493 AA. AC A0A0A0J0I6; DT 07-JAN-2015, integrated into UniProtKB/TrEMBL. DT 07-JAN-2015, sequence version 1. DT 07-JUN-2017, entry version 18. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=N798_15925 {ECO:0000313|EMBL:KGN29101.1}; OS Knoellia flava TL1. OC Bacteria; Actinobacteria; Micrococcales; Intrasporangiaceae; Knoellia. OX NCBI_TaxID=1385518 {ECO:0000313|EMBL:KGN29101.1, ECO:0000313|Proteomes:UP000029990}; RN [1] {ECO:0000313|EMBL:KGN29101.1, ECO:0000313|Proteomes:UP000029990} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=TL1 {ECO:0000313|EMBL:KGN29101.1, RC ECO:0000313|Proteomes:UP000029990}; RA Zhu W., Wang G.; RT "The genome sequence of Knoellia flava."; RL Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KGN29101.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AVPI01000067; KGN29101.1; -; Genomic_DNA. DR RefSeq; WP_035950220.1; NZ_AVPI01000067.1. DR EnsemblBacteria; KGN29101; KGN29101; N798_15925. DR Proteomes; UP000029990; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 2. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000313|EMBL:KGN29101.1}; KW Complete proteome {ECO:0000313|Proteomes:UP000029990}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900, KW ECO:0000313|EMBL:KGN29101.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000029990}. FT DOMAIN 275 440 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 493 AA; 53779 MW; BF7FB8A287E90329 CRC64; MTERHHIFSG HADALSDDAY DDEGFVVEGE EEGDRPSALY DGDQLEREER AALRRVAGLS TELEDVTEVE YRQLRLERVV LASVWSEGTL VDAENSLREL AALAETAGAL VLEGVIQRRQ KPDTATYLGK GKAEELRDIV INEGADTVIC DTELAPSQRR ALEDVVKVKV IDRTALILDI FAQHAKSREG KAQVELAQLQ YLLPRLRGWG ESMSRQAGGQ AAGGQGMGSR GPGETKIELD RRRINSRIAK LKRDIAGMKT HRDTKRGSRR SNGIPSVAIA GYTNAGKSSI LNRLTGAGVL VQNQLFATLD PTVRRSETPD GREFTFTDTV GFVRQLPHQL VEAFRSTLEE VADSDLLLHV VDGSHPDPEG QISAVRAVLA DVDATDVLEV IVVNKADIAD PEVVDRILRH EKHAVAVSAR TGQGLDELRA LIAEELPQPD IDVDVLLPYG RGDLVSRIHD EGEILASDHV SEGTRVTARV NADLAAELTA YGV // ID A0A0A0JQT9_9MICO Unreviewed; 494 AA. AC A0A0A0JQT9; DT 07-JAN-2015, integrated into UniProtKB/TrEMBL. DT 07-JAN-2015, sequence version 1. DT 07-JUN-2017, entry version 18. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=N803_00780 {ECO:0000313|EMBL:KGN39084.1}; OS Knoellia subterranea KCTC 19937. OC Bacteria; Actinobacteria; Micrococcales; Intrasporangiaceae; Knoellia. OX NCBI_TaxID=1385521 {ECO:0000313|EMBL:KGN39084.1, ECO:0000313|Proteomes:UP000030011}; RN [1] {ECO:0000313|EMBL:KGN39084.1, ECO:0000313|Proteomes:UP000030011} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=KCTC 19937 {ECO:0000313|EMBL:KGN39084.1, RC ECO:0000313|Proteomes:UP000030011}; RA Zhu W., Wang G.; RT "The genome sequence of Knoellia subterranea."; RL Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KGN39084.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AVPK01000001; KGN39084.1; -; Genomic_DNA. DR RefSeq; WP_035901757.1; NZ_AVPK01000001.1. DR EnsemblBacteria; KGN39084; KGN39084; N803_00780. DR Proteomes; UP000030011; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 2. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000313|EMBL:KGN39084.1}; KW Complete proteome {ECO:0000313|Proteomes:UP000030011}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900, KW ECO:0000313|EMBL:KGN39084.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000030011}. FT DOMAIN 275 440 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 494 AA; 53726 MW; 49207378245E8FEB CRC64; MTARHDIFSG QAEALSDDAY DDDGYLLDGD EDGTRPSALY DGDQLEREER AALRRVAGLS TELEDVTEVE YRQLRLERVV LASVWSEGTL VDAENSLREL AALAETAGAE VLEGVIQRRQ KPDTATYLGK GKAEELRDIV ISEGADTVIA DSELAPSQRR ALEDVVKVKV IDRTALILDI FAQHAKSREG KAQVELAQLQ YLLPRLRGWG ESMSRQAGGQ AAGGQGMGSR GPGETKIELD RRRINSRIAK LKRDIAGMKT HRDTKRGSRR ANGIPSVAIA GYTNAGKSSI LNRLTGAGVL VQNQLFATLD PTVRRGETPD GREFTFTDTV GFVRALPHQL VEAFRSTLEE VAESDLLLHV VDGSHPDPEG QISAVRAVLA DVDATDVKEV IVVNKADIAD PEVVDRLLRN EKHVVAVSAR TGEGMDALVR LIADELPQPD ISVDVLLPYN RGDLVSRLHE EGEILASEHV SEGTRVTARV NADLAAELTA YKAV // ID A0A0A0L0G1_CUCSA Unreviewed; 234 AA. AC A0A0A0L0G1; DT 07-JAN-2015, integrated into UniProtKB/TrEMBL. DT 07-JAN-2015, sequence version 1. DT 16-MAR-2016, entry version 7. DE SubName: Full=GTP-binding protein hflx {ECO:0000313|EMBL:KGN53616.1}; GN ORFNames=Csa_4G090350 {ECO:0000313|EMBL:KGN53616.1}; OS Cucumis sativus (Cucumber). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae; OC Pentapetalae; rosids; fabids; Cucurbitales; Cucurbitaceae; OC Benincaseae; Cucumis. OX NCBI_TaxID=3659 {ECO:0000313|EMBL:KGN53616.1, ECO:0000313|Proteomes:UP000029981}; RN [1] {ECO:0000313|EMBL:KGN53616.1, ECO:0000313|Proteomes:UP000029981} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=19881527; DOI=10.1038/ng.475; RA Huang S., Li R., Zhang Z., Li L., Gu X., Fan W., Lucas W.J., Wang X., RA Xie B., Ni P., Ren Y., Zhu H., Li J., Lin K., Jin W., Fei Z., Li G., RA Staub J., Kilian A., van der Vossen E.A., Wu Y., Guo J., He J., RA Jia Z., Ren Y., Tian G., Lu Y., Ruan J., Qian W., Wang M., Huang Q., RA Li B., Xuan Z., Cao J., Asan null, Wu Z., Zhang J., Cai Q., Bai Y., RA Zhao B., Han Y., Li Y., Li X., Wang S., Shi Q., Liu S., Cho W.K., RA Kim J.Y., Xu Y., Heller-Uszynska K., Miao H., Cheng Z., Zhang S., RA Wu J., Yang Y., Kang H., Li M., Liang H., Ren X., Shi Z., Wen M., RA Jian M., Yang H., Zhang G., Yang Z., Chen R., Liu S., Li J., Ma L., RA Liu H., Zhou Y., Zhao J., Fang X., Li G., Fang L., Li Y., Liu D., RA Zheng H., Zhang Y., Qin N., Li Z., Yang G., Yang S., Bolund L., RA Kristiansen K., Zheng H., Li S., Zhang X., Yang H., Wang J., Sun R., RA Zhang B., Jiang S., Wang J., Du Y., Li S.; RT "The genome of the cucumber, Cucumis sativus L."; RL Nat. Genet. 41:1275-1281(2009). RN [2] {ECO:0000313|EMBL:KGN53616.1, ECO:0000313|Proteomes:UP000029981} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=19495411; DOI=10.1371/journal.pone.0005795; RA Ren Y., Zhang Z., Liu J., Staub J.E., Han Y., Cheng Z., Li X., Lu J., RA Miao H., Kang H., Xie B., Gu X., Wang X., Du Y., Jin W., Huang S.; RT "An integrated genetic and cytogenetic map of the cucumber genome."; RL PLoS ONE 4:E5795-E5795(2009). RN [3] {ECO:0000313|EMBL:KGN53616.1, ECO:0000313|Proteomes:UP000029981} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=20565788; DOI=10.1186/1471-2164-11-384; RA Guo S., Zheng Y., Joung J.G., Liu S., Zhang Z., Crasta O.R., RA Sobral B.W., Xu Y., Huang S., Fei Z.; RT "Transcriptome sequencing and comparative analysis of cucumber flowers RT with different sex types."; RL BMC Genomics 11:384-384(2010). RN [4] {ECO:0000313|EMBL:KGN53616.1, ECO:0000313|Proteomes:UP000029981} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=22047402; DOI=10.1186/1471-2164-12-540; RA Li Z., Zhang Z., Yan P., Huang S., Fei Z., Lin K.; RT "RNA-Seq improves annotation of protein-coding genes in the cucumber RT genome."; RL BMC Genomics 12:540-540(2011). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CM002925; KGN53616.1; -; Genomic_DNA. DR Proteomes; UP000029981; Chromosome 4. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF13167; GTP-bdg_N; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000029981}; KW Reference proteome {ECO:0000313|Proteomes:UP000029981}. FT DOMAIN 136 200 GTP-bdg_N. {ECO:0000259|Pfam:PF13167}. SQ SEQUENCE 234 AA; 26327 MW; F931BA95C5D31104 CRC64; MLRIISLSQP RVSPLAHYVN TVCSASTSCL LPSNSPSSKL LHSRILILSS PFSHSSKHKK EDSDDLSLFN RDLTAPPKLF VVQPRLRPYT FLQAKLNEAL CLANSLEEQR DGYFHIDFFD KDVPPYVVVQ NPSVRGARAD TYFGPGTVDT IKCHLNAAES KSEVDAIFVN ATLSGSQQRN LEWAWNKPVL DRVGLIIEIF NAHAYTKEAK LQVFFMVPIK HIIALLLLDY TYSH // ID A0A0A0LH30_CUCSA Unreviewed; 548 AA. AC A0A0A0LH30; DT 07-JAN-2015, integrated into UniProtKB/TrEMBL. DT 07-JAN-2015, sequence version 1. DT 07-JUN-2017, entry version 13. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:KGN59997.1}; GN ORFNames=Csa_3G860330 {ECO:0000313|EMBL:KGN59997.1}; OS Cucumis sativus (Cucumber). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae; OC Pentapetalae; rosids; fabids; Cucurbitales; Cucurbitaceae; OC Benincaseae; Cucumis. OX NCBI_TaxID=3659 {ECO:0000313|EMBL:KGN59997.1, ECO:0000313|Proteomes:UP000029981}; RN [1] {ECO:0000313|EMBL:KGN59997.1, ECO:0000313|Proteomes:UP000029981} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=19881527; DOI=10.1038/ng.475; RA Huang S., Li R., Zhang Z., Li L., Gu X., Fan W., Lucas W.J., Wang X., RA Xie B., Ni P., Ren Y., Zhu H., Li J., Lin K., Jin W., Fei Z., Li G., RA Staub J., Kilian A., van der Vossen E.A., Wu Y., Guo J., He J., RA Jia Z., Ren Y., Tian G., Lu Y., Ruan J., Qian W., Wang M., Huang Q., RA Li B., Xuan Z., Cao J., Asan null, Wu Z., Zhang J., Cai Q., Bai Y., RA Zhao B., Han Y., Li Y., Li X., Wang S., Shi Q., Liu S., Cho W.K., RA Kim J.Y., Xu Y., Heller-Uszynska K., Miao H., Cheng Z., Zhang S., RA Wu J., Yang Y., Kang H., Li M., Liang H., Ren X., Shi Z., Wen M., RA Jian M., Yang H., Zhang G., Yang Z., Chen R., Liu S., Li J., Ma L., RA Liu H., Zhou Y., Zhao J., Fang X., Li G., Fang L., Li Y., Liu D., RA Zheng H., Zhang Y., Qin N., Li Z., Yang G., Yang S., Bolund L., RA Kristiansen K., Zheng H., Li S., Zhang X., Yang H., Wang J., Sun R., RA Zhang B., Jiang S., Wang J., Du Y., Li S.; RT "The genome of the cucumber, Cucumis sativus L."; RL Nat. Genet. 41:1275-1281(2009). RN [2] {ECO:0000313|EMBL:KGN59997.1, ECO:0000313|Proteomes:UP000029981} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=19495411; DOI=10.1371/journal.pone.0005795; RA Ren Y., Zhang Z., Liu J., Staub J.E., Han Y., Cheng Z., Li X., Lu J., RA Miao H., Kang H., Xie B., Gu X., Wang X., Du Y., Jin W., Huang S.; RT "An integrated genetic and cytogenetic map of the cucumber genome."; RL PLoS ONE 4:E5795-E5795(2009). RN [3] {ECO:0000313|EMBL:KGN59997.1, ECO:0000313|Proteomes:UP000029981} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=20565788; DOI=10.1186/1471-2164-11-384; RA Guo S., Zheng Y., Joung J.G., Liu S., Zhang Z., Crasta O.R., RA Sobral B.W., Xu Y., Huang S., Fei Z.; RT "Transcriptome sequencing and comparative analysis of cucumber flowers RT with different sex types."; RL BMC Genomics 11:384-384(2010). RN [4] {ECO:0000313|EMBL:KGN59997.1, ECO:0000313|Proteomes:UP000029981} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=22047402; DOI=10.1186/1471-2164-12-540; RA Li Z., Zhang Z., Yan P., Huang S., Fei Z., Lin K.; RT "RNA-Seq improves annotation of protein-coding genes in the cucumber RT genome."; RL BMC Genomics 12:540-540(2011). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CM002924; KGN59997.1; -; Genomic_DNA. DR RefSeq; XP_004147849.1; XM_004147801.2. DR GeneID; 101219907; -. DR KEGG; csv:101219907; -. DR KO; K03665; -. DR Proteomes; UP000029981; Chromosome 3. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000029981}; KW Reference proteome {ECO:0000313|Proteomes:UP000029981}. FT DOMAIN 325 491 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 548 AA; 60677 MW; 9CD1EC01C6F69CA3 CRC64; MTSASLAGFF PRPSIREPCS PCTSSNNNRV FFPFISRKDT RNSICTLASA FQQEPAVVSS DNLPFHGSFI KPIQEVGGTG DVDEPIRGVS STEPEPKSQL PSRVKKKTQE DGDSIEGRFK LRNGREVFEE KAYLVGVERK GDVAQLFSID ESLKELAQLA DTAGLKVVGS TYQKLASPNP RTYIGSGKVA EIKSAIHALG IETVIFDDEL SAGQLRNLEK SFGGDVRVCD RTALILDIFN QRAATHEASL QVALAQMEYQ LPRLTKMWTH LERQAGGQVK GMGEKQIEVD KRILRTQIGV LRKELESVRV HRKQYRSRRF SVPVPVVSLV GYTNAGKSTL LNHLTGAEVL AEDRLFATLD PTTRRVQMKN GNEFLLTDTV GFIQKLPTML VAAFRATLEE ISESSLLVHV VDISHPLAEQ QIEAVDKVLS ELDVSSIPKL MVWNKVDKVT DPQHIRLEAD KRGDVVCVSA LSGDGLDKFC DAVQSKLKDS MVWIEALIPF DRGELLSTVH QVGVVEKAEY TENGTLVQAH VPLRFSRLLT PMRQLCIT // ID A0A0A0M5V9_9LACT Unreviewed; 437 AA. AC A0A0A0M5V9; DT 07-JAN-2015, integrated into UniProtKB/TrEMBL. DT 07-JAN-2015, sequence version 1. DT 12-APR-2017, entry version 16. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=Q757_00305 {ECO:0000313|EMBL:KGO32559.1}; OS Oenococcus alcoholitolerans. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Leuconostocaceae; OC Oenococcus. OX NCBI_TaxID=931074 {ECO:0000313|EMBL:KGO32559.1, ECO:0000313|Proteomes:UP000030023}; RN [1] {ECO:0000313|EMBL:KGO32559.1, ECO:0000313|Proteomes:UP000030023} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=UFRJ-M7.2.18 {ECO:0000313|EMBL:KGO32559.1, RC ECO:0000313|Proteomes:UP000030023}; RX PubMed=25315101; DOI=10.1007/s10482-014-0296-z; RA Badotti F., Moreira A.P., Tonon L.A., de Lucena B.T., Gomes Fde C., RA Kruger R., Thompson C.C., de Morais M.A.Jr., Rosa C.A., Thompson F.L.; RT "Oenococcus alcoholitolerans sp. nov., a lactic acid bacteria isolated RT from cachaca and ethanol fermentation processes."; RL Antonie Van Leeuwenhoek 106:1259-1267(2014). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KGO32559.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AXCV01000005; KGO32559.1; -; Genomic_DNA. DR EnsemblBacteria; KGO32559; KGO32559; Q757_00305. DR Proteomes; UP000030023; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000030023}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000030023}. FT DOMAIN 211 383 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 170 197 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 437 AA; 49050 MW; C8653A705451770F CRC64; MTTKINETKQ AAVKAVIIAV ENQQNEEIFD YKIEETKHLA EANKIKIVGS LNQKINRINS ATYFGKGKIQ QLKELVASSD ADLVISQDDL TATQIRNIEK ELSGDVHVVD RTAVILDIFA ARAKTKIAKL QVRLAQKQYQ LPRLHTSLAK ELDQQAGAGG ASFTSRGSGE TKLELNRRTL EAQISQIKKE LNDLLEAASI QSKQRQRSGL RRVAFVGYTN AGKSSWMNQM IKHFSDKVAS NADKQVFEKN MLFATLDSTV RSIRLRNNRR FLLSDTVGFV SDLPHDLVAS FKSTLDEAKN ADLLVQIVDI SDPNYHAMID TTKETLAEIG ADQIPMIMIF NKADLAGIEY PQQEGENLIA SSFDERSVEE FAKVIDQKLF ADFKKVRLLL PFDQGGLLNR LSKENDILEQ RFTEAGTEIM VELAPEQLQR YKSFLKA // ID A0A0A0M7X7_9GAMM Unreviewed; 428 AA. AC A0A0A0M7X7; DT 07-JAN-2015, integrated into UniProtKB/TrEMBL. DT 07-JAN-2015, sequence version 1. DT 07-JUN-2017, entry version 18. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=N791_11980 {ECO:0000313|EMBL:KGO98319.1}; OS Lysobacter defluvii IMMIB APB-9 = DSM 18482. OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales; OC Xanthomonadaceae; Lysobacter. OX NCBI_TaxID=1385515 {ECO:0000313|EMBL:KGO98319.1, ECO:0000313|Proteomes:UP000030003}; RN [1] {ECO:0000313|EMBL:KGO98319.1, ECO:0000313|Proteomes:UP000030003} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=IMMIB APB-9 {ECO:0000313|EMBL:KGO98319.1, RC ECO:0000313|Proteomes:UP000030003}; RA Wang Q., Wang G.; RT "Genomic analysis of Lysobacter defluvii."; RL Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KGO98319.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AVBH01000097; KGO98319.1; -; Genomic_DNA. DR RefSeq; WP_027070228.1; NZ_AVBH01000097.1. DR EnsemblBacteria; KGO98319; KGO98319; N791_11980. DR Proteomes; UP000030003; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000030003}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000030003}. FT DOMAIN 199 364 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 158 192 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 428 AA; 46698 MW; 72F6C0FD250508EE CRC64; MFERSRKGEH ALLIQPHAGG PPDPDVLEEF TELARSAGAS IAAVVPARID RPTAATLIGS GKLEEVIAAA DASGADLVLV NHPLSPVQER NLEKLLQRRV VDRTGLILDI FAQRAHSHEG KLQVELAQLR HLATRLVRGW THLERQRGGS IGLRGPGETQ LETDRRLLQK RLEQLQKRLD KVEVQRAQMR RARVRSELPR VALVGYTNAG KSTLFNTLTG AGAYAADQLF ATLDPTVRRV DLAAGAVVLA DTVGFVRDLP HELVAAFRST LSEAREADLL LHVVDASDPH RDERIAQVDQ VLADIGAGEL PQLLVFNKID RLEDARPRID RPAEGHPRAW ISARDGEGME LLATAIGEVL ELRNVSGTIA LPSRAGRLRA RLHELGAVRG EQACEDGWRI QVELAEAEAR RLAAGPEGHA LAPLLPTP // ID A0A0A1AWF3_9GAMM Unreviewed; 426 AA. AC A0A0A1AWF3; DT 04-FEB-2015, integrated into UniProtKB/TrEMBL. DT 04-FEB-2015, sequence version 1. DT 30-AUG-2017, entry version 20. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=PSNIH2_00540 {ECO:0000313|EMBL:AIX72404.1}; OS Pantoea sp. PSNIH2. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; OC Erwiniaceae; Pantoea. OX NCBI_TaxID=1484157 {ECO:0000313|EMBL:AIX72404.1, ECO:0000313|Proteomes:UP000030310}; RN [1] {ECO:0000313|EMBL:AIX72404.1, ECO:0000313|Proteomes:UP000030310} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=PSNIH2 {ECO:0000313|EMBL:AIX72404.1}; RX PubMed=25232178; RG NISC Comparative Sequencing Program; RA Conlan S., Thomas P.J., Deming C., Park M., Lau A.F., Dekker J.P., RA Snitkin E.S., Clark T.A., Luong K., Song Y., Tsai Y.C., Boitano M., RA Dayal J., Brooks S.Y., Schmidt B., Young A.C., Thomas J.W., RA Bouffard G.G., Blakesley R.W., Mullikin J.C., Korlach J., RA Henderson D.K., Frank K.M., Palmore T.N., Segre J.A.; RT "Single-molecule sequencing to track plasmid diversity of hospital- RT associated carbapenemase-producing Enterobacteriaceae."; RL Sci. Transl. Med. 6:254RA126-254RA126(2014). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP009866; AIX72404.1; -; Genomic_DNA. DR RefSeq; WP_038623883.1; NZ_CP009866.1. DR EnsemblBacteria; AIX72404; AIX72404; PSNIH2_00540. DR KEGG; panp:PSNIH2_00540; -. DR KO; K03665; -. DR Proteomes; UP000030310; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000030310}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000030310}. FT DOMAIN 198 365 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 426 AA; 47991 MW; 2A20BD5FF808A6F0 CRC64; MFDRYDAGEQ AILVHIWFSQ DKETEDLQEF ETLVSSSGVE ALRVITGSRK APHPKYFVGE GKAVEIAEAV KATGASVVIF DHALSPAQER NLERLCECRV IDRTGLILDI FAQRARTHEG KLQVELAQLR HLATRLVRGW THLERQKGGI GLRGPGETQL ETDRRLLRNR ISQILSRLER VEKQRDQGRQ ARAKADIPTV SLVGYTNAGK STLFNSVTSA DVYAADQLFA TLDPTLRRID VSDVGEVVLA DTVGFIRHLP HDLVAAFKAT LQETRQAALL LHIIDAADVR MDENIEAVET VLEEIEADEI PMLQVMNKID MLDGFEPRID RNDENQPVRV WLSAQSGAGL PLLFQALTER LSGEIAQYEL CLPPEAGRLR SRFYQLQAIE KEWNEEDGSV GLMIRLPIVD WRRLCKQEPT LVDYIV // ID A0A0A1D362_9MICC Unreviewed; 551 AA. AC A0A0A1D362; DT 04-FEB-2015, integrated into UniProtKB/TrEMBL. DT 04-FEB-2015, sequence version 1. DT 10-MAY-2017, entry version 19. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=ART_4301 {ECO:0000313|EMBL:AIY03900.1}; OS Arthrobacter sp. PAMC 25486. OC Bacteria; Actinobacteria; Micrococcales; Micrococcaceae; Arthrobacter. OX NCBI_TaxID=1494608 {ECO:0000313|EMBL:AIY03900.1, ECO:0000313|Proteomes:UP000030301}; RN [1] {ECO:0000313|EMBL:AIY03900.1, ECO:0000313|Proteomes:UP000030301} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=PAMC25486 {ECO:0000313|EMBL:AIY03900.1, RC ECO:0000313|Proteomes:UP000030301}; RA Jung J.-H., Joe M.-H., Cho Y.-J., Lee S.G., Han S.J., Lim S., RA Choi J.-I.; RT "Complete genome sequence of Arthrobacter sp. PAMC25486 isolated from RT the Arctic."; RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP007595; AIY03900.1; -; Genomic_DNA. DR EnsemblBacteria; AIY03900; AIY03900; ART_4301. DR KEGG; arm:ART_4301; -. DR KO; K03665; -. DR Proteomes; UP000030301; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000030301}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000030301}. FT DOMAIN 330 495 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 551 AA; 59496 MW; AE209DF7571B3550 CRC64; MSNASAHHGS DDKSQPKSGG TTPHGPDESA QELSAAEIEA VIDRILAKDA AAGHAVRAES ELEEQDPYEG TPTARPLAGS AQAVSSLDFQ HSRFDGDQSE LADRKALRRQ ASLSTELEDV SEVEYRQLRL ERVVLAGLWS GGTMADAENS LRELAALAET AGSEVLDGLV QRRAKPDPAT FLGQGKAQEL KEIVHATGAD TVIIDGDLSP SQRRTLEEVV KVKVIDRTAL ILDIFAQHAQ SREGRAQVEL AQMEYLLPRL RGWGESMSRQ AGGRVGAAGG GIGSRGPGET KMELDRRKIR NRMAKLRREI AAMAPARETK RANRKRNSVP SVAIAGYTNA GKSSLLNRLT DAGVLVENAL FATLDPTVRK TETADGLGYT LVDTVGFVRA LPTQLVEAFR STLEEVADAD LILHIVDASH PDPEGQISAV RSVFAEVGAL QIPEIIILNK ADIADPFVVE RLRQREPRTV VVSARTGQGI QELLDAISEG IPHPSVLLTL MIPYDRGDVL NKLHRSDAEI VSLEHGEHGT LASVRVREDL AAEVEPFVHH A // ID A0A0A1DIA9_NOCSI Unreviewed; 513 AA. AC A0A0A1DIA9; DT 04-FEB-2015, integrated into UniProtKB/TrEMBL. DT 04-FEB-2015, sequence version 1. DT 05-JUL-2017, entry version 20. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=KR76_05735 {ECO:0000313|EMBL:AIY16382.1}, GN SAMN05421671_4780 {ECO:0000313|EMBL:SFN03386.1}; OS Nocardioides simplex (Arthrobacter simplex). OC Bacteria; Actinobacteria; Propionibacteriales; Nocardioidaceae; OC Pimelobacter. OX NCBI_TaxID=2045 {ECO:0000313|EMBL:AIY16382.1, ECO:0000313|Proteomes:UP000030300}; RN [1] {ECO:0000313|EMBL:AIY16382.1, ECO:0000313|Proteomes:UP000030300} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=VKM Ac-2033D {ECO:0000313|EMBL:AIY16382.1, RC ECO:0000313|Proteomes:UP000030300}; RX PubMed=25573942; RA Shtratnikova V.Y., Schelkunov M.I., Pekov Y.A., Fokina V.V., RA Logacheva M.D., Sokolov S.L., Bragin E.Y., Ashapkin V.V., Donova M.V.; RT "Complete Genome Sequence of Steroid-Transforming Nocardioides simplex RT VKM Ac-2033D."; RL Genome Announc. 3:0-0(2015). RN [2] {ECO:0000313|EMBL:SFN03386.1, ECO:0000313|Proteomes:UP000183394} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 6946 {ECO:0000313|EMBL:SFN03386.1, RC ECO:0000313|Proteomes:UP000183394}; RA de Groot N.N.; RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP009896; AIY16382.1; -; Genomic_DNA. DR EMBL; FOUK01000006; SFN03386.1; -; Genomic_DNA. DR EnsemblBacteria; AIY16382; AIY16382; KR76_05735. DR KEGG; psim:KR76_05735; -. DR KO; K03665; -. DR Proteomes; UP000030300; Chromosome. DR Proteomes; UP000183394; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 2. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000030300}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000030300}. FT DOMAIN 295 460 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 254 288 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 513 AA; 55515 MW; F9C489CF784214E2 CRC64; MTNHAEDFSL AAALRATEGW DDPDDLTDPT DLTDADDAAE DDGWESGYAD ADPEDGDDPT TGDLDLVERH ELRRVAGLRT ELEDITEVEY RQLRLERVVL VGVWTEGTVA DVENAMAELA LLAETAGSEV LDAIYQRRQS PDPATYIGRG KVEGLREIVQ ATGADTVICD GELAPSQLRN LEDKVKVKVV DRTALILDIF AQHAKSKEGQ AQVELAQLSY MKQRLRGWGG NLSRQAGGRV GADGGGIGGR GPGETKIETD RRRINDKIAK LRRELKAMKG TRDTKRQERR RNEIPSVAIA GYTNAGKSSL LNRLTGAGVL VEDALFATLD PTTRRTTTGD GRVYTMSDTV GFVRHLPHQL VEAFRSTLEE VADADLIVHV VDGSHPDPEG QLSAVREVLA DIEAGQVPEL VIINKVDAAD PLVVDRLLRR EPHSVAVSAR TGEGIAAAIA AIEADLPRPQ VEFTALVPYA RGDLIDRIHK DGEIGSLEHT ADGTRVTGRA TEALAGELAV YAV // ID A0A0A1FG76_9BURK Unreviewed; 367 AA. AC A0A0A1FG76; DT 04-FEB-2015, integrated into UniProtKB/TrEMBL. DT 04-FEB-2015, sequence version 1. DT 12-APR-2017, entry version 15. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:AIY41857.1}; GN ORFNames=LT85_2699 {ECO:0000313|EMBL:AIY41857.1}; OS Collimonas arenae. OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Oxalobacteraceae; Collimonas. OX NCBI_TaxID=279058 {ECO:0000313|EMBL:AIY41857.1, ECO:0000313|Proteomes:UP000030302}; RN [1] {ECO:0000313|EMBL:AIY41857.1, ECO:0000313|Proteomes:UP000030302} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Cal35 {ECO:0000313|EMBL:AIY41857.1, RC ECO:0000313|Proteomes:UP000030302}; RA Uroz S., Tech J.J., Sawaya N.A., Frey-Klett P., Leveau J.H.J.; RT "Structure and function of bacterial communities in ageing soils: RT insights from the Mendocino ecological staircase."; RL Soil Biol. Biochem. 69:265-274(2014). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP009962; AIY41857.1; -; Genomic_DNA. DR EnsemblBacteria; AIY41857; AIY41857; LT85_2699. DR KEGG; care:LT85_2699; -. DR KO; K03665; -. DR Proteomes; UP000030302; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000030302}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}. FT DOMAIN 183 349 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 149 176 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 367 AA; 40250 MW; 3A4688434A9F2F88 CRC64; MDFGKGDFAA SLEELSLLAK SAGALPLVTI TGKRSSPDAA LFVGSGKAQE IADAVFDDEL EIVIFNHALS PAQQRNLERV LKVRVLDRTS LILDIFAQRA KSHEGKVQVE LAQLQHLATR LIRGWTHLER QKGGIGLRGP GETQLETDRR LLGDRVKALR ARLDKLHKQH ATQRRARGRS ATISISLVGY TNAGKSTLFN ALAKAGVYAA DQLFATLDTT SRRVYLGEAG SVVISDTVGF IRELPHQLVA AFRATLEETI HADLLLHVVD AASPARMEQI EQVNLVLKEI GADHIPQILV WNKIDVAELE PSVERDEYDK IQRVFISAQK GIGLDLLRQA ITEFVTQNPT APAYSVIPAA DLESNQI // ID A0A0A1FRG4_9MYCO Unreviewed; 469 AA. AC A0A0A1FRG4; DT 04-FEB-2015, integrated into UniProtKB/TrEMBL. DT 04-FEB-2015, sequence version 1. DT 07-JUN-2017, entry version 19. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=G155_12805 {ECO:0000313|EMBL:AIY46315.1}; OS Mycobacterium sp. VKM Ac-1817D. OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae; OC Mycobacterium. OX NCBI_TaxID=1273687 {ECO:0000313|EMBL:AIY46315.1, ECO:0000313|Proteomes:UP000030340}; RN [1] {ECO:0000313|EMBL:AIY46315.1, ECO:0000313|Proteomes:UP000030340} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=VKM Ac-1817D {ECO:0000313|EMBL:AIY46315.1, RC ECO:0000313|Proteomes:UP000030340}; RX PubMed=23474435; DOI=10.1016/j.jsbmb.2013.02.016; RA Bragin E.Y., Shtratnikova V.Y., Dovbnya D.V., Schelkunov M.I., RA Pekov Y.A., Malakho S.G., Egorova O.V., Ivashina T.V., Sokolov S.L., RA Ashapkin V.V., Donova M.V.; RT "Comparative analysis of genes encoding key steroid core oxidation RT enzymes in fast-growing Mycobacterium spp. strains."; RL J. Steroid Biochem. Mol. Biol. 138:41-53(2013). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP009914; AIY46315.1; -; Genomic_DNA. DR RefSeq; WP_003880560.1; NZ_CP009914.1. DR EnsemblBacteria; AIY46315; AIY46315; G155_12805. DR KEGG; myv:G155_12805; -. DR KO; K03665; -. DR Proteomes; UP000030340; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000030340}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000030340}. FT DOMAIN 246 415 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 205 239 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 469 AA; 50649 MW; 59702B1BA70E86B8 CRC64; MTHPEHPVTP STGELALEDR ASLRRVAGLS TELTDVTEVE YRQLRLERVV LVGVWTEGSA ADADASLTEL AALAETAGSE VLEGLVQRRD KPDPSTYIGS GKAQELREIV LATGADTVIC DGELSPAQLN SLEKVVKVKV IDRTALILDI FAQHATSREG KAQVSLAQME YMLPRLRGWG ESMSRQAGGR AGGAGGGVGT RGPGETKIET DRRRIRERMS KLRREIREMK KIRDTQRSRR LSSDAASVAI VGYTNAGKSS LLNALTGAGV LVENALFATL EPTTRRGEFD DGRPFVLTDT VGFVRHLPTQ LVEAFRSTLE EVVDADLLVH VVDGSDEHPL AQVNAVRQVV NDVVAEYDIA PPPELLVVNK IDAATDLSLA ALRRALPDAV FVSAQTGDGL DRLRARMAEM IPPTDATVDV TIPYDRGDLV ARVHADGRVD ATEHTAEGTR IKARVPMALA ASLDEFGTF // ID A0A0A1GZI2_9LACO Unreviewed; 429 AA. AC A0A0A1GZI2; DT 04-FEB-2015, integrated into UniProtKB/TrEMBL. DT 04-FEB-2015, sequence version 1. DT 07-JUN-2017, entry version 23. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=LOOC260_119070 {ECO:0000313|EMBL:BAP86413.1}; OS Lactobacillus hokkaidonensis JCM 18461. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; OC Lactobacillus. OX NCBI_TaxID=1291742 {ECO:0000313|EMBL:BAP86413.1, ECO:0000313|Proteomes:UP000031620}; RN [1] {ECO:0000313|EMBL:BAP86413.1, ECO:0000313|Proteomes:UP000031620} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=LOOC260 {ECO:0000313|EMBL:BAP86413.1, RC ECO:0000313|Proteomes:UP000031620}; RA Tanizawa Y., Tohno M., Kaminuma E., Nakamura Y., Arita M.; RT "Complete genome sequence and analysis of Lactobacillus hokkaidonensis RT LOOC260T."; RL Submitted (NOV-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AP014680; BAP86413.1; -; Genomic_DNA. DR RefSeq; WP_041094467.1; NZ_AP014680.1. DR EnsemblBacteria; BAP86413; BAP86413; LOOC260_119070. DR KEGG; lho:LOOC260_119070; -. DR KO; K03665; -. DR Proteomes; UP000031620; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000031620}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}. FT DOMAIN 202 371 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 429 AA; 47991 MW; 32E9D3C6B2AF7069 CRC64; MANVEATRPV IIAGLNNNQA NFDYSMDELK NLVIANNMTA KETMIQNLER PNPATYFGKG KVEELAQLAA AQEVDTVVVN GELSPSQIRN LEEQAKIRIM DRTALILEIF AQRAQTKEAK LQVQIAQLRY RLPRLRTSVN EQLDQQTGAG GGSFTNRGAG ETKLEMNRRT IKNSISHLRG ELAEIDKSAV TRRAQRDKND IPTAALVGYT NAGKSTIMNS LIKMFGIDDE KQVFEKDMLF ATLDTSVRQL TLPDNKQFLL SDTVGFVSQL PTHLVEAFKS TLAEAAQADV LIQVIDYSDP HYKEMMQTTA DTLDEIGIKD IPMINVFNKA DKLTIDYPAL EGDDQIVLSA KDPKSLEMLV DLIRQHLFKD YVTADLLIPF SDGDVVSFLN DAANIIKTEY VENGTKLTVE LSKVDLQRFK KYIVLKKDE // ID A0A0A1H4H6_9BURK Unreviewed; 388 AA. AC A0A0A1H4H6; DT 04-FEB-2015, integrated into UniProtKB/TrEMBL. DT 04-FEB-2015, sequence version 1. DT 07-JUN-2017, entry version 18. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=E1O_10040 {ECO:0000313|EMBL:BAP88135.1}; OS Burkholderiales bacterium GJ-E10. OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales. OX NCBI_TaxID=1469502 {ECO:0000313|EMBL:BAP88135.1, ECO:0000313|Proteomes:UP000031649}; RN [1] {ECO:0000313|EMBL:BAP88135.1, ECO:0000313|Proteomes:UP000031649} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=GJ-E10 {ECO:0000313|EMBL:BAP88135.1, RC ECO:0000313|Proteomes:UP000031649}; RA Fukushima J., Tojo F., Asano R., Kobayashi Y., Shimura Y., Okano K., RA Miyata N.; RT "Complete Genome Sequence of the Unclassified Iron-Oxidizing, RT Chemolithoautotrophic Burkholderiales bacterium GJ-E10 Isolated from RT Acid River."; RL Submitted (NOV-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AP014683; BAP88135.1; -; Genomic_DNA. DR RefSeq; WP_045467234.1; NZ_AP014683.1. DR EnsemblBacteria; BAP88135; BAP88135; E1O_10040. DR KEGG; bbag:E1O_10040; -. DR KO; K03665; -. DR Proteomes; UP000031649; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000031649}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000031649}. FT DOMAIN 194 360 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 388 AA; 42345 MW; EC9D72E2780AA62F CRC64; MPRAFLVQVA LQGAACDDDA LEEFGLLTES SGMTVAGTMR ARRDRPDPAY YLGSGKVEAL REEIAAAGPV DAVLIDAQLS PVQQRNLERE LGVAVLDRTG LILDIFARRA QSREGKLQVE LAQLEYLSTR LVRGWTHLER QRGGIGLRGG PGEKQIELDR RMIGVRVKQL RDKLRTLERQ RGTQRRARER GGVFRVSLVG YTNAGKSTLF NALTQAHAYC ADQLFATLDT TSRRCHIADG KSIVLSDTVG FVRALPHSLV AAFRSTLDEA VHADLLLHVV DAAGPARADQ MRNVDEVLKE IGADAVPRLI VHNKIDRVGR AAGVDRDACG RIGAVWLSAR TGEGLGLLRE AIAERMEEEA VRSARISDPA ETSAYSFHDA PDAFPDAA // ID A0A0A1I2H5_9PSED Unreviewed; 438 AA. AC A0A0A1I2H5; DT 04-FEB-2015, integrated into UniProtKB/TrEMBL. DT 04-FEB-2015, sequence version 1. DT 30-AUG-2017, entry version 24. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=BN844_4952 {ECO:0000313|EMBL:CDF96497.1}; OS Pseudomonas sp. SHC52. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=984195 {ECO:0000313|EMBL:CDF96497.1, ECO:0000313|Proteomes:UP000031550}; RN [1] {ECO:0000313|EMBL:CDF96497.1, ECO:0000313|Proteomes:UP000031550} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SHC52 {ECO:0000313|EMBL:CDF96497.1, RC ECO:0000313|Proteomes:UP000031550}; RA Van der Voort M., Mendes R., Raaijmakers J.M.; RT "Genome mining of the rhizosphere bacterium Pseudomonas sp. SH-C52."; RL Submitted (MAY-2013) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:CDF96497.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CBLV010000327; CDF96497.1; -; Genomic_DNA. DR RefSeq; WP_041024055.1; NZ_CBLV010000327.1. DR EnsemblBacteria; CDF96497; CDF96497; BN844_4952. DR Proteomes; UP000031550; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000031550}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}. FT DOMAIN 199 366 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 438 AA; 49638 MW; 83359FD882315246 CRC64; MFFERHGGGE RAILVHLDGQ DPEAREDPQE FQELALSAGA ETVAFFNVPR HRPTAKFLIG SGKVEELRDL VKSEEADLVI FNHILTPSQE RNLERVFECR VIDRTGLILD IFAQRARTHE GKLQVELAQL EHMSTRLVRG WTHLERQKGG IGLRGPGETQ LETDRRLLRI RLRQIKGRLE KVRSQREQSR RGRKRADIPT VSLVGYTNAG KSTLFNNVTQ SDVYAADQLF ATLDPTLRRL DLDDLGPIVL ADTVGFIRHL PHKLVEAFRA TLEESSNSDL LLHVIDAAEP DRMLQIEQVM VVLGEIGAQD LPILEVYNKL DLLEGVEPQI QRDADGKPQR VWLSARDGTG LELLEQAVAE LLGSDLFVGT LKLPQRFARL RAQFFELGAV QKEEHDEEGT CLLAVRLPRS ELNRLGRXRL VSREGLKPME FIEQHTLQ // ID A0A0A1MER0_9BACI Unreviewed; 413 AA. AC A0A0A1MER0; DT 04-FEB-2015, integrated into UniProtKB/TrEMBL. DT 04-FEB-2015, sequence version 1. DT 07-JUN-2017, entry version 17. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:CEI83835.1}; GN ORFNames=BN997_03756 {ECO:0000313|EMBL:CEI83835.1}; OS Oceanobacillus oncorhynchi. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; OC Oceanobacillus. OX NCBI_TaxID=545501 {ECO:0000313|EMBL:CEI83835.1, ECO:0000313|Proteomes:UP000040453}; RN [1] {ECO:0000313|EMBL:CEI83835.1, ECO:0000313|Proteomes:UP000040453} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Oc5 {ECO:0000313|EMBL:CEI83835.1, RC ECO:0000313|Proteomes:UP000040453}; RA Urmite Genomes Urmite Genomes; RL Submitted (NOV-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CDGG01000001; CEI83835.1; -; Genomic_DNA. DR RefSeq; WP_042534301.1; NZ_CDGG01000001.1. DR EnsemblBacteria; CEI83835; CEI83835; BN997_03756. DR Proteomes; UP000040453; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000040453}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000040453}. FT DOMAIN 196 358 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 413 AA; 46926 MW; 5519B72BD59D42C4 CRC64; MTVENVLVIA VNQSERSEPQ FDSSLDELVS LCKTAGGQVQ DVITQNRERI HPATYIGEGK LQEVAQIIRA EGIDLVVANN ELSAGQVRNL ADTLDVRVLD RSQLILDIFA MRAQTKEGKL QVELAQLEYL LPRLHGQGAN LSRLGGGIGT RGPGETKLET DRRHIERRIY DIKRRLQLVV KQRDQYRKRR RSNDVFQIAI VGYTNAGKST IFNRLTNSHS LEEDQLFATL DPLTRRIQFP SGLKSLITDT VGFIQDLPTA LIAAFKSTLE EVTEADFLLH VVDISDPDLL QQQETVRKLL QELDAGHIPV LTVYNKKDQL EADFFLANQF PNIQISALEE EDLHALLIKM EEVLKEEWDL FDIVLDSSEG DLLYQLQSAA LVVKKELLEE TNQFHVQGYV RKNHPFHRFV EEK // ID A0A0A1VLC8_9BURK Unreviewed; 378 AA. AC A0A0A1VLC8; DT 04-FEB-2015, integrated into UniProtKB/TrEMBL. DT 04-FEB-2015, sequence version 1. DT 12-APR-2017, entry version 16. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=AVS7_03981 {ECO:0000313|EMBL:GAD24221.1}; OS Acidovorax sp. MR-S7. OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Comamonadaceae; Acidovorax. OX NCBI_TaxID=1268622 {ECO:0000313|EMBL:GAD24221.1, ECO:0000313|Proteomes:UP000030646}; RN [1] {ECO:0000313|EMBL:GAD24221.1, ECO:0000313|Proteomes:UP000030646} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MR-S7 {ECO:0000313|EMBL:GAD24221.1, RC ECO:0000313|Proteomes:UP000030646}; RA Miura T., Kusada H., Kamagata Y., Hanada S., Kimura N.; RT "Genome Sequence of the Multiple-beta-Lactam-Antibiotic-Resistant RT Bacterium Acidovorax sp. Strain MR-S7."; RL Genome Announc. 1:e00412-13(2013). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; DF238983; GAD24221.1; -; Genomic_DNA. DR EnsemblBacteria; GAD24221; GAD24221; AVS7_03981. DR Proteomes; UP000030646; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000030646}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000030646}. FT DOMAIN 188 361 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 378 AA; 41514 MW; 31CB59F5AC91DE51 CRC64; MLVGVDFGAP HFDAELEELG LLAQTAGLAP VARLTCKRKA PDAALFVGSG KADEIRTLAQ MHGAKEVLFD QALSPAQQRN LERHLQLPVN DRTLLILEIF AQRARSHEGK LQVELARLQY LSTRLVRRWS HLERQRGGIG TRGGPGETQI ELDRRMIGEA IKRTRERLVK VKRQRATQRK QRERRDTFNI SLVGYTNAGK STLFNALVKA RAYAADQLFA TLDTTTRQLY LGELAGSVSL SDTVGFIRDL PHGLVDAFQA TLQEAVDADL LLHVVDAANP GYPEQIAQVQ HVLAEIGASD IPQILVFNKL DAMPADVRPV AVQDVYELDG RQVPRIFVSA RQGDGLAALR EQLASMVQAA SQDAMTPNGT AELPAPSD // ID A0A0A1YNJ2_9PSED Unreviewed; 433 AA. AC A0A0A1YNJ2; DT 04-FEB-2015, integrated into UniProtKB/TrEMBL. DT 04-FEB-2015, sequence version 1. DT 30-AUG-2017, entry version 20. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=TMS3_0105955 {ECO:0000313|EMBL:KFX71467.1}; OS Pseudomonas taeanensis MS-3. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=1395571 {ECO:0000313|EMBL:KFX71467.1, ECO:0000313|Proteomes:UP000030063}; RN [1] {ECO:0000313|EMBL:KFX71467.1, ECO:0000313|Proteomes:UP000030063} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MS-3 {ECO:0000313|EMBL:KFX71467.1, RC ECO:0000313|Proteomes:UP000030063}; RX PubMed=24407626; RA Lee S.Y., Kim S.H., Lee D.G., Shin S., Yun S.H., Choi C.W., RA Chung Y.H., Choi J.S., Kahng H.Y., Kim S.I.; RT "Draft Genome Sequence of Petroleum Oil-Degrading Marine Bacterium RT Pseudomonas taeanensis Strain MS-3, Isolated from a Crude Oil- RT Contaminated Seashore."; RL Genome Announc. 2:0-0(2014). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KFX71467.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AWSQ01000001; KFX71467.1; -; Genomic_DNA. DR RefSeq; WP_025164313.1; NZ_AWSQ01000001.1. DR ProteinModelPortal; A0A0A1YNJ2; -. DR EnsemblBacteria; KFX71467; KFX71467; TMS3_0105955. DR Proteomes; UP000030063; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000030063}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000030063}. FT DOMAIN 199 366 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 165 192 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 433 AA; 48783 MW; E9E061687740C9FD CRC64; MFFERHEGGE RAILVHLDGQ DSEAREDPQE FQELALSAGA DAVAFLSVPS NRLTAKYLIG SGKVEELRDQ VKLLEADLVI FNYVLTPSQE RNLERVFECR VLDRTGLILD IFAQRARTHE GKLQVELAQL DHMSTRLVRG WTHLERQKGG IGLRGPGETQ LETDRRLLRV RIRQIKQKLE KVRSQREQAR RGRKRADIPS VSLVGYTNAG KSTLFNALTR SEVYAADQLF ATLDPTLRRL ELDDLGPVVL ADTVGFIRHL PHKLVEAFRA TLEESSNSDL LLHVIDAHEP ERMAQIEQVM AVLGEIGADE LPVLEVYNKL DLLEGVEPQI QRNAEGKPQR VWLSARDGRG LPLLEQAIAE LLGHDLFVGT LHLPQQLARL RAQFFALGVV QSEGHAEDGS SLLAVRLPRV ELNRLVSREG LKPLEFIEQH TLQ // ID A0A0A2DV94_9PORP Unreviewed; 416 AA. AC A0A0A2DV94; DT 04-FEB-2015, integrated into UniProtKB/TrEMBL. DT 04-FEB-2015, sequence version 1. DT 07-JUN-2017, entry version 18. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=JT26_03790 {ECO:0000313|EMBL:KGN70583.1}; OS Porphyromonas sp. COT-108 OH1349. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; OC Porphyromonadaceae; Porphyromonas. OX NCBI_TaxID=1537504 {ECO:0000313|EMBL:KGN70583.1, ECO:0000313|Proteomes:UP000030126}; RN [1] {ECO:0000313|EMBL:KGN70583.1, ECO:0000313|Proteomes:UP000030126} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=COT-108 OH1349 {ECO:0000313|Proteomes:UP000030126}; RA Wallis C., Deusch O., O'Flynn C., Davis I., Jospin G., Darling A.E., RA Coil D.A., Alexiev A., Horsfall A., Kirkwood N., Harris S., RA Eisen J.A.; RT "Porphyromonas sp. COT-108_OH1349 Genome sequencing."; RL Submitted (AUG-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KGN70583.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JRAH01000013; KGN70583.1; -; Genomic_DNA. DR RefSeq; WP_036846102.1; NZ_JRAH01000013.1. DR EnsemblBacteria; KGN70583; KGN70583; JT26_03790. DR Proteomes; UP000030126; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000030126}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000030126}. FT DOMAIN 204 389 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 416 AA; 47647 MW; E0253E1107E1CA03 CRC64; MKDFIITNTE SEKAVLVGLI LPEQTESEIT EYLDELAFLA QTAGVEPVMR FTQRLDHPQP ATFVGKGKLE EIKMYIEAQE GEIGVVIFDD ELGPKQMRNI EKELKVKILD RTSLILDIFA ARARTAHAKT QVELAQYNYM LPRLTGLWTH LERQRGGVGM RGPGETQLET DRRIILDKIA KLKRDLQTID RQMSVQRKNR AQLIRVALVG YTNVGKSTIM NVVSKSDVFA ENKLFATLDT TVRKVIIRNL PFLLSDTVGF IRKLPTQLIE SFKSTLDEVR EADLILHVVD VSHPSFEDHI AVVESTLSEI LKEERKPTIM VFNKIDAFSF VQKDEDDLTP ETKENICLED IKQTWLKNLG ADVLFISAKS GEGLEEFRSR IYDRVKELHT LRYPYNDFLF DEYTDLTDEF DSNGTK // ID A0A0A2E000_9PORP Unreviewed; 410 AA. AC A0A0A2E000; DT 04-FEB-2015, integrated into UniProtKB/TrEMBL. DT 04-FEB-2015, sequence version 1. DT 07-JUN-2017, entry version 18. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=HQ37_00800 {ECO:0000313|EMBL:KGN72181.1}; OS Porphyromonas sp. COT-239 OH1446. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; OC Porphyromonadaceae; Porphyromonas. OX NCBI_TaxID=1515613 {ECO:0000313|EMBL:KGN72181.1, ECO:0000313|Proteomes:UP000030150}; RN [1] {ECO:0000313|EMBL:KGN72181.1, ECO:0000313|Proteomes:UP000030150} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=COT-239 OH1446 {ECO:0000313|Proteomes:UP000030150}; RA Wallis C., Deusch O., O'Flynn C., Davis I., Jospin G., Darling A.E., RA Coil D.A., Alexiev A., Horsfall A., Kirkwood N., Harris S., RA Eisen J.A.; RT "Porphyromonas sp. COT-239_OH1446 Genome sequencing."; RL Submitted (AUG-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KGN72181.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JRAO01000003; KGN72181.1; -; Genomic_DNA. DR RefSeq; WP_036878881.1; NZ_JRAO01000003.1. DR EnsemblBacteria; KGN72181; KGN72181; HQ37_00800. DR Proteomes; UP000030150; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000030150}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000030150}. FT DOMAIN 202 387 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 163 197 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 410 AA; 47270 MW; 22307B2E82720A78 CRC64; MKDFIITQVK SEEAVLVGLI TRTQTEEQVK EYLDELDFLS ETAGVRPVKR FIQKLDAAHP VTFVGKGKLE EIRLYVEEHE IGLVIFDDEL SPKQLRNIEQ TLKVKILDRT SLILDIFASR AQTAYAKTQV ELAQYHYMLP RLTRLWTHLE RQRGGVGMRG PGETQLETDK RIIQDRIAHL KEELKAIDKQ MSVQRKNRGK MVRVALVGYT NVGKSTLMNV LAKSEVFAEN KLFATLDTTV RKVIVHNLPF LLSDTVGFIR KLPTELVESF KSTLDEVREA DLLLHVVDVS HPNFEEQIDI VNTTLREING SEDKPMLLIF NKVDAFTFEA KDEDDLSPRT RRNVSMQELQ ETWMAKMQGD CLFISARESV GLDELKQLLY DRVREIHVTR FPYNDFLFQD YALEGDEPTV // ID A0A0A2EBG7_9PORP Unreviewed; 409 AA. AC A0A0A2EBG7; DT 04-FEB-2015, integrated into UniProtKB/TrEMBL. DT 04-FEB-2015, sequence version 1. DT 07-JUN-2017, entry version 16. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=HQ47_03460 {ECO:0000313|EMBL:KGN74977.1}; OS Porphyromonas macacae. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; OC Porphyromonadaceae; Porphyromonas. OX NCBI_TaxID=28115 {ECO:0000313|EMBL:KGN74977.1, ECO:0000313|Proteomes:UP000030103}; RN [1] {ECO:0000313|EMBL:KGN74977.1, ECO:0000313|Proteomes:UP000030103} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=COT-192 OH2859 {ECO:0000313|Proteomes:UP000030103}; RA Wallis C., Deusch O., O'Flynn C., Davis I., Horsfall A., Kirkwood N., RA Harris S., Eisen J.A., Coil D.A., Darling A.E., Jospin G., Alexiev A.; RT "Draft Genome Sequence of Porphyromonas macacae COT-192_OH2859."; RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KGN74977.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JRFA01000009; KGN74977.1; -; Genomic_DNA. DR RefSeq; WP_036873293.1; NZ_JRFA01000009.1. DR EnsemblBacteria; KGN74977; KGN74977; HQ47_03460. DR Proteomes; UP000030103; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000030103}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000030103}. FT DOMAIN 202 387 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 409 AA; 47019 MW; 1800E0987520F652 CRC64; MKEFIITETK TERAVLIGIV TPEQNEVAIN EYLDELAFLS ETAGVEPLKR FTQKIDQPNS VTFVGKGKLS EIAQYVEENE IGVAIFDDEL SPKQIRNIEQ VLKIKILDRT GLILDIFARR AQTAHAKTQV ELAQYRYMLP RLTRLWTHLE RQRGGVGMRG PGETQLETDR RIILDKISLL KQQLKAIDKQ KSVQRKNRGK MVRVALVGYT NVGKSTLMNL LVKSEVFAEN KLFATLDTTV RKMVIHNLPF LLTDTVGFIR KLPTELIESF KSTLDEVREA DLLVHVVDVS HPNFEEQITV VENTLREITA GEEKPYLLVF NKLDAFSWVP KEDDDLSPVK RENITPEELK KTWMAKLGPD CLFISAKNGT GVEELKRILY ERVKEIHVQR YPYNDFLFQD YDNLSESEI // ID A0A0A2EIJ0_9PORP Unreviewed; 395 AA. AC A0A0A2EIJ0; DT 04-FEB-2015, integrated into UniProtKB/TrEMBL. DT 04-FEB-2015, sequence version 1. DT 07-JUN-2017, entry version 18. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=HW49_10635 {ECO:0000313|EMBL:KGN77457.1}; OS Porphyromonadaceae bacterium COT-184 OH4590. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; OC Porphyromonadaceae; unclassified Porphyromonadaceae. OX NCBI_TaxID=1517682 {ECO:0000313|EMBL:KGN77457.1, ECO:0000313|Proteomes:UP000030107}; RN [1] {ECO:0000313|EMBL:KGN77457.1, ECO:0000313|Proteomes:UP000030107} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=COT-184 OH4590 {ECO:0000313|Proteomes:UP000030107}; RA Wallis C., Deusch O., O'Flynn C., Davis I., Jospin G., Darling A.E., RA Coil D.A., Alexiev A., Horsfall A., Kirkwood N., Harris S., RA Eisen J.A.; RT "Porphyromonadaceae COT-184_OH4590 Genome sequencing."; RL Submitted (AUG-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KGN77457.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JRAN01000072; KGN77457.1; -; Genomic_DNA. DR RefSeq; WP_036830264.1; NZ_JRAN01000072.1. DR EnsemblBacteria; KGN77457; KGN77457; HW49_10635. DR Proteomes; UP000030107; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000030107}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000030107}. FT DOMAIN 193 377 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 395 AA; 45648 MW; 1E1ACAC3C351AABE CRC64; MENAILIGII TPQQPENKAK EYIEELAFLS ETAGATPVKC FFQHLPYPNP RTFVGEGKLA EIRKYIVDNE NIDLVIFDDE LSPVQLKNIE SELKVKILDR TNLILDIFAQ RAQTANAKTQ VELAQCQYML PRLTRLWTHL ERQRGGIGMR GPGETQIETD RRILLSKISL LKEKLKKIDQ QKSIQRKNRE KMVRVALVGY TNAGKSTIMN MFSKANVFAE NKLFATLDTT VRKVIIDNLP FLLSDTVGFI RKLPHHLIES FKSTLDELNE ADILLHVSDI SHSNFEEHYT IVNETIKSIV KMEKPTIVVF NKIDNYSFVE KDEADLSERT KENISLKELE KTYMAKFSGN CVFISAKEKI NTDNFKLMLY EKVKEVYSQK YPYSNFIFEK YDDLE // ID A0A0A2F6K5_9PORP Unreviewed; 415 AA. AC A0A0A2F6K5; DT 04-FEB-2015, integrated into UniProtKB/TrEMBL. DT 04-FEB-2015, sequence version 1. DT 07-JUN-2017, entry version 19. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=HQ41_00630 {ECO:0000313|EMBL:KGN86633.1}; OS Porphyromonas sp. COT-290 OH860. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; OC Porphyromonadaceae; Porphyromonas. OX NCBI_TaxID=1515615 {ECO:0000313|EMBL:KGN86633.1, ECO:0000313|Proteomes:UP000030116}; RN [1] {ECO:0000313|EMBL:KGN86633.1, ECO:0000313|Proteomes:UP000030116} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=COT-290 OH860 {ECO:0000313|Proteomes:UP000030116}; RA Wallis C., Deusch O., O'Flynn C., Davis I., Jospin G., Darling A.E., RA Coil D.A., Alexiev A., Horsfall A., Kirkwood N., Harris S., RA Eisen J.A.; RT "Porphyromonas sp. strain:COT-290_OH860 Genome sequencing."; RL Submitted (AUG-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KGN86633.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JRAR01000003; KGN86633.1; -; Genomic_DNA. DR RefSeq; WP_044186497.1; NZ_JRAR01000003.1. DR EnsemblBacteria; KGN86633; KGN86633; HQ41_00630. DR Proteomes; UP000030116; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000030116}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000030116}. FT DOMAIN 202 387 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 415 AA; 47683 MW; C1C2B9FEA1AD5F5B CRC64; MKDFIITEVK SEEAVLVGLI TRTQSEEQVK EYLDELDFLS ETAGVRPVKR FVQRLESAHP VTFVGKGKLE EIRLYVEENE IGLVIFDDEL SPKQLRNIEA ALKVKILDRT SLILDIFASR AQTAYAKTQV ELAQYRYMLP RLTRLWTHLE RQRGGVGMRG PGETQLETDK RIIQDRISHL KEELKLIDRQ MSMQRKNRGK MVRAALVGYT NVGKSTLMNA LAKSEVFAEN KLFATLDTTV RKVIVHNLPF LLSDTVGFIR KLPTELVESF KSTLDEVREA DLLLHVVDVS HPNFEEQIEV VNATLREVLG QEDKPMLLIF NKLDAFTWEE KDADDLSPRT KRNISAEELQ QTWLARMGDD CRFISARHGE GIDDLKALLY QRVKEIHVTR FPYNDFLFQD YDSALADEGP LLSSE // ID A0A0A2FVS6_9PORP Unreviewed; 410 AA. AC A0A0A2FVS6; DT 04-FEB-2015, integrated into UniProtKB/TrEMBL. DT 04-FEB-2015, sequence version 1. DT 07-JUN-2017, entry version 20. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=HQ45_04035 {ECO:0000313|EMBL:KGN90000.1}; OS Porphyromonas crevioricanis. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; OC Porphyromonadaceae; Porphyromonas. OX NCBI_TaxID=393921 {ECO:0000313|EMBL:KGN90000.1, ECO:0000313|Proteomes:UP000030139}; RN [1] {ECO:0000313|EMBL:KGN90000.1, ECO:0000313|Proteomes:UP000030139} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=COT-253 OH2125 {ECO:0000313|Proteomes:UP000030139}; RA Wallis C., Deusch O., O'Flynn C., Davis I., Jospin G., Darling A.E., RA Coil D.A., Alexiev A., Horsfall A., Kirkwood N., Harris S., RA Eisen J.A.; RT "Porphyromonas crevioricanis strain:COT-253_OH2125 Genome RT sequencing."; RL Submitted (AUG-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KGN90000.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JQJB01000006; KGN90000.1; -; Genomic_DNA. DR RefSeq; WP_023936213.1; NZ_JQJC01000020.1. DR EnsemblBacteria; KGN90000; KGN90000; HQ45_04035. DR Proteomes; UP000030139; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000030139}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000030139}. FT DOMAIN 202 387 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 170 197 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 410 AA; 47105 MW; 089B7C2D9DEA1461 CRC64; MKEFVISTLK SETAVLVGLI SQTETDEQVK ENLDELEFLA ETAGLTTLRR FTQKLDLPNS TTFVGKGKLE EIASYIEEHE VGVIIFDDEL SPKQIRNIEL ALKIKVIDRT GLILDIFATR AQTAHAKTQV ELAQYQYMLP RLTRLWTHLE RQRGGVGMRG PGETQLETDR RIVLDKIARL KEQLRDIDKQ KTVQRKNRGK MVRVALVGYT NVGKSTLMNV LSKTDLFAEN KLFATLDTTV RKVVIHNLPF LLSDTVGFIR KLPTQLVESF KSTLDEVREA DLLVHVVDIS HPNFEEQIQV VQQTLKEILD GEDKPSILVF NKIDAFTFVL KEEDDLTPMT KENISLEQLR QTWMAQAGPD CLFVSAKDMR GMDMLKSLLY ERVKQIHVER YPYNDFLFQD YNDVLQEDTE // ID A0A0A2G7C7_9PORP Unreviewed; 406 AA. AC A0A0A2G7C7; DT 04-FEB-2015, integrated into UniProtKB/TrEMBL. DT 04-FEB-2015, sequence version 1. DT 07-JUN-2017, entry version 18. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=HQ36_05135 {ECO:0000313|EMBL:KGN98280.1}; OS Porphyromonas gingivicanis. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; OC Porphyromonadaceae; Porphyromonas. OX NCBI_TaxID=266762 {ECO:0000313|EMBL:KGN98280.1, ECO:0000313|Proteomes:UP000030134}; RN [1] {ECO:0000313|EMBL:KGN98280.1, ECO:0000313|Proteomes:UP000030134} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=COT-022 OH1391 {ECO:0000313|Proteomes:UP000030134}; RA Wallis C., Deusch O., O'Flynn C., Davis I., Jospin G., Darling A.E., RA Coil D.A., Alexiev A., Horsfall A., Kirkwood N., Harris S., RA Eisen J.A.; RT "Porphyromonas gingivicanis strain:COT-022_OH1391 Genome sequencing."; RL Submitted (AUG-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KGN98280.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JQZW01000008; KGN98280.1; -; Genomic_DNA. DR RefSeq; WP_025842254.1; NZ_JQZW01000008.1. DR EnsemblBacteria; KGN98280; KGN98280; HQ36_05135. DR Proteomes; UP000030134; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000030134}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000030134}. FT DOMAIN 202 387 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 170 197 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 406 AA; 46697 MW; 44292F56D0F347CC CRC64; MKDFILTATQ GEKAVLIGLI TPKVTEQQAK DYLDELAFLS ETAGVQPIKS FIQKLDMAHS STFVGKGKLN EIAQYIQEEG IDMAIFDDEL SPKQLRNIET TLKVRILDRT SLILDIFATR AQTAHAKTQV ELAQYRYMLP RLTRLWTHLE RQRGGVGMRG PGETQLETDK RIILDRISKL KEELKQIDRQ KSVQRKNRGK MVRVALVGYT NVGKSTLMNV LSKSDVFAEN KLFATLDTTV RKVILHNLPF LISDTVGFIR KLPTELIESF KSTLDEVREA DLLIHVVDIS HPDFESQINV VDATLRELLG KEEKPQILLF NKTDAFTYTP KDEDDLTPRS RENYSREELE RSWMAKIGRD CLFVSAYTGD GIEALKSMLY ERVKEIHIRR YPYNDFLFQD YEGLEE // ID A0A0A2HWQ5_9DELT Unreviewed; 546 AA. AC A0A0A2HWQ5; DT 04-FEB-2015, integrated into UniProtKB/TrEMBL. DT 04-FEB-2015, sequence version 1. DT 12-APR-2017, entry version 15. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=JT06_08910 {ECO:0000313|EMBL:KGO34473.1}; OS Desulfobulbus sp. Tol-SR. OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfobacterales; OC Desulfobulbaceae; Desulfobulbus. OX NCBI_TaxID=1536652 {ECO:0000313|EMBL:KGO34473.1, ECO:0000313|Proteomes:UP000030148}; RN [1] {ECO:0000313|EMBL:KGO34473.1, ECO:0000313|Proteomes:UP000030148} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Abu Laban N., Tan B.-F., Dao A., Foght J.; RT "Draft genome of Desulfobulbaceae bacterium Tol-SR obtained by stable RT isotope probing of toluene-degrading sulfate-reducing culture enriched RT from oil sands tailing of Alberta, Canada."; RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KGO34473.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JROS01000039; KGO34473.1; -; Genomic_DNA. DR EnsemblBacteria; KGO34473; KGO34473; JT06_08910. DR Proteomes; UP000030148; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000030148}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000030148}. FT DOMAIN 379 546 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 160 187 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 546 AA; 61653 MW; A34A993B93FA202D CRC64; MANLTGNLDG LKKNQIRLLE RLAGKKIHRD LIVSPEIART LSELSFEINR QIGLLIHRSG QIEMVIVGTF SGLMIPQLNA IRTAGGRLRG LRLVHTHPGG EDISDEDLMD LLFLRLDLLS VLKITADGLP ERLYSVHLLP EDTAGRGWTF LPPVHPANQN ESFEELINAL EGEFTRLQRA RRRVERREDR AILVSVSTEA KIVAEESLGE LVELARSDNI EVLDTVLQRQ RQINPRLIVG KGKLADIMIR ALQLDANLLI FNQELNPSQI RSITDFTDLR VIDRTQLILD IFAHRAMSRE GKLQVEMAQL KYMLPRLSTR DDALSRLTGG IGARGPGETR LEIDRRRISD RLARLGGELK AIASERYRRR SKRRKKDLPV ISLVGYTNAG KSTLLNTLTH SDIIAEDKLF ATLDPTSRRL RFPTEMEVII TDTVGFIRHL PDTLLQAFKA TLEELQEADL LVHVIDLSNP VYREQMAVVD RLLGELELDE IPCLRVFNKI DKAPYPVQAR AEAEKEGVVI SAIDPGTLRP FLERAERMMG KALEPM // ID A0A0A2M4W3_9FLAO Unreviewed; 410 AA. AC A0A0A2M4W3; DT 04-FEB-2015, integrated into UniProtKB/TrEMBL. DT 04-FEB-2015, sequence version 1. DT 07-JUN-2017, entry version 18. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=Q763_05035 {ECO:0000313|EMBL:KGO83380.1}; OS Flavobacterium beibuense F44-8. OC Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales; OC Flavobacteriaceae; Flavobacterium. OX NCBI_TaxID=1406840 {ECO:0000313|EMBL:KGO83380.1, ECO:0000313|Proteomes:UP000030129}; RN [1] {ECO:0000313|EMBL:KGO83380.1, ECO:0000313|Proteomes:UP000030129} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=F44-8 {ECO:0000313|EMBL:KGO83380.1, RC ECO:0000313|Proteomes:UP000030129}; RA Zeng Z., Chen C.; RL Submitted (SEP-2013) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KGO83380.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JRLV01000004; KGO83380.1; -; Genomic_DNA. DR RefSeq; WP_035131792.1; NZ_JRLV01000004.1. DR EnsemblBacteria; KGO83380; KGO83380; Q763_05035. DR Proteomes; UP000030129; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000030129}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000030129}. FT DOMAIN 201 387 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 410 AA; 47454 MW; 208AAFB3DB6093AC CRC64; MLEKEEIKFE KTVIVGIITQ NQTEEKLSEY LDELEFLTFT AGGEVIKRFS QKMEKPNPKT FLGTGKMDEI HHFIKEKDIS TVIFDDELSP AQQKNITKIF GECKVLDRTN LILDIFAQRA QTSYARTQVE LAQCQYLLPR LSGMWTHLER QRGGIGMRGP GETEIETDRR IVRDRIALLK DKIKTIDKQM SVQRSNRGAL VRVALVGYTN VGKSTLMNTI SKSEVFVENK LFATLDTTVR KVVIKNLPFL LSDTVGFIRK LPTQLVESFK STLDEVREAD LLLHVVDISH PDFEDHIASV NQILQDIDSI DKPTIMVFNK IDAYKPLVID EDDLMTERTS KHYSLEEWKA TWMSNVGEKN ALFISATNKE NFEEFREKVY EAVREIHITR FPYNNFLYPD YKENHSEEKE // ID A0A0A2MMV0_9FLAO Unreviewed; 409 AA. AC A0A0A2MMV0; DT 04-FEB-2015, integrated into UniProtKB/TrEMBL. DT 04-FEB-2015, sequence version 1. DT 07-JUN-2017, entry version 18. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=Q766_11780 {ECO:0000313|EMBL:KGO92788.1}; OS Flavobacterium subsaxonicum WB 4.1-42 = DSM 21790. OC Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales; OC Flavobacteriaceae; Flavobacterium. OX NCBI_TaxID=1121898 {ECO:0000313|EMBL:KGO92788.1, ECO:0000313|Proteomes:UP000030111}; RN [1] {ECO:0000313|EMBL:KGO92788.1, ECO:0000313|Proteomes:UP000030111} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=WB 4.1-42 {ECO:0000313|EMBL:KGO92788.1, RC ECO:0000313|Proteomes:UP000030111}; RA Zeng Z., Chen C.; RL Submitted (SEP-2013) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KGO92788.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JRLY01000008; KGO92788.1; -; Genomic_DNA. DR RefSeq; WP_026992871.1; NZ_KE383910.1. DR EnsemblBacteria; KGO92788; KGO92788; Q766_11780. DR Proteomes; UP000030111; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000030111}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000030111}. FT DOMAIN 200 386 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 409 AA; 47182 MW; 462A8CC5D254C09F CRC64; MLEKETITFE KTIIAGIVTK GQNEDKLNEY LDELEFLTFT AGGEVIKRFF QRMEKPNPKT FLGTGKIEEI HLYIKEHDIK TVIFDDELTP SQQKNLTKIL DIKVLDRTNL ILDIFAQRAE TSYARTQVEL AQCIYLLPRL SGMWTHLERQ RGGIGMRGPG ETEIETDRRI VRDRIALLKE KIKTIDKQMG VQRGNRGAMV RVALVGYTNV GKSTLMNVIS KSEVFVENKL FATLDTTVRK VVIKNLPFLL SDTVGFIRKL PTQLIDSFKS TLDEVREADL LLHVVDISHP EFEHHIESVN QILQDIKSGD KPVIMVFNKI DAYKPLVIDE DDLITEKTAR HNTLEDWKAT WMGTVGEDKA LFISATSKEN YEEFREKVYE AVRAIHISRF PYNNFLYPDY KENHAEEKE // ID A0A0A2T8N3_9GAMM Unreviewed; 414 AA. AC A0A0A2T8N3; DT 04-FEB-2015, integrated into UniProtKB/TrEMBL. DT 04-FEB-2015, sequence version 1. DT 07-JUN-2017, entry version 18. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=EP47_06130 {ECO:0000313|EMBL:KGP63793.1}; OS Legionella norrlandica. OC Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales; OC Legionellaceae; Legionella. OX NCBI_TaxID=1498499 {ECO:0000313|EMBL:KGP63793.1, ECO:0000313|Proteomes:UP000054422}; RN [1] {ECO:0000313|EMBL:KGP63793.1, ECO:0000313|Proteomes:UP000054422} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=LEGN {ECO:0000313|EMBL:KGP63793.1, RC ECO:0000313|Proteomes:UP000054422}; RA Rizzardi K., Winiecka-Krusnell J., Ramliden M., Alm E., Andersson S., RA Byfors S.; RL Submitted (MAY-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KGP63793.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JNCF01000010; KGP63793.1; -; Genomic_DNA. DR RefSeq; WP_035887991.1; NZ_JNCF01000010.1. DR EnsemblBacteria; KGP63793; KGP63793; EP47_06130. DR Proteomes; UP000054422; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000054422}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000054422}. FT DOMAIN 198 363 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 414 AA; 46551 MW; 145F9D42AB91FDE3 CRC64; MFERPQSGER AVLVQLALPG IDSEKALAEF EELALSAKAE VLDCVLGARA TPDAKYYVGK GKAEEIANLV KTLDAELVLV NHELSPSQER NLEKLLGCRV VDRSGLILDI FAQRARTFEG KLQVELAQLQ HLSTRLIRGW THLERQKGGI GLRGPGETQL ETDRRLLRER IRYINKRLEK VRCSRDQNRQ ARRKAAMPTV SLVGYTNAGK STLFNALTGE NTYVADQLFA TLDPTMRKLD LPGSSSVIVT DTVGFIRDLP HHLVEAFRAT LEETQQADLL LHVIDISDPN WRETVFEVQK VLDELEVNNI PVIQVFNKID LQESWEPKID YTEESCKVWL SAATGAGLDL LKEAIATQLH GKILIEDIVI KSSQAKLRAQ LYELGAVLNE AITEDGDWLM KIRITGEQKR RLFP // ID A0A0A2TD72_9BACI Unreviewed; 414 AA. AC A0A0A2TD72; DT 04-FEB-2015, integrated into UniProtKB/TrEMBL. DT 04-FEB-2015, sequence version 1. DT 07-JUN-2017, entry version 19. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=N782_04605 {ECO:0000313|EMBL:KGP73504.1}; OS Pontibacillus yanchengensis Y32. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Pontibacillus. OX NCBI_TaxID=1385514 {ECO:0000313|EMBL:KGP73504.1, ECO:0000313|Proteomes:UP000030147}; RN [1] {ECO:0000313|EMBL:KGP73504.1, ECO:0000313|Proteomes:UP000030147} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Y32 {ECO:0000313|EMBL:KGP73504.1, RC ECO:0000313|Proteomes:UP000030147}; RX PubMed=26561516; DOI=10.1186/s40793-015-0085-y; RA Huang J., Qiao Z.X., Tang J.W., Wang G.; RT "High quality draft genome sequence of the moderately halophilic RT bacterium Pontibacillus yanchengensis Y32(T) and comparison among RT Pontibacillus genomes."; RL Stand. Genomic Sci. 10:93-93(2015). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KGP73504.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AVBF01000012; KGP73504.1; -; Genomic_DNA. DR RefSeq; WP_036817517.1; NZ_AVBF01000012.1. DR EnsemblBacteria; KGP73504; KGP73504; N782_04605. DR Proteomes; UP000030147; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000030147}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000030147}. FT DOMAIN 197 358 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 156 190 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 414 AA; 47843 MW; 879A68DFFE04E815 CRC64; MEQHERVLVA ACHLPSQDEE RFQSSLEELT SLTETAHGVV DKIVTQKRQK IHQAIYMGEG KIEEIKAYID ERGIELVIFN DELSPGQMNN LADHLEVRII DRTQLILDIF AQRANTKEGK LQVELAQLQY MLPRIYGQGK NLSRLGGGIG TRGPGETKLE TDRRHIQRRI DDIKRQIQQV ATQRQQYRKR RKENKAYQIA IVGYTNAGKS TLFNRITNSQ SFEENQLFAT LDPLTRQVQL PSGFQALMSD TVGFIQDLPT TLIAAFQSTL EEVTEADFIV HVVDASHADH IQHEETVQKH LKELKADHLP MLTVYNKKDL LQDQFIPVTL PAVTISAYDP IDIKRLFDKI EEVLLKEWEP FQTYVPATDG ELLHRLSKHA IVRERDFLEE DELYFVKGFI HPEHPLYHQI RKRQ // ID A0A0A2TKR2_9FIRM Unreviewed; 533 AA. AC A0A0A2TKR2; DT 04-FEB-2015, integrated into UniProtKB/TrEMBL. DT 04-FEB-2015, sequence version 1. DT 07-JUN-2017, entry version 15. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=JT05_05625 {ECO:0000313|EMBL:KGP76279.1}; OS Desulfosporosinus sp. Tol-M. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Peptococcaceae; OC Desulfosporosinus. OX NCBI_TaxID=1536651 {ECO:0000313|EMBL:KGP76279.1, ECO:0000313|Proteomes:UP000030439}; RN [1] {ECO:0000313|EMBL:KGP76279.1, ECO:0000313|Proteomes:UP000030439} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Abu Laban N., Tan B., Dao A., Foght J.; RT "Draft genome of Desulfosporosinus sp. Tol-M obtained by stable RT isotope probing of toluene- degrading methanogenic culture enriched RT from oil sands tailing of Alberta, Canada."; RL Submitted (OCT-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KGP76279.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JQID01000075; KGP76279.1; -; Genomic_DNA. DR EnsemblBacteria; KGP76279; KGP76279; JT05_05625. DR Proteomes; UP000030439; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000030439}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000030439}. FT DOMAIN 364 533 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 323 350 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 533 AA; 59318 MW; 65092B858944F7C7 CRC64; MDISGELSGI RESQLQELNK LSELKTARSE LIHPEILAKL LRLTQLWNRE IAVYLSRSGT LLAAAVGRHA NVTLPPVKGR SMWKHLRCIH THPNGDSRLS PLDQSALLSL QLESMASVGV CEGLLTGIQI AYRTGGNDPF IVNLSSKDWQ SFDYHDSLSS LSKGTSKIER TPAKECAYLI ALVDSELDAL EDLTELQELA RSAGVDVVGQ LVQLRRYGQS RSYLGSGKIE ELVHRLQETE ANVVICDDEL SPTQLRTLET ETGLKVLDRT GLILDIFAQR AHSREGKLQV ELAQLKHLLP YLSGQGQALS QLGAGIGTRG PGETKLELDR RRMRERITQL EKELKLVLQH RDVQRRQRTR SGLPIVAVVG YTNAGKTTFL EVAMEQTGSR SDIPSGENKL FATLDPIVRR VRVSPSLEIL LSDTVGFIQK LPTQLLRAFL ATLEEVQQAD ILLHVVDASH PQALQHAETV HEVLKQLGCE NKPILTLLNK VDNVMAEDDL SELVERLPHP IKLSLVRRDS LKPVWNYLIT LLS // ID A0A0A2U7K4_9BACL Unreviewed; 428 AA. AC A0A0A2U7K4; DT 04-FEB-2015, integrated into UniProtKB/TrEMBL. DT 04-FEB-2015, sequence version 1. DT 07-JUN-2017, entry version 20. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=P364_0112140 {ECO:0000313|EMBL:KGP82446.1}; OS Paenibacillus sp. MAEPY2. OC Bacteria; Firmicutes; Bacilli; Bacillales; Paenibacillaceae; OC Paenibacillus. OX NCBI_TaxID=1395587 {ECO:0000313|EMBL:KGP82446.1, ECO:0000313|Proteomes:UP000030061}; RN [1] {ECO:0000313|EMBL:KGP82446.1, ECO:0000313|Proteomes:UP000030061} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MAEPY2 {ECO:0000313|EMBL:KGP82446.1, RC ECO:0000313|Proteomes:UP000030061}; RX PubMed=24526641; RA Chua P., Yoo H.S., Gan H.M., Lee S.M.; RT "Draft Genome Sequences of Two Cellulolytic Paenibacillus sp. Strains, RT MAEPY1 and MAEPY2, from Malaysian Landfill Leachate."; RL Genome Announc. 2:0-0(2014). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KGP82446.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AWUK01000013; KGP82446.1; -; Genomic_DNA. DR RefSeq; WP_024630468.1; NZ_AWUK01000013.1. DR EnsemblBacteria; KGP82446; KGP82446; P364_0112140. DR Proteomes; UP000030061; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000030061}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000030061}. FT DOMAIN 208 372 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 428 AA; 48032 MW; BACC553D25E51E5C CRC64; MTNGTHDTDM VKKDRAVLVS LVTDEVKRSG INPEYSLEEL VKLAETAGVE VLSVLSQNLK TRDTKWFIGK GKVEELRAVA EEMGATTAIF DQELSGAQVR NLEEALDLKI IDRTQLILDI FAQRANTREG IIQVELAQLS YLLPRLSGHG KNLSRLGGGI GTRGPGESKL ETDRRHIRGR IDDLKRHLEE VTRHRKLHRE RRKKTGIVQV ALVGYTNAGK STLLKQLTAA DVYIQDQLFA TLDPTSRTME LPSGKEIVLT DTVGFIQNLP HDLIAAFRAT LEEVNEADLI LHVVDASSAM REDQMRTVHT ILQQLGSGDK PQLVLYNKKD ACTPEQLEML PLDKEHIKVS ALDADDLLKI RELIQAELTG ATKRFRIPAE RGDLTSVLYK IGDVVETTFE DNDVIYEVEL QKGEYEKFGY LLEDFIQL // ID A0A0A2V1P1_9BACI Unreviewed; 414 AA. AC A0A0A2V1P1; DT 04-FEB-2015, integrated into UniProtKB/TrEMBL. DT 04-FEB-2015, sequence version 1. DT 07-JUN-2017, entry version 17. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=N780_11390 {ECO:0000313|EMBL:KGP92943.1}; OS Pontibacillus chungwhensis BH030062. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Pontibacillus. OX NCBI_TaxID=1385513 {ECO:0000313|EMBL:KGP92943.1, ECO:0000313|Proteomes:UP000030153}; RN [1] {ECO:0000313|EMBL:KGP92943.1, ECO:0000313|Proteomes:UP000030153} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BH030062 {ECO:0000313|EMBL:KGP92943.1, RC ECO:0000313|Proteomes:UP000030153}; RA Wang Q., Wang G.; RT "Genome of Pontibacillus chungwhensis."; RL Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KGP92943.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AVBG01000001; KGP92943.1; -; Genomic_DNA. DR RefSeq; WP_036778896.1; NZ_AVBG01000001.1. DR EnsemblBacteria; KGP92943; KGP92943; N780_11390. DR Proteomes; UP000030153; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000030153}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000030153}. FT DOMAIN 194 355 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 414 AA; 47723 MW; 0DC7835841DF02EE CRC64; MEQAVIVACQ LPNTDEERFQ SSIEELQSLT ETAHGQVHKI YIQKRNKIHP ALYIGEGKLQ EIKEYIETND IGLVIFNDEL SPGQMSKLAD YLDVGIIDRT QLILDIFAKR ANTKEGKLQV ELAQLQYMLP RIYGQGKNMS RLGGGIGTRG PGETKLETDR RHIRRRIDDI KMRLSQVVSQ RNQYRKRRKE NRAFQIAVVG YTNAGKSTLF NRLTNSDSFE ENQLFATLDP LTRQIQLPSG FRSLLSDTVG FIQDLPTTLI AAFRSTLEEV TEADFILHMV DASHPDHIQH EKTVHQLLTD LGADHLPMLT VYNKRDLLDA NFFPATMPAV TISAHDPIDL KRLLDKIEEV IIEEWEPFQI YLHASESDFI HRVESNSIVK ERDFLEEDEK YLLKGWIDRE HPLYHQLKNN HRGE // ID A0A0A2WIS7_9GAMM Unreviewed; 442 AA. AC A0A0A2WIS7; DT 04-FEB-2015, integrated into UniProtKB/TrEMBL. DT 04-FEB-2015, sequence version 1. DT 07-JUN-2017, entry version 18. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=LF41_2601 {ECO:0000313|EMBL:KGQ19663.1}; OS Lysobacter dokdonensis DS-58. OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales; OC Xanthomonadaceae; Lysobacter. OX NCBI_TaxID=1300345 {ECO:0000313|EMBL:KGQ19663.1, ECO:0000313|Proteomes:UP000030518}; RN [1] {ECO:0000313|EMBL:KGQ19663.1, ECO:0000313|Proteomes:UP000030518} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DS-58 {ECO:0000313|EMBL:KGQ19663.1, RC ECO:0000313|Proteomes:UP000030518}; RA Kim J.F., Kwak M.-J.; RT "Genome sequences of Lysobacter dokdonensis DS-58."; RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KGQ19663.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JRKJ01000006; KGQ19663.1; -; Genomic_DNA. DR RefSeq; WP_036167328.1; NZ_JRKJ01000006.1. DR EnsemblBacteria; KGQ19663; KGQ19663; LF41_2601. DR PATRIC; fig|1300345.3.peg.1167; -. DR Proteomes; UP000030518; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000030518}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000030518}. FT DOMAIN 199 373 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 158 192 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 442 AA; 48214 MW; 9AFBA0102DE78A85 CRC64; MFERSKKGET ALLIQPHAGG PPDDGAVEEF ADLARSAGAT VAHMLTARVD RPNPATLIGS GKLEEVKAAA DATGADLILV NHPLSPGQER NLEKALERRV VDRTGLILDI FAQRARSHEG KLQVELAQLR HMATRLVRGW THLERQRGGS IGLRGPGETQ LETDRRLLQK RVEQLQRRLE KVEVQRTQMR RARVRSELPR VALVGYTNAG KSTLFNALTG ADAYAADLLF ATLDPTVRRI ALPGGSVVLA DTVGFVRDLP HELVAAFRST LAEAREADLL LHVIDAADPL RDERIAQVDA VLEEIGAGEI PQLLVYNKID RIEGAQARHD LPTDGHDHAH PKAARERVWL SARDRDGLGL LRDALGARLG LRRVSGEVQL PPGAGRLRAR LHELGAVLAE HHDEHGWTLS LDLAEADAAR IVAHAYGEPL RPLLLEGASA PT // ID A0A0A3HSX6_9BACI Unreviewed; 422 AA. AC A0A0A3HSX6; DT 04-FEB-2015, integrated into UniProtKB/TrEMBL. DT 04-FEB-2015, sequence version 1. DT 05-JUL-2017, entry version 19. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=CD33_10435 {ECO:0000313|EMBL:KGR75549.1}; OS Lysinibacillus sinduriensis BLB-1 = JCM 15800. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; OC Lysinibacillus. OX NCBI_TaxID=1384057 {ECO:0000313|EMBL:KGR75549.1, ECO:0000313|Proteomes:UP000030408}; RN [1] {ECO:0000313|EMBL:KGR75549.1, ECO:0000313|Proteomes:UP000030408} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=JCM 15800 {ECO:0000313|EMBL:KGR75549.1, RC ECO:0000313|Proteomes:UP000030408}; RA Zhang F., Wang G., Zhang L.; RT "Draft genome sequence of Lysinibacillus sinduriensis JCM 15800."; RL Submitted (FEB-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KGR75549.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JPVO01000050; KGR75549.1; -; Genomic_DNA. DR EnsemblBacteria; KGR75549; KGR75549; CD33_10435. DR Proteomes; UP000030408; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000030408}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000030408}. FT DOMAIN 200 368 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 159 193 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 422 AA; 48026 MW; CF7D2A96AA40CF28 CRC64; METIIEKAIL VGVNLQNDRN FNYSMEELES LAEALDVEVI GSVIQNLERV NPSHYVGTGK IEEIKNFVDE AEANLVIFND ELSPSQIRNL EHDLECKVID RTMLILDIFD RRANTREAQM QVELAQLQYM LPRLVGLHAS LSRQGGGTGG GFRNRGAGET KLELDRRKIE DQIAKLRKDL EVVKNIRETQ RKKRRKNEVP VVSLVGYTNA GKSTIMNRLL KKIGQEDNKQ VFEKDMLFAT LDTSVRNIEL PDRKTFLLTD TVGFVSKLPH HLVKAFRSTL EEAREADLLL HVVDVSNEQH PFMMDVTNKT LSEVDVEGIP TIYVYNKSDL ANVKYPLVSG DNIWVSAQDG QGLDELVELI RQHVFSDYVE CEMLIPFDRG DVVSYLNANA QVKDTEYEEN GTKLLVELKG ADLKKYEQYV IK // ID A0A0A3IMV5_9BACI Unreviewed; 428 AA. AC A0A0A3IMV5; DT 04-FEB-2015, integrated into UniProtKB/TrEMBL. DT 04-FEB-2015, sequence version 1. DT 12-APR-2017, entry version 16. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=CD32_06895 {ECO:0000313|EMBL:KGR86119.1}; OS Lysinibacillus odysseyi 34hs-1 = NBRC 100172. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; OC Lysinibacillus. OX NCBI_TaxID=1220589 {ECO:0000313|EMBL:KGR86119.1, ECO:0000313|Proteomes:UP000030437}; RN [1] {ECO:0000313|EMBL:KGR86119.1, ECO:0000313|Proteomes:UP000030437} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NBRC 100172 {ECO:0000313|EMBL:KGR86119.1, RC ECO:0000313|Proteomes:UP000030437}; RA Zhang F., Wang G., Zhang L.; RT "Draft genome sequence of Lysinibacillus odysseyi NBRC 100172."; RL Submitted (FEB-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KGR86119.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JPVP01000052; KGR86119.1; -; Genomic_DNA. DR EnsemblBacteria; KGR86119; KGR86119; CD32_06895. DR Proteomes; UP000030437; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000030437}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000030437}. FT DOMAIN 206 374 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 165 202 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 428 AA; 48402 MW; 23232310B2CAD580 CRC64; MNNLKDIEIL QEKGVLVGVN LQSDKHFDYS MEELANLAVA LDVEIAGYVT QNLERVNPSH YVGTGKIEEI KAFVEEKNAN IVIFNDELSP SQIRNLERDL ECKVIDRTML ILDIFSRRAK TREAQMQVEL AQLQYMLPRL VGLHASLSRQ GGGTGGGFKN RGAGETKLEL DRRKIEDQIA KLRRELEQVK EQRETQRKQR RKNAMPVVSL VGYTNAGKST IMNQLLAKIG QEDSKRVFEK DMLFATLETS VRNIELSDNK TFLLTDTVGF VSKLPHHLVK AFRSTLEEAR DADLLLHVVD VSNEEHSFMI NVTNETLKAV GVEDIPTIYV YNKSDLAGVK YPLVSGDNVW TAAKEGEGLD ELVQMIKQHI FSNYVTCKML IPYDKGGVVS YLNEAATIFS TSYEEEGTLV ELELKEADFQ KYEQYVVS // ID A0A0A3ISQ2_9BACI Unreviewed; 426 AA. AC A0A0A3ISQ2; DT 04-FEB-2015, integrated into UniProtKB/TrEMBL. DT 04-FEB-2015, sequence version 1. DT 07-JUN-2017, entry version 18. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=CD29_13170 {ECO:0000313|EMBL:KGR77837.1}; OS Lysinibacillus manganicus DSM 26584. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; OC Lysinibacillus. OX NCBI_TaxID=1384049 {ECO:0000313|EMBL:KGR77837.1, ECO:0000313|Proteomes:UP000030416}; RN [1] {ECO:0000313|EMBL:KGR77837.1, ECO:0000313|Proteomes:UP000030416} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 26584 {ECO:0000313|EMBL:KGR77837.1, RC ECO:0000313|Proteomes:UP000030416}; RA Zhang F., Wang G., Zhang L.; RT "Draft genome sequence of Lysinibacillus manganicus DSM 26584T."; RL Submitted (FEB-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KGR77837.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JPVN01000015; KGR77837.1; -; Genomic_DNA. DR RefSeq; WP_036187619.1; NZ_JPVN01000015.1. DR EnsemblBacteria; KGR77837; KGR77837; CD29_13170. DR Proteomes; UP000030416; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000030416}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000030416}. FT DOMAIN 203 371 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 162 196 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 426 AA; 48870 MW; 24FA17E2D727F4E9 CRC64; MKEVEVLVER GILVGVNIQS NQNFEYSMVE LRELARALNV EIVGTITQNL DRVTPSHYVG TGKIEEIKRY YEESGANLVI FNDELSPSQI RNLEHELDSK VIDRTMLILD IFERRAKTRE AKMQVELAQL QYMLPRLVGL HASLSRQGGG TGGGFRNRGA GETKLELDRR KIEDQISKLR KELEVVKDQR ETQRKQRKKN EIPVVSLVGY TNAGKSTIMN QLLKKFGQLE NKQVFEKDML FATLETSVRS IELEDNKSFL LTDTVGFVSK LPHHLVKAFR STLEEAKNSD LLLHVVDVSN EEYEFMMDVT TNTLKEIEVV DVPTIYVYNK SDLANLTYPL VSGDNIWLSA KEDKGLDELV EIIRQRIFAN YTKCQMLIPF DRGDIVSYLN TNASILSTDY EELGTLLTLE LKHSDYQKYE EFVIKM // ID A0A0A3J464_9BACI Unreviewed; 426 AA. AC A0A0A3J464; DT 04-FEB-2015, integrated into UniProtKB/TrEMBL. DT 04-FEB-2015, sequence version 1. DT 07-JUN-2017, entry version 18. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=CD30_04220 {ECO:0000313|EMBL:KGR91789.1}; OS Lysinibacillus massiliensis 4400831 = CIP 108448 = CCUG 49529. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; OC Lysinibacillus. OX NCBI_TaxID=1211035 {ECO:0000313|EMBL:KGR91789.1, ECO:0000313|Proteomes:UP000030595}; RN [1] {ECO:0000313|EMBL:KGR91789.1, ECO:0000313|Proteomes:UP000030595} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CCUG 49529 {ECO:0000313|EMBL:KGR91789.1, RC ECO:0000313|Proteomes:UP000030595}; RA Zhang F., Wang G., Zhang L.; RT "Draft genome sequence of Lysinibacillus massiliensis CCUG 49529."; RL Submitted (FEB-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KGR91789.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JPVQ01000004; KGR91789.1; -; Genomic_DNA. DR RefSeq; WP_036172898.1; NZ_JPVQ01000004.1. DR EnsemblBacteria; KGR91789; KGR91789; CD30_04220. DR Proteomes; UP000030595; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000030595}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000030595}. FT DOMAIN 203 371 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 162 199 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 426 AA; 48688 MW; E6E477A8AAD69865 CRC64; MKEIEVLIEK GILVGVNLQN ESNFQYSMEE LADLAEALDV QVVGTITQNL ERVTPSHYVG TGKIEEIKSL YDETNANLVI FNDELSPSQI RNLEHDLDCK VIDRTMLILD IFERRAKTSE AKLQVQLAQL QYMLPRLVGL HASLSRQGGG TGGGFRNRGA GETKLELDRR KIEDQISKLK NELENIKDQR ETQRKKRRKN QVPVVSLVGY TNAGKSTIMN QLLFKMGQQE NKQVFEKDML FATLETSVRN IELSDNKSFL LTDTVGFVSK LPHHLVRAFR STLEEAKDAD LLLHVVDVSN EQYQFMMDIT NQTLKEIGVV DVPTIYVYNK SDRADVSYPL ISGNNIWLSA KEDVGLDELI EMIRLRIFDD YIKCKMLIPF DRGDIVSYLN QNASIFTTEY EENGTLISLE LKEADYKKFE QYAIIK // ID A0A0A3X2V6_9GAMM Unreviewed; 446 AA. AC A0A0A3X2V6; DT 04-FEB-2015, integrated into UniProtKB/TrEMBL. DT 04-FEB-2015, sequence version 1. DT 30-AUG-2017, entry version 17. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=GW12_17210 {ECO:0000313|EMBL:KGT47248.1}; OS Acinetobacter sp. HR7. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Moraxellaceae; Acinetobacter. OX NCBI_TaxID=1509403 {ECO:0000313|EMBL:KGT47248.1, ECO:0000313|Proteomes:UP000032870}; RN [1] {ECO:0000313|EMBL:KGT47248.1, ECO:0000313|Proteomes:UP000032870} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=HR7 {ECO:0000313|EMBL:KGT47248.1, RC ECO:0000313|Proteomes:UP000032870}; RA Ahn S., Kim B.-C.; RT "Genome sequencing of Acinetobacter sp. strain HR7."; RL Submitted (OCT-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KGT47248.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JPQO01000168; KGT47248.1; -; Genomic_DNA. DR RefSeq; WP_034586497.1; NZ_JPQO01000168.1. DR EnsemblBacteria; KGT47248; KGT47248; GW12_17210. DR PATRIC; fig|1509403.3.peg.1707; -. DR Proteomes; UP000032870; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000032870}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}. FT DOMAIN 199 364 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 446 AA; 50206 MW; 5504D53029E8D8D0 CRC64; MEIIQHRRTP DRVILVSVSV QMLEDLDAEE FHLLASSAGA EILEHLHVQR LKPDPKFFIG SGKAEEIAEQ VEALEADLVI FDHSLTPAQA RNLEKVVKCR VVDRTELILD IFAQRARTYE GKLQVELAQL QHMASRLIRS RGNLDSQKGG IGLRGPGETL LETDRRLLRV RMGQLKAKLE KVRQTRMQGR VARQKAAVPT ISLVGYTNAG KSTLFNILAK SDVYAADQLF ATLDPTLRRL EWEGIGTVVI ADTVGFVRNL SHSLVESFKA TLEETLEATL LLHVIDSSSP EILEQIEAVE TVLKEIGADV PVLRVYNKID RSGEDAKIIY SKPNQPERVY VSAHTGEGIE LLRKAVHEAL MGQIQQFDLK LQHAHGKLRN QLYDLNVIQS EHYDEDGQLH LQVRIAPQKL EQIIRQAHLS LEDILGDQAV QFQRPLEEFE IPGKID // ID A0A0A5FTS5_9BACI Unreviewed; 444 AA. AC A0A0A5FTS5; DT 04-FEB-2015, integrated into UniProtKB/TrEMBL. DT 04-FEB-2015, sequence version 1. DT 12-APR-2017, entry version 12. DE SubName: Full=GTPase {ECO:0000313|EMBL:KGX83314.1}; DE Flags: Fragment; GN ORFNames=N783_04515 {ECO:0000313|EMBL:KGX83314.1}; OS Pontibacillus marinus BH030004 = DSM 16465. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Pontibacillus. OX NCBI_TaxID=1385511 {ECO:0000313|EMBL:KGX83314.1, ECO:0000313|Proteomes:UP000030403}; RN [1] {ECO:0000313|EMBL:KGX83314.1, ECO:0000313|Proteomes:UP000030403} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BH030004 {ECO:0000313|EMBL:KGX83314.1, RC ECO:0000313|Proteomes:UP000030403}; RA Huang J., Wang G.; RL Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KGX83314.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AVPF01000121; KGX83314.1; -; Genomic_DNA. DR EnsemblBacteria; KGX83314; KGX83314; N783_04515. DR Proteomes; UP000030403; Unassembled WGS sequence. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000030403}; KW Reference proteome {ECO:0000313|Proteomes:UP000030403}. FT DOMAIN 228 389 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 194 221 {ECO:0000256|SAM:Coils}. FT NON_TER 1 1 {ECO:0000313|EMBL:KGX83314.1}. SQ SEQUENCE 444 AA; 51336 MW; 6AFEABF600AFBF7F CRC64; KRALALLYVV GSHFHPTFGM IVALMERRGI LMEQKEHVLL AACRLPFQDD ERFQSSLEEL RSLTETAHGE VDKIVIQNRN KVHQALYLGQ GKLEEIKTYI EEHEIDLVII NDELSPSQTK NISDFLDIAV IDRTQLILDI FARRANTKEG KLQVELAQLQ YLLPRLYGQG KNLSRLGGGI GTRGPGETKL ETDRRHIQRR IDDIRKQIQQ VATQREQYRK RRKENKAFQI AIVGYTNAGK STLFNRITNS QSFEENQLFA TLDPLTRQVQ LPSGFQALIS DTVGFIQDLP TTLIAAFRST LEEVREADLV LHMVDASHPD HVHHEKTVHK LLKELEADHI PMLNVYNKKD LLNEDFMPVS LPAITISAND PIDIKRLFDK IEEVLMKEWE PYQTYVHASK GDMLHRLSKH SIMTERDFLE EDEVYFVKGW INPDHPLYHQ LRKE // ID A0A0A5GPK5_9BACI Unreviewed; 413 AA. AC A0A0A5GPK5; DT 04-FEB-2015, integrated into UniProtKB/TrEMBL. DT 04-FEB-2015, sequence version 1. DT 07-JUN-2017, entry version 17. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=N781_11745 {ECO:0000313|EMBL:KGX93085.1}; OS Pontibacillus halophilus JSM 076056 = DSM 19796. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Pontibacillus. OX NCBI_TaxID=1385510 {ECO:0000313|EMBL:KGX93085.1, ECO:0000313|Proteomes:UP000030528}; RN [1] {ECO:0000313|EMBL:KGX93085.1, ECO:0000313|Proteomes:UP000030528} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=JSM 076056 {ECO:0000313|EMBL:KGX93085.1, RC ECO:0000313|Proteomes:UP000030528}; RA Huang J., Wang G.; RL Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KGX93085.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AVPE01000003; KGX93085.1; -; Genomic_DNA. DR RefSeq; WP_026799865.1; NZ_AVPE01000003.1. DR EnsemblBacteria; KGX93085; KGX93085; N781_11745. DR Proteomes; UP000030528; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000030528}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000030528}. FT DOMAIN 198 359 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 413 AA; 47165 MW; D2D8B38B6A7914F8 CRC64; MEEREHVLLA ACHFPNQDDE HFHSSLDELR ALTETAGGEV MKVVTQKRPR AHPALYMGEG KVHEMLEEVE ARDIELVIFN GELSPSQMRN LSNELGGIRV IDRTQLILDI FAGRAETKEG KLQVELAQLQ YLLPRLSGQG AFLSRQGGGI GTRGPGETKL ESDRRHIQRR ITDIKRRFET VVSQRDQYRK RRKENNVFQI AVVGYTNAGK STLFNHLTNS KSLQEDQLFA TLDPLTRQIQ LPSGFEALLS DTVGFIQDLP TTLVAAFRST LEEVTEADFI LHMVDASHPD HVQHEKTVQK LLGDLEADHV PQLTVYNKKD LLSAEFMPLN IPSITISALD PIDYKRLFEK IETVLKEGWE PYDVSVPAYE AQLLHRLERH TIRTLQEFNE EDETFRVEGY IKHDHPLAHQ LKK // ID A0A0A5HNN8_9VIBR Unreviewed; 429 AA. AC A0A0A5HNN8; DT 04-FEB-2015, integrated into UniProtKB/TrEMBL. DT 04-FEB-2015, sequence version 1. DT 30-AUG-2017, entry version 25. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=NM06_18560 {ECO:0000313|EMBL:KGY07167.1}; OS Vibrio sinaloensis. OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; OC Vibrionaceae; Vibrio; Vibrio oreintalis group. OX NCBI_TaxID=379097 {ECO:0000313|EMBL:KGY07167.1, ECO:0000313|Proteomes:UP000030451}; RN [1] {ECO:0000313|EMBL:KGY07167.1, ECO:0000313|Proteomes:UP000030451} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=T08 {ECO:0000313|EMBL:KGY07167.1, RC ECO:0000313|Proteomes:UP000030451}; RA Chan K.-G., Mohamad N.I.; RT "Genome sequencing of Vibrio sinaloensis T08."; RL Submitted (OCT-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KGY07167.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JRWP01000052; KGY07167.1; -; Genomic_DNA. DR RefSeq; WP_038192836.1; NZ_JRWP01000052.1. DR EnsemblBacteria; KGY07167; KGY07167; NM06_18560. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR Proteomes; UP000030451; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000030451}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000030451}. FT DOMAIN 198 365 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 429 AA; 48720 MW; 63F7A02E3ED8D2C0 CRC64; MFDRYEAGER AVLVHINFTQ EGEWEDLSEF EMLVSSAGVS SLQVVTGSRQ SPHPKYYVGE GKAQEIAQAV QLAGADIVIF NHALSPAQER NLEALCKCRV LDRTGLILDI FAQRARTHEG KLQVELAQLR HISTRLIRGW THLERQKGGI GLRGPGETQL ETDRRLLRVR IKTILRRLEK VAKQREQGRR ARSRAEIPTV SLVGYTNAGK STLFNRITEA GVYAADQLFA TLDPTLRKIE LSDVGPAILA DTVGFIRHLP HDLVAAFKAT LQETQEADIL LHVVDASDER FRENIHAVHD VLEEIEANEI PALIVMNKID NLDGQNPRIE RDDEGVVQTV WVSAMEGKGI ELLFEALTER LASQMVQYQM RIPPQHQGRL RSTFFQMKCI QHEEYDQDGN LLIDVRMQQV DWSRLEKREE AVLRDFIVT // ID A0A0A5HXL2_9BACI Unreviewed; 414 AA. AC A0A0A5HXL2; DT 04-FEB-2015, integrated into UniProtKB/TrEMBL. DT 04-FEB-2015, sequence version 1. DT 07-JUN-2017, entry version 18. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=N784_06760 {ECO:0000313|EMBL:KGX88357.1}; OS Pontibacillus litoralis JSM 072002. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Pontibacillus. OX NCBI_TaxID=1385512 {ECO:0000313|EMBL:KGX88357.1, ECO:0000313|Proteomes:UP000030401}; RN [1] {ECO:0000313|EMBL:KGX88357.1, ECO:0000313|Proteomes:UP000030401} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=JSM 072002 {ECO:0000313|EMBL:KGX88357.1, RC ECO:0000313|Proteomes:UP000030401}; RA Huang J., Wang G.; RL Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KGX88357.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AVPG01000002; KGX88357.1; -; Genomic_DNA. DR RefSeq; WP_036831786.1; NZ_AVPG01000002.1. DR EnsemblBacteria; KGX88357; KGX88357; N784_06760. DR Proteomes; UP000030401; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000030401}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000030401}. FT DOMAIN 197 358 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 163 190 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 414 AA; 48050 MW; E5A3E900900196E5 CRC64; MNQRERVLIA ACQLPNQDDE RFQSSLNELV SLTETAHGEV VSIVTQKRQR IHQAYYIGTG KVEEMNVYIE QEQIDLVIFN DELTPSQMNH LADFLEVRII DRTQLILDIF ASRANTREGK LQVELAQMSY LLPRLHGQGK NLSRLGGGIG TRGPGETKLE SDRRHILRRM DDIKRQMEQV AKQRLQYRKR RKENQAFQIA IVGYTNAGKS TLFNRMTDSE SFEENQLFAT LDPLTRQVQL TSGFHVLMSD TVGFIQDLPT ALIAAFRSTL EEVTEADFIL HVVDASHPDH AEHEKTVQKH LEQLEAHHIP MLTVYNKMDL VTETFVPVSV PHITISAYQM DDIHRLFKRI EEVILKQFVA YQLYVKPSEA DYLHRLSRQS IVTEQTFLEE QELYIVKGYI HTEHPMYYQM RIDN // ID A0A0A6D1X3_9SPHN Unreviewed; 430 AA. AC A0A0A6D1X3; DT 04-FEB-2015, integrated into UniProtKB/TrEMBL. DT 04-FEB-2015, sequence version 1. DT 07-JUN-2017, entry version 17. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=NI18_04550 {ECO:0000313|EMBL:KHA65108.1}; OS Sphingomonas sp. Ant20. OC Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales; OC Sphingomonadaceae; Sphingomonas. OX NCBI_TaxID=104605 {ECO:0000313|EMBL:KHA65108.1, ECO:0000313|Proteomes:UP000033201}; RN [1] {ECO:0000313|EMBL:KHA65108.1, ECO:0000313|Proteomes:UP000033201} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Ant20 {ECO:0000313|EMBL:KHA65108.1, RC ECO:0000313|Proteomes:UP000033201}; RA Ronca S., Frossard A., Guerrero L.D., Makhalanyane T.P., RA Aislabie J.M., Cowan D.A.; RT "Draft Genome Sequence of Spingomonas sp. strain Ant20, isolated from RT oil-polluted soil near Scott Base, Antarctica."; RL Submitted (OCT-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KHA65108.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JRVI01000020; KHA65108.1; -; Genomic_DNA. DR RefSeq; WP_037528497.1; NZ_JRVI01000020.1. DR EnsemblBacteria; KHA65108; KHA65108; NI18_04550. DR Proteomes; UP000033201; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000033201}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000033201}. FT DOMAIN 208 377 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 174 201 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 430 AA; 47471 MW; C10FF1DED945AC1D CRC64; MSSGFDRDRD EFARGTKAIV VLPDQGDATR DIDARLEETA GLAAAIGVEV VERIAYRVRQ AKPATLIGSG QVELLATQVR MEEAGLVVFD ASLSPIQQRN LEKALETKVI DRTGLILEIF GERAATAEGR LQVELAHLDY QAGRLVRSWT HLERQRGGFG FLGGPGETQI EADRRLIRDR MARLRRELEQ VSRTRGLHRE RRQRAPWPVI ALVGYTNAGK STLFNRLTGA DVMAEDLLFA TLDPTLRQIR LPGIDKAILS DTVGFVSDLP TQLVAAFKAT LEEVVSADLL IHVRDIAHPD TEAQRADVEA VLADIGVDDM TPRFEVWNKL DLLDPADHDE IVGEAEHRED VVAISALSGE GVDHLVEQVA AKLTDAHRRY HITLDATDGA GAAWLHAHGE VLSSFADGLA TTYDVRLSDT DYDRFSRRDV // ID A0A0A6Q4N1_9BURK Unreviewed; 395 AA. AC A0A0A6Q4N1; DT 04-FEB-2015, integrated into UniProtKB/TrEMBL. DT 04-FEB-2015, sequence version 1. DT 05-JUL-2017, entry version 18. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=NH14_31440 {ECO:0000313|EMBL:KHD17432.1}; OS Paraburkholderia sacchari. OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Paraburkholderia. OX NCBI_TaxID=159450 {ECO:0000313|EMBL:KHD17432.1, ECO:0000313|Proteomes:UP000030460}; RN [1] {ECO:0000313|EMBL:KHD17432.1, ECO:0000313|Proteomes:UP000030460} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=LMG 19450 {ECO:0000313|EMBL:KHD17432.1, RC ECO:0000313|Proteomes:UP000030460}; RA Alexandrino P., Mendonca T., Bautista L., Cherix J., Lozano G., RA Fujita A., Filho E., Long P., Padilla G., Taciro M., Gomez J., RA Silva L.; RT "Draft Genome Sequence of the Polyhydroxyalkanoate-producing Bacterium RT Burkholderia sacchari LMG 19450 Isolated from Brazilian Sugarcane RT Plantation Soil."; RL Submitted (NOV-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KHD17432.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JTDB01000049; KHD17432.1; -; Genomic_DNA. DR EnsemblBacteria; KHD17432; KHD17432; NH14_31440. DR Proteomes; UP000030460; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000030460}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000030460}. FT DOMAIN 196 367 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 395 AA; 43296 MW; 57278E25EC0A5FCA CRC64; MISANLINAA LVGIDFGKTD FEASLEELSL LAKSAGASPA VTLTGRRSSP DAAMFIGSGK AEELRLACEA NDIEIVIFNH ALSPAQQRNL ERALNRRVVD RTSLILDIFA QRARSHEGKL QVELAQLQYL ATRLVRAWTH LERQKGGIGL RGPGETQLET DRRLIGERIK MLQGKLAKLR RQHGTQRRQR ERTRTMSVSL VGYTNAGKST LFNALTKAQA YAADQLFATL DTTSRRVWLG DDVGQIVLSD TVGFIRELPH QLVAAFRATL QETVQADLLL HVVDASSSVR LDQIDQVNEV LHEIGADTIR QVLVFNKIDA VPELAARGGT VERDEYGNIS RVFLSARTGV GLDALRAAIA EIATAEPLAQ PSQFLAADWS AAPLEQPSRE PELGR // ID A0A0A6UFI4_ACTUT Unreviewed; 470 AA. AC A0A0A6UFI4; DT 04-FEB-2015, integrated into UniProtKB/TrEMBL. DT 04-FEB-2015, sequence version 1. DT 05-JUL-2017, entry version 20. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=MB27_26775 {ECO:0000313|EMBL:KHD74722.1}, GN MB27_36225 {ECO:0000313|EMBL:KHD73089.1}; OS Actinoplanes utahensis. OC Bacteria; Actinobacteria; Micromonosporales; Micromonosporaceae; OC Actinoplanes. OX NCBI_TaxID=1869 {ECO:0000313|EMBL:KHD73089.1, ECO:0000313|Proteomes:UP000054537}; RN [1] {ECO:0000313|EMBL:KHD73089.1, ECO:0000313|Proteomes:UP000054537} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NRRL 12052 {ECO:0000313|EMBL:KHD73089.1, RC ECO:0000313|Proteomes:UP000054537}; RA Velasco-Bucheli B., del Cerro C., Hormigo D., Garcia J.L., Acebal C., RA Arroyo M., de la Mata I.; RT "Draft genome sequence of Actinoplanes utahensis NRRL 12052."; RL Submitted (OCT-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KHD73089.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JRTT01000133; KHD73089.1; -; Genomic_DNA. DR EMBL; JRTT01000037; KHD74722.1; -; Genomic_DNA. DR EnsemblBacteria; KHD73089; KHD73089; MB27_36225. DR EnsemblBacteria; KHD74722; KHD74722; MB27_26775. DR Proteomes; UP000054537; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 2. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000313|EMBL:KHD73089.1}; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000054537}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900, KW ECO:0000313|EMBL:KHD73089.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000054537}. FT DOMAIN 252 417 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 211 245 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 470 AA; 51343 MW; C931D8D383CCBF4B CRC64; MRNTYQTPVL DELDPTTGDL ELEERHSLRR VAGLSTELTD VTEVEYRQLR LERVVLVGVW TEGSVEDADN SLTELAALAE TAGSQVLEGL IQRRKQPDAA TFIGRGKVDE LRDVVVMTGA DTVICDGELS PSQLRNLEQQ VKVKVVDRTA LILDIFAQHA KSREGKAQVE LAQLQYLLPR LRGWGESLSR QGGGAGGGSG GGGVGTRGPG ETKLETDRRR INTRIAKLRR EIKAMKTVRE TKRSRRVANG IPAVAIAGYT NAGKSSLLNR LTQAGVLVEN ALFATLDPTT RRTAAEDGRV FTLSDTVGFV RHLPHQIVEA FRSTLEEVAQ SDLVVHVVDG AHPDPEGQVS AVREVLGEVG ADRLPELLVI NKVDAADEET VLRLKRAWPD AVFVSARSGT GIAELHKAIA DRLPRPAVEM RILIPYDRGD LVARIHRSGQ VLQSRHLDDG TELTVRVDEQ FAAELSGFRA // ID A0A0A6Y193_9BACI Unreviewed; 417 AA. AC A0A0A6Y193; DT 04-FEB-2015, integrated into UniProtKB/TrEMBL. DT 04-FEB-2015, sequence version 1. DT 07-JUN-2017, entry version 17. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=NG54_05505 {ECO:0000313|EMBL:KHD86072.1}; OS Bacillus ginsengihumi. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus. OX NCBI_TaxID=363870 {ECO:0000313|EMBL:KHD86072.1, ECO:0000313|Proteomes:UP000030588}; RN [1] {ECO:0000313|EMBL:KHD86072.1, ECO:0000313|Proteomes:UP000030588} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=M2.11 {ECO:0000313|EMBL:KHD86072.1, RC ECO:0000313|Proteomes:UP000030588}; RA Toymentseva A., Boulygina E.A., Kazakov S.V., Kayumov I., RA Suleimanova A.D., Mardanova A.M., Maria S.N., Sergey M.Y., RA Sharipova M.R.; RT "Draft genome of phytase producing Bacillus ginsengihumi strain RT M2.11."; RL Submitted (OCT-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KHD86072.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JRUN01000011; KHD86072.1; -; Genomic_DNA. DR RefSeq; WP_035353776.1; NZ_JRUN01000011.1. DR EnsemblBacteria; KHD86072; KHD86072; NG54_05505. DR Proteomes; UP000030588; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000030588}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000030588}. FT DOMAIN 199 360 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 417 AA; 47840 MW; 0389EDB6812FDD24 CRC64; MNEEMLKEKV IIVGCQLNDH QERFLYSMDE LKSLTETAQG TVVMQVTQNR ERVDASTYIG KGKVEEIKAL EEELEVDLII FNDELSPSQL RNLAKHFSSR VIDRTQLILD IFAQRARSKE GKLQVELAQL QYLLPRLGGQ GADLSRLGGG IGTRGPGETK LESDRRHIRR RISEIKTQLN TIVHHRERYR ERRKRNQAFQ IALVGYTNAG KSTLFNRLSS ADSYEENQLF ATLDPMTRKF VLPSGYSALL TDTVGFIQDL PTTLIAAFRS TLEEVKEADL LLHVVDASNP DYDQHQKTVQ HLLEELQMDH LPQFTVYNKI DEQHPNFIPT VTNCILMSAL KEEDRLQLKI EIEKQVLHTM IPYDALIPQT GGKLLSTLKN DTILRELVFQ EDEQAYRCKG YVLPNHPVLG LLKQYER // ID A0A0A6YSR3_9FLAO Unreviewed; 396 AA. AC A0A0A6YSR3; DT 04-FEB-2015, integrated into UniProtKB/TrEMBL. DT 04-FEB-2015, sequence version 1. DT 07-JUN-2017, entry version 19. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=HMPREF9074_08801 {ECO:0000313|EMBL:KHE68920.1}; OS Capnocytophaga sp. oral taxon 329 str. F0087. OC Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales; OC Flavobacteriaceae; Capnocytophaga. OX NCBI_TaxID=706436 {ECO:0000313|EMBL:KHE68920.1, ECO:0000313|Proteomes:UP000030579}; RN [1] {ECO:0000313|EMBL:KHE68920.1, ECO:0000313|Proteomes:UP000030579} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=F0087 {ECO:0000313|EMBL:KHE68920.1, RC ECO:0000313|Proteomes:UP000030579}; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Hou S., Chen J., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Zhang X., Suruliraj S., Warren W., Chinwalla A., RA Mardis E.R., Wilson R.K.; RL Submitted (OCT-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KHE68920.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFHP02000141; KHE68920.1; -; Genomic_DNA. DR RefSeq; WP_009390964.1; NZ_KN390019.1. DR STRING; 706436.HMPREF9074_03266; -. DR EnsemblBacteria; KHE68920; KHE68920; HMPREF9074_08801. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR Proteomes; UP000030579; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000030579}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000030579}. FT DOMAIN 200 385 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 396 AA; 45697 MW; 2599E4A462F7AF7D CRC64; MLEQVNLTYE KVVLIGIINQ LQTEEKSKEY LDELEFLTYT AGGEVLKRFT QKLDVPNPKT FIGTGKMEEV QQYVEENEVG TVIFDDELTP AQQKNIERIL KAKILDRTGL ILDIFAQRAQ TSYSRTQVEL AQYEYLLPRL TGLWTHLERQ RGGIGMRGPG ETEIETDRRI VRDRIALLKK KLSAIDKQMA TQRSNRGALV RVALIGYTNV GKSTLMNVIS KSEVFAENKL FATLDTTVRK VVIENLPFLL SDTVGFIRKL PTQLIESFKS TLDEVREADL LLHVVDISHP NFEEHIQSVN QILAEIHSAD KPTIMVFNKI DAYTHEVIAE DDLATERTTK HFTLEEWKQT WMQKVGKDVL FISALNKENL EEFRKVVYEK VKEIHITRFP YNNFLY // ID A0A0A7EF24_9GAMM Unreviewed; 427 AA. AC A0A0A7EF24; DT 04-MAR-2015, integrated into UniProtKB/TrEMBL. DT 04-MAR-2015, sequence version 1. DT 30-AUG-2017, entry version 15. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=OM33_05470 {ECO:0000313|EMBL:AIY64651.1}; OS Pseudoalteromonas sp. OCN003. OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales; OC Pseudoalteromonadaceae; Pseudoalteromonas. OX NCBI_TaxID=1348114 {ECO:0000313|EMBL:AIY64651.1, ECO:0000313|Proteomes:UP000030341}; RN [1] {ECO:0000313|EMBL:AIY64651.1, ECO:0000313|Proteomes:UP000030341} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=OCN003 {ECO:0000313|EMBL:AIY64651.1, RC ECO:0000313|Proteomes:UP000030341}; RA Beurmann S., Videau P., Ushijima B., Smith A.M., Aeby G.S., RA Callahan S.M., Belcaid M.; RT "Complete Genome Sequence of Pseudoalteromonas sp. Strain OCN003 RT Isolated from Kaneohe Bay, Oahu, Hawaii."; RL Submitted (NOV-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP009888; AIY64651.1; -; Genomic_DNA. DR RefSeq; WP_038639719.1; NZ_CP009888.1. DR EnsemblBacteria; AIY64651; AIY64651; OM33_05470. DR KEGG; pseo:OM33_05470; -. DR KO; K03665; -. DR Proteomes; UP000030341; Chromosome 1. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000030341}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000030341}. FT DOMAIN 198 365 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 427 AA; 48392 MW; 441D1EA6F4F9591A CRC64; MFDRYEAGEQ AVLVHIEFPN EGDREDLQEL EMLVSSAGVN ALTIVQGSRQ SPHAKFFVGS GKAEEIAEIV KIHDADVIIF NHELSPSQER NLEAICKCRV LDRTSLILDI FAQRARTHEG KLQVELAQLR HISTRLIRGW THLERQKGGI GLRGPGETQL ETDRRLIRGK IKNILKRLEK VAKQREQGRR ARNRNEIPTV SLVGYTNAGK STLFNRITDS DVYAADQLFA TLDPTLRKIE VPDLGSTILA DTVGFIRHLP HDLVAAFKST LAETREADLQ LHVVDVADAR RQENIEQVQD VLREIDADDV PQLLVYNKID LVEEISPRID RNDEGRPIRV WLSAQTGVGC ELLLQAIGEC LAEQMFDENM CIPPKLGRLQ GALYRLNAVQ KESFDEHGNW LLDVRLPMSD WQRLKKEFGE QITELVV // ID A0A0A7FWW4_9CLOT Unreviewed; 599 AA. AC A0A0A7FWW4; DT 04-MAR-2015, integrated into UniProtKB/TrEMBL. DT 04-MAR-2015, sequence version 1. DT 07-JUN-2017, entry version 17. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:AIY83286.1}; GN ORFNames=U729_3045 {ECO:0000313|EMBL:AIY83286.1}; OS Clostridium baratii str. Sullivan. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=1415775 {ECO:0000313|EMBL:AIY83286.1, ECO:0000313|Proteomes:UP000030635}; RN [1] {ECO:0000313|EMBL:AIY83286.1, ECO:0000313|Proteomes:UP000030635} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Sullivan {ECO:0000313|EMBL:AIY83286.1}; RX PubMed=25489752; DOI=10.1016/j.meegid.2014.12.002; RA Smith T.J., Hill K.K., Xie G., Foley B.T., Williamson C.H., RA Foster J.T., Johnson S.L., Chertkov O., Teshima H., Gibbons H.S., RA Johnsky L.A., Karavis M.A., Smith L.A.; RT "Genomic sequences of six botulinum neurotoxin-producing strains RT representing three clostridial species illustrate the mobility and RT diversity of botulinum neurotoxin genes."; RL Infect. Genet. Evol. 30:102-113(2014). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP006905; AIY83286.1; -; Genomic_DNA. DR RefSeq; WP_039316462.1; NZ_CP006905.1. DR EnsemblBacteria; AIY83286; AIY83286; U729_3045. DR GeneID; 31580227; -. DR KEGG; cbv:U729_3045; -. DR KO; K03665; -. DR Proteomes; UP000030635; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000030635}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000030635}. FT DOMAIN 364 542 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 599 AA; 67408 MW; 49522FB4C58AF527 CRC64; MIHGNVEGIK NSYLSELDDL YSVKTLKQEA CNIEIIETIS RISSQIEREV SIAIDRRGKV TSIAIGDSTS VELPVLDINE KRLAGVRVIH THPNGLCNLS ALDLTALLKL KLDAIISIGI YDGKIIDFSL ANLTVYNDNL VYEEMQNLSL EKLMSIDILE KIRYAESLIK ENDVIEDDGE KAILVGSDTR ESLDELAELT KACDIPVLAK VYQGRSKIDP AFFIGRGKVL EIAHLRQTER ANVIIFDDEL SGSQVRNLEN AIGAKVIDRT TLILEIFARR AKSKEANIQV ELAQLKYRLS RLQGLGTVLS RTGGGIGTRG PGEKKLETDR RHIRETIYDL NSELKKIKKI REVQREKRNK ESIPKVSLVG YTNAGKSTLR NALCKIAASK DNRHKEEVFE ADMLFATLDI TTRAIILKNK GLITLTDTVG FVRKLPHDLV EAFKSTLEEV IYSDLLCHVV DASSDDCLDQ IKAVEEVLSE LGAIDKETIL VLNKVDKISE EVLDEIEEKL SYYDNVIRIS AKEELNLDKL LEEIEEKLPY SLKKCEYIIP YDKGDVVSFL HRNGRILSED YVNEGTKLTV EVDTEAYNKT KEYIINELN // ID A0A0A7I3L9_9BIFI Unreviewed; 498 AA. AC A0A0A7I3L9; DT 04-MAR-2015, integrated into UniProtKB/TrEMBL. DT 04-MAR-2015, sequence version 1. DT 12-APR-2017, entry version 17. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=AH68_07480 {ECO:0000313|EMBL:AIZ14917.1}; OS Bifidobacterium kashiwanohense PV20-2. OC Bacteria; Actinobacteria; Bifidobacteriales; Bifidobacteriaceae; OC Bifidobacterium. OX NCBI_TaxID=1447716 {ECO:0000313|EMBL:AIZ14917.1, ECO:0000313|Proteomes:UP000030625}; RN [1] {ECO:0000313|EMBL:AIZ14917.1, ECO:0000313|Proteomes:UP000030625} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=PV20-2 {ECO:0000313|EMBL:AIZ14917.1, RC ECO:0000313|Proteomes:UP000030625}; RX PubMed=25614572; RA Vazquez-Gutierrez P., Lacroix C., Chassard C., Klumpp J., Jans C., RA Stevens M.J.; RT "Complete and Assembled Genome Sequence of Bifidobacterium RT kashiwanohense PV20-2, Isolated from the Feces of an Anemic Kenyan RT Infant."; RL Genome Announc. 3:0-0(2015). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP007456; AIZ14917.1; -; Genomic_DNA. DR EnsemblBacteria; AIZ14917; AIZ14917; AH68_07480. DR KEGG; bka:AH68_07480; -. DR KO; K03665; -. DR Proteomes; UP000030625; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000030625}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}. FT DOMAIN 278 444 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 498 AA; 54670 MW; 12139DF522A1E843 CRC64; MPLSQENDIE HSMSANDVSG VLADQSEVLL DTNGENHFNE SHDEQWQERE SRNALKHVSG LGEIQDVTEV EYRKVRLERV VLVGVWSSRE TTQAQAEESL RELAALAETA GAVVCDGLLQ HRIKPDAATY VGSGKARELA GIVAQEEADT IVVDDDLPPS QRRALEDATK VKVVDRTAVI LDIFAQHATS REGKAQVELA QLQYMLPRLR GWGGSLSRQA GGRAAGDAGI GSRGPGETKI EMDRRVIRSR IAKLRKQIEQ MAPARDVKRG ARRRFGLPTV AVVGYTNAGK SSLTNRLTGS AELVENALFA TLDTAVRRAR AKDGRQYAYV DTVGFVRRLP TQLIEAFKST LEEVSESDLI VHVVDGSHPD PFSQIDAVDD VLSDIDGVET IPTIIVFNKA DRMDEATHER IEALMPEAYI VSAFSGEGVD ELRMQVESML PTPNVHVEAL LPYTAGSLVS RVREYGKVIN VEYRDDGMML EAEVDDHLAA QIVEQSIG // ID A0A0A7I9A0_9BIFI Unreviewed; 505 AA. AC A0A0A7I9A0; DT 04-MAR-2015, integrated into UniProtKB/TrEMBL. DT 04-MAR-2015, sequence version 1. DT 12-APR-2017, entry version 14. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=AH67_06560 {ECO:0000313|EMBL:AIZ16616.1}; OS Bifidobacterium pseudolongum PV8-2. OC Bacteria; Actinobacteria; Bifidobacteriales; Bifidobacteriaceae; OC Bifidobacterium. OX NCBI_TaxID=1447715 {ECO:0000313|EMBL:AIZ16616.1, ECO:0000313|Proteomes:UP000030636}; RN [1] {ECO:0000313|EMBL:AIZ16616.1, ECO:0000313|Proteomes:UP000030636} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=PV8-2 {ECO:0000313|EMBL:AIZ16616.1, RC ECO:0000313|Proteomes:UP000030636}; RX PubMed=25614573; RA Vazquez-Gutierrez P., Lacroix C., Chassard C., Klumpp J., RA Stevens M.J., Jans C.; RT "Bifidobacterium pseudolongum Strain PV8-2, Isolated from a Stool RT Sample of an Anemic Kenyan Infant."; RL Genome Announc. 3:0-0(2015). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP007457; AIZ16616.1; -; Genomic_DNA. DR EnsemblBacteria; AIZ16616; AIZ16616; AH67_06560. DR KEGG; bpsp:AH67_06560; -. DR KO; K03665; -. DR Proteomes; UP000030636; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000030636}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000030636}. FT DOMAIN 281 447 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 505 AA; 55106 MW; 40C0E708354AB949 CRC64; MTESTQSWQG DQELTDQGAP GAHGLLADQS DVLLDDDGMG AQPGDEIWRE RESRNQLKHV VGLGELEDVT EVEYRKVRLE RVVLVGVWSS RNGSQREAEE SLRELAALAE TAGAQVCDAV LQHRYRPDPS TYVGSGKAQE IAQIVAANDA DTIIVDDDLP PSQRRALEDA TKVKVVDRTA VILDIFAQHA TSREGKAQVE LAQLQYMLPR LRGWGAALSR QAGGRAAGAD GGIGSRGPGE TKIEMDRRVI RTRIARLRRQ IAQMAPAREV KRGSRKRYAL PTISVVGYTN AGKSSLTNRL TGSDELVENA LFATLDTAVR RARAKDGRFY AYVDTVGFVR RLPTQLVEAF KSTLEEIGES DVMVHVVDAS HPDPFGQIDA VNEVLKTIDG VDRLPVVTVF NKVDLIDAVT RERLEQLAPG TFFVSSATGE GVDALRAHIE GMLPAPGVHV EALLPYTAGS LVSQIREYGN VDAVEYRDTG ILLQADVDER LAAQIMDQAL EEPVD // ID A0A0A7KK80_9DEIO Unreviewed; 569 AA. AC A0A0A7KK80; DT 04-MAR-2015, integrated into UniProtKB/TrEMBL. DT 04-MAR-2015, sequence version 1. DT 30-AUG-2017, entry version 17. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=QR90_12000 {ECO:0000313|EMBL:AIZ45644.1}; OS Deinococcus swuensis. OC Bacteria; Deinococcus-Thermus; Deinococci; Deinococcales; OC Deinococcaceae; Deinococcus. OX NCBI_TaxID=1182571 {ECO:0000313|EMBL:AIZ45644.1, ECO:0000313|Proteomes:UP000030634}; RN [1] {ECO:0000313|Proteomes:UP000030634} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DY59 {ECO:0000313|Proteomes:UP000030634}; RA Jung H.-Y., Kim M.K., Srinivasan S., Lim S.; RT "Hymenobacter sp. DG25B genome submission."; RL Submitted (NOV-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP010028; AIZ45644.1; -; Genomic_DNA. DR RefSeq; WP_039684837.1; NZ_CP010028.1. DR EnsemblBacteria; AIZ45644; AIZ45644; QR90_12000. DR KEGG; dsw:QR90_12000; -. DR KO; K03665; -. DR Proteomes; UP000030634; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000030634}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000030634}. FT DOMAIN 382 550 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 569 AA; 61969 MW; 3BA907C082AF6EC5 CRC64; MLGNTSGLRP AQLKSLGNLY RRRVEPGRVG SPELARTLAE LSHEIRREVS VLIDRRGRVL SVSVADAKAA ELPAIRAGEN RLAGYHLLHA HPKGGPLSKG DLSALFLNRL DAVSAIDAKN EGQPGMVYTA HLTPPGTVGE EEDWRILPPV PVFQIDDFDL GAQVSALEEE IARAARTRES KKDRERALLV QIDQGEFDAE ERLEELGELA RTAGAEVVYK ELIYRRNLKA GTLVGAGKLE ELTSRAYHLD ADLLIFGQEL GAAQAREIEA ATGLKVIDRT QLILDIFALH AQGVESRLQV ELAQLRYMKP RLLGAGAQLS RIGGGGGSAA GGAIGTRGPG ETKLELDRRR INDRLSFLEK QLEGGSLRRE ERRKSRERND IPVVSIVGYT NAGKSTLLNA FTHAMDAPRR VLAANKLFAT LRPTSRQGFI DGIGPVIFTD TVGFIRDLPK DLTRAFRATL EEIGDADVLL HVVDAASPGA DTRLSAVNRI LEDLGFVEMS TVVALNKADA AEPDALEREV ERTEGVPVSA LKSIGIPELK EALADAIGQV QRRELAQREE ARELAAQYR // ID A0A0A7LQ53_9BACT Unreviewed; 412 AA. AC A0A0A7LQ53; DT 04-MAR-2015, integrated into UniProtKB/TrEMBL. DT 04-MAR-2015, sequence version 1. DT 05-JUL-2017, entry version 17. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=PK28_16550 {ECO:0000313|EMBL:AIZ65324.1}; OS Hymenobacter sp. DG25B. OC Bacteria; Bacteroidetes; Cytophagia; Cytophagales; Hymenobacteraceae; OC Hymenobacter. OX NCBI_TaxID=1385664 {ECO:0000313|EMBL:AIZ65324.1, ECO:0000313|Proteomes:UP000030789}; RN [1] {ECO:0000313|EMBL:AIZ65324.1, ECO:0000313|Proteomes:UP000030789} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DG25B {ECO:0000313|EMBL:AIZ65324.1, RC ECO:0000313|Proteomes:UP000030789}; RA Jung H.-Y., Kim M.K., Srinivasan S., Lim S.; RT "Hymenobacter radioresistens genome sequence."; RL Submitted (NOV-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP010054; AIZ65324.1; -; Genomic_DNA. DR EnsemblBacteria; AIZ65324; AIZ65324; PK28_16550. DR KEGG; hyd:PK28_16550; -. DR KO; K03665; -. DR Proteomes; UP000030789; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000030789}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000030789}. FT DOMAIN 207 398 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 175 202 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 412 AA; 46281 MW; 07524524346C9606 CRC64; MLAKSEKGTY ETSPEEETAV LVAVPDKRQA DVLTQEYLDE LAFLAETAGA TVTKRFVQRL EKPDIRTFVG EGKLAEIKAY VQHSGASMVI FDDDLSPSQL RNLEAELKVK IVDRSLLIID IFASRAQSAT ARTQVELAQY QYLLPRLTGL WTHLDKQRGG VGQRGPGETE IETDRRVARD RIAFLKEKLK ELDKQSHTQR KTRTSTVRVA LVGYTNVGKS TIMNLLSRAD VFAENKLFAT VDSTVRKVVL DTVPFLLSDT VGFIRKLPTR LIESFKSTLD EIREADLLVH VVDISHPSFE EHIAVVNDTL KDIGASDKPT LLVFNKIDQY DLHAEANHHG GFEGMNPDED ETPRPTLEQL QATYMAKMHD PVIFISAQER TNIDELRALL VRHVSAIQQR RFPNQPIPEA AG // ID A0A0A7RZT4_9GAMM Unreviewed; 432 AA. AC A0A0A7RZT4; DT 04-MAR-2015, integrated into UniProtKB/TrEMBL. DT 04-MAR-2015, sequence version 1. DT 30-AUG-2017, entry version 15. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=FPB0191_00288 {ECO:0000313|EMBL:AJA44132.1}; OS Frischella perrara. OC Bacteria; Proteobacteria; Gammaproteobacteria; Orbales; Orbaceae; OC Frischella. OX NCBI_TaxID=1267021 {ECO:0000313|EMBL:AJA44132.1, ECO:0000313|Proteomes:UP000030901}; RN [1] {ECO:0000313|EMBL:AJA44132.1, ECO:0000313|Proteomes:UP000030901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=PEB0191 {ECO:0000313|EMBL:AJA44132.1}; RX PubMed=25527542; RA Engel P., Vizcaino M.I., Crawford J.M.; RT "Gut symbionts from distinct hosts exhibit genotoxic activity via RT divergent colibactin biosynthetic pathways."; RL Appl. Environ. Microbiol. 0:0-0(2014). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP009056; AJA44132.1; -; Genomic_DNA. DR RefSeq; WP_039103473.1; NZ_CP009056.1. DR EnsemblBacteria; AJA44132; AJA44132; FPB0191_00288. DR KEGG; fpp:FPB0191_00288; -. DR KO; K03665; -. DR Proteomes; UP000030901; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000030901}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000030901}. FT DOMAIN 198 365 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 432 AA; 49062 MW; 3CA23467C47376DD CRC64; MFERYKGGEK ALLVHVFFSH ESDIEDLKEF EVLVSSARIE ILDIITTSRK SPQIKYFVGE GKAQEIAELV KLHNASVILV NHSLTPTQER NLEKLCECRV VDRTGLILDI FAQRARTHEG KLQVELAQLQ YLSTRLVRGW THLERQKGGI GLRGPGETQL ETDRRLIRHR IQVILNRLDK VEKQRALNRQ SRLKANLSTV SLVGYTNAGK STLFNALTNS DVYAANQLFA TLDPTLRRIQ VEDVGEIVLA DTVGFIRHLP HDLVAAFKAT LLETKESELI LHVIDASNAN LYDNIEAVDQ VLTEIGADNI PVLLIMNKID LLDGRQASID RDENGLPFRV WLSAENKVGL DLLLLALKER LCKQIYNCHI KLPINLISLR SRFYQLNSIV KEIVNEDGSF SLAIRIPLIE WNRLCKQNPD LLYLINDKVE IS // ID A0A0A7UYW0_9ARCH Unreviewed; 356 AA. AC A0A0A7UYW0; DT 04-MAR-2015, integrated into UniProtKB/TrEMBL. DT 04-MAR-2015, sequence version 1. DT 07-JUN-2017, entry version 13. DE SubName: Full=GTP-binding protein HflX {ECO:0000313|EMBL:AJA91972.1}; GN Name=hflX {ECO:0000313|EMBL:AJA91972.1}; GN ORFNames=T478_1323 {ECO:0000313|EMBL:AJA91972.1}; OS Candidatus Nitrosopelagicus brevis. OC Archaea; Thaumarchaeota; unclassified Thaumarchaeota. OX NCBI_TaxID=1410606 {ECO:0000313|EMBL:AJA91972.1, ECO:0000313|Proteomes:UP000030944}; RN [1] {ECO:0000313|EMBL:AJA91972.1, ECO:0000313|Proteomes:UP000030944} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=V2 {ECO:0000313|Proteomes:UP000030944}; RX PubMed=25587132; DOI=10.1073/pnas.1416223112; RA Santoro A.E., Dupont C.L., Richter R.A., Craig M.T., Carini P., RA McIlvin M.R., Yang Y., Orsi W.D., Moran D.M., Saito M.A.; RT "Genomic and proteomic characterization of "Candidatus RT Nitrosopelagicus brevis": an ammonia-oxidizing archaeon from the open RT ocean."; RL Proc. Natl. Acad. Sci. U.S.A. 112:1173-1178(2015). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP007026; AJA91972.1; -; Genomic_DNA. DR RefSeq; WP_048106228.1; NZ_CP007026.1. DR EnsemblBacteria; AJA91972; AJA91972; T478_1323. DR GeneID; 24817202; -. DR KEGG; nbv:T478_1323; -. DR KO; K03665; -. DR Proteomes; UP000030944; Chromosome. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000030944}; KW Reference proteome {ECO:0000313|Proteomes:UP000030944}. FT DOMAIN 184 355 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 356 AA; 40670 MW; 0112267D0FA7456E CRC64; MKSCILITNV NENISLEAKS LCEAAQYNVL YTIKVDDLQK RKYGITESKV EELEEKLEKL KPDVIVFDEL LKPNQNYSLA AKLKIEIVDR ESLILEIFEN RASSAESKLQ VKLAQLRYER ARAKERVRLA KGGEQPGFMG IGKYDIDAYY DDIKNRGTVI KKKLEKAGKQ RALHRQGRDR LGFKTISLAG YTSAGKTTLF NNLTGETKEK SAELFTTLTT TTRRLKLGRE ISLITDTVGF ISKLPAYMIE AFKSTLEELI FTDIILLVID SLDDDELMKK KFSTCYKTLV ELGVERKNMI FLFNKSESID DKKFLHVMNN LKIDEVENCL DVSALTGKNL TDLKQILQKR FYGKTE // ID A0A0A8BA12_9ACTN Unreviewed; 423 AA. AC A0A0A8BA12; DT 04-MAR-2015, integrated into UniProtKB/TrEMBL. DT 04-MAR-2015, sequence version 1. DT 07-JUN-2017, entry version 16. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=JI75_04130 {ECO:0000313|EMBL:AJC11977.1}; OS Coriobacteriaceae bacterium 68-1-3. OC Bacteria; Actinobacteria; Coriobacteriia; Coriobacteriales; OC Coriobacteriaceae. OX NCBI_TaxID=1531429 {ECO:0000313|EMBL:AJC11977.1, ECO:0000313|Proteomes:UP000031121}; RN [1] {ECO:0000313|Proteomes:UP000031121} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=68-1-3 {ECO:0000313|Proteomes:UP000031121}; RA Looft T., Bayles D.O., Stanton T.B.; RT "Coriobacteriaceae sp. complete genome."; RL Submitted (AUG-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP009302; AJC11977.1; -; Genomic_DNA. DR RefSeq; WP_039690493.1; NZ_CP009302.1. DR EnsemblBacteria; AJC11977; AJC11977; JI75_04130. DR KEGG; cbac:JI75_04130; -. DR KO; K03665; -. DR Proteomes; UP000031121; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000031121}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000031121}. FT DOMAIN 205 370 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 423 AA; 46312 MW; 582A16FD2BC8C29D CRC64; MTAVEAPRER AVVVGVDRPG LDWPVASSLQ ELSRLVDTAG AEVVGSFTQR LVKPNPRTLI GSGKVSEIAE AARSLKADVV VFDDELTPSQ QANLEKGFDK AIKVLDRTAL ILDIFALHAT TKEGRLQVKL AQNQYLLPRL RGMWAHLASN RMGGGVGSRF GEGESQLEVD RRMVRKRITS IKRELEHVKS VRSVQREGRY STGVFKVAIA GYTNAGKSTL INHLTDAGVY SDDKLFATLD STTRRFALPE GRIITLTDTV GFIKKLPTTL VESFKSTLDE INGADLILHV VDASSDELSF HIEAVNEVLG QIGAEKIPRL LVFNKTDALD EATLGAFRKR YSEGVFISAA TGDGMDDLLA VVSHAASADE ALFEVEIPFS CGELVSLAHE RCRVVSESYT EQGTRLSLFV PPAHERFFRP YAI // ID A0A0A8HQ89_STAHY Unreviewed; 409 AA. AC A0A0A8HQ89; DT 04-MAR-2015, integrated into UniProtKB/TrEMBL. DT 04-MAR-2015, sequence version 1. DT 30-AUG-2017, entry version 17. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:AJC96308.1}; GN ORFNames=SHYC_07845 {ECO:0000313|EMBL:AJC96308.1}; OS Staphylococcus hyicus. OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae; OC Staphylococcus. OX NCBI_TaxID=1284 {ECO:0000313|EMBL:AJC96308.1, ECO:0000313|Proteomes:UP000031102}; RN [1] {ECO:0000313|EMBL:AJC96308.1, ECO:0000313|Proteomes:UP000031102} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 11249 {ECO:0000313|EMBL:AJC96308.1, RC ECO:0000313|Proteomes:UP000031102}; RX PubMed=25700402; RA Calcutt M.J., Foecking M.F., Hsieh H.Y., Adkins P.R., Stewart G.C., RA Middleton J.R.; RT "Sequence Analysis of Staphylococcus hyicus ATCC 11249T, an RT Etiological Agent of Exudative Epidermitis in Swine, Reveals a Type RT VII Secretion System Locus and a Novel 116-Kilobase Genomic Island RT Harboring Toxin-Encoding Genes."; RL Genome Announc. 3:e01525-14(2015). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP008747; AJC96308.1; -; Genomic_DNA. DR RefSeq; WP_039645952.1; NZ_CP008747.1. DR EnsemblBacteria; AJC96308; AJC96308; SHYC_07845. DR KEGG; shu:SHYC_07845; -. DR KO; K03665; -. DR Proteomes; UP000031102; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000031102}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}. FT DOMAIN 205 366 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 178 201 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 409 AA; 47045 MW; 8190816F3AE0652C CRC64; MTYRQSYSTE KIKEKALLIG VHTQSSEFNF ESTMSELEAL SDTCGLEVKG TLSQNLKDMH PKHYMGKGKL QEVQDAVHFH DIDVIVTNDE LTTAQSKHLN DILGIKIIDR TQLILEIFAM RAQSKEGKLQ VEFAQLDYLL PRLMGHGKSL SRLGGGIGTR GPGETKLETD RRHIRTRMNE IKRKLKEVEI HRERYRQQRE QNEVFQIALV GYTNAGKSSW FNVLTEDETY EKNQLFATLD PKTRQITIND GFQLVISDTV GFIQKLPTTL IDAFKSTLVE AKQADLLIHV VDASHKEAKI QYETVLQLIK DLNMDHIPQV VLFNKKDLMH EAPPISPHAS LSVSSKDEQD QKRVRQLLFE QLKRQLTHYE TSLEVAKADQ LYTLKRHTLV TSIDFNETDE TYHIQGYRK // ID A0A0A8JEH9_BACSX Unreviewed; 423 AA. AC A0A0A8JEH9; DT 04-MAR-2015, integrated into UniProtKB/TrEMBL. DT 04-MAR-2015, sequence version 1. DT 07-JUN-2017, entry version 18. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=OXB_0533 {ECO:0000313|EMBL:BAQ09005.1}; OS Bacillus sp. (strain OxB-1). OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus. OX NCBI_TaxID=98228 {ECO:0000313|EMBL:BAQ09005.1, ECO:0000313|Proteomes:UP000031651}; RN [1] {ECO:0000313|Proteomes:UP000031651} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=OxB-1 {ECO:0000313|Proteomes:UP000031651}; RA Yamaguchi T., Asano Y.; RT "Complete genome of an aldoxime degrader Bacillus sp. OxB-1."; RL Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AP013294; BAQ09005.1; -; Genomic_DNA. DR RefSeq; WP_041071742.1; NZ_AP013294.1. DR EnsemblBacteria; BAQ09005; BAQ09005; OXB_0533. DR KEGG; baco:OXB_0533; -. DR KO; K03665; -. DR Proteomes; UP000031651; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000031651}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000031651}. FT DOMAIN 200 368 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 159 193 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 423 AA; 48484 MW; BAF89C4AB95A5C19 CRC64; MDILVEYAIL VGVHEQTDEH FDYTMEELKN LAEAIDVEVV GMVTQNLERR HPSLYVGKGK VGEIRRLYEE TDANLVIFND ELTPSQIRNM EQELECKVID RTMLILDIFA RRARTKESRM QVELAQLQYT LPRLVGLRAS LSRQGGGTGG GFQNKGAGET KLELDRRKIE DQIAKLRRDL EHMKDQRETQ RKQRKKSGTP VVSIVGYTNA GKSTLMNKLL AEMDPEHAKQ VFEEDMLFAT LDTSVRRVKL IDNKQFILTD TVGFVSKLPH HLVKAFRSTL EEARDADLLL HVVDVSNAEY QFMMNVTNDT LHDVGVENVE TLKVYNKADL ANVPYPEIRG DSVWISAKEE AGLEELISLI KKKIFEQYVT CKLLVPFERG DVVAYLNDKA TVKNTEYEED GTLLTVEMDI MERERFEEFI ISH // ID A0A0A8K3R5_9RHIZ Unreviewed; 444 AA. AC A0A0A8K3R5; DT 04-MAR-2015, integrated into UniProtKB/TrEMBL. DT 04-MAR-2015, sequence version 1. DT 07-JUN-2017, entry version 17. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=GL4_2150 {ECO:0000313|EMBL:BAQ17593.1}; OS Methyloceanibacter caenitepidi. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Methyloceanibacter. OX NCBI_TaxID=1384459 {ECO:0000313|EMBL:BAQ17593.1, ECO:0000313|Proteomes:UP000031643}; RN [1] {ECO:0000313|EMBL:BAQ17593.1, ECO:0000313|Proteomes:UP000031643} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Gela4 {ECO:0000313|EMBL:BAQ17593.1, RC ECO:0000313|Proteomes:UP000031643}; RA Takeuchi M., Susumu S., Kamagata Y., Oshima K., Hattori M., RA Iwasaki W.; RT "Genome sequencing of Methyloceanibacter caenitepidi Gela4."; RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AP014648; BAQ17593.1; -; Genomic_DNA. DR RefSeq; WP_052464375.1; NZ_AP014648.1. DR EnsemblBacteria; BAQ17593; BAQ17593; GL4_2150. DR KEGG; mcg:GL4_2150; -. DR KO; K03665; -. DR Proteomes; UP000031643; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000031643}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000031643}. FT DOMAIN 210 381 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 444 AA; 48579 MW; 7A531B21EEE3FFDA CRC64; MRAVVFAPIL DARAGRSRRE SSLSPSAGAA DRTPQARLEE AVGLAAAIDL DIRASGIVPV PQPKPATLFG SGKVEELAGL VRMEDADLVI VDHPLTPVQQ RNLETAWQAK VLDRTGLILE IFGERARTRE GRLQVELAHL VYQKSRLVRS WTHLERQRGG FGFLGGPGET QIETDRRLLS ERITKIQNEL EHVRQTRTLH RKSRQRVPYP AVALVGYTNA GKSTLFNTLT GAEVLAQDIL FATLDPTIRA LQLPNGSKSV LSDTVGFISD LPTTLVAAFR ATLEEVQEAD LILHVRDISD GASASQRADV NAVLADLGIN ADEEPDRVLE VWNKADLLDP DALEHARNEA ARHGAILVSA VSGEGLEALL AEIETRLNRR RQTLQIEVQP QEGALSNWIY ENCEVISRAD LGEGVVSLRI RVAPEKRDKL ARVAGASRLQ AAVE // ID A0A0A8UJY6_LEGHA Unreviewed; 422 AA. AC A0A0A8UJY6; DT 04-MAR-2015, integrated into UniProtKB/TrEMBL. DT 04-MAR-2015, sequence version 1. DT 07-JUN-2017, entry version 17. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:CEK09135.1}; GN ORFNames=LHA_0009 {ECO:0000313|EMBL:CEK09135.1}; OS Legionella hackeliae. OC Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales; OC Legionellaceae; Legionella. OX NCBI_TaxID=449 {ECO:0000313|EMBL:CEK09135.1, ECO:0000313|Proteomes:UP000032803}; RN [1] {ECO:0000313|EMBL:CEK09135.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC35250 {ECO:0000313|EMBL:CEK09135.1}; RA GOMEZ-VALERO Laura; RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LN681225; CEK09135.1; -; Genomic_DNA. DR RefSeq; WP_045104725.1; NZ_LN681225.1. DR EnsemblBacteria; CEK09135; CEK09135; LHA_0009. DR KEGG; lha:LHA_0009; -. DR KO; K03665; -. DR Proteomes; UP000032803; Chromosome I. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000032803}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}. FT DOMAIN 198 363 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 422 AA; 47377 MW; C384D46D9416FC02 CRC64; MFDRPQGGER AILVQLALPE VDAAKALAEF KELAISAQAE VVACVEGARS TPEAKYYVGL GKAEEIKQQV LAYEAELVLV NHELSPSQER NLERLLECRV VGRSGLILDI FAQRARTFEG KLQVELAQLQ HLSTRLVRGW THLERQKGGI GLRGPGETQL ETDRRLLRER IKSINKRLEK VRRSRDQNRR ARQKAALPTV SLVGYTNAGK STLFNALTGE HIYAANQLFA TLDPTMRKLE LPGSTSVILT DTVGFIRDLP HQLIEAFRAT LEETQEANLL LHVIDISDPH WRDMVLAVEQ VLDELGVKDI PMIQVFNKID QQENWEAKID QQEEGIKVWI SAKTGAGLDL LQQAISTQLQ GAIVEEEILL APTDAKLRAA LYEMDAVLGE KEELEGGWSL KIKLTQEQKK RLFSRHAKNL TP // ID A0A0A8X7F4_9BACI Unreviewed; 418 AA. AC A0A0A8X7F4; DT 04-MAR-2015, integrated into UniProtKB/TrEMBL. DT 04-MAR-2015, sequence version 1. DT 07-JUN-2017, entry version 16. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=SAMD00020551_3093 {ECO:0000313|EMBL:GAM14937.1}; OS Bacillus selenatarsenatis SF-1. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus. OX NCBI_TaxID=1321606 {ECO:0000313|EMBL:GAM14937.1, ECO:0000313|Proteomes:UP000031014}; RN [1] {ECO:0000313|EMBL:GAM14937.1, ECO:0000313|Proteomes:UP000031014} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SF-1 {ECO:0000313|EMBL:GAM14937.1, RC ECO:0000313|Proteomes:UP000031014}; RA Kuroda M., Sei K., Yamashita M., Ike M.; RT "Whole genome shotgun sequence of Bacillus selenatarsenatis SF-1."; RL Submitted (JUN-2013) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:GAM14937.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BASE01000071; GAM14937.1; -; Genomic_DNA. DR RefSeq; WP_041966633.1; NZ_BASE01000071.1. DR EnsemblBacteria; GAM14937; GAM14937; SAMD00020551_3093. DR Proteomes; UP000031014; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000031014}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000031014}. FT DOMAIN 199 361 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 418 AA; 47738 MW; D42AA00BF64B7A7C CRC64; MEQENVFEKV ILVGCQTTEE DLRFQYSMEE LESLTETAKG NVLMQVVQKR PKVHPATYIG KGKVEELQAL EEELEPDLII FNDELSPSQN RNLSAGLKAR VIDRTQLILD IFAQRARSKE GKLQVELAQL QYLLPRLGGK GIEMSRLGAG IGTRGPGETK LESDRRHIRK RIDDIKTQLS VIVQHRDRYR ERRKKNKTFQ IALVGYTNAG KSTLFNRLTE AESFEENQLF ATLDPMTRKA ILPSGFTALL TDTVGFIQDL PTTLIAAFRS TLEEVREADL LLHVVDMSSE DYFSHEQTVN KLLEDLEVHH IPQITVYNKR DIAHQDFVPN AKNETAFISA FSEEDRRNLL LKIEQSIIGM MEPFHVLVPS DEGKLLAQLK NETILRELAF DEEKQGYVCR GFSLVDHQIT GQLKRFSI // ID A0A0B0D1Z2_9BACI Unreviewed; 339 AA. AC A0A0B0D1Z2; DT 04-MAR-2015, integrated into UniProtKB/TrEMBL. DT 04-MAR-2015, sequence version 1. DT 07-JUN-2017, entry version 14. DE SubName: Full=GTPase {ECO:0000313|EMBL:KHE71956.1}; DE Flags: Fragment; GN ORFNames=LD39_07090 {ECO:0000313|EMBL:KHE71956.1}; OS Halobacillus sp. BBL2006. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Halobacillus. OX NCBI_TaxID=1543706 {ECO:0000313|EMBL:KHE71956.1, ECO:0000313|Proteomes:UP000030879}; RN [1] {ECO:0000313|EMBL:KHE71956.1, ECO:0000313|Proteomes:UP000030879} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BBL2006 {ECO:0000313|EMBL:KHE71956.1, RC ECO:0000313|Proteomes:UP000030879}; RA Kirchner G., Treves D., Francis J.III.; RT "Draft Genome Sequence of the Halophilic Bacterium Halobacillus sp. RT Strain BBL2006."; RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KHE71956.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JRNX01000202; KHE71956.1; -; Genomic_DNA. DR RefSeq; WP_035544524.1; NZ_JRNX01000202.1. DR EnsemblBacteria; KHE71956; KHE71956; LD39_07090. DR Proteomes; UP000030879; Unassembled WGS sequence. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000030879}; KW Reference proteome {ECO:0000313|Proteomes:UP000030879}. FT DOMAIN 197 339 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT NON_TER 339 339 {ECO:0000313|EMBL:KHE71956.1}. SQ SEQUENCE 339 AA; 38423 MW; 1FA5407149F9BA69 CRC64; MNAKEQVILI ARMDPQEQEE RFQSSLAELQ SLTETANGEV CKIITQKRDR VHPATYLGQG KLEEIKQAAD EVDADLVIFN DELSPGQLRN ITDRIERRVI DRSQLILDIF AGRARTKEGK LQVELAQLQY LLPRLAGQGT ELSRLGGGIG TRGPGETKLE TDRRHIQRRI DDIKIRLNTV VKQREQYRKR RKENKAFQIA IVGYTNAGKS TFFNRVTESE SFEEDLLFAT LDPLTRQMSL PSGFQAIVSD TVGFIQDLPT TLIAAFRSTL EEVTEADFII HMVDASHPDH IQQERTVLRL LDDLDASHLP ILTVYNKKDL LNDAFIPNTH PSLTVSVHD // ID A0A0B0EFV6_9BACT Unreviewed; 430 AA. AC A0A0B0EFV6; DT 04-MAR-2015, integrated into UniProtKB/TrEMBL. DT 04-MAR-2015, sequence version 1. DT 07-JUN-2017, entry version 15. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=SCABRO_02289 {ECO:0000313|EMBL:KHE91977.1}; OS Candidatus Scalindua brodae. OC Bacteria; Planctomycetes; Planctomycetia; Candidatus Brocadiales; OC Candidatus Brocadiaceae; Candidatus Scalindua. OX NCBI_TaxID=237368 {ECO:0000313|EMBL:KHE91977.1, ECO:0000313|Proteomes:UP000030652}; RN [1] {ECO:0000313|EMBL:KHE91977.1, ECO:0000313|Proteomes:UP000030652} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=RU1 {ECO:0000313|EMBL:KHE91977.1}; RA Speth D.R., Russ L., Kartal B., Op den Camp H.J., Dutilh B.E., RA Jetten M.S.; RT "Draft genome of anammox bacterium scalindua brodae, obtained using RT differential coverage binning of sequence data from two enrichment RT reactors."; RL Submitted (OCT-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KHE91977.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JRYO01000159; KHE91977.1; -; Genomic_DNA. DR PATRIC; fig|237368.3.peg.2471; -. DR Proteomes; UP000030652; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000030652}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000030652}. FT DOMAIN 202 368 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 430 AA; 48210 MW; 9F0A815D79D667EF CRC64; MVELKRTNLS VRSERAILLY TLLHKDKNDD APIEELKSLA ETAGAKVLDR VVQRRRKVDP SHYIGKGKVS QLAELCKDKK IDVVICDDDL TPAQVSNLEK IIDTKVIDRS ELILDIFAAR AKTAQAKLQV ELAQLEYTRP RLKRMWSHLS RIEGGIGTRG PGEKQLEVDK RLVSKRVLAL KKRLGQVTER RKRQAQSRKE HTTVSLVGYT NSGKSTLMNR LTEAGVLVED KLFATLDTKT SICDLGNGKK VILSDTVGFL RKLPHHLISS FEATLEEVIW ADFLLHVVDV SSPDVIEQVK AANNVLKELE CNKKPTIMVL NKVDVLKDSS IITFFQSKYD NVVTISALTG NGVEKLKQEM VGFANRGIAE IKLECNASNG KLLAYIYEHS QVLKRTFVNS GVNFHIMINE KNLSKLYQLG GGHFKVTQLS // ID A0A0B0HAQ5_SOVGS Unreviewed; 430 AA. AC A0A0B0HAQ5; DT 04-MAR-2015, integrated into UniProtKB/TrEMBL. DT 04-MAR-2015, sequence version 1. DT 30-AUG-2017, entry version 17. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:KHF26170.1}; GN ORFNames=JV46_15160 {ECO:0000313|EMBL:KHF26170.1}; OS Solemya velum gill symbiont. OC Bacteria; Proteobacteria; Gammaproteobacteria; OC sulfur-oxidizing symbionts. OX NCBI_TaxID=2340 {ECO:0000313|EMBL:KHF26170.1, ECO:0000313|Proteomes:UP000030856}; RN [1] {ECO:0000313|EMBL:KHF26170.1, ECO:0000313|Proteomes:UP000030856} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=WH {ECO:0000313|EMBL:KHF26170.1, RC ECO:0000313|Proteomes:UP000030856}; RX PubMed=25342549; DOI=10.1186/1471-2164-15-924; RA Dmytrenko O., Russell S.L., Loo W.T., Fontanez K.M., Liao L., RA Roeselers G., Sharma R., Stewart F.J., Newton I.L., Woyke T., Wu D., RA Lang J.M., Eisen J.A., Cavanaugh C.M.; RT "The genome of the intracellular bacterium of the coastal bivalve, RT Solemya velum: a blueprint for thriving in and out of symbiosis."; RL BMC Genomics 15:924-924(2014). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KHF26170.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JRAA01000001; KHF26170.1; -; Genomic_DNA. DR RefSeq; WP_043115904.1; NZ_JRAA01000001.1. DR EnsemblBacteria; KHF26170; KHF26170; JV46_15160. DR GeneID; 31575309; -. DR PATRIC; fig|2340.3.peg.680; -. DR Proteomes; UP000030856; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000030856}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000030856}. FT DOMAIN 200 367 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 430 AA; 48001 MW; CE9B6FAA0FA94201 CRC64; MELFERPDSG ERAVLVHVGF SGQPDEEELQ EFAELAGSAG AEAIAQLTGV RTSPDSRTFI GKGKLEELKE LLAMHDGELV IFDHELSPAQ ERNLEAELSC RVLDRSGLML DIFAQRARSF EGKLQVELAQ LKHLSTRLVR GWTHLERQKG GIGLRGPGET QLETDRRLIG ARITRIQKRL DKVDAQRELG RKARRRADTP TVSLVGYTNA GKSTLFNRLV EADVYAQDQL FATLDPTLRR LELPNNTSLV LADTVGFISR LPHELIAAFK STLQETIDAS LLLHVVDASN PQYQIQVAEV DDVLQQINAE TIPQLIVMNK IDRMEEVEPR IERDDEGRPI KVWLSAVSGE GINLLIEVLA ELAASEQVTK TVELPPSEGA LRAALYREAD ILEEKYSEKG DTIVSFRMPL RSFNQLKKNF PLLGEEPSAE // ID A0A0B0HKK6_9BACI Unreviewed; 56 AA. AC A0A0B0HKK6; DT 04-MAR-2015, integrated into UniProtKB/TrEMBL. DT 04-MAR-2015, sequence version 1. DT 07-JUN-2017, entry version 6. DE SubName: Full=GTPase HflX {ECO:0000313|EMBL:KHF29550.1}; GN Name=hflX_3 {ECO:0000313|EMBL:KHF29550.1}; GN ORFNames=LR68_01620 {ECO:0000313|EMBL:KHF29550.1}; OS Anoxybacillus sp. BCO1. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Anoxybacillus. OX NCBI_TaxID=1548750 {ECO:0000313|EMBL:KHF29550.1, ECO:0000313|Proteomes:UP000030702}; RN [1] {ECO:0000313|EMBL:KHF29550.1, ECO:0000313|Proteomes:UP000030702} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BCO1 {ECO:0000313|EMBL:KHF29550.1, RC ECO:0000313|Proteomes:UP000030702}; RA Patel B.K.; RT "Draft genome sequence of an Anoxybacillus isolate BCO1 associated RT with a thermophilic microbial mat colonising an outflow from a Great RT Artesian Basin bore well."; RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KHF29550.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JRLC01000009; KHF29550.1; -; Genomic_DNA. DR EnsemblBacteria; KHF29550; KHF29550; LR68_01620. DR PATRIC; fig|1548750.3.peg.1674; -. DR Proteomes; UP000030702; Unassembled WGS sequence. DR InterPro; IPR025121; GTPase_HflX_N. DR Pfam; PF13167; GTP-bdg_N; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000030702}; KW Reference proteome {ECO:0000313|Proteomes:UP000030702}. FT DOMAIN 23 56 GTP-bdg_N. {ECO:0000259|Pfam:PF13167}. SQ SEQUENCE 56 AA; 6385 MW; 7DB743FB8F695ED2 CRC64; MEKERVIIVG CQLPHVDDER FSYSLEELVS LVHTANGEVV ITLTQKRDTI HSATYI // ID A0A0B0HNP8_9BACI Unreviewed; 150 AA. AC A0A0B0HNP8; DT 04-MAR-2015, integrated into UniProtKB/TrEMBL. DT 04-MAR-2015, sequence version 1. DT 07-JUN-2017, entry version 11. DE SubName: Full=GTPase HflX {ECO:0000313|EMBL:KHF29549.1}; GN Name=hflX_2 {ECO:0000313|EMBL:KHF29549.1}; GN ORFNames=LR68_01619 {ECO:0000313|EMBL:KHF29549.1}; OS Anoxybacillus sp. BCO1. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Anoxybacillus. OX NCBI_TaxID=1548750 {ECO:0000313|EMBL:KHF29549.1, ECO:0000313|Proteomes:UP000030702}; RN [1] {ECO:0000313|EMBL:KHF29549.1, ECO:0000313|Proteomes:UP000030702} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BCO1 {ECO:0000313|EMBL:KHF29549.1, RC ECO:0000313|Proteomes:UP000030702}; RA Patel B.K.; RT "Draft genome sequence of an Anoxybacillus isolate BCO1 associated RT with a thermophilic microbial mat colonising an outflow from a Great RT Artesian Basin bore well."; RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KHF29549.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JRLC01000009; KHF29549.1; -; Genomic_DNA. DR EnsemblBacteria; KHF29549; KHF29549; LR68_01619. DR PATRIC; fig|1548750.3.peg.1673; -. DR Proteomes; UP000030702; Unassembled WGS sequence. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000030702}; KW Reference proteome {ECO:0000313|Proteomes:UP000030702}. FT DOMAIN 3 46 GTP-bdg_N. {ECO:0000259|Pfam:PF13167}. FT DOMAIN 48 126 GTP-bdg_M. {ECO:0000259|Pfam:PF16360}. SQ SEQUENCE 150 AA; 17123 MW; 5235DAE2FEBE187D CRC64; MRLVEQFEPD VVIFNDELSP SQNRNLTKLL NVRVIDRTQL ILDIFASRAR SKEGKLQVEL AQLQYILPRL SGQGAALSRL GGGIGTRGPG ETKLETDRRH IRRRIDEIKA QLKVIVEHRE RYRERRKKNA VFQIALVGYT NAGKSSFLTA // ID A0A0B0I2T0_9BACL Unreviewed; 429 AA. AC A0A0B0I2T0; DT 04-MAR-2015, integrated into UniProtKB/TrEMBL. DT 04-MAR-2015, sequence version 1. DT 07-JUN-2017, entry version 16. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX_2 {ECO:0000313|EMBL:KHF34031.1}; GN Synonyms=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=CM49_03701 {ECO:0000313|EMBL:KHF34031.1}; OS Paenibacillus sp. P1XP2. OC Bacteria; Firmicutes; Bacilli; Bacillales; Paenibacillaceae; OC Paenibacillus. OX NCBI_TaxID=1472719 {ECO:0000313|EMBL:KHF34031.1, ECO:0000313|Proteomes:UP000030851}; RN [1] {ECO:0000313|EMBL:KHF34031.1, ECO:0000313|Proteomes:UP000030851} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=P1XP2 {ECO:0000313|EMBL:KHF34031.1, RC ECO:0000313|Proteomes:UP000030851}; RA Adelskov J., Patel B.K.; RT "Draft genome of Paenibacillus sp. strain P1XP2 isolated from a RT commercial food-waste degrading bioreactor."; RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KHF34031.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JRNV01000027; KHF34031.1; -; Genomic_DNA. DR RefSeq; WP_036712201.1; NZ_JRNV01000027.1. DR EnsemblBacteria; KHF34031; KHF34031; CM49_03701. DR PATRIC; fig|1472719.3.peg.3988; -. DR Proteomes; UP000030851; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000030851}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000030851}. FT DOMAIN 204 375 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 163 190 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 429 AA; 48781 MW; 316B79B8CB7008E0 CRC64; MKQPELLETI DQRAVLVGVN LNNQRDFDYS MEELGNLAEA CGVEVVGQLT QNMERVNKSH YIGTGKVEEL AGLYKGLEAN LIIFNDELSP SQLRNLEADL ECKVIDRTIL ILDIFEKRAK TREAQLQVEV AQLQYMLPRL VGLRESLGRQ SGGVGLKNRG AGETKLELDR RRIEEKITAL NKELESLVFQ RQTQRKKRKK NELPVVSLVG YTNAGKSTIM NAMIERFGAA GSAEEKSVFE KDMLFATLET SVRNIQLEDN KSFLLTDTVG FVSKLPHHLV KAFRSTLEEV AEADLLIHVV DFANEKYEQL IEITENTLKD IGVTDIPTVF AYNKCDLTGR DIPEVQENGI YLAAKPRIGI DELVDLIKSF IFKDYVRCEM LIPYDQGQVV SYLNEHADIQ ATEYENEGTR LTLECRQKDY DRYREYVIG // ID A0A0B0I8G6_9BACL Unreviewed; 361 AA. AC A0A0B0I8G6; DT 04-MAR-2015, integrated into UniProtKB/TrEMBL. DT 04-MAR-2015, sequence version 1. DT 07-JUN-2017, entry version 14. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX_1 {ECO:0000313|EMBL:KHF36434.1}; GN Synonyms=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=CM49_01418 {ECO:0000313|EMBL:KHF36434.1}; OS Paenibacillus sp. P1XP2. OC Bacteria; Firmicutes; Bacilli; Bacillales; Paenibacillaceae; OC Paenibacillus. OX NCBI_TaxID=1472719 {ECO:0000313|EMBL:KHF36434.1, ECO:0000313|Proteomes:UP000030851}; RN [1] {ECO:0000313|EMBL:KHF36434.1, ECO:0000313|Proteomes:UP000030851} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=P1XP2 {ECO:0000313|EMBL:KHF36434.1, RC ECO:0000313|Proteomes:UP000030851}; RA Adelskov J., Patel B.K.; RT "Draft genome of Paenibacillus sp. strain P1XP2 isolated from a RT commercial food-waste degrading bioreactor."; RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KHF36434.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JRNV01000007; KHF36434.1; -; Genomic_DNA. DR EnsemblBacteria; KHF36434; KHF36434; CM49_01418. DR PATRIC; fig|1472719.3.peg.1532; -. DR Proteomes; UP000030851; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000030851}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000030851}. FT DOMAIN 166 330 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 361 AA; 39599 MW; 2AFBF54BE9EDA849 CRC64; MAETAGVEVL DVIPQNRDVP DARWLIGKGK VEELRQAILA VQANTAIFDH DLSGAQVRNL EQSLDVKIID RTQLILDIFA QRAKTREGII QVELAQLSYL LPRLSGHGKN LSRLGGGIGT RGPGESKLET DRRHIRSRIG DLKRQLEAVI KHRKLHRGRR QKSGAIQVAL VGYTNAGKST LLKQLTSADV YIENQLFATL DPTSRTLELP GGSEVILTDT VGFIQNLPHD LVAAFRATLE EANEADLILH VVDASSPMRE EQMKVVDSIL EDLGAADKPQ LVLFNKKDVC TQEQLEMLPS GPGHLKISAL DEGDLLAVKQ AIQGRLSGGI LSFRVLPRMA TPWLCCTGSG TLWSKNPKNM I // ID A0A0B0IM54_9BACI Unreviewed; 430 AA. AC A0A0B0IM54; DT 04-MAR-2015, integrated into UniProtKB/TrEMBL. DT 04-MAR-2015, sequence version 1. DT 07-JUN-2017, entry version 17. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=LQ50_08160 {ECO:0000313|EMBL:KHF40746.1}; OS Bacillus okhensis. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus. OX NCBI_TaxID=333138 {ECO:0000313|EMBL:KHF40746.1, ECO:0000313|Proteomes:UP000030832}; RN [1] {ECO:0000313|EMBL:KHF40746.1, ECO:0000313|Proteomes:UP000030832} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Kh10-101T {ECO:0000313|Proteomes:UP000030832}; RA Prakash J.S.; RT "Genome sequencing and annotation of Bacillus Okhensis strain Kh10- RT 101T."; RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KHF40746.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JRJU01000007; KHF40746.1; -; Genomic_DNA. DR RefSeq; WP_034627774.1; NZ_JRJU01000007.1. DR EnsemblBacteria; KHF40746; KHF40746; LQ50_08160. DR Proteomes; UP000030832; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000030832}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000030832}. FT DOMAIN 201 363 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 430 AA; 48800 MW; 93B19BFC914C4F68 CRC64; MQEINHKETE SVVLVGCQFD TDDIAFTNSM DELKSLVETA KGKVVGTITQ KRQKPEPSTY IGRGKVDELQ VLLDETDVDT IVFNDELSPS QIRNVHTRTK KTVIDRTQLI LDIFASRAQS REGKLQVELA QLSYLLPRLA GQGLALSRQG GGIGSKGPGE TQLESDRRHI RRRMDEIKHQ LEAVVGHRQR YRERRKQNDA FQVAIVGYTN AGKSTILNRL AEVDTLEENQ LFATLDPTTR QFNLPSGMKI LLSDTVGFIQ DLPTTLVAAF RSTLEELQEA NLLLHVVDSS NPDYEQHERT VKELIQELDS ENIPQLVVYN KSEEKDDNFF PTHDEDSIEI SAFDQDDLNS LKQAIEEKLM EQMSEYHVVL KAEEGSLLSK CRESTIIKKQ NWNEETEHYE IQGYVIATTA LGHDLAIRSI IEPKKVKVEE // ID A0A0B0MYL5_GOSAR Unreviewed; 610 AA. AC A0A0B0MYL5; DT 04-MAR-2015, integrated into UniProtKB/TrEMBL. DT 04-MAR-2015, sequence version 1. DT 12-APR-2017, entry version 11. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:KHG04604.1}; GN ORFNames=F383_29000 {ECO:0000313|EMBL:KHG04604.1}; OS Gossypium arboreum (Tree cotton) (Gossypium nanking). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae; OC Pentapetalae; rosids; malvids; Malvales; Malvaceae; Malvoideae; OC Gossypium. OX NCBI_TaxID=29729 {ECO:0000313|EMBL:KHG04604.1, ECO:0000313|Proteomes:UP000032142}; RN [1] {ECO:0000313|Proteomes:UP000032142} RP NUCLEOTIDE SEQUENCE. RA Mudge J., Ramaraj T., Lindquist I.E., Bharti A.K., Sundararajan A., RA Cameron C.T., Woodward J.E., May G.D., Brubaker C., Broadhvest J., RA Wilkins T.A.; RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KHG04604.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JRRC01415038; KHG04604.1; -; Genomic_DNA. DR Proteomes; UP000032142; Unassembled WGS sequence. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR CDD; cd01878; HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 2. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000032142}; KW Reference proteome {ECO:0000313|Proteomes:UP000032142}. FT DOMAIN 302 578 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 610 AA; 67900 MW; 6F6CF10D8FF8604C CRC64; MLRILTWSRS SLRSRSQFAP SSPFSILSSS YSTFNKGSED NQSAAGSVFS RYPSDPPRLF VVQPRLRPAT FLQAKLNEAL CLANSLEEQR DGYFHSDFFD KELPPHVVVQ NPSLKSAKIR ADTYFGPGTV ENIKCHLNAL ESKARQLLLM FFDGVDAVFV NIILSGVQQR NLERILGKPV LDRVGLIIEI FNAHAHTKEA KLQAELAALM YKKSRLVRVR RLDGRNTFGA SGEVEVVSAR GRGSGGRGFI SGAGETELQL QRRRILERRN HLLSQIEEVR RTRAVQRAAR KKRGGLDGRG LATVAVVGYT NAGKSTLISA LSDSNLYSDA RLFATLDARL KSVVLPSGRK VLLSDTVGFI SDLPVQLVEA FHSTLEEVLE ANLLVHVIDC TAPNRDEHRS TVLQVLQQIG VSEEKLQNMI EVWNKIDYEE EMGAGEDVEM SDFSAAEDVE MSDFSAAEDG ETKDSPGEDC DVAFELLDGK SVDGSDALKP SLGELQQTMD DKQDDYSDGW LLSEDDTADD YWNTLNEQQQ AETSNECKVE KDSESQPQHV PHVKVSALTG VGLQELLEII DEKLKVQDDR LKSEKVVGNS YIDRKWRPPR KEDEEVAVEQ // ID A0A0B0PQ77_GOSAR Unreviewed; 524 AA. AC A0A0B0PQ77; DT 04-MAR-2015, integrated into UniProtKB/TrEMBL. DT 04-MAR-2015, sequence version 1. DT 07-JUN-2017, entry version 13. DE SubName: Full=GTPase HflX {ECO:0000313|EMBL:KHG27002.1}; GN ORFNames=F383_09059 {ECO:0000313|EMBL:KHG27002.1}; OS Gossypium arboreum (Tree cotton) (Gossypium nanking). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae; OC Pentapetalae; rosids; malvids; Malvales; Malvaceae; Malvoideae; OC Gossypium. OX NCBI_TaxID=29729 {ECO:0000313|EMBL:KHG27002.1, ECO:0000313|Proteomes:UP000032142}; RN [1] {ECO:0000313|Proteomes:UP000032142} RP NUCLEOTIDE SEQUENCE. RA Magalhaes I.L.F., Oliveira U., Santos F.R., Vidigal T.H.D.A., RA Brescovit A.D., Santos A.J.; RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; KN439500; KHG27002.1; -; Genomic_DNA. DR Proteomes; UP000032142; Unassembled WGS sequence. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 2. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000032142}; KW Reference proteome {ECO:0000313|Proteomes:UP000032142}. FT DOMAIN 301 467 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 524 AA; 58712 MW; 7D56DCB888E8F599 CRC64; MMSLCFCSLI SPRPSPLIYD SNFSWNLNLY RSVGPLTFST HGNDRSFVAM VAQRGYEVDN ISLQSPTIEA EEENEVVDEL VNGSVIAEPV EEDTPRPVRV RKKRDDGDGS DDESFEDRFK LRNGREVFEE KAYLLGVERK GETSDSFAIE ESLKELAQLA DTAGLMVVGS TYQKLASPNP RTYIGSGKVA EIKSAIRAFE VETVIFDDEL SPGQLRNLEK AFGGDVRVAL AQMEYQLPRL TKMWTHLERQ AGGKVKGMGE KQIEVDKRIL RTQIGVLKKE LESVRKHRKQ YRNHRFSVPV PVVSLVGYTN AGKSILLNQL TGANVLSEDR LFATLDPTTR RVQMKNGSEF LLTDTVGFIQ KLPTTLVAAF RATLEEISES SLLVHVVDIS HPLAEQQIDA VEKVLAELDV SEIPKLMVWN KVDKVTDPEK IKLEAERRED IVCISALTGE GLLEFCNAVQ EKLKDSMVPV EALVPFDKGE LLSTIHQVGM VEKTEYTENG TFVKAFVPLR FARLLTPMRQ LCKS // ID A0A0B1TIQ8_OESDE Unreviewed; 520 AA. AC A0A0B1TIQ8; DT 04-MAR-2015, integrated into UniProtKB/TrEMBL. DT 04-MAR-2015, sequence version 1. DT 10-MAY-2017, entry version 11. DE SubName: Full=Putative GTP-binding protein HflX {ECO:0000313|EMBL:KHJ95295.1}; GN ORFNames=OESDEN_04763 {ECO:0000313|EMBL:KHJ95295.1}; OS Oesophagostomum dentatum (Nodular worm). OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida; OC Strongylida; Strongyloidea; Cloacinidae; Oesophagostomum. OX NCBI_TaxID=61180 {ECO:0000313|EMBL:KHJ95295.1, ECO:0000313|Proteomes:UP000053660}; RN [1] {ECO:0000313|EMBL:KHJ95295.1, ECO:0000313|Proteomes:UP000053660} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=OD-Hann {ECO:0000313|EMBL:KHJ95295.1, RC ECO:0000313|Proteomes:UP000053660}; RA Mitreva M.; RT "Draft genome of the hookworm Oesophagostomum dentatum."; RL Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; KN550014; KHJ95295.1; -; Genomic_DNA. DR Proteomes; UP000053660; Unassembled WGS sequence. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR CDD; cd01878; HflX; 1. DR InterPro; IPR008584; DUF866_euk. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR Pfam; PF05907; DUF866; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000053660}; KW Reference proteome {ECO:0000313|Proteomes:UP000053660}. FT DOMAIN 152 316 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 520 AA; 58859 MW; 2E1B895A8F45352B CRC64; MGVDYNTKRK AVWGTGQIEA LLRKKMQSRV TALMVNVDML TPTQQHELFR IFHVPIYDRY NIVLSIFKHY AKTQEARLQI QLAEIPYIRS RLHYLNKYRS DPSTLHVERQ TEKASVDEFE VLRLREQSLR KKLQLVVDKN LDKATEESRD AAMVAVVGYT NAGKTSLVKC LTGASSLLPK DRLFATLDTT RHAARLPSGR RVVFTDTIGF LSDLPMHLLA AFQATLSHVS LADVIVHIRD LSNPDWPAQS EDVEKTLENI GLSQDRIRDI IIADNKVDIE GAAISNTPGA VRISCKTADG VEELIAKVDE KVLQATGCKQ RRLRLKFSSP AIPYLYKYYL AQFLTRPILS LDLKCNMVGV TKFAPSDPET HRWFLKFRCM NCGESPDHWQ YLVVNEVLEV PGSRGEANLV EKCKLCNRVN TVGELQNKCA LAIVPDSIGS YDSVEHNEEW QSMIQFDCRG LEPIEFDPRN GWTAVGNESG TVFDDIDLSE KAWADYDEKA GEATEISDIE VRFVHAKNKK // ID A0A0B1ZLT9_9SPHN Unreviewed; 442 AA. AC A0A0B1ZLT9; DT 04-MAR-2015, integrated into UniProtKB/TrEMBL. DT 04-MAR-2015, sequence version 1. DT 05-JUL-2017, entry version 18. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=LK12_11840 {ECO:0000313|EMBL:KHK91511.1}; OS Novosphingobium malaysiense. OC Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales; OC Sphingomonadaceae; Novosphingobium. OX NCBI_TaxID=1348853 {ECO:0000313|EMBL:KHK91511.1, ECO:0000313|Proteomes:UP000031057}; RN [1] {ECO:0000313|EMBL:KHK91511.1, ECO:0000313|Proteomes:UP000031057} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MUSC 273 {ECO:0000313|EMBL:KHK91511.1, RC ECO:0000313|Proteomes:UP000031057}; RA Lee L.-H.; RT "Genome sequence of Novosphingobium malaysiense MUSC 273(T)."; RL Submitted (OCT-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KHK91511.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JTDI01000003; KHK91511.1; -; Genomic_DNA. DR EnsemblBacteria; KHK91511; KHK91511; LK12_11840. DR Proteomes; UP000031057; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000031057}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000031057}. FT DOMAIN 206 386 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 442 AA; 48536 MW; 017996D010764E96 CRC64; MNDELKGEVT RGARAFVAYP QMRGRGDLDP DARLEEAKGL ALAIGLVVAD AVAIPIREPR PGTLFGEGQI QNIATGCELS EAELVIVDGS LSAIQQRNLE EKLKRKVIDR TGLILEIFGE RAATAEGRLQ VELAHLDYQA GRLVRSWTHL ERQRGGFGFL GGPGETQIEA DRRLIRDRMA KIRRELEQVR RTRGLHRERR EKAPWPVVAL VGYTNAGKST LFNRLTGADV MAQDLLFATL DPTMRSVRLP GVEKAILSDT VGFISDLPTQ LVAAFRATLE EVTAADVILH VRDIANPDTE AQKKQVLDVL ADLGIVPGED GEESEFPIPI IEVWNKWDLL GPMQADELRE AMAHREGETI VPLSALTGEG CDNLLDVVGK KLTAGSKIYD FVLPAADGQR IAFLHARGDV MSEEQAGEGA DGPQLRLKVR LTERELGRFA SL // ID A0A0B1ZZV5_9MICO Unreviewed; 502 AA. AC A0A0B1ZZV5; DT 04-MAR-2015, integrated into UniProtKB/TrEMBL. DT 04-MAR-2015, sequence version 1. DT 07-JUN-2017, entry version 17. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=LK09_16085 {ECO:0000313|EMBL:KHK96246.1}; OS Microbacterium mangrovi. OC Bacteria; Actinobacteria; Micrococcales; Microbacteriaceae; OC Microbacterium. OX NCBI_TaxID=1348253 {ECO:0000313|EMBL:KHK96246.1, ECO:0000313|Proteomes:UP000031030}; RN [1] {ECO:0000313|EMBL:KHK96246.1, ECO:0000313|Proteomes:UP000031030} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MUSC 115 {ECO:0000313|EMBL:KHK96246.1, RC ECO:0000313|Proteomes:UP000031030}; RA Lee L.-H.; RT "Genome sequence of Microbacterium mangrovi MUSC 115(T)."; RL Submitted (NOV-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KHK96246.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JTDK01000016; KHK96246.1; -; Genomic_DNA. DR RefSeq; WP_039402024.1; NZ_JTDK01000016.1. DR EnsemblBacteria; KHK96246; KHK96246; LK09_16085. DR Proteomes; UP000031030; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000031030}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000031030}. FT DOMAIN 283 448 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 502 AA; 54264 MW; 0174A86C6C18523B CRC64; MIETSHPADP TDPIERVLQN ADSHSGVHRF GPAQALQDDA TAEGGDFDGG QWDREDRAAL RRVVGLSTEL EDVTEVEYRQ LRLENVVLVG VHPQGATEDA ENSLRELAAL AETAGAVVLD GVLQRRPHPD PATYVGRGKA EELRDIVAAV GADTVIADTE LAPSQRRALE DVVKVKVIDR TTVILDIFSQ HAKSREGKAQ VELAQLEYLL PRLRGWGDSM SRQAGGQVGA GGAGMGSRGP GETKIELDRR RIRTKMALLR RQIKDYAPAR EAKRAERKRN TIPSVAIAGY TNAGKSSLLN RITHAGVLVE NALFATLDAT VRRVEAEDGR IYTLADTVGF VRNLPHQLVE AFRSTLEEVG DADIIVHVVD AAHPDPAGQI QTVRDVLGEI GARDIPEMVV FNKADLVDDD TRLVLRGLEP RAHFASSRTG EGIADLRTAI EAALPLPAVE IRAVVPYDRG DLIAAVHETG HVVSLEHGPD GSQLHAFVGE RLAARLAPFL AA // ID A0A0B2AG23_9MICC Unreviewed; 533 AA. AC A0A0B2AG23; DT 04-MAR-2015, integrated into UniProtKB/TrEMBL. DT 04-MAR-2015, sequence version 1. DT 07-JUN-2017, entry version 19. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=LK10_18565 {ECO:0000313|EMBL:KHL00841.1}; OS Sinomonas humi. OC Bacteria; Actinobacteria; Micrococcales; Micrococcaceae; Sinomonas. OX NCBI_TaxID=1338436 {ECO:0000313|EMBL:KHL00841.1, ECO:0000313|Proteomes:UP000030982}; RN [1] {ECO:0000313|EMBL:KHL00841.1, ECO:0000313|Proteomes:UP000030982} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MUSC 117 {ECO:0000313|EMBL:KHL00841.1, RC ECO:0000313|Proteomes:UP000030982}; RA Lee L.-H.; RT "Genome sequence of Sinomonas sp. MUSC 117."; RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KHL00841.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JTDL01000147; KHL00841.1; -; Genomic_DNA. DR RefSeq; WP_043127220.1; NZ_JTDL01000147.1. DR EnsemblBacteria; KHL00841; KHL00841; LK10_18565. DR Proteomes; UP000030982; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 2. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000030982}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000030982}. FT DOMAIN 312 477 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 533 AA; 58110 MW; 6AC9B2AF3978D648 CRC64; MTNHDAAREP QPQDLSAQDI QAVIDRILAK EEAAAAKGAG HRAEDNGDRA PSARRGGLTS GKALALSELD DEHGEYDGEQ RDLEERRALR RTAGLSTELE DVTEVEYRQL RLERVVLAGL WSEGSLEDAE NSLQELAALA ETAGSEVLDG IVQRRLKPDA GTFLGSGKAQ ELKDIVYSTG ADTVIVDSEL SPSQRRGLED IVKVKVIDRT ALILDIFAQH AKSREGKAQV ELAQLEYLLP RLRGWGESMS RQAGGRVGAA GGGIGSRGPG ETKIELDRRR IRTRMAKLRR EIAGMKPARE TKRANRKRNE VPSVAIAGYT NAGKSSLLNR LTDAGVLVEN ALFATLDPTV RRAETPDGLP YTLSDTVGFV RSLPTQLVEA FRSTLEEVAD ADLILHVVDA SHPDPEGQIA AVREVFSEVD ARKIPEIIVL NKADAADPFV LERLRQHEPR NVVVSARTGL GIDELKQTIS AAIPRPDVML TLLIPYSRGD LLSKLHESSS EIRSLEHTAD GTVARVVVRE EFAAELEPFV VDD // ID A0A0B2BAP0_9ACTN Unreviewed; 396 AA. AC A0A0B2BAP0; DT 04-MAR-2015, integrated into UniProtKB/TrEMBL. DT 04-MAR-2015, sequence version 1. DT 12-APR-2017, entry version 17. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=LK11_39955 {ECO:0000313|EMBL:KHL11919.1}; OS Mumia flava. OC Bacteria; Actinobacteria; Propionibacteriales; Nocardioidaceae; Mumia. OX NCBI_TaxID=1348852 {ECO:0000313|EMBL:KHL11919.1, ECO:0000313|Proteomes:UP000031002}; RN [1] {ECO:0000313|EMBL:KHL11919.1, ECO:0000313|Proteomes:UP000031002} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MUSC 201 {ECO:0000313|EMBL:KHL11919.1, RC ECO:0000313|Proteomes:UP000031002}; RA Lee L.-H.; RT "Genome sequence of Mumia flava MUSC 201(T)."; RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KHL11919.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JTDJ01000124; KHL11919.1; -; Genomic_DNA. DR ProteinModelPortal; A0A0B2BAP0; -. DR EnsemblBacteria; KHL11919; KHL11919; LK11_39955. DR Proteomes; UP000031002; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000031002}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000031002}. FT DOMAIN 196 367 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 162 189 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 396 AA; 43375 MW; 47D984E2194E3583 CRC64; MTPENLINAA LVGIDFGKTD FEASLEELSL LASSAGARPA VTLTGRRSSP DAKMFIGSGK AEELRLACDA HNVEIVIFNH ALAPAQQRNL EQALNRRVVD RTSLILDIFA QRARSHEGKL QVELAQLQYL STRLIRAWTH LERQKGGIGL RGPGETQLET DRRLIGERIK MLKSRLDRLR RQHSTQRRQR ARSGTMSVSL VGYTNAGKST LFNALTKAQA YAADQLFATL DTTSRRVYLG DEVGQIVVSD TVGFIRELPH QLVAAFRATL EETIHADLLL HVVDASSAVR LEQIEQVNGV LHEIGADTIR QVLVFNKIDA VPELAARGDA VERDEYGNIS RVFLSARTGQ GLDTLRAAIA EIASAEHLSS ATLPNGALDG APAEPHEDHT ISEHGR // ID A0A0B2BZA6_9SPHN Unreviewed; 440 AA. AC A0A0B2BZA6; DT 04-MAR-2015, integrated into UniProtKB/TrEMBL. DT 04-MAR-2015, sequence version 1. DT 07-JUN-2017, entry version 17. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=PK98_04585 {ECO:0000313|EMBL:KHL26744.1}; OS Porphyrobacter mercurialis. OC Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales; OC Erythrobacteraceae; Porphyrobacter. OX NCBI_TaxID=1572751 {ECO:0000313|EMBL:KHL26744.1, ECO:0000313|Proteomes:UP000030988}; RN [1] {ECO:0000313|EMBL:KHL26744.1, ECO:0000313|Proteomes:UP000030988} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Coronado {ECO:0000313|EMBL:KHL26744.1, RC ECO:0000313|Proteomes:UP000030988}; RA Coil D.A., Eisen J.A.; RT "Draft genome sequence of Kirrobacter mercurialis."; RL Submitted (NOV-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KHL26744.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JTDN01000001; KHL26744.1; -; Genomic_DNA. DR RefSeq; WP_039096240.1; NZ_JTDN01000001.1. DR EnsemblBacteria; KHL26744; KHL26744; PK98_04585. DR Proteomes; UP000030988; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000030988}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000030988}. FT DOMAIN 209 384 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 440 AA; 48377 MW; EB29D79BA387A50A CRC64; MNFGDEIEGE VSRGARALVI CPEIRSQRQT RDADARLEEA RGLALAIGLD VREATIVPVR DVRPGTLFGE GQIERIATDA TMAEAELIIV DGSLSAIQQR NLEDKLKRKV IDRTGLILEI FGERAATAEG RLQVELAHLD YQQSRLVRSW THLERQRGGF GFLGGPGETQ IEADRRMIRA RMGRLRRELE QVRRTRALHR SRRERAPWPV IALVGYTNAG KSTIFNRLTG AGVLAQDLLF ATLDPTMRAI SLPGLDKAIL SDTVGFISDL PTQLVAAFRA TLEEVTAASV ILHVRDIANP DSADQKREVL NILAELGVGT GEGEFADIPI IEIWNKWDLL PPEQQDELAH VSEGEPDILR LSAITGEGMD EMLARLGAVL TGGARVHAIT VDAADGQRLA WLHAHGEVLG EHDAGDGSAG PRRRLDVRLT ERELGRFNTL // ID A0A0B2K020_9FIRM Unreviewed; 602 AA. AC A0A0B2K020; DT 04-MAR-2015, integrated into UniProtKB/TrEMBL. DT 04-MAR-2015, sequence version 1. DT 07-JUN-2017, entry version 18. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=NZ47_00475 {ECO:0000313|EMBL:KHM53144.1}; OS Anaerovibrio lipolyticus. OC Bacteria; Firmicutes; Negativicutes; Selenomonadales; OC Selenomonadaceae; Anaerovibrio. OX NCBI_TaxID=82374 {ECO:0000313|EMBL:KHM53144.1, ECO:0000313|Proteomes:UP000030993}; RN [1] {ECO:0000313|EMBL:KHM53144.1, ECO:0000313|Proteomes:UP000030993} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=5S {ECO:0000313|EMBL:KHM53144.1, RC ECO:0000313|Proteomes:UP000030993}; RX PubMed=23950883; RA Prive F., Kaderbhai N.N., Girdwood S., Worgan H.J., Pinloche E., RA Scollan N.D., Huws S.A., Newbold C.J.; RT "Identification and characterization of three novel lipases belonging RT to families II and V from Anaerovibrio lipolyticus 5ST."; RL PLoS ONE 8:E69076-E69076(2013). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KHM53144.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JSCE01000009; KHM53144.1; -; Genomic_DNA. DR RefSeq; WP_039205688.1; NZ_JSCE01000009.1. DR EnsemblBacteria; KHM53144; KHM53144; NZ47_00475. DR Proteomes; UP000030993; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000030993}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000030993}. FT DOMAIN 380 549 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 346 380 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 602 AA; 66584 MW; 1AD71A14D54CF615 CRC64; MVVNGKLDNI KSGVIQELEA LYELEIPQGQ IITREAAEKM LELTGVLGRE VAVYINRKGT VVQVSVGDDA TVELPDIKQR SAIRLSGIRC VHTHPSADTR LSAPDLSSLR SMRFDCMVAI GLKKNNKIYG SLAFLNGELT EDGGYVVSGT KELPLKELNN IDLVQLIVLV NNALGKNRLK DTEEQMEKAI LAGVAFSSRR DDWQVEDSLA ELRGLVETAG AEIVGEVIQN KDKPDNAYFL GKGKVEEIAM LAQNVEADLL VIDDEISPSQ QRNLELSTGL RVVDRTALIL DIFAQRARSS AGKLQVELAQ LKYNLPRLGG QGLVMSRLGG GIGTRGPGET KLEMDRRRIH GRIHDLEEQL KKLKNQRKLH RNQRKQSRLA SAALVGYTNA GKSTILNALS DSDVLAEDKL FATLDPTTRL VDLDEKLQIL LTDTVGFIQK LPHTLVSAFQ ATLEETTEAD LLVHVVDASD PNYELQIKAV IKVLDEIGAK EKPAIFVFNK ADRLMEKGGT DFDAQRMLQG REGVVISAKK SEDLQKLREK LASFFNQGKV IIKLCIPYTE GNVITRLHED GNVLKTDYDE KGTVLEVELP VTDAETYKQY EI // ID A0A0B2PYM9_GLYSO Unreviewed; 529 AA. AC A0A0B2PYM9; DT 04-MAR-2015, integrated into UniProtKB/TrEMBL. DT 04-MAR-2015, sequence version 1. DT 07-JUN-2017, entry version 14. DE SubName: Full=GTPase HflX {ECO:0000313|EMBL:KHN12677.1}; GN ORFNames=glysoja_008640 {ECO:0000313|EMBL:KHN12677.1}; OS Glycine soja (Wild soybean). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae; OC Pentapetalae; rosids; fabids; Fabales; Fabaceae; Papilionoideae; OC Phaseoleae; Glycine; Soja. OX NCBI_TaxID=3848 {ECO:0000313|EMBL:KHN12677.1, ECO:0000313|Proteomes:UP000053555}; RN [1] {ECO:0000313|Proteomes:UP000053555} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. W05 {ECO:0000313|Proteomes:UP000053555}; RX PubMed=25004933; DOI=10.1038/ncomms5340; RA Qi X., Li M.W., Xie M., Liu X., Ni M., Shao G., Song C., RA Kay-Yuen Yim A., Tao Y., Wong F.L., Isobe S., Wong C.F., Wong K.S., RA Xu C., Li C., Wang Y., Guan R., Sun F., Fan G., Xiao Z., Zhou F., RA Phang T.H., Liu X., Tong S.W., Chan T.F., Yiu S.M., Tabata S., RA Wang J., Xu X., Lam H.M.; RT "Identification of a novel salt tolerance gene in wild soybean by RT whole-genome sequencing."; RL Nat. Commun. 5:4340-4340(2014). RN [2] {ECO:0000313|EMBL:KHN12677.1, ECO:0000313|Proteomes:UP000053555} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. W05 {ECO:0000313|Proteomes:UP000053555}; RC TISSUE=Root {ECO:0000313|EMBL:KHN12677.1}; RA Lam H.-M., Qi X., Li M.-W., Liu X., Xie M., Ni M., Xu X.; RT "Identification of a novel salt tolerance gene in wild soybean by RT whole-genome sequencing."; RL Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; KN663007; KHN12677.1; -; Genomic_DNA. DR Proteomes; UP000053555; Unassembled WGS sequence. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000053555}; KW Reference proteome {ECO:0000313|Proteomes:UP000053555}. FT DOMAIN 304 470 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 529 AA; 59100 MW; 02C8A83B9CD2A36E CRC64; MSGTGTFFYG SVIQPLIRYH YLSPPIPIRP LCCISPLITS IHSNDAVSPQ NGTLRFQTEH QQHSEEPLPV PSLSAAEENK ATTKLRKKKE DDVVSDNRFK LRNGREVFEE KAYLVGVERK NDVQDFGIEE SLSELSQLAD TAGLLVVGST YQKLTSPNPR TYIGSGKVSE IKSAIHALGV ETVIFDDELS AGQLRNLEKI FGGDVRVCDR TALILDIFNQ RAATHEASLQ VSLAQMEYQL PRLTKMWTHL ERQAGGKVKG MGEKQIEVDK RILRNQIGIL KKELESVRKH RKQYRNRRFS VPVAVVSLVG YTNAGKSTLL NQLTGADVLA EDKLFATLDP TTRRVQMKNG KEFLLTDTVG FIQKLPTTLV AAFRATLEEI SESSLLVHVV DISHPLAEQQ INAVDKVLSE LDVSSIPKLI VWNKVDKVSD PQKLRLEAEK RDDVVCISAL SGNGLQEFCN AVQDKLKDSM VWVEALVPFE NGDLLSTIHQ VGMVEKTEYT EQGTYIKAHV PLRFARMLTP MRQLCVSQP // ID A0A0B3BU09_9PSED Unreviewed; 433 AA. AC A0A0B3BU09; A0A0B2DCI2; DT 04-MAR-2015, integrated into UniProtKB/TrEMBL. DT 04-MAR-2015, sequence version 1. DT 30-AUG-2017, entry version 20. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=PT85_10130 {ECO:0000313|EMBL:KHO64551.1}, GN SAMN05421672_1014 {ECO:0000313|EMBL:SIP86244.1}; OS Pseudomonas flexibilis. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=706570 {ECO:0000313|EMBL:KHO64551.1, ECO:0000313|Proteomes:UP000030980}; RN [1] {ECO:0000313|EMBL:KHO64551.1, ECO:0000313|Proteomes:UP000030980} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=JCM 14085 {ECO:0000313|EMBL:KHO64551.1, RC ECO:0000313|Proteomes:UP000030980}; RA Shin S.-K., Yi H.; RT "Genome sequence of Pseudomonas tuomuerensis JCM 14085."; RL Submitted (NOV-2014) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:SIP86244.1, ECO:0000313|Proteomes:UP000186079} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29606 {ECO:0000313|EMBL:SIP86244.1, RC ECO:0000313|Proteomes:UP000186079}; RA Mah S.A., Swanson W.J., Moy G.W., Vacquier V.D.; RL Submitted (JAN-2017) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JTAK01000004; KHO64551.1; -; Genomic_DNA. DR EMBL; FTMC01000001; SIP86244.1; -; Genomic_DNA. DR RefSeq; WP_039559333.1; NZ_JTAK01000004.1. DR EnsemblBacteria; KHO64551; KHO64551; PT85_10130. DR PATRIC; fig|706570.3.peg.125; -. DR Proteomes; UP000030980; Unassembled WGS sequence. DR Proteomes; UP000186079; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000030980}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000030980}. FT DOMAIN 199 366 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 165 192 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 433 AA; 48976 MW; 9C3F5E9F1DB9EE04 CRC64; MFFERPGGGE RAILVHLEGQ DPEAREDPQE FQELANSAGA DTVAFVSVSR HQPSAKFLIG SGKVEEIRDL VKAEDVELVI FNHTLTPSQE RNLEREFECR VLDRTGLILD IFAQRARTHE GKLQVELAQL EHMSTRLVRG WTHLERQKGG IGLRGPGETQ LETDRRLLRV RIRQIKSRLE KVRSQREQAR RGRRRADIPS VSLVGYTNAG KSTLFNALTT SEVYAANQLF ATLDPTLRRL ELDDLGPVIL ADTVGFIRHL PHKLVEAFRA TLEESSNADL LLHVIDSHEP ERDQQIDQVL RVLGEIGADQ LPMLEVYNKI DLLEGVEPQI QRDGEGKPQR VWLSAREGKG LDLLRQTIAE LLGEDLFVGT LCLPQRLGRL RAQFFELGAV QEETHDERGA SLLSVRLPRI ELNRLVSREG LQPSEFLAQH TLQ // ID A0A0B3STE1_9RHOB Unreviewed; 425 AA. AC A0A0B3STE1; DT 04-MAR-2015, integrated into UniProtKB/TrEMBL. DT 04-MAR-2015, sequence version 1. DT 07-JUN-2017, entry version 16. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:KHQ53724.1}; GN ORFNames=OA50_01713 {ECO:0000313|EMBL:KHQ53724.1}; OS Mameliella alba. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae; Mameliella. OX NCBI_TaxID=561184 {ECO:0000313|EMBL:KHQ53724.1, ECO:0000313|Proteomes:UP000030960}; RN [1] {ECO:0000313|EMBL:KHQ53724.1, ECO:0000313|Proteomes:UP000030960} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=UMTAT08 {ECO:0000313|EMBL:KHQ53724.1, RC ECO:0000313|Proteomes:UP000030960}; RA Gan H.Y., Muhd D.-D., Mohd Noor M.E., Yeong Y.S., Usup G.; RT "Genome sequence of Ponticoccus sp. strain UMTAT08 isolated from RT clonal culture of toxic dinoflagellate Alexandrium tamiyavanichii."; RL Submitted (OCT-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KHQ53724.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JSUQ01000006; KHQ53724.1; -; Genomic_DNA. DR EnsemblBacteria; KHQ53724; KHQ53724; OA50_01713. DR PATRIC; fig|1515334.3.peg.1721; -. DR Proteomes; UP000030960; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000030960}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000030960}. FT DOMAIN 204 373 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 425 AA; 47315 MW; B103A486576CADD4 CRC64; MREHAPPVTR AWVLHPDIKS DPARRDAQMA LEEAVSLAHA LPGLEVVGSQ IVPLRDPNPG ALFGSGKIEE LRAKLEAEDI DLVLVDGPVT PVQQRNLERD WKVKLLDRTG LILEIFSDRA ATREGVLQVE MAHLSYQRTR LVRAWTHLER QRGGLGFVGG PGETQIEADR RAIDEQLVRL RRQLDKVVKT RELHRKARAK VPYPIVALVG YTNAGKSTLF NRLTGAEVMA KDMLFATLDP TMRAVRLPTG ADVILSDTVG FISDLPTELV AAFRATLEEV LAADVVVHVR DISHPETEEQ AEDVRGILDS LGVGEETAQI ELWNKLDRLG PEELETVRIR AARNPDVFVT SALTGEGLDD FLEAVTEALG AERVEEDLVL GFAEGKRRAW LFEKGLVEDE RQEEDGFHLR VLWSALDKAR FETLG // ID A0A0B3W4T6_9FIRM Unreviewed; 425 AA. AC A0A0B3W4T6; DT 04-MAR-2015, integrated into UniProtKB/TrEMBL. DT 04-MAR-2015, sequence version 1. DT 07-JUN-2017, entry version 18. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=QX51_08235 {ECO:0000313|EMBL:KHS57432.1}; OS Terrisporobacter othiniensis. OC Bacteria; Firmicutes; Clostridia; Clostridiales; OC Peptostreptococcaceae; Terrisporobacter. OX NCBI_TaxID=1577792 {ECO:0000313|EMBL:KHS57432.1, ECO:0000313|Proteomes:UP000031189}; RN [1] {ECO:0000313|EMBL:KHS57432.1, ECO:0000313|Proteomes:UP000031189} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=08-306576 {ECO:0000313|EMBL:KHS57432.1, RC ECO:0000313|Proteomes:UP000031189}; RA Lund L.C., Sydenham T.V., Hogh S.V., Skov M.N., Kemp M., RA Justesen U.S.; RT "Draft genome sequence of Terrisporobacter sp. 08-306576, isolated RT from the blood culture of a bacteremia patient."; RL Submitted (DEC-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KHS57432.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JWHR01000075; KHS57432.1; -; Genomic_DNA. DR RefSeq; WP_039679434.1; NZ_JWHR01000075.1. DR EnsemblBacteria; KHS57432; KHS57432; QX51_08235. DR Proteomes; UP000031189; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000031189}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000031189}. FT DOMAIN 202 372 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 168 195 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 425 AA; 48432 MW; AED48E9A44CDB7C7 CRC64; MEKQQERALL IGLNITTNVK KIDDIDINES MEELKELTKA AGAEVVGSLI QNRPAVDAAY YVGKGKVEEL RAYCEATDAT MVIFNDELSG AHIRNLEEAV GRKVIDRTTL ILDIFAQRAL SKEGKLQVEL AQLRYRMPRL YGMGGEMSRT GAGIGTRGPG EQKLEIDKRI ILNKIADIRR ELKEVSKNRE TQRVQRMKSN MPIVALVGYT NAGKSTLLNE LIKTHKDYEE EKEVFVKNML FATLDVTLRK ATLPNKRDFL VVDTVGFVSK LPHDLVDAFK ATLEEVQYAD LILHVIDATN SSYELQKQTT ESVLKDLDVG DKKTIIVYNK VDKLELDIYP KNQKDKVYIS AKKGINMDKL LKLIEEALMK DTYKVNLILP YERGDIFSKI KDKYNVNDFN YEENGISVDV NLDEEDYNIY KDYIK // ID A0A0B4C2G7_9RHOB Unreviewed; 423 AA. AC A0A0B4C2G7; DT 04-MAR-2015, integrated into UniProtKB/TrEMBL. DT 04-MAR-2015, sequence version 1. DT 07-JUN-2017, entry version 16. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=RA29_13505 {ECO:0000313|EMBL:KIC48711.1}; OS Tateyamaria sp. ANG-S1. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae; Tateyamaria. OX NCBI_TaxID=1577905 {ECO:0000313|EMBL:KIC48711.1, ECO:0000313|Proteomes:UP000031171}; RN [1] {ECO:0000313|Proteomes:UP000031171} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ANG-S1 {ECO:0000313|Proteomes:UP000031171}; RX PubMed=25755651; DOI=10.3389/fmicb.2015.00123; RA Collins A.J., Fullmer M.S., Gogarten J.P., Nyholm S.V.; RT "Comparative genomics of Roseobacter clade bacteria isolated from the RT accessory nidamental gland of Euprymna scolopes."; RL Front. Microbiol. 6:123-123(2015). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KIC48711.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JWLL01000006; KIC48711.1; -; Genomic_DNA. DR RefSeq; WP_039686753.1; NZ_JWLL01000006.1. DR EnsemblBacteria; KIC48711; KIC48711; RA29_13505. DR Proteomes; UP000031171; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000031171}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000031171}. FT DOMAIN 203 372 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 423 AA; 46792 MW; FB00ABEA936AE8A1 CRC64; MGEMPEFTRA WVLHPDIKSD PDRREASFAL AEAVSLAHAL PELEVVGSEI VPLPRPQAGL LFGSGKIEEL AERLHDAEVE LVLIDGPVTP VQQRNLEKAW KVKLLDRTGL ILEIFSDRAA TREGVLQVEM AALSYQRTRL VRAWTHLERQ RGGLGFVGGP GETQIEADRR AIDTQLVRLR RQLDKVVKTR TLHRAARAKV PYPIVALVGY TNAGKSTLFN RLTGADVMAK DMLFATLDPT MRRVELENGP EVILSDTVGF ISALPTELVA AFRATLEEVL AADVILHVRD ISHPETEAQA EDVRTILSDL GVGEGREMVE VWNKIDLLPE EEADAARARA ERDEGVFAMS AITGEGIDAL LADVAATLQG SVSEETLLLP YAEGRKRAWL FEQDVVQAER QGEDGFEFDV RWTAIQKARF DGL // ID A0A0B4R966_9BACL Unreviewed; 423 AA. AC A0A0B4R966; DT 01-APR-2015, integrated into UniProtKB/TrEMBL. DT 01-APR-2015, sequence version 1. DT 07-JUN-2017, entry version 17. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=Plano_0352 {ECO:0000313|EMBL:AIY04317.1}; OS Planococcus sp. PAMC 21323. OC Bacteria; Firmicutes; Bacilli; Bacillales; Planococcaceae; OC Planococcus. OX NCBI_TaxID=1526927 {ECO:0000313|EMBL:AIY04317.1, ECO:0000313|Proteomes:UP000031496}; RN [1] {ECO:0000313|EMBL:AIY04317.1, ECO:0000313|Proteomes:UP000031496} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=PAMC 21323 {ECO:0000313|EMBL:AIY04317.1, RC ECO:0000313|Proteomes:UP000031496}; RA Jung J.-H., Joe M.-H., Cho Y.-J., Lee S.G., Han S.J., Lim S., RA Choi J.-i.; RT "Complete genome sequence of Planococcus sp. PAMC21323 isolated from RT the Antarctica."; RL Submitted (AUG-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP009129; AIY04317.1; -; Genomic_DNA. DR RefSeq; WP_038702443.1; NZ_CP009129.1. DR EnsemblBacteria; AIY04317; AIY04317; Plano_0352. DR KEGG; pln:Plano_0352; -. DR KO; K03665; -. DR Proteomes; UP000031496; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000031496}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000031496}. FT DOMAIN 200 368 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 159 186 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 423 AA; 47865 MW; E9EE219DD085166C CRC64; MDELQEKAVI VGVQLQKDLH FDYGMEELRN LAEACNVEVV GEVTQNLERI NPSHYVGSGK VEEIKAFYEE SDANLVIFND ELSPSQIRNL EEDLECKVID RTMLILDIFS RRAKTREAQV QVELAQLQYM LPRLIGLRAS LGRQGGSSSG GVANRGAGET KLELDRRKIE DQISKLHKEL EHIKDQRITQ RKQRTKKGMP VVSLVGYTNA GKSTVMNGLL TKTGQNEEKQ VFEKDMLFAT LETSVRQIRL EDNKSFLLTD TVGFVSKLPH HLVKAFRSTL EEARNADLLL HVVDVSNEEH RYMMDVTNLT LQAVGVENVP TLYIFNKSDL AGVNYPAMSG DGLWIAAKEG VGLDELLEVI KKQIFADYVT CRMIVPFNRG DIVAYLNEYA SIHETEYEEE GTLLKVELSR ADYDRYEQFV VGS // ID A0A0B4S140_9FIRM Unreviewed; 424 AA. AC A0A0B4S140; DT 01-APR-2015, integrated into UniProtKB/TrEMBL. DT 01-APR-2015, sequence version 1. DT 05-JUL-2017, entry version 18. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=NW74_03460 {ECO:0000313|EMBL:AIZ36460.1}; OS Parvimonas micra. OC Bacteria; Firmicutes; Tissierellia; Tissierellales; Peptoniphilaceae; OC Parvimonas. OX NCBI_TaxID=33033 {ECO:0000313|EMBL:AIZ36460.1, ECO:0000313|Proteomes:UP000031386}; RN [1] {ECO:0000313|EMBL:AIZ36460.1, ECO:0000313|Proteomes:UP000031386} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=KCOM 1535 / ChDC B708 {ECO:0000313|Proteomes:UP000031386}; RA Kook J.-K., Park S.-N., Lim Y.K., Roh H.; RT "Complete genome sequence of Parvimonas micra KCOM 1535 (= ChDC RT B708)."; RL Submitted (OCT-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP009761; AIZ36460.1; -; Genomic_DNA. DR RefSeq; WP_041953834.1; NZ_CP009761.1. DR EnsemblBacteria; AIZ36460; AIZ36460; NW74_03460. DR KEGG; pmic:NW74_03460; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR KO; K03665; -. DR Proteomes; UP000031386; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000031386}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000031386}. FT DOMAIN 194 368 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 160 187 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 424 AA; 48617 MW; 5132E8D072457A4E CRC64; MNQRVITVTV NIDMDEKTLE DKVIELEKLV EALDGEVVLS LTQNKSYVDK AFYVGKGKVN EIKDYCEKLE AEFVVFNNEL TGSQVKNLEE IIGIRVIDRT NLILDIFSER ARTKEAKLQV KLAKLKYTLP RLSALRSGFS RQQGGIGGKG IGEQQIELDR RIINREISSI TSQLKEIEKN RSEIRKKRIN SKQPIISLIG YTNAGKSTLI NKLISYGKDE NSEIKEVFVK DMLFATLDTF VREGSLLNGS RVMYIDTVGF VSDIPHNLVE SFKGTLEEIK YSDLILHVVD ISNVNVDEQI KITNDMIKKL ECEDKNVIYV FNKIDKLADE NIKFQYANIE NKVFISAKND EDIILLLKEI EKVLFSSLVK TELLIPYDKQ KIVSNILNNY MPEFVEHIET GSFLKVSLKK EDYEIYKGYE VNEK // ID A0A0B4WZS3_9RHIZ Unreviewed; 441 AA. AC A0A0B4WZS3; DT 01-APR-2015, integrated into UniProtKB/TrEMBL. DT 01-APR-2015, sequence version 1. DT 07-JUN-2017, entry version 16. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:AJD41179.1}; GN ORFNames=RGR602_CH01847 {ECO:0000313|EMBL:AJD41179.1}; OS Rhizobium gallicum bv. gallicum R602. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium. OX NCBI_TaxID=1418105 {ECO:0000313|EMBL:AJD41179.1, ECO:0000313|Proteomes:UP000031368}; RN [1] {ECO:0000313|EMBL:AJD41179.1, ECO:0000313|Proteomes:UP000031368} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=R602 {ECO:0000313|EMBL:AJD41179.1, RC ECO:0000313|Proteomes:UP000031368}; RA Bustos P., Santamaria R.I., Lozano L., Acosta J.L., Ormeno-Orrillo E., RA Rogel M.A., Romero D., Cevallos M.A., Martinez-Romero E., Gonzalez V.; RT "Complete genome sequence of Rhizobium gallicum bv. gallicum R602."; RL Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP006877; AJD41179.1; -; Genomic_DNA. DR RefSeq; WP_039844832.1; NZ_CP006877.1. DR EnsemblBacteria; AJD41179; AJD41179; RGR602_CH01847. DR KEGG; rga:RGR602_CH01847; -. DR KO; K03665; -. DR Proteomes; UP000031368; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000031368}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000031368}. FT DOMAIN 204 376 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 163 197 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 441 AA; 48738 MW; 116804C1F38767F5 CRC64; MRATVVVPVL KQARSRSTPI EGAATRSPES RLEEATGLAE AIDLDVVNGA IVPISDPRPA TLLGTGKIED IKAQLDEHDS GLVIVDHPLT PVQQRNLEKE WNAKVIDRTG LILEIFGRRA STKEGTLQVD LAHLNYQKGR LVRSWTHLER QRGGGGFMGG PGETQIEADR RLLQDRIIKL ERELEQVVRT RQLHRAKRKK VPHPIVALVG YTNAGKSTLF NRITGAGVLA EDMLFATLDP TLRRMKLPHG RTVILSDTVG FISDLPTHLV AAFRATLEEV LESDLILHVR DMSDADNQAQ SADVMRILKD LGIDEAEGAR RIVEVWNKID RLEPETHDAI VQKVAGAENV VAVSAISGEG IDHLMQEISK RLSGVMTATT IKLPLGKLAL LPWLYEHSIV DGREDNEDGT VTLDVRLAES EAAELERRMG DGPKPQKEDW E // ID A0A0B4XQV0_9GAMM Unreviewed; 458 AA. AC A0A0B4XQV0; DT 01-APR-2015, integrated into UniProtKB/TrEMBL. DT 01-APR-2015, sequence version 1. DT 30-AUG-2017, entry version 16. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=S7S_15745 {ECO:0000313|EMBL:AJD49561.1}; OS Alcanivorax pacificus W11-5. OC Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales; OC Alcanivoracaceae; Alcanivorax. OX NCBI_TaxID=391936 {ECO:0000313|EMBL:AJD49561.1, ECO:0000313|Proteomes:UP000006764}; RN [1] {ECO:0000313|EMBL:AJD49561.1, ECO:0000313|Proteomes:UP000006764} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=W11-5 {ECO:0000313|EMBL:AJD49561.1}; RX PubMed=23209202; DOI=10.1128/JB.01845-12; RA Lai Q., Shao Z.; RT "Genome sequence of an alkane-degrading bacterium, Alcanivorax RT pacificus type strain W11-5, isolated from deep sea sediment."; RL J. Bacteriol. 194:6936-6936(2012). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP004387; AJD49561.1; -; Genomic_DNA. DR RefSeq; WP_008733406.1; NZ_CP004387.1. DR EnsemblBacteria; AJD49561; AJD49561; S7S_15745. DR KEGG; apac:S7S_15745; -. DR KO; K03665; -. DR Proteomes; UP000006764; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000006764}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Hydrolase {ECO:0000313|EMBL:AJD49561.1}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Protease {ECO:0000313|EMBL:AJD49561.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000006764}. FT DOMAIN 210 376 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 458 AA; 51060 MW; 5BF07C80A4EFE8EA CRC64; MEFFERPDAP KTGATPDHPA ERAVLVHLEL PDSLGVDDLE EFHHLVVSSG VSPVAEVLGR RERPDPATYV GSGKVQEILD VVEAHEADVV LFNHALSPAQ ERNLERALKC RVLDRTGLIL DIFALRARTH EGRLQVELAQ LRHLSTRLVR GWTHLERQKG GIGLRGPGET QLETDRRLVR ERIRSIEGRL LKVRSQRAQG RRARERSETP LISLVGYTNA GKSTLFNRLT QAEVYVADKL FATLDPTLRR VRVPGIGPAI LADTVGFIRH LPHRLVDAFR ATLEETLGAS LLLHVTDGSA AERDANVDAV NEVLEEISAD ELPVLHVYNK VDLLGETPRI ERDEQGRPWR VWMSAQTGAG LDLLHQAMAE RLASGWVDQW VRLPAFAGRL RARLHEAGEV LNEETDERGD MLLRVRVNRI HFQRLLRSEG LTETDVAAVA PVAGGGDASY NPSRPHSH // ID A0A0B4XY27_9PROT Unreviewed; 459 AA. AC A0A0B4XY27; DT 01-APR-2015, integrated into UniProtKB/TrEMBL. DT 01-APR-2015, sequence version 1. DT 10-MAY-2017, entry version 16. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=TH3_09875 {ECO:0000313|EMBL:AJD52091.1}; OS Thalassospira xiamenensis M-5 = DSM 17429. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales; OC Rhodospirillaceae; Thalassospira. OX NCBI_TaxID=1123366 {ECO:0000313|EMBL:AJD52091.1, ECO:0000313|Proteomes:UP000007127}; RN [1] {ECO:0000313|EMBL:AJD52091.1, ECO:0000313|Proteomes:UP000007127} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=M-5 {ECO:0000313|EMBL:AJD52091.1}; RX PubMed=23209216; DOI=10.1128/JB.01904-12; RA Lai Q., Shao Z.; RT "Genome sequence of Thalassospira xiamenensis type strain M-5."; RL J. Bacteriol. 194:6957-6957(2012). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP004388; AJD52091.1; -; Genomic_DNA. DR EnsemblBacteria; AJD52091; AJD52091; TH3_09875. DR KEGG; txi:TH3_09875; -. DR KO; K03665; -. DR Proteomes; UP000007127; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000007127}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000007127}. FT COILED 191 221 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 459 AA; 51136 MW; B7B745E74B80B9B5 CRC64; MIRASLRRTK KIADESLTAG ANGDDDSPRV LVFHPELKRA DQAGSWRDAS SRLEEAVSLT GALDFEVVGA EVVPIAKTRP ATLFGTGVVE RLGNQIKAEE ADIVMINGQL SPIQQRNLER EWKCKVIDRT GLILEIFADR ARTREGRLQV QLALLSYQKS RLVRTWTHLE RQRGGRGFLA GPGERQIEID RRLIGDKLAK LRRELEEVKR TRELHREARR RVPYPIVALV GYTNAGKSTL FNQLTVSDVF AEDMLFATLD PTMRGLELPS GRKVILSDTV GFVSDLPHDL VAAFRATLEE VLEADLIVHV RDASSHEAEA QKLDVLEVLK ALGLQKAIDG EELVEALNKC DQLEGEDLTA VQEYSARNAN TIAISAIKGT NCDALLALIE DRLTEDMPVF ELLVPYSDGK ALARLYEQGE VLKRIDGEDG ISVQVRIDDS RVGRFEDWCA KSGFDLHLV // ID A0A0B5AST8_9BACL Unreviewed; 411 AA. AC A0A0B5AST8; DT 01-APR-2015, integrated into UniProtKB/TrEMBL. DT 01-APR-2015, sequence version 1. DT 07-JUN-2017, entry version 16. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=JMA_17770 {ECO:0000313|EMBL:AJD91094.1}; OS Jeotgalibacillus malaysiensis. OC Bacteria; Firmicutes; Bacilli; Bacillales; Planococcaceae; OC Jeotgalibacillus. OX NCBI_TaxID=1508404 {ECO:0000313|EMBL:AJD91094.1, ECO:0000313|Proteomes:UP000031449}; RN [1] {ECO:0000313|EMBL:AJD91094.1, ECO:0000313|Proteomes:UP000031449} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=D5 {ECO:0000313|EMBL:AJD91094.1, RC ECO:0000313|Proteomes:UP000031449}; RA Yaakop A.S., Chan K.-G., Goh K.M.; RT "Complete genome of a marine bacteria Jeotgalibacillus malaysiensis."; RL Submitted (AUG-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP009416; AJD91094.1; -; Genomic_DNA. DR RefSeq; WP_039809059.1; NZ_CP009416.1. DR EnsemblBacteria; AJD91094; AJD91094; JMA_17770. DR KEGG; jeo:JMA_17770; -. DR KO; K03665; -. DR Proteomes; UP000031449; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000031449}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000031449}. FT DOMAIN 198 359 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 157 184 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 411 AA; 46581 MW; 6D94E7614E711F46 CRC64; MVYIKLEKAI LVGVNTDRTD QDFIESMNEL HALAETAGAD PVLDLIQNME KVHPATFIGK GKLEELISAS EELEPELIIF NSELSPSQNR NLSEVLSARV IDRTQLILDI FAQRARSKEG KLQVQLAQLE YMLPRLGGQG VELSRLGGGI GTRGPGETKL ETDRRHIRRE IREIKKKLEQ VVRHRSIYRE RRKQNQAFQI ALIGYTNAGK STLFNLLTYA DSFEENQLFA TLDPLSRKCI LPSGFETIMT DTVGFIKDLP TSLIASFRST LEEVKEADFL LHVVDASHPN HADHEKTVKK LLNDLEMDQI PRMTVYNKED LLSSEFVADR SDPFVLMSAA KKESNKVLVE IEKEVKQQFV PYNMTVSSDD GKVLAQLKKE SMLLKLSFIE EEEHYLAEGY ISKDHPLAAR I // ID A0A0B5CR42_NEIEG Unreviewed; 394 AA. AC A0A0B5CR42; DT 01-APR-2015, integrated into UniProtKB/TrEMBL. DT 01-APR-2015, sequence version 1. DT 05-JUL-2017, entry version 17. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=NELON_07375 {ECO:0000313|EMBL:AJE18726.1}; OS Neisseria elongata subsp. glycolytica ATCC 29315. OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=546263 {ECO:0000313|EMBL:AJE18726.1, ECO:0000313|Proteomes:UP000031392}; RN [1] {ECO:0000313|Proteomes:UP000031392} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29315 {ECO:0000313|Proteomes:UP000031392}; RA Veyrier F.J., Taha M.-K.; RT "Complete Genome sequence of Neisseria elongata subsp. glycolytica."; RL Submitted (MAY-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP007726; AJE18726.1; -; Genomic_DNA. DR EnsemblBacteria; AJE18726; AJE18726; NELON_07375. DR KEGG; nel:NELON_07375; -. DR PATRIC; fig|546263.7.peg.1579; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR KO; K03665; -. DR Proteomes; UP000031392; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000031392}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000031392}. FT DOMAIN 212 381 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 394 AA; 43444 MW; A12CF7D3BCB01201 CRC64; MSKQPDKFLS KPERIMLVGM MFDADYTGAN ESRERAFAAA MAEAEELVRA TGGELVCRQT AKRDRAHPAL FVGTGKAEEL AQAVSEQQIE LAVFNHELTP TQERNLEKAL QCRVLDRVGL ILAIFAQRAQ SQEGRLQVEL AQLTHLSGRL VRGYGHLQSQ KGGIGLKGPG ETQLETDRRL IAQKITALKK RLEATRRQRA TRRKAREHGG LPTFALVGYT NTGKSSLFNR LTKADVLAKN QLFATLDTTA RRLYLNPSAS IILTDTVGFV RDLPHGLVAA FSATLEETAL ADVLLHVVDA AHPEHERQID DVNEVLREIG AGDIPQIVLY NKTDLLPPEK RRFGVLRDVQ GRAVAANISV KTGEGLDALR EILAEHAVSD GLNGYKPTFH KEIE // ID A0A0B5DQP3_9ACTN Unreviewed; 496 AA. AC A0A0B5DQP3; DT 01-APR-2015, integrated into UniProtKB/TrEMBL. DT 01-APR-2015, sequence version 1. DT 07-JUN-2017, entry version 18. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=SNOD_24695 {ECO:0000313|EMBL:AJE42886.1}; OS Streptomyces nodosus. OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae; OC Streptomyces. OX NCBI_TaxID=40318 {ECO:0000313|EMBL:AJE42886.1, ECO:0000313|Proteomes:UP000031526}; RN [1] {ECO:0000313|Proteomes:UP000031526} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 14899 {ECO:0000313|Proteomes:UP000031526}; RA Sweeney P., Stephens N., Murphy C., Caffrey P.; RT "Sequence of the Streptomyces nodosus genome."; RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP009313; AJE42886.1; -; Genomic_DNA. DR RefSeq; WP_043444505.1; NZ_CP009313.1. DR EnsemblBacteria; AJE42886; AJE42886; SNOD_24695. DR Proteomes; UP000031526; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 2. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000313|EMBL:AJE42886.1}; KW Complete proteome {ECO:0000313|Proteomes:UP000031526}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900, KW ECO:0000313|EMBL:AJE42886.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000031526}. FT DOMAIN 274 439 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 496 AA; 54029 MW; 202CB7C8EBAF39DC CRC64; MTSSSSLPQD STRFAHAYPE GLRADALMEE DVAWSHGIDG ERDGDQFDRS ERAALRRVAG LSTELEDVTE VEYRQLRLER VVLVGVWTSG TAQDAENSLA ELAALAETAG ALVLDGVMQR RDTPDASTYI GSGKATELRD IVLETGADTV VCDGELSPAQ LIHLEDIVKV KVIDRTALIL DIFAQHAKSR EGKAQVALAQ MQYMLPRLRG WGQSLSRQMG GGSGGLATRG PGETKIETDR RRIREKMAKM RREIAEMKTG REIKRQERRR HKVPSVAIAG YTNAGKSSLL NRLTGAGVLV ENALFATLDP TVRRAETPSG RLYTLADTVG FVRHLPHHLV EAFRSTMEEV GDADLILHVV DGSHPVPEEQ LAAVREVIRD VGATDVPEIV VINKADAADP LVLQRLLRVE KRSLAVSART GAGIEELLAL IDDELPKPSV EIEALVPYTH GRLVALAHTE GEVNSEEHTP EGTLLKARVH PELAAELAPY IPASAL // ID A0A0B5E1P3_9RHOB Unreviewed; 432 AA. AC A0A0B5E1P3; DT 01-APR-2015, integrated into UniProtKB/TrEMBL. DT 01-APR-2015, sequence version 1. DT 07-JUN-2017, entry version 16. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=P73_2251 {ECO:0000313|EMBL:AJE46966.1}; OS Celeribacter indicus. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae; Celeribacter. OX NCBI_TaxID=1208324 {ECO:0000313|EMBL:AJE46966.1, ECO:0000313|Proteomes:UP000031521}; RN [1] {ECO:0000313|EMBL:AJE46966.1, ECO:0000313|Proteomes:UP000031521} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=P73 {ECO:0000313|EMBL:AJE46966.1}; RX PubMed=25256706; DOI=10.1099/ijs.0.069039-0; RA Lai Q., Cao J., Yuan J., Li F., Shao Z.; RT "Celeribacter indicus sp. nov., a polycyclic aromatic hydrocarbon- RT degrading bacterium from deep-sea sediment and reclassification of RT Huaishuia halophila as Celeribacter halophilus comb. nov."; RL Int. J. Syst. Evol. Microbiol. 64:4160-4167(2014). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP004393; AJE46966.1; -; Genomic_DNA. DR RefSeq; WP_052453206.1; NZ_FNNW01000007.1. DR EnsemblBacteria; AJE46966; AJE46966; P73_2251. DR KEGG; cid:P73_2251; -. DR KO; K03665; -. DR Proteomes; UP000031521; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000031521}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000031521}. FT DOMAIN 207 380 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 432 AA; 48830 MW; E5CB7313EF62F14C CRC64; MAELHEHEIL PTRAWVLHPD ITSDRDRRDP VAGLEEAVAL AEALPNLEVV GSEIVRLPKI QPGHLFGTGK IEELNQRMKA AEVELVLIDG PVSPVQQRNL EKEWKVKILD RTGLILEIFS DRARTREGVL QVEMAALSYQ RTRLVRAWTH LERQRGGLGF VGGPGETQIE ADRRAIDEQL VRLRRQLDKV VKTRELHRAS RAKVPFPIVA LVGYTNAGKS TFFNKVTGAD VFAKDMLFAT LDPTMRQLSI PNAHGGDREI ILSDTVGFIS KLPTQLVAAF RATLEEVLDA DLILHVRDIA AEETEEQKED VLKILHDLGI REDTPMFEVW NKIDLLPEEA RAARLERAGR EPNVFAISAV TGEGIDALLA AVSAWFEEDK IERDLVLPYA EGRKRAWLFE EGVVLNEEMT QDGYDLKVLW TPRQEKQFRE MT // ID A0A0B5EK07_STRA4 Unreviewed; 501 AA. AC A0A0B5EK07; DT 01-APR-2015, integrated into UniProtKB/TrEMBL. DT 01-APR-2015, sequence version 1. DT 12-APR-2017, entry version 16. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=SLNWT_1473 {ECO:0000313|EMBL:AJE81849.1}; OS Streptomyces albus (strain ATCC 21838 / DSM 41398 / FERM P-419 / JCM OS 4703 / NBRC 107858). OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae; OC Streptomyces. OX NCBI_TaxID=1081613 {ECO:0000313|EMBL:AJE81849.1, ECO:0000313|Proteomes:UP000031523}; RN [1] {ECO:0000313|EMBL:AJE81849.1, ECO:0000313|Proteomes:UP000031523} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 21838 / DSM 41398 / FERM P-419 / JCM 4703 / NBRC 107858 RC {ECO:0000313|Proteomes:UP000031523}; RA Lu C.; RT "Enhanced salinomycin production by adjusting the supply of polyketide RT extender units in Streptomyce albus DSM 41398."; RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP010519; AJE81849.1; -; Genomic_DNA. DR EnsemblBacteria; AJE81849; AJE81849; SLNWT_1473. DR KEGG; sals:SLNWT_1473; -. DR KO; K03665; -. DR Proteomes; UP000031523; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000031523}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000031523}. FT DOMAIN 279 444 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 501 AA; 54325 MW; E07F9FE510EC1503 CRC64; MTSSSSLPQA AQSSAQTPVE GLAKDLRADA LMEEDVAWSH GIDTERDGAQ YDRSDRAALR RVAGLSTELQ DVTEVEYRQL RLERVVLVGV WTTGTSQEAE NSLAELAALA ETAGALVLDG VIQRRDKPDA ATYIGSGKAR ELLDLVLESG ADTVICDGEL SPGQLIHLED VVKVKVIDRT ALILDIFAQH AKSREGKAQV ALAQMQYMLP RLRGWGQSLS RQMGGGKGGG LATRGPGETK IETDRRRIRE KMAKMRREIA EMKTGREIKR QERRRNKVPS VAIAGYTNAG KSSLLNRLTG AGVLVENALF ATLDPTVRRA ETPSGRLYTL ADTVGFVRHL PHHLVEAFRS TMEEVGDSDL ILHVVDGSHP APEEQLAAVR EVVRDVGATK VPEIVVVNKA DAADPLVLQR LLRQEKRALV VSARTGQGIA ELRALIDAEL PRPEVEVTAL VPYALGRLVA RAHDDGEVIS EEHTPEGTLL KARVHEELAA ELAPYTPAAA G // ID A0A0B5FFR4_9DELT Unreviewed; 552 AA. AC A0A0B5FFR4; DT 01-APR-2015, integrated into UniProtKB/TrEMBL. DT 01-APR-2015, sequence version 1. DT 07-JUN-2017, entry version 16. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=GSUB_05685 {ECO:0000313|EMBL:AJF06158.1}; OS Geoalkalibacter subterraneus. OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfuromonadales; OC Geobacteraceae; Geoalkalibacter. OX NCBI_TaxID=483547 {ECO:0000313|EMBL:AJF06158.1, ECO:0000313|Proteomes:UP000035036}; RN [1] {ECO:0000313|EMBL:AJF06158.1, ECO:0000313|Proteomes:UP000035036} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Red1 {ECO:0000313|EMBL:AJF06158.1, RC ECO:0000313|Proteomes:UP000035036}; RX PubMed=25767222; RA Badalamenti J.P., Krajmalnik-Brown R., Torres C.I., Bond D.R.; RT "Genomes of Geoalkalibacter ferrihydriticus Z-0531T and RT Geoalkalibacter subterraneus Red1T, Two Haloalkaliphilic Metal- RT Reducing Deltaproteobacteria."; RL Genome Announc. 3:0-0(2015). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP010311; AJF06158.1; -; Genomic_DNA. DR RefSeq; WP_040199680.1; NZ_CP010311.1. DR EnsemblBacteria; AJF06158; AJF06158; GSUB_05685. DR KEGG; gsb:GSUB_05685; -. DR KO; K03665; -. DR Proteomes; UP000035036; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000035036}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000035036}. FT DOMAIN 377 541 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 336 363 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 552 AA; 61526 MW; 095A439B460BA8B8 CRC64; MLDGNLTGLK PSQIKALERV HKRRTAADQV IGADLARFLT ELSGEIRRQL AVLIDRQGTV VHVIVGDDRE IVIPDLSRYR LGRSGLRGLR CIHTHLGGEP LSQDDLTDLA LLRLDLMAAI AVGAHGLPGR IDYAHLLPPT PEGKGVELLS APSVHDLHLD FPHFISSLES EMERKMGETF DLSDPREKAI LISAGREPRA ELEDSLSELA ELARTADVVV LDQVVQRTQK IHPRFLMGEG KLKEVIIRAL QQGATLLIFD QELSPGQARA IGAMTEMKVI DRSQLILDIF ARRAHTLDGK VQVELAQLKY IMPRLLGKGT SMSRLMGGLG GRGPGETKLE IDRRRIRDRI TRLEKQLASL SKGRRQRRQR RIRSQLPIIS IVGYTNAGKS TLLNALTQSA VFTEDLLFAT LDTSSRRLRF PQEREVIITD TVGFIRKLPK SLLGAFKATL EELEDADLLL HVVDISDPRF EEQIVAVERI LQDLDLGTLP RQLVFNKTDK VSSQEVAALC RRFNAIGVSA LDRSSFNPML AELESRFWPG EADDALHEHS EP // ID A0A0B5RJX6_9FLAO Unreviewed; 410 AA. AC A0A0B5RJX6; DT 01-APR-2015, integrated into UniProtKB/TrEMBL. DT 01-APR-2015, sequence version 1. DT 05-JUL-2017, entry version 18. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=MPR_0052 {ECO:0000313|EMBL:AJH13271.1}; OS Myroides profundi. OC Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales; OC Flavobacteriaceae; Myroides. OX NCBI_TaxID=480520 {ECO:0000313|EMBL:AJH13271.1, ECO:0000313|Proteomes:UP000031842}; RN [1] {ECO:0000313|Proteomes:UP000031842} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=D25 {ECO:0000313|Proteomes:UP000031842}; RA Qin Q., Zhang Y.; RT "Complete genome of Myroides profundi D25."; RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP010817; AJH13271.1; -; Genomic_DNA. DR RefSeq; WP_006257874.1; NZ_FOFY01000001.1. DR EnsemblBacteria; AJH13271; AJH13271; MPR_0052. DR GeneID; 31879647; -. DR KEGG; mpw:MPR_0052; -. DR KO; K03665; -. DR Proteomes; UP000031842; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000031842}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000031842}. FT DOMAIN 200 386 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 410 AA; 47679 MW; F90E549DAA167FF8 CRC64; MIDREEINFE RSVIVGIITQ DQDESKLNEY LDELEFLTFT AGGQVYKRFT QKMDKPNPKT FVGTGKMQEI HNYIVENDIH TVIFDDELSP AQQKNISREL DCKVLDRTNL ILDIFAQRAQ TSYARTQVEL AQFQYLLPRL SGMWTHLERQ RGGIGMRGPG ETEIETDRRI VRDRITLLRD KLKVIDKQMA SQRGNRGAMV RVALVGYTNV GKSTLMNAVG KSEVFVENKL FATLDTTVRK IVIGNLPFLL SDTVGFIRKL PTQLVESFKS TLDEVREADL LLHVVDISHH DFVDHIESVN EILKDIKSND KPTIMIFNKI DAYQPERIEE DDLMTERTSK HYSIEEWKKT WMNKVGENNA IFISATNKEN FEEFRKKVYE AVREIHITRF PYNNFLFPDY DHLIESSEEE // ID A0A0B6TWE7_9CORY Unreviewed; 508 AA. AC A0A0B6TWE7; DT 01-APR-2015, integrated into UniProtKB/TrEMBL. DT 01-APR-2015, sequence version 1. DT 07-JUN-2017, entry version 16. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:AJK69076.1}; GN ORFNames=B840_07390 {ECO:0000313|EMBL:AJK69076.1}; OS Corynebacterium marinum DSM 44953. OC Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae; OC Corynebacterium. OX NCBI_TaxID=1224162 {ECO:0000313|EMBL:AJK69076.1, ECO:0000313|Proteomes:UP000031928}; RN [1] {ECO:0000313|EMBL:AJK69076.1, ECO:0000313|Proteomes:UP000031928} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 44953 {ECO:0000313|EMBL:AJK69076.1, RC ECO:0000313|Proteomes:UP000031928}; RA Schaffert L., Albersmeier A., Kalinowski J., Ruckert C.; RT "Complete genome sequence of Corynebacterium marinum DSM 44953."; RL Submitted (MAY-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP007790; AJK69076.1; -; Genomic_DNA. DR RefSeq; WP_042621599.1; NZ_CP007790.1. DR EnsemblBacteria; AJK69076; AJK69076; B840_07390. DR KEGG; cmq:B840_07390; -. DR KO; K03665; -. DR Proteomes; UP000031928; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000031928}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000031928}. FT DOMAIN 275 444 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 234 261 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 508 AA; 55158 MW; 7CFD9F21147A85E6 CRC64; MTNENDDLLA RAFRDNEPQP ATPEDPGTDL SGLLAPTTGE LDLAERNRLR RGASDTEIRS TDTEDITEVE YRKLRLEQVI LVGVWTEGTS AEVDANMAEL AALAETAGAE VLETLYQRRD KPDPGTYIGS GKVQELKDII AATGADTVVC DGELSPGQLV ALETALNTKV IDRTMLILDI FAQHAKSKEG KAQVSLAQME YLYTRVRGWG GNLSRQAGGR AGSNGGVGLR GPGETRIEAD RRRLRTDMSK LRRELSGMKT AREIKRQRRR SSTIPQIAIA GYTNAGKSSL INALTGAGVL VENALFATLD PTTRRAELAD GRAVVFTDTV GFVRHLPTQL VEAFKSTLEE VLGADLVLHV VDGSDPFPLK QIEAVNKVIY SIVKETGEQA PPEMIVVNKI DQADPLVLAE LRHAVEDAVY VSAKTGEGIA ELQARIELFL NSLDAHLVLL VPFTRGDVIS RLHEYGTVRS EEYTEHGTRI DVRLPMSLAA ELAEFAVDPD AGTVPDAS // ID A0A0B6WT01_9BACT Unreviewed; 601 AA. AC A0A0B6WT01; DT 01-APR-2015, integrated into UniProtKB/TrEMBL. DT 01-APR-2015, sequence version 1. DT 12-APR-2017, entry version 15. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=PYK22_00098 {ECO:0000313|EMBL:CDM64106.1}; OS Pyrinomonas methylaliphatogenes. OC Bacteria; Acidobacteria; Blastocatellia; Pyrinomonas. OX NCBI_TaxID=454194 {ECO:0000313|EMBL:CDM64106.1, ECO:0000313|Proteomes:UP000031518}; RN [1] {ECO:0000313|EMBL:CDM64106.1, ECO:0000313|Proteomes:UP000031518} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K22 {ECO:0000313|EMBL:CDM64106.1, RC ECO:0000313|Proteomes:UP000031518}; RA Stott M.; RL Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:CDM64106.1, ECO:0000313|Proteomes:UP000031518} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K22 {ECO:0000313|EMBL:CDM64106.1, RC ECO:0000313|Proteomes:UP000031518}; RA Lee K.C.Y., Power J.F., Dunfield P.F., Morgan X.C., Huttenhower C., RA Stott M.B.; RT "Complete genome sequence of Pyrinomonas methylaliphatogenes type RT strain K22T."; RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CBXV010000001; CDM64106.1; -; Genomic_DNA. DR EnsemblBacteria; CDM64106; CDM64106; PYK22_00098. DR Proteomes; UP000031518; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000031518}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000031518}. FT DOMAIN 412 582 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 371 405 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 601 AA; 67327 MW; 48C2EC48F3B407F2 CRC64; MRISAPAVCC AGGCGSGSSF FLGGSTISQI YGHTGGLKPS QQRRVAKLYE RRVAPQQIVT PELARQLAEL SHETRRQIGV LVDRKGRVEY VIVGDAHRIE LPDFRRMRTS PERFRGLRCI HTHLHAEPLT QDDLTDLALL RLDLMAAIVV DGQTGLPTVV YAAHLLPATA HQLREAHRSP YVFLEPRPPS QLNLDFLALI SSLEEEMARN RRAARQAGTE ERAILIGVTT GPLSEAEESM AELRELAASA NIAVLDCVIQ RRSAIDPHTV LGRGKLEEVL IRAMQLGADL IIFDRELQPA QVRSISEATD LKVIDRAQLI LDIFAQRAQS REGKIQVELA QLRYRLPRLV VGQDSAFSRL AGGIGGRGPG ETKLETDRRR VRDRINRLER EIELLRERRQ ERRKQRIRRH RPIVSLVGYT NAGKSTLLNA LTASDVHVER RMFATLDPTA RRLRLPRERE VIINDTVGFI RDLPPDLIAA FRATLEEIRD SDLLLHVVDV SDEGWPRRFE AVERILRELG FATIPRLTVF NKTDLVDPAS IAAAERQIEA CGVRAHVFVS AIDRKTLDPL LARLDEALAH EDSLCGQPDW SAAELAAMRK I // ID A0A0B7H0X3_9FLAO Unreviewed; 435 AA. AC A0A0B7H0X3; DT 01-APR-2015, integrated into UniProtKB/TrEMBL. DT 01-APR-2015, sequence version 1. DT 12-APR-2017, entry version 14. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:CEN33181.1}; GN ORFNames=CCYN2B_140089 {ECO:0000313|EMBL:CEN33181.1}; OS Capnocytophaga cynodegmi. OC Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales; OC Flavobacteriaceae; Capnocytophaga. OX NCBI_TaxID=28189 {ECO:0000313|EMBL:CEN33181.1, ECO:0000313|Proteomes:UP000038055}; RN [1] {ECO:0000313|EMBL:CEN33181.1, ECO:0000313|Proteomes:UP000038055} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Ccyn2B {ECO:0000313|EMBL:CEN33181.1, RC ECO:0000313|Proteomes:UP000038055}; RA Xiang T., Song Y., Huang L., Wang B., Wu P.; RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CDOD01000006; CEN33181.1; -; Genomic_DNA. DR EnsemblBacteria; CEN33181; CEN33181; CCYN2B_140089. DR Proteomes; UP000038055; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000038055}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000038055}. FT DOMAIN 228 413 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 435 AA; 50610 MW; 46C28E849C06DC26 CRC64; MIYRHKYTFF PYRKNYFVIF ANETIKHTML EQINLNYEKV VLVGIINQMQ DEEKSKEYLD ELEFLTYTAG GEVLQRFTQK LDVPNPKTFI GTGKMEEVQQ FVEENRVGTV IFDDELSPAQ QKNIERILKA KILDRTGLIL DIFAQRAQTS YSRTQVELAQ YQYLLPRLTG LWTHLERQRG GIGMRGPGET EIETDRRIVR DRIALLKKKL ATIDRQMAVQ RSNRGAMVRV ALIGYTNVGK STIMNVISKS DVFAENKLFA TLDTTVRKVV IGNLPFLLSD TVGFIRKLPT QLIESFKSTL DEVREADLLL HIVDISHPNF EEHIHSVNQI LSEIKSADKP TIMVFNKIDA YKHQTIAEDD LITEPTSKHF TLEQWKQTWM NKVGNDVLFI SALNKDNLEE FREKVYAKVR EIHITRFPYN NFLYPEFIEE DTETN // ID A0A0B7INN8_9FLAO Unreviewed; 406 AA. AC A0A0B7INN8; DT 01-APR-2015, integrated into UniProtKB/TrEMBL. DT 01-APR-2015, sequence version 1. DT 07-JUN-2017, entry version 18. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:CEN52179.1}; GN ORFNames=CCAND38_100035 {ECO:0000313|EMBL:CEN43374.1}, GN CCAND93_220021 {ECO:0000313|EMBL:CEN52179.1}; OS Capnocytophaga canis. OC Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales; OC Flavobacteriaceae; Capnocytophaga. OX NCBI_TaxID=1848903 {ECO:0000313|EMBL:CEN52179.1, ECO:0000313|Proteomes:UP000038200}; RN [1] {ECO:0000313|EMBL:CEN52179.1, ECO:0000313|Proteomes:UP000038200, ECO:0000313|Proteomes:UP000045051} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CcD38 {ECO:0000313|EMBL:CEN43374.1, RC ECO:0000313|Proteomes:UP000045051}, and RC CcD93 {ECO:0000313|EMBL:CEN52179.1, RC ECO:0000313|Proteomes:UP000038200}; RA MANFREDI Pablo; RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CDOI01000002; CEN43374.1; -; Genomic_DNA. DR EMBL; CDOL01000135; CEN52179.1; -; Genomic_DNA. DR RefSeq; WP_042006829.1; NZ_CDOL01000135.1. DR EnsemblBacteria; CEN43374; CEN43374; CCAND38_100035. DR EnsemblBacteria; CEN52179; CEN52179; CCAND93_220021. DR Proteomes; UP000038200; Unassembled WGS sequence. DR Proteomes; UP000045051; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000045051}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000045051}. FT DOMAIN 200 385 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 406 AA; 46728 MW; B6581F80859571A6 CRC64; MLEQMNLNYE KVVLVGIINQ TQDEEKSKEY LDELEFLTYT AGGEVLKRFT QRLDVPNPKT FIGTGKMEEV QLFVEENGVG TVIFDDELSP AQQKNIERIL KAKILDRTGL ILDIFAQRAQ TSYSRTQVEL AQYQYLLPRL TGLWTHLERQ RGGIGMRGPG ETEIETDRRI VRDRIALLKK KLSSIDRQMA VQRSNRGALV RVALIGYTNV GKSTLMNVIS KSEVFAENKL FATLDTTVRK VVIGNLPFLL SDTVGFIRKL PTQLIESFKS TLDEVREADL LLHIVDISHP NFEEHIQSVN QILTEIKSAD KPTIMVFNKI DAYTHESIAD DDLTTEFTKK HFTLEDWKQT WMNKVGDDVL FISALNKDNL AEFREKVYAK VREIHITRFP YNNFLYPEFV EISEDE // ID A0A0B7IZM7_9PROT Unreviewed; 375 AA. AC A0A0B7IZM7; DT 01-APR-2015, integrated into UniProtKB/TrEMBL. DT 01-APR-2015, sequence version 1. DT 30-AUG-2017, entry version 19. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:CEN55877.1}; GN ORFNames=BN1209_0834 {ECO:0000313|EMBL:CEN55877.1}; OS Candidatus Methylopumilus turicensis. OC Bacteria; Proteobacteria; Betaproteobacteria; Nitrosomonadales; OC Methylophilaceae; Candidatus Methylopumilus. OX NCBI_TaxID=1581680 {ECO:0000313|EMBL:CEN55877.1, ECO:0000313|Proteomes:UP000056322}; RN [1] {ECO:0000313|EMBL:CEN55877.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=MMS-10A-171 {ECO:0000313|EMBL:CEN55877.1}; RA Salcher M Michaela; RL Submitted (DEC-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LN794158; CEN55877.1; -; Genomic_DNA. DR RefSeq; WP_045751083.1; NZ_LN794158.1. DR EnsemblBacteria; CEN55877; CEN55877; BN1209_0834. DR KEGG; mbac:BN1209_0834; -. DR KO; K03665; -. DR Proteomes; UP000056322; Chromosome 1. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000056322}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000056322}. FT DOMAIN 199 365 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 158 192 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 375 AA; 41847 MW; 9080FF93EE956E92 CRC64; MLDRPETSSD AILVSLDFGE SGYEESLEEL KQLAISAGIN IRGVVEGKRD KPDAKLYLGS GKAEELAEMV KATESRAVVF NHDLSPSQQR NLERLLECRV ADRTGLILDI FAQRAKSHEG KLQVELAQLE HLSTRLVRGW THLERQKGGI GVRGGPGETQ LELDRRMLRV RVKQLREKLD KLKQQRGMQR RSRQRSQVMS VSLVGYTNAG KSTLFNRLTQ SKVLAADQLF ATLDTTSRKL YIPDAGAMVI SDTVGFIKHL PHALVEAFGA TLEESVQSDL LLHIVDSAST NRDEQIEQVN KVLGEIGAQD VAQILVMNQI DRAGLQAGLE RDEYGRICKV LISAKTGAGL QYLEQALKEH QQRLYDYRTT EAAYL // ID A0A0B8N5K3_9NOCA Unreviewed; 518 AA. AC A0A0B8N5K3; DT 01-APR-2015, integrated into UniProtKB/TrEMBL. DT 01-APR-2015, sequence version 1. DT 07-JUN-2017, entry version 21. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=NS07_v2contig00012-0053 {ECO:0000313|EMBL:GAM45191.1}, GN NS506_06085 {ECO:0000313|EMBL:APB00122.1}; OS Nocardia seriolae. OC Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae; Nocardia. OX NCBI_TaxID=37332 {ECO:0000313|EMBL:GAM45191.1, ECO:0000313|Proteomes:UP000019401}; RN [1] {ECO:0000313|EMBL:GAM45191.1, ECO:0000313|Proteomes:UP000019401} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=N-2927 {ECO:0000313|EMBL:GAM45191.1, RC ECO:0000313|Proteomes:UP000019401}; RA Imajoh M., Fukumoto Y., Yamane J., Sukeda M., Shimizu M., Ohnishi K., RA Oshima S.; RT "Draft Genome Sequence of Nocardia seriolae Strain N-2927 (NBRC RT 110360), Isolated as the Causal Agent of Nocardiosis of Yellowtail RT (Seriola quinqueradiata) in Kochi Prefecture, Japan."; RL Genome Announc. 3:e00082-15(2015). RN [2] {ECO:0000313|EMBL:APB00122.1, ECO:0000313|Proteomes:UP000180166} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=EM150506 {ECO:0000313|EMBL:APB00122.1, RC ECO:0000313|Proteomes:UP000180166}; RA Han H.-J.; RT "Genome sequence of Nocardia seriolae strain EM150506, isolated from RT Anguila japonica."; RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP017839; APB00122.1; -; Genomic_DNA. DR EMBL; BAWD02000012; GAM45191.1; -; Genomic_DNA. DR EnsemblBacteria; GAM45191; GAM45191; NS07_v2contig00012-0053. DR KEGG; nsr:NS506_06085; -. DR PATRIC; fig|37332.12.peg.6252; -. DR KO; K03665; -. DR Proteomes; UP000019401; Unassembled WGS sequence. DR Proteomes; UP000180166; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 2. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000019401}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000019401}. FT DOMAIN 269 438 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 228 262 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 518 AA; 55947 MW; 8C7686623049B073 CRC64; MSKPETYEFT PAEDLDEETK DVPGTGRGGW SAAPTVGEQQ LEERAALRRV AGLSTELEDV TEVEYRQLRL ERVVLVGVWT EGTAAQADAS MAELAALAET AGSEVLDALI QRRDKPDKST YIGSGKADEL RGIVLETGAD TVICDGELTP AQLTALEKVV KVKVIDRTAL ILDIFAQHAT SREGKAQVSL AQMEYMLPRL RGWGESMSRQ AGGRAGSNGG VGLRGPGETK IETDRRRIRE RMAKLRREIR EMKTARDTKR AKRAESGIPQ VAIVGYTNAG KSSLMNALTD AGILVQDALF ATLDPTTRRA ALEDGREVVF TDTVGFVRHL PTQLVEAFRS TLEEVTGADL LLHVVDGSDP LPDQQIKAVR EVIADVLRES KTPAPPEFLV VNKIDALDPL ELTQLRGWLP DAAFVSARTG EGLDQLRDRL GQILGGLDVE VSVLLPYTRG DLLARIHADG KILSSEHEES GTRVRARVPN SLAGQLAQFA HAGGSADDVS LNGSAASDEF ASLEDSQS // ID A0A0B8PYI4_9VIBR Unreviewed; 238 AA. AC A0A0B8PYI4; DT 01-APR-2015, integrated into UniProtKB/TrEMBL. DT 01-APR-2015, sequence version 1. DT 16-MAR-2016, entry version 9. DE SubName: Full=GTP-binding protein hflX {ECO:0000313|EMBL:GAM69767.1}; GN ORFNames=JCM19236_2556 {ECO:0000313|EMBL:GAM69767.1}; OS Vibrio sp. JCM 19236. OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; OC Vibrionaceae; Vibrio. OX NCBI_TaxID=1481926 {ECO:0000313|EMBL:GAM69767.1, ECO:0000313|Proteomes:UP000031680}; RN [1] {ECO:0000313|EMBL:GAM69767.1, ECO:0000313|Proteomes:UP000031680} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=JCM19236 {ECO:0000313|EMBL:GAM69767.1, RC ECO:0000313|Proteomes:UP000031680}; RA Sawabe T., Meirelles P., Feng G., Sayaka M., Hattori M., Ohkuma M.; RT "Vibrio sp. C94 JCM 19236 whole genome shotgun sequence."; RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:GAM69767.1, ECO:0000313|Proteomes:UP000031680} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=JCM19236 {ECO:0000313|EMBL:GAM69767.1, RC ECO:0000313|Proteomes:UP000031680}; RG NBRP consortium; RA Sawabe T., Meirelles P., Feng G., Sayaka M., Hattori M., Ohkuma M.; RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:GAM69767.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BBSB01000012; GAM69767.1; -; Genomic_DNA. DR EnsemblBacteria; GAM69767; GAM69767; JCM19236_2556. DR Proteomes; UP000031680; Unassembled WGS sequence. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000031680}; KW Reference proteome {ECO:0000313|Proteomes:UP000031680}. FT DOMAIN 25 112 GTP-bdg_N. {ECO:0000259|Pfam:PF13167}. FT DOMAIN 114 192 GTP-bdg_M. {ECO:0000259|Pfam:PF16360}. SQ SEQUENCE 238 AA; 27641 MW; 0BCC44245E496E6E CRC64; MFDRYESGEQ AVLVHINFTQ EGEWEDLAEF EMLVSSAGVN NLQTVTGSRQ SPHPKYYVGE GKAQEISDVV QQTGAEIVIF NHALSPAQER NLEQLCKCRV LDRTGLILDI FAQRARTHEG KLQVELAQLR HISTRLIRGW THLERQKGGI GLRGPGETQL ETDRRLLRDR IKAILRRLER VAKQREQGRR ARKRARSLHF RWWVIPMPVN RPYSTALLRQ VCMRLTNYLQ LLTLHCVR // ID A0A0B8QUV7_9VIBR Unreviewed; 429 AA. AC A0A0B8QUV7; A0A0B8P035; DT 01-APR-2015, integrated into UniProtKB/TrEMBL. DT 01-APR-2015, sequence version 1. DT 30-AUG-2017, entry version 18. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=JCM19231_2482 {ECO:0000313|EMBL:GAM56673.1}, GN JCM19241_2159 {ECO:0000313|EMBL:GAM78753.1}; OS Vibrio ishigakensis. OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; OC Vibrionaceae; Vibrio. OX NCBI_TaxID=1481914 {ECO:0000313|EMBL:GAM78753.1, ECO:0000313|Proteomes:UP000031666}; RN [1] {ECO:0000313|EMBL:GAM56673.1, ECO:0000313|Proteomes:UP000031671} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=JCM 19231 {ECO:0000313|Proteomes:UP000031671}, and RC JCM19231 {ECO:0000313|EMBL:GAM56673.1}; RA Sawabe T., Meirelles P., Feng G., Sayaka M., Hattori M., Ohkuma M.; RT "Vibrio sp. C1 JCM 19231 whole genome shotgun sequence."; RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:GAM78753.1, ECO:0000313|Proteomes:UP000031666} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=JCM 19241 {ECO:0000313|Proteomes:UP000031666}, and RC JCM19241 {ECO:0000313|EMBL:GAM78753.1}; RA Sawabe T., Meirelles P., Feng G., Sayaka M., Hattori M., Ohkuma M.; RT "Vibrio sp. C94 JCM 19241 whole genome shotgun sequence."; RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases. RN [3] {ECO:0000313|EMBL:GAM78753.1, ECO:0000313|Proteomes:UP000031666, ECO:0000313|Proteomes:UP000031671} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=JCM 19231 {ECO:0000313|Proteomes:UP000031671}, RC JCM 19241 {ECO:0000313|Proteomes:UP000031666}, RC JCM19231 {ECO:0000313|EMBL:GAM56673.1}, and RC JCM19241 {ECO:0000313|EMBL:GAM78753.1}; RG NBRP consortium; RA Sawabe T., Meirelles P., Feng G., Sayaka M., Hattori M., Ohkuma M.; RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:GAM78753.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BBRZ01000034; GAM56673.1; -; Genomic_DNA. DR EMBL; BBSC01000018; GAM78753.1; -; Genomic_DNA. DR EnsemblBacteria; GAM56673; GAM56673; JCM19231_2482. DR EnsemblBacteria; GAM78753; GAM78753; JCM19241_2159. DR Proteomes; UP000031666; Unassembled WGS sequence. DR Proteomes; UP000031671; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000031671}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000031671}. FT DOMAIN 198 365 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 429 AA; 49006 MW; 30C8092CE6AAB041 CRC64; MFDRYESGEQ AVLVHINFTQ EGEWEDLAEF EMLVSSAGVN NLQTVTGSRQ SPHPKYYVGE GKAQEISDVV QQTGAEIVIF NHALSPAQER NLEQLCKCRV LDRTGLILDI FAQRARTHEG KLQVELAQLR HISTRLIRGW THLERQKGGI GLRGPGETQL ETDRRLLRDR IKAILRRLER VAKQREQGRR ARKRAEIPTL SLVGYTNAGK STLFNRITEA SVYAADQLFA TLDPTLRKIE LDDVGLAILA DTVGFIRHLP HDLVAAFKAT LQETQEADIL LHVIDASDER FRENIHAVDV VLEEIDAHEI PTLLVMNKID NLEGATPRIE YDDENKPVRV WVSAMEGQGI ELLFQALTER LASQMVEYKL CIPPRFQGRL RSVLFNMKSI RQEEYDTEGN LLIDIRMQQA DWARLQKREE VELDDFIVV // ID A0A0B8T7G2_9SPHI Unreviewed; 396 AA. AC A0A0B8T7G2; DT 01-APR-2015, integrated into UniProtKB/TrEMBL. DT 01-APR-2015, sequence version 1. DT 07-JUN-2017, entry version 17. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=DI53_1841 {ECO:0000313|EMBL:KGE14414.1}; OS Sphingobacterium deserti. OC Bacteria; Bacteroidetes; Sphingobacteriia; Sphingobacteriales; OC Sphingobacteriaceae; Sphingobacterium. OX NCBI_TaxID=1229276 {ECO:0000313|EMBL:KGE14414.1, ECO:0000313|Proteomes:UP000031802}; RN [1] {ECO:0000313|EMBL:KGE14414.1, ECO:0000313|Proteomes:UP000031802} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ACCC05744 {ECO:0000313|Proteomes:UP000031802}; RA Teng C., Zhou Z., Li X., Chen M., Lin M., Wang L., Su S., Zhang C., RA Zhang W.; RT "Whole-Genome optical mapping and complete genome sequence of RT Sphingobacterium deserti sp. nov., a new spaces isolated from desert RT in the west of China."; RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KGE14414.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JJMU01000026; KGE14414.1; -; Genomic_DNA. DR RefSeq; WP_037497908.1; NZ_JJMU01000026.1. DR EnsemblBacteria; KGE14414; KGE14414; DI53_1841. DR PATRIC; fig|1229276.3.peg.1897; -. DR Proteomes; UP000031802; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000031802}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000031802}. FT DOMAIN 204 385 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 396 AA; 45057 MW; 05BB53008D4C2279 CRC64; MARTKIYDTA IKPETAVLVS VITPDTTEAK AHEYLEELAF LVETAGGVNK GIFTQKLAYP DRATFVGSGK LEEIKADIIA EEVDMVVFDD ELSPSQLRNI EKEFQIKVLD RSNLILDIFA RHAQTAQAKT QVELAQLQYV LPRLTRMWTH LERQRGGIGM RGPGESQIES DRRMILNKIS LLKERLKQID KQNETQRKNR GELIRAALVG YTNVGKSTIM NMVSKSDVLI ENKLFATLDT TVRKVVIDNL PFLLSDTVGF IRKLPHHLVE CFKSTLDEVR EADILIHVVD ISHPNFEDHI QAVNETLKEL GALDKPVVTV FNKIDAYKAP VSETEEGEEV KVTLDDFRNS WMARNSDPAI FISATDKTNV EEFKERLYSI VVDLHNQRYP YNNLLY // ID A0A0B8WTB4_9DELT Unreviewed; 421 AA. AC A0A0B8WTB4; DT 01-APR-2015, integrated into UniProtKB/TrEMBL. DT 01-APR-2015, sequence version 1. DT 12-APR-2017, entry version 16. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=OM95_11595 {ECO:0000313|EMBL:KHD87911.1}; OS Bdellovibrio sp. ArHS. OC Bacteria; Proteobacteria; Deltaproteobacteria; Bdellovibrionales; OC Bdellovibrionaceae; Bdellovibrio. OX NCBI_TaxID=1569284 {ECO:0000313|EMBL:KHD87911.1, ECO:0000313|Proteomes:UP000031468}; RN [1] {ECO:0000313|EMBL:KHD87911.1, ECO:0000313|Proteomes:UP000031468} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Lal R., Sangwan N., Lambert C., Sharma A., Gupta V., Khurana P., RA Khurana J.P., Sockett R.E., Gilbert J.A.; RT "Predation in situ: Arsenic rich Himalayan hot spring metagenomics RT reveal genetically novel predator-prey genotypes."; RL Submitted (NOV-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KHD87911.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JTEV01000020; KHD87911.1; -; Genomic_DNA. DR Proteomes; UP000031468; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000031468}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}. FT DOMAIN 204 367 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 421 AA; 47426 MW; B7592701682D94B1 CRC64; MTNQAHVSAQ DRVIVIGVGL KTEPLSEIKE NLLELEELVS AAGGEVVGSI IQVLPQWNPA TLIGSGKVEE VAEMVRDSRA NIVVMDHQLS GVQQRNLAQV MKARVIDRNQ LILDIFAQRA QTFEGKLQVE LAQLLDQMPR MVGAWLESLS RQGGGIGTRG PGETALENDR RRIRERVAII KKKLEGVRKN RAQHRQSRRR HEIPSFALIG YTNSGKSSLL NRLTGAQVMA KNQVFATLDP TTRKIFLPDG PPGVVTDTVG FIRKLPTQLI EAFKATLEES SDADVLLHVI DLSSPNMERQ IEVVEALVKE FNWQDKKIIH VYNKCDVAPL ERQFRVKHYP RVFVSALTGQ GIEQLKKLMA QTVSEMQTDV QLYFPRSEEY KIFDLGREAQ ITRKETATEG TVCYTQLTPS LLNRWKEYLV K // ID A0A0B8WWQ7_9DELT Unreviewed; 475 AA. AC A0A0B8WWQ7; DT 01-APR-2015, integrated into UniProtKB/TrEMBL. DT 01-APR-2015, sequence version 1. DT 12-APR-2017, entry version 16. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=OM95_13880 {ECO:0000313|EMBL:KHD87532.1}; OS Bdellovibrio sp. ArHS. OC Bacteria; Proteobacteria; Deltaproteobacteria; Bdellovibrionales; OC Bdellovibrionaceae; Bdellovibrio. OX NCBI_TaxID=1569284 {ECO:0000313|EMBL:KHD87532.1, ECO:0000313|Proteomes:UP000031468}; RN [1] {ECO:0000313|EMBL:KHD87532.1, ECO:0000313|Proteomes:UP000031468} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Lal R., Sangwan N., Lambert C., Sharma A., Gupta V., Khurana P., RA Khurana J.P., Sockett R.E., Gilbert J.A.; RT "Predation in situ: Arsenic rich Himalayan hot spring metagenomics RT reveal genetically novel predator-prey genotypes."; RL Submitted (NOV-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KHD87532.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JTEV01000026; KHD87532.1; -; Genomic_DNA. DR Proteomes; UP000031468; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 2. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000031468}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}. FT DOMAIN 256 421 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 475 AA; 52425 MW; 06B1BF7A3B083D96 CRC64; MDILNKSKLK AVLVGVQLPR VSDEETRGSL AELSRLVTTL GYEVVGQTSQ KRNSTKSGTV LGDGKLKELA SWTGGTGVIG PLVVKKKHKA ALRFKNQDED EADEFAAEED DFAEVPEESE DLSLDADSDV PQEKAQVVIF DCDLSPSQLR NLESATGAQV LDRTGVIIEI FSRHARTKAA RLQVEIARLT YVAPRLRETS GGEDRGGGGI GGKGAGETSV ELDRRKIRDR IKELKHELAA ISQEHITRRS RRNQEISVAL VGYTNAGKSS LMRALTGSEV LVADKLFATL DTTVRVLYPE SRPKILISDT VGFIKKLPHD LVASFKSTLD EAANASLLLY VVDSSDPTFR SQLQVTRAVL DEVGASDIDS LLVLNKVDRL SAEEREKLQQ EYPEALFLSA HNKEDVANLR LRLIKHFETA MIDQELLIPY DVQGAIGEIR AKMRVLSENY DNRGVTLTIR AHIQDIEKIR TKFGI // ID A0A0B8YBY7_9SPHI Unreviewed; 400 AA. AC A0A0B8YBY7; DT 01-APR-2015, integrated into UniProtKB/TrEMBL. DT 01-APR-2015, sequence version 1. DT 07-JUN-2017, entry version 18. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:KHJ36721.1}; GN ORFNames=PBAC_31100 {ECO:0000313|EMBL:KHJ36721.1}; OS Pedobacter glucosidilyticus. OC Bacteria; Bacteroidetes; Sphingobacteriia; Sphingobacteriales; OC Sphingobacteriaceae; Pedobacter. OX NCBI_TaxID=1122941 {ECO:0000313|EMBL:KHJ36721.1, ECO:0000313|Proteomes:UP000031461}; RN [1] {ECO:0000313|EMBL:KHJ36721.1, ECO:0000313|Proteomes:UP000031461} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DD6b {ECO:0000313|EMBL:KHJ36721.1, RC ECO:0000313|Proteomes:UP000031461}; RA Poehlein A., Daniel R., Simeonova D.D.; RT "Draft genome sequence of Pedobacter glucosidilyticus DD6b."; RL Submitted (MAY-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KHJ36721.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JMTN01000045; KHJ36721.1; -; Genomic_DNA. DR RefSeq; WP_039454625.1; NZ_JMTN01000045.1. DR EnsemblBacteria; KHJ36721; KHJ36721; PBAC_31100. DR PATRIC; fig|1122941.3.peg.3115; -. DR Proteomes; UP000031461; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000031461}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000031461}. FT DOMAIN 204 389 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 172 206 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 400 AA; 46161 MW; 9E15D2D2E0C72C3E CRC64; MARKKFYDTA PKPERAVLVG IITPGTTELQ QKEYLEELAF LVDTAGGITE KVFTQRMQKP DRATFVGTGK LEEIQTYVKA EEIDIVVFDD ELSPMQLRNI ENELKVKVLD RSNLILDIFA RRAQTFQAKT QVELAQLQYL LPRLTRMWTH LERQKGGIGM RGPGETQIES DRRMINEKIS LLKERLKEID KQNETQRKNR KELVRVALVG YTNVGKSTIM NMLSKSEVFA ENKLFATLDT TVRKVVLENV PFLMSDTVGF IRKLPHHLIE CFKSTLDEVR EADILMHVVD ISHPNFEDHM QTVNETLKDL GAIDKETITV FNKIDAYNPI EVEQDWEVED EEKPTMGLAE FKNSWMAKNS SPAVFISATA KENVDELRDV IYHRVKAVNE KIYPYNNFLY // ID A0A0B9AX80_BRELN Unreviewed; 490 AA. AC A0A0B9AX80; DT 01-APR-2015, integrated into UniProtKB/TrEMBL. DT 01-APR-2015, sequence version 1. DT 07-JUN-2017, entry version 17. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=AE0388_0411 {ECO:0000313|EMBL:KHS53950.1}; OS Brevibacterium linens. OC Bacteria; Actinobacteria; Micrococcales; Brevibacteriaceae; OC Brevibacterium. OX NCBI_TaxID=1703 {ECO:0000313|EMBL:KHS53950.1, ECO:0000313|Proteomes:UP000031488}; RN [1] {ECO:0000313|EMBL:KHS53950.1, ECO:0000313|Proteomes:UP000031488} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=AE038-8 {ECO:0000313|EMBL:KHS53950.1, RC ECO:0000313|Proteomes:UP000031488}; RA Maizel D., Utturkar S.M., Brown S.D., Ferrero M., Rosen B.P.; RT "Draft Genome Sequence of Brevibacterium linens AE038-8."; RL Submitted (NOV-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KHS53950.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JTJZ01000012; KHS53950.1; -; Genomic_DNA. DR RefSeq; WP_039206650.1; NZ_JTJZ01000012.1. DR EnsemblBacteria; KHS53950; KHS53950; AE0388_0411. DR PATRIC; fig|1703.6.peg.298; -. DR Proteomes; UP000031488; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 2. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000031488}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000031488}. FT DOMAIN 265 431 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 490 AA; 53722 MW; CB86F9668036D192 CRC64; MTSEDKERRN AMLDRVLSRG AQALDDHDTT HEDDQFDLAE RAALTRVAGL STELEDITEV EYRQVRLERV VLAGIWNTTQ AEAENSIREL AALAETAGSE VLDALIQRRD KPDPGTYLGK GKAAELADIV ASVGADTVII DSELAPSQRR GLEDVIKVKV VDRVALILDI FAQHAKSREG KAQVELAQLE YLLPRLRGWG ESLSRQAGGR VAGGAGIGSR GPGETKIELD RRRIRARMSK LRREINAMAP SRETKRKNRA RHHVPSVAIV GYTNAGKSSL LNLLTNAEVM VQNALFATLD PTVRQAKTAD GIVFTYTDTV GFVRNLPHQL VEAFRSTLEE AAGSDLLLHV VDASHPDPHG QIQAVRDVLG DVETGDIPEL LVFNKSDIAE EAVITGLRAE YPDAQFVSAV SKEGIDDLID AIENRLPVPD IDMTVLIPYE RGDLVSKIYA LGTVEHESHG VEGTSLQVKV PAELVDELRE FQRPDLVIDE // ID A0A0C1EXJ8_9FLAO Unreviewed; 408 AA. AC A0A0C1EXJ8; DT 01-APR-2015, integrated into UniProtKB/TrEMBL. DT 01-APR-2015, sequence version 1. DT 07-JUN-2017, entry version 18. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=OA84_03345 {ECO:0000313|EMBL:KIA84558.1}; OS Chryseobacterium solincola. OC Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales; OC Flavobacteriaceae; Chryseobacterium. OX NCBI_TaxID=510955 {ECO:0000313|EMBL:KIA84558.1, ECO:0000313|Proteomes:UP000031275}; RN [1] {ECO:0000313|EMBL:KIA84558.1, ECO:0000313|Proteomes:UP000031275} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 22468 {ECO:0000313|EMBL:KIA84558.1, RC ECO:0000313|Proteomes:UP000031275}; RA Newman J.D.; RT "Kaistella solincola genome."; RL Submitted (OCT-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KIA84558.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JSYK01000002; KIA84558.1; -; Genomic_DNA. DR RefSeq; WP_039342244.1; NZ_JSYK01000002.1. DR EnsemblBacteria; KIA84558; KIA84558; OA84_03345. DR Proteomes; UP000031275; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000031275}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000031275}. FT DOMAIN 200 384 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 408 AA; 47438 MW; AFC35363E74A1BD2 CRC64; MLEKNDHQYE KAVLVGLITQ NQSEEKLTEY LDELEFLAYT AGASVDKRFT QRLTKPDSKT FIGSGKAQEI RDYVKENEIG TVIFDDELSP SQLKNLEKEI EVKILDRTNL ILDIFAQRAQ TSYARTQVEL AQYEYLLPRL TRMWTHLERQ QGGIGMRGPG ETEIETDRRI IRDRISLLKD KLKTIDRQMA TQRNNRGKMV RVALVGYTNV GKSTLMNALS KSDVFAEDKL FATLDTTVRK VVIGNLPFLL TDTVGFIRKL PTQLVESFKS TLDEVREADL LIHVVDISHE SFEDHINSVN QTLMEIEAHQ KPMIMVFNKI DAFAYEKKSD DDLSPETRKN ISLEEWMKTW MSKSKYPTVF ISALKKENFP ELKKMIYDEV LKIHISRFPY NDFLFQYFDE EEESTEEL // ID A0A0C1FGD7_9FLAO Unreviewed; 414 AA. AC A0A0C1FGD7; DT 01-APR-2015, integrated into UniProtKB/TrEMBL. DT 01-APR-2015, sequence version 1. DT 07-JUN-2017, entry version 17. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=OA85_05250 {ECO:0000313|EMBL:KIA87029.1}; OS Flavobacterium sp. AED. OC Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales; OC Flavobacteriaceae; Flavobacterium. OX NCBI_TaxID=1423323 {ECO:0000313|EMBL:KIA87029.1, ECO:0000313|Proteomes:UP000031403}; RN [1] {ECO:0000313|EMBL:KIA87029.1, ECO:0000313|Proteomes:UP000031403} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=AED {ECO:0000313|EMBL:KIA87029.1, RC ECO:0000313|Proteomes:UP000031403}; RA Gale A.N., Newman J.D.; RT "Flavobacterium sp. AED Genome."; RL Submitted (OCT-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KIA87029.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JSYM01000001; KIA87029.1; -; Genomic_DNA. DR RefSeq; WP_039108435.1; NZ_JSYM01000001.1. DR EnsemblBacteria; KIA87029; KIA87029; OA85_05250. DR Proteomes; UP000031403; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000031403}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000031403}. FT DOMAIN 201 387 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 414 AA; 47784 MW; BC3317059B90DDDD CRC64; MLEKEVINFE KTAIVGIVTQ NQSEEKLNEY LDELEFLTFT AGGQVVKRFS QKMERPNPKT FVGTGKIEEI HQFVKENDIS TLVFDDELSP SQQKNISKII EECKILDRTH LILDIFAQRA ETSYARTQVE LAQCQYLLPR LSGMWTHLER QKGGIGMRGP GETEIETDRR IVRDRIALLK EKIKTIDKQM GVQRGNRGAM VRVALVGYTN VGKSTLMNAV GKSDVFVENK LFATLDTTVR KVVIKNLPFL LSDTVGFIRK LPTQLVDSFK STLDEVREAD LLLHVVDISH PEFEDHIASV NQTLLDIKAN DKPVIMVFNK IDAYKPLTID EDDLMTEKTP RHFTLEEWKS TWMSRVGEQN ALFISATNKE NFEEFRERVY EAVRQIHITR FPYNKFLYPD YKDAVEKEEK EEID // ID A0A0C1FJZ4_9SPHI Unreviewed; 396 AA. AC A0A0C1FJZ4; DT 01-APR-2015, integrated into UniProtKB/TrEMBL. DT 01-APR-2015, sequence version 1. DT 07-JUN-2017, entry version 18. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=OC25_14445 {ECO:0000313|EMBL:KIA93232.1}; OS Pedobacter kyungheensis. OC Bacteria; Bacteroidetes; Sphingobacteriia; Sphingobacteriales; OC Sphingobacteriaceae; Pedobacter. OX NCBI_TaxID=1069985 {ECO:0000313|EMBL:KIA93232.1, ECO:0000313|Proteomes:UP000031246}; RN [1] {ECO:0000313|EMBL:KIA93232.1, ECO:0000313|Proteomes:UP000031246} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=KACC 16221 {ECO:0000313|EMBL:KIA93232.1, RC ECO:0000313|Proteomes:UP000031246}; RA Anderson B.M., Newman J.D.; RT "Pedobacter Kyungheensis."; RL Submitted (OCT-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KIA93232.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JSYN01000016; KIA93232.1; -; Genomic_DNA. DR RefSeq; WP_039477290.1; NZ_JSYN01000016.1. DR EnsemblBacteria; KIA93232; KIA93232; OC25_14445. DR Proteomes; UP000031246; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000031246}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000031246}. FT DOMAIN 204 384 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 396 AA; 44973 MW; 54594783F727030D CRC64; MGRQKFYDTA IVQERAILVG VVTPGEKEAQ TKEYLDELAF LVDTAGGKVE KVFTQKMLKP ERATFVGTGK LEEIKAYVKS EEIDTVVFDD ELSPSQLRNI DRELGVKVLD RSNLILDIFA NRAQTAQAKT QVELAQLQYV LPRLTGMWTH LERQKGGIGM RGPGETQIES DRRIILNKIS LLKERLRNID RQNETQRKNR GQLIRVALVG YTNVGKSTIM NMLSKSEVFA ENKLFATLDT TVRKVVIENL PFLLSDTVGF IRKLPHHLVE CFKSTLDEVR EADLLVHVVD VSHPNFEDQI NTVNETLKDI GAIDKDMILV FNKIDAYVSP EVEGGDDDGK LTLEDFKNSW MSHGKVPVLF ISATQRENIE EFKTLLYDKI KAAHVARYPY DSNLLY // ID A0A0C1G198_9FLAO Unreviewed; 411 AA. AC A0A0C1G198; DT 01-APR-2015, integrated into UniProtKB/TrEMBL. DT 01-APR-2015, sequence version 1. DT 07-JUN-2017, entry version 15. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=OA93_12380 {ECO:0000313|EMBL:KIA97773.1}; OS Flavobacterium sp. KMS. OC Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales; OC Flavobacteriaceae; Flavobacterium. OX NCBI_TaxID=1566023 {ECO:0000313|EMBL:KIA97773.1, ECO:0000313|Proteomes:UP000031466}; RN [1] {ECO:0000313|EMBL:KIA97773.1, ECO:0000313|Proteomes:UP000031466} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=KMS {ECO:0000313|EMBL:KIA97773.1, RC ECO:0000313|Proteomes:UP000031466}; RA Smith A.K., Newman J.; RT "Flavobacterium sp. KMS."; RL Submitted (OCT-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KIA97773.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JSYP01000011; KIA97773.1; -; Genomic_DNA. DR RefSeq; WP_039113593.1; NZ_JSYP01000011.1. DR EnsemblBacteria; KIA97773; KIA97773; OA93_12380. DR Proteomes; UP000031466; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000031466}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000031466}. FT DOMAIN 200 386 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 411 AA; 47519 MW; 266DB47B34A175AF CRC64; MLEKEVLNFE KTAIVGIVTQ NQSEEKLNEY LDELEFLTFT AGGEVIKRFT QKMERPNPKT FVGTGKIDEI NLFVKEHGIS TLVFDDELSP SQQKNISKII DCKILDRTHL ILDIFAQRAE TSYARTQVEL AQCQYLLPRL SGMWTHLERQ KGGIGMRGPG ETEIETDRRI VRDRIALLKE KIKTIDKQMG VQRSNRGAMV RVALVGYTNV GKSTLMNAVG KSDVFVENKL FATLDTTVRK VVIKNLPFLL SDTVGFIRKL PTQLVDSFKS TLDEVREADL LLHIVDISHA DFEDHIESVN QTLLDIKAND KPVIMVFNKI DAYKHLTIDE DDLITEKTPR HYTLEEWKTT WMHRLGEQNA LFISATNKEN FEEFRERVYE AVRQIHITRF PYNKFLYPDY KDAIEKEEDE D // ID A0A0C1ID93_9BACT Unreviewed; 393 AA. AC A0A0C1ID93; DT 01-APR-2015, integrated into UniProtKB/TrEMBL. DT 01-APR-2015, sequence version 1. DT 05-JUL-2017, entry version 20. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=HY58_00110 {ECO:0000313|EMBL:KIC92025.1}; OS Flavihumibacter sp. ZG627. OC Bacteria; Bacteroidetes; Chitinophagia; Chitinophagales; OC Chitinophagaceae; Flavihumibacter. OX NCBI_TaxID=1463156 {ECO:0000313|EMBL:KIC92025.1, ECO:0000313|Proteomes:UP000031400}; RN [1] {ECO:0000313|EMBL:KIC92025.1, ECO:0000313|Proteomes:UP000031400} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ZG627 {ECO:0000313|EMBL:KIC92025.1, RC ECO:0000313|Proteomes:UP000031400}; RA Zhou G., Li M., Wang G.; RT "Genome sequence of Flavihumibacter carbonis ZG627."; RL Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KIC92025.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JPHF01000001; KIC92025.1; -; Genomic_DNA. DR EnsemblBacteria; KIC92025; KIC92025; HY58_00110. DR Proteomes; UP000031400; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000031400}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000031400}. FT DOMAIN 195 377 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 393 AA; 45715 MW; 03C031D40F8E8002 CRC64; MLTDEKAVLV GVVQKDQNEQ QVKEYLEELA FLAETAGAVT HRKFMQKLSH PDSKTFVGKG KLEEIKEYII RHEINLVIFD DELTGSQILN IEKALGVKTI DRSDLILDIF ARRAQTAQAK TQVELAQYQY ILPRLKGMWK HLERQGGGIG SRGPGETEIE TDRRIVKEKI ALLRRRLAEI DKQSFTQRKD RGEFIRVALV GYTNVGKSTI MNLLAKSEVF AENKLFATLD TTTRKVVFDT TPFLLSDTVG FIRKLPHHLV ESFKSTLDEV READILLHVV DLSHPQYEDQ FNVVNKTLQE LKVTEKPMIT IFNKLDQYEK NTFDEWLEPD VRNQILEELR ERWENVTLGN CVFISALERR NLEGLRATIL NRVRKLYRER YPYKTEFFWS DEP // ID A0A0C1JBG8_9RHOB Unreviewed; 423 AA. AC A0A0C1JBG8; DT 01-APR-2015, integrated into UniProtKB/TrEMBL. DT 01-APR-2015, sequence version 1. DT 05-JUL-2017, entry version 18. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=RA28_16640 {ECO:0000313|EMBL:KIC44526.1}; OS Ruegeria sp. ANG-S4. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae; Ruegeria. OX NCBI_TaxID=1577904 {ECO:0000313|EMBL:KIC44526.1, ECO:0000313|Proteomes:UP000031326}; RN [1] {ECO:0000313|Proteomes:UP000031326} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ANG-S4 {ECO:0000313|Proteomes:UP000031326}; RX PubMed=25755651; DOI=10.3389/fmicb.2015.00123; RA Collins A.J., Fullmer M.S., Gogarten J.P., Nyholm S.V.; RT "Comparative genomics of Roseobacter clade bacteria isolated from the RT accessory nidamental gland of Euprymna scolopes."; RL Front. Microbiol. 6:123-123(2015). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KIC44526.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JWLK01000005; KIC44526.1; -; Genomic_DNA. DR RefSeq; WP_039531021.1; NZ_JWLK01000005.1. DR EnsemblBacteria; KIC44526; KIC44526; RA28_16640. DR Proteomes; UP000031326; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000031326}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000031326}. FT DOMAIN 203 372 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 423 AA; 47124 MW; 7D16DE2F11E18112 CRC64; MEHERMRTRA WVLHPEIKSD EQRRVSEPAL EEAVALAAAL PDLDVIGSEV VRLPRAQAGL LFGSGKIDEL GERFHENEVE LVLIDGPVTP VQQRNLEKAW KVKILDRTGL ILEIFSDRAR TREGVLQVEM AALSYQRTRL VRAWTHLERQ RGGLGFVGGP GETQIEADRR AIDEQLVRLR RQLQKVVKTR TLHRAARAKV PYPIVALVGY TNAGKSTLFN SLTGAEVMAK DMLFATLDPT MRRVVLPDGP EVILSDTVGF ISNLPTELVA AFRATLEEVL GADLIVHVRD ISHEESDAQA QDVEAILSSL GVEEDRPRLE VWNKIDLLTG EDREATLARA DRDASIFAIS AVTGEGVGPL LAEIATQLQG VRHETTLDLS FAEGDKRAWL FRQDVVRDEK QTDDGFRVTV LWTDKQAAQY SAL // ID A0A0C1NNP3_9PSEU Unreviewed; 504 AA. AC A0A0C1NNP3; DT 01-APR-2015, integrated into UniProtKB/TrEMBL. DT 01-APR-2015, sequence version 1. DT 07-JUN-2017, entry version 16. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=HQ32_02080 {ECO:0000313|EMBL:KID30577.1}; OS Prauserella sp. Am3. OC Bacteria; Actinobacteria; Pseudonocardiales; Pseudonocardiaceae; OC Prauserella. OX NCBI_TaxID=1515610 {ECO:0000313|EMBL:KID30577.1, ECO:0000313|Proteomes:UP000031395}; RN [1] {ECO:0000313|EMBL:KID30577.1, ECO:0000313|Proteomes:UP000031395} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Am3 {ECO:0000313|EMBL:KID30577.1, RC ECO:0000313|Proteomes:UP000031395}; RA Sarkar I., Sen A., Bose D., Ngom M., Ghazal S.M., Oshone R.T., RA Tisa L.S.; RT "Draft genome sequence of Prauserella sp. strain AM3."; RL Submitted (NOV-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KID30577.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JTJI01000005; KID30577.1; -; Genomic_DNA. DR EnsemblBacteria; KID30577; KID30577; HQ32_02080. DR PATRIC; fig|1515610.3.peg.2263; -. DR Proteomes; UP000031395; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000031395}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000031395}. FT DOMAIN 272 441 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 504 AA; 54028 MW; 95F2F90D86CC2B20 CRC64; MSNPDRGDVL TSQADLSADS FDEXVDEALG AMPGTSPSTG ELELEDRASL RRVAGLSTEL SDITEVEYRQ LRLERVVLVG VWTEGTAAQS EASLEELARL AETAGSTVLE GVVQRRNRPD PATYVGSGKV RELFDIVAST GADTVICDGE LSPGQLRQLE EKLKVKVIDR TALILDIFAQ HARSKEGKAQ VELAQLQYLI PRLRGWGAAL SRQAGGRAGS NGGVGLRGPG ETKLETDRRR ISKRVAKLRR EIAAMDTIRE TKRGRRVANA VPSVAIVGYT NAGKSSLLNA VTDAGVLVED ALFATLDPTT RRAVTPDGRA YTLTDTVGFV RHLPHQLVDA FRSTLDEAAD ADLLLHVVDG SDPAPEEQVQ AVREVLAEIG SKRAEALPPE LIVINKSDAS DEVSLARLRH LLPEAHVVSA HTGQGVPELV ATLSERLPRP DTVVDVLVPY ARGELVARAH ADGEVLSEEH TADGTRLCAR VHADLAGALE PYRMSAEAVG DPVV // ID A0A0C1PMN9_9LACO Unreviewed; 421 AA. AC A0A0C1PMN9; DT 01-APR-2015, integrated into UniProtKB/TrEMBL. DT 01-APR-2015, sequence version 1. DT 05-JUL-2017, entry version 18. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=LfDm3_0685 {ECO:0000313|EMBL:KID42017.1}; OS Lactobacillus fructivorans. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; OC Lactobacillus. OX NCBI_TaxID=1614 {ECO:0000313|EMBL:KID42017.1, ECO:0000313|Proteomes:UP000031397}; RN [1] {ECO:0000313|EMBL:KID42017.1, ECO:0000313|Proteomes:UP000031397} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DmCS_002 {ECO:0000313|EMBL:KID42017.1, RC ECO:0000313|Proteomes:UP000031397}; RA Newell P.D., Chaston J.M., Douglas A.E.; RT "Functional and comparative genomic analyses of the Drosophila gut RT microbiota identify candidate symbiosis factors."; RL Submitted (JUN-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KID42017.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JOJZ01000013; KID42017.1; -; Genomic_DNA. DR RefSeq; WP_039144118.1; NZ_JOJZ01000013.1. DR EnsemblBacteria; KID42017; KID42017; LfDm3_0685. DR PATRIC; fig|1614.7.peg.655; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR Proteomes; UP000031397; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000031397}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000031397}. FT DOMAIN 198 366 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 421 AA; 47429 MW; EF6477927BFFC15C CRC64; MNDNLTDVIT IGLDLNDANF QYSMEELNNL VTANNMQSVE TVTQKLDHPD PATYFGKGKV EFLEQLVKTT ETDVIVANDE LSPSQIRNLE KLTNAKIIDR TGLILEIFAN RARSREAKLQ VQLAKLNYQL PRLRTSASQR LDQQSAGGGL ANRGAGETQI ELNRRTIQHQ INHVRHELKE IDKSYDTQSK KRKQNDLKTI ALVGYTNAGK STIMNQLVKR FGENEGKEVT VKNMLFATLD TSVRKIELPN HKRFLATDTV GFVSQLPHQL IQAFKSTLAE AANADLLIQV VDYSDPNQEL MMQTTEATLK EIGVPDIPMI KVFNKADKSG ENYPVREGNN IIMSALDPSS INRLVDIISE NLFKDYIKKT YLVPFSNGQV VSDLNENETV YQTDYTDQGT VLRVELPETS AGKYKKYEVN E // ID A0A0C1QYK7_9CYAN Unreviewed; 559 AA. AC A0A0C1QYK7; DT 01-APR-2015, integrated into UniProtKB/TrEMBL. DT 01-APR-2015, sequence version 1. DT 12-APR-2017, entry version 18. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=DA73_0218955 {ECO:0000313|EMBL:KIE10604.1}; OS Tolypothrix bouteillei VB521301. OC Bacteria; Cyanobacteria; Nostocales; Tolypothrichaceae; Tolypothrix. OX NCBI_TaxID=1479485 {ECO:0000313|EMBL:KIE10604.1, ECO:0000313|Proteomes:UP000029738}; RN [1] {ECO:0000313|EMBL:KIE10604.1, ECO:0000313|Proteomes:UP000029738} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=VB521301 {ECO:0000313|EMBL:KIE10604.1, RC ECO:0000313|Proteomes:UP000029738}; RA Tripathy S.; RL Submitted (NOV-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KIE10604.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JHEG02000048; KIE10604.1; -; Genomic_DNA. DR EnsemblBacteria; KIE10604; KIE10604; DA73_0218955. DR Proteomes; UP000029738; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000029738}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000029738}. FT DOMAIN 387 557 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 346 380 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 559 AA; 61717 MW; 4DA81E0F154C7520 CRC64; MAAISTELNQ PVCTYLNRRG QVIRVGVGTP RQTQIPPLEL PRYGAERLSG IRCIATHLRS EPPNEAALTS MALQRLDALV MLNVTGTGFQ RRGGGATGYV KEAYLAHLAP QDARAFITSP AMRTAAPYLS SEGGNEEPKG QQSNPTPANW SASWSISPAL SLDMLTKQDF IELVEGLEEE FRREYVAQDV DTNHDRVLIV GVMTDELTLQ QFHDTLEELG RLVETAGGEV LQNMRQKRSR THPQTVVGEG KVQEIALTAQ TLGANLIVFD RDLSPAQIRN LESQIGVRVV DRTEVILDIF AQRAQSRAGK LQVELAQLEY MLPRLTGRGQ AMSRQGGGIG TRGPGETKLE TERRAIQRRI ARLQQEVNQL QAHRERLRQR RQHQEVPSIA IVGYTNAGKS TLLNALTNAE VYTADQLFAT LDPTTRRLVV PDGMNGDTQE ILVTDTVGFI HELPASLMDA FRATLEEVTE ADALLHLVDL SHPAWLSHIR SVRDILAQMP VTPGPALVVF NKIDQADSET LALAREEFPL AVFISASNRL GLETLRQRLG QLVQYATSC // ID A0A0C1R475_9CYAN Unreviewed; 568 AA. AC A0A0C1R475; DT 01-APR-2015, integrated into UniProtKB/TrEMBL. DT 01-APR-2015, sequence version 1. DT 07-JUN-2017, entry version 19. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=DA73_0218555 {ECO:0000313|EMBL:KIE10538.1}; OS Tolypothrix bouteillei VB521301. OC Bacteria; Cyanobacteria; Nostocales; Tolypothrichaceae; Tolypothrix. OX NCBI_TaxID=1479485 {ECO:0000313|EMBL:KIE10538.1, ECO:0000313|Proteomes:UP000029738}; RN [1] {ECO:0000313|EMBL:KIE10538.1, ECO:0000313|Proteomes:UP000029738} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=VB521301 {ECO:0000313|EMBL:KIE10538.1, RC ECO:0000313|Proteomes:UP000029738}; RA Tripathy S.; RL Submitted (NOV-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KIE10538.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JHEG02000048; KIE10538.1; -; Genomic_DNA. DR RefSeq; WP_038089588.1; NZ_JHEG02000048.1. DR EnsemblBacteria; KIE10538; KIE10538; DA73_0218555. DR Proteomes; UP000029738; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000029738}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000029738}. FT DOMAIN 392 562 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 351 388 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 568 AA; 63076 MW; 7DB2FC6F201A0070 CRC64; METIHGNTQS LKSSQIKKLQ QIYEQREPSH SLITPEFAQA VAAIATEIHQ PICSYINRRG QVIRVAVGTP SQTQIPPEQR PRSDAERLSG LRCIATQFKS EPPDEASLIA MVRQRLDALV VLTLADGKDG KRGKDNTDLV KKAFLAHIVP NEEKPWEVIS SLSSDNLIEQ DFDDLVDEWE REISESAVGM PFQDILSDTD KVLLVGLKTD DISQQRFEDG LQELVRLVET AGGTVGDTVQ QKRSRPHPQT VVGQGKVEEI ALSAQKIGAN LIVFDRDISP SQARNLENEI GIRVVDRTEV ILDIFAQRAQ SQAGKLQVEL AQLEYMLPRL RGQGREMSRL GGGIGTRGPG ETKLETERRA IQRRIAQLQQ EVNQLQAHRA RIRQQRQKQE IPAVALVGYT NAGKSTLLNV LTHAEVYVAD KLFATLDPTT RKLVIVDPET QERRTILLTD TVGFIHELPP PLVDAFRATL EEVTEADILL HVVDLSHPAW ENHIASVEAV LAEMPAISGP TLIAFNKVDG VNSETLALAK EKYPEALFIS ATHQLGLDTL RQRLLQAIDR QVLQVPSS // ID A0A0C1RG80_9ACTN Unreviewed; 417 AA. AC A0A0C1RG80; DT 01-APR-2015, integrated into UniProtKB/TrEMBL. DT 01-APR-2015, sequence version 1. DT 10-MAY-2017, entry version 17. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=MB54_04045 {ECO:0000313|EMBL:KIE49621.1}; OS marine actinobacterium MedAcidi-G2B. OC Bacteria; Actinobacteria. OX NCBI_TaxID=1550401 {ECO:0000313|EMBL:KIE49621.1, ECO:0000313|Proteomes:UP000031352}; RN [1] {ECO:0000313|EMBL:KIE49621.1, ECO:0000313|Proteomes:UP000031352} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mizuno C.M., Rodriguez-Valera F., Ghai R.; RT "Novel reconstructed genomes of marine planktonic Acidimicrobiales."; RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KIE49621.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JUEO01000006; KIE49621.1; -; Genomic_DNA. DR Proteomes; UP000031352; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000031352}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000031352}. FT DOMAIN 199 363 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 158 192 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 417 AA; 46235 MW; C70DF6EA854AD2DA CRC64; MDRSFRERIV LAAVTLEKVE SEETEASLQE LALLVDTAGA DPVAQIVQNR QVPDRTTYVG RGKAEEIRQV SDSLDADTVV FDNELTPAQQ GNLEKILKRS ALDRTAVILD IFAQNASSPE GKTQVELAQL RYLLPRLRRS GHAFSQQGGG IGTRGPGETQ LEVDRRRLMR RISKLESNLK QLKKNRATQS KSRKRTNNHA VTIVGYTNAG KSTLLNSLTN AGVLVEDRLF ATLDATTRRL QLPGGEKVYL TDTVGFVRKL PHQLVEAFTS TLDVVIDADL LIHVVDSSDP DPKGSIEAVH SVLREIGADG ITQIYAFNKA DLDQSAAQRL VRQEQDAVAV SAVTGEGLED LLKKIGEHLR ELSQVIELFI PYDRGDVLAK THREGQVLEE VPEEKGWKVF ARLEKSSVGR LEEFMRE // ID A0A0C1SKF6_9ACTN Unreviewed; 449 AA. AC A0A0C1SKF6; DT 01-APR-2015, integrated into UniProtKB/TrEMBL. DT 01-APR-2015, sequence version 1. DT 07-JUN-2017, entry version 18. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=PL81_22635 {ECO:0000313|EMBL:KIF03725.1}; OS Streptomyces sp. RSD-27. OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae; OC Streptomyces. OX NCBI_TaxID=1571774 {ECO:0000313|EMBL:KIF03725.1, ECO:0000313|Proteomes:UP000031573}; RN [1] {ECO:0000313|EMBL:KIF03725.1, ECO:0000313|Proteomes:UP000031573} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=RSD-27 {ECO:0000313|EMBL:KIF03725.1, RC ECO:0000313|Proteomes:UP000031573}; RA Debnath R., Saikia R.; RT "Streptomyces sp. RSD-27 isolated from Se La Pass, Arunachal Pradesh, RT India."; RL Submitted (DEC-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KIF03725.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JWZS01001299; KIF03725.1; -; Genomic_DNA. DR RefSeq; WP_042814748.1; NZ_JWZS01001299.1. DR EnsemblBacteria; KIF03725; KIF03725; PL81_22635. DR Proteomes; UP000031573; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000313|EMBL:KIF03725.1}; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000031573}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900, KW ECO:0000313|EMBL:KIF03725.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000031573}. FT DOMAIN 231 396 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 197 224 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 449 AA; 48101 MW; A7C2094AFB17DB98 CRC64; MDAREETGLR HVASLSTELR DVVEVEQRQV RLERVVLVGV WTSGTVAEAE SSLAELAALA ETAGALVLDG VIQRRDKPDP ATYIGSGKAK ELRDIVLETG ADTVVCDGEL SPSQLVRLEE FVQVKVVDRT ALILDIFAQR ATSREGKAQV ALAQMQYMLP RLRGWGASLS RQMGGGGAGG GGMATRGPGE TKIETDRRRL RDKMAKMRRD IDEMKTARDL KRQERRRNKV PSVAIAGYTN AGKSSLLNRL TGAEVHVQNA LFATLDPTVR RSETPAGRAY TLADTVGFVR HLPHQLVDAF RSTLEEVAEA DLILHVVDGS HPDPEAQIEA VRAVIGEVGG AGVPEVVVVN KADTADPQTL ARLLEAEPGA VAVSARTGEG VAALLSRIEA ELPHPETEIE VLIPYSEGHL VARIHASGEI LSESHGETGT LLKANVDAAL AAELSDYAA // ID A0A0C1U4C2_9CLOT Unreviewed; 598 AA. AC A0A0C1U4C2; DT 01-APR-2015, integrated into UniProtKB/TrEMBL. DT 01-APR-2015, sequence version 1. DT 07-JUN-2017, entry version 18. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:KIE47639.1}; GN ORFNames=U732_2948 {ECO:0000313|EMBL:KIE47639.1}; OS Clostridium argentinense CDC 2741. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=1418104 {ECO:0000313|EMBL:KIE47639.1, ECO:0000313|Proteomes:UP000031366}; RN [1] {ECO:0000313|EMBL:KIE47639.1, ECO:0000313|Proteomes:UP000031366} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CDC 2741 {ECO:0000313|EMBL:KIE47639.1, RC ECO:0000313|Proteomes:UP000031366}; RX PubMed=25489752; DOI=10.1016/j.meegid.2014.12.002; RA Smith T.J., Hill K.K., Xie G., Foley B.T., Williamson C.H., RA Foster J.T., Johnson S.L., Chertkov O., Teshima H., Gibbons H.S., RA Johnsky L.A., Karavis M.A., Smith L.A.; RT "Genomic sequences of six botulinum neurotoxin-producing strains RT representing three clostridial species illustrate the mobility and RT diversity of botulinum neurotoxin genes."; RL Infect. Genet. Evol. 30:102-113(2014). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KIE47639.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AYSO01000014; KIE47639.1; -; Genomic_DNA. DR RefSeq; WP_039631286.1; NZ_AYSO01000014.1. DR EnsemblBacteria; KIE47639; KIE47639; U732_2948. DR Proteomes; UP000031366; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000031366}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000031366}. FT DOMAIN 366 543 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 598 AA; 67344 MW; 83677F59537B2188 CRC64; MINGNIESVK KSILNRLDTI YEMKIPKDMI FTEELANLLN EVTLDLEREI SVAIDRKGNI IGVAIGDSST VDIPIIDVKE GKLSGVRVIH THPNGNPKLS GLDISALIKL KLDAMVAIGV NNEGNLKYHI GFCDINNNIL VEEELEFKTT EDVMQFKFLD KVKHIESLIK ENDVIEDNTE RAILVGTEDE ESLEELGELT KACEAIPVYS ILQKRSKSKI DPAYYIGRGK VEEIALVRQS LRANVVIFDE ELSGAQVRNL EGALGVKVID RTTLILEIFA RRAKTKEGKI QVELSQLKYR LSRLGGLGTV LSRTGGGIGT RGPGEKKLET DKRHIRETIY DLTKELERIK HVRNTQREKR NKDSISKISL VGYTNAGKST LRNTLCDIYP LKSSNIKEKV FEADMLFATL DTTTRGILLP DNRVATITDT VGFIRKLPHE LVEAFKSTLE EVIYSDLLLH VVDSSSDSAD KQIEVVEEVL KELDACDKPT ILVLNKTDKA SEEKLQDLRE KYKNYKIIEV SAKERINLEK LLNESTELLP YKLKAFKVLI PYADSSTAAY LHRNGKVDSE EYVEEGTVMM VQGDEEVYNK CKDYIIEE // ID A0A0C1UAX0_9CLOT Unreviewed; 605 AA. AC A0A0C1UAX0; DT 01-APR-2015, integrated into UniProtKB/TrEMBL. DT 01-APR-2015, sequence version 1. DT 07-JUN-2017, entry version 18. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:KIE44730.1}; GN ORFNames=U732_196 {ECO:0000313|EMBL:KIE44730.1}; OS Clostridium argentinense CDC 2741. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=1418104 {ECO:0000313|EMBL:KIE44730.1, ECO:0000313|Proteomes:UP000031366}; RN [1] {ECO:0000313|EMBL:KIE44730.1, ECO:0000313|Proteomes:UP000031366} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CDC 2741 {ECO:0000313|EMBL:KIE44730.1, RC ECO:0000313|Proteomes:UP000031366}; RX PubMed=25489752; DOI=10.1016/j.meegid.2014.12.002; RA Smith T.J., Hill K.K., Xie G., Foley B.T., Williamson C.H., RA Foster J.T., Johnson S.L., Chertkov O., Teshima H., Gibbons H.S., RA Johnsky L.A., Karavis M.A., Smith L.A.; RT "Genomic sequences of six botulinum neurotoxin-producing strains RT representing three clostridial species illustrate the mobility and RT diversity of botulinum neurotoxin genes."; RL Infect. Genet. Evol. 30:102-113(2014). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KIE44730.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AYSO01000020; KIE44730.1; -; Genomic_DNA. DR RefSeq; WP_039635910.1; NZ_AYSO01000020.1. DR EnsemblBacteria; KIE44730; KIE44730; U732_196. DR Proteomes; UP000031366; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000031366}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000031366}. FT DOMAIN 371 547 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 330 357 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 605 AA; 68083 MW; 78F8D20B6AA12504 CRC64; MITGNINGIK KIILEKLEAL YELAIDSHSI FSYELVEEIN EISRTIKKEI CVVINRRGKI TAISVGKINN VEIPYINVAD KKLSGFRVIH THPNGESKLS SMDISALVNL KLDAIVAIGV KENIEDTNIN IGFCDVYNNS LTFKELENLS LEDSLQLNFK DNIDYIDKII GDVVQYENDV ERAILVGTDS EESLEELSNL AKACNVIPIY KIFQKKNKVH SAYYAGQGKV QQIAHLRQLK NANVIIFDDE LSGSQIRNLK EAIKCKVIDR TTLILDIFAR RAKSKESILQ VELTMLTHKL SRLRNANANL ARIKGGVGVK GGVGSKGPGE RKLETDKRHI ESRIEEIKNE LSKIINQRAI QKVKRSKNNI SKVAIVGYTN AGKSTLRNKI CKIAASNIIN KKDVLEADML FATLDTTVRA ITLSDNRKTT LSDTVGFISK LPHELVEAFK STLEEVIEAD LLLHVVDGSN EEAIKQIKSV NMVLNELNAK DKNTIIVLNK IDKASDKNLK ELKDFLKDEK IIEISAIEEI NLNDLLHMIG KEIPIKLVEK DFIIPYSEQE LVSMLHENSN IINEDYIEEG TRIKALVHEE IYKRCADFEV KTFIN // ID A0A0C1ULT5_9ACTN Unreviewed; 475 AA. AC A0A0C1ULT5; DT 01-APR-2015, integrated into UniProtKB/TrEMBL. DT 01-APR-2015, sequence version 1. DT 12-APR-2017, entry version 16. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=MB55_06900 {ECO:0000313|EMBL:KIE52818.1}; OS marine actinobacterium MedAcidi-G3. OC Bacteria; Actinobacteria. OX NCBI_TaxID=1550402 {ECO:0000313|EMBL:KIE52818.1, ECO:0000313|Proteomes:UP000031370}; RN [1] {ECO:0000313|EMBL:KIE52818.1, ECO:0000313|Proteomes:UP000031370} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mizuno C.M., Rodriguez-Valera F., Ghai R.; RT "Novel reconstructed genomes of marine planktonic Acidimicrobiales."; RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KIE52818.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JUEP01000011; KIE52818.1; -; Genomic_DNA. DR Proteomes; UP000031370; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000031370}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000031370}. FT DOMAIN 249 414 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 208 242 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 475 AA; 52222 MW; 450F7E38E996F5B1 CRC64; MRRERANADR TRTIRRSHRS FCMTKSMDNQ PDEATHRGGF GEFAGEATGL IDRSFREQIV LVGVQFPGAS DDEVDANLNE LAQLVDTAGA DPVDRVIQKR ETPDPATYVG KGKAAEIQAT SEGLDADTVV FDDELSPGQQ FNLEKILKRT ALDRTAVILD IFAQNATTLE GKTQVELAQL RYHLPRLRGR GNQLSQQAGG IGTRGPGETQ LEVDRRRIQR RLAKLEKDLS GLRRTRRNQR KSRRRSRFHT VAIVGYTNAG KSTLLNQLTG AEVLVEDRLF ATLDATTRRL QLPGGETVLM TDTVGFIQKL PTGLVEAFKS TLEEVAEADL LLHVVDGAGP DPEGQMAAVR AVLREIGAGD VPELIAFNKA DQVKAGGLDH LLLGHEGSIA FSARSGEGLE ILLSSIGDRL RSLTEVVELV IPWSRGDVVA AVHREGEVLM EQHEEGGTRI RARLDEVSKD LLAEFIDENM SEETR // ID A0A0C1URX8_9CYAN Unreviewed; 561 AA. AC A0A0C1URX8; DT 01-APR-2015, integrated into UniProtKB/TrEMBL. DT 01-APR-2015, sequence version 1. DT 05-JUL-2017, entry version 20. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=QQ91_28205 {ECO:0000313|EMBL:KIF40528.1}; OS Lyngbya confervoides BDU141951. OC Bacteria; Cyanobacteria; Oscillatoriophycideae; Oscillatoriales; OC Oscillatoriaceae; Lyngbya. OX NCBI_TaxID=1574623 {ECO:0000313|EMBL:KIF40528.1, ECO:0000313|Proteomes:UP000031561}; RN [1] {ECO:0000313|EMBL:KIF40528.1, ECO:0000313|Proteomes:UP000031561} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BDU141951 {ECO:0000313|EMBL:KIF40528.1, RC ECO:0000313|Proteomes:UP000031561}; RA Malar M.C., Sen D., Tripathy S.; RT "Draft genome sequence of Lyngbya confervoides BDU141951."; RL Submitted (NOV-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KIF40528.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JTHE01000274; KIF40528.1; -; Genomic_DNA. DR EnsemblBacteria; KIF40528; KIF40528; QQ91_28205. DR Proteomes; UP000031561; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000031561}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000031561}. FT DOMAIN 389 559 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 348 385 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 561 AA; 62348 MW; 6B0F6D0E3CAD384B CRC64; METIHGNLRG LKPNQLKQLQ RLYHQRLPGD RVTTPEFAQR LAAISTDLGQ PLCVYLNRRG QVIRVGVGTP QQTRIPPVEL PRYGAERLCG IRCIATRLKH EPPSTSDLTA MAMQRLDSLV AVTLSGDGFE RRGGGATGYV DEVYLAHLVP HPEARWTVSD PMSLDTLAQQ DFVSLTDALE EEFRRVFVAQ QVDADHDRVI VVGLMTGNVS KTQFRYGLME VRRLVETAGG EVLATLHQRR DRPHPQTVLG AGKIQEIALE AQTLGATLVV FDRDLSPAQV RNLEAQMGVR VVDRTEVILD IFAQRARTGA GKLQVELAQL EYQLPRLTGR GQAMSRLGGG IGTRGPGETK LETERRAIQR RISRLQREVN QLQAHRDRLR QRRQQSDIPS IAVVGYTNAG KSTLLNALTN SEIYAADQLF ATLDPTTRRL SVLDSDTQEQ TQLVLTDTVG FIRDLPESLV DAFRATLEEV TEADALLHVV DLSHPAWQSQ IRSVMRILGE MPVTPGPILL AFNKLDRVDS EALAIAKEEF PNAVFVSAQD RIGLETLRKQ LIELASYALC Q // ID A0A0C1VAT0_9ACTN Unreviewed; 501 AA. AC A0A0C1VAT0; DT 01-APR-2015, integrated into UniProtKB/TrEMBL. DT 01-APR-2015, sequence version 1. DT 07-JUN-2017, entry version 18. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=PL81_38155 {ECO:0000313|EMBL:KIF00972.1}; OS Streptomyces sp. RSD-27. OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae; OC Streptomyces. OX NCBI_TaxID=1571774 {ECO:0000313|EMBL:KIF00972.1, ECO:0000313|Proteomes:UP000031573}; RN [1] {ECO:0000313|EMBL:KIF00972.1, ECO:0000313|Proteomes:UP000031573} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=RSD-27 {ECO:0000313|EMBL:KIF00972.1, RC ECO:0000313|Proteomes:UP000031573}; RA Debnath R., Saikia R.; RT "Streptomyces sp. RSD-27 isolated from Se La Pass, Arunachal Pradesh, RT India."; RL Submitted (DEC-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KIF00972.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JWZS01002175; KIF00972.1; -; Genomic_DNA. DR RefSeq; WP_042819477.1; NZ_JWZS01002175.1. DR EnsemblBacteria; KIF00972; KIF00972; PL81_38155. DR Proteomes; UP000031573; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 2. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000313|EMBL:KIF00972.1}; KW Complete proteome {ECO:0000313|Proteomes:UP000031573}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900, KW ECO:0000313|EMBL:KIF00972.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000031573}. FT DOMAIN 280 445 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 501 AA; 54697 MW; 7FCD000DB9D52020 CRC64; MTSSSSPSQD PRDAQNVRDP QRFTESLRAD ALMEEDVAWS HEIDGDRDGD QFDRSERAAL RRVAGLSTEL EDVTEVEYRQ LRLERVVLVG VWTSGTVGDA ENSLAELAAL AETAGALVLD GVIQRRDKPD PATFIGSGKA RELRDIVLES GADTVVCDGE LSPGQLIALE DVVKVKVVDR TALILDIFAQ HAKSREGKAQ VALAQMQYML PRLRGWGQSL SRQMGGGGGG GMATRGPGET KIETDRRRIR EKMAKMRREI AEMKTGRDIK RQERRRNKVP SVAIAGYTNA GKSSLLNRLT GAGVLVENAL FATLDPTVRR AETPSGRVYT LADTVGFVRH LPHHLVEAFR STMEEVGDSD LILHIVDGSH PAPEEQLAAV REVIREVGAV NVPEIVVVNK ADAADPLVLQ RLLRIERHSI AVSARTGQGI EKLLALIDSE LPRPAVEVEA LVPYTRGALI ARAHAEGEVI SEEHTPEGTL LKARVHRELA AELTPYVPAK Q // ID A0A0C1WYG1_9ACTN Unreviewed; 505 AA. AC A0A0C1WYG1; DT 01-APR-2015, integrated into UniProtKB/TrEMBL. DT 01-APR-2015, sequence version 1. DT 07-JUN-2017, entry version 18. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=HY68_01040 {ECO:0000313|EMBL:KIF67528.1}; OS Streptomyces sp. AcH 505. OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae; OC Streptomyces. OX NCBI_TaxID=352211 {ECO:0000313|EMBL:KIF67528.1, ECO:0000313|Proteomes:UP000031567}; RN [1] {ECO:0000313|EMBL:KIF67528.1, ECO:0000313|Proteomes:UP000031567} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=AcH 505 {ECO:0000313|EMBL:KIF67528.1, RC ECO:0000313|Proteomes:UP000031567}; RA Tarkka M.T., Feldhahn L., Buscot F., Wubet T.; RT "Genome sequence of the mycorrhiza helper bacterium Streptomyces."; RL Submitted (NOV-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KIF67528.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JTIY01000001; KIF67528.1; -; Genomic_DNA. DR RefSeq; WP_041983474.1; NZ_JTIY01000001.1. DR EnsemblBacteria; KIF67528; KIF67528; HY68_01040. DR Proteomes; UP000031567; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 2. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000313|EMBL:KIF67528.1}; KW Complete proteome {ECO:0000313|Proteomes:UP000031567}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900, KW ECO:0000313|EMBL:KIF67528.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000031567}. FT DOMAIN 280 445 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 505 AA; 54670 MW; 141B1D5BC41E055A CRC64; MTSSSSPSQD AQSFADASNT DPRTDSLRAN ALMEEDVAWS HEIDGERDGD QFDRSDRAAL RRVAGLSTEL EDVTEVEYRQ LRLERVVLVG VWTSGTAQDA ENSLAELAAL AETAGALVLD GVVQRRDKPD AATYIGSGKA NELRDIVLET GADTVVCDGE LSPGQLIHLE DVVKVKVVDR TALILDIFAQ HAKSREGKAQ VALAQMQYML PRLRGWGQSL SRQMGGGGGG GMATRGPGET KIETDRRRIR EKMAKMRREI AEMKTGREIK RQERRRHKVP SVAIAGYTNA GKSSLLNRLT GAGVLVENAL FATLDPTVRR AETPGGRLYT LTDTVGFVRH LPHHLVEAFR STMEEVGDSD LILHVVDGSH PAPEEQLAAV REVVRDVGAV NVREIVVINK ADAADPVVLQ RLLSAERHAI AVSARTGQGI AELLALLDME LPRPQVEVEV LVPYTHGGLV SRIHAEGEVL SEEHTPEGTQ LKAQVHEELA AALAPYAPVA VPAAT // ID A0A0C1XM94_9CYAN Unreviewed; 532 AA. AC A0A0C1XM94; DT 01-APR-2015, integrated into UniProtKB/TrEMBL. DT 01-APR-2015, sequence version 1. DT 07-JUN-2017, entry version 18. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=PI95_33720 {ECO:0000313|EMBL:KIF33084.1}; OS Hassallia byssoidea VB512170. OC Bacteria; Cyanobacteria; Nostocales; Tolypothrichaceae; Hassallia. OX NCBI_TaxID=1304833 {ECO:0000313|EMBL:KIF33084.1, ECO:0000313|Proteomes:UP000031549}; RN [1] {ECO:0000313|EMBL:KIF33084.1, ECO:0000313|Proteomes:UP000031549} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=VB512170 {ECO:0000313|EMBL:KIF33084.1, RC ECO:0000313|Proteomes:UP000031549}; RA Singh D., Malar M.C., Panda A., Sen D., Das A., Bhattacharyya S., RA Adhikary S.P., Tripathy S.; RT "The genome sequences of Hassallia byssoidea."; RL Submitted (NOV-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KIF33084.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JTCM01000037; KIF33084.1; -; Genomic_DNA. DR EnsemblBacteria; KIF33084; KIF33084; PI95_33720. DR Proteomes; UP000031549; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000031549}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000031549}. FT DOMAIN 359 529 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 332 355 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 532 AA; 58218 MW; 9E9ADBA412D5E8EE CRC64; MNQAVCAYLN RRGQVIRVGV GSPRQTQIPL LELPRYGAER LSGIRCISTH LKSEPPNEAA LTSMALQRLD ALVVLNITGT GFTKRGGGAT GYVKEAYLAH LTAQSRVAIA SPATLTASSN IPSPSWNISP PLSLDVLTNQ DFLDLVEALE ADFRREFVAQ EVDADRDSVL IVGVFTDDTT PQQFQDTLAE LARLVDTAGG DVLQTVQQKR SRIHPQTVVG EGKVQEIALT AQTIGANLVV FDRDLSPAQV RNLELQIGVR VVDRTEVILD IFAQRAQSRA GKLQVELAQL EYMLPRLTGR GQAMSRLGGG IGTRGPGETK LETERRGIGR RISRLQQEVN QLQAHRSRLR QKRQHREVPS VALVGYTNAG KSTLLNALTN AEIYTADQLF ATLDPTTRRL IIPHADTGET QEILLTDTVG FIHELPASLM DAFRATLEEV TEADALLHLV DLSHPAWLSH IRAVREILAA MPVTPGPALV AFNKIDQVDS ETLALAQEEF PLAVFISASD RLGLETLRQR LALLIEYATS SR // ID A0A0C1XZ71_9CYAN Unreviewed; 574 AA. AC A0A0C1XZ71; DT 01-APR-2015, integrated into UniProtKB/TrEMBL. DT 01-APR-2015, sequence version 1. DT 12-APR-2017, entry version 18. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=PI95_10565 {ECO:0000313|EMBL:KIF37259.1}; OS Hassallia byssoidea VB512170. OC Bacteria; Cyanobacteria; Nostocales; Tolypothrichaceae; Hassallia. OX NCBI_TaxID=1304833 {ECO:0000313|EMBL:KIF37259.1, ECO:0000313|Proteomes:UP000031549}; RN [1] {ECO:0000313|EMBL:KIF37259.1, ECO:0000313|Proteomes:UP000031549} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=VB512170 {ECO:0000313|EMBL:KIF37259.1, RC ECO:0000313|Proteomes:UP000031549}; RA Singh D., Malar M.C., Panda A., Sen D., Das A., Bhattacharyya S., RA Adhikary S.P., Tripathy S.; RT "The genome sequences of Hassallia byssoidea."; RL Submitted (NOV-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KIF37259.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JTCM01000011; KIF37259.1; -; Genomic_DNA. DR EnsemblBacteria; KIF37259; KIF37259; PI95_10565. DR Proteomes; UP000031549; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000031549}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000031549}. FT DOMAIN 392 562 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 351 388 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 574 AA; 64209 MW; 7D2402A2D406A805 CRC64; MQNIYGNIQG IKSSQIKLLQ RFYEQRQPGD RFITLEFAQA LGEISTEIHQ PICCYINRRG QVIRIAVGTP SQTQIPPEEL PRHSAERLSG IHCVATQFKS DPPDEAALIA MARQRLDALV VLILVGGEGG RHKKAANGNV KEAFLANLVP NAEKPWEISP PLSLDDLIEQ DFDDLVDEWE REISENSDRT LFPDIVSDTD KVLLVGLKTD DIPQQRFEDG LQELVRLVET AGGIVADTVE QKRSRPHPQT VVGKGKVEEI AFQAQKVGAN LIVFDRDISA SQARNLENEI GIRVIDRTEV ILDIFAQRAQ SQAGKLQVEL AQLEYMLPRL RGQGREMSRL GAGIGTRGPG ETKLETERRV IQRRIAQLQQ EVNQLQAHRD RIRQQRQKQE IPVLALVGYT NAGKSTLLNV LTNAEVYTAD QLFATLDPTT RKLVITNPET QERRTILLTD TVGFIHELPP ALIDAFRATL EEVVEANVLL HLVDLSHPAW ESHIASVQEI LAEMPTIPEK SLIVFNKIDS VDSETLKKAQ QEYPSAVFIS ATKRLGLETL KERSLQLIDE TLAKPELQNA VTQS // ID A0A0C1YWE5_9BURK Unreviewed; 422 AA. AC A0A0C1YWE5; DT 01-APR-2015, integrated into UniProtKB/TrEMBL. DT 01-APR-2015, sequence version 1. DT 07-JUN-2017, entry version 18. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=BurMR1_3150 {ECO:0000313|EMBL:KIG09114.1}; OS Burkholderia sp. MR1. OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Burkholderia. OX NCBI_TaxID=870478 {ECO:0000313|EMBL:KIG09114.1, ECO:0000313|Proteomes:UP000031560}; RN [1] {ECO:0000313|EMBL:KIG09114.1, ECO:0000313|Proteomes:UP000031560} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MR1 {ECO:0000313|EMBL:KIG09114.1, RC ECO:0000313|Proteomes:UP000031560}; RA Pawitwar S., Utturkar S.M., Brown S.D., Yoshinaga M., Rosen B.P.; RT "Draft Genome Sequence of Burkholderia sp. MR1."; RL Submitted (DEC-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KIG09114.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JWHM01000017; KIG09114.1; -; Genomic_DNA. DR RefSeq; WP_040050130.1; NZ_JWHM01000017.1. DR EnsemblBacteria; KIG09114; KIG09114; BurMR1_3150. DR PATRIC; fig|870478.3.peg.1837; -. DR Proteomes; UP000031560; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000031560}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000031560}. FT DOMAIN 191 362 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 157 184 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 422 AA; 46176 MW; 1446D73701A79A9D CRC64; MINAALVGID FGKIDFEASL EELSLLAESA GAHPAVTLTG RRSSPDAKMF IGSGKVEELR LSCEANDVEL VIFNHALAPA QQRNLEMALN RRVVDRTSLI LDIFAQRARS HEGKLQVELA QLQYLSTRLI RAWTHLERQK GGIGLRGPGE TQLETDRRLI GERIKALKTR LAKLRRQHGT QRRQRQRNQT MSVSLVGYTN AGKSTLFNAL TKAQAYAANQ LFATLDTTSR RVFLGEEAGH VVVSDTVGFI RELPHQLVAA FRATLEETIH ADLLLHVVDA SSAVRLDQID QVNEVLRSIG ADGIRQVLVF NKIDAVPELA ARGDAVERDE YGNISRVFLS ARTGQGLDAL RAAIAEIATA ESGESEESMP SVFAETGEPA QTSEATQSTQ SGPTETHDAN AQPEDHRPAG EREGHEVPEH GH // ID A0A0C1ZUV3_9DELT Unreviewed; 458 AA. AC A0A0C1ZUV3; DT 01-APR-2015, integrated into UniProtKB/TrEMBL. DT 01-APR-2015, sequence version 1. DT 12-APR-2017, entry version 15. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=DB30_06296 {ECO:0000313|EMBL:KIG14843.1}; OS Enhygromyxa salina. OC Bacteria; Proteobacteria; Deltaproteobacteria; Myxococcales; OC Enhygromyxa. OX NCBI_TaxID=215803 {ECO:0000313|EMBL:KIG14843.1, ECO:0000313|Proteomes:UP000031599}; RN [1] {ECO:0000313|EMBL:KIG14843.1, ECO:0000313|Proteomes:UP000031599} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 15201 {ECO:0000313|EMBL:KIG14843.1, RC ECO:0000313|Proteomes:UP000031599}; RA Sharma G., Subramanian S.; RT "Genome assembly of Enhygromyxa salina DSM 15201."; RL Submitted (DEC-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KIG14843.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JMCC02000065; KIG14843.1; -; Genomic_DNA. DR EnsemblBacteria; KIG14843; KIG14843; DB30_06296. DR Proteomes; UP000031599; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000031599}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000031599}. FT DOMAIN 234 401 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 202 229 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 458 AA; 50048 MW; 66FE3FB25AA41CB2 CRC64; MKFHSKPIEE HTEVPLADDG RWEQLVAHWA QLDAAPGGPV HGKNACYVVS VGVWEDLAQE RAQLAEILAL VRAQGDRVVG YESYQRGRPD PRTYLGTGTS EAIAARASAA GATLLVVDAE LSPSQTRNLE DATGLSVSDR EGVILNVFLI HAKSRKARIQ VEIAQLEYLR PRIRGIGLDM DQQAGGMMAA RGPGETASEL LARQLDGRLA ELRKQNAKLE RAEQTQRKGR ESCQRVALVG YTNAGKTSLM NGLTAAELSA KDMPFETLDT TSRSLTRHGG DVVLSDTVGF IRRLPERLLA SFETTLAELR EASLLAIVVD LSDPEWGMHV DTTQAVLARI GAEAIPRYYV YNKVDRVAQP PTNDELRACS RGHDFTVLSS TDAPAVAQLR TALIDAARQE HRRVRLFVPY RATELTTSIY ASCRVIETMA VEHGLVFTIE AASHVIAQIQ KAAKAVQA // ID A0A0C2B710_9ACTN Unreviewed; 501 AA. AC A0A0C2B710; DT 01-APR-2015, integrated into UniProtKB/TrEMBL. DT 01-APR-2015, sequence version 1. DT 07-JUN-2017, entry version 19. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=QR77_31020 {ECO:0000313|EMBL:KIF77095.1}; OS Streptomyces sp. 150FB. OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae; OC Streptomyces. OX NCBI_TaxID=1576605 {ECO:0000313|EMBL:KIF77095.1, ECO:0000313|Proteomes:UP000031584}; RN [1] {ECO:0000313|EMBL:KIF77095.1, ECO:0000313|Proteomes:UP000031584} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=150FB {ECO:0000313|EMBL:KIF77095.1, RC ECO:0000313|Proteomes:UP000031584}; RA Tarkka M.T., Feldhahn L., Kruger D., Buscot F., Wubet T.; RT "Genome sequence of the mycoparasite antagonist Streptomyces sp. RT strain FB 150."; RL Submitted (NOV-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KIF77095.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JTHL01000001; KIF77095.1; -; Genomic_DNA. DR RefSeq; WP_040025315.1; NZ_JTHL01000001.1. DR EnsemblBacteria; KIF77095; KIF77095; QR77_31020. DR Proteomes; UP000031584; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 2. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000313|EMBL:KIF77095.1}; KW Complete proteome {ECO:0000313|Proteomes:UP000031584}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900, KW ECO:0000313|EMBL:KIF77095.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000031584}. FT DOMAIN 280 445 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 501 AA; 54318 MW; E1B457E59584D585 CRC64; MTSSSSPSQD AQTLADDRTA DPRTDSLRAD ALMEEDVAWS HEIDGERDGD QLDRSDRAAL RRVAGLSTEL EDVTEVEYRQ LRLERVVLVG VWTSGSVLDA ENSLAELAAL AETAGALVLD GVVQRRDKPD PATYIGSGKA NELRDIVLDS GADTVVCDGE LSPGQLIHLE DVVKVKVVDR TALILDIFAQ HAKSREGKAQ VALAQMQYML PRLRGWGQSL SRQMGGGGGG GMATRGPGET KIETDRRRIR EKMAKMRREI GEMKTGRELK RQERRRHKVP SVAIAGYTNA GKSSLLNWLT GAGVLVENSL FATLDPTVRR AETPGGRLYT LTDTVGFVRH LPHHLVEAFR STMEEVGDSD LILHVVDGAH PAPEEQLAAV REVIHDVGAV NVREIVVINK ADAADPLVLQ RLLSAERYAI AVSARTGQGM AELLALIDAE LPRPETEVEV LVPYTLGALV SRVHAEGEVL SEEHTPEGTL LKARVHEGLA SALAPYLPVA S // ID A0A0C2C5L2_9BILA Unreviewed; 335 AA. AC A0A0C2C5L2; DT 01-APR-2015, integrated into UniProtKB/TrEMBL. DT 01-APR-2015, sequence version 1. DT 07-JUN-2017, entry version 10. DE SubName: Full=Putative GTP-binding protein HflX {ECO:0000313|EMBL:KIH51553.1}; GN ORFNames=ANCDUO_18361 {ECO:0000313|EMBL:KIH51553.1}; OS Ancylostoma duodenale. OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida; OC Strongylida; Ancylostomatoidea; Ancylostomatidae; Ancylostomatinae; OC Ancylostoma. OX NCBI_TaxID=51022 {ECO:0000313|EMBL:KIH51553.1, ECO:0000313|Proteomes:UP000054047}; RN [1] {ECO:0000313|EMBL:KIH51553.1, ECO:0000313|Proteomes:UP000054047} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Zhejiang {ECO:0000313|EMBL:KIH51553.1, RC ECO:0000313|Proteomes:UP000054047}; RA Mitreva M.; RT "Draft genome of the parsitic nematode Ancylostoma duodenale."; RL Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; KN746231; KIH51553.1; -; Genomic_DNA. DR Proteomes; UP000054047; Unassembled WGS sequence. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 2. DR SUPFAM; SSF52540; SSF52540; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000054047}; KW Reference proteome {ECO:0000313|Proteomes:UP000054047}. FT DOMAIN 152 226 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 335 AA; 38013 MW; 2FB6A95543F4A566 CRC64; MGVDYNTKRK AVWGSGQIEA LVRKKMQSRV TALMVNVDML TPFQQHELFR IFHVPIYDRY NIVLSIFKHY AKTQEARLQI QLAEIPYIRN RLHYLNKYRS DPSTLHVERQ TERANVDEFE VLRLREQSLR KKLQQVIEKN VGKASEETRD AAMVAVVGYT NAGKTSLVKC LTGASSLLPK DRLFATLDTT RHTARLPSGR KVVFTDTIGF LSDLPMHLLA AFQATLSHVN LAVRGIQEFL QGFCNCRMYF KDVIIHIRDM SNPDWPAQSE DVDKTLESIG LSQSRISDII VADNKVDVDG AAMSLTTGAI RISCKTSEGV DDLIEKVDEV ISFFM // ID A0A0C2CTW8_9DELT Unreviewed; 636 AA. AC A0A0C2CTW8; DT 01-APR-2015, integrated into UniProtKB/TrEMBL. DT 01-APR-2015, sequence version 1. DT 12-APR-2017, entry version 15. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=DB30_00597 {ECO:0000313|EMBL:KIG13060.1}; OS Enhygromyxa salina. OC Bacteria; Proteobacteria; Deltaproteobacteria; Myxococcales; OC Enhygromyxa. OX NCBI_TaxID=215803 {ECO:0000313|EMBL:KIG13060.1, ECO:0000313|Proteomes:UP000031599}; RN [1] {ECO:0000313|EMBL:KIG13060.1, ECO:0000313|Proteomes:UP000031599} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 15201 {ECO:0000313|EMBL:KIG13060.1, RC ECO:0000313|Proteomes:UP000031599}; RA Sharma G., Subramanian S.; RT "Genome assembly of Enhygromyxa salina DSM 15201."; RL Submitted (DEC-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KIG13060.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JMCC02000108; KIG13060.1; -; Genomic_DNA. DR EnsemblBacteria; KIG13060; KIG13060; DB30_00597. DR Proteomes; UP000031599; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000031599}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000031599}. FT DOMAIN 399 564 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 358 392 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 636 AA; 70310 MW; 2E609C9E98D62895 CRC64; MSDVVYGDTS NLKPSQARAL ARLGDRRVPA DQIVTGPLAR DLLELSHELN RRIGLFIDRR GRISRVILGD AHSLELPEFT RVRGADGRLR GVRLVSTHLV ADALNREELA DLTKLRLDLL AAVHDSPGGV QVDIANLQPA RDGKRGFELH TFSRAPLALL SPDAASRNQD GHPRPDLPTD FSAFITELEG LLVAATARTI AAGVGVRAMV LQVHTDDMNR QGGIEARQAE LRELCRTAGV ALVDLVVQRR RYPDPRTFLG SGKLREVLIH ALEQDVELLI CDPELSASQA RVISEQTDLR VIDRTTLILD IFAQHASSSD GKLQVELAQL RYWLPRMVGK GTMMSRLAGG IGGRGPGETK LELDRRRAQN RIHDLDKRLD HLRKQRQQRR ARRQRSEVPV VAIVGYTNAG KSTLLNTVTE STVRAENKLF ATLDPTVRRV RFPEEREVVM LDTVGFIRDL PPALMQAFSA TLEEVAEADL LLHVVDATDP DNTQQIRTVE RILDELGAAD VDRFMVFNKC DLLPDGQLVP ESELATGSYQ VSALDRRSTR RLMEAIESHL WARGKVEAPG SHRDGPWIEA SSDADDEDDE DDEDVSDDED DADDEDDDGD VSEDDDGDVS EDDEDDSGDV SDPSGA // ID A0A0C2ECT4_9DELT Unreviewed; 553 AA. AC A0A0C2ECT4; DT 01-APR-2015, integrated into UniProtKB/TrEMBL. DT 01-APR-2015, sequence version 1. DT 07-JUN-2017, entry version 18. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=GFER_09175 {ECO:0000313|EMBL:KIH76398.1}; OS Geoalkalibacter ferrihydriticus DSM 17813. OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfuromonadales; OC Geobacteraceae; Geoalkalibacter. OX NCBI_TaxID=1121915 {ECO:0000313|EMBL:KIH76398.1, ECO:0000313|Proteomes:UP000035068}; RN [1] {ECO:0000313|EMBL:KIH76398.1, ECO:0000313|Proteomes:UP000035068} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 17813 {ECO:0000313|EMBL:KIH76398.1, RC ECO:0000313|Proteomes:UP000035068}; RA Badalamenti J.P., Torres C.I., Krajmalnik-Brown R., Bond D.R.; RT "Genomes of Geoalkalibacter ferrihydriticus and Geoalkalibacter RT subterraneus, two haloalkaliphilic metal-reducing members of the RT Geobacteraceae."; RL Submitted (DEC-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KIH76398.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JWJD01000003; KIH76398.1; -; Genomic_DNA. DR RefSeq; WP_040098855.1; NZ_JWJD01000003.1. DR EnsemblBacteria; KIH76398; KIH76398; GFER_09175. DR Proteomes; UP000035068; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000035068}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000035068}. FT DOMAIN 377 541 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 336 370 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 553 AA; 62370 MW; 000EB8CF3C8A3D95 CRC64; MLDGNLTGLK PSQIKALERI DRRRIPPDQV VTGDLARFLT ELSRDIRRQL GIIVDRQGLI LHVLVGDDRE ILIPDLSRFG LGRSRLRGLR CIHTHLKGEA LSHDDLTDLA LLRLDLMVAI AVGEEGLPGR VDYAHLLPDN PEGKTVEVLS ASSVYDLHLD FSQFIDSLES EMERRMGETF DLSDTREKAI LISAGCEARV ELEDSLNELA ELARTADVVV LDRVVQRTQK VNPRFLMGEG KIREVIIRAL QQGATLLIFD QDLSPGQVRS ISEMTEMKVI DRTQLILDIF ARRAHTLDGK VQVEVAQLKY LMPRLLGKGT VMSRLMGGIG GRGPGETKLE IDRRRIRERL SRLEKQLESL SRGRRQRRQR RIRADVPIIS IVGYTNAGKS TLLNALTQST VFTEDLLFAT LDTSTRRLRF PQEREVIITD TVGFIRKLPK SLLGAFKATL EELEDADLLL HVVDISAPRF EEHIAAVERI LQDLDLGDLP RLLVFNKIDR VPAGEAAALC RRFEAIGVSA LDRSTFESLL EELQRRFWPQ ESFDDGPEKD SLL // ID A0A0C2JAS1_9ACTN Unreviewed; 496 AA. AC A0A0C2JAS1; DT 01-APR-2015, integrated into UniProtKB/TrEMBL. DT 01-APR-2015, sequence version 1. DT 07-JUN-2017, entry version 17. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=LP52_12760 {ECO:0000313|EMBL:KIH98561.1}; OS Streptomonospora alba. OC Bacteria; Actinobacteria; Streptosporangiales; Nocardiopsaceae; OC Streptomonospora. OX NCBI_TaxID=183763 {ECO:0000313|EMBL:KIH98561.1, ECO:0000313|Proteomes:UP000031675}; RN [1] {ECO:0000313|Proteomes:UP000031675} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=YIM 90003 {ECO:0000313|Proteomes:UP000031675}; RX PubMed=25601074; DOI=10.1016/j.chembiol.2014.11.017; RA Metelev M., Tietz J.I., Melby J.O., Blair P.M., Zhu L., Livnat I., RA Severinov K., Mitchell D.A.; RT "Structure, bioactivity, and resistance mechanism of streptomonomicin, RT an unusual lasso Peptide from an understudied halophilic RT actinomycete."; RL Chem. Biol. 22:241-250(2015). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KIH98561.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JROO01000023; KIH98561.1; -; Genomic_DNA. DR RefSeq; WP_040273549.1; NZ_JROO01000023.1. DR EnsemblBacteria; KIH98561; KIH98561; LP52_12760. DR Proteomes; UP000031675; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 2. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000313|EMBL:KIH98561.1}; KW Complete proteome {ECO:0000313|Proteomes:UP000031675}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900, KW ECO:0000313|EMBL:KIH98561.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000031675}. FT DOMAIN 277 442 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 496 AA; 54220 MW; F51AE48F5457FE59 CRC64; MNTFVDRGSL DSAEEIFAEA ADRTAAVRPY TAEDAVEAGS PDQGELELAE RHALRRVEGL STELTDVSEV EQRSLRLERV VLMGVWTSGT QQDADNSLIE LKHLAETAGA AVLEGMTQRR RKPDPATYIG RGKAEELREA VESTGADTLV CDGELAPGQL RQLEDIVKVK VIDRTALILD IFAQHARSRE GKAQVELAQL SYLVTRLRGW GTTLSRQAGG RAGGGNGGVG LRGPGETKIE TDRRRISARM SKLRRQISHM ATSRDVKRDK RQTRQVPAVS ISGYTNAGKS SLLNRLTNAG VLVHDELFAT LDPTVRQART PDGRAFTLSD TVGFVRHLPH ELVEAFRSTL EEVADADLIL HVVDASHPDP EQQLSSVREV FAEIGAEDVP EVVVLNKTDA ADPLVLKQLR AKEPHALEVS AHTGAGIEEL IAAVADALPD LDREVRVMLP YDRGDLVSRV YEEGRIVEKE HTGEGTRMHA YVPRLLAGKL DEYAAV // ID A0A0C2LV83_9CYAN Unreviewed; 571 AA. AC A0A0C2LV83; DT 01-APR-2015, integrated into UniProtKB/TrEMBL. DT 01-APR-2015, sequence version 1. DT 07-JUN-2017, entry version 19. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=SD81_05755 {ECO:0000313|EMBL:KIJ78806.1}; OS Tolypothrix campylonemoides VB511288. OC Bacteria; Cyanobacteria; Nostocales; Tolypothrichaceae; Tolypothrix. OX NCBI_TaxID=1245935 {ECO:0000313|EMBL:KIJ78806.1, ECO:0000313|Proteomes:UP000031981}; RN [1] {ECO:0000313|EMBL:KIJ78806.1, ECO:0000313|Proteomes:UP000031981} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=VB511288 {ECO:0000313|EMBL:KIJ78806.1, RC ECO:0000313|Proteomes:UP000031981}; RA Tripathy S., Das S., Gupta A., Malar M.C., Adhikary S.P.; RT "Draft whole genome shotgun sequence of Tolypothrix campylonemoides RT VB511288."; RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KIJ78806.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JXCB01000004; KIJ78806.1; -; Genomic_DNA. DR RefSeq; WP_041032981.1; NZ_JXCB01000004.1. DR EnsemblBacteria; KIJ78806; KIJ78806; SD81_05755. DR Proteomes; UP000031981; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000031981}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000031981}. FT DOMAIN 392 566 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 351 388 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 571 AA; 63211 MW; 848F7DD97CB6E958 CRC64; METIYGNIQG LKSSQSKKLQ QLYEQRQPSH TVTTPEFAQA LAAISTEIHQ PVCSYINRRG QVIRVAVGTP SQTQIPPEQL PRHSAERLSG IHCVATQFKS VPPDEAALIA MARQRLDALV VLTVADGKDG RRGKEATGDI KEAFLAHIVP DPQNPWVISP PLSLDDLTEQ DFDDLVDEWE REISESGDGM PFQEIVSDSD KVLLVGLKTD DISQQRFEDG LQELARLVET AGGTVADIVQ QKRSSPHPQT VVGQGKIEEI ALQAQKLGAN LIVFDRDISP SQARNLENEI GIRVVDRTEV ILDIFAQRAQ SQAGKLQVEL AQLEYMLPRL RGQGREMSRL GGGIGTRGPG ETKLETERRA IQRRIAQLQQ EVNQLQAHRA RIRQQRQQQE IPAVALVGYT NAGKSTLLNV LTHAEVYTAD QLFATLDPTT RKLVITEPET QERRTILLTD TVGFIHELPP PLVDAFRATL EEVTEADVLL HVVDLSHPAW ESHIASVEEV LAEMPTLSDP TLIAFNKVDQ VDSETLALAG QKYPEAVFIS ATQRLGLDTL RQRLLQVIDQ PVEAISVTQD S // ID A0A0C2QC66_9CYAN Unreviewed; 557 AA. AC A0A0C2QC66; DT 01-APR-2015, integrated into UniProtKB/TrEMBL. DT 01-APR-2015, sequence version 1. DT 12-APR-2017, entry version 18. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=SD81_15725 {ECO:0000313|EMBL:KIJ75945.1}; OS Tolypothrix campylonemoides VB511288. OC Bacteria; Cyanobacteria; Nostocales; Tolypothrichaceae; Tolypothrix. OX NCBI_TaxID=1245935 {ECO:0000313|EMBL:KIJ75945.1, ECO:0000313|Proteomes:UP000031981}; RN [1] {ECO:0000313|EMBL:KIJ75945.1, ECO:0000313|Proteomes:UP000031981} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=VB511288 {ECO:0000313|EMBL:KIJ75945.1, RC ECO:0000313|Proteomes:UP000031981}; RA Tripathy S., Das S., Gupta A., Malar M.C., Adhikary S.P.; RT "Draft whole genome shotgun sequence of Tolypothrix campylonemoides RT VB511288."; RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KIJ75945.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JXCB01000008; KIJ75945.1; -; Genomic_DNA. DR EnsemblBacteria; KIJ75945; KIJ75945; SD81_15725. DR Proteomes; UP000031981; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000031981}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000031981}. FT DOMAIN 384 554 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 343 377 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 557 AA; 61294 MW; 2228021D78BBF42C CRC64; MAAISTEINQ PVCAYLNRRG QVIRVGVGTP RQTQIPPLEL PRYGAERLSG IRCIATQLKP EPPNETALTA MALQRLDALV MLNITGTGFQ RRGGGATGYV KQAYLAHLTP QDARALITSP AVQKVSADLP AAGGGNQGGR EQKSNLPYTS WSISPPMSVD MLSQQDFMDL VEALEAEFRR EYVAQEVDAD HDRVLIVGVM TDDMTAQQFQ DTLDELGRLV DTAGGEVLEM MRQKRSRIHP QTVVGEGKVQ EIAITAQTLG ANLVVFDHDL SPAQIRNLES QIGVRVVDRT EVILDIFAQR AQSRAGKLQV ELAQLEYMLP RLAGRGQAMS RLGGGIGTRG PGETKLETER RAIGRRIARL QQQVNQLQAH RERLRQRRQH QEVPSVAIVG YTNAGKSTLL NALTNAEVYT ADQLFATLDP TTRRLVVPHA QMGELQEILV TDTVGFIHEL PASLMDAFRA TLEEVTEADA LLHLVDLSHP AWLSHIRSVR EILAQMPVTP GPALVVFNKI DEVDSETLAL AQEEFPLAVF ISASQRLGLE TLRQRLGQLV EYAASYR // ID A0A0C2QTP5_9CYAN Unreviewed; 598 AA. AC A0A0C2QTP5; DT 01-APR-2015, integrated into UniProtKB/TrEMBL. DT 01-APR-2015, sequence version 1. DT 07-JUN-2017, entry version 17. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=SD80_12865 {ECO:0000313|EMBL:KIJ83408.1}; OS Scytonema tolypothrichoides VB-61278. OC Bacteria; Cyanobacteria; Nostocales; Scytonemataceae; Scytonema. OX NCBI_TaxID=1233231 {ECO:0000313|EMBL:KIJ83408.1, ECO:0000313|Proteomes:UP000031959}; RN [1] {ECO:0000313|EMBL:KIJ83408.1, ECO:0000313|Proteomes:UP000031959} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=VB-61278 {ECO:0000313|EMBL:KIJ83408.1, RC ECO:0000313|Proteomes:UP000031959}; RA Tripathy S., Das A., Panda A., Malar M.C., Adhikary S.P.; RT "Draft genome sequence of Scytonema tolypothrichoides VB-61278."; RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KIJ83408.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JXCA01000009; KIJ83408.1; -; Genomic_DNA. DR RefSeq; WP_048868642.1; NZ_JXCA01000009.1. DR EnsemblBacteria; KIJ83408; KIJ83408; SD80_12865. DR Proteomes; UP000031959; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000031959}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000031959}. FT DOMAIN 425 595 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 384 418 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 598 AA; 66416 MW; 906C5EA70640E16C CRC64; MLIETIFGNL QGLKSSQLKQ IQRLYHQRIS GDRITTPEFS QRLAAISTEI NQPVCAYLNR RGQVIRVGVG TPRQTQIPPL ELPRYGAERL SGIRCIATHL KPEPPNEAAL TAMALQRLDA LVMLNITGTG FQRRGGGATG YVKEAYLAHL KPQDARALIT SPTIEKVSHL PPAGGENKEG KEQKNNLPYT SWTVSPPMSV DMLTNQDLME LVEGLEAEFR REFVAQDVDT DNDRVLIVGV MTDDMTAQQF QDTLEELARL VDTAGGEVLQ MMRQKRSRIH PQTVVGEGKV QEIAVAAQTL GANLIVFDRD LSPTQVRNLE LQIGVRVVDR TEVILDIFAQ RAQSRAGKLQ VELAQLEYML PRLAGRGQAM SRLGGGIGTR GPGETKLETE RRAIGRRISR LQQEVNQLQA HRERLRQRRQ HQEVPSVAIV GYTNAGKSTL LNTLTNAEVY TADQLFATLD PTTRRLVVPH GETDQPQEIL VTDTVGFIHE LPASLMDAFR ATLEEVTEAD ALLHLVDLSH PAWLSHIRSV REILAQMPIT PGPALVVFNK IDEVDSKNLA LAQEEFPLAV FISASQRLGL ETLRQRLGQL VEYAASYH // ID A0A0C2S180_9BACL Unreviewed; 423 AA. AC A0A0C2S180; DT 01-APR-2015, integrated into UniProtKB/TrEMBL. DT 01-APR-2015, sequence version 1. DT 07-JUN-2017, entry version 18. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=KR50_19760 {ECO:0000313|EMBL:KIL47809.1}; OS Jeotgalibacillus campisalis. OC Bacteria; Firmicutes; Bacilli; Bacillales; Planococcaceae; OC Jeotgalibacillus. OX NCBI_TaxID=220754 {ECO:0000313|EMBL:KIL47809.1, ECO:0000313|Proteomes:UP000031972}; RN [1] {ECO:0000313|EMBL:KIL47809.1, ECO:0000313|Proteomes:UP000031972} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SF-57 {ECO:0000313|EMBL:KIL47809.1, RC ECO:0000313|Proteomes:UP000031972}; RA Goh K.M., Chan K.-G., Yaakop A.S., Ee R., Gan H.M., Chan C.S.; RT "Jeotgalibacillus campisalis genome sequencing."; RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KIL47809.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JXRR01000014; KIL47809.1; -; Genomic_DNA. DR RefSeq; WP_041057644.1; NZ_JXRR01000014.1. DR EnsemblBacteria; KIL47809; KIL47809; KR50_19760. DR PATRIC; fig|220754.4.peg.1996; -. DR Proteomes; UP000031972; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000031972}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000031972}. FT DOMAIN 200 362 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 159 193 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 423 AA; 48423 MW; E131A06D51B613FC CRC64; MTDQNFNKEK AILVGVQLNQ TDNHIQQSLQ ELQALTETAK GEVVSILTQN RDRIHSGTYI GKGKVEELQA LEEEHEPDVI IFNSELSPSQ NRNLSKVLSA RIIDRTQLIL DIFAQRARSR EGKLQVQLAQ LEYMLPRLGG QGIELSRLGG GIGTRGPGET KLETDRRHIR NEIAEVKRQL NQVVKHRDQY RERRRKNNVF QIALVGYTNA GKSTLFNRLA EADSFEEDQL FATLDPMTRK LLLPSGYSVL MTDTVGFIQD LPTTLIASFR STLEEVNEAD MLLHIVDASH PDYVEHEKTV HKLFAELKMD HIPNMTVYNK KDNVWDEFTA LPDQQWMLIS AFDPNDIEAL KNKIEESMID QMILFEIVLS SNEGSLLAKF KREAVIKELT FIEEKEEYKL SGYMLKDSPI TGYIKEHKNL NDN // ID A0A0C2SDC3_9BACL Unreviewed; 420 AA. AC A0A0C2SDC3; DT 01-APR-2015, integrated into UniProtKB/TrEMBL. DT 01-APR-2015, sequence version 1. DT 07-JUN-2017, entry version 18. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=KP78_03440 {ECO:0000313|EMBL:KIL51974.1}; OS Jeotgalibacillus soli Cunha et al. 2012. OC Bacteria; Firmicutes; Bacilli; Bacillales; Planococcaceae; OC Jeotgalibacillus. OX NCBI_TaxID=889306 {ECO:0000313|EMBL:KIL51974.1, ECO:0000313|Proteomes:UP000031938}; RN [1] {ECO:0000313|EMBL:KIL51974.1, ECO:0000313|Proteomes:UP000031938} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=P9 {ECO:0000313|EMBL:KIL51974.1, RC ECO:0000313|Proteomes:UP000031938}; RA Goh K.M., Chan K.-G., Yaakop A.S., Ee R., Gan H.M., Chan C.S.; RT "Genome sequencing of Jeotgalibacillus soli."; RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KIL51974.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JXRP01000006; KIL51974.1; -; Genomic_DNA. DR RefSeq; WP_041085735.1; NZ_JXRP01000006.1. DR EnsemblBacteria; KIL51974; KIL51974; KP78_03440. DR PATRIC; fig|889306.3.peg.346; -. DR Proteomes; UP000031938; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000031938}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000031938}. FT DOMAIN 198 366 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 157 191 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 420 AA; 47611 MW; 6EC7E2C2DB2D3E8E CRC64; MTALNEKAVI VGVELQHQED FEYSMEELVN LAAACDVVVV GKVTQKLNRI NPSHYIGTGK VEEVRVLLEE NEGNVVIFND ELSPSQIRNL EAELVCKVID RTILILDIFA QRAKTREAQL QVEIAHLQYM LPRLIGLGES LGRQSGGVGT KNKGAGETKL ELDRRRIEEK ITALNKELEA LVAQRRIQRK QRQKNEIPRV SLVGYTNAGK STTMNALLDL FSESKEKHVF EKDMLFATLE TSVRNIQLPG NKSFLLTDTV GFVNKLPHHL VKAFRSTLEE VAESDLLIHV VDYSNPEYAQ LIKTTERTLR DIGVEDIPMV YAYNKADLTE QSIPKTEENR VYLSAKENIG IDELLTMVRQ HIFQGYVECE LLIPYDQGKV VAYFNEKATI HSISYEENGT LIKVECKQAD AKRYQQYVMG // ID A0A0C2V649_9BACL Unreviewed; 438 AA. AC A0A0C2V649; DT 01-APR-2015, integrated into UniProtKB/TrEMBL. DT 01-APR-2015, sequence version 1. DT 07-JUN-2017, entry version 18. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=SD70_19780 {ECO:0000313|EMBL:KIL39528.1}; OS Paenibacillus sp. VKM B-2647. OC Bacteria; Firmicutes; Bacilli; Bacillales; Paenibacillaceae; OC Paenibacillus. OX NCBI_TaxID=1590651 {ECO:0000313|EMBL:KIL39528.1, ECO:0000313|Proteomes:UP000031967}; RN [1] {ECO:0000313|EMBL:KIL39528.1, ECO:0000313|Proteomes:UP000031967} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=VKM B-2647 {ECO:0000313|EMBL:KIL39528.1, RC ECO:0000313|Proteomes:UP000031967}; RA Karlyshev A.V., Kudryashova E.B.; RT "Draft genome sequence of Paenibacillus kamchatkensis strain B-2647."; RL Submitted (DEC-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KIL39528.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JXAK01000036; KIL39528.1; -; Genomic_DNA. DR RefSeq; WP_041049254.1; NZ_JXAK01000036.1. DR EnsemblBacteria; KIL39528; KIL39528; SD70_19780. DR Proteomes; UP000031967; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000031967}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000031967}. FT DOMAIN 207 372 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 438 AA; 48826 MW; BC50757219D3D16D CRC64; MDDAAYDARS ANDRAVLVSL VTSVQKRSEA MAAYSLQELV RLAETAGVQV LETMTQHRET PDARSFIGKG KVEELKQRIE QLEANTAIFD QELSGAQVRN LEAALDVKII DRTQLILDIF AQRANTREGI IQVELAQLSY LLPRLSGHGK NLSRLGGGIG TRGPGETKLE TDRRHIRNRI SDLKAQLSEV VRHRELHRER RRKSGVFQVA LVGYTNAGKS TLLKRLTNAD VYVENQLFAT LDPTSRTMSL PSGKEIVLTD TVGFIQNLPH DLIAAFRATL EEANEADLIL HVVDSSAEMR SEQMRVVDEV LEELGAGGKE RLTVFNKMDL LPPAEQEELL VADGDYIRIT AYSDADLERL RHSIQEKLLG DRKTFRVPVG KGDVISLVYR IGDVLEGEVD GGDMRFEVRV NKDDYAKMGY LLAAYDESAA GERQRGEN // ID A0A0C2VLY4_9BACL Unreviewed; 420 AA. AC A0A0C2VLY4; DT 01-APR-2015, integrated into UniProtKB/TrEMBL. DT 01-APR-2015, sequence version 1. DT 07-JUN-2017, entry version 18. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=KP78_25370 {ECO:0000313|EMBL:KIL44993.1}; OS Jeotgalibacillus soli Cunha et al. 2012. OC Bacteria; Firmicutes; Bacilli; Bacillales; Planococcaceae; OC Jeotgalibacillus. OX NCBI_TaxID=889306 {ECO:0000313|EMBL:KIL44993.1, ECO:0000313|Proteomes:UP000031938}; RN [1] {ECO:0000313|EMBL:KIL44993.1, ECO:0000313|Proteomes:UP000031938} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=P9 {ECO:0000313|EMBL:KIL44993.1, RC ECO:0000313|Proteomes:UP000031938}; RA Goh K.M., Chan K.-G., Yaakop A.S., Ee R., Gan H.M., Chan C.S.; RT "Genome sequencing of Jeotgalibacillus soli."; RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KIL44993.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JXRP01000018; KIL44993.1; -; Genomic_DNA. DR RefSeq; WP_041089234.1; NZ_JXRP01000018.1. DR EnsemblBacteria; KIL44993; KIL44993; KP78_25370. DR PATRIC; fig|889306.3.peg.2551; -. DR Proteomes; UP000031938; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000031938}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Hydrolase {ECO:0000313|EMBL:KIL44993.1}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Protease {ECO:0000313|EMBL:KIL44993.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000031938}. FT DOMAIN 201 363 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 420 AA; 48265 MW; BD695197A425E1E7 CRC64; MNKHDFPRER AILVGVQVGQ TEDERFAQSL EELKALTETA QGEVVSVMTQ NRDRIHSSTY MGKGKLEELQ VLEEELEPDV IIFNSELSPS QNRNISKVLN ARIIDRTQLI LDIFAQRARS REGKLQVQLA QLEYLLPRLS GQGIELSRLG GGIGTRGPGE TKLETDRRHI RGEISEIKRQ LKNVVKHREQ YRERRRKNHV FQISLVGYTN AGKSTLFNRL ADADSYEENQ LFATLDPMTR KLTLPSQHSI LMTDTVGFIQ DLPTTLIASF RSTLEEVNEA DLLLHVVDSA HPDHVNHEQT VQRLLVDLHM DHIPQLTVYN KRDLSSADFV PSPNHDYLWM SALNEQDLQQ LLLEVEKQML DRMKLYEVVV PSTEGKLISR LKRETIVRDV TFNETDDQYI IQGHVMEDHP VLGQIYEHGR // ID A0A0C2YGP5_BACBA Unreviewed; 416 AA. AC A0A0C2YGP5; DT 01-APR-2015, integrated into UniProtKB/TrEMBL. DT 01-APR-2015, sequence version 1. DT 30-AUG-2017, entry version 21. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=SD77_0536 {ECO:0000313|EMBL:KIL80688.1}; OS Bacillus badius. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus. OX NCBI_TaxID=1455 {ECO:0000313|EMBL:KIL80688.1, ECO:0000313|Proteomes:UP000031982}; RN [1] {ECO:0000313|EMBL:KIL80688.1, ECO:0000313|Proteomes:UP000031982} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MTCC 1458 {ECO:0000313|EMBL:KIL80688.1, RC ECO:0000313|Proteomes:UP000031982}; RA Verma A., Khatri I., Mual P., Subramanian S., Krishnamurthi S.; RT "Genome Assembly of Bacillus badius MTCC 1458."; RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KIL80688.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JXLP01000001; KIL80688.1; -; Genomic_DNA. DR EnsemblBacteria; KIL80688; KIL80688; SD77_0536. DR PATRIC; fig|1455.4.peg.3477; -. DR Proteomes; UP000031982; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000031982}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000031982}. FT DOMAIN 198 360 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 416 AA; 47290 MW; DE765B52138FBB46 CRC64; MTKMEKEKVI LAGCQLTDDT EQFLYSMQEL KSLIETAQGE SLAMITQKRE RIHPGTYIGK GKVEELKRLE EELEPDLIIF NGELSPSQIR NLSAEFSARV IDRTQLILDI FARRARSREG QLQVELAQLQ YLLPRLSGQG TALSRLGGGI GTRGPGETKL ESDRRHIRRR IDEIKRQLHT IVHHRERYRS RRKKNRAFQI ALVGYTNAGK STLFNRLTAA DSLEENQLFA TLDPLTRKLV LPSGYQAILT DTVGFIQDLP TTLVAAFRST LEEVSEADLL LHVVDSANPD LMQHQETVRS LLEQLEMDHL PELTVYNKRD IQHEEFVPSS ASANILISAV NEADRLKLKE VIERMIREQM TSYNGRIPAS AGKLLAQLKT ETIVDSILFD EEEQVYRVKG FAFKDHPIAG EISKYI // ID A0A0C3HTC4_9VIBR Unreviewed; 429 AA. AC A0A0C3HTC4; DT 01-APR-2015, integrated into UniProtKB/TrEMBL. DT 01-APR-2015, sequence version 1. DT 30-AUG-2017, entry version 19. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=SU60_07680 {ECO:0000313|EMBL:KIN11436.1}; OS Vibrio mytili. OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; OC Vibrionaceae; Vibrio. OX NCBI_TaxID=50718 {ECO:0000313|EMBL:KIN11436.1, ECO:0000313|Proteomes:UP000031977}; RN [1] {ECO:0000313|EMBL:KIN11436.1, ECO:0000313|Proteomes:UP000031977} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CAIM 528 {ECO:0000313|EMBL:KIN11436.1, RC ECO:0000313|Proteomes:UP000031977}; RA Gonzalez-Castillo A., Gomez-Gil B., Enciso-Ibarra J.; RT "Draft genome of Vibrio mytili type strain CAIM 528."; RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KIN11436.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JXOK01000022; KIN11436.1; -; Genomic_DNA. DR RefSeq; WP_041154997.1; NZ_JXOK01000022.1. DR EnsemblBacteria; KIN11436; KIN11436; SU60_07680. DR Proteomes; UP000031977; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000031977}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000031977}. FT DOMAIN 198 365 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 429 AA; 48793 MW; D049098F9C08A05B CRC64; MFDRYESGER AVLVHINFTQ EGEWEDLAEF EMLVSSAGVE ALQVITGSRQ SPHPKYYVGE GKAQEIATAV QSTDAEIVIF NHSLSPAQER NLEALCQCRV LDRTGLILDI FAQRARTHEG KLQVELAQLR HLSTRLIRGW THLERQKGGI GLRGPGETQL ETDRRLLRDR IKAILRRLDK VAKQREQGRR ARNRAEIPTV SLVGYTNAGK STLFNRITEA GVYAADQLFA TLDPTLRKIE LSDVGPVILA DTVGFIRHLP HDLVAAFKAT LQETQEADIL LHVVDASDER FRENIQAVHE VLEEIDAHEV PTLVVMNKID NLDSQNPRIE RDEEGVPRAV WVSAMDGLGI ELLFDALTER LASQMVEYQL CIPPQYQGRF RSTFFQMKCI QREDYDQDGN LLIDVRMQQV DWFRLEKREG AVLTDFIVT // ID A0A0C3NDV3_9PORP Unreviewed; 407 AA. AC A0A0C3NDV3; DT 01-APR-2015, integrated into UniProtKB/TrEMBL. DT 01-APR-2015, sequence version 1. DT 07-JUN-2017, entry version 17. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=BA92_08735 {ECO:0000313|EMBL:KIO44287.1}; OS Sanguibacteroides justesenii. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; OC Porphyromonadaceae; Sanguibacteroides. OX NCBI_TaxID=1547597 {ECO:0000313|EMBL:KIO44287.1, ECO:0000313|Proteomes:UP000031980}; RN [1] {ECO:0000313|EMBL:KIO44287.1, ECO:0000313|Proteomes:UP000031980} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=OUH 308042 {ECO:0000313|EMBL:KIO44287.1, RC ECO:0000313|Proteomes:UP000031980}; RA Sydenham T.V., Hasman H., Justensen U.S.; RT "Porphyromonadaceae bacterium OUH 308042 = ATCC BAA-2681 = DSM 28342 RT draft genome."; RL Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KIO44287.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JPIU01000039; KIO44287.1; -; Genomic_DNA. DR RefSeq; WP_041503520.1; NZ_JPIU01000039.1. DR EnsemblBacteria; KIO44287; KIO44287; BA92_08735. DR Proteomes; UP000031980; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000031980}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000031980}. FT DOMAIN 205 389 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 173 200 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 407 AA; 46795 MW; A266002C615A745A CRC64; MGNYFYTEKK AEKAILVGVA LQSENISYDT MCEYLNELAF LAETAGAETV KVFTQNLDKP VTATFIGKGK LEEIKNYVEE NDIDLIIFDD ELTPTQLRNI ERELKGRKVL DRTNLILDIF AKRARTAEAK AQVELAQYQY LLPRLTGMWT HLERQKGGIG LRGPGETEIE TDRRIIRDKI SRLKEQLDKI DKQMITQRKN RGKLVRVALV GYTNVGKSTL MNLLSKSEVF AENKLFATLD TTVRKIAIKN VPLLLADTVG FIRKLPHHLV ESFKSTLDEV READVILHVV DISHPQFEDQ IRVVNETLAE LIENPKPTIT IFNKIDAFTF VPKEEDDLTP IERENYSLDH LKQMWMAKQG GETVYISAKN KENIEELKEK LYNIAKEIHS ARFPFNDFLY QDTIIED // ID A0A0C3REW2_9PROT Unreviewed; 390 AA. AC A0A0C3REW2; DT 01-APR-2015, integrated into UniProtKB/TrEMBL. DT 01-APR-2015, sequence version 1. DT 07-JUN-2017, entry version 17. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=SQ11_01810 {ECO:0000313|EMBL:KIO50425.1}; OS Nitrosospira sp. NpAV. OC Bacteria; Proteobacteria; Betaproteobacteria; Nitrosomonadales; OC Nitrosomonadaceae; Nitrosospira. OX NCBI_TaxID=58133 {ECO:0000313|EMBL:KIO50425.1, ECO:0000313|Proteomes:UP000031969}; RN [1] {ECO:0000313|EMBL:KIO50425.1, ECO:0000313|Proteomes:UP000031969} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NpAV {ECO:0000313|EMBL:KIO50425.1, RC ECO:0000313|Proteomes:UP000031969}; RA Rice M.C., Lim C.K., Sayavedra-Soto L.A., Norton J.M., Klotz M.G.; RT "Nitrosospira sp. NpAV genome sequencing."; RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KIO50425.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JXQM01000001; KIO50425.1; -; Genomic_DNA. DR RefSeq; WP_041512374.1; NZ_JXQM01000001.1. DR EnsemblBacteria; KIO50425; KIO50425; SQ11_01810. DR Proteomes; UP000031969; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000031969}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000031969}. FT DOMAIN 202 371 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 390 AA; 43042 MW; 24E287FFBF115A75 CRC64; MLDLPAGNTA EANSAVLVSL DFSDGDYAEN LEELRQLAAS DALTIRAVIK GKRSRPDPAT FAGRGKVDEI TMALEQTGAS LVIFNHDLSP AQQRNLERHL KCRVIDRTSL ILDIFAQRAK SHEGKLQVEL AQLEHLSTRL VRGWTHLERQ KGGIGLRGPG ETQLETDRRL LGKRVKLLKE KLVKFQRQRK LQRRSRQRAQ VMSVSIVGYT NAGKSTLFNQ LTRAHTYVAD QLFATLDATT RKLFIPDHGS LVISDTVGFI RDLPHTLVAA FRATLEETVE ADMLLHVVDA GSSNRDEQIA EVNKVLKEIG ADSVPQILVL NKIDLMNLSA GGAGYGRDEC GRIAQIRLSA KTGEGLEFIK LALSEAMQEH IIQRHEDLSE TGSVISGYAA // ID A0A0C4Y426_9BURK Unreviewed; 415 AA. AC A0A0C4Y426; DT 29-APR-2015, integrated into UniProtKB/TrEMBL. DT 29-APR-2015, sequence version 1. DT 07-JUN-2017, entry version 15. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=RR42_m2657 {ECO:0000313|EMBL:AJG20042.1}; OS Cupriavidus basilensis. OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Cupriavidus. OX NCBI_TaxID=68895 {ECO:0000313|EMBL:AJG20042.1, ECO:0000313|Proteomes:UP000031843}; RN [1] {ECO:0000313|EMBL:AJG20042.1, ECO:0000313|Proteomes:UP000031843} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=4G11 {ECO:0000313|EMBL:AJG20042.1}; RX PubMed=25977418; RA Ray J., Waters R.J., Skerker J.M., Kuehl J.V., Price M.N., Huang J., RA Chakraborty R., Arkin A.P., Deutschbauer A.; RT "Complete Genome Sequence of Cupriavidus basilensis 4G11, Isolated RT from the Oak Ridge Field Research Center Site."; RL Genome Announc. 3:0-0(2015). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP010536; AJG20042.1; -; Genomic_DNA. DR RefSeq; WP_043347447.1; NZ_CP010536.1. DR EnsemblBacteria; AJG20042; AJG20042; RR42_m2657. DR KEGG; cbw:RR42_m2657; -. DR KO; K03665; -. DR Proteomes; UP000031843; Chromosome main. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000031843}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000031843}. FT DOMAIN 202 372 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 161 195 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 415 AA; 46007 MW; 37E0D1AB7EE1EE86 CRC64; MQSRATSNSE SSRAILVGVD FGKHDFQESL SELALLTSTA GSTPVHTLTG RRSRPDPALF IGSGKAEELK EAADALDADV VVFNHSLSPA QQRNLERFLQ RHVIDRTGLI LDIFGQRAQS HVGKVQVELA QVQYQASRLV RAWSHLERQK GGIGMRGGPG ERQLELDRRL LDERAKRLKA DLTRLQRQHS TQRRARARND TLSISLVGYT NAGKSTLFNA LTKARAYAAD QLFATLDTTS RRLYLEGVGN VVLSDTVGFI RDLPTQLVAA FRATLEETVH ADLLLHVVDA SSPVRHEQIE QVNRVLAEIN ADDIPQIVVM NKIDASPELL EQGPRVERNE EGVPTRVFVS ARDGIGLDAL REALVEVARW LAERPPERPP LDPRLADAQP YPDDDLDNDL DGDDTRADPE EPDTQ // ID A0A0C5BEE8_9MICO Unreviewed; 514 AA. AC A0A0C5BEE8; DT 29-APR-2015, integrated into UniProtKB/TrEMBL. DT 29-APR-2015, sequence version 1. DT 07-JUN-2017, entry version 20. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=VT73_05355 {ECO:0000313|EMBL:KKM45817.1}; OS Rathayibacter toxicus. OC Bacteria; Actinobacteria; Micrococcales; Microbacteriaceae; OC Rathayibacter. OX NCBI_TaxID=145458 {ECO:0000313|EMBL:KKM45817.1, ECO:0000313|Proteomes:UP000052979}; RN [1] {ECO:0000313|EMBL:KKM45817.1, ECO:0000313|Proteomes:UP000052979} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=FH142 {ECO:0000313|EMBL:KKM45817.1, RC ECO:0000313|Proteomes:UP000052979}; RG Consortium for Microbial Forensics and Genomics (microFORGE); RA Knight B.M., Roberts D.P., Lin D., Hari K., Fletcher J., Melcher U., RA Blagden T., Luster D.G., Sechler A.J., Schneider W.L., Winegar R.A.; RT "Draft genome sequence of Rathayibacter toxicus strain FH-142 (AKA RT 70134 or CS 32), a Western Australian isolate."; RL Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KKM45817.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LBFI01000031; KKM45817.1; -; Genomic_DNA. DR RefSeq; WP_027692122.1; NZ_LBFI01000031.1. DR EnsemblBacteria; KKM45817; KKM45817; VT73_05355. DR KEGG; rtc:APU90_01960; -. DR KEGG; rtx:TI83_04515; -. DR PATRIC; fig|145458.7.peg.1044; -. DR KO; K03665; -. DR Proteomes; UP000052979; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 2. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000052979}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000052979}. FT DOMAIN 289 454 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 514 AA; 55564 MW; 9E6A85E31DB0292E CRC64; MTEDRKETTT NDDVDVVSRI LASTQSPSAK YSRFVAGEAQ ALHSTGYAEE GQVGDGDQRD REDRQALRRV AGLSTELEDV TEVEYRQLRL ENVVLIGVYS QYSLADAENS LHELAALAET AGATVLDGML QRRSHPDPST YLGKGKAEEL AGLVAALGAD TVVADTELAP SQRRALEDIV KVKVIDRTAV ILDIFSQHAT SREGKAQVEL AQLEYLLPRL RGWGESMSRQ AGGQVGAGAG MGSRGPGETK IELDRRRIHT RMARLRKQIA AMKPARAAKR AQRRRNAVPS VAIAGYTNAG KSSLLNRMTH AGVLVENALF ATLDATVRKA QTPDGRGYTL TDTVGFVRAL PHQLVEAFRS TLEEVADAEV IVHVVDASHS DPASQIATVH DVIGELGARD IPEIIVFNKS DLVDDGTRLV LRGLAPGAVF VSARRGEGIG ELEARIAQLL PEPEIEIDLL VPYDRGDVVS QLHRGGRILT THYVEGGTRI RALVHADLAG SLRAFASPHT TAER // ID A0A0C5GI76_9ACTN Unreviewed; 497 AA. AC A0A0C5GI76; DT 29-APR-2015, integrated into UniProtKB/TrEMBL. DT 29-APR-2015, sequence version 1. DT 07-JUN-2017, entry version 17. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=TU94_24570 {ECO:0000313|EMBL:AJP04171.1}; OS Streptomyces cyaneogriseus subsp. noncyanogenus. OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae; OC Streptomyces. OX NCBI_TaxID=477245 {ECO:0000313|EMBL:AJP04171.1, ECO:0000313|Proteomes:UP000032234}; RN [1] {ECO:0000313|EMBL:AJP04171.1, ECO:0000313|Proteomes:UP000032234} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NMWT 1 {ECO:0000313|EMBL:AJP04171.1, RC ECO:0000313|Proteomes:UP000032234}; RA Wang H., Li C., Xiang W., Wang X.; RT "Genome sequence of thermotolerant Streptomyces cyaneogriseus subsp. RT Noncyanogenus NMWT1, the producer of nematocidal antibiotics RT nemadectin."; RL Submitted (FEB-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP010849; AJP04171.1; -; Genomic_DNA. DR RefSeq; WP_044384658.1; NZ_CP010849.1. DR EnsemblBacteria; AJP04171; AJP04171; TU94_24570. DR KEGG; scw:TU94_24570; -. DR PATRIC; fig|477245.3.peg.5183; -. DR KO; K03665; -. DR Proteomes; UP000032234; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 2. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000313|EMBL:AJP04171.1}; KW Complete proteome {ECO:0000313|Proteomes:UP000032234}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900, KW ECO:0000313|EMBL:AJP04171.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000032234}. FT DOMAIN 275 440 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 497 AA; 54404 MW; 4F14E2E0B748C939 CRC64; MTSSSSPSQD TKRLAHAYPE GLRADALMEE DVAWSHEIDS EWDGDQFDRS ERAALRRVAG LSTELEDVTE VEYRQLRLER VVLVGVWTSG TVQDAENSLA ELAALAETAG ALVLDGVIQR RDKPDAATYI GSGKAQELRE IVLETGADTV ICDGELSPGQ LIHLEDVVKV KVIDRTALIL DIFAQHAKSR EGKAQVALAQ MQYMLPRLRG WGQSLSRQMG GGKGGGLATR GPGETKIETD RRRIREKMAK MRREIAEMKT GREIKRQERK RNKVPSVAIA GYTNAGKSSL LNRLTGAGVL VENALFATLD PTVRRAETPS GRLYTLADTV GFVRHLPHHL VEAFRSTMEE VGDSDLILHV VDGSHPNPEE QLAAVREVIR DVGATGVPEI VVVNKADLAD PLVLQRLLRI EKRPIAVSAR TGQNIGELLA LIDNELPRPS VEIEALVPYT HGKLVARAHD EGEVISEEHT PEGTLLKVRV HEELAAELTP YVPAPAA // ID A0A0C5JB77_9RHOO Unreviewed; 71 AA. AC A0A0C5JB77; DT 29-APR-2015, integrated into UniProtKB/TrEMBL. DT 29-APR-2015, sequence version 1. DT 07-JUN-2017, entry version 10. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AJP49058.1}; GN ORFNames=PG1C_07310 {ECO:0000313|EMBL:AJP48322.1}, GN PG1C_12705 {ECO:0000313|EMBL:AJP49058.1}; OS Rugosibacter aromaticivorans. OC Bacteria; Proteobacteria; Betaproteobacteria; Rhodocyclales; OC Rhodocyclaceae; Rugosibacter. OX NCBI_TaxID=1565605 {ECO:0000313|EMBL:AJP49058.1, ECO:0000313|Proteomes:UP000061603}; RN [1] {ECO:0000313|EMBL:AJP49058.1, ECO:0000313|Proteomes:UP000061603} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Ca6 {ECO:0000313|EMBL:AJP49058.1}, and RC PG1-Ca6 {ECO:0000313|Proteomes:UP000061603}; RX PubMed=25858839; RA Singleton D.R., Dickey A.N., Scholl E.H., Wright F.A., Aitken M.D.; RT "Complete Genome Sequence of a Novel Bacterium within the Family RT Rhodocyclaceae That Degrades Polycyclic Aromatic Hydrocarbons."; RL Genome Announc. 3:0-0(2015). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP010554; AJP48322.1; -; Genomic_DNA. DR EMBL; CP010554; AJP49058.1; -; Genomic_DNA. DR EnsemblBacteria; AJP48322; AJP48322; PG1C_07310. DR EnsemblBacteria; AJP49058; AJP49058; PG1C_12705. DR KEGG; rbu:PG1C_07310; -. DR KEGG; rbu:PG1C_12705; -. DR PATRIC; fig|1565605.3.peg.1539; -. DR Proteomes; UP000061603; Chromosome. DR InterPro; IPR025121; GTPase_HflX_N. DR Pfam; PF13167; GTP-bdg_N; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000061603}; KW Reference proteome {ECO:0000313|Proteomes:UP000061603}. FT DOMAIN 28 65 GTP-bdg_N. {ECO:0000259|Pfam:PF13167}. SQ SEQUENCE 71 AA; 7800 MW; F5B0D5BE68A6C03C CRC64; MQKEVKEKPR YAVVAAVQLP SVSDVEFEAS LTELRELAKT LGFTVTRTFM QKRSGFDSTA YLGVGGDTPL C // ID A0A0C5L3N0_9SPHN Unreviewed; 430 AA. AC A0A0C5L3N0; DT 29-APR-2015, integrated into UniProtKB/TrEMBL. DT 29-APR-2015, sequence version 1. DT 07-JUN-2017, entry version 16. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=TS85_07355 {ECO:0000313|EMBL:AJP71643.1}; OS Sphingomonas hengshuiensis. OC Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales; OC Sphingomonadaceae; Sphingomonas. OX NCBI_TaxID=1609977 {ECO:0000313|EMBL:AJP71643.1, ECO:0000313|Proteomes:UP000032300}; RN [1] {ECO:0000313|EMBL:AJP71643.1, ECO:0000313|Proteomes:UP000032300} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=WHSC-8 {ECO:0000313|EMBL:AJP71643.1, RC ECO:0000313|Proteomes:UP000032300}; RA Wei S., Guo J., Su C., Wu R., Zhang Z., Liang K., Li H., Wang T., RA Liu H., Zhang C., Li Z., Wang Q., Meng J.; RT "The complete genome of Sphingomonas hengshuiensis sp. WHSC-8 isolated RT from soil of Hengshui Lake."; RL Submitted (FEB-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP010836; AJP71643.1; -; Genomic_DNA. DR RefSeq; WP_044331399.1; NZ_CP010836.1. DR EnsemblBacteria; AJP71643; AJP71643; TS85_07355. DR KEGG; sphi:TS85_07355; -. DR PATRIC; fig|1609977.7.peg.1518; -. DR KO; K03665; -. DR Proteomes; UP000032300; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000032300}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000032300}. FT DOMAIN 208 377 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 174 201 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 430 AA; 47405 MW; 0AFCD024599F145B CRC64; MSTGFDRDPD EFSRGAKAAV VYPDMGGSSR DADARLEETA GLAAAIGIHV REKVALRIRS PKPGTLIGSG QVEALAETVR DQELQLAVFD ASLTPVQQRN LETALGCKVI DRTGLILEIF GERARTAEGR LQVELAHLDY QAGRLVRSWT HLERQRGGFG FLGGPGETQI EADRRLIRDR MARLRRELDQ VSRTRSLHRD RRQRAPWPVI ALVGYTNAGK STLFNRLTGA DVMAENLLFA TLDPTLRQIA LPGIDKAILS DTVGFVSELP TQLVAAFKAT LEEVVSADLL IHVRDVAHPD SEAQKDDVEQ VLSDIGVAEE TPRFEAWNKL DLLDADSRAY LTAEAAKRDD VMPISAITGE GVDALVEAVA ARLTQGHRRY HIELDPADGA GAAWLHQHGE VLEQSIADDR ALYEVRMAPR DYDRFWLRAG // ID A0A0C5VLZ2_9GAMM Unreviewed; 437 AA. AC A0A0C5VLZ2; DT 29-APR-2015, integrated into UniProtKB/TrEMBL. DT 29-APR-2015, sequence version 1. DT 07-JUN-2017, entry version 16. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=YC6258_02340 {ECO:0000313|EMBL:AJQ94378.1}; OS Gynuella sunshinyii YC6258. OC Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales; OC Saccharospirillaceae; Gynuella. OX NCBI_TaxID=1445510 {ECO:0000313|EMBL:AJQ94378.1, ECO:0000313|Proteomes:UP000032266}; RN [1] {ECO:0000313|EMBL:AJQ94378.1, ECO:0000313|Proteomes:UP000032266} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=YC6258 {ECO:0000313|EMBL:AJQ94378.1, RC ECO:0000313|Proteomes:UP000032266}; RA Khan H., Chung E.J., Chung Y.R.; RT "Full genme sequencing of cellulolytic bacterium Gynuella sunshinyii RT YC6258T gen. nov., sp. nov."; RL Submitted (JAN-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP007142; AJQ94378.1; -; Genomic_DNA. DR RefSeq; WP_044616912.1; NZ_CP007142.1. DR EnsemblBacteria; AJQ94378; AJQ94378; YC6258_02340. DR KEGG; gsn:YC6258_02340; -. DR PATRIC; fig|1445510.3.peg.2296; -. DR KO; K03665; -. DR Proteomes; UP000032266; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000032266}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000032266}. FT DOMAIN 199 366 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 158 192 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 437 AA; 48962 MW; E53335BCA2A1DB8B CRC64; MLFDRAQAGD LAVLVHIDFP EGDDREDPRE FEELVISAGA NPLALITGVR SVPDPKLFVG SGKVAEIKQA VIDTQADVVL FNHALRPSQE RNLERELECR VLDRTGLILD IFAQRARTHE GKLQVELAQL NYQSTRLIRG WTHLERQKGG IGLRGPGETQ LESDRRLLQA RINSIQNRLK KVEKQRDQSR RSRTRSDTPT VSLVGYTNAG KSTLFNYLTE AEVYAADQMF ATLDPTLRKL HVSDLGPVIL ADTVGFIRHL PHRLVDAFKA TLQETVEADL LLHVIDAASD ERDHNIEQVE TVLSEIGAEQ VPILEVYNKI DLMEHAAPGI ERNDDGTPKR VWVSAKTGQG TELIGRAIAE ILGEEIFDQQ IRISPGEGQL RALFFAKKAV LNESYADNGD ILLHVRLQQK DMLQVLTQAG VETSRFVPAP EKEFYEH // ID A0A0C5W5S5_9GAMM Unreviewed; 429 AA. AC A0A0C5W5S5; DT 29-APR-2015, integrated into UniProtKB/TrEMBL. DT 29-APR-2015, sequence version 1. DT 30-AUG-2017, entry version 15. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=H744_2c0052 {ECO:0000313|EMBL:AJR06821.1}; OS Photobacterium gaetbulicola Gung47. OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; OC Vibrionaceae; Photobacterium. OX NCBI_TaxID=658445 {ECO:0000313|EMBL:AJR06821.1, ECO:0000313|Proteomes:UP000032303}; RN [1] {ECO:0000313|EMBL:AJR06821.1, ECO:0000313|Proteomes:UP000032303} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Gung47 {ECO:0000313|EMBL:AJR06821.1, RC ECO:0000313|Proteomes:UP000032303}; RA Kim Y.-O.; RT "Complete genome sequence of the lipase-producing bacterium RT Photobacterium gaetbulicola Gung47."; RL Submitted (MAY-2013) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP005974; AJR06821.1; -; Genomic_DNA. DR RefSeq; WP_044622049.1; NZ_CP005974.1. DR EnsemblBacteria; AJR06821; AJR06821; H744_2c0052. DR KEGG; pgb:H744_2c0052; -. DR PATRIC; fig|658445.3.peg.1952; -. DR KO; K03665; -. DR Proteomes; UP000032303; Chromosome 2. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000032303}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000032303}. FT DOMAIN 198 365 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 429 AA; 48432 MW; 322427C909237439 CRC64; MFDRYETGEQ AILVHINFTQ EGEWEDLSEF EMLVSSAGVN TLRVVTGSRK TPHPKFYVGE GKAQEIAEAV RAEDAEIVIF NHSLSPAQER NLEQICKCRV LDRTGLILDI FAQRARTHEG KLQVELAQLR HISTRLIRGW THLERQKGGI GLRGPGETQL ETDRRLLRDR IKTILRRLEK VAKQRDQGRR ARNRAEIPTI SLVGYTNAGK STLFNRVTDA GVYAADQLFA TLDPTLRKID VADVGTSILA DTVGFIRHLP HDLVAAFKAT LKETQDASLL LHVVDASDDR FRENIEAVET VLEEIDANEV PTLVVMNKID NLEGALPRIE RDDAGVPQRV WVSAMEGQGI DLLFDALTER LSGTMVKHTL RLPPQFIGRY RSKFYQLGCI VSEEYDDDGS LKIDIRLPLA EWSRLQKRES TSLDDFIVA // ID A0A0C5WBI6_9FLAO Unreviewed; 406 AA. AC A0A0C5WBI6; DT 29-APR-2015, integrated into UniProtKB/TrEMBL. DT 29-APR-2015, sequence version 1. DT 07-JUN-2017, entry version 15. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=AW14_02650 {ECO:0000313|EMBL:AJR02709.1}; OS Siansivirga zeaxanthinifaciens CC-SAMT-1. OC Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales; OC Flavobacteriaceae; Siansivirga. OX NCBI_TaxID=1454006 {ECO:0000313|EMBL:AJR02709.1, ECO:0000313|Proteomes:UP000032229}; RN [1] {ECO:0000313|EMBL:AJR02709.1, ECO:0000313|Proteomes:UP000032229} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CC-SAMT-1 {ECO:0000313|EMBL:AJR02709.1, RC ECO:0000313|Proteomes:UP000032229}; RA Young C.-C., Hameed A., Huang H.-C., Shahina M.; RL Submitted (FEB-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP007202; AJR02709.1; -; Genomic_DNA. DR RefSeq; WP_044637390.1; NZ_CP007202.1. DR EnsemblBacteria; AJR02709; AJR02709; AW14_02650. DR KEGG; sze:AW14_02650; -. DR PATRIC; fig|1454006.5.peg.505; -. DR KO; K03665; -. DR Proteomes; UP000032229; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000032229}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000032229}. FT DOMAIN 200 385 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 406 AA; 46709 MW; C07BAB85355A304E CRC64; MLEKKDITLE KAVLIGVITK EQDEVKSKEY LDELEFLTYT AGGEVVKRFT QKMEMPNPKT FIGTGKMEDV RLYIEENDIG TAIFDDELSS AQERNISKIL NCKVLDRTNL ILDIFAQRAQ TSYARTQVEL AQCEYLLPRL RGMWTHLERQ KGGIGMRGPG ETEIETDRRI VRDKIALLKE RIKTIDKQMS VQRGNRGAMV RVALVGYTNV GKSTLMNVIS KSEVFAENKL FATLDTTVRK VVIQNLPFLL SDTVGFIRKL PTQLVESFKS TLDEVREADL LLHVVDISHP NYEEHIDSVN KILGEIKSAD KPTIMVFNKI DAYKPEKLDT DDLETEKTTK HYTLEEWKST WMSKVGNNAL FISAINKSNL EDFKKRVYDE VREIHITRFP YNKFLYPDYD ATIDSE // ID A0A0C9N9U6_SPHPI Unreviewed; 381 AA. AC A0A0C9N9U6; DT 29-APR-2015, integrated into UniProtKB/TrEMBL. DT 29-APR-2015, sequence version 1. DT 12-APR-2017, entry version 13. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:GAN12972.1}; GN ORFNames=SP6_14_01280 {ECO:0000313|EMBL:GAN12972.1}; OS Sphingomonas paucimobilis NBRC 13935. OC Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales; OC Sphingomonadaceae; Sphingomonas. OX NCBI_TaxID=1219050 {ECO:0000313|EMBL:GAN12972.1, ECO:0000313|Proteomes:UP000032025}; RN [1] {ECO:0000313|EMBL:GAN12972.1, ECO:0000313|Proteomes:UP000032025} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NBRC 13935 {ECO:0000313|EMBL:GAN12972.1, RC ECO:0000313|Proteomes:UP000032025}; RA Hosoyama A., Hashimoto M., Hosoyama Y., Noguchi M., Uohara A., RA Ohji S., Katano-Makiyama Y., Ichikawa N., Kimura A., Yamazoe A., RA Fujita N.; RT "Whole genome shotgun sequence of Sphingomonas paucimobilis NBRC RT 13935."; RL Submitted (AUG-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:GAN12972.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BBJS01000014; GAN12972.1; -; Genomic_DNA. DR EnsemblBacteria; GAN12972; GAN12972; SP6_14_01280. DR Proteomes; UP000032025; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000032025}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000032025}. FT DOMAIN 159 328 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 381 AA; 42277 MW; 359614449A9A14F3 CRC64; MVERIALRVR SPKPATLIGS GQVEQVAQQV RMEEAQLVVF DGSLTPVQQR NLETTLEAKV IDRTGLILEI FGERAATAEG RLQVELAHLD YQAGRLVRSW THLERQRGGF GFLGGPGETQ IEADRRMIRD RMARLRRELD QVSRTRGLHR DRRQRAPWPI IALVGYTNAG KSTLFNRLTG AHVMAKDLLF ATLDPTLRQI QLPGIDKAIL SDTVGFVSDL PTQLVAAFKA TLEEVVSADL LIHVRDIAHP DSEAQRADVE AVLTEIGVDP ETPRFEAWNK IDLVEGELRE DLLAEAGRRP HIVAVSAMSG EGIDQLVEQV AAALTSGHRR YWITLDAGDG AGAAWLHAHG EVLDQVIEGT EATYEVRLSE SDYERFNRRG A // ID A0A0C9PK82_9BACT Unreviewed; 432 AA. AC A0A0C9PK82; DT 29-APR-2015, integrated into UniProtKB/TrEMBL. DT 29-APR-2015, sequence version 1. DT 07-JUN-2017, entry version 16. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=BROSI_C0010 {ECO:0000313|EMBL:GAN35406.1}; OS Candidatus Brocadia sinica JPN1. OC Bacteria; Planctomycetes; Planctomycetia; Candidatus Brocadiales; OC Candidatus Brocadiaceae; Candidatus Brocadia. OX NCBI_TaxID=1197129 {ECO:0000313|EMBL:GAN35406.1, ECO:0000313|Proteomes:UP000032309}; RN [1] {ECO:0000313|EMBL:GAN35406.1, ECO:0000313|Proteomes:UP000032309} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=JPN1 {ECO:0000313|EMBL:GAN35406.1, RC ECO:0000313|Proteomes:UP000032309}; RA Oshiki M., Shinyako-Hata K., Satoh H., Okabe S.; RT "Draft Genome Sequence of an Anaerobic Ammonium-Oxidizing Bacterium, RT "Candidatus Brocadia sinica"."; RL Genome Announc. 3:e00267-15(2015). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:GAN35406.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BAFN01000003; GAN35406.1; -; Genomic_DNA. DR RefSeq; WP_052566038.1; NZ_BAFN01000003.1. DR Proteomes; UP000032309; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000032309}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000032309}. FT DOMAIN 202 368 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 170 197 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 432 AA; 49236 MW; 7AB8E43F85C03066 CRC64; MKLKDTAFTV RAERAVLFRV MLSGDHSEDE APLEELRRLA KTAGANVVHS VVQKRPNIDP VYYVGKGKAA ELSRISKELD ADVFICDDDL TPAQVRNLEK VIEKKVIDRS ELILDIFATR AKTFQAKLQV ELAQLEYTRP RLKRMWTHLS RIEGGIGTRG PGEKQLEVDK RIVSRKIHDL RKKLHEIEKR QERLVASRKE FFTVSIVGYT NAGKSTLMNV LTEIDTFVED KLFATLDTKT SICKLENGRK ILVSDTVGFI QKLPHHLVSS FKATLEEARH ADLLLHVADI SSPLIQRQVE AVNVVLKELG CDKKPTIIVL NKVDAIKDES LIPLLQSYYR DCIMISAKTH LGIEELKRKI GEILEKNFMD IEITCSPGNG RLIAYLHEHA HVLSSRFEEH RVTFRLLIED KLMQKLRMLD DTIQMKETTG SN // ID A0A0D0GNZ6_9SPHI Unreviewed; 397 AA. AC A0A0D0GNZ6; DT 29-APR-2015, integrated into UniProtKB/TrEMBL. DT 29-APR-2015, sequence version 1. DT 30-AUG-2017, entry version 17. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=TH53_16075 {ECO:0000313|EMBL:KIO76231.1}; OS Pedobacter lusitanus. OC Bacteria; Bacteroidetes; Sphingobacteriia; Sphingobacteriales; OC Sphingobacteriaceae; Pedobacter. OX NCBI_TaxID=1503925 {ECO:0000313|EMBL:KIO76231.1, ECO:0000313|Proteomes:UP000032049}; RN [1] {ECO:0000313|EMBL:KIO76231.1, ECO:0000313|Proteomes:UP000032049} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NL19 {ECO:0000313|EMBL:KIO76231.1, RC ECO:0000313|Proteomes:UP000032049}; RA Santos T., Caetano T., Covas C., Cruz A., Mendo S.; RT "Draft genome sequence of Pedobacter sp. NL19 isolated from sludge of RT an effluent treatment pond in an abandoned uranium mine."; RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KIO76231.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JXRA01000068; KIO76231.1; -; Genomic_DNA. DR RefSeq; WP_041883367.1; NZ_JXRA01000068.1. DR EnsemblBacteria; KIO76231; KIO76231; TH53_16075. DR Proteomes; UP000032049; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000032049}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}. FT DOMAIN 204 386 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 397 AA; 45477 MW; 04393986B7F758AC CRC64; MGKAKTYDTA VKQERAVLVG VIRPGEKPEE TKEYLDELTF LVDTAGGVVD SVFTQKMLKP ERATFVGTGK LEEIRAYVKS EDIDMVVFDD ELSPSQLRNI ERELEVKILD RSNLILDIFA GRAQTSQAKT QVELAQLQYL LPRLTRLWTH LERQKGGIGM RGPGETQIES DRRMILEKIS LLKSRLKLID KQNETQRKNR NELIRVALVG YTNVGKSTIM NMISKSEVFA ENKLFATLDT TVRKVVIDNL PFLLSDTVGF IRKLPHHLVE CFKSTLDEVR EADILIHVVD VSHSSFEDQI NVVNETLKDL GARDKETIVV FNKIDAYVNP EADEMNEEEK VTLTLEDFKK SWMAQHNTPS IFISALNKEN LEEFKQLLYD KVVALHTVRY PYDKLLY // ID A0A0D0ISG1_9MICO Unreviewed; 518 AA. AC A0A0D0ISG1; DT 29-APR-2015, integrated into UniProtKB/TrEMBL. DT 29-APR-2015, sequence version 1. DT 07-JUN-2017, entry version 16. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=SD72_00305 {ECO:0000313|EMBL:KIP53902.1}; OS Leucobacter komagatae. OC Bacteria; Actinobacteria; Micrococcales; Microbacteriaceae; OC Leucobacter. OX NCBI_TaxID=55969 {ECO:0000313|EMBL:KIP53902.1, ECO:0000313|Proteomes:UP000032120}; RN [1] {ECO:0000313|EMBL:KIP53902.1, ECO:0000313|Proteomes:UP000032120} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=VKM ST2845 {ECO:0000313|EMBL:KIP53902.1, RC ECO:0000313|Proteomes:UP000032120}; RA Karlyshev A.V., Kudryashova E.B.; RT "Draft genome sequence of Leucobacter komagatae strain VKM ST2845."; RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KIP53902.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JXSQ01000001; KIP53902.1; -; Genomic_DNA. DR EnsemblBacteria; KIP53902; KIP53902; SD72_00305. DR Proteomes; UP000032120; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 2. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000032120}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000032120}. FT DOMAIN 300 465 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 107 134 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 518 AA; 56134 MW; D0FFE694FA9E53A6 CRC64; MTDASEPEHA ADPADEMTDP LERVLRRAAG AGASVIRDLS EAQALGSSAD DGLGDADHGI QMDREDRASL TRVAGLSTEL EDVTDVEYRQ LRLENVVLIG VYSSSRSQSA QDALEEAENS LRELAALAET AGATVLDGVL QRRANPDPAT YLGKGKAKEL AELVAALGAD TVIADDELGP SQRRVLEDVV NAKVIDRTTV ILDIFSQHAK SREGKAQVEL AQLQYLLPRL RGWGDSMSRQ AGGQVGAAGA GMGSRGPGET KIELDRRRIN TRMARLRKQI AEFAPAREAK RANRKRGEVP SVAIAGYTNA GKSSLLNRLT GTQELVQNQL FATLDTAVRH AETTDGRTFT YVDTVGFVRN LPHQLVEAFR STFEEVGEAD VILHVVDGSH PDPEAQLNTV RGVIAEVDAQ AIPEVVVFNK ADLIDDSRRM LLHGLAPDGV FVSARSGEGI DELKARIDAA LPTPDREVTV VVPYDRGDLV AELHERNRIL ELDYDEAGTR VRALVTPEMF SKLDDFLV // ID A0A0D0LQ14_9NOCA Unreviewed; 488 AA. AC A0A0D0LQ14; DT 29-APR-2015, integrated into UniProtKB/TrEMBL. DT 29-APR-2015, sequence version 1. DT 07-JUN-2017, entry version 17. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=RU01_00975 {ECO:0000313|EMBL:KIQ20669.1}; OS Rhodococcus sp. MEB064. OC Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae; OC Rhodococcus. OX NCBI_TaxID=1587522 {ECO:0000313|EMBL:KIQ20669.1, ECO:0000313|Proteomes:UP000032087}; RN [1] {ECO:0000313|EMBL:KIQ20669.1, ECO:0000313|Proteomes:UP000032087} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MEB064 {ECO:0000313|EMBL:KIQ20669.1, RC ECO:0000313|Proteomes:UP000032087}; RA Perisin M.A., Vetter M., Gilbert J.A., Bergelson J.; RT "16Stimator: statistical estimation of ribosomal gene copy numbers RT from draft genome assemblies."; RL Submitted (DEC-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KIQ20669.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JXQS01000002; KIQ20669.1; -; Genomic_DNA. DR RefSeq; WP_042572615.1; NZ_JXQS01000002.1. DR EnsemblBacteria; KIQ20669; KIQ20669; RU01_00975. DR Proteomes; UP000032087; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000032087}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000032087}. FT DOMAIN 264 433 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 223 257 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 488 AA; 52609 MW; B76C8E463128D9B9 CRC64; MTTTNASAPK SDTTAADTTE PHSEHDAEWS TGDMQLDDRS ALRRVAGLST ELTDVTEVEY RQLRLERVVL VGVWTSGSAE EAESSMTELA ALAETAGSEV LEGLVQRRDR PDASTYIGSG KAKELREVVI ATGADTVVCD GELTPAQLTA LEKIVKVKVI DRTALILDIF AQHASSREGK AQVALAQMEY MLPRLRGWGE SMSRQAGGRA GSNGGVGLRG PGETKIETDR RRIRERMAKL RREIRGMKQA RDTKRERRLT SNVPSIAIVG YTNAGKSSLL NSLTGSGVLV QNALFATLDP TTRKATLEDG RECVLTDTVG FVRHLPTQLV EAFRSTLEEV TDADLLLHVV DGSDPLPVGQ IEAVREVIVS VVREQNTVAP EELIVVNKID AADPVTLTQL RGLLPGAVFV SAKTGEGIEE LRTRLGELVR PPEVSVSVLV PYDRGDLVSR IHADGRIAST THEDGGTRID ATVPTALASQ LTSFAYSA // ID A0A0D0PZ59_9RHOB Unreviewed; 424 AA. AC A0A0D0PZ59; DT 29-APR-2015, integrated into UniProtKB/TrEMBL. DT 29-APR-2015, sequence version 1. DT 05-JUL-2017, entry version 18. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=Wenmar_03788 {ECO:0000313|EMBL:KIQ67659.1}; OS Wenxinia marina DSM 24838. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae; Wenxinia. OX NCBI_TaxID=1123501 {ECO:0000313|EMBL:KIQ67659.1, ECO:0000313|Proteomes:UP000035100}; RN [1] {ECO:0000313|EMBL:KIQ67659.1, ECO:0000313|Proteomes:UP000035100} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 24838 {ECO:0000313|EMBL:KIQ67659.1, RC ECO:0000313|Proteomes:UP000035100}; RA Fiebig A., Goeker M., Klenk H.-P.P.; RL Submitted (JAN-2013) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KIQ67659.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AONG01000021; KIQ67659.1; -; Genomic_DNA. DR EnsemblBacteria; KIQ67659; KIQ67659; Wenmar_03788. DR PATRIC; fig|1123501.6.peg.3917; -. DR Proteomes; UP000035100; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000035100}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Hydrolase {ECO:0000313|EMBL:KIQ67659.1}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000035100}. FT DOMAIN 204 373 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 424 AA; 47390 MW; 663BC1ADB40AEA0F CRC64; MPEHDPPVTR AWVIHPEIRA DRDRREAEPA LDEAVALAAA LPGLDVVGSE IVRLPRRHPG MLFGTGKIEE LKTRLKAAEV ELVLIDGHVG PVQQRNLEKE WGVKLLDRTG LILEIFSDRA RTREGVLQVE MAALTYQRTR LVRAWTHLER QRGGLGFVGG PGETQIEADR RAIDEQLVRL KRQLEKVVKT RTLHREARAK VPFPIVALVG YTNAGKSTLF NRLTGSEVFA KDMLFATLDP TMRRIALPTG EDIILSDTVG FISDLPTELV AAFRATLEEV LDADLVCHVR DISHPQTEEQ AEDVAAILTS LGVGEATPQI EVWNKIDLIP ADERDAAFAR AGRRGEIHAI SALTGEGVAE LMVAIAERLR PPTVTDTIRL SFAAGRERAW LHEEGVVEDE RQTDEGYSLT VRWTERQKDR FRRL // ID A0A0D0Q091_KITGR Unreviewed; 499 AA. AC A0A0D0Q091; DT 29-APR-2015, integrated into UniProtKB/TrEMBL. DT 29-APR-2015, sequence version 1. DT 07-JUN-2017, entry version 17. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=TR51_08250 {ECO:0000313|EMBL:KIQ64343.1}; OS Kitasatospora griseola (Streptomyces griseolosporeus). OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae; OC Kitasatospora. OX NCBI_TaxID=2064 {ECO:0000313|EMBL:KIQ64343.1, ECO:0000313|Proteomes:UP000032066}; RN [1] {ECO:0000313|EMBL:KIQ64343.1, ECO:0000313|Proteomes:UP000032066} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MF730-N6 {ECO:0000313|EMBL:KIQ64343.1, RC ECO:0000313|Proteomes:UP000032066}; RA Arens J.C., Haltli B., Kerr R.G.; RT "Draft genome sequence of Kitasatospora griseola MF730-N6, a RT bafilomycin, terpentecin and satosporin producer."; RL Submitted (FEB-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KIQ64343.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JXZB01000002; KIQ64343.1; -; Genomic_DNA. DR RefSeq; WP_043909802.1; NZ_JXZB01000002.1. DR EnsemblBacteria; KIQ64343; KIQ64343; TR51_08250. DR PATRIC; fig|2064.6.peg.1759; -. DR Proteomes; UP000032066; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 2. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000313|EMBL:KIQ64343.1}; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000032066}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900, KW ECO:0000313|EMBL:KIQ64343.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000032066}. FT DOMAIN 278 443 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 237 271 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 499 AA; 54211 MW; 6D8F95AEA1F6387A CRC64; MTSTFDSRTR SSESANRLAD LKAEALMDED LAAIDEGLGN YDGEQYDRSE RAALRRVAGL STELQDVTEV EYRQLRLERV VLVGVWTDGT LEEAENSMAE LAALAETAGS EVLDGVIQRR DKPDAATYIG SGKAQELRDL VASTGADTVV CDGELTPGQL IHLEDVVKVK VVDRTALILD IFAQHAKSRE GKAQVSLAQM QYMLPRLRGW GQSLSRQMGG GGSGTSGGGM ATRGPGETKI ETDRRRIREK MAKLRKEIAE MKKGRDTKRQ ERRRHQVPSV AIAGYTNAGK SSLLNRLTGA GVLVENALFA TLDPTVRRAQ TPSGRLYTLA DTVGFVRHLP HHLVEAFRST MEEVADADLI LHVVDGSHPE PETQLASVRE VIVSVEAQNV PEIVVINKAD AADPAVLQRL LRREPHAIVV SARSGQGIDE LLALIDEELP RPAVEVRALV PYTRGDLVSR VHAEGELLSA EHTAEGTLLH AKVAAVLAAE LERYAVVTA // ID A0A0D0R9E3_9GAMM Unreviewed; 435 AA. AC A0A0D0R9E3; DT 29-APR-2015, integrated into UniProtKB/TrEMBL. DT 29-APR-2015, sequence version 1. DT 07-JUN-2017, entry version 17. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=TI01_0252 {ECO:0000313|EMBL:KIQ98154.1}; OS Lysobacter sp. A03. OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales; OC Xanthomonadaceae; Lysobacter. OX NCBI_TaxID=1199154 {ECO:0000313|EMBL:KIQ98154.1, ECO:0000313|Proteomes:UP000032077}; RN [1] {ECO:0000313|EMBL:KIQ98154.1, ECO:0000313|Proteomes:UP000032077} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=A03 {ECO:0000313|EMBL:KIQ98154.1, RC ECO:0000313|Proteomes:UP000032077}; RA Pereira J.Q., Ambrosini A., Sant'Anna F.H., Tadra-Sfeir M., Faoro H., RA Pedrosa F.O., de Souza E.M., Brandelli A., Passaglia L.M.; RT "Genome sequence of Lysobacter sp. A03."; RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KIQ98154.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JXSS01000021; KIQ98154.1; -; Genomic_DNA. DR RefSeq; WP_043957432.1; NZ_JXSS01000021.1. DR EnsemblBacteria; KIQ98154; KIQ98154; TI01_0252. DR PATRIC; fig|1199154.3.peg.1000; -. DR Proteomes; UP000032077; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000032077}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000032077}. FT DOMAIN 199 364 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 158 192 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 435 AA; 48039 MW; 38FCB34A6CF756D8 CRC64; MFERSRKGES ALLIQPHAGG PVDEDQLEEF TELARSAGAT VVATLNARID HPNASILIGT GKLEEVQAAV AATEADLVLV NHPLSPVQER NLERILGCRV VDRTGLILDI FAQRARSHEG KLQVELAQLK HMSTRLVRGW THLDSLRGGS IGLRGPGETQ LETDRRLLQK RLEQLQKRLE KVEVQRTQMR RARVRNELPR VALVGYTNAG KSTLFNALTG ADAYAADQLF ATLDPTVRRI ELSGHAMVLA DTVGFVRDLP HELVAAFRST LSEAREADLL LHLVDAADPL REERIAQVDE VLAEIGAGDI PQLLVYNKID QLEQAKPRVD RPSEGHPRVW VSAKEREGLD LLPEAIGEIL DLQRVTGSIE VPSRAGKLHA KLHELGAVRD EVSVEDGWRM QVDMSLADAA RLHEQPDGDV LHALLPPPEA DHDLH // ID A0A0D0RFW9_9FIRM Unreviewed; 407 AA. AC A0A0D0RFW9; DT 29-APR-2015, integrated into UniProtKB/TrEMBL. DT 29-APR-2015, sequence version 1. DT 07-JUN-2017, entry version 17. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=P261_01869 {ECO:0000313|EMBL:KIR03054.1}; OS Lachnospiraceae bacterium TWA4. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Lachnospiraceae. OX NCBI_TaxID=1392836 {ECO:0000313|EMBL:KIR03054.1, ECO:0000313|Proteomes:UP000032079}; RN [1] {ECO:0000313|EMBL:KIR03054.1, ECO:0000313|Proteomes:UP000032079} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=TWA4 {ECO:0000313|EMBL:KIR03054.1, RC ECO:0000313|Proteomes:UP000032079}; RX PubMed=25495654; RA Gagen E.J., Wang J., Padmanabha J., Liu J., de Carvalho I., Liu J., RA Webb R.I., Al Jassim R., Morrison M., Denman S.E., McSweeney C.S.; RT "Investigation of a new acetogen isolated from an enrichment of the RT tammar wallaby forestomach."; RL BMC Microbiol. 14:314-314(2014). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KIR03054.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JPZU01000001; KIR03054.1; -; Genomic_DNA. DR RefSeq; WP_042736234.1; NZ_JPZU01000001.1. DR EnsemblBacteria; KIR03054; KIR03054; P261_01869. DR PATRIC; fig|1392836.3.peg.2123; -. DR Proteomes; UP000032079; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000032079}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000032079}. FT DOMAIN 193 357 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 407 AA; 46075 MW; 0D987049445D145F CRC64; MFENKEEKER LILVGIGEES SLDELEELIY TAKATVVGRM LQNREMVHPG TYLGSGKLQE LRELIEELDA TGIVCDDELS PAQIRNMEDV LQIKILDRTL VILDIFAARA NTHEGKIQVE LAQLKYRATR LVGMRRSLSR LGGGIGTRGP GEKKLEMDRR LIHNRISQLK AELKEVMTHR EITRGRRDKN KIPVIALVGY TNAGKSTLFN YLTGAGVLEE DKLFATLDPA VRQVELEEGQ KILLTDTVGF IHKLPHHLVE AFRSTLEEAK YADIILHVVD TTSPQMEMHM HVVYETLAEL GVVDKPILTV FNKIDLLEQP QVLKDLKAKK TFQISAKTGR GVDALLAGIN EELTKNQVYV EKLFPYERVG EIQVIRQYGQ LLSEEYTEDG VVVTAYVPIE IYNKYNI // ID A0A0D0VYA6_9ACTN Unreviewed; 483 AA. AC A0A0D0VYA6; DT 29-APR-2015, integrated into UniProtKB/TrEMBL. DT 29-APR-2015, sequence version 1. DT 07-JUN-2017, entry version 17. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=TK50_09985 {ECO:0000313|EMBL:KIR65678.1}; OS Micromonospora carbonacea. OC Bacteria; Actinobacteria; Micromonosporales; Micromonosporaceae; OC Micromonospora. OX NCBI_TaxID=47853 {ECO:0000313|EMBL:KIR65678.1, ECO:0000313|Proteomes:UP000032254}; RN [1] {ECO:0000313|EMBL:KIR65678.1, ECO:0000313|Proteomes:UP000032254} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=JXNU-1 {ECO:0000313|EMBL:KIR65678.1, RC ECO:0000313|Proteomes:UP000032254}; RA Long Z., Huang Y., Jiang Y.; RT "Sequencing and annotation of Micromonospora carbonacea strain JXNU-1 RT genome."; RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KIR65678.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JXSX01000001; KIR65678.1; -; Genomic_DNA. DR RefSeq; WP_043962486.1; NZ_JXSX01000001.1. DR EnsemblBacteria; KIR65678; KIR65678; TK50_09985. DR PATRIC; fig|47853.6.peg.2125; -. DR Proteomes; UP000032254; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000313|EMBL:KIR65678.1}; KW Complete proteome {ECO:0000313|Proteomes:UP000032254}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900, KW ECO:0000313|EMBL:KIR65678.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000032254}. FT DOMAIN 255 420 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 483 AA; 52753 MW; F8381D8D84E3A4AE CRC64; MRDQETYVPF TDDELEATTG EFELSERQAL RRVPGLSTEL TDITEVEYRQ LRLERVVLVG VWTEGTQTDA ENSLTELAQL AETAGSQVLE GLIQRRSRPD PATYIGRGKV DDLGAVVLAS GADTVICDGE LSPSQLRNLE QRTKVKVVDR TALILDIFAQ HAKSKEGRAQ VELAQLEYLL PRLRGWGETL SRQTGGSGRG GGAGGGVGVR GPGETKLETD RRRIRHRISR LRREIKAMRT VRQTKRARRS RNAVPAVAIA GYTNAGKSSL LNRLTGAGVL VENALFATLD PTTRKATAPD GRIYTLSDTV GFVRHLPHQI VEAFRSTLEE VAESDLVVHV VDGTHPDPEE QVRAVREVLA EVGADRLPEL LVVNKTDAAD EETLLRLKRL WPDAVFASAR SGRGIDEVRA AIETRLPSPA VEVRAVLPYD RGALVARVHR QGEVLSSAHL PEGTMLHVRV SEALAAELAP FATDEGRVAA AAR // ID A0A0D1A7Z7_9LACO Unreviewed; 424 AA. AC A0A0D1A7Z7; DT 29-APR-2015, integrated into UniProtKB/TrEMBL. DT 29-APR-2015, sequence version 1. DT 07-JUN-2017, entry version 17. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:KIS03950.1}; GN ORFNames=WDC_0402 {ECO:0000313|EMBL:KIS03950.1}; OS Lactobacillus wasatchensis. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; OC Lactobacillus. OX NCBI_TaxID=1335616 {ECO:0000313|EMBL:KIS03950.1, ECO:0000313|Proteomes:UP000032279}; RN [1] {ECO:0000313|EMBL:KIS03950.1, ECO:0000313|Proteomes:UP000032279} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=WDC04 {ECO:0000313|EMBL:KIS03950.1, RC ECO:0000313|Proteomes:UP000032279}; RA Oberg C.J., Culumber M., McMahon D.J., Broadbent J.R., Oberg T.S., RA Ortaki F.; RT "Lactobacillus wasatchii sp. WDC04, a late gas producing bacteria RT isolated from aged chedder cheese."; RL Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KIS03950.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AWTT01000006; KIS03950.1; -; Genomic_DNA. DR RefSeq; WP_044010131.1; NZ_AWTT01000006.1. DR EnsemblBacteria; KIS03950; KIS03950; WDC_0402. DR PATRIC; fig|1335616.4.peg.403; -. DR Proteomes; UP000032279; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000032279}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000032279}. FT DOMAIN 202 371 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 424 AA; 47238 MW; 2CCF349E19781DFB CRC64; METTQATQPV IIAGLNNNQA NFDYSMSELG NLVAANQMTV AETMIQNLER PNPATYFGKG KVEELTQLAA SLAVDTVVVN DELTPSQIRN LEEQSKVRII DRTALILEIF AQRAQTKEAK LQVEIAQLQY RLPRLRTSVN QRLDQQTGAG GGSFTNRGAG ETKLEMNRRT IKNSISHLRA ELNEIDKSAV TRRAQRDKND IPNAALVGYT NAGKSTIMNG LIKLFGIDDD KQVFEKDMLF ATLDTSVRQL TLPDNKQFLL SDTVGFVSQL PTHLVEAFKS TLAEAAQADL LIQVIDYSDP HYKEMMQTTA DTLAEIGIKD IPTINVFNKA DKLTIEYPAL EGDDQIVLSA QDPKSLQMLV DLIRQHLFKN FVTADLLIPF SNGDVVSFLN DQANIIKTEY LANGTKLKVE LSKVDLERFK QYVV // ID A0A0D1CPW0_9SPHN Unreviewed; 469 AA. AC A0A0D1CPW0; DT 29-APR-2015, integrated into UniProtKB/TrEMBL. DT 29-APR-2015, sequence version 1. DT 07-JUN-2017, entry version 16. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=TQ38_08680 {ECO:0000313|EMBL:KIS33461.1}; OS Novosphingobium sp. P6W. OC Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales; OC Sphingomonadaceae; Novosphingobium. OX NCBI_TaxID=1609758 {ECO:0000313|EMBL:KIS33461.1, ECO:0000313|Proteomes:UP000032296}; RN [1] {ECO:0000313|EMBL:KIS33461.1, ECO:0000313|Proteomes:UP000032296} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=P6W {ECO:0000313|EMBL:KIS33461.1, RC ECO:0000313|Proteomes:UP000032296}; RA Gogoleva N.E., Nikolaichik Y.A., Shlykova L.V., Gorshkov V.Y., RA Safronova V.I., Belimov A., Gogolev Y.V.; RT "The Draft Genome Sequence of the Abscisic Acid Degrading Bacterium RT Novosphingobium sp. Strain P6W."; RL Submitted (FEB-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KIS33461.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JXZE01000003; KIS33461.1; -; Genomic_DNA. DR EnsemblBacteria; KIS33461; KIS33461; TQ38_08680. DR PATRIC; fig|1609758.3.peg.3455; -. DR Proteomes; UP000032296; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000032296}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000032296}. FT DOMAIN 210 413 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 469 AA; 52150 MW; 990E078E29A64A03 CRC64; MNDELMDEVT RGARALVVYP QMRGPRGQMS DLDVDARLEE AKGLALAIGL EVVEAMAIVI REPRAATLFG EGQIQNISVA CTLNEAELII VDGSLTAIQQ RNLEEKLKRK VIDRTGLILE IFGERAATAE GRLQVELAHL DYQAGRLVRS WTHLERQRGG FGFLGGPGET QIEADRRLIR DRMAKIRREL EQVRRTRGLH RDRREKAPWP IVALVGYTNA GKSTLFNRLT GAEVMAEDLL FATLDPTMRA VRLPGLEKAI LSDTVGFISD LPTQLVAAFR ATLEEVTAAD VIVHVRDMAN PDTEAQKRQV LDILADLGVM EPKIDERALR RKEQDDRVIG WGRDDEEEEG PAPLIPIIEV WNKWDLLDPE QIEALREAMS HRDGETIIPV SALTGEGCEN MLAVVSRTLT LGSKVYSFVI PAADGQRLAF LHARGEVVAE EDAGEGEEGP LLRIQARLSE RELGRFTSL // ID A0A0D1EKU0_9RHOB Unreviewed; 464 AA. AC A0A0D1EKU0; DT 29-APR-2015, integrated into UniProtKB/TrEMBL. DT 29-APR-2015, sequence version 1. DT 07-JUN-2017, entry version 14. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:KIT18199.1}; GN ORFNames=jaqu_00620 {ECO:0000313|EMBL:KIT18199.1}; OS Jannaschia aquimarina. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae; Jannaschia. OX NCBI_TaxID=935700 {ECO:0000313|EMBL:KIT18199.1, ECO:0000313|Proteomes:UP000032232}; RN [1] {ECO:0000313|EMBL:KIT18199.1, ECO:0000313|Proteomes:UP000032232} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=GSW-M26 {ECO:0000313|EMBL:KIT18199.1, RC ECO:0000313|Proteomes:UP000032232}; RA Voget S., Daniel R.; RT "Genome Sequence of Jannaschia aquimarina DSM28248, a member of the RT Roseobacter clade."; RL Submitted (FEB-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KIT18199.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JYFE01000002; KIT18199.1; -; Genomic_DNA. DR EnsemblBacteria; KIT18199; KIT18199; jaqu_00620. DR PATRIC; fig|935700.4.peg.65; -. DR Proteomes; UP000032232; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000032232}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000032232}. FT DOMAIN 216 386 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 464 AA; 50641 MW; 8EF5ACEFB944498A CRC64; MARRRPLAKP EPHSTEARPT RALVLHPDTR AGDRSGREPA DALAEAVSLA AALPGLKVVG SDVVRLPRPH PGMLFGSGKV EELRARIEAD EIELILIDGP VTPVQQRNLE RAWKVKLLDR TSLILEIFAD RAATREGVLQ VELAALSYQR TRLVRAWTHL ERQRGGLGFV GGPGETQIEA DRRAIDEQIV RIRKQLEKVT KTRELHRAAR AKVPYPIVAF VGYTNAGKST LFNRLTGAEV MAKDMLFATL DPTMRAVRLP GGGPETILSD TVGFISDLPT QLVAAFRATL EEVLAANLIL HVRDISHPET EAQAGDVAAI LEDLGVRDEV PVLELWNKAD TLDAEARETA TNRAARSETI FLGSALTGEG LDPLMAAIAE HLSGLRRPAI LTVPYSEGAA RAWLHDADVI DSEAQQDEAW HVTVSWTDDQ AAAFAREFPA LAPKTEAQTV ETAAPRSEPW SPLD // ID A0A0D1JU01_9MYCO Unreviewed; 470 AA. AC A0A0D1JU01; DT 29-APR-2015, integrated into UniProtKB/TrEMBL. DT 29-APR-2015, sequence version 1. DT 07-JUN-2017, entry version 17. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=TL10_15075 {ECO:0000313|EMBL:KIU16044.1}; OS Mycobacterium llatzerense. OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae; OC Mycobacterium. OX NCBI_TaxID=280871 {ECO:0000313|EMBL:KIU16044.1, ECO:0000313|Proteomes:UP000032221}; RN [1] {ECO:0000313|EMBL:KIU16044.1, ECO:0000313|Proteomes:UP000032221} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CLUC14 {ECO:0000313|EMBL:KIU16044.1, RC ECO:0000313|Proteomes:UP000032221}; RA Greninger A.L., Langelier C., Cunningham G., Chiu C.Y., Miller S.; RT "Genome sequence of Mycobacterium llatzerense and Mycobacterium RT immunogenum recovered from brain abscess."; RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KIU16044.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JXST01000020; KIU16044.1; -; Genomic_DNA. DR RefSeq; WP_043986226.1; NZ_JXST01000020.1. DR EnsemblBacteria; KIU16044; KIU16044; TL10_15075. DR PATRIC; fig|280871.6.peg.3130; -. DR Proteomes; UP000032221; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000313|EMBL:KIU16044.1}; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000032221}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900, KW ECO:0000313|EMBL:KIU16044.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000032221}. FT DOMAIN 247 416 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 206 233 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 470 AA; 50605 MW; 1B20CEA9BC923AE6 CRC64; MTYPFDPDNT PSVGELALED RAALRRVAGL STELADISEV EYRQLRLERV VLVGVWTDGT SADADNSLAE LAALAETAGS EVLEGLIQRR NKPDASTYIG SGKALELRET VLATGADTVI CDGELSPAQL NSLEKVVKVK VIDRTALILD IFAQHATSRE GKAQVSLAQM EYMLPRLRGW GESMSRQAGG RAGGAGGGVG TRGPGETKIE TDRRRIRERM SKLRREIKDM KKIRDTQRHS RRASDAPSVA IVGYTNAGKS SLLNALTGAG VLVQNALFAT LEPTTRRGQL DDGRPFTLTD TVGFVRHLPT QLVEAFRSTL EEVVDADLLV HVVDGADADP LAQINAVRKV VGEVVAEYDV AAPRELLVVN KIDAAGDLAL AHLRRALPDA VFVSAHTGEG LDRLRLRMCE LVEPTDAAVD VTIPYDRGDL VARVHAEGRV EATEHTADGT RIKGWVPMAL AASLGEFVTA // ID A0A0D1LER8_9LACT Unreviewed; 427 AA. AC A0A0D1LER8; DT 29-APR-2015, integrated into UniProtKB/TrEMBL. DT 29-APR-2015, sequence version 1. DT 07-JUN-2017, entry version 16. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:KIU19080.1}; GN ORFNames=QX99_02107 {ECO:0000313|EMBL:KIU19080.1}; OS Weissella cibaria. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Leuconostocaceae; OC Weissella. OX NCBI_TaxID=137591 {ECO:0000313|EMBL:KIU19080.1, ECO:0000313|Proteomes:UP000032287}; RN [1] {ECO:0000313|EMBL:KIU19080.1, ECO:0000313|Proteomes:UP000032287} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MG1 {ECO:0000313|EMBL:KIU19080.1, RC ECO:0000313|Proteomes:UP000032287}; RX PubMed=25678547; RA Lynch K.M., Lucid A., Arendt E.K., Sleator R.D., Lucey B., Coffey A.; RT "Genomics of the Weissella cibaria species with an examination of its RT metabolic traits."; RL Microbiology (Mosc.) 0:0-0(2015). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KIU19080.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JWHU01000042; KIU19080.1; -; Genomic_DNA. DR STRING; 911104.WcibK1_010100000662; -. DR EnsemblBacteria; KIU19080; KIU19080; QX99_02107. DR PATRIC; fig|137591.25.peg.2073; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR Proteomes; UP000032287; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000032287}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000032287}. FT DOMAIN 204 373 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 427 AA; 47492 MW; C81843D1D97EA007 CRC64; MIENELHPVR KVILAGLDRQ NAEFDYEMIE LANLAEANYM EVVGTVTQKL ERPNAATYFG KGKVEELKEA VEYYEADMVV TNDELSPSQI RNLESGTGAG IMDRTALILD IFASRAKTKV AKLQVAIAQL QYQLPRLRTS MNVRLDQQTG GGGGSFTSRG AGETKLETNR RHIEHQISLL RQELKDVEAD DQTRRARREK ESIKNVALVG YTNAGKSTIM NGLVRRYGEN QDKTVFQADM LFATLETSVR KLNLPDNQNF LLSDTVGFVS KLPHGLVAAF RATLAEAAQA DLLLQVVDYA DENYKEMMST TAKTLKEIGV GDIPMITIYN KADKIEGMSF PDRDGDTLTL SAQDDASLDM LIEVIRQHIY SDHVQTKVLI PFEQGQLVSE LNEQASVHSI DYVEAGTMMD VTLTPVQAAR FAAYVVD // ID A0A0D1NNZ6_PSEPU Unreviewed; 443 AA. AC A0A0D1NNZ6; DT 29-APR-2015, integrated into UniProtKB/TrEMBL. DT 29-APR-2015, sequence version 1. DT 30-AUG-2017, entry version 20. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=QV12_21395 {ECO:0000313|EMBL:KIU46575.1}; OS Pseudomonas putida (Arthrobacter siderocapsulatus). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=303 {ECO:0000313|EMBL:KIU46575.1, ECO:0000313|Proteomes:UP000032298}; RN [1] {ECO:0000313|EMBL:KIU46575.1, ECO:0000313|Proteomes:UP000032298} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=UASWS0946 {ECO:0000313|EMBL:KIU46575.1, RC ECO:0000313|Proteomes:UP000032298}; RA Crovadore J., Chablais R., Cochard B., Calmin G., Lefort F.; RT "Characterization of nitrifying bacteria from sewage sludge usable in RT agronomy."; RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KIU46575.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JXOG01000185; KIU46575.1; -; Genomic_DNA. DR RefSeq; WP_043863534.1; NZ_JXOG01000185.1. DR EnsemblBacteria; KIU46575; KIU46575; QV12_21395. DR PATRIC; fig|303.170.peg.4276; -. DR Proteomes; UP000032298; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000032298}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000032298}. FT DOMAIN 199 366 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 443 AA; 49972 MW; DCB50440CE401E03 CRC64; MFFERHGGGE RAILVHLEGQ SPEAREDPQE FRELALSAGA DIVAFANVAR HQPTAKFLIG SGKVEEFRDL VKAEQADLVI FNHTLTPSQE RNLERVFECR VLDRTGLILD IFAQRARTHE GKLQVELAQL EHMSTRLVRG WTHLERQKGG IGLRGPGETQ LETDRRLLRI RLRQIKGRLE KVRSQREQAR RGRKRADIPS VSLVGYTNAG KSTLFNALTQ SEVYAADQLF ATLDPTLRRL ELDDVGPVVL ADTVGFIRHL PHKLVEAFRA TLEESSNSDL LLHVIDAHEP ERMEQIEQVM AVLGEIGAEG LPILEVYNKL DLLEGVEPQI QRDADGKPQR VWVSARDGRG LELVGQAIAE LLGDDLFIGT LRLEQRFARL RALFFDLGAV QSEDHDEDGN TLLAVRLSRV EFNRLVSREG MKPLEFIEQH TLQYKPDLAV GQP // ID A0A0D1NTK0_BRAEL Unreviewed; 464 AA. AC A0A0D1NTK0; DT 29-APR-2015, integrated into UniProtKB/TrEMBL. DT 29-APR-2015, sequence version 1. DT 07-JUN-2017, entry version 17. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=QU41_14880 {ECO:0000313|EMBL:KIU48265.1}; OS Bradyrhizobium elkanii. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Bradyrhizobiaceae; Bradyrhizobium. OX NCBI_TaxID=29448 {ECO:0000313|EMBL:KIU48265.1, ECO:0000313|Proteomes:UP000032215}; RN [1] {ECO:0000313|EMBL:KIU48265.1, ECO:0000313|Proteomes:UP000032215} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=UASWS1015 {ECO:0000313|EMBL:KIU48265.1, RC ECO:0000313|Proteomes:UP000032215}; RA Crovadore J., Chablais R., Cochard B., Calmin G., Lefort F.; RT "Characterization of nitrifying bacteria from sewage sludge usable in RT agronomy."; RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KIU48265.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JXOF01000177; KIU48265.1; -; Genomic_DNA. DR RefSeq; WP_024584175.1; NZ_JXOF01000177.1. DR EnsemblBacteria; KIU48265; KIU48265; QU41_14880. DR PATRIC; fig|29448.7.peg.3092; -. DR Proteomes; UP000032215; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000032215}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000032215}. FT DOMAIN 229 405 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 464 AA; 51279 MW; 8FC2C8EC272637E3 CRC64; MEPFDREGGA ERTKSRPGSA GDTGTGRVIV IGPYLRTRRG DGDAQTESSV RDYEARIEEA AGLAGAIDLT VVESVIAPIS QIRPATYLGK GKVEEINGLV ASNKVELVVM DCALSPIQQR NLEKAWSTKV LDRTGLILEI FGRRAKTKEG ALQVELAHLN YQRSRLVRSW THLERQRGGF GFMGGPGETQ IEADRRLISE RITKLEGELK KVQATRRLHR AGRQRVPYRV VALVGYTNAG KSTLFNRLTR ADVQAADMLF ATLDPTLRAL SLPHGGKAML SDTVGFISNL PTQLVAAFRA TLEEVLEADI ILHVRDISHE DAEAQERDVE GVLRQLGIDA DADGGQRIIE VWNKIDRFDP EERDNLRNIA ARRPPERPCF LVSAVTGEGI DALLTAIEDR LAAKRITLDL SIDAADGAGI SWLHRNAEVL SKELRGERFD MTVRVDETKR DIVMSRFDAL PHGT // ID A0A0D1Y6X8_ANEMI Unreviewed; 419 AA. AC A0A0D1Y6X8; DT 29-APR-2015, integrated into UniProtKB/TrEMBL. DT 29-APR-2015, sequence version 1. DT 07-JUN-2017, entry version 21. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=AF333_18970 {ECO:0000313|EMBL:KON97237.1}; OS Aneurinibacillus migulanus (Bacillus migulanus). OC Bacteria; Firmicutes; Bacilli; Bacillales; Paenibacillaceae; OC Aneurinibacillus group; Aneurinibacillus. OX NCBI_TaxID=47500 {ECO:0000313|EMBL:KON97237.1, ECO:0000313|Proteomes:UP000037269}; RN [1] {ECO:0000313|EMBL:KON97237.1, ECO:0000313|Proteomes:UP000037269} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 2895 {ECO:0000313|EMBL:KON97237.1, RC ECO:0000313|Proteomes:UP000037269}; RA Liu B., Wang J., Zhu Y., Liu G., Chen Q., Chen Z., Lan J., Che J., RA Ge C., Shi H., Pan Z., Liu X.; RT "Fjat-14205 dsm 2895."; RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KON97237.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LGUG01000004; KON97237.1; -; Genomic_DNA. DR RefSeq; WP_043063333.1; NZ_LGUG01000004.1. DR EnsemblBacteria; KON97237; KON97237; AF333_18970. DR PATRIC; fig|47500.8.peg.5855; -. DR Proteomes; UP000037269; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000037269}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000037269}. FT DOMAIN 200 362 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 419 AA; 47774 MW; 090360F12D57F313 CRC64; MVDEQKTERA ILVGYYKKSG DQRQFELSME ELAELAHTAE AEVVATLTQG RDQVDSRLYV GKGKVEEINV LVQELEADLV IFNDELTPMQ IRNLEHIIEC KVIDRTQLIL DIFAQRARSR EGKWQVELAQ LQYRLPRLTG KGAELSRLGA GIGTRGPGET KLETDRRHIR RRISEIEGHL AEVKRHRQLY RERRKKNAVF QVAIVGYTNA GKSTILNRLT DAGILEENKL FATLDPTSRR VNLPGGEEII VTDTVGFIQH LPHQLVAAFR STLEEAAEAD LILQVIDASH PDYQIHMEVV DEVLTELGAE SIPRLTVFNK MDRVEERPIS AVSGKVLYLS AYVEEDMQRL LQAIEAHIES QYNRYVLRLP TERGDLYALV RRNLHVLREK IGEDGMYYEL EVKGKGIEQL SPELVTFLS // ID A0A0D2GJ77_9DELT Unreviewed; 546 AA. AC A0A0D2GJ77; DT 29-APR-2015, integrated into UniProtKB/TrEMBL. DT 29-APR-2015, sequence version 1. DT 05-JUL-2017, entry version 18. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=X474_06820 {ECO:0000313|EMBL:KIX14852.1}; OS Dethiosulfatarculus sandiegensis. OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfarculales; OC Desulfarculaceae; Dethiosulfatarculus. OX NCBI_TaxID=1429043 {ECO:0000313|EMBL:KIX14852.1, ECO:0000313|Proteomes:UP000032233}; RN [1] {ECO:0000313|EMBL:KIX14852.1, ECO:0000313|Proteomes:UP000032233} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SPR {ECO:0000313|EMBL:KIX14852.1, RC ECO:0000313|Proteomes:UP000032233}; RA Davidova I.A., Callaghan A.V., Wawrik B., Pruitt S., Marks C., RA Duncan K.E., Suflita J.M.; RT "Metagenomic analysis of a methanogenic consortium involved in long RT chain n-alkane degradation."; RL Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KIX14852.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AZAC01000008; KIX14852.1; -; Genomic_DNA. DR EnsemblBacteria; KIX14852; KIX14852; X474_06820. DR PATRIC; fig|1429043.3.peg.1447; -. DR Proteomes; UP000032233; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000032233}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000032233}. FT DOMAIN 380 546 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 339 373 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 546 AA; 60846 MW; 98B532409393B826 CRC64; MAAKVLGNTT GIKASHLKRL NNFYRRRMSP AELILAEQAR DLSRLSFEIG RQIGLLISRK GEVMQVVVGE PELLPLPFMS RLRRGRTRLA GYHLLHTRLN AKGLNRGDVN LLANRRLDFV ASLEVNSEGL AGDIFLAHIL PEPQGDSDYR LLDPFRAGYP PEDISRLVWS LEQELNRLSE TMDVEKSGSA VLVSVTTKPR RIARESLDEL EELAGSAGLL VKGKIIQTRP KLNPRTIIGP GKLDEVLIFC LRQGADVIIF DQELNPSQAH SLARLTNSEI KFLDRTQLIL DIFAQRALTR EGKLQVEMAQ LRYLGPRLGS RDDGLSRLTG GIGGRGPGET KLEIDRRRVR TRLNRLENEL QKVAKQRKNR RSRRKKMGLP IISIVGYTNA GKSTLLNALT GSKVLSQDRL FATLDPTTRR LRFPEEQEVI ITDTVGFIRD LPKDLKKAFA ATLEELHQAD LLLHLADASH PQVDQQIKAV TGILNDLDLN ETPALLVLNK KDLTPPDVLE RLSNQYPEAA VISALDAATL PVLLKALQGM VKGLNC // ID A0A0D2SPW1_GOSRA Unreviewed; 433 AA. AC A0A0D2SPW1; DT 29-APR-2015, integrated into UniProtKB/TrEMBL. DT 29-APR-2015, sequence version 1. DT 07-JUN-2017, entry version 13. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:KJB43971.1}; GN ORFNames=B456_007G227000 {ECO:0000313|EMBL:KJB43971.1}; OS Gossypium raimondii (New World cotton). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae; OC Pentapetalae; rosids; malvids; Malvales; Malvaceae; Malvoideae; OC Gossypium. OX NCBI_TaxID=29730 {ECO:0000313|EMBL:KJB43971.1, ECO:0000313|Proteomes:UP000032304}; RN [1] {ECO:0000313|EMBL:KJB43971.1, ECO:0000313|Proteomes:UP000032304} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=23257886; DOI=10.1038/nature11798; RA Paterson A.H., Wendel J.F., Gundlach H., Guo H., Jenkins J., Jin D., RA Llewellyn D., Showmaker K.C., Shu S., Udall J., Yoo M.J., Byers R., RA Chen W., Doron-Faigenboim A., Duke M.V., Gong L., Grimwood J., RA Grover C., Grupp K., Hu G., Lee T.H., Li J., Lin L., Liu T., RA Marler B.S., Page J.T., Roberts A.W., Romanel E., Sanders W.S., RA Szadkowski E., Tan X., Tang H., Xu C., Wang J., Wang Z., Zhang D., RA Zhang L., Ashrafi H., Bedon F., Bowers J.E., Brubaker C.L., Chee P.W., RA Das S., Gingle A.R., Haigler C.H., Harker D., Hoffmann L.V., Hovav R., RA Jones D.C., Lemke C., Mansoor S., ur Rahman M., Rainville L.N., RA Rambani A., Reddy U.K., Rong J.K., Saranga Y., Scheffler B.E., RA Scheffler J.A., Stelly D.M., Triplett B.A., Van Deynze A., RA Vaslin M.F., Waghmare V.N., Walford S.A., Wright R.J., Zaki E.A., RA Zhang T., Dennis E.S., Mayer K.F., Peterson D.G., Rokhsar D.S., RA Wang X., Schmutz J.; RT "Repeated polyploidization of Gossypium genomes and the evolution of RT spinnable cotton fibres."; RL Nature 492:423-427(2012). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CM001746; KJB43971.1; -; Genomic_DNA. DR Proteomes; UP000032304; Chromosome 7. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR CDD; cd01878; HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000032304}; KW Reference proteome {ECO:0000313|Proteomes:UP000032304}. FT DOMAIN 293 433 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 433 AA; 47948 MW; 03A568D79CE159B8 CRC64; MLRILTWSRS SLRSRSQLSP SSSFSILSSS YSTLNQGSED NQSTAGSVFS RDPSDPPRLF VVQPRVRPAT FLQAKLNEAL CLANSLEEQR DGYFHSDFFD KELPPHVVVQ NPSLKSAKIR ADTYFGPGTV ENIKCHLNAL ESKDGVDAVF VNTILSGVQQ RNLERILGKP VLDRVGLIIE IFNAHAHTKE AKLQAELAAL MYKKSRLVRV RGLDGRNTFG ASGEVEVVSA RGRGSGGRGF ISGAGETELQ LQRRRILERR NHLLSQIEEV RRTRAVQRAA RKKRGGLDGR GLATVAVVGY TNAGKSTLIS ALSDSNLYSD ARLFATLDAR LKSVVLPSGR KVLLSDTVGF ISDLPVQLVE AFHSTLEEVL EANLLLHVID CTAPNRDEHR STVLQVLQQI GVSEEKLQNM IEVWNKVFYH SFLSKNNNKN DVF // ID A0A0D2TJT8_GOSRA Unreviewed; 596 AA. AC A0A0D2TJT8; DT 29-APR-2015, integrated into UniProtKB/TrEMBL. DT 29-APR-2015, sequence version 1. DT 07-JUN-2017, entry version 14. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:KJB43970.1}; GN ORFNames=B456_007G227000 {ECO:0000313|EMBL:KJB43970.1}; OS Gossypium raimondii (New World cotton). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae; OC Pentapetalae; rosids; malvids; Malvales; Malvaceae; Malvoideae; OC Gossypium. OX NCBI_TaxID=29730 {ECO:0000313|EMBL:KJB43970.1, ECO:0000313|Proteomes:UP000032304}; RN [1] {ECO:0000313|EMBL:KJB43970.1, ECO:0000313|Proteomes:UP000032304} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=23257886; DOI=10.1038/nature11798; RA Paterson A.H., Wendel J.F., Gundlach H., Guo H., Jenkins J., Jin D., RA Llewellyn D., Showmaker K.C., Shu S., Udall J., Yoo M.J., Byers R., RA Chen W., Doron-Faigenboim A., Duke M.V., Gong L., Grimwood J., RA Grover C., Grupp K., Hu G., Lee T.H., Li J., Lin L., Liu T., RA Marler B.S., Page J.T., Roberts A.W., Romanel E., Sanders W.S., RA Szadkowski E., Tan X., Tang H., Xu C., Wang J., Wang Z., Zhang D., RA Zhang L., Ashrafi H., Bedon F., Bowers J.E., Brubaker C.L., Chee P.W., RA Das S., Gingle A.R., Haigler C.H., Harker D., Hoffmann L.V., Hovav R., RA Jones D.C., Lemke C., Mansoor S., ur Rahman M., Rainville L.N., RA Rambani A., Reddy U.K., Rong J.K., Saranga Y., Scheffler B.E., RA Scheffler J.A., Stelly D.M., Triplett B.A., Van Deynze A., RA Vaslin M.F., Waghmare V.N., Walford S.A., Wright R.J., Zaki E.A., RA Zhang T., Dennis E.S., Mayer K.F., Peterson D.G., Rokhsar D.S., RA Wang X., Schmutz J.; RT "Repeated polyploidization of Gossypium genomes and the evolution of RT spinnable cotton fibres."; RL Nature 492:423-427(2012). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CM001746; KJB43970.1; -; Genomic_DNA. DR RefSeq; XP_012492020.1; XM_012636566.1. DR GeneID; 105804072; -. DR KEGG; gra:105804072; -. DR Proteomes; UP000032304; Chromosome 7. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR CDD; cd01878; HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 2. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000032304}; KW Reference proteome {ECO:0000313|Proteomes:UP000032304}. FT DOMAIN 293 564 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 596 AA; 66088 MW; D61916883867BF9F CRC64; MLRILTWSRS SLRSRSQLSP SSSFSILSSS YSTLNQGSED NQSTAGSVFS RDPSDPPRLF VVQPRVRPAT FLQAKLNEAL CLANSLEEQR DGYFHSDFFD KELPPHVVVQ NPSLKSAKIR ADTYFGPGTV ENIKCHLNAL ESKDGVDAVF VNTILSGVQQ RNLERILGKP VLDRVGLIIE IFNAHAHTKE AKLQAELAAL MYKKSRLVRV RGLDGRNTFG ASGEVEVVSA RGRGSGGRGF ISGAGETELQ LQRRRILERR NHLLSQIEEV RRTRAVQRAA RKKRGGLDGR GLATVAVVGY TNAGKSTLIS ALSDSNLYSD ARLFATLDAR LKSVVLPSGR KVLLSDTVGF ISDLPVQLVE AFHSTLEEVL EANLLLHVID CTAPNRDEHR STVLQVLQQI GVSEEKLQNM IEVWNKIDYE EEMGAGEYMD DGEDVEMSNF SAAEDGETKD SPGEDCDVAF ELLDGKSVDG SDALKPSLGE LQQTMDDKQD DYSDGWLLSE DDTADDYWNT LNEQQQAETS NECKVEKDSE SQPQHVPHVK VSALTGVGLQ ELLELIDEKL KVQDDQLKSE KVVGNSYIDR KWRPPRKEDE EVAVEQ // ID A0A0D2TMV3_GOSRA Unreviewed; 548 AA. AC A0A0D2TMV3; DT 29-APR-2015, integrated into UniProtKB/TrEMBL. DT 29-APR-2015, sequence version 1. DT 07-JUN-2017, entry version 13. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:KJB58194.1}; GN ORFNames=B456_009G198600 {ECO:0000313|EMBL:KJB58194.1}; OS Gossypium raimondii (New World cotton). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae; OC Pentapetalae; rosids; malvids; Malvales; Malvaceae; Malvoideae; OC Gossypium. OX NCBI_TaxID=29730 {ECO:0000313|EMBL:KJB58194.1, ECO:0000313|Proteomes:UP000032304}; RN [1] {ECO:0000313|EMBL:KJB58194.1, ECO:0000313|Proteomes:UP000032304} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=23257886; DOI=10.1038/nature11798; RA Paterson A.H., Wendel J.F., Gundlach H., Guo H., Jenkins J., Jin D., RA Llewellyn D., Showmaker K.C., Shu S., Udall J., Yoo M.J., Byers R., RA Chen W., Doron-Faigenboim A., Duke M.V., Gong L., Grimwood J., RA Grover C., Grupp K., Hu G., Lee T.H., Li J., Lin L., Liu T., RA Marler B.S., Page J.T., Roberts A.W., Romanel E., Sanders W.S., RA Szadkowski E., Tan X., Tang H., Xu C., Wang J., Wang Z., Zhang D., RA Zhang L., Ashrafi H., Bedon F., Bowers J.E., Brubaker C.L., Chee P.W., RA Das S., Gingle A.R., Haigler C.H., Harker D., Hoffmann L.V., Hovav R., RA Jones D.C., Lemke C., Mansoor S., ur Rahman M., Rainville L.N., RA Rambani A., Reddy U.K., Rong J.K., Saranga Y., Scheffler B.E., RA Scheffler J.A., Stelly D.M., Triplett B.A., Van Deynze A., RA Vaslin M.F., Waghmare V.N., Walford S.A., Wright R.J., Zaki E.A., RA Zhang T., Dennis E.S., Mayer K.F., Peterson D.G., Rokhsar D.S., RA Wang X., Schmutz J.; RT "Repeated polyploidization of Gossypium genomes and the evolution of RT spinnable cotton fibres."; RL Nature 492:423-427(2012). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CM001748; KJB58194.1; -; Genomic_DNA. DR RefSeq; XP_012446696.1; XM_012591242.1. DR GeneID; 105770164; -. DR KEGG; gra:105770164; -. DR KO; K03665; -. DR Proteomes; UP000032304; Chromosome 9. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000032304}; KW Reference proteome {ECO:0000313|Proteomes:UP000032304}. FT DOMAIN 325 491 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 548 AA; 61249 MW; 94CC12739821F6B0 CRC64; MMSLCFCSLI SPCPSPLIYD SNFPWNLNLN RSVSPLTFST HGNDRSFVAR VAQRGYEVGN ISLQSPTIEA EEENEVVDEL VNGSVVAESV EEDTPRSVRV RKKRDDGDGS DDESFEDRFK LRNGREVFEE KAYLVGVERK GETSDSFAIE ESLKELAQLA DTAGLMVVGS TYQKLASPNP RTYIGSGKVA EIKSAIRAFE VETVIFDDEL SPGQLRNLEK AFGGDVRVCD RTALILDIFN QRAATHEAAL QVALAQMEYQ LPRLTKMWTH LERQAGGKVK GMGEKQIEVD KRILRTQIGV LKKELESVRK HRKQYRNRRF SVPVPVVSLV GYTNAGKSTL LNQLTGANVL SEDRLFATLD PTTRRVQMKN GSEFLLTDTV GFIQKLPTTL VAAFRATLEE ISESSLLVHV VDISHPLAEQ QIDAVEKVLA ELDVSEIPKL MVWNKVDKVT DPEKIKLEAE RREDIVCISA LTGEGLLEFC TAVQEKLKDS MVPVEAFVPF DKGELLSTIH QVGMVEKTEY TENGTFVKAF VPLRFARLLT PMRQLCKS // ID A0A0D2VX11_9PROT Unreviewed; 429 AA. AC A0A0D2VX11; DT 29-APR-2015, integrated into UniProtKB/TrEMBL. DT 29-APR-2015, sequence version 1. DT 07-JUN-2017, entry version 16. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=N826_15170 {ECO:0000313|EMBL:KJB93588.1}; OS Skermanella aerolata KACC 11604. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales; OC Rhodospirillaceae; Skermanella. OX NCBI_TaxID=1385368 {ECO:0000313|EMBL:KJB93588.1, ECO:0000313|Proteomes:UP000032292}; RN [1] {ECO:0000313|EMBL:KJB93588.1, ECO:0000313|Proteomes:UP000032292} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=KACC 11604 {ECO:0000313|Proteomes:UP000032292}; RA Zhu W., Wang G.; RT "The genome sequence of Skermanella aerotala."; RL Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KJB93588.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AVFK01000018; KJB93588.1; -; Genomic_DNA. DR EnsemblBacteria; KJB93588; KJB93588; N826_15170. DR PATRIC; fig|1385368.3.peg.3137; -. DR Proteomes; UP000032292; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000032292}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000032292}. FT DOMAIN 199 370 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 429 AA; 47434 MW; AD160012067FA625 CRC64; MIHPILRDPN PTEGARSPES RLEEAVGLAA AIDLDVVHAE AVKVNRPQPG TLLGSGTVDH FAELIHQAEE DGHPIDLVVM DHALSPVQQR NLERALECKV IDRTGLILEI FGARARTREG QLQVELAALS YQRSRLVRSW THLERQRGGF GFLGGPGESQ LEIDRRLIGD RIIKLKRELE EVRRTRDLHR KARSKVPYPV VALVGYTNAG KSSLFNRMAG ADVFAKDLLF ATLDPTMRAI ELPTGRKVIL SDTVGFISDL PTHLVAAFRA TLEEVQAADI ILHVRDIAHP DSEAQKGDVD AVLRDLGIDQ GEDNRVVEVL NKIDLLDSGA RNALLAQAAR NDHMQAVSAL TGDGLGELFG LLDRHMTADR VTVDLNVRID DGAALAWLHD RGDILERQDD EQFAHLRIAL DKADLARFES RYDYHAASS // ID A0A0D3ALC1_BRAOL Unreviewed; 545 AA. AC A0A0D3ALC1; DT 29-APR-2015, integrated into UniProtKB/TrEMBL. DT 29-APR-2015, sequence version 1. DT 07-JUN-2017, entry version 14. DE SubName: Full=Uncharacterized protein {ECO:0000313|EnsemblPlants:Bo2g028950.1}; OS Brassica oleracea var. oleracea. OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae; OC Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Brassiceae; OC Brassica. OX NCBI_TaxID=109376 {ECO:0000313|EnsemblPlants:Bo2g028950.1, ECO:0000313|Proteomes:UP000032141}; RN [1] {ECO:0000313|EnsemblPlants:Bo2g028950.1, ECO:0000313|Proteomes:UP000032141} RP NUCLEOTIDE SEQUENCE. RC STRAIN=cv. TO1000 {ECO:0000313|Proteomes:UP000032141}; RX PubMed=24916971; DOI=10.1186/gb-2014-15-6-r77; RA Parkin I.A., Koh C., Tang H., Robinson S.J., Kagale S., Clarke W.E., RA Town C.D., Nixon J., Krishnakumar V., Bidwell S.L., Denoeud F., RA Belcram H., Links M.G., Just J., Clarke C., Bender T., Huebert T., RA Mason A.S., Pires J.C., Barker G., Moore J., Walley P.G., Manoli S., RA Batley J., Edwards D., Nelson M.N., Wang X., Paterson A.H., King G., RA Bancroft I., Chalhoub B., Sharpe A.G.; RT "Transcriptome and methylome profiling reveals relics of genome RT dominance in the mesopolyploid Brassica oleracea."; RL Genome Biol. 15:R77-R77(2014). RN [2] {ECO:0000313|EnsemblPlants:Bo2g028950.1} RP IDENTIFICATION. RG EnsemblPlants; RL Submitted (MAR-2015) to UniProtKB. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR RefSeq; XP_013620066.1; XM_013764612.1. DR EnsemblPlants; Bo2g028950.1; Bo2g028950.1; Bo2g028950. DR GeneID; 106326695; -. DR Gramene; Bo2g028950.1; Bo2g028950.1; Bo2g028950. DR OMA; VILEIFH; -. DR Proteomes; UP000032141; Chromosome C2. DR GO; GO:0009507; C:chloroplast; IEA:EnsemblPlants. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000032141}; KW Reference proteome {ECO:0000313|Proteomes:UP000032141}. FT DOMAIN 311 477 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 545 AA; 61207 MW; 88FB8656B25C1710 CRC64; MSSFLFPSSS PIPKSHWRAN SIPKPNRPIT LSLLHGNSYS WRLSCKLSLD YFEESVEEDE IPQFLDFSAE GEEPDLEKET VSAPTMTLMQ RKKKKGDEES LEDRFKLRNG KEVFEEKAYL VGVERKGDGE CLFDIEESLE ELEQLADTAG LMVVGSTYQK LASPNPRTYI GSGKVSEIKS AINALDVETV IFDDELSPGQ LRNLEKAFGG DVRVCDRTAL ILDIFNQRAA THEAALQVAL AQMEYQLPRL TRMWTHLERQ SGGQVKGMGE KQIEVDKRIL RTQIGVLKKE LESVRKHRKQ YRTRRVAIPV PVVSLVGYTN AGKSTLLNQL TGANVLAENR LFATLDPTTR RVQMHNGKEF LLTDTVGFIQ KLPTTLVAAF RATLEEISES SLLVHVVDIS HPLANQQIEA VEKVMSELDV SSIPKLVVWN KVDRVDDPQK VKLEAEEHGD VICISALTGE GLDKFCNAVH EKLKDSMVWV EALLPFDKGD LLSTIHKVGM VKETEYTENG TLIRAHVPLR FAQLLKPMRH LVKEASYAKK GEIES // ID A0A0D3DRP0_BRAOL Unreviewed; 435 AA. AC A0A0D3DRP0; DT 29-APR-2015, integrated into UniProtKB/TrEMBL. DT 29-APR-2015, sequence version 1. DT 07-JUN-2017, entry version 12. DE SubName: Full=Uncharacterized protein {ECO:0000313|EnsemblPlants:Bo8g078980.1}; OS Brassica oleracea var. oleracea. OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae; OC Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Brassiceae; OC Brassica. OX NCBI_TaxID=109376 {ECO:0000313|EnsemblPlants:Bo8g078980.1, ECO:0000313|Proteomes:UP000032141}; RN [1] {ECO:0000313|EnsemblPlants:Bo8g078980.1, ECO:0000313|Proteomes:UP000032141} RP NUCLEOTIDE SEQUENCE. RC STRAIN=cv. TO1000 {ECO:0000313|Proteomes:UP000032141}; RX PubMed=24916971; DOI=10.1186/gb-2014-15-6-r77; RA Parkin I.A., Koh C., Tang H., Robinson S.J., Kagale S., Clarke W.E., RA Town C.D., Nixon J., Krishnakumar V., Bidwell S.L., Denoeud F., RA Belcram H., Links M.G., Just J., Clarke C., Bender T., Huebert T., RA Mason A.S., Pires J.C., Barker G., Moore J., Walley P.G., Manoli S., RA Batley J., Edwards D., Nelson M.N., Wang X., Paterson A.H., King G., RA Bancroft I., Chalhoub B., Sharpe A.G.; RT "Transcriptome and methylome profiling reveals relics of genome RT dominance in the mesopolyploid Brassica oleracea."; RL Genome Biol. 15:R77-R77(2014). RN [2] {ECO:0000313|EnsemblPlants:Bo8g078980.1} RP IDENTIFICATION. RG EnsemblPlants; RL Submitted (MAR-2015) to UniProtKB. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EnsemblPlants; Bo8g078980.1; Bo8g078980.1; Bo8g078980. DR Gramene; Bo8g078980.1; Bo8g078980.1; Bo8g078980. DR OMA; NGPEAIS; -. DR Proteomes; UP000032141; Chromosome C8. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR CDD; cd01878; HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 2. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 2. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 4: Predicted; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000032141}; KW Reference proteome {ECO:0000313|Proteomes:UP000032141}. FT DOMAIN 155 402 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 295 323 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 435 AA; 48780 MW; 4C7B4B7C2FD28CE8 CRC64; MLAQEEVDAV FINAILSAIQ QRNLERIWGK PVLDRVGLII EIFNAHAHTK EAKLQAELAA LMYKKSRLVR VRGTDGRQTF GQFGEAEVVS ARGRAASKGT GFVGGAGETE LQLQRRRIAD RRLRLLSQIK EAQRTRLLQR AARKRQSGLE GKSLATIAVV GYTNAGKSTL TSALTRTALY CNERLFATLD PTLKNAILPS GRKVLFSDTV GFISDLPIQL VEAFQSTLEE VVEADLLLHV VDSTAPNIEE HRSTVFHVLN QIGVPEEKLK NMIEVWNKID YEEEEEEDMH YLDDGKGEEE EEEEEEEEEA ELSEDSIAEE TLEASSEATV DEDQIQNQED DSDEWLLSED ENVSDSELWK VPEEAKEDAA QKSGPDVRVS ALTGVGLKEL MYLIDEKLSG EDEKRKSGTI VERNDFQSRK WRPSFKDGEE FAAGQ // ID A0A0D3HNL4_9ORYZ Unreviewed; 552 AA. AC A0A0D3HNL4; DT 29-APR-2015, integrated into UniProtKB/TrEMBL. DT 29-APR-2015, sequence version 1. DT 30-AUG-2017, entry version 15. DE SubName: Full=Uncharacterized protein {ECO:0000313|EnsemblPlants:OBART11G18670.1}; OS Oryza barthii. OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; BOP clade; OC Oryzoideae; Oryzeae; Oryzinae; Oryza. OX NCBI_TaxID=65489 {ECO:0000313|EnsemblPlants:OBART11G18670.1, ECO:0000313|Proteomes:UP000026960}; RN [1] {ECO:0000313|EnsemblPlants:OBART11G18670.1, ECO:0000313|Proteomes:UP000026960} RP NUCLEOTIDE SEQUENCE. RC STRAIN=IRGC 105608 {ECO:0000313|EnsemblPlants:OBART11G18670.1}; RA Rounsley S., Marri P.R., Yu Y., He R., Sisneros N., Goicoechea J.L., RA Lee S.J., Angelova A., Kudrna D., Luo M., Affourtit J., Desany B., RA Knight J., Niazi F., Egholm M., Wing R.A.; RT "De Novo Next Generation Sequencing of Plant Genomes."; RL Submitted (JUL-2008) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EnsemblPlants:OBART11G18670.1, ECO:0000313|Proteomes:UP000026960} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=IRGC 105608 {ECO:0000313|EnsemblPlants:OBART11G18670.1}; RX DOI=10.1007/s12284-009-9025-z; RA Rounsley S., Marri P.R., Yu Y., He R., Sisneros N., Goicoechea J.L., RA Lee S.J., Angelova A., Kudrna D., Luo M., Affourtit J., Desany B., RA Knight J., Niazi F., Egholm M., Wing R.A.; RT "De novo next generation sequencing of plant genomes."; RL Rice 2:35-43(2009). RN [3] {ECO:0000313|EnsemblPlants:OBART11G18670.1} RP IDENTIFICATION. RG EnsemblPlants; RL Submitted (MAR-2015) to UniProtKB. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EnsemblPlants; OBART11G18670.1; OBART11G18670.1; OBART11G18670. DR Gramene; OBART11G18670.1; OBART11G18670.1; OBART11G18670. DR OrthoDB; EOG093609UJ; -. DR Proteomes; UP000026960; Chromosome 11. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000026960}; KW Reference proteome {ECO:0000313|Proteomes:UP000026960}. FT DOMAIN 328 493 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 294 321 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 552 AA; 60749 MW; 306AAEBC313B7B50 CRC64; MRAACFFTGA AATASLPLPS TSASASACCQ RRPASLRCSR PRRSFGVARA LDERLVEAAP PAETEVEEPG VADGGGEGEG EVEDSAPSGE EEEEEQPARA PVRSRRRQEE EEEEAAPGHD RFKLINGKEI FQEKAYLVGV ECKRSGGSMF SIEESLEELE QLADTAGLMV VGSTYQKLST PNPRTYIGSG KVAEIKSAIH AHDVETVIFD DELSPGQLRN LEKSFGGGVR VCDRTALILD IFNQRAATHE AALQVTLAQM EYQLPRLTKM WSHLERQSGG QVKGMGEKQI EVDKRILRTQ ISALRKELES VRKHRKLYRN RRQSVPIPVV SLVGYTNAGK STLLNRLTGA DVLAEDKLFA TLDPTTRRVL MKNGTEFLLT DTVGFIQKLP TMLVAAFRAT LEEISESSVI VHLVDISHPL AQQQIDAVDK VLKELDIESI PKLVVWNKID NTDDTLRVKE EAEKQGIICI SAINGDGLEE FCNAIQAKLK DSLVPIEAFV PYDKGELLSD IHKVGMVEKT EYMENGTFVK AHVPLPLARL LTPLRQQVAA VS // ID A0A0D3LGV0_9BACT Unreviewed; 406 AA. AC A0A0D3LGV0; DT 27-MAY-2015, integrated into UniProtKB/TrEMBL. DT 27-MAY-2015, sequence version 1. DT 07-JUN-2017, entry version 17. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=D770_13390 {ECO:0000313|EMBL:AHM60932.1}; OS Flammeovirgaceae bacterium 311. OC Bacteria; Bacteroidetes; Cytophagia; Cytophagales; Flammeovirgaceae; OC unclassified Flammeovirgaceae. OX NCBI_TaxID=1257021 {ECO:0000313|EMBL:AHM60932.1, ECO:0000313|Proteomes:UP000064112}; RN [1] {ECO:0000313|EMBL:AHM60932.1, ECO:0000313|Proteomes:UP000064112} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=311 {ECO:0000313|EMBL:AHM60932.1, RC ECO:0000313|Proteomes:UP000064112}; RA Fang C.; RT "Complete bacteria genome obtained just from illumina data."; RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP004371; AHM60932.1; -; Genomic_DNA. DR RefSeq; WP_061988603.1; NZ_CP004371.1. DR EnsemblBacteria; AHM60932; AHM60932; D770_13390. DR KEGG; fbt:D770_13390; -. DR PATRIC; fig|1257021.3.peg.3043; -. DR KO; K03665; -. DR Proteomes; UP000064112; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000064112}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000064112}. FT DOMAIN 202 375 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 163 190 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 406 AA; 46280 MW; 18512B37941095E1 CRC64; MIEPISTAAK VEKAVLVALV TPRQSAEQAK EYLEELSFLA ETSGVQTLAT FTQRLDRPDT RTFVGKGKLE DIKAFVQEHE ADIVIFDDEL TPSQVRNLEQ ELQCKILDRS LLILNIFSIR AKTAQAKAQV ELAQYQYLLP RLTRMWSHLS KQKGGIGMRG PGEKELETDR RIVRDKIAFL REKLDKIEKQ SLTQRKGRKQ LARVALVGYT NVGKSTLMRL LSKSDVFAEN KLFATVDSTV RKVVINEIPF LLTDTVGFIR KLPHTLVECF KSTLDEIREA DLLLHVVDIS HPASHEQIEI VNSTLAEIGA GDKPMIMVYN KVDAMPEEER LNLQESGVPE ESEQPVVDRV FISALEKRNI ESLRSKVNEQ VKERHYEIYP NYLQPQIYEG SWSMDGEEWS LDGEEE // ID A0A0D3V7N4_9BACL Unreviewed; 428 AA. AC A0A0D3V7N4; DT 27-MAY-2015, integrated into UniProtKB/TrEMBL. DT 27-MAY-2015, sequence version 1. DT 07-JUN-2017, entry version 15. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=UB51_07100 {ECO:0000313|EMBL:AJS58304.1}; OS Paenibacillus sp. IHBB 10380. OC Bacteria; Firmicutes; Bacilli; Bacillales; Paenibacillaceae; OC Paenibacillus. OX NCBI_TaxID=1566358 {ECO:0000313|EMBL:AJS58304.1, ECO:0000313|Proteomes:UP000032320}; RN [1] {ECO:0000313|EMBL:AJS58304.1, ECO:0000313|Proteomes:UP000032320} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=IHBB 10380 {ECO:0000313|EMBL:AJS58304.1, RC ECO:0000313|Proteomes:UP000032320}; RX PubMed=25908145; RA Pal M., Swarnkar M.K., Thakur R., Kiran S., Chhibber S., Singh A.K., RA Gulati A.; RT "Complete Genome Sequence of Paenibacillus sp. Strain IHBB 10380 Using RT PacBio Single-Molecule Real-Time Sequencing Technology."; RL Genome Announc. 3:0-0(2015). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP010976; AJS58304.1; -; Genomic_DNA. DR RefSeq; WP_044876711.1; NZ_CP010976.1. DR EnsemblBacteria; AJS58304; AJS58304; UB51_07100. DR KEGG; pih:UB51_07100; -. DR PATRIC; fig|1566358.3.peg.1537; -. DR KO; K03665; -. DR Proteomes; UP000032320; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000032320}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000032320}. FT DOMAIN 208 372 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 167 201 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 428 AA; 48306 MW; E7AB5FE2D93D6454 CRC64; MINSTYDTET DLQDRAVLVS LVTDEVKRKG IDPEYSLHEL VQLAETAGVE VLDSLSQNLQ KPDPKWFIGK GKVEELRLVM EATDANTAIF DHELSGAQVR HLEESLDVKI IDRTQLILDI FAQRAKTREG IIQVELAQLT YLLPRLSGQS QNLSRLGGGI GTRGPGESKL EMDRRHIRDR VNDLKQQLDE ITKHRKLYRE RRQKSGVTQV ALVGYTNAGK STLLKQLTDA DVYIQDQLFA TLDPTSRVLE LPSGKEVVLT DTVGFIQNLP HDLIAAFRAT LEEVNEADLI LHVVDSSSEM REDQMKVVQS ILQDLGAADK PQITLYNKKD MCNPEQLQML GSGEGYLKIS AFDEADLLVI REAVQTTLTG DTLTFRIPAN RGDLTSLLYR VGDVLEQEFD ESDLLYKVLL HKADYVKHEY MLKEYIEL // ID A0A0D3VHJ6_9BACL Unreviewed; 421 AA. AC A0A0D3VHJ6; DT 27-MAY-2015, integrated into UniProtKB/TrEMBL. DT 27-MAY-2015, sequence version 1. DT 07-JUN-2017, entry version 16. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=UB51_24965 {ECO:0000313|EMBL:AJS61147.1}; OS Paenibacillus sp. IHBB 10380. OC Bacteria; Firmicutes; Bacilli; Bacillales; Paenibacillaceae; OC Paenibacillus. OX NCBI_TaxID=1566358 {ECO:0000313|EMBL:AJS61147.1, ECO:0000313|Proteomes:UP000032320}; RN [1] {ECO:0000313|EMBL:AJS61147.1, ECO:0000313|Proteomes:UP000032320} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=IHBB 10380 {ECO:0000313|EMBL:AJS61147.1, RC ECO:0000313|Proteomes:UP000032320}; RX PubMed=25908145; RA Pal M., Swarnkar M.K., Thakur R., Kiran S., Chhibber S., Singh A.K., RA Gulati A.; RT "Complete Genome Sequence of Paenibacillus sp. Strain IHBB 10380 Using RT PacBio Single-Molecule Real-Time Sequencing Technology."; RL Genome Announc. 3:0-0(2015). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP010976; AJS61147.1; -; Genomic_DNA. DR RefSeq; WP_044879621.1; NZ_CP010976.1. DR EnsemblBacteria; AJS61147; AJS61147; UB51_24965. DR KEGG; pih:UB51_24965; -. DR PATRIC; fig|1566358.3.peg.5409; -. DR KO; K03665; -. DR Proteomes; UP000032320; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000032320}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000032320}. FT DOMAIN 200 368 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 421 AA; 48110 MW; 1140F44CB465E3B3 CRC64; MEEQQQRAII VGVNLSHQKD FDFEYSMEEL SNLASACHVE VVGRMTQNLE RVNKSHYIGK GKVLEVMNLY EAADANVVIF NDELSPSHIR NLESDLQCKV IDRTILILDI FERRAQTREA QLQVEVAQLQ YMLPRLIGLR ESLGRQSGGV GTKNKGAGET RLELDRRRIE DKISALNKEL EALVMGRQTQ RKQRKNNGIP VVSLVGYTNA GKSTIMNALV ESFGPANDKK VFEKDMLFAT LETSVRNIQL PDHKSFLLTD TVGFVSKLPH HLIKAFRSTL EEVAEADLLI HVIDYSNPKH EQLTQITEHT LQEIGITDIP TLFAYNKCDR IDCDIPKVED NSVYLAAKSR VGITELVNRI RDHIFKDYIQ CEMMIPYEQG QLVSYFNEHA HITATEYENE GTRLTLECRT MDYEKYGEYV I // ID A0A0D4C347_9MICC Unreviewed; 520 AA. AC A0A0D4C347; DT 27-MAY-2015, integrated into UniProtKB/TrEMBL. DT 27-MAY-2015, sequence version 1. DT 07-JUN-2017, entry version 17. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=UM93_01875 {ECO:0000313|EMBL:AJT42796.1}; OS Arthrobacter sp. IHBB 11108. OC Bacteria; Actinobacteria; Micrococcales; Micrococcaceae; Arthrobacter. OX NCBI_TaxID=1618207 {ECO:0000313|EMBL:AJT42796.1, ECO:0000313|Proteomes:UP000061839}; RN [1] {ECO:0000313|EMBL:AJT42796.1, ECO:0000313|Proteomes:UP000061839} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=IHBB 11108 {ECO:0000313|EMBL:AJT42796.1, RC ECO:0000313|Proteomes:UP000061839}; RX PubMed=25908143; RA Kiran S., Swarnkar M.K., Pal M., Thakur R., Tewari R., Singh A.K., RA Gulati A.; RT "Complete Genome Sequencing of Protease-Producing Novel Arthrobacter RT sp. Strain IHBB 11108 Using PacBio Single-Molecule Real-Time RT Sequencing Technology."; RL Genome Announc. 3:0-0(2015). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP011005; AJT42796.1; -; Genomic_DNA. DR RefSeq; WP_045076710.1; NZ_CP011005.1. DR EnsemblBacteria; AJT42796; AJT42796; UM93_01875. DR KEGG; ari:UM93_01875; -. DR PATRIC; fig|1618207.4.peg.383; -. DR KO; K03665; -. DR Proteomes; UP000061839; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 2. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000061839}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000061839}. FT DOMAIN 295 460 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 520 AA; 56531 MW; 05674BB6D6BB52F3 CRC64; MTTQNNADHQ AGADMSPAEI QAVIDRILAK DSGVEPAEHG VLASRAQALS DSGREHGEYD GEQEDLQERR ALRRVAGLST ELEDVTEVEY RQLRLERVVL AGLWSEGTLA DAENSLRELA ALAETAGSEV LDGLVQRRMK PDPGTFLGSG KALELKDVVM ATGADTVVVD AELAPSQRRG LEDIVKVKVI DRTALILDIF AQHAKSREGK AQVELAQLEY LLPRLRGWGE SMSRQAGGQV GGAGAGMGSR GPGETKIELD RRRIRTRMAK LRREIAAMKP ARETKRANRR RTEIPSVAIA GYTNAGKSSI LNRLTQAGVL VENALFATLD PTVRKASTPD GIGFTLADTV GFVRSLPTQL VEAFRSTLEE VADADLILHV VDVSHPDPEG QIAAVRAVFS EVDARNIPEI IVLNKADAAD PEVIERLRLR EPRSVLVSAR TGAGMTELME QISSSIPRPN VQLELLIPYD RGDLVNKLHQ SDADILSQEH RETGTWLRVK VREGLAAELA PFREGPQPAA // ID A0A0D4CI02_9LACO Unreviewed; 426 AA. AC A0A0D4CI02; DT 27-MAY-2015, integrated into UniProtKB/TrEMBL. DT 27-MAY-2015, sequence version 1. DT 07-JUN-2017, entry version 14. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=LBLM1_00805 {ECO:0000313|EMBL:AJT49787.1}; OS Lactobacillus mucosae LM1. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; OC Lactobacillus. OX NCBI_TaxID=1130798 {ECO:0000313|EMBL:AJT49787.1, ECO:0000313|Proteomes:UP000003645}; RN [1] {ECO:0000313|EMBL:AJT49787.1, ECO:0000313|Proteomes:UP000003645} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=LM1 {ECO:0000313|EMBL:AJT49787.1, RC ECO:0000313|Proteomes:UP000003645}; RX PubMed=22887668; DOI=10.1128/JB.01011-12; RA Lee J.H., Valeriano V.D., Shin Y.R., Chae J.P., Kim G.B., Ham J.S., RA Chun J., Kang D.K.; RT "Genome sequence of Lactobacillus mucosae LM1, isolated from piglet RT feces."; RL J. Bacteriol. 194:4766-4766(2012). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP011013; AJT49787.1; -; Genomic_DNA. DR RefSeq; WP_039946003.1; NZ_CVQW01000012.1. DR EnsemblBacteria; AJT49787; AJT49787; LBLM1_00805. DR KEGG; lmu:LBLM1_00805; -. DR KO; K03665; -. DR Proteomes; UP000003645; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000003645}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000003645}. FT DOMAIN 202 371 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 426 AA; 48195 MW; D6DD75A5B15F8DFA CRC64; MDTNIQSAEP VIIIGLNMDQ EDYEYSMEEL AALAEANQME VIDRLDQALD RPNPATYFGS GKVEELRHLA EAEEVATVIA NDELTPSQLQ NLADQTGVRI LDRTALILEI FAKRAQSREA KIQVEIAQLQ YQLPRLQTAA NQRLDQQTGG GSGFTNRGAG ETKLEMNRRT INHKISHLRA ELKEIAKSED VKRAKREKSD TPTAALVGYT NAGKSTIMNQ LVSRFGVSEE KQVFEKNMLF ATLDTSVRQL TLPDQKRFLL SDTVGFVSKL PTHLIEAFKS TLAEAASADL LIQVIDYSDP NYEAMMRTTE KTLKQIGIEN IPMLYVFNKA DQTEFEYPVM EGDNRIIISA KDDESIQLLV QALRRHLFKD YVLTELLIPF ADGRTVSYVN ENCNILETEY LNNGTRLKVE MSPQDFARFE RYVIKN // ID A0A0D4DJG7_9ACTN Unreviewed; 495 AA. AC A0A0D4DJG7; DT 27-MAY-2015, integrated into UniProtKB/TrEMBL. DT 27-MAY-2015, sequence version 1. DT 05-JUL-2017, entry version 16. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=T261_2288 {ECO:0000313|EMBL:AJT63971.1}; OS Streptomyces lydicus. OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae; OC Streptomyces. OX NCBI_TaxID=47763 {ECO:0000313|EMBL:AJT63971.1, ECO:0000313|Proteomes:UP000032413}; RN [1] {ECO:0000313|Proteomes:UP000032413} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=A02 {ECO:0000313|Proteomes:UP000032413}; RA Wu H., Yan J., Liu W., Liu T., Dong D., Li J., Liu H., Lu C., RA Zhang D., Zhang T., Tian Z.; RT "Complete genome sequence of the natamycin-producing actinomycete RT Streptomyces lydicus A02."; RL Submitted (MAY-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP007699; AJT63971.1; -; Genomic_DNA. DR RefSeq; WP_046925657.1; NZ_CP007699.2. DR EnsemblBacteria; AJT63971; AJT63971; T261_2288. DR KEGG; sld:T261_2288; -. DR PATRIC; fig|1403539.3.peg.2415; -. DR KO; K03665; -. DR Proteomes; UP000032413; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 2. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000032413}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}. FT DOMAIN 275 440 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 495 AA; 54104 MW; 836D8EA4B80628D1 CRC64; MTSSSSLPQD RQRLPESLRA DALMEEDVAW SHEIDGERDG DQYDRSERAA LRRVAGLSTE LEDVTEVEYR QLRLERVVLV GVWTTGSVQE SENSLAELAA LAETAGAVVL DGVIQRRDKP DPATYIGSGK ALELRDIVLE SGADTVVCDG ELSPGQLIHL EDVVKVKVVD RTALILDIFA QHAKSREGKA QVSLAQMQYM LPRLRGWGQS LSRQMGGGGS GSAGGGMATR GPGETKIETD RRRIREKMAK MRREIAEMKT GRDIKRQERK RHKVPSVAIA GYTNAGKSSL LNRLTGAGVL VENALFATLD PTVRRAETPS GRLYTLADTV GFVRHLPHHL VEAFRSTMEE VGDSDLILHV VDGSHPVPEE QLAAVREVIR EVGATDVPEI VVVNKADAAD PLVLQRLLRN EKHALAVSAR TGQGMTELLE LLDEELPRPR VEIVALVPYT QGALVSRAHA EGEVISEEHT AEGTVLKARV HEELAAEFRP FVPAA // ID A0A0D5A8F9_9NOCA Unreviewed; 516 AA. AC A0A0D5A8F9; DT 27-MAY-2015, integrated into UniProtKB/TrEMBL. DT 27-MAY-2015, sequence version 1. DT 07-JUN-2017, entry version 14. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=NY08_1284 {ECO:0000313|EMBL:AJW39314.1}; OS Rhodococcus sp. B7740. OC Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae; OC Rhodococcus. OX NCBI_TaxID=1564114 {ECO:0000313|EMBL:AJW39314.1, ECO:0000313|Proteomes:UP000032410}; RN [1] {ECO:0000313|EMBL:AJW39314.1, ECO:0000313|Proteomes:UP000032410} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=B7740 {ECO:0000313|EMBL:AJW39314.1}; RX PubMed=25931596; RA Zhang D., Li L., Zhu S., Zhang N., Yang J., Ma X., Chen J.; RT "Complete Genome Sequence of Rhodococcus sp. B7740, a Carotenoid- RT Producing Bacterium Isolated from the Arctic Sea."; RL Genome Announc. 3:0-0(2015). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP010797; AJW39314.1; -; Genomic_DNA. DR EnsemblBacteria; AJW39314; AJW39314; NY08_1284. DR KEGG; rhb:NY08_1284; -. DR PATRIC; fig|1564114.4.peg.1257; -. DR KO; K03665; -. DR Proteomes; UP000032410; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 2. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000032410}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000032410}. FT DOMAIN 289 458 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 248 282 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 516 AA; 55999 MW; 80C3E704F8062ED0 CRC64; MTNSHETSPA GEPVDDGRDD IDGAPETESA WTREESDAWS RRLARSPLGD ENSPSSGDMQ LEDRTALRRV AGLSTELTDV TEVEYRQLRL ERVVLVGVWT TGTAAQAESS MTELAALAET AGSEVLEALM QRRDKPDAAT YIGSGKAKEV RDIVLATGAD TVICDGELTP AQLNALEKVV KVKVIDRTAL ILDIFAQHAT SREGKAQVAF AQMEYMLPRL RGWGESMSRQ AGGRAGSNGG VGLRGPGETK IETDRRRIRE RMAKLRREIK GMKQARDTKR EQRLSGTVPS IAIVGYTNAG KSSLLNALTG SGVLVQNALF ATLDPTTRKS TLEDGREIVL TDTVGFVRHL PTQLVEAFRS TLEEVTDADL LLHVVDGSDP LPIDQIKAVR EVITEVVREQ DAKMPPELLV VNKIDAADPV QLTQLRGLLD GARFVSAKTG EGIDALRDHL AEILSEPDVL VDVLVPYTRG DLVARIHTDG RIVKTAHEEE GTRVEARVPQ SLAAALVEFT AIVPSV // ID A0A0D5LS74_9RHIZ Unreviewed; 420 AA. AC A0A0D5LS74; DT 27-MAY-2015, integrated into UniProtKB/TrEMBL. DT 27-MAY-2015, sequence version 1. DT 07-JUN-2017, entry version 13. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=TM49_16515 {ECO:0000313|EMBL:AJY46921.1}; OS Martelella endophytica. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Aurantimonadaceae; Martelella. OX NCBI_TaxID=1486262 {ECO:0000313|EMBL:AJY46921.1, ECO:0000313|Proteomes:UP000032611}; RN [1] {ECO:0000313|EMBL:AJY46921.1, ECO:0000313|Proteomes:UP000032611} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=YC6887 {ECO:0000313|EMBL:AJY46921.1}; RX PubMed=25953177; RA Khan A., Khan H., Chung E.J., Hossain M.T., Chung Y.R.; RT "Complete Genome Sequence of Martelella endophytica YC6887, Which Has RT Antifungal Activity Associated with a Halophyte."; RL Genome Announc. 3:0-0(2015). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP010803; AJY46921.1; -; Genomic_DNA. DR EnsemblBacteria; AJY46921; AJY46921; TM49_16515. DR KEGG; mey:TM49_16515; -. DR PATRIC; fig|1486262.3.peg.3414; -. DR KO; K03665; -. DR Proteomes; UP000032611; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000032611}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000032611}. FT DOMAIN 193 365 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 152 186 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 420 AA; 46612 MW; FCAA0F5F19CA7760 CRC64; MKADRRSDGE GLSSRAPESR QQEAEGLARA IGLEVVASVI VQVNDPRPAT LIGTGKIKEI DELLDENNIG LVIVDHPLSP VQQRNLEKEW VAKVIDRTGL ILEIFGERAS TKEGRLQVEL AHLNYQRGRL VRSWTHLERQ RGGGGFMGGP GETQIEADRR LLRERITKLE RELEQVVRTR QLHRSKRKKV PHPIVALVGY TNAGKSTLFN RITGAGVLAE DMLFATLDPT LRRMKLPHGR TVILSDTVGF ISDLPTHLVA AFRATLEEVL EADLILHVRD MADPARDAQS GDVLRILGEL GIDEKAQNER IIEVWNKVDL LEPEDHDALM ARAEPNDDVM AVSAVTGEGV EALVDRIAAR LAGVLTETTI TLAPEQLHLL PWLYEHALVD ERRDLEDGSV SLDIRLADTE AQRLDSMLAG // ID A0A0D5M4W9_9GAMM Unreviewed; 436 AA. AC A0A0D5M4W9; DT 27-MAY-2015, integrated into UniProtKB/TrEMBL. DT 27-MAY-2015, sequence version 1. DT 30-AUG-2017, entry version 18. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=KO116_02731 {ECO:0000313|EMBL:AJY51206.1}; OS Halomonas sp. KO116. OC Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales; OC Halomonadaceae; Halomonas. OX NCBI_TaxID=1504981 {ECO:0000313|EMBL:AJY51206.1, ECO:0000313|Proteomes:UP000028645}; RN [1] {ECO:0000313|EMBL:AJY51206.1, ECO:0000313|Proteomes:UP000028645} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=KO116 {ECO:0000313|EMBL:AJY51206.1, RC ECO:0000313|Proteomes:UP000028645}; RX PubMed=25953187; RA O'Dell K.B., Woo H.L., Utturkar S., Klingeman D., Brown S.D., RA Hazen T.C.; RT "Genome Sequence of Halomonas sp. Strain KO116, an Ionic Liquid- RT Tolerant Marine Bacterium Isolated from a Lignin-Enriched Seawater RT Microcosm."; RL Genome Announc. 3:0-0(2015). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP011052; AJY51206.1; -; Genomic_DNA. DR RefSeq; WP_035566413.1; NZ_CP011052.1. DR EnsemblBacteria; AJY51206; AJY51206; KO116_02731. DR KEGG; hak:KO116_02731; -. DR KO; K03665; -. DR Proteomes; UP000028645; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000028645}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}. FT DOMAIN 199 365 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 436 AA; 49006 MW; 450901644BF22B09 CRC64; MFFERPDAGE TAVLVHVDFH DEQKREDPGE FLELVRSAGA EPATLLTASR HRPDSRTFIG SGKLEELRAL LAAHAAELVI FNHSLSPSQE RNVEQELKCR VLDRTGLILD IFAQRARTHE GKLQVELAQL EYMSTRLVRG WTHLERQKGG IGLRGPGETQ LETDRRLLRG RIKSIHKRLD KVRSQRDQNR RARARAEIHS VSLVGYTNAG KSTLFNALTN SDVYAADQLF ATLDPTLRRL EIEDVGPVVM ADTVGFIRHL PHKLVEAFQA TLQEASEASL LVHVIDAADP DRELNVEQVE LVLKEIGADD VPVLKVMNKI DKLDSVPRIE RDGHGVPEVV WLSAQQGQGL ELLHEALTER LANDVIGFSL TLNPEQGKLR AGLHELNAVR EEAFDEQGHS VLDVRLPRRD FNQLMAQLGE RANTYLPVAL RESDEW // ID A0A0D5NPH4_9BACL Unreviewed; 428 AA. AC A0A0D5NPH4; DT 27-MAY-2015, integrated into UniProtKB/TrEMBL. DT 27-MAY-2015, sequence version 1. DT 07-JUN-2017, entry version 15. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=VN24_24180 {ECO:0000313|EMBL:AJY77080.1}; OS Paenibacillus beijingensis. OC Bacteria; Firmicutes; Bacilli; Bacillales; Paenibacillaceae; OC Paenibacillus. OX NCBI_TaxID=1126833 {ECO:0000313|EMBL:AJY77080.1, ECO:0000313|Proteomes:UP000032633}; RN [1] {ECO:0000313|Proteomes:UP000032633} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 24997 {ECO:0000313|Proteomes:UP000032633}; RA Kwak Y., Shin J.-H.; RT "Genome sequence of Paenibacillus beijingensis strain DSM 24997T."; RL Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP011058; AJY77080.1; -; Genomic_DNA. DR RefSeq; WP_045672505.1; NZ_CP011058.1. DR EnsemblBacteria; AJY77080; AJY77080; VN24_24180. DR KEGG; pbj:VN24_24180; -. DR PATRIC; fig|1126833.4.peg.5319; -. DR KO; K03665; -. DR Proteomes; UP000032633; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000032633}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000032633}. FT DOMAIN 208 373 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 428 AA; 47439 MW; 4CF633621A3FBEE1 CRC64; MRNTTYETKT GMRDKAILVS LITPDIKRGP ADPEHSLEEL VNLAETAGVE VLTAVTQNKE SADPKWLIGK GKVEEIRAVK DELEATTIIF DQELSGAQVR NLEEALDAKI IDRTQLILDI FAGRAKTREG IIQVELAQLS YLLPRLSGHG KNLSRLGGGI GTRGPGESKL ETDRRHIRGR ISELKAQLAE VVRHRQLHRE RRRKSGVIQA ALVGYTNAGK STLLRELTNS DVYVENQLFA TLDPTSRTLE LPSGKEIVLT DTVGFIQNLP HDLVAAFRAT LEEVNEADLV LHVVDSSSPM RQEQMRVVEE LLEQLGASGK PTVTVFNKKD LRPQLPDVYL PTDSESTLLV SAFDSGDMKR LLELIQDKLA GDTRTFSLPA ERGDLIALAY RCGEVVSQEV DGDSLRLTIE LNKGDYEVNG HRLQPFEV // ID A0A0D5V5X5_9BURK Unreviewed; 390 AA. AC A0A0D5V5X5; DT 27-MAY-2015, integrated into UniProtKB/TrEMBL. DT 27-MAY-2015, sequence version 1. DT 30-AUG-2017, entry version 15. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:AJZ57543.1}; GN ORFNames=OI25_2897 {ECO:0000313|EMBL:AJZ57543.1}; OS Paraburkholderia fungorum. OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Paraburkholderia. OX NCBI_TaxID=134537 {ECO:0000313|EMBL:AJZ57543.1, ECO:0000313|Proteomes:UP000032614}; RN [1] {ECO:0000313|EMBL:AJZ57543.1, ECO:0000313|Proteomes:UP000032614} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-463 {ECO:0000313|EMBL:AJZ57543.1, RC ECO:0000313|Proteomes:UP000032614}; RX PubMed=25931592; RA Johnson S.L., Bishop-Lilly K.A., Ladner J.T., Daligault H., RA Jaissle J., Frey K.G., Koroleva G.I., Bruce D.C., Coyne S.R., RA Broomall S.M., Li P., Teshima H., Gibbons H.S., Palacios G.F., RA Rosenzweig C.N., McMurry K., Redden C.L., Xu Y., Currie B., Mayo M., RA Minogue T.D., Chain P.S.; RT "Complete genome sequences for 59 burkholderia isolates, both RT pathogenic and near neighbor."; RL Genome Announc. 3:0-0(2015). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP010026; AJZ57543.1; -; Genomic_DNA. DR EnsemblBacteria; AJZ57543; AJZ57543; OI25_2897. DR KEGG; bfn:OI25_2897; -. DR PATRIC; fig|134537.4.peg.3076; -. DR KO; K03665; -. DR Proteomes; UP000032614; Chromosome 1. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000032614}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}. FT DOMAIN 191 362 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 157 184 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 390 AA; 42910 MW; E159C4CC52E8F27D CRC64; MINAALVGID FGKIDFEASL EELSLLAQSA GANPIVTLTG RRSSPDAKMF VGSGKAEELR LACEANDIEL VIFNHALAPA QQRNLEQALN RRVIDRTSLI LDIFAQRARS HEGKLQVELA QLQYLSTRLI RAWTHLERQK GGIGLRGPGE TQLETDRRLI GERIKALKTR LEKLRRQHGT QRRARSRNQT MSVSLVGYTN AGKSTLFNAL TKAQAYAADQ LFATLDTTSR RVYLGDEAGQ VVVSDTVGFI RELPHQLVAA FRATLEETIH ADLLLHVVDA SSAVRLDQID QVNEVLHAIG ADTIRQVLVF NKIDAVPELA ARGDAVERDE YGNISRVFLS ARTGQGLDTL RAAIAEIATA EPLSDTLVDL SEEDRSAAPR EDRKVSELGH // ID A0A0D5YS52_9FLAO Unreviewed; 402 AA. AC A0A0D5YS52; DT 27-MAY-2015, integrated into UniProtKB/TrEMBL. DT 27-MAY-2015, sequence version 1. DT 07-JUN-2017, entry version 15. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=VC82_1468 {ECO:0000313|EMBL:AKA35090.1}; OS Muricauda lutaonensis. OC Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales; OC Flavobacteriaceae; Muricauda. OX NCBI_TaxID=516051 {ECO:0000313|EMBL:AKA35090.1, ECO:0000313|Proteomes:UP000032726}; RN [1] {ECO:0000313|EMBL:AKA35090.1, ECO:0000313|Proteomes:UP000032726} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CC-HSB-11 {ECO:0000313|EMBL:AKA35090.1, RC ECO:0000313|Proteomes:UP000032726}; RA Kim K.M.; RT "Complete genome sequence of Muricauda lutaonensis CC-HSB-11T, RT isolated from a coastal hot spring."; RL Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP011071; AKA35090.1; -; Genomic_DNA. DR RefSeq; WP_045801787.1; NZ_CP011071.1. DR EnsemblBacteria; AKA35090; AKA35090; VC82_1468. DR KEGG; mlt:VC82_1468; -. DR PATRIC; fig|516051.4.peg.1515; -. DR KO; K03665; -. DR Proteomes; UP000032726; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000032726}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000032726}. FT DOMAIN 200 385 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 402 AA; 46270 MW; FDEB3431227956BD CRC64; MLEERNIALE KTVLIGIINQ SQNAEKVAEY LDELEFLTYT AGGEVVKRFV QRMEVPNPKT FIGSGKMEEV QRFVKENEVG AVIFDDELTP AQQNNIEKIL RCKILDRTGL ILDIFAQRAQ TSYARTQVEL AQYEYLLPRL TGLWTHLERQ RGGIGMRGPG ETEIETDRRI VRDRIALLKK KLAKIDKQME TQRGNRGSLV RVALVGYTNV GKSTLMNVIS KSDVFAENKL FATLDTTVRK VVIGNLPFLL SDTVGFIRKL PTQLVESFKS TLDEVREADM LLHVVDISHP NFEEHIESVN QILDEIGSAD KKTIMVFNKI DLYRPETIDE DDLTTEKTSA HLTLEEWQKT WYNRVGDDVL FISALNKENL DEFRKKVYDA VREIHVSRFP YNNFLYPEHL EE // ID A0A0D6A4P5_9LACO Unreviewed; 427 AA. AC A0A0D6A4P5; DT 27-MAY-2015, integrated into UniProtKB/TrEMBL. DT 27-MAY-2015, sequence version 1. DT 07-JUN-2017, entry version 17. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=LBAT_1408 {ECO:0000313|EMBL:BAQ57797.1}; OS Lactobacillus acetotolerans. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; OC Lactobacillus. OX NCBI_TaxID=1600 {ECO:0000313|EMBL:BAQ57797.1, ECO:0000313|Proteomes:UP000035709}; RN [1] {ECO:0000313|EMBL:BAQ57797.1, ECO:0000313|Proteomes:UP000035709} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NBRC 13120 {ECO:0000313|EMBL:BAQ57797.1, RC ECO:0000313|Proteomes:UP000035709}; RA Toh H., Morita H., Fujita N.; RT "Complete genome sequence of Lactobacillus acetotolerans NBRC 13120."; RL Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AP014808; BAQ57797.1; -; Genomic_DNA. DR RefSeq; WP_054682202.1; NZ_LTDX01000002.1. DR EnsemblBacteria; BAQ57797; BAQ57797; LBAT_1408. DR KEGG; lae:LBAT_1408; -. DR PATRIC; fig|1600.4.peg.1438; -. DR KO; K03665; -. DR Proteomes; UP000035709; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000035709}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000035709}. FT DOMAIN 205 374 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 427 AA; 48235 MW; 34615603C5E789B3 CRC64; MIDNEPHKTK AYIAGVNLND PNFDYYMTEL ANLTEANNME VVGQSRQNTE QIVAGTYFGL GKINEIKSMA HGLKAKVLVL NDELSPVQIR NLEKLTKLRV IDRTELILEI FANRAKTKQA KLQVQLARLQ YELPRLHPSE NSLDQQRGNG GSTGGGFANR GAGESKLEMN RRTIDKQISA IKKELKKVAN QEDIKSKRRN KKQIPKVALV GYTNAGKSTT MNGLLKEFTD ESSDKEVFVK NMLFATLDTS VRRIDLNKNF SFILSDTVGF ISKLPHNLVE SFKATLQEAK DADLLINVVD ASDPNMIQMI RTTQSVLREI GIKNIPMITA YNKADKTDRN YPQIEGNDIL YSATDEKSIK LLAKLITKRV FANYKKFNLL LPLSDGKTLA YLHEHAQVMK ESYENDGVHA EVRLAPENQE RFKKYLV // ID A0A0D6ADM4_9CHRO Unreviewed; 558 AA. AC A0A0D6ADM4; DT 27-MAY-2015, integrated into UniProtKB/TrEMBL. DT 27-MAY-2015, sequence version 1. DT 07-JUN-2017, entry version 17. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=GM3708_1269 {ECO:0000313|EMBL:BAQ60863.1}; OS Geminocystis sp. NIES-3708. OC Bacteria; Cyanobacteria; Oscillatoriophycideae; Chroococcales; OC Chroococcaceae; Geminocystis. OX NCBI_TaxID=1615909 {ECO:0000313|EMBL:BAQ60863.1, ECO:0000313|Proteomes:UP000060542}; RN [1] {ECO:0000313|EMBL:BAQ60863.1, ECO:0000313|Proteomes:UP000060542} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NIES-3708 {ECO:0000313|EMBL:BAQ60863.1, RC ECO:0000313|Proteomes:UP000060542}; RA Hirose Y.; RT "Geminocystis sp. NIES-3708 complete genome sequence."; RL Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AP014815; BAQ60863.1; -; Genomic_DNA. DR RefSeq; WP_066344932.1; NZ_AP014815.1. DR EnsemblBacteria; BAQ60863; BAQ60863; GM3708_1269. DR KEGG; gee:GM3708_1269; -. DR PATRIC; fig|1615909.3.peg.1295; -. DR KO; K03665; -. DR Proteomes; UP000060542; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000060542}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000060542}. FT DOMAIN 393 558 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 352 389 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 558 AA; 61942 MW; 90F8D58E840EF407 CRC64; MTTENIYGNL QGLKPNQLKQ LQKLYHQRIR SDRLTTTELA ERIAAISTDL KQPVCVYLNR RGQVIRVGVG TPRQTQIPPL ELPRYGAERL SGIRCLATSL KSDAPSEACL TAMARQRLDA LVMFSLTGGG VMRKGGGASG FIKDTYLAHL LPISENDTYW EVSSPQDLED LAEQDFLDLV DSLEAEFSRE FIAQDVSSQE DKVLLVGLMT AKMTEQKFQD SLQELALLVD SAGGKILATI EQKRSNPHPQ TLVGAGKVEE IALQVQTLGA NLVAFDRELS PAQVRNLELQ FGVRVVDRTE VILDIFAQRA QSGAGKLQVE LAQLEYMLPR LTGRGQAMSR LGGGIGTRGP GETKLETERR AIKKRITRLQ QEVNQLQNHR SRLRQQRQQQ EIPSVAIVGY TNAGKSTLIN ALTNAEVYAA DKLFATLDPT TRRLTITDKN TSESRTILLT DTVGFIHELP PQLVDSFRAT LEEVTEADAM LHVVDLSHPT WESQINSVKA ILADMPLAPN IELIVFNKID KADSEHLETA KNNYPQALFI SAEKRLGLET LRSRLVNF // ID A0A0D6B292_RHOSU Unreviewed; 429 AA. AC A0A0D6B292; DT 27-MAY-2015, integrated into UniProtKB/TrEMBL. DT 27-MAY-2015, sequence version 1. DT 05-JUL-2017, entry version 16. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=NHU_02124 {ECO:0000313|EMBL:BAQ69278.1}; OS Rhodovulum sulfidophilum (Rhodobacter sulfidophilus). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae; Rhodovulum. OX NCBI_TaxID=35806 {ECO:0000313|EMBL:BAQ69278.1, ECO:0000313|Proteomes:UP000064912}; RN [1] {ECO:0000313|EMBL:BAQ69278.1, ECO:0000313|Proteomes:UP000064912} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 2351 {ECO:0000313|EMBL:BAQ69278.1, RC ECO:0000313|Proteomes:UP000064912}; RA Nagao N.; RT "Genome sequene of Rhodovulum sulfidophilum DSM 2351."; RL Submitted (FEB-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AP014800; BAQ69278.1; -; Genomic_DNA. DR EnsemblBacteria; BAQ69278; BAQ69278; NHU_02124. DR KEGG; rsu:NHU_02124; -. DR PATRIC; fig|35806.4.peg.2187; -. DR KO; K03665; -. DR Proteomes; UP000064912; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000064912}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000064912}. FT DOMAIN 209 378 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 429 AA; 47255 MW; BDC00A265897A28C CRC64; MSPSEAEGSE PRITRAWVLH PDIASDRERR DAGPALEEAV ALAGALPDLE VVGAETVPLA RPRAGHLFGS GKIDELKERL GEAEVELVLI DGPVSPVQQR NLEKAWKVKI LDRTGLILEI FADRARTREG VLQVELAALS YQRTRLVRAW THLERQRGGL GFVGGPGETQ IEADRRAIDE AITRIRRQLS KVVKTRDLHR AARRKVPFPI VALVGYTNAG KSTLFNRLTG AEVLAKDMLF ATLDPTMRAV ALPTGLKVIL SDTVGFISDL PTQLVAAFRA TLEEVLEADL VLHVRDIAHP DSDAQAEDVR AILADLGVAR ETPQIEVWNK TDLLDPERRA ATEAAAARHD EVAAISAWTG QGVGPLLQAV TERLDAARQR RDLHLAHDDG RRRAWLYEQG IVEGEAPDDE GSTLTVNWTA RQEQRFRSL // ID A0A0D6DYC0_9LACT Unreviewed; 412 AA. AC A0A0D6DYC0; DT 27-MAY-2015, integrated into UniProtKB/TrEMBL. DT 27-MAY-2015, sequence version 1. DT 07-JUN-2017, entry version 15. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=LACPI_1752 {ECO:0000313|EMBL:CEN28952.1}; OS Lactococcus piscium MKFS47. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Lactococcus. OX NCBI_TaxID=297352 {ECO:0000313|EMBL:CEN28952.1, ECO:0000313|Proteomes:UP000033166}; RN [1] {ECO:0000313|EMBL:CEN28952.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=MKFS47 {ECO:0000313|EMBL:CEN28952.1}; RA Andreevskaya Margarita; RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LN774769; CEN28952.1; -; Genomic_DNA. DR RefSeq; WP_047915994.1; NZ_LN774769.1. DR EnsemblBacteria; CEN28952; CEN28952; LACPI_1752. DR KEGG; lpk:LACPI_1752; -. DR KO; K03665; -. DR Proteomes; UP000033166; Chromosome I. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000033166}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000033166}. FT DOMAIN 201 361 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 412 AA; 45949 MW; 86C0BE3B346C1A75 CRC64; MIATEIAAEK VVLVGAETYG NRETFDVSLL ELASLAETAG ALVHETFTQK KERLDGKYVV GIGKLEEIKI TIEADDIDMV IFNEKLTPRQ NVNLETFLGV KVIDRMQLIL DIFALRARSH VGMLQVELAQ LKYLLPRLSG SKGLELSRQG GGIGARGAGE SQLETDRRHI RHRVEMIESQ LKKAEKVQEN SRQKRNASSV FKLGLIGYTN AGKSSVFNAL TNKIQYEKDE LFATLDATTK EFSLKDEFMV TMTDTVGFIQ DLPTELVQAF KSTLAESKNV DLLLHIVDAS NPAHSLHEDV VTDIMSSLNM SDIPVLTVYN KLDLAEHFSP TVLPNVQISI KSEAGIARLR QAIIDKISEL FTPFDLKIPF SEAYRLPMIK KIALIDQIIE LDEEEVYAVS GSISQADKWR IV // ID A0A0D6EVV1_9PROT Unreviewed; 378 AA. AC A0A0D6EVV1; DT 27-MAY-2015, integrated into UniProtKB/TrEMBL. DT 27-MAY-2015, sequence version 1. DT 30-AUG-2017, entry version 17. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:CEZ19767.1}; GN ORFNames=BN1208_0882 {ECO:0000313|EMBL:CEZ19767.1}; OS Candidatus Methylopumilus planktonicus. OC Bacteria; Proteobacteria; Betaproteobacteria; Nitrosomonadales; OC Methylophilaceae; Candidatus Methylopumilus. OX NCBI_TaxID=1581557 {ECO:0000313|EMBL:CEZ19767.1, ECO:0000313|Proteomes:UP000064007}; RN [1] {ECO:0000313|EMBL:CEZ19767.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=MMS-10A-171 {ECO:0000313|EMBL:CEZ19767.1}; RA Salcher M Michaela; RL Submitted (DEC-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LN827929; CEZ19767.1; -; Genomic_DNA. DR RefSeq; WP_046488256.1; NZ_LN827929.1. DR EnsemblBacteria; CEZ19767; CEZ19767; BN1208_0882. DR KEGG; mbat:BN1208_0882; -. DR KO; K03665; -. DR Proteomes; UP000064007; Chromosome 1. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000064007}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000064007}. FT DOMAIN 199 365 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 158 192 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 378 AA; 42703 MW; D844E6CD607932BE CRC64; MFERPNEGKS ACVISINFGD NDFEESVEEI KELVLSADMN IVSTVNIKRS APDPKYFLGS GKAEEVKFII QESKADTVIF NHNLSPSQER NLEKYFSTRI FDRTALILLI FAKRAKSHEG KLQVELAQLD HLSTRLIKGW SHLERQKGGI GVRGGPGEKQ LELDRRMLKL RIKQLKEKLD KLKRQRTMQR KKRSRSNVLN ISIVGYTNAG KSTLFNQLTH ANALAMNQLF ATLDTTSRKL FIQEGVECVI SDTVGFIKAL PTTLIEAFKS TLEESREADL LLHVVNMANP NHSEQIIAVN KILEEIKAAS IPQILVLNQI DRLDIKANHE KDEYGRISTI QLSAKTGEGI ELLKEAILQL YVAKHSAETE IFEENPLN // ID A0A0D6JJ60_9RHIZ Unreviewed; 466 AA. AC A0A0D6JJ60; DT 27-MAY-2015, integrated into UniProtKB/TrEMBL. DT 27-MAY-2015, sequence version 1. DT 12-APR-2017, entry version 14. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:CPR21605.1}; GN ORFNames=YBN1229_v1_3123 {ECO:0000313|EMBL:CPR21605.1}; OS Candidatus Filomicrobium marinum. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Hyphomicrobiaceae; Filomicrobium. OX NCBI_TaxID=1608628 {ECO:0000313|EMBL:CPR21605.1, ECO:0000313|Proteomes:UP000033187}; RN [1] {ECO:0000313|Proteomes:UP000033187} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=strain Y {ECO:0000313|Proteomes:UP000033187}; RA Chooi Y.-H.; RL Submitted (FEB-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LN829119; CPR21605.1; -; Genomic_DNA. DR EnsemblBacteria; CPR21605; CPR21605; BN1229_v1_3123. DR KEGG; fil:BN1229_v1_2790; -. DR KEGG; fiy:BN1229_v1_3123; -. DR KO; K03665; -. DR Proteomes; UP000033187; Chromosome 1. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000033187}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000033187}. FT DOMAIN 232 405 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 466 AA; 51556 MW; 664AC18FDA4124A8 CRC64; MATPPTKAPL LLRKTGSDRP SAIVLVPVLP TRRTGTDVSV RTDTSQNSVH SPEERATEAR GLAEAIDLDV RETLIVPVAT PRPATLFGSG KVEELRELIA ESEITLAVID HAISPVQQRN LERAWNIKVL DRTGLILEIF GARARTREGR LQVELAHLSY QKGRLVRAWT HLERQRGGGG GGASFLGGPG EAQIELDRRM LQTRIDAIRR ELNQVVKTRA LHRKGRRKVP YPIVAIVGYT NAGKSTLFNR ITGASVLAKD QVFATLDPTM REVRLASGRQ IILSDTVGFI SDLPTSLVAA FRATLEEVIE ADLILHVRDI SHAESELQRQ DVERVLADLD IDLTPTDRPI LEVWNKIDLL PSDVRGVTEA TAQRQENRPA LVSAQTGEGI EDLLAAIDTR LGADDTYLTL VVPAREGKLL SWLHDNSEIL ERTVDDNGET TLRLRIAAEK RGRLLAQLQH LRLRVQ // ID A0A0D6KIA0_9CYAN Unreviewed; 517 AA. AC A0A0D6KIA0; DT 27-MAY-2015, integrated into UniProtKB/TrEMBL. DT 27-MAY-2015, sequence version 1. DT 07-JUN-2017, entry version 17. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=FDUTEX481_03358 {ECO:0000313|EMBL:EKE99165.1}; OS Tolypothrix sp. PCC 7601. OC Bacteria; Cyanobacteria; Nostocales; Tolypothrichaceae; Tolypothrix. OX NCBI_TaxID=1188 {ECO:0000313|EMBL:EKE99165.1, ECO:0000313|Proteomes:UP000032761}; RN [1] {ECO:0000313|EMBL:EKE99165.1, ECO:0000313|Proteomes:UP000032761} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=PCC 7601 / UTEX B 481 {ECO:0000313|Proteomes:UP000032761}; RX PubMed=25953173; RA Yerrapragada S., Shukla A., Hallsworth-Pepin K., Choi K., Wollam A., RA Clifton S., Qin X., Muzny D., Raghuraman S., Ashki H., Uzman A., RA Highlander S.K., Fryszczyn B.G., Fox G.E., Tirumalai M.R., Liu Y., RA Kim S., Kehoe D.M., Weinstock G.M.; RT "Extreme Sensory Complexity Encoded in the 10-Megabase Draft Genome RT Sequence of the Chromatically Acclimating Cyanobacterium Tolypothrix RT sp. PCC 7601."; RL Genome Announc. 3:0-0(2015). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EKE99165.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGCR01000074; EKE99165.1; -; Genomic_DNA. DR EnsemblBacteria; EKE99165; EKE99165; FDUTEX481_03358. DR PATRIC; fig|1188.3.peg.7436; -. DR Proteomes; UP000032761; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000032761}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000032761}. FT DOMAIN 344 514 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 303 337 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 517 AA; 56782 MW; C087B4D2005BA0A2 CRC64; MGVGTPRQTQ IPPLELPRYG AERLSGIRCI ATNLKPEPPN EAALTAMALQ RLDVLVVLNI TGAGFTRRGG GATGYVKEAY LAHLTPQDSR ALITSPAVLK TGSNNIQSPT WTVSQPLSLD ELAQQDFIDL VENLEAEFQR EFVAQEVDVD HDRVLIVGVM TDEMTPLQFQ DTLAELARLV DTAGGDVLQT VQQKRSRIHP QTVVGEGKVQ EVALTAQTLG ANLVVFDRDL SPAQVRNLEA QIGVRVVDRT EVILDIFAQR AQSGAGKLQV ELAQLEYMLP RLTGRGQAMS RLGGGIGTRG PGETKLETER RAIQRRISRL QQEVNQLQAH RSRLRQRRQH REVPSVALVG YTNAGKSTLL NALTNAEVYT ADQLFATLDP TTRRLVISDA ETGATQEILL TDTVGFIHEL PASLMDAFRA TLEEVTEADA LLHLVDLSHP AWLSHIRSVR EILAQMPVTP GPALVAFNKI DQVSSETLAL AREEFPLAVF ISASQRLGLE TLRHRLTQLI QYAVDSR // ID A0A0D6MKM1_9PROT Unreviewed; 434 AA. AC A0A0D6MKM1; DT 27-MAY-2015, integrated into UniProtKB/TrEMBL. DT 27-MAY-2015, sequence version 1. DT 07-JUN-2017, entry version 15. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=Tasa_014_016 {ECO:0000313|EMBL:GAN53995.1}; OS Tanticharoenia sakaeratensis NBRC 103193. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales; OC Acetobacteraceae; Tanticharoenia. OX NCBI_TaxID=1231623 {ECO:0000313|EMBL:GAN53995.1, ECO:0000313|Proteomes:UP000032679}; RN [1] {ECO:0000313|EMBL:GAN53995.1, ECO:0000313|Proteomes:UP000032679} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NBRC 103193 {ECO:0000313|EMBL:GAN53995.1, RC ECO:0000313|Proteomes:UP000032679}; RA Azuma Y., Hadano H., Hirakawa H., Matsushita K.; RT "Genome sequencing of Tanticharoenia sakaeratensis NBRC 103193."; RL Submitted (OCT-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:GAN53995.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BALE01000014; GAN53995.1; -; Genomic_DNA. DR RefSeq; WP_048848496.1; NZ_BALE01000014.1. DR EnsemblBacteria; GAN53995; GAN53995; Tasa_014_016. DR Proteomes; UP000032679; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000032679}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000032679}. FT DOMAIN 207 376 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 434 AA; 47817 MW; 570B363916119665 CRC64; MSLHETAPKA TRAAVILPWE KPHPQDEIRA AEARLEEAVG LAASIGLVIV RQAVVLLRAR RPATLLGSGQ VEQLAEAVKA DDVTVVIIDA RLSPGQQRNL EKALNCKVMD RTGLILDIFG ARAATREGVL QVELAHLEYQ RSRLVRLWTH LERQRGGFGF LGGPGETQIE ADRRMIGERI VRLRRELDQV RRTRGLHRSA RRRVPFPIVA LVGYTNAGKS TLFNAVTGAA VHAQDQLFAT LDPTMRSLRL PSGRQIILSD TVGFISDLPT ELIAAFRATL EEVSEADVIL HVRDVAHPDS TAQRADVVGV LSDMAKDGML DPNWPERTIE VLNKADLLGG VDAVPKRPGA VAISAITGDG LPDLFEMLDR HLTAAMQTVR VRLDVSDGAA LAWLYAHGEV VERLDREEII ELDVRLFAQD RDRFETYHPG LILA // ID A0A0D6MUN4_ACEAC Unreviewed; 439 AA. AC A0A0D6MUN4; DT 27-MAY-2015, integrated into UniProtKB/TrEMBL. DT 27-MAY-2015, sequence version 1. DT 10-MAY-2017, entry version 14. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=Abac_013_020 {ECO:0000313|EMBL:GAN57058.1}; OS Acetobacter aceti NBRC 14818. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales; OC Acetobacteraceae; Acetobacter; Acetobacter subgen. Acetobacter. OX NCBI_TaxID=887700 {ECO:0000313|EMBL:GAN57058.1, ECO:0000313|Proteomes:UP000032677}; RN [1] {ECO:0000313|EMBL:GAN57058.1, ECO:0000313|Proteomes:UP000032677} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NBRC 14818 {ECO:0000313|EMBL:GAN57058.1, RC ECO:0000313|Proteomes:UP000032677}; RA Azuma Y., Higashiura N., Hirakawa H., Matsushita K.; RT "Whole genome sequence of Acetobacter aceti NBRC 14818."; RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:GAN57058.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BAMU01000013; GAN57058.1; -; Genomic_DNA. DR EnsemblBacteria; GAN57058; GAN57058; Abac_013_020. DR Proteomes; UP000032677; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000032677}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000032677}. FT DOMAIN 209 378 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 439 AA; 48397 MW; 0D0DEBC44BE4CB4E CRC64; MSTIPTETAT PATRAAVILP WEKPDRDQDV RAAEARLDEA VGLTSSIGLV VVLKAVLLLR ARRPATLLGT GQVESLREAV AEKEIKVVVI DAKLSPGQQR NLEKALGCKV IDRTGLILDI FGARAATREG SLQVELAHLE YQRSRLVRLW THLERQRGGF GFLGGPGETQ IEADRRIIGD RIVRLKRELE QVRRTRGLHR SARKRVPFPV VALVGYTNAG KSTLFNALTG ASVYAQDQLF ATLDPTMRAI RLPSGRQVIL SDTVGFISDL PTELIAAFRA TLEEVAEADI ILHVRDIAHP DTAAQRSDVL SVLSGMERDG MLDHEWRSRV IEVLNKADLL GGPEQVEHHG TAVPISAITG DGLPELMAAI DAHMVHAMEL LRYSIPVEAG EALAWLYQHG EVVTREDHET HMDVLVRLRE ADRARFEGQF GDLVKKTDV // ID A0A0D6NGB7_9PROT Unreviewed; 438 AA. AC A0A0D6NGB7; DT 27-MAY-2015, integrated into UniProtKB/TrEMBL. DT 27-MAY-2015, sequence version 1. DT 07-JUN-2017, entry version 17. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=Abor_006_061 {ECO:0000313|EMBL:GAN65107.1}; OS Acetobacter orientalis 21F-2. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales; OC Acetobacteraceae; Acetobacter. OX NCBI_TaxID=1231341 {ECO:0000313|EMBL:GAN65107.1, ECO:0000313|Proteomes:UP000032670}; RN [1] {ECO:0000313|EMBL:GAN65107.1, ECO:0000313|Proteomes:UP000032670} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=21F-2 {ECO:0000313|EMBL:GAN65107.1, RC ECO:0000313|Proteomes:UP000032670}; RA Azuma Y., Higashiura N., Hirakawa H., Matsushita K.; RT "Whole genome sequence of Acetobacter orientalis 21F-2."; RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:GAN65107.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BAMX01000006; GAN65107.1; -; Genomic_DNA. DR RefSeq; WP_048840165.1; NZ_BAMX01000006.1. DR EnsemblBacteria; GAN65107; GAN65107; Abor_006_061. DR Proteomes; UP000032670; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000032670}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000032670}. FT DOMAIN 209 378 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 438 AA; 48135 MW; 28A4B28F45BD7E0E CRC64; MATTLSDTKP TATRGAVILP WERSAHEQDV RAAEARLEEA VGLAASIGLV IVRQAVLLLR TKRSATLLGV GQVDSLKIAV KADGIDVLVV DARLTPGQQR NLEREFGCKV IDRTGLILDI FGARAATKEG TLQVELAHLE YQRSRLVRLW THLERQRGGF GFLGGPGETQ MEADRRMIGE RIVKLKKELE QVRRTRGLHR QARKRVPFPV VALVGYTNAG KSTLFNALTG ATVYAKDQLF ATLDPTMRAI TLPSGRRIIL SDTVGFISDL PTELIAAFRA TLEEVSEADI ILHVRDIAHP DSAAQKKDVF GVLNGMARDD MIEADWAGRM IEVMNKADLL GGPEAVPQTE ETVAISAITG DGLPELMALI DRHITASMEA VRYRMPLAHG AAAAWLYQHG EVTQREDDET STTLTVRLLA EDRARFETQF KDIEPLVA // ID A0A0D6NV33_9PROT Unreviewed; 428 AA. AC A0A0D6NV33; DT 27-MAY-2015, integrated into UniProtKB/TrEMBL. DT 27-MAY-2015, sequence version 1. DT 10-MAY-2017, entry version 15. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=Abol_029_022 {ECO:0000313|EMBL:GAN69226.1}; OS Acetobacter orleanensis JCM 7639. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales; OC Acetobacteraceae; Acetobacter. OX NCBI_TaxID=1231342 {ECO:0000313|EMBL:GAN69226.1, ECO:0000313|Proteomes:UP000032676}; RN [1] {ECO:0000313|EMBL:GAN69226.1, ECO:0000313|Proteomes:UP000032676} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=JCM 7639T {ECO:0000313|EMBL:GAN69226.1, RC ECO:0000313|Proteomes:UP000032676}; RA Azuma Y., Higashiura N., Hirakawa H., Matsushita K.; RT "Whole genome sequence of Acetobacter orleanensis JCM 7639T."; RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:GAN69226.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BAMY01000026; GAN69226.1; -; Genomic_DNA. DR EnsemblBacteria; GAN69226; GAN69226; Abol_029_022. DR Proteomes; UP000032676; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000032676}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000032676}. FT DOMAIN 199 368 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 428 AA; 47227 MW; A0BB81A112EF5ED2 CRC64; MATRGAVILP WEKSAHDQDV RAAEARLEEA VGLAASIGLV IVLQATLLLR ARRSATLLGK GQVDSLKIAV QAEKIDVLVV DARLSPAQQR NLETAFGCKV IDRTGLILDI FGARAATKEG TLQVELAHLE YQRSRLVRLW THLERQRGGF GFLGGPGETQ IEADRRMIGD RIVRLKKDLE QVRRTRGLHR QARKRVPFPV VALVGYTNAG KSTLFNALTG AAVYAKDQLF ATLDPTMRAI TLPSGRRIIL SDTVGFISDL PTELIAAFRA TLEEVAEADI ILHVRDIAHP DSAAQKKDVF HVLDGMARDN MIEPDWSSRM IEVLNKVDLL GGPEELAQLG DATAISAMTG DGLPELMALI DRQMTEAMEE VRYRVPLSDG AASAWLYQHG EVLDRTDDES CANIFVRIKA EDRARFEMLF KQVEPILA // ID A0A0D6NXN3_9PROT Unreviewed; 439 AA. AC A0A0D6NXN3; DT 27-MAY-2015, integrated into UniProtKB/TrEMBL. DT 27-MAY-2015, sequence version 1. DT 07-JUN-2017, entry version 16. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=Absy_003_133 {ECO:0000313|EMBL:GAN70111.1}; OS Acetobacter syzygii 9H-2. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales; OC Acetobacteraceae; Acetobacter. OX NCBI_TaxID=1231343 {ECO:0000313|EMBL:GAN70111.1, ECO:0000313|Proteomes:UP000032666}; RN [1] {ECO:0000313|EMBL:GAN70111.1, ECO:0000313|Proteomes:UP000032666} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=9H-2 {ECO:0000313|EMBL:GAN70111.1, RC ECO:0000313|Proteomes:UP000032666}; RA Azuma Y., Higashiura N., Hirakawa H., Matsushita K.; RT "Whole genome sequence of Acetobacter syzygii 9H-2."; RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:GAN70111.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BAMZ01000003; GAN70111.1; -; Genomic_DNA. DR RefSeq; WP_048852822.1; NZ_BAMZ01000003.1. DR EnsemblBacteria; GAN70111; GAN70111; Absy_003_133. DR Proteomes; UP000032666; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000032666}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000032666}. FT DOMAIN 210 379 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 439 AA; 48716 MW; 95C3FECB098D70B1 CRC64; MATSFTEKKQ TVATRAAVIL PWERSAHGQD VRAAEARLEE AVGLTASIGL VIVRKAVLLL RARRSATLLG KGQIDSLRIA VKADNIDVLV VDTKLTPAQQ RNLETEFGCK VIDRTGLILD IFGARAATRE GTLQVELAHL EYQRSRLVRL WTHLERQRGG FGFLGGPGET QIEADRRMIG ERIVRLKKDL EQVRRTRGLH RQARKRVPFP VVALVGYTNA GKSTLFNALT GATVYAQDQL FATLDPTMRA IELPSGRQVI LSDTVGFISD LPTELIAAFR ATLEEVAEAD IILHVRDIAH PDSTTQKKDV LGVLESMAKD NMLEQDWPNR MIEVLNKVDL LGGQAAVPQG DETVAISAIT GDGLDRLLAR IDQRITSGME VVRYAMPLAD GAALAWLYQH GEVVDRKDQE EETDITVRLL AEDRARFERQ FRHITPQMA // ID A0A0D6P2E0_9PROT Unreviewed; 446 AA. AC A0A0D6P2E0; DT 27-MAY-2015, integrated into UniProtKB/TrEMBL. DT 27-MAY-2015, sequence version 1. DT 07-JUN-2017, entry version 16. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=Asru_0024_08 {ECO:0000313|EMBL:GAN75925.1}; OS Acidisphaera rubrifaciens HS-AP3. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales; OC Acetobacteraceae; Acidisphaera. OX NCBI_TaxID=1231350 {ECO:0000313|EMBL:GAN75925.1, ECO:0000313|Proteomes:UP000032680}; RN [1] {ECO:0000313|EMBL:GAN75925.1, ECO:0000313|Proteomes:UP000032680} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=HS-AP3 {ECO:0000313|EMBL:GAN75925.1, RC ECO:0000313|Proteomes:UP000032680}; RA Azuma Y., Higashiura N., Hirakawa H., Matsushita K.; RT "Whole genome sequence of Acidisphaera rubrifaciens HS-AP3."; RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:GAN75925.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BANB01000024; GAN75925.1; -; Genomic_DNA. DR RefSeq; WP_048859674.1; NZ_BANB01000024.1. DR EnsemblBacteria; GAN75925; GAN75925; Asru_0024_08. DR Proteomes; UP000032680; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000032680}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000032680}. FT DOMAIN 216 390 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 446 AA; 48099 MW; F20301723C02D3F7 CRC64; MTEEPGRAAR GAAPQAGPTR AAVILPWERP DGTADATRAA DARLSEAIGL AASIGLIIVH SAIVPLRGRR PATLLGSGQV EAQHRELETA EVTVTIVDAA LSPVQQRNLE RAWGCKVIDR TGLILDIFGE RAATREGTLQ VELAHLEYQR SRLVRSWTHL ERQRGGFGFL GGPGETQIEA DRRLIGDRIV RLKKELEQVR RTRGLHRSAR RRVPFPVVAL VGYTNAGKST LFNALTGAEV TARDQLFATL DPTMRGLRLP SGRRAILSDT VGFISELPTE LVAAFRATLE EVAEADVILH VRDAAHPDTQ GQRADVIAVL DGLAAEGTLD ADWPDRTIEV LNKADLLGGV AEVPLRLGGV GDSAVAVSAI TGEGLEALRD AVDGRIAAGM EVASYDIPPE DGARLAWLYR HGEVVTRSDH SDAIRLTVRL LPADRARFER PDALAE // ID A0A0D6PGF0_9PROT Unreviewed; 413 AA. AC A0A0D6PGF0; DT 27-MAY-2015, integrated into UniProtKB/TrEMBL. DT 27-MAY-2015, sequence version 1. DT 10-MAY-2017, entry version 14. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=Aam_055_102 {ECO:0000313|EMBL:GAN80722.1}; OS Acidocella aminolytica 101 = DSM 11237. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales; OC Acetobacteraceae; Acidocella. OX NCBI_TaxID=1120923 {ECO:0000313|EMBL:GAN80722.1, ECO:0000313|Proteomes:UP000032668}; RN [1] {ECO:0000313|EMBL:GAN80722.1, ECO:0000313|Proteomes:UP000032668} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=101 / DSM 11237 {ECO:0000313|Proteomes:UP000032668}; RA Azuma Y., Higashiura N., Hirakawa H., Matsushita K.; RT "Whole genome sequence of Acidocella aminolytica 101 = DSM 11237."; RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:GAN80722.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BANC01000054; GAN80722.1; -; Genomic_DNA. DR EnsemblBacteria; GAN80722; GAN80722; Aam_055_102. DR Proteomes; UP000032668; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000032668}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000032668}. FT DOMAIN 194 362 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 413 AA; 45048 MW; C490BE106152599B CRC64; MLPWDRQAAF AASQTRSAEA RLAEAVGLAA SIGLVIVHEQ VFPLRTITPA TLLGKGQVEA AAAALRAAQV DVVVVDAALT PVQQRNLEKA WGTKVIDRTG LILDIFGARA RTREGALQVE LAHLEYQRSR LVRSWTHLER QRGGFGFLGG PGETQIEADR RLIGDRIVRL KAELEDVRRT RGLHRGARKK VPYPIVALVG YTNAGKSTLF NALTGATVMA EDQLFATLDP TMRGLVLPSG RNIILSDTVG FISELPTELV AAFRATLEEV AEADLLLHVR DVSHPDTEAQ AKDVRNVLNR MAKEGALDED WPIRTLEVLN KADVLGGIEH VVQGEGIAVS ALTGEGLPQL LADIDSRLAA AQEVFTLEVP VSDGARIAWL YRHGEVLFRT DDETHVKLEV RLSATDKARF ETL // ID A0A0D6T0P3_9PSED Unreviewed; 433 AA. AC A0A0D6T0P3; DT 27-MAY-2015, integrated into UniProtKB/TrEMBL. DT 27-MAY-2015, sequence version 1. DT 30-AUG-2017, entry version 18. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=SZ55_0632 {ECO:0000313|EMBL:KIV74495.1}; OS Pseudomonas sp. FeS53a. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=1604022 {ECO:0000313|EMBL:KIV74495.1, ECO:0000313|Proteomes:UP000032531}; RN [1] {ECO:0000313|EMBL:KIV74495.1, ECO:0000313|Proteomes:UP000032531} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=FeS53a {ECO:0000313|EMBL:KIV74495.1, RC ECO:0000313|Proteomes:UP000032531}; RA de Souza R., Sant'Anna F.H., Ambrosini A., Tadra-Sfeir M., Faoro H., RA Alvarenga S.M., Pedrosa F.O., Souza E.M., Passaglia L.M.; RT "Genome of Pseudomonas sp. FeS53a associated with rice cropped in RT iron-stressed soils."; RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KIV74495.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JYFT01000008; KIV74495.1; -; Genomic_DNA. DR RefSeq; WP_044401176.1; NZ_JYFT01000008.1. DR EnsemblBacteria; KIV74495; KIV74495; SZ55_0632. DR PATRIC; fig|1604022.3.peg.5294; -. DR Proteomes; UP000032531; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000032531}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000032531}. FT DOMAIN 199 366 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 165 192 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 433 AA; 48861 MW; 1F9ACFB05B47DA35 CRC64; MFFERPGGGE RAVLVHLEGH DPEAREDPQE FQELARSAGA DTVAFISVSR HQPTAKYLIG SGKVEELHDL VKAEQAELVI FNHTLTPSQE RNLERAFECR VLDRTGLILD IFAQRARTHE GKLQVELAQL EHMSTRLVRG WTHLERQKGG IGLRGPGETQ LETDRRLLRV RIRQIKQRLE KVRSQREQAR RGRKRADIPS VSLVGYTNAG KSTLFNALTT SEVYAADQLF ATLDPTLRRL ELADLGPIVL ADTVGFIRHL PHKLVEAFRA TLEESSNSDL LLHVIDAHEP ERMAQIEQVL AVLGEIGADG LPMLEVYNKI DLLESMEPQI QRDEHGKPER VWLSAREGKG LELLEQAIAE LLGEDLFVGT LKLPQRLGRL RAQFFALGAV QSEQHDEAGD TLLAVRLPRV ELNRLVSREG WQPQAFIEQH TLQ // ID A0A0D6TK63_9FLAO Unreviewed; 407 AA. AC A0A0D6TK63; DT 27-MAY-2015, integrated into UniProtKB/TrEMBL. DT 27-MAY-2015, sequence version 1. DT 07-JUN-2017, entry version 17. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=SY27_11795 {ECO:0000313|EMBL:KIX20585.1}; OS Flavobacterium sp. 316. OC Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales; OC Flavobacteriaceae; Flavobacterium. OX NCBI_TaxID=1603293 {ECO:0000313|EMBL:KIX20585.1, ECO:0000313|Proteomes:UP000032747}; RN [1] {ECO:0000313|EMBL:KIX20585.1, ECO:0000313|Proteomes:UP000032747} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=316 {ECO:0000313|EMBL:KIX20585.1, RC ECO:0000313|Proteomes:UP000032747}; RA Karczewska-Golec J., Kochanowska-Lyzen M., Balut M., Golec P., RA Madanecki P., Markert S., Piotrowski A., Schweder T., RA Szalewska-Palasz A.; RT "Three Bacterial Inhabitants of the Baltic Sea under Osmotic Stress: a RT Genomic and a Proteomic Perspective."; RL Submitted (FEB-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KIX20585.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JYGZ01000005; KIX20585.1; -; Genomic_DNA. DR RefSeq; WP_045970532.1; NZ_JYGZ01000005.1. DR EnsemblBacteria; KIX20585; KIX20585; SY27_11795. DR PATRIC; fig|1603293.4.peg.2435; -. DR Proteomes; UP000032747; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000032747}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000032747}. FT DOMAIN 200 386 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 407 AA; 47311 MW; C84FEF313B4855DC CRC64; MLEIEKHEFE KTAIVGIVTQ NQDEEKLREY LDELEFLTYT AGGEVVKRFS QKMDKPNPKT FVGTGKLDEI NYYIKDNDIK TVIFDDELSP SQLKNITKEL DCKVLDRTNL ILDIFAQRAQ TSYARTQVEL AQCQYLLPRL TGMWTHLERQ RGGIGMRGPG ETEIETDRRI VRDRISLLKE KIKTIDKQMS VQRGNRGAMV RVALVGYTNV GKSTLMNAIG KSDVFVENKL FATLDTTVRK TVIKNLPFLL SDTVGFIRKL PTQLVESFKS TLDEVREADL LLHVVDISHP DFEDHISSVN DILKEIKSDN KPTIMVFNKI DAYNPIYFDY DNLEIEKEAK HYTLDEWKQT WMNKIGENNA LFISATDKLN FEEFREKVYE AVREIHITRF PYNKFLYPEY KEAMDTE // ID A0A0D6XNV7_9STAP Unreviewed; 412 AA. AC A0A0D6XNV7; DT 27-MAY-2015, integrated into UniProtKB/TrEMBL. DT 27-MAY-2015, sequence version 1. DT 07-JUN-2017, entry version 17. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=TP70_08095 {ECO:0000313|EMBL:KIX90357.1}; OS Staphylococcus microti. OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae; OC Staphylococcus. OX NCBI_TaxID=569857 {ECO:0000313|EMBL:KIX90357.1, ECO:0000313|Proteomes:UP000032366}; RN [1] {ECO:0000313|EMBL:KIX90357.1, ECO:0000313|Proteomes:UP000032366} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 22147 {ECO:0000313|EMBL:KIX90357.1, RC ECO:0000313|Proteomes:UP000032366}; RA Guo J.; RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KIX90357.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JXWY01000053; KIX90357.1; -; Genomic_DNA. DR RefSeq; WP_044360875.1; NZ_JXWY01000053.1. DR EnsemblBacteria; KIX90357; KIX90357; TP70_08095. DR PATRIC; fig|569857.6.peg.2049; -. DR Proteomes; UP000032366; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000032366}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}. FT DOMAIN 205 366 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 412 AA; 47608 MW; D152CFD54D9574F0 CRC64; MQNQQPYTTE KAREKAVLVG VDLYQSDYDF ESTMTELDAL ANTCELDVKG AFSQRKNFMD QRYYVGKGKL QEIEDFIDFH DIDVLITNDE LTTAQSKNLN QTLGIKIIDR TQLILEIFAL RAKSREGQLQ VEYAQLDYLL PRLMGHGKSL SRLGGGIGTR GPGETKLETD RRHIRTRMTE IRRKLSEVSA HRERYRQKRD QHDVFQIALV GYTNAGKSSW FNTLTDAGTY EKDQLFATLD PKTRQLKLND GFEVVISDTV GFIQKLPTTL IEAFKSTLEE AKRADLLLHV VDASHVDYKS QYDTVNDLIK TLDMEHIPQI VLFNKRDLHT GELPVTNKPM VFVSAKDQAD IEKVKSTLLT QMKQQMAYYE TEVPSHQANR LYDLKQHTLI TRLEFDETTE NYRVEGYKKY RK // ID A0A0D6YEN9_MASLA Unreviewed; 540 AA. AC A0A0D6YEN9; DT 27-MAY-2015, integrated into UniProtKB/TrEMBL. DT 27-MAY-2015, sequence version 1. DT 07-JUN-2017, entry version 19. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=SP67_23780 {ECO:0000313|EMBL:KIY11236.1}; OS Mastigocladus laminosus UU774. OC Bacteria; Cyanobacteria; Nostocales; Hapalosiphonaceae; Mastigocladus. OX NCBI_TaxID=1594576 {ECO:0000313|EMBL:KIY11236.1, ECO:0000313|Proteomes:UP000032368}; RN [1] {ECO:0000313|EMBL:KIY11236.1, ECO:0000313|Proteomes:UP000032368} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=UU774 {ECO:0000313|EMBL:KIY11236.1, RC ECO:0000313|Proteomes:UP000032368}; RA Tripathy S., Malar M.C., Sen D., Adhikary S.P.; RT "Draft whole genome shotgun sequence of Mastigocladus laminosus RT UU774."; RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KIY11236.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JXIJ01000130; KIY11236.1; -; Genomic_DNA. DR EnsemblBacteria; KIY11236; KIY11236; SP67_23780. DR PATRIC; fig|1594576.4.peg.753; -. DR Proteomes; UP000032368; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000032368}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000032368}. FT DOMAIN 367 537 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 326 367 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 540 AA; 59530 MW; 1F7583FE9A5F5868 CRC64; MAAISTEINQ PVCTYLNRRG QVIRVGVGTP RQTQIPPLEL PRYGAERLSG IRCIATHLKS EPPNESALTS MALQRLDALA VINITGTGFQ KRGGGATGYV KEAYLAHLIS QDSRTLITSP SFKPENGNVP SPSWNVSPPM SLDALTKQDL VDLVEELEEG FRREFVAQEV DTDHDRVVIV GVLTDDLSSQ QFQDIVAELG RLVDTAGGEV LQTLWQKRSR IHPQTVVGEG KVQEIALTAQ TLGANLVVFD RDLSPSQVRN LETQIGLRVV DRTEVILDIF AQRAQSRAGK LQVELAQLEY MLPRLTGRGQ AMSRLGGGIG TRGPGETKLE TERRAIGRRI SRLQQEVNQL QAHRERLRQR RQNREISSVA LVGYTNAGKS TLLNALTNAE VYTADQLFAT LDPTTRRLVV PHAATNEPQE ILITDTVGFI HELPASLMDA FRATLEEVTE ADALLHLVDL SHPAWLSHIR SVREILAQMP VTPGPALVVF NKIDQVSSET LAQAREEFPL AVFISASNRL GLETLRQRLG QLVQYATSSR // ID A0A0D6ZAZ6_9BACI Unreviewed; 419 AA. AC A0A0D6ZAZ6; DT 27-MAY-2015, integrated into UniProtKB/TrEMBL. DT 27-MAY-2015, sequence version 1. DT 07-JUN-2017, entry version 15. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=UB32_05270 {ECO:0000313|EMBL:KIY22989.1}; OS Bacillus subterraneus. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus. OX NCBI_TaxID=285983 {ECO:0000313|EMBL:KIY22989.1, ECO:0000313|Proteomes:UP000032512}; RN [1] {ECO:0000313|EMBL:KIY22989.1, ECO:0000313|Proteomes:UP000032512} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MITOT1 {ECO:0000313|EMBL:KIY22989.1, RC ECO:0000313|Proteomes:UP000032512}; RA Peet K.C., Thompson J.R.; RT "Draft genome sequences of the supercritical CO2 tolerant bacteria RT Bacillus subterraneus MITOT1 and Bacillus cereus MIT0214."; RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KIY22989.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JXIQ01000029; KIY22989.1; -; Genomic_DNA. DR RefSeq; WP_044391835.1; NZ_JXIQ01000029.1. DR EnsemblBacteria; KIY22989; KIY22989; UB32_05270. DR PATRIC; fig|285983.3.peg.3567; -. DR Proteomes; UP000032512; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000032512}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000032512}. FT DOMAIN 200 362 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 419 AA; 47993 MW; 7A0B29DD9A513E4D CRC64; MEQDTVFEKV ILVGCQTTED EDLRFQYSME ELESLTETAK GKVLMQIVQK RPKIHPATYI GKGKVEELQA LVDELEPDLI IFNDELSPSQ NRNLSSGLKA RIIDRTQLIL DIFAQRARSK EGKLQVELAQ LQYLLPRLSG QGIEMSRLGA GIGTRGPGET KLESDRRHIR KKIDDIKSQL SVIVQHRDRY RERRKKNKAF QIALVGYTNA GKSTLFNRLT EADSFEENRL FATLDPMTRK TILPSGFTAL LTDTVGFIQD LPTTLIAAFR STLEEVGEAD LLLHVVDMSN EDYFSHEQTV NKLLEDLDVH QIPQITVYNK RDIAHQDFVP NARNETAFIS AFSEEDRKNL LIKMEQSIIG LMEPYHVMVP SDEGKLLVQL KNDTILRELR FDEEKQHYEC KGFSLTDHQI TGQLKRFSK // ID A0A0D7EFI3_RHOPL Unreviewed; 460 AA. AC A0A0D7EFI3; DT 27-MAY-2015, integrated into UniProtKB/TrEMBL. DT 27-MAY-2015, sequence version 1. DT 07-JUN-2017, entry version 15. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=OO17_20905 {ECO:0000313|EMBL:KIZ39270.1}; OS Rhodopseudomonas palustris. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Bradyrhizobiaceae; Rhodopseudomonas. OX NCBI_TaxID=1076 {ECO:0000313|EMBL:KIZ39270.1, ECO:0000313|Proteomes:UP000032515}; RN [1] {ECO:0000313|EMBL:KIZ39270.1, ECO:0000313|Proteomes:UP000032515} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BAL398 {ECO:0000313|EMBL:KIZ39270.1, RC ECO:0000313|Proteomes:UP000032515}; RA Bentzon-Tilia M., Severin I., Hansen L.H., Riemann L.; RT "Genomics and ecophysiology of heterotrophic nitrogen fixing bacteria RT isolated from estuarine surface water."; RL Submitted (NOV-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KIZ39270.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JXXE01000447; KIZ39270.1; -; Genomic_DNA. DR RefSeq; WP_044415159.1; NZ_JXXE01000447.1. DR EnsemblBacteria; KIZ39270; KIZ39270; OO17_20905. DR PATRIC; fig|1076.23.peg.4857; -. DR Proteomes; UP000032515; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000032515}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000032515}. FT DOMAIN 225 399 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 460 AA; 51019 MW; 5FA947111CA220C3 CRC64; MEPRSLDGGA DRPRSVHDEQ TGRVIVVGPY LRARRGDPDS TDSIAVRGSD ARLDEAAGLA RAIDLVIAEL VLAPIGQIRP ATYLGKGKVE EILGIIQGHE ADLVVMDCAL SPIQQRNLEK AWNTKVLDRT GLILEIFGRR AKTKEGALQV ELAHLNYQRS RLVRSWTHLE RQRGGFGFMG GPGETQIEAD RRLIGDRITK IENEIKKVQG TRRLHRAGRQ RVPYRVVALV GYTNAGKSTL FNRLTRSEVQ AADMLFATLD PTLRGLTLPH GGKAMLSDTV GFISNLPTQL VAAFRATLEE VLEADLILHV RDISHEDAEA QQRDVDAVLR QLGIDPEAGG RILEVWNKID RFEPEQRENL SNIAARRPAE HPCFMVSAVT GEGIDELLAA IEQRLALSRI ALDLSIDAAD GAGISWLHRN AEVLRKDLHE GRFEMTVRVD ETKRDIVVNR FGATPHPDEH // ID A0A0D7K778_9BURK Unreviewed; 382 AA. AC A0A0D7K778; DT 27-MAY-2015, integrated into UniProtKB/TrEMBL. DT 27-MAY-2015, sequence version 1. DT 07-JUN-2017, entry version 16. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=RP29_14775 {ECO:0000313|EMBL:KJA09807.1}; OS Acidovorax temperans. OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Comamonadaceae; Acidovorax. OX NCBI_TaxID=80878 {ECO:0000313|EMBL:KJA09807.1, ECO:0000313|Proteomes:UP000032566}; RN [1] {ECO:0000313|EMBL:KJA09807.1, ECO:0000313|Proteomes:UP000032566} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=KY4 {ECO:0000313|EMBL:KJA09807.1, RC ECO:0000313|Proteomes:UP000032566}; RA Sheng K.-Y., Chin P.-S., Chan K.-G., Tan G.S.; RT "Isolation of bacteria from lake water."; RL Submitted (DEC-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KJA09807.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JXYQ01000051; KJA09807.1; -; Genomic_DNA. DR RefSeq; WP_044399994.1; NZ_JXYQ01000051.1. DR EnsemblBacteria; KJA09807; KJA09807; RP29_14775. DR PATRIC; fig|80878.5.peg.2853; -. DR Proteomes; UP000032566; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000032566}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000032566}. FT DOMAIN 197 370 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 382 AA; 42334 MW; 9CDBEAE8E7B81091 CRC64; MKPQSAPSVI LVGVDLGLPH FDAELEELGL LAQTAGLQPV ARITCKRKAP DAALFVGSGK ADEIRSLAQM HGAVEVLFDQ ALSPAQQRNL ERYLELPVND RTLLILEIFA QRARSHEGKL QVELAKLQYL STRLVRRWSH LERQRGGIGT RGGPGETQIE LDRRMIGDAI KRTKERLQKV KRQRNTQRRQ RERREAFTIS LVGYTNAGKS TLFNALVKAR AYAADQLFAT LDTTTRQLYL SEAQRSVSLS DTVGFIRDLP HGLVDAFQAT LQEAVDADFL LHVVDGSNPA YPEQIEQVQR VLAEIGADLI PQLLVFNKMD ALDGSLRPIA EIDSYELAGR EHRRVFVSAL TGSGLGTLRS VLGEIVAKES DEMSPVPTVE LT // ID A0A0D7QLP4_9MICO Unreviewed; 510 AA. AC A0A0D7QLP4; DT 27-MAY-2015, integrated into UniProtKB/TrEMBL. DT 27-MAY-2015, sequence version 1. DT 07-JUN-2017, entry version 15. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=TZ00_15505 {ECO:0000313|EMBL:KJC63458.1}; OS Agreia bicolorata. OC Bacteria; Actinobacteria; Micrococcales; Microbacteriaceae; Agreia. OX NCBI_TaxID=110935 {ECO:0000313|EMBL:KJC63458.1, ECO:0000313|Proteomes:UP000032503}; RN [1] {ECO:0000313|EMBL:KJC63458.1, ECO:0000313|Proteomes:UP000032503} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=VKM Ac-1804 {ECO:0000313|EMBL:KJC63458.1, RC ECO:0000313|Proteomes:UP000032503}; RX PubMed=11760949; DOI=10.1099/00207713-51-6-2073; RA Evtushenko L.I., Dorofeeva L.V., Dobrovolskaya T.G., RA Streshinskaya G.M., Subbotin S.A., Tiedje J.M.; RT "Agreia bicolorata gen. nov., sp. nov., to accommodate actinobacteria RT isolated from narrow reed grass infected by the nematode Heteroanguina RT graminophila."; RL Int. J. Syst. Evol. Microbiol. 51:2073-2079(2001). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KJC63458.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JYFC01000007; KJC63458.1; -; Genomic_DNA. DR RefSeq; WP_044443020.1; NZ_JYFC01000007.1. DR EnsemblBacteria; KJC63458; KJC63458; TZ00_15505. DR PATRIC; fig|110935.6.peg.3406; -. DR Proteomes; UP000032503; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 2. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000032503}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000032503}. FT DOMAIN 290 455 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 510 AA; 55680 MW; 7170708F2564FBFE CRC64; MTEKTEATTE NHDSDDVVAR VLARAETRAA GYSLFTNSAA QALQLDTTGR ESGFDGDQSE REDRQALRRV VGLSTELEDV TEVEYRQLRI ENVILIGVYT QGSLTDAENS MHELAALAET AGAVVLEGLL QRRPTPDPST YFGKGKAQEL RDLVQSLGAD TVIADNELAP SQRRALEDVV KVKVIDRTAV ILDIFSQHAK SREGKAQVEL AQLEYLLPRL RGWGDSMSRQ AGGQVGGAGA GMGSRGPGET KIELDRRRIH TRMARLRKQI VEMKPARDAK RANRKRNAVP SVAIAGYTNA GKSSLLNRVT RAGVLVENAL FATLDSTVRK STAADGRQYT FADTVGFVRN LPHQLVEAFR STLEEVADAD VIIHVVDGAH PDPASQLATV RDVIGEVGAR GIPEIVAFNK SDLISESDRI VLRGLEPRSV FVSARTGEGI AELLEMVEQA LPKPTITVDV LLPYERGDLV ALLHDHNTVL STDYEEAGTR VRALVNPEYE QTLEEFAVSR // ID A0A0D7W1F6_9FLAO Unreviewed; 407 AA. AC A0A0D7W1F6; DT 27-MAY-2015, integrated into UniProtKB/TrEMBL. DT 27-MAY-2015, sequence version 1. DT 07-JUN-2017, entry version 17. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=PK35_13075 {ECO:0000313|EMBL:KJD31687.1}; OS Tamlana nanhaiensis. OC Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales; OC Flavobacteriaceae; Tamlana. OX NCBI_TaxID=1382798 {ECO:0000313|EMBL:KJD31687.1, ECO:0000313|Proteomes:UP000032361}; RN [1] {ECO:0000313|Proteomes:UP000032361} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=FHC16 {ECO:0000313|Proteomes:UP000032361}; RX PubMed=25735434; DOI=10.1007/s10482-015-0410-x; RA Liu X., Lai Q., Du Y., Li G., Sun F., Shao Z.; RT "Tamlana nanhaiensis sp. nov., isolated from surface seawater RT collected from the South China Sea."; RL Antonie Van Leeuwenhoek 107:1189-1196(2015). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KJD31687.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JTDV01000013; KJD31687.1; -; Genomic_DNA. DR RefSeq; WP_044627009.1; NZ_JTDV01000013.1. DR EnsemblBacteria; KJD31687; KJD31687; PK35_13075. DR PATRIC; fig|1382798.3.peg.1176; -. DR Proteomes; UP000032361; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000032361}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000032361}. FT DOMAIN 200 385 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 407 AA; 46824 MW; 23BF610B07934599 CRC64; MIEKKDITLE KAVLIGIITQ NQHETKLKEY LDELEFLTFT AGGYAVKRFT QKMDVPNSKT FIGSGKMEEV KQFIDDNDIG TAIFDDELSA AQERNISKIL NVKVLDRTNL ILDIFAQRAQ TSYARTQVEL AQCEYLLPRL RGMWTHLERQ KGGIGMRGPG ETEIETDRRI VRDKIALLKA KIKTIDKQMA VQRGNRGKMV RVALVGYTNV GKSTLMNTIS KSEVFAENKL FATLDTTVRK VVIQNLPFLL SDTVGFIRKL PTQLVDSFKS TLDEVREADL LLHVVDISHP NFEEHIESVN KILGEIESSD KPTIMVFNKI DAYQAEPIDD DDLETERTEK HYSLEEWKST WMNKIGNNAL FISALNKKNL DDFKKRVYDE VRDIHVTRFP YNHFLYPDYN EFDEDDA // ID A0A0D8CTT3_9GAMM Unreviewed; 428 AA. AC A0A0D8CTT3; DT 27-MAY-2015, integrated into UniProtKB/TrEMBL. DT 27-MAY-2015, sequence version 1. DT 30-AUG-2017, entry version 17. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=SG35_17920 {ECO:0000313|EMBL:KJE40006.1}; OS Thalassomonas actiniarum. OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales; OC Colwelliaceae; Thalassomonas. OX NCBI_TaxID=485447 {ECO:0000313|EMBL:KJE40006.1, ECO:0000313|Proteomes:UP000032568}; RN [1] {ECO:0000313|EMBL:KJE40006.1, ECO:0000313|Proteomes:UP000032568} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=A5K-106 {ECO:0000313|EMBL:KJE40006.1, RC ECO:0000313|Proteomes:UP000032568}; RA Olonade I., van Zyl L.J., Tuffin M.I.; RT "Genome sequence of Japanese sea anemone isolate Thalassomonas RT actiniarum."; RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KJE40006.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JYNI01000045; KJE40006.1; -; Genomic_DNA. DR RefSeq; WP_044833834.1; NZ_JYNI01000045.1. DR EnsemblBacteria; KJE40006; KJE40006; SG35_17920. DR PATRIC; fig|485447.4.peg.3645; -. DR Proteomes; UP000032568; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000032568}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000032568}. FT DOMAIN 198 365 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 428 AA; 48622 MW; 9C48009846E7E202 CRC64; MFDRYQAGEQ AILVHVDFPD DSSREDLQEF KMLVSSAGVS ELTVVSGKRN TPHPKYFVGS GKAQEIADAV ALYDANVILF NHSLSPSQEK HIEALCQCRV VDRTTLILDI FAQRARTHEG KLQVELAQLR HISSRLIRGW THLERQKGGI GLRGPGETQL ETDRRLLRER MNNILKRLDK VEKQRQQGRR SRTRAEIPTI SLVGYTNAGK STLFNRLTDS DVYAADQLFA TLDPTLRKIE VEDVGRVILA DTVGFIRHLP HDLVAAFKAT LTETREAELL LHVVDISDER RSENIDQVTD VLTEIEAHEV PQLMICNKID NLHDVEPRID RDETGMPIRV WLSAQANIGI DLFFQALAER LGRQIVRHSL KIPPAAGKLR GMLYQLNCIA DEHFDEQGNC LVDVKLPARE WNRLIKQDKA GLERFIEN // ID A0A0D8FWB6_9ACTN Unreviewed; 429 AA. AC A0A0D8FWB6; DT 27-MAY-2015, integrated into UniProtKB/TrEMBL. DT 27-MAY-2015, sequence version 1. DT 07-JUN-2017, entry version 16. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:KJE77396.1}; GN ORFNames=FEAC_08300 {ECO:0000313|EMBL:KJE77396.1}; OS Ferrimicrobium acidiphilum DSM 19497. OC Bacteria; Actinobacteria; Acidimicrobiia; Acidimicrobiales; OC Acidimicrobiaceae; Ferrimicrobium. OX NCBI_TaxID=1121877 {ECO:0000313|EMBL:KJE77396.1, ECO:0000313|Proteomes:UP000032336}; RN [1] {ECO:0000313|EMBL:KJE77396.1, ECO:0000313|Proteomes:UP000032336} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=T23 {ECO:0000313|EMBL:KJE77396.1, RC ECO:0000313|Proteomes:UP000032336}; RA Poehlein A., Eisen S., Schloemann M., Johnson B.D., Daniel R., RA Muehling M.; RT "Draft genome of the acidophilic iron oxidizer Ferrimicrobium RT acidiphilum strain T23."; RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KJE77396.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JXUW01000005; KJE77396.1; -; Genomic_DNA. DR RefSeq; WP_035388775.1; NZ_JXUW01000005.1. DR EnsemblBacteria; KJE77396; KJE77396; FEAC_08300. DR PATRIC; fig|1121877.4.peg.884; -. DR Proteomes; UP000032336; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000032336}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000032336}. FT DOMAIN 202 361 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 161 195 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 429 AA; 47628 MW; A058901CE4E99137 CRC64; MTLIERSFQE RILLVGVATS GRERQMVNDQ LDELASLVDT AGALVVHREI QVRERPDPAT YIGKGKVDEL AVLSESFDVD TVVFDDELTP GQQRNLEKVL GRTAIDRTAV ILDVFAQNAR SQEGKAQVEL ALLRYRLPRL VGRRTNLSQQ VGRIGTRGPG ETKLEEDRRR IQERIGQLRR ELAALERQRR LQRKSRLHGR NSQVALVGYT NVGKSSLLNA LTGADVVVED RLFATLDPRT RRLKLPGGET ILLADTVGFI RKLPHQLIEA FRSTLDAVAE ADLLIHVVDA SSVHALDQMR EVRATLAEIG ASEVPELVVL NKIDLGYASD DLPDGIAISV TSGEGVNNLL AVVGDRLRAL NRVEVFRVPF DRGDILAEIH REAEVLSEEN QDDGIEVRVR ADDAARALLR RHIESVVSDR AVEDTDELS // ID A0A0D8HPG1_9ACTN Unreviewed; 421 AA. AC A0A0D8HPG1; DT 27-MAY-2015, integrated into UniProtKB/TrEMBL. DT 27-MAY-2015, sequence version 1. DT 07-JUN-2017, entry version 16. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:KJF19011.1}; GN ORFNames=AXFE_00480 {ECO:0000313|EMBL:KJF19011.1}; OS Acidithrix ferrooxidans. OC Bacteria; Actinobacteria; Acidimicrobiia; Acidimicrobiales; OC Acidimicrobiaceae; Acidithrix. OX NCBI_TaxID=1280514 {ECO:0000313|EMBL:KJF19011.1, ECO:0000313|Proteomes:UP000032360}; RN [1] {ECO:0000313|EMBL:KJF19011.1, ECO:0000313|Proteomes:UP000032360} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Py-F3 {ECO:0000313|EMBL:KJF19011.1, RC ECO:0000313|Proteomes:UP000032360}; RA Poehlein A., Eisen S., Schloemann M., Johnson B.D., Daniel R., RA Muehling M.; RT "Draft genome of the acidophilic iron oxidizer Acidithrix ferrooxidans RT strain Py-F3."; RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KJF19011.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JXYS01000001; KJF19011.1; -; Genomic_DNA. DR EnsemblBacteria; KJF19011; KJF19011; AXFE_00480. DR PATRIC; fig|1280514.3.peg.69; -. DR Proteomes; UP000032360; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000032360}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000032360}. FT DOMAIN 202 365 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 161 188 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 421 AA; 46824 MW; C9B3A272B30742D3 CRC64; MTLIERSFRE KIVLVGAVFP GDSPMAVEES LTELALLVDT AGADVVGRLT QRMAARDPGY FLGKGKVEEL KELSYATDCD TVIFDDELTP AQQRNLEKVL GRTAIDRTAL ILDIFAQNAK SMEGKAQVEL ALLSYRLPRL RGRGISLSQQ TGRIGTRGPG ETKLEEDRRR IQARISRLKH QLDDYAKNRR VQASSRVASR TQTASLVGYT NAGKSSLINA LCDSDVFVEN KLFATLDTRT RRMLLPGGEG FLLSDTVGFI KKLPHQLIES FRSTLEVVRE SDFLLHVVDA TSPDPHGQMR AVREVLIEID AENVRELLVF NKIDLVEDLS TLRLDFPQAV FVSAVRGDGL EELRLQIAAL IREQTKIYYL KIALSRGDIL ARLHSEGEIL SMTSTDEGYE ITARLDSGSL GLFEEFVVPS L // ID A0A0D8ICY0_9CLOT Unreviewed; 432 AA. AC A0A0D8ICY0; DT 27-MAY-2015, integrated into UniProtKB/TrEMBL. DT 27-MAY-2015, sequence version 1. DT 07-JUN-2017, entry version 16. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:AKL95055.1}; GN ORFNames=CACET_c16060 {ECO:0000313|EMBL:AKL95055.1}; OS Clostridium aceticum. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=84022 {ECO:0000313|EMBL:AKL95055.1, ECO:0000313|Proteomes:UP000035704}; RN [1] {ECO:0000313|EMBL:AKL95055.1, ECO:0000313|Proteomes:UP000035704} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 1496 {ECO:0000313|EMBL:AKL95055.1, RC ECO:0000313|Proteomes:UP000035704}; RA Poehlein A., Schiel-Bengelsdorf B., Gottschalk G., Duerre P., RA Daniel R.; RT "Genome sequence of Clostridium aceticum DSM 1496."; RL Submitted (OCT-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP009687; AKL95055.1; -; Genomic_DNA. DR RefSeq; WP_044823796.1; NZ_JYHU01000004.1. DR EnsemblBacteria; AKL95055; AKL95055; CACET_c16060. DR KEGG; cace:CACET_c16060; -. DR PATRIC; fig|84022.5.peg.3062; -. DR KO; K03665; -. DR Proteomes; UP000035704; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000035704}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000035704}. FT DOMAIN 208 378 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 432 AA; 48775 MW; 76A93A4FCFAA42DD CRC64; MEKENLETLE EAQKIRSLLV GLQVSNKPQD ESLDESMKEL EELAKAAGAE VIAVVVQNRP AIHVAYYIGK GKVQEIAELC QHHEIDVVIF NDELSGSQIR NLEEVVGVDV IDRTNLILDI FAQRAQTKEG KLQVELAQLK YRLPRLTGLG KQLSRQGGGI GTKGPGEMKL ETDRRHILRR IDDIRGQLKE VKKVRETQRA QRLKSDLPIV ALVGYTNAGK SSLMNTFLRQ SEGYDEKREV YAKNQLFATL DTSLRKISLP NKTEFLLTDT VGFVSKLPHD LVDAFKSTLE EVKYADLLLH IIDASNENYE LQKLTTSKVL KELGVDNKKI IDVFNKCDLL EDMPATSKSE NVISISALTG KNLDQLTEMI DSIIGKKILE INLLVPYSEG SIVSQLHKEA EVLSTDYQEE GIVLKVKIEE DYYERYKKFH LV // ID A0A0D8PPF8_9GAMM Unreviewed; 429 AA. AC A0A0D8PPF8; DT 27-MAY-2015, integrated into UniProtKB/TrEMBL. DT 27-MAY-2015, sequence version 1. DT 30-AUG-2017, entry version 14. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=UB37_16145 {ECO:0000313|EMBL:KJG19867.1}; OS Photobacterium iliopiscarium. OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; OC Vibrionaceae; Photobacterium. OX NCBI_TaxID=56192 {ECO:0000313|EMBL:KJG19867.1, ECO:0000313|Proteomes:UP000032448}; RN [1] {ECO:0000313|EMBL:KJG19867.1, ECO:0000313|Proteomes:UP000032448} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51761 {ECO:0000313|EMBL:KJG19867.1, RC ECO:0000313|Proteomes:UP000032448}; RA Timme R., Allard M.W., Strain E., Evans P.S., Brown E.; RT "Whole genome shotgun sequencing of cultured foodborne pathogen."; RL Submitted (FEB-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KJG19867.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JZSR01000041; KJG19867.1; -; Genomic_DNA. DR RefSeq; WP_045038387.1; NZ_JZSR01000041.1. DR EnsemblBacteria; KJG19867; KJG19867; UB37_16145. DR PATRIC; fig|56192.3.peg.3416; -. DR Proteomes; UP000032448; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000032448}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000032448}. FT DOMAIN 198 365 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 429 AA; 48430 MW; 8F3594497DC168C8 CRC64; MFDRYEAGEQ AILVHINFTQ DEEWEDLSEF EMLVSSAGVN ALHVVTGSRK TPLPKYYVGE GKAQEIADAV SAVDADIIIF NHALSPAQER NLEQLCQCRV IDRTGLILDI FAQRARTHEG KLQVELAQLR HLSTRLIRGW THLERQKGGI GLRGPGETQL ETDRRLLRER IKTILRRLDK VAKQRDQGRR ARNRAEIPTV SLVGYTNAGK STLFNCITDA GVYAADQLFA TLDPTLRKIE VADVGIAILA DTVGFIRHLP HDLVAAFKAT LKETQEADLL LHVVDASDDR FRENIEAVDT VLDEIDAGDV PVLLVMNKID NLDNAQPRIE RDEEGLPRRV WVSAMEGQGI DLLFQALTER LAGTMIKHSL RLPPEMIGRL RSKFYQMGCI LREEYESDGC LMIDIRLPMA EWSRLQKRES TSLDDYIVA // ID A0A0D8Q0S2_9GAMM Unreviewed; 447 AA. AC A0A0D8Q0S2; DT 27-MAY-2015, integrated into UniProtKB/TrEMBL. DT 27-MAY-2015, sequence version 1. DT 07-JUN-2017, entry version 15. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=UB37_06035 {ECO:0000313|EMBL:KJG23787.1}; OS Photobacterium iliopiscarium. OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; OC Vibrionaceae; Photobacterium. OX NCBI_TaxID=56192 {ECO:0000313|EMBL:KJG23787.1, ECO:0000313|Proteomes:UP000032448}; RN [1] {ECO:0000313|EMBL:KJG23787.1, ECO:0000313|Proteomes:UP000032448} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51761 {ECO:0000313|EMBL:KJG23787.1, RC ECO:0000313|Proteomes:UP000032448}; RA Timme R., Allard M.W., Strain E., Evans P.S., Brown E.; RT "Whole genome shotgun sequencing of cultured foodborne pathogen."; RL Submitted (FEB-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KJG23787.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JZSR01000009; KJG23787.1; -; Genomic_DNA. DR RefSeq; WP_045036493.1; NZ_JZSR01000009.1. DR EnsemblBacteria; KJG23787; KJG23787; UB37_06035. DR PATRIC; fig|56192.3.peg.1270; -. DR Proteomes; UP000032448; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000032448}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000032448}. FT DOMAIN 226 391 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 187 221 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 447 AA; 49917 MW; 138F2CECDC7C84B7 CRC64; MQLTAKASQN RALLISIQTP QFKGDEAKAS LAELARLVTT LGFKVVGTQS QKLSSNQRMN VLGSGKMAEI AHLTGNQGFV DDFDDDDDIV DEMLFSELPS EDLPFGSADV VVFDCDLSPS QLRNVENQLG VEVFDRTGII IEIFSRHART RTARLQVEIA RLNYLAPRLR ESTSGNKERQ MGKGAGETTL ELDRRKVRDQ LAELRRELVS VQDELKGRRT QRSELFCVAL VGYTNAGKSS MMRALTGSEV LVENKLFATL DTTVRALQPI TQPRILVSDT VGFIKKLPHD LVASFHSTLA EAHDASLLLY VVDASDPSFR SQLDVVHEVL HEVGVDDIPK QLVLNKSDQL SEEEQQALMV EFPDAVMTST RNPADIAKLH QYIVNIAQDE MTEEEIIVPY TANGIIGEIR SSMSVTKEEY EYEHIIFTVR SNPINLARLK KQMQNKD // ID A0A0D8TXE4_RAOPL Unreviewed; 344 AA. AC A0A0D8TXE4; DT 27-MAY-2015, integrated into UniProtKB/TrEMBL. DT 27-MAY-2015, sequence version 1. DT 30-AUG-2017, entry version 13. DE SubName: Full=GTPase HflX {ECO:0000313|EMBL:KJG72010.1}; DE Flags: Fragment; GN ORFNames=UA70_02170 {ECO:0000313|EMBL:KJG72010.1}; OS Raoultella planticola (Klebsiella planticola). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; OC Enterobacteriaceae; Raoultella. OX NCBI_TaxID=575 {ECO:0000313|EMBL:KJG72010.1, ECO:0000313|Proteomes:UP000032530}; RN [1] {ECO:0000313|EMBL:KJG72010.1, ECO:0000313|Proteomes:UP000032530} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=GCSL-DIFS-295 {ECO:0000313|EMBL:KJG72010.1, RC ECO:0000313|Proteomes:UP000032530}; RA Timme R., Allard M.W., Strain E., Evans P.S., Brown E.; RT "Whole genome shotgun sequencing of cultured foodborne pathogen."; RL Submitted (FEB-2015) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KJG72010.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JZSG01000068; KJG72010.1; -; Genomic_DNA. DR EnsemblBacteria; KJG72010; KJG72010; UA70_02170. DR PATRIC; fig|575.7.peg.807; -. DR Proteomes; UP000032530; Unassembled WGS sequence. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000032530}; KW Reference proteome {ECO:0000313|Proteomes:UP000032530}. FT DOMAIN 116 283 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT NON_TER 1 1 {ECO:0000313|EMBL:KJG72010.1}. SQ SEQUENCE 344 AA; 39139 MW; 5957344AE3A26CA1 CRC64; ALSPAQERNL ERLCECRVID RTGLILDIFA QRARTHEGKL QVELAQLRHM ATRLVRGWTH LERQKGGIGL RGPGETQLET DRRLLRNRIM QILSRLEKVS KQREQGRRSR AKADIPTVSL VGYTNAGKST LFNQITEAEV YAANQLFATL DPTLRRIDVT DVGETVLADT VGFIRHLPHD LVAAFKATLQ ETRQATLLLH VIDAADVRVQ ENIDAVNTVL AEIEADEIPM LLVMNKIDML DDFEPRIDRD EENKPIRVWL SAQTGVGVPL LFQALTERLS GEVAQHTLRL PPQEGRLRSR FYQLQAIEKE WLEDDGSVGL QVRMPIVDWR RLCKQEPALV DYVI // ID A0A0D8XGT3_DICVI Unreviewed; 1333 AA. AC A0A0D8XGT3; DT 27-MAY-2015, integrated into UniProtKB/TrEMBL. DT 27-MAY-2015, sequence version 1. DT 12-APR-2017, entry version 10. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:KJH41576.1}; GN ORFNames=DICVIV_12453 {ECO:0000313|EMBL:KJH41576.1}; OS Dictyocaulus viviparus (Bovine lungworm). OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida; OC Strongylida; Trichostrongyloidea; Dictyocaulidae; Dictyocaulinae; OC Dictyocaulus. OX NCBI_TaxID=29172 {ECO:0000313|EMBL:KJH41576.1, ECO:0000313|Proteomes:UP000053766}; RN [1] {ECO:0000313|EMBL:KJH41576.1, ECO:0000313|Proteomes:UP000053766} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=HannoverDv2000 {ECO:0000313|EMBL:KJH41576.1, RC ECO:0000313|Proteomes:UP000053766}; RA Mitreva M.; RT "Draft genome of the bovine lungworm Dictyocaulus viviparus."; RL Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; KN716795; KJH41576.1; -; Genomic_DNA. DR Proteomes; UP000053766; Unassembled WGS sequence. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 4: Predicted; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000053766}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000053766}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 124 151 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 1290 1333 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 620 654 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 1333 AA; 152138 MW; 06B468653FA683CF CRC64; MISSVKRSYG GGESFISVCQ LQYHETLRAL CNEAPSLRDS RNRFQSGSDV FIQVNDQLHD KNLERIVNDF SVVGRFDITP ELVDFGVRLR DLTNEFSTMT ARQPNETLWK EIFYKTTSNQ AITWYYITSM CQFSIGYLPF YSLLVNFYIL IFRNTYRIRF YCIVAVYGCD NITSTYYTSF LMGSLDIDRT VIACYSFYSP YSIWRMSEPH SAKEADYMQQ FHDTCISGNN EILGSQQLIS QPEINFEYQS QPHVSSYAMS VASPYISSQP IVQNSAVTTA QELSLQNTPT YKTSQLVPPV PLNCGDEPML IDYGINAKNC TAPDIGPELD ITTAHCTLAE VGDSESAERS QLSSTSFSYE SGAHKRKTTV PHRREELVAH TAQTLIVPNG VLVELDANGV ANNASVFPFC EDNEELSEFA TNMCDSYSLN DTHENELVQE ETQEMFSEPI HLRLRVDQAD NLQFSEPYSV KSRSLDEGEI ISDESLHVEK SQKPASSVPT ETKPEQPDTT LRREKPIALR NELRRSSLDS GKEKRSEKKV ADRLKEFNRN PPRIDVRTKK STTDRAEIHD AVIHEARNVP RVSPTCVGGG RLSRGSGRCF ASLFDEVCSG PSSRESSPHR EKVNKKEEER RRREKEMERE RQREKERLKR QRRDRDTRHD KERCSRTSPN RKTAETKALR REEEEKVEIR EKERRRDYAS DDRETTKSGD EIDDEVMNSC VDSPTSDAQH TARSNSDIDI ANKRELQAQE DKIHFRKLEN KKNVEPLCKS AVQENEDNVS FAENDERLRK TSKEEARAGK NVSEVKKSFI PSTTARRREE TKKVAVKPLE PGMMMNDTSV LDRINKEMES LTSRNRPTCT RSPEGSSCAK NTCSSKKSFV ISSGLSTTSL NQLVFSKAHS SRLGMFLEKV SDKHKKLMDR ENDQALASPE DNERNGVSTN VSQFPKQQQQ RFAPQKRPLP ASSLDSYLGS PTQVSDKILC LFKNSPDNRD MEATSSRSLG KKSKIDLSKM PDIIERLYGG KNCDTATVYI LCSMKRQLVF PLHSAQRSLR LFSNSSIDVR YDPILDAVEN DDFVAVGNKV DRWKCKRLSS SHDFLVVHPK VRWGSSSASR LKDPRRQLDE AIALVNTLPS FRVVESAIFG VDYNTKRKTV WGSGQIDALI TIKEQARVTA LMVNVDMLSP LQQHELFQIF RIPIYDRYNI VLSIFKQYAN TLEAHLQIKL AEIPYIRHRL HYVNRFRANP AVLHIERHSE YCKVDEFEVL RMQEQRLRKK LKQLIEKDVE KATEKAQNAM MVAVVGYTNA GKTSLVKCLT GAMTLLPENR LFATLDTTRH VAR // ID A0A0D8ZTC9_9CYAN Unreviewed; 561 AA. AC A0A0D8ZTC9; DT 27-MAY-2015, integrated into UniProtKB/TrEMBL. DT 27-MAY-2015, sequence version 1. DT 07-JUN-2017, entry version 18. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=UH38_11700 {ECO:0000313|EMBL:KJH71704.1}; OS Aliterella atlantica CENA595. OC Bacteria; Cyanobacteria; Chroococcidiopsidales; OC Chroococcidiopsidaceae; Aliterella. OX NCBI_TaxID=1618023 {ECO:0000313|EMBL:KJH71704.1, ECO:0000313|Proteomes:UP000032452}; RN [1] {ECO:0000313|EMBL:KJH71704.1, ECO:0000313|Proteomes:UP000032452} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CENA595 {ECO:0000313|EMBL:KJH71704.1, RC ECO:0000313|Proteomes:UP000032452}; RA Rigonato J., Alvarenga D.O., Branco L.H., Varani A.M., Brandini F.P., RA Fiore M.F.; RT "Draft genome of a novel marine cyanobacterium (Chroococcales) RT isolated from South Atlantic Ocean."; RL Submitted (FEB-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KJH71704.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JYON01000010; KJH71704.1; -; Genomic_DNA. DR RefSeq; WP_045054820.1; NZ_JYON01000010.1. DR EnsemblBacteria; KJH71704; KJH71704; UH38_11700. DR PATRIC; fig|1618023.3.peg.4167; -. DR Proteomes; UP000032452; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000032452}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000032452}. FT DOMAIN 389 559 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 348 382 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 561 AA; 61869 MW; 5968CF33968F6736 CRC64; METIYGNLQG LKSSQIKQLQ RLYHQRIPGD RITTPEFAQR LAAISTEINQ PVCTYLNRRG QVIRVGVGTP RQTQIPPLEL PRYGAERLSG IRCVATQLKA EPPNEAALTA MAIQRLDVLV VLNVTGSGFE RRGGGATGYV KDGYIAHLTP EGSPSWEVTP PISLDILSNQ DFIDLIEDIE AEFQQEFVGQ QVDTDRDRVI LVGMMTDNLA PHQFQDTIEE LERLVNTAGG EVLQVLRQKR SRPHPQTVVG EGKVQEIALT AQTLGANLIV FDRDLSPAQI RNLETQIGIR VVDRTEVILD IFAQRAQSRA GKLQVELAQL EYMLPRLTGR GQAMSRLGGG IGTRGPGETK LETERRAIAR RISRLQAEVN QLQAHRSRLR QQRQHQEVPS IAIVGYTNAG KSTLLNALTN SEVYTADQLF ATLDPTTRRM TIADAATGEP QPIVLTDTVG FIHELPASLM DAFRATLEEV TEADALLHVV DVSHPAWQSQ IRAVMSILSE MPVTPGPALL VLNKIDSADG DALALAREEF PQAVFIAARD RLGLETLRQR IAQLVRYAVA S // ID A0A0D9QDH2_PLAFR Unreviewed; 671 AA. AC A0A0D9QDH2; DT 27-MAY-2015, integrated into UniProtKB/TrEMBL. DT 27-MAY-2015, sequence version 1. DT 07-JUN-2017, entry version 13. DE SubName: Full=GTP-binding protein HflX {ECO:0000313|EMBL:KJP85029.1}; GN ORFNames=AK88_05334 {ECO:0000313|EMBL:KJP85029.1}; OS Plasmodium fragile. OC Eukaryota; Alveolata; Apicomplexa; Aconoidasida; Haemosporida; OC Plasmodiidae; Plasmodium; Plasmodium (Plasmodium). OX NCBI_TaxID=5857 {ECO:0000313|EMBL:KJP85029.1, ECO:0000313|Proteomes:UP000054561}; RN [1] {ECO:0000313|EMBL:KJP85029.1, ECO:0000313|Proteomes:UP000054561} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=nilgiri {ECO:0000313|Proteomes:UP000054561}; RG The Broad Institute Genomics Platform; RG The Broad Institute Genome Sequencing Center for Infectious Disease; RA Neafsey D., Duraisingh M., Young S.K., Zeng Q., Gargeya S., RA Abouelleil A., Alvarado L., Chapman S.B., Gainer-Dewar J., RA Goldberg J., Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., RA Larimer J., Pearson M., Poon T.W., Priest M., Roberts A., Saif S., RA Shea T., Sykes S., Wortman J., Nusbaum C., Birren B.; RT "The Genome Sequence of Plasmodium fragile nilgiri."; RL Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; KQ001759; KJP85029.1; -; Genomic_DNA. DR RefSeq; XP_012338359.1; XM_012482936.1. DR EnsemblProtists; KJP85029; KJP85029; AK88_05334. DR GeneID; 24270648; -. DR Proteomes; UP000054561; Unassembled WGS sequence. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 4: Predicted; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000054561}; KW Reference proteome {ECO:0000313|Proteomes:UP000054561}. FT DOMAIN 428 598 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 396 423 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 671 AA; 77044 MW; C3F493E464D23BF8 CRC64; MLRWSTTLRI FPRTQKRSFT NGRKKEIIVL HPILKKTKDG RKSFDEIIYD AQEALGLARS AGFKVANGIS MPLGGWTFFE HPNGSKEEGD GDDLGNSYRE EDTFRGSRES NEGADTRVGA ASEEVSPQGD DLEKKIAESI IIKTNRIDNK FYFGKGKLNE LSTYFLKHPT PYVFINTLLS PEQFRNLDML FNSLLRSHHD ELKLRRQKER GEDCLSVRAS EFNAEDDGGA EDARGEELAY VDMYNEWMER QAQQEDQEDG HLSLEEEGEE EEGVVFGDDV DDGDVPLYVE LFDRYSIILQ ILKSRAKNNL SKIQLELARA NFIFNTYAED NKSRMKYIKY IENNVLGKSN FDYEEKYNRQ NTFDVDRQLG KKKNYDSLGY TSSYIKSSET YKEYEKRIIQ NLYAKLKKEL AKCKNNNELQ SSARKHKALI AVVGYTNVGK TKLINYLTNS NLKARNLLFQ TLDNAFKSAK IWDGHSSIFV DSIGFIQNIP FSLYESFKVT LEAIKNADVL IHVIDVCHPY REQHKKCVID TLLKIGTPSD FLKCNMIEVW NKVDKLGDEE LLNLYKTKPK NVLPISARVG TNCDVLIKII QTMINRIKDV QVLTLQFPAI EAQERIAYLM KNFKVVPNSI SYSSDGNTTF IKLVENHRNL KKYYERFDKG EKGDPQGGGS T // ID A0A0D9XTR8_9ORYZ Unreviewed; 564 AA. AC A0A0D9XTR8; DT 27-MAY-2015, integrated into UniProtKB/TrEMBL. DT 27-MAY-2015, sequence version 1. DT 30-AUG-2017, entry version 14. DE SubName: Full=Uncharacterized protein {ECO:0000313|EnsemblPlants:LPERR11G15080.1}; OS Leersia perrieri. OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; BOP clade; OC Oryzoideae; Oryzeae; Oryzinae; Leersia. OX NCBI_TaxID=77586 {ECO:0000313|EnsemblPlants:LPERR11G15080.1, ECO:0000313|Proteomes:UP000032180}; RN [1] {ECO:0000313|EnsemblPlants:LPERR11G15080.1, ECO:0000313|Proteomes:UP000032180} RP NUCLEOTIDE SEQUENCE. RA Wing R.A.; RT "Oryza genome evolution."; RL Submitted (AUG-2012) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EnsemblPlants:LPERR11G15080.1, ECO:0000313|Proteomes:UP000032180} RP NUCLEOTIDE SEQUENCE. RA Yu Y., Lee S., de Baynast K., Wissotski M., Liu L., Talag J., RA Goicoechea J., Angelova A., Jetty R., Kudrna D., Golser W., Rivera L., RA Zhang J., Wing R.; RL Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases. RN [3] {ECO:0000313|EnsemblPlants:LPERR11G15080.1} RP IDENTIFICATION. RG EnsemblPlants; RL Submitted (APR-2015) to UniProtKB. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EnsemblPlants; LPERR11G15080.1; LPERR11G15080.1; LPERR11G15080. DR Gramene; LPERR11G15080.1; LPERR11G15080.1; LPERR11G15080. DR Proteomes; UP000032180; Chromosome 11. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000032180}; KW Reference proteome {ECO:0000313|Proteomes:UP000032180}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1 22 {ECO:0000256|SAM:SignalP}. FT CHAIN 23 564 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5002350684. FT DOMAIN 331 505 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 297 324 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 564 AA; 62182 MW; BE5A7AACFBF5C703 CRC64; MRAACFSFTA AAAAATATAT AAASLPLPST SPRCQLRPAS LRCSRPRRRV ARALDERLVE AAPPAETEVE DPGVEDGGGE GEVEVEEVEH AGRGEREEEE TARAPVRSRR RQQPEEESSP EHDRFKLING KEIFQEKAYL VGVECKRAGG SLFGIEESLK ELEQLADTAG LMAVGSTYQK LSTPNPRTYI GSGKVSEIKS AIHALDVETV IFDDELSPGQ LRNLEKAFGG GVRVCDRTAL ILDIFNQRAA THEAALQVTL AQMEYQLPRL TKMWTHLERQ SGGQVKGMGE KQIEVDKRIL RTQISALRKE LESVRKHRKL YRNRRQSVPI PVVSLLGYTN AGKSTLLNRL TGADVLAEDK LFATLDPTTR RVLMKNGTEF LLTDTVGFIQ KLPTMLSKLS ITTSQVAAFR ATLEEISESS VIVHLVDISH PLAQQQIDAV DKVLKQLDIE SIPKLVVWNK IDNTDDTLRV KEEAEKQGII CISAINGDGL EEFCNAIQAK LKDSMVPIEA IVPYDKGELL SDIHKVGMVE KTEYMENGTF VKAHVPLPLA RLLTPLRQQV VAAL // ID A0A0D9XTR9_9ORYZ Unreviewed; 555 AA. AC A0A0D9XTR9; DT 27-MAY-2015, integrated into UniProtKB/TrEMBL. DT 27-MAY-2015, sequence version 1. DT 12-APR-2017, entry version 10. DE SubName: Full=Uncharacterized protein {ECO:0000313|EnsemblPlants:LPERR11G15080.2}; OS Leersia perrieri. OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; BOP clade; OC Oryzoideae; Oryzeae; Oryzinae; Leersia. OX NCBI_TaxID=77586 {ECO:0000313|EnsemblPlants:LPERR11G15080.2, ECO:0000313|Proteomes:UP000032180}; RN [1] {ECO:0000313|EnsemblPlants:LPERR11G15080.2, ECO:0000313|Proteomes:UP000032180} RP NUCLEOTIDE SEQUENCE. RA Wing R.A.; RT "Oryza genome evolution."; RL Submitted (AUG-2012) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EnsemblPlants:LPERR11G15080.2, ECO:0000313|Proteomes:UP000032180} RP NUCLEOTIDE SEQUENCE. RA Yu Y., Lee S., de Baynast K., Wissotski M., Liu L., Talag J., RA Goicoechea J., Angelova A., Jetty R., Kudrna D., Golser W., Rivera L., RA Zhang J., Wing R.; RL Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases. RN [3] {ECO:0000313|EnsemblPlants:LPERR11G15080.2} RP IDENTIFICATION. RG EnsemblPlants; RL Submitted (APR-2015) to UniProtKB. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EnsemblPlants; LPERR11G15080.2; LPERR11G15080.2; LPERR11G15080. DR Gramene; LPERR11G15080.2; LPERR11G15080.2; LPERR11G15080. DR Proteomes; UP000032180; Chromosome 11. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000032180}; KW Reference proteome {ECO:0000313|Proteomes:UP000032180}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1 22 {ECO:0000256|SAM:SignalP}. FT CHAIN 23 555 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5002350808. FT DOMAIN 331 496 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 297 324 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 555 AA; 61236 MW; 32DE8DEACF31A15F CRC64; MRAACFSFTA AAAAATATAT AAASLPLPST SPRCQLRPAS LRCSRPRRRV ARALDERLVE AAPPAETEVE DPGVEDGGGE GEVEVEEVEH AGRGEREEEE TARAPVRSRR RQQPEEESSP EHDRFKLING KEIFQEKAYL VGVECKRAGG SLFGIEESLK ELEQLADTAG LMAVGSTYQK LSTPNPRTYI GSGKVSEIKS AIHALDVETV IFDDELSPGQ LRNLEKAFGG GVRVCDRTAL ILDIFNQRAA THEAALQVTL AQMEYQLPRL TKMWTHLERQ SGGQVKGMGE KQIEVDKRIL RTQISALRKE LESVRKHRKL YRNRRQSVPI PVVSLLGYTN AGKSTLLNRL TGADVLAEDK LFATLDPTTR RVLMKNGTEF LLTDTVGFIQ KLPTMLVAAF RATLEEISES SVIVHLVDIS HPLAQQQIDA VDKVLKQLDI ESIPKLVVWN KIDNTDDTLR VKEEAEKQGI ICISAINGDG LEEFCNAIQA KLKDSMVPIE AIVPYDKGEL LSDIHKVGMV EKTEYMENGT FVKAHVPLPL ARLLTPLRQQ VVAAL // ID A0A0E0BKU0_9ORYZ Unreviewed; 557 AA. AC A0A0E0BKU0; DT 27-MAY-2015, integrated into UniProtKB/TrEMBL. DT 27-MAY-2015, sequence version 1. DT 30-AUG-2017, entry version 14. DE SubName: Full=Uncharacterized protein {ECO:0000313|EnsemblPlants:OGLUM11G18090.1}; OS Oryza glumipatula. OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; BOP clade; OC Oryzoideae; Oryzeae; Oryzinae; Oryza. OX NCBI_TaxID=40148 {ECO:0000313|EnsemblPlants:OGLUM11G18090.1, ECO:0000313|Proteomes:UP000026961}; RN [1] {ECO:0000313|EnsemblPlants:OGLUM11G18090.1, ECO:0000313|Proteomes:UP000026961} RP NUCLEOTIDE SEQUENCE. RA Wing R.A., Panaud O., Oliveira A.C.; RT "Oryza genome evolution."; RL Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EnsemblPlants:OGLUM11G18090.1} RP IDENTIFICATION. RG EnsemblPlants; RL Submitted (APR-2015) to UniProtKB. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EnsemblPlants; OGLUM11G18090.1; OGLUM11G18090.1; OGLUM11G18090. DR EnsemblPlants; OGLUM11G18090.2; OGLUM11G18090.2; OGLUM11G18090. DR Gramene; OGLUM11G18090.1; OGLUM11G18090.1; OGLUM11G18090. DR Gramene; OGLUM11G18090.2; OGLUM11G18090.2; OGLUM11G18090. DR OrthoDB; EOG093609UJ; -. DR Proteomes; UP000026961; Chromosome 11. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000026961}; KW Reference proteome {ECO:0000313|Proteomes:UP000026961}. FT DOMAIN 333 498 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 299 326 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 557 AA; 61201 MW; 27753857944242E3 CRC64; MRAACFFTGA AATASLPLPS TSASASACCQ RRPASLRCSR PRRSFGVARA LDERLVEAAP PAPPAETEVE EPGVADGGGE GEGEGEVEEA APSGEEEEEE EQPARAPVRS RRRQEEEEET APGHDRFKLI NGKEIFQEKA YLVGVECKRS GGSMFSIEES LEELEQLADT AGLMVVGSTY QKLSSPNPRT YIGSGKVAEI KSAIHAHDVE TVIFDDELSP GQLRNLEKSF GGGVRVCDRT ALILDIFNQR AATHEAALQV TLAQMEYQLP RLTKMWSHLE RQSGGQVKGM GEKQIEVDKR ILRTQISALR KELESVRKHR KLYRNRRQSV PIPVVSLVGY TNAGKSTLLN RLTGADVLAE DKLFATLDPT TRRVLMKNGT EFLLTDTVGF IQKLPTMLVA AFRATLEEIS ESSVIVHLVD ISHPLAQQQI DAVDKVLKEL DIESIPKLVV WNKIDNTDDT LRVKEEAEKQ GIICISAING DGLEEFCNAV QAKLKDSLVP IEAFVPYDKG ELLSDIHKVG MVEKTEYMEN GTFVKAHVPL PLARLLTPLR QQVAAVS // ID A0A0E0MGT0_ORYPU Unreviewed; 555 AA. AC A0A0E0MGT0; DT 27-MAY-2015, integrated into UniProtKB/TrEMBL. DT 27-MAY-2015, sequence version 1. DT 07-JUN-2017, entry version 13. DE SubName: Full=Uncharacterized protein {ECO:0000313|EnsemblPlants:OPUNC11G15300.1}; OS Oryza punctata (Red rice). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; BOP clade; OC Oryzoideae; Oryzeae; Oryzinae; Oryza. OX NCBI_TaxID=4537 {ECO:0000313|EnsemblPlants:OPUNC11G15300.1, ECO:0000313|Proteomes:UP000026962}; RN [1] {ECO:0000313|EnsemblPlants:OPUNC11G15300.1, ECO:0000313|Proteomes:UP000026962} RP NUCLEOTIDE SEQUENCE. RA Wing R.; RT "Oryza genome evolution."; RL Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EnsemblPlants:OPUNC11G15300.1} RP IDENTIFICATION. RG EnsemblPlants; RL Submitted (APR-2015) to UniProtKB. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EnsemblPlants; OPUNC11G15250.1; OPUNC11G15250.1; OPUNC11G15250. DR EnsemblPlants; OPUNC11G15300.1; OPUNC11G15300.1; OPUNC11G15300. DR Gramene; OPUNC11G15250.1; OPUNC11G15250.1; OPUNC11G15250. DR Gramene; OPUNC11G15300.1; OPUNC11G15300.1; OPUNC11G15300. DR OMA; VILEIFH; -. DR OrthoDB; EOG093609UJ; -. DR Proteomes; UP000026962; Chromosome 11. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000026962}; KW Reference proteome {ECO:0000313|Proteomes:UP000026962}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1 19 {ECO:0000256|SAM:SignalP}. FT CHAIN 20 555 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5007399046. FT DOMAIN 331 496 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 297 324 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 555 AA; 61081 MW; 0E9292F33069F3D3 CRC64; MRAACFFTAA ASLPLPSTST SASACCQRRP TSLRCSRPRR SFGSGGRGVV RALDERLVEA ALQAETEVEV EDPGVADGGG EGEGEGEVEE AAPSGEEEEE QPARAPVRTK RRQEEEEAAP GHDRFKLING KEIFQEKAYL VGVECKRSGG SMFSIEESLE ELEQLADTAG LMVVGSTYQK LSTPNPRTYI GSGKVAEIKS AIHAHDVETV IFDDELSPGQ LRNLEKSFGG GVRVCDRTAL ILDIFNQRAA THEAALQVTL AQMEYQLPRL TKMWSHLERQ SGGQVKGMGE KQIEVDKRIL RTQISALRKE LESVRKHRKL YRNRRQSVPI PVVSLVGYTN AGKSTLLNRL TGADVLAEDK LFATLDPTTR RVLMKNGTEF LLTDTVGFIQ KLPTMLVAAF RATLEEISES SVIVHLVDIS HPLAQQQIEA VDKVLKELDI ESIPKLVVWN KIDNTDDTLR VKEEAEKQGI ICISAINGDG LEEFCNAIQA KLKDSLVPIE AFVPYDKGEL LSDIHKVGMV EKTEYMENGT FVKAHVPLPL ARLLTPLRQQ VAAVS // ID A0A0E0RAE2_ORYRU Unreviewed; 552 AA. AC A0A0E0RAE2; DT 27-MAY-2015, integrated into UniProtKB/TrEMBL. DT 27-MAY-2015, sequence version 1. DT 30-AUG-2017, entry version 15. DE SubName: Full=Uncharacterized protein {ECO:0000313|EnsemblPlants:ORUFI11G19880.1}; OS Oryza rufipogon (Brownbeard rice) (Asian wild rice). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; BOP clade; OC Oryzoideae; Oryzeae; Oryzinae; Oryza. OX NCBI_TaxID=4529 {ECO:0000313|EnsemblPlants:ORUFI11G19880.1, ECO:0000313|Proteomes:UP000008022}; RN [1] {ECO:0000313|EnsemblPlants:ORUFI11G19880.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=W1943 {ECO:0000313|EnsemblPlants:ORUFI11G19880.1}; RX PubMed=22408737; DOI=10.1002/ece3.66; RA Waters D.L.E., Nock C.J., Rice N., Ishikawa R., Henry R.J.; RT "Chloroplast genome sequence confirms distinctness of Australian and RT Asian wild rice."; RL Ecol Evol 2:211-217(2012). RN [2] {ECO:0000313|Proteomes:UP000008022} RP NUCLEOTIDE SEQUENCE. RA Zhao Q.; RL Submitted (JUN-2013) to the EMBL/GenBank/DDBJ databases. RN [3] {ECO:0000313|EnsemblPlants:ORUFI11G19880.1} RP IDENTIFICATION. RG EnsemblPlants; RL Submitted (JUN-2015) to UniProtKB. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR ProteinModelPortal; A0A0E0RAE2; -. DR EnsemblPlants; ORUFI11G19880.1; ORUFI11G19880.1; ORUFI11G19880. DR Gramene; ORUFI11G19880.1; ORUFI11G19880.1; ORUFI11G19880. DR OMA; VILEIFH; -. DR Proteomes; UP000008022; Unassembled WGS sequence. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000008022}; KW Reference proteome {ECO:0000313|Proteomes:UP000008022}. FT DOMAIN 328 493 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 294 321 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 552 AA; 60736 MW; 9BD066B73EB83E26 CRC64; MRAACFFTGA AATASLPLPS TSASASSCCQ RRPASLRCSR PRRSFGVARA LDERLVEAAP PAETEVEEPG VADGGGEGEG EVEDSAPSGE EEEEEEPARA PVRSRRRQEE EEEEAAPGHD RFKLINGKEI FQEKAYLVGV ECKRSGGSMF SIEESLEELE QLADTAGLMV VGSTYQKLST PNPRTYIGSG KVAEIKSAIH AHDVETVIFD DELSPGQLRN LEKSFGGGVR VCDRTALILD IFNQRAATHE AALQVTLAQM EYQLPRLTKM WSHLERQSGG QVKGMGEKQI EVDKRILRTQ ISALRKELES VRKHRKLYRN RRQSVPIPVV SLVGYTNAGK STLLNRLTGA DVLAEDKLFA TLDPTTRRVL MKNGTEFLLT DTVGFIQKLP TMLVAAFRAT LEEISESSVI VHLVDISHPL AQQQIDAVDK VLKELDIESI PKLVVWNKID NTDDTLRVKE EAEKQGIICI SAINGDGLEE FCNAIQAKLK DSLVPIEAFV PYDKGELLSD IHKVGMVEKT EYTENGTFVK AHVPLPLARL LTPLRQQVAA VS // ID A0A0E3L639_9EURY Unreviewed; 426 AA. AC A0A0E3L639; DT 24-JUN-2015, integrated into UniProtKB/TrEMBL. DT 24-JUN-2015, sequence version 1. DT 07-JUN-2017, entry version 15. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=MSMTP_0882 {ECO:0000313|EMBL:AKB24351.1}; OS Methanosarcina sp. MTP4. OC Archaea; Euryarchaeota; Methanomicrobia; Methanosarcinales; OC Methanosarcinaceae; Methanosarcina. OX NCBI_TaxID=1434100 {ECO:0000313|EMBL:AKB24351.1, ECO:0000313|Proteomes:UP000033049}; RN [1] {ECO:0000313|EMBL:AKB24351.1, ECO:0000313|Proteomes:UP000033049} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MTP4 {ECO:0000313|EMBL:AKB24351.1, RC ECO:0000313|Proteomes:UP000033049}; RA Henriksen J.R., Luke J., Reinhart S., Benedict M.N., Youngblut N.D., RA Metcalf M.E., Whitaker R.J., Metcalf W.W.; RT "Methanogenic archaea and the global carbon cycle."; RL Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP009505; AKB24351.1; -; Genomic_DNA. DR RefSeq; WP_048178048.1; NZ_CP009505.1. DR EnsemblBacteria; AKB24351; AKB24351; MSMTP_0882. DR GeneID; 24856129; -. DR KEGG; metm:MSMTP_0882; -. DR PATRIC; fig|1434100.4.peg.1137; -. DR KO; K03665; -. DR OrthoDB; POG093Z07D6; -. DR Proteomes; UP000033049; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000033049}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000033049}. FT DOMAIN 200 369 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 426 AA; 48322 MW; 01F17314A0096632 CRC64; MNPEKQPGNG TKVILVKRDN PRSEGERNAN LFEELRELAK AAGYRSVGEI SQTRFPDRKY QLGRGKVEEL AELVEITEAE KVIFYNRLST TQIYNISELC QCRVIDKFQL ILEIFAKRAT THRSKLQVEL AKLKYELPRA RAVVSILKKE EKPGFMGLGG YEDSYEQDLK KRITRIKSEL ETAEKDDASL RVFRRRQGLS LISLAGYTNA GKSTLFNTLV DEESEAMNML FTTLVPMTRA LDLGGRKALL TDTVGFIEEL PHWMVDAFKS TLDGIFLSDI ILLVADVSEK PEIVHQKLAT CHDTLWDRIN GVPVITVLNK VDRLDLEELE TRLEQIKYLA PNPILVSAKN GTGIPELKAE IFRHLPPWKT CSLTLPNSPK GMSALSWLYE EGIVHNVEYG EKISVDYEAR ASIIRKARNL EQDLAE // ID A0A0E3UVJ9_9BACT Unreviewed; 395 AA. AC A0A0E3UVJ9; DT 24-JUN-2015, integrated into UniProtKB/TrEMBL. DT 24-JUN-2015, sequence version 1. DT 07-JUN-2017, entry version 15. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=PKOR_04955 {ECO:0000313|EMBL:AKD02592.1}; OS Pontibacter korlensis. OC Bacteria; Bacteroidetes; Cytophagia; Cytophagales; Hymenobacteraceae; OC Pontibacter. OX NCBI_TaxID=400092 {ECO:0000313|EMBL:AKD02592.1, ECO:0000313|Proteomes:UP000033109}; RN [1] {ECO:0000313|EMBL:AKD02592.1, ECO:0000313|Proteomes:UP000033109} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=X14-1T {ECO:0000313|EMBL:AKD02592.1, RC ECO:0000313|Proteomes:UP000033109}; RX PubMed=26057562; DOI=10.1038/srep10929; RA Dai J., Dai W., Qiu C., Yang Z., Zhang Y., Zhou M., Zhang L., Fang C., RA Gao Q., Yang Q., Li X., Wang Z., Wang Z., Jia Z., Chen X.; RT "Unraveling adaptation of Pontibacter korlensis to radiation and RT infertility in desert through complete genome and comparative RT transcriptomic analysis."; RL Sci. Rep. 5:10929-10929(2015). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP009621; AKD02592.1; -; Genomic_DNA. DR RefSeq; WP_046309481.1; NZ_CP009621.1. DR EnsemblBacteria; AKD02592; AKD02592; PKOR_04955. DR KEGG; pko:PKOR_04955; -. DR PATRIC; fig|400092.3.peg.1105; -. DR KO; K03665; -. DR Proteomes; UP000033109; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000033109}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000033109}. FT DOMAIN 204 387 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 395 AA; 45530 MW; 3F1B357B104FB95F CRC64; MAKKKFYETS KPQETAVLVA VPNYRQTDEQ TEEYLDELAF LAETAGAQTL KRFVQKLDKP DVRTFVGSGK LEEIKAYVKE YEVDMVIFDD DLSPSQVRNI EREMQVKIVD RSLLILDIFA LRAKTAQAHA QVEMAQYQYL LPRLTNLWTH LSKQKGGIGM KGPGETEIET DRRIVRDKIS LLRERLRKFE KQNFEQRKAR AGIVRVALVG YTNVGKSTLM NLLSKSEVFA ENKLFATVDA TVRKVVLENI PFLLSDTVGF IRKLPTKLIE SFKSTLDEIR EADLLVHVVD ISHPSFEDHI AVVNETLKDI NSADKPVLLV FNKIDQYLEK RQQELQEEDM NIRPSIEDLK ETYMAKEHAP AMFISATDKL NIDALREELQ RRVAEIHFQR YPNNV // ID A0A0E3W2X3_9FIRM Unreviewed; 363 AA. AC A0A0E3W2X3; DT 24-JUN-2015, integrated into UniProtKB/TrEMBL. DT 24-JUN-2015, sequence version 1. DT 07-JUN-2017, entry version 14. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=927 {ECO:0000313|EMBL:CFX28590.1}; OS Syntrophomonas zehnderi OL-4. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Syntrophomonadaceae; OC Syntrophomonas. OX NCBI_TaxID=690567 {ECO:0000313|EMBL:CFX28590.1, ECO:0000313|Proteomes:UP000045545}; RN [1] {ECO:0000313|EMBL:CFX28590.1, ECO:0000313|Proteomes:UP000045545} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=OL-4 {ECO:0000313|EMBL:CFX28590.1, RC ECO:0000313|Proteomes:UP000045545}; RA Murphy D.; RL Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CGIH01000013; CFX28590.1; -; Genomic_DNA. DR RefSeq; WP_052729605.1; NZ_CGIH01000013.1. DR Proteomes; UP000045545; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000045545}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000045545}. FT DOMAIN 199 363 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 165 192 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 363 AA; 40643 MW; 8A741DF395834593 CRC64; MNDNKPEKAI LVGVELKSDA GFNFQASLQE LQALTEAAGG EVAAVLVQSR ERVHGATYIG KGKLEELKHL AAELEPDLII FDNELSPVQL RNLEEALNIK IIDRTMLILD IFSQRAKSNE GILQVELARL QYQLPRLTGQ GVTLSRLGAG IGTRGSGEQK LELDRRYIRQ RIQDIKKRMQ KVENTRKLHR VQRQRSGMKQ VSLVGYTNAG KSSLFNTLCQ TGHRSKTAQV KADQQLFRTL DTTIRKIRWA DQKEILLTDT VGFIQNLPHH LVAAFKSTLE EVIEADLLLH VVDISDPDAA DKIEVVEKVL WELGADSDRI VTVFNKSDLL QDPPDNSGPA IYVSARTGQG IDDLLKRLEI ILF // ID A0A0E3Y8U6_9ENTR Unreviewed; 434 AA. AC A0A0E3Y8U6; DT 24-JUN-2015, integrated into UniProtKB/TrEMBL. DT 24-JUN-2015, sequence version 1. DT 07-JUN-2017, entry version 15. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:AKC60259.1}; GN ORFNames=BOBLI757_081 {ECO:0000313|EMBL:AKC60259.1}; OS Blochmannia endosymbiont of Camponotus (Colobopsis) obliquus. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; OC Enterobacteriaceae; ant endosymbionts; Candidatus Blochmannia. OX NCBI_TaxID=1505597 {ECO:0000313|EMBL:AKC60259.1, ECO:0000313|Proteomes:UP000033104}; RN [1] {ECO:0000313|EMBL:AKC60259.1, ECO:0000313|Proteomes:UP000033104} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=757 {ECO:0000313|EMBL:AKC60259.1}; RX PubMed=25861561; RA Williams L.E., Wernegreen J.J.; RT "Genome evolution in an ancient bacteria-ant symbiosis: parallel gene RT loss among Blochmannia spanning the origin of the ant tribe RT Camponotini."; RL PeerJ 3:E881-E881(2015). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP010049; AKC60259.1; -; Genomic_DNA. DR RefSeq; WP_046304547.1; NZ_CP010049.1. DR EnsemblBacteria; AKC60259; AKC60259; BOBLI757_081. DR KEGG; ben:BOBLI757_081; -. DR PATRIC; fig|1505597.4.peg.77; -. DR KO; K03665; -. DR Proteomes; UP000033104; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000033104}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000033104}. FT DOMAIN 198 365 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 434 AA; 50281 MW; DA6E8E7883215109 CRC64; MFRHYSRFGQ AILVRVFFKK KNIEVLQEFK NLVTASGIKI FRVITVCRSS PHPKFYVGTG KIKEIAFLAK NNLIPVIIFD HILSPNQEKH LEDLCQCKII DRTELILHIF SQRAKTSAGK LQVKLAQLRY LSTRLVHGWT HLEKQKGDIK RLRGPGETQL EVDRRLLRTQ INHVLFRLKK VAKQREQERQ SRARSNIPSV LLVGYTNVGK STVFNLLTNS SVYIANKFFA TLDPIHRRIA VHGIGEVILI DTVGFIKDFP SDLVSAFQVT LQEALYATLL LHIVDASDDQ YEEKIAAVIH ILDKIKIHHI PILTVMNKID LLDDFKPRID RDVDHYPTRV WISAKNTIGQ ALFIQTLSEC LYGIMMQYEL LLPPEAYYLN VKFYQMKVVQ YCRIKPDGNF YLIIKLSIAN WLKLCQQYSF LNKYLITNSS QRCL // ID A0A0E3YU93_9BACT Unreviewed; 433 AA. AC A0A0E3YU93; DT 24-JUN-2015, integrated into UniProtKB/TrEMBL. DT 24-JUN-2015, sequence version 1. DT 07-JUN-2017, entry version 15. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=IMCC26134_09210 {ECO:0000313|EMBL:AKC82907.1}; OS Verrucomicrobia bacterium IMCC26134. OC Bacteria; Verrucomicrobia; unclassified Verrucomicrobia. OX NCBI_TaxID=1637999 {ECO:0000313|EMBL:AKC82907.1, ECO:0000313|Proteomes:UP000033046}; RN [1] {ECO:0000313|EMBL:AKC82907.1, ECO:0000313|Proteomes:UP000033046} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=IMCC26134 {ECO:0000313|EMBL:AKC82907.1, RC ECO:0000313|Proteomes:UP000033046}; RA Choi A., Kang I., Cho J.-C.; RT "Complete genome sequence of Verrucomicrobia strain IMCC26134."; RL Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP011265; AKC82907.1; -; Genomic_DNA. DR RefSeq; WP_046298286.1; NZ_CP011265.1. DR EnsemblBacteria; AKC82907; AKC82907; IMCC26134_09210. DR KEGG; vba:IMCC26134_09210; -. DR PATRIC; fig|1637999.3.peg.1996; -. DR KO; K03665; -. DR Proteomes; UP000033046; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000033046}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000033046}. FT DOMAIN 213 378 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 172 199 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 433 AA; 47644 MW; 96D9BB50F8B73770 CRC64; MADFLDQVPA TDSKRCQRAF LVGIQTTEMA PGEAAELLAE LEELVQNLRI DVVGMELVNL RQPTPATLTG SGKTEELIAR AKELDADLIV IDESLSPAQQ RNWEKQSELA VIDREEVILD IFADRASTRE AVLQVALARM QYSLPRLTRA WTHLSRQRGG GGGGGAMGGE GETQLEQDRR LVNDRIVRLK RELLEVRKQR GVQRHKRQRV PVPTAAIVGY TNAGKSSLLN ALTGASVLAE DKLFATLDPT TRQLLLRGNQ KVLVTDTVGF IRRLPHGLVE AFKATLEEAL VADFLIHVLD VTAPNLAAHH QTTLDVLKEL GADEKRMVTV FNKVDAADEG HLLRAKLLVP EGIFLSAKSG QGMDGLVDQC LELIADAFGQ MDLLIPHSRY DLIAKLHAVG HIQHEEERDN GVFLKVRLSP GQAGVYQPFV VES // ID A0A0E4CXD3_9BACL Unreviewed; 429 AA. AC A0A0E4CXD3; DT 24-JUN-2015, integrated into UniProtKB/TrEMBL. DT 24-JUN-2015, sequence version 1. DT 07-JUN-2017, entry version 18. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:CQR56255.1}; GN ORFNames=PRIO_3852 {ECO:0000313|EMBL:CQR56255.1}; OS Paenibacillus riograndensis SBR5. OC Bacteria; Firmicutes; Bacilli; Bacillales; Paenibacillaceae; OC Paenibacillus. OX NCBI_TaxID=1073571 {ECO:0000313|EMBL:CQR56255.1, ECO:0000313|Proteomes:UP000033163}; RN [1] {ECO:0000313|EMBL:CQR56255.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=SBR5 {ECO:0000313|EMBL:CQR56255.1}; RA Wibberg Daniel; RL Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LN831776; CQR56255.1; -; Genomic_DNA. DR RefSeq; WP_020431133.1; NZ_LN831776.1. DR EnsemblBacteria; CQR56255; CQR56255; PRIO_3852. DR KEGG; pri:PRIO_3852; -. DR PATRIC; fig|1073571.4.peg.4112; -. DR KO; K03665; -. DR Proteomes; UP000033163; Chromosome I. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000033163}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000033163}. FT DOMAIN 208 372 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 167 201 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 429 AA; 47787 MW; 6736D1EC73940A1B CRC64; MAITTHDTET EIQDRAILVS LVTDKIKRTG VDPELSLQEL VQLAETAGVI VLDVLRQNKE TPDSKWFIGK GKVEELRMAA DGLGANTAIF DQELSGAQVR NLEEALDLKI IDRTQLILDI FAGRAKTREG IIQVELAQLS YLLPRLSGHG KNLSRLGGGI GTRGPGESKL ETDRRHIRDR ISELKRQLDE VVKTRELHRE RRRKSGAVQV ALVGYTNAGK STLLKQLTDA DVYIENQLFA TLDPTSRVLQ LPAGKEVVLT DTVGFIQNLP HDLVASFRAT LEEVNEANLV LHVVDASSPM REEQMEVVQS ILQDLGAAGK PQIVLFNKSD ICRPEQLQML PSGPGFLKIS AFNPDDLTRI TEMIADELAG DTLTFRIPGD RGDLSSLLYR VGEVLEQNVE DNDVLYQVRL NKEDYGKWSY KLAEYVEQE // ID A0A0E4H714_9BACL Unreviewed; 423 AA. AC A0A0E4H714; DT 24-JUN-2015, integrated into UniProtKB/TrEMBL. DT 24-JUN-2015, sequence version 1. DT 07-JUN-2017, entry version 18. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=PRIO_0372 {ECO:0000313|EMBL:CQR51625.1}; OS Paenibacillus riograndensis SBR5. OC Bacteria; Firmicutes; Bacilli; Bacillales; Paenibacillaceae; OC Paenibacillus. OX NCBI_TaxID=1073571 {ECO:0000313|EMBL:CQR51625.1, ECO:0000313|Proteomes:UP000033163}; RN [1] {ECO:0000313|EMBL:CQR51625.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=SBR5 {ECO:0000313|EMBL:CQR51625.1}; RA Wibberg Daniel; RL Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LN831776; CQR51625.1; -; Genomic_DNA. DR RefSeq; WP_020427985.1; NZ_LN831776.1. DR EnsemblBacteria; CQR51625; CQR51625; PRIO_0372. DR KEGG; pri:PRIO_0372; -. DR PATRIC; fig|1073571.4.peg.364; -. DR KO; K03665; -. DR Proteomes; UP000033163; Chromosome I. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000033163}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000033163}. FT DOMAIN 198 366 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 157 184 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 423 AA; 47310 MW; EB0B6D2F865C89F1 CRC64; METVHQKAVI VGVQLQNDKD FAYSMEELRN LAAACELEVV GELSQKSSRI NPAHYIGTGK IGELEALLEA LEAPIVIFND ELSPSQIRNL ESALDRQVID RTVLILNIFA ERAKTKEAQL QVEVAQLQYM LPRLAGMRES LGRQGGGAGL KNRGAGETKL ELDRRRIEER ITALQLELQT QVARRQVQRK QRRKNEVPVV CLVGYTNTGK SSLMNTIMET YHPGSQKGVL AKDMLFATLE TSVRSIELPD RKTFLLTDTV GFVSQLPHHL VKAFRSTLEE VTEADLLIHV ADISDPQVGQ HIAVTEETLK ALGADGIPAI KAYNKADLTE LPYPVVKENT VTLSAKQKSG IAELIDLVRQ HVFNDYIRCE ILVPFDRGSV VSYFNDHADV QEVSYEEQGT RLKLECRAAD YERFKSDFVV ISQ // ID A0A0E9LXS5_9BACT Unreviewed; 410 AA. AC A0A0E9LXS5; DT 24-JUN-2015, integrated into UniProtKB/TrEMBL. DT 24-JUN-2015, sequence version 1. DT 07-JUN-2017, entry version 15. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=JCM15548_12299 {ECO:0000313|EMBL:GAO30054.1}; OS Geofilum rubicundum JCM 15548. OC Bacteria; Bacteroidetes; Bacteroidia; Marinilabiliales; OC Marinilabiliaceae; Geofilum. OX NCBI_TaxID=1236989 {ECO:0000313|EMBL:GAO30054.1, ECO:0000313|Proteomes:UP000032900}; RN [1] {ECO:0000313|EMBL:GAO30054.1, ECO:0000313|Proteomes:UP000032900} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=JCM 15548 {ECO:0000313|EMBL:GAO30054.1}; RX PubMed=25736980; RA Inoue J., Oshima K., Suda W., Sakamoto M., Iino T., Noda S., RA Hongoh Y., Hattori M., Ohkuma M.; RT "Distribution and evolution of nitrogen fixation genes in the phylum RT bacteroidetes."; RL Microbes Environ. 30:44-50(2015). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:GAO30054.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BAZW01000017; GAO30054.1; -; Genomic_DNA. DR RefSeq; WP_062124788.1; NZ_BAZW01000017.1. DR EnsemblBacteria; GAO30054; GAO30054; JCM15548_12299. DR Proteomes; UP000032900; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000032900}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000032900}. FT DOMAIN 203 386 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 410 AA; 46856 MW; 35BF0AC81216739B CRC64; MSDLISTDTD LEKVILVAVR TPGLSESLVN EYLDELAFLA ETAGAVPVRR FVQSLTMADN RTYVGSGKLQ EILEYLKVHE DVSGVIFDDE LSPSQLKNIE ATLKRRVLDR TNLILDIFAR RARTAHAKTQ VELAQYQYLL PRLTRMWTHL ERQRGGIGMR GPGEKEIETD RRIIRDIISK LKNDLVKIDR QMATQRKNRG KLVRVALVGY TNVGKSTLMN ALSKSEVFAE NKLFATLDTT VRKVVIGNLP FLLADTVGFI RKLPHHLVES FKSTLDEVRE ADLLLHIVDI SHPGFEQQID VVNETLHEID DREKPSILVF NKVDAFSHIE KEADDLTPST RANVSLEELK QTWMARGTPS IFISALEKTN FEEFRDTLYH EVMKIHVTRF PYNDFLYPDA EDMDDAEDDF // ID A0A0E9M870_9PROT Unreviewed; 393 AA. AC A0A0E9M870; DT 24-JUN-2015, integrated into UniProtKB/TrEMBL. DT 24-JUN-2015, sequence version 1. DT 30-AUG-2017, entry version 15. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:GAO33601.1}; GN ORFNames=OYT1_01656 {ECO:0000313|EMBL:GAO33601.1}; OS Ferriphaselus amnicola. OC Bacteria; Proteobacteria; Betaproteobacteria; Nitrosomonadales; OC Gallionellaceae; Ferriphaselus. OX NCBI_TaxID=1188319 {ECO:0000313|EMBL:GAO33601.1, ECO:0000313|Proteomes:UP000033070}; RN [1] {ECO:0000313|EMBL:GAO33601.1, ECO:0000313|Proteomes:UP000033070} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=OYT1 {ECO:0000313|EMBL:GAO33601.1, RC ECO:0000313|Proteomes:UP000033070}; RA Kato S., Ohkuma M.; RT "Draft genome sequence of Ferriphaselus amnicola strain OYT1."; RL Submitted (FEB-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:GAO33601.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BBTH01000004; GAO33601.1; -; Genomic_DNA. DR RefSeq; WP_062626834.1; NZ_BBTH01000004.1. DR EnsemblBacteria; GAO33601; GAO33601; OYT1_01656. DR Proteomes; UP000033070; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000033070}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000033070}. FT DOMAIN 198 374 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 157 191 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 393 AA; 43382 MW; 21C2D7D3E61D6B6E CRC64; MSASQPATEV AVLVSLNFGE PDYAESREEL RLLAESAGVK VCAMVEGRRY RPDPSLFAGS GKVDEVAAIA EQFEASVVIF NHDLSPAQMR NLTARMNIRV IDRTMLILDI FALRANSHEG KVQVELAQLK YLSTRLVGLN QDMGQQKFAV GARGPGETQL ELDRRKLARR VELLNDRLKQ LKKQRALQRR ARQRNAVLSV SIVGYTNAGK STMFNRLTQA GVYAANQLFA TLDTTSRRIW LPGQASVEDG RVVGSQVVVS DTVGFIRHLP HGLVAAFRGT LEETAQADLL LHVVDINSPD RDIQIAEVNK VLAEIDADQI PQVLVFNKID LVGLPASVER DECGRICRVF VSSVTGDGMD GLRQALVEAN EQRQVAQPRQ VEEATQQDGM TWD // ID A0A0E9MM80_9SPHN Unreviewed; 428 AA. AC A0A0E9MM80; DT 24-JUN-2015, integrated into UniProtKB/TrEMBL. DT 24-JUN-2015, sequence version 1. DT 07-JUN-2017, entry version 14. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:GAO38521.1}; GN ORFNames=SCH01S_16_00380 {ECO:0000313|EMBL:GAO38521.1}; OS Sphingomonas changbaiensis NBRC 104936. OC Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales; OC Sphingomonadaceae; Sphingomonas. OX NCBI_TaxID=1219043 {ECO:0000313|EMBL:GAO38521.1, ECO:0000313|Proteomes:UP000033202}; RN [1] {ECO:0000313|EMBL:GAO38521.1, ECO:0000313|Proteomes:UP000033202} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NBRC 104936 {ECO:0000313|EMBL:GAO38521.1, RC ECO:0000313|Proteomes:UP000033202}; RA Katano-Makiyama Y., Hosoyama A., Hashimoto M., Noguchi M., RA Tsuchikane K., Ohji S., Yamazoe A., Ichikawa N., Kimura A., Fujita N.; RT "Whole genome shotgun sequence of Sphingomonas changbaiensis NBRC RT 104936."; RL Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:GAO38521.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BBWU01000016; GAO38521.1; -; Genomic_DNA. DR RefSeq; WP_046347372.1; NZ_BBWU01000016.1. DR EnsemblBacteria; GAO38521; GAO38521; SCH01S_16_00380. DR Proteomes; UP000033202; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000033202}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000033202}. FT DOMAIN 208 375 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 428 AA; 47310 MW; 7380AA5FCF492734 CRC64; MTGFERDYDE FARGARAVIA YPDLRNADGR DVEARLDEAA GLAEAIGIEV AERQAFRIRA PKPATLFGSG QVEEIATAVR AQDAQLVIVD GAITPVQQRN LEEGTKAKVI DRTGLILEIF GERAATAEGR LQVELAHLDY QAGRLVRSWT HLERQRGGFG FLGGPGETQI EADRRLIRDR MAKLRRELET VSRTRTLHRD RRRRAPWPVI ALVGYTNAGK STLFNRLTGA DVMAENLLFA TLDPTMRQIA LPGLDKAILS DTVGFVSDLP TQLVAAFRAT LEEVISADLI VHVRDIAHPD SDAQRADVER VLTEIGAEAP RIEAWNKLDS LDPERRTAIA AEAAKRDDVV LISALTGEGV DALKRLVSDR LTGSNRVRHI EVPMTDGAAA AWLHEHGEVV GEETIDGDRI AYDVRLSDRD WDRFQARV // ID A0A0E9N068_9BACT Unreviewed; 418 AA. AC A0A0E9N068; DT 24-JUN-2015, integrated into UniProtKB/TrEMBL. DT 24-JUN-2015, sequence version 1. DT 12-APR-2017, entry version 13. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:GAO42765.1}; GN ORFNames=FPE01S_01_17830 {ECO:0000313|EMBL:GAO42765.1}; OS Flavihumibacter petaseus NBRC 106054. OC Bacteria; Bacteroidetes; Chitinophagia; Chitinophagales; OC Chitinophagaceae; Flavihumibacter. OX NCBI_TaxID=1220578 {ECO:0000313|EMBL:GAO42765.1, ECO:0000313|Proteomes:UP000033121}; RN [1] {ECO:0000313|EMBL:GAO42765.1, ECO:0000313|Proteomes:UP000033121} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NBRC 106054 {ECO:0000313|EMBL:GAO42765.1, RC ECO:0000313|Proteomes:UP000033121}; RA Miyazawa S., Hosoyama A., Hashimoto M., Noguchi M., Tsuchikane K., RA Ohji S., Yamazoe A., Ichikawa N., Kimura A., Fujita N.; RT "Whole genome shotgun sequence of Flavihumibacter petaseus NBRC RT 106054."; RL Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:GAO42765.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BBWV01000001; GAO42765.1; -; Genomic_DNA. DR EnsemblBacteria; GAO42765; GAO42765; FPE01S_01_17830. DR Proteomes; UP000033121; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000033121}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000033121}. FT DOMAIN 212 394 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 418 AA; 48057 MW; C2FA59CE8AD46F8A CRC64; MLIFAALIRS GLIEKKQILE AEKCVLVGVV QKDQTELQVK EYLDELAFLA ETAGAITARK FTQKLAHPDS KTFVGKGKLE EIRDYLTGRD INLVIFDDEL TGSQIINIEK ALGVKTIDRS DLILDIFARR AKTAQAKTQV ELAQYQYLLP RLKGMWKHLE RQGGGIGTRG PGETEIETDR RIVKEKIALL RRRLAEIDKQ AYTQRKDRGE FIRVALVGYT NVGKSTIMNI LAKSEVFAEN KLFATLDTTT RKVVFDATPF LLSDTVGFIR KLPHHLVESF KSTLDEVREA DILLHVVDLS HPAYEDQFNV VNKTLQELKV TEKPVITIFN KLDQYEKNTF DEWLNEEVKT QILEELRERW ENDTLGNCVF ISALEKRNLE GLRATILNRV RRLYRERYPY KTEFFGISLD DEDAAEFI // ID A0A0F0CKE2_9CLOT Unreviewed; 422 AA. AC A0A0F0CKE2; DT 24-JUN-2015, integrated into UniProtKB/TrEMBL. DT 24-JUN-2015, sequence version 1. DT 07-JUN-2017, entry version 14. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:KJJ75612.1}; GN ORFNames=CLFS41_07090 {ECO:0000313|EMBL:KJJ75612.1}; OS Clostridium sp. FS41. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=1609975 {ECO:0000313|EMBL:KJJ75612.1, ECO:0000313|Proteomes:UP000033604}; RN [1] {ECO:0000313|EMBL:KJJ75612.1, ECO:0000313|Proteomes:UP000033604} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=FS41 {ECO:0000313|EMBL:KJJ75612.1, RC ECO:0000313|Proteomes:UP000033604}; RA Poehlein A., Daniel R.; RT "Genome sequencing of Clostridium sp. FS41."; RL Submitted (FEB-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KJJ75612.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JYHN01000025; KJJ75612.1; -; Genomic_DNA. DR EnsemblBacteria; KJJ75612; KJJ75612; CLFS41_07090. DR PATRIC; fig|1609975.3.peg.765; -. DR Proteomes; UP000033604; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000033604}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000033604}. FT DOMAIN 199 371 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 422 AA; 47685 MW; 833A71DE5DF9ADEB CRC64; MIDLKELQEK VILIAVSTGE EDHTEASLDE LEELAATAGA VTIARVTQNR ERVHPGTYLG KGKIDEVRDL IWELGATGVV CDDELSPAQL RNLEDALDTK VMDRTMVILD IFAARANTRE GKIQVELAQL KYRAVRLVGM RNSLSRLGGG IGTRGPGEKK LETDRRLIHQ RIGQLKEELE DVKRHREVTR QQREKNFALT AAIVGYTNAG KSTLLNRLTG AGILAEDKLF ATLDPTTRSF YLEDGQQILL TDTVGFIRKL PHHLIEAFKS TLEEARYSDI ILHVVDCANP QMDMQMHVVK ETLRELEIVD KTVVTVFNKT DRFREMESEG QPLQQVPRDF SSDYQVRISA KTGEGLDELE KIFLTIIRSR RVLLEKVYAY SQAGRIQTIR KYGQLLEEEY RDDGIAVKAY VPAELFAGLY SD // ID A0A0F0CPF9_9BACT Unreviewed; 420 AA. AC A0A0F0CPF9; DT 24-JUN-2015, integrated into UniProtKB/TrEMBL. DT 24-JUN-2015, sequence version 1. DT 07-JUN-2017, entry version 16. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=OMAG_002819 {ECO:0000313|EMBL:KJJ83310.1}; OS Candidatus Omnitrophus magneticus. OC Bacteria; Candidatus Omnitrophica; Candidatus Omnitrophus. OX NCBI_TaxID=1609969 {ECO:0000313|EMBL:KJJ83310.1, ECO:0000313|Proteomes:UP000033428}; RN [1] {ECO:0000313|EMBL:KJJ83310.1, ECO:0000313|Proteomes:UP000033428} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SKK-01 {ECO:0000313|EMBL:KJJ83310.1}; RA Kolinko S., Richter M., Glockner F.O., Brachmann A., Schuler D.; RT "Single-cell genomics of uncultivated deep-branching MTB reveals a RT conserved set of magnetosome genes."; RL Submitted (FEB-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KJJ83310.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JYNY01000623; KJJ83310.1; -; Genomic_DNA. DR EnsemblBacteria; KJJ83310; KJJ83310; OMAG_002819. DR PATRIC; fig|1609969.3.peg.3029; -. DR Proteomes; UP000033428; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000033428}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000033428}. FT DOMAIN 196 362 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 155 182 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 420 AA; 47688 MW; C79B1915598D9033 CRC64; MKEKAILVTI EKPEVGEWSL DEKRIELEKL VKASGEAEIV FSIMCRLREI TPAFLIGKGK VEEIKNLLIE HGADLVVFSD DLSPSQQRNL EEILEAKTID RTQLILDIFA RRATSNEGKL EVELAQLMYL VPRLSGMGIY LSRLGGGIGT RGPGEQKLEV DRRRIRERIE KLKKDLKDIT RKRGVQSAQR ERFSILTIAL VGYTNSGKST LFNVLTDSHI KAKDQLFSTL DPTVRKMVLP NNQIVLVADT VGFLNDLPHH LIESFKATLE EARRADVLFH VIDVSDPSIE LKYSAVCKVL SELGVSEKPV FIVLNKSDKV EDTIEIERIK RKFENPIVIS ALRKEGLTEL LEAVMTATQD EMDDIELNLP HKYYSIVNMI QEKGIIKKQD YKDDGIFIKA RVPKKVKFAI LKKLKELSQE // ID A0A0F0EVK0_9MICO Unreviewed; 501 AA. AC A0A0F0EVK0; DT 24-JUN-2015, integrated into UniProtKB/TrEMBL. DT 24-JUN-2015, sequence version 1. DT 07-JUN-2017, entry version 14. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=UB45_09470 {ECO:0000313|EMBL:KJK12181.1}; OS Terrabacter sp. 28. OC Bacteria; Actinobacteria; Micrococcales; Intrasporangiaceae; OC Terrabacter. OX NCBI_TaxID=1619947 {ECO:0000313|EMBL:KJK12181.1, ECO:0000313|Proteomes:UP000033603}; RN [1] {ECO:0000313|EMBL:KJK12181.1, ECO:0000313|Proteomes:UP000033603} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=28 {ECO:0000313|EMBL:KJK12181.1, RC ECO:0000313|Proteomes:UP000033603}; RA Roco C.A., Bergaust L., Bakken L., Yavitt J., Shapleigh J.P.; RT "The modularity of denitrifying soil bacteria: using gas kinetics and RT genome sequencing to connect denitrifier phenotype to genotype."; RL Submitted (FEB-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KJK12181.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JYOE01000012; KJK12181.1; -; Genomic_DNA. DR RefSeq; WP_045190453.1; NZ_JYOE01000012.1. DR EnsemblBacteria; KJK12181; KJK12181; UB45_09470. DR PATRIC; fig|1619947.3.peg.402; -. DR Proteomes; UP000033603; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 2. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000033603}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000033603}. FT DOMAIN 280 445 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 501 AA; 54837 MW; 0A948573EA312F30 CRC64; MTSNHSNHTS DSARGTDRER HLFGTRATAL AADDLETDGA QFPLYDGDQL EREERAALRR VQGLSTELED ITEVEYRQLR LERVVLAGVW TEGSAEDAEN SIRELAALAE TAGSTVLEGV IQRRQRPDPA TWLGKGKAVE LRDIVVAEGA DTVICDGELA PSQRRALEDV VKVKVIDRTA LILDIFAQHA KSREGRAQVE LAQLQYLLPR LRGWGESMSR QAGGRVAGGE GIGSRGPGET KIELDRRRIN TKIAKLRRDI KGMKTSRDTR RQSRRVGGVP SVAIAGYTNA GKSSLLNRLT GAGVLVENQL FATLDPTVRR TETEDGRVYT LADTVGFVRS LPHQLVEAFR STLEEVGDSD LLLHVVDGSH PDPEGQITAV RGVLAEVGGD QIKEIIVVNK ADIADPEVLD RLRRHEKHCV TVSARTGEGL AELRALIADE LPKPDIEVEV LVPYDRGDLV SRLHDEAEIL ESEHVADGTR VRAKVTPEIE ADLTAYVVVA S // ID A0A0F0H8A1_9ACTN Unreviewed; 501 AA. AC A0A0F0H8A1; DT 24-JUN-2015, integrated into UniProtKB/TrEMBL. DT 24-JUN-2015, sequence version 1. DT 07-JUN-2017, entry version 15. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=UK14_13205 {ECO:0000313|EMBL:KJK50547.1}; OS Streptomyces sp. NRRL F-4428. OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae; OC Streptomyces. OX NCBI_TaxID=1609137 {ECO:0000313|EMBL:KJK50547.1, ECO:0000313|Proteomes:UP000033569}; RN [1] {ECO:0000313|EMBL:KJK50547.1, ECO:0000313|Proteomes:UP000033569} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NRRL F-4428 {ECO:0000313|EMBL:KJK50547.1, RC ECO:0000313|Proteomes:UP000033569}; RA Ju K.-S., Doroghazi J.R., Metcalf W.; RL Submitted (FEB-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KJK50547.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JYJI01000094; KJK50547.1; -; Genomic_DNA. DR RefSeq; WP_030027323.1; NZ_JYJI01000094.1. DR EnsemblBacteria; KJK50547; KJK50547; UK14_13205. DR PATRIC; fig|1609137.3.peg.2803; -. DR Proteomes; UP000033569; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000313|EMBL:KJK50547.1}; KW Complete proteome {ECO:0000313|Proteomes:UP000033569}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900, KW ECO:0000313|EMBL:KJK50547.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000033569}. FT DOMAIN 280 445 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 501 AA; 54636 MW; E5D7EC1AB87E11C1 CRC64; MTSSSSPSQD ARDATDVRDS QSFTESLRAD ALMEEDVAWS HEIDGDRDGD QFDRSDRAAL RRVAGLSTEL EDVTEVEYRQ LRLERVVLVG VWTSGTVQDA DNSLAELAAL AETAGALVLD GVIQRRDKPD PATFIGSGKA RELRDIVMES GADTVVCDGE LSPGQLIALE DVVKVKVVDR TALILDIFAQ HAKSREGKAQ VALAQMQYML PRLRGWGQSL SRQMGGGGGG GMATRGPGET KIETDRRRIR EKMAKMRREI AEMKTGRDIK RQERRRNRVP SVAIAGYTNA GKSSLLNRLT GAGVLVENAL FATLDPTVRR AETPSGRIYT LADTVGFVRH LPHHLVEAFR STMEEVGDSD LILHIVDGSH PAPEEQLAAV REVIREVGAV DVPEIVVINK ADAADPLVLQ RLLRIERHSI AVSARTGMGI EELLALIDSE LPRPEVEVEA LVPYTRGSLV AKAHAEGEVI SEEHTPEGTL LKARVHQELA ADLAPYALAK Q // ID A0A0F0HG46_NOCAE Unreviewed; 486 AA. AC A0A0F0HG46; DT 24-JUN-2015, integrated into UniProtKB/TrEMBL. DT 24-JUN-2015, sequence version 1. DT 07-JUN-2017, entry version 13. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=UK23_01055 {ECO:0000313|EMBL:KJK53282.1}; OS Lechevalieria aerocolonigenes (Nocardia aerocolonigenes) OS (Saccharothrix aerocolonigenes). OC Bacteria; Actinobacteria; Pseudonocardiales; Pseudonocardiaceae; OC Lechevalieria. OX NCBI_TaxID=68170 {ECO:0000313|EMBL:KJK53282.1, ECO:0000313|Proteomes:UP000033393}; RN [1] {ECO:0000313|EMBL:KJK53282.1, ECO:0000313|Proteomes:UP000033393} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NRRL B-16140 {ECO:0000313|EMBL:KJK53282.1, RC ECO:0000313|Proteomes:UP000033393}; RA Ju K.-S., Doroghazi J.R., Metcalf W.; RL Submitted (FEB-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KJK53282.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JYJG01000003; KJK53282.1; -; Genomic_DNA. DR RefSeq; WP_045309402.1; NZ_JYJG01000003.1. DR EnsemblBacteria; KJK53282; KJK53282; UK23_01055. DR PATRIC; fig|68170.10.peg.221; -. DR Proteomes; UP000033393; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000313|EMBL:KJK53282.1}; KW Complete proteome {ECO:0000313|Proteomes:UP000033393}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900, KW ECO:0000313|EMBL:KJK53282.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000033393}. FT DOMAIN 259 428 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 486 AA; 53044 MW; CA2EC421C285D20F CRC64; MTENIQSTEF DPEFDSSWEE EDFSTGDFER AERAALRRVA GLSTELEDIT EVEYRQLRLE RVVLVGVWTE GTAADSDASM AELARLAETA GSEVLEGVVQ RRDKPDAATY IGSGKVSELR DVVQATGADT VICDGELSPG QLRQLEERLK VKVIDRTALI LDIFAQHARS KEGKAQVELA QLQYLMPRLR GWGETLSRQA GGRAGGGNGG VGLRGPGETK IETDRRRIRD RISKLRRELA AIKVIRETKR SRRVANEIPS VAIAGYTNAG KSSLLNALTD AGVLVEDALF ATLDPTTRRA LTPEGLPYTL TDTVGFVRHL PHQLVEAFRS TLEEVGQADL LVHVVDGSDA MPESQVKAVR EVLAEINEES GTPMPRELLV VNKIDAVGDL GLARLRHLFP DASFVSAHSG LGIEELKVRI AELMPRPEVV VEALVPYARG EVVARVHRDG EVLSEKHTES GTLLSARVRP DLAGLLEEFA TNGTPA // ID A0A0F0HX35_9PSEU Unreviewed; 501 AA. AC A0A0F0HX35; DT 24-JUN-2015, integrated into UniProtKB/TrEMBL. DT 24-JUN-2015, sequence version 1. DT 07-JUN-2017, entry version 15. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=UK12_11385 {ECO:0000313|EMBL:KJK58283.1}; OS Saccharothrix sp. ST-888. OC Bacteria; Actinobacteria; Pseudonocardiales; Pseudonocardiaceae; OC Saccharothrix. OX NCBI_TaxID=1427391 {ECO:0000313|EMBL:KJK58283.1, ECO:0000313|Proteomes:UP000033409}; RN [1] {ECO:0000313|EMBL:KJK58283.1, ECO:0000313|Proteomes:UP000033409} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ST-888 {ECO:0000313|EMBL:KJK58283.1, RC ECO:0000313|Proteomes:UP000033409}; RA Ju K.-S., Doroghazi J.R., Metcalf W.; RL Submitted (FEB-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KJK58283.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JYJF01000024; KJK58283.1; -; Genomic_DNA. DR RefSeq; WP_045302480.1; NZ_JYJF01000024.1. DR EnsemblBacteria; KJK58283; KJK58283; UK12_11385. DR PATRIC; fig|1427391.3.peg.3296; -. DR Proteomes; UP000033409; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000313|EMBL:KJK58283.1}; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000033409}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900, KW ECO:0000313|EMBL:KJK58283.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000033409}. FT DOMAIN 279 444 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 238 272 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 501 AA; 54482 MW; 68F3FD3A1FC18870 CRC64; MTSTFDSRSN SSESARRLAG LKAEALMDED LAAIDEDLDQ HFDGEQYDRS ERAALRRVAG LSTELEDVTE VEYRQLRLER VVLVGVWTDG TAEEAENSLA ELAALAETAG SQVLDGVIQR RDKPDAATYI GSGKALELRD IVASTGADTV VCDGELTPGQ LIHLEDVVKV KVVDRTALIL DIFAQHAKSR EGKAQVSLAQ MQYMLPRLRG WGQSLSRQMG GGGSGSSGGG MATRGPGETK IETDRRRIRE KMAKLRKEIA EMKKGRDTKR QERRRNQVPS VAIAGYTNAG KSSLLNRLTG AGVLVENALF ATLDPTVRRA QTPSGRVYTL ADTVGFVRHL PHHLVEAFRS TMEEVADADL ILHVVDGSHP EPETQLAAVR EVVVSVEAQN VPEIVVINKA DAADPHVLQR LLRREPHAIV VSARTGLGME ELLQLIDDEL PRPAIEVQAL VPYTRGDLVS RVHAEGELLD TEHTGDGTLL RAKVSAELAA ELGRFAVVAQ S // ID A0A0F0KAD9_9MICO Unreviewed; 502 AA. AC A0A0F0KAD9; DT 24-JUN-2015, integrated into UniProtKB/TrEMBL. DT 24-JUN-2015, sequence version 1. DT 30-AUG-2017, entry version 17. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:KJL17912.1}; GN ORFNames=RN50_03018 {ECO:0000313|EMBL:KJL17912.1}; OS Microbacterium foliorum. OC Bacteria; Actinobacteria; Micrococcales; Microbacteriaceae; OC Microbacterium. OX NCBI_TaxID=104336 {ECO:0000313|EMBL:KJL17912.1, ECO:0000313|Proteomes:UP000033572}; RN [1] {ECO:0000313|EMBL:KJL17912.1, ECO:0000313|Proteomes:UP000033572} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 12966 {ECO:0000313|EMBL:KJL17912.1, RC ECO:0000313|Proteomes:UP000033572}; RA Corretto E.; RT "Draft genome sequences of ten Microbacterium spp. with emphasis on RT heavy metal contaminated environments."; RL Submitted (FEB-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KJL17912.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JYIU01000046; KJL17912.1; -; Genomic_DNA. DR RefSeq; WP_045255301.1; NZ_JYIU01000046.1. DR EnsemblBacteria; KJL17912; KJL17912; RN50_03018. DR GeneID; 31897400; -. DR PATRIC; fig|104336.4.peg.3056; -. DR Proteomes; UP000033572; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 2. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000033572}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000033572}. FT DOMAIN 283 448 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 502 AA; 54133 MW; BA4A03210CF433BE CRC64; MTDTTSHSTG DEAVDRVLAN AEKRTEARVF GAAQALQDRS TASHATSDGD QWDLEDRHAL RRVGGLSTEL EDVTEVEYRQ LRLENVVLVG VYPQGTQEDA ENSLRELAAL AETAGAVVLD GVLQRRPHPD AATYIGRGKA QELKDIVAAT GADTVIADTE LAPSQRRALE DVVKVKVIDR TTVILDIFSQ HAKSREGKAQ VELAQLEYLL PRLRGWGDSM SRQAGGQVGA GGAGMGSRGP GETKIELDRR RIRTKMALLR KQIRDFGPAR EAKRAERKRN TIPSVAIAGY TNAGKSSLLN ALTSAGVLVE NALFATLDAT VRRSETSDGR VYTLTDTVGF VRNLPHQLVE AFRSTLEEVG DADVVLHVVD GSHPDPAGQL QTVRDVMGDV GVRDMPELVV FNKADLIDDG DRLVLQGLEP KAHFVSSRSG EGVEELRAAI EEALPKPAVE VHAVVPYDRG DLVAAIHETG MLLSVEHSED GTVVHARVSE RLAADLAPFA AA // ID A0A0F0KH89_9MICO Unreviewed; 501 AA. AC A0A0F0KH89; DT 24-JUN-2015, integrated into UniProtKB/TrEMBL. DT 24-JUN-2015, sequence version 1. DT 07-JUN-2017, entry version 13. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:KJL19515.1}; GN ORFNames=RL72_03164 {ECO:0000313|EMBL:KJL19515.1}; OS Microbacterium azadirachtae. OC Bacteria; Actinobacteria; Micrococcales; Microbacteriaceae; OC Microbacterium. OX NCBI_TaxID=582680 {ECO:0000313|EMBL:KJL19515.1, ECO:0000313|Proteomes:UP000033448}; RN [1] {ECO:0000313|EMBL:KJL19515.1, ECO:0000313|Proteomes:UP000033448} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 23848 {ECO:0000313|EMBL:KJL19515.1, RC ECO:0000313|Proteomes:UP000033448}; RA Corretto E.; RT "Draft genome sequences of ten Microbacterium spp. with emphasis on RT heavy metal contaminated environments."; RL Submitted (FEB-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KJL19515.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JYIT01000084; KJL19515.1; -; Genomic_DNA. DR RefSeq; WP_045251816.1; NZ_JYIT01000084.1. DR EnsemblBacteria; KJL19515; KJL19515; RL72_03164. DR PATRIC; fig|582680.7.peg.3226; -. DR Proteomes; UP000033448; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 2. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000033448}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000033448}. FT DOMAIN 283 448 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 501 AA; 54165 MW; 6CDE035192CB7D38 CRC64; MTQSTTQDEH GDAVERVLQA AERRAESHVF GSAQALQDTA TAGHTSADGE QWDLEERHAL RRVAGLSTEL EDVTEVEYRQ LRLENVVLVG VYPQGAQEDA ENSLRELAAL AETAGAVVLD GLLQRRPHPD PATYLGRGKA QELKDIVAAV GADTVIADTE LASSQRRALE DVVKVKVIDR TTVILDIFSQ HAKSREGRAQ VELAQLEYLL PRLRGWGESM SRQAGGQVGA GGAGMGSRGP GETKIELDRR RIRTRMAMLR KQIRDFTPAR EAKRAERKRH TIPSVAIAGY TNAGKSSLLN ALTSAGVLVE NALFATLDAT VRRSETADGR VYTLTDTVGF VRNLPHQLVE AFRSTLEEVA DADVIVHVVD GSHPDPAGQI KTVRDVMGDV GARGIPEIVA FNKADLLDDD ERMVLRGLVP GAHFVSSRSG EGIDELRAAI DDALPKPAVE IRAVVPYDRG DLVAAVHETG LLLEVAHEEA GTRIHAHVGE RLAAELAPFA V // ID A0A0F0L4S6_9MICO Unreviewed; 501 AA. AC A0A0F0L4S6; DT 24-JUN-2015, integrated into UniProtKB/TrEMBL. DT 24-JUN-2015, sequence version 1. DT 07-JUN-2017, entry version 13. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:KJL28168.1}; GN ORFNames=RS83_03237 {ECO:0000313|EMBL:KJL28168.1}; OS Microbacterium oxydans. OC Bacteria; Actinobacteria; Micrococcales; Microbacteriaceae; OC Microbacterium. OX NCBI_TaxID=82380 {ECO:0000313|EMBL:KJL28168.1, ECO:0000313|Proteomes:UP000033640}; RN [1] {ECO:0000313|EMBL:KJL28168.1, ECO:0000313|Proteomes:UP000033640} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BEL4b {ECO:0000313|EMBL:KJL28168.1, RC ECO:0000313|Proteomes:UP000033640}; RA Corretto E.; RT "Draft genome sequences of ten Microbacterium spp. with emphasis on RT heavy metal contaminated environments."; RL Submitted (FEB-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KJL28168.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JYIW01000026; KJL28168.1; -; Genomic_DNA. DR RefSeq; WP_045280469.1; NZ_JYIW01000026.1. DR EnsemblBacteria; KJL28168; KJL28168; RS83_03237. DR PATRIC; fig|82380.11.peg.3267; -. DR Proteomes; UP000033640; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 2. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000033640}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000033640}. FT DOMAIN 283 448 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 501 AA; 54107 MW; 9861E5302245F687 CRC64; MTDTSTPHTG DEALDRVLAN AETRTEARVF GAAQALQDSS TAAHTSSDGN QWDLEDRHAL RRVGGLSTEL EDVTEVEYRQ LRLENVVLVG VYPQGAQEDA ENSLRELAAL AETAGAVVLD GVLQRRPHPD AATYLGRGKA QELKDIVAAV GADTVIADTE LAPSQRRALE DVVKVKVIDR TTVILDIFSQ HAKSREGKAQ VELAQLEYLL PRLRGWGDSM SRQAGGQVGA GGAGMGSRGP GETKIELDRR RIRTKMALLR RQIRDFGPAR EAKRAERRRN TIPSVAIAGY TNAGKSSLLN ALTSAGVLVE NALFATLDAT VRRSETADGR VYTITDTVGF VRNLPPQLVE AFRSTLEEVG EADVVLHVVD GSHPDPAGQL QTVRDVMGDV GVRDLPEIVV FNKADLIPDD ERLVLRGLQP NAHFVSSRSG EGVPELRAAI EEALPKPAVE VNAVVPYDRG DLVAAIHETG MLLAVEHQED GTAVHARVSE RLAAELAPYT R // ID A0A0F0LVL7_9MICO Unreviewed; 507 AA. AC A0A0F0LVL7; DT 24-JUN-2015, integrated into UniProtKB/TrEMBL. DT 24-JUN-2015, sequence version 1. DT 07-JUN-2017, entry version 13. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:KJL36345.1}; GN ORFNames=RR49_01677 {ECO:0000313|EMBL:KJL36345.1}; OS Microbacterium ginsengisoli. OC Bacteria; Actinobacteria; Micrococcales; Microbacteriaceae; OC Microbacterium. OX NCBI_TaxID=400772 {ECO:0000313|EMBL:KJL36345.1, ECO:0000313|Proteomes:UP000033451}; RN [1] {ECO:0000313|EMBL:KJL36345.1, ECO:0000313|Proteomes:UP000033451} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 18659 {ECO:0000313|EMBL:KJL36345.1, RC ECO:0000313|Proteomes:UP000033451}; RA Corretto E.; RT "Draft genome sequences of ten Microbacterium spp. with emphasis on RT heavy metal contaminated environments."; RL Submitted (FEB-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KJL36345.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JYIY01000074; KJL36345.1; -; Genomic_DNA. DR RefSeq; WP_045247612.1; NZ_JYIY01000074.1. DR EnsemblBacteria; KJL36345; KJL36345; RR49_01677. DR PATRIC; fig|400772.4.peg.1699; -. DR Proteomes; UP000033451; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000033451}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000033451}. FT DOMAIN 289 454 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 507 AA; 54642 MW; 6B6F99364ECF8BF8 CRC64; MTDDIDTARA SRQDDAVERV LARAEARAGV RRFDELGSAQ ALQDASTAYG GETDGEQWDR EERAALRRVP GLSTELEDVT EVEYRQLRLE NVVLVGVHPQ GEQEDAENSL RELAALAETA GAAVLDGVLQ RRPHPDPATY VGRGKAEELR DIVAAVGADT VIADTELAPS QRRALEDVVK VKVIDRTTVI LDIFSQHAKS REGKAQVELA QLEYLLPRLR GWGDSMSRQA GGQVGAGGAG MGSRGPGETK IELDRRRIRT RMAMLRRQIR DFAPARDAKR AERKRNTIPS VAIAGYTNAG KSSLLNRLTS AGVLVENALF ATLDATVRRA EASDGRVYTL TDTVGFVRNL PHQLVEAFRS TLEEVGDADV IVHVVDGSHP DPAAQLATVR DVIGEVGARA TQELVVFNKA DLVDADARLV LRGLVPGAYF VSSRTGEGIA ELRAAVEAAL PLPAVEITAL VPYGRGDLVS AVHDTGLIVS QSHEETGTLL HAHVSERLAA ELAPFAR // ID A0A0F2C579_9MICO Unreviewed; 503 AA. AC A0A0F2C579; DT 24-JUN-2015, integrated into UniProtKB/TrEMBL. DT 24-JUN-2015, sequence version 1. DT 07-JUN-2017, entry version 13. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:KJQ53054.1}; GN ORFNames=RS85_03135 {ECO:0000313|EMBL:KJQ53054.1}; OS Microbacterium sp. SA39. OC Bacteria; Actinobacteria; Micrococcales; Microbacteriaceae; OC Microbacterium. OX NCBI_TaxID=1263625 {ECO:0000313|EMBL:KJQ53054.1, ECO:0000313|Proteomes:UP000033425}; RN [1] {ECO:0000313|EMBL:KJQ53054.1, ECO:0000313|Proteomes:UP000033425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SA39 {ECO:0000313|EMBL:KJQ53054.1, RC ECO:0000313|Proteomes:UP000033425}; RA Corretto E., Antonielli L., Sessitsch A., Kidd P., Weyens N., RA Brader G.; RT "Draft genome sequences of ten Microbacterium spp. with emphasis on RT heavy metal contaminated environments."; RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KJQ53054.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JXRU01000038; KJQ53054.1; -; Genomic_DNA. DR RefSeq; WP_046014368.1; NZ_JXRU01000038.1. DR EnsemblBacteria; KJQ53054; KJQ53054; RS85_03135. DR PATRIC; fig|1263625.4.peg.3147; -. DR Proteomes; UP000033425; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 2. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000033425}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000033425}. FT DOMAIN 283 448 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 503 AA; 54617 MW; 5AAC5B03F0253748 CRC64; MTETTTHSTD DEAVDRVLAN AEKRSEVRVF GAAQALQDES TAAHSTTDGN QWDLEDRHAL RRVGGLSTEL EDVTEVEYRQ LRLENVVLVG VYPQGSQEDA ENSLRELAAL AETAGAVVLD GVLQRRPHPD AATYIGRGKA QELKDIVAAV GADTVIADTE LAPSQRRALE DVVKVKVIDR TTVILDIFSQ HAKSREGKAQ VELAQLEYLL PRLRGWGDSM SRQAGGQVGA GGAGMGSRGP GETKIELDRR RIRTKMALLR RQIRDFGPAR EAKRAERKRN TIPSVAIAGY TNAGKSSLLN ALTSAGVLVE NALFATLDAT VRRSETEDGR VYTITDTVGF VRNLPHQLVE AFRSTLEEVG QADVVLHVVD GSHPDPAGQL QTVRDVLGDV GVRDLPEIVV FNKADLISED ERLVLRGLQP HAHFVSSRSG EGIADLRATI EEALPKPAVE VHAVVPYDRG DLIAAIHETG MLLSVEHRED GTAVHARVSE RLAVDLAPFT SRS // ID A0A0F2J0H8_9BACT Unreviewed; 440 AA. AC A0A0F2J0H8; DT 24-JUN-2015, integrated into UniProtKB/TrEMBL. DT 24-JUN-2015, sequence version 1. DT 07-JUN-2017, entry version 13. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=MCHI_001308 {ECO:0000313|EMBL:KJR42796.1}; OS Candidatus Magnetoovum chiemensis. OC Bacteria; Nitrospirae; Nitrospirales; Nitrospiraceae; OC Candidatus Magnetoovum. OX NCBI_TaxID=1609970 {ECO:0000313|EMBL:KJR42796.1, ECO:0000313|Proteomes:UP000033718}; RN [1] {ECO:0000313|EMBL:KJR42796.1, ECO:0000313|Proteomes:UP000033718} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CS-04 {ECO:0000313|EMBL:KJR42796.1, RC ECO:0000313|Proteomes:UP000033718}; RA Kolinko S., Richter M., Glockner F.O., Brachmann A., Schuler D.; RT "Single-cell genomics of uncultivated deep-branching MTB reveals a RT conserved set of magnetosome genes."; RL Submitted (FEB-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KJR42796.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JZJI01000347; KJR42796.1; -; Genomic_DNA. DR EnsemblBacteria; KJR42796; KJR42796; MCHI_001308. DR PATRIC; fig|1609970.3.peg.1446; -. DR Proteomes; UP000033718; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000033718}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000033718}. FT DOMAIN 261 390 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 76 99 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 440 AA; 49896 MW; 8088925602B75A12 CRC64; MRFDYIAAIG VKDGQPNMFY AAHLMPAGSK QLYDIISGNF YSLEVEFDKE IAVLEAQMER KTMQADGKYQ ESAILISVSK DLRHEQEESL DELEELAKSS DILVLEKVIQ SPKEINPKYL MGIGRLKELI IDALGKGASL LIFDQDLSAS QVRSITDLTE IKVIDRSQLI LDIFARRAHS GDGKVQVELA QLKYMLPRLT GKGSAMSRLM GGIGARGPGE MKLEIDRRRV KDRVHLLERQ LKKLSDARYE RKKNRIKSAI PIVSIIGYTN AGKSTLLNAL TKSSAFVEDK MFATLDTASR RLRFPHERDI IVTDTVGFIR DLPKDLLSAF KATLEELEDA QLLLHLVDIS NPRFMQHISS VETILEELNF KDKPQLLVFN KIDLISNEEA LNLANRYNAA PVCAKDNSTF AALLNELEDR IFCKQHVTHD YYETRELCRY // ID A0A0F2J6U6_9BACT Unreviewed; 170 AA. AC A0A0F2J6U6; DT 24-JUN-2015, integrated into UniProtKB/TrEMBL. DT 24-JUN-2015, sequence version 1. DT 07-JUN-2017, entry version 10. DE SubName: Full=GTP-binding protein HflX {ECO:0000313|EMBL:KJR44053.1}; GN ORFNames=MCHI_000052 {ECO:0000313|EMBL:KJR44053.1}; OS Candidatus Magnetoovum chiemensis. OC Bacteria; Nitrospirae; Nitrospirales; Nitrospiraceae; OC Candidatus Magnetoovum. OX NCBI_TaxID=1609970 {ECO:0000313|EMBL:KJR44053.1, ECO:0000313|Proteomes:UP000033718}; RN [1] {ECO:0000313|EMBL:KJR44053.1, ECO:0000313|Proteomes:UP000033718} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CS-04 {ECO:0000313|EMBL:KJR44053.1, RC ECO:0000313|Proteomes:UP000033718}; RA Kolinko S., Richter M., Glockner F.O., Brachmann A., Schuler D.; RT "Single-cell genomics of uncultivated deep-branching MTB reveals a RT conserved set of magnetosome genes."; RL Submitted (FEB-2015) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KJR44053.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JZJI01000017; KJR44053.1; -; Genomic_DNA. DR EnsemblBacteria; KJR44053; KJR44053; MCHI_000052. DR PATRIC; fig|1609970.3.peg.59; -. DR Proteomes; UP000033718; Unassembled WGS sequence. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR Gene3D; 1.10.45.10; -; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR016171; Vanillyl_alc_oxidase_C-sub2. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000033718}; KW Reference proteome {ECO:0000313|Proteomes:UP000033718}. FT DOMAIN 122 170 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 170 AA; 19486 MW; 33B3B6B0B3749E2B CRC64; MMIFDTELTP AQIRSITDFV EMKVIDRTQL ILDIFARRAK SREGKLQVEL ALLKYLMPRL ITKNTAMSRL TGGIGGRGPG ETKLEINRRR VREKITFLGK EIEKIRKQRN QQRAKRNRKQ VPVISIIGYT NAGKSTLLNT LTKSEITAED KLFATLDPYN ILNPGKIFRV // ID A0A0F2J8A3_9FIRM Unreviewed; 542 AA. AC A0A0F2J8A3; DT 24-JUN-2015, integrated into UniProtKB/TrEMBL. DT 24-JUN-2015, sequence version 1. DT 07-JUN-2017, entry version 13. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=UF75_4420 {ECO:0000313|EMBL:KJR45192.1}; OS Desulfosporosinus sp. I2. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Peptococcaceae; OC Desulfosporosinus. OX NCBI_TaxID=1617025 {ECO:0000313|EMBL:KJR45192.1, ECO:0000313|Proteomes:UP000033442}; RN [1] {ECO:0000313|EMBL:KJR45192.1, ECO:0000313|Proteomes:UP000033442} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=I2 {ECO:0000313|EMBL:KJR45192.1, RC ECO:0000313|Proteomes:UP000033442}; RA Mardanov A.V., Karnachuk O.V., Beletsky A.V., Kadnikov V.V., RA Ravin N.V.; RL Submitted (FEB-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KJR45192.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JYNH01000129; KJR45192.1; -; Genomic_DNA. DR EnsemblBacteria; KJR45192; KJR45192; UF75_4420. DR PATRIC; fig|1617025.3.peg.4666; -. DR Proteomes; UP000033442; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000033442}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000033442}. FT DOMAIN 373 542 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 332 366 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 542 AA; 60120 MW; 483441743857012C CRC64; MRVLMSIDIS GDLSGIRASQ IQELQNLAEI KTERTELIHS EILAELIRLT QLWNREIAIY LSRPGSLLAA AVGRHATVAL PPIKGRSVGK HLRCIHTHPG GNYSLSPLDH SALSSLELES MASIGVLDGQ LTGIQIAYQT GEDNPYLVNL SPNDWQSFDY QESLKPLSKG FSRGTKTLTQ PSGERAFLIA LEESDQESQD NLAELRELTR STGVAVVGQL VQLKRYSQSR SYFGSGKLEE LVHRVQETEA NVIICDDELS PTQLRTLETE TGLKVLDRTA LILDIFAERA QSREGKLQVE LAQLKHLLPY LSGQGQALSR LGGGVGTRGP GETKLELDRR RMRDRITQLE RELKLVLQQR EVQRRQRTKS GLPIIALVGY TNAGKTTFMK NAMEQAGSRS DLPVGENKLF ATLDPIVRSI KINSSLEILL SDTVGFIRKL PTHLLNAFIA TLEEVQQADV LIHVLDASNP QALQHAETVQ DVLKQLGCVE KPMITLLNKI DKVSDEDALN HLTQYLPYPI KLSLTRGDSL KPVWNYVSSA LN // ID A0A0F2L3V1_9CREN Unreviewed; 363 AA. AC A0A0F2L3V1; DT 24-JUN-2015, integrated into UniProtKB/TrEMBL. DT 24-JUN-2015, sequence version 1. DT 07-JUN-2017, entry version 13. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=TU36_02820 {ECO:0000313|EMBL:KJR72312.1}; OS Vulcanisaeta sp. AZ3. OC Archaea; Crenarchaeota; Thermoprotei; Thermoproteales; OC Thermoproteaceae; Vulcanisaeta. OX NCBI_TaxID=1609231 {ECO:0000313|EMBL:KJR72312.1, ECO:0000313|Proteomes:UP000054362}; RN [1] {ECO:0000313|EMBL:KJR72312.1, ECO:0000313|Proteomes:UP000054362} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Servin-Garciduenas L.E., Martinez-Romero E.; RT "Metagenome Sequencing of an Archaeal-Dominated Microbial Community RT from a Hot Spring at the Los Azufres Geothermal Field, Mexico."; RL Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KJR72312.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JZWU01000061; KJR72312.1; -; Genomic_DNA. DR PATRIC; fig|1609231.3.peg.1730; -. DR Proteomes; UP000054362; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000054362}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000054362}. FT DOMAIN 187 357 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 363 AA; 41892 MW; C58485148394FC94 CRC64; MGGKALLLIA DKVDDGKIRE FTALAEVGGY EVVGTVVQRR RPDSRYYLGL GKLSEVESLV EKYGPTIIIT YHQLNPIQYV NLERKLRVRV MDRVLLILEI FEKRAGSKEA KLQIELTRLR LEIPRVREFI RFVKMGEQIG FYGGGEYAIE AYYRHMIRRA SHIRRELERI RERRRELVLR RRSYGLPQVA LTGYTSAGKT TLFNRLIKEN KYVDGKPFAT LDTYSRLAYF NGINAILTDT IGFIDDLPPL LIESFYATIA EVLNADLILF LADLSDDYEE FRRKFLSSLH IFMDLGVQRD RIIPVLNKVD LTDGQDLSDK LALVKQEFND YAIISAKLGI GIDEMRNMVK NRLELLMVNG KNK // ID A0A0F2LBZ5_9CREN Unreviewed; 400 AA. AC A0A0F2LBZ5; DT 24-JUN-2015, integrated into UniProtKB/TrEMBL. DT 24-JUN-2015, sequence version 1. DT 07-JUN-2017, entry version 12. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=TU35_00390 {ECO:0000313|EMBL:KJR74399.1}; OS Thermoproteus sp. AZ2. OC Archaea; Crenarchaeota; Thermoprotei; Thermoproteales; OC Thermoproteaceae; Thermoproteus. OX NCBI_TaxID=1609232 {ECO:0000313|EMBL:KJR74399.1, ECO:0000313|Proteomes:UP000033636}; RN [1] {ECO:0000313|EMBL:KJR74399.1, ECO:0000313|Proteomes:UP000033636} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Servin-Garciduenas L.E., Martinez-Romero E.; RT "Metagenome Sequencing of an Archaeal-Dominated Microbial Community RT from a Hot Spring at the Los Azufres Geothermal Field, Mexico."; RL Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KJR74399.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JZWT01000002; KJR74399.1; -; Genomic_DNA. DR PATRIC; fig|1609232.3.peg.801; -. DR Proteomes; UP000033636; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000033636}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000033636}. FT DOMAIN 186 305 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 400 AA; 45960 MW; 48592E7BED6AE29F CRC64; MRSRALLAYV GPKDRRVAKR LEEFEALVEA AHMEHVDTIT QYGEQDSRFY FGRGKLEEIA SKDFDILITY HSLSPIQIYN IQKFLKRDVI DRVLLILKIF EERASGLESK LQIELAKLRY QLPMVKEYVR RAKMGEQIGF LGAGEYAIDA YYRHMVDRIS TIRRRLDKIR ENRVSLMNKR KEAGVPEVVL TGYTSVGKTT LFNRLTKENK YVDGKPFATL DTYSRRISLW GKDVVLTDTI GFIEDLPPVL IESFYSTLEE VAGADVVLLV MDASDDDEQF AAELETSIKT LSDIGIYKDK IIPILNKIDR IQNNEIINKS KIIRKYFNYF LPASARLGVG IDVLKFFLFW RTPGYAIYEV RPPIGGLVLG DRSYLPVKAE RAASVEAELS NLYIEIRRVA // ID A0A0F2NAX6_9FIRM Unreviewed; 424 AA. AC A0A0F2NAX6; DT 24-JUN-2015, integrated into UniProtKB/TrEMBL. DT 24-JUN-2015, sequence version 1. DT 07-JUN-2017, entry version 13. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=VR68_10660 {ECO:0000313|EMBL:KJR98320.1}; OS Peptococcaceae bacterium BRH_c4a. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Peptococcaceae. OX NCBI_TaxID=1629716 {ECO:0000313|EMBL:KJR98320.1, ECO:0000313|Proteomes:UP000033439}; RN [1] {ECO:0000313|EMBL:KJR98320.1, ECO:0000313|Proteomes:UP000033439} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BRH_c4a {ECO:0000313|EMBL:KJR98320.1}; RA Bagnoud A., Chourey K., Hettich R.L., de Bruijn I., Andersson A.F., RA Leupin O.X., Schwyn B., Bernier-Latmani R.; RT "Microbial metabolic network in the subsurface."; RL Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KJR98320.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LADN01000068; KJR98320.1; -; Genomic_DNA. DR PATRIC; fig|1629716.3.peg.3600; -. DR Proteomes; UP000033439; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000033439}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000033439}. FT DOMAIN 203 367 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 162 196 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 424 AA; 46709 MW; 8BD560A58ED76C23 CRC64; MHRNDNGERI ERAVLVGIEL PGDDSRSAEE SMRELERLTD TAGAEVAGRI IQKKSRPDGS TFLGKGKARE LTDLCGETGA DLVICDRELS PAQTRNLEDL AGVSVIDRSR LILDIFACRA KTREGKLQVE LAQLNFLLPR LTGKGIALSR LGGGIGTRGP GETKLEVDRR RIRKRISDLK KEIEEVRRHR EIMRRGRKDV PLPQVSLVGY TNAGKSTLLK KLTGADVLVE DKLFATLDPT TRRVDLPNNE IVLLTDTVGF INNLPHHLVA AFRATLEEVA ESDVLVHVID ISHPNACGQA QTVIKVLDSL GAGEKPIITV YNKIDRVAED QPPIPDYGDD PVQVSALSGY GMAALLERIA RVAAIKRVRR RFFLPFDRSG LLPLLHQKGL VIKQDHGPGG ITVDVELEEV WAARLESMLR DPSA // ID A0A0F2NCJ2_9DELT Unreviewed; 542 AA. AC A0A0F2NCJ2; DT 24-JUN-2015, integrated into UniProtKB/TrEMBL. DT 24-JUN-2015, sequence version 1. DT 07-JUN-2017, entry version 13. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=VR65_15355 {ECO:0000313|EMBL:KJR99813.1}; OS Desulfobulbaceae bacterium BRH_c16a. OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfobacterales; OC Desulfobulbaceae. OX NCBI_TaxID=1629713 {ECO:0000313|EMBL:KJR99813.1, ECO:0000313|Proteomes:UP000033378}; RN [1] {ECO:0000313|EMBL:KJR99813.1, ECO:0000313|Proteomes:UP000033378} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BRH_c16a {ECO:0000313|EMBL:KJR99813.1}; RA Bagnoud A., Chourey K., Hettich R.L., de Bruijn I., Andersson A.F., RA Leupin O.X., Schwyn B., Bernier-Latmani R.; RT "Microbial metabolic network in the subsurface."; RL Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KJR99813.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LADS01000044; KJR99813.1; -; Genomic_DNA. DR PATRIC; fig|1629713.4.peg.3813; -. DR Proteomes; UP000033378; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000033378}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000033378}. FT DOMAIN 368 532 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 183 206 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 542 AA; 60568 MW; F2C642A89DB1E0FE CRC64; MKTNQLKVLE RLGAKRVQRD KIINPEMARV LSELSFELNR QIGLLVHRSG QVESVIVGNH SQIMIPPLGS VRASGGRLRG LRLIHTHLAG EDISDEDLMD LLFLRLDLIS VIKVAADGLP EKMYSAHLLP GGKDGKSWAF LPPVHPANQQ DSVEDLIAAI EGELSAGRKT SLVDQKEDRA ILISVTTEAK KQAEEALAEL AELAKSDNIT VLDTVLQRRS KVNPRLILGK GRLAEIMVTA LQLDANLLIF NQELNPSQIR SITDFTDLRV IDRTQLILDI FANRAMSREG KLQVEMAQLK YMLPRLSSRD DALSRLTGGI GARGPGETKL EIDRRRINDR LTRLAKELDQ VSKERYRRRA KRRKKELPVL SLVGYTNAGK STLLNTLTNS DIIAEDKLFA TLDPTSRRLR FPTEMEVIIT DTVGFISKLP ADLLQAFMAT LEELKEADLL VHVVDVANPC YRENMAVVEQ LLQQLELGDL PRMTLFNKID LVEDRVSVVR AVGAEGFIIS ALEPESLRDF LIQAERVIGK AMDDKLHPQV EP // ID A0A0F2NYM3_9FLAO Unreviewed; 400 AA. AC A0A0F2NYM3; DT 24-JUN-2015, integrated into UniProtKB/TrEMBL. DT 24-JUN-2015, sequence version 1. DT 07-JUN-2017, entry version 13. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=VR77_08965 {ECO:0000313|EMBL:KJS05367.1}; OS Flavobacteriales bacterium BRH_c54. OC Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales. OX NCBI_TaxID=1629721 {ECO:0000313|EMBL:KJS05367.1, ECO:0000313|Proteomes:UP000033681}; RN [1] {ECO:0000313|EMBL:KJS05367.1, ECO:0000313|Proteomes:UP000033681} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BRH_c54 {ECO:0000313|EMBL:KJS05367.1}; RA Bagnoud A., Chourey K., Hettich R.L., de Bruijn I., Andersson A.F., RA Leupin O.X., Schwyn B., Bernier-Latmani R.; RT "Microbial metabolic network in the subsurface."; RL Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KJS05367.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LADZ01000044; KJS05367.1; -; Genomic_DNA. DR PATRIC; fig|1629721.3.peg.2535; -. DR Proteomes; UP000033681; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000033681}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000033681}. FT DOMAIN 205 390 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 400 AA; 46130 MW; C12713F580A38048 CRC64; MIKKSHDTQD LSVERAVLVG LIIKGEQDEE QLQEYLDELA FLAETAGAET VKRFTQKVGH PDTKTFVGKG KLEEIRTFIK ENEVGLVIFD DELSPSQLRN IERELECKIL DRSNLILDIF ASRAQTAHAR AQVELAQLQY LLPRLTRMWT HLERQKGGIG MRGPGETQIE TDRRIILDKI ALLKEKLKKI DKQKATQRKQ RAQMVRVALV GYTNVGKSTI MNMLSKSEVF AENKLFATLD TTIRKVVIEN LPFLLTDTVG FIRKLPHHLI ESFKSTLDEV KEAEVLVHVV DISHPAFEDH IRVVNETLQD LNALDKPTIM VFNKIDAFTY VKKDEDDLLP KTRENYSLED LKKMWMSRES EVPSVYISAE KKINIEEFKQ LLYDNIKKTH LSIYPNQLLY // ID A0A0F2P453_9GAMM Unreviewed; 439 AA. AC A0A0F2P453; DT 24-JUN-2015, integrated into UniProtKB/TrEMBL. DT 24-JUN-2015, sequence version 1. DT 30-AUG-2017, entry version 14. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=VR73_03510 {ECO:0000313|EMBL:KJS09043.1}; OS Gammaproteobacteria bacterium BRH_c0. OC Bacteria; Proteobacteria; Gammaproteobacteria. OX NCBI_TaxID=1629722 {ECO:0000313|EMBL:KJS09043.1, ECO:0000313|Proteomes:UP000033581}; RN [1] {ECO:0000313|EMBL:KJS09043.1, ECO:0000313|Proteomes:UP000033581} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BRH_c0 {ECO:0000313|EMBL:KJS09043.1}; RA Bagnoud A., Chourey K., Hettich R.L., de Bruijn I., Andersson A.F., RA Leupin O.X., Schwyn B., Bernier-Latmani R.; RT "Microbial metabolic network in the subsurface."; RL Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KJS09043.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LADM01000029; KJS09043.1; -; Genomic_DNA. DR PATRIC; fig|1629722.3.peg.545; -. DR Proteomes; UP000033581; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000033581}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000033581}. FT DOMAIN 199 366 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 439 AA; 48888 MW; 09A2F1579AFDE5BD CRC64; MFFDRPKSGE LAVLVHMDLN TENEPDDPRE FEELVLSAGG DPVEFLTGHR ASPNAKYFIG TGKLEELREA VEHHCAEVVI FNHTLSPSQE RNLEKELKCR VLDRTGLILD IFAQRARTYE GKLQVELAQL QHMSTRLVRG WTHLERQKGG IGLRGPGETQ LETDRRLLRV RLKSIQKRLE KVRSQRQQGR RSRQRAEMPT ISLVGYTNAG KSTLFNRLTD SEVFAADKLF ATLDPTMRRL DLAEFGSVIL ADTVGFISHL PHKLVDAFSA TLEEAASATL LLHIVDAGSD ERQRNMDSVM TVLEEIGAAE NPQLLVYNKI DLLDGMEPHI DRNDSGRPVA VWLSAQTGAG VDLLADAIRE CLGGELVVGR FYVAPERARL RARLYELGAI QSEETLDDGG VILRLSLPVA DFNRLLKAES LNPGDFPALT DIPVIAESA // ID A0A0F2PB61_9FIRM Unreviewed; 421 AA. AC A0A0F2PB61; DT 24-JUN-2015, integrated into UniProtKB/TrEMBL. DT 24-JUN-2015, sequence version 1. DT 07-JUN-2017, entry version 13. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=VR67_17175 {ECO:0000313|EMBL:KJS10626.1}; OS Peptococcaceae bacterium BRH_c8a. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Peptococcaceae. OX NCBI_TaxID=1629715 {ECO:0000313|EMBL:KJS10626.1, ECO:0000313|Proteomes:UP000033493}; RN [1] {ECO:0000313|EMBL:KJS10626.1, ECO:0000313|Proteomes:UP000033493} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BRH_c8a {ECO:0000313|EMBL:KJS10626.1}; RA Bagnoud A., Chourey K., Hettich R.L., de Bruijn I., Andersson A.F., RA Leupin O.X., Schwyn B., Bernier-Latmani R.; RT "Microbial metabolic network in the subsurface."; RL Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KJS10626.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LADP01000042; KJS10626.1; -; Genomic_DNA. DR PATRIC; fig|1629715.3.peg.1111; -. DR Proteomes; UP000033493; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000033493}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000033493}. FT DOMAIN 202 367 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 161 195 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 421 AA; 46708 MW; 1187B9B59A85D904 CRC64; MHEVKGEKKE RVILAALELP GMESEDVEES LIELAGLAET AGAEVVDSDV QRRQRPNFAT YFGKGKVEEL AERARQLEAD LLIVDRELQP AQRRNLEENM ELPVVDRTQL ILDIFARRAR TREGKMQVEL AQLQYLLPRL TGLGTQLSRL GGGIGTRGPG ETKLEVDRRR IRKRITDLKN EIEEVRRHRA LLRRGRQTVP LPLATLVGYT NAGKSTLLNA LTGSDVLAED KLFATLDPTT RRVVLPTGDA VLLIDTVGFI QNLPHHLVAA FRATLEEVVE ADIIIHVVDT SHPRMDAQMS AVEKVLTSLQ VEGKPRLTVY NKVDRVDGTT GGLQSRSLPE GVAVSALRGG GLDEMLKRLS VMLAAGRVTE TFFVPYHKSS VLPLIHENGR VLEEEHGPEG LLITAELGMV WASRVRVKLK Q // ID A0A0F2PSF2_9FIRM Unreviewed; 422 AA. AC A0A0F2PSF2; DT 24-JUN-2015, integrated into UniProtKB/TrEMBL. DT 24-JUN-2015, sequence version 1. DT 07-JUN-2017, entry version 12. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=VR69_13150 {ECO:0000313|EMBL:KJS15507.1}; OS Peptococcaceae bacterium BRH_c4b. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Peptococcaceae. OX NCBI_TaxID=1629717 {ECO:0000313|EMBL:KJS15507.1, ECO:0000313|Proteomes:UP000033446}; RN [1] {ECO:0000313|EMBL:KJS15507.1, ECO:0000313|Proteomes:UP000033446} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BRH_c4b {ECO:0000313|EMBL:KJS15507.1}; RA Bagnoud A., Chourey K., Hettich R.L., de Bruijn I., Andersson A.F., RA Leupin O.X., Schwyn B., Bernier-Latmani R.; RT "Microbial metabolic network in the subsurface."; RL Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KJS15507.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LADO01000051; KJS15507.1; -; Genomic_DNA. DR PATRIC; fig|1629717.3.peg.1687; -. DR Proteomes; UP000033446; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000033446}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000033446}. FT DOMAIN 201 365 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 160 187 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 422 AA; 46473 MW; 313FE435A6CD0F62 CRC64; MENNSPVPER AYLIGVELPG KNDLDAHESI QELVRLVETA GGMVTGWSLQ KRNRPGAATF LGKGKIEEIK SVLSDLEVDL VICDRELSPA QARNLGEALD ARVIDRTQLI LDIFAQRART REGKLQVELA QLNYMLPRLT GMGIQLSRLG GGIGTRGPGE TKLEADRRRI RKRISDLRHE IDEIKKHRAL LRSGRKKVPF PLIALVGYTN AGKSTLLNTL TGSKVLVEDK LFATLDPTIR KVVLPDNRTV LVSDTVGFIS NLPHHLVAAF RATLEEVVEA DLLLHVADAG HPNLEAQVKA VDKVLSSLDA LAKPTIMVYN KADQIDANYP LGQPTDKEMV LIAAKTGFNI DGLLQKIAEH LSGKKIIKTF FIPHNKSSLL PLVHGNGKIL RRQHCSDGME LDVEIDELWA NRISARLSGT NS // ID A0A0F2QA00_9CLOT Unreviewed; 596 AA. AC A0A0F2QA00; DT 24-JUN-2015, integrated into UniProtKB/TrEMBL. DT 24-JUN-2015, sequence version 1. DT 07-JUN-2017, entry version 13. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=VR72_06240 {ECO:0000313|EMBL:KJS22386.1}; OS Clostridiaceae bacterium BRH_c20a. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae. OX NCBI_TaxID=1629719 {ECO:0000313|EMBL:KJS22386.1, ECO:0000313|Proteomes:UP000033488}; RN [1] {ECO:0000313|EMBL:KJS22386.1, ECO:0000313|Proteomes:UP000033488} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BRH_c20a {ECO:0000313|EMBL:KJS22386.1}; RA Bagnoud A., Chourey K., Hettich R.L., de Bruijn I., Andersson A.F., RA Leupin O.X., Schwyn B., Bernier-Latmani R.; RT "Microbial metabolic network in the subsurface."; RL Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KJS22386.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LADT01000018; KJS22386.1; -; Genomic_DNA. DR PATRIC; fig|1629719.3.peg.1729; -. DR Proteomes; UP000033488; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000033488}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000033488}. FT DOMAIN 377 539 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 336 370 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 596 AA; 67400 MW; 70D8530B557EA70E CRC64; MTKVWGELNS LSNQVIIELE KIYTEKIPYG QIASLELLNT IIELSKKINR ELAVYIDRKG VVKLVTVGTW DLVKIPQMWS KRSREGYSGI RCIHTHPNGD SSFSDADLNA LINLKLDAMI ALGIGKNTLC SFANLLPVEG LLTSEYEVQE NLTVLKLLTL PFMDLLIELE KRLEFKGHLL DTGKEKALLV IVDWRKIVDL EIDDIKEELI NLAKTANLEV SDVLIQKRDK RDPSYLVGKG KINEIALKVQ EDQVDCVIFE DSLSPSQQAN LMEYLGIKVF DRTTLILDIF AQRAKTREGK LQVELAQLSY LLPRLSGHGI NLSRLGGGVG TRGPGETKLE TDRRHVRNRI HNLKNEIEVI EKHRNLLQTD RKGKLLPIVA LVGYTNAGKS SLLNSMASDN VLVEDKLFAT LDTTTRSFQV DSQQILLTDT IGFIRNLPHQ LISAFQSTLE EVKLADLLLH VIDVNNKNME SNIKTVQGVL KDLDVLDKPM IYVFNKADLI NNEPIIHPEY NPYCLVSAKT GFGLQQLNSV INEFFSKEEV KTKLHIPYNQ GYLLDKAYQS GKVEIIDYDD QGTTIFLVAQ ENKIINELKK LRVLEY // ID A0A0F2QET0_9RHOB Unreviewed; 441 AA. AC A0A0F2QET0; DT 24-JUN-2015, integrated into UniProtKB/TrEMBL. DT 24-JUN-2015, sequence version 1. DT 07-JUN-2017, entry version 13. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=VR75_12615 {ECO:0000313|EMBL:KJS25003.1}; OS Hyphomonadaceae bacterium BRH_c29. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Hyphomonadaceae. OX NCBI_TaxID=1629720 {ECO:0000313|EMBL:KJS25003.1, ECO:0000313|Proteomes:UP000033495}; RN [1] {ECO:0000313|EMBL:KJS25003.1, ECO:0000313|Proteomes:UP000033495} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BRH_c29 {ECO:0000313|EMBL:KJS25003.1}; RA Bagnoud A., Chourey K., Hettich R.L., de Bruijn I., Andersson A.F., RA Leupin O.X., Schwyn B., Bernier-Latmani R.; RT "Microbial metabolic network in the subsurface."; RL Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KJS25003.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LADW01000075; KJS25003.1; -; Genomic_DNA. DR PATRIC; fig|1629720.5.peg.1568; -. DR Proteomes; UP000033495; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000033495}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000033495}. FT DOMAIN 205 379 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 441 AA; 48616 MW; F26544B05DE96879 CRC64; MGDKLIDRLP ALEIAGAIIP WFTPANRPSA DRLQETAGLI EALGCELAFL RPEHVRQVNS AQLLSGGILD RMAADLEAAD CSLAVIDGAL TPVQQRNLEK KLGVKVIDRT GLILEIFGLR ARTKEGRLQV ELARLLYERS RLVRTWTHLE RQRGGGGFLS GPGESQLEAD RRMLDDKIVR LKADLEDVRR TRAVQRAGRQ RTGKPVVALV GYTNSGKSTL FNRLTGANVF AKDMPFATLD PTIRRLDLPT LGEAALIDTV GFITDLPTHL IDSFQATLEE AMQADLLVHV RDRSSPADND QADDVMRVLE RLEKETGLPL PPMIEAWNKA DLLLPERADA LESFAETQEE MPAVLISAIT GRGIDDLLAL IEHGLLRSAT HVRVILGPED GRARAWLHRN GEVLSDEAQE DGGTLVSVRL KTDRLGQFRA EFPEVDVEPA D // ID A0A0F2R2C8_9DELT Unreviewed; 551 AA. AC A0A0F2R2C8; DT 24-JUN-2015, integrated into UniProtKB/TrEMBL. DT 24-JUN-2015, sequence version 1. DT 07-JUN-2017, entry version 13. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=VR64_08505 {ECO:0000313|EMBL:KJS32136.1}; OS Desulfatitalea sp. BRH_c12. OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfobacterales; OC Desulfobacteraceae; Desulfatitalea. OX NCBI_TaxID=1629708 {ECO:0000313|EMBL:KJS32136.1, ECO:0000313|Proteomes:UP000033431}; RN [1] {ECO:0000313|EMBL:KJS32136.1, ECO:0000313|Proteomes:UP000033431} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BRH_c12 {ECO:0000313|EMBL:KJS32136.1}; RA Bagnoud A., Chourey K., Hettich R.L., de Bruijn I., Andersson A.F., RA Leupin O.X., Schwyn B., Bernier-Latmani R.; RT "Microbial metabolic network in the subsurface."; RL Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KJS32136.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LADR01000023; KJS32136.1; -; Genomic_DNA. DR PATRIC; fig|1629708.4.peg.2732; -. DR Proteomes; UP000033431; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000033431}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000033431}. FT DOMAIN 379 543 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 551 AA; 62026 MW; B60FC88F0F7399E6 CRC64; MKTIWGNTKG LKAGQLHRLE SYYRRRVPSE YLVTPELARD IAELSVEIQR QIGLLINRAG KVAYVLVGDA QSILFPKMYE YRAAPGRLRG VRCIHTHLKN EGLSQEDLTD LALLRLDMIA AITLTDDGFP HKIHWAHILP NQDIQQAPYQ TREVLQPHQL DVGCLELIHA LEREMGQLRA RSMLSAGGER AMLISVTSAP RKKALDSLAE LTELSRSGGI EVLDSVLQIR KDIDSRTLMG SGKLQELAIR AMQLDVTLII FDQELNASQI RSITDQIDLK VIDRTQLILD IFAQRARSKE GKLQVELAQL KYMQPRLVTK NTAMSRLTGG IGGRGPGETK LEINRRRVRD KIHHLEKALV LVQKQRQQQR RKREQKGVPI ISIIGYTNAG KSTLLNTLTH SHVMAESRLF ATLDPSSRRL RFPRDLEVLI TDTVGFIRNL PKDLVVAFRA TLEELESADL LLHVIDVSNP RHAQQIDVVE SILEDLALDQ IPQVRALNKM DLLPPDLVAQ LARQLDGVPI SARDRTTLPP LIDKMAFIID KESDGDKNPS V // ID A0A0F2RCN1_9RHOB Unreviewed; 439 AA. AC A0A0F2RCN1; DT 24-JUN-2015, integrated into UniProtKB/TrEMBL. DT 24-JUN-2015, sequence version 1. DT 07-JUN-2017, entry version 13. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=VR74_12915 {ECO:0000313|EMBL:KJS36398.1}; OS Hyphomonas sp. BRH_c22. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Hyphomonadaceae; Hyphomonas. OX NCBI_TaxID=1629710 {ECO:0000313|EMBL:KJS36398.1, ECO:0000313|Proteomes:UP000033765}; RN [1] {ECO:0000313|EMBL:KJS36398.1, ECO:0000313|Proteomes:UP000033765} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BRH_c22 {ECO:0000313|EMBL:KJS36398.1}; RA Bagnoud A., Chourey K., Hettich R.L., de Bruijn I., Andersson A.F., RA Leupin O.X., Schwyn B., Bernier-Latmani R.; RT "Microbial metabolic network in the subsurface."; RL Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KJS36398.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LADU01000092; KJS36398.1; -; Genomic_DNA. DR PATRIC; fig|1629710.3.peg.1748; -. DR Proteomes; UP000033765; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000033765}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000033765}. FT DOMAIN 205 379 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 164 191 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 439 AA; 48571 MW; 75A275F4C8FA9062 CRC64; MNDKLIDRLP ETEIAGAVIP WFTPANRPTE ERLQETAGLV EALGCKLAFL RADHVRNVNS SVLFSGGLLD RFAADLDEHH CTVAIVDGAL TPVQQRNLET RLGVKVIDRT GLILEIFGLR ARTKEGRLQV ELARLLYERS RLVRTWTHLE RQRGGGGFLS GPGESQLEAD RRMLDDKIVR LRRDLEDVRR TRAVQRAGRK RGGKPIIALV GYTNSGKSTL FNRLSGAKVF AKDMPFATLD PTIRRIDLPT IGEAALIDTV GFITDLPTHL IDSFKATLEE ALQADLLVHV RDRSSPADRD QARDVELVLE RLEKETGITL PPMIEAWNKS DALAPERAEI LEIAAQGKTD VPAVLVSALT GKGMGPLLDA IELALLRGAR DVAVMLDARD GRARAWLHSH GDVNTETNLK DGRVALSVRL PVERVGQFKS EFPDIEIED // ID A0A0F2RK98_9PROT Unreviewed; 428 AA. AC A0A0F2RK98; DT 24-JUN-2015, integrated into UniProtKB/TrEMBL. DT 24-JUN-2015, sequence version 1. DT 07-JUN-2017, entry version 12. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=VR70_11945 {ECO:0000313|EMBL:KJS37627.1}; OS Rhodospirillaceae bacterium BRH_c57. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales; OC Rhodospirillaceae. OX NCBI_TaxID=1629718 {ECO:0000313|EMBL:KJS37627.1, ECO:0000313|Proteomes:UP000033468}; RN [1] {ECO:0000313|EMBL:KJS37627.1, ECO:0000313|Proteomes:UP000033468} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BRH_c57 {ECO:0000313|EMBL:KJS37627.1}; RA Bagnoud A., Chourey K., Hettich R.L., de Bruijn I., Andersson A.F., RA Leupin O.X., Schwyn B., Bernier-Latmani R.; RT "Microbial metabolic network in the subsurface."; RL Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KJS37627.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LAEA01000165; KJS37627.1; -; Genomic_DNA. DR PATRIC; fig|1629718.3.peg.2889; -. DR Proteomes; UP000033468; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000033468}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000033468}. FT DOMAIN 205 377 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 171 198 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 428 AA; 47558 MW; D3E5B6082D5C69B4 CRC64; MTDTDRLARS RAFVIHPALR RGPVDARLPE ARLDEAVGLA EAIDLDVALA EVIPVSKYKP ATYLGTGAVE RLVPLIKEHG AELVVMDCHL SPVQQRNLEK AFEAKVIDRT GLILEIFGER ARTREGQLQV ELAHLSYQKS RLVRSWTHLE RQRGGLGFVG GPGETQIELD RRLIGERIAK LRRELDEVKR TRELHRASRR RVPYPIVALV GYTNAGKSTL FNRVTKATVF AEDLLFATLD PTMRSLELPS GRKIILSDTV GFVSDLPHEL VAAFHATLEE VLEADVIIHV RDIAHPDSEA QKADVERVLR KELGLEDQVE KGLIEALNKI DLLPPDDAVQ VTAQARRDDR LIAVSAHTGQ GVGDLLDLID ERLSMARVTI EVSVPVSDGA TLSWLYRKGE ILSREDGEDA IALLVRLDAA DAARFETR // ID A0A0F2S0N6_9RHOB Unreviewed; 424 AA. AC A0A0F2S0N6; DT 24-JUN-2015, integrated into UniProtKB/TrEMBL. DT 24-JUN-2015, sequence version 1. DT 07-JUN-2017, entry version 13. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=VR71_09340 {ECO:0000313|EMBL:KJS43851.1}; OS Roseovarius sp. BRH_c41. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae; Roseovarius. OX NCBI_TaxID=1629709 {ECO:0000313|EMBL:KJS43851.1, ECO:0000313|Proteomes:UP000033676}; RN [1] {ECO:0000313|EMBL:KJS43851.1, ECO:0000313|Proteomes:UP000033676} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BRH_c41 {ECO:0000313|EMBL:KJS43851.1}; RA Bagnoud A., Chourey K., Hettich R.L., de Bruijn I., Andersson A.F., RA Leupin O.X., Schwyn B., Bernier-Latmani R.; RT "Microbial metabolic network in the subsurface."; RL Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KJS43851.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LADY01000026; KJS43851.1; -; Genomic_DNA. DR ProteinModelPortal; A0A0F2S0N6; -. DR PATRIC; fig|1629709.5.peg.2627; -. DR Proteomes; UP000033676; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000033676}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000033676}. FT DOMAIN 203 373 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 424 AA; 46740 MW; 8022C2A43CE79159 CRC64; MDHARPITRA WVIHPEIAGA SRTREPALAL EEAVALAQAL PDIDVVGSDV VRLRKPDAGR LFGKGKLEEL HQAMEAADVE LVLVDGPVTP VQQRNLEKAW GVKLLDRTGL ILEIFSDRAA TREGVLQVEM AALSYQRTRL VRAWTHLERQ RGGLGFVGGP GETQIEADRR AIDDQLVRLR RQLEKVAKTR TLHRAARAKV PFPIVALVGY TNAGKSTLFN RLTGADVMAK DMLFATLDPT MRRVALPEGG PEVILSDTVG FISDLPTELV AAFRATLEEV LSADLICHVR DISHPETVSQ SRDVAAILES LGVSDKTPQI EIWNKIDQLE DEARAAAVTQ AERQDDVLAI SAITGQGIND LVAAIGAKLA DVTHETVLHL QFGEGRKRAW LFEKELVESE RQTDDGFDLT VHWTARQEAQ FRDL // ID A0A0F2SAJ9_9FIRM Unreviewed; 536 AA. AC A0A0F2SAJ9; DT 24-JUN-2015, integrated into UniProtKB/TrEMBL. DT 24-JUN-2015, sequence version 1. DT 07-JUN-2017, entry version 12. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=VR66_20795 {ECO:0000313|EMBL:KJS47256.1}; OS Peptococcaceae bacterium BRH_c23. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Peptococcaceae. OX NCBI_TaxID=1629714 {ECO:0000313|EMBL:KJS47256.1, ECO:0000313|Proteomes:UP000033503}; RN [1] {ECO:0000313|EMBL:KJS47256.1, ECO:0000313|Proteomes:UP000033503} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BRH_c23 {ECO:0000313|EMBL:KJS47256.1}; RA Bagnoud A., Chourey K., Hettich R.L., de Bruijn I., Andersson A.F., RA Leupin O.X., Schwyn B., Bernier-Latmani R.; RT "Microbial metabolic network in the subsurface."; RL Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KJS47256.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LADV01000252; KJS47256.1; -; Genomic_DNA. DR PATRIC; fig|1629714.3.peg.1694; -. DR Proteomes; UP000033503; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000033503}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000033503}. FT DOMAIN 367 536 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 326 360 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 536 AA; 59735 MW; 13B7469CDAB32DB6 CRC64; MDISGDLSGI RASQIQELKN LSEIKTERTE LINSTILEEL IRLTQLWNRE IAVYLSRPGT LLAGAVGRHA TVALPPIKGR SVGKHLRCIH THPKGNYSLS PLDHSALSSL QLESMASLGV LDGQLTGIQI AYRTDEDNPY LVNLSPKNWN SFDYNQALNE LSKGTSRGTK PQTPPNSERA FLIALEESDQ ENQDYLDELR ELTRSAGVEV VGQLVQLRRY SQNRSYFGTG KLEELVHRLQ ETEANVIICD DELSTTQLRT LEAETGLKVL DRSGLILDIF AQRAQSREGK LQVELAQLKH LLPYLTGQGQ ALSRLGGGVG TRGPGETKLE MDRRRMRDRI TQLERELKLV LQHREVQRRQ RSRSGLPIIA LVGYTNAGKT TFMKNAMEQA GSRSDLPLGE NRLFATLDPI VRSIRVSSSL EVLLSDTVGF IRKLPTQLIN AFIATLEEVQ QADVLIHVLD ASHPQALQQA EAVHQVLKQL GCVEKPMLSL LNKVDKALDE DALNDLAQQL PYPVKMSLTR GDSLKPVWKY VSSLLT // ID A0A0F2TC26_9ACTN Unreviewed; 500 AA. AC A0A0F2TC26; DT 24-JUN-2015, integrated into UniProtKB/TrEMBL. DT 24-JUN-2015, sequence version 1. DT 07-JUN-2017, entry version 14. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=VM95_19035 {ECO:0000313|EMBL:KJS60763.1}; OS Streptomyces rubellomurinus. OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae; OC Streptomyces. OX NCBI_TaxID=359131 {ECO:0000313|EMBL:KJS60763.1, ECO:0000313|Proteomes:UP000033699}; RN [1] {ECO:0000313|EMBL:KJS60763.1, ECO:0000313|Proteomes:UP000033699} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 31215 {ECO:0000313|EMBL:KJS60763.1, RC ECO:0000313|Proteomes:UP000033699}; RA Ju K.-S., Doroghazi J.R., Metcalf W.; RL Submitted (FEB-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KJS60763.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JZKH01000037; KJS60763.1; -; Genomic_DNA. DR RefSeq; WP_045698367.1; NZ_JZKH01000037.1. DR EnsemblBacteria; KJS60763; KJS60763; VM95_19035. DR PATRIC; fig|359131.3.peg.4450; -. DR Proteomes; UP000033699; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000313|EMBL:KJS60763.1}; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000033699}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900, KW ECO:0000313|EMBL:KJS60763.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000033699}. FT DOMAIN 278 443 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 237 271 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 500 AA; 54446 MW; E77AF0096B6A6F37 CRC64; MTSTFEARDH ADAPRRIDGR RAEALMDEDL AAIDEDLGHH YDGDQYDRSE RAALRRVAGL STELEDVTEV EYRQLRLERV VLVGVWTDGT LEEAENSMAE LAALAETAGS EVLDGVIQRR DKPDAATYIG SGKAQELRDI VASSGADTVV CDGELTPGQL IHLEDVVKVK VVDRTALILD IFAQHAKSRE GKAQVSLAQM QYMLPRLRGW GQSLSRQMGG GGSGSSGGGM ATRGPGETKI ETDRRRIREK MAKLRREIAD MKKGRDTKRQ ERKRHQVPSV AIAGYTNAGK SSLLNRLTGA GVLVENALFA TLDPTVRRAQ TPSGRVYTLA DTVGFVRHLP HHLVEAFRST MEEVADADLI LHVVDGSHPE PETQLAAVRE VIVSVDAQNV PEIVVINKAD AADPHVLQRL LRREPHAIVV SARTGAGMDE LLQLIDDELP RPAIEVRALV PYTQGALVSR VHAEGELIAT EHTGEGTLVH AKVPAELAAE LEHFAVALQG // ID A0A0F3G2P1_9LACO Unreviewed; 425 AA. AC A0A0F3G2P1; DT 24-JUN-2015, integrated into UniProtKB/TrEMBL. DT 24-JUN-2015, sequence version 1. DT 07-JUN-2017, entry version 14. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=AH70_03710 {ECO:0000313|EMBL:KJU74918.1}; OS Pediococcus damnosus LMG 28219. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; OC Pediococcus. OX NCBI_TaxID=1448143 {ECO:0000313|EMBL:KJU74918.1, ECO:0000313|Proteomes:UP000033638}; RN [1] {ECO:0000313|EMBL:KJU74918.1, ECO:0000313|Proteomes:UP000033638} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=LMG 28219 {ECO:0000313|EMBL:KJU74918.1, RC ECO:0000313|Proteomes:UP000033638}; RA Snnauwaert I., Stragier P., De Vuyst L., Vandamme P.; RT "Comparative genome analysis of Pediococcus damnosus LMG 28219, a RT strain well-adapted to the beer environment."; RL BMC Genomics 16:267-267(2015). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KJU74918.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JANK01000023; KJU74918.1; -; Genomic_DNA. DR RefSeq; WP_046870864.1; NZ_JANK01000023.1. DR EnsemblBacteria; KJU74918; KJU74918; AH70_03710. DR PATRIC; fig|1448143.3.peg.721; -. DR Proteomes; UP000033638; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000033638}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}. FT DOMAIN 198 367 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 157 184 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 425 AA; 47613 MW; 7EBF5C168EB74D28 CRC64; MTEKVIIAGL ELPNQDMDYA MQELAALVEA NNMEAAETVI QKLDRPNAAT YFGSGKVVEL HELGESINVH TLVVNAELSP SQIRNLEKES KLDVIDRTGL ILEIFANRAK SREAKLQVEI AKLNYQMPRL RTSSSQRLDQ QSAGDAGGGY TNRGAGETKL EMNRRTIQQR INNLNHELKE MTTSSAVQRQ KRDQTGLPSV ALVGYTNAGK STTMNGLVRL YGESDEKQVF EKNMLFATLD TSVRKLTFPD QKQLLLSDTV GFVSNLPHQL IKAFRSTLAE AAQADLLVQV VDVSDPHFRE MIQTTNETLQ EVGVTKAPMI VAFNKADVAD VEFPTLEGNE EITYSAKDKK SLILLTNMIK QKVFTGYREA TFLIPFDQGQ IVDYLNQHTN VLKTDYKETG TEIVTELSSD DYQRFHKYLV EPVED // ID A0A0F3GL56_9BACT Unreviewed; 539 AA. AC A0A0F3GL56; DT 24-JUN-2015, integrated into UniProtKB/TrEMBL. DT 24-JUN-2015, sequence version 1. DT 07-JUN-2017, entry version 12. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=MBAV_005245 {ECO:0000313|EMBL:KJU82562.1}; OS Candidatus Magnetobacterium bavaricum. OC Bacteria; Nitrospirae; Nitrospirales; Nitrospiraceae; OC Candidatus Magnetobacterium. OX NCBI_TaxID=29290 {ECO:0000313|EMBL:KJU82562.1, ECO:0000313|Proteomes:UP000033423}; RN [1] {ECO:0000313|EMBL:KJU82562.1, ECO:0000313|Proteomes:UP000033423} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=TM-1 {ECO:0000313|EMBL:KJU82562.1}; RA Kolinko S., Richter M., Glockner F.O., Brachmann A., Schuler D.; RT "Single-cell genomics of uncultivated deep-branching MTB reveals a RT conserved set of magnetosome genes."; RL Submitted (FEB-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KJU82562.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LACI01002263; KJU82562.1; -; Genomic_DNA. DR EnsemblBacteria; KJU82562; KJU82562; MBAV_005245. DR PATRIC; fig|29290.4.peg.6936; -. DR Proteomes; UP000033423; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000033423}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000033423}. FT DOMAIN 372 536 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 331 358 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 539 AA; 60942 MW; 899A2BDFA3974C4C CRC64; MYGHIAGLKK KTVYDLERIY RRKVPVREVI SQELARFIAE ISHEINRQIG VLIAREGVIT HVICGDASGL FLPELTDYPL GKKPLRGLRF IHTHLKNEGL SGDDLTDLAL LRFDYLGAIG LRNGLPDKFY GAYLLPRNPD KLYEVSDAVG MYDLDVDFRE FIDSLQEQMQ RQRAISKDGT QERAILISVS QAPRYQQEES LNELEELAAS CDVMVLDKVI QRAKEINPRY LIGTGKVREL VIDALGKGAT LLVFDQDLSP SQRRAITDIT ELKVIDRPQL ILDIFARRAH SGDGKVQVEL AQLKYRLPHL TGKGTAMSRL MGGVGGRGPG EMKLEIDRRR VRDRITLLER ELDKLAMARL QRKRRRLKMS LPILSIIGYT NAGKSTLLNS LTRSTTFVQD KMFATLDTAS RRLRFPQERD VIITDTVGFI RDLPPDLMAA FKATLEELQD ADVFIHVVDI SNPRFEEHMD SVRNILTELE LIEKPQLLVF NKCDKVAPDV VQNLLARYNA LAIAAIDNGT FGPLLEAIHD RVFETAALH // ID A0A0F3GS47_9BACT Unreviewed; 415 AA. AC A0A0F3GS47; DT 24-JUN-2015, integrated into UniProtKB/TrEMBL. DT 24-JUN-2015, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=MBAV_003028 {ECO:0000313|EMBL:KJU84775.1}; OS Candidatus Magnetobacterium bavaricum. OC Bacteria; Nitrospirae; Nitrospirales; Nitrospiraceae; OC Candidatus Magnetobacterium. OX NCBI_TaxID=29290 {ECO:0000313|EMBL:KJU84775.1, ECO:0000313|Proteomes:UP000033423}; RN [1] {ECO:0000313|EMBL:KJU84775.1, ECO:0000313|Proteomes:UP000033423} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=TM-1 {ECO:0000313|EMBL:KJU84775.1}; RA Kolinko S., Richter M., Glockner F.O., Brachmann A., Schuler D.; RT "Single-cell genomics of uncultivated deep-branching MTB reveals a RT conserved set of magnetosome genes."; RL Submitted (FEB-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KJU84775.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LACI01001293; KJU84775.1; -; Genomic_DNA. DR EnsemblBacteria; KJU84775; KJU84775; MBAV_003028. DR PATRIC; fig|29290.4.peg.4010; -. DR Proteomes; UP000033423; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000033423}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000033423}. FT DOMAIN 248 415 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 207 234 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 415 AA; 47176 MW; 499B4A0290A53F56 CRC64; MPDNFYGAHL LPRNPDKLYE VSDPVGTYNL ELDFREFIDS LQEQMQRQRA FSKDDTHERA ILISVSQVPR YQQEESLNEL EELAASCDVM VLDKVVQRAK EINPRYLIGT GKVRELVIDA LGKGATLLVF DQDLSPSQRR AITDITELKV IDRSQLILDI FARRAHSGDG KVQVELAQLK YRLPHLTGKG TAMSRLMGGV GGRGPGEMKL EIDRRRVRDR INLLERELDK LAMARLQRKR RRLKMSLPIL SIIGYTNAGK STLLNSLTRS TTFVQDKMFA TLDTASRRLR FPHERDVIIT DTVGFIRDLP PDLMAAFKAT LEELEDADVF IHVVDISNPR FEEHMDSVRN ILTELELIEK PQLLVFNKCD KIAPDVVQNL LTRYNALAIV AIDNSTFGPL LDAIHYRVFE GAAPL // ID A0A0F3IP15_9PROT Unreviewed; 437 AA. AC A0A0F3IP15; DT 24-JUN-2015, integrated into UniProtKB/TrEMBL. DT 24-JUN-2015, sequence version 1. DT 07-JUN-2017, entry version 13. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=VZ95_17595 {ECO:0000313|EMBL:KJV08471.1}; OS Elstera litoralis. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales; OC Rhodospirillaceae; Elstera. OX NCBI_TaxID=552518 {ECO:0000313|EMBL:KJV08471.1, ECO:0000313|Proteomes:UP000033774}; RN [1] {ECO:0000313|EMBL:KJV08471.1, ECO:0000313|Proteomes:UP000033774} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Dia-1 {ECO:0000313|EMBL:KJV08471.1, RC ECO:0000313|Proteomes:UP000033774}; RA Rahalkar M.C., Dhakephalkar P.K., Pore S.D., Arora P., Kapse N.G., RA Pandit P.S.; RT "Draft genome sequence of Elstera litoralis."; RL Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KJV08471.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LAJY01000572; KJV08471.1; -; Genomic_DNA. DR RefSeq; WP_045777022.1; NZ_LAJY01000572.1. DR EnsemblBacteria; KJV08471; KJV08471; VZ95_17595. DR PATRIC; fig|552518.3.peg.3592; -. DR Proteomes; UP000033774; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000033774}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000033774}. FT DOMAIN 208 377 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 174 201 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 437 AA; 48183 MW; C249C49846E64536 CRC64; MEAADLGEHA ATRAFVIHPD LGRQEGPDSR SIEGRVNEAV GLAEAIGLDV QRAEAVRLKI LRPATLFGTG VLERLKQGIE EVQAAVVIVD GHLSPVQQRN LEREWQVKVI DRTGLILEIF GARARTHEGR LQVELAALTY QRSRLVRSWT HLERQRGGFG FLGGPGESQL EIDRRLIGDR IAKLKRELEE VKRTRELHRG ARKKVPQPVI ALVGYTNAGK STLFNRLTNA DVMAEDMLFA TLDPTMRGLT LPSGRRVILS DTVGFISALP TQLVAAFRAT LEEVLEADII LHVRDASHPD SMAQKADVEA VLRSLGLEKQ VDAGLPEVLN KVDRLDGEGL AEQTRRVTGT ALPLSALTGQ GIDSLLTYLD EALRDRQQVI AVTIDPADGR HLAWLYAHGE VLSREDDETG QAHLTVGLDP MELSRYQRQF PQSVIGL // ID A0A0F3KT46_9NEIS Unreviewed; 460 AA. AC A0A0F3KT46; DT 24-JUN-2015, integrated into UniProtKB/TrEMBL. DT 24-JUN-2015, sequence version 1. DT 07-JUN-2017, entry version 13. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=VI06_00480 {ECO:0000313|EMBL:KJV34341.1}; OS Aquitalea magnusonii. OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Chromobacteriaceae; Aquitalea. OX NCBI_TaxID=332411 {ECO:0000313|EMBL:KJV34341.1, ECO:0000313|Proteomes:UP000033764}; RN [1] {ECO:0000313|EMBL:KJV34341.1, ECO:0000313|Proteomes:UP000033764} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SM6 {ECO:0000313|EMBL:KJV34341.1, RC ECO:0000313|Proteomes:UP000033764}; RA Sulaiman J., Priya K., Chan K.-G.; RT "Draft genome sequence of Aquitalea magnusonii strain SM6."; RL Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KJV34341.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JZRC01000003; KJV34341.1; -; Genomic_DNA. DR RefSeq; WP_045844795.1; NZ_JZRC01000003.1. DR EnsemblBacteria; KJV34341; KJV34341; VI06_00480. DR PATRIC; fig|332411.4.peg.1757; -. DR Proteomes; UP000033764; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000033764}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000033764}. FT DOMAIN 227 394 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 190 222 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 460 AA; 51649 MW; E297232A5B4F3C26 CRC64; MQETEVKEQP RYAIIASVQL PEVSDVEFAS SLAELSELAK TLGFQVVHTF VQKRNGFDRT AYLGVGKLEE IHMYVNRGLR ADELADAPQW LDPSAIEIDV LLVDHEISPS QARNLELAVG CEVMDRTMVI LEIFHRNARS RAAKAQVEIA RLGYMAPRLR EAAKLAGPQG RQRSGMGGRG SGESHTELDR RKVRDRIAEL QREILAMELE RKTQRARRLE RQGQGLAGVS LVGYTNAGKS TLMRALTGSE VLVANKLFAT LDTTVRAIYP ESVPRVLVSD TVGFIKNLPH GLVASFKSTL EEALDAGLLL HVIDASDPGF ERQLEVTDTV LHEIGADEVP RIRVFNKIDH VADESGWRAE LEQRYPGCVV MSARRPEDVS ALRARIVAFF QQDLTEDEIL LPWSAQQLRG EIYSHCQVLE ERADEEGSWF RVRGEPEQLR RLHEKLNPGS GGREKEYWEV // ID A0A0F3KUQ8_9NEIS Unreviewed; 376 AA. AC A0A0F3KUQ8; DT 24-JUN-2015, integrated into UniProtKB/TrEMBL. DT 24-JUN-2015, sequence version 1. DT 07-JUN-2017, entry version 13. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=VI06_00280 {ECO:0000313|EMBL:KJV34677.1}; OS Aquitalea magnusonii. OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Chromobacteriaceae; Aquitalea. OX NCBI_TaxID=332411 {ECO:0000313|EMBL:KJV34677.1, ECO:0000313|Proteomes:UP000033764}; RN [1] {ECO:0000313|EMBL:KJV34677.1, ECO:0000313|Proteomes:UP000033764} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SM6 {ECO:0000313|EMBL:KJV34677.1, RC ECO:0000313|Proteomes:UP000033764}; RA Sulaiman J., Priya K., Chan K.-G.; RT "Draft genome sequence of Aquitalea magnusonii strain SM6."; RL Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KJV34677.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JZRC01000002; KJV34677.1; -; Genomic_DNA. DR RefSeq; WP_045844771.1; NZ_JZRC01000002.1. DR EnsemblBacteria; KJV34677; KJV34677; VI06_00280. DR PATRIC; fig|332411.4.peg.1009; -. DR Proteomes; UP000033764; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000033764}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000033764}. FT DOMAIN 198 364 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 164 191 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 376 AA; 41746 MW; 0C8857AFED58574B CRC64; MFDRPDIGDQ AVLVCLDFGD PDHQENVAEC AELVRSANVT VTGIIQGKRQ RPDAALFAGK GKVEEVGVMV RATGANVVIF NHQLSPAQER NLERALQCRV IDRTSLILDI FAQRARSHEG KLQVELAQLS HIATRLVRGW THLERQKGGI GLRGPGESQL ETDRRLLGNR VKALKERLAQ VQKQRNTQRR GRQRTGIASV SIVGYTNAGK STLFNALTKA RAYAADQLFA TLDTTSRKLF LNTETSIIVS DTVGFIRDLP HTLVAAFRAT LEETIQADLL LHVVDSSNPL RDVQIEEVNK VLAEIGAESV PQLIVWNKTD LRQLPADIER DEHGEIQAVR LSALTGEGLE LLREALAERL QSPDNQHEEQ DEYVAE // ID A0A0F3L0Q7_9GAMM Unreviewed; 436 AA. AC A0A0F3L0Q7; DT 24-JUN-2015, integrated into UniProtKB/TrEMBL. DT 24-JUN-2015, sequence version 1. DT 07-JUN-2017, entry version 14. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=VI08_02370 {ECO:0000313|EMBL:KJV37043.1}; OS Luteibacter yeojuensis. OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales; OC Rhodanobacteraceae; Luteibacter. OX NCBI_TaxID=345309 {ECO:0000313|EMBL:KJV37043.1, ECO:0000313|Proteomes:UP000033651}; RN [1] {ECO:0000313|EMBL:KJV37043.1, ECO:0000313|Proteomes:UP000033651} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SU11 {ECO:0000313|EMBL:KJV37043.1, RC ECO:0000313|Proteomes:UP000033651}; RA Sulaiman J., Priya K., Chan K.-G.; RT "Draft genome sequence of Luteibacter yeojuensis strain SU11."; RL Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KJV37043.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JZRB01000003; KJV37043.1; -; Genomic_DNA. DR RefSeq; WP_045827916.1; NZ_JZRB01000003.1. DR EnsemblBacteria; KJV37043; KJV37043; VI08_02370. DR PATRIC; fig|345309.4.peg.2334; -. DR Proteomes; UP000033651; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000033651}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000033651}. FT DOMAIN 200 367 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 166 193 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 436 AA; 47475 MW; CE79CD90D1EF9E1F CRC64; MFDRQKKGDR AVLVLPHSRG EGDAVRRGEE FAELVASAGA EVLTSIPARV AEPNPRFYIG SGKADEVAEA VRALEADLVL VDHVLTPVQE RNLEKHLKTR VVDRAGLILD IFAQRARSHE GKLEVELAQL KHLATRLVRG WTHLDAQRGG AIGNRGPGET QLETDRRLLA ERVKMLTKRL EKVQVQRDQQ RRSRLRNTVP RVALVGYTNA GKSTLFNALT TGGVYAADQL FATLDPTVRK VEGLACGPAV VADTVGFIRE LPHDLVAAFR ATLAEARDAD LLLHVSDAAD EERELLRRVV NSVLEEIGAG DVPQLMVMNK IDLIEDAEPR IDRGDDGKPR TVWLSAHSGQ GLDGLREALG ELLGGDRIKA GVRLPLTAGR LHARLKAAGA IAGEAIDEDG WQLDIDAPRS VLAPLVGDDI HGAPLRELID PPHAEH // ID A0A0F3LH72_9CAUL Unreviewed; 437 AA. AC A0A0F3LH72; DT 24-JUN-2015, integrated into UniProtKB/TrEMBL. DT 24-JUN-2015, sequence version 1. DT 07-JUN-2017, entry version 14. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=VH88_07975 {ECO:0000313|EMBL:KJV41619.1}; OS Brevundimonas sp. KM4. OC Bacteria; Proteobacteria; Alphaproteobacteria; Caulobacterales; OC Caulobacteraceae; Brevundimonas. OX NCBI_TaxID=1628191 {ECO:0000313|EMBL:KJV41619.1, ECO:0000313|Proteomes:UP000033583}; RN [1] {ECO:0000313|EMBL:KJV41619.1, ECO:0000313|Proteomes:UP000033583} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=KM4 {ECO:0000313|EMBL:KJV41619.1, RC ECO:0000313|Proteomes:UP000033583}; RA Sulaiman J., Priya K., Chan K.-G.; RT "Draft genome sequence of Brevundimonas sp. KM4."; RL Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KJV41619.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JZRG01000012; KJV41619.1; -; Genomic_DNA. DR RefSeq; WP_045810777.1; NZ_JZRG01000012.1. DR EnsemblBacteria; KJV41619; KJV41619; VH88_07975. DR PATRIC; fig|1628191.3.peg.264; -. DR Proteomes; UP000033583; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000033583}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000033583}. FT DOMAIN 206 380 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 437 AA; 48759 MW; 8A177078513B5CA5 CRC64; MTQKLIDHTV PLIRAVVIHP DRRSDSPRLA SERLEEAAGL ARALDLNVRA EEIVRLRSTT PATLFGTGKV EELAALVRAA DAEAVIIDDA LTPVQQRNLE KAWEVKVIDR TGLILEIFGR RARTKEGRLQ VELARLDYER SRLVRTWTHL ERQRGGTGST GGPGETQIEL DRRLIADRIV RLKSELEEVR RTRGLHRKQR QKAPFPTIAL VGYTNAGKST LFNRLTGSEV FAKDLLFATL DTTQRTIRLP QGRPAIVADT VGFISDLPHE LVESFRATLE EVGEADLILH VRDIASPDSA AQAKDVEAVL KQIETPEGKT RRVLEVWNKI DLLDDEARET VLGQAERLAK DGEAVAVSAW TGEGIEPLRQ IIAGLIDDDP ETQLTLEPHQ GDALAWLYEH GRVTARDADE LGRTHVTVRL HPAALGRFER LYPDLTD // ID A0A0F3RP71_9LACO Unreviewed; 428 AA. AC A0A0F3RP71; DT 24-JUN-2015, integrated into UniProtKB/TrEMBL. DT 24-JUN-2015, sequence version 1. DT 07-JUN-2017, entry version 13. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=VC81_11065 {ECO:0000313|EMBL:KJW11771.1}; OS Lactobacillus spicheri. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; OC Lactobacillus. OX NCBI_TaxID=216463 {ECO:0000313|EMBL:KJW11771.1, ECO:0000313|Proteomes:UP000033491}; RN [1] {ECO:0000313|EMBL:KJW11771.1, ECO:0000313|Proteomes:UP000033491} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=LP38 {ECO:0000313|EMBL:KJW11771.1, RC ECO:0000313|Proteomes:UP000033491}; RA Zheng J., Ganezle M.; RL Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KJW11771.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JZCR01000024; KJW11771.1; -; Genomic_DNA. DR RefSeq; WP_045808135.1; NZ_JZCR01000024.1. DR EnsemblBacteria; KJW11771; KJW11771; VC81_11065. DR PATRIC; fig|216463.3.peg.1465; -. DR Proteomes; UP000033491; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000033491}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}. FT DOMAIN 199 367 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 172 196 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 428 AA; 47154 MW; D02B9BF67B5AB1F1 CRC64; MDETPATPVV TIGLNSGQAT FDYSMEELKA LVEANHMTVV EQVQQALTKP NPGTYFGTGK VEELATIVAD DGVDTVVVND ELTPSQIRNL ENGTKARIID RTGLILEIFA NRAQSREAKL QVQLAMLQYQ LPRLHTSASQ RLDQQGGAGG LANRGSGESQ TEMSRRTIER SINHVNHELK EINQAAETQR AQRERNELPS VALVGYTNAG KSTIMNALVQ RFGKNEDKQV FVKNMLFATL DTSVRQLIFP DQKKLLLSDT VGFVSQLPTN LVKAFRSTLS EAANADLLIQ VVDYADPNRD AMMQTTEDTL QEIGVTDVPM ITVFNKADLT DAEYPSRAGD QLIVSAKDDA SIDILVQVMK EKVFHNYVTA NFLIPFAAGD VVAYFNDHAN VLSTDYQADG TAMRVELPSA DFNKYKRYVV TDADAAED // ID A0A0F4IS57_9ACTN Unreviewed; 501 AA. AC A0A0F4IS57; DT 24-JUN-2015, integrated into UniProtKB/TrEMBL. DT 24-JUN-2015, sequence version 1. DT 05-JUL-2017, entry version 15. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=VR44_34160 {ECO:0000313|EMBL:KJY24855.1}; OS Streptomyces katrae. OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae; OC Streptomyces. OX NCBI_TaxID=68223 {ECO:0000313|EMBL:KJY24855.1, ECO:0000313|Proteomes:UP000033551}; RN [1] {ECO:0000313|EMBL:KJY24855.1, ECO:0000313|Proteomes:UP000033551} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NRRL ISP-5550 {ECO:0000313|EMBL:KJY24855.1, RC ECO:0000313|Proteomes:UP000033551}; RA Ju K.-S., Doroghazi J.R., Metcalf W.; RL Submitted (FEB-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KJY24855.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JZWV01001158; KJY24855.1; -; Genomic_DNA. DR EnsemblBacteria; KJY24855; KJY24855; VR44_34160. DR PATRIC; fig|68223.7.peg.3800; -. DR Proteomes; UP000033551; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 2. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000313|EMBL:KJY24855.1}; KW Complete proteome {ECO:0000313|Proteomes:UP000033551}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900, KW ECO:0000313|EMBL:KJY24855.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000033551}. FT DOMAIN 280 445 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 501 AA; 54599 MW; A3A3387EA4E346AE CRC64; MTSSSSPSQD PRDAQDVRDP QRFTESLRAD ALMEEDVAWS HEIDGDRDGD QFDRSERAAL RRVAGLSTEL EDVTEVEYRQ LRLERVVLVG VWTSGTVSDA ENSLAELAAL AETAGALVLD GVIQRRDKPD PATFIGSGKA RELRDIVLES GADTVVCDGE LSPGQLIALE DVVKVKVVDR TALILDIFAQ HAKSREGKAQ VALAQMQYML PRLRGWGQSL SRQMGGGGGG GMATRGPGET KIETDRRRIR EKMAKMRREI AEMKTGRDIK RQERRRNKVP SVAIAGYTNA GKSSLLNRLT GAGVLVENAL FATLDPTVRR AETPSGRIYT LADTVGFVRH LPHHLVEAFR STMEEVGDSD LILHIVDGSH PAPEEQLAAV REVIREVGAV NVPEIVVINK ADAADPLVLQ RLLRIERHSI AVSARTGQGI GELLALIDSE LPRPAVEVEA LVPYTRGGLV ARAHAEGEVI SEEHTPEGTL LKARVHQELA AELAPYVPAK Q // ID A0A0F4JL97_9ACTN Unreviewed; 502 AA. AC A0A0F4JL97; DT 24-JUN-2015, integrated into UniProtKB/TrEMBL. DT 24-JUN-2015, sequence version 1. DT 07-JUN-2017, entry version 15. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=VR45_16575 {ECO:0000313|EMBL:KJY34594.1}; OS Streptomyces sp. NRRL S-495. OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae; OC Streptomyces. OX NCBI_TaxID=1609133 {ECO:0000313|EMBL:KJY34594.1, ECO:0000313|Proteomes:UP000033484}; RN [1] {ECO:0000313|EMBL:KJY34594.1, ECO:0000313|Proteomes:UP000033484} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NRRL S-495 {ECO:0000313|EMBL:KJY34594.1, RC ECO:0000313|Proteomes:UP000033484}; RA Ju K.-S., Doroghazi J.R., Metcalf W.; RL Submitted (FEB-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KJY34594.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JZWY01000293; KJY34594.1; -; Genomic_DNA. DR RefSeq; WP_045940533.1; NZ_JZWY01000293.1. DR EnsemblBacteria; KJY34594; KJY34594; VR45_16575. DR PATRIC; fig|1609133.3.peg.5499; -. DR Proteomes; UP000033484; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000313|EMBL:KJY34594.1}; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000033484}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900, KW ECO:0000313|EMBL:KJY34594.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000033484}. FT DOMAIN 278 443 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 237 271 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 502 AA; 54467 MW; 8F6EF68708278B80 CRC64; MTSTFDTRDQ TDATRRIDGL RAEALMDEDL AAIDEDHGHH YDGDQYDRSE RAALRRVAGL STELEDVTEV EYRQLRLERV VLVGVWTDGT LEEAENSMAE LAALAETAGS EVLDGVIQRR DKPDAATYIG SGKAKDLRDI VAASGADTVV CDGELTPGQL IHLEDVVKVK VVDRTALILD IFAQHAKSRE GKAQVSLAQM QYMLPRLRGW GQSLSRQMGG GGSGSSGGGM ATRGPGETKI ETDRRRIREK MSKLRKEIAD MKKGRDTKRQ ERKRHQVPSV AIAGYTNAGK SSLLNRLTGA GVLVENSLFA TLDPTVRRAQ TPSGRVYTLA DTVGFVRHLP HHLVEAFRST MEEVADADLI LHVVDGSHPE PETQLAAVRE VVVSVDAQNV PEIVVINKAD AADPLVLQRL LRREPHAIVV SARTGVGIEE LLALIDDELP RPAVEVHALV PYTQGALVSR VHAEGELLGA EHTGEGTLLH AKVPAELAAE LEPFAVALTP QG // ID A0A0F4KCW3_9ACTN Unreviewed; 455 AA. AC A0A0F4KCW3; DT 24-JUN-2015, integrated into UniProtKB/TrEMBL. DT 24-JUN-2015, sequence version 1. DT 07-JUN-2017, entry version 11. DE SubName: Full=ATP-binding protein {ECO:0000313|EMBL:KJY44492.1}; DE Flags: Fragment; GN ORFNames=VR46_20185 {ECO:0000313|EMBL:KJY44492.1}; OS Streptomyces sp. NRRL S-444. OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae; OC Streptomyces. OX NCBI_TaxID=1609134 {ECO:0000313|EMBL:KJY44492.1, ECO:0000313|Proteomes:UP000033406}; RN [1] {ECO:0000313|EMBL:KJY44492.1, ECO:0000313|Proteomes:UP000033406} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NRRL S-444 {ECO:0000313|EMBL:KJY44492.1, RC ECO:0000313|Proteomes:UP000033406}; RA Ju K.-S., Doroghazi J.R., Metcalf W.; RL Submitted (FEB-2015) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KJY44492.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JZWX01000796; KJY44492.1; -; Genomic_DNA. DR EnsemblBacteria; KJY44492; KJY44492; VR46_20185. DR Proteomes; UP000033406; Unassembled WGS sequence. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 2. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000313|EMBL:KJY44492.1}; KW Complete proteome {ECO:0000313|Proteomes:UP000033406}; KW Nucleotide-binding {ECO:0000313|EMBL:KJY44492.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000033406}. FT DOMAIN 280 445 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT NON_TER 455 455 {ECO:0000313|EMBL:KJY44492.1}. SQ SEQUENCE 455 AA; 49636 MW; F9B8F3D2D0DD2B6B CRC64; MTSSSSPSQD ARDARDVPDS QSFTESLRAD ALMEEDVAWS HEVDGDRDGE QFERSERAAL RRVAGLSTEL EDVTEVEYRQ LRLERVVLVG VWTSGTVQDA ENSLAELAAL AETAGALVLD GVIQRRDKPD PATFIGSGKA RELRDIVLES GADTVVCDGE LSPGQLIALE DVVKVKVVDR TALILDIFAQ HAKSREGKAQ VALAQMQYML PRLRGWGASL SRQMGGGGGG GMATRGPGET KIETDRRRIR EKMAKMRREI ADMKTGRDIK RQERRRNKVP SVAIAGYTNA GKSSLLNRLT GAGVLVENAL FATLDPTVRR AETPSGRIYT LADTVGFVRH LPHHLVEAFR STMEEVGDSD LILHIVDGSH PAPEEQLAAV REVIRDVGAV NVPEIVVINK ADAADPLVLQ RLLRIERHSI AVSARTGQGI EELLGLIDSE LPRPEVEVEA LVPYT // ID A0A0F4KTB2_9LACO Unreviewed; 418 AA. AC A0A0F4KTB2; DT 24-JUN-2015, integrated into UniProtKB/TrEMBL. DT 24-JUN-2015, sequence version 1. DT 07-JUN-2017, entry version 12. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:KJY48421.1}; GN ORFNames=JG29_14820 {ECO:0000313|EMBL:KJY48421.1}; OS Lactobacillus mellis. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; OC Lactobacillus. OX NCBI_TaxID=1218508 {ECO:0000313|EMBL:KJY48421.1, ECO:0000313|Proteomes:UP000033695}; RN [1] {ECO:0000313|EMBL:KJY48421.1, ECO:0000313|Proteomes:UP000033695} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Hon2 {ECO:0000313|EMBL:KJY48421.1, RC ECO:0000313|Proteomes:UP000033695}; RA Ellegaard K.M., Tamarit D., Javelind E., Olofsson T., Andersson S.G., RA Vasquez A.; RT "Comparative genomics of the lactic acid bacteria isolated from the RT honey bee gut."; RL Submitted (DEC-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KJY48421.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JXBZ01000009; KJY48421.1; -; Genomic_DNA. DR EnsemblBacteria; KJY48421; KJY48421; JG29_14820. DR PATRIC; fig|1218508.4.peg.1473; -. DR Proteomes; UP000033695; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000033695}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000033695}. FT DOMAIN 196 365 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 155 189 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 418 AA; 47567 MW; C2092582BFA96E75 CRC64; MQITQNVIIA GVSHLQENFD YSMEELVHLA AADNLKVVTQ VRQHLDHINN QFYFGQGKVQ EIKHLAQYYN VQLVIVNDEL SPAQVRNLEK ATQLQFLDRT ELILQVFAQR AHSRQAQLQV AIAQLQYQLP RIHPSGNPLD QQRGHGGLAN RGAGESQLEL NRRTIRQQIN KLQQDLRHVR QTLNIQSNRR QNAHLPQVAL VGYTNAGKST TMNGLLSLAK ESADKQVLVK DQLFATLDTS IRKISLPQMP DFLISDTVGF ISKLPHNLIE AFRSTLAEAQ TADLLIQVVD ASSSQLPQML DTTQQALTAI GIHNKPMIYA YNKADRTTNF VKPEIIGNSI YYSALQTSSL KTLINLIYKH LFKQYHVIKV LIPFADKKLH HYIHQLTIQR QEYTFAGTIY QLFVSPQQAL KLQKYQLN // ID A0A0F4LR53_9LACO Unreviewed; 421 AA. AC A0A0F4LR53; DT 24-JUN-2015, integrated into UniProtKB/TrEMBL. DT 24-JUN-2015, sequence version 1. DT 07-JUN-2017, entry version 13. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:KJY60784.1}; GN ORFNames=JG30_14740 {ECO:0000313|EMBL:KJY60784.1}; OS Lactobacillus mellifer. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; OC Lactobacillus. OX NCBI_TaxID=1218492 {ECO:0000313|EMBL:KJY60784.1, ECO:0000313|Proteomes:UP000033558}; RN [1] {ECO:0000313|EMBL:KJY60784.1, ECO:0000313|Proteomes:UP000033558} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Bin4 {ECO:0000313|EMBL:KJY60784.1, RC ECO:0000313|Proteomes:UP000033558}; RA Ellegaard K.M., Tamarit D., Javelind E., Olofsson T., Andersson S.G., RA Vasquez A.; RT "Comparative genomics of the lactic acid bacteria isolated from the RT honey bee gut."; RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KJY60784.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JXJQ01000010; KJY60784.1; -; Genomic_DNA. DR RefSeq; WP_046317616.1; NZ_KQ034029.1. DR EnsemblBacteria; KJY60784; KJY60784; JG30_14740. DR PATRIC; fig|1218492.5.peg.1528; -. DR Proteomes; UP000033558; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000033558}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000033558}. FT DOMAIN 196 365 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 155 189 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 421 AA; 47779 MW; 237FA4FAC8DD9517 CRC64; MTDQIPVLIG GVDHLQTDFN YSMAELRSLA QAADFKVIQQ VHQRLPQVNN KTYFGPGKVQ QIQHLAATHA IQTVIVNDEL TPAQLRNLER STQLYFLDRT ELILQIFQKR AHSQQAQLQV AIAQLQYQLP RIHPSQNPLD QQRGGQGINN RGAGESQLEL KQRQLRQRIT QLQNKLQHTK QALTTQSERR QQQHLPQVAL VGYTNAGKST TFNQILAAVP HSKVSPVLVQ DQLFATLDTT IRRIDVPQLP TFLLSDTIGF ISQLPTTLIA AFRSTLQEAQ TADLLIQVID ATHPQKETMI ATTQQILTEL GIAQKPMIYA YNKADQLPAT AIPQISGPTI YYSAYQKKSI QALLHLIGQQ LFRNYRSLKL LIPFNEYQII SYLEHQVFIQ NRSYHATGIL YQVLVQPADL PRLRPFIIEK T // ID A0A0F4P9Z2_PSEO7 Unreviewed; 429 AA. AC A0A0F4P9Z2; DT 24-JUN-2015, integrated into UniProtKB/TrEMBL. DT 24-JUN-2015, sequence version 1. DT 30-AUG-2017, entry version 14. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=TW75_02620 {ECO:0000313|EMBL:KJY92230.1}; OS Pseudoalteromonas piscicida. OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales; OC Pseudoalteromonadaceae; Pseudoalteromonas. OX NCBI_TaxID=43662 {ECO:0000313|EMBL:KJY92230.1, ECO:0000313|Proteomes:UP000033511}; RN [1] {ECO:0000313|EMBL:KJY92230.1, ECO:0000313|Proteomes:UP000033511} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=S2040 {ECO:0000313|EMBL:KJY92230.1, RC ECO:0000313|Proteomes:UP000033511}; RX PubMed=25879706; DOI=10.1186/s12864-015-1365-z; RA Machado H., Sonnenschein E.C., Melchiorsen J., Gram L.; RT "Genome mining reveals unlocked bioactive potential of marine Gram- RT negative bacteria."; RL BMC Genomics 16:158-158(2015). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KJY92230.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JXXW01000005; KJY92230.1; -; Genomic_DNA. DR RefSeq; WP_017217034.1; NZ_JXXW01000005.1. DR EnsemblBacteria; KJY92230; KJY92230; TW75_02620. DR PATRIC; fig|43662.8.peg.550; -. DR Proteomes; UP000033511; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000033511}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000033511}. FT DOMAIN 198 365 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 429 AA; 48349 MW; 673748FD3D189573 CRC64; MFDRYEAGEQ AVLVHIEFPH EGDREDLREL EMLVSSAGVS SVAVVQGSRQ APHAKLFVGT GKAEEIAEIV NIHNADVIIF NHQLSPSQER NLERVCKCRV LDRTTLILDI FAQRARTHEG KLQVELAQLR HISTRLIRGW THLERQKGGI GLRGPGETQL ETDRRLLRER IKSIRKRLDK VAVVREQGRR ARSRNEIPTV SLVGYTNAGK STLFNKITDA DVYAADQLFA TLDPTLRKIE IDDVGPVILA DTVGFIRHLP HDLVAAFKAT LTETREADLQ LHVIDVADPR RKENIEQVQL VLEEIEANDI PQLLVYNKID LMDEVAPRID RDDEGKPIRV WLSAHSGEGI PLLFDAVKEL LAKTVFTAEL AVPPALGRLR GALFELNAVD EKGYDEQGNW LVSVRMPKIE WEKLNKEFGR NLNDLVVGS // ID A0A0F4Q289_9GAMM Unreviewed; 427 AA. AC A0A0F4Q289; DT 24-JUN-2015, integrated into UniProtKB/TrEMBL. DT 24-JUN-2015, sequence version 1. DT 30-AUG-2017, entry version 15. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=TW72_02195 {ECO:0000313|EMBL:KJZ01778.1}; OS Pseudoalteromonas ruthenica. OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales; OC Pseudoalteromonadaceae; Pseudoalteromonas. OX NCBI_TaxID=151081 {ECO:0000313|EMBL:KJZ01778.1, ECO:0000313|Proteomes:UP000033664}; RN [1] {ECO:0000313|EMBL:KJZ01778.1, ECO:0000313|Proteomes:UP000033664} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=S3137 {ECO:0000313|EMBL:KJZ01778.1, RC ECO:0000313|Proteomes:UP000033664}; RX PubMed=25879706; DOI=10.1186/s12864-015-1365-z; RA Machado H., Sonnenschein E.C., Melchiorsen J., Gram L.; RT "Genome mining reveals unlocked bioactive potential of marine Gram- RT negative bacteria."; RL BMC Genomics 16:158-158(2015). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KJZ01778.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JXXZ01000002; KJZ01778.1; -; Genomic_DNA. DR RefSeq; WP_022945615.1; NZ_JXXZ01000002.1. DR EnsemblBacteria; KJZ01778; KJZ01778; TW72_02195. DR PATRIC; fig|151081.8.peg.1616; -. DR Proteomes; UP000033664; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000033664}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000033664}. FT DOMAIN 198 365 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 427 AA; 48294 MW; A7A2FFB96FD35FE6 CRC64; MFDRYEAGEQ AVLVHIEFPH EGDREDLHEL EMLVSSAGVS SLAVVQGSRQ APHPKLFVGT GKAEEIAEIV KSHNADVIIF NHELSPSQER NLEKLCQCRV LDRTALILDI FAQRARTHEG KLQVELAQLR HISTRLIRGW THLERQKGGI GLRGPGETQL ETDRRLLRGR IKSILKRLDK VAKQREQGRR ARNRNEIPSV SLVGYTNAGK STLFNRITES EVYAADQLFA TLDPTLRKLE VPDIGSVILA DTVGFIRHLP HDLVAAFKAT LTETREADLQ LHVIDAADSR RKENIEQVQE VLEEIEANEI PQLLIYNKID QLEDVEARID RDDEGKPMRV WLSAQQGQGM ELLKQAISEL LAKQMLNADL RVPPSQGRLR GALYNLNSIS SEDFDEQGNW LLSVNVPMSE WNKLKKEIGE QIDGYLT // ID A0A0F4QRG6_9GAMM Unreviewed; 444 AA. AC A0A0F4QRG6; DT 24-JUN-2015, integrated into UniProtKB/TrEMBL. DT 24-JUN-2015, sequence version 1. DT 30-AUG-2017, entry version 14. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=TW85_20680 {ECO:0000313|EMBL:KJZ09929.1}; OS Marinomonas sp. S3726. OC Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales; OC Marinomonas. OX NCBI_TaxID=579484 {ECO:0000313|EMBL:KJZ09929.1, ECO:0000313|Proteomes:UP000033747}; RN [1] {ECO:0000313|EMBL:KJZ09929.1, ECO:0000313|Proteomes:UP000033747} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=S3726 {ECO:0000313|EMBL:KJZ09929.1, RC ECO:0000313|Proteomes:UP000033747}; RX PubMed=25879706; DOI=10.1186/s12864-015-1365-z; RA Machado H., Sonnenschein E.C., Melchiorsen J., Gram L.; RT "Genome mining reveals unlocked bioactive potential of marine Gram- RT negative bacteria."; RL BMC Genomics 16:158-158(2015). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KJZ09929.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JXYC01000031; KJZ09929.1; -; Genomic_DNA. DR RefSeq; WP_046019052.1; NZ_JXYC01000031.1. DR EnsemblBacteria; KJZ09929; KJZ09929; TW85_20680. DR PATRIC; fig|579484.3.peg.4243; -. DR Proteomes; UP000033747; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000033747}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000033747}. FT DOMAIN 200 367 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 159 186 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 444 AA; 49313 MW; 71B0F0FBA2E2784B CRC64; MFFERPESGD VSVLVHIEFH NGETQYGPEE FVELATSAGI APVAVVTGTR QKPDPKYFIG KGKLDEVREI VEREEAQVVL FDHALSPSQE RNLEESLQCR VLDRTGLILD IFAQRARTHE GKLQVELAQL QHMATRLVRG WTHLERQKGG IGVRGGPGET QLESDRRQLR ERITSIQKRL DKVSSQRDQN RRARDRSAVP TVSLVGYTNA GKSTLFNFIT GAEVFAADQL FATLDPTLRR LDLAQVGAVV LADTVGFIRQ LPHKLIKAFQ ATLKESSEAD LLLHVVDASD VNRDENVGHV NAVLKEIDAD EIPTLLIFNK IDALSNVEPR IDRNEDGLPY RVWLSAKDGT GIDLLRQAIA EVLAIDVIRE TLVLPASAGR LRAMLFEQGA VLSETYDDAG SSVLKICIPK DDYLTILANA GVKPESGLSA FMQDRQELDP WLLD // ID A0A0F4QX27_9GAMM Unreviewed; 429 AA. AC A0A0F4QX27; DT 24-JUN-2015, integrated into UniProtKB/TrEMBL. DT 24-JUN-2015, sequence version 1. DT 30-AUG-2017, entry version 14. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=TW77_04080 {ECO:0000313|EMBL:KJZ12238.1}; OS Pseudoalteromonas rubra. OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales; OC Pseudoalteromonadaceae; Pseudoalteromonas. OX NCBI_TaxID=43658 {ECO:0000313|EMBL:KJZ12238.1, ECO:0000313|Proteomes:UP000033452}; RN [1] {ECO:0000313|EMBL:KJZ12238.1, ECO:0000313|Proteomes:UP000033452} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=S2471 {ECO:0000313|EMBL:KJZ12238.1, RC ECO:0000313|Proteomes:UP000033452}; RX PubMed=25879706; DOI=10.1186/s12864-015-1365-z; RA Machado H., Sonnenschein E.C., Melchiorsen J., Gram L.; RT "Genome mining reveals unlocked bioactive potential of marine Gram- RT negative bacteria."; RL BMC Genomics 16:158-158(2015). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KJZ12238.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JXYA01000006; KJZ12238.1; -; Genomic_DNA. DR RefSeq; WP_046003673.1; NZ_JXYA01000006.1. DR EnsemblBacteria; KJZ12238; KJZ12238; TW77_04080. DR PATRIC; fig|43658.5.peg.854; -. DR Proteomes; UP000033452; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000033452}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000033452}. FT DOMAIN 198 365 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 429 AA; 48573 MW; 1C2829CA5CFC8A29 CRC64; MFDRYEAGEQ AVLVHIEFPN EGDREDLREL EMLVSSAGVS CLTVVQGSRQ APHPKLFVGT GKAEEIAEIV RTHNADVIIF NHQLSPSQER NLERVCRCRV LDRTTLILDI FAQRARTHEG KLQVELAQLR HISTRLIRGW THLERQKGGI GLRGPGETQL ETDRRLLRER IKSIRKRLEK VATVREQGRR ARSRNEIPTV SLVGYTNAGK STLFNHVTNA DVYAADQLFA TLDPTLRKLE ITDVGPVIFA DTVGFIRHLP HDLVAAFKAT LTETREADLQ LHVVDVADQR RKENIEEVQS VLKEIEADEI PQLLVYNKID LVDEINPKID RDDQGVPVRV WLSAHTGEGI ELLEQAISEL LAKKIFASKL LVPPAFGKLR GALFNLNAVN GESYDEAGNW LLDVRLPQAD WERLKKEQGQ EIEQFVVED // ID A0A0F4QYH3_9GAMM Unreviewed; 438 AA. AC A0A0F4QYH3; DT 24-JUN-2015, integrated into UniProtKB/TrEMBL. DT 24-JUN-2015, sequence version 1. DT 30-AUG-2017, entry version 14. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=TW86_11680 {ECO:0000313|EMBL:KJZ12753.1}; OS Halomonas sp. S2151. OC Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales; OC Halomonadaceae; Halomonas. OX NCBI_TaxID=579478 {ECO:0000313|EMBL:KJZ12753.1, ECO:0000313|Proteomes:UP000033642}; RN [1] {ECO:0000313|EMBL:KJZ12753.1, ECO:0000313|Proteomes:UP000033642} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=S2151 {ECO:0000313|EMBL:KJZ12753.1, RC ECO:0000313|Proteomes:UP000033642}; RX PubMed=25879706; DOI=10.1186/s12864-015-1365-z; RA Machado H., Sonnenschein E.C., Melchiorsen J., Gram L.; RT "Genome mining reveals unlocked bioactive potential of marine Gram- RT negative bacteria."; RL BMC Genomics 16:158-158(2015). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KJZ12753.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JXYB01000049; KJZ12753.1; -; Genomic_DNA. DR RefSeq; WP_045993096.1; NZ_JXYB01000049.1. DR EnsemblBacteria; KJZ12753; KJZ12753; TW86_11680. DR PATRIC; fig|579478.3.peg.2446; -. DR Proteomes; UP000033642; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000033642}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000033642}. FT DOMAIN 199 365 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 438 AA; 49137 MW; 5905EE4D7CFF6F1C CRC64; MFFERPDAGE TAVLVHIDFQ DEKEREDPGE FHELVRSAGA EPATLVTGSR QRPDPRSFVG SGKLEEIGEA LAVHKAELVI FNHALSPSQE RNVEQTLKCR VLDRTGLILD IFAQRARTHE GKLQVELAQL EYMSTRLVRG WTHLERQKGG IGLRGPGETQ LETDRRLLRA RIKSIHKRLD KVRSQRSQNR RARSRAEIPS VSLVGYTNAG KSTLFNSLTA SEVYAADQLF ATLDPTLRRL EVEDVGPVVL ADTVGFIRHL PHKLVEAFRA TLQEAAEASL LVHVIDSADP DRELNVTQVE AVLDEIGALD VPTLKVMNKI DLFDSSPRIE RDEHGVPQTV WLSAQKGLGL DLLTQALTER LAEDIIDFSL TLTPEQGKLR AALHELNAVR DESFDEDGQT QLDVRLPRRD FNQLMARLGE RAADYLPVAL QERDVWEA // ID A0A0F4RJK1_9RHOB Unreviewed; 424 AA. AC A0A0F4RJK1; DT 24-JUN-2015, integrated into UniProtKB/TrEMBL. DT 24-JUN-2015, sequence version 1. DT 05-JUL-2017, entry version 14. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=TW80_04655 {ECO:0000313|EMBL:KJZ20131.1}; OS Loktanella sp. S4079. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae; Loktanella. OX NCBI_TaxID=579483 {ECO:0000313|EMBL:KJZ20131.1, ECO:0000313|Proteomes:UP000033741}; RN [1] {ECO:0000313|EMBL:KJZ20131.1, ECO:0000313|Proteomes:UP000033741} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=S4079 {ECO:0000313|EMBL:KJZ20131.1, RC ECO:0000313|Proteomes:UP000033741}; RX PubMed=25879706; DOI=10.1186/s12864-015-1365-z; RA Machado H., Sonnenschein E.C., Melchiorsen J., Gram L.; RT "Genome mining reveals unlocked bioactive potential of marine Gram- RT negative bacteria."; RL BMC Genomics 16:158-158(2015). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KJZ20131.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JXYE01000002; KJZ20131.1; -; Genomic_DNA. DR EnsemblBacteria; KJZ20131; KJZ20131; TW80_04655. DR PATRIC; fig|579483.3.peg.951; -. DR Proteomes; UP000033741; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000033741}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000033741}. FT DOMAIN 204 373 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 424 AA; 47060 MW; 1DEA4ECCA4FA583D CRC64; MQTHDRPVTR AWVLHPDLKT DHQRRAAGSA LEEAVSLAAA LPDLEVVGSN TVRLPKIHPG KLFGTGKIEE LKAVFKENDV ALVLIDGPVT PVQQRNLEKE WGVKLLDRTG LILEIFSDRA RTSEGVLQVE MAALSYQRTR LVRAWTHLER QRGGLGFVGG PGETQIEADR RAIDEQLGRL RRQLAKVVKT RELHRASRAK VPFPIVALVG YTNAGKSTLF NRLTGAEVFA KDMLFATLDP TMRKIVLPTG DEVILSDTVG FISDLPTELV AAFRATLEEV LDADLIVHVR DISHEQTEEQ AQDVMAILQS LGVAEEAPLI EVWNKIDQLS DEDHDAMITQ AGRTDDLFAV SAVTGEGMEP LLAAIPNKLK DPRSEAQVTL SFAEGRRRAW LFDAGIVTQE VQTDTGYTIS VFWTELQKER FSRL // ID A0A0F5ASL0_9GAMM Unreviewed; 430 AA. AC A0A0F5ASL0; DT 24-JUN-2015, integrated into UniProtKB/TrEMBL. DT 24-JUN-2015, sequence version 1. DT 30-AUG-2017, entry version 14. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=WN56_07175 {ECO:0000313|EMBL:KKA45183.1}; OS Salinivibrio sp. KP-1. OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; OC Vibrionaceae; Salinivibrio. OX NCBI_TaxID=1406902 {ECO:0000313|EMBL:KKA45183.1, ECO:0000313|Proteomes:UP000033449}; RN [1] {ECO:0000313|EMBL:KKA45183.1, ECO:0000313|Proteomes:UP000033449} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=KP-1 {ECO:0000313|EMBL:KKA45183.1, RC ECO:0000313|Proteomes:UP000033449}; RA Kaur G., Kumar A., Mathan Kumar R., Kumar N., Singh N.K., Arora A., RA Kaur N., Bala M., Mayilraj S.; RT "Taxonomic description and genome sequence of Salinivibrio halophilus RT sp. nov., a novel halotolerant gammaproteobacterium isolated from RT marine sediment and emended description of the genus Salinivibrio."; RL Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KKA45183.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LAQR01000003; KKA45183.1; -; Genomic_DNA. DR RefSeq; WP_046074380.1; NZ_LAQR01000003.1. DR EnsemblBacteria; KKA45183; KKA45183; WN56_07175. DR PATRIC; fig|1406902.3.peg.1476; -. DR Proteomes; UP000033449; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000033449}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000033449}. FT DOMAIN 198 365 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 430 AA; 48306 MW; 0FED2CF73C4F6972 CRC64; MFDRYEAGEQ AVLVHINFTH DGEWDDLSEF QMLVSSSGVD ALQVVVGSRQ SPHPKYFVGE GKAQEIADTV QQVGADIVIF NHTLSAAQER NLEQRFKCRV LDRTGLILDI FAQRARTHEG KLQVELAQLR HLSTRLVRGW THLERQKGGI GLRGPGETQL ETDRRLVRDR VKAILKRLDK VAKQREQGRR ARARAEVPTV SLVGYTNAGK STLFNRITEA GVYSADQLFA TLDPTLRRIE VDDVGTAILA DTVGFIRHLP HDLVAAFKAT LQETQEASLL LHVVDASDER FGDNIEAVNS VLDEIDAADV PHLIIMNKID SLDQAEPRIE RDEEGVPKAV WVSALSGQGI ALIFEALTER LSGTMVRHQL RLPPSMAGRM QSKFHQMRCV ISEEYQDDGH LLVDVRLPQT DWYRLEKREG NQLGDFIVSD // ID A0A0F5EZR0_AVIPA Unreviewed; 437 AA. AC A0A0F5EZR0; DT 24-JUN-2015, integrated into UniProtKB/TrEMBL. DT 24-JUN-2015, sequence version 1. DT 30-AUG-2017, entry version 14. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=Z012_02905 {ECO:0000313|EMBL:KKB02104.1}; OS Avibacterium paragallinarum (Haemophilus gallinarum). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Avibacterium. OX NCBI_TaxID=728 {ECO:0000313|EMBL:KKB02104.1, ECO:0000313|Proteomes:UP000033614}; RN [1] {ECO:0000313|EMBL:KKB02104.1, ECO:0000313|Proteomes:UP000033614} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CL {ECO:0000313|EMBL:KKB02104.1, RC ECO:0000313|Proteomes:UP000033614}; RA Horta-Valerdi G., Sanchez-Alonso P., Negrete-Abascal E., Perez V., RA Olmedo G., Hernandez I., Gomez Z., Vazquez-Cruz C.; RT "Sequence of Avibacterium paragallinarum strain CL genome contains RT many ISs."; RL Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KKB02104.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LAEN01000014; KKB02104.1; -; Genomic_DNA. DR RefSeq; WP_046097904.1; NZ_LAEN01000014.1. DR EnsemblBacteria; KKB02104; KKB02104; Z012_02905. DR PATRIC; fig|728.38.peg.452; -. DR Proteomes; UP000033614; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000033614}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000033614}. FT DOMAIN 209 376 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 175 205 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 437 AA; 49360 MW; 0DC6C4CE6863E56D CRC64; MSTALFLSSE TPSTADPVRD RGIIVQAFFS AEKNLDDLNE FQLLAKSAQV EIAATITTSR ATPQAKYFIG QGKAEEIAQA VQTYNANVIL VNHCLTPAQT RNLEALCECR VVDRTGLILD IFAQRARSHE GKLQVELAQL KHLSTRLIRR KTGLDQQKGT VGLRGPGETQ LESDRRLIKV RIAQLQNRLN KVEKQRNQNR QTRKKADIPT LSLVGYTNAG KSTLFNVLTN AEVYAADQLF ATLDPTLRRL TIQDIGATIL ADTVGFIREL PHDLVSAFKS TLQETTEASL LLHVVDCTDA RKLDNIQAVN EVLQEIQADS VPTLLVYNKI DQVENLAPHI EYDEQNRPIA VYISAHQQQG IELLTDAIRQ RLSKNMLHLH LTLPPQEGQI RHWLYEMGCI RQEQISEQGE FLLEINLEQS EWKKLLKKRS HLIHYQT // ID A0A0F5FIY3_9RHIZ Unreviewed; 453 AA. AC A0A0F5FIY3; DT 24-JUN-2015, integrated into UniProtKB/TrEMBL. DT 24-JUN-2015, sequence version 1. DT 07-JUN-2017, entry version 14. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=VE25_18550 {ECO:0000313|EMBL:KKB08515.1}; OS Devosia geojensis. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Hyphomicrobiaceae; Devosia. OX NCBI_TaxID=443610 {ECO:0000313|EMBL:KKB08515.1, ECO:0000313|Proteomes:UP000033632}; RN [1] {ECO:0000313|EMBL:KKB08515.1, ECO:0000313|Proteomes:UP000033632} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BD-c194 {ECO:0000313|EMBL:KKB08515.1, RC ECO:0000313|Proteomes:UP000033632}; RA Hassan Y.I., Lepp D., Li X.-Z., Zhou T.; RL Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KKB08515.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JZEX01000157; KKB08515.1; -; Genomic_DNA. DR RefSeq; WP_046110147.1; NZ_JZEX01000157.1. DR EnsemblBacteria; KKB08515; KKB08515; VE25_18550. DR PATRIC; fig|443610.3.peg.2017; -. DR Proteomes; UP000033632; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000033632}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000033632}. FT DOMAIN 219 393 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 453 AA; 49737 MW; 72545277B0193DA2 CRC64; MGDFSEDADR SAGPQAFIDR QEKPVRAGVV CPDVRGSGYQ RTAESRLAEF EGLAEAIRLE VVFSEIVRVR EVRPATFIGG GQVETLGQRV EAEGIELLLF DASLSPIQQR NLERETGAKV LDRTALILEI FGERAATREG VLQVELAHLN YQKSRLVRSW THLERQRGGF GFLGGPGETQ IESDRRLLQE RISLIEERLD KVKRTRAVQR RRRNVVSFPI VALVGYTNAG KSSLFNILTG AGVFAEDLLF ATLDTTVRKI ELPHGREVML SDTVGFVSEL PTDLVAAFRA TLEEVVEADV VLHVRDVSNP DHAAQANDVL GVLADLGVTA ETTPIIEVWN KIDLLAGEEG RETALAGVTP ASKVSAAVPV SARTGEGLDT LRLAVEAALA DRSGTYRVHV PHSAGGDIGW LHSNTEVLSR EEPDERGSSF VVRVEPRHLT MFLERFNGRL ERV // ID A0A0F5FNB1_9RHIZ Unreviewed; 437 AA. AC A0A0F5FNB1; DT 24-JUN-2015, integrated into UniProtKB/TrEMBL. DT 24-JUN-2015, sequence version 1. DT 05-JUL-2017, entry version 14. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=VE26_06365 {ECO:0000313|EMBL:KKB10318.1}; OS Devosia chinhatensis. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Hyphomicrobiaceae; Devosia. OX NCBI_TaxID=429727 {ECO:0000313|EMBL:KKB10318.1, ECO:0000313|Proteomes:UP000033649}; RN [1] {ECO:0000313|EMBL:KKB10318.1, ECO:0000313|Proteomes:UP000033649} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=IPL18 {ECO:0000313|EMBL:KKB10318.1, RC ECO:0000313|Proteomes:UP000033649}; RA Hassan Y., Lepp D., Li X.-Z., Zhou T.; RL Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KKB10318.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JZEY01000054; KKB10318.1; -; Genomic_DNA. DR EnsemblBacteria; KKB10318; KKB10318; VE26_06365. DR PATRIC; fig|429727.3.peg.1316; -. DR Proteomes; UP000033649; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000033649}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000033649}. FT DOMAIN 204 375 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 170 197 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 437 AA; 48093 MW; 4749F1D317AF78EB CRC64; MDRQEKPTRT GLVCPDVRGK LSSHDIDARQ AEFEGLAGAI RLDIAFSEVV KVREIRPATY MGAGHVEALA ERVKAEHIEL LLVDAALSPI QQRNLERETG TKVLDRTALI LEIFGERAAT REGVLQVELA HLNYQKGRLV RSWTHLERQR GSGGMGFMGG PGETQIESDR RQISDRIALL EARLDKVKKT RAQQRSQRTR AQIPVVALVG YTNAGKSSLF NRLTGAGVFA EDLLFATLDT TVRKIELPHG REVMLSDTVG FVADLPHDLV AAFRATLEEV TDADIILHVR DIANPDHAAQ AQDVLTVLEE LGVSSEVTPI IEVWNKIDLL DEPGLVLAAA TPVGKVLATL PLSAHTGQGV DQLLLQIETS LGEQSRTYHV HVPHTAGSDI GWLHNHAEVI SRDEPTEKGS DFVVRVDPRH RSAFLERFNG RIATSEI // ID A0A0F5IA92_9BACI Unreviewed; 420 AA. AC A0A0F5IA92; DT 24-JUN-2015, integrated into UniProtKB/TrEMBL. DT 24-JUN-2015, sequence version 1. DT 07-JUN-2017, entry version 15. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=QY95_00305 {ECO:0000313|EMBL:KKB42456.1}; OS Bacillaceae bacterium MTCC 8252. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; OC unclassified Bacillaceae. OX NCBI_TaxID=1123719 {ECO:0000313|EMBL:KKB42456.1, ECO:0000313|Proteomes:UP000031563}; RN [1] {ECO:0000313|EMBL:KKB42456.1, ECO:0000313|Proteomes:UP000031563} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MTCC 8252 {ECO:0000313|EMBL:KKB42456.1, RC ECO:0000313|Proteomes:UP000031563}; RA Verma A., Khatri I., Mual P., Subramanian S., Krishnamurthi S.; RT "Genome Assembly of Bacillaceae bacterium MTCC 8252."; RL Submitted (FEB-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KKB42456.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JWIR02000012; KKB42456.1; -; Genomic_DNA. DR RefSeq; WP_039232507.1; NZ_JWIR02000012.1. DR EnsemblBacteria; KKB42456; KKB42456; QY95_00305. DR Proteomes; UP000031563; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000031563}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000031563}. FT DOMAIN 200 362 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 420 AA; 48174 MW; BA52D994D7D4B9D0 CRC64; MDNHQREKEY AILAGCQLTD DSEQFAYSME ELRSLTETAQ GEVKAVITQK RERIDSSTYI GKGKLEELKR LEEEIEPDLI IFNDELSPSQ IRNLSTELNA RVIDRTQLIL DIFAQRARSR EGQLQVELAQ LEYLLPRLAG QGTALSRLGG GIGTRGPGET KLESDRRHIR RRIDDIKRQL QTIVHHRERY RSRRKKNKAF QIALVGYTNA GKSTLFNRLT TAESLEENQL FATLDPLTRK VVLPSGYQAI LTDTVGFIQD LPTTLVAAFR STLEEVREAD LLLHVVDSSN PDFNQHQETV NELLKQLEMD HLPELTVYNK KDQRHDEFVP SSRSEHLLIS AFLEEDRLEL KSAIEKMMKE QMAPYRGRIP ASEGRLLTQL KTETIVESAV FDEEDETYFV KGFAFSDHPI AGDIRKYTEE // ID A0A0F5L7I0_9RHIZ Unreviewed; 428 AA. AC A0A0F5L7I0; DT 24-JUN-2015, integrated into UniProtKB/TrEMBL. DT 24-JUN-2015, sequence version 1. DT 07-JUN-2017, entry version 13. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=VW35_13555 {ECO:0000313|EMBL:KKB78159.1}; OS Devosia soli. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Hyphomicrobiaceae; Devosia. OX NCBI_TaxID=361041 {ECO:0000313|EMBL:KKB78159.1, ECO:0000313|Proteomes:UP000033514}; RN [1] {ECO:0000313|EMBL:KKB78159.1, ECO:0000313|Proteomes:UP000033514} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=GH2-10 {ECO:0000313|EMBL:KKB78159.1, RC ECO:0000313|Proteomes:UP000033514}; RA Hassan Y.I., Lepp D., Zhou T.; RL Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KKB78159.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LAJG01000023; KKB78159.1; -; Genomic_DNA. DR EnsemblBacteria; KKB78159; KKB78159; VW35_13555. DR PATRIC; fig|361041.3.peg.2098; -. DR Proteomes; UP000033514; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000033514}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000033514}. FT DOMAIN 195 366 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 161 188 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 428 AA; 46973 MW; CADDC12DE1C8FDA5 CRC64; MGLICPDVRG KSSYHSIEAR QAEFEGLAEA IRLDVRFSDV VKVREIRPAT YIGGGQVEAI AEKVKAEEIE LLLVDTALSP IQQRNLERET GTKVLDRTAL ILEIFGERAA TREGVLQVEL AHLNYQKGRL VRSWTHLERQ RGSGGMGFMG GPGETQIESD RRQITDRIVL LEERLDKVKK TRAQQRAQRT RAAIPVVALV GYTNAGKSSL FNRLTGAGVF AEDLLFATLD TTVRKIELPH GREVMLSDTV GFVADLPHDL VAAFRATLEE VVDADIILHV RDIANPDNAA QAQDVLEVLD ELGVSSETTP VIEVWNKVDL LGEPGFALAG ASPAGKVLAT MPVSAHTGQG VEELRALIEK SLGEQSRTYH VHVPHSAGAD IGWLHSNAEV ISRDEPTEKG QDYVVRVDPR HKSAFLERFN GRIALSDL // ID A0A0F5LMJ4_9RHIZ Unreviewed; 459 AA. AC A0A0F5LMJ4; DT 24-JUN-2015, integrated into UniProtKB/TrEMBL. DT 24-JUN-2015, sequence version 1. DT 07-JUN-2017, entry version 14. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=SAMN02745223_02838 {ECO:0000313|EMBL:SHF50380.1}, GN VW29_15170 {ECO:0000313|EMBL:KKB82887.1}; OS Devosia limi DSM 17137. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Hyphomicrobiaceae; Devosia. OX NCBI_TaxID=1121477 {ECO:0000313|EMBL:KKB82887.1, ECO:0000313|Proteomes:UP000033608}; RN [1] {ECO:0000313|EMBL:KKB82887.1, ECO:0000313|Proteomes:UP000033608} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 17137 {ECO:0000313|EMBL:KKB82887.1, RC ECO:0000313|Proteomes:UP000033608}; RA Hassan Y.I., Lepp D., Zhou T.; RL Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:SHF50380.1, ECO:0000313|Proteomes:UP000184533} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 17137 {ECO:0000313|EMBL:SHF50380.1, RC ECO:0000313|Proteomes:UP000184533}; RA Jaros S., Januszkiewicz K., Wedrychowicz H.; RL Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LAJF01000091; KKB82887.1; -; Genomic_DNA. DR EMBL; FQVC01000008; SHF50380.1; -; Genomic_DNA. DR RefSeq; WP_046136100.1; NZ_LAJF01000091.1. DR EnsemblBacteria; KKB82887; KKB82887; VW29_15170. DR PATRIC; fig|1121477.3.peg.4206; -. DR Proteomes; UP000033608; Unassembled WGS sequence. DR Proteomes; UP000184533; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000033608}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000033608}. FT DOMAIN 222 397 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 188 215 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 459 AA; 50077 MW; 5BF03D01BEECB6A2 CRC64; MSDHEGDEAG HKGGPKAFID RRQLATRVGL VCPDVRGSFS QHSIEARKSE FEGLAGAIEL DIVFSEVFKV REVKPATFIG GGHVETLAQR VKDEDIDLLI IDAALTAIQQ RNLEKETGAK VLDRTALILE IFGERAATRE GVLQVELAHL NYQKGRLVRS WTHLERQRGS GGYGFMGGPG ETQIESDRRQ ITDRIVLLEE RLEKVKKTRA QQRRQRDDTP FPIVALVGYT NAGKSSLFNT LTGAGVFAED LLFATLDTTV RKLELPHGRE VMLSDTVGFV ADLPTDLVAA FRATLEEVVD ADVVLHVRDI SNPDHLAQAQ DVLKVLGDLG VSSETTPVIE VWNKIDLLTA GSEDGEDVLA SVTPAGRVAA VIRASAKTGD GLAALKLAIE AALSEKSRTY HVHVPHSAGS DIGWLHSHAE IISRDEPTEQ GSGFVVRVDP RHKTAFLERF NGRIESSDA // ID A0A0F5P9L8_9SPHN Unreviewed; 438 AA. AC A0A0F5P9L8; DT 24-JUN-2015, integrated into UniProtKB/TrEMBL. DT 24-JUN-2015, sequence version 1. DT 07-JUN-2017, entry version 13. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=WP12_15725 {ECO:0000313|EMBL:KKC25128.1}; OS Sphingomonas sp. SRS2. OC Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales; OC Sphingomonadaceae; Sphingomonas. OX NCBI_TaxID=133190 {ECO:0000313|EMBL:KKC25128.1, ECO:0000313|Proteomes:UP000033680}; RN [1] {ECO:0000313|EMBL:KKC25128.1, ECO:0000313|Proteomes:UP000033680} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SRS2 {ECO:0000313|EMBL:KKC25128.1, RC ECO:0000313|Proteomes:UP000033680}; RA Nielsen T.K., Sorensen S.R., Hansen L.H.; RT "Draft genome sequence of isoproturon-mineralizing Sphingomonas sp. RT SRS2, isolated from an agricultural field in the United Kingdom."; RL Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KKC25128.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LARW01000104; KKC25128.1; -; Genomic_DNA. DR RefSeq; WP_046194631.1; NZ_LARW01000104.1. DR EnsemblBacteria; KKC25128; KKC25128; WP12_15725. DR PATRIC; fig|133190.4.peg.162; -. DR Proteomes; UP000033680; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000033680}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000033680}. FT DOMAIN 209 387 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 175 202 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 438 AA; 47465 MW; 80DE0C608818B68E CRC64; MSVFNRDEDD GLSRGARALV ALPERAGDSQ RSAEARLDEA AGLAAAIGVD VVEKLAFKLR DPKPATLFGS GQVDQIATAA RMGEAELIIV DAALTPIQQR NLEKATEAKV IDRTGLILEI FGERAATAEG RLQVELAHLD YQAGRLVRSW THLERQRGGF GFLGGPGETQ IEADRRLIRD RMAKLRRELE QVRRTRGLHR ARRQRAPWPV IALVGYTNAG KSTLFNRMTG AKVMAEDLLF ATLDPTMRQI GLPGIDKAIL SDTVGFVSDL PTQLVAAFRA TLEEVTGADI ILHVRDIAHP DSDAQAADVL GVLGEIGVGP RAPEGEAGEG APIIEVWNKI DMLDPETRDA TDAEAGRRED VVTLSALTGD GVDTLRRVVS ERLSTGNRVR TLAVSTSDGA AMAWLHANGE VIGQEVEGER MVVEVRLSDK DLARFEAR // ID A0A0F5Q1Y8_9RHIZ Unreviewed; 433 AA. AC A0A0F5Q1Y8; DT 24-JUN-2015, integrated into UniProtKB/TrEMBL. DT 24-JUN-2015, sequence version 1. DT 05-JUL-2017, entry version 14. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=WH91_00635 {ECO:0000313|EMBL:KKC34890.1}; OS Devosia psychrophila. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Hyphomicrobiaceae; Devosia. OX NCBI_TaxID=728005 {ECO:0000313|EMBL:KKC34890.1, ECO:0000313|Proteomes:UP000033519}; RN [1] {ECO:0000313|EMBL:KKC34890.1, ECO:0000313|Proteomes:UP000033519} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Cr7-05 {ECO:0000313|EMBL:KKC34890.1, RC ECO:0000313|Proteomes:UP000033519}; RA Lepp D., Hassan Y.I., Li X.-Z., Zhou T.; RL Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KKC34890.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LAPV01000009; KKC34890.1; -; Genomic_DNA. DR EnsemblBacteria; KKC34890; KKC34890; WH91_00635. DR PATRIC; fig|728005.3.peg.4175; -. DR Proteomes; UP000033519; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000033519}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000033519}. FT DOMAIN 202 371 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 170 197 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 433 AA; 47310 MW; 61E7782E15830864 CRC64; MDRRSQQTRA GLVVPDVRGH TSQHSIEARK AEFEGLAHAI HLDVAFSEII KVREVKPATF IGGGHTENLA ARVKAEDIDI LLIDVSLTAI QQRNLEKETG AKVLDRTALI LEIFGERAAT REGVLQVELA HLNYQKGRLV RSWTHLERQR GSGGYGFMGG PGETQIESDR RQITDRIVLL EDRLEKVKKT RAQQRQQRSD TPIVALVGYT NAGKSSLFNT LTGAGVFAED LLFATLDTTV RKLELPHGRE VVLSDTVGFV ADLPTDLVAA FRATLEEVLD ADVILHARDI ANEDHAAQAQ DVLKVLGDLG VSAETTSIIE VWNKVDLVNE ADLVGIAPAS KVAGVVHASA KTGQGLEDLK LAIEKALGEK SRTYHVNVPH TAGADIGWLH SHSEIVSRDE PTEQGSGFTV RVEPRHKAAF LERFNGRIKS SDA // ID A0A0F5QH07_9RHIZ Unreviewed; 458 AA. AC A0A0F5QH07; DT 24-JUN-2015, integrated into UniProtKB/TrEMBL. DT 24-JUN-2015, sequence version 1. DT 07-JUN-2017, entry version 13. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=WH87_03520 {ECO:0000313|EMBL:KKC39304.1}; OS Devosia epidermidihirudinis. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Hyphomicrobiaceae; Devosia. OX NCBI_TaxID=1293439 {ECO:0000313|EMBL:KKC39304.1, ECO:0000313|Proteomes:UP000033411}; RN [1] {ECO:0000313|EMBL:KKC39304.1, ECO:0000313|Proteomes:UP000033411} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=E84 {ECO:0000313|EMBL:KKC39304.1, RC ECO:0000313|Proteomes:UP000033411}; RA Lepp D., Hassan Y.I., Li X.-Z., Zhou T.; RL Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KKC39304.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LANJ01000011; KKC39304.1; -; Genomic_DNA. DR RefSeq; WP_046138467.1; NZ_LANJ01000011.1. DR EnsemblBacteria; KKC39304; KKC39304; WH87_03520. DR PATRIC; fig|1293439.3.peg.259; -. DR Proteomes; UP000033411; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000033411}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000033411}. FT DOMAIN 223 396 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 189 216 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 458 AA; 49950 MW; 1694C964DC8CA792 CRC64; MNDFDDEDEA GHKGGPQAFI DRREAPTRAG LVCPDVRGQI SQHTIEARKA EFEGLAEAIR LDVIFSEVIK VREIKPSTFI GGGHAATLAE RVKAEDIDLL LVDASLTAIQ QRNLEKETGT KVLDRTALIL EIFGERAATR EGVLQVELAH LNYQKGRLVR SWTHLERQRG SGGSGFMGGP GETQIESDRR QIADRIVLLE NRLEKVKKTR AQQRQKREGT PYPVVAIVGY TNAGKSSIFN KMTGAGVFAE DLLFATLDTT VRKLELPHGR EVMLSDTVGF VADLPTDLVA AFRATLEEVI DADVILHVRD IANPDHPAQA LDVLKVLGDL GVSAETIPII EVWNKIDLLG IDPDQDPLAG VSPAGRVAAS VPVSAKTGHG LDTLKLAVES ALADKSRTYH VHVPHSAGSD IGWLHSHSEV ISRDEPNENG SGFVVRVEPR HKTAFLERFN GRIESSDA // ID A0A0F5R7Q0_9BACL Unreviewed; 428 AA. AC A0A0F5R7Q0; DT 24-JUN-2015, integrated into UniProtKB/TrEMBL. DT 24-JUN-2015, sequence version 1. DT 07-JUN-2017, entry version 16. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=VE23_20925 {ECO:0000313|EMBL:KKC48986.1}; OS Paenibacillus sp. D9. OC Bacteria; Firmicutes; Bacilli; Bacillales; Paenibacillaceae; OC Paenibacillus. OX NCBI_TaxID=665792 {ECO:0000313|EMBL:KKC48986.1, ECO:0000313|Proteomes:UP000036611}; RN [1] {ECO:0000313|EMBL:KKC48986.1, ECO:0000313|Proteomes:UP000036611} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=D9 {ECO:0000313|EMBL:KKC48986.1, RC ECO:0000313|Proteomes:UP000036611}; RA Sharma V., Lin J.; RT "Genome sequence of surfactant producing, diesel degrading RT Paenibacillus sp. D9, isolated from diesel contaminated soil."; RL Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KKC48986.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JZEJ01000001; KKC48986.1; -; Genomic_DNA. DR RefSeq; WP_049868996.1; NZ_JZEJ01000001.1. DR EnsemblBacteria; KKC48986; KKC48986; VE23_20925. DR PATRIC; fig|665792.3.peg.4654; -. DR Proteomes; UP000036611; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000036611}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000036611}. FT DOMAIN 201 369 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 160 194 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 428 AA; 48441 MW; 7DFC3D73D9DFAA01 CRC64; MTIAPKEKAI LVGVHEQNNH QFAYSMEELR NLAEACNVEP VTELTQKAER IHKTHYLGSG KIEELAALVE QFDQPTVICN NELSPSQIRN LEAELKTKVI DRTILILDIF AERAQTREAQ LQVEVARLSY MLPRLVGLRE SLGRQGGGGG SGLANRGAGE TKLELDRRRI EERIHGLETE LEKLVAQRQI QRQRRKKNEI PVVCLVGYTN AGKSTLLNAM VDTFHPDSGK GVLAKDMLFA TLETSVRSIE LPDRKSFLLT DTVGFVSGLP HHLIKAFRST LEEVSEADLL VHVVDTSNPE YEQQIRVTEE TLKELRADHI PMLYAYNKSD LAEVSYPRVE DSRIYLSAYR REGIDELVES IRKSIFTDYV QTEIVVPYDK GSWVAFFNDN AHILETEYEE GGTRLKLECR EADLNRFKSE VGDTVSES // ID A0A0F5RBN9_9BACL Unreviewed; 441 AA. AC A0A0F5RBN9; DT 24-JUN-2015, integrated into UniProtKB/TrEMBL. DT 24-JUN-2015, sequence version 1. DT 07-JUN-2017, entry version 16. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=VE23_03455 {ECO:0000313|EMBL:KKC49669.1}; OS Paenibacillus sp. D9. OC Bacteria; Firmicutes; Bacilli; Bacillales; Paenibacillaceae; OC Paenibacillus. OX NCBI_TaxID=665792 {ECO:0000313|EMBL:KKC49669.1, ECO:0000313|Proteomes:UP000036611}; RN [1] {ECO:0000313|EMBL:KKC49669.1, ECO:0000313|Proteomes:UP000036611} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=D9 {ECO:0000313|EMBL:KKC49669.1, RC ECO:0000313|Proteomes:UP000036611}; RA Sharma V., Lin J.; RT "Genome sequence of surfactant producing, diesel degrading RT Paenibacillus sp. D9, isolated from diesel contaminated soil."; RL Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KKC49669.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JZEJ01000001; KKC49669.1; -; Genomic_DNA. DR RefSeq; WP_049869619.1; NZ_JZEJ01000001.1. DR EnsemblBacteria; KKC49669; KKC49669; VE23_03455. DR PATRIC; fig|665792.3.peg.774; -. DR Proteomes; UP000036611; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000036611}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000036611}. FT DOMAIN 208 373 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 441 AA; 48572 MW; AAD2AEFE8051ABE1 CRC64; MDTTTYETDH GVPDRAILVS LVTQEAKRGP SDPEHSLEEL ANLADTAGVE VLATVIQNKE APDPKWLVGK GKVEEIRAVK EELGATTIIF DQELSGAQVR NLEQSLDAKI IDRTQLILDI FAGRAKTREG IIQVELAQLS YLLPRLSGHG KNLSRLGGGI GTRGPGESKL ETDRRHIRGR ISDLKAHLRE LTRTRELHRE RRRKTGVTQV ALVGYTNAGK STLMNELTLA DVLVENRLFA TLDPTSRVLV LPSGNEVVLT DTVGFIQNLP HDLVAAFRAT LEEVAEADLI LHIVDSSSPM RREQMRVVEE LLQQLGASDK PLLLVYNKKD LVGGALRSLL PSSGPRQLLI SAYDAADRSR LLQAIQDELS GETRSFALPA DRGDLIALAY RCGEVLEREA DGDVLWLTVE LNRADYEVNG HQLEPYRQSR TSAGITTQQG D // ID A0A0F5V8T0_9GAMM Unreviewed; 429 AA. AC A0A0F5V8T0; DT 24-JUN-2015, integrated into UniProtKB/TrEMBL. DT 24-JUN-2015, sequence version 1. DT 30-AUG-2017, entry version 15. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=KY46_21160 {ECO:0000313|EMBL:KKC97934.1}; OS Photobacterium halotolerans. OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; OC Vibrionaceae; Photobacterium. OX NCBI_TaxID=265726 {ECO:0000313|EMBL:KKC97934.1, ECO:0000313|Proteomes:UP000033633}; RN [1] {ECO:0000313|EMBL:KKC97934.1, ECO:0000313|Proteomes:UP000033633} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MELD1 {ECO:0000313|EMBL:KKC97934.1, RC ECO:0000313|Proteomes:UP000033633}; RA Mathew D.C., Huang C.-C.; RT "Mercury Reductase activity and rhizosphere competence traits in the RT genome of root associated Photobacterium halotolerans MELD1."; RL Submitted (DEC-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KKC97934.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JWYV01000032; KKC97934.1; -; Genomic_DNA. DR RefSeq; WP_046222546.1; NZ_JWYV01000032.1. DR EnsemblBacteria; KKC97934; KKC97934; KY46_21160. DR PATRIC; fig|265726.11.peg.3324; -. DR Proteomes; UP000033633; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000033633}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000033633}. FT DOMAIN 198 365 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 429 AA; 48495 MW; 361BFC275DF261BF CRC64; MFDRYEAGEQ AILVHINFTQ EGEWEDLSEF EMLVSSAGVN QLRVITGSRQ SPHPKYYVGE GKAQEIADAV RAENAEIVIF NHSLSPAQER NLERLCKCRV LDRTGLILDI FAQRARTHEG KLQVELAQLR HISTRLIRGW THLERQKGGI GLRGPGETQL ETDRRLLRER IKAILRRLDK VSKQRDQGRR ARSRADIPTI SLVGYTNAGK STLFNRVTDA GVYAADQLFA TLDPTLRKID VEDVGTSILA DTVGFIRHLP HDLVAAFKAT LKETQEAALL LHVVDASDER YRENIDAVNT VLEEIDASDV PVLVVMNKID NLEEAEPRIE RDEDGIPRCV WVSAREGTGI DLLFTALTER LSGTMVTHTL RLPPAVIGRF RSKFYQLGAI VREEYEENGN LILDVRLPIA EWARLQKREH QGLDDFILA // ID A0A0F5W690_9ACTN Unreviewed; 499 AA. AC A0A0F5W690; DT 24-JUN-2015, integrated into UniProtKB/TrEMBL. DT 24-JUN-2015, sequence version 1. DT 07-JUN-2017, entry version 14. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=TN53_04550 {ECO:0000313|EMBL:KKD09050.1}; OS Streptomyces sp. WM6386. OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae; OC Streptomyces. OX NCBI_TaxID=1415558 {ECO:0000313|EMBL:KKD09050.1, ECO:0000313|Proteomes:UP000033641}; RN [1] {ECO:0000313|EMBL:KKD09050.1, ECO:0000313|Proteomes:UP000033641} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=WM6386 {ECO:0000313|EMBL:KKD09050.1, RC ECO:0000313|Proteomes:UP000033641}; RA Ju K.-S., Doroghazi J.R., Metcalf W.; RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KKD09050.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JXTE01000005; KKD09050.1; -; Genomic_DNA. DR RefSeq; WP_046257033.1; NZ_JXTE01000005.1. DR EnsemblBacteria; KKD09050; KKD09050; TN53_04550. DR PATRIC; fig|1415558.3.peg.5980; -. DR Proteomes; UP000033641; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 2. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000313|EMBL:KKD09050.1}; KW Complete proteome {ECO:0000313|Proteomes:UP000033641}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900, KW ECO:0000313|EMBL:KKD09050.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000033641}. FT DOMAIN 275 440 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 499 AA; 54518 MW; AC44FEFC21305FD2 CRC64; MTSSSSPSQD SQRFAHTHPE GLRADALMEE DVAWSHEIDG ERDGDQFDRS ERAALRRVAG LSTELEDVTE VEYRQLRLER VVLVGVWTSG TAQDSENSLA ELAALAETAG ALVLDGVIQR RDKPDAATYI GSGKATELRD IVLETGADTV ICDGELSPGQ LIHLEDVVKV KVIDRTALIL DIFAQHAKSR EGKAQVALAQ MQYMLPRLRG WGQSLSRQMG GGKGGGLATR GPGETKIETD RRRIREKMAK MRREIADMKT GREIKRQERK RNKVPSVAIA GYTNAGKSSL LNRLTGAGVL VENSLFATLD PTVRRAETPS GRLYTLADTV GFVRHLPHHL VEAFRSTMEE VGESDLILHV VDGSHPNPEE QLAAVREVIT DVGATRVPEI VVINKADAAD PLTLQRLMRI EKRSIAVSAR TGQGIEELLA LIDNELPRPS VEVEALVPYT LGKLVARAHT EGEVISEEHT PEGTLLKVRV HEELAADLAP YVPVPVSVA // ID A0A0F5YGV4_9CYAN Unreviewed; 591 AA. AC A0A0F5YGV4; DT 24-JUN-2015, integrated into UniProtKB/TrEMBL. DT 24-JUN-2015, sequence version 1. DT 07-JUN-2017, entry version 15. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=WN50_14290 {ECO:0000313|EMBL:KKD37445.1}; OS Limnoraphis robusta CS-951. OC Bacteria; Cyanobacteria; Oscillatoriophycideae; Oscillatoriales; OC Oscillatoriaceae; Limnoraphis. OX NCBI_TaxID=1637645 {ECO:0000313|EMBL:KKD37445.1, ECO:0000313|Proteomes:UP000033607}; RN [1] {ECO:0000313|EMBL:KKD37445.1, ECO:0000313|Proteomes:UP000033607} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CS-951 {ECO:0000313|EMBL:KKD37445.1, RC ECO:0000313|Proteomes:UP000033607}; RA Willis A., Parks M., Burford M.A.; RT "Draft genome assembly of filamentous brackish cyanobacterium RT Limnoraphis robusta strain CS-951."; RL Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KKD37445.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LATL02000141; KKD37445.1; -; Genomic_DNA. DR RefSeq; WP_046279229.1; NZ_LATL02000141.1. DR EnsemblBacteria; KKD37445; KKD37445; WN50_14290. DR PATRIC; fig|1637645.4.peg.2850; -. DR Proteomes; UP000033607; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000033607}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000033607}. FT DOMAIN 418 591 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 377 411 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 591 AA; 64593 MW; 8C4972677AF86DA2 CRC64; MINKSFEYPE NGSGGPIETI YGNLQGLKPS QLKGLQRLYH QRIPGDRITT PEFAQRLAAS STEIGQPVCA YLNRRGQVIR VGVGTPRQTQ IPPLELPRYG GGRLSGIRCI ATQIKSEPPN ESALTAMAIQ RLDVLVVLTL TGSGFQRRGG GGTGYIEQAY LAHLLPPTAE DNNGNITTLQ ATIPHYLSPP QSLDMLSTQD FLDLVDNLEA ELQRELVAQT VDSDGDKVLL VGVKTEDISP QRFEDGLLEL VRLVDTAGGQ VIETLRQKRS RPHPQTVVGE GKVQEIALTA QTIGASLIVF DRSLSPAQVR NLETQIGVRV VDRTEVILDI FAQRAQSGAG KLQVELAQLE YSLPRLTGRG QAMSRLGGGI GTRGPGETKL ETERRAIQRR IARLQQEVNQ LQAHRSRLRQ RRQHQEVPTV AIVGYTNAGK STLLNVLTSS EIYAADQLFA TLDPTSRRLA IPDAITDEPQ TIVLTDTVGF IHELPPALID AFRATLEEVS DADALVHVVD LSHPAWQGQI ESVMKILMSM PITPGPALLA FNKIDQVDGE TLRFAQEEYP QAAFISAGKA LGLETLRQRI GQLIHYVSSL S // ID A0A0F6A238_9GAMM Unreviewed; 429 AA. AC A0A0F6A238; DT 24-JUN-2015, integrated into UniProtKB/TrEMBL. DT 24-JUN-2015, sequence version 1. DT 30-AUG-2017, entry version 15. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=RN22_02720 {ECO:0000313|EMBL:KKD62033.1}; OS Grimontia sp. AD028. OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; OC Vibrionaceae; Grimontia. OX NCBI_TaxID=1581149 {ECO:0000313|EMBL:KKD62033.1, ECO:0000313|Proteomes:UP000033732}; RN [1] {ECO:0000313|EMBL:KKD62033.1, ECO:0000313|Proteomes:UP000033732} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=AD028 {ECO:0000313|EMBL:KKD62033.1, RC ECO:0000313|Proteomes:UP000033732}; RA Adrian T.-G.-S., Chan K.-G.; RT "Genome sequencing of Grimontia sp. AD028."; RL Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KKD62033.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LASY01000010; KKD62033.1; -; Genomic_DNA. DR RefSeq; WP_046302986.1; NZ_LASY01000010.1. DR EnsemblBacteria; KKD62033; KKD62033; RN22_02720. DR PATRIC; fig|1581149.3.peg.40; -. DR Proteomes; UP000033732; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000033732}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000033732}. FT DOMAIN 198 365 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 429 AA; 48476 MW; BC1C1C1B59882A3E CRC64; MFDRYEAGEQ AVLVHINFTQ EGEWEDLSEF EMLVSSAGVS RLQTITGSRQ SPHSKYFVGE GKALEIADAV RLTGADIVIF NHALSPAQER NLERLVKCRV LDRTGLILDI FAQRARTHEG KLQVELAQLR HLSTRLVRGW THLERQKGGI GLRGPGETQL ETDRRLLRDR VKAILRRLEK VSKQREQGRR ARSRAEVPTV SLVGYTNAGK STLFNRITEA GVYAADQLFA TLDPTLRKIE VEDVGDVILA DTVGFIRHLP HDLVAAFKAT LQETQEAALL LHVIDASDDR FRENIEAVDV VLEEIDAHEI PTLLVMNKID NMDEASPRIE RDEEGLPRVV YVSALADQGI DLLFEALTER LAGTMVSYRL RIPPAAIGRM HSKFCQLRCI THEEYEQDGH LLVDVRLPQT DWLRLKKREG SELGDFIVN // ID A0A0F6A5W1_9GAMM Unreviewed; 429 AA. AC A0A0F6A5W1; DT 24-JUN-2015, integrated into UniProtKB/TrEMBL. DT 24-JUN-2015, sequence version 1. DT 30-AUG-2017, entry version 14. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=N479_22410 {ECO:0000313|EMBL:KKE81555.1}; OS Pseudoalteromonas luteoviolacea S4054. OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales; OC Pseudoalteromonadaceae; Pseudoalteromonas. OX NCBI_TaxID=1129367 {ECO:0000313|EMBL:KKE81555.1, ECO:0000313|Proteomes:UP000033434}; RN [1] {ECO:0000313|EMBL:KKE81555.1, ECO:0000313|Proteomes:UP000033434} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=S4054 {ECO:0000313|EMBL:KKE81555.1, RC ECO:0000313|Proteomes:UP000033434}; RX PubMed=25879706; DOI=10.1186/s12864-015-1365-z; RA Machado H., Sonnenschein E.C., Melchiorsen J., Gram L.; RT "Genome mining reveals unlocked bioactive potential of marine Gram- RT negative bacteria."; RL BMC Genomics 16:158-158(2015). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KKE81555.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AUXW01000186; KKE81555.1; -; Genomic_DNA. DR RefSeq; WP_046357995.1; NZ_AUXW01000186.1. DR EnsemblBacteria; KKE81555; KKE81555; N479_22410. DR GeneID; 31723825; -. DR PATRIC; fig|1129367.4.peg.4653; -. DR Proteomes; UP000033434; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000033434}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000033434}. FT DOMAIN 198 365 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 429 AA; 48669 MW; 4FAA628D8592230D CRC64; MFDRYEAGEQ AVLVHIEFPN EGDREDLQEL EMLVSSAGVS SVAVVQGSRQ APHPKLFVGT GKAEEIAEIV RTYKADVIIF NHQLSPSQER NLEHICRCRV LDRTTLILDI FAQRARTHEG KLQVELAQLR HISTRLIRGW THLERQKGGI GLRGPGETQL ETDRRLLRER IKSIRKRLDK VAVVREQGRR ARSRNEIPTV SLVGYTNAGK STLFNQITNS DVYAADQLFA TLDPTLRKLE IADVGPIILA DTVGFIRHLP HDLVAAFKAT LTETREADLQ LHVVDVADQR RKENIEQVQS VLEEIEADEI PQLLVYNKID LVEEIQPKID RDENGVPIRV WLSAQANIGI ELLSQAISEL LAKKMFCNQL IVPPAFGKLR GALFNLNAVC EESYDERGNW LLDVRLPQAD WERLKKDQGP EIERFIAQD // ID A0A0F6R0P3_9CORY Unreviewed; 553 AA. AC A0A0F6R0P3; DT 22-JUL-2015, integrated into UniProtKB/TrEMBL. DT 22-JUL-2015, sequence version 1. DT 10-MAY-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:AKE41400.1}; GN ORFNames=UL82_06170 {ECO:0000313|EMBL:AKE41400.1}; OS Corynebacterium kutscheri. OC Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae; OC Corynebacterium. OX NCBI_TaxID=35755 {ECO:0000313|EMBL:AKE41400.1, ECO:0000313|Proteomes:UP000033457}; RN [1] {ECO:0000313|EMBL:AKE41400.1, ECO:0000313|Proteomes:UP000033457} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 20755 {ECO:0000313|EMBL:AKE41400.1, RC ECO:0000313|Proteomes:UP000033457}; RX PubMed=26021937; RA Ruckert C., Albersmeier A., Winkler A., Tauch A.; RT "Complete Genome Sequence of Corynebacterium kutscheri DSM 20755, a RT Corynebacterial Type Strain with Remarkably Low G+C Content of RT Chromosomal DNA."; RL Genome Announc. 3:e00571-15(2015). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP011312; AKE41400.1; -; Genomic_DNA. DR EnsemblBacteria; AKE41400; AKE41400; UL82_06170. DR KEGG; cku:UL82_06170; -. DR KO; K03665; -. DR Proteomes; UP000033457; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000033457}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000033457}. FT DOMAIN 329 505 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 288 315 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 553 AA; 60614 MW; 01E5318088ACB79E CRC64; MTKNNFKPEF NRDQQPQESE TKKKYSLGAH TQEPKNSVRD SLLDKAFSDH LPTQPAEPHS EDLTGLIRSG TDDEIFDTSL LDQFSNQHAP TTGELDLEAR SSLRRLTRGS EIHATDQDDG YDVEYRKLRL ERVILVGVWT SGTTAEIEAT MNELAALAET AGSEIVDMLY QKRDRPDPGT YIGSGKVKEL AEIVQATGVD TVVCDGELSP GQMIALEKAL DVKVIDRTML ILDIFAQHAK SKEGKAQVSL AQMEYLITRV RGWGGALSRQ AGGRAGSNGG VGLRGPGETK IEADRRRLRA DMAKLRKEIA GMKTAREIKR SQRRAATIPQ IAIAGYTNAG KSSLINAMTG AGVLVEDALF ATLDPTTRRA ELGDGRTVVF TDTVGFVRHL PTQLVEAFRS TLEEVVEADL VLHVVDGSDP FPLKQIEAVN GVISDIVREL GVEAPPEIIV VNKIDAADPL VLAELKHAFD DVIFVSAHTG QGIPELETRV ELFLNTLDAH VELLIPFTRG DIVSRLHEQA TVVYEEYTDA GTKLDIRLPQ SMADELKEFI VTS // ID A0A0F6TBR8_9CORY Unreviewed; 502 AA. AC A0A0F6TBR8; DT 22-JUL-2015, integrated into UniProtKB/TrEMBL. DT 22-JUL-2015, sequence version 1. DT 07-JUN-2017, entry version 12. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=UL81_06965 {ECO:0000313|EMBL:AKE39349.1}; OS Corynebacterium camporealensis. OC Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae; OC Corynebacterium. OX NCBI_TaxID=161896 {ECO:0000313|EMBL:AKE39349.1, ECO:0000313|Proteomes:UP000033566}; RN [1] {ECO:0000313|EMBL:AKE39349.1, ECO:0000313|Proteomes:UP000033566} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 44610 {ECO:0000313|EMBL:AKE39349.1, RC ECO:0000313|Proteomes:UP000033566}; RX PubMed=26021938; RA Ruckert C., Albersmeier A., Winkler A., Tauch A.; RT "Complete Genome Sequence of Corynebacterium camporealensis DSM 44610, RT Isolated from the Milk of a Manchega Sheep with Subclinical RT Mastitis."; RL Genome Announc. 3:e00572-15(2015). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP011311; AKE39349.1; -; Genomic_DNA. DR RefSeq; WP_035104927.1; NZ_JRUB01000001.1. DR EnsemblBacteria; AKE39349; AKE39349; UL81_06965. DR KEGG; ccj:UL81_06965; -. DR PATRIC; fig|161896.4.peg.1361; -. DR KO; K03665; -. DR Proteomes; UP000033566; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000033566}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000033566}. FT DOMAIN 274 445 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 240 267 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 502 AA; 55164 MW; C13571AB1CD5F209 CRC64; MTSSSEKNPS HDELLAQAFR DNAPQPDIAE PSDEPTTGEL DLAERNAFRR VTKDTNIRAE DTTDGYEVEY RKLRLEQVIL VGVWTEGTVA EVEATMAELA ALTETAGADV VEMLYQKRDR PDPGTYIGSG KVRELADIVQ ATGADTVVCD GELNPGQLSA LERALNTKVI DRTMLILDIF AQHAKSKEGK AQVSLAQLEY LYTHTRGWGG NLSRQAGGRA GSNGGVGLRG PGETKIETDR RRIRTEMARL RKELKSMKTA REVKRSRRQE SVIPQIAIAG YTNAGKSSLI NAMTGAGVLV EDALFATLDP TTRKAELSDG RQVVFTDTVG FVRHLPTQLV EAFKSTLEEV LAADIMLHVV DGSDPFPLKQ IEAVNKVIYD IVKETGEEAP PEIIVINKID QADPLVLAEL RHVLDRDNVV YVSAKTGEGI KELTARVELF LNSQDAHVRM LVPFTRGDVV ARAHAQGTVR EEEYTSEGTV LDVRLPQVVA RELDEFVTEH VS // ID A0A0F6TRL8_9GAMM Unreviewed; 429 AA. AC A0A0F6TRL8; DT 22-JUL-2015, integrated into UniProtKB/TrEMBL. DT 22-JUL-2015, sequence version 1. DT 30-AUG-2017, entry version 13. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=TQ33_1849 {ECO:0000313|EMBL:AKE52787.1}; OS Kangiella geojedonensis. OC Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales; OC Kangiellaceae; Kangiella. OX NCBI_TaxID=914150 {ECO:0000313|EMBL:AKE52787.1, ECO:0000313|Proteomes:UP000034071}; RN [1] {ECO:0000313|EMBL:AKE52787.1, ECO:0000313|Proteomes:UP000034071} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=YCS-5 {ECO:0000313|EMBL:AKE52787.1, RC ECO:0000313|Proteomes:UP000034071}; RA Kim K.M.; RT "Complete genome sequence of Kangiella geojedonensis strain YCS-5T."; RL Submitted (FEB-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP010975; AKE52787.1; -; Genomic_DNA. DR RefSeq; WP_046561812.1; NZ_CP010975.1. DR EnsemblBacteria; AKE52787; AKE52787; TQ33_1849. DR KEGG; kge:TQ33_1849; -. DR PATRIC; fig|914150.5.peg.1875; -. DR KO; K03665; -. DR Proteomes; UP000034071; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000034071}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000034071}. FT DOMAIN 198 365 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 429 AA; 48780 MW; 15BF58127D4D8574 CRC64; MFDRHSGGES AILVHIDFDQ ESNQEDLQEF VELVRSAGLK VMDIVTAKRH SPDPKFFIGK GKIEEIQSVK EATEANVIIF NHNLSPTQER NIEKVAKCRV IDRIGLILDI FAQRAFTFEG KLQVELAQLR HLSTRLVRGW THLERQKGGI GMRGPGETQL ETDRRLIRDR IKHIEKRLDK VGRQREQGRR SRKRANIKTV SIVGYTNAGK STLFNLLTEA DVLAEDKLFA TLDPTLRRVS LPQGSDVILA DTVGFIRHLP HELVAAFRAT LEESVEADIL LHVIDAASER RDENIEQVWE VLSDIGANEI RTLEVYNKID MIEGAEPRIE RDDEGIPIRV WTSAVKEQGI ELLLEAIEEL AEEQQFSAQL RLPPQEGRLR GLLYELQAIE EEGVADNGDM LLDIRLEQAD WIRLGKQLDK DLSQFVLSS // ID A0A0F6W6I9_9DELT Unreviewed; 466 AA. AC A0A0F6W6I9; DT 22-JUL-2015, integrated into UniProtKB/TrEMBL. DT 22-JUL-2015, sequence version 1. DT 07-JUN-2017, entry version 12. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=DB32_005924 {ECO:0000313|EMBL:AKF08775.1}; OS Sandaracinus amylolyticus. OC Bacteria; Proteobacteria; Deltaproteobacteria; Myxococcales; OC Sorangiineae; Sandaracinaceae; Sandaracinus. OX NCBI_TaxID=927083 {ECO:0000313|EMBL:AKF08775.1, ECO:0000313|Proteomes:UP000034883}; RN [1] {ECO:0000313|EMBL:AKF08775.1, ECO:0000313|Proteomes:UP000034883} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 53668 {ECO:0000313|EMBL:AKF08775.1, RC ECO:0000313|Proteomes:UP000034883}; RA Sharma G., Subramanian S.; RT "Genome assembly of Sandaracinus amylolyticus DSM 53668."; RL Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP011125; AKF08775.1; -; Genomic_DNA. DR RefSeq; WP_053235881.1; NZ_CP011125.1. DR EnsemblBacteria; AKF08775; AKF08775; DB32_005924. DR KEGG; samy:DB32_005924; -. DR KO; K03665; -. DR Proteomes; UP000034883; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000034883}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000034883}. FT DOMAIN 249 414 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 209 243 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 466 AA; 51075 MW; 55ABF7EDB48250B8 CRC64; MATHDEEGLP RSRRDLQGRP RAVVVGVQLP GVDDVEFEAS LIELERLGTT LGLLPITRIT QKRSALAPAA VLGEGKLVEL ASWTGGTGIV PSGAPQKKKR KIDQADDEPE DEAEEAGAVA PTGEPRATVV LVDHDLAPSQ ALNLERATGA EVLDRTSVIV SIFQRHARTR EARIQVEIAR LTYLAPRLRE AGAGGDRQRG GIGGKGAGES AVELDRRRIR DRIAELRNEL SQVQRESDVR RARRVQRGDT FALVGYTNAG KSSWFRMLTG GEVYVADELF ATLDTTVRAL APETRPRILV SDTVGFIDRL PHDLVASFRS TLEEARDASL LVHVVDASDP AFRAQLDVTK RVLAEIDADQ APSLVLLNKV DRIDAQAREA LAIEYPDAMQ VSARSKDDVA TVRERIVAFF ERDMVEDELF VPYAKSAIVN RVHESARVLD ETHEDEGTRL KVRAPAAVLA QLRAQL // ID A0A0F6YKB7_9DELT Unreviewed; 717 AA. AC A0A0F6YKB7; DT 22-JUL-2015, integrated into UniProtKB/TrEMBL. DT 22-JUL-2015, sequence version 1. DT 12-APR-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=DB32_006244 {ECO:0000313|EMBL:AKF09095.1}; OS Sandaracinus amylolyticus. OC Bacteria; Proteobacteria; Deltaproteobacteria; Myxococcales; OC Sorangiineae; Sandaracinaceae; Sandaracinus. OX NCBI_TaxID=927083 {ECO:0000313|EMBL:AKF09095.1, ECO:0000313|Proteomes:UP000034883}; RN [1] {ECO:0000313|EMBL:AKF09095.1, ECO:0000313|Proteomes:UP000034883} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 53668 {ECO:0000313|EMBL:AKF09095.1, RC ECO:0000313|Proteomes:UP000034883}; RA Sharma G., Subramanian S.; RT "Genome assembly of Sandaracinus amylolyticus DSM 53668."; RL Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP011125; AKF09095.1; -; Genomic_DNA. DR EnsemblBacteria; AKF09095; AKF09095; DB32_006244. DR KEGG; samy:DB32_006244; -. DR KO; K03665; -. DR Proteomes; UP000034883; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR002575; Aminoglycoside_PTrfase. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR011009; Kinase-like_dom. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF01636; APH; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF56112; SSF56112; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000034883}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000034883}. FT DOMAIN 195 359 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 156 183 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 717 AA; 78511 MW; 601DED7AF8BDE669 CRC64; MTRPRSSSST DRSSDLAILL APSGEASSSE LERLLAGLGI RVAHTVPLTR DPGAGKRAEV RASIDALARA PDQRVLVVVD RALDPGAQRE LEIELDVEVL DRTAVVLRVF EQRARTRLAQ LEVELARLAY EIPRVRDDGA RRDREGGGGG RGARGHTEVE LRKQQLRERS ARLEREVERL RASRATQAAA RRDVPRVALV GYTNAGKSSL LRALTGSDVL VEDALFATLD TTVRALSPAT TPRVLVSDTV GFMRNLPHAL VASFHTTLDE ARDADLLLLV VDASDPEHRE QLRVTREVLE TIGATSPTRI VLSKIDRVDP ERRASLLREL PGALAISAHD PADVRRLRDA IVAFFARDEE HDVLVVPFTE GRLMAEIRAE AHVVSEHHDE PGTALAVRAR PDVLERWRTA LPPLPAITTA ADLVGAAARY GLRVAPERDA LDASGLDFLV LHARDDAGSP WVVRTPRRPD VIASAQREAR VLRLVAPSLP AAVPEWRVHA RDVIAYRRIE GTPGWRFDDA GALQWAFDPS APPDAFLDTY ARLIASLQSI PVDRIHDAGV RVEAAGDARA ELARAMHATR DVLAPSDAVW SRWQRWIDDD ASWPAHVALA HGDLHPGHLL LDDASRITGV LDWTEARATD PSLDLAMFFG CYGRDALESV VDRFARAGGV TWPAIVSHTI ERWAAYAVVI AEWALRTGDD AVLAHARHHL ATITAST // ID A0A0F6YM60_9DELT Unreviewed; 625 AA. AC A0A0F6YM60; DT 22-JUL-2015, integrated into UniProtKB/TrEMBL. DT 22-JUL-2015, sequence version 1. DT 07-JUN-2017, entry version 12. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=DB32_006215 {ECO:0000313|EMBL:AKF09066.1}; OS Sandaracinus amylolyticus. OC Bacteria; Proteobacteria; Deltaproteobacteria; Myxococcales; OC Sorangiineae; Sandaracinaceae; Sandaracinus. OX NCBI_TaxID=927083 {ECO:0000313|EMBL:AKF09066.1, ECO:0000313|Proteomes:UP000034883}; RN [1] {ECO:0000313|EMBL:AKF09066.1, ECO:0000313|Proteomes:UP000034883} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 53668 {ECO:0000313|EMBL:AKF09066.1, RC ECO:0000313|Proteomes:UP000034883}; RA Sharma G., Subramanian S.; RT "Genome assembly of Sandaracinus amylolyticus DSM 53668."; RL Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP011125; AKF09066.1; -; Genomic_DNA. DR RefSeq; WP_053236153.1; NZ_CP011125.1. DR EnsemblBacteria; AKF09066; AKF09066; DB32_006215. DR KEGG; samy:DB32_006215; -. DR KO; K03665; -. DR Proteomes; UP000034883; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000034883}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000034883}. FT DOMAIN 385 549 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 351 378 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 625 AA; 68420 MW; B559423D5C289425 CRC64; MTIHGNTNGL SPSDLHALER LYRRRVPFDR LLTPELARSM AEISASTGRQ VGVIADRSGH VQFVVVGDSS KLMLPDVGRV RAAQGRFRGL RLIHTHLTPE GLTRDDLVDL TRLRLDLVAA INVGKNGEPE TVHYGHNVPV APGSSESPHR TIGPLSYQAL IGELVQVDPA ALIAGLEQEF ARVARTRVVD AKDGRAILVH VCEKHDAWRA EESLRELAEL ARTAGVEVVD QVLQVRDRID PKFVMGRGKL DEIVQRSMQV DASVLIFDRN LGPAQAAAIA KAIDLKVIDR SQLILDIFAQ RAESRDGKLQ VELAQMKYLL PRIGQKDDSL SRLTGGIGGR GPGETVLEIG KRRARERISR LESELEKLAV QRRNRRQRRN RRDVPIVSIV GYTNAGKSTL LNALTGSETI VEDKLFATLD TRSRRIRFPE EREVVITDTV GFIRDLPVDL FAAFRATFEE AQDADLLLHV VDASDPALGE HIKTTEQLLG QLELSNVPTL LVLNKCDRVP ASEVASMVRA RDAVPVSAID PSTFGPLLER LERMLFERGS GVVTRSATGS DELDLDDAIP PSITSVRLTA ARPVEEAPAP RGPYFDDAAI DALIAGSGSK SAPAAAPART RSRAR // ID A0A0F7FYS2_9ACTN Unreviewed; 469 AA. AC A0A0F7FYS2; DT 22-JUL-2015, integrated into UniProtKB/TrEMBL. DT 22-JUL-2015, sequence version 1. DT 07-JUN-2017, entry version 13. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=SXIM_45360 {ECO:0000313|EMBL:AKG45920.1}; OS Streptomyces xiamenensis. OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae; OC Streptomyces. OX NCBI_TaxID=408015 {ECO:0000313|EMBL:AKG45920.1, ECO:0000313|Proteomes:UP000034034}; RN [1] {ECO:0000313|EMBL:AKG45920.1, ECO:0000313|Proteomes:UP000034034} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MCCC 1A01550 {ECO:0000313|Proteomes:UP000034034}; RA Xu J.; RT "Complete genome sequence of a mangrove-derived Streptomyces RT xiamenensis."; RL Submitted (FEB-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP009922; AKG45920.1; -; Genomic_DNA. DR EnsemblBacteria; AKG45920; AKG45920; SXIM_45360. DR KEGG; sxi:SXIM_45360; -. DR PATRIC; fig|408015.6.peg.4592; -. DR KO; K03665; -. DR Proteomes; UP000034034; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 2. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000313|EMBL:AKG45920.1}; KW Complete proteome {ECO:0000313|Proteomes:UP000034034}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900, KW ECO:0000313|EMBL:AKG45920.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000034034}. FT DOMAIN 247 412 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 469 AA; 51291 MW; F7420F6B93B9571A CRC64; MDEDADWSTF DEERDGEQFD REERAALRRV AGLSTELEDV TEVEYRQLRL ERVVLVGVWT SGTAQDADNS LAELAALAET AGAQVLEGVT QRRTKPDPAT YIGSGKAQEL RDLVLETGAD TVVCDGELSP GQLIKLEDVV KVKVVDRTAL ILDIFAQHAK SREGKAQVSL AQMQYMLPRL RGWGQSLSRQ MGGGGGGGMA TRGPGETKIE TDRRRIREKM AKMRREIAEM KTGREIKRGE RRRNHVPSVA IAGYTNAGKS SLLNRLTGAG VLVENALFAT LDPTVRRAET PSGRLYTLAD TVGFVRHLPH HLVEAFRSTM EEVGEADLIL HVVDGSHPVP EEQLAAVREV IREVGATQVP EIVVINKADA ADELTLQRLL RAERRAIAVS AHSGLGIEQL LAWIDDELPR PDVEVAALVP YTEGALVSRV HSEGEVLREE HTGEGTLLTA RVHPELGALL EPYALATQG // ID A0A0F7GE72_9CHLR Unreviewed; 380 AA. AC A0A0F7GE72; DT 22-JUL-2015, integrated into UniProtKB/TrEMBL. DT 22-JUL-2015, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:AKG53509.1}; GN ORFNames=DGWBC_0842 {ECO:0000313|EMBL:AKG53509.1}; OS Dehalogenimonas sp. WBC-2. OC Bacteria; Chloroflexi; Dehalococcoidia; Dehalogenimonas. OX NCBI_TaxID=943347 {ECO:0000313|EMBL:AKG53509.1, ECO:0000313|Proteomes:UP000034106}; RN [1] {ECO:0000313|Proteomes:UP000034106} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=WBC-2 {ECO:0000313|Proteomes:UP000034106}; RA Molenda O., Edwards E.A.; RT "Identification of trans-1,2-dichloroethene reductive dehalogenase RT (TdrA) in Dehalogenimonas sp. WBC-2."; RL Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP011392; AKG53509.1; -; Genomic_DNA. DR KEGG; dew:DGWBC_0842; -. DR PATRIC; fig|943347.4.peg.881; -. DR KO; K03665; -. DR Proteomes; UP000034106; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000034106}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000034106}. FT DOMAIN 204 380 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 380 AA; 42659 MW; 0E7C00BF2B386F96 CRC64; MIDTALKPEK VMLVAVDSGD DAKNIGWTAE DSMKELEQLV RTAGGVVVGH IIQRLSHPQK TTYLGRGKLE DLVSSREINN FDTVVFDDEL TPLQQKTLED ALKVKVIDRV ALILDIFARH AQTREGKLQV ELAQHQYLLP RLAGQWSHLE RLGGGIGTRG PGESQLETDR RILQRKIVTL KTKLAEVSHH RELYRDKRRQ GGVPIAALVG YTNSGKSSLL KALTKAEVII EDKLFATLDP TTRRLNTGDN RPFLITDTVG FIKKLPPAIV NAFHATLEEL TEASLLIHVI DITSENAVEQ CQTVESILKD LNISNKPRIT VYNKIDLLPE VSIDWDETKA LEHLAEYGDY RPENTILTSA VKRWGLRNLI GSIDKMIYRQ // ID A0A0F7HA11_SERFO Unreviewed; 426 AA. AC A0A0F7HA11; DT 22-JUL-2015, integrated into UniProtKB/TrEMBL. DT 22-JUL-2015, sequence version 1. DT 30-AUG-2017, entry version 17. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=BSQ40_26195 {ECO:0000313|EMBL:OKP21383.1}, GN WN53_10315 {ECO:0000313|EMBL:AKG69464.1}; OS Serratia fonticola. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; OC Yersiniaceae; Serratia. OX NCBI_TaxID=47917 {ECO:0000313|EMBL:AKG69464.1, ECO:0000313|Proteomes:UP000034699}; RN [1] {ECO:0000313|EMBL:AKG69464.1, ECO:0000313|Proteomes:UP000034699} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 4576 {ECO:0000313|EMBL:AKG69464.1, RC ECO:0000313|Proteomes:UP000034699}; RA Chan K.-G., Ee R.; RT "Complete Genome Sequencing of Serratia Fonticola DSM-4576."; RL Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:OKP21383.1, ECO:0000313|Proteomes:UP000186436} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=5l {ECO:0000313|EMBL:OKP21383.1, RC ECO:0000313|Proteomes:UP000186436}; RA Goncharov A., Grigoriev S., Azarov D., Kolodzhieva V., Tikhonov A., RA Akhremenko Y., Tarasova L., Zueva L., Suvorov A.; RT "Draft genome sequence of Serratia fonticola 5l isolated from RT intestinal tract content of a 9000-year-old elk (Alces alces) from RT permafrost on the Omoloy river."; RL Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP011254; AKG69464.1; -; Genomic_DNA. DR EMBL; MQRH01000037; OKP21383.1; -; Genomic_DNA. DR RefSeq; WP_024483336.1; NZ_MQRH01000037.1. DR EnsemblBacteria; AKG69464; AKG69464; WN53_10315. DR KEGG; sfw:WN53_10315; -. DR PATRIC; fig|47917.8.peg.2128; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR Proteomes; UP000034699; Chromosome. DR Proteomes; UP000186436; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000034699}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000034699}. FT DOMAIN 198 365 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 426 AA; 47970 MW; F84CC0C69926C0B3 CRC64; MFDRYEAGEQ AVLVHIYFSQ DKDTEDLSEF ESLVSSAGVE ALQVVTGSRK APHPKYFVGE GKAEEIADAV KASGASVVLF DHALSAAQER NLERLCECRV IDRTGLILDI FAQRARTHEG KLQVELAQLR HIATRLVRGW THLERQKGGI GLRGPGETQL ETDRRLLRDR ISLILRRLER VEKQRDQGRR ARTRADVPTV SLVGYTNAGK STLFNRITSA GVYVADQLFA TLDPTLRRID VADVGDTVLA DTVGFIRHLP HDLVAAFKAT LQETRQASLL LHVIDAADTR VDENIEAVNS VLAEIESDEI PTLLVMNKID MLDDFVPRID RNEENLPIRV WLSAASGEGI PLLFQALTER LSGEIAHYEL RLPPQAGRLR SRFYQLQAIE KEWNEEDGSI GVVVRMPIVE WRRLCKQEQE LINFIV // ID A0A0F7HLT7_9STAP Unreviewed; 411 AA. AC A0A0F7HLT7; DT 22-JUL-2015, integrated into UniProtKB/TrEMBL. DT 22-JUL-2015, sequence version 1. DT 07-JUN-2017, entry version 14. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=AAT16_06060 {ECO:0000313|EMBL:AKG73826.1}; OS Salinicoccus halodurans. OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae; OC Salinicoccus. OX NCBI_TaxID=407035 {ECO:0000313|EMBL:AKG73826.1, ECO:0000313|Proteomes:UP000034029}; RN [1] {ECO:0000313|Proteomes:UP000034029} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=H3B36 {ECO:0000313|Proteomes:UP000034029}; RA Ma Y., Jiang K., Xue Y.; RT "Complete genome sequence of Salinicoccus halodurans strain H3B36, RT isolated from the Qaidam basin of China."; RL Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP011366; AKG73826.1; -; Genomic_DNA. DR RefSeq; WP_046790014.1; NZ_FOTB01000001.1. DR EnsemblBacteria; AKG73826; AKG73826; AAT16_06060. DR KEGG; shv:AAT16_06060; -. DR PATRIC; fig|407035.3.peg.1258; -. DR KO; K03665; -. DR Proteomes; UP000034029; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000034029}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000034029}. FT DOMAIN 195 296 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 411 AA; 46842 MW; DA86C52CBA09B3E7 CRC64; MTETYKGIII AVNTPDRKNI DAEINELISL AGSIGVEISG VHVQNRSTMD RRAYVGSGFL NEVAEQYADD ELGYIIVNDE ITASQNRSIE AVMDTRIIDR TQVILDIFSL RAHSKAGQLQ VELAQLQYLV PRLRGQGINL SRLGAGIGTR GPGETKLETD RRHINQRIKE IRKQLKVIES HRERYREKRN RNQVVKVSLI GYTNAGKSSL FNTMAQSNTL EEDALFATLD PKTRRLVLPS GFECVVSDTV GFIQNLPTTL IESFKSTLEE AADSDFLIHV IDNSSEDLQT HYDTVKDLTG QLDMKEIPSL IFFNKTDIDD TRHYTPPEAH EYVHKDMESQ HILGLLETFM KKHMESYKAE IPLSEPQKLY DLKRHTIVDK EILDEEAEVY RLEGHEPDGA WSKRIMERNE E // ID A0A0F7JQB9_9DEIO Unreviewed; 569 AA. AC A0A0F7JQB9; DT 22-JUL-2015, integrated into UniProtKB/TrEMBL. DT 22-JUL-2015, sequence version 1. DT 30-AUG-2017, entry version 14. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=SY84_05800 {ECO:0000313|EMBL:AKH16650.1}; OS Deinococcus soli Cha et al. 2016. OC Bacteria; Deinococcus-Thermus; Deinococci; Deinococcales; OC Deinococcaceae; Deinococcus. OX NCBI_TaxID=1309411 {ECO:0000313|EMBL:AKH16650.1, ECO:0000313|Proteomes:UP000034024}; RN [1] {ECO:0000313|EMBL:AKH16650.1, ECO:0000313|Proteomes:UP000034024} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=N5 {ECO:0000313|EMBL:AKH16650.1, RC ECO:0000313|Proteomes:UP000034024}; RA Kim M.K., Srinivasan S., Lee J.-J.; RT "Deinococcus soli/N5/whole genome sequencing."; RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP011389; AKH16650.1; -; Genomic_DNA. DR RefSeq; WP_046843222.1; NZ_CP011389.1. DR EnsemblBacteria; AKH16650; AKH16650; SY84_05800. DR KEGG; dch:SY84_05800; -. DR PATRIC; fig|1309411.5.peg.1188; -. DR KO; K03665; -. DR Proteomes; UP000034024; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000034024}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}. FT DOMAIN 382 551 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 341 368 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 569 AA; 61885 MW; 339295175AF8F3B1 CRC64; MHGNTSGLRP AQMKALGNLY RRRIEPGRVG SPELARNLAE LSNDVRREVG VLIDRRGRVI SVSVADAKGT EFPDLRMGEN RLSGFHLLHT HPRGGALSKG DLSTLFLKRL DAVSAIEVRN EGQAGLVHTA HLTPPGTVGE EEDWRILPPV PAFQIDEFDL GAQVQALEEE IARAARTRVA KKDHERAILV QIDQGEFDAE DRLDELAELA RTAGAEVVHR ELVFRRNLKP GTLVGAGKLE ELTSRAYHLD ADLLIFGQEL GAAQAREIEA ATGLKIIDRT QLILDIFALH AQGVESRLQV ELAQLRYMKP RLLGAGAALS RIGGGGGSAG GGAIGTRGPG ETKLELDRRR INDRLSFLEK QLEGVAQRRE ERRKGRERNA VPVISIVGYT NAGKSTLLNA FTHAAEEPRR VLAENKLFAT LRPTSRQGYL EGIGPVVLTD TVGFIRDLPK DLTRAFRSTL EEIGDADVLL HVVDAASPGA DTRLDAVNRI LEDLGFRDMP TVVALNKADA ADPEALDREL ECTGGIAVSA LKNRGLAELK EALADAVSGV QRAELARQEE ARALAAQYR // ID A0A0F7JYB2_9GAMM Unreviewed; 428 AA. AC A0A0F7JYB2; DT 22-JUL-2015, integrated into UniProtKB/TrEMBL. DT 22-JUL-2015, sequence version 1. DT 07-JUN-2017, entry version 14. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=AAY24_05210 {ECO:0000313|EMBL:AKH19850.1}; OS Sedimenticola thiotaurini. OC Bacteria; Proteobacteria; Gammaproteobacteria; Sedimenticola. OX NCBI_TaxID=1543721 {ECO:0000313|EMBL:AKH19850.1, ECO:0000313|Proteomes:UP000034410}; RN [1] {ECO:0000313|EMBL:AKH19850.1, ECO:0000313|Proteomes:UP000034410} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SIP-G1 {ECO:0000313|EMBL:AKH19850.1, RC ECO:0000313|Proteomes:UP000034410}; RX PubMed=26089430; RA Flood B.E., Jones D.S., Bailey J.V.; RT "Complete Genome Sequence of Sedimenticola thiotaurini Strain SIP-G1, RT a Polyphosphate- and Polyhydroxyalkanoate-Accumulating Sulfur- RT Oxidizing Gammaproteobacterium Isolated from Salt Marsh Sediments."; RL Genome Announc. 3:e00671-15(2015). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP011412; AKH19850.1; -; Genomic_DNA. DR RefSeq; WP_046858786.1; NZ_CP011412.1. DR EnsemblBacteria; AKH19850; AKH19850; AAY24_05210. DR KEGG; seds:AAY24_05210; -. DR PATRIC; fig|1543721.4.peg.1079; -. DR KO; K03665; -. DR Proteomes; UP000034410; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000034410}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000034410}. FT DOMAIN 198 365 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 428 AA; 47966 MW; E74610C96691A47E CRC64; MFERPKIGEK AILVHVDMDA RADSDEIDEF RELVVSAGAM PVGMVTGSRR SPDPRLFIGS GKADEIRDLI RMEEAELVIF NHALSPSQER NLEREFQCRV VDRTGLILDI FAQRARSFEG KLQVELAQLR HLSTRLVRGW THLERQKGGI GLRGPGETQL ETDRRLLNHR IAQIRRRLEK VDSQRNQGRK ARSKAEIPTV SLVGYTNAGK STLFNRLTDA EVYAKDQLFA TLDPTLRRLD LPGEGACVVA DTVGFISNLP HALVAAFRST LQETSEASLL LHVIDAASPQ RAVCIAEVND VLKQIGADKI PQIEIYNKID LTETEGPRIE RDEDGLVKRI WLSALTGDGI DLLKQALAEF YHQEHVHKLL QLQPADGRLR ARLFELGGVI SETVTESGGW DMEIDLPRVA YERLLQQELV LESRLVGG // ID A0A0F7KBC2_9PROT Unreviewed; 447 AA. AC A0A0F7KBC2; DT 22-JUL-2015, integrated into UniProtKB/TrEMBL. DT 22-JUL-2015, sequence version 1. DT 07-JUN-2017, entry version 12. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=AAW31_07750 {ECO:0000313|EMBL:AKH37720.1}; OS Nitrosomonas communis. OC Bacteria; Proteobacteria; Betaproteobacteria; Nitrosomonadales; OC Nitrosomonadaceae; Nitrosomonas. OX NCBI_TaxID=44574 {ECO:0000313|EMBL:AKH37720.1, ECO:0000313|Proteomes:UP000034156}; RN [1] {ECO:0000313|Proteomes:UP000034156} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Nm2 {ECO:0000313|Proteomes:UP000034156}; RA Kozlowski J.A., Kits K.D., Stein L.Y.; RT "Draft genome of Nitrosomonas communis strain Nm2."; RL Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP011451; AKH37720.1; -; Genomic_DNA. DR RefSeq; WP_046849794.1; NZ_CP011451.1. DR EnsemblBacteria; AKH37720; AKH37720; AAW31_07750. DR KEGG; nco:AAW31_07750; -. DR PATRIC; fig|44574.3.peg.1881; -. DR KO; K03665; -. DR Proteomes; UP000034156; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000034156}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000034156}. FT DOMAIN 222 392 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 180 214 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 447 AA; 50046 MW; 21669373F3D0EE2C CRC64; MPIEVREKSR YAVVAAVQLP SVSDIEFEAS LSELRELAKT LGYEIINTFV QKRASFDTTA YLGFGKRQEI RRFVNSETES AEFEEIAANP KSRDIDAILV DHEISPSQAR NLEKEVGCEV MDRTMVILEI FHRNARSRAA RAQVEIARLG YMAPRLREAA KLAGPQGRQR SGVGGRGGGE SHTELDRRKI RDRIAELQQE IIAMDAERKT QRARRQTRQK LASVALVGYT NAGKSTLMRG LTGSEVLVAN KLFATLDTTV RALYPESMPR VLVSDTVGFI KNLPHGLVAS FKSTLDEALD ASLLLHVIDA SDPGFERQLE VTDQVLEEIG ADVVPRMRVF NKIDHVGDAT AQAKCEAVLR TQYPDCVVMS ARRPDEVAKL RQKIVAFFQQ DLVEAELFLP WSAQQLRGEI YASCQVLEER SNYEGVFFRV RGEPDSVKNL CEQFSQA // ID A0A0F7KEZ9_9PROT Unreviewed; 403 AA. AC A0A0F7KEZ9; DT 22-JUL-2015, integrated into UniProtKB/TrEMBL. DT 22-JUL-2015, sequence version 1. DT 07-JUN-2017, entry version 13. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=AAW31_05510 {ECO:0000313|EMBL:AKH37389.1}; OS Nitrosomonas communis. OC Bacteria; Proteobacteria; Betaproteobacteria; Nitrosomonadales; OC Nitrosomonadaceae; Nitrosomonas. OX NCBI_TaxID=44574 {ECO:0000313|EMBL:AKH37389.1, ECO:0000313|Proteomes:UP000034156}; RN [1] {ECO:0000313|Proteomes:UP000034156} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Nm2 {ECO:0000313|Proteomes:UP000034156}; RA Kozlowski J.A., Kits K.D., Stein L.Y.; RT "Draft genome of Nitrosomonas communis strain Nm2."; RL Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP011451; AKH37389.1; -; Genomic_DNA. DR RefSeq; WP_046849470.1; NZ_CP011451.1. DR EnsemblBacteria; AKH37389; AKH37389; AAW31_05510. DR KEGG; nco:AAW31_05510; -. DR PATRIC; fig|44574.3.peg.1325; -. DR KO; K03665; -. DR Proteomes; UP000034156; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000034156}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000034156}. FT DOMAIN 201 369 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 403 AA; 45050 MW; 4B0FC2C7E36B04A9 CRC64; MINHTELKAE KNNIAILVGL NLGDSDKESL EELRQLAISD QLIVLAVVEG KRSRPDPATF VGSGKLDEIY QVLSQTSASL VIFNHDLSPI QQRNLTERLQ CRVIDRTSLI LDIFAQRAKS REGKLQVELA QLEHLASRLV RGWTHLERQK GGIGLRGPGE TQLETDRRLL AKRVKFLREK LIKLQRQRGT QRRARQRTKV MSVSIVGYTN AGKSTLFNNL TRSQTYAADQ LFATLDTTTR KLFIPKCGEV VISDTVGFIR GLPHTLVAAF RATLEETVQA DMLLHVVDAA DPSRNEHIAE VNKLLKEIGA ESIPQILVFN KIDCAESSRT ANYVRDEYGR IMSIRLSAKT GDGLEFVKLA LAEAIAQNSV DLRESFLEVG KVNDSSATPF LEREEGLNYH GIK // ID A0A0F7KPX8_9SPHN Unreviewed; 424 AA. AC A0A0F7KPX8; DT 22-JUL-2015, integrated into UniProtKB/TrEMBL. DT 22-JUL-2015, sequence version 1. DT 07-JUN-2017, entry version 12. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:AKH41609.1}; GN ORFNames=WYH_00551 {ECO:0000313|EMBL:AKH41609.1}; OS Altererythrobacter atlanticus. OC Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales; OC Erythrobacteraceae; Altererythrobacter. OX NCBI_TaxID=1267766 {ECO:0000313|EMBL:AKH41609.1, ECO:0000313|Proteomes:UP000034392}; RN [1] {ECO:0000313|EMBL:AKH41609.1, ECO:0000313|Proteomes:UP000034392} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=26DY36 {ECO:0000313|EMBL:AKH41609.1, RC ECO:0000313|Proteomes:UP000034392}; RA Wu Y.-H., Cheng H., Wu X.-W.; RT "The complete genome of Altererythrobacter atlanticus strain 26DY36."; RL Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP011452; AKH41609.1; -; Genomic_DNA. DR EnsemblBacteria; AKH41609; AKH41609; WYH_00551. DR KEGG; aay:WYH_00551; -. DR PATRIC; fig|1267766.3.peg.557; -. DR KO; K03665; -. DR Proteomes; UP000034392; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000034392}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000034392}. FT DOMAIN 191 366 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 157 184 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 424 AA; 46602 MW; DCFCE4BD55C5D5B9 CRC64; MVCPDIRGQR QSQDPESRLE EAKGLAQAIG IVVAEAFILP VRDVRPGTLF GEGQIERIDS ACNLNEAELV IVDGALSAIQ QRNLEEKLKR KVIDRTGLIL EIFGERAATA EGRLQVELAH LDYQQSRLVR SWTHLERQRG GFGFLGGPGE TQIEADRRMI RARMGKLRRE LEQVRKTRAL HRARRGRAPW PVVALVGYTN AGKSTLFNRL TGSDVMAEDL LFATLDPTMR AIQLPGVEKA IISDTVGFIS DLPTQLVAAF RATLEEVTAA DIICHVRDMS NPDNAQQKAQ VLEVLSGLGV IEGEGSDPAM PIVELWNKWD LLDEDRAAEL KAIADSDPDI LPISAETGFG IEELRARLGA VLTAGARLHS IVVSASDGAR IAWLHAHGEV LAEEDAGEGE EGPLRRIDVR LTEKEWGRFE SLNS // ID A0A0F7M5B9_9GAMM Unreviewed; 431 AA. AC A0A0F7M5B9; DT 22-JUL-2015, integrated into UniProtKB/TrEMBL. DT 22-JUL-2015, sequence version 1. DT 30-AUG-2017, entry version 14. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=IMCC21906_03075 {ECO:0000313|EMBL:AKH70715.1}; OS Spongiibacter sp. IMCC21906. OC Bacteria; Proteobacteria; Gammaproteobacteria; Cellvibrionales; OC Spongiibacteraceae; Spongiibacter. OX NCBI_TaxID=1620392 {ECO:0000313|EMBL:AKH70715.1, ECO:0000313|Proteomes:UP000035013}; RN [1] {ECO:0000313|EMBL:AKH70715.1, ECO:0000313|Proteomes:UP000035013} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=IMCC21906 {ECO:0000313|EMBL:AKH70715.1, RC ECO:0000313|Proteomes:UP000035013}; RA Cho J.-C., Yang S.-J., Kang I.; RT "Complete genome sequence of IMCC21906 belonging to the RT Gammaproteobacteria."; RL Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP011477; AKH70715.1; -; Genomic_DNA. DR RefSeq; WP_047012862.1; NZ_CP011477.1. DR EnsemblBacteria; AKH70715; AKH70715; IMCC21906_03075. DR KEGG; spoi:IMCC21906_03075; -. DR PATRIC; fig|1620392.3.peg.3185; -. DR KO; K03665; -. DR Proteomes; UP000035013; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000035013}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000035013}. FT DOMAIN 199 365 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 165 192 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 431 AA; 48317 MW; 42CDC8719D7DC9F2 CRC64; MLFERPDSGE RAVLVHLDLN SEDEREDANE FVQLVTSAGG DPVAFITGKR QHPDSRLFVG SGKLEEIRSA LADNDGQLVL FNHALSPSQE RNVEQELKCR VLDRTGLILD IFAQRARTHE GKLQVELAQL EHMSTRLIRG WTHLERQKGG IGLRGPGETQ LETDRRLLRA RIKSIQARLQ KVRKQRDQAR RARRRADVPA VSLVGYTNAG KSTLFNTLTE SEVYAADQLF ATLDPTVRRI PITDVGPVVL ADTVGFIRHL PHKLVEAFRA TLEEAVQSDL LVHVVDAADP ERQENARQVM SVLTEIGADA IPMLEVYNKT DLMGVEPRID RDDEGKPIRV WLSARRQQGL QLLEQALTEL LCAEVVETDI RLSPKQGRLR AKLYNLNAVQ NEEADVNGGV KLHVRLPAVD WQRFLAAESV HEEDLLLGAD A // ID A0A0F7N9I9_9ACTN Unreviewed; 498 AA. AC A0A0F7N9I9; DT 22-JUL-2015, integrated into UniProtKB/TrEMBL. DT 22-JUL-2015, sequence version 1. DT 07-JUN-2017, entry version 12. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=AA958_26610 {ECO:0000313|EMBL:AKH85210.1}; OS Streptomyces sp. CNQ-509. OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae; OC Streptomyces. OX NCBI_TaxID=444103 {ECO:0000313|EMBL:AKH85210.1, ECO:0000313|Proteomes:UP000034283}; RN [1] {ECO:0000313|EMBL:AKH85210.1, ECO:0000313|Proteomes:UP000034283} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CNQ-509 {ECO:0000313|EMBL:AKH85210.1, RC ECO:0000313|Proteomes:UP000034283}; RA Ruckert C., Albersmeier A., Leipoldt F., Winkler A., Zeyhle P., RA Kalinowski J., Heide L., Kaysser L.; RT "Complete Genome Sequence of Streptomyces sp. CNQ-509, a Prolific RT Producer of Meroterpenoid Chemistry."; RL Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP011492; AKH85210.1; -; Genomic_DNA. DR RefSeq; WP_047018447.1; NZ_CP011492.1. DR EnsemblBacteria; AKH85210; AKH85210; AA958_26610. DR KEGG; strc:AA958_26610; -. DR PATRIC; fig|444103.5.peg.5599; -. DR KO; K03665; -. DR Proteomes; UP000034283; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000313|EMBL:AKH85210.1}; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000034283}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900, KW ECO:0000313|EMBL:AKH85210.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000034283}. FT DOMAIN 275 440 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 234 261 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 498 AA; 54001 MW; 02A612228F593B1E CRC64; MTSPTHLPQD DQRLPEGLRA DALMEAEAAW SAGSDADRDG DQFDREDRAA LRRVVGLSTE LEDVTEVEYR QLRLERVVLV GVWTSGTAQE AENSLAELAA LAETAGALVL DGVVQRREKP DPATYIGSGK ALELRDIVVE TAADTVVCDG ELSPGQLIHL EDVVKVKVVD RTALILDIFA QHAKSREGKA QVALAQMQYM LPRLRGWGQS LSRQMGGGGS GSAGGGMATR GPGETKIETD RRRIREKMAK LRREIADMKT GRDVKRQERK RHKVPSAAIA GYTNAGKSSL LNRLTGAGVL VENALFATLD PTVRRAETPS GRLYTLADTV GFVRHLPHHL VEAFRSTMEE VGDADLILHV VDGSHPAPEE QLVSVREVIR DVGATSVPEI VVINKADIAD PDVLRRLLRI EPRAIAVSAS TGEGIEELKA LIDVELPRPQ VEIEAVVPYT KGGLVSRVHD EGEVLVEEHI AAGTLLKALV HEELAAELRR YAPAGQAD // ID A0A0F7PIQ5_9RHIZ Unreviewed; 471 AA. AC A0A0F7PIQ5; DT 22-JUL-2015, integrated into UniProtKB/TrEMBL. DT 22-JUL-2015, sequence version 1. DT 07-JUN-2017, entry version 14. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=IMCC20628_01978 {ECO:0000313|EMBL:AKI00683.1}; OS Hoeflea sp. IMCC20628. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Phyllobacteriaceae; Hoeflea. OX NCBI_TaxID=1620421 {ECO:0000313|EMBL:AKI00683.1, ECO:0000313|Proteomes:UP000050665}; RN [1] {ECO:0000313|EMBL:AKI00683.1, ECO:0000313|Proteomes:UP000050665} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=IMCC20628 {ECO:0000313|EMBL:AKI00683.1, RC ECO:0000313|Proteomes:UP000050665}; RA Cho J.-C., Yang S.-J., Kang I.; RT "Complete genome sequence of IMCC20628 belonging to the RT Alphaproteobacteria."; RL Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP011479; AKI00683.1; -; Genomic_DNA. DR EnsemblBacteria; AKI00683; AKI00683; IMCC20628_01978. DR KEGG; hoe:IMCC20628_01978; -. DR PATRIC; fig|1620421.3.peg.2045; -. DR KO; K03665; -. DR Proteomes; UP000050665; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000050665}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000050665}. FT DOMAIN 235 406 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 194 228 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 471 AA; 51861 MW; F3823F09BF488897 CRC64; MRTPQPAPDR TTHIETVDST GNFTDADSKS GVTSAIVLIP TLRTRNAAPG SGEVVKRPDT HRMEEAIGLA GAIDLKVAEA LIIPVSTPRP STLFGKGKML EILALIESSG ADLVIVDHPL TPVQQRNLEE QWKLKVIDRT GLILEIFGRR ASTKEGVLQV ELAHLNYQKG RLVRSWTHLE RQRGGGGFMG GPGETQIEAD RRQLQERIIK LERELDQVRR TRQLHRAKRK KVPHPIVALV GYTNAGKSTL FNRLTGAEVL AEDMLFATLD PTLRRMKLPH GKMVILSDTV GFISSLPTHL VAAFRATLEE VIEADLILHV RDMADPDRSA QAKDVEAILK SLGVGEVAEQ KLVEVWNKID LLPEDAAADL KVRAENSENA IAVSSITGEG IDVLLTRIES VISGKLVSRK INIAPDQMTL VPWIYQRGRV SGREDMEDGS VLIEAEFTGA DSDELDRRMG NGPKPDDDFL E // ID A0A0F9Z311_9BACT Unreviewed; 168 AA. AC A0A0F9Z311; DT 22-JUL-2015, integrated into UniProtKB/TrEMBL. DT 22-JUL-2015, sequence version 1. DT 07-JUN-2017, entry version 9. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:KKP33066.1}; GN ORFNames=UR23_C0050G0009 {ECO:0000313|EMBL:KKP33066.1}; OS Candidatus Roizmanbacteria bacterium GW2011_GWA2_32_13. OC Bacteria; Candidatus Roizmanbacteria. OX NCBI_TaxID=1618475 {ECO:0000313|EMBL:KKP33066.1, ECO:0000313|Proteomes:UP000034349}; RN [1] {ECO:0000313|EMBL:KKP33066.1, ECO:0000313|Proteomes:UP000034349} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A., RA Wilkins M.J., Williams K.H., Banfield J.F.; RT "rRNA introns, odd ribosomes, and small enigmatic genomes across a RT large radiation of phyla."; RL Nature 0:0-0(2015). CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KKP33066.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LBOK01000050; KKP33066.1; -; Genomic_DNA. DR EnsemblBacteria; KKP33066; KKP33066; UR23_C0050G0009. DR PATRIC; fig|1618475.3.peg.540; -. DR Proteomes; UP000034349; Unassembled WGS sequence. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000034349}; KW Reference proteome {ECO:0000313|Proteomes:UP000034349}. FT DOMAIN 25 115 GTP-bdg_N. {ECO:0000259|Pfam:PF13167}. FT DOMAIN 118 168 GTP-bdg_M. {ECO:0000259|Pfam:PF16360}. SQ SEQUENCE 168 AA; 18984 MW; 2AB23D34143BC112 CRC64; MPKLKKVVIV DIVNPYQKIE EAIKNLEEIK SLVSTYHGID VVDVIQHRSR PDKATFIGKG KVEELVGIVN KQKIDIVVVN AIVNPSVLFN LTQFLWNDNP EIQVWDRFDL ILNIFDKHAH TAEAKLQIEL AKMHHMGPRI YGLGENYFSR QGGGGTNTKG QGETNIEI // ID A0A0G0AA00_9BACT Unreviewed; 369 AA. AC A0A0G0AA00; DT 22-JUL-2015, integrated into UniProtKB/TrEMBL. DT 22-JUL-2015, sequence version 1. DT 07-JUN-2017, entry version 13. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=UR43_C0004G0200 {ECO:0000313|EMBL:KKP53659.1}; OS candidate division TM6 bacterium GW2011_GWF2_33_332. OC Bacteria; Candidatus Dependentiae. OX NCBI_TaxID=1619080 {ECO:0000313|EMBL:KKP53659.1, ECO:0000313|Proteomes:UP000034634}; RN [1] {ECO:0000313|EMBL:KKP53659.1, ECO:0000313|Proteomes:UP000034634} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A., RA Wilkins M.J., Williams K.H., Banfield J.F.; RT "rRNA introns, odd ribosomes, and small enigmatic genomes across a RT large radiation of phyla."; RL Nature 0:0-0(2015). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KKP53659.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LBPE01000004; KKP53659.1; -; Genomic_DNA. DR EnsemblBacteria; KKP53659; KKP53659; UR43_C0004G0200. DR PATRIC; fig|1619080.3.peg.686; -. DR Proteomes; UP000034634; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000034634}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000034634}. FT DOMAIN 205 369 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 369 AA; 42367 MW; 504A5A2D27F987AB CRC64; MAKKSISIED IRPKILLLGI YTPQNKFRDM EAYFEEFVSL VETLGAVYDE KLFIKLRNID PSYFLTTGKI EEVTAFCEEH KIDEIICSES LSALQERNLT DAFGCVISDR ARLILEIFKN SAHSAEGKTQ VEIAELEYLK TRMSGRGIDM AQQAGFIGSR GPGETVKEAI RRTYATKIRQ AQKRLHILEK SRDEQRKRRL QSNIPLVSLI GYTNSGKSSI LNRLTKSNVL VENKLFATLD TTTKIYYPSP QKKILLSDTV GFISELPHHL IESFKSTLDE LKYSDLLLIV VDISNNIWKD QIEVVRDTLH SLKIEKPYIF VFNKIDKIAN IEEIKPDLEE FKPYILTSVK PKDGLNDLVT YLKDFEFKK // ID A0A0G0AD29_9BACT Unreviewed; 377 AA. AC A0A0G0AD29; DT 22-JUL-2015, integrated into UniProtKB/TrEMBL. DT 22-JUL-2015, sequence version 1. DT 07-JUN-2017, entry version 13. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=SZ59_C0001G0118 {ECO:0000313|EMBL:KKP24800.1}; OS candidate division TM6 bacterium GW2011_GWF2_28_16. OC Bacteria; Candidatus Dependentiae. OX NCBI_TaxID=1619077 {ECO:0000313|EMBL:KKP24800.1, ECO:0000313|Proteomes:UP000033842}; RN [1] {ECO:0000313|EMBL:KKP24800.1, ECO:0000313|Proteomes:UP000033842} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A., RA Wilkins M.J., Williams K.H., Banfield J.F.; RT "rRNA introns, odd ribosomes, and small enigmatic genomes across a RT large radiation of phyla."; RL Nature 0:0-0(2015). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KKP24800.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LBNX01000001; KKP24800.1; -; Genomic_DNA. DR EnsemblBacteria; KKP24800; KKP24800; SZ59_C0001G0118. DR PATRIC; fig|1619077.4.peg.119; -. DR Proteomes; UP000033842; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000033842}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000033842}. FT DOMAIN 211 377 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 377 AA; 43290 MW; 9F944242086BC383 CRC64; MTREKIMTRK ATPTDTPELT TLLIGVDAPY NQMRPIQEYY DEFLSLAQTM NLKYEHSLFI KIRTIDKGLF FTKGKLLDLK KFCDENNIEE VIVSEILTPL QERNLEDYLN CTVWDREKLI LEIFKKSAIT AEGRIQVEMA EIDFLKSRLS GKGIDFAQQE GMIGGKGPGE TAKEALKQYF AIQYTRAKKR LETLKQSREV QRKKRLESNL PLISLVGYTN AGKSSLLNVL TKSQVLVEDK LFATLDITTK ELYLENKKIG LVSDTVGFIS QLPHHLIEAF KSTLDELKYA SLLLHVIDIS NNTWQDQIKV VNNTLKELGI DKPILHVFNK IDKLTEQELS LIKLETGDFE QKVFIHTKDK SGIKELTNFL SKYNFKS // ID A0A0G0AT29_9BACT Unreviewed; 453 AA. AC A0A0G0AT29; DT 22-JUL-2015, integrated into UniProtKB/TrEMBL. DT 22-JUL-2015, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=UR12_C0001G0015 {ECO:0000313|EMBL:KKP29880.1}; OS candidate division TM6 bacterium GW2011_GWF2_30_66. OC Bacteria; Candidatus Dependentiae. OX NCBI_TaxID=1619078 {ECO:0000313|EMBL:KKP29880.1, ECO:0000313|Proteomes:UP000034862}; RN [1] {ECO:0000313|EMBL:KKP29880.1, ECO:0000313|Proteomes:UP000034862} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A., RA Wilkins M.J., Williams K.H., Banfield J.F.; RT "rRNA introns, odd ribosomes, and small enigmatic genomes across a RT large radiation of phyla."; RL Nature 0:0-0(2015). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KKP29880.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LBOA01000001; KKP29880.1; -; Genomic_DNA. DR EnsemblBacteria; KKP29880; KKP29880; UR12_C0001G0015. DR PATRIC; fig|1619078.3.peg.15; -. DR Proteomes; UP000034862; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 2. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000034862}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000034862}. FT DOMAIN 207 332 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 453 AA; 51930 MW; AE9546E996BB05E7 CRC64; MKHSKAPVST SIMPKTLLIG VEAPYNKIRN FESYYEEFEN LARSNNITEY DIVTVKLREI NPSYFVGTGK LDEIKDYCVN NKIKQVIISE TLSAQQQRNL SDYIYCNVFD RTQLILDIFE KNAHSAEGKI QVEIAMLRHK KTRLAGKGID MSQQTGISGA IAGSGETAKE KETRVLDEKI TTLRRKLVHL EKIRDTQRKT RFKNNVPHIC LIGYTNTGKS TLLNILTKSH VLAEDKLFAT LDTATKELYV DGEKKGIISD SVGFIQNLPH NLIEAFKSTL EELQYADLLL QVVDISDPNW EFHIKVVKEI LDELEVKKDM LYVFNKIDKI SGKKSSSKSE TCDNTCAECE CDIEDCICEQ EFWEKECTES ECENECDEAT AEQYDNKQER DQDLDKTPEI SVKKDKNPTF TFEQTLEQIK KYEPNVIISA KSKTGIKPLL DYLKAWKKKE LIK // ID A0A0G0BAI2_9BACT Unreviewed; 367 AA. AC A0A0G0BAI2; DT 22-JUL-2015, integrated into UniProtKB/TrEMBL. DT 22-JUL-2015, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=UR26_C0002G0095 {ECO:0000313|EMBL:KKP35795.1}; OS candidate division TM6 bacterium GW2011_GWF2_32_72. OC Bacteria; Candidatus Dependentiae. OX NCBI_TaxID=1619079 {ECO:0000313|EMBL:KKP35795.1, ECO:0000313|Proteomes:UP000034766}; RN [1] {ECO:0000313|EMBL:KKP35795.1, ECO:0000313|Proteomes:UP000034766} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A., RA Wilkins M.J., Williams K.H., Banfield J.F.; RT "rRNA introns, odd ribosomes, and small enigmatic genomes across a RT large radiation of phyla."; RL Nature 0:0-0(2015). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KKP35795.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LBON01000002; KKP35795.1; -; Genomic_DNA. DR EnsemblBacteria; KKP35795; KKP35795; UR26_C0002G0095. DR PATRIC; fig|1619079.3.peg.342; -. DR Proteomes; UP000034766; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000034766}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000034766}. FT DOMAIN 205 367 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 367 AA; 41853 MW; BBA6297EFE73A002 CRC64; MAKKLYYEDV KPKVLIIGVQ TPDNRTSNIE AYYDEFKNLL KTNDVVYEEE LYIKLREIDK VTFLTKGKLQ EVKDFCEKNQ IEEVVFSEIL TPLQERNLRD FLECNVADRT QLILEIFEKA AHTAEGKLQV ELATLQHKKT RLAGKGVHMS QQGGGIGVKG GSGETEKERE TRYIEEAILR LKKHLEKIQT SRATQRKQRL GAGIPQICLI GYTNAGKSTI LNALAKSDVL AKDQLFATLD TTTRELFISG KKKGVLSDTV GFIQNLPPKL IEAFKSTLSE LLYADLLLQV IDLSDPNFEN HIRVVNAILK DLEVEKNMLY VFNKADRVEN LEEREILIEK YEPHVVISSL SKDGLKPLID FLDKWEK // ID A0A0G0E869_9BACT Unreviewed; 371 AA. AC A0A0G0E869; DT 22-JUL-2015, integrated into UniProtKB/TrEMBL. DT 22-JUL-2015, sequence version 1. DT 07-JUN-2017, entry version 14. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=UR68_C0033G0007 {ECO:0000313|EMBL:KKP71535.1}; OS Candidatus Roizmanbacteria bacterium GW2011_GWA2_35_19. OC Bacteria; Candidatus Roizmanbacteria. OX NCBI_TaxID=1618478 {ECO:0000313|EMBL:KKP71535.1, ECO:0000313|Proteomes:UP000034457}; RN [1] {ECO:0000313|EMBL:KKP71535.1, ECO:0000313|Proteomes:UP000034457} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A., RA Wilkins M.J., Williams K.H., Banfield J.F.; RT "rRNA introns, odd ribosomes, and small enigmatic genomes across a RT large radiation of phyla."; RL Nature 0:0-0(2015). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KKP71535.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LBQC01000033; KKP71535.1; -; Genomic_DNA. DR EnsemblBacteria; KKP71535; KKP71535; UR68_C0033G0007. DR PATRIC; fig|1618478.3.peg.1009; -. DR Proteomes; UP000034457; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000034457}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000034457}. FT DOMAIN 202 371 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 371 AA; 42293 MW; 4A250B172C13F4E2 CRC64; MKKHRVVLVD TVDPRHTKEE AIKNLHELRS LVSTYNGIDV VDIIQHRNRP DKATFIGSGK VDELIQVVEN KRINIVVVNA IVNPSILFNL TKKLWDVNLE IQVWDRVDLI LNIFDKHAVT TEAKLQIEIA RMHHMGPRIY GLGEGYFSRQ GGGLNTKGQG ETNIELMKRH WREQIKAKKE QLEKISAQHL TQLERRKNNN VPSISIVGYT NAGKTSLFNL LSKKKKDVEN ALFVTLDSVT SKLYFPSQKM EATVSDTIGF IKDLPSSLIE SFKSTLIESV HADLLLHVID ISDPEMNEKI FVVEQILKEL QVKAKKTIYV FNKIDAFKGD AEKILKDVKD QYSQFSPVFI SVTTNYGIEK LKTEVEKALF S // ID A0A0G0F1F0_9BACT Unreviewed; 307 AA. AC A0A0G0F1F0; DT 22-JUL-2015, integrated into UniProtKB/TrEMBL. DT 22-JUL-2015, sequence version 1. DT 12-APR-2017, entry version 8. DE SubName: Full=GTPase HflX {ECO:0000313|EMBL:KKQ11597.1}; DE Flags: Fragment; GN ORFNames=US22_C0020G0001 {ECO:0000313|EMBL:KKQ11597.1}; OS candidate division TM6 bacterium GW2011_GWF2_36_6. OC Bacteria; Candidatus Dependentiae. OX NCBI_TaxID=1619082 {ECO:0000313|EMBL:KKQ11597.1, ECO:0000313|Proteomes:UP000034938}; RN [1] {ECO:0000313|EMBL:KKQ11597.1, ECO:0000313|Proteomes:UP000034938} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A., RA Wilkins M.J., Williams K.H., Banfield J.F.; RT "rRNA introns, odd ribosomes, and small enigmatic genomes across a RT large radiation of phyla."; RL Nature 0:0-0(2015). CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KKQ11597.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LBSD01000020; KKQ11597.1; -; Genomic_DNA. DR EnsemblBacteria; KKQ11597; KKQ11597; US22_C0020G0001. DR Proteomes; UP000034938; Unassembled WGS sequence. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR CDD; cd01878; HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 4: Predicted; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000034938}; KW Reference proteome {ECO:0000313|Proteomes:UP000034938}. FT DOMAIN 206 307 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 172 199 {ECO:0000256|SAM:Coils}. FT NON_TER 307 307 {ECO:0000313|EMBL:KKQ11597.1}. SQ SEQUENCE 307 AA; 34859 MW; 474FD72DC7E4E792 CRC64; MAKRVSVAIQ DIHPKTLAVG VYTPYVKISS AENYYEEFLS LIKTLGMHYD ETYFIKVRAV DTNTFFTKGK LEELKLICDQ KQIEVIIFSE TLNPLQERNL EDALDCSIMD REQLILEIFK KSAHTAEGKI QVEMAEVQFL KTRIIGKGVE YSQQLGVIGT KGPGETATEK MRQVFADKLR QAKQKLETLQ KARDNQRKRR LSSNIPNLCI VGYTNSGKSS LLNNLTKSTI LAEDKLFATL DTTTREFYIG GKTKILISDT VGFISQLPHK LVEAFRSTLD ELKYASLLLH VVDLSNLEWR SQINVVN // ID A0A0G0GPZ1_9BACT Unreviewed; 370 AA. AC A0A0G0GPZ1; DT 22-JUL-2015, integrated into UniProtKB/TrEMBL. DT 22-JUL-2015, sequence version 1. DT 07-JUN-2017, entry version 12. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=US49_C0002G0028 {ECO:0000313|EMBL:KKQ33133.1}; OS candidate division TM6 bacterium GW2011_GWF2_37_49. OC Bacteria; Candidatus Dependentiae. OX NCBI_TaxID=1619083 {ECO:0000313|EMBL:KKQ33133.1, ECO:0000313|Proteomes:UP000033926}; RN [1] {ECO:0000313|EMBL:KKQ33133.1, ECO:0000313|Proteomes:UP000033926} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A., RA Wilkins M.J., Williams K.H., Banfield J.F.; RT "rRNA introns, odd ribosomes, and small enigmatic genomes across a RT large radiation of phyla."; RL Nature 0:0-0(2015). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KKQ33133.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LBTE01000002; KKQ33133.1; -; Genomic_DNA. DR EnsemblBacteria; KKQ33133; KKQ33133; US49_C0002G0028. DR PATRIC; fig|1619083.3.peg.405; -. DR Proteomes; UP000033926; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000033926}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000033926}. FT DOMAIN 206 370 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 370 AA; 42260 MW; D05FAE5993FE622D CRC64; MSKKAAKAFS EMHPKTLALG IYTPFVKIAS PENYYVEFLS LIDTLGLPYD ETYYTKVRAV DPNTFFTKGK MSEVQQVVEQ GTFEFVIISE SLSPLQQRNL EDVFNCEIMG REHLILEIFK KSAHSAEGKI QVEMAEVEFL KTRVIGRDRN YAQQLGVIGT IGPGETATEK MRRVFADKLR QSKQRLDTLQ KARDNQRKKR MSSNLPQVCI VGYTNAGKSS LLNRLTKSTA LVEDKLFATL DTTTREFFVD SNRKILISDT VGFISNLPHN LIEAFKSTLN ELKYADLLMH VVDVSNPEWR GQIEIVQDTL KEIDVEKPVL YVFNKVDLMN TGMIELMMHE FNDYLPHVFV STKSKEGVKP LVNFLSKYKV // ID A0A0G0HDD0_9BACT Unreviewed; 367 AA. AC A0A0G0HDD0; DT 22-JUL-2015, integrated into UniProtKB/TrEMBL. DT 22-JUL-2015, sequence version 1. DT 07-JUN-2017, entry version 11. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:KKQ01946.1}; GN ORFNames=US11_C0002G0005 {ECO:0000313|EMBL:KKQ01946.1}; OS Candidatus Roizmanbacteria bacterium GW2011_GWA2_36_23. OC Bacteria; Candidatus Roizmanbacteria. OX NCBI_TaxID=1618480 {ECO:0000313|EMBL:KKQ01946.1, ECO:0000313|Proteomes:UP000034344}; RN [1] {ECO:0000313|EMBL:KKQ01946.1, ECO:0000313|Proteomes:UP000034344} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A., RA Wilkins M.J., Williams K.H., Banfield J.F.; RT "rRNA introns, odd ribosomes, and small enigmatic genomes across a RT large radiation of phyla."; RL Nature 0:0-0(2015). CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KKQ01946.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LBRS01000002; KKQ01946.1; -; Genomic_DNA. DR EnsemblBacteria; KKQ01946; KKQ01946; US11_C0002G0005. DR PATRIC; fig|1618480.3.peg.192; -. DR Proteomes; UP000034344; Unassembled WGS sequence. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR CDD; cd01878; HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000034344}; KW Reference proteome {ECO:0000313|Proteomes:UP000034344}. FT DOMAIN 204 367 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 367 AA; 41503 MW; B91B0106007D43F0 CRC64; MTQNQFNSLA IKVIGPHDHS SDELQKFREI ESLVSVLGGK IIVKQIQHRL FPDESTYIGK GKIEEIKDLI RYSHIRVIIL NDIVNPAQIF RLEKSLWSTD PNIKVWDRAD VILEIFDKRA HSSEAKLQIE LARMKHLGPR IYGLGGGLLS RQGGGIGMRG LGETNIEIMK RQIKDKLRLT EEKLKKIIHS RQEKMLYRKK GGYKTIALVG YTNAGKTTLF NNLTGKTKKV ENAVFTTLDS YVGKLNHQTN KPILISDTIG FIQDLPPSLI QAFKSTLLET LTADLIYHVI DSSDSEIERK IEMVNEILAE FNIESNKVVY IFNKIDTISD SKRQLLNRLY PGKSLFVSSA SGEGINSMLS SIHTIFP // ID A0A0G0I2X2_9BACT Unreviewed; 391 AA. AC A0A0G0I2X2; DT 22-JUL-2015, integrated into UniProtKB/TrEMBL. DT 22-JUL-2015, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=US69_C0003G0013 {ECO:0000313|EMBL:KKQ49658.1}; OS candidate division TM6 bacterium GW2011_GWF2_38_10. OC Bacteria; Candidatus Dependentiae. OX NCBI_TaxID=1619084 {ECO:0000313|EMBL:KKQ49658.1, ECO:0000313|Proteomes:UP000034625}; RN [1] {ECO:0000313|EMBL:KKQ49658.1, ECO:0000313|Proteomes:UP000034625} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A., RA Wilkins M.J., Williams K.H., Banfield J.F.; RT "rRNA introns, odd ribosomes, and small enigmatic genomes across a RT large radiation of phyla."; RL Nature 0:0-0(2015). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KKQ49658.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LBTY01000003; KKQ49658.1; -; Genomic_DNA. DR EnsemblBacteria; KKQ49658; KKQ49658; US69_C0003G0013. DR PATRIC; fig|1619084.3.peg.199; -. DR Proteomes; UP000034625; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000034625}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000034625}. FT DOMAIN 227 391 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 193 220 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 391 AA; 44728 MW; A696D1E4A7A93F6D CRC64; MLATIYWKKF IELIEFLPVR IVVKNKPIEQ RYEHPKTLLL GVFAPGNKMG SAEYYFEEFL NLVKTADIPY DDTFFMKVRA TDNNMYFTKG KLEELSQKCQ ELGVDILVVS ELLHPLQERN LENVLNCRII DREQLILTIF KQSAHTSEGK IQIEMADIEF MKTRMSGRGR ELAQQSGIIG TRGPGETEKE ELKRVFADKL RQAQKKLETL ERARSVQRKQ RLESNQPLLC IIGYTNAGKS TLLNAIAKGN VLSEDKLFAT LDTTTRELFI DGKKKGLISD TVGFISQLPH HLISAFKSTL DELKYADLLL HVVDASCPAW ENQIAVVHEM LQELGVNKPM LYVFNKIDKL THEQREAQIA KLILYTPHVL VSALTKDGLT PLIDYLRTYQ L // ID A0A0G0ISG0_9BACT Unreviewed; 377 AA. AC A0A0G0ISG0; DT 22-JUL-2015, integrated into UniProtKB/TrEMBL. DT 22-JUL-2015, sequence version 1. DT 07-JUN-2017, entry version 12. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=US32_C0019G0004 {ECO:0000313|EMBL:KKQ18961.1}; OS candidate division TM6 bacterium GW2011_GWA2_36_9. OC Bacteria; Candidatus Dependentiae. OX NCBI_TaxID=1619072 {ECO:0000313|EMBL:KKQ18961.1, ECO:0000313|Proteomes:UP000034219}; RN [1] {ECO:0000313|EMBL:KKQ18961.1, ECO:0000313|Proteomes:UP000034219} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A., RA Wilkins M.J., Williams K.H., Banfield J.F.; RT "rRNA introns, odd ribosomes, and small enigmatic genomes across a RT large radiation of phyla."; RL Nature 0:0-0(2015). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KKQ18961.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LBSN01000019; KKQ18961.1; -; Genomic_DNA. DR EnsemblBacteria; KKQ18961; KKQ18961; US32_C0019G0004. DR PATRIC; fig|1619072.4.peg.921; -. DR Proteomes; UP000034219; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000034219}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000034219}. FT DOMAIN 208 376 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 174 201 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 377 AA; 42874 MW; 1869913651B22269 CRC64; MTKPQNIETI AHVPTLIIGI QAPYNDTENI DAYYDEFKNL LKTNGTTFDA EHFIKIREIN QKTFITPGKL EEIRKLCEKH AIEEVYISEP ITTLQAKHLE DYLNCKVFDR TDLILEIFKK AAQTAEGKTQ VAIATLEHAK TRLAGKGIFL EQQRGGGGAG TKGGPGETLK EREKRVINAK IQQLRKQLET LHRARETQRK KRIAAHVPQI CLIGYTNAGK STILNTLTKA QVLAENKLFA TLDTTTRELY INGIKKGVLS DTVGFIQYLP HKLIDAFKST LSELQYADLL LEVVDASDPD WKAHIDVVQD ILDDLEVEKP ILYVFNKIDK CSEEIKQRLE DDAQKYQPYV IISAKERETM KPLIDFLDQW KVEKLPS // ID A0A0G0Q1R2_9BACT Unreviewed; 330 AA. AC A0A0G0Q1R2; DT 22-JUL-2015, integrated into UniProtKB/TrEMBL. DT 22-JUL-2015, sequence version 1. DT 07-JUN-2017, entry version 11. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:KKR34073.1}; DE Flags: Fragment; GN ORFNames=UT63_C0007G0028 {ECO:0000313|EMBL:KKR34073.1}; OS Candidatus Gottesmanbacteria bacterium GW2011_GWC2_39_8. OC Bacteria; Candidatus Gottesmanbacteria. OX NCBI_TaxID=1618450 {ECO:0000313|EMBL:KKR34073.1, ECO:0000313|Proteomes:UP000034539}; RN [1] {ECO:0000313|EMBL:KKR34073.1, ECO:0000313|Proteomes:UP000034539} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A., RA Wilkins M.J., Williams K.H., Banfield J.F.; RT "rRNA introns, odd ribosomes, and small enigmatic genomes across a RT large radiation of phyla."; RL Nature 0:0-0(2015). CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KKR34073.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LBXN01000007; KKR34073.1; -; Genomic_DNA. DR EnsemblBacteria; KKR34073; KKR34073; UT63_C0007G0028. DR PATRIC; fig|1618450.3.peg.250; -. DR Proteomes; UP000034539; Unassembled WGS sequence. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR CDD; cd01878; HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 4: Predicted; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000034539}; KW Reference proteome {ECO:0000313|Proteomes:UP000034539}. FT DOMAIN 162 330 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 128 155 {ECO:0000256|SAM:Coils}. FT NON_TER 1 1 {ECO:0000313|EMBL:KKR34073.1}. SQ SEQUENCE 330 AA; 37321 MW; AE0DE4B1CA8DBF0F CRC64; YAASAQNANR GSRATYIGKG KVEEISETIV RENIDIIVIN GQAKPQQIHN LKIYLGKFKP KIVVWDKVEL ILQIFSKHAA TSEAKLQIKI AAMKHMGPRI YGMGFIMSQQ GGGIGTKGIG ETNTELMRRH WRNEMRQVQN ELEKQTDNRE RQMENRKKTG FQTVSLIGYT NSGKTTLFNS LTGSHNLVEN ALFATLDSNV NKLFLKEINK EIYLTDTIGF IQDLPPDLID AFRSTLMETI HADLLLHVID ITDPRMTDKI TVVENILRDL GIDNKNQIYV FNKIDITNGV NQDDLISQFG SFHPEFISAE KGKNLESLLE QIQILLSHPV // ID A0A0G0RZZ7_9BACT Unreviewed; 374 AA. AC A0A0G0RZZ7; DT 22-JUL-2015, integrated into UniProtKB/TrEMBL. DT 22-JUL-2015, sequence version 1. DT 07-JUN-2017, entry version 14. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=UT94_C0002G0001 {ECO:0000313|EMBL:KKR58213.1}; OS Candidatus Uhrbacteria bacterium GW2011_GWF2_40_263. OC Bacteria; Candidatus Uhrbacteria. OX NCBI_TaxID=1618996 {ECO:0000313|EMBL:KKR58213.1, ECO:0000313|Proteomes:UP000034197}; RN [1] {ECO:0000313|EMBL:KKR58213.1, ECO:0000313|Proteomes:UP000034197} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A., RA Wilkins M.J., Williams K.H., Banfield J.F.; RT "rRNA introns, odd ribosomes, and small enigmatic genomes across a RT large radiation of phyla."; RL Nature 0:0-0(2015). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KKR58213.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LBYS01000002; KKR58213.1; -; Genomic_DNA. DR EnsemblBacteria; KKR58213; KKR58213; UT94_C0002G0001. DR PATRIC; fig|1618996.3.peg.53; -. DR Proteomes; UP000034197; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000034197}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000034197}. FT DOMAIN 208 374 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 170 197 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 374 AA; 42651 MW; F3EABECDB1C21C01 CRC64; MLRSLRHSMQ EKQKAILIDL IHPRMNKEQS LDRLLELEEL VNTYGGIVVV KEYQRRFAPH PKTFIGPGKV HELAQEGKML GVSLVIINDI LKPRQIFEIG EQLREAKIQV WDRVDLILKI FAKHAKTTEA RLEIELASIR HMGPRIFGMG MELSRQGGGI GTSGIGETNT EIMRRHLKEK ERKIKEKLEK YQNVREGHRQ SRKRKGLKTV SLVGYTNAGK TTLLNVLTGR KEYVANALFA TLDTRVGSLW LPGRQETVLV SDTIGFIKEL PPELLNAFSS TLSEAIDADL LIQVLDVSDP HWLQHMCVVE EILERLNIEE KPRLLVCHKA DQVSPKAKKE IEQHLSMLPL WVSSVKHTGL EELTIAIEKI LFEK // ID A0A0G0V8Q3_9BACT Unreviewed; 376 AA. AC A0A0G0V8Q3; DT 22-JUL-2015, integrated into UniProtKB/TrEMBL. DT 22-JUL-2015, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=UU47_C0001G0107 {ECO:0000313|EMBL:KKR97334.1}; OS candidate division TM6 bacterium GW2011_GWE2_41_16. OC Bacteria; Candidatus Dependentiae. OX NCBI_TaxID=1619075 {ECO:0000313|EMBL:KKR97334.1, ECO:0000313|Proteomes:UP000034748}; RN [1] {ECO:0000313|EMBL:KKR97334.1, ECO:0000313|Proteomes:UP000034748} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A., RA Wilkins M.J., Williams K.H., Banfield J.F.; RT "rRNA introns, odd ribosomes, and small enigmatic genomes across a RT large radiation of phyla."; RL Nature 0:0-0(2015). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KKR97334.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LCAT01000001; KKR97334.1; -; Genomic_DNA. DR EnsemblBacteria; KKR97334; KKR97334; UU47_C0001G0107. DR PATRIC; fig|1619075.3.peg.112; -. DR Proteomes; UP000034748; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000034748}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000034748}. FT DOMAIN 204 376 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 376 AA; 42680 MW; D437BF9A2882B7CA CRC64; MTRETFSTRI NPKALIVGIQ TPENYSIDIE SYFEEFRNLV ETNGIVYDHE VYMKLRSIEP STFITKGKLT ELICLCEKEN IEEVVFSEVL NTQQVKNLKK LLKVSVFDRT ELILEIFEKN ALSAEGKLQV ELAWLQHKKA RLAGRGIGMS QQAGHIGGRG PGETQKEKET QHIELHILKI KKNLERLSQV RATQRKQRLG TSTPRFCIIG YTNAGKSSLL NALTKSDVLA ENKLFATLDT TTRELFIDGK KKALISDTVG FIQQLPHSLI EAFKSTLDEL VYAHLLIHVV DSSNKNWQQH IRVVTTLLKE MGLEQKPLFT VFNKIDLLSE EEKQKLLVQA QEHAPFCLAS TLSDAGLQDL LSYLSSWTMP QESSHE // ID A0A0G1B5M7_9BACT Unreviewed; 369 AA. AC A0A0G1B5M7; DT 22-JUL-2015, integrated into UniProtKB/TrEMBL. DT 22-JUL-2015, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=UV38_C0001G0206 {ECO:0000313|EMBL:KKS68665.1}; OS candidate division TM6 bacterium GW2011_GWE2_42_60. OC Bacteria; Candidatus Dependentiae. OX NCBI_TaxID=1619076 {ECO:0000313|EMBL:KKS68665.1, ECO:0000313|Proteomes:UP000034453}; RN [1] {ECO:0000313|EMBL:KKS68665.1, ECO:0000313|Proteomes:UP000034453} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A., RA Wilkins M.J., Williams K.H., Banfield J.F.; RT "rRNA introns, odd ribosomes, and small enigmatic genomes across a RT large radiation of phyla."; RL Nature 0:0-0(2015). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KKS68665.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LCEG01000001; KKS68665.1; -; Genomic_DNA. DR EnsemblBacteria; KKS68665; KKS68665; UV38_C0001G0206. DR PATRIC; fig|1619076.3.peg.221; -. DR Proteomes; UP000034453; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000034453}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000034453}. FT DOMAIN 205 369 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 164 198 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 369 AA; 41357 MW; 69823F49D71B198B CRC64; MKELISTSTM DEHPILIIGV QTPQNRSIDS QSYLQEFRNL VLSSGITKYE EYTTKLRSVD SSYFFTQGKL EEIIALCTKH HIEEVVISEP LTPQQERNLD ELLSTPIVDR TALILRIFER GAQTAEGKMQ VEMAFLHHKK TRLAGKGISL SQQGGNKGAK GPGETKKEIE ARHLERQINK LTADLVQLQK VRETQRKRRT TLGIPHVSII GYTNAGKSTL LNAITKSTVL AENKLFATLD TTTRELFVGG LKRGTISDTV GFIQNLPHEL IEAFKSTLID LQYASLLLQV IDLSDANYQN HIRVVKKILD ELGVIDKPML YVFNKADLVE KTPEVLADEL AQYQPHVVVS ALSKEKLAPL IAFLSSWKA // ID A0A0G1BJ98_9BACT Unreviewed; 374 AA. AC A0A0G1BJ98; DT 22-JUL-2015, integrated into UniProtKB/TrEMBL. DT 22-JUL-2015, sequence version 1. DT 07-JUN-2017, entry version 14. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=UV09_C0018G0027 {ECO:0000313|EMBL:KKS46351.1}; OS Candidatus Gottesmanbacteria bacterium GW2011_GWA2_42_18. OC Bacteria; Candidatus Gottesmanbacteria. OX NCBI_TaxID=1618442 {ECO:0000313|EMBL:KKS46351.1, ECO:0000313|Proteomes:UP000034320}; RN [1] {ECO:0000313|EMBL:KKS46351.1, ECO:0000313|Proteomes:UP000034320} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A., RA Wilkins M.J., Williams K.H., Banfield J.F.; RT "rRNA introns, odd ribosomes, and small enigmatic genomes across a RT large radiation of phyla."; RL Nature 0:0-0(2015). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KKS46351.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LCDD01000018; KKS46351.1; -; Genomic_DNA. DR EnsemblBacteria; KKS46351; KKS46351; UV09_C0018G0027. DR PATRIC; fig|1618442.3.peg.846; -. DR Proteomes; UP000034320; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000034320}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000034320}. FT DOMAIN 205 374 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 374 AA; 42379 MW; 1CDDBBB799B348EA CRC64; MFEHNLNKRF LLVGFFPKGF SDDRIMPHLE ELDSLVKTYG GETVAVSIQR GFQPSRVTYV GSGKAQEIAE KVAAEKIEVV VLNDILKSGQ LYTLEKIWQR GNLQIKVWDK VGLILHIFDL HADTAESKLQ IKLASFRHMG PRIYGMGYVL SRQGGGIGTR GIGETNTEIM KRHWRNEIRL IKGKLAKIVK DHETHIGKRK KSGTLSVSLV GYTNSGKTSL YNALTGKNKL VEDKLFATLD SSLGRLYLPE INHPVLLSDT IGFISQLPPL LFDSFKSTLM ESLNSDLILH VIDISDQYID SKIKVVEDIL RQDLKLENRR QINVFNKTDK VSLEIIKIFK NKYPEEKTCF VSSVKGQGLD ILKQRITQEL KELL // ID A0A0G1DL82_9BACT Unreviewed; 362 AA. AC A0A0G1DL82; DT 22-JUL-2015, integrated into UniProtKB/TrEMBL. DT 22-JUL-2015, sequence version 1. DT 07-JUN-2017, entry version 13. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:KKS98342.1}; GN ORFNames=UV73_C0002G0056 {ECO:0000313|EMBL:KKS98342.1}; OS Candidatus Gottesmanbacteria bacterium GW2011_GWA2_43_14. OC Bacteria; Candidatus Gottesmanbacteria. OX NCBI_TaxID=1618443 {ECO:0000313|EMBL:KKS98342.1, ECO:0000313|Proteomes:UP000034894}; RN [1] {ECO:0000313|EMBL:KKS98342.1, ECO:0000313|Proteomes:UP000034894} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A., RA Wilkins M.J., Williams K.H., Banfield J.F.; RT "rRNA introns, odd ribosomes, and small enigmatic genomes across a RT large radiation of phyla."; RL Nature 0:0-0(2015). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KKS98342.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LCFP01000002; KKS98342.1; -; Genomic_DNA. DR EnsemblBacteria; KKS98342; KKS98342; UV73_C0002G0056. DR PATRIC; fig|1618443.3.peg.332; -. DR Proteomes; UP000034894; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000034894}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000034894}. FT DOMAIN 195 362 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 362 AA; 40356 MW; 3D107C81A7BC2596 CRC64; MLVGLFPKKY GNDVILSYLE ELDSLVRTYG GETTAVSVQK GDHSHRATYI GSGKANEVAD KIAENQIDTV VFNDILKSGQ LYTLEKIFQR SNPEIKVLDK IGLILLIFDN QADTAEAKLQ IKLASLRHMG PRTYGMGYIL SRQGGGIGTR GIGETNTEIM QRHWRNEIRA IKTKLTKIIK DRQLQIAKRK KAGTVSVSLV GYTNAGKTSL YNALTGKNKL VENRLFATLD SSIGRLYLPE FKNNLMVSDT IGFIQNLPPQ LLESFKSTLL ESIHADLILH VIDVSDRLFR EKIEVVEEIL AELDLQEKNQ IYIFNKADKI TAEIKNQAAL QFAGVPFCFV SAKTGLGLQE LKGKITGEIK KL // ID A0A0G1DWZ4_9BACT Unreviewed; 370 AA. AC A0A0G1DWZ4; DT 22-JUL-2015, integrated into UniProtKB/TrEMBL. DT 22-JUL-2015, sequence version 1. DT 07-JUN-2017, entry version 12. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=UV79_C0002G0019 {ECO:0000313|EMBL:KKT02135.1}; OS candidate division TM6 bacterium GW2011_GWF2_43_17. OC Bacteria; Candidatus Dependentiae. OX NCBI_TaxID=1619085 {ECO:0000313|EMBL:KKT02135.1, ECO:0000313|Proteomes:UP000034620}; RN [1] {ECO:0000313|EMBL:KKT02135.1, ECO:0000313|Proteomes:UP000034620} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A., RA Wilkins M.J., Williams K.H., Banfield J.F.; RT "rRNA introns, odd ribosomes, and small enigmatic genomes across a RT large radiation of phyla."; RL Nature 0:0-0(2015). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KKT02135.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LCFV01000002; KKT02135.1; -; Genomic_DNA. DR EnsemblBacteria; KKT02135; KKT02135; UV79_C0002G0019. DR PATRIC; fig|1619085.3.peg.77; -. DR Proteomes; UP000034620; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000034620}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000034620}. FT DOMAIN 205 370 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 370 AA; 41294 MW; D4C9803FCBDD17BE CRC64; MSTKNLIDTA TQISVLIIGV QTPHNKTFDV ESYFQEFKNL VATSGIVPAE EVYTKLRTID HSYFFTKGKL NELISLCEQK HFDEIIISEP LSTQQARNLK DALNAPIVDR TELILRIFEQ GAQSAEGKVQ VEMAILKFQK SRLAGYGIHL SQQGGTIGTK GPGETAKEKA TQHLERSITQ TRKELDQLEK VRITQRKRRL ESKTPHIGIV GYTNAGKSTL LNTLTNSNIL AENKLFATLD TTTRELFLNG TKKGTISDTV GFIQNLPHSL VAAFKSTLSE LQYALLLLLV VDISDKNWRN HISVVEDTLT EIGAGGIPKI FVFNKLDQTK LTPEQKNEIA LQFSPAVFIS ARDKDKIEEL TSLLESWKPA // ID A0A0G1DYQ4_9BACT Unreviewed; 374 AA. AC A0A0G1DYQ4; DT 22-JUL-2015, integrated into UniProtKB/TrEMBL. DT 22-JUL-2015, sequence version 1. DT 07-JUN-2017, entry version 13. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:KKT02986.1}; GN ORFNames=UV80_C0001G0088 {ECO:0000313|EMBL:KKT02986.1}; OS Candidatus Peregrinibacteria bacterium GW2011_GWF2_43_17. OC Bacteria; Candidatus Peregrinibacteria. OX NCBI_TaxID=1619068 {ECO:0000313|EMBL:KKT02986.1, ECO:0000313|Proteomes:UP000034674}; RN [1] {ECO:0000313|EMBL:KKT02986.1, ECO:0000313|Proteomes:UP000034674} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A., RA Wilkins M.J., Williams K.H., Banfield J.F.; RT "rRNA introns, odd ribosomes, and small enigmatic genomes across a RT large radiation of phyla."; RL Nature 0:0-0(2015). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KKT02986.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LCFW01000001; KKT02986.1; -; Genomic_DNA. DR EnsemblBacteria; KKT02986; KKT02986; UV80_C0001G0088. DR PATRIC; fig|1619068.3.peg.89; -. DR Proteomes; UP000034674; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000034674}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000034674}. FT DOMAIN 207 374 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 166 193 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 374 AA; 42791 MW; 9E2FBF16F088D3DE CRC64; MRDYEHPLTP GGEKAIIIDV IPPGMNKREA LERLEELERL IDTFGGVTIL KIIQKRGRPS AKTYIGSGKA EEVVKLQKEL GATMVVINGF MKANQFHNLT LMIDCEVMDR FELILKIFAK HARTEKARLQ IRLAFLKYEF PRLFGKQAGH AQQRGGTGTV TRGKGEKLLE LKREHLRDQI RAIEKKLESI QKVHSGQRQR RKRQGFLTVA IVGYTNSGKS TLLKQITHKK NAYTANKLFA TLETKLGSLY IEDFPRTVLL ADTIGFIQDL PPLLFESFIT TLEEVTEADL VLHIIDAADL KIYEKIDTVE KILKDLECDK KPQLYVLNKM DMVKDKQKIL KTYAYLNPVT ISALQKEGFQ ELKTAIKNKF YEIF // ID A0A0G1ILK9_9BACT Unreviewed; 371 AA. AC A0A0G1ILK9; DT 22-JUL-2015, integrated into UniProtKB/TrEMBL. DT 22-JUL-2015, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=UW09_C0001G0147 {ECO:0000313|EMBL:KKT24084.1}; OS candidate division TM6 bacterium GW2011_GWF2_43_87. OC Bacteria; Candidatus Dependentiae. OX NCBI_TaxID=1619086 {ECO:0000313|EMBL:KKT24084.1, ECO:0000313|Proteomes:UP000034056}; RN [1] {ECO:0000313|EMBL:KKT24084.1, ECO:0000313|Proteomes:UP000034056} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A., RA Wilkins M.J., Williams K.H., Banfield J.F.; RT "rRNA introns, odd ribosomes, and small enigmatic genomes across a RT large radiation of phyla."; RL Nature 0:0-0(2015). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KKT24084.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LCGZ01000001; KKT24084.1; -; Genomic_DNA. DR EnsemblBacteria; KKT24084; KKT24084; UW09_C0001G0147. DR PATRIC; fig|1619086.3.peg.148; -. DR Proteomes; UP000034056; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000034056}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000034056}. FT DOMAIN 205 371 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 164 191 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 371 AA; 41915 MW; 5312FBAB738AC28A CRC64; MKPSISTHLL DQPALLIVGV QTPQNRSIDP DSYFQEFRNL VRSDGFETFE EHMIKLRSID SAYFFTRGKL DEIIGLCKSH TIGKVIISEP LSHQQTRNLT DVLEAEVMDR TELILEIFEK GAQSSEGKLQ VAVALLNHKK ARVAGKGIHL SQQAGSIGTR GPGETQKEKD LRHLERLISK LDRDLEHLSK VRETQRKKRS LSALPHISII GYTNAGKSTL LNALTKSSVY AENKLFATLD TTTRELFIDG SKKGTVSDTV GFIQNLPHEL IEAFKSTLSD LEYAHMLLQV VDLSDKNWRN HIRVVQGILD ELKVSDTPML YVFNKVDMLN DEERKAFEDQ ASLYQPHVLI SALSKEGLQP LLSYLREWKP S // ID A0A0G1SI22_9BACT Unreviewed; 361 AA. AC A0A0G1SI22; DT 22-JUL-2015, integrated into UniProtKB/TrEMBL. DT 22-JUL-2015, sequence version 1. DT 07-JUN-2017, entry version 14. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=UX45_C0012G0026 {ECO:0000313|EMBL:KKU32985.1}; OS Candidatus Uhrbacteria bacterium GW2011_GWF2_46_218. OC Bacteria; Candidatus Uhrbacteria. OX NCBI_TaxID=1619001 {ECO:0000313|EMBL:KKU32985.1, ECO:0000313|Proteomes:UP000034705}; RN [1] {ECO:0000313|EMBL:KKU32985.1, ECO:0000313|Proteomes:UP000034705} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A., RA Wilkins M.J., Williams K.H., Banfield J.F.; RT "rRNA introns, odd ribosomes, and small enigmatic genomes across a RT large radiation of phyla."; RL Nature 0:0-0(2015). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KKU32985.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LCMG01000012; KKU32985.1; -; Genomic_DNA. DR EnsemblBacteria; KKU32985; KKU32985; UX45_C0012G0026. DR PATRIC; fig|1619001.3.peg.586; -. DR Proteomes; UP000034705; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000034705}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000034705}. FT DOMAIN 197 361 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 361 AA; 40793 MW; 0F2BEAFE1DD45FAE CRC64; MRKAILADVI HPCMRGVQSL ERMQELEELV STYGGIVVVK TFQRRFAPHP KTFLGTGKIK QLGEEGKLLH ADLLVINDLL KPRQIYEISE QLRSVKIEVW DRIDLILKIF AKHAHTTEAK LEIELASIRH MGPRIFGMGM ELSRQGGGIG TSGIGETNTE IMRRHLSERE KLIKEKLDKC QVVREGHRIF RRRKGLKTIS IVGYTNAGKT TLLNALTGRR EYAANKLFAT LDTRVGSLWL PHVQSKILVS DTIGFIKQLP PELISAFTST LSEAVEADIL LQVLDASDSH LWQHLQVVED ILKRLGISDK PRILICHKSD QVTSKQRKII DQKLGDTVHV WVSSQEEKGI GDLIEMIESK L // ID A0A0G1XLC5_9BACT Unreviewed; 202 AA. AC A0A0G1XLC5; DT 22-JUL-2015, integrated into UniProtKB/TrEMBL. DT 22-JUL-2015, sequence version 1. DT 11-MAY-2016, entry version 8. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:KKW32088.1}; DE Flags: Fragment; GN ORFNames=UY77_C0037G0007 {ECO:0000313|EMBL:KKW32088.1}; OS Candidatus Uhrbacteria bacterium GW2011_GWA2_53_10. OC Bacteria; Candidatus Uhrbacteria. OX NCBI_TaxID=1618980 {ECO:0000313|EMBL:KKW32088.1, ECO:0000313|Proteomes:UP000034711}; RN [1] {ECO:0000313|EMBL:KKW32088.1, ECO:0000313|Proteomes:UP000034711} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A., RA Wilkins M.J., Williams K.H., Banfield J.F.; RT "rRNA introns, odd ribosomes, and small enigmatic genomes across a RT large radiation of phyla."; RL Nature 0:0-0(2015). CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KKW32088.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LCRI01000037; KKW32088.1; -; Genomic_DNA. DR EnsemblBacteria; KKW32088; KKW32088; UY77_C0037G0007. DR Proteomes; UP000034711; Unassembled WGS sequence. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000034711}; KW Reference proteome {ECO:0000313|Proteomes:UP000034711}. FT DOMAIN 26 116 GTP-bdg_N. {ECO:0000259|Pfam:PF13167}. FT DOMAIN 118 196 GTP-bdg_M. {ECO:0000259|Pfam:PF16360}. FT NON_TER 202 202 {ECO:0000313|EMBL:KKW32088.1}. SQ SEQUENCE 202 AA; 23237 MW; 692C77E733FC3D53 CRC64; MQNPEKTKAI LVDLIHPRMR ASESMERLSE LEELVQTYGG IVIVKTYQRR FAPHPRTFLG PGKITDLAKE GKSLGAKLLI INDRLKPRQI YNVDELLKGS GLRVWDRIDM ILKIFAKHAR TTEARLEIEL ASIRHMGPRI FGMGMELSRQ GGGIGTLGIG ETNTEIMHRH LKKRERRLLE KLEQYQTVRA GHRKSRQRKD LP // ID A0A0G2A0V7_9BACT Unreviewed; 369 AA. AC A0A0G2A0V7; DT 22-JUL-2015, integrated into UniProtKB/TrEMBL. DT 22-JUL-2015, sequence version 1. DT 07-JUN-2017, entry version 12. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=UY79_C0001G0061 {ECO:0000313|EMBL:KKW34422.1}; OS Parcubacteria group bacterium GW2011_GWA2_53_21. OC Bacteria; unclassified Parcubacteria group. OX NCBI_TaxID=1618858 {ECO:0000313|EMBL:KKW34422.1, ECO:0000313|Proteomes:UP000033913}; RN [1] {ECO:0000313|EMBL:KKW34422.1, ECO:0000313|Proteomes:UP000033913} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A., RA Wilkins M.J., Williams K.H., Banfield J.F.; RT "rRNA introns, odd ribosomes, and small enigmatic genomes across a RT large radiation of phyla."; RL Nature 0:0-0(2015). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KKW34422.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LCRK01000001; KKW34422.1; -; Genomic_DNA. DR EnsemblBacteria; KKW34422; KKW34422; UY79_C0001G0061. DR PATRIC; fig|1618858.3.peg.63; -. DR Proteomes; UP000033913; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000033913}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000033913}. FT DOMAIN 204 369 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 170 197 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 369 AA; 41768 MW; 69D292238DC6A776 CRC64; MKTLAGTPRA ILVDLIRPQT KKHEAIERME ELEELMRTYG GLVVVKKLQR RNHPDNRTYI GKGKVEELKT LARELNTSVL VLNNILKPGQ IYNLSEALKD EKVTVWDRVD LILSIFAKHA QSQEAKLQIE LARIRHMGPR IFGLGGEELA RQAGGIGTRG IGETNTEIMK RHLRERERRV RERLERTQKM RAEQRKNRQR NGFKTAAIVG YTNTGKTTLL NALTGRKEYA ANKLFATLDT RTGKLYLPGK NASLLVSDTI GFIRDLPPEL IEAFASTLSE TVHADVLLHV VDAGNPRRDE QIGVVEAVLR KLEIENKPII HVFNKADRLK KGEAEHVKEA FAERRPVIVS ALTNDGMDIL IERLEHVLS // ID A0A0G2ZDC5_9BACT Unreviewed; 416 AA. AC A0A0G2ZDC5; DT 16-SEP-2015, integrated into UniProtKB/TrEMBL. DT 16-SEP-2015, sequence version 1. DT 07-JUN-2017, entry version 10. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=IX53_09815 {ECO:0000313|EMBL:AKI98076.1}; OS Kosmotoga pacifica. OC Bacteria; Thermotogae; Kosmotogales; Kosmotogaceae; Kosmotoga. OX NCBI_TaxID=1330330 {ECO:0000313|EMBL:AKI98076.1, ECO:0000313|Proteomes:UP000035159}; RN [1] {ECO:0000313|EMBL:AKI98076.1, ECO:0000313|Proteomes:UP000035159} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SLHLJ1 {ECO:0000313|EMBL:AKI98076.1, RC ECO:0000313|Proteomes:UP000035159}; RA Jiang L.J., Shao Z.Z., Jebbar M.; RT "Complete Genome Sequence of Kosmotoga pacifica SLHLJ1."; RL Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP011232; AKI98076.1; -; Genomic_DNA. DR EnsemblBacteria; AKI98076; AKI98076; IX53_09815. DR KEGG; kpf:IX53_09815; -. DR PATRIC; fig|1330330.3.peg.2001; -. DR KO; K03665; -. DR Proteomes; UP000035159; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000035159}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000035159}. FT DOMAIN 193 358 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 152 186 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 416 AA; 47652 MW; 61C53C5F45B9FFF1 CRC64; MRKAILACVF NRQEQGARRE VISELERLAN TAGYCVVDTL IQNLDSPNPR HYFGAGKLGE LKHLVQLFEP DVVITRHNLT PSQRKNLIHE LGIEIEDRTQ LILEIFEKHA FTREGKYEVE LARLRYEMPF FKGKGVELSN PGGGIGTRGP GEKKLELDRR KALQRIAFLK KELEKLGLER KIMRKRRQKA GIPLIALVGY TNAGKSSLLN VLCDAGALVE DKLFSTLDTR IRKSKLPSGR EVLFIDTVGF IRELPHQLLE SFKSTLEEIN FADLLLIVMD ASETNEEGKL TVIEETLKKI GAEDVPRLLV LNKVDRCTNE RIQMLEKKFP EAVFVSALKG FNLDELKCNI DRIFNLMRKK YILRVPFAEY EAIMKVREKL EILSEKYESD LIEIEYVTDS ATNKWLLNRI KGAGKR // ID A0A0G2ZJ03_9DELT Unreviewed; 477 AA. AC A0A0G2ZJ03; DT 16-SEP-2015, integrated into UniProtKB/TrEMBL. DT 16-SEP-2015, sequence version 1. DT 07-JUN-2017, entry version 13. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=AA314_03239 {ECO:0000313|EMBL:AKJ01613.1}; OS Archangium gephyra. OC Bacteria; Proteobacteria; Deltaproteobacteria; Myxococcales; OC Cystobacterineae; Archangiaceae; Archangium. OX NCBI_TaxID=48 {ECO:0000313|EMBL:AKJ01613.1, ECO:0000313|Proteomes:UP000035579}; RN [1] {ECO:0000313|EMBL:AKJ01613.1, ECO:0000313|Proteomes:UP000035579} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 2261 {ECO:0000313|EMBL:AKJ01613.1, RC ECO:0000313|Proteomes:UP000035579}; RA Sharma G., Subramanian S.; RT "Genome assembly of Archangium gephyra DSM 2261."; RL Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP011509; AKJ01613.1; -; Genomic_DNA. DR RefSeq; WP_047856152.1; NZ_CP011509.1. DR EnsemblBacteria; AKJ01613; AKJ01613; AA314_03239. DR KEGG; age:AA314_03239; -. DR PATRIC; fig|48.3.peg.3293; -. DR KO; K03665; -. DR Proteomes; UP000035579; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 2. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000035579}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000035579}. FT DOMAIN 258 423 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 87 121 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 477 AA; 52551 MW; B2EE85D49A65D2D9 CRC64; MSNSSTPRPL AVLVGVQLPG VSDTEHAADL AELGRLVHTL GYKVVATVSQ RRDKLAPGTV LGSGKLAELA QLTGGRGTVP SGAQGRKSKA RERWEAEAEE ADEAEEQQAA AEADEDVAEE DEVPEEELSA EASEEPLTER PTVVVVDHEL SPSQLSNLER ATGAQVFDRT GVIVDIFHRH ARSREAKMQV EIARLNYLAP RMRESTGSSE RQQGRGSGDS AVELDRRKIR DRLAELREGL AAIQQDQDHR RYARRDQLRV ALVGYTNAGK SSLMRALTGS EVLVADQLFA TLDTTVRALQ PETRPRVLIS DTVGFIQKLP HDLVASFRST LDEALEASLL LYVVDGSDPT WEAQLEVTRS VLREIGAQSV PSRLLFNKAD RLTPEAREAL LQQHPEALVL SAHAPDDVAA LRQTIIEFFE RSMVEAELVI PYSRQARIGE VYEHARVLSE AYDETGRRLK VRALPAAMAR LTRAFET // ID A0A0G2ZQL4_9DELT Unreviewed; 585 AA. AC A0A0G2ZQL4; DT 16-SEP-2015, integrated into UniProtKB/TrEMBL. DT 16-SEP-2015, sequence version 1. DT 07-JUN-2017, entry version 12. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=AA314_02655 {ECO:0000313|EMBL:AKJ01029.1}; OS Archangium gephyra. OC Bacteria; Proteobacteria; Deltaproteobacteria; Myxococcales; OC Cystobacterineae; Archangiaceae; Archangium. OX NCBI_TaxID=48 {ECO:0000313|EMBL:AKJ01029.1, ECO:0000313|Proteomes:UP000035579}; RN [1] {ECO:0000313|EMBL:AKJ01029.1, ECO:0000313|Proteomes:UP000035579} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 2261 {ECO:0000313|EMBL:AKJ01029.1, RC ECO:0000313|Proteomes:UP000035579}; RA Sharma G., Subramanian S.; RT "Genome assembly of Archangium gephyra DSM 2261."; RL Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP011509; AKJ01029.1; -; Genomic_DNA. DR EnsemblBacteria; AKJ01029; AKJ01029; AA314_02655. DR KEGG; age:AA314_02655; -. DR PATRIC; fig|48.3.peg.2698; -. DR KO; K03665; -. DR Proteomes; UP000035579; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000035579}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000035579}. FT DOMAIN 378 542 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 337 371 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 585 AA; 64476 MW; 3437FD78AA27C8FB CRC64; MKEIYGNTLG LKASEQSRLR NTYRRRVSPH EIVSPELARH LTELSRETNR QVGVLLNRKG EIEYVVVGNA HKLELPDIGR ARAGQVRLRG LRLVHTHLKS EPLTKDDLTD LALLRLDMVA AVGVGDTGLP GVLHYAHLVP ENGTGDFWSV TTLPDVHDSQ PDVLDTLEAL EEELNRKAAA RTVSGRDKAI LVAVCLNGNR AQAEASLAEL KELARTAGVE VIDSVLQMRR EADPRYLIGR GKLEDLNLRS MQAMADVLIF DKDLTPSQGR HISEATSLKV IDRSQLILDI FAQRAQSAEG KLQVELAQLK YRLPRLVQSD TSLSRLAGGI GGRGPGETKL EIDRRRARDR INHLEKRIDA LSREREVRRA QRNRRELPVI SIVGYTNAGK STLLNAITGS EVLAENKLFA TLDPTSRRLR FPQEREVIIT DTVGFIRDLP KDLVAAFRAT LEELYDADLL LHVVDASDPS RDEQVQAVEN ILDSLDLMQK PRLMVWNKAD LLTPEEVGSL LRTSGGVAIS AASREGLAAL LAKADTTLFA EGASRNLGVV TRDASHTHGT IGFDEAPSEE PLEDAEEPTQ NLGAA // ID A0A0G3ADB7_9ACTN Unreviewed; 496 AA. AC A0A0G3ADB7; DT 16-SEP-2015, integrated into UniProtKB/TrEMBL. DT 16-SEP-2015, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=ABB07_09920 {ECO:0000313|EMBL:AKJ10322.1}; OS Streptomyces incarnatus. OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae; OC Streptomyces. OX NCBI_TaxID=665007 {ECO:0000313|EMBL:AKJ10322.1, ECO:0000313|Proteomes:UP000035366}; RN [1] {ECO:0000313|EMBL:AKJ10322.1, ECO:0000313|Proteomes:UP000035366} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NRRL8089 {ECO:0000313|Proteomes:UP000035366}; RX PubMed=26159526; RA Oshima K., Hattori M., Shimizu H., Fukuda K., Nemoto M., Inagaki K., RA Tamura T.; RT "Draft Genome Sequence of Streptomyces incarnatus NRRL8089, which RT Produces the Nucleoside Antibiotic Sinefungin."; RL Genome Announc. 3:e00715-15(2015). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP011497; AKJ10322.1; -; Genomic_DNA. DR EnsemblBacteria; AKJ10322; AKJ10322; ABB07_09920. DR PATRIC; fig|665007.5.peg.2165; -. DR Proteomes; UP000035366; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 2. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000313|EMBL:AKJ10322.1}; KW Complete proteome {ECO:0000313|Proteomes:UP000035366}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900, KW ECO:0000313|EMBL:AKJ10322.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000035366}. FT DOMAIN 274 439 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 496 AA; 54170 MW; C02DAE7BD02BE23C CRC64; MTSSSSPSQD TKRLAHAYPE GLRADALMEE DVAWSYEIDG ERDGDQFDRS ERAALRRVAG LSTELEDVTE VEYRQLRLER VVLVGVWTTG TAQDAENSLA ELAALAETAG ALVLDGVIQR RDKPDAATYI GSGKAQELRD IVLETGADTV ICDGELSPGQ LIQLEDVVKV KVIDRTALIL DIFAQHAKSR EGKAQVALAQ MQYMLPRLRG WGQSLSRQMG GGRGGLATRG PGETKIETDR RRIREKMAKM RREIADMKTG REIKRQERRR NKVPSVAIAG YTNAGKSSLL NRLTGAGVLV ENALFATLDP TVRRAETPSG RLYTLADTVG FVRHLPHHLV EAFRSTMEEV GGSDLILHVV DGSHPNPEEQ LAAVREVIRD VGATDVPEIV VINKADAADP LVLQRLLRVE KRSIAVSART GRGLEKLLAL IDDELPRPAV EVEALVPYTH GKLVARAHSE GEVISEEHTA EGTLLKVRVH EELAADLAPY APVSAA // ID A0A0G3BNQ9_9BURK Unreviewed; 400 AA. AC A0A0G3BNQ9; DT 16-SEP-2015, integrated into UniProtKB/TrEMBL. DT 16-SEP-2015, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:AKJ28986.1}; GN ORFNames=AAW51_2295 {ECO:0000313|EMBL:AKJ28986.1}; OS [Polyangium] brachysporum. OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales. OX NCBI_TaxID=413882 {ECO:0000313|EMBL:AKJ28986.1, ECO:0000313|Proteomes:UP000035352}; RN [1] {ECO:0000313|EMBL:AKJ28986.1, ECO:0000313|Proteomes:UP000035352} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 7029 {ECO:0000313|EMBL:AKJ28986.1, RC ECO:0000313|Proteomes:UP000035352}; RA Tang B., Yu Y.; RL Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP011371; AKJ28986.1; -; Genomic_DNA. DR EnsemblBacteria; AKJ28986; AKJ28986; AAW51_2295. DR KEGG; pbh:AAW51_2295; -. DR PATRIC; fig|413882.6.peg.2403; -. DR KO; K03665; -. DR Proteomes; UP000035352; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000035352}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000035352}. FT DOMAIN 187 361 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 400 AA; 43892 MW; E725495F374B67C8 CRC64; MGVDLGPGSP FDPTLDELAL LAESAGDTPV ARLTAKRKAP DAALFVGEGK ADEIKALVTA HDAQSVLFDQ ALSPAQQRNL ERHLGVPVAD RTMLILEIFG RRAQSHEGKL QVELARLQYL STRLVRRWTH LERQRGGVGH RGGPGEAQIE LDRRMIAQRI KALKFQLEKV KRQRNTQRRS RERSGTFRVS LVGYTNAGKS TLFNALVKAR SYAANQLFAT LDTTTRQMYL ADAERSVSLS DTVGFIRDLP HTLVEAFQAT LQEAADADLL LHVVDAASPV WREQIDEVQR VLREIGANDL PQLLVFNKLD ALPDSQRPRQ RVDAFEIEPH RPAHRVFVSA AQGEGLDDLR RLIAEAATGA LPLPQPGPPD SSAEPHPEQS VEGGGDTAPP AQNSVSNARA // ID A0A0G3CP27_9GAMM Unreviewed; 426 AA. AC A0A0G3CP27; DT 16-SEP-2015, integrated into UniProtKB/TrEMBL. DT 16-SEP-2015, sequence version 1. DT 30-AUG-2017, entry version 16. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=QQ39_02135 {ECO:0000313|EMBL:AKJ43714.1}; OS Pragia fontium. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; OC Budviciaceae; Pragia. OX NCBI_TaxID=82985 {ECO:0000313|EMBL:AKJ43714.1, ECO:0000313|Proteomes:UP000068021}; RN [1] {ECO:0000313|EMBL:AKJ43714.1, ECO:0000313|Proteomes:UP000068021} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=24613 {ECO:0000313|EMBL:AKJ43714.1, RC ECO:0000313|Proteomes:UP000068021}; RX PubMed=26159528; RA Snopkova K., Sedlar K., Bosak J., Chaloupkova E., Provaznik I., RA Smajs D.; RT "Complete Genome Sequence of Pragia fontium 24613, an Environmental RT Bacterium from the Family Enterobacteriaceae."; RL Genome Announc. 3:e00740-15(2015). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP010423; AKJ43714.1; -; Genomic_DNA. DR RefSeq; WP_047782448.1; NZ_CP010423.1. DR EnsemblBacteria; AKJ43714; AKJ43714; QQ39_02135. DR KEGG; pfq:QQ39_02135; -. DR PATRIC; fig|82985.3.peg.441; -. DR KO; K03665; -. DR Proteomes; UP000068021; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000068021}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000068021}. FT DOMAIN 198 365 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 426 AA; 48007 MW; F6829E2A88624199 CRC64; MFDRYDAGEL AVLVHVYFSQ EKDTEDLREF ESLVSSAGVE TLLVVTGSRK APHAKYFVGE GKAQEIADAV HATGATVVLF NHSLSPAQER NLERLCECRV IDRTGLILDI FAQRARTHEG KLQVELAQLR HLATRLVRGW THLERQKGGI GLRGPGETQL ETDRRLLRDR IRQILGRLEK VEKQREQGRR ARMRADIPTV SLVGYTNAGK STLFNCITTA GVYAADQLFA TLDPTLRRID VEDVGVTVLA DTVGFIRHLP HDLVAAFKAT LQETRQASLL LHIVDAADGR IDENIAAVND VLAEIEADEI PVLLVMNKID MLEDFAPRID RDENNLPFRV WLSAESGDGV DLLFRALTER LSGEIAQYEL KLPVAEGRLR SRFYQLQAIT REWIEEDGSI GLVIRMPIVD WRRLCKQEQA LENFIV // ID A0A0G3EH43_9BACT Unreviewed; 426 AA. AC A0A0G3EH43; DT 16-SEP-2015, integrated into UniProtKB/TrEMBL. DT 16-SEP-2015, sequence version 1. DT 07-JUN-2017, entry version 13. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:AKJ64130.1}; GN ORFNames=L21SP4_00867 {ECO:0000313|EMBL:AKJ64130.1}; OS Kiritimatiella glycovorans. OC Bacteria; Kiritimatiellaeota; Kiritimatiellae; Kiritimatiellales; OC Kiritimatiellaceae; Kiritimatiella. OX NCBI_TaxID=1307763 {ECO:0000313|EMBL:AKJ64130.1, ECO:0000313|Proteomes:UP000035268}; RN [1] {ECO:0000313|Proteomes:UP000035268} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=L21-Fru-AB {ECO:0000313|Proteomes:UP000035268}; RA Spring S., Bunk B., Sproer C., Klenk H.-P.; RT "Description and complete genome sequence of the first cultured RT representative of the subdivision 5 of the Verrucomicrobia phylum."; RL Submitted (FEB-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP010904; AKJ64130.1; -; Genomic_DNA. DR RefSeq; WP_052881494.1; NZ_CP010904.1. DR EnsemblBacteria; AKJ64130; AKJ64130; L21SP4_00867. DR KEGG; vbl:L21SP4_00867; -. DR PATRIC; fig|1609981.3.peg.904; -. DR KO; K03665; -. DR Proteomes; UP000035268; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000035268}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000035268}. FT DOMAIN 205 371 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 171 198 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 426 AA; 47464 MW; BF0EE540F82AA268 CRC64; MGGTDSVSDR RKERAVLVGV VLGDEPEHET RESLDELGRL AGSAGAEETG RFVCRQNKVR PGYYIGTGKA AEIGAWAEEH PADTLVFDEN LSPVQGRNLE KATGLRVIDR TQLIMDIFAQ HARTREGQLQ VELAQLEYLL PRLRRMWTHL ERQKGGIGLR GPGETQIEMD RRRIQMQIKR LKRDLELVRR RRAEQRKGRK RGGWSLVSIV GYTNAGKSTL LNRLAGASVH ADSALFATLD PTIRRVELPG HEPVLLSDTV GFISKLPHSL VEAFKATLEE VVEADLLLHV VDASHPRAAD QARAVNEVLE ELGVGDKPVF CALNKIDRAE GRHRSRRLLR DLAPAAALSA RSGEGVETLK EALADRLRSS KTLVEMRIPI GEGRLIAELH RRGTVLEEAY DHDAARIKAR IPPDMRDDCA RFVTFS // ID A0A0G3EKG5_9BURK Unreviewed; 388 AA. AC A0A0G3EKG5; DT 16-SEP-2015, integrated into UniProtKB/TrEMBL. DT 16-SEP-2015, sequence version 1. DT 05-JUL-2017, entry version 18. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=ABW99_03365 {ECO:0000313|EMBL:AKJ67415.1}; OS Pandoraea thiooxydans. OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Pandoraea. OX NCBI_TaxID=445709 {ECO:0000313|EMBL:AKJ67415.1, ECO:0000313|Proteomes:UP000036700}; RN [1] {ECO:0000313|Proteomes:UP000036700} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 25325 {ECO:0000313|Proteomes:UP000036700}; RA Lim Y.L., Ee R., Yong D., How K.Y., Yin W.F., Chan K.G.; RL Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP011568; AKJ67415.1; -; Genomic_DNA. DR RefSeq; WP_047212981.1; NZ_CP014839.1. DR KEGG; ptx:ABW99_03365; -. DR PATRIC; fig|445709.3.peg.720; -. DR KO; K03665; -. DR Proteomes; UP000036700; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000036700}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000036700}. FT DOMAIN 191 361 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 157 184 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 388 AA; 42289 MW; 6548743B4A5EA330 CRC64; MINAALVGID FGKVDFEASL AELDLLSRSA GADPVVAVTG RRGSPDAAMF VGSGKAQEIK DAIALHRVDL VIFNHALSPA QQRNLERFLE RRVVDRTSLI LDIFAQRAKS HEGKLQVELA QLQYLATRLV RAWSHLERQK GGIGLRGPGE TQLETDRRLL GERVKSLKVR LDKLRRQHAT QRRARKRSDT FSISLVGYTN AGKSTLFNAL TKAQAYAADQ LFATLDTTSR RVYLGEVGQV VLSDTVGFIR ELPHQLVAAF RATLEETVHA DLLLHVVDAS SAVRQEQIDQ VNTVLTEIGA DGIPQILVWN KIDAAPELLA DGPRIERDES GNVTRVFVSA RDGIGLDLLR AAIAETIARP ATALQSSGQS PNHLPAESGV GFHTAGNL // ID A0A0G3GQ48_9CORY Unreviewed; 522 AA. AC A0A0G3GQ48; DT 16-SEP-2015, integrated into UniProtKB/TrEMBL. DT 16-SEP-2015, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:AKK03336.1}; GN ORFNames=CEPID_07425 {ECO:0000313|EMBL:AKK03336.1}; OS Corynebacterium epidermidicanis. OC Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae; OC Corynebacterium. OX NCBI_TaxID=1050174 {ECO:0000313|EMBL:AKK03336.1, ECO:0000313|Proteomes:UP000035368}; RN [1] {ECO:0000313|EMBL:AKK03336.1, ECO:0000313|Proteomes:UP000035368} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 45586 {ECO:0000313|EMBL:AKK03336.1, RC ECO:0000313|Proteomes:UP000035368}; RA Ruckert C., Albersmeier A., Winkler A., Tauch A.; RT "Complete genome sequence of Corynebacterium epidermidicanis DSM RT 45586, isolated from the skin of a dog suffering from pruritus."; RL Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP011541; AKK03336.1; -; Genomic_DNA. DR EnsemblBacteria; AKK03336; AKK03336; CEPID_07425. DR KEGG; cei:CEPID_07425; -. DR PATRIC; fig|1050174.4.peg.1496; -. DR KO; K03665; -. DR Proteomes; UP000035368; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000035368}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000035368}. FT DOMAIN 299 468 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 258 285 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 522 AA; 56855 MW; 5391E1CCB04E53BB CRC64; MTNRDFDELL SDAFKDHRPT TEPAESAGTD LSGVIRSSQR SVLPSYAAEN VAETASDDIP TVGDLDLEER SSLRKLSRGG TVRDTEHREG YEVEYRKLRL ERVVLVGVWT EGTTAEIEAN MAELKALAET AGSEVTEMLY QKRDKPDPGT FIGSGKVKEV KEIVSATDSD TVICDGELSP SQLIALEQAL NVKVIDRTML ILDIFAQHAK SKEGKAQVAL AQMEYLFNRV RGWGGNLSRQ AGGRAGSNGG VGLRGPGETK IEADRRRLRA DMARLRKEIA GMKTTRETKR ARRKASTTPQ IAIAGYTNAG KSSLINAMTG AGVLVENALF ATLDPTTRRA ELADGRAVTF TDTVGFVRHL PTSFVEAFRS TLEEVVEADL VLHVVDGSDP FPLKQIDAVR TVILDIVRET GVEAPPELIV VNKIDQADPL TLAELRHALD DAVFVSARTG EGIAELQARI ELFLNTLDAH VKLLVPFTRG DVIARLHEQA TVLSENYGEN GTLIDVRLPQ SLAAELSQFA VD // ID A0A0G3H4X5_9CORY Unreviewed; 566 AA. AC A0A0G3H4X5; DT 16-SEP-2015, integrated into UniProtKB/TrEMBL. DT 16-SEP-2015, sequence version 1. DT 07-JUN-2017, entry version 12. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:AKK06132.1}; GN ORFNames=CMUST_09075 {ECO:0000313|EMBL:AKK06132.1}; OS Corynebacterium mustelae. OC Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae; OC Corynebacterium. OX NCBI_TaxID=571915 {ECO:0000313|EMBL:AKK06132.1, ECO:0000313|Proteomes:UP000035199}; RN [1] {ECO:0000313|Proteomes:UP000035199} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 45274 {ECO:0000313|Proteomes:UP000035199}; RA Ruckert C., Albersmeier A., Winkler A., Tauch A.; RT "Complete genome sequence of Corynebacterium mustelae DSM 45274, RT isolated from various tissues of a male ferret with lethal sepsis."; RL Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP011542; AKK06132.1; -; Genomic_DNA. DR EnsemblBacteria; AKK06132; AKK06132; CMUST_09075. DR KEGG; cmv:CMUST_09075; -. DR PATRIC; fig|571915.4.peg.1924; -. DR KO; K03665; -. DR Proteomes; UP000035199; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000035199}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000035199}. FT DOMAIN 341 510 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 300 327 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 566 AA; 61904 MW; B9486B5E19509E80 CRC64; MVLFRLGQLL NNGRLSLRHN QVLAVLQVAW KNNVVTMTTH MNDKKKTENS TETILKRAFR GTTAIVGADQ QESESGLEPV SVPQPQPVTE PYFSVGVSAE AQPTVGELDL EDRSSLRSLS RGRSYATDQD DGYDVEYRKL RLERVILVGV WTEGTTAEID ANMQELAALA ETAGSEVVEM FYQRRDRPDP GTYIGSGKVQ ELREIVAATS VDTVICDGEL SPGQMIALEK ALDVKVIDRT MLILDIFAQH AKSKEGKAQV SLAQMEYLIT RVRGWGSALS RQAGGRAGSN GGVGLRGPGE TKIEADRRRL RSDMAKLRKE IAGMKTARDV KRAQRKSSTI PQIAIAGYTN AGKSSLINAL TGAGVLVEDA LFATLDPTTR RAELADGRSV VFTDTVGFVR HLPTQLVEAF RSTLEEVVEA DLVLHVVDGS DPFPLKQIEA VNGVITDIVR ELKVDAPPEI VVVNKIDAAD PLVLAQLRHA LEDVVFVSAH TGEGIAELEA RIELFLNSKD AHVELLIPFA RGEIVSRLHR NGTVLREDYL PEGTVIEVRL PHALAEELKE FVVGEN // ID A0A0G3H6J0_9CORY Unreviewed; 514 AA. AC A0A0G3H6J0; DT 16-SEP-2015, integrated into UniProtKB/TrEMBL. DT 16-SEP-2015, sequence version 1. DT 30-AUG-2017, entry version 13. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:AKK08989.1}; GN ORFNames=CTEST_07795 {ECO:0000313|EMBL:AKK08989.1}; OS Corynebacterium testudinoris. OC Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae; OC Corynebacterium. OX NCBI_TaxID=136857 {ECO:0000313|EMBL:AKK08989.1, ECO:0000313|Proteomes:UP000035540}; RN [1] {ECO:0000313|Proteomes:UP000035540} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 44614 {ECO:0000313|Proteomes:UP000035540}; RA Ruckert C., Albersmeier A., Winkler A., Tauch A.; RT "Complete genome sequence of Corynebacterium testudinoris DSM 44614, RT recovered from necrotic lesions in the mouth of a tortoise."; RL Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP011545; AKK08989.1; -; Genomic_DNA. DR RefSeq; WP_047253252.1; NZ_CP011545.1. DR EnsemblBacteria; AKK08989; AKK08989; CTEST_07795. DR KEGG; cted:CTEST_07795; -. DR PATRIC; fig|136857.5.peg.1549; -. DR KO; K03665; -. DR Proteomes; UP000035540; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000035540}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000035540}. FT DOMAIN 284 455 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 243 277 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 514 AA; 56114 MW; D200D8D3233D2DD8 CRC64; MTESDNNNRT SHDSHEDLLA RAFRDNAPQP SADEDPGTDL SGIISPTVGE LDLEERNALR RTSDTTIRSE EIQDGFEVEY RKLRLEQVIL VGVWTEGTSA EVEANMAELS ALAETAGAEV LETLYQRRDK PDPGTFIGSG KVNELKEIIA ATGADTVVCD GELTPGQLVA LESALNLKVI DRTMLILDIF AQHAKSKEGK AQVGLAQMEY LYTRVRGWGG NLSRQAGGRA GSNGGVGLRG PGETRIEADR RRLRTDMAKL RRELAGMKTA REIKRQRRQD STIPQIAIAG YTNAGKSSLI NAMTGAGVLV ENALFATLDP TTRRAELADG RAVVFTDTVG FVRHLPTQLV EAFKSTLEEV LAADLMLHVV DGSDPFPLKQ IDAVNKVIYD IVKETGESAP PEIIVVNKID AADPLVLAEL RHAFDRENVV YVSALTKEGI PELEARIELF LNSLDAHVVV LIPFTRGDIV SRLHEYGTVR KEEYGADGTL IDVRLPRSLA AELAEFIVED NPGD // ID A0A0G3HEY7_9CORY Unreviewed; 509 AA. AC A0A0G3HEY7; DT 16-SEP-2015, integrated into UniProtKB/TrEMBL. DT 16-SEP-2015, sequence version 1. DT 07-JUN-2017, entry version 12. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:AKK11290.1}; GN ORFNames=CUTER_06505 {ECO:0000313|EMBL:AKK11290.1}; OS Corynebacterium uterequi. OC Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae; OC Corynebacterium. OX NCBI_TaxID=1072256 {ECO:0000313|EMBL:AKK11290.1, ECO:0000313|Proteomes:UP000035548}; RN [1] {ECO:0000313|Proteomes:UP000035548} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 45634 {ECO:0000313|Proteomes:UP000035548}; RA Ruckert C., Albersmeier A., Winkler A., Tauch A.; RT "Complete genome sequence of Corynebacterium uterequi DSM 45634, RT isolated from the uterus of a maiden mare."; RL Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP011546; AKK11290.1; -; Genomic_DNA. DR RefSeq; WP_047259732.1; NZ_CP011546.1. DR EnsemblBacteria; AKK11290; AKK11290; CUTER_06505. DR KEGG; cut:CUTER_06505; -. DR PATRIC; fig|1072256.5.peg.1285; -. DR KO; K03665; -. DR Proteomes; UP000035548; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000035548}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000035548}. FT DOMAIN 280 451 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 239 273 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 509 AA; 55679 MW; A4834B533874C806 CRC64; MTKFTSYDTD QLLSQAFKDN APQASEHNPD EGVDLSGLES PTTGQLDLEE RNSFRSVAQG STGKTSEKEA EFEVEYRKLR LEQVILVGVW TEGTTAQVEA NMQELASLAE TAGAEVLELL YQKRDRPDPG TYIGSGKVEE LRRIVEATGA DTVVCDGELS PGQMVALEDR LKVKVIDRTM LILDIFAQHA KSKEGKAQVS LAQMEYLYTR VRGWGGNLSR QAGGRAGSNG GVGLRGPGET RIEADRRRLR TEMARLRREL QGMKTAREVK RARRQESTVP KIAIAGYTNA GKSSLINAMT GAGVLVEDAL FATLDPTTRR TTLPDGRAIV FTDTVGFVRH LPTQLVEAFK STLEEVLGAD LILHVVDGSA PFPLQQIEAV NAVIYDVVKE SGEEVPPEII VINKIDAADP LILAELRHVL DRDNVVYVSA ATGEGVAELA TRIELFLNSL DARVTLVVPF TRGDVVSRVH ELGTVLKEDY EAAGTRLDVR LPQRLADELR EFVVSPTEG // ID A0A0G3IPM6_9MYCO Unreviewed; 466 AA. AC A0A0G3IPM6; DT 16-SEP-2015, integrated into UniProtKB/TrEMBL. DT 16-SEP-2015, sequence version 1. DT 07-JUN-2017, entry version 12. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=AB431_11790 {ECO:0000313|EMBL:AKK27251.1}; OS Mycobacterium sp. EPa45. OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae; OC Mycobacterium. OX NCBI_TaxID=1545728 {ECO:0000313|EMBL:AKK27251.1, ECO:0000313|Proteomes:UP000035237}; RN [1] {ECO:0000313|Proteomes:UP000035237} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=EPa45 {ECO:0000313|Proteomes:UP000035237}; RA Kato H., Ogawa N., Ohtsubo Y., Ohshima K., Toyoda A., Yamazoe A., RA Mori H., Maruyama F., Nagata Y., Hattori M., Fujiyama A., Kurokawa K., RA Tsuda M.; RT "Complete Genome Sequence of a Phenanthrene Degrader, Mycobacterium RT sp. Strain EPa45, Isolated from a Phenanthrene-Degrading Consortium."; RL Genome Announc.0:0-0(2015). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP011773; AKK27251.1; -; Genomic_DNA. DR RefSeq; WP_047330077.1; NZ_CP011773.1. DR EnsemblBacteria; AKK27251; AKK27251; AB431_11790. DR KEGG; mye:AB431_11790; -. DR PATRIC; fig|1545728.4.peg.2402; -. DR KO; K03665; -. DR Proteomes; UP000035237; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000313|EMBL:AKK27251.1}; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000035237}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900, KW ECO:0000313|EMBL:AKK27251.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000035237}. FT DOMAIN 244 413 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 203 237 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 466 AA; 50300 MW; 479B1B74DA733480 CRC64; MTKANSPDPS VGELALEDRA ALRRVAGLST ELTDVSEVEY RQLRLERVVL VGVWTEGSAA DSEASLAELA ALAETAGSEV LEGLIQRRDK PDPSTYIGSG KAQELRQIVI ATGADTVICD GELSPAQLNA LEKVVKVKVI DRTALILDIF AQHATSREGK AQVAYAQMEY MLPRLRGWGE SMSRQGGGAG GSGGGVGTRG PGETKIETDR RRIRERMSKL RREIKDMKQI RDTQRSRRLH SDTASIAIVG YTNAGKSSLL NALTGAGVLV QNALFATLEP TTRRGELDDG RPFVLTDTVG FVRHLPTQLV EAFRSTLEEV VDADLLVHVV DGSDSNPLAQ IEAVRQVIRE VQNDHHAPPA PELLVVNKID AADDLTLAQL RRALPGAVFV SAHTGEGLPR LRSRLGELIE PREVTVDVTI PYDRGDLVAR LHSDGHVDAV EHTDAGTRLK ARVPAALAAG LRDFSS // ID A0A0G3M1X9_9FLAO Unreviewed; 407 AA. AC A0A0G3M1X9; DT 16-SEP-2015, integrated into UniProtKB/TrEMBL. DT 16-SEP-2015, sequence version 1. DT 05-JUL-2017, entry version 13. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=OK18_08405 {ECO:0000313|EMBL:AKK72640.1}; OS Chryseobacterium gallinarum. OC Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales; OC Flavobacteriaceae; Chryseobacterium. OX NCBI_TaxID=1324352 {ECO:0000313|EMBL:AKK72640.1, ECO:0000313|Proteomes:UP000035213}; RN [1] {ECO:0000313|EMBL:AKK72640.1, ECO:0000313|Proteomes:UP000035213} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 27622 {ECO:0000313|EMBL:AKK72640.1, RC ECO:0000313|Proteomes:UP000035213}; RA Park G.-S., Hong S.-J., Jung B.K., Khan A.R., Kwak Y., Shin J.-H.; RL Submitted (NOV-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP009928; AKK72640.1; -; Genomic_DNA. DR RefSeq; WP_050021670.1; NZ_CP009928.1. DR EnsemblBacteria; AKK72640; AKK72640; OK18_08405. DR GeneID; 31907388; -. DR KEGG; cgn:OK18_08405; -. DR PATRIC; fig|1324352.5.peg.1764; -. DR KO; K03665; -. DR Proteomes; UP000035213; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000035213}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000035213}. FT DOMAIN 200 384 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 407 AA; 47249 MW; 818DFF4D10F69148 CRC64; MLEKKEHNYE KAVLVGVITQ NQDEEKLVEY MDELEFLAFT AGATVQKRFT QKLTQPDSKT FIGSGKALEI KEYVKENEIG TVIFDDELSP SQLKNLEREM EVKILDRTNL ILDIFAQRAQ TSYARTQVEL AQYQYLLPRL TRMWTHLERQ KGGIGMRGPG ETEIETDRRI IRDRITLLKD KLKTIDKQMA TQRNNRGKVV RAALVGYTNV GKSTLMNSLS KSEVFAENKL FATLDTTVRK VVIGNLPFLL TDTVGFIRKL PTQLVESFKS TLDEVREADL LIHVVDISHE SFEDHIASVN QILMEINAHQ KPMIMVFNKI DDFSYEKKDE DDLTPGTKKN ISLEEWKKTW MAKSKYPTVF ISALTKENFP EMKKLIYDEV MKIHISRFPY NDFLFEYFDN DEEENTN // ID A0A0G3QHV7_KLUIN Unreviewed; 426 AA. AC A0A0G3QHV7; DT 16-SEP-2015, integrated into UniProtKB/TrEMBL. DT 16-SEP-2015, sequence version 1. DT 30-AUG-2017, entry version 15. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=AB182_22885 {ECO:0000313|EMBL:AKL15404.1}, GN B2M27_01575 {ECO:0000313|EMBL:ORJ52101.1}; OS Kluyvera intermedia (Enterobacter intermedius). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; OC Enterobacteriaceae; Kluyvera. OX NCBI_TaxID=61648 {ECO:0000313|EMBL:AKL15404.1, ECO:0000313|Proteomes:UP000035479}; RN [1] {ECO:0000313|EMBL:AKL15404.1, ECO:0000313|Proteomes:UP000035479} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CAV1151 {ECO:0000313|EMBL:AKL15404.1, RC ECO:0000313|Proteomes:UP000035479}; RA Sheppard A.E., Stoesser N., Wilson D., Sebra R., Kasarskis A., RA Anson L., Giess A., Pankhurst L., Vaughan A., Grim C.J., Cox H., RA Yeh A., Sifri C.D., Walker S., Peto T.E., Crook D.W., Mathers A.J.; RT "Rapid spread of a carbapenem resistance gene driven by multiple RT levels of genetic mobility."; RL Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:ORJ52101.1, ECO:0000313|Proteomes:UP000192521} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=FOSA7093 {ECO:0000313|EMBL:ORJ52101.1, RC ECO:0000313|Proteomes:UP000192521}; RA Thele R.; RT "Draft genome sequence of a Kluyvera intermedia isolate from a patient RT with a pancreatic abscess."; RL Submitted (FEB-2017) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP011602; AKL15404.1; -; Genomic_DNA. DR EMBL; MWPR01000002; ORJ52101.1; -; Genomic_DNA. DR RefSeq; WP_047373417.1; NZ_MWPR01000002.1. DR EnsemblBacteria; AKL15404; AKL15404; AB182_22885. DR GeneID; 32370428; -. DR KEGG; kin:AB182_22885; -. DR PATRIC; fig|61648.5.peg.4185; -. DR KO; K03665; -. DR Proteomes; UP000035479; Chromosome. DR Proteomes; UP000192521; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000035479, KW ECO:0000313|Proteomes:UP000192521}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}. FT DOMAIN 198 365 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 426 AA; 48149 MW; 40497DC2334661C8 CRC64; MFDRYDAGEQ AVLVHIYFSQ DKDMEDLQEF ESLVSSAGVE AMQVITGSRK APHPKYFVGE GKAVEIADAV KATGASVVLF DHALTPAQER NLERLCECRV IDRTGLILDI FAQRARTHEG KLQVELAQLR HLATRLVRGW THLERQKGGI GLRGPGETQL ETDRRLLRNR ITQILSRLER VEKQREQGRR SRTKADIPTV SLVGYTNAGK STLFNQITEA QVYAADQLFA TLDPTLRRID VADVGETVLA DTVGFIRHLP HDLVAAFKAT LQETRQATLL LHVIDAADVR VADNIDAVNI VLEEIDAHEI PTLLVMNKID MLDDFEPRID RDDENKPIRV WLSAQTGIGV PLLFQALTER LSGEVAQHTL RLPAKEGRLR SRFYQLQAIE KEWMEEDGSL GIQVRMPIVD WRRLCKQEPA LEDYVV // ID A0A0G3V1Y1_9ACTN Unreviewed; 436 AA. AC A0A0G3V1Y1; DT 16-SEP-2015, integrated into UniProtKB/TrEMBL. DT 16-SEP-2015, sequence version 1. DT 07-JUN-2017, entry version 12. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=IMCC26256_11836 {ECO:0000313|EMBL:AKL73129.1}; OS Actinobacteria bacterium IMCC26256. OC Bacteria; Actinobacteria. OX NCBI_TaxID=1650658 {ECO:0000313|EMBL:AKL73129.1, ECO:0000313|Proteomes:UP000035517}; RN [1] {ECO:0000313|EMBL:AKL73129.1, ECO:0000313|Proteomes:UP000035517} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=IMCC26256 {ECO:0000313|EMBL:AKL73129.1, RC ECO:0000313|Proteomes:UP000035517}; RA Kim S.; RT "Genome sequencing of freshwater Actinobacteria."; RL Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP011489; AKL73129.1; -; Genomic_DNA. DR RefSeq; WP_052608489.1; NZ_CP011489.1. DR EnsemblBacteria; AKL73129; AKL73129; IMCC26256_11836. DR KEGG; abai:IMCC26256_11836; -. DR PATRIC; fig|1650658.3.peg.831; -. DR KO; K03665; -. DR Proteomes; UP000035517; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000035517}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000035517}. FT DOMAIN 217 382 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 176 203 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 436 AA; 47724 MW; 60B5B29BCC0013E6 CRC64; MSSGQQGRGR RRLTATEVDL EVVRQRALLV GTGIGTRSVE VAEESLAELA RLTDTAGADA VEIVLQRRDH PDSRTYIGKG KAEELRESVK ALDIDVVIFD DELSPAQQRN LEKIFEVDVV DRVALILDIF AQHAASQEGM LQVELAQLRY QMPRLRGRGG VLSQQGGGIG TRGPGETQLE VDRRRIQRRV ARLERDLSEL VRKRGTQRKA RMKIPMPNVA LVGYTNAGKS TVLNRITEAD VLVENRLFST LDPTTRRLRL SGGEIVLVSD TVGFVRRLPH QLVEAFRSTL EEVADADLLL HIVDAGAADI IGQVAAVRAV LTAVGASDLP EFMVINKTDT VDDATIAEVR RMLPDATTVS ALTGEGIPDL LELIATQLRS VSNVVVLGVP YARGDVLASL HREGEVLVEV HEAEQVRVQV RISEAAAGRF AEFRIP // ID A0A0G3X8W1_9SPHN Unreviewed; 449 AA. AC A0A0G3X8W1; DT 16-SEP-2015, integrated into UniProtKB/TrEMBL. DT 16-SEP-2015, sequence version 1. DT 05-JUL-2017, entry version 14. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=AM2010_959 {ECO:0000313|EMBL:AKM07036.1}; OS Altererythrobacter marensis. OC Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales; OC Erythrobacteraceae; Altererythrobacter. OX NCBI_TaxID=543877 {ECO:0000313|EMBL:AKM07036.1, ECO:0000313|Proteomes:UP000037643}; RN [1] {ECO:0000313|EMBL:AKM07036.1, ECO:0000313|Proteomes:UP000037643} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=KCTC 22370 {ECO:0000313|EMBL:AKM07036.1, RC ECO:0000313|Proteomes:UP000037643}; RA Kim K.M.; RL Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP011805; AKM07036.1; -; Genomic_DNA. DR EnsemblBacteria; AKM07036; AKM07036; AM2010_959. DR KEGG; amx:AM2010_959; -. DR PATRIC; fig|543877.4.peg.969; -. DR KO; K03665; -. DR Proteomes; UP000037643; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000037643}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000037643}. FT DOMAIN 215 391 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 181 208 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 449 AA; 48940 MW; 9FDE42DA2E47A86B CRC64; MGRRRRLSFD DNLLSEVSRG ARAVVVCPDI RGQQHDLDAD SRLAEACGLA LAIGIVVADA SVIPVRQVKP GTLFGSGQVE NIATACEQHE AELVVIDGAL SAIQQRNLEE SLRRKVIDRT GLILEIFGER AATAEGRLQV ELAHLDYQQS RLVRSWTHLE RQRGGFGFLG GPGETQIEAD RRMIRQRMGR LRKELEQVRK TRALHRERRS RAPWPVIALV GYTNAGKSTL FNKLTGEAVM AEDLLFATLD PTMRSVRLPG VEKVILSDTV GFISDLPTQL VAAFRATLEE VTGADVIVHV RDMANPASAA QKAQVLAVLG DLGVANGEEG QGDAIPVVEA WNKTDLLTSP EHDRLIESAQ LDENSVPISA VTGEGVEALL TRLDALLTAG AKVHEIVLPA ASGQKIAWLH AHGEVIEDDV VDEGGEEPRR RVLVRLTPKE LGRFESLVD // ID A0A0G3XFW4_9SPHN Unreviewed; 455 AA. AC A0A0G3XFW4; DT 16-SEP-2015, integrated into UniProtKB/TrEMBL. DT 16-SEP-2015, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=AB433_08810 {ECO:0000313|EMBL:AKM10052.1}; OS Croceicoccus naphthovorans. OC Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales; OC Erythrobacteraceae; Croceicoccus. OX NCBI_TaxID=1348774 {ECO:0000313|EMBL:AKM10052.1, ECO:0000313|Proteomes:UP000035287}; RN [1] {ECO:0000313|EMBL:AKM10052.1, ECO:0000313|Proteomes:UP000035287} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=PQ-2 {ECO:0000313|EMBL:AKM10052.1, RC ECO:0000313|Proteomes:UP000035287}; RA Zeng Y., Huang Y.; RL Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP011770; AKM10052.1; -; Genomic_DNA. DR RefSeq; WP_047820730.1; NZ_CP011770.1. DR EnsemblBacteria; AKM10052; AKM10052; AB433_08810. DR KEGG; cna:AB433_08810; -. DR PATRIC; fig|1348774.3.peg.1848; -. DR KO; K03665; -. DR Proteomes; UP000035287; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000035287}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000035287}. FT DOMAIN 222 399 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 188 215 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 455 AA; 49584 MW; 5C910C6F7B434B4D CRC64; MSTCPVIGTK KTKGKTLTED VSGEVSRGAK AVVVLPDIRA AHIQDPEARL AEGCGLALAI GIEVVESFIV PVRDVRPATL FGSGQVDRIK LACDMEEAEL VIVDGALSAI QQRNLEEKIG RKVIDRTGLI LEIFGERAAT AEGRLQVELA HLDYQAGRLV RSWTHLERQR GGFGFLGGPG ETQIEADRRM IRDRMGRLRR ELEQVRRTRA LHRARRGRAP WPVVALVGYT NAGKSTLFNR MTGAGVMAED LLFATLDPTM RGITLPGVEK AILSDTVGFI SDLPTQLVAA FRATLEEVTG ADVIVHVRDI SSPMTDMQKA EVEQVLADLG VNTGEEDSLV IPVVEAWNKW DALTEVRSEE LTEQAEREER AVVPLSALTG LGVVALERTV SDILTASAVV HSFTLPATDG QRIAWLHAHG EVLDERTGKG EDGSPQLEMA VRLDPREYGK FLALS // ID A0A0G4EVX6_VITBC Unreviewed; 719 AA. AC A0A0G4EVX6; DT 16-SEP-2015, integrated into UniProtKB/TrEMBL. DT 16-SEP-2015, sequence version 1. DT 07-JUN-2017, entry version 10. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:CEM02357.1}; GN ORFNames=Vbra_8316 {ECO:0000313|EMBL:CEM02357.1}; OS Vitrella brassicaformis (strain CCMP3155). OC Eukaryota; Alveolata; Chromerida; Vitrella. OX NCBI_TaxID=1169540 {ECO:0000313|EMBL:CEM02357.1, ECO:0000313|Proteomes:UP000041254}; RN [1] {ECO:0000313|EMBL:CEM02357.1, ECO:0000313|Proteomes:UP000041254} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Zhu J., Qi W., Song R.; RL Submitted (NOV-2014) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CDMY01000324; CEM02357.1; -; Genomic_DNA. DR EnsemblProtists; CEM02357; CEM02357; Vbra_8316. DR OMA; IIVLHPI; -. DR Proteomes; UP000041254; Unassembled WGS sequence. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR CDD; cd01878; HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000041254}; KW Reference proteome {ECO:0000313|Proteomes:UP000041254}. FT DOMAIN 451 621 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 719 AA; 80415 MW; 3BBAA807AEFF0363 CRC64; MAARALSVAR RGLQRHHSIY QRTSARLLRR FSSAREAARS PEEASSDSSN SADVSWDVTG NLKHKLHGSR PLVMVIHPVL KGKRKREILW DAEEALGLVR AAHWDPLPGP TEPANGWNQN ELAKVGHLQR LVQEGNLTLP KEWHFHRTMR DDDENTDEES GDEDLDPNEA AWRNSTLRRQ WAESCCVRVR QVHPGNFFQK GKLEELAMIY TYQPAHYVFV NSSLTGTQQR NLELIFKNAL NVWAARKMER KELPIAGLVH SATSIAANTT ELDILAQDRL KLQADSGKAL VGTEGQADAL AQIGADHLGE AVAPVDETEE EIDERRGAAT RVEVVDRNRV VLEIFALRAR TRQAILQVAL ARTNYFKSRL SLNTPNRFKQ LLMSVKAAAG VQSTYADWVE DVSTTYHLGD GEQIGEYEGR LLEIAMTKLR AQLEEVKKAR KLQREARRGA GTVALVGYTN VGKTAIMNRL TGSDLRVRDV LFQTLDTTMR KVRLPSGTKA ILVDSVGFIQ DLPHALYDAF QATLEETINA DVLLHVRDVS HPQWEMHKQV VLDSLHDCGM SLERLSSNVV EVWNKVDLLD EEGFRSMLSE LPPNAVPVSA MDASGLDVLL KLLDQVVNSV LSRSTITLRL PVREVQERMR VLNRLGITIS YGRSLDAGMT SDSEGWRETF AKEDEDEEGG IRVSEDGQSV LVDVIADYPA LARYEALYEK RGGEPGEGR // ID A0A0G4F628_VITBC Unreviewed; 741 AA. AC A0A0G4F628; DT 16-SEP-2015, integrated into UniProtKB/TrEMBL. DT 16-SEP-2015, sequence version 1. DT 12-APR-2017, entry version 7. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:CEM07548.1}; GN ORFNames=Vbra_14466 {ECO:0000313|EMBL:CEM07548.1}; OS Vitrella brassicaformis (strain CCMP3155). OC Eukaryota; Alveolata; Chromerida; Vitrella. OX NCBI_TaxID=1169540 {ECO:0000313|EMBL:CEM07548.1, ECO:0000313|Proteomes:UP000041254}; RN [1] {ECO:0000313|EMBL:CEM07548.1, ECO:0000313|Proteomes:UP000041254} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Zhu J., Qi W., Song R.; RL Submitted (NOV-2014) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CDMY01000376; CEM07548.1; -; Genomic_DNA. DR EnsemblProtists; CEM07548; CEM07548; Vbra_14466. DR Proteomes; UP000041254; Unassembled WGS sequence. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000041254}; KW Reference proteome {ECO:0000313|Proteomes:UP000041254}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1 19 {ECO:0000256|SAM:SignalP}. FT CHAIN 20 741 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5005188344. FT DOMAIN 365 533 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 741 AA; 82314 MW; C861642002A61D55 CRC64; MTLLAVTFTL LGFVVFADAF VPHSSSLVLR FHSKRPASPR PLLQQQQHQQ QQQQRQHSAE DAARLWEFDD RASEKAEEWT RDEVKEASIL VDEIQHKQGE ADGQGQGVAD GGEVEDADAS VGYIRDLDEI LMERAIRYYD PRESHIKRRE KCFLVGLEMK RQPGSRSSDG SSQEDEFTLE ESLGELSELA GTAGLEVVGS TYQRVAKPNA KTFIGPGKVN EIRRSMQALG CKTAIIDAEL TPAQQKNLEE AFGGIPGGIK VLDRTALILD IFAQHARTRE GKLQVELALA QYRLPRLTRL WTHLERQVGG KGGEGSVGLR GPGESQIETD RRLLYDQILT LQKRLDKVKQ HREMHRKRRK KLGMPVIALV GYTNTGKSTI LNALTRAGVL AEPMLFATLD PTTRKIRLPG SSIHPEVLVT DTVGFIQKLP TTLVASFRAT LEEVREADVI VHMVDKSNPL NDKQQRAVLG VLHELECDDK PIVTVWNKID LLDDPGQVQI DAALAGCVAV SAKTAMGMED VTAALGDALE KLLQPIEVDI PYAEGQLVSK VFELGTVDFV EYREGSTYLS AKVPVDLLGR LEPYLVQEDD TQQQQEDGAG EPTKPESRER EVDWNAIAKR RHRVRDRTHE LIWGENSQHQ EQQQEEQPTP KTPVAAPAAV QASSNSRPHV KPHVPPSPSP AALQPPAVTM STTPMQPQLL HGGHLSLSPP AEAEDLHYHQ LKEQMEHDAL QLWLEMTHTG S // ID A0A0G9FFG8_LACPN Unreviewed; 431 AA. AC A0A0G9FFG8; DT 16-SEP-2015, integrated into UniProtKB/TrEMBL. DT 16-SEP-2015, sequence version 1. DT 05-JUL-2017, entry version 22. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=A8P51_02025 {ECO:0000313|EMBL:ANM73241.1}, GN AVR82_15715 {ECO:0000313|EMBL:AOB20984.1}, GN AYO51_14575 {ECO:0000313|EMBL:KYK50823.1}, GN BIZ32_03595 {ECO:0000313|EMBL:ARO03033.1}, GN IV39_GL000907 {ECO:0000313|EMBL:KRN35755.1}, GN Lp19_2293 {ECO:0000313|EMBL:KZU94319.1}, GN LPJSA22_00872 {ECO:0000313|EMBL:ODO60923.1}, GN Nizo1839_1264 {ECO:0000313|EMBL:KZT81466.1}, GN Nizo2802_2935 {ECO:0000313|EMBL:KZU49336.1}, GN SRCM101060_02928 {ECO:0000313|EMBL:OAZ72395.1}; OS Lactobacillus plantarum. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; OC Lactobacillus. OX NCBI_TaxID=1590 {ECO:0000313|EMBL:KRN35755.1, ECO:0000313|Proteomes:UP000051742}; RN [1] {ECO:0000313|EMBL:KRN35755.1, ECO:0000313|Proteomes:UP000051742} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 13273 {ECO:0000313|EMBL:KRN35755.1, RC ECO:0000313|Proteomes:UP000051742}; RX PubMed=26415554; DOI=10.1038/ncomms9322; RA Sun Z., Harris H.M., McCann A., Guo C., Argimon S., Zhang W., Yang X., RA Jeffery I.B., Cooney J.C., Kagawa T.F., Liu W., Song Y., Salvetti E., RA Wrobel A., Rasinkangas P., Parkhill J., Rea M.C., O'Sullivan O., RA Ritari J., Douillard F.P., Paul Ross R., Yang R., Briner A.E., RA Felis G.E., de Vos W.M., Barrangou R., Klaenhammer T.R., RA Caufield P.W., Cui Y., Zhang H., O'Toole P.W.; RT "Expanding the biotechnology potential of lactobacilli through RT comparative genomics of 213 strains and associated genera."; RL Nat. Commun. 6:8322-8322(2015). RN [2] {ECO:0000313|EMBL:AOB20984.1, ECO:0000313|Proteomes:UP000093269} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=KP {ECO:0000313|EMBL:AOB20984.1, RC ECO:0000313|Proteomes:UP000093269}; RA Petkau K., Fast D., Duggal A., Foley E.; RT "Comparative evaluation of the genomes of common bacterial members of RT the Drosophila intestinal community."; RL Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases. RN [3] {ECO:0000313|Proteomes:UP000076835, ECO:0000313|Proteomes:UP000076882, ECO:0000313|Proteomes:UP000077044} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=19.1 {ECO:0000313|EMBL:KZU94319.1, RC ECO:0000313|Proteomes:UP000076882}, RC Nizo1839 {ECO:0000313|EMBL:KZT81466.1, RC ECO:0000313|Proteomes:UP000077044}, and RC Nizo2802 {ECO:0000313|EMBL:KZU49336.1, RC ECO:0000313|Proteomes:UP000076835}; RA Martino M.E.; RT "Comparative genomics of 54 Lactobacillus plantarum strains reveals RT genomic uncoupling from niche constraints."; RL Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases. RN [4] {ECO:0000313|EMBL:KYK50823.1, ECO:0000313|Proteomes:UP000075744} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=E2C2 {ECO:0000313|EMBL:KYK50823.1, RC ECO:0000313|Proteomes:UP000075744}; RA Ploux O.; RL Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases. RN [5] {ECO:0000313|EMBL:OAZ72395.1, ECO:0000313|Proteomes:UP000093664} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SRCM101060 {ECO:0000313|EMBL:OAZ72395.1, RC ECO:0000313|Proteomes:UP000093664}; RA Song Y.R.; RT "Genome sequencing of Lactobacillus plantarum strain SRCM101060."; RL Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases. RN [6] {ECO:0000313|EMBL:ANM73241.1, ECO:0000313|Proteomes:UP000078583} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NCU116 {ECO:0000313|EMBL:ANM73241.1, RC ECO:0000313|Proteomes:UP000078583}; RA Huang T., Xiong T.; RT "Lactobacillus plantarum NCU116 Genome sequencing and assembly RT isolated from Chinese pickle."; RL Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases. RN [7] {ECO:0000313|EMBL:ODO60923.1, ECO:0000313|Proteomes:UP000094892} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=JSA22 {ECO:0000313|EMBL:ODO60923.1, RC ECO:0000313|Proteomes:UP000094892}; RA Choi H.S.; RT "Genome sequencing of Lactobacillus plantarum JSA22, isolated from RT fermented soybean paste."; RL Submitted (AUG-2016) to the EMBL/GenBank/DDBJ databases. RN [8] {ECO:0000313|EMBL:ARO03033.1, ECO:0000313|Proteomes:UP000193023} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=TMW 1.277 {ECO:0000313|EMBL:ARO03033.1, RC ECO:0000313|Proteomes:UP000193023}; RA Kafka T.A., Vogel R.F.; RT "Lactobacillus species Genome sequencing and assembly."; RL Submitted (SEP-2016) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP016071; ANM73241.1; -; Genomic_DNA. DR EMBL; CP013749; AOB20984.1; -; Genomic_DNA. DR EMBL; CP017363; ARO03033.1; -; Genomic_DNA. DR EMBL; JQAW01000065; KRN35755.1; -; Genomic_DNA. DR EMBL; LSST01000110; KYK50823.1; -; Genomic_DNA. DR EMBL; LUWB01000030; KZT81466.1; -; Genomic_DNA. DR EMBL; LUWZ01000089; KZU49336.1; -; Genomic_DNA. DR EMBL; LUXM01000033; KZU94319.1; -; Genomic_DNA. DR EMBL; LYUK01000080; OAZ72395.1; -; Genomic_DNA. DR EMBL; MCOL01000001; ODO60923.1; -; Genomic_DNA. DR RefSeq; WP_003641141.1; NZ_MUZE01000008.1. DR EnsemblBacteria; ANM73241; ANM73241; A8P51_02025. DR EnsemblBacteria; KRN35755; KRN35755; IV39_GL000907. DR EnsemblBacteria; KYK50823; KYK50823; AYO51_14575. DR EnsemblBacteria; KZT81466; KZT81466; Nizo1839_1264. DR EnsemblBacteria; KZU49336; KZU49336; Nizo2802_2935. DR EnsemblBacteria; KZU94319; KZU94319; Lp19_2293. DR EnsemblBacteria; OAZ72395; OAZ72395; SRCM101060_02928. DR EnsemblBacteria; ODO60923; ODO60923; LPJSA22_00872. DR KEGG; lpb:SH83_03625; -. DR PATRIC; fig|1590.142.peg.745; -. DR KO; K03665; -. DR Proteomes; UP000051742; Unassembled WGS sequence. DR Proteomes; UP000075744; Unassembled WGS sequence. DR Proteomes; UP000076835; Unassembled WGS sequence. DR Proteomes; UP000076882; Unassembled WGS sequence. DR Proteomes; UP000077044; Unassembled WGS sequence. DR Proteomes; UP000078583; Chromosome. DR Proteomes; UP000093269; Chromosome. DR Proteomes; UP000093664; Unassembled WGS sequence. DR Proteomes; UP000094892; Unassembled WGS sequence. DR Proteomes; UP000193023; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000051742, KW ECO:0000313|Proteomes:UP000075744, ECO:0000313|Proteomes:UP000076835, KW ECO:0000313|Proteomes:UP000076882}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}. FT DOMAIN 207 375 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 431 AA; 47764 MW; F2514DE3865A4ECF CRC64; MSETNAQKVQ EVIIAGMSKT VANYDYAMSE LEALVAANNM HAALRIDQGL EKPNPATFFG KGKVVEIKEV AAANDLHIMV INADLTPSQV RNLEEQTDIQ IIDRTGLILE IFGNRARSKE AKLQVKIAQL QYQLPRLRTS ISNRLDQQAG AAAGGGGGFT NRGAGETQLE LNRRTIQDRI SHAKHELKEL NKDEVVRRSQ RDKAGLPNVA LVGYTNAGKS TTMNGLVKLF GKGEDKQVFE KDMLFATLDT SIRQLTFPDN KQLLLSDTVG FVSDLPHNLI NAFRSTLAEA ANADLLIQVI DYADPHYKEM MATTEKTLKE IGVHDVPMIY AFNKADLTEA DYPNQQDDQL IYTARDEASL QALTSMIKAK VFKNYVTTTL LIPFNDGEVV AYLNDHANIL KTDYLADGTQ LTVELNTVDA QRYEKYVVTP A // ID A0A0G9HCV3_9GAMM Unreviewed; 435 AA. AC A0A0G9HCV3; DT 16-SEP-2015, integrated into UniProtKB/TrEMBL. DT 16-SEP-2015, sequence version 1. DT 07-JUN-2017, entry version 15. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=BJI69_00420 {ECO:0000313|EMBL:APG02516.1}, GN Y883_08705 {ECO:0000313|EMBL:KLD67316.1}; OS Luteibacter rhizovicinus DSM 16549. OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales; OC Rhodanobacteraceae; Luteibacter. OX NCBI_TaxID=1440763 {ECO:0000313|EMBL:KLD67316.1, ECO:0000313|Proteomes:UP000035585}; RN [1] {ECO:0000313|EMBL:KLD67316.1, ECO:0000313|Proteomes:UP000035585} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 16549 {ECO:0000313|EMBL:KLD67316.1, RC ECO:0000313|Proteomes:UP000035585}; RX PubMed=25481407; DOI=10.1007/s10482-014-0344-8; RA Naushad S., Adeolu M., Wong S., Sohail M., Schellhorn H.E., RA Gupta R.S.; RT "A phylogenomic and molecular marker based taxonomic framework for the RT order Xanthomonadales: proposal to transfer the families Algiphilaceae RT and Solimonadaceae to the order Nevskiales ord. nov. and to create a RT new family within the order Xanthomonadales, the family RT Rhodanobacteraceae fam. nov., containing the genus Rhodanobacter and RT its closest relatives."; RL Antonie Van Leeuwenhoek 107:467-485(2015). RN [2] {ECO:0000313|EMBL:APG02516.1, ECO:0000313|Proteomes:UP000182987} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=LJ96T {ECO:0000313|EMBL:APG02516.1, RC ECO:0000313|Proteomes:UP000182987}; RA Capua I., De Benedictis P., Joannis T., Lombin L.H., Cattoli G.; RL Submitted (SEP-2016) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP017480; APG02516.1; -; Genomic_DNA. DR EMBL; JPLB01000028; KLD67316.1; -; Genomic_DNA. DR RefSeq; WP_046967361.1; NZ_JPLB01000028.1. DR EnsemblBacteria; KLD67316; KLD67316; Y883_08705. DR KEGG; lrz:BJI69_00420; -. DR PATRIC; fig|1440763.5.peg.1569; -. DR KO; K03665; -. DR Proteomes; UP000035585; Unassembled WGS sequence. DR Proteomes; UP000182987; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000035585}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000035585}. FT DOMAIN 200 366 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 166 193 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 435 AA; 47236 MW; 9EFB3A087F591480 CRC64; MFDRQKKGER AVLVLPHSRG EGDAIRRGEE FAELVASAGA EVLASIPARV ATPNPRFYIG SGKADEVAEA VRALEADLVL VDHELTPVQE RNLEKHLGTR VVDRAGLILD IFAQRARSHE GKLEVELAQL KHVATRLVRG WTHLDAQRGG AIGNRGPGET QLETDRRLLA ERVKMLSKRL EKVQTQRDQQ RRSRLRNTVP RVALVGYTNA GKSTLFNALT TGGVYVADQL FATLDPTVRK IDGLACGPAV VADTVGFIRE LPHDLVAAFR ATLAEARDAD LLIHVSDAAD EEREILRKVV NEVLEEIGAG DVPQLSVMNK VDLIDAEPRV DRGDDGKPRQ VWLSAASGAG LDGLRDALGE LLGGDRIRAG LELPLTAGRL HARLKAAGAI AGEAIDEHGW HLDIDAPRSV LAPLIGDDVH GRPLRDLIDP PHAEF // ID A0A0G9MQ54_9SPHN Unreviewed; 421 AA. AC A0A0G9MQ54; DT 16-SEP-2015, integrated into UniProtKB/TrEMBL. DT 16-SEP-2015, sequence version 1. DT 05-JUL-2017, entry version 13. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=AAW01_02265 {ECO:0000313|EMBL:KLE32867.1}, GN BMF35_a1874 {ECO:0000313|EMBL:APE28703.1}; OS Erythrobacter gangjinensis. OC Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales; OC Erythrobacteraceae; Erythrobacter. OX NCBI_TaxID=502682 {ECO:0000313|EMBL:KLE32867.1, ECO:0000313|Proteomes:UP000053070}; RN [1] {ECO:0000313|EMBL:KLE32867.1, ECO:0000313|Proteomes:UP000053070} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K7-2 {ECO:0000313|EMBL:KLE32867.1, RC ECO:0000313|Proteomes:UP000053070}; RA Zhuang L., Liu Y., Shao Z.; RT "The draft genome sequence of Erythrobacr gangjinensis K7-2."; RL Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:APE28703.1, ECO:0000313|Proteomes:UP000183202} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CGMCC1.15024 {ECO:0000313|EMBL:APE28703.1, RC ECO:0000313|Proteomes:UP000183202}; RA Xu L., Wu Y.-H., Cheng H., Zhou Y.-G., Wu M., Cheng L., Xu X.-W.; RT "Complete genome sequence of two-chromosomal Erythrobacter RT gangjinensis CGMCC 1.15024T, isolated from seawater."; RL Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP018097; APE28703.1; -; Genomic_DNA. DR EMBL; LBHC01000001; KLE32867.1; -; Genomic_DNA. DR EnsemblBacteria; KLE32867; KLE32867; AAW01_02265. DR PATRIC; fig|502682.8.peg.463; -. DR Proteomes; UP000053070; Unassembled WGS sequence. DR Proteomes; UP000183202; Chromosome i. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000053070}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000053070}. FT DOMAIN 190 365 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 156 183 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 421 AA; 46495 MW; 9071DEC8631E3967 CRC64; MCPDIRGQRR DEDPEARLEE AKGLALAIGI VVAHSFVLPV REVKPNTLFG EGQVQRIATD CELHEAELVI VDGALSPIQQ RNLEEKIGRK VIDRTGLILE IFGERAATAE GRLQVELAHL DYQQSRLVRS WTHLERQRGG FGFLGGPGET QIEADRRMIR DRMGRLRREL EQVRKTRELH RKRRGRAPWP VIALVGYTNA GKSTLFNRLT GADVMAEDLL FATLDPTMRA ITLPGVEKAI LSDTVGFISD LPTQLVAAFR ATLEEVTAAD IVLHVRDIAN PDNAAQKKQV LNILQDLGVV DETGQAQDAV LLEVWNKWDK LSAEQAEALA EIADQQDDVI RMSAQTGEGI DALGEKLGKV LTSGARTLSL TISASDGARI AWLHQHGEVL ADEDGGEGED GPMRQIEVRL TEKELGRFEA L // ID A0A0G9MXP8_9SPHN Unreviewed; 440 AA. AC A0A0G9MXP8; DT 16-SEP-2015, integrated into UniProtKB/TrEMBL. DT 16-SEP-2015, sequence version 1. DT 07-JUN-2017, entry version 12. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=AAW00_03850 {ECO:0000313|EMBL:KLE35562.1}; OS Erythrobacter luteus. OC Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales; OC Erythrobacteraceae; Erythrobacter. OX NCBI_TaxID=1581420 {ECO:0000313|EMBL:KLE35562.1, ECO:0000313|Proteomes:UP000053464}; RN [1] {ECO:0000313|EMBL:KLE35562.1, ECO:0000313|Proteomes:UP000053464} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=KA37 {ECO:0000313|EMBL:KLE35562.1, RC ECO:0000313|Proteomes:UP000053464}; RA Zhuang L., Liu Y., Shao Z.; RT "The draft genome sequence of Erythrobacter luteus KA37."; RL Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KLE35562.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LBHB01000001; KLE35562.1; -; Genomic_DNA. DR RefSeq; WP_047002965.1; NZ_LBHB01000001.1. DR EnsemblBacteria; KLE35562; KLE35562; AAW00_03850. DR PATRIC; fig|1581420.6.peg.778; -. DR Proteomes; UP000053464; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000053464}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000053464}. FT DOMAIN 207 382 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 173 200 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 440 AA; 48386 MW; 6A3C7B0C09D0DC56 CRC64; MDDDIEGEVT RGARALVVCP DVRGQRSAQD PEARLEEAGG LALAIGIVVA ESYVLNVRDV RPNTLFGEGQ VQRIATDCEL HEAELVIVDG ALSGIQQRNL EEKIGRKVID RTGLILEIFG ERAATAEGRL QVELAHLDYQ QSRLVRSWTH LERQRGGFGF LGGPGETQIE ADRRMIRDRM GKLRRELEQV RKTRELHRKR RGRAPWPVIA LVGYTNAGKS TLFNRMTGAD VMAEDLLFAT LDPTMRAIGL PGVEKAILSD TVGFISDLPT QLVAAFRATL EEVTAADIVL HVRDMANPDS TAQKREVLAV LEELGVVDEA GEGVDAPVIE VWNKWDALSE ERRVELEPLA GMDEDVLALS AITGEGVDAL RERLGEVLTA GAKRYSLLLP ASDGARIAWL HAHGEVIDDE DGGEGEDGPM RRLDVRLTDK EFGRFETLPS // ID A0A0H0DJ43_9ENTR Unreviewed; 426 AA. AC A0A0H0DJ43; A0A181CR47; DT 16-SEP-2015, integrated into UniProtKB/TrEMBL. DT 16-SEP-2015, sequence version 1. DT 30-AUG-2017, entry version 18. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:SAY91094.1}; GN ORFNames=AN693_0218640 {ECO:0000313|EMBL:OEH13386.1}, GN SAMEA3181516_00396 {ECO:0000313|EMBL:SAY91094.1}; OS Enterobacter kobei. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; OC Enterobacteriaceae; Enterobacter; Enterobacter cloacae complex. OX NCBI_TaxID=208224 {ECO:0000313|EMBL:SAY91094.1, ECO:0000313|Proteomes:UP000078120}; RN [1] {ECO:0000313|EMBL:OEH13386.1, ECO:0000313|Proteomes:UP000050484} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ST434:953099839 {ECO:0000313|EMBL:OEH13386.1, RC ECO:0000313|Proteomes:UP000050484}; RA Evans L.H., Alamgir A., Owens N., Weber N.D., Virtaneva K., RA Barbian K., Babar A., Rosenke K.; RL Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:SAY91094.1, ECO:0000313|Proteomes:UP000078120} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=3380STDY6027363 {ECO:0000313|EMBL:SAY91094.1, RC ECO:0000313|Proteomes:UP000078120}; RG Pathogen Informatics; RL Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LJEW02000095; OEH13386.1; -; Genomic_DNA. DR EMBL; FKLS01000001; SAY91094.1; -; Genomic_DNA. DR RefSeq; WP_014882228.1; NZ_LVUX01000021.1. DR EnsemblBacteria; KLG25460; KLG25460; YA53_04865. DR EnsemblBacteria; SAY91094; SAY91094; SAMEA3181516_00396. DR PATRIC; fig|1619246.3.peg.4975; -. DR Proteomes; UP000050484; Unassembled WGS sequence. DR Proteomes; UP000078120; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000050484, KW ECO:0000313|Proteomes:UP000078120}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}. FT DOMAIN 198 365 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 426 AA; 48034 MW; D6ADB6D3ABDAB53B CRC64; MFDRYDAGEQ AVLVHIYFSQ DKDMEDLQEF ESLVSSAGVE AMQVITGSRK APHPKYFVGE GKAVEIADAV KATGASVVLF DHALSPAQER NLEALCECRV IDRTGLILDI FAQRARTHEG KLQVELAQLR HLATRLVRGW THLERQKGGI GLRGPGETQL ETDRRLLRGR ITQILSRLER VEKQREQGRR ARTKADIPTV SLVGYTNAGK STLFNQITEA QVYAADQLFA TLDPTLRRID VADVGETVLA DTVGFIRHLP HDLVAAFKAT LQETRQATLL LHVIDAADVR VQENIDAVNV VLEEIDAHEI PTLLVMNKID MLEDFEPRID RDEENKPIRV WLSAQTGIGV PLLFQALTER LSGEVAQHTL RLPPQEGRLR SRFYQLQAIE KEWMEDDGSV GMQVRMPIVD WRRLCKQEPA LADYIV // ID A0A0H0XPD3_9SPHN Unreviewed; 444 AA. AC A0A0H0XPD3; DT 16-SEP-2015, integrated into UniProtKB/TrEMBL. DT 16-SEP-2015, sequence version 1. DT 07-JUN-2017, entry version 12. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=AAV99_09115 {ECO:0000313|EMBL:KLI63851.1}; OS Erythrobacter marinus. OC Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales; OC Erythrobacteraceae; Erythrobacter. OX NCBI_TaxID=874156 {ECO:0000313|EMBL:KLI63851.1, ECO:0000313|Proteomes:UP000053455}; RN [1] {ECO:0000313|EMBL:KLI63851.1, ECO:0000313|Proteomes:UP000053455} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=HWDM-33 {ECO:0000313|EMBL:KLI63851.1, RC ECO:0000313|Proteomes:UP000053455}; RA Zhuang L., Liu Y., Shao Z.; RT "The draft genome sequence of Erythrobacter marinus HWDM-33."; RL Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KLI63851.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LBHU01000002; KLI63851.1; -; Genomic_DNA. DR RefSeq; WP_047093666.1; NZ_LDCP01000002.1. DR EnsemblBacteria; KLI63851; KLI63851; AAV99_09115. DR PATRIC; fig|874156.12.peg.1868; -. DR Proteomes; UP000053455; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000053455}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000053455}. FT DOMAIN 209 384 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 175 202 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 444 AA; 48700 MW; 7BB16C3F6C90588B CRC64; MIVDDDIEGE VTRGARALVV SPEIRGQRSG EDPDARLEEA RGLALAIGIV VAESYVLKVR DVRPNTLFGE GQVQRIATDC ELHEAELVIV DGALSAIQQR NLEEKIGRKV IDRTGLILEI FGERAATAEG RLQVELAHLD YQQSRLVRSW THLERQRGGF GFLGGPGETQ IEADRRMIRE RMGKLRRELE QVRKTRELHR KRRGRAPWPV IALVGYTNAG KSTLFNRMTG ADVMAEDLLF ATLDPTMRAI SLPGVEKAIL SDTVGFISDL PTQLVAAFRA TLEEVTAADI VLHVRDIANP DTAQQKRQVL AVLEDLGVVD ENGDGVDAPV IEVWNKLDLL SEEDREDLAA IATNDDSVLP ISAITGEGIE ALASRLGAVL TEGARTYSFL LSASDGARIA WLHAHGEVLS EVEAGEGEIE GDLVRRIEVR LTDKEYGRFE GLAG // ID A0A0H0ZK14_9MICC Unreviewed; 522 AA. AC A0A0H0ZK14; DT 16-SEP-2015, integrated into UniProtKB/TrEMBL. DT 16-SEP-2015, sequence version 1. DT 07-JUN-2017, entry version 15. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=AA310_18550 {ECO:0000313|EMBL:KLI87408.1}, GN ATC04_12630 {ECO:0000313|EMBL:ALQ31319.1}; OS Arthrobacter sp. YC-RL1. OC Bacteria; Actinobacteria; Micrococcales; Micrococcaceae; Arthrobacter. OX NCBI_TaxID=1652545 {ECO:0000313|EMBL:KLI87408.1, ECO:0000313|Proteomes:UP000037645}; RN [1] {ECO:0000313|EMBL:KLI87408.1, ECO:0000313|Proteomes:UP000037645} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=YC-RL1 {ECO:0000313|EMBL:KLI87408.1, RC ECO:0000313|Proteomes:UP000037645}; RA Ren L., Shi Y., Jia Y., Yan Y.; RT "Genome sequence of Arthrobacter sp. YC-RL1."; RL Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:ALQ31319.1, ECO:0000313|Proteomes:UP000061913} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=YC-RL1 {ECO:0000313|EMBL:ALQ31319.1, RC ECO:0000313|Proteomes:UP000061913}; RA Zhang Y., Guo Z.; RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP013297; ALQ31319.1; -; Genomic_DNA. DR EMBL; LCYH01000017; KLI87408.1; -; Genomic_DNA. DR RefSeq; WP_047121157.1; NZ_LCYH01000017.1. DR EnsemblBacteria; ALQ31319; ALQ31319; ATC04_12630. DR EnsemblBacteria; KLI87408; KLI87408; AA310_18550. DR KEGG; ary:ATC04_12630; -. DR PATRIC; fig|1652545.3.peg.3793; -. DR KO; K03665; -. DR Proteomes; UP000037645; Unassembled WGS sequence. DR Proteomes; UP000061913; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 2. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000037645}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000037645}. FT DOMAIN 301 466 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 522 AA; 56899 MW; 77036101AA6A2031 CRC64; MTNSESHEHD PSSMDDAQIQ AAIDRILAAD EAQGPQVQHF ASDDESIFSG QATALNRFSS GYSTYDGEQD DLAERRALRR VAGLSTELED VTEVEYRQLR LERVVLAGVW TDGSVTEAEN SLRELAALAE TAGSEVLDGV VQRRSKPDPS TYLGSGKAME LREIVASTGA DTVIVDAELA PSQRRALEDV VKVKVIDRTS LILDIFAQHA KSREGKAQVE LAQLEYLLPR LRGWGESMSR QAGGRVGAAG GGIGSRGPGE TKIEMDRRRI RDRMAKLRRE IKAMKPAREA KRANRRRNEV PAVAIAGYTN AGKSSLLNRL TNAGVLVENA LFATLDPTVR QAATEDGLTY TLADTVGFVS NLPTQLVEAF RSTLEEIADS DLILHVVDAS HPDPEGQIQA VRTVLGEVDA LNIPEIIVLN KADVADPFVI ERVRNRESNT VVVSAHTGEG IKELLAKVSS SIPRPGVQME VLIPYNRGDL IAKLHQSESE ILESEHLENG TRLIVKVRES LAAELETFNL HG // ID A0A0H1A8J4_9RHIZ Unreviewed; 462 AA. AC A0A0H1A8J4; DT 16-SEP-2015, integrated into UniProtKB/TrEMBL. DT 16-SEP-2015, sequence version 1. DT 07-JUN-2017, entry version 13. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=XW59_07985 {ECO:0000313|EMBL:KLI95289.1}; OS Mesorhizobium sp. LC103. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Phyllobacteriaceae; Mesorhizobium. OX NCBI_TaxID=1120658 {ECO:0000313|EMBL:KLI95289.1, ECO:0000313|Proteomes:UP000050670}; RN [1] {ECO:0000313|EMBL:KLI95289.1, ECO:0000313|Proteomes:UP000050670} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=LC103 {ECO:0000313|EMBL:KLI95289.1, RC ECO:0000313|Proteomes:UP000050670}; RA Lee M., Gan H.Y., Gan H.M.; RT "Whole Genome Sequencing of Six Isolated Bacteria from Oligotrophic RT Conditions within Lechuguilla Cave, New Mexico."; RL Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KLI95289.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LBCQ01000003; KLI95289.1; -; Genomic_DNA. DR RefSeq; WP_047144896.1; NZ_LBCQ01000003.1. DR EnsemblBacteria; KLI95289; KLI95289; XW59_07985. DR PATRIC; fig|1120658.4.peg.3959; -. DR Proteomes; UP000050670; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000050670}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000050670}. FT DOMAIN 232 404 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 191 225 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 462 AA; 50852 MW; 366937648A818CED CRC64; MAPSKRAGRN ADGAEAGGTP PAVALTRAVI IVPVLTRQSR NQDDATAGRP RLARSPQARL EEATGLAAAI DLETVHREIV TVNDPRPATL LGAGKVAEFA EIMKERKAEL VVVDHPLTPV QQRNLEKELN AKVLDRTGII LEIFGRRART REGTLQVDLA HLNYQKGRLV RSWTHLERQR GGAGFLGGPG ETQIEADRRI LQEKIVRLKR ELETVRRTRD LHRAKRKKVP YPVVAIVGYT NAGKSTLFNR LTGASVLAED MLFATLDPTL RRVRLPHGTT IILSDTVGFI SDLPTHLVAA FRATLEEVVE ANLVIHLRDI SDPDTAAQAE DVERILLDLG IDAGDASRVL EVWNKVDRLE PADRERLAET ARADGSHPVA ISAISGEGTD RLLAIVEERI SGEVATITVV LKPEEIGEID WLYRNGEVIE RKDLEDGGAE ILLKATADIR REIEERLATR KG // ID A0A0H1ALK6_9GAMM Unreviewed; 439 AA. AC A0A0H1ALK6; DT 16-SEP-2015, integrated into UniProtKB/TrEMBL. DT 16-SEP-2015, sequence version 1. DT 07-JUN-2017, entry version 13. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=WQ56_16235 {ECO:0000313|EMBL:KLI97845.1}; OS Luteimonas sp. FCS-9. OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales; OC Xanthomonadaceae; Luteimonas. OX NCBI_TaxID=1547516 {ECO:0000313|EMBL:KLI97845.1, ECO:0000313|Proteomes:UP000035397}; RN [1] {ECO:0000313|EMBL:KLI97845.1, ECO:0000313|Proteomes:UP000035397} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=FCS-9 {ECO:0000313|EMBL:KLI97845.1, RC ECO:0000313|Proteomes:UP000035397}; RA Bala M., Kumar A., Kaur N., Mathan Kumar R., Kaur G., Singh N.K., RA Mayilraj S.; RT "Taxonomic description and genome sequence of Luteimonas RT oceanisediminis sp. nov., a novel gammaproteobacteria isolated from a RT marine sediment."; RL Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KLI97845.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LASZ01000028; KLI97845.1; -; Genomic_DNA. DR RefSeq; WP_047138186.1; NZ_LASZ01000028.1. DR EnsemblBacteria; KLI97845; KLI97845; WQ56_16235. DR PATRIC; fig|1547516.3.peg.3410; -. DR Proteomes; UP000035397; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000035397}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000035397}. FT DOMAIN 199 370 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 158 192 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 439 AA; 48002 MW; 5894666EB15AD2A7 CRC64; MFERSRKGEN ALLIQPHAHG PADEGVLEEF SELARSAGAN VAMVIAARID RPNAATLIGS GKLEEVKAAA EASGADLILV NHRLSPGQER NLERALERRV VDRTGLILDI FAQRARSHEG KLQVELAQLR HMATRLVRGW THLERQRGGS IGLRGPGETQ LETDRRLLQK RVEQLQARLG KVEVQRTQMR RARVRSELPR VALVGYTNAG KSTLFNTLSG ADAYAADQLF ATLDPTVRRV DLSGGAIVLA DTVGFVRDLP HELVAAFRST LSEAREADLL LHVIDAADPL RNERIAQVDA VLGEIGAGDL PQLLVFNKID RIEGATPRYD EDPAALADDA VREAVWISAR DGLGLDLLSQ ALARRLGMRR IVGDVLLPHE AGRLHARLHA LEAVREEVVE SDGWRLRVDL AHADAARLAA QPDGAPLRPL LPPDDPDTI // ID A0A0H1RAI6_9RHIZ Unreviewed; 465 AA. AC A0A0H1RAI6; DT 16-SEP-2015, integrated into UniProtKB/TrEMBL. DT 16-SEP-2015, sequence version 1. DT 07-JUN-2017, entry version 13. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=AA309_15800 {ECO:0000313|EMBL:KLK92218.1}; OS Microvirga vignae. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Methylobacteriaceae; Microvirga. OX NCBI_TaxID=1225564 {ECO:0000313|EMBL:KLK92218.1, ECO:0000313|Proteomes:UP000035489}; RN [1] {ECO:0000313|EMBL:KLK92218.1, ECO:0000313|Proteomes:UP000035489} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BR3299 {ECO:0000313|EMBL:KLK92218.1, RC ECO:0000313|Proteomes:UP000035489}; RA Zilli J.E., Passos S.R., Leite J., Baldani J.I., Xavier G.R., RA Rumjaneck N.G., Simoes-Araujo J.L.; RT "Draft genome sequence of Microvirga vignae strain BR3299, a novel RT nitrogen fixing bacteria isolated from Brazil semi-aired region."; RL Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KLK92218.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LCYG01000039; KLK92218.1; -; Genomic_DNA. DR RefSeq; WP_047189991.1; NZ_LCYG01000039.1. DR EnsemblBacteria; KLK92218; KLK92218; AA309_15800. DR PATRIC; fig|1225564.3.peg.4067; -. DR Proteomes; UP000035489; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000035489}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000035489}. FT DOMAIN 232 406 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 465 AA; 51428 MW; DE3F16DFCCCC86C9 CRC64; MAEPRTPGEH RLAELAEPEK EVAAGTKTLV VGPYLTRKRR PGTGEAEGES SNPRPPEARL DEASGLALAI DLSVVQSLIA PLSSPRPATY IGSGKVDEFA ALIRAEEIGL VVMDCALSPV QQRNLEKAWG AKVIDRTGLI LEIFGRRART KEGTLQVELA HLSYQKGRLV RSWTHLERQR GGFGFLGGPG ETQIEADRRL IQERMNRIER DLEGVVKTRS LHRASRRRVP YPIVALVGYT NAGKSTLFNR MTRAEVLAEN MLFATLDPTT RAIDLPHGEK AILSDTVGFI SDLPTMLVAA FRATLEDVVE ADVLLHVRDV SHGETEAQAG DVAVVLRELG IDPDDTRRII EVWNKADLLS PEDRERLATA SQRTGVERRP ILISALTGEG VHELLETIEQ HLAMGRKAYE VDVAPEDGQG LAWLHENTEI LERKTMENGH TLLQVRLVAG KEPRFLNRFP NARVI // ID A0A0H2KK39_9MICO Unreviewed; 519 AA. AC A0A0H2KK39; DT 16-SEP-2015, integrated into UniProtKB/TrEMBL. DT 16-SEP-2015, sequence version 1. DT 07-JUN-2017, entry version 13. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=FB00_15440 {ECO:0000313|EMBL:KLN33836.1}; OS Cellulosimicrobium funkei. OC Bacteria; Actinobacteria; Micrococcales; Promicromonosporaceae; OC Cellulosimicrobium. OX NCBI_TaxID=264251 {ECO:0000313|EMBL:KLN33836.1, ECO:0000313|Proteomes:UP000035265}; RN [1] {ECO:0000313|EMBL:KLN33836.1, ECO:0000313|Proteomes:UP000035265} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=U11 {ECO:0000313|EMBL:KLN33836.1, RC ECO:0000313|Proteomes:UP000035265}; RA Hu C., Gong Y., Wan W., Jiang M.; RT "Cellulosimicrobium funkei U11 genome."; RL Submitted (MAY-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KLN33836.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JNBQ01000025; KLN33836.1; -; Genomic_DNA. DR RefSeq; WP_047233754.1; NZ_JNBQ01000025.1. DR EnsemblBacteria; KLN33836; KLN33836; FB00_15440. DR PATRIC; fig|264251.5.peg.3145; -. DR Proteomes; UP000035265; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 2. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000035265}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000035265}. FT DOMAIN 298 464 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 519 AA; 55671 MW; 777A701123666475 CRC64; MSATPANTPA TPTPAQDEPT GATRDIASDV VARVLARAGT ARAEGGTVHA QHDGEQLELE ERSALRRVVG LSTELEDVTE VEYRQLRLEK VVLVGLWSPG ADPREDGAPS SAEEAEISLR ELAALAETAG SQVLDGVIQR RAKPDPGTYL GSGKAAELAD VVAASGADTV VIDGELAPSQ RRALEDIVKV KVIDRTALIL DIFAQHAKSR EGKAQVELAQ LEYLLPRLRG WGESMSRQAG GQVGGAGAGM GSRGPGETKI ELDRRRIRNR MAKLRREIQA MAPGRETKRA SRKRHAVPSV AIAGYTNAGK SSLLNAITGA GVLVENALFA TLDPTVRRTR TEDGRVYTLA DTVGFVRALP HQLVEAFRST LEEVGDADLL LHVVDASHPD PEGQIAAVRH VLADIPGVED VPEVIVLNKA DLADPETIAR IRLRERRTVV VSAHTGEGIE HLCELIAHEL PRPDVEIDVV VPYHRGDLVH RVHTEGEIDH EEHTPEGTLL RGRVAQALAT ELVGVSTQG // ID A0A0H2LMC6_PRORE Unreviewed; 426 AA. AC A0A0H2LMC6; DT 16-SEP-2015, integrated into UniProtKB/TrEMBL. DT 16-SEP-2015, sequence version 1. DT 30-AUG-2017, entry version 15. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=AAY77_04505 {ECO:0000313|EMBL:KLN46981.1}; OS Providencia rettgeri. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; OC Morganellaceae; Providencia. OX NCBI_TaxID=587 {ECO:0000313|EMBL:KLN46981.1, ECO:0000313|Proteomes:UP000054201}; RN [1] {ECO:0000313|EMBL:KLN46981.1, ECO:0000313|Proteomes:UP000054201} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MR4 {ECO:0000313|EMBL:KLN46981.1, RC ECO:0000313|Proteomes:UP000054201}; RA Bhadhaniya R.A., Golakiya B.A., Akbari D.L., Parakhia M.V., RA Tomar R.S., Thakkar J.R., Rathod V.M., Padhiyar S.M., Thummar V.D., RA Kheni J.R., Kothari V.; RT "Genome of Providencia rettgeri MR4."; RL Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KLN46981.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LCVM01000152; KLN46981.1; -; Genomic_DNA. DR EnsemblBacteria; KLN46981; KLN46981; AAY77_04505. DR PATRIC; fig|587.20.peg.504; -. DR Proteomes; UP000054201; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000054201}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000054201}. FT DOMAIN 198 365 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 426 AA; 48112 MW; DAB64784A6806408 CRC64; MFDRYEGGEL AVLVHVFFSQ EKDVDNLAEF ESLVTSAGVK PVQIVTGSRK APHPKFFVGE GKAEEIAQAV EESGADVVLF NHTLSPAQER NLERICQCKV VDRTGVILDI FAQRARTHEG KLQVELAQLR HLSTRLVRGW THLERQKGGI GLRGPGETQL ETDRRLLRDK IKQILSRLSR VEKQREQGRQ ARSKADIPTI SLVGYTNAGK SSLFNRMTSA DVYAADQLFA TLDPTLRRID VEDVGVVVLA DTVGFIRHLP HDLVAAFKAT LQETREATLL LHVIDAADAR LDENIHAVES VLEEIEADEI PTLLVMNKVD MLEDFVPRID RDEDNNPVRV WVSAQTGEGI PLLLQALTER LSGEIAHDEL RLPPNEGRLR SRFYQLQSIE REWLEDDGSI GLEVRMPMVD WRRLCKQEQQ LPDYVV // ID A0A0H2M1G3_VARPD Unreviewed; 389 AA. AC A0A0H2M1G3; DT 16-SEP-2015, integrated into UniProtKB/TrEMBL. DT 16-SEP-2015, sequence version 1. DT 07-JUN-2017, entry version 15. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:KLN55901.1}; GN ORFNames=VPARA_29360 {ECO:0000313|EMBL:KLN55901.1}; OS Variovorax paradoxus. OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Comamonadaceae; Variovorax. OX NCBI_TaxID=34073 {ECO:0000313|EMBL:KLN55901.1, ECO:0000313|Proteomes:UP000035170}; RN [1] {ECO:0000313|EMBL:KLN55901.1, ECO:0000313|Proteomes:UP000035170} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=TBEA6 {ECO:0000313|EMBL:KLN55901.1, RC ECO:0000313|Proteomes:UP000035170}; RA Poehlein A., Schuldes J., Wuebbeler J.H., Hiessl S., Steinbuechel A., RA Daniel R.; RT "Genome sequence of Variovorax paradoxus TBEA6."; RL Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KLN55901.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JZWI01000014; KLN55901.1; -; Genomic_DNA. DR RefSeq; WP_047785071.1; NZ_JZWI01000014.1. DR EnsemblBacteria; KLN55901; KLN55901; VPARA_29360. DR PATRIC; fig|34073.19.peg.3015; -. DR Proteomes; UP000035170; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000035170}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000035170}. FT DOMAIN 200 373 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 389 AA; 43228 MW; 06523725B54F2605 CRC64; MSELNSRQEG AAVLVGVDFG LPHFDSELEE LGLLAQTAGL EPVARLVCKR KAPDAALFVG SGKAEEIKEL AALHQASEVI FDQSLSPAQQ RNLERQLDIA VYDRTFLILE IFAQRARSHE GKLQVELARL QYLSTRLVRR WSHLERQTGG AGVRGGPGEK QIELDRRMIS ESIKRTRERL AKVQKQRGTQ RRQRERRETF NISLVGYTNA GKSSLFNALV KARAYAADQL FATLDTTTRN LYLGDARRQV SISDTVGFIR DLPHGLVDAF KATLQEAVDA DLLLHVVDAS NPHYPEQMAE VQSVLRDIGA DTVPQLLVFN KLDALETAQH PLHLQDDMEI DGVQVPRIFL SARSGEGLPL LRAELARRSG SLGDTMTPEA DTELHDTAN // ID A0A0H3J9J7_CLOPA Unreviewed; 594 AA. AC A0A0H3J9J7; DT 16-SEP-2015, integrated into UniProtKB/TrEMBL. DT 16-SEP-2015, sequence version 1. DT 07-JUN-2017, entry version 15. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:AJA51788.1}; GN ORFNames=CLPA_c17300 {ECO:0000313|EMBL:AJA51788.1}; OS Clostridium pasteurianum DSM 525 = ATCC 6013. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=1262449 {ECO:0000313|EMBL:AJA51788.1, ECO:0000313|Proteomes:UP000030905}; RN [1] {ECO:0000313|EMBL:AJA51788.1, ECO:0000313|Proteomes:UP000030905} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 525 / ATCC 6013 {ECO:0000313|Proteomes:UP000030905}; RX PubMed=25700415; RA Poehlein A., Grosse-Honebrink A., Zhang Y., Minton N.P., Daniel R.; RT "Complete Genome Sequence of the Nitrogen-Fixing and Solvent-Producing RT Clostridium pasteurianum DSM 525."; RL Genome Announc. 3:e01591-14(2015). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP009268; AJA51788.1; -; Genomic_DNA. DR RefSeq; WP_003443762.1; NZ_JPGY02000001.1. DR EnsemblBacteria; AJA51788; AJA51788; CLPA_c17300. DR EnsemblBacteria; KRU12204; KRU12204; CP6013_01451. DR KEGG; cpae:CPAST_c17300; -. DR KEGG; cpat:CLPA_c17300; -. DR PATRIC; fig|1262449.3.peg.1565; -. DR KO; K03665; -. DR Proteomes; UP000030905; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000030905}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000030905}. FT COILED 330 357 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 594 AA; 66656 MW; 156A21C741F3E418 CRC64; MILGNIDGIR KSLLEKLEEI YEMKIPKYNI ITEELSYTIC YVTGMINREV SVVIDRRGNV VSVAIGDSST VELPLIDVKE GKLAGVRIVH THPGGNSRLS MIDVSALIKL KLDCITAVGV KEGNMTDITA GFCSVQGDLL KPEIIGPMSI KKAMELNFID KIKYIQDTIK IENIKEDNSE RAIIVGIESK ESLEELEELA KACNVQCLHS VLQKKDKIDT AFYVGSGKVE EINLIRQSLS ANLIIFDDEL TGSQVRNLEE ILGIKVIDRT TLILEIFATR ARTKEAKIQV ELAQLKYRST RLMGLGSVMS RTGGGIGTRG PGEKKLEIDR RRIRERVYDL TKELEKVRRN RETQREKRSN QNIPKISLVG YTNAGKSTLR NKLCSMAAPN DSVKKENVFE ADMLFATLDV TTRAIVLPDN RTATLTDTVG FVRKLPHDLV EAFKSTLEEV IYSDLLLHVI DTSNENALVQ IEAVEKVLEE LGAGDKPVIL VLNKIDKASK EEINCIKDKY SSLYIIEISA KDNVNLDALL ESICNNLPNN LKKVEYIIPY SNQSEVAYLH RNSKIDEEKF LEEGTKIVAE VDDITYNKYL KYKV // ID A0A0H4KLK6_9BACI Unreviewed; 420 AA. AC A0A0H4KLK6; DT 14-OCT-2015, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 1. DT 07-JUN-2017, entry version 14. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=BEH_17625 {ECO:0000313|EMBL:AKO93731.1}; OS Bacillus endophyticus. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus. OX NCBI_TaxID=135735 {ECO:0000313|EMBL:AKO93731.1, ECO:0000313|Proteomes:UP000036202}; RN [1] {ECO:0000313|Proteomes:UP000036202} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Hbe603 {ECO:0000313|Proteomes:UP000036202}; RA Jia N., Du J., Ding M.-Z., Gao F., Yuan Y.-J.; RT "Genome Sequence of Bacillus endophyticus and Analysis of its RT Companion Mechanism in the Ketogulonigenium vulgare-Bacillus strain RT Consortium."; RL Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP011974; AKO93731.1; -; Genomic_DNA. DR RefSeq; WP_046217774.1; NZ_CP011974.1. DR EnsemblBacteria; AKO93731; AKO93731; BEH_17625. DR KEGG; beo:BEH_17625; -. DR PATRIC; fig|135735.6.peg.3749; -. DR KO; K03665; -. DR Proteomes; UP000036202; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000036202}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000036202}. FT DOMAIN 202 363 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 420 AA; 47431 MW; C82730D326F3FFB6 CRC64; MHTLQRNEKE KTVLVGCQLP GDDEVRFGHS LDELESLTET AGGEVILTLT QKRERVHPAT YIGKGKLEEL LAAVEETEPD LVVFNDELSP SQLRNLTDML SVRIIDRTQL ILDIFAQRAA TKEGHLQVEL AQLNYLLPRL SGQGVNLSRL GAGIGTRGPG ETKLETDRRH IRGRIHDLKQ QLKTVVEHRK RYRARRKENQ SIQVSLVGYT NAGKSTLFNK LTNAGTFEEN QLFATLDPLT RKTQLPSGLD ILLTDTVGFI QDLPTTLVAA FRSTLEEVTE ADFILHVVDS SNPDYTTHEK TVHKLLEELN VTDVPMLTVY NKKDEVDPEF IPSTTESLLI SALDAKDIEE LKAKTSDLIK SSMEHYNVEL SPSEGEWLST LKRDSILEGF HFNEEKEVYE CSGYIAKTHP LYESLREREK // ID A0A0H4KRA2_9RHOB Unreviewed; 424 AA. AC A0A0H4KRA2; DT 14-OCT-2015, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 1. DT 05-JUL-2017, entry version 14. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=MALG_01457 {ECO:0000313|EMBL:AKO96642.1}; OS Marinovum algicola DG 898. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae; Marinovum. OX NCBI_TaxID=988812 {ECO:0000313|EMBL:AKO96642.1, ECO:0000313|Proteomes:UP000036352}; RN [1] {ECO:0000313|EMBL:AKO96642.1, ECO:0000313|Proteomes:UP000036352} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DG 898 {ECO:0000313|EMBL:AKO96642.1, RC ECO:0000313|Proteomes:UP000036352}; RX PubMed=26079637; DOI=10.1111/1462-2920.12947; RA Frank O., Goker M., Pradella S., Petersen J.; RT "Ocean's twelve: Flagellar and biofilm chromids in the multipartite RT genome of Marinovum algicola DG898 exemplify functional RT compartmentalization."; RL Environ. Microbiol. 17:4019-4034(2015). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP010855; AKO96642.1; -; Genomic_DNA. DR EnsemblBacteria; AKO96642; AKO96642; MALG_01457. DR KEGG; malg:MALG_01457; -. DR PATRIC; fig|988812.14.peg.1461; -. DR KO; K03665; -. DR Proteomes; UP000036352; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000036352}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Hydrolase {ECO:0000313|EMBL:AKO96642.1}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000036352}. FT DOMAIN 204 373 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 424 AA; 46728 MW; B921447A2A7DAC67 CRC64; MKEHDTHVTR AWVLHPDIKS DQDRRTPEPA LAEAVALAAA LPDLEVVGAE VVGLRSVQPG KLFGSGKIEE LGARFKAEDV ELVLVDGPVT PVQQRNLEKD WGVKLLDRTG LILEIFSDRA ATREGVLQVE MAALSYQRTR LVRAWTHLER QRGGLGFVGG PGETQIEADR RAIDDQLVRL RRQLDKVVKT RDLHRKARAK VPFPIVALVG YTNAGKSTLF NRLTGAEVMA KDMLFATLDP TMRAVELDNG LEVILSDTVG FISDLPTELV AAFRATLEEV LAADVICHVR DISHEGSEEQ AEDVRAILGS LGVPDSTPQL EIWNKIDRIA AEDRAALQAR AARDDAIVTL SAVTGDGMGD FLDAVTRALE AEKHETEVAL GFGEGRKRAW LFERGLVTDE AQDETGYRLK VAWSRKQEAQ FARL // ID A0A0H4LQZ1_9LACO Unreviewed; 430 AA. AC A0A0H4LQZ1; DT 14-OCT-2015, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 1. DT 07-JUN-2017, entry version 12. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=ABB44_04395 {ECO:0000313|EMBL:AKS51224.1}, GN ABB45_04385 {ECO:0000313|EMBL:AKP02924.1}; OS Lactobacillus farciminis. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; OC Lactobacillus. OX NCBI_TaxID=1612 {ECO:0000313|EMBL:AKP02924.1, ECO:0000313|Proteomes:UP000036225}; RN [1] {ECO:0000313|Proteomes:UP000036225} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CNCM-I-3699-S {ECO:0000313|Proteomes:UP000036225}; RA Raouf T., Marion B., Agnes I., Jean Paul V.; RT "Genome sequence of R and S variants of pleomorphic strain RT Lactobacillus farciminis CNCM-I-3699."; RL Genome Announc.0:0-0(2015). RN [2] {ECO:0000313|EMBL:AKP02924.1, ECO:0000313|Proteomes:UP000065868} RP NUCLEOTIDE SEQUENCE. RC STRAIN=CNCM-I-3699-R {ECO:0000313|EMBL:AKS51224.1, RC ECO:0000313|Proteomes:UP000065868}, and RC CNCM-I-3699-S {ECO:0000313|EMBL:AKP02924.1}; RX PubMed=26383668; RA Tareb R., Bernardeau M., Vernoux J.P.; RT "Genome Sequence of Rough and Smooth Variants of Pleomorphic Strain RT Lactobacillus farciminis CNCM-I-3699."; RL Genome Announc. 3:e01059-15(2015). RN [3] {ECO:0000313|EMBL:AKP02924.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=CNCM-I-3699-S {ECO:0000313|EMBL:AKP02924.1}; RA Hoefler B.C., Straight P.D.; RL Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases. RN [4] {ECO:0000313|EMBL:AKS51224.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=CNCM-I-3699-R {ECO:0000313|EMBL:AKS51224.1}; RA Noorani M.; RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP011952; AKP02924.1; -; Genomic_DNA. DR EMBL; CP012177; AKS51224.1; -; Genomic_DNA. DR EnsemblBacteria; AKP02924; AKP02924; ABB45_04385. DR EnsemblBacteria; AKS51224; AKS51224; ABB44_04395. DR PATRIC; fig|1612.27.peg.873; -. DR Proteomes; UP000036225; Chromosome. DR Proteomes; UP000065868; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000036225}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000036225}. FT DOMAIN 202 372 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 430 AA; 48538 MW; 9A2F9DA3B5519CFC CRC64; MKESNLTFEK TRVIVAGVSH LQADFEYTMQ ELASLVEANN MEVADTIIQN ADTVSGATYF GSGKVHEIKE IANADDVQIV VLNDELTPSQ IRNLEKETKL SFMDRTELIL QVFSTRAQTK QAKLQVEIAK LQYQLPRIHP SGNPLDQQSA SGGLANRGAG ESKLELDRRV IRKRITALRN ELKTVDKTIN VQSRRRTNTS LPLVSLVGYT NAGKSTTMNG LLNFNKEDSQ DRKVFEKNML FATLDTSVRR IDLEDNTSFL LSDTVGFVSK LPHNLVESFK TTLKEAQAAD LLIQVIDVSD EHWKNMIDVT EKTLKEIGVT DKPMIYAFNK ADLKKGQQFP TIEGDNIYYS ALDKESIEKL VDLIKLKIFN NYQKADLLVP YSDQKITEEI LQNSQVLKKE FTNDGSLITA NLSPTELEKF NKYIKTEMSE // ID A0A0H4P4B0_9BACI Unreviewed; 417 AA. AC A0A0H4P4B0; DT 14-OCT-2015, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 1. DT 07-JUN-2017, entry version 13. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=BSM4216_2014 {ECO:0000313|EMBL:AKP47268.1}; OS Bacillus smithii. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus. OX NCBI_TaxID=1479 {ECO:0000313|EMBL:AKP47268.1, ECO:0000313|Proteomes:UP000036353}; RN [1] {ECO:0000313|EMBL:AKP47268.1, ECO:0000313|Proteomes:UP000036353} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 4216 {ECO:0000313|EMBL:AKP47268.1, RC ECO:0000313|Proteomes:UP000036353}; RA Bosma E.F., Koehorst J.J., van Hijum S.A.F.T., Renckens B., RA Vriesendorp B., van de Weijer A.H.P., Schaap P.J., de Vos W.M., RA van der Oost J., van Kranenburg R.; RT "Complete genome sequence of thermophilic Bacillus smithii type strain RT DSM 4216T."; RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP012024; AKP47268.1; -; Genomic_DNA. DR RefSeq; WP_048623397.1; NZ_CP012024.1. DR EnsemblBacteria; AKP47268; AKP47268; BSM4216_2014. DR KEGG; bsm:BSM4216_2014; -. DR KO; K03665; -. DR Proteomes; UP000036353; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000036353}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000036353}. FT DOMAIN 197 359 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 417 AA; 47785 MW; 6E87500D7B313031 CRC64; MTNQKEKAIL VGCLLDGDEE SFYYSLEELA SLTHTADGEV VCTITQKRDR IDPSTYIGKG KLEELKHLVE ELETDVVIFN DELTPSQIRH LTDTLRIRII DRTQLILDIF ARRARSKEGK LQVELAQLEY LLPRLSGRGT ELSRLGGGIG TRGPGETKLE SDRRHIRRRI HDIKEQLQSV VHHRERYRSR RKKNHTFRIA LVGYTNAGKS TLFNRLTTGG SLEENQLFAT LDPLTKKMTL PSGFTSLLSD TVGFIQDLPT TLVAAFRSTL EEVREADLLL HVVDSSNPDY LQHEETVNQL LAQLDMDELP RLLVYNKIDQ KCSGFVPVSK DDHIMISALS EEDRTRLKIK IEQVMKNLMI PFRAEIPADE GKLLARIKTE TMLQHLSFHD ETFFYLVKGY MMEDHPLSGI LKKYQQQ // ID A0A0H4QGN0_9LACO Unreviewed; 428 AA. AC A0A0H4QGN0; DT 14-OCT-2015, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 1. DT 07-JUN-2017, entry version 13. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=ABM34_08490 {ECO:0000313|EMBL:AKP67564.1}; OS Lactobacillus ginsenosidimutans. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; OC Lactobacillus. OX NCBI_TaxID=1007676 {ECO:0000313|EMBL:AKP67564.1, ECO:0000313|Proteomes:UP000036106}; RN [1] {ECO:0000313|Proteomes:UP000036106} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=EMML 3041 {ECO:0000313|Proteomes:UP000036106}; RA Kim M.K., Im W.-T., Srinivasan S., Lee J.-J.; RT "Lactobacillus ginsenosidimutans/EMML 3141/ whole genome sequencing."; RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP012034; AKP67564.1; -; Genomic_DNA. DR RefSeq; WP_048704978.1; NZ_CP012034.1. DR EnsemblBacteria; AKP67564; AKP67564; ABM34_08490. DR KEGG; lgn:ABM34_08490; -. DR PATRIC; fig|1007676.4.peg.1715; -. DR KO; K03665; -. DR Proteomes; UP000036106; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000036106}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000036106}. FT DOMAIN 200 334 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 428 AA; 48133 MW; 9BB30EFEEDFD19F8 CRC64; MEDLNNTKER VIIAGVSHLQ PDFDYTMEEL GSLVVANNME VADVIKQNAD SVSGATYFGK GKVTEIAEIA NADDVTTIIL NDELTPSQIR NLEKSTKLSF MDRTELILQV FSNRAHTKQA KLQVEIAKLQ YQLPRIHPSG NPLDQQSSSG GLANRGAGET KLEMDRRVIR KRIDYLRTQL KAVDKTIDVQ SRRRTNTTVP LVSLVGYTNA GKSTTMNGLL NFNKDDSEDR KVFEKDMLFA TLDTSVRKID LEDNTSFLLS DTVGFVSKLP HNLIESFKTT LKEAADADLL IQVIDVSDEH WRNMIEVTEK TLNEVGVKGK PMIYAFNKAD LKPGQQFPMI EGDNIYYSAI DKESIAKLVD LIKLKLFANY EEVTLMIPYK NQKIAEEILR NTQIISKDFT NDGSLLTAKL SPEQINNYKG FVQEKAPE // ID A0A0H4VLK2_9BACT Unreviewed; 400 AA. AC A0A0H4VLK2; DT 14-OCT-2015, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 1. DT 07-JUN-2017, entry version 14. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=TH63_15260 {ECO:0000313|EMBL:AKQ46675.1}; OS Rufibacter sp. DG31D. OC Bacteria; Bacteroidetes; Cytophagia; Cytophagales; Hymenobacteraceae; OC Rufibacter. OX NCBI_TaxID=1379910 {ECO:0000313|EMBL:AKQ46675.1, ECO:0000313|Proteomes:UP000036458}; RN [1] {ECO:0000313|EMBL:AKQ46675.1, ECO:0000313|Proteomes:UP000036458} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DG31D {ECO:0000313|EMBL:AKQ46675.1, RC ECO:0000313|Proteomes:UP000036458}; RA Kim M.K., Srinivasan S., Lee J.-J.; RT "Rufibacter sp./DG31D/ whole genome sequencing."; RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP010777; AKQ46675.1; -; Genomic_DNA. DR RefSeq; WP_048921701.1; NZ_CP010777.1. DR EnsemblBacteria; AKQ46675; AKQ46675; TH63_15260. DR KEGG; ruf:TH63_15260; -. DR PATRIC; fig|1379910.4.peg.3330; -. DR KO; K03665; -. DR Proteomes; UP000036458; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000036458}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000036458}. FT DOMAIN 204 387 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 400 AA; 46142 MW; D245B0873766A66B CRC64; MKKSLHITAK DQETAVLVAV PAYKQTDEKT KEYLDELAFL TETVGAKTLK RFVQKLDKPD MRTYVGKGKL EEVNAYVKEH KVDMVIFDDD LSPSQVRNLE RELEVKIIDR SLLILDIFAL RAQTATARAQ VELAQYRYLL PRLTNMWTHL SRQKGGGVAM RGPGETEIET DRRIVREKIT LLKEKLDKFE KQNFEQRKSR TGIVRVSLVG YTNVGKSTLM NLLTKADVFA ENKLFATVDS TVRKMVIDNI PFLLSDTVGF IRKLPTKLIE SFKTTLDEIR ESDLLLHVVD VSHPSFEEHI NVVNSTLKDI HSADKPVILV FNKTDLYLEE REREMQEHNP EARPDISELK STYMAKQHTP AIFISATNRI NIDELREVLF KEVARIHNER YPNNAPQEEY // ID A0A0H4VYR7_9SPHN Unreviewed; 423 AA. AC A0A0H4VYR7; DT 14-OCT-2015, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 1. DT 05-JUL-2017, entry version 14. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=CP97_10140 {ECO:0000313|EMBL:AKQ42303.1}; OS Erythrobacter atlanticus. OC Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales; OC Erythrobacteraceae; Erythrobacter. OX NCBI_TaxID=1648404 {ECO:0000313|EMBL:AKQ42303.1, ECO:0000313|Proteomes:UP000059113}; RN [1] {ECO:0000313|Proteomes:UP000059113} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=s21-N3 {ECO:0000313|Proteomes:UP000059113}; RA Zhuang L., Liu Y., Shao Z.; RT "The complete genome sequence of Erythrobacter sp. s21-N3."; RL Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP011310; AKQ42303.1; -; Genomic_DNA. DR EnsemblBacteria; AKQ42303; AKQ42303; CP97_10140. DR KEGG; ery:CP97_10140; -. DR PATRIC; fig|1648404.4.peg.2114; -. DR KO; K03665; -. DR Proteomes; UP000059113; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000059113}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000059113}. FT DOMAIN 190 365 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 156 183 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 423 AA; 46625 MW; 51DBA76ED9F0D475 CRC64; MCPDIRGQRS SEDPTARLEE ARGLALAIGI VVAESYILNV RVVRPNTLFG EGQVQRIATD CELHEAELVI VDGALSAIQQ RNLEEKIGRK VIDRTGLILE IFGERAATAE GRLQVELAHL DYQQSRLVRS WTHLERQRGG FGFLGGPGET QIEADRRMIR DRMGKLRREL EQVRKTRELH RKRRGRAPWP VIALVGYTNA GKSTLFNRMT GADVMAEDLL FATLDPTMRA IGLPGVEKAI LSDTVGFISD LPTQLVAAFR ATLEEVTAAD IVLHVRDIAN PDSVQQKRQV LAVLADLGVV NEEGEGVDAP VIEVWNKWDL LNEERRDELQ TIASTDDSVI PISAITGTGV DALGDRLGAI LTKGARTYAF VIPASDGARI AWLHAHGEVL DEEGAGQGED GPLRRIDVRL TQKEFGRFEA LDD // ID A0A0H4W1Y7_9BORD Unreviewed; 368 AA. AC A0A0H4W1Y7; DT 14-OCT-2015, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 1. DT 30-AUG-2017, entry version 14. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:AKQ56732.1}; GN ORFNames=ACR54_03435 {ECO:0000313|EMBL:AKQ56732.1}; OS Bordetella hinzii. OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Alcaligenaceae; Bordetella. OX NCBI_TaxID=103855 {ECO:0000313|EMBL:AKQ56732.1, ECO:0000313|Proteomes:UP000036382}; RN [1] {ECO:0000313|Proteomes:UP000036382} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=F582 {ECO:0000313|Proteomes:UP000036382}; RA Weigand M.R., Changayil S., Kulasekarapandian Y., Batra D., RA Williams M.M., Tondella M.L.; RT "Complete Genome Sequences of Two Bordetella hinzii Isolated from RT Humans."; RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP012076; AKQ56732.1; -; Genomic_DNA. DR RefSeq; WP_029578829.1; NZ_CP012076.1. DR EnsemblBacteria; AKQ56732; AKQ56732; ACR54_03435. DR GeneID; 29514898; -. DR KEGG; bhz:ACR54_03435; -. DR PATRIC; fig|103855.15.peg.3416; -. DR KO; K03665; -. DR Proteomes; UP000036382; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000036382}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000036382}. FT DOMAIN 190 354 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 156 183 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 368 AA; 40180 MW; A1FCFAD3A9B353F0 CRC64; MRALIISVDL GNPDHQAHAD EFVMLAEGAG AEIVGTLTAR RDRPDAKYFI GSGKVEEGVA MAGAALADIV LFDQPLSPAQ QRNLEREFNL RVVDRVALIL DIFALRAKSH EGKLQVELAQ LQHLATRLTR LWTHLERQRG GIGMRGPGES QLEMDRRMIG AKVKMLRERL DRVERQRVTQ RRARARGGAL SVSLVGYTNA GKSTLFNALT RAGAYAADQL FATLDTTTRR IWIEGAGSVV LSDTVGFIRD LPPNLIAAFR ATLEETVHAD LLLHVVDAAS PQREEQIFEV NKVLAEIGAA GIPTILVYNK IDRAGLEPRV ERDAHGTIAR VFVSATERAG LDALRGAIAE IGQIAGNNAS NHQTLQSE // ID A0A0H5CET5_9PSEU Unreviewed; 483 AA. AC A0A0H5CET5; DT 14-OCT-2015, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 1. DT 07-JUN-2017, entry version 14. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; OS Alloactinosynnema sp. L-07. OC Bacteria; Actinobacteria; Pseudonocardiales; Pseudonocardiaceae. OX NCBI_TaxID=1653480 {ECO:0000313|EMBL:CRK55768.1, ECO:0000313|Proteomes:UP000076116}; RN [1] {ECO:0000313|EMBL:CRK55768.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=L-07 {ECO:0000313|EMBL:CRK55768.1}; RA Ramaraj Thiru; RL Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LN850107; CRK55768.1; -; Genomic_DNA. DR RefSeq; WP_054045507.1; NZ_LN850107.1. DR EnsemblBacteria; CRK55768; CRK55768; CRK55768. DR KEGG; all:CRK55768; -. DR KO; K03665; -. DR Proteomes; UP000076116; Chromosome i. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000076116}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000076116}. FT DOMAIN 256 425 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 483 AA; 52530 MW; DFC77FDF2FCBDF6F CRC64; MTEEFTQQEI NGAVADPAEF SLGDLEREER SSLRRVAGLS TELQDITEVE YRQLRLERVV LVGVWTDGSA LESEASLAEL ARLAETAGSE VLDGLVQRRD KPDSATYIGS GKVAELGDIV RATGADTVIC DGELSPSQLQ QLEARLKVKV IDRTALILDI FAQHARSREG KSQVELAQLQ YLLPRLRGWG ETLSRQAGGR AGGGNGGVGL RGPGETKLET DRRRIRAKIS KLRKEIKAMS TVRDTKRGRR MANEIPSVAI AGYTNAGKSS LLNALTGAGV LVDDSLFATL DATTRRTETP DGHTYTLTDT VGFVRHLPHQ LVEAFRTTLD EVADADLVLH VVDGSDPMPE WQVTAVREVL NDIGERRDLK MPPELVVVNK VDATSEFAMA RLRHLLPGAM FVSAHTGAGI AELRERVAEL LPRPSTEIDV LVPYARGELV ARVHREGDVL FEDHTEAGTQ LRARVKADLA GVLEGFAVNG TSA // ID A0A0I9TI25_9MYCO Unreviewed; 484 AA. AC A0A0I9TI25; DT 14-OCT-2015, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 1. DT 07-JUN-2017, entry version 12. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=ABH38_13770 {ECO:0000313|EMBL:KLO35951.1}; OS Mycobacterium haemophilum. OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae; OC Mycobacterium. OX NCBI_TaxID=29311 {ECO:0000313|EMBL:KLO35951.1, ECO:0000313|Proteomes:UP000036334}; RN [1] {ECO:0000313|EMBL:KLO35951.1, ECO:0000313|Proteomes:UP000036334} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=UC1 {ECO:0000313|Proteomes:UP000036334}; RA Greninger A.L., Cunningham G., Miller S.; RT "Genome sequence of Mycobacterium haemophilum."; RL Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KLO35951.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LDPR01000011; KLO35951.1; -; Genomic_DNA. DR RefSeq; WP_047315325.1; NZ_LDPT01000013.1. DR EnsemblBacteria; KLO35951; KLO35951; ABH38_13770. DR PATRIC; fig|29311.18.peg.923; -. DR Proteomes; UP000036334; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000313|EMBL:KLO35951.1}; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000036334}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900, KW ECO:0000313|EMBL:KLO35951.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000036334}. FT DOMAIN 258 430 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 224 251 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 484 AA; 51932 MW; E401458F72F11317 CRC64; MTFPDSPQKT EPPNAGTAES APSIGELALE DRSALRRVAG LSTELTDISE VEYRQLRLER VVLVGVWTEG SAADNQASMA ELAALAETAG SQVLEGLIQR RDRPDPSTYI GSGKAAELRE VVLATGADTV ICDGELSPAQ LTALEKAVKV KVIDRTALIL DIFAQHAASR EGKAQVSLAQ MEYMLPRLRG WGESMSRQAG GRAGGSGGGV GLRGPGETKI ETDRRRIRER MAKLRRDIRD MKQARDTQRS RRLHSGVPSI AIVGYTNAGK SSLLNALTGA GVLVQDALFA TLEPTTRRAE FDNGQPFVLT DTVGFVRHLP TQLVEAFRST LEEVVDADLL LHIVDGSDAN PLAQINAVRQ VICEVVADHG GGGSEAPHEL LVVNKIDAAS DLMLAKLRHG LPGAVFISAR TGDGIDVLRR RIVELAVATD TAVDVVIPYD RGDLVARLHA NGRVQQAEHH LNGTRIRARV PVALAASLQE FSAY // ID A0A0I9W2Z4_9MICO Unreviewed; 494 AA. AC A0A0I9W2Z4; DT 14-OCT-2015, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 1. DT 07-JUN-2017, entry version 13. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=AA983_06300 {ECO:0000313|EMBL:KLO62995.1}; OS Dermacoccus sp. PE3. OC Bacteria; Actinobacteria; Micrococcales; Dermacoccaceae; Dermacoccus. OX NCBI_TaxID=1641401 {ECO:0000313|EMBL:KLO62995.1, ECO:0000313|Proteomes:UP000036330}; RN [1] {ECO:0000313|EMBL:KLO62995.1, ECO:0000313|Proteomes:UP000036330} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=PE3 {ECO:0000313|EMBL:KLO62995.1, RC ECO:0000313|Proteomes:UP000036330}; RA Sharma R.; RT "Genome sequence of Dermacoccus sp. PE3."; RL Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KLO62995.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LDCM01000002; KLO62995.1; -; Genomic_DNA. DR RefSeq; WP_047311406.1; NZ_LDCM01000002.1. DR EnsemblBacteria; KLO62995; KLO62995; AA983_06300. DR PATRIC; fig|1641401.3.peg.1311; -. DR Proteomes; UP000036330; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 2. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000036330}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000036330}. FT DOMAIN 272 436 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 494 AA; 54089 MW; 9E9C08A5A0E1D72C CRC64; MNERNPADFL SRRAQALADG DDATVVYDDR GFVVDSYDGD QIEREERAAL RRVHGLSTEL EDVSEVEYRQ LRLERVVLAG VWSEGSSEDA ENSLRELAAL AETAGSQVLA GVVQRRLRPD PGTWLGKGKA EELKEIVVAE GADTVIANGE LAPSQRRALE DVVKVKVIDR TALILDIFAQ HAKSKEGKAQ VELAQMQYLL PRLRGWGESM SRQAGGQAAG GQGMGSRGPG ETKIELDRRR INTRMAKLRR EIAEMKTTRD TKRSGRRNNN VPSVAIAGYT NAGKSSILNR LTNAGVLVQN QLFATLDPTV RRAETPDGRG YTLADTVGFV RDLPHQLVEA FRSTLEEVAD ADLLLHVVDG SHPDPESQIS AVREVLADVD ASDVKEVIVI NKADIAAPDV IDRLMRHEKH CIAVSARTGE GLPELLQLIA DELPHPDVRV ELLLPYERGD LLSRVHADGD VLGVEHRPEG THVHAKVTKE LAGELEPYLT SSVA // ID A0A0J0YHA6_9ACTN Unreviewed; 472 AA. AC A0A0J0YHA6; DT 14-OCT-2015, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 1. DT 07-JUN-2017, entry version 13. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=IMCC26207_110659 {ECO:0000313|EMBL:KLR60408.1}; OS Actinobacteria bacterium IMCC26207. OC Bacteria; Actinobacteria. OX NCBI_TaxID=1641811 {ECO:0000313|EMBL:KLR60408.1, ECO:0000313|Proteomes:UP000036180}; RN [1] {ECO:0000313|EMBL:KLR60408.1, ECO:0000313|Proteomes:UP000036180} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=IMCC26207 {ECO:0000313|EMBL:KLR60408.1, RC ECO:0000313|Proteomes:UP000036180}; RA Kim S., Cho J.-C.; RT "Genome sequence of freshwater Actinobacteria."; RL Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KLR60408.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LCZK01000010; KLR60408.1; -; Genomic_DNA. DR RefSeq; WP_052603678.1; NZ_LCZK01000010.1. DR EnsemblBacteria; KLR60408; KLR60408; IMCC26207_110659. DR PATRIC; fig|1641811.3.peg.2972; -. DR Proteomes; UP000036180; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000036180}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000036180}. FT DOMAIN 244 407 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 472 AA; 51262 MW; 6BCD833AEB5EC86F CRC64; MSSADQDQVD LDPVDQALQD PELLDPNESH RGGFGDFGGQ SNSLIDRNFR ERIILVGVSF PPHDDDLLSA SLDELELLVD TAGADVVGRV VQRRNNPDPA TFIGKGKVQE IKELALETDC DTVVFDDELS PSQQFNLEKI LGRTAIDRTA VILDIFGQNA HSQEGKAQVQ LALFKYRLPR LRGKGTAMSQ QAGGIGTRSG PGETQFEIDR RRITKMIHKL EADLRQIAHH RATQRKSRRR STLRHVVIVG YTNAGKSTLL NSLTEAGVLV ENRLFATLDA TTRKLQLPGG ESVLLTDTVG FVKKLPHQLV QAFASTLDVV AEGDLLIHVV DGSGPDPEGQ MQAVRAVVKE IGGDAVPELL VFNKADCSDQ AARLAADSPG SVAISAVTGE GIPELLLRIG DRLRSLIPAV QMYIPYHRGD VLAALHRCGE VLTETAEPEG VRVSVRLEDS ELGRFEEFLS QALPETATAS SL // ID A0A0J1BIE4_9SPHI Unreviewed; 396 AA. AC A0A0J1BIE4; DT 14-OCT-2015, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 1. DT 07-JUN-2017, entry version 13. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=AB669_14820 {ECO:0000313|EMBL:KLT64983.1}; OS Pedobacter sp. BMA. OC Bacteria; Bacteroidetes; Sphingobacteriia; Sphingobacteriales; OC Sphingobacteriaceae; Pedobacter. OX NCBI_TaxID=1663685 {ECO:0000313|EMBL:KLT64983.1, ECO:0000313|Proteomes:UP000036014}; RN [1] {ECO:0000313|EMBL:KLT64983.1, ECO:0000313|Proteomes:UP000036014} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BMA {ECO:0000313|EMBL:KLT64983.1, RC ECO:0000313|Proteomes:UP000036014}; RA Anderson B.M., Pipes S.E., Miller J.R., Newman J.D.; RT "Pedobacter sp. BMA."; RL Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KLT64983.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LECU01000006; KLT64983.1; -; Genomic_DNA. DR RefSeq; WP_047800061.1; NZ_LECU01000006.1. DR EnsemblBacteria; KLT64983; KLT64983; AB669_14820. DR PATRIC; fig|1663685.3.peg.3109; -. DR Proteomes; UP000036014; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000036014}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000036014}. FT DOMAIN 204 384 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 396 AA; 45235 MW; 45FE358CBC1B7AA1 CRC64; MGKKKFYDTA IKQERAILVG VVTPDEKEEQ TKEYLDELAF LVDTAGGKVE KVFTQKMLKP ERATFVGTGK LEEIKAYVKS EEIDTVVFDD ELSPSQLRNI DRELGVKVLD RSNLILDIFA SRAQTAQAKT QVELAQLQYV LPRLTGMWTH LERQKGGIGM RGPGETQIES DRRIILNKIS LLKERLRNID RQNETQRKNR GQLIRVALVG YTNVGKSTIM NMLSKSEVFA ENKLFATLDT TVRKVVIENL PFLLSDTVGF IRKLPHHLVE CFKSTLDEVR EADLLIHVVD VSHPNFEDQI NTVNETLKDL GAVDKDTILV FNKIDAYVSP EVDNEEDDGK LTLEDFKRSW MSHDKVPVLF ISATEKENIE EFKTLLYDKI KAAHVARYPY DSNLLY // ID A0A0J1C5B7_9NEIS Unreviewed; 390 AA. AC A0A0J1C5B7; DT 14-OCT-2015, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 1. DT 07-JUN-2017, entry version 13. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=PL75_02735 {ECO:0000313|EMBL:KLT73498.1}; OS Neisseria arctica. OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=1470200 {ECO:0000313|EMBL:KLT73498.1, ECO:0000313|Proteomes:UP000036027}; RN [1] {ECO:0000313|EMBL:KLT73498.1, ECO:0000313|Proteomes:UP000036027} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=KH1503 {ECO:0000313|EMBL:KLT73498.1, RC ECO:0000313|Proteomes:UP000036027}; RA Hansen C.M., Hueffer K., Choi S.C.; RT "Genome of a novel goose pathogen."; RL Submitted (NOV-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KLT73498.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JTDO01000003; KLT73498.1; -; Genomic_DNA. DR EnsemblBacteria; KLT73498; KLT73498; PL75_02735. DR PATRIC; fig|1470200.3.peg.1628; -. DR Proteomes; UP000036027; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000036027}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000036027}. FT DOMAIN 218 387 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 390 AA; 43246 MW; B23AB8CF778FE62A CRC64; MLSRKPSLFQ IDKSLSKPER VMLVGVMLST DYSGANETRE RDFESAVAEA ADLVHATGGD LVRIETAKRE RAQSAFFVGT GKAEELAEQV RLHEIELVVF NHELTPTQER NLEKVLQCRV LDRVGLILAI FAQRAQSQEG KLQVELAQLS HLSGRLVRGY GHLQSQRGGI GLKGPGETQL ETDRRLINVR ITALKRQLEQ VKKQRATRRK SRMSGSLPTF ALVGYTNAGK SSLFNRLTKA DVLAKDQLFA TLDTTARRLY LSPEASVILT DTVGFVRDLP HKLVSAFSAT LEETALADVL LHVVDISHPH FERQMDDVNE VLKEIGAHEI PQLVVYNKID LLPGKAHQAG ILRDHEGRAA AVNISAVNGD GLDDLRVAMV EYVALKQDRK // ID A0A0J1CJP8_9BURK Unreviewed; 426 AA. AC A0A0J1CJP8; DT 14-OCT-2015, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 1. DT 30-AUG-2017, entry version 15. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=EOS_39280 {ECO:0000313|EMBL:KLU20799.1}; OS Caballeronia mineralivorans PML1(12). OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Caballeronia. OX NCBI_TaxID=908627 {ECO:0000313|EMBL:KLU20799.1, ECO:0000313|Proteomes:UP000035963}; RN [1] {ECO:0000313|EMBL:KLU20799.1, ECO:0000313|Proteomes:UP000035963} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=PML1(12) {ECO:0000313|Proteomes:UP000035963}; RX PubMed=26205858; RA Uroz S., Oger P.; RT "Draft Genome Sequence of Burkholderia sp. Strain PML1(12), an RT Ectomycorrhizosphere-Inhabiting Bacterium with Effective Mineral- RT Weathering Ability."; RL Genome Announc. 3:e00798-15(2015). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KLU20799.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AEJF01000238; KLU20799.1; -; Genomic_DNA. DR RefSeq; WP_047897638.1; NZ_AEJF01000238.1. DR EnsemblBacteria; KLU20799; KLU20799; EOS_39280. DR PATRIC; fig|908627.4.peg.8795; -. DR Proteomes; UP000035963; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000035963}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000035963}. FT DOMAIN 206 377 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 172 199 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 426 AA; 46911 MW; 5891E69449188D1E CRC64; MNVLIHRSLQ NENIDLINAA LVGIDFGKID FDASLEELSL LAQSAGAHPA VTLTGRRSSP DAKMFVGSGK VEELRLACDA NDVELVIFNH ALAPAQQRNL ETALDRRVID RTSLILDIFA QRARSHEGKL QVELAQLQYL STRLIRAWTH LERQKGGIGL RGPGETQLET DRRLIGERIK ALKARLMKLR RQHGTQRRQR VRNRTTSVSL VGYTNAGKST LFNALTKAQA YAADQLFATL DTTSRRVYLS EEAGQAVVSD TVGFIRDLPH QLVAAFRATL EETVQADLLL HVVDASSMVR LDQIDEVNKV LSSIGADGIP QILVFNKIDA VPELAARGDA VERDEYGNIL RVFLSARTGQ GLDALRAAIA EFAASEPKDN NEYTELPDGT IVPESMDSTS DDGTTLPEDH RSADESEDRK VPEHGH // ID A0A0J1GJI2_9GAMM Unreviewed; 429 AA. AC A0A0J1GJI2; DT 14-OCT-2015, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 1. DT 30-AUG-2017, entry version 14. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=ABT58_15875 {ECO:0000313|EMBL:KLU99720.1}; OS Photobacterium aphoticum. OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; OC Vibrionaceae; Photobacterium. OX NCBI_TaxID=754436 {ECO:0000313|EMBL:KLU99720.1, ECO:0000313|Proteomes:UP000036426}; RN [1] {ECO:0000313|EMBL:KLU99720.1, ECO:0000313|Proteomes:UP000036426} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 25995 {ECO:0000313|EMBL:KLU99720.1, RC ECO:0000313|Proteomes:UP000036426}; RA Machado H., Gram L.; RT "Photobacterium galathea sp. nov."; RL Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KLU99720.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LDOV01000028; KLU99720.1; -; Genomic_DNA. DR RefSeq; WP_047875421.1; NZ_LDOV01000028.1. DR EnsemblBacteria; KLU99720; KLU99720; ABT58_15875. DR PATRIC; fig|754436.4.peg.3367; -. DR Proteomes; UP000036426; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000036426}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000036426}. FT DOMAIN 198 365 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 429 AA; 48391 MW; D57094ACC7EFA530 CRC64; MFDRYESGEQ AILVHINFTQ EGEWEDLSEF EMLVSSAGVN TLQVVTGSRK TPHPKYYVGE GKAQEIAEAV RALDADIVIF NHSLSPAQER NLEQICKCRV LDRTGLILDI FAQRARTHEG KLQVELAQLR HISTRLIRGW THLERQKGGI GLRGPGETQL ETDRRLLRER IKTILRRLEK VAKQRDQGRR ARNRAEIPTI SLVGYTNAGK STLFNRVTNA GVYAADQLFA TLDPTLRKIE VADVGTSILA DTVGFIRHLP HDLVAAFKAT LKETQEATLL LHVVDASDDR FRENIEAVDS VLEEIEASDV PTLVVMNKID NLEGATPRIE RDDEGVPRRV WVSAMEGQGI DLLFDALTDC LSGTMVKHTL CLPPQYVGRY RSKFYQLGCI VHEEYDPDGN LKIDIRLPLA EWSRLQKRES TSLDDFIVA // ID A0A0J1GMM6_9FIRM Unreviewed; 404 AA. AC A0A0J1GMM6; DT 14-OCT-2015, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 1. DT 07-JUN-2017, entry version 12. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=AA931_00075 {ECO:0000313|EMBL:KLU40086.1}; OS Peptococcaceae bacterium 1109. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Peptococcaceae. OX NCBI_TaxID=1655638 {ECO:0000313|EMBL:KLU40086.1, ECO:0000313|Proteomes:UP000036486}; RN [1] {ECO:0000313|EMBL:KLU40086.1, ECO:0000313|Proteomes:UP000036486} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=1109 {ECO:0000313|EMBL:KLU40086.1}; RA Town J.R., Dumonceaux T.J.; RL Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KLU40086.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LDJB01000001; KLU40086.1; -; Genomic_DNA. DR EnsemblBacteria; KLU40086; KLU40086; AA931_00075. DR PATRIC; fig|1655638.3.peg.16; -. DR Proteomes; UP000036486; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000036486}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000036486}. FT DOMAIN 192 351 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 404 AA; 44719 MW; 984B1228DCF41306 CRC64; MQRTYLVSLQ LPGDSDWDVE DSLRELKDLA EDAGLEVVDW FVQKRPFPDA ATFIGSGKAE ELAAVVEPED LVIFDNELSP AQQGNLSDII GAAVIDRTQL ILDIFAQRAW TREGKIQVEL AQLNYLLPRL VGSGAALSRL GGGIGTRGPG ETKLETDRRR VRKRITDLKA ELETVRHVRA TQRARREKLA VPLVALVGYT NAGKSTLLRA LTGSETFVAD QLFATLDPTV RRWELPDGRW VFLSDTVGFI RRLPHTLVAA FRATLEEILY ADLLLHVIDI SHPQAREQQE AVEKVLAEIG AAQPVINVYN KIDICPDGQE FTGLGVAVSG VTGENLDRLA HEVTAFFSKY LSVQTFRFAF SDLGSASKLR ELGRVLEERY TAEGLEITAE VDPATAGLLR DYRI // ID A0A0J1GZ23_9GAMM Unreviewed; 429 AA. AC A0A0J1GZ23; DT 14-OCT-2015, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 1. DT 30-AUG-2017, entry version 14. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=ABT57_22940 {ECO:0000313|EMBL:KLV04868.1}; OS Photobacterium ganghwense. OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; OC Vibrionaceae; Photobacterium. OX NCBI_TaxID=320778 {ECO:0000313|EMBL:KLV04868.1, ECO:0000313|Proteomes:UP000035909}; RN [1] {ECO:0000313|EMBL:KLV04868.1, ECO:0000313|Proteomes:UP000035909} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 22954 {ECO:0000313|EMBL:KLV04868.1, RC ECO:0000313|Proteomes:UP000035909}; RA Machado H., Gram L.; RT "Photobacterium galathea sp. nov."; RL Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KLV04868.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LDOU01000031; KLV04868.1; -; Genomic_DNA. DR RefSeq; WP_047887590.1; NZ_LDOU01000031.1. DR EnsemblBacteria; KLV04868; KLV04868; ABT57_22940. DR PATRIC; fig|320778.3.peg.4908; -. DR Proteomes; UP000035909; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000035909}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000035909}. FT DOMAIN 198 365 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 429 AA; 48400 MW; CCAC122A633B2255 CRC64; MFDRYESGEQ AILVHINFTQ EGEWEDLSEF EMLVSSAGVN ALRVVTGSRK TPHPKYYVGE GKAQEIAEAV RAEGAEIVLF NHSLSPAQER NLEQICKCRV LDRTGLILDI FAQRARTHEG KLQVELAQLR HISTRLIRGW THLERQKGGI GLRGPGETQL ETDRRLLRER IKTILRRLDK VAKQRDQGRR ARNRAEIPTI SLVGYTNAGK STLFNRVTDA GVYAADQLFA TLDPTLRKID VADVGTTILA DTVGFIRHLP HDLVAAFKAT LKETQDATLL LHVVDASDDR FRENIEAVDT VLEEIEANEV PSLVVMNKID NLEGAEPRIE RDDDGVPRRV WVSAIDGQGI DLLFEALTER LSGTMVKHTL RVPPQYIGRI RSKFYQMGCI ISEEYDTDGS LKIDIRLPLA EWSRLQKRES TSLDDFIVA // ID A0A0J1IBG7_BACCI Unreviewed; 418 AA. AC A0A0J1IBG7; DT 14-OCT-2015, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 1. DT 07-JUN-2017, entry version 13. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=ABW02_19845 {ECO:0000313|EMBL:KLV23296.1}; OS Bacillus circulans. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus. OX NCBI_TaxID=1397 {ECO:0000313|EMBL:KLV23296.1, ECO:0000313|Proteomes:UP000036045}; RN [1] {ECO:0000313|EMBL:KLV23296.1, ECO:0000313|Proteomes:UP000036045} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=RIT379 {ECO:0000313|EMBL:KLV23296.1, RC ECO:0000313|Proteomes:UP000036045}; RA Lee Y.P., Gan H.M., Eng W., Wheatley M.S., Caraballo A., Polter S., RA Savka M.A., Hudson A.O.; RT "Whole genome sequence and identification of bacterial endophytes from RT Costus igneus."; RL Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KLV23296.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LDPH01000026; KLV23296.1; -; Genomic_DNA. DR RefSeq; WP_047944022.1; NZ_LDPH01000026.1. DR EnsemblBacteria; KLV23296; KLV23296; ABW02_19845. DR PATRIC; fig|1397.4.peg.2707; -. DR Proteomes; UP000036045; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000036045}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000036045}. FT DOMAIN 197 365 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 156 183 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 418 AA; 47232 MW; 4F09C549354F31F5 CRC64; MEGKQKAIVV GVHYDQKEDF ANSMEELIQL AEACDIEVVG EITQKLDRVH SGHYIGKGKL QELTALLAEK DVQAVLFNDE LSPSQVRNLE EATDCRIIDR TVLILDIFAQ RAKTKEAMLQ VEIAKLQYML PRLAGLGESL GRQGGGSGLI NRGSGETKLE LDRRRIEDRI SRLHKELDTL VVQRKNQRKM RKKKELPSIA LVGYTNAGKS TLMNVLLEKY HAATEKMVFE KNMLFATLET SVRNITLPKN KSFLLTDTVG FISKLPHQLV KAFRSTLEEV AEADLLIHVV DYSNPNYQEQ INVTNKTLKE LNAENIPAIY AFNKIDLAAG DTSMAGTDGV YLSAKRQIGI NELVEAISKN VFKQYISCEM TIPYDKGNVL SYLTEKANIL STEYKEEGIF LSIECKEEDY NRYREYVI // ID A0A0J1J2D9_9FIRM Unreviewed; 421 AA. AC A0A0J1J2D9; DT 14-OCT-2015, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 1. DT 07-JUN-2017, entry version 12. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=RHS_2908 {ECO:0000313|EMBL:KLU71271.1}; OS Robinsoniella sp. RHS. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Lachnospiraceae; OC Robinsoniella. OX NCBI_TaxID=1504536 {ECO:0000313|EMBL:KLU71271.1, ECO:0000313|Proteomes:UP000036477}; RN [1] {ECO:0000313|EMBL:KLU71271.1, ECO:0000313|Proteomes:UP000036477} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=RHS {ECO:0000313|EMBL:KLU71271.1}; RX PubMed=25284151; DOI=10.1016/j.cell.2014.09.008; RA Seedorf H., Griffin N.W., Ridaura V.K., Reyes A., Cheng J., Rey F.E., RA Smith M.I., Simon G.M., Scheffrahn R.H., Woebken D., Spormann A.M., RA Van Treuren W., Ursell L.K., Pirrung M., Robbins-Pianka A., RA Cantarel B.L., Lombard V., Henrissat B., Knight R., Gordon J.I.; RT "Bacteria from diverse habitats colonize and compete in the mouse RT gut."; RL Cell 159:253-266(2014). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KLU71271.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JNGB01000026; KLU71271.1; -; Genomic_DNA. DR EnsemblBacteria; KLU71271; KLU71271; RHS_2908. DR PATRIC; fig|1504536.3.peg.3512; -. DR Proteomes; UP000036477; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000036477}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000036477}. FT DOMAIN 207 371 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 421 AA; 47190 MW; F527DFFC53DA2F52 CRC64; MTGENMADLF DIEKLEEKVI LVGVSTSDDD DTMESLDELT DLASTAGAVT VGRIIQNREQ VHPGTYIGKG KIQELREMVY ELSATGVICD DELSPAQLRN LEQELDIKVM DRTLIILDIF AARASTSEGK IQVELAQLKY RLARLVGLRS SLSRLGGGIG TRGPGEKKLE MDRRLIKDRI AQLGRELADV KRHREVVRMK RSKNQTLVAA IVGYTNAGKS TLLNQLTDAK VLEEDKLFAT LDPTTRMLAL NGGQEILLTD TVGFIRKLPH HLIEAFRSTL EEAKYADIIL HVVDASNTQM EKQMFVVYET LANLGVTDKT VVTLFNKQDR VIEKETLRDF KADKTLCISA KTGEGLEELK NILEQILQEK NILIERIYPY ADAGLIQLIR KYGQLLEEDY RAEGIYVKAY VPMEIYGNVT G // ID A0A0J1KN65_BACCI Unreviewed; 431 AA. AC A0A0J1KN65; DT 14-OCT-2015, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 1. DT 07-JUN-2017, entry version 13. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=ABW02_24405 {ECO:0000313|EMBL:KLV18130.1}; OS Bacillus circulans. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus. OX NCBI_TaxID=1397 {ECO:0000313|EMBL:KLV18130.1, ECO:0000313|Proteomes:UP000036045}; RN [1] {ECO:0000313|EMBL:KLV18130.1, ECO:0000313|Proteomes:UP000036045} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=RIT379 {ECO:0000313|EMBL:KLV18130.1, RC ECO:0000313|Proteomes:UP000036045}; RA Lee Y.P., Gan H.M., Eng W., Wheatley M.S., Caraballo A., Polter S., RA Savka M.A., Hudson A.O.; RT "Whole genome sequence and identification of bacterial endophytes from RT Costus igneus."; RL Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KLV18130.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LDPH01000045; KLV18130.1; -; Genomic_DNA. DR RefSeq; WP_047944751.1; NZ_LDPH01000045.1. DR EnsemblBacteria; KLV18130; KLV18130; ABW02_24405. DR PATRIC; fig|1397.4.peg.4397; -. DR Proteomes; UP000036045; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000036045}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000036045}. FT DOMAIN 207 369 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 431 AA; 49624 MW; C8F820A164A76635 CRC64; MERRFTYLKE TKIEKEKVIL VGCETQNDAA RFAYSMEELA NLTKTANGVV VATLTQMRER IHPSTYIGKG KVEELEMLAE ELEADLIIFN DELSPSQVRN VSKNLDARII DRTQLILDIF ASRARSKEGK LQVELAQLQY LLPRLGGQGL QLSRLGAGIG TRGPGETKLE SDRRHIRRRI DDIKTQLSVI VEHRDRYRER RKKNRAFQIA LVGYTNAGKS TLFNRLSEAD SFEEDILFAT LDPMTRKIIL PSGFSALITD TVGFIQDLPT TLVAAFRSTL EEVREADLLL HVVDSSNEEY YQHEETVHKL LEDLEIPAIP HLTVYNKKDL VHPKFVPTSK TESILISAFN KEDREQLKQT IEQMMMENME YYETTVESNN GKLLSQLKNE TVLRSLIFDE ETQNYLCKGY AFKEHAILNY KKSIEKEEWE K // ID A0A0J5G1K1_9NEIS Unreviewed; 462 AA. AC A0A0J5G1K1; DT 14-OCT-2015, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 1. DT 07-JUN-2017, entry version 13. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=ACG97_16565 {ECO:0000313|EMBL:KMJ48299.1}; OS Vogesella sp. EB. OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Chromobacteriaceae; Vogesella. OX NCBI_TaxID=1526735 {ECO:0000313|EMBL:KMJ48299.1, ECO:0000313|Proteomes:UP000054352}; RN [1] {ECO:0000313|EMBL:KMJ48299.1, ECO:0000313|Proteomes:UP000054352} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=EB {ECO:0000313|EMBL:KMJ48299.1, RC ECO:0000313|Proteomes:UP000054352}; RA Arrua Day P., Revale S., Alvarez H.M.; RT "Genome wide analysis of metabolism in the polyhydroxybutyrate- RT producing Vogesella sp. strain EB."; RL Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KMJ48299.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LFDT01000053; KMJ48299.1; -; Genomic_DNA. DR RefSeq; WP_047968493.1; NZ_LFDT01000053.1. DR EnsemblBacteria; KMJ48299; KMJ48299; ACG97_16565. DR PATRIC; fig|1526735.3.peg.3521; -. DR Proteomes; UP000054352; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000054352}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000054352}. FT DOMAIN 226 348 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 189 221 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 462 AA; 51426 MW; 7AF6BB1E621836AA CRC64; MQTEVKEKPR YALVASVQLP DVSDVEFEAS LAELSELAKT LGFQVVQTFV QKRSSFDRTA YLGVGKLEEV SMFVNRGVRN DELEAGSPAL DADAVEFDVL LVDHEISPSQ ARNLELAVGC AVMDRTMVIL EIFHRNARSR AARAQVEIAR LGYMAPRLRE AAKLAGPQGR QRSGVGGRGA GESHTELDRR KVRDRIAELQ REIIAMELER KTQRARRLER QGLGLGGVSL VGYTNAGKST LMRALTGSEV LVANKLFATL DTTVRALYPE SVPRVLVSDT VGFIKNLPHG LVASFKSTLE EALDAALLLH VIDASDPGFL RQLEVTDEVL QEIGADEVPR IRVFNKIDHV GDETAQAAWT AELQQRYPGC VVMSARRPEE VASLHATIVS FFQQDLVEDE LLLPWSVQQL RGDIYSHCQV LEERAEEDGS WFRVRGEPEK LRSLREQLSP GAQGREKEYW EV // ID A0A0J5GHQ2_9NEIS Unreviewed; 378 AA. AC A0A0J5GHQ2; DT 14-OCT-2015, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 1. DT 07-JUN-2017, entry version 13. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=ACG97_04305 {ECO:0000313|EMBL:KMJ54039.1}; OS Vogesella sp. EB. OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Chromobacteriaceae; Vogesella. OX NCBI_TaxID=1526735 {ECO:0000313|EMBL:KMJ54039.1, ECO:0000313|Proteomes:UP000054352}; RN [1] {ECO:0000313|EMBL:KMJ54039.1, ECO:0000313|Proteomes:UP000054352} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=EB {ECO:0000313|EMBL:KMJ54039.1, RC ECO:0000313|Proteomes:UP000054352}; RA Arrua Day P., Revale S., Alvarez H.M.; RT "Genome wide analysis of metabolism in the polyhydroxybutyrate- RT producing Vogesella sp. strain EB."; RL Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KMJ54039.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LFDT01000005; KMJ54039.1; -; Genomic_DNA. DR RefSeq; WP_047966109.1; NZ_LFDT01000005.1. DR EnsemblBacteria; KMJ54039; KMJ54039; ACG97_04305. DR PATRIC; fig|1526735.3.peg.919; -. DR Proteomes; UP000054352; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000054352}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000054352}. FT DOMAIN 198 364 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 378 AA; 41639 MW; 22479C0292C5AA62 CRC64; MFDRPDLGDI AVLVCLDFGA PDYDEGVQEC VDLVRSAGVT VAGTIHGKRQ RPDAALFAGK GKVEEIAALV NAVAANVVIF NHALGPGQER NLERVLQCRV VDRVTLILDI FAQRARSHEG KLQVELAQLS HLSTRLVRGW THLERQKGGI GLRGPGETQL ETDRRLLGLR VKMLKDRLAA VARQRKTQRR SRERSGLQSV SIVGYTNAGK STLFNAMTKA QAYAADQLFA TLDTTSRKLY LSPELSIVLS DTVGFIRDLP HSLVAAFRAT LEETIQADML LHVVDSASPD KDRQIEEVDK VLAEIGASST PQLLVWNKTD LRGLPPQIER GEHGEPVAVR VSALTGEGLE LLRQAIAERL HGFNNDHNIE DRDRYGTE // ID A0A0J5P292_PLUGE Unreviewed; 426 AA. AC A0A0J5P292; DT 14-OCT-2015, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 1. DT 30-AUG-2017, entry version 15. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=ABW06_07645 {ECO:0000313|EMBL:KMK14702.1}; OS Pluralibacter gergoviae (Enterobacter gergoviae). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; OC Enterobacteriaceae; Pluralibacter. OX NCBI_TaxID=61647 {ECO:0000313|EMBL:KMK14702.1, ECO:0000313|Proteomes:UP000036196}; RN [1] {ECO:0000313|EMBL:KMK14702.1, ECO:0000313|Proteomes:UP000036196} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=JS81F13 {ECO:0000313|EMBL:KMK14702.1, RC ECO:0000313|Proteomes:UP000036196}; RA Greninger A.L., Miller S.; RT "Genome sequences of Pluralibacter gergoviae."; RL Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KMK14702.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LDZF01000006; KMK14702.1; -; Genomic_DNA. DR RefSeq; WP_048278599.1; NZ_LDZF01000006.1. DR EnsemblBacteria; KMK14702; KMK14702; ABW06_07645. DR PATRIC; fig|61647.15.peg.4767; -. DR Proteomes; UP000036196; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000036196}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000036196}. FT DOMAIN 198 365 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 426 AA; 48118 MW; FB52C48270BB5B65 CRC64; MFDRYDAGEQ AVLVHIYFSQ DKDMEDLQEF ESLVSSAGVE AMQVITGSRK APHPKYFVGE GKAVEIAEAV KATGASVVLL DHALSPAQER NLEQLCQCRV IDRTGLILDI FAQRARTHEG KLQVELAQLR HLATRLVRGW THLERQKGGI GLRGPGETQL ETDRRLLRNR IMQILSRLER VEKQREQGRR SRTKADIPTV SLVGYTNAGK STLFNQITEA QVYAADQLFA TLDPTLRRIN VADVGETVLA DTVGFIRHLP HDLVAAFKAT LQETRQATLL LHVIDAADVR VQENIDAVNV VLDEIDASEI PMLLVMNKID ALENFEPRID RDEENKPIRV WLSAQTGIGV PLLFQALTER LSGEVAQHTL RLPPQEGRLR SRFYQLQAIE KEWMEDDGSV GLEVRMPIVD WRRLCKQEPA LEDYLV // ID A0A0J5P9V5_9PAST Unreviewed; 451 AA. AC A0A0J5P9V5; DT 14-OCT-2015, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 1. DT 07-JUN-2017, entry version 13. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=RO21_00430 {ECO:0000313|EMBL:KMK52520.1}; OS Muribacter muris. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Muribacter. OX NCBI_TaxID=67855 {ECO:0000313|EMBL:KMK52520.1, ECO:0000313|Proteomes:UP000036270}; RN [1] {ECO:0000313|EMBL:KMK52520.1, ECO:0000313|Proteomes:UP000036270} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Ackerman80-443D {ECO:0000313|EMBL:KMK52520.1, RC ECO:0000313|Proteomes:UP000036270}; RA Christensen H., Nicklas W., Bisgaard M.; RT "Reclassification of Actinobacillus muris as Muribacter muris."; RL Submitted (DEC-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KMK52520.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JWIZ01000002; KMK52520.1; -; Genomic_DNA. DR EnsemblBacteria; KMK52520; KMK52520; RO21_00430. DR PATRIC; fig|67855.3.peg.525; -. DR Proteomes; UP000036270; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000036270}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000036270}. FT DOMAIN 216 383 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 451 AA; 50237 MW; 9246154B72482851 CRC64; MISQPSTDNV FGLAQSGKAP TSAQTERAIL VHLYLSQVKD TENLLEFQTL AQSAGVEIAA VLTGSRQTPH IKYYVGQGKA QEIAQAVETF NAAVILVNHA LSPAQNRNLS QLCGCRVVDR TGLILDIFAQ RARSHEGKLQ VELAQLRHLS SRLVRRLGHQ DQQKGGAVGL RGPGETQLET DKRLIKLKIL QLQNRLEKVH KQRSQNRKTR QKADIPTISL VGYTNAGKST LFNRLTNANV YAADQLFATL DPTLRRLSLQ DVGTAILADT VGFIRFLPHD LVSAFKSTLQ ETSEADLLLH VIDAADSRRD ENIAAVNQVL ENIQAHDVPS LLVFNKIDRL EGVAPHITYD DEGSPTAVYL AAETEQGIDL LLHAISAKLK NELTRQTLLL PVTSGRIYAK FYQQQCILSE QLTPFGDRLI DIEVDHIQWQ KWLKQYPELN EFAELAKWEQ A // ID A0A0J5PCL0_9LACT Unreviewed; 435 AA. AC A0A0J5PCL0; DT 14-OCT-2015, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 1. DT 07-JUN-2017, entry version 13. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:KMK53299.1}; GN ORFNames=FEFB_09710 {ECO:0000313|EMBL:KMK53299.1}; OS Fructobacillus sp. EFB-N1. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Leuconostocaceae; OC Fructobacillus. OX NCBI_TaxID=1658766 {ECO:0000313|EMBL:KMK53299.1, ECO:0000313|Proteomes:UP000036087}; RN [1] {ECO:0000313|EMBL:KMK53299.1, ECO:0000313|Proteomes:UP000036087} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=EFB-N1 {ECO:0000313|EMBL:KMK53299.1, RC ECO:0000313|Proteomes:UP000036087}; RA Djukic M., Poehlein A., Daniel R.; RT "Genome sequence of Fructobacillus sp. EFB-N1."; RL Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KMK53299.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LDUY01000016; KMK53299.1; -; Genomic_DNA. DR RefSeq; WP_047975097.1; NZ_LDUY01000016.1. DR EnsemblBacteria; KMK53299; KMK53299; FEFB_09710. DR PATRIC; fig|1658766.3.peg.980; -. DR Proteomes; UP000036087; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000036087}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000036087}. FT DOMAIN 209 382 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 435 AA; 48139 MW; 26AD81488DD45778 CRC64; MPTTFKESSQ QPSRPVLLAG LRTDQKQNLE YELTELKNLA LANNLQPVET FLQSLDRPNP ATYFGKGKVD ELKVAVETYG ADLIVTNDEL SPSQIRNLEA ETGATVVDRT GLILDIFAKR AQTKVAKLQV QLARLQYQLP RLRTSMSVSL DQQTGAGGAG FTSRGSGETK LEQSRRRLTN EMVAIKKDLA ELQKDASTQA KQRQESELPT VALVGYTNAG KSTLMNQLLA RFGQGAGSDQ SKQVFEKDML FATLNTTIRQ LTLPDKTQFL LSDTVGFVSK LPHHLVAAFE STLQEAAQAD LLLQVVDISD AHYQEMMATT QETLNRLGIT DKPMITIYNK ADVAEMAFPL VDGDQSITIS ARDRTSQDEV LILIKKTLFA DMAEVSLHVP FADSKVVAEI LDKHALLDQD FNESGTTIRV SLKPKEIEQY KQYLA // ID A0A0J5QDG5_9RHOB Unreviewed; 424 AA. AC A0A0J5QDG5; DT 14-OCT-2015, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 1. DT 07-JUN-2017, entry version 13. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=IMCC21224_111828 {ECO:0000313|EMBL:KMK66966.1}; OS Puniceibacterium sp. IMCC21224. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae; Puniceibacterium. OX NCBI_TaxID=1618204 {ECO:0000313|EMBL:KMK66966.1, ECO:0000313|Proteomes:UP000036046}; RN [1] {ECO:0000313|EMBL:KMK66966.1, ECO:0000313|Proteomes:UP000036046} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=IMCC21224 {ECO:0000313|EMBL:KMK66966.1, RC ECO:0000313|Proteomes:UP000036046}; RA Cho J.-C., Yang S.-J., Kang I.; RT "Complete genome sequence of IMCC21224 belonging to the RT Alphaproteobacteria."; RL Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KMK66966.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LDPY01000001; KMK66966.1; -; Genomic_DNA. DR RefSeq; WP_047995049.1; NZ_LDPY01000001.1. DR EnsemblBacteria; KMK66966; KMK66966; IMCC21224_111828. DR PATRIC; fig|1618204.4.peg.1865; -. DR Proteomes; UP000036046; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000036046}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000036046}. FT DOMAIN 204 373 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 424 AA; 46860 MW; 3470551043B85C28 CRC64; MNEHDTHVTR AWVLHPDIKS DRDRRDALAA LDEAVALAAA LPNLEVVGST VVPLPKPHAG RLFGSGKIAE LKAQLEEAEA ELVLVDGPVT PVQQRNLEKD WNVKLLDRTG LILEIFSDRA ATREGVLQVE MAALSYQRTR LVRAWTHLER QRGGLGFVGG PGETQIEADR RAIDDQLVRI RRQIDKVSKT RGLHRAARAK VPFPIVALVG YTNAGKSTLF NRLTGAEVMA KDMLFATLDP TMRAVRLDGR LDVILSDTVG FISDLPTELV AAFRATLEEV LAADLIVHVR DIHHANTAEQ AEDVRSILKA LGVGEETPQL EVWNKVDLLE DEAREAALNR SGRDDNIISV SALTGEGLPD FLAAVMQRLE VEKRTEQLHL GYDDGKRRAW LFQKGLVEAE SESEAGFDLT VRWSAQEALA FGRL // ID A0A0J5TRZ6_9BACI Unreviewed; 423 AA. AC A0A0J5TRZ6; DT 14-OCT-2015, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 1. DT 07-JUN-2017, entry version 13. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=AB990_13245 {ECO:0000313|EMBL:KMK76179.1}; OS Bacillus pseudalcaliphilus. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus. OX NCBI_TaxID=79884 {ECO:0000313|EMBL:KMK76179.1, ECO:0000313|Proteomes:UP000035915}; RN [1] {ECO:0000313|EMBL:KMK76179.1, ECO:0000313|Proteomes:UP000035915} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 8725 {ECO:0000313|EMBL:KMK76179.1, RC ECO:0000313|Proteomes:UP000035915}; RA Liu B., Wang J., Zhu Y., Liu G., Chen Q., Zheng C., Lan J., Che J., RA Ge C., Shi H., Pan Z., Liu X.; RL Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KMK76179.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LFJO01000005; KMK76179.1; -; Genomic_DNA. DR RefSeq; WP_047989056.1; NZ_LFJO01000005.1. DR EnsemblBacteria; KMK76179; KMK76179; AB990_13245. DR PATRIC; fig|79884.3.peg.4106; -. DR Proteomes; UP000035915; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000035915}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000035915}. FT DOMAIN 198 367 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 157 184 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 423 AA; 48417 MW; EEB395F8DDD8F2EE CRC64; MEERIEKALL IGAELAKQEH INVSLEELEQ LALACDVEVV ATLTQRLDKV NPSTYVGAGK LQEAKVLLEQ FEANVVIFDD ELSPSQIRNI EAILECKVID RTILILDIFS KRAKTKEARL QVELAQMQYM LPRLVGLRQS LGRQVGGVGT TNRGAGETKL ELDRRKIEEK MVILKKELSR LVKQRQIQRE RRKKDGIPVV ALVGYTNAGK STLLNALLDM DVNLGEKKLV LEKNMLFATL ETAVRKVTLE KKRSFLLTDT VGFVHKLPHH LVQAFRSTLE EVKEADLLIH VVDYSNSAHE QHIKVTNDTL KEIGVEQVPM VYVFNKSDLV EKHFQWKDKG VIYVSAKEGT GFLELQEQLE QHLFYDDVEA EFLFPYSAGE LVAYFQQHAD VLEVKHDELG TYMKVLCRQK DFKKYKQFVK ENE // ID A0A0J6CZY8_9BACI Unreviewed; 420 AA. AC A0A0J6CZY8; DT 14-OCT-2015, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 1. DT 07-JUN-2017, entry version 13. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=AB986_04930 {ECO:0000313|EMBL:KMM38623.1}; OS Anaerobacillus macyae. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; OC Anaerobacillus. OX NCBI_TaxID=157733 {ECO:0000313|EMBL:KMM38623.1, ECO:0000313|Proteomes:UP000035996}; RN [1] {ECO:0000313|EMBL:KMM38623.1, ECO:0000313|Proteomes:UP000035996} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 16346 {ECO:0000313|EMBL:KMM38623.1, RC ECO:0000313|Proteomes:UP000035996}; RA Liu B., Wang J., Zhu Y., Liu G., Chen Q., Zheng C., Che J., Ge C., RA Shi H., Pan Z., Liu X.; RL Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KMM38623.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LELK01000001; KMM38623.1; -; Genomic_DNA. DR RefSeq; WP_048309740.1; NZ_LELK01000001.1. DR EnsemblBacteria; KMM38623; KMM38623; AB986_04930. DR PATRIC; fig|157733.3.peg.3222; -. DR Proteomes; UP000035996; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000035996}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000035996}. FT DOMAIN 202 363 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 420 AA; 47764 MW; 43F6BE53F16CED0B CRC64; MNKERIEIAE PAILIGCQLQ KYTDEQFAYS MDELAALTKT AGGVVEGTLT QKRERIHSAT FIGKGKVEEL AELIEEKEAS IVIFNSELSP SQLRNLSEEL DARVIDRTQL ILDIFAQRAR SREGMLQVEL AQLQYMLPRL AGQGTSLSRL GGGIGTRGPG ETKLETDRRY IRNRITDLKK QLDHTVKHRE QYRARRKRNE TLQVALVGYT NAGKSTIFNR LTNSDSYEED KLFATLDPMT RQLKLPNGFN VLLTDTVGFI QDLPTTLVAS FKSTLEEATE ADLILHVIDA AHPDRARHEE IVLKLLKDLK ASHIPVLTVF NKMDKADPAV QSSVNEQIHI SAIKESDLKS LNDRLQKEVL KQMEYFSISI QADQGDKLAY LQSNTVLLER KWDEEKDHYR CKGYAPAHLY ERIVKDWNND // ID A0A0J6GG83_9CELL Unreviewed; 515 AA. AC A0A0J6GG83; DT 14-OCT-2015, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 1. DT 07-JUN-2017, entry version 13. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=CWIS_08895 {ECO:0000313|EMBL:KMM45767.1}; OS Cellulomonas sp. A375-1. OC Bacteria; Actinobacteria; Micrococcales; Cellulomonadaceae; OC Cellulomonas. OX NCBI_TaxID=1672219 {ECO:0000313|EMBL:KMM45767.1, ECO:0000313|Proteomes:UP000036147}; RN [1] {ECO:0000313|EMBL:KMM45767.1, ECO:0000313|Proteomes:UP000036147} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=A375-1 {ECO:0000313|EMBL:KMM45767.1, RC ECO:0000313|Proteomes:UP000036147}; RA Wadler C.S., Steinberger A.J., Suen G.; RT "Draft Genome Sequence of Cellulomonas wisconsinensis."; RL Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KMM45767.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LFKW01000079; KMM45767.1; -; Genomic_DNA. DR RefSeq; WP_048342912.1; NZ_LFKW01000079.1. DR EnsemblBacteria; KMM45767; KMM45767; CWIS_08895. DR PATRIC; fig|1672219.3.peg.3246; -. DR Proteomes; UP000036147; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 2. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000036147}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000036147}. FT DOMAIN 293 459 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 515 AA; 55238 MW; 8EF8FF8AE21ED27D CRC64; MSETHHTTTP STTPDEPRSP QQVADDVVAR VLARAGTALH AGGTVHSAYD GDQLDLEERT SLRRVAGLST ELEDVTEVEY RELRLEKVVL VGVWGSSSSA GTSNGTLQDA EVSLRELAAL AETAGSTVLD GLLQRRAKPD PGTYLGSGKA AELASVVAAV GADTVVIDGE LAPSQRRALE DIVRVKVVDR TALILDIFAQ HAKSREGKAQ VELAQLEYLL PRLRGWGESM SRQAGGQVGG AGAGMGSRGP GETKIELDRR RIRNRMAKLR REIAAMEPAR MTKRASRKRH AIPSVAIAGY TNAGKSSLLN RLTNAGVLVE NALFATLDPT VRRAETVDGR VYTLADTVGF VRSLPHQLVE AFRSTLEEVA DADLILHVVD ASHPDPEGQI AAVRHVFADI PGAMDVPEII VLNKADLASP EVIARLRSRE LHSIVVSAHS GEGIAELQAL VADQLPRPGV TVDVVVPYQR GDLVSRVHEH GDIDHEEHTA DGTLLRARVD ESLAAELEEA SVRRA // ID A0A0J6NGV4_9NEIS Unreviewed; 376 AA. AC A0A0J6NGV4; DT 14-OCT-2015, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 1. DT 07-JUN-2017, entry version 13. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=VK98_21325 {ECO:0000313|EMBL:KMN76347.1}; OS Chromobacterium sp. LK11. OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Chromobacteriaceae; Chromobacterium. OX NCBI_TaxID=1628212 {ECO:0000313|EMBL:KMN76347.1, ECO:0000313|Proteomes:UP000036114}; RN [1] {ECO:0000313|EMBL:KMN76347.1, ECO:0000313|Proteomes:UP000036114} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=LK11 {ECO:0000313|EMBL:KMN76347.1, RC ECO:0000313|Proteomes:UP000036114}; RA Chan X.Y.; RT "Draft genome of Chromobacterium aquaticum LK11."; RL Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KMN76347.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LDUR01000045; KMN76347.1; -; Genomic_DNA. DR RefSeq; WP_048415951.1; NZ_LDUR01000045.1. DR EnsemblBacteria; KMN76347; KMN76347; VK98_21325. DR PATRIC; fig|1628212.3.peg.3786; -. DR Proteomes; UP000036114; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000036114}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000036114}. FT DOMAIN 198 364 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 164 191 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 376 AA; 41537 MW; 8EFB23B4996C3674 CRC64; MFDRPDLGDQ AVLVCLDFGD ADYQENIAEC AELVRSAGVE VMGVVQGKRQ RPDAALFAGK GKVEEIGLLV RATDANVVIF NHALAPGQER NLERALQCRV IDRNSLILDI FAQRARSHEG KLQVELAQLS HMSTRLVRGW THLERQKGGI GLRGPGETQL ETDRRLLGIR VKALKERLAQ VQKQRNTQRK GRGRAGIASV SIVGYTNAGK STLFNALTKA RIYAADQLFA TLDTTSRKLF LNHQTSIVIS DTVGFIRDLP HTLVAAFRAT LEETVRADLL LHVVDCSSDM RDVQIEEVNK VLAEIGADGI PQLLVWNKCD LREMEPEIER DAAGRPVSVR VSALTGAGLE LLRAAVAECV HPSQNNHKDY YEHVAE // ID A0A0J6NPS8_9NEIS Unreviewed; 462 AA. AC A0A0J6NPS8; DT 14-OCT-2015, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 1. DT 07-JUN-2017, entry version 13. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=VK98_06910 {ECO:0000313|EMBL:KMN82757.1}; OS Chromobacterium sp. LK11. OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Chromobacteriaceae; Chromobacterium. OX NCBI_TaxID=1628212 {ECO:0000313|EMBL:KMN82757.1, ECO:0000313|Proteomes:UP000036114}; RN [1] {ECO:0000313|EMBL:KMN82757.1, ECO:0000313|Proteomes:UP000036114} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=LK11 {ECO:0000313|EMBL:KMN82757.1, RC ECO:0000313|Proteomes:UP000036114}; RA Chan X.Y.; RT "Draft genome of Chromobacterium aquaticum LK11."; RL Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KMN82757.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LDUR01000010; KMN82757.1; -; Genomic_DNA. DR RefSeq; WP_048413338.1; NZ_LDUR01000010.1. DR EnsemblBacteria; KMN82757; KMN82757; VK98_06910. DR PATRIC; fig|1628212.3.peg.311; -. DR Proteomes; UP000036114; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000036114}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000036114}. FT DOMAIN 226 396 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 189 216 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 462 AA; 51594 MW; F5135BF4B4F04793 CRC64; MQTEVKEKPR YALVASVQLP DVSDVEFEAS LTELSELAKT LGFQVVRTFV QKRNSFDRTA YMGVGKLEEI SQFVNRGLRN DELDDAPPVL DASAVEIDAL LVDHEISPSQ ARNLELAVGC EVMDRTMVIL EIFHRNARSR AARAQVEIAR LGYMAPRLRE AAKLAGPQGR QRSGMGGRGA GESHTELDRR KVRDRIAELQ REIIAMELER KTQRARRVER QGQGLGGVSL VGYTNAGKST LMRALTGSEV LVANKLFATL DTTVRAIYPE SVPRVLVSDT VGFIKNLPHG LVASFKSTLE EALDAALLLH VIDASDPGFQ RQLEVTDEVL REIGADEVPR IRVFNKIDHV GDAAAQAACA AELRQRYPDC VVMSARRPEE VAALRALIVA FFQRDLEEGE LLLPWSAQQL RGEIYSHCQV LEERADEEGS WFRVRGEPDK LRSLREQLNP GSQGREKEYW EL // ID A0A0J6TS60_9RHIZ Unreviewed; 459 AA. AC A0A0J6TS60; DT 14-OCT-2015, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 1. DT 07-JUN-2017, entry version 12. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=QR78_21345 {ECO:0000313|EMBL:KMO15401.1}; OS Methylobacterium platani. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Methylobacteriaceae; Methylobacterium. OX NCBI_TaxID=427683 {ECO:0000313|EMBL:KMO15401.1, ECO:0000313|Proteomes:UP000036498}; RN [1] {ECO:0000313|EMBL:KMO15401.1, ECO:0000313|Proteomes:UP000036498} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SE2.11 {ECO:0000313|EMBL:KMO15401.1, RC ECO:0000313|Proteomes:UP000036498}; RA Chaudhry V., Patil P.B.; RT "Comparative genomics of Methylobacterium species."; RL Submitted (NOV-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KMO15401.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JTHF01000185; KMO15401.1; -; Genomic_DNA. DR RefSeq; WP_048429572.1; NZ_JTHF01000185.1. DR EnsemblBacteria; KMO15401; KMO15401; QR78_21345. DR PATRIC; fig|427683.5.peg.2481; -. DR Proteomes; UP000036498; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000036498}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000036498}. FT DOMAIN 222 396 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 459 AA; 51126 MW; B3F9ED625DD7FE9E CRC64; MEPRTPGEIR LQRQAEPEAA IAAETRTLVI GPYQTRRDHG GEPRAPLARL DEAVGLAAAI ELDVADRLLV TVQQIRPSTF LGKGRVEEIA GRIEADGIRL VVMDCALSPV QQRNLEKAWG VKVIDRTGLI LEIFGRRAST REGTLQVEHA HLAYQRSRLV RSWTHLERQR GGFGFLGGPG ETQIEADRRM IQERMTRIER DLETVTRTRG LHRRSRRRVP YPIVALVGYT NAGKSTLFNR LTRAEVLAED MLFATLDPTA RAIKLPHGET AILSDTVGFI SDLPTMLIAA FRATLEDVIE ADILLHVRDI AHEDAEAQGA DVAQVLTELG IEPNTDRVIE VWNKADLLDE AERERLMNLS RPNGKEGPKP VLLSALTGEG IDRLMSRIEA RIAATRTSFA VILDPAQGAE LHWLYENAEV LDRREDAEGA MHLVVRVAPE KEPRFLNRFG AARRLRGGG // ID A0A0J7HP27_9BACT Unreviewed; 390 AA. AC A0A0J7HP27; DT 14-OCT-2015, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 1. DT 07-JUN-2017, entry version 13. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=CHISP_2589 {ECO:0000313|EMBL:KMQ50471.1}; OS Chitinispirillum alkaliphilum. OC Bacteria; Fibrobacteres; Chitinispirillia; Chitinispirillales; OC Chitinispirillaceae; Chitinispirillum. OX NCBI_TaxID=1008392 {ECO:0000313|EMBL:KMQ50471.1, ECO:0000313|Proteomes:UP000036214}; RN [1] {ECO:0000313|EMBL:KMQ50471.1, ECO:0000313|Proteomes:UP000036214} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ACht6-1 {ECO:0000313|EMBL:KMQ50471.1, RC ECO:0000313|Proteomes:UP000036214}; RA Sorokin D.Y., Rakitin A.L., Gumerov V.M., Beletsky A.V., RA Sinninghe Damste J.S., Mardanov A.V., Ravin N.V.; RT "Phenotypic and genomic properties of Chitinispirillum alkaliphilum RT gen. nov., sp. nov., a haloalkaliphilic anaerobic chitinolytic RT bacterium from the candidate phylum TG3."; RL Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KMQ50471.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LDWW01000020; KMQ50471.1; -; Genomic_DNA. DR EnsemblBacteria; KMQ50471; KMQ50471; CHISP_2589. DR PATRIC; fig|1008392.3.peg.2854; -. DR Proteomes; UP000036214; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000036214}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000036214}. FT DOMAIN 199 365 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 160 187 {ECO:0000256|SAM:Coils}. FT COILED 343 370 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 390 AA; 44165 MW; 76D560D5CBB6AEBA CRC64; MIENKHIHEK VIIAGLLIKD ENPKLFEEDI EEMVMLCTTA GAEVADVVVQ KRLRPEASTY LGEGKLVELR ALMRQKGAKT LVVDAHLSPG QVRNVEKLIN AKVLDRGQVI LDIFALHART VEAKVQVELA QMRTLYPRLT HAWTHFSQQV GGIGTRGPGE KQLEVDRRLV QKKIRDLKQR LQKIERNREV QGKGRSKVFK ASLVGYTNVG KSSVLNALSG SDVLVENKLF ATLDTSTRRT YIPGAGSIVI SDTVGFLRKL PHHLVASFRS TLRVVSEAQL LLVVLDASSE FFDQQLATVE KVLEELKAEK IPKILVFNKF DLVQDPFTRK KLSLAYPEAM FVSAFSKEDM DRLKERISEY IKQHKREEQA ESIIKTGTKK IMRDIEHHLF // ID A0A0J7IZA6_9FLAO Unreviewed; 403 AA. AC A0A0J7IZA6; DT 14-OCT-2015, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 1. DT 07-JUN-2017, entry version 13. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=ACM44_06910 {ECO:0000313|EMBL:KMQ71347.1}; OS Chryseobacterium koreense CCUG 49689. OC Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales; OC Flavobacteriaceae; Chryseobacterium. OX NCBI_TaxID=1304281 {ECO:0000313|EMBL:KMQ71347.1, ECO:0000313|Proteomes:UP000035900}; RN [1] {ECO:0000313|EMBL:KMQ71347.1, ECO:0000313|Proteomes:UP000035900} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CCUG 49689 {ECO:0000313|EMBL:KMQ71347.1, RC ECO:0000313|Proteomes:UP000035900}; RX PubMed=15545478; DOI=10.1099/ijs.0.02998-0; RA Kim M.K., Im W.T., Shin Y.K., Lim J.H., Kim S.H., Lee B.C., Park M.Y., RA Lee K.Y., Lee S.T.; RT "Kaistella koreensis gen. nov., sp. nov., a novel member of the RT Chryseobacterium-Bergeyella-Riemerella branch."; RL Int. J. Syst. Evol. Microbiol. 54:2319-2324(2004). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KMQ71347.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LFNG01000008; KMQ71347.1; -; Genomic_DNA. DR RefSeq; WP_048499308.1; NZ_LFNG01000008.1. DR EnsemblBacteria; KMQ71347; KMQ71347; ACM44_06910. DR PATRIC; fig|1304281.5.peg.1481; -. DR Proteomes; UP000035900; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000035900}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000035900}. FT DOMAIN 200 384 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 403 AA; 46782 MW; 2C9F38474273CD5A CRC64; MLEKKEHLYE KAVLVGLITQ NQDEAKLKEY LDELEFLAFT AGATVDKRFT QKMSQPDSKT FVGSGKAEEI RNYIKENGIT TVIFDDELSP SQLKNLEKEM EVKILDRTNL ILDIFAQRAQ TSYARTQVEL AQYEYLLPRL TRMWTHLERQ RGGIGMRGPG ETEIETDRRI IRDRISLLKE KLKTIDKQMS TQRQNRGKMV RVALVGYTNV GKSTLMNAIS KSEVFAENKL FATLDTTVRK VVVGNLPFLL TDTVGFIRKL PTQLVESFKS TLDEVREADL LIHVVDISHD SFEDHINSVN QILMEIGAHQ KPMIMVFNKI DAFAYEKKEE DDLTPSNRKN ISLAEWEKTW MSKSKYPTVF ISALTKENFP EMKKMIYDEV LKIHISRFPY NDFLFEYYDD EEN // ID A0A0J7KPW5_LASNI Unreviewed; 463 AA. AC A0A0J7KPW5; DT 14-OCT-2015, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 1. DT 10-MAY-2017, entry version 8. DE SubName: Full=Gtp-binding protein 6 {ECO:0000313|EMBL:KMQ92316.1}; GN ORFNames=RF55_7715 {ECO:0000313|EMBL:KMQ92316.1}; OS Lasius niger (Black garden ant). OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; OC Pterygota; Neoptera; Holometabola; Hymenoptera; Apocrita; Aculeata; OC Vespoidea; Formicidae; Formicinae; Lasius; Lasius. OX NCBI_TaxID=67767 {ECO:0000313|EMBL:KMQ92316.1, ECO:0000313|Proteomes:UP000036403}; RN [1] {ECO:0000313|EMBL:KMQ92316.1, ECO:0000313|Proteomes:UP000036403} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC TISSUE=Whole {ECO:0000313|EMBL:KMQ92316.1}; RA Konorov E.A., Nikitin M.A., Kirill M.V., Chang P.; RT "Lasius niger genome sequencing."; RL Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KMQ92316.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LBMM01004533; KMQ92316.1; -; Genomic_DNA. DR Proteomes; UP000036403; Unassembled WGS sequence. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR CDD; cd01878; HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000036403}; KW Reference proteome {ECO:0000313|Proteomes:UP000036403}. FT DOMAIN 245 405 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 463 AA; 52253 MW; 0938905E5930CA05 CRC64; MCNKVNTICK RSGIMLQNIV CRFNHDSEEY VSADEKDQEA YAEISNHYLG VAVEGHRTFV LQPYVKWGKD KKRNTSPELQ MAEAVTLINT LSNWCVVGAK YAPLLSLQKK HLLGTGAMEN LKKELNNCEN PTAIFVSTNL LKFIQIVELE KILGLPVYDR YSIIIHIFRQ HAKSAEAKLQ VALAEVPYIR QKVFETCMTH NGVINITEKT KLMFNTREKK LKNELKKLKQ HRTIIRSQRK KHGFPTVAVV GYTNSGKTSL IKALTDDKSL QPKNKLFATL DTTAHEGVLP STLKVLYMDT IGFIQDVPET LIEPFVVTLE DAMIADVIIH IYDVSHPDIK AQYQHVQKTI KPMIDEAHPI INVANKCDLV QSDCIPKDAI AVSATNLTGI DLLRLEIEKV LLAVTGLLRT RIRVESGSPA VSWLYKMTTV TNAQSDPNDA QYLILEVLAT SVDIQKFKKF LRQ // ID A0A0J7L0P6_LASNI Unreviewed; 441 AA. AC A0A0J7L0P6; DT 14-OCT-2015, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 1. DT 10-MAY-2017, entry version 7. DE SubName: Full=Gtp-binding gtpase hsr1 {ECO:0000313|EMBL:KMQ96196.1}; GN ORFNames=RF55_3532 {ECO:0000313|EMBL:KMQ96196.1}; OS Lasius niger (Black garden ant). OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; OC Pterygota; Neoptera; Holometabola; Hymenoptera; Apocrita; Aculeata; OC Vespoidea; Formicidae; Formicinae; Lasius; Lasius. OX NCBI_TaxID=67767 {ECO:0000313|EMBL:KMQ96196.1, ECO:0000313|Proteomes:UP000036403}; RN [1] {ECO:0000313|EMBL:KMQ96196.1, ECO:0000313|Proteomes:UP000036403} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC TISSUE=Whole {ECO:0000313|EMBL:KMQ96196.1}; RA Konorov E.A., Nikitin M.A., Kirill M.V., Chang P.; RT "Lasius niger genome sequencing."; RL Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KMQ96196.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LBMM01001500; KMQ96196.1; -; Genomic_DNA. DR Proteomes; UP000036403; Unassembled WGS sequence. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000036403}; KW Reference proteome {ECO:0000313|Proteomes:UP000036403}. FT DOMAIN 215 387 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 441 AA; 49173 MW; 8235176DDA809908 CRC64; MHLENQTGTI PLELEEEKDP QNVLVILPWG HGPVASSRAQ ARLEEAAGLA EAINLNIVWK GIFPLRAPRP ATLMGKGQVE ELREITHASG AGLVVVDHAL TPIQQRNLEK ALNVKVIDRT GLILDIFGAR AATKEGVLQV ELAHLEYQRS RLVRLWTHLE RQRGGFGFLG GPGETQMEAD RRMIGTRIIK IKKELEQVRR TRGLHRQSRE RVPFPVVALV GYTNAGKSTL FNRLTGADVT AKDQLFATLD PSMRALELPS GRKVILSDTV GFISDLPTEL VEAFRATLEE VAFADVILHV RDVSAPDTNA QKKDVIGVLE KLEEDEFLDK NWEHRLIEVK NKCDLLPESE TQEEKETLGE DERISALTGQ GCDRLLAKLD AVLTADFVEQ EFILNPEEGA KWAWLNENGE ILEKEISDEG ISTLLVKISP PLLEKFHSKF G // ID A0A0J7Y2L3_9SPHN Unreviewed; 449 AA. AC A0A0J7Y2L3; DT 14-OCT-2015, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 1. DT 07-JUN-2017, entry version 15. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=V473_07725 {ECO:0000313|EMBL:KMS58039.1}; OS Sphingobium czechense LL01. OC Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales; OC Sphingomonadaceae; Sphingobium. OX NCBI_TaxID=1420583 {ECO:0000313|EMBL:KMS58039.1, ECO:0000313|Proteomes:UP000052232}; RN [1] {ECO:0000313|EMBL:KMS58039.1, ECO:0000313|Proteomes:UP000052232} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=LL01 {ECO:0000313|EMBL:KMS58039.1, RC ECO:0000313|Proteomes:UP000052232}; RX PubMed=25850427; DOI=10.1534/g3.114.015933; RA Pearce S.L., Oakeshott J.G., Pandey G.; RT "Insights into Ongoing Evolution of the Hexachlorocyclohexane RT Catabolic Pathway from Comparative Genomics of Ten Sphingomonadaceae RT Strains."; RL G3 (Bethesda) 5:1081-1094(2015). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KMS58039.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JACT01000001; KMS58039.1; -; Genomic_DNA. DR RefSeq; WP_066602104.1; NZ_KQ130434.1. DR EnsemblBacteria; KMS58039; KMS58039; V473_07725. DR PATRIC; fig|1420583.3.peg.1555; -. DR Proteomes; UP000052232; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0016810; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds; IEA:InterPro. DR CDD; cd01878; HflX; 1. DR Gene3D; 2.30.40.10; -; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR011059; Metal-dep_hydrolase_composite. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000052232}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000052232}. FT DOMAIN 214 395 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 449 AA; 49074 MW; 3AEB19BACE13F594 CRC64; MAIFNRDSDD EVARGARAIV VHAETHNGAN SSIDRRDSDA RLEEARGLAL AIGIDVRASQ AFRVRDPKPA TLFGSGQVDQ IATLARQEEA DLIIVDNSLS PVQQSNLEKA CEAKVIDRTG LILEIFGERA ATNEGRLQVE LAHLDYQAGR LVRSWTHLER QRGGFGFLGG PGETQIEADR RMIRDRMAKI RKELDQVTRT RGLHRARRQR APWPVIALVG YTNAGKSTLF NRMTGADVMA EDLLFATLDP TMRQIALPGL DKAILSDTVG FVSDLPTQLI AAFRATLEEV LSADLIVHVR DIAHPDSDAQ RDDVLDVLGE LGVAGEAALD RGVGDPDAPP ILEAWNKLDL LSEENAALAR ETASRRDDVV ILSALTGQGV DMLQRTISDC MTRGAKVYGL RVPVSDGATV AWLHEHGEVL STIVEDEESR VDVRLSDAAF ARYAKRSEG // ID A0A0J7ZKW9_STRVR Unreviewed; 497 AA. AC A0A0J7ZKW9; DT 14-OCT-2015, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 1. DT 07-JUN-2017, entry version 14. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=ACM01_07565 {ECO:0000313|EMBL:KMS76067.1}; OS Streptomyces viridochromogenes. OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae; OC Streptomyces. OX NCBI_TaxID=1938 {ECO:0000313|EMBL:KMS76067.1, ECO:0000313|Proteomes:UP000037432}; RN [1] {ECO:0000313|EMBL:KMS76067.1, ECO:0000313|Proteomes:UP000037432} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NRRL 3414 {ECO:0000313|EMBL:KMS76067.1, RC ECO:0000313|Proteomes:UP000037432}; RA Ju K.-S., Doroghazi J.R., Metcalf W.W.; RL Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KMS76067.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LFNT01000005; KMS76067.1; -; Genomic_DNA. DR RefSeq; WP_048580303.1; NZ_LGUR01000230.1. DR EnsemblBacteria; KMS76067; KMS76067; ACM01_07565. DR PATRIC; fig|1938.3.peg.663; -. DR Proteomes; UP000037432; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 2. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000313|EMBL:KMS76067.1}; KW Complete proteome {ECO:0000313|Proteomes:UP000037432}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900, KW ECO:0000313|EMBL:KMS76067.1}. FT DOMAIN 275 440 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 497 AA; 54261 MW; 5535280FDE74EA0F CRC64; MTSSSSPSQD TQRFAHTYPE GLRADALMEE DVAWSHEIDG ERDGDQFDRS ERAALRRVAG LSTELEDVTE VEYRQLRLER VVLVGVWTSG TAQDADNSLA ELAALAETAG ALVLDGVIQR RDKPDAATYI GSGKAGELRD IVLETGADTV ICDGELSPGQ LIHLEDVVKV KVIDRTALIL DIFAQHAKSR EGKAQVALAQ MQYMLPRLRG WGQSLSRQMG GGKGGGLATR GPGETKIETD RRRIREKMAK MRREIAEMKT GRDIQRQVRR RNKVPSVAIA GYTNAGKSSL LNRLTGAGVL VENALFATLD PTVRRAETPS GRLYTLADTV GFVRHLPHHL VEAFRSTMEE VGASDLILHV VDGSHPNPEE QLAAVREVIR DVGATDVPEI VVINKADAAD PLTLQRLMRI EKRSIAVSAR TGQGIDELLA LIDNELPRPS VEIEALVPYT HGKLVARAHT EGEVISEEHT PEGTLLKVRV HEELAADLAP YVPAPTV // ID A0A0J8C8G1_BETVU Unreviewed; 560 AA. AC A0A0J8C8G1; DT 14-OCT-2015, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 1. DT 10-MAY-2017, entry version 13. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:KMT09887.1}; GN ORFNames=BVRB_6g128610 {ECO:0000313|EMBL:KMT09887.1}; OS Beta vulgaris subsp. vulgaris. OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae; OC Pentapetalae; Caryophyllales; Chenopodiaceae; Betoideae; Beta. OX NCBI_TaxID=3555 {ECO:0000313|EMBL:KMT09887.1, ECO:0000313|Proteomes:UP000035740}; RN [1] {ECO:0000313|EMBL:KMT09887.1, ECO:0000313|Proteomes:UP000035740} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC TISSUE=Taproot {ECO:0000313|EMBL:KMT09887.1}; RX PubMed=24352233; DOI=10.1038/nature12817; RA Dohm J.C., Minoche A.E., Holtgrawe D., Capella-Gutierrez S., RA Zakrzewski F., Tafer H., Rupp O., Sorensen T.R., Stracke R., RA Reinhardt R., Goesmann A., Kraft T., Schulz B., Stadler P.F., RA Schmidt T., Gabaldon T., Lehrach H., Weisshaar B., Himmelbauer H.; RT "The genome of the recently domesticated crop plant sugar beet (Beta RT vulgaris)."; RL Nature 505:546-549(2014). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; KQ090109; KMT09887.1; -; Genomic_DNA. DR EnsemblPlants; KMT09887; KMT09887; BVRB_6g128610. DR Gramene; KMT09887; KMT09887; BVRB_6g128610. DR Proteomes; UP000035740; Chromosome 6. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR CDD; cd01878; HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 2. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000035740}; KW Reference proteome {ECO:0000313|Proteomes:UP000035740}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1 26 {ECO:0000256|SAM:SignalP}. FT CHAIN 27 560 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5005295411. FT DOMAIN 291 416 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 560 AA; 62594 MW; 61839E489650518C CRC64; MNNSKLALRG FSLSLLQLRS LHLLQSHCCF SHTPSLRRNS NEDDPNLDPQ GPPKILVVQP RVRPNTHLQT KLNEALNLAN SLDEQRDGFF STDLSLKNSP PHLVVQNPLS GSNKSRSDTY FGPGTVDNIK CHIHAIESKH DDELDAVFVN AILSAIQQRN LERVWEKPVL DRVGLIIEIF NAHAYTKEAK LQAELAAIMY KKSRLVRARG SDGRYTFGTK GEAEVVSARG RGSGGRGFIS GAGETELELQ RRRISERRKR LLAEIEVVRR TRAVQRAGRR KQGVLDAPGL ASVAVVGYTN AGKSTLVSAL SDTDLYSDDR LFATVDPKVR GVTLPSGRKV LLSDTVGFIS DLPVQLVEAF HATLEEVVEA DLLVHVLDSS APNLEEQRQA VLDVLQRIGV SGKKIQDMIE VWNKIDIQRD TDTGVENFND DFDSKFEEDE DEVTDEQLLQ KDKMQEDQRS EFSSDRLGPG VEPHDQKGEF FIVSRMKEKG PDSHPESEHV PHVKTSAVAR IGLQELLGLI DEKLVQNDKE QQSSQIVLER GKLDRKWRPP QAEKIEISVE // ID A0A0J8FYK0_BETVU Unreviewed; 543 AA. AC A0A0J8FYK0; DT 14-OCT-2015, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 1. DT 30-AUG-2017, entry version 13. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:KMT20701.1}; GN ORFNames=BVRB_1g006760 {ECO:0000313|EMBL:KMT20701.1}; OS Beta vulgaris subsp. vulgaris. OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae; OC Pentapetalae; Caryophyllales; Chenopodiaceae; Betoideae; Beta. OX NCBI_TaxID=3555 {ECO:0000313|EMBL:KMT20701.1, ECO:0000313|Proteomes:UP000035740}; RN [1] {ECO:0000313|EMBL:KMT20701.1, ECO:0000313|Proteomes:UP000035740} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC TISSUE=Taproot {ECO:0000313|EMBL:KMT20701.1}; RX PubMed=24352233; DOI=10.1038/nature12817; RA Dohm J.C., Minoche A.E., Holtgrawe D., Capella-Gutierrez S., RA Zakrzewski F., Tafer H., Rupp O., Sorensen T.R., Stracke R., RA Reinhardt R., Goesmann A., Kraft T., Schulz B., Stadler P.F., RA Schmidt T., Gabaldon T., Lehrach H., Weisshaar B., Himmelbauer H.; RT "The genome of the recently domesticated crop plant sugar beet (Beta RT vulgaris)."; RL Nature 505:546-549(2014). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; KQ090029; KMT20701.1; -; Genomic_DNA. DR RefSeq; XP_010672784.1; XM_010674482.2. DR EnsemblPlants; KMT20701; KMT20701; BVRB_1g006760. DR GeneID; 104889285; -. DR Gramene; KMT20701; KMT20701; BVRB_1g006760. DR KEGG; bvg:104889285; -. DR KO; K03665; -. DR Proteomes; UP000035740; Chromosome 1. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000035740}; KW Reference proteome {ECO:0000313|Proteomes:UP000035740}. FT DOMAIN 321 487 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 543 AA; 60970 MW; 4E655BED75818348 CRC64; MSSTNFCWLI SSKKSSSLSS FRRSQSSPFQ TCPSNSTTWV KTHQHKKPKN CIIVKSLQVH GVDEFLSPLP LPTIEPETVE IEQELSDFEE EIEDPVSISS RERQEEEEEE EDRRFKLRNG KEVLAERAYL VGVEQKGVKV NSFGIEESLK ELEQLADTAG LQLVGSTYQK LAAPNPRTYI GSGKVSEIKS AIHALDVETV LFDDELSPGQ LRNLEKIFGG DVRVCDRTAL ILDIFNQRAA THEAALQVAL AQMEYQLPRL TKMWNHLERQ AGGKVKGMGE KQIEVDKRIL RDQIGVLKKE LESVRRHRKL YRNRRVSVPI PVVSLVGYTN AGKSTLLNQL TGANVLAEDR LFATLDPTTR RVQMKNGKEF LLTDTVGFIQ KLPTMLVAAF RATLEEIAES SLLVHVVDIS HPLAEQQIDA VDEVLSELDV SSIPILMVWN KVDKVSDPEK IKAEAERRGD VVCLSALSGD GLDDFCKAIR EKLKDSMVWI EALVPFDKGE LLSSIHQLGM VERTDYTENG TLIKAFVPLR LARLLTPMRQ LCV // ID A0A0J8V712_9GAMM Unreviewed; 429 AA. AC A0A0J8V712; DT 14-OCT-2015, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 1. DT 30-AUG-2017, entry version 14. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=AB733_19875 {ECO:0000313|EMBL:KMV29041.1}; OS Photobacterium swingsii. OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; OC Vibrionaceae; Photobacterium. OX NCBI_TaxID=680026 {ECO:0000313|EMBL:KMV29041.1, ECO:0000313|Proteomes:UP000037287}; RN [1] {ECO:0000313|EMBL:KMV29041.1, ECO:0000313|Proteomes:UP000037287} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CAIM 1393 {ECO:0000313|EMBL:KMV29041.1, RC ECO:0000313|Proteomes:UP000037287}; RX PubMed=20228205; DOI=10.1099/ijs.0.019687-0; RA Gomez-Gil B., Roque A., Rotllant G., Peinado L., Romalde J.L., RA Doce A., Cabanillas-Beltran H., Chimetto L.A., Thompson F.L.; RT "Photobacterium swingsii sp. nov., isolated from marine organisms."; RL Int. J. Syst. Evol. Microbiol. 61:315-319(2011). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KMV29041.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LELC01000025; KMV29041.1; -; Genomic_DNA. DR RefSeq; WP_048900350.1; NZ_LELC01000025.1. DR EnsemblBacteria; KMV29041; KMV29041; AB733_19875. DR PATRIC; fig|680026.4.peg.4682; -. DR Proteomes; UP000037287; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000037287}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}. FT DOMAIN 198 365 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 429 AA; 48419 MW; CC2A0C8DD3BF29CB CRC64; MFDRYEAGEQ AILVHINFTQ EGEWEDLSEC EMLVSSAGVN TLRVVTGSRK TPHPKYYVGE GKAQEIADAV RMEGAEIVIF NHALSPAQER NLEYLCKCRV LDRTGLILDI FAQRARTHEG KLQVELAQLR HISTRLIRGW THLERQKGGI GLRGPGETQL ETDRRLLRDR IKAILRRLEK VSKQRDQGRR ARNRAEIPTI SLVGYTNAGK STLFNRITDA GVYAADQLFA TLDPTLRKIE VADVGTSILA DTVGFIRHLP HDLVAAFKAT LKETQEASLL LHVVDASDDR FRENIEAVDD VLEEIDAGEV PMLIVMNKID NLEGAEPRIE RDDEGVPRRV WVSAMEGIGI DLLFQALTER LAGTMICHTL RLPPQHIGRI RSKFCQLDCI LREEYEPDGS LTIDIRLPQA DWSRLEKRDS ASLDDFVVS // ID A0A0J8YG19_9BACT Unreviewed; 426 AA. AC A0A0J8YG19; DT 14-OCT-2015, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 1. DT 30-AUG-2017, entry version 15. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=AI28_00385 {ECO:0000313|EMBL:KMV68786.1}; OS bacteria symbiont BFo1 of Frankliniella occidentalis. OC Bacteria. OX NCBI_TaxID=1628855 {ECO:0000313|EMBL:KMV68786.1, ECO:0000313|Proteomes:UP000037152}; RN [1] {ECO:0000313|EMBL:KMV68786.1, ECO:0000313|Proteomes:UP000037152} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BFo1 {ECO:0000313|EMBL:KMV68786.1, RC ECO:0000313|Proteomes:UP000037152}; RA Facey P.D., Hitchings M.D., Hegarty M.J., Pachebat J.A., Morgan L.V., RA Hoeppner J.E., Whitten M.A., Dyson P.J., Del Sol R.; RT "The draft genomes, genome evolution and classification of BFo1 and RT BFo2 two insect symbionts isolated from Western Flower Thrips RT (Frankliniella occidentalis [Pergande])."; RL Submitted (MAY-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KMV68786.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JMSO01000196; KMV68786.1; -; Genomic_DNA. DR EnsemblBacteria; KMV68786; KMV68786; AI28_00385. DR PATRIC; fig|1628855.3.peg.79; -. DR Proteomes; UP000037152; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000037152}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000037152}. FT DOMAIN 198 365 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 426 AA; 48036 MW; C5376FA6EB5C2414 CRC64; MFDRYDAGEQ AVLVHIYFSQ DRDTEDLQEF ETLVSSAGVE ALRVVTGSRK APHPKYFVGE GKAVEIAEAV KESGATVVLF DHALSPAQER NLEALCECRV IDRTGLILDI FAQRARTHEG KLQVELAQLR HLATRLVRGW THLERQKGGI GLRGPGETQL ETDRRLLRNR ITLILSRLER VSKQREQGRQ ARNKADVPTV SLVGYTNAGK STLFNRLTTS EVYVADQLFA TLDPTLRRVD VVDVGEVVLA DTVGFIRHLP HDLVAAFKAT LQETREAALL LHVIDATDVR VDENIEAVNE VLEEIESDEI PSLLVMNKID MLDGFVPRID RDEENLPIRV WLSAQSGEGI PLLFQALTER LAGEIAQYDL RLPPAAGRLR SRFYQLQAIE KEWNEEDGSV GLHVRMPIVD WRRLCKQEPT LVDYIV // ID A0A0J8YNC0_9BACT Unreviewed; 427 AA. AC A0A0J8YNC0; DT 14-OCT-2015, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 1. DT 30-AUG-2017, entry version 14. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=AI29_11615 {ECO:0000313|EMBL:KMV71331.1}; OS bacteria symbiont BFo2 of Frankliniella occidentalis. OC Bacteria. OX NCBI_TaxID=1628856 {ECO:0000313|EMBL:KMV71331.1, ECO:0000313|Proteomes:UP000036794}; RN [1] {ECO:0000313|EMBL:KMV71331.1, ECO:0000313|Proteomes:UP000036794} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BFo2 {ECO:0000313|EMBL:KMV71331.1, RC ECO:0000313|Proteomes:UP000036794}; RA Facey P.D., Hitchings M.D., Hegarty M.J., Pachebat J.A., Morgan L.V., RA Hoeppner J.E., Whitten M.A., Dyson P.J., Del Sol R.; RT "The draft genomes, genome evolution and classification of BFo1 and RT BFo2 two insect symbionts isolated from Western Flower Thrips RT (Frankliniella occidentalis [Pergande])."; RL Submitted (MAY-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KMV71331.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JMSP01000291; KMV71331.1; -; Genomic_DNA. DR EnsemblBacteria; KMV71331; KMV71331; AI29_11615. DR PATRIC; fig|1628856.3.peg.2337; -. DR Proteomes; UP000036794; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000036794}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000036794}. FT DOMAIN 198 365 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 427 AA; 47864 MW; 3DC25ACFBA642E49 CRC64; MFERYDAGEQ AVLVHIWFAQ DKESEDLQEF ETLVSSAGVE ALQVVTGSRK SPHPKYFVGE GKAEEIADAV KATGASVVIF DHALSPAQER NLERLCECRV IDRTGLILDI FAQRARTHEG KLQVELAQLR HLATRLVRGW THLERQKGGI GLRGPGETQL ETDRRLLRNR ITLILSRLQR VEKQREQGRQ ARAKADIPTV SLVGYTNAGK STLFNSITSA EVYAADQLFA TLDPTLRRLS VTDVGEVVLA DTVGFIRHLP HDLVAAFKAT LQETREATLL LHVIDAADLR VNENIEAVDD VLAEIEADEI PALHVMNKID QLEGFVPRID RNEEGVPIRV WLSAQSGLGL PLLWQALSER LSGEIAQHTL TLPPEAGRLR SRFYQLDAIK EEWNQDDGSI GLQVRLPIVE WHRLNKQYPA LSDYVVK // ID A0A0J9GUU6_9RHOB Unreviewed; 431 AA. AC A0A0J9GUU6; DT 14-OCT-2015, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 1. DT 07-JUN-2017, entry version 12. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=AIOL_002316 {ECO:0000313|EMBL:KMW57353.1}; OS Candidatus Rhodobacter lobularis. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae; Rhodobacter. OX NCBI_TaxID=1675527 {ECO:0000313|EMBL:KMW57353.1, ECO:0000313|Proteomes:UP000037178}; RN [1] {ECO:0000313|EMBL:KMW57353.1, ECO:0000313|Proteomes:UP000037178} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=IGS {ECO:0000313|EMBL:KMW57353.1}; RA Jourda C., Santini S., Claverie J.-M.; RT "Draft genome sequence of an Alphaproteobacteria species associated to RT the Mediterranean sponge Oscarella lobularis."; RL Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KMW57353.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LFTY01000002; KMW57353.1; -; Genomic_DNA. DR EnsemblBacteria; KMW57353; KMW57353; AIOL_002316. DR PATRIC; fig|1675527.3.peg.2430; -. DR Proteomes; UP000037178; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000037178}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000037178}. FT DOMAIN 204 373 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 431 AA; 47187 MW; 5D90EFE616FAD139 CRC64; MREIEVADTC AWVLHPEIQN APRSRAAETA LEEAVALAVA LPGLAVAGAE VVRISKPHPG QLFGSGKVAE LAERLHDAEV ELVLIDGPLS PVQQRNLEKA WKVKILDRTG LILEIFSDRA RTREGVLQVE MAALSYQRTR LVRAWTHLER QRGGLGFVGG PGETQIEADR RAIDDQLGRL RRQLEKVVRT RTLHRAARKK VPFPIVALVG YTNAGKSTLF NRMTGAKVMA KDMLFATLDP TMRRVTLATG REVILSDTVG FISDLPTQLV AAFRATLEEV LEADLILHVR DIADAETEAQ AEDVASIMGD LGVNEDVKQL EVWNKLDLLE GEARETVETQ AGRRDDVLVT SALTGQGLDA LTEAIEAALA EKSFDEALEL PFSAGRARAW LHDQGVVLSE ETGDTGFRLE LRWSGAQRDK FHAGPGADLS P // ID A0A0K0EHH4_STRER Unreviewed; 1019 AA. AC A0A0K0EHH4; DT 14-OCT-2015, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 1. DT 12-APR-2017, entry version 6. DE SubName: Full=Uncharacterized protein {ECO:0000313|WBParaSite:SSTP_0000892900.1}; OS Strongyloides stercoralis (Threadworm). OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida; OC Panagrolaimoidea; Strongyloididae; Strongyloides. OX NCBI_TaxID=6248 {ECO:0000313|Proteomes:UP000035681, ECO:0000313|WBParaSite:SSTP_0000892900.1}; RN [1] {ECO:0000313|Proteomes:UP000035681, ECO:0000313|WBParaSite:SSTP_0000892900.1} RP NUCLEOTIDE SEQUENCE. RA Martin A.A.; RL Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|WBParaSite:SSTP_0000892900.1} RP IDENTIFICATION. RG WormBaseParasite; RL Submitted (AUG-2015) to UniProtKB. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR WBParaSite; SSTP_0000892900.1; SSTP_0000892900.1; SSTP_0000892900. DR Proteomes; UP000035681; Unassembled WGS sequence. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR006594; LisH. DR InterPro; IPR027417; P-loop_NTPase. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR PROSITE; PS51705; G_HFLX; 1. DR PROSITE; PS50896; LISH; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000035681}; KW Reference proteome {ECO:0000313|Proteomes:UP000035681}. FT DOMAIN 14 46 LisH. {ECO:0000259|PROSITE:PS50896}. FT DOMAIN 785 957 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 1019 AA; 114947 MW; CD90AD69C472FFEF CRC64; MAVPYLNREY EKNIRNEVES LFADYLSRHK FAKTLEVFLQ ESGYRKQNFS QMSGRPFVQN SHSTIEDIIM NANFRENANK KYLFSTCKSF ADAIAENSFR LINLICENSL YANNKNDFKS HERYPHSFMN EGNLNNNRAF VCSQASTHNT DLTHNNSCSM SYETSYTPSR YGLNTCSANT LPSNINTITP YQHVGSSFLC RTGNFSINSG ELNGFHPMDG HCLESPCSRA NVNCDRSMDH NGCFVPNNSS TPRVIESDLN GKKGTNVLFQ NGSLTAQNYY VNTTKVIHSN EDHINSTQYN EHLHRDNKDI LSDSGLPNFS NHSSNIPNIV HSSGNVEGRE KKTRVNSSSK STPKGKAIKE GGKKLQKFDS GSVCRSGVLD FQTTLSPTQF RKAAKDVDLE KEPHLAKQYL PDDSQNEKPF GPDNFLNASK FKNENVRPTN SIEENSLPQT GGISNSSSLN VPGFGRKSLD RDKSASSIND VFKSPTQINS SKNYGNSKKS SSLTNKDDSK ISSSQDQSNV SSDNLEGGFD DLTNIDDCFT PYELCQDNSL EYNSDCGFDL DTFYDPGRDL ELFDEIGRII HPKIRWGQYA TPPNEKNDEL QLSEAISLVK TIPGFSVSQS VIVGTDYTTK KKQIWGQGRI DSLLQLKSTC RVSAIMINVE YLTPLQQSEL YNIFQVPIYD RYNIVLKIFK IYAKTKLAYY QIQLAEIPYI KHRLHYLENN SCNSDILHVT DAINALSKSG LNQKETLRFR EQTLRKKIKH CIEMSKNEII EKKLRQNKKS ANNSLTIAII GYTNVGKTTF IKKITGSSQL NPEDKLFATL DTTIHPFSLP SKNNVFVADT IGFMGSLPIG LFESFSATLM HATSADLLVH LYDLSHPDVF SQKKNVIKSL IDLQFPEKLL NNMINVGNKL DKISNDDKCK LIENGIIDKN DLVISCTTGY GIDELISKID KTIMNMNNSR VRRFKLKPES KIISYFYENR LVTKEPVVSE CGKYLIFDVY LSDSQLNKLA KKTNFKIKQ // ID A0A0K0FN70_9BILA Unreviewed; 495 AA. AC A0A0K0FN70; DT 14-OCT-2015, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 1. DT 30-AUG-2017, entry version 7. DE SubName: Full=Putative GTP-binding protein 6 (inferred by orthology to a human protein) {ECO:0000313|WBParaSite:SVE_1045000.1}; OS Strongyloides venezuelensis. OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida; OC Panagrolaimoidea; Strongyloididae; Strongyloides. OX NCBI_TaxID=75913 {ECO:0000313|Proteomes:UP000035680, ECO:0000313|WBParaSite:SVE_1045000.1}; RN [1] {ECO:0000313|Proteomes:UP000035680, ECO:0000313|WBParaSite:SVE_1045000.1} RP NUCLEOTIDE SEQUENCE. RA Martin A.A, De Silva N.; RL Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|WBParaSite:SVE_1045000.1} RP IDENTIFICATION. RG WormBaseParasite; RL Submitted (AUG-2015) to UniProtKB. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR WBParaSite; SVE_1045000.1; SVE_1045000.1; SVE_1045000. DR Proteomes; UP000035680; Unassembled WGS sequence. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000035680}; KW Reference proteome {ECO:0000313|Proteomes:UP000035680}. FT DOMAIN 260 432 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 495 AA; 56452 MW; 34D97E540044CF88 CRC64; MLRFVSLLPS KTFRRSLFYC RNFCSIIKEE EGSLLSDIDL NMPSVSYVQH SFLVVHPKIR WGRNATPPKE KNDELQVEEA IALVKTIPGF SVSQSVIVGT DYTTKKKHIW GQGRIEDLLK LKVSSRVSAL MINVDQITPL QQTELYSIFR VPIYDRYNIV LKIFKLFAKT KLAYYQIQLA EIPYIRNRLH YLDNNDTNCD VLQITDAVNA LAKSGLDRKE ALRLREHALR KRIKSSIESA KNEVAERKLR QDKKNAGNSL VIAIIGYTNV GKTTFIKRIT GASQLNPEDK LFATLDTTIH PFSLPSRNNV FIADTIGFMA SLPVGLFESF SATLMHATSA DLLIHLIDLS HPDVLAQKKN VLKTLIDLKF PQKLIDNMIC VGNKLDKISD YDKHKLIESE VLNKNDSVIS STSGYGINEL ILKIDKTIMN INNSRIRRFK LKPESKLISY FYENNLVTTE PVVSECGEYL IFDICLNDGQ LNKLKKKMNF MIKQQ // ID A0A0K0G8V4_9FIRM Unreviewed; 408 AA. AC A0A0K0G8V4; DT 14-OCT-2015, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 1. DT 07-JUN-2017, entry version 12. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=WH51_13205 {ECO:0000313|EMBL:KKE78441.1}; OS Bacilli bacterium VT-13-104. OC Bacteria; Firmicutes; Bacilli. OX NCBI_TaxID=1637974 {ECO:0000313|EMBL:KKE78441.1, ECO:0000313|Proteomes:UP000034981}; RN [1] {ECO:0000313|EMBL:KKE78441.1, ECO:0000313|Proteomes:UP000034981} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=VT-13-104 {ECO:0000313|EMBL:KKE78441.1, RC ECO:0000313|Proteomes:UP000034981}; RA Tetz V., Tetz G.; RT "Bacilli bacterium VT-13-104."; RL Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KKE78441.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LAZH01000051; KKE78441.1; -; Genomic_DNA. DR RefSeq; WP_047186117.1; NZ_LAZH01000051.1. DR EnsemblBacteria; KKE78441; KKE78441; WH51_13205. DR PATRIC; fig|1637974.4.peg.2784; -. DR Proteomes; UP000034981; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000034981}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000034981}. FT DOMAIN 196 320 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 408 AA; 46684 MW; 0F80BEB882EC3907 CRC64; MPEEKILIIA VKKPTQKDEQ FQSSLEELIS LGRTAGGNVV ETITQNRNRI HPATYIGEGK MEEIKQEVEK LDIDLVISND ELSPGQLRNL SNFLGVRIID RSQLILDIFA RRAKTKEGKL QVELAQLEYM LPRLAGHGVE MSRLGAGIGT RGPGETKLET DRRHIRNRIV DIKRKLKIVV RQREQYRKRR KTNEAFQIAI VGYTNAGKST IFNRLTKSDS LEEDKLFATL DPLTRKINFP SGFEALVTDT VGFLQDLPTA LIAAFRSTLE EVKEADFLIH VVDASQENQE EQQRTVMKLL AELDSHTIPM LTVYNKKDLL QTEFFPIHHP NILISAYNHE ELNQMLAQIE KIVMEQWKSY SIQINDGNML AKLERDTIIT AKQFDEQSNK FNVSGYIRAN HPLNHLMN // ID A0A0K0TUT3_9RHIZ Unreviewed; 437 AA. AC A0A0K0TUT3; DT 11-NOV-2015, integrated into UniProtKB/TrEMBL. DT 11-NOV-2015, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=HflX {ECO:0000313|EMBL:AKR55492.1}; GN Synonyms=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=XM25_06665 {ECO:0000313|EMBL:AKR55492.1}; OS Devosia sp. H5989. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Hyphomicrobiaceae; Devosia. OX NCBI_TaxID=1643450 {ECO:0000313|EMBL:AKR55492.1, ECO:0000313|Proteomes:UP000037066}; RN [1] {ECO:0000313|EMBL:AKR55492.1, ECO:0000313|Proteomes:UP000037066} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=H5989 {ECO:0000313|EMBL:AKR55492.1, RC ECO:0000313|Proteomes:UP000037066}; RX PubMed=26337876; RA Nicholson A.C., Whitney A.M., Humrighouse B., Emery B., Loparev V., RA McQuiston J.R.; RT "Complete Genome Sequence of Strain H5989 of a Novel Devosia RT Species."; RL Genome 3:e00934-15(2015). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP011300; AKR55492.1; -; Genomic_DNA. DR EnsemblBacteria; AKR55492; AKR55492; XM25_06665. DR KEGG; deq:XM25_06665; -. DR PATRIC; fig|1643450.3.peg.1354; -. DR KO; K03665; -. DR Proteomes; UP000037066; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000037066}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000037066}. FT DOMAIN 202 377 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 161 195 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 437 AA; 48457 MW; 9F07C061DD465CF2 CRC64; MDQREAPTRV GLIVPDVRGA SVYHSIEARK AEFEGLAAAI RLEIVFSEVI RVREVRPATF IGGGQVEAIA RRVQEEDIEL LLVDTALTPI QQRNLERETK AKVLDRTALI LEIFGERAAT REGVLQVELA HLNYQKSRLV RSWTHLERQR GGFGFLGGPG ETQIESDRRL LQERIALLEE RIEKVRKTRQ QQRRNRDEVP YPIVALVGYT NAGKSSLFNT LTGAGVFAEN LLFATLDTTV RKLELPHGRQ VIVSDTVGFV ADLPHDLVAA FRATLEEVTQ ADVVLHIRDV ANPDHQAQAR DVLTVLGELG VSSETVPVIE VWNKIDLLPR AEDGSIPALA NTAPVGRVAA TIPVSAKTGE GLEDLKIAIE AALSAGSRTY RVHVPHAAGG DVGWLYGHAE IIERIEPDEK GQDFVVRVEP RHLREFQERF NGRIEGE // ID A0A0K0XVN1_9GAMM Unreviewed; 361 AA. AC A0A0K0XVN1; DT 11-NOV-2015, integrated into UniProtKB/TrEMBL. DT 11-NOV-2015, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=WM2015_1318 {ECO:0000313|EMBL:AKS41691.1}; OS Wenzhouxiangella marina. OC Bacteria; Proteobacteria; Gammaproteobacteria; Chromatiales; OC Wenzhouxiangellaceae; Wenzhouxiangella. OX NCBI_TaxID=1579979 {ECO:0000313|EMBL:AKS41691.1, ECO:0000313|Proteomes:UP000066624}; RN [1] {ECO:0000313|EMBL:AKS41691.1, ECO:0000313|Proteomes:UP000066624} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=KCTC 42284 {ECO:0000313|EMBL:AKS41691.1, RC ECO:0000313|Proteomes:UP000066624}; RA Noorani M.; RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP012154; AKS41691.1; -; Genomic_DNA. DR EnsemblBacteria; AKS41691; AKS41691; WM2015_1318. DR KEGG; wma:WM2015_1318; -. DR PATRIC; fig|1579979.3.peg.1352; -. DR KO; K03665; -. DR Proteomes; UP000066624; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000066624}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000066624}. FT DOMAIN 129 295 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 95 122 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 361 AA; 40132 MW; 7088087BA577E619 CRC64; MAELSAELVL VNGRLSPIQE RNLVRRLGVN VLDRTTLILD IFAQRARSHE GKLQVELAQL KHLSTRLVRG WTHLERQRGG IGMRGPGETQ LETDRRLLAN RIRALTARLD KVEQRRAEGR RARERGETPL IALVGYTNAG KSTLFNRLTE SAVMARDQLF ATLDPTVRRI ESLAGSPVLL SDTVGFIRDL PHELVAAFRA TLEETLGASL VVHVIDAADP DRARHQAVVE EVLDDIGAAD LPLLRVYNKA DLTDHAPGLE RDEGGEIRAV WVSAATGEGM DALKRALSER VGEGRIHRWI DLGPDHARLR SRLFALGVVQ QERIDEEGIC HLEVELDRRD ARLLTRLGGA DGKLVEEVLL N // ID A0A0K0Y577_9RHOB Unreviewed; 451 AA. AC A0A0K0Y577; DT 11-NOV-2015, integrated into UniProtKB/TrEMBL. DT 11-NOV-2015, sequence version 1. DT 07-JUN-2017, entry version 13. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:AKS45987.1}; GN ORFNames=OSB_14350 {ECO:0000313|EMBL:AKS45987.1}; OS Octadecabacter temperatus. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae; Octadecabacter. OX NCBI_TaxID=1458307 {ECO:0000313|EMBL:AKS45987.1, ECO:0000313|Proteomes:UP000067444}; RN [1] {ECO:0000313|EMBL:AKS45987.1, ECO:0000313|Proteomes:UP000067444} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SB1 {ECO:0000313|EMBL:AKS45987.1, RC ECO:0000313|Proteomes:UP000067444}; RX PubMed=26358607; RA Voget S., Billerbeck S., Simon M., Daniel R.; RT "Closed Genome Sequence of Octadecabacter temperatus SB1, the First RT Mesophilic Species of the Genus Octadecabacter."; RL Genome Announc. 3:e01051-15(2015). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP012160; AKS45987.1; -; Genomic_DNA. DR RefSeq; WP_049834325.1; NZ_FSRP01000001.1. DR EnsemblBacteria; AKS45987; AKS45987; OSB_14350. DR KEGG; otm:OSB_14350; -. DR PATRIC; fig|1458307.3.peg.1453; -. DR KO; K03665; -. DR Proteomes; UP000067444; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000067444}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000067444}. FT DOMAIN 203 372 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 451 AA; 49953 MW; 254639BD523A5D82 CRC64; MGEERSATRA FVLHPEIKSN QTRRHAASAL EEGMSLARAL PELELVGGQV VSLPKVHAGK LFGKGKIAEI DQWLKDAEAG LVLIDGHVSP VQQRNLEKEW GVKLLDRTGL ILEIFSDRAR TREGVLQVEM AALTYQRTRL VRAWTHLERQ RGGLGFVGGP GETQIEADRR AIDIQLNNLK KQLSKVVKTR ELHRKARAKV PYPIVALVGY TNAGKSTLFN RLTGADVFAK DMLFATLDPT MRRVELPSGE DVIMSDTVGF ISELPTQLVA SFRATLEEVL EADIILHVRD VSHPQSAEQK KAVLDTLRQL DVNPDVPMIE VLNKVDLLSE EDAGYLQALN KDDEGVFAIS AVTGEGLDRL LGTVSEILKG STRTMTLSLD WAQGAAQSWL QREGVIVDDK QTETGWTIDV RWSAIQQAQF EKQFPDAMPT VEADKSDKDE DAPSGEYHPL D // ID A0A0K1F4Q5_9ACTN Unreviewed; 436 AA. AC A0A0K1F4Q5; DT 11-NOV-2015, integrated into UniProtKB/TrEMBL. DT 11-NOV-2015, sequence version 1. DT 07-JUN-2017, entry version 12. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=ADJ70_13195 {ECO:0000313|EMBL:AKT49677.1}; OS Olsenella sp. oral taxon 807. OC Bacteria; Actinobacteria; Coriobacteriia; Coriobacteriales; OC Atopobiaceae; Olsenella. OX NCBI_TaxID=712411 {ECO:0000313|EMBL:AKT49677.1, ECO:0000313|Proteomes:UP000059853}; RN [1] {ECO:0000313|EMBL:AKT49677.1, ECO:0000313|Proteomes:UP000059853} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=F0089 {ECO:0000313|EMBL:AKT49677.1, RC ECO:0000313|Proteomes:UP000059853}; RA Babu N.S., Beckwith C.J., Beseler K.G., Brison A., Carone J.V., RA Caskin T.P., Diamond M., Durham M.E., Foxe J.M., Go M., RA Henderson B.A., Jones I.B., McGettigan J.A., Micheletti S.J., RA Nasrallah M.E., Ortiz D., Piller C.R., Privatt S.R., Schneider S.L., RA Sharp S., Smith T.C., Stanton J.D., Ullery H.E., Wilson R.J., RA Serrano M.G., Buck G., Lee V., Wang Y., Carvalho R., Voegtly L., RA Shi R., Duckworth R., Johnson A., Loviza R., Walstead R., Shah Z., RA Kiflezghi M., Wade K., Ball S.L., Bradley K.W., Asai D.J., RA Bowman C.A., Russell D.A., Pope W.H., Jacobs-Sera D., Hendrix R.W., RA Hatfull G.F.; RL Submitted (AUG-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP012069; AKT49677.1; -; Genomic_DNA. DR RefSeq; WP_050344370.1; NZ_CP012069.2. DR EnsemblBacteria; AKT49677; AKT49677; ADJ70_13195. DR KEGG; olo:ADJ70_13195; -. DR PATRIC; fig|712411.3.peg.1402; -. DR KO; K03665; -. DR Proteomes; UP000059853; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000059853}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000059853}. FT DOMAIN 210 375 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 436 AA; 48113 MW; C600DF67E3CCE91E CRC64; MPKPQPQSTM PEAERAILVG IELGRSEWPL CESLAELGRL AHTAGAEVVS TVTQQLSRPK SRTLIGRGKA EELARLACSL EADVVIFDDE LTPSQQGNLE RIIGRSTKVI DRTALILDIF GRHAKTHEGR LQVQLAQLQY LLPRLKGMWG HLVSEQARGG IGGRFGQGES QLEIDRRLVR DRISSLKREL TELDKHRAVQ SKARWDSGIF RVALVGYTNA GKSMLLNRLT GAGVYVKDEL FATLDPTTRT LELEAGRKIT ITDTVGFIQK LPTTLVESFN STLAEARAAD LILKVVDASD PNREKQLVAV DEVLDRIGAS GIPFVAVYNK CDLLDEASYS ALATSHPDAI LISALEGTGL QGLRYRIAQR AAQDDTTLTA LIPYREGFLQ RVVHERCQIM HEQYLPEGLL VTARVPVRVA AMFKPHLHES EPADPQ // ID A0A0K1FBW3_9MICO Unreviewed; 494 AA. AC A0A0K1FBW3; DT 11-NOV-2015, integrated into UniProtKB/TrEMBL. DT 11-NOV-2015, sequence version 1. DT 07-JUN-2017, entry version 13. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=ADJ73_14515 {ECO:0000313|EMBL:AKT52184.1}; OS Arsenicicoccus sp. oral taxon 190. OC Bacteria; Actinobacteria; Micrococcales; Intrasporangiaceae; OC Arsenicicoccus. OX NCBI_TaxID=1658671 {ECO:0000313|EMBL:AKT52184.1, ECO:0000313|Proteomes:UP000065578}; RN [1] {ECO:0000313|EMBL:AKT52184.1, ECO:0000313|Proteomes:UP000065578} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=F0371 {ECO:0000313|EMBL:AKT52184.1, RC ECO:0000313|Proteomes:UP000065578}; RA Noorani M.; RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP012070; AKT52184.1; -; Genomic_DNA. DR RefSeq; WP_050348848.1; NZ_CP012070.1. DR EnsemblBacteria; AKT52184; AKT52184; ADJ73_14515. DR KEGG; ars:ADJ73_14515; -. DR PATRIC; fig|1658671.3.peg.2954; -. DR KO; K03665; -. DR Proteomes; UP000065578; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 2. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000065578}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000065578}. FT DOMAIN 267 432 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 494 AA; 54006 MW; 7C6F4177005D64CD CRC64; MTSTSHHNLF RSRAEALAEE QDPWLDEGVE AYDGEQLDRE ERAALRRVGG LSTELEDITE VEYRQLRLER VVLAGVWTEG TAEDAENSIR ELAALAETAG STVLDGVIQR RLRPDAGTFL GSGKAEELRE IVQAEGADTV ICDGELTPGQ RRALEDVVKV KVIDRTALIL DIFAQHAKSR EGKAQVELAQ LQYLLPRLRG WGESMSRQAG GQAAGGVGIG SRGPGETKIE LDRRRINTKI AQLKRDIKKM KTSRDAKRSS RRASEVPSVA IAGYTNAGKS SLLNRLTGAG VLVENQLFAT LDPTVRRAET PDGRPYTLAD TVGFVRSLPH QLVEAFRSTL EEVGDSDLLL HVVDGSHPDP EGQISAVRAV MSEIGGDRLR EIIVINKADA ADPEVLLRLR AHEKHAIVVS ARTGAGIDEL RRLIAEELPQ PEIAVEVLLP YDRGDLVSRL HSEADLESEE HTGAGTLVRA MVHPRLAGEL EPYAVTRHRP VRAG // ID A0A0K1J1L5_9RHOO Unreviewed; 386 AA. AC A0A0K1J1L5; DT 11-NOV-2015, integrated into UniProtKB/TrEMBL. DT 11-NOV-2015, sequence version 1. DT 30-AUG-2017, entry version 14. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=AzCIB_0726 {ECO:0000313|EMBL:AKU10631.1}; OS Azoarcus sp. CIB. OC Bacteria; Proteobacteria; Betaproteobacteria; Rhodocyclales; OC Zoogloeaceae; Azoarcus. OX NCBI_TaxID=198107 {ECO:0000313|EMBL:AKU10631.1, ECO:0000313|Proteomes:UP000066621}; RN [1] {ECO:0000313|EMBL:AKU10631.1, ECO:0000313|Proteomes:UP000066621} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CIB {ECO:0000313|EMBL:AKU10631.1, RC ECO:0000313|Proteomes:UP000066621}; RA Martin-Moldes Z., Zamarro M.T., del Cerro C., Valencia A., Gomez M.J., RA Udaondo Z., Garcia J.L., Nogales J., Carmona M., Diaz E.; RT "Whole-genome analysis of Azoarcus sp. strain CIB provides genetic RT insights to its different lifestyles and predicts novel metabolic RT features."; RL Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP011072; AKU10631.1; -; Genomic_DNA. DR RefSeq; WP_050414634.1; NZ_CP011072.1. DR EnsemblBacteria; AKU10631; AKU10631; AzCIB_0726. DR KEGG; azi:AzCIB_0726; -. DR PATRIC; fig|198107.6.peg.741; -. DR KO; K03665; -. DR Proteomes; UP000066621; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000066621}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000066621}. FT DOMAIN 198 364 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 386 AA; 42036 MW; 8ECE24C256A10EA1 CRC64; MFERPDAGER AVLVQLDLNQ GALDERLSEL KLLALSAGAS VEAVVGGRRA RPDPALFAGR GKVDEIAETL RAHEADFVIF NHALSPAQQR NLERTLQCRV VDRTALILDI FAQRARSHEG KLQVELAQLD HLSTRLVRGW THLERQKGGI GLRGPGETQL ETDRRLLGKR VKVLKERLAQ IEKQRRVRRR GREGRNVLSV SLVGYTNAGK STLFNALTKA GAYAADQLFA TLDTTSRRLY VGEGGNVVLS DTVGFIRDLP HALVAAFHAT LEETANADLL LHVVDSASED REAQIEAVNG VLAEIGAGAV PQFMVMNKVD LTRAEPGVQR DEYGKIVRVF LSARTGEGLG LLREALAEAA RSAVTDAPGD PDGIAPDFTD KDPIQT // ID A0A0K1JKP5_9MICO Unreviewed; 489 AA. AC A0A0K1JKP5; DT 11-NOV-2015, integrated into UniProtKB/TrEMBL. DT 11-NOV-2015, sequence version 1. DT 07-JUN-2017, entry version 13. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=VV02_17815 {ECO:0000313|EMBL:AKU17276.1}; OS Luteipulveratus mongoliensis. OC Bacteria; Actinobacteria; Micrococcales; Dermacoccaceae; OC Luteipulveratus. OX NCBI_TaxID=571913 {ECO:0000313|EMBL:AKU17276.1, ECO:0000313|Proteomes:UP000066480}; RN [1] {ECO:0000313|EMBL:AKU17276.1, ECO:0000313|Proteomes:UP000066480} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MN07-A0370 {ECO:0000313|EMBL:AKU17276.1, RC ECO:0000313|Proteomes:UP000066480}; RA Juboi H., Basik A., Shamsul S.S., Arnold P., Schmitt E.K., RA Sanglier J.-J., Yeo T.; RT "Luteipulveratus halotolerans sp. nov., a novel actinobacterium RT (Dermacoccaceae) from Sarawak, Malaysia."; RL Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP011112; AKU17276.1; -; Genomic_DNA. DR RefSeq; WP_052593631.1; NZ_CP011112.1. DR EnsemblBacteria; AKU17276; AKU17276; VV02_17815. DR KEGG; lmoi:VV02_17815; -. DR PATRIC; fig|571913.6.peg.3614; -. DR KO; K03665; -. DR Proteomes; UP000066480; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 2. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000066480}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000066480}. FT DOMAIN 270 435 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 489 AA; 53394 MW; B4F321F91C12CD11 CRC64; MTTRDHLLST RAEALSDGSD TDPRYDEAGF LIDDVDGEQL DRQERAALRR VEGLSTELED VTEVEYRQLR LERVVLAGVW TDGTAEEAEN SLRELSALAE TAGSTVLAGV LQRRSRPDPG TWMGSGKAQE LRDIVIDEGA DTVIADTELA PSQRRALEDV VKVKVIDRTA LILDIFAQHA KSKEGKAQVE LAQLSYLLPR LRGWGESMSR QAGGQAAGGQ GMGSRGPGET KIELDRRRIN SRMAKLRKEI AQMKTSRDTK RHSRKAHHVP SVAIAGYTNA GKSSLLNRLT GAGVLVENQL FATLDPTVRR SETTDGRLFT LTDTVGFVAN LPHQLIEAFR STLEEVGDAD LVLHVVDGSH PDPESQISAV RAVMAEVGGD AVKEVIVVNK ADLALPDVVD RLLRAEKHSI AVSARTGEGF EQLQELIARE LPRPDIQVEV VLPYDRGDLL SRLHDEGEIL STEHQDEGTL VHAKVTPTLQ ADLASYAVS // ID A0A0K1K570_9BURK Unreviewed; 381 AA. AC A0A0K1K570; DT 11-NOV-2015, integrated into UniProtKB/TrEMBL. DT 11-NOV-2015, sequence version 1. DT 07-JUN-2017, entry version 13. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=ACZ75_26780 {ECO:0000313|EMBL:AKU24535.1}; OS Massilia sp. NR 4-1. OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Oxalobacteraceae; Massilia. OX NCBI_TaxID=1678028 {ECO:0000313|EMBL:AKU24535.1, ECO:0000313|Proteomes:UP000056897}; RN [1] {ECO:0000313|EMBL:AKU24535.1, ECO:0000313|Proteomes:UP000056897} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NR 4-1 {ECO:0000313|EMBL:AKU24535.1, RC ECO:0000313|Proteomes:UP000056897}; RA Sul W.J.; RT "Massilia sp. NR 4-1 isolated from rhizosphere of Torreya nucifera in RT national heritage Bijarim forest, volcanic Jeju Island, Korea."; RL Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP012201; AKU24535.1; -; Genomic_DNA. DR RefSeq; WP_050412231.1; NZ_CP012201.1. DR KEGG; mnr:ACZ75_26780; -. DR PATRIC; fig|1678028.3.peg.5433; -. DR KO; K03665; -. DR Proteomes; UP000056897; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000056897}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000056897}. FT DOMAIN 190 357 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 381 AA; 41918 MW; 3549F43482866603 CRC64; MRAALVGVDF GQGDFAASIE ELMLLARSAG ANPVATVTGK RSSPDAAYFV GSGKADEIGH AVQDHKLEIV IFNHALSPAQ QRNLEKRLNV RVLDRTSLIL DIFAQRAQSH EGKLQVELAQ LQHLATRLIR GWTHLERQKG GIGLRGPGET QLETDRRLIG ERVKMLRARL AKLRKQHETQ RRARGRNNTF SVSLVGYTNA GKSTLFNSMT KAGVYVADQL FATLDTTSRR VYMGEEVGTV VVSDTVGFVR ELPHQLVAAF RATLEETIHA DLLLHVVDAA SPVRMEQIEQ VNLVLKEIGA DHIPQILVWN KIDAAGLEPS VERDEYDKIS RVFISARTGQ GLDLLRGAIT EAARDAQDRA GAEEDYPAPD SISTFTHVGS H // ID A0A0K1PFH2_9DELT Unreviewed; 529 AA. AC A0A0K1PFH2; DT 11-NOV-2015, integrated into UniProtKB/TrEMBL. DT 11-NOV-2015, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=AKJ08_2665 {ECO:0000313|EMBL:AKU92278.1}; OS Vulgatibacter incomptus. OC Bacteria; Proteobacteria; Deltaproteobacteria; Myxococcales; OC Cystobacterineae; Vulgatibacteraceae; Vulgatibacter. OX NCBI_TaxID=1391653 {ECO:0000313|EMBL:AKU92278.1, ECO:0000313|Proteomes:UP000055590}; RN [1] {ECO:0000313|EMBL:AKU92278.1, ECO:0000313|Proteomes:UP000055590} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 27710 {ECO:0000313|EMBL:AKU92278.1, RC ECO:0000313|Proteomes:UP000055590}; RA Babu N.S., Beckwith C.J., Beseler K.G., Brison A., Carone J.V., RA Caskin T.P., Diamond M., Durham M.E., Foxe J.M., Go M., RA Henderson B.A., Jones I.B., McGettigan J.A., Micheletti S.J., RA Nasrallah M.E., Ortiz D., Piller C.R., Privatt S.R., Schneider S.L., RA Sharp S., Smith T.C., Stanton J.D., Ullery H.E., Wilson R.J., RA Serrano M.G., Buck G., Lee V., Wang Y., Carvalho R., Voegtly L., RA Shi R., Duckworth R., Johnson A., Loviza R., Walstead R., Shah Z., RA Kiflezghi M., Wade K., Ball S.L., Bradley K.W., Asai D.J., RA Bowman C.A., Russell D.A., Pope W.H., Jacobs-Sera D., Hendrix R.W., RA Hatfull G.F.; RL Submitted (AUG-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP012332; AKU92278.1; -; Genomic_DNA. DR EnsemblBacteria; AKU92278; AKU92278; AKJ08_2665. DR KEGG; vin:AKJ08_2665; -. DR PATRIC; fig|1391653.3.peg.2769; -. DR KO; K03665; -. DR Proteomes; UP000055590; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000055590}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000055590}. FT DOMAIN 348 512 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 307 334 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 529 AA; 57716 MW; 94ED84CBD495B34A CRC64; MSPELARHLT EISRETGRQI GVLLTRKGEV EHVIVGDAHK LLLPDVGRAR AGQVRLRGLR LVHTHLRGET LTKDDLTDLA LLRLDLVCEI QALDNGLPGA AQVAHLLPEN PEGELWRITD YPSVHELDFD FGAEIRALEE QLAGAARARV VGDGEKAILV GLSVGRGRAT AESSLAELAE LANTAGVQVL ESIVQLRREH DPKYLIGKGK LEEIVLKSMQ LGADLIVFDK DLSPSQARHI AKETSLKVLD RTQLILDIFA QRAQSAEGKL QVELAQTRYL MPRLTAGTDA GLSRLMGGGV GGRGPGETKL EMDRRRARDR ITFLEKKIEA LSSSRAVRRK ERNRRGIPVV SIVGYTNAGK STLLNALTRS EVLAEDKLFA TLDPTSRRLR FPRDREVIIT DTVGFIRDLP KDLVAAFRAT LEELEDADLL LHVVDVADPE RDEHIAAVDR ILESLGLAQT PKLLVFNKAD KLAPEAKDGG AKVNDAILTS AITRRGFDDL LEKADALLWS EGATSRASAA SGGLPARIG // ID A0A0K1PT16_9DELT Unreviewed; 454 AA. AC A0A0K1PT16; DT 11-NOV-2015, integrated into UniProtKB/TrEMBL. DT 11-NOV-2015, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=AKJ09_03180 {ECO:0000313|EMBL:AKU96516.1}; OS Labilithrix luteola. OC Bacteria; Proteobacteria; Deltaproteobacteria; Myxococcales; OC Sorangiineae; Labilitrichaceae; Labilithrix. OX NCBI_TaxID=1391654 {ECO:0000313|EMBL:AKU96516.1, ECO:0000313|Proteomes:UP000064967}; RN [1] {ECO:0000313|EMBL:AKU96516.1, ECO:0000313|Proteomes:UP000064967} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 27648 {ECO:0000313|EMBL:AKU96516.1, RC ECO:0000313|Proteomes:UP000064967}; RA Babu N.S., Beckwith C.J., Beseler K.G., Brison A., Carone J.V., RA Caskin T.P., Diamond M., Durham M.E., Foxe J.M., Go M., RA Henderson B.A., Jones I.B., McGettigan J.A., Micheletti S.J., RA Nasrallah M.E., Ortiz D., Piller C.R., Privatt S.R., Schneider S.L., RA Sharp S., Smith T.C., Stanton J.D., Ullery H.E., Wilson R.J., RA Serrano M.G., Buck G., Lee V., Wang Y., Carvalho R., Voegtly L., RA Shi R., Duckworth R., Johnson A., Loviza R., Walstead R., Shah Z., RA Kiflezghi M., Wade K., Ball S.L., Bradley K.W., Asai D.J., RA Bowman C.A., Russell D.A., Pope W.H., Jacobs-Sera D., Hendrix R.W., RA Hatfull G.F.; RL Submitted (AUG-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP012333; AKU96516.1; -; Genomic_DNA. DR EnsemblBacteria; AKU96516; AKU96516; AKJ09_03180. DR KEGG; llu:AKJ09_03180; -. DR PATRIC; fig|1391654.3.peg.3216; -. DR KO; K03665; -. DR Proteomes; UP000064967; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 2. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000064967}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000064967}. FT DOMAIN 233 398 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 194 221 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 454 AA; 50451 MW; BB2949A470D8BE21 CRC64; MLVAVHLPDA DDLEFTSSLE ELERLVSTLG YKTVAKVTQN RTHLETAAVL GEGKLKELGD LTGGDGHVGT TAPKKKDKAR LRREAEAGGD FDDDGDVDVE EEDDDFGVDG ERTAKVDLVA VDHDLSPSQA RNLERATGAA VLDRTGVIIE IFHRHAKSRE ARLQVEIARL TYTAPRLRES PSGKERQRGR GAGEAALELD RRKVRDRIAE LKEELVAVQR DQDVRRSHRR QARRIALVGY TNAGKSSLMR ALTGSDVYVE NKLFATLDTT VRALYPEPKP RILVSDTVGF IKKLPHDLVA SFKSTLDEAL EASHLLHVVD AADPSWESQL AVTREVLEEI GAGEVPSTLV MNKIDRLAPE ELAALRVRLP DAWFVSAHDP SDVASVRERI IGIFEATYVE SEFVIPYDRQ AVLSEMHDSG RVSAERYEEN GVIVTYRAEP EVIARFRSKL ERAR // ID A0A0K1Q710_9DELT Unreviewed; 565 AA. AC A0A0K1Q710; DT 11-NOV-2015, integrated into UniProtKB/TrEMBL. DT 11-NOV-2015, sequence version 1. DT 07-JUN-2017, entry version 12. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=AKJ09_07853 {ECO:0000313|EMBL:AKV01190.1}; OS Labilithrix luteola. OC Bacteria; Proteobacteria; Deltaproteobacteria; Myxococcales; OC Sorangiineae; Labilitrichaceae; Labilithrix. OX NCBI_TaxID=1391654 {ECO:0000313|EMBL:AKV01190.1, ECO:0000313|Proteomes:UP000064967}; RN [1] {ECO:0000313|EMBL:AKV01190.1, ECO:0000313|Proteomes:UP000064967} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 27648 {ECO:0000313|EMBL:AKV01190.1, RC ECO:0000313|Proteomes:UP000064967}; RA Babu N.S., Beckwith C.J., Beseler K.G., Brison A., Carone J.V., RA Caskin T.P., Diamond M., Durham M.E., Foxe J.M., Go M., RA Henderson B.A., Jones I.B., McGettigan J.A., Micheletti S.J., RA Nasrallah M.E., Ortiz D., Piller C.R., Privatt S.R., Schneider S.L., RA Sharp S., Smith T.C., Stanton J.D., Ullery H.E., Wilson R.J., RA Serrano M.G., Buck G., Lee V., Wang Y., Carvalho R., Voegtly L., RA Shi R., Duckworth R., Johnson A., Loviza R., Walstead R., Shah Z., RA Kiflezghi M., Wade K., Ball S.L., Bradley K.W., Asai D.J., RA Bowman C.A., Russell D.A., Pope W.H., Jacobs-Sera D., Hendrix R.W., RA Hatfull G.F.; RL Submitted (AUG-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP012333; AKV01190.1; -; Genomic_DNA. DR EnsemblBacteria; AKV01190; AKV01190; AKJ09_07853. DR KEGG; llu:AKJ09_07853; -. DR PATRIC; fig|1391654.3.peg.7960; -. DR KO; K03665; -. DR Proteomes; UP000064967; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000064967}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000064967}. FT DOMAIN 337 506 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 565 AA; 62821 MW; 8BBE466ED3E4446B CRC64; METGRQVGAL VHRSGQVDYV IVGDSGKLML PDIGRLRAAE GRFRGLRLIH THVRGEALTR DDLVDLVRLR LDLVCAIQIN ARGEARSLHY AYNIPGEEGA LPYREHGPTP IGQERVHVGE LMSGLEAEFA KRTRGRAVRA PAGRALLVHV ADKSERDVAR RADESVRELR ELARTAGVEV VDTIVQLRER VDPKTVLGKG KLDDVILRSM QLDSDVLIFD RELTPAQASA IAKESDLKVI DRTQLILDIF AQRAESKDGK VQVELAQLKY NMPRLVMKDD SLSRLTGGIG GRGPGETKLE IGRRRAKERV SHLEAQLKKF GRQREQRRHK RTREGVPTVA IVGYTNAGKS TLLNTLTGAD VLAEDKLFAT LDTRSRHLKV GWAGYGDREV VISDTVGFIR SLPKDLFAAF RATFEEASDA DLLLVVVDAT DDAKQEHIAT TESLLEELGL QDIPRVLVFN KIELLAPIDR ALLQRKNPDA VLLSATQRET TRPLVERIAK ELAERWTESA KTPETMDLEG QVTPPSEEPA EDADVSASTL VELLRRAGRR VRPPRLVEEK APRRV // ID A0A0K1QA86_9DELT Unreviewed; 481 AA. AC A0A0K1QA86; DT 11-NOV-2015, integrated into UniProtKB/TrEMBL. DT 11-NOV-2015, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=AKJ09_09317 {ECO:0000313|EMBL:AKV02654.1}; OS Labilithrix luteola. OC Bacteria; Proteobacteria; Deltaproteobacteria; Myxococcales; OC Sorangiineae; Labilitrichaceae; Labilithrix. OX NCBI_TaxID=1391654 {ECO:0000313|EMBL:AKV02654.1, ECO:0000313|Proteomes:UP000064967}; RN [1] {ECO:0000313|EMBL:AKV02654.1, ECO:0000313|Proteomes:UP000064967} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 27648 {ECO:0000313|EMBL:AKV02654.1, RC ECO:0000313|Proteomes:UP000064967}; RA Babu N.S., Beckwith C.J., Beseler K.G., Brison A., Carone J.V., RA Caskin T.P., Diamond M., Durham M.E., Foxe J.M., Go M., RA Henderson B.A., Jones I.B., McGettigan J.A., Micheletti S.J., RA Nasrallah M.E., Ortiz D., Piller C.R., Privatt S.R., Schneider S.L., RA Sharp S., Smith T.C., Stanton J.D., Ullery H.E., Wilson R.J., RA Serrano M.G., Buck G., Lee V., Wang Y., Carvalho R., Voegtly L., RA Shi R., Duckworth R., Johnson A., Loviza R., Walstead R., Shah Z., RA Kiflezghi M., Wade K., Ball S.L., Bradley K.W., Asai D.J., RA Bowman C.A., Russell D.A., Pope W.H., Jacobs-Sera D., Hendrix R.W., RA Hatfull G.F.; RL Submitted (AUG-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP012333; AKV02654.1; -; Genomic_DNA. DR EnsemblBacteria; AKV02654; AKV02654; AKJ09_09317. DR KEGG; llu:AKJ09_09317; -. DR PATRIC; fig|1391654.3.peg.9442; -. DR KO; K03665; -. DR Proteomes; UP000064967; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000064967}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000064967}. FT DOMAIN 257 424 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 225 252 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 481 AA; 53631 MW; 7647A5AA9CC42CB3 CRC64; MRLRRDLAKH RIQSISSRTD GQMPKFTSKA ISEHIEVPLA DDGQLETLVE HWDAKRSNES AGRAFESASY VVSVGEARDP RIRAAQMDEI VSLVESQGGH VVGQEVLHLS EPNPRTLLGK GTAEEVAARA RAAGATMLVL DAELSPSQTR NLEDVAGIPI CDREAIILNV FLRHARTRRA KLQVELAQLQ YLRPRIRGVG LDMDQQTGAT KNARGPGETA SELMARKLDR RLEELQKALR KLTVTARTQR LQRTDCHRIV LVGYTNAGKT SLMNALTNAG LSARDMPFET LDTTSRCLTR HGGDVLICDT VGFIRRLPER LLASFESTLA EVVEASLLVI VVDTSDYERQ LQLKTTLEIL ERMGAADIPR FYVFNKRDRL PFVPDEEVLE RWSDGHPHAL ISTTDPNAVT ELQEALLHVV RSHDEEELTT FVPYGASEVI ALAYGRCRVV RTEPVDDGMT MTIQGPIAEI SRVRRLLEEV Q // ID A0A0K1R9X4_9CORY Unreviewed; 499 AA. AC A0A0K1R9X4; DT 11-NOV-2015, integrated into UniProtKB/TrEMBL. DT 11-NOV-2015, sequence version 1. DT 07-JUN-2017, entry version 12. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=AK829_02520 {ECO:0000313|EMBL:AKV58227.1}; OS Corynebacterium riegelii. OC Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae; OC Corynebacterium. OX NCBI_TaxID=156976 {ECO:0000313|EMBL:AKV58227.1, ECO:0000313|Proteomes:UP000060016}; RN [1] {ECO:0000313|EMBL:AKV58227.1, ECO:0000313|Proteomes:UP000060016} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=PUDD_83A45 {ECO:0000313|EMBL:AKV58227.1, RC ECO:0000313|Proteomes:UP000060016}; RA Babu N.S., Beckwith C.J., Beseler K.G., Brison A., Carone J.V., RA Caskin T.P., Diamond M., Durham M.E., Foxe J.M., Go M., RA Henderson B.A., Jones I.B., McGettigan J.A., Micheletti S.J., RA Nasrallah M.E., Ortiz D., Piller C.R., Privatt S.R., Schneider S.L., RA Sharp S., Smith T.C., Stanton J.D., Ullery H.E., Wilson R.J., RA Serrano M.G., Buck G., Lee V., Wang Y., Carvalho R., Voegtly L., RA Shi R., Duckworth R., Johnson A., Loviza R., Walstead R., Shah Z., RA Kiflezghi M., Wade K., Ball S.L., Bradley K.W., Asai D.J., RA Bowman C.A., Russell D.A., Pope W.H., Jacobs-Sera D., Hendrix R.W., RA Hatfull G.F.; RL Submitted (AUG-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP012342; AKV58227.1; -; Genomic_DNA. DR RefSeq; WP_052203967.1; NZ_CP012342.1. DR EnsemblBacteria; AKV58227; AKV58227; AK829_02520. DR PATRIC; fig|156976.3.peg.501; -. DR Proteomes; UP000060016; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000060016}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000060016}. FT DOMAIN 273 446 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 232 259 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 499 AA; 54990 MW; F65FF3B6FFF8BDD7 CRC64; MTEFDNEHDE LHNELLARAF RHNSPQPGVG ADDSTVGSLD LEDRNALRRL TRDTSIRSED HEDIYEVEYR KLRLEQVILV GAWTEGTTAE MEASMMELAA LTDTAGAEVL DILYQKRDKP DPGTYIGSGK VKELAQIVQS TGADTVIFDG ELSPGQMVAL EEALKVKVID RTMLILDIFA QHAKSKEGKA QVSLAQMEYL YTRTRGWGGN LSRQAGGRAG SNGGVGLRGP GETRIEADRR RLRTEMAKLR HQLRDMATAR EVKRAQRARS TTPKIAIAGY TNAGKSSLIN AMTNAGVLVE DALFATLDPS TRKAQLADGR SVVLTDTVGF VRHLPTQLVE AFKSTLEEVS GADLVLHVVD GSDPFPLKQI EAVNEVLSEI TRESGETLPP ELVVVNKIDE ADPVVLAELR HAFDHAGRDV VFVSALTGEG IAELESKIEM FLNTLDEHVT MLVPFTRGDV VSLLHEHGTV RSEEYQEQGT LIDVRLPRVL VEQHREFVV // ID A0A0K1XD30_9GAMM Unreviewed; 434 AA. AC A0A0K1XD30; DT 11-NOV-2015, integrated into UniProtKB/TrEMBL. DT 11-NOV-2015, sequence version 1. DT 30-AUG-2017, entry version 15. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=AKN88_04235 {ECO:0000313|EMBL:AKX59231.1}; OS Oblitimonas alkaliphila. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Oblitimonas. OX NCBI_TaxID=1697053 {ECO:0000313|EMBL:AKX59231.1, ECO:0000313|Proteomes:UP000063953}; RN [1] {ECO:0000313|EMBL:AKX59231.1, ECO:0000313|Proteomes:UP000063953} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=E5571 {ECO:0000313|EMBL:AKX59231.1, RC ECO:0000313|Proteomes:UP000063953}; RX PubMed=26679585; RA Lauer A.C., Nicholson A.C., Humrighouse B.W., Emery B., Drobish A., RA Juieng P., Loparev V., McQuiston J.R.; RT "Genome Sequences of Oblitimonas alkaliphila gen. nov. sp. nov. RT (Proposed), a Novel Bacterium of the Pseudomonadaceae Family."; RL Genome Announc. 3:e01474-15(2015). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP012365; AKX59231.1; -; Genomic_DNA. DR RefSeq; WP_053100335.1; NZ_CP012365.1. DR EnsemblBacteria; AKX59231; AKX59231; AKN88_04235. DR PATRIC; fig|1698449.3.peg.847; -. DR Proteomes; UP000063953; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000063953}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000063953}. FT DOMAIN 199 366 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 165 192 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 434 AA; 48877 MW; BFF2B9E995986C3D CRC64; MSNADAAVRE AALLVHLDNY DPAAREDPYE FQDLVRSAGA HIVHFVTVHR PQFTARFLIG AGKVDEIAQL VQLYEADLVI FNHALTPSQE RNLEQALGCR VIDRIGLILD IFAQRAYTHE GKLQVELAQL EHISTRLVRS RTDLSRQQGG IGLRGPGETQ LETDRRLLRI RVRQIKARLE KVRNQRDLAR RARKRAEMPA VSLVGYTNAG KSTLFNRLTE SGVYAADQLF ATLDPTVRRV ELADVGAITL ADTVGFIRHL PHKLVESFRA TLEESAAADL LLHVIDAGAE ERQEQIEQVL EVLHEIDADQ VTLLEVYNKI DTLAQIEPHI QRNAEGKPER VWLSAQSGQG IELLIQAMQE LLVDDLVVTT LVLPQQLSRL RAKLFDLQAI VQEHYDEQGQ SVVDIRIARV ELNRLLSHEG LAAETFLQEY TKSH // ID A0A0K2BLP5_9GAMM Unreviewed; 428 AA. AC A0A0K2BLP5; DT 11-NOV-2015, integrated into UniProtKB/TrEMBL. DT 11-NOV-2015, sequence version 1. DT 30-AUG-2017, entry version 15. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:AKZ66107.1}; GN ORFNames=AB162_527 {ECO:0000313|EMBL:AKZ66107.1}; OS Candidatus Baumannia cicadellinicola. OC Bacteria; Proteobacteria; Gammaproteobacteria; Candidatus Baumannia. OX NCBI_TaxID=186490 {ECO:0000313|EMBL:AKZ66107.1, ECO:0000313|Proteomes:UP000056466}; RN [1] {ECO:0000313|EMBL:AKZ66107.1, ECO:0000313|Proteomes:UP000056466} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=B-GSS {ECO:0000313|EMBL:AKZ66107.1, RC ECO:0000313|Proteomes:UP000056466}; RA Bennett G.M., McCutcheon J.P., McDonald B.R., Moran N.A.; RT "Lineage-specific patterns of genome deterioration in obligate RT symbionts."; RL Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP011787; AKZ66107.1; -; Genomic_DNA. DR RefSeq; WP_053097238.1; NZ_CP011787.1. DR EnsemblBacteria; AKZ66107; AKZ66107; AB162_527. DR KEGG; bcig:AB162_527; -. DR PATRIC; fig|186490.8.peg.496; -. DR KO; K03665; -. DR Proteomes; UP000056466; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000056466}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}. FT DOMAIN 200 367 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 428 AA; 48339 MW; EE6539A651B96550 CRC64; MLNCYYLGKH KQAILVHICF QKNHNFKDDL DEFESLVCSA GVSILNIVTG SRNTPNAKYF VGEGKANEIA EKVKNNAASI VIFNHSLSPA QERNLELLFE CSVIDRTGLI LSIFAQRART NEGKLQVELA QLSHQSTRLV RGWKHLERQK GGIGLLSGPG ETQLETDRRL LRKRINTILL RIKKLENRRE QGRLTRASIP TVLLVGYTNA GKSTLFNYLT KASVETADKL FTTLDTKIKN INIKTVGNIV LADTVGFIRD LPHHLVASFQ ATLKEIRQAT LLLHVVDASD NCINIKISSV EKVLAEINAN LISKLLVMNK IDKLNNFTPR IDRNEFNNPV SVWLSAQSGH GISLLLKALE ECLVGDITSY HLCLPPRAGR LLSYFYQLNA IEKYWIETDG SVRLIIRLPK NKWFRLCKQE VELLEYIV // ID A0A0K2DG89_9RHIZ Unreviewed; 463 AA. AC A0A0K2DG89; DT 11-NOV-2015, integrated into UniProtKB/TrEMBL. DT 11-NOV-2015, sequence version 1. DT 05-JUL-2017, entry version 14. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=AL346_17985 {ECO:0000313|EMBL:ALA18956.1}; OS Chelatococcus sp. CO-6. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Beijerinckiaceae; Chelatococcus. OX NCBI_TaxID=1702325 {ECO:0000313|EMBL:ALA18956.1, ECO:0000313|Proteomes:UP000065824}; RN [1] {ECO:0000313|EMBL:ALA18956.1, ECO:0000313|Proteomes:UP000065824} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CO-6 {ECO:0000313|EMBL:ALA18956.1, RC ECO:0000313|Proteomes:UP000065824}; RA Babu N.S., Beckwith C.J., Beseler K.G., Brison A., Carone J.V., RA Caskin T.P., Diamond M., Durham M.E., Foxe J.M., Go M., RA Henderson B.A., Jones I.B., McGettigan J.A., Micheletti S.J., RA Nasrallah M.E., Ortiz D., Piller C.R., Privatt S.R., Schneider S.L., RA Sharp S., Smith T.C., Stanton J.D., Ullery H.E., Wilson R.J., RA Serrano M.G., Buck G., Lee V., Wang Y., Carvalho R., Voegtly L., RA Shi R., Duckworth R., Johnson A., Loviza R., Walstead R., Shah Z., RA Kiflezghi M., Wade K., Ball S.L., Bradley K.W., Asai D.J., RA Bowman C.A., Russell D.A., Pope W.H., Jacobs-Sera D., Hendrix R.W., RA Hatfull G.F.; RL Submitted (AUG-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP012398; ALA18956.1; -; Genomic_DNA. DR EnsemblBacteria; ALA18956; ALA18956; AL346_17985. DR KEGG; chel:AL346_17985; -. DR PATRIC; fig|1702325.3.peg.3760; -. DR KO; K03665; -. DR Proteomes; UP000065824; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000065824}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000065824}. FT DOMAIN 228 402 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 463 AA; 50937 MW; 57FC08C2D43BC935 CRC64; MTEPKNRKGA LAAHLTEPEK TVASGTATFV VGPYPARKAR VREEGGANLR DPQARLDEAA GLARAIDLDV VEAFIVTLDD VRPSTYLGKG KVEELTGAIK ASDIGLVVMD CALSPVQQRN LERAWGCKVI DRTGLILEIF GRRAQTREGA LQVELAHLAY QKSRLVRSWT HLERQRGGFG FLGGPGETQI EADRRIIQER MTRIERDLEQ VKRTRSLHRA SRRRVPYPVI ALVGYTNAGK STLFNRLTTA SVMAEDMLFA TLDPTARAIT LPHGEKAILS DTVGFISDLP TMLVAAFRAT LEDVVEADVL LHVRDVSHED TEAQAADVET ILRELGIDEA RQRSLIEVWN KADLLDDAGR ERLATLAVRK GDGPQPVLVS AQTGYGIDTL LAEIEARIAA GRPVYQVDLA PTEGATLNWL YEEAEILKRE EGEDGHIALT IRLSPDKEAR LTRRCPGARR VAA // ID A0A0K2DXP1_PISSA Unreviewed; 417 AA. AC A0A0K2DXP1; DT 11-NOV-2015, integrated into UniProtKB/TrEMBL. DT 11-NOV-2015, sequence version 1. DT 07-JUN-2017, entry version 10. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:ALA25130.1}; GN ORFNames=KW89_1664 {ECO:0000313|EMBL:ALA25130.1}; OS Piscirickettsia salmonis. OC Bacteria; Proteobacteria; Gammaproteobacteria; Thiotrichales; OC Piscirickettsiaceae; Piscirickettsia. OX NCBI_TaxID=1238 {ECO:0000313|EMBL:ALA25130.1, ECO:0000313|Proteomes:UP000029541}; RN [1] {ECO:0000313|EMBL:ALA25130.1, ECO:0000313|Proteomes:UP000029541} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=A1-15972 {ECO:0000313|Proteomes:UP000029541}; RA Babu N.S., Beckwith C.J., Beseler K.G., Brison A., Carone J.V., RA Caskin T.P., Diamond M., Durham M.E., Foxe J.M., Go M., RA Henderson B.A., Jones I.B., McGettigan J.A., Micheletti S.J., RA Nasrallah M.E., Ortiz D., Piller C.R., Privatt S.R., Schneider S.L., RA Sharp S., Smith T.C., Stanton J.D., Ullery H.E., Wilson R.J., RA Serrano M.G., Buck G., Lee V., Wang Y., Carvalho R., Voegtly L., RA Shi R., Duckworth R., Johnson A., Loviza R., Walstead R., Shah Z., RA Kiflezghi M., Wade K., Ball S.L., Bradley K.W., Asai D.J., RA Bowman C.A., Russell D.A., Pope W.H., Jacobs-Sera D., Hendrix R.W., RA Hatfull G.F.; RL Submitted (AUG-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP012413; ALA25130.1; -; Genomic_DNA. DR EnsemblBacteria; ALA25130; ALA25130; KW89_1664. DR Proteomes; UP000029541; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000029541}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000029541}. FT DOMAIN 189 314 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 417 AA; 46826 MW; 34538083683A7289 CRC64; MIYLTVRSLE STGPLTEFRE LIVSAGREIV NEICLSRSDV HAASFLGQGQ IERVKEEFIN SNEGISEVII NHALTSVQVR NLSTLFSCRV LDRTDLILDI FAKRARTFEG KLQVELTQLQ HQATRLVQKS GHYDQQRGGI GVRGGAGETG LEVDRRVLRQ RIATLKKRLV HIRDSRALGR QRRQRSQQPT IALVGYTNAG KSTLFNALSD SSAYADDRLF ATLDPTLRRA VIPGFGDIVL ADTVGFIQQL PPQLIDAFRA TLEETAQADL LLHVIDGASE DYLLRIEQVN EVLVEIGAEH IPQILVFNKV DLLDNLASSA LKLDCQESWA RVSAVKQLGF DVLYEKILYA IGGEAVDTVL RIPMNRAEVR TELHRLRTVL SERYDEDWAW IHVKGSYAVL NHALDRYGLS LIQCKQY // ID A0A0K2GCC3_9BACT Unreviewed; 528 AA. AC A0A0K2GCC3; DT 11-NOV-2015, integrated into UniProtKB/TrEMBL. DT 11-NOV-2015, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:ALA58499.1}; GN ORFNames=NITMOv2_2082 {ECO:0000313|EMBL:ALA58499.1}; OS Nitrospira moscoviensis. OC Bacteria; Nitrospirae; Nitrospirales; Nitrospiraceae; Nitrospira. OX NCBI_TaxID=42253 {ECO:0000313|EMBL:ALA58499.1, ECO:0000313|Proteomes:UP000069205}; RN [1] {ECO:0000313|EMBL:ALA58499.1, ECO:0000313|Proteomes:UP000069205} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NSP M-1 {ECO:0000313|EMBL:ALA58499.1, RC ECO:0000313|Proteomes:UP000069205}; RX PubMed=26305944; DOI=10.1073/pnas.1506533112; RA Koch H., Lucker S., Albertsen M., Kitzinger K., Herbold C., Spieck E., RA Nielsen P.H., Wagner M., Daims H.; RT "Expanded metabolic versatility of ubiquitous nitrite-oxidizing RT bacteria from the genus Nitrospira."; RL Proc. Natl. Acad. Sci. U.S.A. 112:11371-11376(2015). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP011801; ALA58499.1; -; Genomic_DNA. DR EnsemblBacteria; ALA58499; ALA58499; NITMOv2_2082. DR KEGG; nmv:NITMOv2_2082; -. DR PATRIC; fig|42253.5.peg.2053; -. DR KO; K03665; -. DR Proteomes; UP000069205; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000069205}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000069205}. FT DOMAIN 342 506 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 528 AA; 58767 MW; 69515AEE6924512A CRC64; MARTLCQLSL DIRRPLAVLL TRRGLVQEII VGTDLTLSPT TLAKFRAGVR SLRGLRLIRT QLHDQPLSQE ALTDLAYLRL DLIGVLSVTS DGNPGNLYLA HLLPPSETGQ LFKVLKAVPL HHCTIAFDEF IEELEADLQA ARGHHTVGGG KESAILVSAS PQGKAEQEDR LVELAELATS ADVTVIDRMA QRTPDGHQRY LLGSGKLKEV LIQTLHKGAD MVIFDQTLTP AQSRAISEMT DIKVIDRTQL ILDIFARRAH SREGKVQVEL AQLRYMLPRL SGKGTHLSRL GGGIGTRGPG ETKLETDRRR IHDRITHLER ELAHFARHQD QRRARRGRHG LPVISLVGYT NAGKSTLLNV LTKSQVSAQN RVFETLDTTS RRLRCPEDRE VIVTDTVGFI RDLPKELVGA FRTTLEELRE ADLLLHVVDA SAADIDIQIT AVTDILQELH LDTIPRLLVF NKCDRLPAHQ VEPLCRRYRA IGISALNPAT LRPLLAQLEA HVRSLTAETP AWPDFHPDRD LVALASRR // ID A0A0K2LV13_9NOST Unreviewed; 578 AA. AC A0A0K2LV13; DT 11-NOV-2015, integrated into UniProtKB/TrEMBL. DT 11-NOV-2015, sequence version 1. DT 07-JUN-2017, entry version 12. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=AA650_02705 {ECO:0000313|EMBL:ALB39519.1}; OS Anabaena sp. WA102. OC Bacteria; Cyanobacteria; Nostocales; Nostocaceae; Anabaena. OX NCBI_TaxID=1647413 {ECO:0000313|EMBL:ALB39519.1, ECO:0000313|Proteomes:UP000056652}; RN [1] {ECO:0000313|EMBL:ALB39519.1, ECO:0000313|Proteomes:UP000056652} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=WA102 {ECO:0000313|EMBL:ALB39519.1, RC ECO:0000313|Proteomes:UP000056652}; RA Brown N.M.; RT "The finished genome of an anatoxin-a-producing Anabaena isolate RT reveals extensive genome rearrangement."; RL Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP011456; ALB39519.1; -; Genomic_DNA. DR RefSeq; WP_053537864.1; NZ_CP011456.1. DR EnsemblBacteria; ALB39519; ALB39519; AA650_02705. DR KEGG; awa:AA650_02705; -. DR PATRIC; fig|1647413.5.peg.643; -. DR KO; K03665; -. DR Proteomes; UP000056652; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000056652}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}. FT DOMAIN 405 575 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 364 391 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 578 AA; 63577 MW; C8C92FD67ACBF2BD CRC64; METIFGNVQG LKSSQLKQLQ RLYHQRISGD CITTTDFAQR LAAVSTEINQ PVCVYINRRG QVIRVGVGTP RQTQIPPLEL PRYGAERLSG IRCLSTNLKS EPPNEAALTA MALQRLDALV VLNITGAGFT KRGGGSTGYV KEAYLAHLVA NSRQLVTTQS SDMSISDAVM YSHVSSPLSL DALADQDFLN LVEGLEEEFS REFVGQEVDA DHDRVLIVGV LTENTNPQQF QDIIVELTRL VDTAGGTVLQ VLQQKRSRIH PQTVIGEGKV QEAALTAQTL GANLVVFDRD LSPSQVRNLE AQIGVRVVDR TEVILDIFAQ RAQSGAGKLQ VELAQLEYMM PRLAGRGQSM SRLGGGIGTR GPGETKLETE RRAIQKRISR LQQEVNQLQA HRCRLRQRRQ HREVPSVALV GYTNAGKSTL LNALTNSEVY TADQLFATLD PTTRRLTLPH AETAAPQETL MTDTVGFIHE LPASLMDAFR ATLEEVTEAD ALLHLVDLSH PAWLNHIRAV RDILAQMPIT PGPALVAFNK IDQVNSETLA LAREEFPLAV FISASQRLGL ETLRQRLSLL IQYAVGDD // ID A0A0K2REI8_9MICC Unreviewed; 520 AA. AC A0A0K2REI8; DT 11-NOV-2015, integrated into UniProtKB/TrEMBL. DT 11-NOV-2015, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=AHiyo8_13450 {ECO:0000313|EMBL:BAS13042.1}; OS Arthrobacter sp. Hiyo8. OC Bacteria; Actinobacteria; Micrococcales; Micrococcaceae; Arthrobacter. OX NCBI_TaxID=1588023 {ECO:0000313|EMBL:BAS13042.1, ECO:0000313|Proteomes:UP000060353}; RN [1] {ECO:0000313|Proteomes:UP000060353} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Hiyo8 {ECO:0000313|Proteomes:UP000060353}; RA Hiraoka S., Machiyama A., Iwasaki W.; RT "Microbial genome analysis of tsunami-affected soil."; RL Submitted (FEB-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AP014719; BAS13042.1; -; Genomic_DNA. DR EnsemblBacteria; BAS13042; BAS13042; AHiyo8_13450. DR KEGG; arh:AHiyo8_13450; -. DR PATRIC; fig|1588023.3.peg.1419; -. DR KO; K03665; -. DR Proteomes; UP000060353; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000060353}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000060353}. FT DOMAIN 299 464 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 520 AA; 56780 MW; 93DE0DE1684BBEE0 CRC64; MTTQKNTGPD SDAQDMSPEE IQAVIDRILS KDAPAIVQDR DEPRGVFGKA QAISRLDEEH SIYDGDQEDL AERRALRRTA GLSTELEDVT EVEYRQLRLE RVVLAGLWTE GTLADAENSL RELAALAETA GSEVLDGIVQ RRMKPDPGTF LGSGKAMELK DIVMSTGADT VVVDAELAPS QRRGLEDIVK VKVVDRTTLI LDIFAQHAKS REGKAQVELA QLEYLLPRLR GWGDSMSRQA GGQVGGAGAG MGSRGPGETK IELDRRRIRT RMAKLRREIA AMKPSRETKR ANRRRNAVPS VAIAGYTNAG KSSLLNRLTD AGVLVENALF ATLDPTVRKA QTPDGIGYTL SDTVGFVRSL PTQLVEAFRS TLEEVADADL ILHVVDVSHP DPEGQIAAVR TVFSEVDARK IPEIIVLNKA DAADPFVIER LKQKEPRHVV VSTRTGQGIA ELLGAISEAI PRPGVRLEVL IPYNRGELIN KLHNTDAEIL SLEHEEEGTR VVAMVHENLA AELESFVSNG // ID A0A0K2SPK3_9FIRM Unreviewed; 424 AA. AC A0A0K2SPK3; DT 11-NOV-2015, integrated into UniProtKB/TrEMBL. DT 11-NOV-2015, sequence version 1. DT 30-AUG-2017, entry version 13. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=LIP_3103 {ECO:0000313|EMBL:BAS28932.1}; OS Limnochorda pilosa. OC Bacteria; Firmicutes; Limnochordia; Limnochordales; Limnochordaceae; OC Limnochorda. OX NCBI_TaxID=1555112 {ECO:0000313|EMBL:BAS28932.1, ECO:0000313|Proteomes:UP000065807}; RN [1] {ECO:0000313|Proteomes:UP000065807} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=HC45 {ECO:0000313|Proteomes:UP000065807}; RA Watanabe M., Kojima H., Fukui M.; RT "Complete genome sequence and phylogenetic analysis of Limnochorda RT pilosa."; RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AP014924; BAS28932.1; -; Genomic_DNA. DR EnsemblBacteria; BAS28932; BAS28932; LIP_3103. DR KEGG; lpil:LIP_3103; -. DR PATRIC; fig|1555112.3.peg.3150; -. DR KO; K03665; -. DR Proteomes; UP000065807; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000065807}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000065807}. FT DOMAIN 195 361 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 154 181 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 424 AA; 46987 MW; 5C7D62D3270C971B CRC64; MQLRETVILA GLKEADNPMA GSLFRELGSL VEAAGGEVAG EVTSSRRRPH PATLIGPGKV EDLQAMVVRT GADLVVFNDE LSPAQARNLS AALKCRVIDR TQLILDIFAQ RARSREGKLQ VERAQLEYLL PRLGGTVEEL SRLGGGIGTR GPGETQLERD RRRVRRRLAR LRRELASFEG TRRVQRATRQ QHGIPLVALV GYTNAGKSTL FNRLTGAGVT AGDRLFETLD PTLRRLRLGS PPGDEVILAD TVGFLRRLPH RLVAAFHATL EEVVEADLLL HVVDASDPEH PQQMQAVQAV LRELGTEDKP HVVAFNKVDR LGGRRPLAMR MEPHAVAISA LEGRGLDALQ EEIRRCLPER LVVREYRFPY GAAGLVAWFH RGGRVLEEEY GPEEIRLRVE LRESLAREAG AVVGARRSQR RVPQ // ID A0A0K2YM89_9NOCA Unreviewed; 487 AA. AC A0A0K2YM89; DT 11-NOV-2015, integrated into UniProtKB/TrEMBL. DT 11-NOV-2015, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:CRK53132.1}; GN ORFNames=RHCRD62_50335 {ECO:0000313|EMBL:CRK53132.1}; OS Rhodococcus sp. RD6.2. OC Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae; OC Rhodococcus. OX NCBI_TaxID=260936 {ECO:0000313|EMBL:CRK53132.1, ECO:0000313|Proteomes:UP000044872}; RN [1] {ECO:0000313|EMBL:CRK53132.1, ECO:0000313|Proteomes:UP000044872} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=RD6.2 {ECO:0000313|EMBL:CRK53132.1, RC ECO:0000313|Proteomes:UP000044872}; RA Wang D.B., Wang M.; RL Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CVQP01000008; CRK53132.1; -; Genomic_DNA. DR RefSeq; WP_050066156.1; NZ_CVQP01000008.1. DR EnsemblBacteria; CRK53132; CRK53132; RHCRD62_50335. DR Proteomes; UP000044872; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 2. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000044872}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000044872}. FT DOMAIN 262 431 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 221 255 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 487 AA; 52670 MW; D9AAD43114FF6EC2 CRC64; MTKSDEMTDM SRADRGEPDF DRSGHDPSVG ELQLDDRSAL RRVAGLSTEL TDVTEVEYRQ LRLERVVLVG VWTSGTAAQA EASMTELAAL AETAGSEVLE GLVQRRDKPD AATYIGSGKA DELREVVLAT GADTVVCDGE LTPAQLTALE KVVKVKVIDR TALILDIFAQ HATSSEGKAQ VALAQMEYML PRLRGWGESM SRQAGGRAGS NGGVGLRGPG ETKIETDRRR IRERMAKLRR EIKGMKAARD TKRTRRLRSD TPSVAIVGYT NAGKSSLLNA LTGAGVLVQD ALFATLDPTT RKAEFPDGRQ YVLTDTVGFV RHLPTQLIEA FRSTLEEVAD ADLLLHVVDG SDPLPTEQIK AVREVIVDVL RESDAPPPPE LLVVNKIDAA DPVTLTQLRA LLTDAKFVSA HTGEGIEELR ATLAELVSPP ELEIEVLVPY SRGDLVARIH ADGRLLDSSH EADGTLVRAK VPPALAAALD EYRHSAV // ID A0A0K8J9G8_9FIRM Unreviewed; 598 AA. AC A0A0K8J9G8; DT 11-NOV-2015, integrated into UniProtKB/TrEMBL. DT 11-NOV-2015, sequence version 1. DT 07-JUN-2017, entry version 14. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=P22_0333 {ECO:0000313|EMBL:CUH94267.1}; OS Propionispora sp. 2/2-37. OC Bacteria; Firmicutes; Negativicutes; Selenomonadales; Sporomusaceae; OC Propionispora. OX NCBI_TaxID=1677858 {ECO:0000313|EMBL:CUH94267.1, ECO:0000313|Proteomes:UP000041641}; RN [1] {ECO:0000313|EMBL:CUH94267.1, ECO:0000313|Proteomes:UP000041641} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=2/2 {ECO:0000313|EMBL:CUH94267.1}; RA Jackson K.R., Lunt B.L., Fisher J.N.B., Gardner A.V., Bailey M.E., RA Deus L.M., Earl A.S., Gibby P.D., Hartmann K.A., Liu J.E., Manci A.M., RA Nielsen D.A., Solomon M.B., Breakwell D.P., Burnett S.H., Grose J.H.; RL Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CYSP01000001; CUH94267.1; -; Genomic_DNA. DR RefSeq; WP_054258458.1; NZ_CYSP01000001.1. DR EnsemblBacteria; CUH94267; CUH94267; P22_0333. DR Proteomes; UP000041641; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000041641}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000041641}. FT DOMAIN 377 542 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 598 AA; 66782 MW; B07C6C007D39FEA0 CRC64; MKEILGNISG IRHNTIERLK QLYNEIVPSG QPVSQKIVNT LAALTQEINR EIALYINRRG QIVALAVGDA HTVALPDIKE KRSANKLSGI RCIHTHPDGN SMLSSIDFAS LKEMRFDSMT AIGVREGTAV AASCGFISGF ADGIYKTEAV GPLALFEFIN LDHTALIQDI ERILCRQTTA NTQEEIEQAL LVGIENIRLW DVQDSLQELA QLAETAGAVV VGQTWQKRER PDSTFFVGKG KLREISLLCQ QCHANLILFD DELLPSQQRN IEQELGVKVL DRTALILDIF AQRARSHEGK LQVELAQLKY SLPRLSGQGL SLSRLGGGIG TRGPGETKLE VDRRRIRSRI STIEEEIDTI RAQRSLHRAK RQESRVPMVA LVGYTNAGKS TLLNRLTAAK VMVEDKLFAT LDPTTRRFPL NNGREILLTD TVGFIQKLPH QLIAAFRATL EEISYASLLL HVVDGSSTLY QEQSTAVMQV LQELQLRDKP LLTVFNKIDK IDNSHVVERL LREENSIAVS ALNNTGIDTL VETIESFFNK QTVDTELSIP YNDSGIISHL YQSAIVYHID YREDAIYVKA SLSRELRNRY GSYTTGED // ID A0A0K8P7C3_IDESA Unreviewed; 434 AA. AC A0A0K8P7C3; DT 11-NOV-2015, integrated into UniProtKB/TrEMBL. DT 11-NOV-2015, sequence version 1. DT 12-APR-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=ISF6_4872 {ECO:0000313|EMBL:GAP38414.1}; OS Ideonella sakaiensis (strain 201-F6). OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Ideonella. OX NCBI_TaxID=1547922 {ECO:0000313|EMBL:GAP38414.1, ECO:0000313|Proteomes:UP000037660}; RN [1] {ECO:0000313|Proteomes:UP000037660} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=201-F6 {ECO:0000313|Proteomes:UP000037660}; RA Yoshida S., Hiraga K., Takehana T., Taniguchi I., Yamaji H., Maeda Y., RA Toyohara K., Miyamoto K., Kimura Y., Oda K.; RT "Discovery of a poly(ethylene terephthalate assimilation."; RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:GAP38414.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BBYR01000076; GAP38414.1; -; Genomic_DNA. DR EnsemblBacteria; GAP38414; GAP38414; ISF6_4872. DR Proteomes; UP000037660; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000037660}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000037660}. FT DOMAIN 209 383 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 434 AA; 47288 MW; 885E562EE2592DF8 CRC64; MSSHDPARPD PAAAPERPRA ILVGVHLGGR PGFDDSLDEL ALLAESAGDE PVARVVARRK APDPALFVGS GKADEIKALV EGHRAEAVLF DQALSPAQQR NLERHLGVAV ADRTMLILEI FGERAQSHEG KLQVELARLQ YLATRLVRRW SHLERQRGGI GGRGGPGEAQ IELDRRMIDE RIKSVKQRLD KVKRQRGTQR RSRERNQTFR ISLVGYTNAG KSTLFNALVK ARSYAADQLF ATLDTTTRQL YLEDVGRSVS LSDTVGFIRD LPHKLVEAFE ATLQEAADAD LLLHVVDAAG SDRPAQIAEV QRVLREIGAE RVPQLLVFNK ADRLDAAERP RVATDQLEIE PGLRVPRIFV SALEGEGLPA LRAALADAVR RRDEAAEAGS DPFDDDPRAA EAGAARDTRA GAADAGADDV RFDPARAATH SSSV // ID A0A0K8Q2Y9_9MICC Unreviewed; 172 AA. AC A0A0K8Q2Y9; DT 11-NOV-2015, integrated into UniProtKB/TrEMBL. DT 11-NOV-2015, sequence version 1. DT 11-MAY-2016, entry version 5. DE SubName: Full=GTPase HflX {ECO:0000313|EMBL:GAP54353.1}; GN ORFNames=AHiyo6_09180 {ECO:0000313|EMBL:GAP54353.1}; OS Arthrobacter sp. Hiyo6. OC Bacteria; Actinobacteria; Micrococcales; Micrococcaceae; Arthrobacter. OX NCBI_TaxID=1588022 {ECO:0000313|EMBL:GAP54353.1, ECO:0000313|Proteomes:UP000037466}; RN [1] {ECO:0000313|Proteomes:UP000037466} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Hiyo6 {ECO:0000313|Proteomes:UP000037466}; RA Hiraoka S., Machiyama A., Iwasaki W.; RT "Microbial genome analysis of tsunami-affected soil."; RL Submitted (FEB-2015) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:GAP54353.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BBUE01000064; GAP54353.1; -; Genomic_DNA. DR EnsemblBacteria; GAP54353; GAP54353; AHiyo6_09180. DR Proteomes; UP000037466; Unassembled WGS sequence. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF13167; GTP-bdg_N; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000037466}; KW Reference proteome {ECO:0000313|Proteomes:UP000037466}. FT DOMAIN 91 172 GTP-bdg_N. {ECO:0000259|Pfam:PF13167}. SQ SEQUENCE 172 AA; 18480 MW; 3613F5307315D792 CRC64; MSKDVPAHKA VPASGESRGV LGAAQAISRQ DSEHSSYDGD QQDLEERRAL RRTAGLSTEL EDVTEVEYRQ LRLERVVLAG LWSEGTLADA ENSLRELAAL AETAGSEVLD GLVQRRAKPD PGTFLGSGKA LELKDIVMST GADTVVVDAE LAPSQRRGLE DIVKVKVIDR TA // ID A0A0K9EVD2_9ACTO Unreviewed; 492 AA. AC A0A0K9EVD2; DT 11-NOV-2015, integrated into UniProtKB/TrEMBL. DT 11-NOV-2015, sequence version 1. DT 07-JUN-2017, entry version 12. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=ACU19_00325 {ECO:0000313|EMBL:KMY24083.1}, GN ACU21_00020 {ECO:0000313|EMBL:OCA96344.1}; OS Actinobaculum suis. OC Bacteria; Actinobacteria; Actinomycetales; Actinomycetaceae; OC Actinobaculum. OX NCBI_TaxID=1657 {ECO:0000313|EMBL:KMY24083.1, ECO:0000313|Proteomes:UP000037036}; RN [1] {ECO:0000313|Proteomes:UP000037036} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=U311 {ECO:0000313|Proteomes:UP000037036}; RA Moreno L.Z., Amigo C.R., Gobbi D.S., Ferreira T.S., Santos A.P., RA Moreno A.M.; RT "Draft genome sequences of Brazilian Actinobaculum suis isolated from RT urine and preputial swab."; RL Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:KMY24083.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=U311 {ECO:0000313|EMBL:KMY24083.1}; RA Hoefler B.C., Straight P.D.; RL Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases. RN [3] {ECO:0000313|EMBL:OCA96344.1, ECO:0000313|Proteomes:UP000093494} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C1-9-1 {ECO:0000313|EMBL:OCA96344.1, RC ECO:0000313|Proteomes:UP000093494}; RA Florea S., Webb J.S., Jaromczyk J., Schardl C.L.; RL Submitted (JUL-2016) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KMY24083.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LFUS01000002; KMY24083.1; -; Genomic_DNA. DR EMBL; MASY01000001; OCA96344.1; -; Genomic_DNA. DR RefSeq; WP_049618802.1; NZ_MASY01000001.1. DR EnsemblBacteria; KMY24083; KMY24083; ACU19_00325. DR EnsemblBacteria; OCA96344; OCA96344; ACU21_00020. DR PATRIC; fig|1657.3.peg.706; -. DR Proteomes; UP000037036; Unassembled WGS sequence. DR Proteomes; UP000093494; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000037036}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000037036}. FT DOMAIN 261 427 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 492 AA; 54273 MW; 01D2C1DBE0444A4D CRC64; MAGTVDLSSL EGTSLQETAE ERWAWSGDTL EREQRQKFQR VSGVHRDLSE DEALELEYRQ VRLERVVLVG IYEFSREEAE ESLRELAALA HTAGSQVLEG VLQRRDTPDK ATFLGKGKAH ELAELVASVG ADTVIVDSEL APSQRRGLED IVDVKVVDRT AVVLDIFARH AKSKEGKAQV ELAQLEYLLP RLRGWGESMS RQAGGQAAGG AGIGSRGPGE TQLELDRRRI RFRMAKLRRD IKKMKPARDT RRAERERTGI PSVVIVGYTN AGKSSLLNRL TGAGVLVDNL LFATLDPTVR RARTATDREF TLSDTVGFVR NLPTQLVEAF RSTLEEVGSA DVLLHAVDSS HSDPVGQIRA VHEVLETVPG AREVPELMVF TKKDLADPVD LAALETRYPD SVAVSALTGE GLEELREKLD EILPRPSHKL EAIVPFDRGE LVSLIYERGE LLAPVEYRAT GTYVHALVPE ELAAEFSPAW QEAAQEDQVS HA // ID A0A0K9GE73_9BACI Unreviewed; 416 AA. AC A0A0K9GE73; DT 11-NOV-2015, integrated into UniProtKB/TrEMBL. DT 11-NOV-2015, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=AC622_11530 {ECO:0000313|EMBL:KMY44776.1}; OS Bacillus sp. FJAT-27916. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus. OX NCBI_TaxID=1679169 {ECO:0000313|EMBL:KMY44776.1, ECO:0000313|Proteomes:UP000036953}; RN [1] {ECO:0000313|Proteomes:UP000036953} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=FJAT-27916 {ECO:0000313|Proteomes:UP000036953}; RA Liu B., Wang J., Zhu Y., Liu G., Chen Q., Chen Z., Che J., Ge C., RA Shi H., Pan Z., Liu X.; RT "Genome sequencing project for genomic taxonomy and phylogenomics of RT Bacillus-like bacteria."; RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KMY44776.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LFZV01000001; KMY44776.1; -; Genomic_DNA. DR RefSeq; WP_049671196.1; NZ_LFZV01000001.1. DR EnsemblBacteria; KMY44776; KMY44776; AC622_11530. DR PATRIC; fig|1679169.3.peg.2471; -. DR Proteomes; UP000036953; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000036953}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000036953}. FT DOMAIN 198 360 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 157 191 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 416 AA; 47202 MW; AC136B3656911F89 CRC64; MEETYEKAIL VGCQREGVED ERFQYSMDEL ESLTETAGGK ALVTISQKRV KPHPATYIGK GKVDELIPLV EELEPDVVIF NDELSPSQIR NLGKELGVRI VDRTQLILDI FAQRARSKEG QMQVELAQLQ YMLPRLAGQG TELSRLGGGI GTRGPGETKL ESDRRHIRRR IDEIKRQLEA VVKHRERYRA RRKRNNRFQM ALAGYTNAGK STLFNQLSEA DSYEENQLFA TLDPMTRECM LPSGYKILIS DTVGFIQDLP TSLVAAFRST LEEVTEADAI MHVVDSSHPD AFHHEETVQK IIKDLGAEEI PQLIVYNKKD IADPGFVPTS REKSIHISAR KEKDIHILLA EMEKMVESFM EPYAVMIPAR EGKIISRLQE ETIVKSREFN EANETYAIEG LALTDHAIMS VIKNYE // ID A0A0K9GNR6_9BACI Unreviewed; 422 AA. AC A0A0K9GNR6; DT 11-NOV-2015, integrated into UniProtKB/TrEMBL. DT 11-NOV-2015, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=AC625_01065 {ECO:0000313|EMBL:KMY48295.1}; OS Bacillus sp. FJAT-27997. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus. OX NCBI_TaxID=1679170 {ECO:0000313|EMBL:KMY48295.1, ECO:0000313|Proteomes:UP000037146}; RN [1] {ECO:0000313|Proteomes:UP000037146} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=FJAT-27997 {ECO:0000313|Proteomes:UP000037146}; RA Liu B., Wang J., Zhu Y., Liu G., Chen Q., Chen Z., Che J., Ge C., RA Shi H., Pan Z., Liu X.; RT "Genome sequencing project for genomic taxonomy and phylogenomics of RT Bacillus-like bacteria."; RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KMY48295.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LFZW01000001; KMY48295.1; -; Genomic_DNA. DR RefSeq; WP_049679614.1; NZ_LFZW01000001.1. DR EnsemblBacteria; KMY48295; KMY48295; AC625_01065. DR PATRIC; fig|1679170.3.peg.196; -. DR Proteomes; UP000037146; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000037146}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000037146}. FT DOMAIN 198 366 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 157 184 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 422 AA; 48155 MW; 79D164D4ECDC6313 CRC64; MEELQQKAVL VGVNINNHRD FAYSMEELAN LAEACGVEVV GEMTQNLQRV NSSHYIGSGK VDEVKTLVEY SEGNLVIFND ELSPSQIRNL ERDLDCKVID RTILILDIFA DRAKTREAQL QVEVAELQYM LPRLIGLRES LGRQSGGVGT KNRGVGEKKL ELDRRRIEEK INVLNKELET LVAHRKTQRK QRKKNAIPVV SLVGYTNAGK STIMNALVEK FHTSTEKQVF EKDMLFATLE TSVRNIPLPD NKEFLLTDTV GFVSKLPHHL VKAFRSTLEE VAEADLLIHV VDFSNANYEQ LIEITHETLK AIGIENIPTV YAYNKADLTE MEIPQVRADS VYLSAKQRIG VDELIEKIRE NIFTDYVRCE LLIPYDQGQI ISYFNEHAQI LETEYEEEGT KIKVECKQSD CEKYRTFVVN ES // ID A0A0K9JSH1_9BURK Unreviewed; 445 AA. AC A0A0K9JSH1; DT 11-NOV-2015, integrated into UniProtKB/TrEMBL. DT 11-NOV-2015, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=BUMB_03765 {ECO:0000313|EMBL:KMY86480.1}; OS Candidatus Paraburkholderia calva. OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Paraburkholderia. OX NCBI_TaxID=242161 {ECO:0000313|EMBL:KMY86480.1, ECO:0000313|Proteomes:UP000053570}; RN [1] {ECO:0000313|Proteomes:UP000053570} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=UZHbot6 {ECO:0000313|Proteomes:UP000053570}; RA Carlier A., Eberl L., Pinto-Carbo M.; RT "Comparative genomics of Burkholderia leaf nodule symbionts."; RL Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KMY86480.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LFLF01000014; KMY86480.1; -; Genomic_DNA. DR EnsemblBacteria; KMY86480; KMY86480; BUMB_03765. DR PATRIC; fig|242161.4.peg.1299; -. DR Proteomes; UP000053570; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000053570}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000053570}. FT DOMAIN 215 386 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 181 208 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 445 AA; 49151 MW; B0CDD220C525D3DD CRC64; MRPVGKKKRT LSNPPVASKP KHTNLINAAL VGIDFGKIDF EASLEELSLL AQSAGAHPAV TLTGRRSSPD AKMFIGSGKV EELRLQCEAN DVELVIFNHA LAPAQQRNLE VALNRRVVDR TSLILDIFAQ RARSHEGKLQ VELAQLQYLS TRLIRAWTHL ERQKGGIGLR GPGETQLETD RRLIGERIKA LKAKLDKLRR QHGTQRRQRT RNRAMSVSLV GYTNAGKSTL FNALTKAQAY AADQLFATLD TTSRRVYLGE ETGHIVMSDT VGFIRELPHQ LVAAFRATLE ETIHADLLLH VVDASSAVRL DQIDQVNDVL RSIGADSIRQ VLVFNKIDAV SELVARGEVV ERDEYGNISR VFLSARSGQG LDALRVAIVE IASAEEDEIE SLPSVLAELA EPHEVSEATN SLQSGSNPKR DTNARPQDQR SAEQRDDHTV PEHGH // ID A0A0K9NYH9_ZOSMR Unreviewed; 554 AA. AC A0A0K9NYH9; DT 11-NOV-2015, integrated into UniProtKB/TrEMBL. DT 11-NOV-2015, sequence version 1. DT 12-APR-2017, entry version 6. DE SubName: Full=GTPase HflX {ECO:0000313|EMBL:KMZ61753.1}; GN ORFNames=ZOSMA_4G00380 {ECO:0000313|EMBL:KMZ61753.1}; OS Zostera marina (Eelgrass). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Zosteraceae; Zostera. OX NCBI_TaxID=29655 {ECO:0000313|EMBL:KMZ61753.1, ECO:0000313|Proteomes:UP000036987}; RN [1] {ECO:0000313|EMBL:KMZ61753.1, ECO:0000313|Proteomes:UP000036987} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Finnish {ECO:0000313|EMBL:KMZ61753.1, RC ECO:0000313|Proteomes:UP000036987}; RA Olsen J.L., Schmutz J., Jenkins J., Grimwood J., Amirebrahimi M., RA Tice H., Chovatia M., Van de Peer Y., Rouze P., Verhelst B., RA Lin Y.-C.; RT "The genome of the seagrass Zostera marina."; RL Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KMZ61753.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LFYR01001430; KMZ61753.1; -; Genomic_DNA. DR Proteomes; UP000036987; Unassembled WGS sequence. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000036987}; KW Reference proteome {ECO:0000313|Proteomes:UP000036987}. FT DOMAIN 329 495 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 554 AA; 62084 MW; 7E6F0FC836C53AE4 CRC64; MNNCCSCFSY LPSTTKTTTA LVSTRNPNRR QWKSEIKPQT YHHLHLFPHP RWIHLVARAL QDATGLEVEQ IGSMEKKEDL VHRSEEETET ESEIEIESRW VKKKKVKKVL TEAVDEDEEY GRFKLKNGKE IFQEKTYLVG VECKSNVPNS FSIDESLKEL AQLADTAGLI VVGSTYQRLS TPNPRTYIGS GKVAEIKTSI NGLDVETVIF DDELSAGQLR NLEKAFGGSV RVCDRTSLIL DIFNQRAATH EASLQVSLAQ MEYQLPRLTK MWTHLERQAG GQVKGMGEKQ IEVDKRILRT QIGILKKELE SVRLHRKQYR NRRLSVPVPV VSLVGYTNAG KSTLLNSLTG ATVLAEDQLF ATLDPTTRRV QVDNGRGFLL TDTVGFIQKL PTTLVAAFRA TLEEISESSL LVHVVDISHP LAQLQMDAVD KVLSELDIAS IPKLIVWNKV DKVPNLSKIK DEAEEQQGVI CISARTGDGV KDFLNAIQEK LKDSLIHIEA LIPYDKGELL STIHEVGVVE GTEYVENGTL VKAHVPLPLA RLLVPLRQKV TQDR // ID A0A0K9Q2B6_ZOSMR Unreviewed; 600 AA. AC A0A0K9Q2B6; DT 11-NOV-2015, integrated into UniProtKB/TrEMBL. DT 11-NOV-2015, sequence version 1. DT 12-APR-2017, entry version 7. DE SubName: Full=GTPase HflX {ECO:0000313|EMBL:KMZ75446.1}; GN ORFNames=ZOSMA_114G00430 {ECO:0000313|EMBL:KMZ75446.1}; OS Zostera marina (Eelgrass). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Zosteraceae; Zostera. OX NCBI_TaxID=29655 {ECO:0000313|EMBL:KMZ75446.1, ECO:0000313|Proteomes:UP000036987}; RN [1] {ECO:0000313|EMBL:KMZ75446.1, ECO:0000313|Proteomes:UP000036987} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Finnish {ECO:0000313|EMBL:KMZ75446.1, RC ECO:0000313|Proteomes:UP000036987}; RA Olsen J.L., Schmutz J., Jenkins J., Grimwood J., Amirebrahimi M., RA Tice H., Chovatia M., Van de Peer Y., Rouze P., Verhelst B., RA Lin Y.-C.; RT "The genome of the seagrass Zostera marina."; RL Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KMZ75446.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LFYR01000167; KMZ75446.1; -; Genomic_DNA. DR Proteomes; UP000036987; Unassembled WGS sequence. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR CDD; cd01878; HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000036987}; KW Reference proteome {ECO:0000313|Proteomes:UP000036987}. FT DOMAIN 310 443 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 600 AA; 66926 MW; D55D2D84076EF8F0 CRC64; MFTALSRTKI TTATTFKSVY RNAKCSVYLS LTSPIPFFFS TSRWNKDQVS DGSGEEDDDV SAFMLHRNID GAAKLFVVQP RLRPEPLLQG KLSEALNLAS SLNDRRNGDN DQVEDDKNKI TPPHIIVQNP LARSKGRADK FFGTGTVENI KCHLNSIDSE DVLDGIFVNA ILSGVQQRNL ENAWGKPVLD RIALIIEIFN AHAQTKEAKL QSELAALMYR SNRLVRVRGP NGRLTFGMSG EAEVVSAKGK GSGGRGFLSG AGESELHLQR RRIHERREHL RHEIEEVRRT RALQRYARKR RGGSQGQGLT TVAVVGYTNA GKSTLVSALS KSNLYRDDRL FATVDPLLRS VILPSGRKTL LSDTVGFISE LPIQLVEAFH ATLEEVVDAD LLVHVLDSSS KSVDEQHSTV LQVLKQIGVS EEKINNMIEV WNKVDLLDKK PEEAPVTPDQ YIDDTGTNEF SSEDDKEVSR EQNMDEFSSN TVDIETDEYC SEVQNKRVGS TLSSCYPIED INKDASDHGD LDDNTESQFV GEPSSDKSLF PRPKYIERVK TSAVMGVGLH ELLRLIDHKL GSQKSLEKGI ISEIYDRKWR PSDAKDKKTL // ID A0A0K9QNM9_SPIOL Unreviewed; 305 AA. AC A0A0K9QNM9; DT 11-NOV-2015, integrated into UniProtKB/TrEMBL. DT 11-NOV-2015, sequence version 1. DT 15-MAR-2017, entry version 8. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:KNA08850.1}; DE Flags: Fragment; GN ORFNames=SOVF_159020 {ECO:0000313|EMBL:KNA08850.1}; OS Spinacia oleracea (Spinach). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae; OC Pentapetalae; Caryophyllales; Chenopodiaceae; Chenopodioideae; OC Anserineae; Spinacia. OX NCBI_TaxID=3562 {ECO:0000313|EMBL:KNA08850.1, ECO:0000313|Proteomes:UP000054095}; RN [1] {ECO:0000313|EMBL:KNA08850.1, ECO:0000313|Proteomes:UP000054095} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Viroflay {ECO:0000313|Proteomes:UP000054095}; RC TISSUE=Leaf {ECO:0000313|EMBL:KNA08850.1}; RX PubMed=24352233; DOI=10.1038/nature12817; RA Dohm J.C., Minoche A.E., Holtgrawe D., Capella-Gutierrez S., RA Zakrzewski F., Tafer H., Rupp O., Sorensen T.R., Stracke R., RA Reinhardt R., Goesmann A., Kraft T., Schulz B., Stadler P.F., RA Schmidt T., Gabaldon T., Lehrach H., Weisshaar B., Himmelbauer H.; RT "The genome of the recently domesticated crop plant sugar beet (Beta RT vulgaris)."; RL Nature 505:546-549(2014). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; KQ168785; KNA08850.1; -; Genomic_DNA. DR Proteomes; UP000054095; Unassembled WGS sequence. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000054095}; KW Reference proteome {ECO:0000313|Proteomes:UP000054095}. FT DOMAIN 158 247 GTP-bdg_N. {ECO:0000259|Pfam:PF13167}. FT DOMAIN 250 305 GTP-bdg_M. {ECO:0000259|Pfam:PF16360}. FT NON_TER 305 305 {ECO:0000313|EMBL:KNA08850.1}. SQ SEQUENCE 305 AA; 34356 MW; 406C59847021E918 CRC64; MSSSSFYWIV SGTNTSPFQV QRSQSHYLCP LQFQQFPFPK SISNLRNCLE SLQYKPPKSS VCVKSLQIDE GVDQFLSSVP PDEQETGEIE EIVSDFEDGF EDPVPFSVSG ERKEGQEEEE DEEDRRFKLR NGKEVLAEKA YLVGVEQKGV KVDSFGIEES LKELAQLADT AGLQVVGSTY QKLATPNPRT YIGSGKVSEM KSAIHALDVE TVIFDDELSP GQLRNLEKVF GKDVRVCDRT ALILDIFNQR AATHEAALQV ALAQMEYQLP RLTRMWSHLE RQAGGRVKGM GEKQIEVDKR ILRDQ // ID A0A0K9RQ73_SPIOL Unreviewed; 447 AA. AC A0A0K9RQ73; DT 11-NOV-2015, integrated into UniProtKB/TrEMBL. DT 11-NOV-2015, sequence version 1. DT 07-JUN-2017, entry version 12. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:KNA21608.1}; GN ORFNames=SOVF_041610 {ECO:0000313|EMBL:KNA21608.1}; OS Spinacia oleracea (Spinach). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae; OC Pentapetalae; Caryophyllales; Chenopodiaceae; Chenopodioideae; OC Anserineae; Spinacia. OX NCBI_TaxID=3562 {ECO:0000313|EMBL:KNA21608.1, ECO:0000313|Proteomes:UP000054095}; RN [1] {ECO:0000313|EMBL:KNA21608.1, ECO:0000313|Proteomes:UP000054095} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Viroflay {ECO:0000313|Proteomes:UP000054095}; RC TISSUE=Leaf {ECO:0000313|EMBL:KNA21608.1}; RX PubMed=24352233; DOI=10.1038/nature12817; RA Dohm J.C., Minoche A.E., Holtgrawe D., Capella-Gutierrez S., RA Zakrzewski F., Tafer H., Rupp O., Sorensen T.R., Stracke R., RA Reinhardt R., Goesmann A., Kraft T., Schulz B., Stadler P.F., RA Schmidt T., Gabaldon T., Lehrach H., Weisshaar B., Himmelbauer H.; RT "The genome of the recently domesticated crop plant sugar beet (Beta RT vulgaris)."; RL Nature 505:546-549(2014). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; KQ136976; KNA21608.1; -; Genomic_DNA. DR Proteomes; UP000054095; Unassembled WGS sequence. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR CDD; cd01878; HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 2. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 2. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 4: Predicted; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000054095}; KW Reference proteome {ECO:0000313|Proteomes:UP000054095}. FT DOMAIN 198 415 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 151 178 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 447 AA; 49842 MW; E928B31A2068FEB6 CRC64; MNSTVQLLDE RPMRHKAAKA IVRNKDTYFG PGTVENIKCH IHAIESQQGE MDAVFVNAIL SAIQQRNLER VWDKPVLDRV GLIIEIFNAH AYTKEAKLQA ELAAIMYKKS RLVRVRASDG RYTFGTKGEA EVVSARGRGS GGRGFISGAG ETELELQRRR ISERRKRLLA EIEEVRKTRA VQRAGRKKQG VLDAPGFATI AVVGYTNAGK STLVSALSDS DLYSDDRLFA TVDPRVRGVT LPSGRKVLLS DTVGFISDLP VQLIEAFHAT LEEVVEADLL VHVLDSSASN LEEQRQAVLD VLRQIGVSGK KIQDMVEVWN KIDIQRDTDT ETETGVSKFD DDSDYKFEED EDEVADDEDD QKLESCNGSK TEEEGPDSHP GPESQHIPLV KTSAVTRVGL QELLELIDEK LVQIDKEQLS SRKVQEKGEF DRKWRPTQAE NVSVAME // ID A0A0K9XD78_9ACTN Unreviewed; 499 AA. AC A0A0K9XD78; DT 11-NOV-2015, integrated into UniProtKB/TrEMBL. DT 11-NOV-2015, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=AC230_17345 {ECO:0000313|EMBL:KNB51335.1}; OS Streptomyces caatingaensis. OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae; OC Streptomyces. OX NCBI_TaxID=1678637 {ECO:0000313|EMBL:KNB51335.1, ECO:0000313|Proteomes:UP000037288}; RN [1] {ECO:0000313|Proteomes:UP000037288} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CMAA 1322 {ECO:0000313|Proteomes:UP000037288}; RA Santos S.N., Gacesa R., Taketani R.G., Long P.F., Melo I.S.; RT "Draft genome sequence of Streptomyces sp. CMAA 1322, a bacterium RT isolated from Caatinga biome, from dry forest semiarid of Brazil."; RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KNB51335.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LFXA01000010; KNB51335.1; -; Genomic_DNA. DR RefSeq; WP_049717164.1; NZ_LFXA01000010.1. DR EnsemblBacteria; KNB51335; KNB51335; AC230_17345. DR PATRIC; fig|1678637.3.peg.3740; -. DR Proteomes; UP000037288; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 2. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000313|EMBL:KNB51335.1}; KW Complete proteome {ECO:0000313|Proteomes:UP000037288}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900, KW ECO:0000313|EMBL:KNB51335.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000037288}. FT DOMAIN 279 444 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 499 AA; 54419 MW; 06F267A7F9F7E8BE CRC64; MTSTSSLPQD RPQDRQSLAE GLRADALMEE DVAWSHEIDG ERDGDQYDRS ERAALRRVAG LSTELEDVTE VEYRQLRLER VVLVGVWTSG TVQDAENSLA ELAALAETAG ALVLDGVIQR RDKPDPATYI GSGKAQELRD IVLETGADTV VCDGELSPGQ LIHLEDVVKV KVVDRTALIL DIFAQHAKSR EGKAQVSLAQ MQYMLPRLRG WGQSLSRQMG GGGSGSSGGG MATRGPGETK IETDRRRIRE KMAKMRREIA EMKTGRDLKR QERKRNKVPS VAIAGYTNAG KSSLLNRLTG AGVLVENALF ATLDPTVRRA ETPGGRLYTL ADTVGFVRHL PHHLVEAFRS TMEEVGDSDL ILHVVDGSHP APEEQLAAVR EVIRDVGATD VPEIVVVNKA DAADPLVLQR LLRVEKHSIA VSARTGEGID ELLALIDDRL PRPAVEVEAL VPYTHGSLTA RIHSDGEVLS EEHTAEGTLV KARVHEELAA ELRKFVQAV // ID A0A0K9Y0L5_9FLAO Unreviewed; 409 AA. AC A0A0K9Y0L5; DT 11-NOV-2015, integrated into UniProtKB/TrEMBL. DT 11-NOV-2015, sequence version 1. DT 05-JUL-2017, entry version 12. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=AC804_05265 {ECO:0000313|EMBL:KNB62272.1}; OS Chryseobacterium sp. Hurlbut01. OC Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales; OC Flavobacteriaceae; Chryseobacterium. OX NCBI_TaxID=1681828 {ECO:0000313|EMBL:KNB62272.1, ECO:0000313|Proteomes:UP000036769}; RN [1] {ECO:0000313|Proteomes:UP000036769} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Hurlbut01 {ECO:0000313|Proteomes:UP000036769}; RA Couger M.B., Youseff N., Elshahed M., French D., Hoff W.; RT "Draft Genome Sequence of the Environmental Isolate Chryseobacterium RT sp. Hurlbut 01."; RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KNB62272.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LGIP01000003; KNB62272.1; -; Genomic_DNA. DR RefSeq; WP_050378010.1; NZ_LGIP01000003.1. DR EnsemblBacteria; KNB62272; KNB62272; AC804_05265. DR PATRIC; fig|1681828.3.peg.3269; -. DR Proteomes; UP000036769; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000036769}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000036769}. FT DOMAIN 200 384 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 409 AA; 47329 MW; C3ED90662014CE3B CRC64; MLEKKQHNYE KAVLVGVVTQ NQDEDKLQEY MDELEFLAFT AGATVDRRFT QKLTQPDSKT FVGSGKAQEI KEYVKENEIG TIIFDDELSP SQLKNLEKEI EVKILDRTNL ILDIFAQRAQ TSYARTQVEL AQYQYLLPRL SKMWSHLDKQ KGGIGMRGPG ETEIETDRRI IRDRISLLKD KLKVIDKQMA TQRNNRGKVV RAALVGYTNV GKSTLMNAIS KSDVFAENKL FATLDTTVRK VVIGNLPFLL TDTVGFIRKL PTQLVESFKS TLDEVREADL LIHVVDISHE SFEDHIESVN QILMEINAHQ KPMIMVFNKI DDFSYEKKDE DDLTPGSHKN ISLEEWKKTW MAKSKHPAVF ISALTRENFP EMKRLVYDEV MKIHISRFPY NDFLFEYFDD EEEGSEKQD // ID A0A0L0BH07_9MICC Unreviewed; 535 AA. AC A0A0L0BH07; DT 11-NOV-2015, integrated into UniProtKB/TrEMBL. DT 11-NOV-2015, sequence version 1. DT 07-JUN-2017, entry version 13. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=AC792_07900 {ECO:0000313|EMBL:KNC19188.1}; OS Arthrobacter sp. RIT-PI-e. OC Bacteria; Actinobacteria; Micrococcales; Micrococcaceae; Arthrobacter. OX NCBI_TaxID=1681197 {ECO:0000313|EMBL:KNC19188.1, ECO:0000313|Proteomes:UP000053253}; RN [1] {ECO:0000313|Proteomes:UP000053253} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=RIT-PI-e {ECO:0000313|Proteomes:UP000053253}; RA Tran P.N., Lee Y.P., Gan H.M., Savka M.A.; RT "Whole genome sequencing of endophytes isolated from poison ivy RT (Toxicodendron radicans)."; RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KNC19188.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LGIU01000056; KNC19188.1; -; Genomic_DNA. DR RefSeq; WP_049830004.1; NZ_LGIU01000056.1. DR EnsemblBacteria; KNC19188; KNC19188; AC792_07900. DR PATRIC; fig|1681197.3.peg.1272; -. DR Proteomes; UP000053253; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 2. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000053253}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000053253}. FT DOMAIN 314 479 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 535 AA; 57884 MW; 6FBCCB444C5CA461 CRC64; MTTNNGRPTG PDMGPEEIQA VIDRILASDE AASAKTAAPD HVPAAEPAGG ASDEAAPTER TWRSRALALS RDAQPSDSDG DQQDLAERRA LRRVAGLSTE LEDVTEVEYR QLRLERVVLA GLWSEGTAQD AENSLQELAA LAETAGSEVL DGMVQRRLKP DPGTFLGSGK AQELKSVVQA TGADTVIVDS ELSPSQRRGL EDIVKVKVID RTALILDIFA QHAKSREGKA QVELAQLEYL LPRLRGWGES MSRQAGGQVG SASAGMGSRG PGETKIELDR RKIRTRMAKL RREIAGMKPA RDTKRSNRRR NQVPSVAIAG YTNAGKSSLL NRLTDAGVLV ENALFATLDP TIRKAETPDG IGYTLADTVG FVRSLPTQLV EAFRSTLEEV ADADLILHVV DASHPDPEGQ IAAVRSVLTD VDARKVPEII VLNKADAADP FVIERLRQRE PRTVVVSART GAGLTELRQL ISTSIPRPGV KLDLMVPYAH GEVVSRLHEE DAEILGIEHV GEGTRLEVMV REGLAAELEP YLRHE // ID A0A0L0BXE5_LUCCU Unreviewed; 541 AA. AC A0A0L0BXE5; DT 11-NOV-2015, integrated into UniProtKB/TrEMBL. DT 11-NOV-2015, sequence version 1. DT 07-JUN-2017, entry version 9. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:KNC24666.1}; GN ORFNames=FF38_13565 {ECO:0000313|EMBL:KNC24666.1}; OS Lucilia cuprina (Green bottle fly) (Australian sheep blowfly). OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; OC Pterygota; Neoptera; Holometabola; Diptera; Brachycera; Muscomorpha; OC Oestroidea; Calliphoridae; Luciliinae; Lucilia. OX NCBI_TaxID=7375 {ECO:0000313|EMBL:KNC24666.1, ECO:0000313|Proteomes:UP000037069}; RN [1] {ECO:0000313|EMBL:KNC24666.1, ECO:0000313|Proteomes:UP000037069} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=LS {ECO:0000313|EMBL:KNC24666.1, RC ECO:0000313|Proteomes:UP000037069}; RC TISSUE=Full body {ECO:0000313|EMBL:KNC24666.1}; RX PubMed=26108605; DOI=10.1038/ncomms8344; RA Anstead C.A., Korhonen P.K., Young N.D., Hall R.S., Jex A.R., RA Murali S.C., Hughes D.S., Lee S.F., Perry T., Stroehlein A.J., RA Ansell B.R., Breugelmans B., Hofmann A., Qu J., Dugan S., Lee S.L., RA Chao H., Dinh H., Han Y., Doddapaneni H.V., Worley K.C., Muzny D.M., RA Ioannidis P., Waterhouse R.M., Zdobnov E.M., James P.J., Bagnall N.H., RA Kotze A.C., Gibbs R.A., Richards S., Batterham P., Gasser R.B.; RT "Lucilia cuprina genome unlocks parasitic fly biology to underpin RT future interventions."; RL Nat. Commun. 6:7344-7344(2015). CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KNC24666.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JRES01001197; KNC24666.1; -; Genomic_DNA. DR EnsemblMetazoa; KNC24666; KNC24666; FF38_13565. DR OMA; MDTVGFM; -. DR Proteomes; UP000037069; Unassembled WGS sequence. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR CDD; cd01878; HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 4: Predicted; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000037069}; KW Reference proteome {ECO:0000313|Proteomes:UP000037069}. FT DOMAIN 310 482 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 276 303 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 541 AA; 61599 MW; A25AFB6FE764111A CRC64; MFLNLVAKRT SSSLFVRCLS LNSFSLSTIL KHFPQQQQQH QQQQRFKYTQ NKGVKGLRNR KHQYEAKEKQ ENAEEMDHSD EFQPSLNLED SEYDLVANGA MNVTRKSTQP QNVLVIQPYV KWGPKRATIT TPDDQLEEAK ALIHSINNWS VALAIKVPLE SLERKALFGK GKMEEIKNLV QELRQAKSHN QQPLTCIFVS KGSLSFAQKA LLEATFHLPV MDRYSVVIQI LRLHATSAEA RLQVAMAEIP YIWSQAKEAN TSKSTKLGYS LTDTQREILK TREKKLKMEL ERIRNHRKLL RNKRKQHNYP IVAVVGYTNA GKTSLIKALT QEQTIQPKDQ LFATLDVTAH AGRLPCNLEV IYMDTVGFMS DLPTGLIECF VATLEDAMLA DVILHVQDVS HACYEAQKQH VEMTLKSLTQ NMCWETEDKV NLPPIISVGN KIDLLHSKDV INSFSGLKVS AKKQQGLSEL MSEIENHILT TTNRRKLTIR VPNGGIEMSW LYKNAAVVNM KADSEDSQNL LMDIVIKESV LQQFKKQFCQ K // ID A0A0L0GQ59_9ENTR Unreviewed; 426 AA. AC A0A0L0GQ59; DT 11-NOV-2015, integrated into UniProtKB/TrEMBL. DT 11-NOV-2015, sequence version 1. DT 30-AUG-2017, entry version 18. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=GM31_20735 {ECO:0000313|EMBL:KNC93178.1}; OS Trabulsiella odontotermitis. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; OC Enterobacteriaceae; Trabulsiella. OX NCBI_TaxID=379893 {ECO:0000313|EMBL:KNC93178.1, ECO:0000313|Proteomes:UP000037393}; RN [1] {ECO:0000313|EMBL:KNC93178.1, ECO:0000313|Proteomes:UP000037393} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=12 {ECO:0000313|EMBL:KNC93178.1, RC ECO:0000313|Proteomes:UP000037393}; RX PubMed=26162887; RA Sapountzis P., Gruntjes T., Otani S., Estevez J., da Costa R.R., RA Plunkett G.3rd., Perna N.T., Poulsen M.; RT "The Enterobacterium Trabulsiella odontotermitis Presents Novel RT Adaptations Related to Its Association with Fungus-Growing Termites."; RL Appl. Environ. Microbiol. 81:6577-6588(2015). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KNC93178.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JNGI01000062; KNC93178.1; -; Genomic_DNA. DR RefSeq; WP_049848591.1; NZ_JNGI01000062.1. DR EnsemblBacteria; KNC93178; KNC93178; GM31_20735. DR PATRIC; fig|379893.3.peg.94; -. DR Proteomes; UP000037393; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000037393}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}. FT DOMAIN 198 365 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 426 AA; 48084 MW; CCCAF8C3297C023F CRC64; MFDRYDAGEQ AVLVHIYFSQ DKDMEDLQEF ESLVSSAGVE AMQVITGSRK APHPKYFVGE GKAVEIADAV KATGASVVLF DHALTPAQER NLERLCECRV IDRTGLILDI FAQRARTHEG KLQVELAQLR HLATRLVRGW THLERQKGGI GLRGPGETQL ETDRRLLRNR IMQILSRLEK VEKQREQGRR SRTKADIPTV SLVGYTNAGK STLFNQITEA QVYAADQLFA TLDPTLRRID VADVGETVLA DTVGFIRHLP HDLVAAFKAT LQETRQATLL LHVIDAADVR VQENIDAVNT VLEEIDAHEI PTLLVMNKID ALENFEPRID RDDENKPIRV WLSAQTGVGV PLLFQALTER LSGQIAQHTL RLPPKEGRLR SRFYQLQAIE KEWLEDDGSV GIQVRMPVVD WRRLCKQEPA LADYIV // ID A0A0L0K4Z7_9ACTN Unreviewed; 497 AA. AC A0A0L0K4Z7; DT 11-NOV-2015, integrated into UniProtKB/TrEMBL. DT 11-NOV-2015, sequence version 1. DT 05-JUL-2017, entry version 15. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:GAQ57470.1}; GN ORFNames=a10_07340 {ECO:0000313|EMBL:GAQ57470.1}, GN IQ63_22500 {ECO:0000313|EMBL:KND32916.1}, GN Saa2_06968 {ECO:0000313|EMBL:GAV44009.1}; OS Streptomyces acidiscabies. OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae; OC Streptomyces. OX NCBI_TaxID=42234 {ECO:0000313|EMBL:KND32916.1, ECO:0000313|Proteomes:UP000037151}; RN [1] {ECO:0000313|EMBL:KND32916.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=NCPPB 4445 {ECO:0000313|EMBL:KND32916.1}; RA Chen X.-L., Norrbom A., Zhu C.-D.; RT "A systematic study of Ichneumonosoma Meijere, Pelmatops Enderlein, RT Pseudopelmatops Shiraki and Soita Walker (Diptera: Tephritidae)."; RL Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Proteomes:UP000037151} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NCPPB 4445 {ECO:0000313|Proteomes:UP000037151}; RA Harrison J., Sapp M., Thwaites R., Studholme D.J.; RT "Genome sequencing of plant-pathogenic Streptomyces species."; RL Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases. RN [3] {ECO:0000313|EMBL:GAV44009.1, ECO:0000313|Proteomes:UP000058287, ECO:0000313|Proteomes:UP000186713} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=a10 {ECO:0000313|Proteomes:UP000058287}, RC a2 {ECO:0000313|Proteomes:UP000186713}, and RC A2 {ECO:0000313|EMBL:GAV44009.1}; RG Cross-ministerial Strategic Innovation Promotion Program (SIP) consortium; RA Tomihama T., Ikenaga M., Sakai M., Okubo T., Ikeda S.; RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases. RN [4] {ECO:0000313|EMBL:GAQ57470.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=A10 {ECO:0000313|EMBL:GAQ57470.1}; RA Tomihama T., Nishi Y., Sakai M., Ikenaga M., Okubo T., Ikeda S.; RT "Draft Genome Sequences of Streptomyces scabiei S58, Streptomyces RT turgidiscabies T45, and Streptomyces acidiscabies a10, the Pathogens RT of Potato Common Scab, Isolated in Japan."; RL Genome Announc. 4:e00062-16(2016). RN [5] {ECO:0000313|Proteomes:UP000058287} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=a10 {ECO:0000313|Proteomes:UP000058287}; RA Tomihama T., Ikenaga M., Sakai M., Okubo T., Ikeda S.; RT "Draft genome of pathogenic Streptomyces sp. in Japan."; RL Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases. RN [6] {ECO:0000313|EMBL:GAV44009.1, ECO:0000313|Proteomes:UP000186713} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=A2 {ECO:0000313|EMBL:GAV44009.1}, and RC a2 {ECO:0000313|Proteomes:UP000186713}; RA Tomihama T., Ikenaga M., Sakai M., Okubo T., Ikeda S.; RT "Draft genome of pathogenic Streptomyces sp. in Japan."; RL Submitted (JAN-2017) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KND32916.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BCMK01000086; GAQ57470.1; -; Genomic_DNA. DR EMBL; BCML01000077; GAV44009.1; -; Genomic_DNA. DR EMBL; JPPY01000132; KND32916.1; -; Genomic_DNA. DR RefSeq; WP_010358935.1; NZ_LYDV01000783.1. DR EnsemblBacteria; GAQ57470; GAQ57470; a10_07340. DR EnsemblBacteria; KND32916; KND32916; IQ63_22500. DR PATRIC; fig|42234.21.peg.4654; -. DR Proteomes; UP000037151; Unassembled WGS sequence. DR Proteomes; UP000058287; Unassembled WGS sequence. DR Proteomes; UP000186713; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000313|EMBL:KND32916.1}; KW Complete proteome {ECO:0000313|Proteomes:UP000037151}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900, KW ECO:0000313|EMBL:KND32916.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000037151}. FT DOMAIN 275 440 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 497 AA; 54247 MW; 81A6FB9F77BAAF98 CRC64; MTSSSSPSQD TKRLAQDYPD GLRADALMEE DVAWSHTIDE ERDGDQFDRS ERAALRRVAG LSTELEDVTE VEYRQLRLER VVLVGVWTTG TARDADNSLA ELAALAETAG ALVLDGVVQR RDKPDPATFI GSGKAQELRD MVLESGADTV ICDGELSPGQ LIALEDVVKV KVIDRTALIL DIFAQHAKSR EGKAQVALAQ MQYMLPRLRG WGQSLSRQMG GGKGGGLATR GPGETKIETD RRRIREKMAK MRREIAEMKT GREIKRQERK RHKVPSVAIA GYTNAGKSSL LNRLTGAGVL VENALFATLD PTVRRAETPS GRLYTLVDTV GFVRHLPHHL VEAFRSTMEE VGESDLILHV VDGSHPAPEE QLAAVREVVR DVGATGVPEI VVINKADAAD PLTLQRLLRI EKRSIAVSAR TGEGIAELLA LIDEELPRPS VEIEALVPYT HGKLIARAHT EGEVLSEEHL AEGTLLKARV HEELAADLAP YVPAQAV // ID A0A0L0M1X6_9BURK Unreviewed; 405 AA. AC A0A0L0M1X6; DT 11-NOV-2015, integrated into UniProtKB/TrEMBL. DT 11-NOV-2015, sequence version 1. DT 05-JUL-2017, entry version 13. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=BPUN_0201 {ECO:0000313|EMBL:KND56642.1}; OS Candidatus Paraburkholderia kirkii. OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Paraburkholderia. OX NCBI_TaxID=198822 {ECO:0000313|EMBL:KND56642.1, ECO:0000313|Proteomes:UP000053677}; RN [1] {ECO:0000313|Proteomes:UP000053677} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=UZHbot2 {ECO:0000313|Proteomes:UP000053677}; RA Carlier A., Eberl L., Pinto-Carbo M.; RT "Comparative genomics of Burkholderia leaf nodule symbionts."; RL Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KND56642.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LFKV01000001; KND56642.1; -; Genomic_DNA. DR EnsemblBacteria; KND56642; KND56642; BPUN_0201. DR PATRIC; fig|198822.17.peg.205; -. DR Proteomes; UP000053677; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000053677}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000053677}. FT DOMAIN 191 362 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 157 184 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 405 AA; 44326 MW; 0AEAACDCB67C0B80 CRC64; MINAALVGID FGKIDFEASL EELSLLAQSA GAHPAVTLTG RRSSPDAKMF IGSGKVEELR LQCEANNVEL VIFNHALAPA QQRNLEMALN RRVVDRTSLI LDIFAQRARS HEGKLQVELA QLQYLSTRLI RAWTHLERQK GGIGLRGPGE TQLETDRRLI GERIKALKTR LDKLRRQHGT QRRQRARNRT MSVSLVGYTN AGKSTLFNAL TKAQAYAADQ LFATLDTTSR RVFLGEEAGH VVVSDTVGFI RELPHQLVAA FRATLEETIH ADLLLHVVDA SSAVRLDQID QVNEVLRGIG ADSIRQILVL NKIDAVPELA ARGEAVERDE YGNISRVFLS ARTGQGLDAL RAAIAETAAA DTEETDAGLP SVLAGFAELH ETSEAKQSTQ SGSNALHDTH AQLED // ID A0A0L0MFC7_9BURK Unreviewed; 418 AA. AC A0A0L0MFC7; DT 11-NOV-2015, integrated into UniProtKB/TrEMBL. DT 11-NOV-2015, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=BVER_02848 {ECO:0000313|EMBL:KND61006.1}; OS Candidatus Burkholderia verschuerenii. OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Burkholderia. OX NCBI_TaxID=242163 {ECO:0000313|EMBL:KND61006.1, ECO:0000313|Proteomes:UP000036959}; RN [1] {ECO:0000313|Proteomes:UP000036959} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=UZHbot4 {ECO:0000313|Proteomes:UP000036959}; RA Carlier A., Eberl L., Pinto-Carbo M.; RT "Comparative genomics of Burkholderia leaf nodule symbionts."; RL Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KND61006.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LFJJ01000036; KND61006.1; -; Genomic_DNA. DR RefSeq; WP_050453089.1; NZ_LFJJ01000036.1. DR EnsemblBacteria; KND61006; KND61006; BVER_02848. DR PATRIC; fig|242163.4.peg.4724; -. DR Proteomes; UP000036959; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000036959}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000036959}. FT DOMAIN 191 362 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 157 184 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 418 AA; 46090 MW; CA52DD8A4499C493 CRC64; MINAALVGID FGKIDFEASL EELSLLAQSA GAHPVVTLTG RRSSPDAKMF IGSGKVEELR LQCEANDVEL VIFNHALAPA QQRNLEVALN RRVVDRTSLI LDIFAQRARS HEGKLQVELA QLQYLSTRLI RAWTHLERQK GGIGLRGPGE TQLETDRRLI GERIKALKAK LDKLRRQHGT QRRQRTRNRT MSVSLVGYTN AGKSTLFNAL TKAQAYAADQ LFATLDTTSR RVYLGEETGH IVMSDTVGFI RELPHQLVAA FRATLEETIH ADLLLHVVDA SSAVRLDQID QVNDVLRSIG ADSIRQVLVF NKIDAVPELA ARGEAIERDE YGNISRVFLS ARSGQGLDAL RAAIVEIASA EEGEIESLPS VLAEPHEVSE ATNPSQSGSN KERDTHAGPQ DQQPAEQRDD HKVPEHGH // ID A0A0L0QPU7_VIRPA Unreviewed; 411 AA. AC A0A0L0QPU7; DT 11-NOV-2015, integrated into UniProtKB/TrEMBL. DT 11-NOV-2015, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=AFK71_17845 {ECO:0000313|EMBL:KNE20253.1}; OS Virgibacillus pantothenticus. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Virgibacillus. OX NCBI_TaxID=1473 {ECO:0000313|EMBL:KNE20253.1, ECO:0000313|Proteomes:UP000036780}; RN [1] {ECO:0000313|Proteomes:UP000036780} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 26 {ECO:0000313|Proteomes:UP000036780}; RA Liu B., Wang J., Zhu Y., Liu G., Chen Q., Chen Z., Lan J., Che J., RA Ge C., Shi H., Pan Z., Liu X.; RT "Fjat-10053 dsm26."; RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KNE20253.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LGTO01000007; KNE20253.1; -; Genomic_DNA. DR RefSeq; WP_050352822.1; NZ_LGTO01000007.1. DR EnsemblBacteria; KNE20253; KNE20253; AFK71_17845. DR PATRIC; fig|1473.5.peg.2292; -. DR Proteomes; UP000036780; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000036780}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000036780}. FT DOMAIN 196 357 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 411 AA; 47001 MW; 2BD55955EFF80EB9 CRC64; MANEKVIIIA VKQQKQTNVH FESSLAELQS LSNTAGGDVV QIFTQNREKM NPATYLGSGK IEEIITSVQE NDVDLVIAND ELSPIQLRNL SIALGVRMID RSQLILDIFA QRARTKEGKL QVELAQLEYL LPRLRGQGTE LSRLGGGIGT RGPGETKLET DQRHIRRRIH DIKQRLQTVV KQREQYRKRR KTNDVVQIAI VGYTNAGKST LFNRLTNSDS LEEDQLFATL DPLTRQIQLP SGMKVLITDT VGFLQDLPTS LIAAFKSTLE EVTEADFLIH MVDGSHPDLN QQQDTVLRLL KELQADTIPM LTVYNKKDLF EQDVIPMNHP YMFMTAHREA DIQQLLRKVE NLLKAEWQFY SLSLLPDQGK LLQQLEQDTI IESKLFLEEK QVYKIKGYMR KDIPLNRLLE E // ID A0A0L0TM92_9BURK Unreviewed; 411 AA. AC A0A0L0TM92; DT 11-NOV-2015, integrated into UniProtKB/TrEMBL. DT 11-NOV-2015, sequence version 1. DT 07-JUN-2017, entry version 12. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=BCRE_0745 {ECO:0000313|EMBL:KNE75649.1}; OS Candidatus Burkholderia crenata. OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Burkholderia. OX NCBI_TaxID=1074049 {ECO:0000313|EMBL:KNE75649.1, ECO:0000313|Proteomes:UP000054148}; RN [1] {ECO:0000313|Proteomes:UP000054148} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=UZHbot9 {ECO:0000313|Proteomes:UP000054148}; RA Carlier A., Eberl L., Pinto-Carbo M.; RT "Comparative genomics of Burkholderia leaf nodule symbionts."; RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KNE75649.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LGTG01000331; KNE75649.1; -; Genomic_DNA. DR EnsemblBacteria; KNE75649; KNE75649; BCRE_0745. DR PATRIC; fig|1074049.7.peg.2438; -. DR Proteomes; UP000054148; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000054148}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000054148}. FT DOMAIN 191 362 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 157 184 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 411 AA; 45234 MW; E0F8A9E4A1AFD3F4 CRC64; MINAALVGVD FGKIDFDASL EELSLLAQSA GAHPAVTLTG RRSSPDAKMF VGSGKTEELR LACEANDVEL VICNHTLAPA QQRNLETALD RRVIDRTSLI LDIFAQRARS HEGKLQVELA QLQYLSTRLI RAWTHLERQK GGIGLRGPGE TQLETDRRLI GERIKALKAR LMKLRRQHGT QRRKRERNRT TSVSLVGYTN AGKSTLFNAL TKAQAYAADQ LFATLDTTSR QVYLSEEAGQ TVVSDTVGFI RDLPHQLIAA FRATLEETVQ ADLLLHVVDA SGMVRLDQID EVNKVLSSIG ADGIPQILVF NKIDAVPELA ARDDAVERDE YGNILHVFLS ARTGQGLDVL RAAIAEFAAS EPKDNNEYTE LPDGTIVPES MDSTSDDGIT LPEDHRSAEE SDDRKVPEHG H // ID A0A0L0WCQ7_CLOPU Unreviewed; 428 AA. AC A0A0L0WCQ7; DT 11-NOV-2015, integrated into UniProtKB/TrEMBL. DT 11-NOV-2015, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:KNF09252.1}; GN ORFNames=CLPU_3c00300 {ECO:0000313|EMBL:KNF09252.1}; OS Clostridium purinilyticum. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Gottschalkia. OX NCBI_TaxID=1503 {ECO:0000313|EMBL:KNF09252.1, ECO:0000313|Proteomes:UP000037267}; RN [1] {ECO:0000313|Proteomes:UP000037267} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 1384 {ECO:0000313|Proteomes:UP000037267}; RA Poehlein A., Schiel-Bengelsdorf B., Bengelsdorf F.R., Daniel R., RA Duerre P.; RT "Draft genome sequence of the purine-degrading Gottschalkia RT purinilyticum DSM 1384 (formerly Clostridium purinilyticum)."; RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KNF09252.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LGSS01000003; KNF09252.1; -; Genomic_DNA. DR RefSeq; WP_050354257.1; NZ_LGSS01000003.1. DR EnsemblBacteria; KNF09252; KNF09252; CLPU_3c00300. DR PATRIC; fig|1503.3.peg.1890; -. DR Proteomes; UP000037267; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000037267}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000037267}. FT DOMAIN 202 373 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 168 195 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 428 AA; 49234 MW; E730C5294EDFCDBD CRC64; MYNIQEKKEE RVLIVGVDTN KKYEINIESS MKELAELVKA AEGVVEASII QNRESIDSAY YIGTGKAQEI AIYCEELNID TVVFNNELTG AQIRNLEEII NRKIIDRTSL ILDIFAKRAT SKEGKLQVEL AQLKYRLPRL IGYRNYLSRA GAGIGTRGPG EQKLEIDRRH ILSRINDIER QLKELTNVRK IKRKKRENSN IPIVALVGYT NAGKSTLLNS IIREDNEYHE DKEVFAYDML FATLETTLRK SMLPNGQDFL ITDTVGFVSK LPTRLVEAFK GTLEEVKYAD LLLHVIDVTN EDINIQVKTT MSILKDLDVL DKPIITVFNK VDIDNNYSLE YDIKEPKVFI SAKTGHNLDR LLKMIQENLP NKYYKVDILV PYDKGELMSY LFDNTKVEKC EYVEKGTLVT TTLDSIDFNR YNEYVFKK // ID A0A0L1ICD2_PLAFA Unreviewed; 698 AA. AC A0A0L1ICD2; DT 11-NOV-2015, integrated into UniProtKB/TrEMBL. DT 11-NOV-2015, sequence version 1. DT 10-MAY-2017, entry version 9. DE SubName: Full=GTP-binding protein {ECO:0000313|EMBL:KNG77311.1}; GN ORFNames=PFMG_03331 {ECO:0000313|EMBL:KNG77311.1}; OS Plasmodium falciparum IGH-CR14. OC Eukaryota; Alveolata; Apicomplexa; Aconoidasida; Haemosporida; OC Plasmodiidae; Plasmodium; Plasmodium (Laverania). OX NCBI_TaxID=580059 {ECO:0000313|EMBL:KNG77311.1, ECO:0000313|Proteomes:UP000054562}; RN [1] {ECO:0000313|Proteomes:UP000054562} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=IGH-CR14 {ECO:0000313|Proteomes:UP000054562}; RG The Broad Institute Genome Sequencing Platform; RA Volkman S.K., Neafsey D.E., Dash A.P., Chitnis C.E., Hartl D.L., RA Young S.K., Zeng Q., Koehrsen M., Alvarado L., Berlin A., RA Borenstein D., Chapman S.B., Chen Z., Engels R., Freedman E., RA Gellesch M., Goldberg J., Griggs A., Gujja S., Heilman E.R., RA Heiman D.I., Howarth C., Jen D., Larson L., Mehta T., Neiman D., RA Park D., Pearson M., Roberts A., Saif S., Shea T., Shenoy N., Sisk P., RA Stolte C., Sykes S., Walk T., White J., Yandava C., Haas B., RA Henn M.R., Nusbaum C., Birren B.; RT "Annotation of Plasmodium falciparum IGH-CR14."; RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Proteomes:UP000054562} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=IGH-CR14 {ECO:0000313|Proteomes:UP000054562}; RG The Broad Institute Genome Sequencing Platform; RA Volkman S.K., Neafsey D.E., Dash A.P., Chitnis C.E., Hartl D.L., RA Young S.K., Kodira C.D., Zeng Q., Koehrsen M., Godfrey P., RA Alvarado L., Berlin A., Borenstein D., Chen Z., Engels R., RA Freedman E., Gellesch M., Goldberg J., Griggs A., Gujja S., Heiman D., RA Hepburn T., Howarth C., Jen D., Larson L., Lewis B., Mehta T., RA Park D., Pearson M., Roberts A., Saif S., Shea T., Shenoy N., Sisk P., RA Stolte C., Sykes S., Walk T., White J., Yandava C., Wirth D.F., RA Nusbaum C., Birren B.; RT "The genome sequence of Plasmodium falciparum IGH-CR14."; RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GG665288; KNG77311.1; -; Genomic_DNA. DR ProteinModelPortal; A0A0L1ICD2; -. DR SMR; A0A0L1ICD2; -. DR EnsemblProtists; KNG77311; KNG77311; PFMG_03331. DR Proteomes; UP000054562; Unassembled WGS sequence. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000054562}; KW Reference proteome {ECO:0000313|Proteomes:UP000054562}. FT DOMAIN 459 629 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 698 AA; 81678 MW; FD385C7811AB7D0C CRC64; MGRILFLLKN VNKIEKRYFT NKSNIYYHNE SQKKEIIVLH PILKRSKNNS NKLFQEIIYD AQEALGLAKS ANFQIAKGIS MPLGGWYLKN EKQKKKNDPK NDKIDEGQVP NKELSQNNEH HHVFEKSEKE IPNEMSFTTD KSSSKYINYD EIERKVAESI LIKVNHIDNK FYFSKGKLNE LSKYYLKNPT PCIFINTLLS PEQFRNLEFL FNSLLKSYQD ELILNNKRER DNSEMYERVS DVKFDNCDSD DIIIDNSSYC LDAYNNFLDK EDEQCDDVDL EQNMNVLNEH IGDTSCEQAN DIPYEQISDT QECSKNIPMY VELFDRYSMI LYILKSRAKN NLSKLQLELA RANFVLNTYS EDSKSRMKYI KYIENNVLGG SCIDYEEKYT KLNFFTVGKQ NKKSNVNFSG YTSNYIKSNE TYKEYEKRII NNLYSKLKNE LIKCKNNMIL QNNSRKHKAI IAIVGYTNVG KTKLINYLTK SNLKARNLLF QTLDNAYKNL NISTCYSTIF VDSIGFIQNI PYSLYESFKI SLEAIKTADV IIHVIDVSHP YKDKHKKCVL ETLNKIGISD EFIKNNVIEV WNKIDKLTDN ELYTLCKNKP KNALPISAKY GTNCNYLIQI IEHLINQIKD VHILNLQFPT SEAKERINFL MKNYKVVPHS ISYSDDGNTT FIKLVENKSN LKKYYEKFEI KETYKSDN // ID A0A0L1L1J0_9BURK Unreviewed; 438 AA. AC A0A0L1L1J0; DT 11-NOV-2015, integrated into UniProtKB/TrEMBL. DT 11-NOV-2015, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=BRCH_03525c {ECO:0000313|EMBL:KNH10138.1}; OS Candidatus Burkholderia brachyanthoides. OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Burkholderia. OX NCBI_TaxID=1090379 {ECO:0000313|EMBL:KNH10138.1, ECO:0000313|Proteomes:UP000053000}; RN [1] {ECO:0000313|Proteomes:UP000053000} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=UZHbot7 {ECO:0000313|Proteomes:UP000053000}; RA Carlier A., Eberl L., Pinto-Carbo M.; RT "Comparative genomics of Burkholderia leaf nodule symbionts."; RL Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KNH10138.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LFJI01000014; KNH10138.1; -; Genomic_DNA. DR EnsemblBacteria; KNH10138; KNH10138; BRCH_03525c. DR PATRIC; fig|1090379.4.peg.678; -. DR Proteomes; UP000053000; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000053000}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000053000}. FT DOMAIN 211 382 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 438 AA; 48401 MW; 9758C3519939E94A CRC64; MRKANIKSNS PVTLKPQNTN LINAALVSID FGKIDFEASL EELSLLTQSA DAHPAVTLIG RRSSPDAKMF IGSGKVEELR LQCEANDVEL VIFNHALAPA QQRNLEVALN RRVVDRTSLI LDIFAQRARS HEGKLQVELA QLQYLSTRLI RAWTHLERQK GGIGLRGPGE TQLETDRRLI GERIKALKTR LDKLHRQHGT QRRQRTHNRT MSVSLVGYTN AGKSTLFNAL TKAQAYAADQ LFATLDTTSR RVYLGEETGH IVMSDTVGFI RELPHQLVAA FRATLEETIH ANLLLHVVDA SSAVRLDQID QVNDVLRSIG ADSIRQVLVF NKIDAVPELA ARGEAAERDE YGNISCVFLS ARSGQGLDVL RAAIVEIASA EEGEIESLPS VLAEPHEVSE ATNSSQSGSN PKRDTNARPQ DQRSAEQRDD HTVPEHGY // ID A0A0L6CYM0_9RHOB Unreviewed; 425 AA. AC A0A0L6CYM0; DT 11-NOV-2015, integrated into UniProtKB/TrEMBL. DT 11-NOV-2015, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:KNX42795.1}; GN ORFNames=ROTO_06450 {ECO:0000313|EMBL:KNX42795.1}; OS Roseovarius tolerans. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae; Roseovarius. OX NCBI_TaxID=74031 {ECO:0000313|EMBL:KNX42795.1, ECO:0000313|Proteomes:UP000037046}; RN [1] {ECO:0000313|Proteomes:UP000037046} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=EL-164 {ECO:0000313|Proteomes:UP000037046}; RA Voget S., Bruns H., Wagner-Doebler I., Schulz S., Daniel R.; RT "Draft Genome Sequence of Roseovarius tolerans EL-164, a producer of RT N-Acylated Alanine Methyl Esters (NAMEs)."; RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KNX42795.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LGVV01000005; KNX42795.1; -; Genomic_DNA. DR RefSeq; WP_050661586.1; NZ_LGVV01000005.1. DR EnsemblBacteria; KNX42795; KNX42795; ROTO_06450. DR PATRIC; fig|74031.6.peg.663; -. DR Proteomes; UP000037046; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000037046}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000037046}. FT DOMAIN 204 374 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 425 AA; 47090 MW; 90F1F87DBC4CD3B8 CRC64; MKEHARPITR AWVIHPEIVG ADRARDPELA LEEAVSLAHA LPDLEVAGAQ VVRLRKPDAG RLFGKGKREE LKEAITAAEA DLVLVDGPLT PVQQRNLEKA WDIKILDRTG LILEIFSDRA ATREGVLQVE MAALSYQRTR LVRAWTHLER QRGGLGFVGG PGETQIEADR RAIDEQLVRL RRQLEKVVKT RTLHRAARAK VPFPIVALVG YTNAGKSTLF NRLTGADVMA KDMLFATLDP TMRRVVLPGG GAEVILSDTV GFISDLPTEL VAAFRATLEE VLEADLICHV RDISHPESAA QGRDVATILE SLGVKDTVPQ IEIWNKIDRL EDEARAAAMT QAARQDGVQA LSAVTGQGID DLVTAVSQAL AEVRHLSDVH LGFDEGRKRA WLFQKDLVED ERQTEDGFDL TVRWTARQEQ QFEDM // ID A0A0L6T9F4_9BURK Unreviewed; 424 AA. AC A0A0L6T9F4; DT 11-NOV-2015, integrated into UniProtKB/TrEMBL. DT 11-NOV-2015, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=AD742_13415 {ECO:0000313|EMBL:KNZ32113.1}; OS Methylibium sp. NZG. OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Methylibium. OX NCBI_TaxID=1686064 {ECO:0000313|EMBL:KNZ32113.1, ECO:0000313|Proteomes:UP000053102}; RN [1] {ECO:0000313|Proteomes:UP000053102} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Bi G.; RT "Draft Genome Sequences of the MTBE Degrading Bacterium Methylibium RT sp. NZG."; RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KNZ32113.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LGRD01000024; KNZ32113.1; -; Genomic_DNA. DR EnsemblBacteria; KNZ32113; KNZ32113; AD742_13415. DR PATRIC; fig|1686064.3.peg.3850; -. DR Proteomes; UP000053102; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000053102}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000053102}. FT DOMAIN 207 381 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 424 AA; 46016 MW; FFC5AF6251107153 CRC64; MSSADSTFSA AADNPARAIL VGVDFGRARS FDGTLDELAL LAESAGDVAV ARLVARRKAP DPALFVGSGK ADEIKALVLA HDAEAVLFDQ ALSPAQQRNL ERHLGVAVAD RTMLILEIFG ERAQSHEGKL QVELARLQYL STRLVRRWSH LERQRGGIGT RGGPGEAQLE LDKRIIGERI KGVKQRLDRV KRQRSTQRRS RERNQTFRVS LVGYTNAGKS TLFNAMVNAR AYAADQLFAT LDTTTRQLFL EDAGRSVSLS DTVGFIRDLP HKLVEAFEAT LKEAADADLL LHVVDCASPV LSEQMAEVQR VLAEIGAQDV PQVLVFNKLD RLDAAQVPRT LHDEFEIDAG LRVPRVFVSA QVGTGLDVLR TLVSAQLAAA DLSTLKPRDA ASPHVAASEH PAAGADPELH DPQPMSTLLS VTTP // ID A0A0L6U0Y2_9FIRM Unreviewed; 601 AA. AC A0A0L6U0Y2; DT 11-NOV-2015, integrated into UniProtKB/TrEMBL. DT 11-NOV-2015, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=AKG39_08630 {ECO:0000313|EMBL:KNZ41997.1}; OS Acetobacterium bakii. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Eubacteriaceae; OC Acetobacterium. OX NCBI_TaxID=52689 {ECO:0000313|EMBL:KNZ41997.1, ECO:0000313|Proteomes:UP000036873}; RN [1] {ECO:0000313|Proteomes:UP000036873} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 8239 {ECO:0000313|Proteomes:UP000036873}; RA Song Y., Hwang S., Cho B.-K.; RT "Draft genome sequence of Acetobacterium bakii DSM 8293, a potential RT psychrophilic chemical producer through syngas fermentation."; RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KNZ41997.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LGYO01000021; KNZ41997.1; -; Genomic_DNA. DR RefSeq; WP_050739988.1; NZ_LGYO01000021.1. DR EnsemblBacteria; KNZ41997; KNZ41997; AKG39_08630. DR PATRIC; fig|52689.4.peg.933; -. DR Proteomes; UP000036873; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000036873}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000036873}. FT DOMAIN 378 547 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 337 364 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 601 AA; 67321 MW; F9B8503C2EA4A9BA CRC64; MADNSKSGIR QTYINELDDL VGYEMENQLL LDEHVLEILK RLTLAIQREI LIATNDKNRV QWVTIGDAST VAIGDKDMLY HEKCLNKYRV IHTHPGGNPN LSEEDFSAAK NQGLQCMVTV GVAEGMATSF GIGVPVIEEE TMVYGQALFK NLKELNAFPL EYYILQANRF IKNDPNTIFD VEDTEERALL LGIELQVNQG VDLADSMEEL AQLVKTAGGK VMERVTQARG QIDSTFYVGK GKIQELTKLI QNKDVNLIVA NDELNSKQIA NIEAVTGTKT VDRTTIILDI FARQSKTREG KLQVELAQQK YRMSHLKGLG IVMSRTGGGI GTRGPGEKKL ETDRRLIRKQ IEDLEARNER INKSNTLNAL QRQKNNIQTV SLIGYTNSGK STLFNVLTQS EAVTKDGLFV TLDSTLRKIG PEQGDYLVSD TVGFIEKLPH DLIKAFKTTL KEVETADVLL HVVDVSNHNY EAQIDVVNQV LADIGVGHKI VIMVYNKIDK LPENQREELI AKNQSAVEEH SLYISAKEGL QIDLLLEVIQ KVLRGEKRQI KLLIPYDDNK ALAALHEKKV VLGIEYEGDG NLVTIEITDE FPIHLFEKYV V // ID A0A0L7R839_9HYME Unreviewed; 481 AA. AC A0A0L7R839; DT 11-NOV-2015, integrated into UniProtKB/TrEMBL. DT 11-NOV-2015, sequence version 1. DT 07-JUN-2017, entry version 12. DE SubName: Full=Putative GTP-binding protein 6 {ECO:0000313|EMBL:KOC67009.1}; GN ORFNames=WH47_12436 {ECO:0000313|EMBL:KOC67009.1}; OS Habropoda laboriosa. OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; OC Pterygota; Neoptera; Holometabola; Hymenoptera; Apocrita; Aculeata; OC Apoidea; Apidae; Habropoda. OX NCBI_TaxID=597456 {ECO:0000313|EMBL:KOC67009.1, ECO:0000313|Proteomes:UP000053825}; RN [1] {ECO:0000313|EMBL:KOC67009.1, ECO:0000313|Proteomes:UP000053825} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=0110345459 {ECO:0000313|EMBL:KOC67009.1}; RA Pan H., Kapheim K.; RT "The genome of Habropoda laboriosa."; RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; KQ414637; KOC67009.1; -; Genomic_DNA. DR Proteomes; UP000053825; Unassembled WGS sequence. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR CDD; cd01878; HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000053825}; KW Reference proteome {ECO:0000313|Proteomes:UP000053825}. FT DOMAIN 258 357 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 481 AA; 55098 MW; 1D409F6A1AC58D37 CRC64; MQFLKRFAYL INKSQYIINK KREFEIVNVI RRCNHESNVV FEEYEESEEE KNIYTQISRD YLGSAVGGNR IFLIQPYIKW GVKKKRNTSP QLQLDEAIAL INTLPNWSVV GKKIVPLLSL QKKQLVGSGS LETLKADIRN CANVTAIFVS TNLLKFIQIA ELQEAFQLPI YDRYSIVIHI FREHAKTSEA KLQVALAEIP YIKQKITDLS AYRIGRIHCN EKTKALLHTR ERKLNNALKK LKEHRHMIKE RRLSFGFPSI AVVGYTNAGK TSLIKALTED DSLQPEDKLF ATLDTTVHQG YLPNKVKVLY IDTIGFIQDV PETLIEPFRV TLEDALNADI LVHVFDISHP DLKAQIQHVQ ITIQRMINEN KVVINVANKY DMVEQGTIET DILPEGTHLV SAAKLTGIDL LRSKMQEQII DASDLLKKRI RVQTGSAIAS WLYNQATVLS AEPDPKDSQY LIMDVLMSTE AFYKFKRFLK N // ID A0A0L7T5J9_9GAMM Unreviewed; 426 AA. AC A0A0L7T5J9; DT 11-NOV-2015, integrated into UniProtKB/TrEMBL. DT 11-NOV-2015, sequence version 1. DT 30-AUG-2017, entry version 13. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=NG42_08230 {ECO:0000313|EMBL:KOC90684.1}, GN NG43_12085 {ECO:0000313|EMBL:KOC93108.1}; OS Erwinia iniecta. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; OC Erwiniaceae; Erwinia. OX NCBI_TaxID=1560201 {ECO:0000313|EMBL:KOC90684.1, ECO:0000313|Proteomes:UP000037088}; RN [1] {ECO:0000313|EMBL:KOC90684.1, ECO:0000313|Proteomes:UP000036851, ECO:0000313|Proteomes:UP000037088} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=B120 {ECO:0000313|EMBL:KOC90684.1, RC ECO:0000313|Proteomes:UP000037088}, and RC B149 {ECO:0000313|EMBL:KOC93108.1, ECO:0000313|Proteomes:UP000036851}; RX PubMed=26198254; RA Campillo T., Luna E., Portier P., Fischer-Le Saux M., Lapitan N., RA Tisserat N.A., Leach J.E.; RT "Erwinia iniecta sp. nov., isolated from Russian wheat aphids RT (Diuraphis noxia)."; RL Int. J. Syst. Evol. Microbiol. 0:0-0(2015). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KOC90684.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JRXE01000009; KOC90684.1; -; Genomic_DNA. DR EMBL; JRXF01000017; KOC93108.1; -; Genomic_DNA. DR RefSeq; WP_052898831.1; NZ_JRXF01000017.1. DR EnsemblBacteria; KOC90684; KOC90684; NG42_08230. DR EnsemblBacteria; KOC93108; KOC93108; NG43_12085. DR PATRIC; fig|1560201.3.peg.1752; -. DR Proteomes; UP000036851; Unassembled WGS sequence. DR Proteomes; UP000037088; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000037088}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000037088}. FT DOMAIN 198 365 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 426 AA; 47957 MW; C01EA2E3BBC9A2E7 CRC64; MFDRYDAGEQ AVLVHIYFSQ DKDMEDLMEF ETLVSSAGVE ALRVVTGSRK APHPKYFVGE GKAVEIADAV KSSGASVVLF DHALTPAQER NLERLCECRV IDRTGLILDI FAQRARTHEG KLQVELAQLR HLATRLVRGW THLERQKGGI GLRGPGETQL ETDRRLLRNR ITLILSRLAR VEKQRDQGRQ ARAKADVPTV SLVGYTNAGK STLFNCITSA DVYAADQLFA TLDPTLRRVD VADVGEVVLA DTVGFIRHLP HDLVAAFKAT LQETRQASLL LHIIDAADQR VDENIEAVDV VLEEIESDAI PQLLVMNKID MLEDFEPRID RNEENMPVRV WLSAQTGVGV PLLFQALTER LAGEIAQYDL RLPPEAGRLR SRFYQLQAIE KEWNEEDGSV GLHIRMPIID WRRLCKQEPA LVDYIV // ID A0A0L8ESB4_9BURK Unreviewed; 368 AA. AC A0A0L8ESB4; DT 11-NOV-2015, integrated into UniProtKB/TrEMBL. DT 11-NOV-2015, sequence version 1. DT 07-JUN-2017, entry version 13. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=AD428_09040 {ECO:0000313|EMBL:KOF54116.1}; OS Achromobacter sp. DMS1. OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Alcaligenaceae; Achromobacter. OX NCBI_TaxID=1688405 {ECO:0000313|EMBL:KOF54116.1, ECO:0000313|Proteomes:UP000053133}; RN [1] {ECO:0000313|Proteomes:UP000053133} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DMS1 {ECO:0000313|Proteomes:UP000053133}; RA Amin S., Shah B., Jain K., Patel A., Joshi C., Madamwar D.; RT "Draft genome of Betaproteobacterium sp. harbouring genes for RT xenobiotic degradation."; RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KOF54116.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LHSJ01000059; KOF54116.1; -; Genomic_DNA. DR RefSeq; WP_053244933.1; NZ_LHSJ01000059.1. DR EnsemblBacteria; KOF54116; KOF54116; AD428_09040. DR PATRIC; fig|1688405.3.peg.4360; -. DR Proteomes; UP000053133; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000053133}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000053133}. FT DOMAIN 190 354 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 368 AA; 40196 MW; 16E5ACFEB45F9782 CRC64; MRALIISVDL GNPDHAAHAE EFAMLAEGAG AEIVGTLTAR RDRPDAKFFI GSGKVEEGVA MAQALLADII LFEQPLSPAQ QRNLERAFNL RVVDRVALIL DIFALRAKSH EGKLQVELAQ LQHLATRLTR LWTHLERQRG GIGMRGPGES QLEMDRRMIG AKVKVLRERL DKVERQRVTQ RRARARGGAL SVSLVGYTNA GKSTLFNALT RADTYAADQL FATLDTTTRR IWIEGAGSVV VSDTVGFIRD LPHGLIAAFR ATLEETVHAD LLLHVVDAAS PQREEQIFEV NKVLAEIGAA SVPTILVYNK IDRVGLEPRV ERDAHGTIAR VFVSATERAG LDALRGAIAE TGQIAGNNAS NQQTLQSE // ID A0A0L8ET61_9BURK Unreviewed; 368 AA. AC A0A0L8ET61; DT 11-NOV-2015, integrated into UniProtKB/TrEMBL. DT 11-NOV-2015, sequence version 1. DT 07-JUN-2017, entry version 13. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=AD428_05685 {ECO:0000313|EMBL:KOF54662.1}; OS Achromobacter sp. DMS1. OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Alcaligenaceae; Achromobacter. OX NCBI_TaxID=1688405 {ECO:0000313|EMBL:KOF54662.1, ECO:0000313|Proteomes:UP000053133}; RN [1] {ECO:0000313|Proteomes:UP000053133} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DMS1 {ECO:0000313|Proteomes:UP000053133}; RA Amin S., Shah B., Jain K., Patel A., Joshi C., Madamwar D.; RT "Draft genome of Betaproteobacterium sp. harbouring genes for RT xenobiotic degradation."; RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KOF54662.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LHSJ01000029; KOF54662.1; -; Genomic_DNA. DR RefSeq; WP_053244494.1; NZ_LHSJ01000029.1. DR EnsemblBacteria; KOF54662; KOF54662; AD428_05685. DR PATRIC; fig|1688405.3.peg.3092; -. DR Proteomes; UP000053133; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000053133}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000053133}. FT DOMAIN 190 354 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 368 AA; 40111 MW; 64E2F6BC76508013 CRC64; MRALIISVDL GNPDHAAHAE EFAMLAEGAG AEIVGTLTAR RDRPDAKFFI GSGKVEEGVA MAQALLADII LFEQPLSPAQ QRNLERAFNL RVVDRVALIL DIFALRAKSH EGKLQVELAQ LQHLATRLTR LWTHLERQRG GIGMRGPGES QLEMDRRMIG AKVKVLREAL DKVERQRVTQ RRARARGGAL SVSLVGYTNA GKSTLFNALT RADTYAADQL FATLDTTTRR IWIEGAGSVV VSDTVGFIRD LPHGLIAAFR ATLEETVHAD LLLHVVDAAS PQREEQIFEV NKVLAEIGAA SVPTILVYNK IDRVGLEPRV ERDAHGTIAR VFVSATERAG LDALRGAIAE TGQIAGNNAS NQQTLQSE // ID A0A0L8HFG0_OCTBM Unreviewed; 550 AA. AC A0A0L8HFG0; DT 11-NOV-2015, integrated into UniProtKB/TrEMBL. DT 11-NOV-2015, sequence version 1. DT 07-JUN-2017, entry version 11. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:KOF87869.1}; GN ORFNames=OCBIM_22015920mg {ECO:0000313|EMBL:KOF87869.1}; OS Octopus bimaculoides (California two-spotted octopus). OC Eukaryota; Metazoa; Lophotrochozoa; Mollusca; Cephalopoda; Coleoidea; OC Neocoleoidea; Octopodiformes; Octopoda; Incirrata; Octopodidae; OC Octopus. OX NCBI_TaxID=37653 {ECO:0000313|EMBL:KOF87869.1, ECO:0000313|Proteomes:UP000053454}; RN [1] {ECO:0000313|Proteomes:UP000053454} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Albertin C.B., Simakov O., Mitros T., Wang Z.Y., Pungot J.R., RA Edsinger-Gonzalez E., Brenner S., Ragsdale C.W., Rokhsar D.S.; RT "WGS assembly of Octopus bimaculoides."; RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; KQ418303; KOF87869.1; -; Genomic_DNA. DR RefSeq; XP_014772769.1; XM_014917283.1. DR EnsemblMetazoa; Ocbimv22015920m; Ocbimv22015920m.p; Ocbimv22015920m.g. DR GeneID; 106871025; -. DR KEGG; obi:106871025; -. DR OMA; MDTVGFM; -. DR Proteomes; UP000053454; Unassembled WGS sequence. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR CDD; cd01878; HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000053454}; KW Reference proteome {ECO:0000313|Proteomes:UP000053454}. FT DOMAIN 312 405 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 550 AA; 62629 MW; E30D307CCC1BFD37 CRC64; MTLQQCTTCR FASFRHMFKV ALRPDFIYDH RLQRQYSQLN TLLRKCNKTS QLPAFVSRLS STLKYSRLFC TNSYLEEMLE GHPDENIEEL LRRDEKYQEY VREYFSIPNT GQRVFLIQPN VKRGPQRSLS SITSQLEESV ALIQTLPNWK VVGKKIVATK SPDSKPVFGK GNFAALTSEI HNCPAVTAIF ISLNMLNTLQ WTYLQNVWKI PVYDRYNIVL QIFKEYAKTK EVKLQVALAE IPYIRSRLPS VHGGSLSITA GGTKHTGGTT PMYLEQRFKY LQDWELKLKK ALKKVRKQRA IVRQNRLKKQ IPIVAVVGYT NAGKTSIIKA LTADAKLQPV DQLFATLDVT AHAGVLPNHM TVIYIDTVGF ISNIPTTLIE AFAATLEDAV IADVVIHVRD ISHEDTTAQS MNVYNTLKGM INPQKLENMI EVKNKVDLLL CRENLESQSE RKCIYTNASS GVGVGKLKHC IQEAILNNSN WKQRKFRINM GSSLFQWLQQ EASIVSAVPD ATKENLIVTV VITDSTYHRF KAEFKKQRKK YLQATIDVTA // ID A0A0L8QWP5_9ACTN Unreviewed; 511 AA. AC A0A0L8QWP5; DT 11-NOV-2015, integrated into UniProtKB/TrEMBL. DT 11-NOV-2015, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=ADK38_03310 {ECO:0000313|EMBL:KOG91416.1}; OS Streptomyces varsoviensis. OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae; OC Streptomyces. OX NCBI_TaxID=67373 {ECO:0000313|EMBL:KOG91416.1, ECO:0000313|Proteomes:UP000037020}; RN [1] {ECO:0000313|Proteomes:UP000037020} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NRRL B-3589 {ECO:0000313|Proteomes:UP000037020}; RG Consortium for Microbial Forensics and Genomics (microFORGE); RA Knight B.M., Roberts D.P., Lin D., Hari K., Fletcher J., Melcher U., RA Blagden T., Winegar R.A.; RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KOG91416.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LGUT01000271; KOG91416.1; -; Genomic_DNA. DR RefSeq; WP_030892190.1; NZ_JOFN01000052.1. DR EnsemblBacteria; KOG91416; KOG91416; ADK38_03310. DR PATRIC; fig|67373.7.peg.766; -. DR Proteomes; UP000037020; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 2. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000313|EMBL:KOG91416.1}; KW Complete proteome {ECO:0000313|Proteomes:UP000037020}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900, KW ECO:0000313|EMBL:KOG91416.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000037020}. FT DOMAIN 290 455 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 511 AA; 55603 MW; C91D34390CA74AD3 CRC64; MTSSSSLPQD RQDRPDAHES TDARSRQSLP ESLRADALME EDVAWSHEID GERDGDQYDR SERAALRRVA GLSTELEDVT EVEYRQLRLE RVVLVGVWTT GTAEEADNSL AELAALAETA GALVLDGVVQ RRDKPDPATY IGSGKAQELR DIVLESGADT VVCDGELSPG QLIHLEDVVK VKVVDRTALI LDIFAQHAKS REGKAQVSLA QMQYMLPRLR GWGQSLSRQM GGGGSAGSGG GMATRGPGET KIETDRRRIR EKMAKMRREI AEMKTGRDIK RQERRRHKVP SVAIAGYTNA GKSSLLNRLT GAGVLVENAL FATLDPTVRR AETPSGRLYT LADTVGFVRH LPHHLVEAFR STMEEVGDSD LILHVVDGSH PAPEEQLAAV REVIRDVGAV NVPEIVVVNK ADAADPVALQ RLLRIEKHAI AVSARTGEGM GLLLALIDER LPRPEVEIEA LVPYTHGALI ARAHADGEVI SEEHTETGTL LKARVHEELA AALQPYVPAS A // ID A0A0L9UVR8_PHAAN Unreviewed; 537 AA. AC A0A0L9UVR8; DT 11-NOV-2015, integrated into UniProtKB/TrEMBL. DT 11-NOV-2015, sequence version 1. DT 07-JUN-2017, entry version 13. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:KOM46634.1}; GN ORFNames=LR48_Vigan07g033800 {ECO:0000313|EMBL:KOM46634.1}; OS Phaseolus angularis (Azuki bean) (Vigna angularis). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae; OC Pentapetalae; rosids; fabids; Fabales; Fabaceae; Papilionoideae; OC Phaseoleae; Vigna. OX NCBI_TaxID=3914 {ECO:0000313|EMBL:KOM46634.1, ECO:0000313|Proteomes:UP000053144}; RN [1] {ECO:0000313|Proteomes:UP000053144} RP NUCLEOTIDE SEQUENCE. RC STRAIN=cv. Jingnong 6 {ECO:0000313|Proteomes:UP000053144}; RX PubMed=26460024; DOI=10.1073/pnas.1420949112; RA Yang K., Tian Z., Chen C., Luo L., Zhao B., Wang Z., Yu L., Li Y., RA Sun Y., Li W., Chen Y., Li Y., Zhang Y., Ai D., Zhao J., Shang C., RA Ma Y., Wu B., Wang M., Gao L., Sun D., Zhang P., Guo F., Wang W., RA Li Y., Wang J., Varshney R.K., Wang J., Ling H.Q., Wan P.; RT "Genome sequencing of adzuki bean (Vigna angularis) provides insight RT into high starch and low fat accumulation and domestication."; RL Proc. Natl. Acad. Sci. U.S.A. 112:13213-13218(2015). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CM003377; KOM46634.1; -; Genomic_DNA. DR RefSeq; XP_017430819.1; XM_017575330.1. DR GeneID; 108338443; -. DR KEGG; var:108338443; -. DR Proteomes; UP000053144; Chromosome 7. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR CDD; cd01878; HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 2. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 2. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000053144}; KW Reference proteome {ECO:0000313|Proteomes:UP000053144}. FT DOMAIN 270 507 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 537 AA; 59834 MW; D7065C821B047595 CRC64; MLRSFSSALR GCSRKFQTSI SCKKLYTSEG EGARERPPKL LVVQPRMRPE KLLQAKLNEA LCLANSLEDQ RDGYFHTDFF DKPLPPHVLV QNRVPRVDSY FGHGTVDNIK CHVNAAAESK DEVDAVFVNA ILSGIQQRNL ERAWGKPVLD RVGLIIEIFN AHAFTKEAKL QAELAALSYK KTRLVRVRGP DGRYTFGASG DAEVVSARGR GSGGQGFMSG AGETELQLQR RRILERRNYL LSQIEEVRRT RALQRAGRRR RGGSSGQGLA TVAVVGYTNA GKSTLVSRLS GSDLYSDCRL FATVDPRVRS AVLPSGKKVL FSDTVGFISD LPVQLVEAFH ATLEEVVEAD LLVHVVDSSA PNLDEHRTTV LQVLRQIGVS EEKLRNMIEV WNKIDMEEEC MDVDEYVVDE DEEGVEVEDD VKSELLAENE GMKEVGFEAM EEKEYSDGWL YDDDDDLGDE GDRQNQSIEK HSGLDKESGP HVKTSAITGV GLQELLELID QKLCVQNNKG AQVVGRSIYE RKWRPSHNQE SGIAVEQ // ID A0A0M0BF75_9ARCH Unreviewed; 419 AA. AC A0A0M0BF75; DT 11-NOV-2015, integrated into UniProtKB/TrEMBL. DT 11-NOV-2015, sequence version 1. DT 07-JUN-2017, entry version 12. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=AC481_05885 {ECO:0000313|EMBL:KON27019.1}; OS miscellaneous Crenarchaeota group archaeon SMTZ-80. OC Archaea; Candidatus Bathyarchaeota. OX NCBI_TaxID=1685135 {ECO:0000313|EMBL:KON27019.1, ECO:0000313|Proteomes:UP000037599}; RN [1] {ECO:0000313|EMBL:KON27019.1, ECO:0000313|Proteomes:UP000037599} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SMTZ-80 {ECO:0000313|EMBL:KON27019.1}; RA Lazar C.S., Baker B.J., Seitz K.W., Hyde A.S., Dick G.J., RA Hinrichs K.-U., Teske A.P.; RT "New insights into the roles of widespread benthic archaea in carbon RT and nitrogen cycling."; RL Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KON27019.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LFWY01000031; KON27019.1; -; Genomic_DNA. DR PATRIC; fig|1685135.3.peg.1416; -. DR Proteomes; UP000037599; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000037599}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000037599}. FT DOMAIN 200 366 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 159 186 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 419 AA; 47068 MW; FA4CFD3328C67835 CRC64; MDNFNYKEKA LLIGTRNVSR RDWEVEDSLE ELSHLAETAG ASVEGTIVQE LKKIDPSLLI GKGKVEEIRD FVSSHNIDLV IFDNELTSTQ QSNLEEIFNT KTIDRTGLIL DIFAQRAKSK EGKLQVELAQ LTYILPRLKG KGVVLSRLGG GIGTRGPGET QLEVDRRKIK ERITRLKKEI DKVQKVRKLH RQGRRSLSQL TIALIGYTNA GKSTLLNYLS HTGVLVENRL FSTLDPKIGK IKLPNKQEVF ISDTVGFINK LPHQLIAAFK ATFEEVKESD LLLHIIDMSN PHFEVHINAV NEVLEEIGMP PKKIFHVLNK IDRVTHKKMI SAWGKKLENG VAISALTGDG VDLLLNMIGD VVSTSMQRVK LKIPFGAWNT TGKIFRNGKI VTKRYLKTGV IIEAEVQRAL IDSLKPYLK // ID A0A0M0BQG1_9ARCH Unreviewed; 424 AA. AC A0A0M0BQG1; DT 11-NOV-2015, integrated into UniProtKB/TrEMBL. DT 11-NOV-2015, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=AC480_00665 {ECO:0000313|EMBL:KON30605.1}; OS miscellaneous Crenarchaeota group archaeon SMTZ1-55. OC Archaea; Candidatus Bathyarchaeota. OX NCBI_TaxID=1685133 {ECO:0000313|EMBL:KON30605.1, ECO:0000313|Proteomes:UP000037456}; RN [1] {ECO:0000313|EMBL:KON30605.1, ECO:0000313|Proteomes:UP000037456} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SMTZ1-55 {ECO:0000313|EMBL:KON30605.1}; RA Lazar C.S., Baker B.J., Seitz K.W., Hyde A.S., Dick G.J., RA Hinrichs K.-U., Teske A.P.; RT "New insights into the roles of widespread benthic archaea in carbon RT and nitrogen cycling."; RL Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KON30605.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LFWX01000007; KON30605.1; -; Genomic_DNA. DR PATRIC; fig|1685133.3.peg.1012; -. DR OrthoDB; POG093Z07D6; -. DR Proteomes; UP000037456; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000037456}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000037456}. FT DOMAIN 186 356 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 424 AA; 47600 MW; 436B2E2293C1F6A7 CRC64; MRTILVQRRN HRDSSNLGEL ASLAEAAGYR VEGRIEQTRR ADARLQIGRG KARELAEMAE RVKADKVIFD NALTPSQAYN LAKIAGVEII DRFQLILEIF SKRASTREAK LQIRLAKLRH QLPRAREMVR LARMEERPGF LGLGTYEVEV YCEDIKRQIH RIRQDLRQIR GQRRLHRDRR TALGFPLVSL AGYTNAGKTS LFNTLTGESK SVDIGVFTTL STTTRAIDLE GGKVLITDTV GFIDRLPLAL VEAFLSTLEE TSLSNAIILL LDFHESVDEI KRKLSCSLDT LNEIGAGGIP IVTALNKIDL LTPDEVAERL SHVLDLAPNP LLISARTGRN LDQLGRRVAR FLGDVFTLIF SLPLTEASIS FVSDLHRRVH SVDTIYNGNE VQIKLRAFRW LIEEIAGEVE KRQGTLLVAQ PPVM // ID A0A0M0G3Z9_9BACI Unreviewed; 421 AA. AC A0A0M0G3Z9; DT 11-NOV-2015, integrated into UniProtKB/TrEMBL. DT 11-NOV-2015, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=AF331_10575 {ECO:0000313|EMBL:KON84498.1}; OS Bacillus marisflavi. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus. OX NCBI_TaxID=189381 {ECO:0000313|EMBL:KON84498.1, ECO:0000313|Proteomes:UP000037405}; RN [1] {ECO:0000313|Proteomes:UP000037405} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=JCM 11544 {ECO:0000313|Proteomes:UP000037405}; RA Liu B., Wang J., Zhu Y., Liu G., Chen Q., Chen Z., Lan J., Che J., RA Ge C., Shi H., Pan Z., Liu X.; RT "Fjat-14235 jcm11544."; RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KON84498.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LGUE01000004; KON84498.1; -; Genomic_DNA. DR RefSeq; WP_053428097.1; NZ_LGUE01000004.1. DR EnsemblBacteria; KON84498; KON84498; AF331_10575. DR PATRIC; fig|189381.12.peg.2122; -. DR Proteomes; UP000037405; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000037405}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000037405}. FT DOMAIN 199 367 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 158 185 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 421 AA; 47953 MW; 72E22CAA130C62A9 CRC64; MEEQKLKAIA IGVNTKDRDN DFEYGMLELK GLAEARHMDV VGEFTQNMQR PDHVHYLGKG KIDELIPLIE EWEADVIISN DELSPSQIRV LEKKLELRVM DRTMLILDIF AERAKTREAQ LQVEVAQLQY MLPRLIGRRE SLGRQGGGSG LANRGAGETK LELDRRRIED RITALRKELD SLVELRSTQR KQRKKSGIPV VSLVGYTNAG KSTTMNAFIE RFHQNNDKQV FEKDMLFATL ETSVRNITLP DQKSFLLTDT VGFVNKLPHQ LVKAFRSTLE EVVEADLIIH VVDLADPHHD TMMDVTDKTL EDIGVGDTPI LYAFNKADLV GGDIPRVEQG GVYYSAKQRI GIEELLGEVK KQIFGDYKTC TMLIPYDQGQ LISYFNQQAT VLETEYDEKG TILKVECRES DAERYRDYII A // ID A0A0M0IFA1_9VIBR Unreviewed; 429 AA. AC A0A0M0IFA1; DT 11-NOV-2015, integrated into UniProtKB/TrEMBL. DT 11-NOV-2015, sequence version 1. DT 30-AUG-2017, entry version 14. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=AKJ18_21155 {ECO:0000313|EMBL:KOO12944.1}; OS Vibrio xuii. OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; OC Vibrionaceae; Vibrio. OX NCBI_TaxID=170661 {ECO:0000313|EMBL:KOO12944.1, ECO:0000313|Proteomes:UP000037421}; RN [1] {ECO:0000313|Proteomes:UP000037421} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 17185 {ECO:0000313|Proteomes:UP000037421}; RA Giubergia S., Machado H., Mateiu R.V., Gram L.; RT "Vibrio galatheae sp. nov., a novel member of the Vibrionaceae family RT isolated from the Solomon Islands."; RL Submitted (AUG-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KOO12944.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LHPK01000054; KOO12944.1; -; Genomic_DNA. DR RefSeq; WP_004415845.1; NZ_LHPK01000054.1. DR ProteinModelPortal; A0A0M0IFA1; -. DR EnsemblBacteria; KOO12944; KOO12944; AKJ18_21155. DR GeneID; 25689876; -. DR PATRIC; fig|170661.3.peg.4329; -. DR Proteomes; UP000037421; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000037421}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}. FT DOMAIN 198 365 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 429 AA; 48633 MW; 86105A3C5593C269 CRC64; MFDRYEAGER AVLVHINFTQ EGEWEDLSEF EMLVSSAGVS TLQVVTGSRQ SPHPKYYVGE GKAQEIAQAV QLAGADIVIF NHSLSPAQER NLEALCKCRV LDRTGLILDI FAQRARTHEG KLQVELAQLR HISTRLIRGW THLERQKGGI GLRGPGETQL ETDRRLLRVR IKTILRRLEK VAKQREQGRR ARSRAEIPTV SLVGYTNAGK STLFNRITEA GVYAADQLFA TLDPTLRKIE LSDVGPAILA DTVGFIRHLP HDLVAAFKAT LQETQEADIL LHVVDASDER FRENIQAVHE VLAEIDADEI PALVVMNKID NLEGQNPRID RDDEGVPQTV WVSAMEGKGI ELLFDALTER LASQMVQHQM RIPPQHQGRL RSTFFQMKCI QREEYDQEGN LLIEVRMQQA DWSRLEKRDE AVLRDFIVT // ID A0A0M0J358_9EUKA Unreviewed; 443 AA. AC A0A0M0J358; DT 11-NOV-2015, integrated into UniProtKB/TrEMBL. DT 11-NOV-2015, sequence version 1. DT 07-JUN-2017, entry version 8. DE SubName: Full=Gtp-binding protein {ECO:0000313|EMBL:KOO20979.1}; GN ORFNames=Ctob_000034 {ECO:0000313|EMBL:KOO20979.1}, GN Ctob_008980 {ECO:0000313|EMBL:KOO28894.1}; OS Chrysochromulina sp. CCMP291. OC Eukaryota; Haptophyceae; Prymnesiales; Chrysochromulinaceae; OC Chrysochromulina. OX NCBI_TaxID=1460289 {ECO:0000313|EMBL:KOO20979.1, ECO:0000313|Proteomes:UP000037460}; RN [1] {ECO:0000313|EMBL:KOO20979.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=CCMP291 {ECO:0000313|EMBL:KOO20979.1}; RA Hovde B.T., Starkenburg S.R., Cattolico R.A.; RT "Draft genome of the oleaginous, mixotrophic haptophyte, RT Chrysochromulina tobin."; RL Submitted (DEC-2014) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Proteomes:UP000037460} RP NUCLEOTIDE SEQUENCE. RC STRAIN=CCMP291 {ECO:0000313|Proteomes:UP000037460}; RX PubMed=26397803; DOI=10.1371/journal.pgen.1005469; RA Hovde B.T., Deodato C.R., Hunsperger H.M., Ryken S.A., Yost W., RA Jha R.K., Patterson J., Monnat R.J. Jr., Barlow S.B., RA Starkenburg S.R., Cattolico R.A.; RT "Genome Sequence and Transcriptome Analyses of Chrysochromulina tobin: RT Metabolic Tools for Enhanced Algal Fitness in the Prominent Order RT Prymnesiales (Haptophyceae)."; RL PLoS Genet. 11:e1005469-e1005469(2015). CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KOO20979.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JWZX01003398; KOO20979.1; -; Genomic_DNA. DR EMBL; JWZX01002497; KOO28894.1; -; Genomic_DNA. DR Proteomes; UP000037460; Unassembled WGS sequence. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000037460}; KW Reference proteome {ECO:0000313|Proteomes:UP000037460}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1 17 {ECO:0000256|SAM:SignalP}. FT CHAIN 18 443 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5007416649. FT DOMAIN 270 443 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 443 AA; 47590 MW; 12D6069BA5D32294 CRC64; MMGHAQLLSL WLLPTTALHF AVPGRSGCSG CSGCIIRRRS PPAAMAAFGA ETINVEPGAK CYLVGAVVKR DRYKTLVNSW GIDDSLDELQ RLCETAGLEV LGRDYQTLQH PSPSTFIGQG KLDEIAALVK SMRVSTVIFD EELTPAQGRN IQNVLIEACG EQVQVLDRTM LILVIFSQRA RTSEAKLQVA AAQMKYMLPR LKFFLTQGAG MDAKGGSGGG MFLKGSGETQ LEEDRRLFRK QLGKIEDDLA AVQAQRDMLR AKRREGDRRP VVAIVGYTNA GKSTLLNTLC GSSEVYADDL LFATLDPTSR LHALPGGKEV LLTDTVGFIQ KLPTKLVAAF RATLDELVDA TLLVHVVDAS SEIAVQQVRS VQGIVKELEA SGKPQILVLN KADAVGADPT LAARAASTDW LHLDGDVTPC AVLAIPLSAS DDTAGARHPA ECL // ID A0A0M0L6I6_9BACI Unreviewed; 416 AA. AC A0A0M0L6I6; DT 11-NOV-2015, integrated into UniProtKB/TrEMBL. DT 11-NOV-2015, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=AMD01_11845 {ECO:0000313|EMBL:KOO46691.1}; OS Bacillus koreensis. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus. OX NCBI_TaxID=284581 {ECO:0000313|EMBL:KOO46691.1, ECO:0000313|Proteomes:UP000037558}; RN [1] {ECO:0000313|Proteomes:UP000037558} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 16467 {ECO:0000313|Proteomes:UP000037558}; RA Liu B., Wang J., Zhu Y., Liu G., Chen Q., Chen Z., Lan J., Che J., RA Ge C., Shi H., Pan Z., Liu X.; RT "Fjat-14210 dsm16467."; RL Submitted (AUG-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KOO46691.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LILC01000013; KOO46691.1; -; Genomic_DNA. DR RefSeq; WP_053401770.1; NZ_LILC01000013.1. DR EnsemblBacteria; KOO46691; KOO46691; AMD01_11845. DR PATRIC; fig|284581.3.peg.2486; -. DR Proteomes; UP000037558; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000037558}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000037558}. FT DOMAIN 198 359 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 157 191 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 416 AA; 47572 MW; 525A75B0363F1CC0 CRC64; MKNEQEKVIL VGCQLQTEDD DRFQYSMDEL ISLTETANGK VVVSLTQKRD RVHSATYIGK GKVEELVQLE EELEPDLIIF NDELSPSQIR NLSAQLDARV IDRTQLILDI FAQRAQTKEG KLQVELAQLE YLLPRLVGQG ASLSRLGGGI GTRGPGETKL ESDRRHIRRK IDDIKQQLKT VVEHRNRYRE RRKRNQALQI AIVGYTNAGK STLFNRMTEA GIYEENQLFA TLDPTTRRLA LPSGFQALIT DTVGFIQDLP TTLVASFRST LEEVQEADLI LHVVDSSNPD YYNHEQTVHD LLRELDVSGI PMLTVYNKKD LQLSDFVPHT NRSMNVSAFV KEDVNELLET IERYVREEMK YYELHVSPSE GKLLASLKRD TIVEKMTFNE ETDLYECAGY APQHHPIHVE KNSENE // ID A0A0M0WVE6_9BACI Unreviewed; 428 AA. AC A0A0M0WVE6; DT 11-NOV-2015, integrated into UniProtKB/TrEMBL. DT 11-NOV-2015, sequence version 1. DT 05-JUL-2017, entry version 12. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=AMS60_19105 {ECO:0000313|EMBL:KOP77669.1}; OS Bacillus sp. FJAT-21945. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus. OX NCBI_TaxID=1581033 {ECO:0000313|EMBL:KOP77669.1, ECO:0000313|Proteomes:UP000036921}; RN [1] {ECO:0000313|Proteomes:UP000036921} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=FJAT-21945 {ECO:0000313|Proteomes:UP000036921}; RA Liu B., Wang J., Zhu Y., Liu G., Chen Q., Chen Z., Lan J., Che J., RA Ge C., Shi H., Pan Z., Liu X.; RT "Fjat-21945."; RL Submitted (AUG-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KOP77669.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LITN01000013; KOP77669.1; -; Genomic_DNA. DR EnsemblBacteria; KOP77669; KOP77669; AMS60_19105. DR PATRIC; fig|1581033.3.peg.215; -. DR Proteomes; UP000036921; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000036921}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000036921}. FT DOMAIN 203 371 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 169 196 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 428 AA; 48808 MW; E1C12F338C0685CC CRC64; MKWRKSFMKR KAILVGVNLN STQSDFEYMM GELANLAGAC DVEVVGEITQ NLHQLNKSHY IGAGKVEELL SLLKEKDANV VIFDDELSPS QIRNLESELD CEVIDRTMLI LEIFSNRAKT RESQLQVEVA RLKYMLPRLV GMRESLGRQG GGAGLKNRGA GETKLELDRR KIEIKITALN KELEKLINQR KTQRKLRKKN NIPVVSLVGY TNAGKSTIMN AMLEKYNEAM DKQVFEKDML FATLETSVRK IKLTKNKTFL LTDTVGFINK LPHHLIKAFR STLEEVGEAD LLIHVLDYSS PHHEEQKRLT NEILSEIGIE GIPVIYANNK ADLTEAEYPF SQQNCVYLSA KNRLGLNELT QLISQEIFSD SIQCELLIPY AQGEIVSYFN ENSHILLSEY EDNGTKIIVE CKRSDAEKYK QYIRLTQV // ID A0A0M0X7U1_9BACI Unreviewed; 418 AA. AC A0A0M0X7U1; DT 11-NOV-2015, integrated into UniProtKB/TrEMBL. DT 11-NOV-2015, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=AMS60_06825 {ECO:0000313|EMBL:KOP82232.1}; OS Bacillus sp. FJAT-21945. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus. OX NCBI_TaxID=1581033 {ECO:0000313|EMBL:KOP82232.1, ECO:0000313|Proteomes:UP000036921}; RN [1] {ECO:0000313|Proteomes:UP000036921} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=FJAT-21945 {ECO:0000313|Proteomes:UP000036921}; RA Liu B., Wang J., Zhu Y., Liu G., Chen Q., Chen Z., Lan J., Che J., RA Ge C., Shi H., Pan Z., Liu X.; RT "Fjat-21945."; RL Submitted (AUG-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KOP82232.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LITN01000002; KOP82232.1; -; Genomic_DNA. DR RefSeq; WP_053475760.1; NZ_LITN01000002.1. DR EnsemblBacteria; KOP82232; KOP82232; AMS60_06825. DR PATRIC; fig|1581033.3.peg.2594; -. DR Proteomes; UP000036921; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000036921}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000036921}. FT DOMAIN 199 361 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 418 AA; 47935 MW; E1DFE8F961305472 CRC64; MEQKTEFEKV ILVGCQTNED DQRFGYSMDE LGSLTETAKG KVVSTVTQKR ERIHPATYIG KGKVAELTAL QEELEADLII FNDELSPSQV RNLSRDFEAR IIDRTQLILD IFAGRARSKE GKLQVELAQL QYLLPRLMGQ GTQLSRLGAG IGTRGPGETK LESDRRHIRN RINDIKTQLE VIVKHRDRYR ERRKKNKAFQ IALVGYTNAG KSTLFNRLTE ADSFEENQLF ATLDPMTRKV ILPSGFLTLL TDTVGFIQDL PTTLIAAFRS TLEEVKEANL LLHLVDSSSP DYYQHEQTVN KLLEDLENEK IPQIVVYNKK DLQHSDFVPT AKTKTIQISA FDEYDRNNLM KLLEEIVLSM MSFYHVEVPS TEGKLLSQLK NETILRELSF HEEKQIYICK GYYLEDHQIA GQISKYKI // ID A0A0M1NNI7_9BACI Unreviewed; 417 AA. AC A0A0M1NNI7; DT 11-NOV-2015, integrated into UniProtKB/TrEMBL. DT 11-NOV-2015, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=AM233_05440 {ECO:0000313|EMBL:KOR83605.1}; OS Bacillus sp. FJAT-22058. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus. OX NCBI_TaxID=1581037 {ECO:0000313|EMBL:KOR83605.1, ECO:0000313|Proteomes:UP000037205}; RN [1] {ECO:0000313|Proteomes:UP000037205} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=FJAT-22058 {ECO:0000313|Proteomes:UP000037205}; RA Liu B., Wang J., Zhu Y., Liu G., Chen Q., Chen Z., Lan J., Che J., RA Ge C., Shi H., Pan Z., Liu X.; RT "Genome sequencing project for genomic taxonomy and phylogenomics of RT Bacillus-like bacteria."; RL Submitted (AUG-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KOR83605.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LIUR01000001; KOR83605.1; -; Genomic_DNA. DR RefSeq; WP_053534436.1; NZ_LIUR01000001.1. DR EnsemblBacteria; KOR83605; KOR83605; AM233_05440. DR PATRIC; fig|1581037.3.peg.1345; -. DR Proteomes; UP000037205; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000037205}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000037205}. FT DOMAIN 198 360 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 417 AA; 47427 MW; 8DA88D6892BCC531 CRC64; MEEAIKETAV LIGCQTTETS EHFEYSLDEL ASLAKTANAE VLMTISQKRE SVDPATYIGK GKVEELRNLE EELEPDLFIF NDELSPSQIR NLSKQLEARV IDRTQLILDI FAQRARSREG KLQVELAQLQ YLLPRLVGQG TAMSRLGGGI GTRGPGETKL ESDRRHIRGK IDEIKQQLSG IVKHRERYRD RRKRNKTFQI ALVGYTNAGK STLFNRLTEA DSYEENQLFA TLDPMTRKAI LPSGFTVLLT DTVGFIQDLP TSLIAAFRST LEEVKEADLL LHVVDSSSTD YFNHQKTVQD LLNDLDVPSI PQLTLYNKKD KVHADFVRSA SRASLMISAY EQSDLNEIME EIEKYVIEEM IPYHVFLPSR EGKLLSQLKN ETILRTLSFN EESERYECKG FCLADHPITG QLEKYSL // ID A0A0M1NSU7_9BACI Unreviewed; 421 AA. AC A0A0M1NSU7; DT 11-NOV-2015, integrated into UniProtKB/TrEMBL. DT 11-NOV-2015, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=AM233_13035 {ECO:0000313|EMBL:KOR84899.1}; OS Bacillus sp. FJAT-22058. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus. OX NCBI_TaxID=1581037 {ECO:0000313|EMBL:KOR84899.1, ECO:0000313|Proteomes:UP000037205}; RN [1] {ECO:0000313|Proteomes:UP000037205} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=FJAT-22058 {ECO:0000313|Proteomes:UP000037205}; RA Liu B., Wang J., Zhu Y., Liu G., Chen Q., Chen Z., Lan J., Che J., RA Ge C., Shi H., Pan Z., Liu X.; RT "Genome sequencing project for genomic taxonomy and phylogenomics of RT Bacillus-like bacteria."; RL Submitted (AUG-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KOR84899.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LIUR01000001; KOR84899.1; -; Genomic_DNA. DR RefSeq; WP_054398354.1; NZ_LIUR01000001.1. DR EnsemblBacteria; KOR84899; KOR84899; AM233_13035. DR PATRIC; fig|1581037.3.peg.3071; -. DR Proteomes; UP000037205; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000037205}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000037205}. FT DOMAIN 197 365 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 156 183 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 421 AA; 47992 MW; 3C44F5DCE51406E4 CRC64; MMELQQRAIL VGVNLNGSKD FEYSMEELAN LTEACEVEVA GTITQNLHRV NSSHFIGTGK IEEVKNLVEH KEANVVIFND QLSPSQLRNL ERDMDCKVID RTILILDIFA HRAKTKEAQL QVEVAKLQYM LPRLVGLRES LGRQSGGVGT NKGAGEKQLE LDRRRIEENI SVLNKELEDL VAHRQTQRKQ RKKNAIPVVS LVGYTNAGKS SIMNALIEVF HPTAEKQVLE KDMLFATLET SVRNIPLPDK KEFLLTDTVG FVSKLPHHLV KAFRSTLEEV VEADLLIHVV DFSNPNHEQQ IEITEKTLND IGIKGIPTIF AYNKADLTDL DIPQVNRGSV YMSAKNKVGI EELINQIRKH IFVDYTHCEM LIPFDQGQLV SYFNENGHIT ETEYEAIGYR LKLECKKTDY EKYKRYVIHP E // ID A0A0M2CV93_9MICC Unreviewed; 542 AA. AC A0A0M2CV93; DT 11-NOV-2015, integrated into UniProtKB/TrEMBL. DT 11-NOV-2015, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=H488_0108915 {ECO:0000313|EMBL:EYT52611.1}; OS Kocuria sp. UCD-OTCP. OC Bacteria; Actinobacteria; Micrococcales; Micrococcaceae; Kocuria. OX NCBI_TaxID=1292021 {ECO:0000313|EMBL:EYT52611.1, ECO:0000313|Proteomes:UP000033173}; RN [1] {ECO:0000313|EMBL:EYT52611.1, ECO:0000313|Proteomes:UP000033173} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=UCD-OTCP {ECO:0000313|EMBL:EYT52611.1, RC ECO:0000313|Proteomes:UP000033173}; RX PubMed=23661474; RA Coil D.A., Doctor J.I., Lang J.M., Darling A.E., Eisen J.A.; RT "Draft Genome Sequence of Kocuria sp. Strain UCD-OTCP (Phylum RT Actinobacteria)."; RL Genome Announc. 1:E00172-13(2013). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EYT52611.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AOSQ01000017; EYT52611.1; -; Genomic_DNA. DR RefSeq; WP_017832904.1; NZ_AOSQ01000017.1. DR EnsemblBacteria; EYT52611; EYT52611; H488_0108915. DR Proteomes; UP000033173; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 2. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000033173}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}. FT DOMAIN 312 477 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 542 AA; 59575 MW; 99BDC9AD12399CF6 CRC64; MTHPRETPAE PRDAAEPENG LSRQDLEDVV ERVLSRARAR EQAAGQDTAP EDDSTAPGRF SGRARELADA EDGHTVHDGD QQDLEERRAL RRVAGLSTEL EDVTELEYRQ LRLERVVLAG LWTEGTLAEA ENSLRELAAL AETAGSEVLD GIVQRRLKPD PATYLGSGKA KELRDIVAAT GADTVVVDSE LAPSQRRGLE DVVKVKVIDR TGLILDIFAQ HAKSKEGKAQ VELAQLEYLL PRLRGWGESL SRQAGGRAAA GEGIGSRGPG ETKIELDRRR IRTRMAKLRR EIAAMKPARE TKRLNRRRHS VPSVAIAGYT NAGKSSLLNR LTDAGVLVEN ALFATLDPTV RRAQTPDGIG YTLSDTVGFV RSLPTQLVEA FRSTLEEVAD SDLILHVVDA SHPDPEGQIR AVRQVFTDID AQNIPEIIAL NKVDAADPFV VERIKQRERN VVVVSARTGE GIEELRQRIS ESIPRPETVL DLLVPYQRGD VVSRLHDWDA EILRTEHLPE GTHLLVKVRE DLAAELAEFA PERAPGFGAE SA // ID A0A0M2GYH9_9MICO Unreviewed; 505 AA. AC A0A0M2GYH9; DT 11-NOV-2015, integrated into UniProtKB/TrEMBL. DT 11-NOV-2015, sequence version 1. DT 07-JUN-2017, entry version 10. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:KJL39127.1}; GN ORFNames=RS81_02221 {ECO:0000313|EMBL:KJL39127.1}; OS Microbacterium ketosireducens. OC Bacteria; Actinobacteria; Micrococcales; Microbacteriaceae; OC Microbacterium. OX NCBI_TaxID=92835 {ECO:0000313|EMBL:KJL39127.1, ECO:0000313|Proteomes:UP000033956}; RN [1] {ECO:0000313|EMBL:KJL39127.1, ECO:0000313|Proteomes:UP000033956} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 12510 {ECO:0000313|EMBL:KJL39127.1, RC ECO:0000313|Proteomes:UP000033956}; RA Corretto E.; RT "Draft genome sequences of ten Microbacterium spp. with emphasis on RT heavy metal contaminated environments."; RL Submitted (FEB-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KJL39127.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JYIZ01000052; KJL39127.1; -; Genomic_DNA. DR RefSeq; WP_045276149.1; NZ_JYIZ01000052.1. DR EnsemblBacteria; KJL39127; KJL39127; RS81_02221. DR PATRIC; fig|92835.4.peg.2256; -. DR Proteomes; UP000033956; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000033956}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000033956}. FT DOMAIN 287 453 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 505 AA; 54643 MW; A0BD8BF6B9E3C3C9 CRC64; MTDTTTPQST DESPVDPVDR VLSRAEARSG VRLFGGAQAL QDQATVGRAD SDGEQWDREE RAALRRVPGL STELEDVTEV EYRQLRLENV VLVGVHPQGA TEDAENSLRE LAALAETAGA VVLDGVLQRR PNPDPATYVG RGKADELRDI VAAVGADTVI ADTELAPSQR RALEDVVKVK VIDRTTVILD IFSQHAKSRE GKAQVELAQL EYLLPRLRGW GDSMSRQAGG QVGAGGAGMG SRGPGETKIE LDRRRIRTKM ALLRKQIRDF APARDAKRAE RKRNTIPSVA IAGYTNAGKS SLLNRLTSAG VLVENALFAT LDATVRRSQT DDGRIFTLTD TVGFVRNLPH QLVEAFRSTL EEVGQADVIV HVVDGSHPDP AAQLATVRDV IGDVGARDIP EIVVFNKADL IDDDTRLLLR GLEPKAVFAS SRTGEGIDEL RELVEETLPV PAVEIRAVVP YDRGDLVSAV HEHGMLLSQT HEEAGTVIHA RVGELLAARL APFAV // ID A0A0M2HIZ7_9MICO Unreviewed; 505 AA. AC A0A0M2HIZ7; DT 11-NOV-2015, integrated into UniProtKB/TrEMBL. DT 11-NOV-2015, sequence version 1. DT 07-JUN-2017, entry version 10. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:KJL44287.1}; GN ORFNames=RS82_00930 {ECO:0000313|EMBL:KJL44287.1}; OS Microbacterium trichothecenolyticum. OC Bacteria; Actinobacteria; Micrococcales; Microbacteriaceae; OC Microbacterium. OX NCBI_TaxID=69370 {ECO:0000313|EMBL:KJL44287.1, ECO:0000313|Proteomes:UP000034098}; RN [1] {ECO:0000313|EMBL:KJL44287.1, ECO:0000313|Proteomes:UP000034098} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 8608 {ECO:0000313|EMBL:KJL44287.1, RC ECO:0000313|Proteomes:UP000034098}; RA Corretto E.; RT "Draft genome sequences of ten Microbacterium spp. with emphasis on RT heavy metal contaminated environments."; RL Submitted (FEB-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KJL44287.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JYJA01000027; KJL44287.1; -; Genomic_DNA. DR RefSeq; WP_045297263.1; NZ_JYJA01000027.1. DR EnsemblBacteria; KJL44287; KJL44287; RS82_00930. DR PATRIC; fig|69370.6.peg.961; -. DR Proteomes; UP000034098; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000034098}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000034098}. FT DOMAIN 287 452 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 505 AA; 54781 MW; 076506A3B30D782C CRC64; MTDTTTPQST DETPVDPVDR VLARAEARSG VHVFGAAQAL QDEATIGRAD TDGEQWDREE RAALRRVPGL STELEDVTEV EYRQLRLENV VLVGVHPQGE TEDAENSLRE LSALAETAGA VVLDGVLQRR PHPDPATYVG RGKAEELRDI VASVGADTVI ADTELAPSQR RALEDVVKVK VIDRTTVILD IFSQHAKSRE GKAQVELAQL EYLLPRLRGW GDSMSRQAGG QVGAGGAGMG SRGPGETKIE LDRRRIRTRM AQLRKQIRDF APARDAKRAE RKRNTIPSVA IAGYTNAGKS SLLNRLTSAG VLVENALFAT LDATVRRTET GDGRIYTLTD TVGFVRNLPH QLVEAFRSTL EEVGDADVIV HVVDGSHPDP AAQLATVRDV IGDVGARDIP EIIVFNKADL IDDDARLLLR GLEPKAVFAS SRTGEGIDEL RALIEETLPL PAVEVRALVP YDRGDLVSAI HEQGMILSQE HEEGGTAVHA RVGQHLAARL SPFTV // ID A0A0M2HNW7_9MICO Unreviewed; 503 AA. AC A0A0M2HNW7; DT 11-NOV-2015, integrated into UniProtKB/TrEMBL. DT 11-NOV-2015, sequence version 1. DT 07-JUN-2017, entry version 10. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:KJL46628.1}; GN ORFNames=RS84_03268 {ECO:0000313|EMBL:KJL46628.1}; OS Microbacterium hydrocarbonoxydans. OC Bacteria; Actinobacteria; Micrococcales; Microbacteriaceae; OC Microbacterium. OX NCBI_TaxID=273678 {ECO:0000313|EMBL:KJL46628.1, ECO:0000313|Proteomes:UP000033900}; RN [1] {ECO:0000313|EMBL:KJL46628.1, ECO:0000313|Proteomes:UP000033900} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SA35 {ECO:0000313|EMBL:KJL46628.1, RC ECO:0000313|Proteomes:UP000033900}; RA Corretto E.; RT "Draft genome sequences of ten Microbacterium spp. with emphasis on RT heavy metal contaminated environments."; RL Submitted (FEB-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KJL46628.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JYJB01000010; KJL46628.1; -; Genomic_DNA. DR RefSeq; WP_045258778.1; NZ_JYJB01000010.1. DR EnsemblBacteria; KJL46628; KJL46628; RS84_03268. DR PATRIC; fig|273678.4.peg.3262; -. DR Proteomes; UP000033900; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 2. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000033900}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000033900}. FT DOMAIN 283 448 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 503 AA; 54347 MW; 472035AD80DAEB5A CRC64; MTDTSKHSTD DEAVERVLAN ADRRTEARVF GAAQALQDAA TAGYGSGDGD QWDLEDRHAL RRVQGLSTEL EDVTEVEYRQ LRLENVVLVG VYPQGAQEDA ENSLRELAAL AETAGAVVLD GVLQRRPHPD AATYIGRGKA QELKDIVAAT GADTVIADTE LAPSQRRALE DVVKVKVIDR TTVILDIFSQ HAKSREGKAQ VELAQLEYLL PRLRGWGESM SRQAGGQVGA GGAGMGSRGP GETKIELDRR RIRTKMALLR KQIRDFAPGR EAKRAERKRN TIPSVAIAGY TNAGKSSLLN ALTSAGVLVE NALFATLDAT VRRSETADGR VYTLTDTVGF VRNLPHQLVE AFRSTLEEVG DADVVLHVVD GSHPDPAGQL QTVRDVMGDV GVRDMPEIVV FNKADLIDDD ERLVLRGLEP KAHFVSSRSG EGIAELRAAI EEALPTPAVE VTAVIPYDRG DLVAAIHETG MLLSVDHRED GTAVHARVSE RLAAELAEFA TAD // ID A0A0M2JZA6_9MYCO Unreviewed; 482 AA. AC A0A0M2JZA6; DT 11-NOV-2015, integrated into UniProtKB/TrEMBL. DT 11-NOV-2015, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=WN67_21220 {ECO:0000313|EMBL:KKE99961.1}; OS Mycobacterium obuense. OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae; OC Mycobacterium. OX NCBI_TaxID=1807 {ECO:0000313|EMBL:KKE99961.1, ECO:0000313|Proteomes:UP000034150}; RN [1] {ECO:0000313|EMBL:KKE99961.1, ECO:0000313|Proteomes:UP000034150} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=UC1 {ECO:0000313|EMBL:KKE99961.1, RC ECO:0000313|Proteomes:UP000034150}; RA Greninger A.L., Cunningham G., Chiu C.Y., Miller S.; RT "Genome sequence of Mycobacterium obuense UC1."; RL Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KKE99961.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LAUZ02000085; KKE99961.1; -; Genomic_DNA. DR RefSeq; WP_046365028.1; NZ_LAUZ02000085.1. DR EnsemblBacteria; KKE99961; KKE99961; WN67_21220. DR PATRIC; fig|1807.13.peg.5076; -. DR Proteomes; UP000034150; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000313|EMBL:KKE99961.1}; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000034150}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900, KW ECO:0000313|EMBL:KKE99961.1}. FT DOMAIN 259 428 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 218 245 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 482 AA; 51570 MW; 39B781B4D8591925 CRC64; MNSVLRANLD SPMTSPEFRN DTPSAGELAL EERAALRRVA GLSTELADIS EVEYRQLRLE RVVLVGVWTE GSAADADASL AELAALAETA GSEVLEGVIQ RRDKPDPATY IGSGKAAELR EVVIATGADT VICDGELSPA QLNALEKVVK VKVIDRTALI LDIFAQHATS REGKAQVSLA QMEYMLPRLR GWGESMSRQA GGRAGGAGGG VGTRGPGETK IETDRRRIRE RMAKLRREIK DMKKIRDTQR SGRRRSEVPS VAIVGYTNAG KSSLLNALTG AGVLVENALF ATLEPTTRRG QFDDGRPFVL TDTVGFVRHL PTQLVEAFRS TLEEVVDAEL LVHVVDGSDV NPLAQINAVR AVINDVVAEY GIAAPRELLV VNKTDAASGL MLATLRRALP GAVFVSAHTG DGLDQLRATM AELVEPTDTA VDVTIPYDRG DLVARMHSEG RIDATEHTEA GTRITARVPV ALAAGLAEFA TA // ID A0A0M2KH37_9GAMM Unreviewed; 426 AA. AC A0A0M2KH37; DT 11-NOV-2015, integrated into UniProtKB/TrEMBL. DT 11-NOV-2015, sequence version 1. DT 30-AUG-2017, entry version 12. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=SY86_13790 {ECO:0000313|EMBL:KKF36266.1}; OS Erwinia tracheiphila. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; OC Erwiniaceae; Erwinia. OX NCBI_TaxID=65700 {ECO:0000313|EMBL:KKF36266.1, ECO:0000313|Proteomes:UP000033924}; RN [1] {ECO:0000313|EMBL:KKF36266.1, ECO:0000313|Proteomes:UP000033924} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BuffGH {ECO:0000313|EMBL:KKF36266.1, RC ECO:0000313|Proteomes:UP000033924}; RA Shapiro L.R.; RT "Erwinia tracheiphila."; RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KKF36266.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JXNU01000003; KKF36266.1; -; Genomic_DNA. DR RefSeq; WP_016190787.1; NZ_JXNU01000003.1. DR EnsemblBacteria; KKF36266; KKF36266; SY86_13790. DR PATRIC; fig|65700.7.peg.3471; -. DR Proteomes; UP000033924; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000033924}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000033924}. FT DOMAIN 198 365 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 426 AA; 48128 MW; 371C1175CD3B74F1 CRC64; MFDRYDAGEQ AVLVHIYFSQ EKDTEDLQEF ESLASSAGVC ALRVVIGSRK VPHPKYFVGE GKAIEIAEAV KSSGASVVLF DHSLSPAQER NLEKLCECRV IDRTGLILDI FAQRARTHEG KLQVELAQLR HLATRLVRGW THLERQKGGI GLRGPGETQL ETDRRLLRNR ITLILSRLER VEKQREQGRQ ARHKADIATI SLVGYTNAGK STLFNRLTSA DVYAADQLFA TLDPTLRRID VADVGEVVLA DTVGFIRHLP HDLVAAFKAT LQETRQAMLL MHVIDAADLR INENIAAVEE VLTEIESDEI PTLQVMNKID MLEDFVPRID RNEENLPVRV WLSAQTGEGI PLLFQALTER LAGEIAEYKL RLPPETGRLR SRFYQLQAIV KEWNEDDGSV GLAVRMPVVD WRRLCKQEPE LVNYII // ID A0A0M2LJ50_9SPHN Unreviewed; 435 AA. AC A0A0M2LJ50; DT 11-NOV-2015, integrated into UniProtKB/TrEMBL. DT 11-NOV-2015, sequence version 1. DT 07-JUN-2017, entry version 10. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=XM50_14870 {ECO:0000313|EMBL:KKI17575.1}; OS Sphingomonas sp. Ag1. OC Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales; OC Sphingomonadaceae; Sphingomonas. OX NCBI_TaxID=1642949 {ECO:0000313|EMBL:KKI17575.1, ECO:0000313|Proteomes:UP000033997}; RN [1] {ECO:0000313|EMBL:KKI17575.1, ECO:0000313|Proteomes:UP000033997} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Ag1 {ECO:0000313|EMBL:KKI17575.1, RC ECO:0000313|Proteomes:UP000033997}; RA Pei D., Yu W., Kukutla P., Xu J.; RT "Draft Genome Sequences of Sphingomonas sp. Ag1 from Mosquito RT Anopheles gambiae."; RL Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KKI17575.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LAZX01000094; KKI17575.1; -; Genomic_DNA. DR RefSeq; WP_046410582.1; NZ_LAZX01000094.1. DR EnsemblBacteria; KKI17575; KKI17575; XM50_14870. DR PATRIC; fig|1642949.3.peg.668; -. DR Proteomes; UP000033997; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000033997}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000033997}. FT DOMAIN 208 377 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 174 201 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 435 AA; 47712 MW; C631D6E6B108C42D CRC64; MSTGFDRDRE EFARGARAIV VYPDLGGSSR DADARLEETA GLAAAIGVDV VERHAVRVRT PRAATLIGSG QVEQLATLGR QEEATLFVFD AALSPIQQRN LETQLEAKVI DRTGLILEIF GERAATAEGR LQVELAHLDY QAGRLVRSWT HLERQRGGFG FLGGPGETQI EADRRLIRDR MARLRRELDQ VTRTRGLHRE RRQRAPWPVI ALVGYTNAGK STLFNRLTGA HVMAEDLLFA TLDPTLRQIS LPGIDKAILS DTVGFVSELP TQLVAAFKAT LEEVISADLL VHVRDVAHPD TTAQKADVEA VLAEIGVSEA TPRIEAWNKI DLLDGPDRDH LLAEAARRDD VVPLSAIKGE GVDELVRLLS DRLTQGHQRY SIRLATSDGA GAAWLHQHGE VIDQVIEGDT AIYEVRMAPG DFARFNERSA GAAET // ID A0A0M2LRR2_9MICO Unreviewed; 518 AA. AC A0A0M2LRR2; DT 11-NOV-2015, integrated into UniProtKB/TrEMBL. DT 11-NOV-2015, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=XM48_10985 {ECO:0000313|EMBL:KKI18414.1}; OS Leucobacter sp. Ag1. OC Bacteria; Actinobacteria; Micrococcales; Microbacteriaceae; OC Leucobacter. OX NCBI_TaxID=1642040 {ECO:0000313|EMBL:KKI18414.1, ECO:0000313|Proteomes:UP000033836}; RN [1] {ECO:0000313|EMBL:KKI18414.1, ECO:0000313|Proteomes:UP000033836} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Ag1 {ECO:0000313|EMBL:KKI18414.1, RC ECO:0000313|Proteomes:UP000033836}; RA Pei D., Kukutla P., Yu W., Xu J.; RT "Draft Genome Sequences of Leucobacter sp. Ag1 from Mosquito Anopheles RT gambiae."; RL Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KKI18414.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LAYO01000102; KKI18414.1; -; Genomic_DNA. DR RefSeq; WP_046455867.1; NZ_LAYO01000102.1. DR EnsemblBacteria; KKI18414; KKI18414; XM48_10985. DR PATRIC; fig|1642040.3.peg.165; -. DR Proteomes; UP000033836; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000033836}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000033836}. FT DOMAIN 298 463 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 518 AA; 56121 MW; E068C2637EF2E1CF CRC64; MTKRISEDPG TDVTDPIERI LARASGSGST GATVIRDGGV ENLTGGAQAL GDEAHDQLSA DIDAIRLERE QRASLRRVPG LSTELEDVTE VEYRQLRLEN VVLIGVYPQG SLDDAENSLR ELAALAETAG AQVLDGLLQR RPHPDKSTYL GKGKAHELAE LVASVGADTV VADTELAPSQ RRALEDVVKV KVIDRTAVIL DIFSQHAKSR EGKAQVELAQ LEYLLPRLRG WGESMSRQAG GQVGSGGAGM GSRGPGETKM ELDRRKIHTR MAKLRKQIAG FAPAREAKRA NRKRGEVPSV AIAGYTNAGK SSLLNRLTGS AALVQNQLFA TLDTTVRHAE TADGRTFTYS DTVGFVRNLP HQLVEAFRST FEEVGDADVV LHIVDGSHPD PESQLRTVRD VIAEVDAQGI PEIVVFNKSD LIDDAQRLVL HGLAPDAVFA SARTGEGLEE LRARIDVALP VPDREVDVVI PYDRGDLVAE LHERNRVLET EYVETGTRVR AFVTGETVAK LEPFLRAG // ID A0A0M2NMM2_9FIRM Unreviewed; 578 AA. AC A0A0M2NMM2; DT 11-NOV-2015, integrated into UniProtKB/TrEMBL. DT 11-NOV-2015, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=CHK_0349 {ECO:0000313|EMBL:KKI52241.1}; OS Catabacter hongkongensis. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Catabacteriaceae; OC Catabacter. OX NCBI_TaxID=270498 {ECO:0000313|EMBL:KKI52241.1, ECO:0000313|Proteomes:UP000034076}; RN [1] {ECO:0000313|EMBL:KKI52241.1, ECO:0000313|Proteomes:UP000034076} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=HKU16 {ECO:0000313|EMBL:KKI52241.1, RC ECO:0000313|Proteomes:UP000034076}; RA Lau S.K., Teng J.L., Huang Y., Curreem S.O., Tsui S.K., Woo P.C.; RT "Draft genome sequence of bacteremic isolate Catabacter hongkongensis RT type strain HKU16T."; RL Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KKI52241.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LAYJ01000033; KKI52241.1; -; Genomic_DNA. DR RefSeq; WP_046442264.1; NZ_LLYX01000020.1. DR EnsemblBacteria; KKI52241; KKI52241; CHK_0349. DR PATRIC; fig|270498.16.peg.2957; -. DR Proteomes; UP000034076; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000034076}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000034076}. FT DOMAIN 368 528 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 578 AA; 63860 MW; 2C7A18FFE785E5CD CRC64; MEIHGNLNGI RDSIKEELNE LYDYKMQTQE FASVSLIEEM ARLTDILGKE ISVFLSRGGK VLDVSVGDDK SVKMPYMRMR RGFEGVSGVR SLHTHPNGSP MLSEVDIGTL ISTRFDAMAA ISVRNGKAAM MCVGFLGDAL DQVKIAGPFR AGRIPQQALM QEIAFATERV SRLVRMHDTQ GEAERVLLVG LNAPEESMEE LRRLAQTADA EVVGVVTQSR ERDRAYYIGK GKAQELSLQL AAADADAVIF NDELTPLETK NLEELLGVKV IDRTMLILDI FAKRARTREG RLQVELAQLQ YTLPRLQGEG TALSRLGGGI GTRGPGEKKI EVDRRRIRRR IFELTQDIEK VKQQRDLRRS ARRENEVKEV ALVGYTNAGK SSLLNALTDA GVLAEDKLFA TLDPVTRKVM LPDVGETVFT DTVGFIEKLP HDLVSAFRST LEEVTHADLL LCVTDAANPN AQKQMDVVDG LLESLGAAEK PKITVMNKAD LLAVVPPDEA DTIYISTRSG YGMEALLAKA AEKLAPQMMS YEGRIGYDKG DLLALVNRHG KEIELEYLPE GIEIKAKLPV ETIKKLKS // ID A0A0M2PMG6_9BACI Unreviewed; 435 AA. AC A0A0M2PMG6; DT 11-NOV-2015, integrated into UniProtKB/TrEMBL. DT 11-NOV-2015, sequence version 1. DT 07-JUN-2017, entry version 10. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=WQ54_11685 {ECO:0000313|EMBL:KKI91948.1}; OS Bacillus sp. SA1-12. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus. OX NCBI_TaxID=1455638 {ECO:0000313|EMBL:KKI91948.1, ECO:0000313|Proteomes:UP000034887}; RN [1] {ECO:0000313|EMBL:KKI91948.1, ECO:0000313|Proteomes:UP000034887} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SA1-12 {ECO:0000313|EMBL:KKI91948.1, RC ECO:0000313|Proteomes:UP000034887}; RA Kumar A., Mathan Kumar R., Kaur N., Kumar N., Singh N.K., Kaur G., RA Mayilraj S.; RT "Taxonomic description and genome sequence of Bacillus tuticoriensis RT sp. nov., a novel member of the genus Bacillus isolated from solar RT saltern."; RL Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KKI91948.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LATZ01000017; KKI91948.1; -; Genomic_DNA. DR RefSeq; WP_046516639.1; NZ_LATZ01000017.1. DR EnsemblBacteria; KKI91948; KKI91948; WQ54_11685. DR PATRIC; fig|1455638.3.peg.2586; -. DR Proteomes; UP000034887; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000034887}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}. FT DOMAIN 210 372 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 435 AA; 49857 MW; 102EA8F3A1FC5641 CRC64; MQKKEWLLLN NTLDHLKEKV ILVGCQLQEM HDDHFQYSME ELASLTKTAN GEVLTSIIQK RERPHPATYI GKGKVDELLN LVKELEPDLV IFNDELSPSQ LRNLSSTLDV RIIDRTQLIL DIFAQRAKTK EGKLQVELAQ LQYLLPRLMG QGIALSRQGG GIGTRGPGET QLETDRRHIR NRIHEIKQQL STVVRHRNRY RERRKKNQAF QIALVGYTNA GKSTIFNRLT TAESFEENLL FATLDPLTRK VLLPSNYQAL ITDTVGFIQD LPTTLVAAFR STLEEVREAN LILHVVDSSN EDYANHEQTV YKLLEQLEVT DIPVLTVYNK KDVALDSFVP SPKEDYIHIT AFSEEDLHKL MTHVERFIKD SMNLYNVRIP ASEGRLISQL KTESLVNKLN FNEQDELYEI EGYVLPTHSI NGQLEKYNGE GKNNV // ID A0A0M2PTN0_PROHO Unreviewed; 560 AA. AC A0A0M2PTN0; DT 11-NOV-2015, integrated into UniProtKB/TrEMBL. DT 11-NOV-2015, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=PROH_12840 {ECO:0000313|EMBL:KKI99479.1}; OS Prochlorothrix hollandica PCC 9006 = CALU 1027. OC Bacteria; Cyanobacteria; Synechococcales; Pseudanabaenaceae; OC Prochlorothrix. OX NCBI_TaxID=317619 {ECO:0000313|EMBL:KKI99479.1, ECO:0000313|Proteomes:UP000034681}; RN [1] {ECO:0000313|EMBL:KKI99479.1, ECO:0000313|Proteomes:UP000034681} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CALU 1027 {ECO:0000313|EMBL:KKI99479.1}; RA Shanker A., Yadav P., Khan S., Sharma V.; RL Submitted (APR-2012) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:KKI99479.1, ECO:0000313|Proteomes:UP000034681} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CALU 1027 {ECO:0000313|EMBL:KKI99479.1}; RA Syromyatnikov M.Y., Popov V.N.; RL Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KKI99479.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AJTX02000005; KKI99479.1; -; Genomic_DNA. DR RefSeq; WP_026099866.1; NZ_KB235942.1. DR Proteomes; UP000034681; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000034681}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000034681}. FT DOMAIN 389 559 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 348 382 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 560 AA; 61931 MW; F26DB8AA570DD5DE CRC64; METIYGKLNG LKSSHLKQLQ RLYQQRIPGD RLTTPEFAQR LAALSSEMGQ PLSVYLNRRG QVIRVGVGTP RQTQIPPLEL PRYGAERLCG IRCITTDLKG EAPSSATLTA MVLQRLDVLV SLNITGQGFT RRGGTATGYV ETTYVAHLLS QPDTPWQVLP PQSLEVVAEQ DFLDLVEGLE EEFRQDVVGN VVDLDHDRVI VVGLKTQGRR DLQFEQGLTE VRRLVESAGG EVLDTLRQNR DRPHPQTVVG EGKVEEIALA AQTLGANLIV FDRDLSPAQG RNLERQIGLR VVDRTQVILD IFAQRAQSGA GKLQVELAQL QYCMPRLTGQ GQAMSRLGGG IGTRGPGETQ LETERRTIQQ RISRLQREVS QLQAHRARLR HQRQHQDVPS VALVGYTNAG KSTLLNVLTS AEVYVADQLF ATLDPTTRRL VLPQTEATPP KALLVTDTVG FIHELPPSLV DAFRATLEEV TESDALLHVV DLSHDAWKTQ IEAVNKILGE MSMPPGPSLL VFNKVDQVPS EVLATAQEHY PQAVFVSATD RLGLTTLRQR IEQLVTYAQL // ID A0A0M2R1F7_9PROT Unreviewed; 445 AA. AC A0A0M2R1F7; DT 11-NOV-2015, integrated into UniProtKB/TrEMBL. DT 11-NOV-2015, sequence version 1. DT 07-JUN-2017, entry version 12. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=WH95_17955 {ECO:0000313|EMBL:KKJ75481.1}; OS Kiloniella litopenaei. OC Bacteria; Proteobacteria; Alphaproteobacteria; Kiloniellales; OC Kiloniellaceae; Kiloniella. OX NCBI_TaxID=1549748 {ECO:0000313|EMBL:KKJ75481.1, ECO:0000313|Proteomes:UP000034491}; RN [1] {ECO:0000313|EMBL:KKJ75481.1, ECO:0000313|Proteomes:UP000034491} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=P1-1 {ECO:0000313|EMBL:KKJ75481.1, RC ECO:0000313|Proteomes:UP000034491}; RA Shao Z., Wang L., Li X.; RT "Genome sequence of Kiloniella sp. P1-1, isolated from the gut RT microflora of Pacific white shrimp, Penaeus vannamei."; RL Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KKJ75481.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LANI01000031; KKJ75481.1; -; Genomic_DNA. DR RefSeq; WP_046509757.1; NZ_LANI01000031.1. DR EnsemblBacteria; KKJ75481; KKJ75481; WH95_17955. DR PATRIC; fig|1549748.8.peg.2862; -. DR Proteomes; UP000034491; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000034491}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000034491}. FT DOMAIN 211 382 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 445 AA; 50315 MW; 4C5D2D879B8C1020 CRC64; MGSKIIDDGV DRKKQVRAIV LHPELKKGSQ STRSSEARLE EAYGLALAID LEIIRHEVIT VARPKPSTLF GSGIIDKYHD YIHENEVEVV IVDTALTPVQ QRNLEKGWEA KVIDRTGLIL EIFGERARTK EGKLQVDLAQ LSYQRSRLVR SWTHLERQRG GAGFMGGPGE RQIEIDRRLI DEKIVRLKSD LEMVKKTREL HRSARRKVPF PIVSLVGYTN AGKSTLFNRL TESKVFAEDL LFATLDPTMR RVNLPSGREI ILSDTVGFIS ELPTDLIASF RATLEEVREA NVLVHVRDVS HEDTEAQKDD VKAVLNDLEL DPDIQKNMIE VWNKSDLLSD EIKSSLEIQS GHQDTTLLCS AITGEGCSEF LHMVEQLLDA QNLVYEFEIP YENGAALSWL HDNAKVLEQD HHEEGVWVSL SILQADADKF ISKFAINPLE EEPEV // ID A0A0M2RNG4_9ACTN Unreviewed; 487 AA. AC A0A0M2RNG4; DT 11-NOV-2015, integrated into UniProtKB/TrEMBL. DT 11-NOV-2015, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=LQ51_26230 {ECO:0000313|EMBL:KKJ96036.1}; OS Micromonospora sp. HK10. OC Bacteria; Actinobacteria; Micromonosporales; Micromonosporaceae; OC Micromonospora. OX NCBI_TaxID=1538294 {ECO:0000313|EMBL:KKJ96036.1, ECO:0000313|Proteomes:UP000034330}; RN [1] {ECO:0000313|EMBL:KKJ96036.1, ECO:0000313|Proteomes:UP000034330} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=HK10 {ECO:0000313|EMBL:KKJ96036.1, RC ECO:0000313|Proteomes:UP000034330}; RA Talukdar M., Das D., Borah C., Deka Boruah H.P., Bora T.C., RA Singh A.K.; RT "Draft genome sequence of Micromonospora HK10, isolated from Kaziranga RT National park, Assam, India."; RL Submitted (NOV-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KKJ96036.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JTGL01000202; KKJ96036.1; -; Genomic_DNA. DR RefSeq; WP_046563037.1; NZ_KQ058670.1. DR EnsemblBacteria; KKJ96036; KKJ96036; LQ51_26230. DR PATRIC; fig|1538294.3.peg.580; -. DR Proteomes; UP000034330; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000313|EMBL:KKJ96036.1}; KW Complete proteome {ECO:0000313|Proteomes:UP000034330}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900, KW ECO:0000313|EMBL:KKJ96036.1}. FT DOMAIN 255 420 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 487 AA; 53255 MW; 8DB4BD66E927B00E CRC64; MREQETYPPF EDDELDATTG EFELSERQAL RRVPGLSTEL SDITEVEYRQ LRLERVVLVG VWTEGTQDDA DNSLTELAAL AETAGSQVLE GLIQRRNRPD PATYIGRGKV DDLGAVVLAT GADTVICDGE LSPSQLRNLE QRTKVKVVDR TALILDIFAQ HAKSKEGKAQ VELAQLEYLL PRLRGWGETL SRQTGGSGRG GGAGGGVGLR GPGETKLETD RRRIRHRIAR LRREIKGMAT VRQTKRARRT RNSVPAVAIA GYTNAGKSSL LNRLTGAGVL VENALFATLD PTTRRATTSD GRLYTLSDTV GFVRHLPHQI VEAFRSTLEE VADADLVVHV VDGTHPDPEE QVRAVREVLA EVGADRLPEL LVVNKTDAAD EETLLRLKRL WPEAVFVSAH SGRGIDGLRE AVEQRLPRPA VEVRAVLPYD RGDLVARVHR QGEVLSTAHL PEGTLVHVRV GQALAAELAP YRAGDRLTTD ERVGVGG // ID A0A0M2T2N6_9BACI Unreviewed; 420 AA. AC A0A0M2T2N6; DT 11-NOV-2015, integrated into UniProtKB/TrEMBL. DT 11-NOV-2015, sequence version 1. DT 07-JUN-2017, entry version 12. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=WQ57_02170 {ECO:0000313|EMBL:KKK39517.1}; OS Bacillus campisalis. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus. OX NCBI_TaxID=1408103 {ECO:0000313|EMBL:KKK39517.1, ECO:0000313|Proteomes:UP000034166}; RN [1] {ECO:0000313|EMBL:KKK39517.1, ECO:0000313|Proteomes:UP000034166} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SA2-6 {ECO:0000313|EMBL:KKK39517.1, RC ECO:0000313|Proteomes:UP000034166}; RA Mathan Kumar R., Kaur G., Kumar A., Singh N.K., Kaur N., Kumar N., RA Mayilraj S.; RT "Taxonomic description and genome sequence of Bacillus campisalis sp. RT nov., a novel member of the genus Bacillus isolated from solar RT saltern."; RL Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KKK39517.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LAYY01000002; KKK39517.1; -; Genomic_DNA. DR RefSeq; WP_046522090.1; NZ_LAYY01000002.1. DR EnsemblBacteria; KKK39517; KKK39517; WQ57_02170. DR PATRIC; fig|1408103.3.peg.496; -. DR Proteomes; UP000034166; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000034166}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000034166}. FT DOMAIN 200 362 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 420 AA; 47878 MW; FD804BEA8528A079 CRC64; MDPKTASEKA ILVGCQTTLE DDLRFQYSME ELASLTETAQ GTVLISVVQK RDRIHPSTYI GKGKVEELKT LVEEFEADLI IFNDELSPSQ IRNLARELEV RIIDRTQLIL DIFARRARSK EGKLQVELAQ LQYLLPRLMG QGTALSRLGA GIGTRGPGET KLESDRRHIR RRIDDIKGQL EIIVQHRDRY RERRKKNKAF QIALVGYTNA GKSTLFNRLT EADSFEENQL FATLDPMTRK VILPSGFSVL LTDTVGFIQD LPTTLIAAFR STLEEVKEAD LLLHVVDMSN QDYFSHEKTV NKLLEELEVN RIPQITVYNK RDIAHPDFVP VAKSETAFIS AYEEEDRSSL KQKIEQTIIE GMEPFHVLIP SGEGKLLSQL KNETILRELA FSEEQDGYVC RGFALKDHQI TGQLKKYTVR // ID A0A0M2U475_9FIRM Unreviewed; 587 AA. AC A0A0M2U475; DT 11-NOV-2015, integrated into UniProtKB/TrEMBL. DT 11-NOV-2015, sequence version 1. DT 07-JUN-2017, entry version 10. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=SY88_22040 {ECO:0000313|EMBL:KKM08885.1}; OS Clostridiales bacterium PH28_bin88. OC Bacteria; Firmicutes; Clostridia; Clostridiales. OX NCBI_TaxID=1605376 {ECO:0000313|EMBL:KKM08885.1, ECO:0000313|Proteomes:UP000034222}; RN [1] {ECO:0000313|EMBL:KKM08885.1, ECO:0000313|Proteomes:UP000034222} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Robbins S., Tyson G.; RT "High quality genome sequence of Candidatus Suratobacter aromatica."; RL Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KKM08885.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LAKY01000072; KKM08885.1; -; Genomic_DNA. DR PATRIC; fig|1605376.3.peg.454; -. DR Proteomes; UP000034222; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000034222}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000034222}. FT DOMAIN 358 533 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 318 345 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 587 AA; 63947 MW; C036DC4FC7BF15EC CRC64; MEVERTSLVS VDLAQRMAVI SGLLQREVAV YLNRRGRVVG VALGEHDRVS LPDFQGRRGA NRLSGIRCVH THPGGSGMLS GVDCTALSSL RLDCMAALGL QNGLVTDIYA GFLRPATGSP DPEYLVKGPM TLHDLEGFDL MALVEAIEEE LRGEEVLYTG DDRAERAVVV GLDMPSRGSA GYSAGESLAE LAQLVEAAGA TVVDAVLQRK GHVDRAYFIG KGLAEQLSLR LRQLRANLVV LDHEVSGTQA RNLEALMGVK VIDRTAVILD IFAQRAKTRE GKLQVELAQL QYMLPRLVGS GAQMSRLAGG IGTRGPGETK LETDRRHIRR RIEEIEKQLA EVQKHRRVQR AGRRGGTPTV ALVGYTNAGK STLRYCLVKR AASSRTNWED EDAGTNRVFA TLDPTLRGIT LPGGKEVLVG DTVGFIQKLP HQLVSAFRAT LEEVVEADLL LHVIDASSPR WEAQMAAVEQ VLEELGVANK PRINVFNKMD LVEPGAVALP PADGNPCVTV SAVMGTGLDL LLEEMARVLR VETRQVRLSI LYRYSGLLSE LYAAVRVVSV NYQEDGIAVE AVVRDDQMHR YSDYLAP // ID A0A0M2UU96_9BACT Unreviewed; 173 AA. AC A0A0M2UU96; DT 11-NOV-2015, integrated into UniProtKB/TrEMBL. DT 11-NOV-2015, sequence version 1. DT 07-JUN-2017, entry version 4. DE SubName: Full=GTP-binding protein {ECO:0000313|EMBL:KKO19170.1}; GN ORFNames=BROFUL_02153 {ECO:0000313|EMBL:KKO19170.1}; OS Candidatus Brocadia fulgida. OC Bacteria; Planctomycetes; Planctomycetia; Candidatus Brocadiales; OC Candidatus Brocadiaceae; Candidatus Brocadia. OX NCBI_TaxID=380242 {ECO:0000313|EMBL:KKO19170.1, ECO:0000313|Proteomes:UP000034954}; RN [1] {ECO:0000313|EMBL:KKO19170.1, ECO:0000313|Proteomes:UP000034954} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=RU1 {ECO:0000313|EMBL:KKO19170.1}; RX PubMed=24267221; DOI=10.1186/1471-2180-13-265; RA Ferousi C., Speth D.R., Reimann J., Op den Camp H.J., Allen J.W., RA Keltjens J.T., Jetten M.S.; RT "Identification of the type II cytochrome c maturation pathway in RT anammox bacteria by comparative genomics."; RL BMC Microbiol. 13:265-265(2013). CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KKO19170.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LAQJ01000213; KKO19170.1; -; Genomic_DNA. DR PATRIC; fig|380242.3.peg.2687; -. DR Proteomes; UP000034954; Unassembled WGS sequence. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000034954}; KW Reference proteome {ECO:0000313|Proteomes:UP000034954}. FT DOMAIN 31 118 GTP-bdg_N. {ECO:0000259|Pfam:PF13167}. FT DOMAIN 120 161 GTP-bdg_M. {ECO:0000259|Pfam:PF16360}. SQ SEQUENCE 173 AA; 19580 MW; CF4376413C94EAC8 CRC64; MKLKETAFTV RAERAILFRV MLSGEQHENE APLEELRRLA TTAGANVIHT VVQKRPQIDP VYYIGKGKAG ELSGLSKDFH ADVLICDDDL TPAQVRNLEK VIEKKVIDRS ELILDIFATR AKTFQAKLQV ELAQLEYTRP RLKRMWTHLS RIEGGIGTRG PVKNNWKSIS ALC // ID A0A0M2VJH5_9GAMM Unreviewed; 458 AA. AC A0A0M2VJH5; DT 11-NOV-2015, integrated into UniProtKB/TrEMBL. DT 11-NOV-2015, sequence version 1. DT 07-JUN-2017, entry version 10. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=VT06_01440 {ECO:0000313|EMBL:KKO50659.1}; OS Arsukibacterium sp. MJ3. OC Bacteria; Proteobacteria; Gammaproteobacteria; Chromatiales; OC Chromatiaceae; Arsukibacterium. OX NCBI_TaxID=1632859 {ECO:0000313|EMBL:KKO50659.1, ECO:0000313|Proteomes:UP000034895}; RN [1] {ECO:0000313|EMBL:KKO50659.1, ECO:0000313|Proteomes:UP000034895} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MJ3 {ECO:0000313|EMBL:KKO50659.1, RC ECO:0000313|Proteomes:UP000034895}; RA Lylloff J.E., Skov L.B., Jepsen M., Hallin P.F., Sorensen S.J., RA Stougaard P., Glaring M.A.; RT "Draft genome sequences of two protease-producing strains of RT Arsukibacterium isolated from two cold and alkaline environments."; RL Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KKO50659.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LAHP01000001; KKO50659.1; -; Genomic_DNA. DR RefSeq; WP_046552457.1; NZ_LAHP01000001.1. DR EnsemblBacteria; KKO50659; KKO50659; VT06_01440. DR PATRIC; fig|1632859.4.peg.286; -. DR Proteomes; UP000034895; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000034895}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000034895}. FT DOMAIN 223 393 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 188 215 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 458 AA; 50243 MW; C4CD95A9E5C97A6D CRC64; MLNPEKQSLP RALIVAVQLD TVSDVEFESS LAELGDLAKT LGLEVVGKFT QKRSSFDSTA YVGVGKREEI RQFLEDHQAE LDTVLQANPL AIGASVDFVL VDHEISPSQA LNLENEVGCE VMDRTVVILE IFHRNAHSHV AQVQVEIARL SYMAPRLREA AKREGSAGRQ RSGTGGRGSG QSRSQMDRIK VRDRITELQK EIDTMEASRD TQRARRQGQP GLAQVALVGY TNAGKSTLMR ALTGSDVLVA NQLFATLDTK VRTLLPESVP RVLVSDTVGF IKNLPHGLVA SFQSTLDEAL NASLLLHVID ASDPGFEMQL KVTDSVLAEI GADSVPRIRV FNKIDYLDDV VAQNALKAEL QAKYPDSIVI SARQQDDITA LHQAIVHFFQ QQLVEAEIFL PWSAQSLRGE IFASCNVLEE RADDAGAFFR FRAAPAVVAR LREMSDNASW GSGSLKVK // ID A0A0M2WDQ7_9BURK Unreviewed; 385 AA. AC A0A0M2WDQ7; DT 11-NOV-2015, integrated into UniProtKB/TrEMBL. DT 11-NOV-2015, sequence version 1. DT 07-JUN-2017, entry version 10. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:KKO60961.1}; GN ORFNames=VM94_04731 {ECO:0000313|EMBL:KKO60961.1}; OS Janthinobacterium sp. KBS0711. OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Oxalobacteraceae; Janthinobacterium. OX NCBI_TaxID=1649647 {ECO:0000313|EMBL:KKO60961.1, ECO:0000313|Proteomes:UP000034315}; RN [1] {ECO:0000313|EMBL:KKO60961.1, ECO:0000313|Proteomes:UP000034315} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=KBS0711 {ECO:0000313|EMBL:KKO60961.1, RC ECO:0000313|Proteomes:UP000034315}; RA Shoemaker W.R., Muscarella M.E., Lennon J.T.; RT "Genome sequence of the soil bacterium Jantinobacterium sp. KBS0711."; RL Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KKO60961.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LBCO01000035; KKO60961.1; -; Genomic_DNA. DR EnsemblBacteria; KKO60961; KKO60961; VM94_04731. DR PATRIC; fig|1649647.5.peg.4861; -. DR Proteomes; UP000034315; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000034315}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000034315}. FT DOMAIN 168 335 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 385 AA; 42648 MW; C0838DB10DD673DB CRC64; MLLSRSAGAD PISTITAKRS SPDSAYFVGS GKADEIGDVV VNDGLEIVIF NHALSPAQQR NLEKRLNVRV LDRTSLILDI FAQRAKSHEG KLQVELAQLQ HLATRLIRGW THLERQKGGI GLRGPGETQL ETDRRLIGDR VKALRARLEK LHKQRETQRR ARGRNHTFSV SLVGYTNAGK STLFNAVTKA GVYVADQLFA TLDTTSRRVY LGQEVGNVVI SDTVGFVREL PHQLVAAFRA TLEETIHADL LLHVVDAASP VRMEQIEQVN LVLKEIGADH IPQILVWNKI DAAGLEPSVE RDEYATISRV FVSAQKGSGL DLLRDAIVEM ARKAPRSAHL YQNDEAPQED QFDGQYDQHD GAAPDQDEEP GEDDRISTHS QVGTR // ID A0A0M2XQ43_9CORY Unreviewed; 490 AA. AC A0A0M2XQ43; DT 11-NOV-2015, integrated into UniProtKB/TrEMBL. DT 11-NOV-2015, sequence version 1. DT 07-JUN-2017, entry version 10. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=WU86_02855 {ECO:0000313|EMBL:KKO82502.1}; OS Corynebacterium xerosis. OC Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae; OC Corynebacterium. OX NCBI_TaxID=1725 {ECO:0000313|EMBL:KKO82502.1, ECO:0000313|Proteomes:UP000034960}; RN [1] {ECO:0000313|EMBL:KKO82502.1, ECO:0000313|Proteomes:UP000034960} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 373 {ECO:0000313|EMBL:KKO82502.1, RC ECO:0000313|Proteomes:UP000034960}; RA Pacheco L.G., Mattos-Guaraldi A.L., Santos C.S., Veras A.O., RA Guimaraes L.C., Abreu V., Pereira F.L., Soares S.C., Dorella F.A., RA Carvalho A.F., Leal C.G., Figueiredo H.C., Ramos J.N., Vieira V., RA Farfour E., Guiso N., Hirata R.Jr., Ramos R.T., Azevedo V., Silva A.; RT "Draft Genome Sequences of Three Species of Emerging Human-Pathogenic RT Corynebacteria."; RL Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KKO82502.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LAYS01000014; KKO82502.1; -; Genomic_DNA. DR RefSeq; WP_046649844.1; NZ_LAYS01000014.1. DR EnsemblBacteria; KKO82502; KKO82502; WU86_02855. DR PATRIC; fig|1725.5.peg.857; -. DR Proteomes; UP000034960; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000034960}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000034960}. FT DOMAIN 258 427 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 217 244 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 490 AA; 53449 MW; B6D279BCC3A503BE CRC64; MTDTPMNDRD IDDSLRAPQP TTGDLDLEAR SSLRRLTRAA THVTDAEDIT EVEYRQLRLE RVILLGVWTQ GTLAEAEAAM GELAALAETA GSEVLESVLQ RRDKPDPGTY IGSGKVAELR DIVKATGADT VIADGELSPG QLVALEDKLD AKVIDRTMLI LDIFAQHAKS KEGKAQVSLA QMQYLITRLR GWGHSLSRQA GGRAGSNGGV GLRGPGETKI ETDRRRLRQD MARIRKELEG MKTSREIKRA RRKAGHLPRI AIAGYTNAGK SSLLNALTGA GVLVEDALFA TLDPTTRRAE LRDGRTVIMT DTVGFVRHLP TQLVEAFRST LEEILEADLI LHVVDGSDPF PLEQIRTVNT VIGDIAAEQK AEVPPELLVV NKVDLADPAT LAEMRHVLDD VVFTSAATGE GIAELETRIE LALNAMDAHV SVLIPFDRGD LVSRLHEQAT VLDEQYGADG TVLDVRLPRS MARELEEFIV DPELPEPEPA // ID A0A0M2XYK7_9SPHI Unreviewed; 396 AA. AC A0A0M2XYK7; DT 11-NOV-2015, integrated into UniProtKB/TrEMBL. DT 11-NOV-2015, sequence version 1. DT 07-JUN-2017, entry version 10. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=AAW12_05845 {ECO:0000313|EMBL:KKO92270.1}; OS Sphingobacterium sp. Ag1. OC Bacteria; Bacteroidetes; Sphingobacteriia; Sphingobacteriales; OC Sphingobacteriaceae; Sphingobacterium. OX NCBI_TaxID=1643451 {ECO:0000313|EMBL:KKO92270.1, ECO:0000313|Proteomes:UP000034524}; RN [1] {ECO:0000313|EMBL:KKO92270.1, ECO:0000313|Proteomes:UP000034524} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Ag1 {ECO:0000313|EMBL:KKO92270.1, RC ECO:0000313|Proteomes:UP000034524}; RA Pei D., Yu W., Kukutla P., Xu J.; RT "Draft Genome Sequences of Sphingobacterium sp. Ag1 from Mosquito RT Anopheles gambiae."; RL Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KKO92270.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LBGU01000028; KKO92270.1; -; Genomic_DNA. DR RefSeq; WP_046672676.1; NZ_LBGU01000028.1. DR EnsemblBacteria; KKO92270; KKO92270; AAW12_05845. DR PATRIC; fig|1643451.3.peg.1737; -. DR Proteomes; UP000034524; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000034524}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000034524}. FT DOMAIN 204 385 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 396 AA; 45349 MW; C5271528B44E3888 CRC64; MARIKIHDTA IKPETAVLVS VITPSVTETK AKEYLEELEF LVQTAGGETK GMFTQKLGFP DRATFVGSGK LEEIKAYVEA EEIDIVVFDD ELSPSQLRNI EKELKRKILD RSNLILDIFA RHAKTAQAKT QVELAQLQYL LPRLTRMWTH LERQRGGIGM RGPGESQIET DRRIILDKIS LFKERLKAID KQNETQRKNR GEMIRVALVG YTNVGKSTIM NMISKSDVLI ENKLFATLDT TVRKVVIDNL PFLLSDTVGF IRKLPHHLVE CFKSTLDEVR EADVLIHVVD ISHPNFEDHI QAVNETLKDL KALDKPVITV FNKIDLYKPA VEEGHDGEEI EVTLDDFRNS WMAKNSDPAI FLSATNKTNI EEFKQKLYDI IVKMHNERYP YNNLLY // ID A0A0M3AQW1_9SPHN Unreviewed; 443 AA. AC A0A0M3AQW1; DT 11-NOV-2015, integrated into UniProtKB/TrEMBL. DT 11-NOV-2015, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=YP76_06590 {ECO:0000313|EMBL:KKW92602.1}; OS Sphingobium chungbukense. OC Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales; OC Sphingomonadaceae; Sphingobium. OX NCBI_TaxID=56193 {ECO:0000313|EMBL:KKW92602.1, ECO:0000313|Proteomes:UP000033874}; RN [1] {ECO:0000313|EMBL:KKW92602.1, ECO:0000313|Proteomes:UP000033874} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DJ77 {ECO:0000313|EMBL:KKW92602.1, RC ECO:0000313|Proteomes:UP000033874}; RA Kim Y.-C., Chae J.-C.; RT "Genome sequence of aromatic hydrocarbons-degrading Sphingobium RT chungbukense DJ77."; RL Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KKW92602.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LBIC01000003; KKW92602.1; -; Genomic_DNA. DR RefSeq; WP_046762818.1; NZ_LBIC01000003.1. DR EnsemblBacteria; KKW92602; KKW92602; YP76_06590. DR PATRIC; fig|56193.3.peg.1360; -. DR Proteomes; UP000033874; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0016810; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds; IEA:InterPro. DR CDD; cd01878; HflX; 1. DR Gene3D; 2.30.40.10; -; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR011059; Metal-dep_hydrolase_composite. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000033874}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000033874}. FT DOMAIN 209 389 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 443 AA; 48400 MW; 4D7775CC6B7AD1A7 CRC64; MAVFNRDSAD EVSRGARAIV VRADVHGPER RDSDARLEEA RGLALAIGID VRAAQAFRVR DRKPATLFGS GQVDQIATLA RMEEAELVIV DNALSPVQQS NLEKATETKV IDRTGLILEI FGERAATNEG RLQVELAHLD YQAGRLVRSW THLERQRGGF GFLGGPGETQ IEADRRMIRD RMAKIRRELD QVTKTRGLHR ARRQRAPWPV IALVGYTNAG KSTLFNRMTG AEVMAEDLLF ATLDPTMRQI ALPGLDKAIL SDTVGFVSDL PTQLIAAFRA TLEEVLSADL IVHVRDIAHP DTEAQRDDVI DVLSELGVAG EGALEAGEGQ EPPPIIEAWN KLDLLDEDAA ALARETAARR DDVVILSALT GEGVDSLQRT ISARLTAGAQ IHQLRVPLAD GAAMAWLHEH GEVIGSRAEG EAMLVDVRLS DSALARFLKR RAN // ID A0A0M3BUG7_9RHIZ Unreviewed; 444 AA. AC A0A0M3BUG7; DT 11-NOV-2015, integrated into UniProtKB/TrEMBL. DT 11-NOV-2015, sequence version 1. DT 07-JUN-2017, entry version 10. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=YH62_00395 {ECO:0000313|EMBL:KKX34468.1}; OS Rhizobium sp. LC145. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium. OX NCBI_TaxID=1120688 {ECO:0000313|EMBL:KKX34468.1, ECO:0000313|Proteomes:UP000034908}; RN [1] {ECO:0000313|EMBL:KKX34468.1, ECO:0000313|Proteomes:UP000034908} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=LC145 {ECO:0000313|EMBL:KKX34468.1, RC ECO:0000313|Proteomes:UP000034908}; RA Lee M., Gan H.Y., Gan H.M.; RT "Whole Genome Sequencing of Six Isolated Bacteria from Oligotrophic RT Conditions within Lechuguilla Cave, New Mexico."; RL Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KKX34468.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LBHV01000001; KKX34468.1; -; Genomic_DNA. DR RefSeq; WP_046792956.1; NZ_LBHV01000001.1. DR EnsemblBacteria; KKX34468; KKX34468; YH62_00395. DR PATRIC; fig|1120688.3.peg.82; -. DR Proteomes; UP000034908; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000034908}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000034908}. FT DOMAIN 206 378 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 165 199 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 444 AA; 48923 MW; 8BD13AD64814DCC0 CRC64; MRAAVVVPVL KQGKPRAGQG DAMPAPQRSN EARLEEAVGL AKAIDLTITE GMIVSVGQPR PATLIGTGKI EEIKALLDEH DAGLVIVDHP LTPVQQRNLE KEWNAKVIDR TGLILEIFGR RASTKEGTLQ VDLAHLNYQK GRLVRSWTHL ERQRGGAGFM GGPGETQIEA DRRLLQDRIV RLERELEQVV RTRQLHRAKR RKVPHPIVAL VGYTNAGKST LFNRITGAGV LAEDMLFATL DPTLRRMKLP HGRTVILSDT VGFISDLPTH LVAAFRATLE EVLEADLILH VRDMSDPDNA AQAGDVLRIL ADLGIGEKEG AERIIEVWNK VDKLDPETHE AITEKAGARE NVMAVSAISG EGIDALMQEI ARRLSGVLTE TTITIPADKL SLVSWIYSDA VVDDRQDNED GSVTLDVRLT ERQAAELERR LGNGPKPAKE DWER // ID A0A0M3CHW5_9SPHI Unreviewed; 395 AA. AC A0A0M3CHW5; DT 11-NOV-2015, integrated into UniProtKB/TrEMBL. DT 11-NOV-2015, sequence version 1. DT 07-JUN-2017, entry version 10. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=L950_0207205 {ECO:0000313|EMBL:KKX51026.1}; OS Sphingobacterium sp. IITKGP-BTPF85. OC Bacteria; Bacteroidetes; Sphingobacteriia; Sphingobacteriales; OC Sphingobacteriaceae; Sphingobacterium. OX NCBI_TaxID=1338009 {ECO:0000313|EMBL:KKX51026.1, ECO:0000313|Proteomes:UP000034376}; RN [1] {ECO:0000313|EMBL:KKX51026.1, ECO:0000313|Proteomes:UP000034376} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=IITKGP-BTPF85 {ECO:0000313|EMBL:KKX51026.1, RC ECO:0000313|Proteomes:UP000034376}; RA Misra B.B., Chatterjee S., Mukhopadhyay S.K., Das S.S., Shankar J., RA Datta D., Singh S.M., Ghosh A.K., Das A.K., Dey S.; RT "Draft Genome Sequence of Psychrotrophic Sphingobacterium sp. Strain RT IITKGP-BTPF85 Isolated from Arctic Permafrost Provides Insights into RT Cold Adaptation."; RL Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KKX51026.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ASZT02000018; KKX51026.1; -; Genomic_DNA. DR RefSeq; WP_021191965.1; NZ_ASZT02000018.1. DR EnsemblBacteria; KKX51026; KKX51026; L950_0207205. DR Proteomes; UP000034376; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000034376}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000034376}. FT DOMAIN 204 384 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 395 AA; 44972 MW; 60996FB339056C92 CRC64; MAKIKIYDTA VRPETALLVS VIPQGLSEEK AHEYLEELEF LVQTAGGITK GIITQKLTYP DRSTYVGAGK LEDIKAFVIA EEIDMVVFDD ELSPSQLRNI ERELQVKILD RSNLILDIFA SHAKSAQAKT QVELAQLQYL LPRLTRLWTH LERQRGGIGM RGPGESQIET DRRIILNKIT VLKERLDLID KQNETQRKNR GEMIRVALVG YTNVGKSTIM NMISKSDVLI ENKLFATLDT TVRKVVIDNL PFLLSDTVGF IRKLPHHLVE CFKSTLDEVR EADVLIHAVD ISHPNFEDHI IAVNETLKDI GALDKPIITV FNKIDAYVPT VEEGEEGEKT VTLEDFENSW MAKNADPAIF ISATNKTNLE EFKQKLYDII VEIHRERYPY NNLLY // ID A0A0M3QDI4_SPHS1 Unreviewed; 442 AA. AC A0A0M3QDI4; DT 09-DEC-2015, integrated into UniProtKB/TrEMBL. DT 09-DEC-2015, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=LH20_11885 {ECO:0000313|EMBL:ALC12653.1}; OS Sphingopyxis sp. (strain 113P3). OC Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales; OC Sphingomonadaceae; Sphingopyxis. OX NCBI_TaxID=292913 {ECO:0000313|EMBL:ALC12653.1, ECO:0000313|Proteomes:UP000061305}; RN [1] {ECO:0000313|EMBL:ALC12653.1, ECO:0000313|Proteomes:UP000061305} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=113P3 {ECO:0000313|EMBL:ALC12653.1, RC ECO:0000313|Proteomes:UP000061305}; RX PubMed=26472829; RA Ohtsubo Y., Nagata Y., Numata M., Tsuchikane K., Hosoyama A., RA Yamazoe A., Tsuda M., Fujita N., Kawai F.; RT "Complete Genome Sequence of Polyvinyl Alcohol-Degrading Strain RT Sphingopyxis sp. 113P3 (NBRC 111507)."; RL Genome Announc. 3:e01169-15(2015). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP009452; ALC12653.1; -; Genomic_DNA. DR EnsemblBacteria; ALC12653; ALC12653; LH20_11885. DR KEGG; sphp:LH20_11885; -. DR PATRIC; fig|292913.6.peg.2406; -. DR KO; K03665; -. DR Proteomes; UP000061305; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 2. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000061305}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000061305}. FT DOMAIN 206 385 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 442 AA; 48800 MW; C1A5A8FE7FA43F55 CRC64; MSPDDVEVTR GARAVLVVPE WRGQGLSRDL DARVAEATGL AVAIGIKIVA VHPLRLRQTR AATLIGVGQI EAIRPDVHEN EAQLVIVDAA LTAIQQRNLE TELGAKVIDR TGLILEIFGE RAATAEGRLQ VELAHLDYQA GRLVRSWTHL ERQRGGFGFL GGPGETQIEA DRRMIRNRMA RIRRSLEDAR RTRQLQRAKR QRAPWPVIAL VGYTNAGKST FFNRLTGSDV MAEDMLFATL DPTMREIRLP GIDKAILSDT VGFVSDLPTE LVAAFRATLE EVTTADLIVH VRDITHPDSE AQYADVVAIL DSLGVNGPQD GEGDAQGAIA QIEIWNKIDA ASPERRAQIE EMAARRRDVA VISAETREGI EAARALMAAD LTARHEVTRV FLRFDQGDAM AWLHARGDLL SDEVVEGGHR LTVRLDPADR ARFERLWPSN QS // ID A0A0M3QG13_9DELT Unreviewed; 545 AA. AC A0A0M3QG13; DT 09-DEC-2015, integrated into UniProtKB/TrEMBL. DT 09-DEC-2015, sequence version 1. DT 07-JUN-2017, entry version 13. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=DSOUD_2239 {ECO:0000313|EMBL:ALC17003.1}; OS Desulfuromonas soudanensis. OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfuromonadales; OC Desulfuromonadaceae; Desulfuromonas. OX NCBI_TaxID=1603606 {ECO:0000313|EMBL:ALC17003.1, ECO:0000313|Proteomes:UP000057158}; RN [1] {ECO:0000313|EMBL:ALC17003.1, ECO:0000313|Proteomes:UP000057158} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=WTL {ECO:0000313|EMBL:ALC17003.1, RC ECO:0000313|Proteomes:UP000057158}; RA Badalamenti J.P., Summers Z.M., Gralnick J.A., Bond D.R.; RT "Isolation and Genomic Characterization of a Novel Halophilic Metal- RT Reducing Deltaproteobacterium from the Deep Subsurface."; RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP010802; ALC17003.1; -; Genomic_DNA. DR RefSeq; WP_053551050.1; NZ_CP010802.1. DR EnsemblBacteria; ALC17003; ALC17003; DSOUD_2239. DR KEGG; des:DSOUD_2239; -. DR PATRIC; fig|1603606.3.peg.2419; -. DR KO; K03665; -. DR Proteomes; UP000057158; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000057158}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000057158}. FT DOMAIN 377 541 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 336 370 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 545 AA; 61198 MW; E5DDD40B90F3F732 CRC64; MIQGHLTGLK PSQIKGLERI YRRRIPPDQV VSVELARYLT EQSSALRRQI GVILDRLGTV IHVIVGDDRE IVIPDLSGFA LGRSGLRGLR CIHTHLKGEP LSQDDLTDLA LLRLDLMVAL GVGGDGLPGA VHYAHILPPN PEEKSVEILK APSVYDFDLD FDQFIRSLEA ELEGKMAETV DLSDTREKAI LISVSQESRQ ETEDSLDELT ELARTADVVV LDRIVQRARQ LNPKYLMGEG KVKEVVIRAL QQGATLLIFD QDLSPAQVRS ITEITEIKVI DRSQLILDIF ARRAHTLDGK VQVELAQLKY IMPRLVGRGT ALSRLMGGIG GRGPGETKLE TDRRRIRDRI TRLEKQLEAL SQGRRQRRQR RIRAEVPIVS IVGYTNAGKS TLLNAMTQSA VLTEDLLFAT LDTATRRLRF PLEREVIITD TVGFIRKLPK SLMGAFKATL EELEDADLLL HVVDLSNPRF EEQMKSVEKI LADLELDRIP TLLVFNKIDL VDPDEVAAYC RRNQAIGVSA RNRTTFLPLL AELQRRFWPD EAGTH // ID A0A0M3RKI8_9ACTO Unreviewed; 552 AA. AC A0A0M3RKI8; DT 09-DEC-2015, integrated into UniProtKB/TrEMBL. DT 09-DEC-2015, sequence version 1. DT 07-JUN-2017, entry version 13. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=AM609_04540 {ECO:0000313|EMBL:ALD00563.1}; OS Actinomyces sp. oral taxon 414. OC Bacteria; Actinobacteria; Actinomycetales; Actinomycetaceae; OC Actinomyces. OX NCBI_TaxID=712122 {ECO:0000313|EMBL:ALD00563.1, ECO:0000313|Proteomes:UP000061022}; RN [1] {ECO:0000313|EMBL:ALD00563.1, ECO:0000313|Proteomes:UP000061022} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=F0588 {ECO:0000313|EMBL:ALD00563.1, RC ECO:0000313|Proteomes:UP000061022}; RA Babu N.S., Beckwith C.J., Beseler K.G., Brison A., Carone J.V., RA Caskin T.P., Diamond M., Durham M.E., Foxe J.M., Go M., RA Henderson B.A., Jones I.B., McGettigan J.A., Micheletti S.J., RA Nasrallah M.E., Ortiz D., Piller C.R., Privatt S.R., Schneider S.L., RA Sharp S., Smith T.C., Stanton J.D., Ullery H.E., Wilson R.J., RA Serrano M.G., Buck G., Lee V., Wang Y., Carvalho R., Voegtly L., RA Shi R., Duckworth R., Johnson A., Loviza R., Walstead R., Shah Z., RA Kiflezghi M., Wade K., Ball S.L., Bradley K.W., Asai D.J., RA Bowman C.A., Russell D.A., Pope W.H., Jacobs-Sera D., Hendrix R.W., RA Hatfull G.F.; RL Submitted (AUG-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP012590; ALD00563.1; -; Genomic_DNA. DR RefSeq; WP_053588023.1; NZ_CP012590.1. DR EnsemblBacteria; ALD00563; ALD00563; AM609_04540. DR KEGG; acq:AM609_04540; -. DR PATRIC; fig|712122.3.peg.1023; -. DR KO; K03665; -. DR Proteomes; UP000061022; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000061022}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000061022}. FT DOMAIN 332 498 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 552 AA; 57762 MW; A5D8EB42664C73EF CRC64; MPHPQAADSA DSANSADSAD SGAAAVRPGP DPAATPDSGS RAGAAPSAED IVSRILSRHG TALASTAGEH ALREADDDGA LEREARAARR TAAPSAGPED VSEVEYRRVR LERVVLVGLD LPGTAPAAPA GTRAASPGAP WPGAAPSQDA ETSLAELAAL AQTAGSEVLD AVIQRRDHPD PATYLGSGKA RELAETVAAV GADTVIVDGE LAPSQRRALE DVVNAKVVDR TAVILDIFAQ HAKSREGKVQ VELAQLEYLL PRLRGWGESM SRQAGGRVAG GAGIGARGPG ETKIELDRRR IRRRMAKLRR EISAMAPSRE VKRGSRRRGP IPSVAIAGYT NAGKSSLMNR LTGADLMVQD ALFATLDPTV RRAETSDGRL YTLTDTVGFV RNLPHELVEA FRSTLEEVAG ADLVVHVVDA AHPDPLGQVA AVRTVLADIP GALEVPELIA LNKADLADGV ALAALRTRLP GAVAVSARTG RGLEELRGRI EEMLPRPDVA VDVVVPYSRG DLVARVHADG EIDSIDYGPE GTRVRARVDA PLAAELWACA VL // ID A0A0M3UAM4_9PSEU Unreviewed; 496 AA. AC A0A0M3UAM4; DT 09-DEC-2015, integrated into UniProtKB/TrEMBL. DT 09-DEC-2015, sequence version 1. DT 07-JUN-2017, entry version 14. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=XF36_05895 {ECO:0000313|EMBL:ALE82745.1}; OS Pseudonocardia sp. HH130629-09. OC Bacteria; Actinobacteria; Pseudonocardiales; Pseudonocardiaceae; OC Pseudonocardia. OX NCBI_TaxID=1641402 {ECO:0000313|EMBL:ALE82745.1, ECO:0000313|Proteomes:UP000062082}; RN [1] {ECO:0000313|EMBL:ALE82745.1, ECO:0000313|Proteomes:UP000062082} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=HH130629-09 {ECO:0000313|EMBL:ALE82745.1, RC ECO:0000313|Proteomes:UP000062082}; RX PubMed=26438860; DOI=10.1073/pnas.1515348112; RA Sit C.S., Van Arnam E.B., Ramadhar T.R.; RT "Variable genetic architectures produce virtually identical molecules RT in bacterial symbionts of fungus-growing ants."; RL Proc. Natl. Acad. Sci. U.S.A. 112:13150-13154(2015). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP011868; ALE82745.1; -; Genomic_DNA. DR RefSeq; WP_051050199.1; NZ_CP011868.1. DR EnsemblBacteria; ALE82745; ALE82745; XF36_05895. DR KEGG; pseh:XF36_05895; -. DR PATRIC; fig|1641402.3.peg.1255; -. DR KO; K03665; -. DR Proteomes; UP000062082; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 2. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000313|EMBL:ALE82745.1}; KW Complete proteome {ECO:0000313|Proteomes:UP000062082}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900, KW ECO:0000313|EMBL:ALE82745.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000062082}. FT DOMAIN 254 423 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 496 AA; 53428 MW; 054DE8014E59EA34 CRC64; MTDAHTHPSV TPSTSNPVPT GGELDLEERT SLRRIHGLST ELTDITEVEY RKLQLERVVL VGVWTEGTAE QADNSMTELA RLAETAGSEV MDGLVQRRSS PDPATFIGSG KVEELLGVVR ATGADTVICD GELSPGQLRQ LEERLKVKVI DRTALILDIF AQHARSRDGK AQVELAQLSY LLPRLRGWGE ALSRQVGGRA AGGVGIGGRG PGETKIELDR RRIRARMSKL RREIGAMRQV RETQRGSRRR NEIPSVAIVG YTNAGKSSLL NQLTDAGVLV QDALFATLDP TTRKAQTPDG HDYTLTDTVG FVRHLPHQLV EAFRSTLEEA ARADLLVHVV DGSDPLPDDQ IAAVRQVLVE VGEAAGDTMP PELLVINKID AAGDLALARL RHAQPDAVFV SAHSGTGIDR LREHIAERLP RPDYEVDLLL PYTEGALVAR LHDDGEILAE SHTADGTRIR ARVKPELGTA VLPFAVAGSA VPTGTGADLP ATAAGH // ID A0A0M4FXP4_9BACI Unreviewed; 419 AA. AC A0A0M4FXP4; DT 09-DEC-2015, integrated into UniProtKB/TrEMBL. DT 09-DEC-2015, sequence version 1. DT 07-JUN-2017, entry version 12. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=AM500_14880 {ECO:0000313|EMBL:ALC90924.1}; OS Bacillus sp. FJAT-18017. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus. OX NCBI_TaxID=1705566 {ECO:0000313|EMBL:ALC90924.1, ECO:0000313|Proteomes:UP000060713}; RN [1] {ECO:0000313|EMBL:ALC90924.1, ECO:0000313|Proteomes:UP000060713} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=FJAT-18017 {ECO:0000313|EMBL:ALC90924.1, RC ECO:0000313|Proteomes:UP000060713}; RA Liu B., Wang J., Zhu Y., Liu G., Chen Q., Chen Z., Lan J., Che J., RA Ge C., Shi H., Pan Z., Liu X.; RT "Genome sequencing project for genomic taxonomy and phylogenomics of RT Bacillus-like bacteria."; RL Submitted (AUG-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP012602; ALC90924.1; -; Genomic_DNA. DR RefSeq; WP_053599921.1; NZ_CP012602.1. DR EnsemblBacteria; ALC90924; ALC90924; AM500_14880. DR PATRIC; fig|1705566.3.peg.3289; -. DR Proteomes; UP000060713; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000060713}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000060713}. FT DOMAIN 200 362 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 419 AA; 47787 MW; 19BF9B361F05E2D2 CRC64; METKLEKERA ILVGCQTTED DDLRFQYSME ELVSLTETAR GEVLVSVIQK RERIHSATYI GKGKVEELKG LVEQLEADLV IFNDELSPSQ KRNLGSELDA RIIDRTQLIL DIFAQRARSK EGKLQVELAQ LQYLLPRLAG QGIALSRLGA GIGTRGPGET KLESDRRHIR RRIDEIKQQL AVIVQHRDRY RERRKKNKAF QIAIAGYTNA GKSTLFNRLS EADSYEENQL FATLDPMTRK VILPSGFVAL ITDTVGFIQD LPTSLIAAFR STLEEVKEAD LILHVVDMSN PDYFHHEKTV NRLLEELDVH NIPQLTVYNK RDIQHPDFVP TANTPTAFIS AFDKDDRDAP KRKIEETAIS MMESYNVLIP ATEGKLLSLL KNETILRELS FIEEHQLYSC KGYTLRDHQV TGHLQKYTV // ID A0A0M4GDF8_9BACI Unreviewed; 420 AA. AC A0A0M4GDF8; DT 09-DEC-2015, integrated into UniProtKB/TrEMBL. DT 09-DEC-2015, sequence version 1. DT 30-AUG-2017, entry version 14. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=AM592_05675 {ECO:0000313|EMBL:ALC84120.1}; OS Bacillus gobiensis. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus. OX NCBI_TaxID=1441095 {ECO:0000313|EMBL:ALC84120.1, ECO:0000313|Proteomes:UP000067625}; RN [1] {ECO:0000313|Proteomes:UP000067625} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=FJAT-4402 {ECO:0000313|Proteomes:UP000067625}; RA Liu B., Wang J., Zhu Y., Liu G., Chen Q., Chen Z., Lan J., Che J., RA Ge C., Shi H., Pan Z., Liu X.; RT "Genome sequencing project for genomic taxonomy and phylogenomics of RT Bacillus-like bacteria."; RL Submitted (AUG-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP012600; ALC84120.1; -; Genomic_DNA. DR EnsemblBacteria; ALC84120; ALC84120; AM592_05675. DR PATRIC; fig|1441095.3.peg.1233; -. DR Proteomes; UP000067625; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000067625}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000067625}. FT DOMAIN 201 363 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 420 AA; 47751 MW; 43A565233ACF06A7 CRC64; MNLLDDIHEK VILVGCQLPH VSDERFEYSM EELSSLTKTA QGEVVSIFTQ KRHSPDSSTF IGKGKLEELA AFTKESGVDL VIFNDELSPS QLRVLASTIE AKVIDRTQLI LDIFAGRART REGKLQIELA QLKYMLPRLV GQGMNLSRLG GGIGTRGPGE TKLETDRRYI RSRIHEIESQ LQTVVRHRSR YRDRRKKNGV LQAALVGYTN AGKSTWFNKL TSSESFEEDL LFATLDPMTR RMELENGYTL LLSDTVGFIQ DLPTTLIAAF RSTLEEVREA DVILHVVDSS NEDNIGHQAT VKNLLTELEA DKIPRLTVYN KRDKKTEEFI PSHEENYVLV SVKDENDGTR LKKQMESFMK EELFVPYSVR IPADHGKLIA EMKSSTMIEG TTFIEEPEVY HISGFAHPNH RIYGELKKFE // ID A0A0M4LFS6_9GAMM Unreviewed; 443 AA. AC A0A0M4LFS6; DT 09-DEC-2015, integrated into UniProtKB/TrEMBL. DT 09-DEC-2015, sequence version 1. DT 07-JUN-2017, entry version 12. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=W908_01670 {ECO:0000313|EMBL:ALE01427.1}; OS Candidatus Thioglobus singularis PS1. OC Bacteria; Proteobacteria; Gammaproteobacteria; Candidatus Thioglobus. OX NCBI_TaxID=1125411 {ECO:0000313|EMBL:ALE01427.1, ECO:0000313|Proteomes:UP000068905}; RN [1] {ECO:0000313|EMBL:ALE01427.1, ECO:0000313|Proteomes:UP000068905} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=PS1 {ECO:0000313|EMBL:ALE01427.1, RC ECO:0000313|Proteomes:UP000068905}; RX PubMed=26494659; RA Marshall K.T., Morris R.M.; RT "Genome Sequence of 'Candidatus Thioglobus singularis' Strain PS1, a RT Mixotroph from the SUP05 Clade of Marine Gammaproteobacteria."; RL Genome Announc. 3:e01155-15(2015). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP006911; ALE01427.1; -; Genomic_DNA. DR RefSeq; WP_053819677.1; NZ_CP006911.1. DR EnsemblBacteria; ALE01427; ALE01427; W908_01670. DR KEGG; tsn:W908_01670; -. DR PATRIC; fig|1125411.7.peg.329; -. DR KO; K03665; -. DR Proteomes; UP000068905; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000068905}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000068905}. FT DOMAIN 207 374 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 443 AA; 49711 MW; F767A7C07AEF632D CRC64; MSMELFDRQK DAVGQGERTI LVHIELTSIS QSPDSVNEFK QLAVSSGLNI IETVLVKRSF TKAQFFIGTG KVDELALSVS DNEIELVIFS HQLSPSQERN LEKALKCQVM DRTGLILDIF ALRASSFEGK LQVELAQLKH LSTRLVRGWT HLERQKGGIG LRGPGETQLE TDKRLVSIRI KNINKRLAKV HKQHDLGRKS RVKNQLPMIS LAGYTNAGKS TLFNLLTNAE VYADDKLFAT LDSTIRRVML PASGEAVIAD TVGFIQDLPH ELVEAFKSTL EETRQANVLL HIVDASDPNN RDKIDQVEDI IEQIGAQKIP RILVMNKIDG LVNFKPRIDK DSEGNISRVW LSAETGEGVD LLYEALSESL SGMMTSARIK LDVQSAYIRS EIHKVGFIKK EIMNEFGQWL LEINVTSHYL ERLLDKQGVS LLWKQKSQQS QTA // ID A0A0M4LTE5_9RHIZ Unreviewed; 417 AA. AC A0A0M4LTE5; DT 09-DEC-2015, integrated into UniProtKB/TrEMBL. DT 09-DEC-2015, sequence version 1. DT 30-AUG-2017, entry version 14. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=PU02_1045 {ECO:0000313|EMBL:ALE03859.1}; OS Bartonella ancashensis. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Bartonellaceae; Bartonella. OX NCBI_TaxID=1318743 {ECO:0000313|EMBL:ALE03859.1, ECO:0000313|Proteomes:UP000057213}; RN [1] {ECO:0000313|EMBL:ALE03859.1, ECO:0000313|Proteomes:UP000057213} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=20.00 {ECO:0000313|EMBL:ALE03859.1, RC ECO:0000313|Proteomes:UP000057213}; RX PubMed=26543106; RA Hang J., Mullins K.E., Clifford R.J., Onmus-Leone F., Yang Y., RA Jiang J., Leguia M., Kasper M.R., Maguina C., Lesho E.P., Jarman R.G., RA Richards A.L., Blazes D.; RT "Complete Genome Sequence of Bartonella ancashensis Strain 20.00, RT Isolated from the Blood of a Patient with Verruga Peruana."; RL Genome Announc. 3:e01217-15(2015). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP010401; ALE03859.1; -; Genomic_DNA. DR EnsemblBacteria; ALE03859; ALE03859; PU02_1045. DR KEGG; banc:PU02_1045; -. DR PATRIC; fig|1318743.3.peg.1060; -. DR KO; K03665; -. DR Proteomes; UP000057213; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000057213}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000057213}. FT DOMAIN 192 364 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 417 AA; 46378 MW; 57F1264F3C5A6639 CRC64; MDKSKGASNE RSIASRVNEA VGLALSIGLN VVHCEVVNIT TKNPATLFGS GKVDAFKQVL SCSEGRDVSV AIVDCTLTPV QQRNLEKLWS CKVIDRTALI LEIFGDRAQT REGVLQVELA HLSYQKGRLV RSWTHLERQR GGSGFLGGPG ETQIESDRRL LQDKITRIRR ELKTVVKTRA LHRAKRKKMQ HLVVALVGYT NAGKSTLFNQ LSGANVLTED MLFATLDPTL RKVTLPHGKT ILLSDTVGFI SNLPTHLVAA FRATLEEVVE ADFIIHVKDI SDPDHHAHAR DVLEILSDLG VDVDNTNRII EVWNKIDMLD EYTLNSLQIS ARALFNPALM VSAKAGEGLK ELLSTIERRI FGEMQAVELV LKPETMSLID WFYKNSGKVE QWSHDDGSVT VRAVLTDEAK RQLDCIK // ID A0A0M4NJ93_9GAMM Unreviewed; 436 AA. AC A0A0M4NJ93; DT 09-DEC-2015, integrated into UniProtKB/TrEMBL. DT 09-DEC-2015, sequence version 1. DT 07-JUN-2017, entry version 14. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=SP60_05450 {ECO:0000313|EMBL:ALE52700.1}; OS Candidatus Thioglobus autotrophicus. OC Bacteria; Proteobacteria; Gammaproteobacteria; Candidatus Thioglobus. OX NCBI_TaxID=1705394 {ECO:0000313|EMBL:ALE52700.1, ECO:0000313|Proteomes:UP000058020}; RN [1] {ECO:0000313|EMBL:ALE52700.1, ECO:0000313|Proteomes:UP000058020} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=EF1 {ECO:0000313|EMBL:ALE52700.1, RC ECO:0000313|Proteomes:UP000058020}; RX PubMed=26494660; RA Shah V., Morris R.M.; RT "Genome Sequence of 'Candidatus Thioglobus autotrophica' Strain EF1, a RT Chemoautotroph from the SUP05 Clade of Marine Gammaproteobacteria."; RL Genome Announc. 3:e01156-15(2015). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP010552; ALE52700.1; -; Genomic_DNA. DR RefSeq; WP_053951664.1; NZ_CP010552.1. DR EnsemblBacteria; ALE52700; ALE52700; SP60_05450. DR KEGG; tho:SP60_05450; -. DR PATRIC; fig|1705394.5.peg.1089; -. DR KO; K03665; -. DR Proteomes; UP000058020; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000058020}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000058020}. FT DOMAIN 205 372 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 436 AA; 49290 MW; E532E4FCFE253BEE CRC64; MELFDRQKDA VGQGERTLLV YVELPSTRNI HNAKSEFKEL AQSSGLDIIE TIQVNRNSAL AQYFIGTGKV DEIAQMVQDL ELDLVIFSPE LTPSQERNLE KTLACQVMDR TGLILDIFAL RASSFEGKLQ VELAQLRHLS TRLVRGWTHL ERQKGGIGMR GPGETQLETD KRLIAVRIKN ITKRLDKVHK QRDLGRKSRT KNELPMIALA GYTNAGKSTL FNTLTDAKVF AHDQLFATLD STIRRVILPA SGEAVIADTV GFIQDLPHDL VDAFKSTLEE TKRSNVLLHV VDAADEYNIE KIGQVDEIIE EIGAGKIPTI LVMNKIDCLE NFAPRLDRDE FGRVYRVWIS SMTGKGVDLL YQALAEQLSG MMTRAKIQLD VKSAYIRSEI HNIGYIHNEK VDDFGQWILE INVTHHYLSK LLNKKGVKLL WEQSRK // ID A0A0M4QZF3_9MICC Unreviewed; 519 AA. AC A0A0M4QZF3; DT 09-DEC-2015, integrated into UniProtKB/TrEMBL. DT 09-DEC-2015, sequence version 1. DT 05-JUL-2017, entry version 15. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=AOC05_04005 {ECO:0000313|EMBL:ALE93973.1}; OS Arthrobacter alpinus. OC Bacteria; Actinobacteria; Micrococcales; Micrococcaceae; Arthrobacter. OX NCBI_TaxID=656366 {ECO:0000313|EMBL:ALE93973.1, ECO:0000313|Proteomes:UP000062833}; RN [1] {ECO:0000313|Proteomes:UP000062833} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=R3.8 {ECO:0000313|Proteomes:UP000062833}; RA See-Too W.S., Chan K.G.; RT "Complete genome of Arthrobacter alpinus strain R3.8."; RL Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP012677; ALE93973.1; -; Genomic_DNA. DR EnsemblBacteria; ALE93973; ALE93973; AOC05_04005. DR KEGG; aaq:AOC05_04005; -. DR PATRIC; fig|656366.3.peg.873; -. DR KO; K03665; -. DR Proteomes; UP000062833; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000062833}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000062833}. FT DOMAIN 298 463 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 519 AA; 56211 MW; 995B158470F87759 CRC64; MSVAEIEAVI DRILAKDIAA SRAVRAEVRL DAEDPQATPA PSHPIIGQAQ AVSNLTFEHS SFDGDQTELA ERNALRRRAG LSTELEDVTE VEYRQLRLER VVLAGLWSTG TMADAENSLR ELAALAETAG SEVLDGMVQR RAKPDPATYL GTGKAEELKE IVHATGADTV IIDGDLAPSQ RRTLEEVVKV KVIDRTALIL DIFAQHAQSR EGRAQVELAQ MEYLLPRLRG WGESMSRQAG GRVGTAGGGI GSRGPGETKM ELDRRKIRTR MAKLRREIAA MKPARETKRA NRKRNSVPSV AIAGYTNAGK SSLLNRLTNA GVLVENALFA TLDPTVRKTE TADGLGYTLV DTVGFVRSLP TQLVEAFRST LEEVADADLI LHIVDASHPD PEGQISAVRT VFAEVGALKI PEIIILNKVD IADPLVVQRL RQREPRSVEV SARTGQGMEG LLAAISDAIP RPGVDLTLLI PYDRGDVLNR LHGSDAEILS IEHGETGTVA HVRVRDDLAA EVAPFVQHG // ID A0A0M5KTG1_9MICC Unreviewed; 547 AA. AC A0A0M5KTG1; DT 09-DEC-2015, integrated into UniProtKB/TrEMBL. DT 09-DEC-2015, sequence version 1. DT 07-JUN-2017, entry version 13. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=AL755_07465 {ECO:0000313|EMBL:ALE05348.1}; OS Arthrobacter sp. ERGS1:01. OC Bacteria; Actinobacteria; Micrococcales; Micrococcaceae; Arthrobacter. OX NCBI_TaxID=1704044 {ECO:0000313|EMBL:ALE05348.1, ECO:0000313|Proteomes:UP000060433}; RN [1] {ECO:0000313|EMBL:ALE05348.1, ECO:0000313|Proteomes:UP000060433} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ERGS1:01 {ECO:0000313|EMBL:ALE05348.1, RC ECO:0000313|Proteomes:UP000060433}; RA Kumar R., Swarnkar M.K., Singh A.K., Singh D.; RT "Complete Genome Sequencing of Arthrobacter sp. ERGS1:01."; RL Submitted (AUG-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP012479; ALE05348.1; -; Genomic_DNA. DR RefSeq; WP_054010463.1; NZ_CP012479.1. DR KEGG; are:AL755_07465; -. DR PATRIC; fig|1704044.3.peg.720; -. DR KO; K03665; -. DR Proteomes; UP000060433; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000060433}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000060433}. FT DOMAIN 326 491 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 547 AA; 58910 MW; 3ED2B0A561A99E68 CRC64; MSNPSAPHGS ADSHGPAEVP AGGDAGQDLS VAEIEAVIDR ILAKDAAATR AVREDAKLDA ADPQSKSAAS HPIIGRAQAL SNLAQEHSRF DGDQSELAER NALRRTAGLS TELEDVTEVE YRQLRLERVV LAGLWSNGTM ADAENSLREL AALAETAGSE VLDGLVQRRA KPDPATYLGQ GKAQELKDIV HATGADTVII DGDLAPSQRR TLEEVVKVKV IDRTALILDI FAQHAQSREG RAQVELAQME YLLPRLRGWG ESMSRQAGGR VGAAGGGIGS RGPGETKMEL DRRKIRTRMA KLRREIAAMK PARETKRANR KRNSVPSVAI AGYTNAGKSS LLNRLTDAGV LVENALFATL DPTVRKTETA DGLGYTLVDT VGFVRSLPTQ LVEAFRSTLE EVADADLILH IVDASHPDPE GQIAAVRTVL SEVDALKIPE IIILNKADIA DPFVVERLRQ REPRTVVVSA RTGAGIDELL AAISEAIPRP SIALDLLIPY DRGDVLNRLH RSDAEIISIE HGEHGTIAKV RVRGDLAAEV EPFVQHE // ID A0A0M5KZE0_9ACTN Unreviewed; 470 AA. AC A0A0M5KZE0; DT 09-DEC-2015, integrated into UniProtKB/TrEMBL. DT 09-DEC-2015, sequence version 1. DT 07-JUN-2017, entry version 13. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=AL705_00840 {ECO:0000313|EMBL:ALE18505.1}; OS Lawsonella clevelandensis. OC Bacteria; Actinobacteria; Corynebacteriales; Lawsonella. OX NCBI_TaxID=1528099 {ECO:0000313|EMBL:ALE18505.1, ECO:0000313|Proteomes:UP000068137}; RN [1] {ECO:0000313|EMBL:ALE18505.1, ECO:0000313|Proteomes:UP000068137} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=X1698 {ECO:0000313|EMBL:ALE18505.1, RC ECO:0000313|Proteomes:UP000068137}; RX PubMed=26659691; RA Nicholson A.C., Bell M., Humrighouse B.W., McQuiston J.R.; RT "Complete Genome Sequences for Two Strains of a Novel Fastidious, RT Partially Acid-Fast, Gram-Positive Corynebacterineae Bacterium, RT Derived from Human Clinical Samples."; RL Genome Announc. 3:e01462-15(2015). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP012390; ALE18505.1; -; Genomic_DNA. DR EnsemblBacteria; ALE18505; ALE18505; AL705_00840. DR KEGG; cbq:AL705_00840; -. DR PATRIC; fig|1562462.4.peg.171; -. DR KO; K03665; -. DR Proteomes; UP000068137; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000313|EMBL:ALE18505.1}; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000068137}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900, KW ECO:0000313|EMBL:ALE18505.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000068137}. FT DOMAIN 248 424 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 214 241 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 470 AA; 51409 MW; 5B33518115FE12F8 CRC64; MLKESTSSLM REPTRGEMEL EERSSLRHVV GLSTELQDIT DAEYRELRLE KVVLVGVWTE GSVAQAEAAM AELAALAETA GAAVLDVLIQ RRDKPDPATY IGSGKVREVK QVVDALGADT VICDGELSAG QLIALEKAIN VKVIDRTALI LDIFAQHASS SEGKAQVTLA QMEYMLPRLR GWGDTLSRQA GGRAGSNGGV GLRGPGETKI ETDRRRIRHR MAKLRRELAE MKMSRQTKRQ RRRAGDTPSI VIVGYTNAGK SSLLNRITGA GVLVQDALFA TLDPTTRRAE LPDGHSVVLT DTVGFVRYLP TQLVEAFRST LEEVADADII VQVVDGSDDF PLQQVESVND VLADVVAEYG IDLPPTVIVI NKCDAAEPLT LAQLRSEIPD AVFVSARTRE GMDDFLVALS HLLDERETTV HALIPYDHGE LVSRLYEHGR VLNEEHGPDG TTIEARVPRA LAQQLELFRV // ID A0A0M5L0A5_9SPHN Unreviewed; 432 AA. AC A0A0M5L0A5; DT 09-DEC-2015, integrated into UniProtKB/TrEMBL. DT 09-DEC-2015, sequence version 1. DT 07-JUN-2017, entry version 12. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=AMC99_01186 {ECO:0000313|EMBL:ALE16481.1}; OS Altererythrobacter epoxidivorans. OC Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales; OC Erythrobacteraceae; Altererythrobacter. OX NCBI_TaxID=361183 {ECO:0000313|EMBL:ALE16481.1, ECO:0000313|Proteomes:UP000057938}; RN [1] {ECO:0000313|EMBL:ALE16481.1, ECO:0000313|Proteomes:UP000057938} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CGMCC 1.7731 {ECO:0000313|EMBL:ALE16481.1, RC ECO:0000313|Proteomes:UP000057938}; RA Li Z., Cheng H., Huo Y., Xu X.; RT "Complete genome sequence of a benzo[a]pyrene-degrading bacterium RT Altererythrobacter epoxidivorans CGMCC 1.7731T."; RL Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP012669; ALE16481.1; -; Genomic_DNA. DR RefSeq; WP_061923991.1; NZ_CP012669.1. DR EnsemblBacteria; ALE16481; ALE16481; AMC99_01186. DR KEGG; aep:AMC99_01186; -. DR PATRIC; fig|361183.4.peg.1158; -. DR KO; K03665; -. DR Proteomes; UP000057938; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000057938}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000057938}. FT DOMAIN 202 377 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 168 195 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 432 AA; 47618 MW; 27499575B7774650 CRC64; MGEVTRGARA LVLCPDIRSQ KYDLDAKERL EEACGLALAI GVVIADAQII PVRDVRPNTL FGSGQVDNIA AACEQNEAEL VIVDGALSPI QQRNLEDKLK RKVIDRTGLI LEIFGERAAT AEGRLQVELA HLDYQQSRLV RSWTHLERQR GGFGFLGGPG ETQIEADRRM IRQRMGRLRR ELEQVRKTRS LHRERRERAP WPVIALVGYT NAGKSTLFNR VTGAEVMAED LLFATLDPTM RAISLPGVEK AILSDTVGFI SDLPTQLVAA FRATLEEVTA ADVILHVRDM ANAGNQAQKK QVLSVLADLG VIDPDDGSSN IPILEVWNKV DLLEPEAADE LRTAAENIDD VAIISALTGE GIDALFEQVG TMLTGQAREC EFVVPASDGR RLAWLYAHGD VLSDEQREGD TGPEHRVRVR LNPKELGQYQ SL // ID A0A0M6XSF8_9RHOB Unreviewed; 416 AA. AC A0A0M6XSF8; DT 09-DEC-2015, integrated into UniProtKB/TrEMBL. DT 09-DEC-2015, sequence version 1. DT 10-MAY-2017, entry version 10. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:CTQ34089.1}; GN ORFNames=JAN5088_02881 {ECO:0000313|EMBL:CTQ34089.1}; OS Jannaschia rubra. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae; Jannaschia. OX NCBI_TaxID=282197 {ECO:0000313|EMBL:CTQ34089.1, ECO:0000313|Proteomes:UP000048908}; RN [1] {ECO:0000313|EMBL:CTQ34089.1, ECO:0000313|Proteomes:UP000048908} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CECT 5088 {ECO:0000313|EMBL:CTQ34089.1, RC ECO:0000313|Proteomes:UP000048908}; RA Noorani M.; RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CXPG01000021; CTQ34089.1; -; Genomic_DNA. DR EnsemblBacteria; CTQ34089; CTQ34089; JAN5088_02881. DR Proteomes; UP000048908; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000048908}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000048908}. FT DOMAIN 170 339 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 416 AA; 45402 MW; 0D101E013AEC1EE2 CRC64; MSLANALPGL DVAGGDVVRL PKPHPGMLFG KGKVAELKQR IEVDEIELVL IDGSVTPVQQ RNLEREWKVK LLDRTGLILE IFADRAATRE GVLQVELAAL SYQRTRLVRA WTHLERQRGG LGFVGGPGET QIEADRRAID EQMVKLKRQL AKVAQTRELH RAARAKVPYP VVALVGYTNA GKSTLFNRLT GAEVMAKDML FATLDPTMRA VELPHGLNVI LSDTVGFISD LPTQLVAAFR ATLEEVLDAD LIVHVRDISH PESELQASDV DTILEHLGVS DEVTRLELWN KADALDDEGR ATATNLAARR DDVYLGSALT GQGLDALLQR IAGELTAALR EDVLTLPFAA GRARAWLHDE GAIRSETQGG DGTRVSLRWT ERQASRFAAT FPDLMTDPTK GTDDAAPPAA PGPWHP // ID A0A0M6YMF3_9RHOB Unreviewed; 464 AA. AC A0A0M6YMF3; DT 09-DEC-2015, integrated into UniProtKB/TrEMBL. DT 09-DEC-2015, sequence version 1. DT 12-APR-2017, entry version 9. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:CTQ50693.1}; GN ORFNames=JDO7802_02719 {ECO:0000313|EMBL:CTQ50693.1}; OS Jannaschia donghaensis. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae; Jannaschia. OX NCBI_TaxID=420998 {ECO:0000313|EMBL:CTQ50693.1, ECO:0000313|Proteomes:UP000049222}; RN [1] {ECO:0000313|EMBL:CTQ50693.1, ECO:0000313|Proteomes:UP000049222} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CECT 7802 {ECO:0000313|EMBL:CTQ50693.1, RC ECO:0000313|Proteomes:UP000049222}; RA Noorani M.; RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CXSU01000012; CTQ50693.1; -; Genomic_DNA. DR EnsemblBacteria; CTQ50693; CTQ50693; JDO7802_02719. DR Proteomes; UP000049222; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000049222}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000049222}. FT DOMAIN 218 387 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 464 AA; 51185 MW; 2B7CC6AFBD1FBB74 CRC64; MVRKKPLAQT PDATHSTEAR PTRALVLHPD TRAGDRSGRD PERALEECIS LAHALPGLDV LGGDTVRLPN PHPGMLFGKG KVEELRLRIE AEEIELILID GIVTPVQQRN LEKVWKTKLL DRTGLILEIF ADRAATREGV LQVELAALTY QRTRLVRAWT HLERQRGGLG FVGGPGETQI EADRRAIDEQ MVKLRRQLDK VVKTRELHRA ARAKVPYPVV ALVGYTNAGK STLFNRLTGA DVLAKDMLFA TLDPTMRAVD LPHDVHVILS DTVGFISDLP TQLVAAFRAT LEEVLDADLI VHVRDISHPD TELQARDVEA ILEALGTSED IPRLEMWNKA DALDMDAMQA AANLAARRDD VYLGSALTGQ GLQRLLERVA TEVTETLQET VLLLPFAAGK ARAWLHDEGA VQGETATEQG TEFTLRWTTR QAQRFAGAFP ELVPAGRDTP DEPEEETSGT GWSP // ID A0A0M7AVR4_9RHOB Unreviewed; 477 AA. AC A0A0M7AVR4; DT 09-DEC-2015, integrated into UniProtKB/TrEMBL. DT 09-DEC-2015, sequence version 1. DT 12-APR-2017, entry version 13. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:CTQ77843.1}; GN ORFNames=LA5096_05310 {ECO:0000313|EMBL:CTQ77843.1}; OS Labrenzia alba. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae; Labrenzia. OX NCBI_TaxID=311410 {ECO:0000313|EMBL:CTQ77843.1, ECO:0000313|Proteomes:UP000049983}; RN [1] {ECO:0000313|EMBL:CTQ77843.1, ECO:0000313|Proteomes:UP000049983} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CECT 5096 {ECO:0000313|EMBL:CTQ77843.1, RC ECO:0000313|Proteomes:UP000049983}; RA Noorani M.; RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CXWC01000014; CTQ77843.1; -; Genomic_DNA. DR EnsemblBacteria; CTQ77843; CTQ77843; LA5096_05310. DR Proteomes; UP000049983; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000049983}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000049983}. FT DOMAIN 240 410 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 477 AA; 52697 MW; 1CCFB94A393AC14B CRC64; MKPKSRADDF SKSNGAEEPG QKSLGMKDTG VDRLPQPFRA MIIEPVLQLR GDAGQQDLRG NRSPEARLDE AIGLSAAINL QIFHAGVVKI NNPKPGTLFG DGKVSELAGI VASEDLDLVV IDHPLSPVQQ RNLERRLKTK VIDRTGLILE IFGDRARTKE GRLQVDLAHL SWQKSRLVRS WTHLERQRGG AGFMGGPGET QIEADRRQIQ DRIIALQKQL DGVRRTRNLH RRKRKKIPQP VVALVGYTNA GKSTLFNRLT ESDVFAKDLL FATLDPTLRK ITLPHGKEVI LSDTVGFISD LPTHLVAAFR ATLEEVLEAD LILHVRDISH SDTEAQAEDV KKTLSDLGVD ALTGAPVIEV WNKIDCLDEA YREKLLSEAG QEGPVALSAL TGAGIEQLAG RIDAFIARHD DILSVKLPVV EGALLAKLYQ MADVMERVDG EDFVTAEVRV SDKQRGPFRE LFSDYVFSDD SDDQPNS // ID A0A0M7BF80_9RHOB Unreviewed; 468 AA. AC A0A0M7BF80; DT 09-DEC-2015, integrated into UniProtKB/TrEMBL. DT 09-DEC-2015, sequence version 1. DT 12-APR-2017, entry version 9. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:CUH40442.1}; GN ORFNames=JSE7799_03174 {ECO:0000313|EMBL:CUH40442.1}; OS Jannaschia seosinensis. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae; Jannaschia. OX NCBI_TaxID=313367 {ECO:0000313|EMBL:CUH40442.1, ECO:0000313|Proteomes:UP000049455}; RN [1] {ECO:0000313|EMBL:CUH40442.1, ECO:0000313|Proteomes:UP000049455} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CECT 7799 {ECO:0000313|EMBL:CUH40442.1, RC ECO:0000313|Proteomes:UP000049455}; RA Jackson K.R., Lunt B.L., Fisher J.N.B., Gardner A.V., Bailey M.E., RA Deus L.M., Earl A.S., Gibby P.D., Hartmann K.A., Liu J.E., Manci A.M., RA Nielsen D.A., Solomon M.B., Breakwell D.P., Burnett S.H., Grose J.H.; RL Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CYPR01000207; CUH40442.1; -; Genomic_DNA. DR EnsemblBacteria; CUH40442; CUH40442; JSE7799_03174. DR Proteomes; UP000049455; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000049455}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000049455}. FT DOMAIN 216 385 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 468 AA; 51925 MW; 5DD90E0B0024074A CRC64; MALTPPETPE TGHSTEARAT RSLVLHPDMR GGDRSGRDPK LALEEAVSLA HALPGLEVVG SEVVRLPKPH PGMLFGSGKV EELRAQIERD EIELVLIDGT VTPVQQRNLE RAWKVKLLDR TSLILEIFAD RAATREGVLQ VELAALSYQR TRLVRAWTHL ERQRGGLGFV GGPGETQIEA DRRAIDEQIV RIRKQLEKVV RTRELHRAAR AKVPYPIVAF VGYTNAGKST LFNRLTGADV MAKNMLFATL DPTMRAVELP HNLNVILSDT VGFISDLPTQ LVAAFRATLE EVLDADLILH VRDISHPETE AQAQDVEEIL EALGVPDDVP RLEMWNKADA LTLEARQTAE NLAARQEDVY LGSALTGQGL DPLLDRIAAD LTETLREVRI RIPFAAGAAR AWLHEEGAVQ DETPTEEGYT LDLRWTERQS ARFAATYPEL APEEARRAAA PKDADPERDR SDDPWEPT // ID A0A0M8KAA6_9CHLR Unreviewed; 436 AA. AC A0A0M8KAA6; DT 09-DEC-2015, integrated into UniProtKB/TrEMBL. DT 09-DEC-2015, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:GAP63506.1}; GN ORFNames=ARMA_1929 {ECO:0000313|EMBL:GAP63506.1}, GN SE16_02765 {ECO:0000313|EMBL:KPL89394.1}; OS Ardenticatena maritima. OC Bacteria; Chloroflexi; Ardenticatenia; Ardenticatenales; OC Ardenticatenaceae; Ardenticatena. OX NCBI_TaxID=872965 {ECO:0000313|EMBL:GAP63506.1, ECO:0000313|Proteomes:UP000037784}; RN [1] {ECO:0000313|EMBL:GAP63506.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=110S {ECO:0000313|EMBL:GAP63506.1}; RA Kawaichi S., Yoshida T., Sako Y., Nakamura R.; RT "Draft Genome Sequence of a Heterotrophic Facultative Anaerobic RT Thermophilic Bacterium, Ardenticatena maritima Strain 110ST."; RL Genome Announc. 3:e01145-15(2015). RN [2] {ECO:0000313|EMBL:KPL89394.1, ECO:0000313|Proteomes:UP000050502} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=110S {ECO:0000313|EMBL:KPL89394.1, RC ECO:0000313|Proteomes:UP000050502}; RA Hemp J., Ward L.M., Pace L.A., Fischer W.W.; RT "Whole genome sequence of Ardenticatena maritima DSM 23922."; RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases. RN [3] {ECO:0000313|Proteomes:UP000037784} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=110S {ECO:0000313|Proteomes:UP000037784}; RA Kawaichi S., Yoshida T., Sako Y., Nakamura R.; RT "Draft Genome Sequence of a Heterotrophic Facultative Anaerobic RT Bacterium Ardenticatena maritima Strain 110S."; RL Submitted (AUG-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:GAP63506.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BBZA01000158; GAP63506.1; -; Genomic_DNA. DR EMBL; LGKN01000003; KPL89394.1; -; Genomic_DNA. DR RefSeq; WP_054493333.1; NZ_LGKN01000003.1. DR EnsemblBacteria; GAP63506; GAP63506; ARMA_1929. DR EnsemblBacteria; KPL89394; KPL89394; SE16_02765. DR PATRIC; fig|872965.6.peg.506; -. DR Proteomes; UP000037784; Unassembled WGS sequence. DR Proteomes; UP000050502; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR Gene3D; 3.40.350.10; -; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR029149; Creatin/AminoP/Spt16_NTD. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000037784}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000037784}. FT DOMAIN 215 381 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 174 208 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 436 AA; 48860 MW; 9AEF66F8B13D8034 CRC64; MAQQYYVPNQ PERAFLVGVE RKGEQGLWTI EDSLEELAQL ARTAGMEVVG RTWQRLDHPN PATYIGKGKV EELKLAVAET GARTVIFDDE LSPAQQRNLE RALGEDIKVI DRTVLILDIF AQHARTREGQ LQVELAQYRY RLPRLTRMWT HLARQAGGRA GGATGGVGLR GPGETQLEVD RREIRRRITH LQRELEAVRA HREQYRRRRR REGVPVVALV GYTNAGKSTL LNALTNANVL AEDKLFATLD PTTRRVRLPE GREVLFTDTV GFIQKLPPDL VAAFRATLEE IHDAHILVHV VDISHPMAAA QIEAVESVLD DLGVAHKPII QAWNKIDRVA DRDAIEEEAA RDPDIVVMSA RTGEGLDHLL ERVQGVLQDL FVEVDVLLPY AHGALLHEIH EQGTIESEEH TADGTRVHAY VPAWLAARLT EATRNA // ID A0A0M8KCZ1_9BACT Unreviewed; 407 AA. AC A0A0M8KCZ1; DT 09-DEC-2015, integrated into UniProtKB/TrEMBL. DT 09-DEC-2015, sequence version 1. DT 12-APR-2017, entry version 10. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=SAMD00024442_15_53 {ECO:0000313|EMBL:GAP71645.1}; OS Candidatus Symbiothrix dinenymphae. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; OC Candidatus Symbiothrix. OX NCBI_TaxID=467085 {ECO:0000313|EMBL:GAP71645.1, ECO:0000313|Proteomes:UP000050180}; RN [1] {ECO:0000313|Proteomes:UP000050180} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=B4-10h {ECO:0000313|Proteomes:UP000050180}; RX PubMed=26079531; RA Yuki M., Kuwahara H., Shintani M., Izawa K., Sato T., Starns D., RA Hongoh Y., Ohkuma M.; RT "Dominant ectosymbiotic bacteria of cellulolytic protists in the RT termite gut also have the potential to digest lignocellulose."; RL Environ. Microbiol. 0:0-0(2015). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:GAP71645.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BBRT01000050; GAP71645.1; -; Genomic_DNA. DR EnsemblBacteria; GAP71645; GAP71645; SAMD00024442_15_53. DR Proteomes; UP000050180; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000050180}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000050180}. FT DOMAIN 208 392 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 176 203 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 407 AA; 46598 MW; 13669C18EDB8150C CRC64; MKEFILTDAI TENAVLVGLI TPAQNEQKAK EYLDELDFLA DTAGIRTVKR FTQRLEQAHP VTFVGSGKLQ EIKAYTEDEN NETGMVIFDD ELSPKQLRNI EAELKVKIMD RTSLILDIFA ARAQTAHAKT QVELAQYNYM LPRLKRLWTH LERQSGTGSG GMRMRGPGET QLEIDRRIIL NKIAKLKEDL KEIDKQKANQ RQNRGKLVRV ALVGYTNVGK STLMNLLSKS DVFAENKLFA TLDTTVRKIT IENLAFLITD TVGFIRKLPT ELIESFKSTL DEVREADLLV HVVDISHPAF EEQLEVVTNT LNDIIKTPKP TIIVFNKTDA FAHIEKDSDD LTPRTKANIP LEELKRTWMN HLSENCIFIS AQERQNIEEL KALLYQKVKE IHIRRFPYND FLYQGAE // ID A0A0M8MJ87_9FLAO Unreviewed; 413 AA. AC A0A0M8MJ87; DT 09-DEC-2015, integrated into UniProtKB/TrEMBL. DT 09-DEC-2015, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=AM493_13525 {ECO:0000313|EMBL:KOS06937.1}; OS Flavobacterium akiainvivens. OC Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales; OC Flavobacteriaceae; Flavobacterium. OX NCBI_TaxID=1202724 {ECO:0000313|EMBL:KOS06937.1, ECO:0000313|Proteomes:UP000037755}; RN [1] {ECO:0000313|EMBL:KOS06937.1, ECO:0000313|Proteomes:UP000037755} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=IK-1 {ECO:0000313|EMBL:KOS06937.1, RC ECO:0000313|Proteomes:UP000037755}; RA Wan X., Hou S., Saito J., Donachie S.; RT "Whole genome sequence of Flavobacterium akiainvivens IK-1T, from RT decaying Wikstroemia oahuensis, an endemic Hawaiian shrub."; RL Submitted (AUG-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KOS06937.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LIYD01000005; KOS06937.1; -; Genomic_DNA. DR RefSeq; WP_054408562.1; NZ_LIYD01000005.1. DR EnsemblBacteria; KOS06937; KOS06937; AM493_13525. DR PATRIC; fig|1202724.3.peg.2801; -. DR Proteomes; UP000037755; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000037755}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000037755}. FT DOMAIN 200 386 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 413 AA; 47981 MW; 1D6F1D1395FBB614 CRC64; MLEKETIQYE KAVLAGIITR EQDEQKLSEY LDELEFLTYT AGGEVVKRFS QRMEKPNPKT FLGTGKIEEI NLYIKEHDIK TVIFDDELTP AQQKNLTREL NAKVLDRTNL ILDIFAQRAQ TSYARTQVEL AQCQYLLPRL SGMWTHLERQ RGGIGMRGPG ETEIETDRRI VRDRIALLKE KLRTIDRQMG VQRSNRGAMV RVALVGYTNV GKSTLMNVIS KSEVFVENKL FATLDTTVRK VVIKNLPFLL SDTVGFIRKL PTQLVESFKS TLDEVREADL LLHVVDISHH DFEDHIASVN QILQEIKSND KPTIMVFNKI DAFKPDVIEE DDLVTEKTTR HYSLDEWKQT WMNNVGENNA LFISATNKEN FEQFREKVYE AVRQIHITRF PYNNFLYPDY KDNHAEEKES NDE // ID A0A0M8MP16_9MICO Unreviewed; 506 AA. AC A0A0M8MP16; DT 09-DEC-2015, integrated into UniProtKB/TrEMBL. DT 09-DEC-2015, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=XI38_06595 {ECO:0000313|EMBL:KOS10950.1}; OS Microbacterium chocolatum. OC Bacteria; Actinobacteria; Micrococcales; Microbacteriaceae; OC Microbacterium. OX NCBI_TaxID=84292 {ECO:0000313|EMBL:KOS10950.1, ECO:0000313|Proteomes:UP000037737}; RN [1] {ECO:0000313|EMBL:KOS10950.1, ECO:0000313|Proteomes:UP000037737} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SIT 101 {ECO:0000313|EMBL:KOS10950.1, RC ECO:0000313|Proteomes:UP000037737}; RA Li X., Xu Y.; RT "Complete genome sequence of Microbacterium chocolatum SIT 101, a RT bacterium enantioselectively hydrolyzing mesomeric diesters."; RL Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KOS10950.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LAVO01000006; KOS10950.1; -; Genomic_DNA. DR RefSeq; WP_053547543.1; NZ_KQ440287.1. DR EnsemblBacteria; KOS10950; KOS10950; XI38_06595. DR KEGG; mcw:A8L33_08560; -. DR PATRIC; fig|84292.3.peg.1346; -. DR KO; K03665; -. DR Proteomes; UP000037737; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000037737}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000037737}. FT DOMAIN 287 452 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 506 AA; 54665 MW; D2A4B3AC3E7A503C CRC64; MTHHTTPPTA DEQPVDPVDR VLSHADTGSG ARVFGNAQAL QDASTAYGAD SDGDQWDREE RAALRRVPGL STELEDVTEV EYRQLRLENV VLVGVHPQGA TEDAENSLRE LAALAETAGA VVLDGVLQRR PHPDPATYVG RGKAEELRDI VAAVGADTVI ADTELAPSQR RALEDVVKVK VIDRTTVILD IFSQHAKSRE GKAQVELAQL EYLLPRLRGW GDSMSRQAGG QVGAGGAGMG SRGPGETKIE LDRRRIRTRM AQLRRQIRDF APARDAKRAE RRRNTIPSVA IAGYTNAGKS SLLNRLTSAG VLVENALFAT LDATVRRAEA EDGRVYTLTD TVGFVRNLPH QLVEAFRSTL EEVGQADVIV HVVDGAHPDP AAQLATVRDV IGDVGARDLP EIVVFNKADL LDDDARLLLR GLQPDAVFAS SRTGEGVAEL RATIEAALPL PAVEVHALVP YDRGELVSAI HEHGMILAEE HEEEGTAVHA RVGEHLAARL APFLRN // ID A0A0M8SNT5_9ACTN Unreviewed; 501 AA. AC A0A0M8SNT5; DT 09-DEC-2015, integrated into UniProtKB/TrEMBL. DT 09-DEC-2015, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=ADK55_35625 {ECO:0000313|EMBL:KOU37665.1}; OS Streptomyces sp. WM4235. OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae; OC Streptomyces. OX NCBI_TaxID=1415551 {ECO:0000313|EMBL:KOU37665.1, ECO:0000313|Proteomes:UP000037699}; RN [1] {ECO:0000313|EMBL:KOU37665.1, ECO:0000313|Proteomes:UP000037699} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=WM4235 {ECO:0000313|EMBL:KOU37665.1, RC ECO:0000313|Proteomes:UP000037699}; RA Noorani M.; RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KOU37665.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LGDE01000479; KOU37665.1; -; Genomic_DNA. DR RefSeq; WP_053685143.1; NZ_LGDE01000479.1. DR EnsemblBacteria; KOU37665; KOU37665; ADK55_35625. DR PATRIC; fig|1415551.3.peg.7784; -. DR Proteomes; UP000037699; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 2. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000313|EMBL:KOU37665.1}; KW Complete proteome {ECO:0000313|Proteomes:UP000037699}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900, KW ECO:0000313|EMBL:KOU37665.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000037699}. FT DOMAIN 280 445 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 501 AA; 54719 MW; 5C15760D3A87B7E5 CRC64; MTSSSSPSQD ARDAQDVRDP QSFTESLRAD ALMEEDVAWS HEIDGDRDGE QLERSERAAL RRVVGLSTEL EDVTEVEYRQ LRLERVVLVG VWTSGTVTDA ENSLAELAAL AETAGALVLD GVIQRRDKPD PATFIGSGKA RELRDIVMES GADTVVCDGE LSPGQLIALE DVVKVKVVDR TALILDIFAQ HAKSREGKAQ VALAQMQYML PRLRGWGASL SRQMGGGGGG GMATRGPGET KIETDRRRIR EKMAKMRREI ADMKTGRDIK RQERRRNKVP SVAIAGYTNA GKSSLLNRLT GAGVLVENSL FATLDPTVRR AETPSGRIYT LADTVGFVRH LPHHLVEAFR STMEEVGDSD LILHIVDGSH PAPEEQLAAV REVIREVGAV NVPEIVVINK ADAADPLVLQ RLLRIERHSI AVSARTGMGI EELLTLIDTE LPRPEVEVEA LVPYTRGSLI ARAHAEGEVI SEEHTPEGTL LKARVHQELA ADLAPYVPAK H // ID A0A0M8SUD7_9ACTN Unreviewed; 500 AA. AC A0A0M8SUD7; DT 09-DEC-2015, integrated into UniProtKB/TrEMBL. DT 09-DEC-2015, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=ADK54_16435 {ECO:0000313|EMBL:KOU44286.1}; OS Streptomyces sp. WM6378. OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae; OC Streptomyces. OX NCBI_TaxID=1415557 {ECO:0000313|EMBL:KOU44286.1, ECO:0000313|Proteomes:UP000037774}; RN [1] {ECO:0000313|EMBL:KOU44286.1, ECO:0000313|Proteomes:UP000037774} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=WM6378 {ECO:0000313|EMBL:KOU44286.1, RC ECO:0000313|Proteomes:UP000037774}; RA Noorani M.; RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KOU44286.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LGDD01000188; KOU44286.1; -; Genomic_DNA. DR RefSeq; WP_053726385.1; NZ_LGDD01000188.1. DR EnsemblBacteria; KOU44286; KOU44286; ADK54_16435. DR PATRIC; fig|1415557.3.peg.3653; -. DR Proteomes; UP000037774; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 2. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000313|EMBL:KOU44286.1}; KW Complete proteome {ECO:0000313|Proteomes:UP000037774}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900, KW ECO:0000313|EMBL:KOU44286.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000037774}. FT DOMAIN 279 444 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 500 AA; 54482 MW; 21324C0381502AD1 CRC64; MTSSSSPSQD EQSFADTHRT ESLRADALME EDVAWSHEID GARDGDQLDR SERAALRRVA GLSTELEDVT EVEYRQLRLE RVVLVGVWTT GTLLDAENSL AELAALAETA GALVLDGVYQ RRDKPDPATY IGSGKAQELR DIVLETGADT VVCDGELSPG QLIHLEDVVK VKVVDRTALI LDIFAQHAKS REGKAQVSLA QMQYMLPRLR GWGQSLSRQM GGGGSSGGGG MATRGPGETK IETDRRRIRE KMAKMRREIA EMKTGREIKR QERRRNKVPS VAIAGYTNAG KSSLLNRLTG AGVLVENSLF ATLDPTVRRA ETPTGRLYTL ADTVGFVRHL PHHLVEAFRS TMEEVGDSDL ILHVVDGSHP APEEQLAAVR EVIRDVGAVD VPEIVVINKA DAADPLVLQR LLRIERHSIA VSARTGEGIE ELLALIDAEL PRPSIEIEAL VPYTHGQLVA RAHAEGEVIS EEHVAEGTVL KARVHEVLAA ELAPYVPAAH // ID A0A0M8UZ01_9ACTN Unreviewed; 497 AA. AC A0A0M8UZ01; DT 09-DEC-2015, integrated into UniProtKB/TrEMBL. DT 09-DEC-2015, sequence version 1. DT 05-JUL-2017, entry version 12. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=ADL00_30350 {ECO:0000313|EMBL:KOV54533.1}; OS Streptomyces sp. AS58. OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae; OC Streptomyces. OX NCBI_TaxID=1519489 {ECO:0000313|EMBL:KOV54533.1, ECO:0000313|Proteomes:UP000037758}; RN [1] {ECO:0000313|EMBL:KOV54533.1, ECO:0000313|Proteomes:UP000037758} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=AS58 {ECO:0000313|EMBL:KOV54533.1, RC ECO:0000313|Proteomes:UP000037758}; RA Noorani M.; RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KOV54533.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LGDU01000363; KOV54533.1; -; Genomic_DNA. DR RefSeq; WP_053761377.1; NZ_LGDU01000363.1. DR EnsemblBacteria; KOV54533; KOV54533; ADL00_30350. DR GeneID; 32592992; -. DR PATRIC; fig|1519489.3.peg.6787; -. DR Proteomes; UP000037758; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000313|EMBL:KOV54533.1}; KW Complete proteome {ECO:0000313|Proteomes:UP000037758}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900, KW ECO:0000313|EMBL:KOV54533.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000037758}. FT DOMAIN 275 440 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 497 AA; 54381 MW; 296828768AC3B015 CRC64; MTSSSSFSQD TKRLAQDYPE GLRADALMEE DVAWSHEIDG ERDGDQFDRS ERAALRRVAG LSTELQDVTE VEYRQLRLER VVLVGVWTSG TVQDAENSLA ELAALAETAG ALVLDGVTQR RDKPDAATYI GSGKAEELRD IVIESGADTV ICDGELSPGQ LIHLEDVVKV KVIDRTALIL DIFAQHAKSR EGKAQVALAQ MQYMLPRLRG WGQSLSRQMG GGKGGGLATR GPGETKIETD RRRIREKMAK MRREIAEMKT GREIKRQERK RHKVPSVAIA GYTNAGKSSL LNRLTGAGVL VENALFATLD PTVRRAETPS GRLYTLADTV GFVRHLPHHL VEAFRSTMEE VGEADLILHV VDGSHPVPEE QLAAVREVIR DVGATDVPEI VVINKADAAD PLVLQRLMRI EKRSIAVSAR TGKGMAELLA LIDDELPRPS VEIEALVPYT HGKLVARAHG EGEVISEEHT PEGTLLKVRV HEELAAELTP YVPTPAA // ID A0A0M8V8J9_9ACTN Unreviewed; 497 AA. AC A0A0M8V8J9; DT 09-DEC-2015, integrated into UniProtKB/TrEMBL. DT 09-DEC-2015, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=ADK64_31210 {ECO:0000313|EMBL:KOV60370.1}; OS Streptomyces sp. MMG1121. OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae; OC Streptomyces. OX NCBI_TaxID=1415544 {ECO:0000313|EMBL:KOV60370.1, ECO:0000313|Proteomes:UP000037687}; RN [1] {ECO:0000313|EMBL:KOV60370.1, ECO:0000313|Proteomes:UP000037687} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MMG1121 {ECO:0000313|EMBL:KOV60370.1, RC ECO:0000313|Proteomes:UP000037687}; RA Noorani M.; RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KOV60370.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LGDV01000214; KOV60370.1; -; Genomic_DNA. DR RefSeq; WP_053664439.1; NZ_LGDV01000214.1. DR EnsemblBacteria; KOV60370; KOV60370; ADK64_31210. DR PATRIC; fig|1415544.3.peg.6737; -. DR Proteomes; UP000037687; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000313|EMBL:KOV60370.1}; KW Complete proteome {ECO:0000313|Proteomes:UP000037687}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900, KW ECO:0000313|EMBL:KOV60370.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000037687}. FT DOMAIN 275 440 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 497 AA; 54182 MW; 15DD748C27685887 CRC64; MTSSSSPSQD TKRLAHAYPE GLRADALMEE DVAWSHEIDG ERDGDQFDRS ERAALRRVVG LSTELEDVTE VEYRQLRLER VVLVGVWTTG TVQDADNSLA ELAALAETAG ALVLDGVIQR RDKPDAATYI GSGKALELRD IVVETGADTV ICDGELSPGQ LIQLEDVVKV KVIDRTALIL DIFAQHAKSR EGKAQVALAQ MQYMLPRLRG WGQSLSRQMG GGKGGGLATR GPGETKIETD RRRIREKMAK MRREIAEMKT GREIKRQERR RNKVPSVAIA GYTNAGKSSL LNRLTGAGVL VENALFATLD PTVRRAETPS GRLYTLADTV GFVRHLPHHL VEAFRSTMEE VGDADLILHV VDGSHPVPEE QLAAVREVIR DVGATDVPEI VVINKADAAD PLVLQRLLRN EKHSLAVSAR TGQGIAELLA LIDNELPRPS VEIEALVPYT HGKLVARAHT EGEVISEEHT AEGTLLKVRV HEELAADLAP YAPVSAA // ID A0A0M8VRF2_9ACTN Unreviewed; 498 AA. AC A0A0M8VRF2; DT 09-DEC-2015, integrated into UniProtKB/TrEMBL. DT 09-DEC-2015, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=ADL01_21035 {ECO:0000313|EMBL:KOV70614.1}; OS Streptomyces sp. NRRL WC-3618. OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae; OC Streptomyces. OX NCBI_TaxID=1519490 {ECO:0000313|EMBL:KOV70614.1, ECO:0000313|Proteomes:UP000037738}; RN [1] {ECO:0000313|EMBL:KOV70614.1, ECO:0000313|Proteomes:UP000037738} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NRRL WC-3618 {ECO:0000313|EMBL:KOV70614.1, RC ECO:0000313|Proteomes:UP000037738}; RA Noorani M.; RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KOV70614.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LGDW01000236; KOV70614.1; -; Genomic_DNA. DR RefSeq; WP_053743550.1; NZ_LGDW01000236.1. DR EnsemblBacteria; KOV70614; KOV70614; ADL01_21035. DR PATRIC; fig|1519490.3.peg.4595; -. DR Proteomes; UP000037738; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 2. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000313|EMBL:KOV70614.1}; KW Complete proteome {ECO:0000313|Proteomes:UP000037738}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900, KW ECO:0000313|EMBL:KOV70614.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000037738}. FT DOMAIN 275 440 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 498 AA; 54387 MW; 25C74EBA5C297AD9 CRC64; MTSSSSPSQD TERLAHTYPE GLRADALMEE DVAWSHEIDG ERDGDQFDRS ERAALRRVAG LSTELEDVTE VEYRQLRLER VVLVGVWTTG TIRDADNSLA ELAALAETAG ALVLDGVVQR RDKPDAATYI GSGKANELRD IVIETGADTV ICDGELSPGQ LIHLEDVVKV KVIDRTALIL DIFAQHAKSR EGKAQVALAQ MQYMLPRLRG WGQSLSRQMG GGKGGGLATR GPGETKIETD RRRIREKMAK MRREIAEMKT GREIKRQERR RNKVPSVAIA GYTNAGKSSL LNRLTGAGVL VENSLFATLD PTVRRAETPS GRLHTLTDTV GFVRHLPHHL VEAFRSTMEE VGDADLILHV VDGSHPDPEE QLAAVREVIR DVGATGVPEI VVINKADAAD PLTLQRLMRM ETRSIAVSAR TGQGIDELLA LIDNELPRPS VEIEALVPYT HGKLVARAHT EGEVISEEHT AEGTLLKARV HEELAAELAP YVPSAAAL // ID A0A0M8W8N4_9NOCA Unreviewed; 485 AA. AC A0A0M8W8N4; DT 09-DEC-2015, integrated into UniProtKB/TrEMBL. DT 09-DEC-2015, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=ADL03_38120 {ECO:0000313|EMBL:KOV79097.1}; OS Nocardia sp. NRRL S-836. OC Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae; Nocardia. OX NCBI_TaxID=1519492 {ECO:0000313|EMBL:KOV79097.1, ECO:0000313|Proteomes:UP000037746}; RN [1] {ECO:0000313|EMBL:KOV79097.1, ECO:0000313|Proteomes:UP000037746} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NRRL S-836 {ECO:0000313|EMBL:KOV79097.1, RC ECO:0000313|Proteomes:UP000037746}; RA Noorani M.; RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KOV79097.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LGDY01000138; KOV79097.1; -; Genomic_DNA. DR RefSeq; WP_053738456.1; NZ_LGDY01000138.1. DR EnsemblBacteria; KOV79097; KOV79097; ADL03_38120. DR PATRIC; fig|1519492.3.peg.8136; -. DR Proteomes; UP000037746; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000313|EMBL:KOV79097.1}; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000037746}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900, KW ECO:0000313|EMBL:KOV79097.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000037746}. FT DOMAIN 258 427 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 217 244 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 485 AA; 53014 MW; 4EDC0DBCBAE7DDA8 CRC64; MTENIQSAEF DPEFDEKWDD DFSTGDYERA ERAALRRVAG LSTELEDITE VEYRQLRLER VVLVGVWTEG TAADSEASLA ELARLAETAG SEVLEGVVQR RDKPDPATYI GSGKVAELRD VVQATGADTV ICDGELSPGQ LRQLEERLKV KVIDRTALIL DIFAQHARSK EGKAQVELAQ LQYLMPRLRG WGETLSRQAG GRAGGGNGGV GLRGPGETKI ETDRRRIRDR IAKLRRELAA IKVIRETKRS RRVANEIPSV AIAGYTNAGK SSLLNALTDA GVLVEDALFA TLDPTTRRSL TPEGLPYTLT DTVGFVRHLP HQLVEAFRST LEEVGQADLL VHVVDGSDAM PESQVKAVRE VLAEINERND VPMPRELLVV NKIDAVGDLG LARLRHLFPD ASFVSAHSGV GIEELRARIA ELMPRPEVVV EALVPYARGE VVARVHRDGE VLSEKHTESG TLLSARVRPD LAGVLEPFAT NGSLA // ID A0A0M8XPQ0_9ACTN Unreviewed; 496 AA. AC A0A0M8XPQ0; DT 09-DEC-2015, integrated into UniProtKB/TrEMBL. DT 09-DEC-2015, sequence version 1. DT 07-JUN-2017, entry version 12. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=ADL04_03590 {ECO:0000313|EMBL:KOX08501.1}; OS Streptomyces sp. NRRL B-3648. OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae; OC Streptomyces. OX NCBI_TaxID=1519493 {ECO:0000313|EMBL:KOX08501.1, ECO:0000313|Proteomes:UP000037702}; RN [1] {ECO:0000313|EMBL:KOX08501.1, ECO:0000313|Proteomes:UP000037702} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NRRL B-3648 {ECO:0000313|EMBL:KOX08501.1, RC ECO:0000313|Proteomes:UP000037702}; RA Noorani M.; RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KOX08501.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LGDZ01000029; KOX08501.1; -; Genomic_DNA. DR RefSeq; WP_053707575.1; NZ_LGDZ01000029.1. DR EnsemblBacteria; KOX08501; KOX08501; ADL04_03590. DR PATRIC; fig|1519493.3.peg.811; -. DR Proteomes; UP000037702; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000313|EMBL:KOX08501.1}; KW Complete proteome {ECO:0000313|Proteomes:UP000037702}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900, KW ECO:0000313|EMBL:KOX08501.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000037702}. FT DOMAIN 274 439 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 496 AA; 54159 MW; 0E1D4AFC15DBA2A4 CRC64; MTSSSSPSQD TKRLAHAYPE GLRADALMEE DVAWSYEIDG ERDGEQFDRS ERAALRRVVG LSTELEDVTE VEYRQLRLER VVLVGVWTTG TAQDADNSLA ELAALAETAG AVVLDGVIQR RDKPDAATYI GSGKAAELRD VVLETGADTV ICDGELSPGQ LIQLEDVVKV KVIDRTALIL DIFAQHAKSR EGKAQVALAQ MQYMLPRLRG WGQSLSRQMG GGRGGLATRG PGETKIETDR RRIREKMAKM RREIADMKTG REIKRQERRR NKVPSVAIAG YTNAGKSSLL NRLTGAGVLV ENALFATLDP TVRRAETPSG RLYTLADTVG FVRHLPHHLV EAFRSTMEEV GDSDLILHVV DGSHPNPEEQ LAAVREVIRD VGATDVPEIV VINKADAADP LVLQRLLRVE KRSIAVSART GRGLGELLAL IDNELPRPAV EIEALVPYTH GKLVARCHTE GEVISEEHTA EGTLLKVRVH EELAADLAPY APVSAA // ID A0A0M8Y172_9ACTN Unreviewed; 497 AA. AC A0A0M8Y172; DT 09-DEC-2015, integrated into UniProtKB/TrEMBL. DT 09-DEC-2015, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=ADL06_33550 {ECO:0000313|EMBL:KOX16388.1}; OS Streptomyces sp. NRRL F-6491. OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae; OC Streptomyces. OX NCBI_TaxID=1519495 {ECO:0000313|EMBL:KOX16388.1, ECO:0000313|Proteomes:UP000037743}; RN [1] {ECO:0000313|EMBL:KOX16388.1, ECO:0000313|Proteomes:UP000037743} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NRRL F-6491 {ECO:0000313|EMBL:KOX16388.1, RC ECO:0000313|Proteomes:UP000037743}; RA Noorani M.; RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KOX16388.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LGEE01000278; KOX16388.1; -; Genomic_DNA. DR RefSeq; WP_053646946.1; NZ_LGEE01000278.1. DR EnsemblBacteria; KOX16388; KOX16388; ADL06_33550. DR PATRIC; fig|1519495.3.peg.7162; -. DR Proteomes; UP000037743; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 2. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000313|EMBL:KOX16388.1}; KW Complete proteome {ECO:0000313|Proteomes:UP000037743}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900, KW ECO:0000313|EMBL:KOX16388.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000037743}. FT DOMAIN 276 441 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 497 AA; 54097 MW; F428A9555ACB0070 CRC64; MTSSSSPSQD NQSFAETSRT ESLRADALME EDVAWSHEID GERDGDQFDR SERAALRRVA GLSTELEDVT EVEYRQLRLE RVVLVGVWTS GTVQDAENSL AELAALAETA GALVLDGVIQ RRDKPDPATF IGSGKARELR DIVVETGADT VVCDGELSPG QLIALEDVVK VKVVDRTALI LDIFAQHAKS REGKAQVALA QMQYMLPRLR GWGQSLSRQM GGGGGGGMAT RGPGETKIET DRRRIREKMA KMRREIAEMK TGRDVKRQER RRNNVPSVAI AGYTNAGKSS LLNRLTGAGV LVENALFATL DPTVRRAETP TGRVYTLADT VGFVRHLPHH LVEAFRSTME EVGDSDLILH VVDGSHPAPE EQLAAVREVF RDVGAVNVPE IVVVNKADAA DPLVLQRLLR TEKHSLAVSA RSGQGIEELL ALIDAELPRP KVEIEALVPY TQGGLVSRVH AEGELESEEH TPEGTLIKAR VHEELAALLA PFVPAAH // ID A0A0M8YA34_9PSEU Unreviewed; 481 AA. AC A0A0M8YA34; DT 09-DEC-2015, integrated into UniProtKB/TrEMBL. DT 09-DEC-2015, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=ADK67_24490 {ECO:0000313|EMBL:KOX22377.1}; OS Saccharothrix sp. NRRL B-16348. OC Bacteria; Actinobacteria; Pseudonocardiales; Pseudonocardiaceae; OC Saccharothrix. OX NCBI_TaxID=1415542 {ECO:0000313|EMBL:KOX22377.1, ECO:0000313|Proteomes:UP000037722}; RN [1] {ECO:0000313|EMBL:KOX22377.1, ECO:0000313|Proteomes:UP000037722} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NRRL B-16348 {ECO:0000313|EMBL:KOX22377.1, RC ECO:0000313|Proteomes:UP000037722}; RA Noorani M.; RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KOX22377.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LGED01000206; KOX22377.1; -; Genomic_DNA. DR RefSeq; WP_053718824.1; NZ_LGED01000206.1. DR EnsemblBacteria; KOX22377; KOX22377; ADK67_24490. DR PATRIC; fig|1415542.3.peg.5263; -. DR Proteomes; UP000037722; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000313|EMBL:KOX22377.1}; KW Complete proteome {ECO:0000313|Proteomes:UP000037722}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900, KW ECO:0000313|EMBL:KOX22377.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000037722}. FT DOMAIN 254 423 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 481 AA; 52581 MW; 23A788DE07A61766 CRC64; MTENTYSSND WLDHEDELST GDLALEERAA LRRVAGLSTE LEDVTEVEYR QLRLERVVLV GVWTEGTTAD SDASMAELAL LAETAGSEVL EGLVQRRERP DPATYIGSGK VHELRDVVIA TGADTVICDG ELSPGQLRQL EEKLKVKVVD RTALILDIFA QHASTREGKA QVEMAQLQYL LPRLRGWGES LSRQAGGRAG GGNGGVGLRG PGETKLETDR RRIRARISKL RREIAAMSVI RETKRHRRVA NSVPNVAIAG YTNAGKSSLL NALTGAGVLV QDALFATLDP TTRRTETPEG LAYTLTDTVG FVRHLPHQLV EAFRSTLEEV ADADLLVHVV DGSDAMPEKQ VMAVREVIRE ISSRRDDPMP TELLVVNKVD AVGELGMARL RHLFPTAVFV SAHTGEGIAD LRERIAAMTP RPEVVVDALV PYARGELVAR VHREGEVLKE RHTEEGTELS ARVRPDLAGV LEKFAVNGSR A // ID A0A0M8YED6_9ACTN Unreviewed; 509 AA. AC A0A0M8YED6; DT 09-DEC-2015, integrated into UniProtKB/TrEMBL. DT 09-DEC-2015, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=ADL05_00375 {ECO:0000313|EMBL:KOX24098.1}; OS Nocardiopsis sp. NRRL B-16309. OC Bacteria; Actinobacteria; Streptosporangiales; Nocardiopsaceae; OC Nocardiopsis. OX NCBI_TaxID=1519494 {ECO:0000313|EMBL:KOX24098.1, ECO:0000313|Proteomes:UP000037694}; RN [1] {ECO:0000313|EMBL:KOX24098.1, ECO:0000313|Proteomes:UP000037694} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NRRL B-16309 {ECO:0000313|EMBL:KOX24098.1, RC ECO:0000313|Proteomes:UP000037694}; RA Noorani M.; RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KOX24098.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LGEC01000002; KOX24098.1; -; Genomic_DNA. DR RefSeq; WP_053614801.1; NZ_LGEC01000002.1. DR EnsemblBacteria; KOX24098; KOX24098; ADL05_00375. DR PATRIC; fig|1519494.3.peg.79; -. DR Proteomes; UP000037694; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 2. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000313|EMBL:KOX24098.1}; KW Complete proteome {ECO:0000313|Proteomes:UP000037694}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900, KW ECO:0000313|EMBL:KOX24098.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000037694}. FT DOMAIN 288 453 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 509 AA; 54482 MW; 01C16BA4D54C15C6 CRC64; MNTADNHGTA QPGREAVGED GFREAITATD GIDTTGAPAA DHGGDDPTTS PDRGEMELAE RHALRRVQGL STELTDVTEV EYRKLRLERV VLIGVWTNGT QADADNSLTE LAALAETAGA LVLEGLTQRR SKPDPATYVG KGKAAELSEI VMATGADTVI CDGELTPGQL RQLEDVVKVK VVDRTALILD IFAQHARSSE GKAQVELAQL SYLLPRLRGW GDSLSRQAGG SGGGGAGGGV GLRGPGETKI ETDRRRINDK MAKLRRQLAH MRTARDVKRD VRRTRDVPSV AIAGYTNAGK SSLLNRLTGA GVLVENALFA TLDPTVRQAR TPDGRAFTLS DTVGFVRHLP HQLVEAFRST LEEVADSDLI LHVVDGSHPD PESQLRAVHE VFADIEATDV PELLVVNKVD AADPDLLKTL RTRYPDIVEV SARTGEGVAE LVEALSGALP ELAHEVHAVV PYSRGDLVAK VHEEGRILSE EHTGDGTAIH AFVPALLASR LEEYVLSTA // ID A0A0M9DS16_9BACT Unreviewed; 406 AA. AC A0A0M9DS16; DT 09-DEC-2015, integrated into UniProtKB/TrEMBL. DT 09-DEC-2015, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=AD998_08180 {ECO:0000313|EMBL:KOY86126.1}; OS bacterium 336/3. OC Bacteria. OX NCBI_TaxID=1664068 {ECO:0000313|EMBL:KOY86126.1, ECO:0000313|Proteomes:UP000037950}; RN [1] {ECO:0000313|EMBL:KOY86126.1, ECO:0000313|Proteomes:UP000037950} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=336/3 {ECO:0000313|EMBL:KOY86126.1, RC ECO:0000313|Proteomes:UP000037950}; RA Isojarvi J., Battchikova N., Aro E.-M.; RT "Draft genome sequence of symbiotic bacteroides-like organism."; RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KOY86126.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LJIE01000001; KOY86126.1; -; Genomic_DNA. DR RefSeq; WP_054038735.1; NZ_LJIE01000001.1. DR EnsemblBacteria; KOY86126; KOY86126; AD998_08180. DR PATRIC; fig|1664068.3.peg.1657; -. DR Proteomes; UP000037950; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000037950}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000037950}. FT DOMAIN 205 385 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 173 203 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 406 AA; 47039 MW; 8304111FE0920D94 CRC64; MIEKKKFPET QAEKEKTILV AVHTPEQTTE QTKEYLDELA FLAETANIEV VKRFIQNLQK PHPKTYLGTG KIQEIAEYIQ TNKVETVIFD DDLSPSQVKH LEEILKCKIL DRSLLILNIF ALRAKTAQAK TQVELAQYQY ILPRLTRMWS HLSKQKGGVG MRGPGEKELE TDRRIVNDKI SLLKEKLKEI EKQSNTRRKS RKNMVRVALV GYTNVGKSTL MNLLSKSDVF AENKLFATVD STVRKVVIDQ IPFLLTDTVG FIRKLPTTLI ECFKSTLNEI VEADILLHVV DISHTSFEEQ ISIVNQTLTD IKATDKKVVL VFNKIDALKA RWEQEEEEPK FTLEELKNSY LKKNLAQEVI FISALKKENI QELRKLVIDV VSERYFQIYP NFLREDFGWH LLQEFE // ID A0A0M9DXE8_9DELT Unreviewed; 539 AA. AC A0A0M9DXE8; DT 09-DEC-2015, integrated into UniProtKB/TrEMBL. DT 09-DEC-2015, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=MHK_010331 {ECO:0000313|EMBL:KPA09499.1}; OS Candidatus Magnetomorum sp. HK-1. OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfobacterales; OC Desulfobacteraceae; Candidatus Magnetomorum. OX NCBI_TaxID=1509431 {ECO:0000313|EMBL:KPA09499.1, ECO:0000313|Proteomes:UP000037988}; RN [1] {ECO:0000313|Proteomes:UP000037988} RP NUCLEOTIDE SEQUENCE. RX PubMed=25079475; DOI=10.1111/1758-2229.12198; RA Kolinko S., Richter M., Glockner F.O., Brachmann A., Schuler D.; RT "Single-cell genomics reveals potential for magnetite and greigite RT biomineralization in an uncultivated multicellular magnetotactic RT prokaryote."; RL Environ. Microbiol. Rep. 6:524-531(2014). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KPA09499.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JPDT01002867; KPA09499.1; -; Genomic_DNA. DR EnsemblBacteria; KPA09499; KPA09499; MHK_010331. DR PATRIC; fig|1509431.4.peg.11867; -. DR Proteomes; UP000037988; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000037988}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000037988}. FT DOMAIN 379 539 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 338 365 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 539 AA; 61883 MW; 817AC98D8A367528 CRC64; MKKIHGNTVG LKSNHLNRLE KLYHRRSPQD FLIAQEIAQD LCRLSHEIHR QIGLLIDRRG MIRFVIVGDH HGLTIPRLDD YRFGPGRLNG LRLIHTHLDH NGLSEEDLAD LILLRMDFIA AITLYPDGNP KHIFAAHLLP KPINKKNYTL FPFFDLSKLQ MDCRKLILAL ETEMSHQESL KTAIEGEERA FLVHVTKPSL KYEALESMDE LDELAKSCGV SVIDSVIQYR QKLDPRFLLG KGKIRSLALQ ALQQNANLMI FDQELNPSQI RSITDMLEIR VIDRTQLILD IFARQAKSRE GKLQVELAQL KYILPRLITK NTAMSRLTGG IGGRGPGETR LEVNRRRARE RIKHLQKQVK TIQNQRSRQH SKRKKRGLPV ISIIGYTNAG KSTLLNTLTQ SQVQAENRLF VTLDPTSRRI KFPQNMDVIL TDTVGFIRDL PDDLMAAFKA TLEQLEDADL LLHVIDCSNP KYENHIQSVD KILEILKIQQ KPCIKVFNKI DQIPEDNRHL FHVEKDCVFV SAKQKQSLAP LIEMCVDRL // ID A0A0M9EIU8_9RHOB Unreviewed; 424 AA. AC A0A0M9EIU8; DT 09-DEC-2015, integrated into UniProtKB/TrEMBL. DT 09-DEC-2015, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:KPA22645.1}; GN ORFNames=shim_09320 {ECO:0000313|EMBL:KPA22645.1}; OS Shimia sp. SK013. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae. OX NCBI_TaxID=1389006 {ECO:0000313|EMBL:KPA22645.1, ECO:0000313|Proteomes:UP000037951}; RN [1] {ECO:0000313|EMBL:KPA22645.1, ECO:0000313|Proteomes:UP000037951} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SK013 {ECO:0000313|EMBL:KPA22645.1, RC ECO:0000313|Proteomes:UP000037951}; RA Voget S., Kanukollu S., Daniel R., Engelen B.; RT "Genome Sequence of Shimia sp. SK013."; RL Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KPA22645.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LAJH01000009; KPA22645.1; -; Genomic_DNA. DR RefSeq; WP_054001419.1; NZ_LAJH01000009.1. DR EnsemblBacteria; KPA22645; KPA22645; shim_09320. DR PATRIC; fig|1389006.3.peg.954; -. DR Proteomes; UP000037951; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000037951}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000037951}. FT DOMAIN 203 373 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 424 AA; 46566 MW; F198FA44F91AFD80 CRC64; MEHETQVTRA WVLHPDITGA GDRREASSAL EEAVALAAAL PNLESVGSTT VRLSKAQPGT LFGTGKIEEL RAMFEANEVE LVLIDGPVSP VQQRNLEKAW KVKILDRTGL ILEIFSDRAR TREGVLQVEM AALSYQRTRL VRAWTHLERQ RGGLGFVGGP GETQIEADRR AIDDQLVRLR RQLAKVVKTR ELHRKARAKV PFPIVALVGY TNAGKSTLFN RVTGADVMAK DMLFATLDPT MRAVELPNNG PEVILSDTVG FISDLPTQLV ASFRATLEEV LAADLVLHVR DISHPETQHQ SEDVTAILET LGLSEATPQI EIWNKIDLLS GEDREAVVAK AAREEAIFAV SAVSGQGLDE MYAAIGQSLA GDKTREQLTL AFADGKGRAW LFKEGVVESE TQTEDGFEIT VLWTAKQRAQ FESI // ID A0A0M9GRH6_9BACI Unreviewed; 422 AA. AC A0A0M9GRH6; DT 09-DEC-2015, integrated into UniProtKB/TrEMBL. DT 09-DEC-2015, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=AAV98_15715 {ECO:0000313|EMBL:KPB03749.1}; OS Bacillus sp. CHD6a. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus. OX NCBI_TaxID=1643452 {ECO:0000313|EMBL:KPB03749.1, ECO:0000313|Proteomes:UP000037908}; RN [1] {ECO:0000313|EMBL:KPB03749.1, ECO:0000313|Proteomes:UP000037908} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CHD6a {ECO:0000313|EMBL:KPB03749.1, RC ECO:0000313|Proteomes:UP000037908}; RA Lin W., Liu Y., Zheng Q., Jiao N.; RT "Genome sequence of Bacillus sp. CHD6a isolated from the shallow-sea RT hydrothermal environment."; RL Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KPB03749.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LBMD01000024; KPB03749.1; -; Genomic_DNA. DR RefSeq; WP_060666494.1; NZ_LBMD01000024.1. DR EnsemblBacteria; KPB03749; KPB03749; AAV98_15715. DR PATRIC; fig|1643452.3.peg.2484; -. DR Proteomes; UP000037908; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000037908}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000037908}. FT DOMAIN 202 364 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 422 AA; 47691 MW; 3A58165D3C94F1E5 CRC64; MNETQKKDKE RVILVGCQLP KDDDQTFFYS MEELSSLTKT ANGEVLVSLT QKRDRVHPAT YIGKGKLEEL VQLEEELEPE IIIFNGELAP SQNRNLSKML NARIIDRTQL ILDIFAQRAK SKEGKLQVEL AQLQYLLPRL GGKGVELSRL GGGIGTRGPG ETKLESDRRH INRRIVDIKT QLTSIVSHRE RYRERRKRNQ AFQLSLVGYT NAGKSTIFNR LTEAGTFEEN LLFATLDPTT RKVMMPSGFN ALLTDTVGFI QDLPTSLVAA FRSTLEEVTE ADLILHVVDS SSPDHVNHEK TVDKLLKELG VEGVPVLTVY NKKDQTTEGF TPAYNEEILH ISALDAQDIA LLTQKIESLI KNQMDTYQII VPSSEGKLIA QLKQETVLTK MEFTEDTESY DLQGYYFDNS KLASVIQQRM KK // ID A0A0M9WYT2_9BACI Unreviewed; 428 AA. AC A0A0M9WYT2; DT 09-DEC-2015, integrated into UniProtKB/TrEMBL. DT 09-DEC-2015, sequence version 1. DT 07-JUN-2017, entry version 12. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=AEA09_15800 {ECO:0000313|EMBL:KOS66961.1}; OS Lysinibacillus contaminans. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; OC Lysinibacillus. OX NCBI_TaxID=1293441 {ECO:0000313|EMBL:KOS66961.1, ECO:0000313|Proteomes:UP000050668}; RN [1] {ECO:0000313|Proteomes:UP000050668} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 25560 {ECO:0000313|Proteomes:UP000050668}; RA Liu B., Wang J., Zhu Y., Liu G., Chen Q., Chen Z., Lan J., Che J., RA Ge C., Shi H., Pan Z., Liu X.; RT "Fjat-14205 dsm 2895."; RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KOS66961.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LGRV01000005; KOS66961.1; -; Genomic_DNA. DR RefSeq; WP_053584918.1; NZ_LGRV01000005.1. DR EnsemblBacteria; KOS66961; KOS66961; AEA09_15800. DR PATRIC; fig|1293441.3.peg.3625; -. DR Proteomes; UP000050668; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000050668}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000050668}. FT DOMAIN 206 374 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 165 199 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 428 AA; 48714 MW; EE84CB21669929D7 CRC64; MDKIKEVDVL LEKAILVGVN LRHDTHFDYS MEELENLAEA LNVEVVGTVT QNLDRVTSSH YVGTGKILEI KNFYDEAQAN LVIFNDELSP SQIRNLERDL ETKVIDRTML ILDIFGRRAK TREAQLQVEL AQLQYMLPRL VGLHASLSRQ GGGTGGGFKN RGAGETKLEL DRRKIEDQIS KIKKDLEQVK EQRETQRKQR RKNALPVVSI VGYTNAGKST IMNQLLTRIG QEEHKQVFEK DMLFATLETS VRQIELPDKK SFLLTDTVGF VSKLPHHLVK AFRSTLEEAR DADLLLHVVD VSNPEYRFMM DVTNETLKAV EVEGIPTIYV YNKADLANVP YPVNSGDNIW ISAKQGVGLT ELIQIIRQYI FSDYVTCKML IPYEQGNIVS YLNENASIHT TEYEEGGTLL ALEVKEADYT KYQKYVIK // ID A0A0M9XA55_9ACTN Unreviewed; 497 AA. AC A0A0M9XA55; DT 09-DEC-2015, integrated into UniProtKB/TrEMBL. DT 09-DEC-2015, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=ADK41_06285 {ECO:0000313|EMBL:KOT43085.1}; OS Streptomyces caelestis. OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae; OC Streptomyces. OX NCBI_TaxID=36816 {ECO:0000313|EMBL:KOT43085.1, ECO:0000313|Proteomes:UP000037773}; RN [1] {ECO:0000313|EMBL:KOT43085.1, ECO:0000313|Proteomes:UP000037773} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NRRL B-24567 {ECO:0000313|EMBL:KOT43085.1, RC ECO:0000313|Proteomes:UP000037773}; RA Noorani M.; RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KOT43085.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LGCN01000063; KOT43085.1; -; Genomic_DNA. DR RefSeq; WP_030826116.1; NZ_LGCN01000063.1. DR EnsemblBacteria; KOT43085; KOT43085; ADK41_06285. DR PATRIC; fig|36816.3.peg.1347; -. DR Proteomes; UP000037773; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 2. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000313|EMBL:KOT43085.1}; KW Complete proteome {ECO:0000313|Proteomes:UP000037773}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900, KW ECO:0000313|EMBL:KOT43085.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000037773}. FT DOMAIN 275 440 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 497 AA; 54161 MW; B18A1CD701B34B08 CRC64; MTSSSSPSQD TKSFAHTYPE GLRADALMEE DVAWSLDIDG ERDGDQFDRS ERAALRRVAG LSTELEDVTE VEYRQLRLER VVLVGVWTSG TAQDAENSLA ELAALAETAG ALVLDGVIQR RDKPDAATYI GSGKAEELRD IVLDTGADTV ICDGELSPGQ LIHLEDVVKV KVIDRTALIL DIFAQHAKSR EGKAQVALAQ MQYMLPRLRG WGQSLSRQMG GGKGGGLATR GPGETKIETD RRRIREKMAK MRREIAEMKT GREIKRQERK RHKVPSVAIA GYTNAGKSSL LNRLTGAGVL VENALFATLD PTVRRAETPS GRLYTLADTV GFVRHLPHHL VEAFRSTMEE VGDADLILHV VDGSHPVPEE QLAAVREVIR DVGATGVPEI VVINKADAAD PLTLQRLLRV EKRSIAVSAR TGRGIPELLA LIDSELPRPS VEIEALVPYT HGKLVARAHD EGEVISEEHT AEGTLLKVRV HEELAAELTP YVPTPAG // ID A0A0M9YXD5_9ACTN Unreviewed; 497 AA. AC A0A0M9YXD5; DT 09-DEC-2015, integrated into UniProtKB/TrEMBL. DT 09-DEC-2015, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=ADK57_10990 {ECO:0000313|EMBL:KOU71539.1}; OS Streptomyces sp. MMG1533. OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae; OC Streptomyces. OX NCBI_TaxID=1415546 {ECO:0000313|EMBL:KOU71539.1, ECO:0000313|Proteomes:UP000037741}; RN [1] {ECO:0000313|EMBL:KOU71539.1, ECO:0000313|Proteomes:UP000037741} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MMG1533 {ECO:0000313|EMBL:KOU71539.1, RC ECO:0000313|Proteomes:UP000037741}; RA Noorani M.; RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KOU71539.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LGDG01000074; KOU71539.1; -; Genomic_DNA. DR RefSeq; WP_053749211.1; NZ_LGDG01000074.1. DR EnsemblBacteria; KOU71539; KOU71539; ADK57_10990. DR PATRIC; fig|1415546.3.peg.2399; -. DR Proteomes; UP000037741; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000313|EMBL:KOU71539.1}; KW Complete proteome {ECO:0000313|Proteomes:UP000037741}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900, KW ECO:0000313|EMBL:KOU71539.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000037741}. FT DOMAIN 275 440 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 497 AA; 54203 MW; E7632AD88069056D CRC64; MTSSSSSSQD TERPAHAYPE GLRADALMEE DVAWSHEIDG DRDGDQFDRS ERAALRRVAG LSTELEDVTE VEYRQLRLER VVLVGVWTTG TARDADNSLA ELAALAETAG ALVLDGVIQR RDKPDAATYI GSGKADELRD IVLETGADTV ICDGELSPGQ LIHLEDVVKV KVIDRTALIL DIFAQHAKSR EGKAQVALAQ MQYMLPRLRG WGQSLSRQMG GGKGGGLATR GPGETKIETD RRRIREKMAK MRREIADMKT GREIKRQERK RNKVPSVAIA GYTNAGKSSL LNRLTGAGVL VENALFATLD PTVRRAETPS GRLYTLADTV GFVRHLPHHL VEAFRSTMEE VGESDLILHV VDGSHPDPEE QLAAVREVIR DVGATGVPEI VVINKADAAD PLTLQRLMRI EKRSIAVSAR TGRGIEELLA LIDNELPRPS VEVEALVPYT HGKLVARAHD EGEVLSAEHT PEGTLLKVRV HEELAADLAP YVPAALA // ID A0A0N0BKP2_9HYME Unreviewed; 531 AA. AC A0A0N0BKP2; DT 09-DEC-2015, integrated into UniProtKB/TrEMBL. DT 09-DEC-2015, sequence version 1. DT 12-APR-2017, entry version 7. DE SubName: Full=Putative GTP-binding protein 6 {ECO:0000313|EMBL:KOX80888.1}; GN ORFNames=WN51_00805 {ECO:0000313|EMBL:KOX80888.1}; OS Melipona quadrifasciata. OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; OC Pterygota; Neoptera; Holometabola; Hymenoptera; Apocrita; Aculeata; OC Apoidea; Apidae; Melipona. OX NCBI_TaxID=166423 {ECO:0000313|EMBL:KOX80888.1, ECO:0000313|Proteomes:UP000053105}; RN [1] {ECO:0000313|EMBL:KOX80888.1, ECO:0000313|Proteomes:UP000053105} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=0111107301 {ECO:0000313|EMBL:KOX80888.1}; RC TISSUE=Whole body {ECO:0000313|EMBL:KOX80888.1}; RA Pan H., Kapheim K.; RT "The genome of Melipona quadrifasciata."; RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; KQ435694; KOX80888.1; -; Genomic_DNA. DR Proteomes; UP000053105; Unassembled WGS sequence. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR CDD; cd01878; HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 4: Predicted; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000053105}; KW Reference proteome {ECO:0000313|Proteomes:UP000053105}. FT DOMAIN 256 355 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 218 252 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 531 AA; 61542 MW; 9E9B7BE25627942E CRC64; MQCLKKFAVL NKSQYIIKRR RKFNILNVIR QCKYESDVAF EYTENEEEKN IYAHVSQDYL GTVVGGNRIF VIQPYIKWGV NKKRNTTPQL QLSEAKALVS NLTSWNVVGE KLVPLLSLQR HKLVGSGALE VLKHDIEKCL HVTAIFISTN SLKFVQIAEL QKTFNLPIYD RYSIVIHIFR ERAKTPEAKL QVALAELPYV KQKMIDFTTY RIGRINYTEK MKNMLQAREK KLRNALQKLK EHRQRIKQQR LSYGFPTIAI VGYTNAGKTS LIKALTDDDS LQPEDKLFAT LDTTVHPGLL PNMLKVLYVD TIGFIQDIPE TLIEPFIVTL EDAMTADILV HIFDVSHPDV KAQIQHVQKT IEPMIDENKL VINVANKCDI VEKHIVESVI PKDTFAISAV KLTGINLLRS RIEEEITNTT NLLKRRIRIR NECLKVEFLD EIYPEVWHAN IRTLESYITC TLNVKLFNPT FLILLQIDVN RYRITLYELS ILDAANLTTL YYPRFQAISS KFQLQLKLCF LDVYVRLHNY V // ID A0A0N0E7M3_9RHOB Unreviewed; 439 AA. AC A0A0N0E7M3; DT 09-DEC-2015, integrated into UniProtKB/TrEMBL. DT 09-DEC-2015, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=SU32_08735 {ECO:0000313|EMBL:KPB01332.1}; OS Ahrensia marina. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae; Ahrensia. OX NCBI_TaxID=1514904 {ECO:0000313|EMBL:KPB01332.1, ECO:0000313|Proteomes:UP000038011}; RN [1] {ECO:0000313|EMBL:KPB01332.1, ECO:0000313|Proteomes:UP000038011} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=LZD062 {ECO:0000313|EMBL:KPB01332.1, RC ECO:0000313|Proteomes:UP000038011}; RA Liu J.; RT "Ahrensia donghaiensis sp. nov., a novel dimethylsulphoniopropionate- RT cleavage bacterium isolated from seawater and emended descriptions of RT the genus Ahrensia and Ahrensia kielensis."; RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KPB01332.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JXMU01000011; KPB01332.1; -; Genomic_DNA. DR RefSeq; WP_053998974.1; NZ_JXMU01000011.1. DR EnsemblBacteria; KPB01332; KPB01332; SU32_08735. DR PATRIC; fig|1514904.3.peg.566; -. DR Proteomes; UP000038011; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000038011}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000038011}. FT DOMAIN 208 383 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 167 194 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 439 AA; 48250 MW; CDEBC1593FEFCC00 CRC64; MEPTRAIVIA PDITQTNQAK STFASGAIER SAAERLVEAE GLALAIDLVI AYSAVVSVAK PRPATLLGSG KVKELAEIVR AEKAKLVVID HALTPVQQRN LEKELHAKVL DRTGLILEIF GRRARTKEGT LQVELAHLNY QRGRLVRSWT HLERQRGGAG FLGGPGETQI EADRRILRDK IKSLESDLEA VRRTRTLHRS KRKKIPLPVV AFVGYTNAGK STLFNRMTGA DVHAEDMLFA TLDPTLRRVQ LPSGTWVILS DTVGFISDLP THLVAAFRAT LEEVQEANLV LHVHDASDSA ASAQADDVQQ VLKDLDIDPE DKSHVIEVWN KIDALEPEDR EALQKRIEPG KGEALNQVAV SALDGSGLPD LLALIEQKIA GSLVSRRLEI SPARFSDVAW LYENGIVRDR EALEDGTIVV EVDLTPENSE AYDRRAKSS // ID A0A0N0H8B1_THEVU Unreviewed; 417 AA. AC A0A0N0H8B1; DT 09-DEC-2015, integrated into UniProtKB/TrEMBL. DT 09-DEC-2015, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=ADL26_17345 {ECO:0000313|EMBL:KPC70260.1}; OS Thermoactinomyces vulgaris. OC Bacteria; Firmicutes; Bacilli; Bacillales; Thermoactinomycetaceae; OC Thermoactinomyces. OX NCBI_TaxID=2026 {ECO:0000313|EMBL:KPC70260.1, ECO:0000313|Proteomes:UP000037969}; RN [1] {ECO:0000313|EMBL:KPC70260.1, ECO:0000313|Proteomes:UP000037969} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NRRL F-5595 {ECO:0000313|EMBL:KPC70260.1, RC ECO:0000313|Proteomes:UP000037969}; RA Noorani M.; RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KPC70260.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LGKI01000700; KPC70260.1; -; Genomic_DNA. DR RefSeq; WP_022737630.1; NZ_LGKI01000700.1. DR EnsemblBacteria; KPC70260; KPC70260; ADL26_17345. DR PATRIC; fig|2026.3.peg.3911; -. DR Proteomes; UP000037969; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000037969}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000037969}. FT DOMAIN 198 360 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 157 191 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 417 AA; 46953 MW; F88DF18492BE29E0 CRC64; MQNSDKEKAI LVGCGPKRNE WELLSTLEEL GRLAETSAAE VIGQAVQFRD RLDPAWLIGK GKAEEVAQMA EEREADLVIF DHELSPAQIR NLERLLPCKV IDRTQLILDI FAQRAQTKEG RIQVELAQLE YMLPRLAGRG KELSRLGGGI GTRGPGEKKL ETDRRHIHRQ IRDLKKQLEE VKKHRRLHSE RRKKNEVVQV ALVGYTNAGK STLLNRLTGA EVLAENKLFA TLDPTSRMLE LPSGQQVILT DTVGFIRNLP HHLVAAFRST LEQVREADLL LHVVDAAHPE AAEQIAAVEK VLEELQATDI PTLMVLNKAD LLDGQGIEPD GREIVRISAL REEDVDKLKR KIENLLRSKP MTVHLEIPIE RGDLLSALHR MAEVVSAKAN DAFMEIECRL TDKQLEKLPS ELKQQVT // ID A0A0N0I6I4_9BACI Unreviewed; 272 AA. AC A0A0N0I6I4; DT 09-DEC-2015, integrated into UniProtKB/TrEMBL. DT 09-DEC-2015, sequence version 1. DT 07-JUN-2017, entry version 6. DE SubName: Full=GTPase HflX {ECO:0000313|EMBL:KPC99582.1}; GN Name=hflX_1 {ECO:0000313|EMBL:KPC99582.1}; GN ORFNames=LR69_02139 {ECO:0000313|EMBL:KPC99582.1}; OS Geobacillus sp. BCO2. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus. OX NCBI_TaxID=1547578 {ECO:0000313|EMBL:KPC99582.1, ECO:0000313|Proteomes:UP000037948}; RN [1] {ECO:0000313|EMBL:KPC99582.1, ECO:0000313|Proteomes:UP000037948} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BCO2 {ECO:0000313|EMBL:KPC99582.1, RC ECO:0000313|Proteomes:UP000037948}; RA Patel B.K.; RT "Draft genome sequence of a Geobacillus isolate, a moderate RT thermophile from the Great Artesian Basin of Australia."; RL Submitted (AUG-2015) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KPC99582.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LJAJ01000017; KPC99582.1; -; Genomic_DNA. DR EnsemblBacteria; KPC99582; KPC99582; LR69_02139. DR PATRIC; fig|1547578.4.peg.2397; -. DR Proteomes; UP000037948; Unassembled WGS sequence. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000037948}; KW Reference proteome {ECO:0000313|Proteomes:UP000037948}. FT DOMAIN 197 253 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 272 AA; 30495 MW; 9BE5EB3ECB867008 CRC64; MSREQAILVG CQLAGVDDER FRYSMEELAS LVATANGEVA AELTQKREAP HPATYIGKGK TEELAALVKE LEPDLVVFNS ELSPSQARNL TRMLGEVKVI DRTQLILDIF AQRARSKEGK LQVELAQLEY MLPRLSGQGE ALSRLGGGIG TRGPGETKLE TDRRHIRRRI DDIKAELRRV AEHRGRYRER RQKNQAFQVA LVGYTNAGKS TIFNRLTAAD SLEENLLFAT LDPLTRKCVL PCGYTVLVTD TVGSFKTCRR RLSPRSARRS RK // ID A0A0N0IBW2_9GAMM Unreviewed; 426 AA. AC A0A0N0IBW2; DT 09-DEC-2015, integrated into UniProtKB/TrEMBL. DT 09-DEC-2015, sequence version 1. DT 30-AUG-2017, entry version 15. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=M992_0382 {ECO:0000313|EMBL:KPD04272.1}; OS Moellerella wisconsensis ATCC 35017. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; OC Morganellaceae; Moellerella. OX NCBI_TaxID=1354267 {ECO:0000313|EMBL:KPD04272.1, ECO:0000313|Proteomes:UP000053226}; RN [1] {ECO:0000313|EMBL:KPD04272.1, ECO:0000313|Proteomes:UP000053226} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 35017 {ECO:0000313|EMBL:KPD04272.1, RC ECO:0000313|Proteomes:UP000053226}; RA Plunkett G.III., Neeno-Eckwall E.C., Glasner J.D., Perna N.T.; RT "ATOL: Assembling a taxonomically balanced genome-scale reconstruction RT of the evolutionary history of the Enterobacteriaceae."; RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KPD04272.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LGAA01000003; KPD04272.1; -; Genomic_DNA. DR RefSeq; WP_047254968.1; NZ_LGAA01000003.1. DR EnsemblBacteria; KPD04272; KPD04272; M992_0382. DR Proteomes; UP000053226; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000053226}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000053226}. FT DOMAIN 198 365 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 426 AA; 48421 MW; FBE405CD480DAD21 CRC64; MFDRYEGGEH AVLVHVFFSQ EKDIDNLEEF ESLVTSANVK PVQIITGSRR APHRKYYVGE GKAEEIAEAV QASGADVVLF NHALSPAQER NLERLCQCKV VDRTGVILDI FAQRARTHEG KLQVELAQLR HLSTRLIRGW THLERQKGGI GLRGPGETQL ETDRRLLRDK IKQILSRLGK VEKQREQGRQ ARSKADIPTV SLVGYTNAGK SSLFNRMTTS DVYAADQLFA TLDPTLRRID VDDVGTVVLA DTVGFIRHLP HDLVAAFKAT LQETREATLL LHVIDAVDNR VDENIQAVES VLEEIEAHEI PTLLVMNKID RLDDFVPRID RDEDNKPIRV WVSAQTGEGI PLLLQALTER LSGEIAHFEL RLPPEEGRLR SRFYQLNAIE HEHVDEDGYL LLEVRLPIVD WRRLCKQEPQ LPDYIL // ID A0A0N0JRV3_9SPHN Unreviewed; 441 AA. AC A0A0N0JRV3; DT 09-DEC-2015, integrated into UniProtKB/TrEMBL. DT 09-DEC-2015, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=IP79_03325 {ECO:0000313|EMBL:KPF65215.1}; OS Porphyrobacter sp. AAP60. OC Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales; OC Erythrobacteraceae; Porphyrobacter. OX NCBI_TaxID=1523423 {ECO:0000313|EMBL:KPF65215.1, ECO:0000313|Proteomes:UP000037996}; RN [1] {ECO:0000313|EMBL:KPF65215.1, ECO:0000313|Proteomes:UP000037996} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=AAP60 {ECO:0000313|EMBL:KPF65215.1, RC ECO:0000313|Proteomes:UP000037996}; RA Zeng Y., Feng F., Liu Y., Koblizek M.; RT "Novel Diversity of Limnic Aerobic Anoxygenic Phototrophic Bacteria as RT Revealed by High-throughput Strain Identification and Genome RT Sequencing."; RL Submitted (AUG-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KPF65215.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LJHV01000002; KPF65215.1; -; Genomic_DNA. DR RefSeq; WP_054117791.1; NZ_LJHV01000002.1. DR EnsemblBacteria; KPF65215; KPF65215; IP79_03325. DR PATRIC; fig|1523423.3.peg.1273; -. DR Proteomes; UP000037996; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000037996}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}. FT DOMAIN 209 383 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 175 202 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 441 AA; 48374 MW; 2736FAF897767EAE CRC64; MSFDSDLQDE VTRGARALVL CPDIRALRYD LDAAERLAEA EGLALAIGVV IGHSAILPVR KMQPNTLFGS GQVQNIAVWC EQYEAELVIV DGALTPIQQR NLEDKLKRKV IDRTGLILEI FGERAATAEG RLQVELAHLD YQQSRLVRSW THLERQRGGF GFLGGPGETQ IEADRRMIRQ RMSRLRRELD QVRKTRTLHR ERRGRAPWPV VALVGYTNAG KSTLFNRLTG AEVMAEDLLF ATLDPTMRAI GLPGVEKVIL SDTVGFISDL PTQLVAAFRA TLEEVTAADV ICHVRDMANP SHAAQKKQVI DVLGDLGVVD AETGTSAIPI LEVWNKCDLL DAESLDELRE LAAGQGTIAL SAVTGEGVDA LEAELARMLT GTAREATFIL PVQDGRRIAW LHAHGEVLAD EDGGEGEDGP VRRLTVRLNP KELGQFSSIS F // ID A0A0N0JV83_9PROT Unreviewed; 388 AA. AC A0A0N0JV83; DT 09-DEC-2015, integrated into UniProtKB/TrEMBL. DT 09-DEC-2015, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=IP84_06620 {ECO:0000313|EMBL:KPF69115.1}; OS beta proteobacterium AAP99. OC Bacteria; Proteobacteria; Betaproteobacteria. OX NCBI_TaxID=1523428 {ECO:0000313|EMBL:KPF69115.1, ECO:0000313|Proteomes:UP000037960}; RN [1] {ECO:0000313|EMBL:KPF69115.1, ECO:0000313|Proteomes:UP000037960} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=AAP99 {ECO:0000313|EMBL:KPF69115.1, RC ECO:0000313|Proteomes:UP000037960}; RA Zeng Y., Feng F., Liu Y., Koblizek M.; RT "Novel Diversity of Limnic Aerobic Anoxygenic Phototrophic Bacteria as RT Revealed by High-throughput Strain Identification and Genome RT Sequencing."; RL Submitted (AUG-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KPF69115.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LJIA01000006; KPF69115.1; -; Genomic_DNA. DR RefSeq; WP_054125158.1; NZ_LJIA01000006.1. DR EnsemblBacteria; KPF69115; KPF69115; IP84_06620. DR PATRIC; fig|1523428.3.peg.2880; -. DR Proteomes; UP000037960; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000037960}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000037960}. FT DOMAIN 190 359 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 156 183 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 388 AA; 42896 MW; C8C5E33F9A310653 CRC64; MRFILVGVDF GDKDFGDSFA ELRLLAESAG AEVVHESIGK RSRPDASLFI GSGKAAEIAG PVKTLPADGV IFNHALTPAQ QRNLQRVFEV RVVDRTTLIL DIFALRAQSH EGKLQVELAQ LRHLSSRLVR QWSHLERQKG GVGMRGPGEK QLELDRRMLD ARVKRLSADL ARLQKQRETQ RRARSRGEVF KVSLVGYTNA GKSTLFNQLT HAGVYSADQL FATLDTTTRR VYLGDGVQIS LADTVGFIRE LPHQLVEAFK ATLEETVHAD LLLHVIDASS ESRDVQIAQV ESVLQEIGAD DIPCIHVLNK IDVTGVPPRW RDLADDGRAA VGELYLSART GAGVELLREQ LLAKARSRVQ QVETRRDESS QMQMAEIFAG GIPLGSDR // ID A0A0N0JXJ3_9BRAD Unreviewed; 460 AA. AC A0A0N0JXJ3; DT 09-DEC-2015, integrated into UniProtKB/TrEMBL. DT 09-DEC-2015, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=IP69_04780 {ECO:0000313|EMBL:KPF71808.1}; OS Bosea sp. AAP35. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Bradyrhizobiaceae; Bosea. OX NCBI_TaxID=1523417 {ECO:0000313|EMBL:KPF71808.1, ECO:0000313|Proteomes:UP000037890}; RN [1] {ECO:0000313|EMBL:KPF71808.1, ECO:0000313|Proteomes:UP000037890} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=AAP35 {ECO:0000313|EMBL:KPF71808.1, RC ECO:0000313|Proteomes:UP000037890}; RA Zeng Y., Feng F., Liu Y., Koblizek M.; RT "Novel Diversity of Limnic Aerobic Anoxygenic Phototrophic Bacteria as RT Revealed by High-throughput Strain Identification and Genome RT Sequencing."; RL Submitted (AUG-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KPF71808.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LJHQ01000010; KPF71808.1; -; Genomic_DNA. DR RefSeq; WP_054141684.1; NZ_LJHQ01000010.1. DR EnsemblBacteria; KPF71808; KPF71808; IP69_04780. DR PATRIC; fig|1523417.3.peg.92; -. DR Proteomes; UP000037890; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000037890}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000037890}. FT DOMAIN 226 400 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 460 AA; 50674 MW; C67F6CD4EAF65626 CRC64; MSARSDADEA RAAVKPLDAI EREIAANTRA YVIGPYQQRR GASDANQRSF AARLDEAVGL AAAIDLTVVE PIQVMLTALR PATYLGKGKV EEIAERIRIE EIGLIVMDCA LSPVQQRNLE KAFGCKVIDR TGLILEIFGR RARTKEGALQ VELAHLNYQK SRLVRSWTHL ERQRGGFGFL GGPGETQIEA DRRIIQERMT KIERDLEAVK RTRGLHRASR KRVPYPVVAL VGYTNAGKST LFNRLTSAEV LAQDMLFATL DPTARALKLP HGARIMLSDT VGFISDLPTQ LVAAFRATLE DAIEADVLLH IRDVAHEDTQ AQAADVQAIL RDLGIDPDDG QRVVEVWNKS DLLTPEERER QLGLAGLKPE VSRPVLVSAV TGDGMGRLTD AIEMRIARSR PIYRLSLAPG DGQSLAWLHA NGEVLDRSDA EDGALALRVR LPPEREGAFG ARFPQAERDN // ID A0A0N0K0T4_9PROT Unreviewed; 443 AA. AC A0A0N0K0T4; DT 09-DEC-2015, integrated into UniProtKB/TrEMBL. DT 09-DEC-2015, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=IP88_07360 {ECO:0000313|EMBL:KPF75166.1}; OS alpha proteobacterium AAP81b. OC Bacteria; Proteobacteria; Alphaproteobacteria. OX NCBI_TaxID=1523432 {ECO:0000313|EMBL:KPF75166.1, ECO:0000313|Proteomes:UP000037971}; RN [1] {ECO:0000313|EMBL:KPF75166.1, ECO:0000313|Proteomes:UP000037971} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=AAP81b {ECO:0000313|EMBL:KPF75166.1, RC ECO:0000313|Proteomes:UP000037971}; RA Zeng Y., Feng F., Liu Y., Koblizek M.; RT "Novel Diversity of Limnic Aerobic Anoxygenic Phototrophic Bacteria as RT Revealed by High-throughput Strain Identification and Genome RT Sequencing."; RL Submitted (AUG-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KPF75166.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LJHX01000068; KPF75166.1; -; Genomic_DNA. DR RefSeq; WP_054128608.1; NZ_LJHX01000068.1. DR EnsemblBacteria; KPF75166; KPF75166; IP88_07360. DR PATRIC; fig|1523432.3.peg.2751; -. DR Proteomes; UP000037971; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000037971}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000037971}. FT DOMAIN 225 392 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 191 218 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 443 AA; 47779 MW; 080A78F2FF2969B3 CRC64; MSAGPGPEHA KGNGKPNGWD AERGIRLGSA AVVVLPVRDD SQEKSLRSPG ARLAEAAGLA CAIALDVVHQ EAVRLRAVSA SSLFGKGQIE RLAATVAAHE AEVVIIDGIV SPIQQRNLEK GLGAKVIDRT GLILEIFGER ASTREGTLQV ELAHLQYQAS RLVRSWTHLE RQRGGFGFLG GPGESQIETD RRLIRDRISR LKKELEEVRR TRGLHRRQRQ KAPWPIVALV GYTNAGKSTL FNRLTGADVF AQDLLFATLD PTMRAITLPG FDKVVLSDTV GFVSDLPTQL VAAFRATLEE VLEADLIVHV RDVAHPDSDA QAADVTSVLG DLGIAETAPL LTVLNKIDAL ESDARAAVLA RGDEATVAVS ALGGEGIDVL RRRIADLLRV EAKTHQFRLA ASDGRRLAWL HEHGEVLGEA SDGETMAVEV RLSDIDRARF AAI // ID A0A0N0K692_9SPHN Unreviewed; 445 AA. AC A0A0N0K692; DT 09-DEC-2015, integrated into UniProtKB/TrEMBL. DT 09-DEC-2015, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=IP83_12250 {ECO:0000313|EMBL:KPF81975.1}; OS Novosphingobium sp. AAP93. OC Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales; OC Sphingomonadaceae; Novosphingobium. OX NCBI_TaxID=1523427 {ECO:0000313|EMBL:KPF81975.1, ECO:0000313|Proteomes:UP000037906}; RN [1] {ECO:0000313|EMBL:KPF81975.1, ECO:0000313|Proteomes:UP000037906} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=AAP93 {ECO:0000313|EMBL:KPF81975.1, RC ECO:0000313|Proteomes:UP000037906}; RA Zeng Y., Feng F., Liu Y., Koblizek M.; RT "Novel Diversity of Limnic Aerobic Anoxygenic Phototrophic Bacteria as RT Revealed by High-throughput Strain Identification and Genome RT Sequencing."; RL Submitted (AUG-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KPF81975.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LJHZ01000076; KPF81975.1; -; Genomic_DNA. DR RefSeq; WP_054122506.1; NZ_LJHZ01000076.1. DR EnsemblBacteria; KPF81975; KPF81975; IP83_12250. DR PATRIC; fig|1523427.4.peg.3342; -. DR Proteomes; UP000037906; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000037906}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000037906}. FT DOMAIN 213 389 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 445 AA; 48694 MW; 7DEB094BD72B49CF CRC64; MSQFEFGRET ELVGEVTRGA RAVVVLPDLR QKGGLDADSR LEEGQGLARA IGIDVVDAFA LPIRNVRPAT LFGEGQVQKI GVAINQSDAE LVIVDGALSA IQQRNLEDKL ERKVIDRTGL ILEIFGERAA TAEGRLQVEL AHLDYQAGRL VRSWTHLERQ RGGFGFLGGP GETQIEADRR LIRGRMARIR RELEQVRRTR SLHRERRQRA PWPVIALVGY TNAGKSTLFN RMTGADVMAQ DLLFATLDPT MRAIRLPGLD KAILSDTVGF ISELPTQLVA AFRATLEEVT AADVIVHVRD IANPATSAQK IEVEEILADL GVIGEGGSLV PIIEAWNKWD LLPEEDRAMR RDLIAAGVPD RRVVPISAQT GEGVDDLVTL LSDLLTGGAQ VLELALPMSE GHKLAWLHAH GEVLSETAGT DAAGAPVQRL TVRLTPRELG RYSRM // ID A0A0N0KEF7_9SPHN Unreviewed; 449 AA. AC A0A0N0KEF7; DT 09-DEC-2015, integrated into UniProtKB/TrEMBL. DT 09-DEC-2015, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=IP81_12700 {ECO:0000313|EMBL:KPF91057.1}; OS Novosphingobium sp. AAP83. OC Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales; OC Sphingomonadaceae; Novosphingobium. OX NCBI_TaxID=1523425 {ECO:0000313|EMBL:KPF91057.1, ECO:0000313|Proteomes:UP000037998}; RN [1] {ECO:0000313|EMBL:KPF91057.1, ECO:0000313|Proteomes:UP000037998} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=AAP83 {ECO:0000313|EMBL:KPF91057.1, RC ECO:0000313|Proteomes:UP000037998}; RA Zeng Y., Feng F., Liu Y., Koblizek M.; RT "Novel Diversity of Limnic Aerobic Anoxygenic Phototrophic Bacteria as RT Revealed by High-throughput Strain Identification and Genome RT Sequencing."; RL Submitted (AUG-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KPF91057.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LJHY01000022; KPF91057.1; -; Genomic_DNA. DR RefSeq; WP_054108345.1; NZ_LJHY01000022.1. DR EnsemblBacteria; KPF91057; KPF91057; IP81_12700. DR PATRIC; fig|1523425.4.peg.1947; -. DR Proteomes; UP000037998; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000037998}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000037998}. FT DOMAIN 217 393 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 176 210 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 449 AA; 48968 MW; 87660EF8649091BC CRC64; MSTFEFGNNT GEVAGEVTRG ARAVVVLPDI KQRGGGFGAD ADMRLEEGQG LARAIGIEVV DSFILPIRAV RPATLFGEGQ VERIGVACNM ADAELVIVDG ALSAIQQRNL EDKLKRKVID RTGLILEIFG ERAATAEGRL QVELAHLDYQ AGRLVRSWTH LERQRGGFGF LGGPGETQIE ADRRQIRNRM ARLRKELEQV RRTRGLHRER RQRAPWPVVA LVGYTNAGKS TLFNRLTGAT VMAEDLLFAT LDPTMRAIRL PGVDKAIMSD TVGFISDLPT QLVAAFRATL EEVTGADVIV HVRDVANPAT AEQKAEVEQI LVDLGINGEG GTMIPVIEVW NKWDLLSSED QAVRRDIITA KVADMPIAPL SALTGAGVEA FLDKLGVMLT GGAQTLELTV PLADGQRLAW LHAHGDIIDE QQVGDESDEP AMRIKVRLTP RELGRFTSL // ID A0A0N0LZL3_9SPHN Unreviewed; 446 AA. AC A0A0N0LZL3; DT 09-DEC-2015, integrated into UniProtKB/TrEMBL. DT 09-DEC-2015, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=ADT71_13995 {ECO:0000313|EMBL:KPH63028.1}; OS Novosphingobium sp. ST904. OC Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales; OC Sphingomonadaceae; Novosphingobium. OX NCBI_TaxID=1684385 {ECO:0000313|EMBL:KPH63028.1, ECO:0000313|Proteomes:UP000037878}; RN [1] {ECO:0000313|EMBL:KPH63028.1, ECO:0000313|Proteomes:UP000037878} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ST904 {ECO:0000313|EMBL:KPH63028.1, RC ECO:0000313|Proteomes:UP000037878}; RA Thijs S., Bottos E.M., Van Hamme J.D., Gkorezis P., Rineau F., RA Vangronsveld J.; RT "Novosphingobium nitrophenolicus strain ST904 degrades p-nitrophenol RT and stimulates plant growth."; RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KPH63028.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LGJH01000146; KPH63028.1; -; Genomic_DNA. DR RefSeq; WP_054437772.1; NZ_LGJH01000146.1. DR EnsemblBacteria; KPH63028; KPH63028; ADT71_13995. DR PATRIC; fig|1684385.3.peg.2488; -. DR Proteomes; UP000037878; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000037878}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000037878}. FT DOMAIN 206 390 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 446 AA; 49083 MW; E6EA141C9B2C0E0B CRC64; MNEELKGEVT RGARALVVYP QMRGRGDLDP EARLEEAKGL ALAIGLIVAD AMAIPIREPR AGTLFGEGQI QNIAVACELH EAELIIVDGS LSAIQQRNLE EKFKRKVIDR TGLILEIFGE RAATAEGRLQ VELAHLDYQA GRLVRSWTHL ERQRGGFGFL GGPGETQIEA DRRMIRDRMA RIRRELEQVR RTRGLHRDRR EKAPWPVVAL VGYTNAGKST LFNYLTGAGV MAQDLLFATL DPTMRAIRLP AVEKAILSDT VGFISDLPTQ LVAAFRATLE EVNAADIILH VRDIANPDTE SQKRQVLEVL ADLGVATGEG QVEEGEEAAP AIPIIEVWNK WDLLEATHAQ ELREAMAQRS DETIVPLSAL TGMGCDFLLE TVGRTLTADA KLYSFVLPAA DGQRLAFLHA RGEVVAEEDA GEGPEGPMLR LQVRLAEREL GRFSAL // ID A0A0N0MZX2_9ACTN Unreviewed; 497 AA. AC A0A0N0MZX2; DT 09-DEC-2015, integrated into UniProtKB/TrEMBL. DT 09-DEC-2015, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=OK074_2264 {ECO:0000313|EMBL:KPI14171.1}; OS Actinobacteria bacterium OK074. OC Bacteria; Actinobacteria. OX NCBI_TaxID=1592327 {ECO:0000313|EMBL:KPI14171.1, ECO:0000313|Proteomes:UP000037991}; RN [1] {ECO:0000313|EMBL:KPI14171.1, ECO:0000313|Proteomes:UP000037991} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=OK074 {ECO:0000313|EMBL:KPI14171.1, RC ECO:0000313|Proteomes:UP000037991}; RA Brown S.D., Utturkar S.M., Klingeman D.M., Pelletier D.; RT "Draft genome sequences for four actinobacteria strains OK006 OK074 RT OV450 and OV320."; RL Submitted (AUG-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KPI14171.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LJCV01000133; KPI14171.1; -; Genomic_DNA. DR RefSeq; WP_054215416.1; NZ_LJCV01000133.1. DR EnsemblBacteria; KPI14171; KPI14171; OK074_2264. DR PATRIC; fig|1592327.3.peg.3713; -. DR Proteomes; UP000037991; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 2. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000037991}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000037991}. FT DOMAIN 274 439 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 497 AA; 53998 MW; 27F326FEB8B9E9FA CRC64; MTSSFSSQAA ERDAHTHPES LRADALMEED VAWSHGVDAD RDGDQFDRSE RAALRRVAGL STELEDVTEV EYRQLRLERV VLVGVWTSGT AQDAENSLAE LAALAETAGA LVLDGVIQRR DKPDAATYIG SGKADELRDL VLESGADTVV CDGELSPGQL IHLEDVVKVK VIDRTALILD IFAQHAKSRE GKAQVALAQM QYMLPRLRGW GQSLSRQMGG GKGGGLATRG PGETKIETDR RRIREKMAKM RREIADMKTG REIKRQERRR NHVPSVAIAG YTNAGKSSLL NRLTGAGVLV ENSLFATLDP TVRRAETPGG RLYTLADTVG FVRHLPHHLV EAFRSTMEEV GNSDLILHVV DGAHPVPEEQ LAAVREVIRD VGAIDVPEIV VINKADAADP LVLQRLLRIE KRAIAVSART GEGIAELLAL LDNELPRPSV EIEALVPYTH GKLVARAHSE GEVLSAEHTA DGTLLKVRVH ADLAADLEPY VPTAVVA // ID A0A0N0N2L0_9ACTN Unreviewed; 498 AA. AC A0A0N0N2L0; DT 09-DEC-2015, integrated into UniProtKB/TrEMBL. DT 09-DEC-2015, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=OK006_2570 {ECO:0000313|EMBL:KPI16749.1}; OS Actinobacteria bacterium OK006. OC Bacteria; Actinobacteria. OX NCBI_TaxID=1592326 {ECO:0000313|EMBL:KPI16749.1, ECO:0000313|Proteomes:UP000037912}; RN [1] {ECO:0000313|EMBL:KPI16749.1, ECO:0000313|Proteomes:UP000037912} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=OK006 {ECO:0000313|EMBL:KPI16749.1, RC ECO:0000313|Proteomes:UP000037912}; RA Brown S.D., Utturkar S.M., Klingeman D.M., Pelletier D.; RT "Draft genome sequences for four Actinobacteria strains OK006 OK074 RT OV450 and OV320."; RL Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KPI16749.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LJCU01000065; KPI16749.1; -; Genomic_DNA. DR RefSeq; WP_054229870.1; NZ_LJCU01000065.1. DR EnsemblBacteria; KPI16749; KPI16749; OK006_2570. DR PATRIC; fig|1592326.3.peg.2480; -. DR Proteomes; UP000037912; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 2. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000037912}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000037912}. FT DOMAIN 275 440 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 498 AA; 54449 MW; EE05CC49449F84AD CRC64; MTSSSSPSQD AQSLAQNYPE GLRADALMEE DVAWSHEIDG ERDGEQFDRS ERAALRRVAG LSTELEDVTE VEYRQLRLER VVLVGVWTTG TIQDADNSLA ELAALAETAG ALVLDGVVQR RDKPDAATYI GSGKANELRD IVLETGADTV ICDGELSPGQ LIHLEDVVKV KVIDRTALIL DIFAQHAKSR EGKAQVALAQ MQYMLPRLRG WGQSLSRQMG GGKGGGLATR GPGETKIETD RRRIREKMAK MRREIADMKT GREIKRQERR RNKVPSVAIA GYTNAGKSSL LNRLTGAGVL VENALFATLD PTVRRAETPS GRLYTLADTV GFVRHLPHHL VEAFRSTMEE VGDSDLILHV VDGSHPAPEE QLAAVREVIR DVGATDVPEI VVINKADAAD PLVLQRLMRI EKRSIAVSAR TGMNMDQLLA LIDNELPRPS VEIEALVPYT HGRLVARAHS EGEVISEEHT PEGTLLKVRV HEELAADLAP YVPAPVAL // ID A0A0N0UMV6_9ACTN Unreviewed; 483 AA. AC A0A0N0UMV6; DT 09-DEC-2015, integrated into UniProtKB/TrEMBL. DT 09-DEC-2015, sequence version 1. DT 05-JUL-2017, entry version 12. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=ISGA_07075 {ECO:0000313|EMBL:KOY49924.1}; OS Gordonia sp. NB4-1Y. OC Bacteria; Actinobacteria; Corynebacteriales; Gordoniaceae; Gordonia. OX NCBI_TaxID=1241906 {ECO:0000313|EMBL:KOY49924.1, ECO:0000313|Proteomes:UP000011989}; RN [1] {ECO:0000313|EMBL:KOY49924.1, ECO:0000313|Proteomes:UP000011989} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NB4-1Y {ECO:0000313|EMBL:KOY49924.1, RC ECO:0000313|Proteomes:UP000011989}; RX PubMed=23744905; DOI=10.1099/mic.0.068932-0; RA Van Hamme J.D., Bottos E.M., Bilbey N.J., Brewer S.E.; RT "Genomic and proteomic characterization of Gordonia sp. NB4-1Y in RT relation to 6 : 2 fluorotelomer sulfonate biodegradation."; RL Microbiology 159:1618-1628(2013). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KOY49924.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; APHK02000030; KOY49924.1; -; Genomic_DNA. DR EnsemblBacteria; KOY49924; KOY49924; ISGA_07075. DR Proteomes; UP000011989; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000313|EMBL:KOY49924.1}; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000011989}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900, KW ECO:0000313|EMBL:KOY49924.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000011989}. FT DOMAIN 256 425 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 215 242 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 483 AA; 52130 MW; 6FB0834E9624E9EA CRC64; MDRDTALAGL HGLTTHRADD PTTGELQLSD RASLQRVAGL STELTDVTEV EYRQLRLERV VLVGVWTTGT SAQAHAAMTE LAALAETAGS QVLDAVIQRR QTPDPATYIG SGKAEELHDI VGSTGADTVI CDGELTPAQL TALEKVVKVK VIDRTALILD IFAQHATSRE GKAQVSLAQM EYMLPRLRGW GESMSRQAGG RAGSNGGVGL RGPGETKIET DRRRIRERMA KLRREIREMK TARLTKRAAR HRGSVPQLTV AGYTNAGKSS LVNAMTGSGV LVQDALFATL DPTTRRATLD DGREVVFTDT VGFVRHLPTQ LVEAFRSTLE EVVDADLLLH VVDGSDQFPL EQIAAVRQVI NEVVAEDDAT PPPELLVINK IDAVDALRMA ELRAAVPGAV FVSARTGEGL PELFERVRDH VRRSDVELTL AVPFTRGDVI SRIHREGEVL SAEHDADGSI LRVRVPEALA GELAGLAVEP AAT // ID A0A0N0VKF1_9PSED Unreviewed; 433 AA. AC A0A0N0VKF1; DT 09-DEC-2015, integrated into UniProtKB/TrEMBL. DT 09-DEC-2015, sequence version 1. DT 30-AUG-2017, entry version 12. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=PF66_01225 {ECO:0000313|EMBL:KPA92545.1}; OS Pseudomonas fuscovaginae. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=50340 {ECO:0000313|EMBL:KPA92545.1, ECO:0000313|Proteomes:UP000037931}; RN [1] {ECO:0000313|EMBL:KPA92545.1, ECO:0000313|Proteomes:UP000037931} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=IRRI 6609 {ECO:0000313|EMBL:KPA92545.1, RC ECO:0000313|Proteomes:UP000037931}; RX PubMed=26422147; RA Quibod I.L., Grande G., Oreiro E.G., Borja F.N., Dossa G.S., RA Mauleon R., Cruz C.V., Oliva R.; RT "Rice-Infecting Pseudomonas Genomes Are Highly Accessorized and Harbor RT Multiple Putative Virulence Mechanisms to Cause Sheath Brown Rot."; RL PLoS ONE 10:E0139256-E0139256(2015). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KPA92545.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JSYZ01000003; KPA92545.1; -; Genomic_DNA. DR RefSeq; WP_054059424.1; NZ_JTBY01000162.1. DR EnsemblBacteria; KPA92545; KPA92545; PF66_01225. DR PATRIC; fig|50340.43.peg.4109; -. DR Proteomes; UP000037931; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000037931}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000037931}. FT DOMAIN 199 366 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 433 AA; 48930 MW; 47B44FAD48522CA6 CRC64; MFFERHGGGE RTILVHLEGQ DPEAREDPQE FQELASSAGA ETVALFSVPR HRPTAKYLIG TGKVEELRDL VKAEQIDIVI FNHVLTPSQE RNLERAFECR VLDRTGLILD IFAQRARTHE GKLQVELAQL EHMSTRLVRG WTHLERQKGG IGLRGPGETQ LETDRRLLRV RLRQIKGRLE KVRSQREQSR RGRKRADIPT VSLVGYTNAG KSTLFNAVTA SEVYAADQLF ATLDPTLRRL DLDDLGPIVL ADTVGFIRHL PHNLVEAFRA TLEESSNSDL LLHVIDAAEP DRMLQIEQVM VVLGEIGAQD LPILEVYNKL DLLEGVEPQI QRGEDGKPQR VWLSARDGVG LELLEQAIAE LLGNDLFVGT LRLPQRFARL RAQFFELGAV QKEEHDEEGA CLLSIRLPMA EFNRVVSREG MKPPEFIEQH TLQ // ID A0A0N0XIA9_9NEIS Unreviewed; 367 AA. AC A0A0N0XIA9; DT 09-DEC-2015, integrated into UniProtKB/TrEMBL. DT 09-DEC-2015, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:KPC52671.1}; GN ORFNames=WG78_12525 {ECO:0000313|EMBL:KPC52671.1}; OS Amantichitinum ursilacus. OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Amantichitinum. OX NCBI_TaxID=857265 {ECO:0000313|EMBL:KPC52671.1, ECO:0000313|Proteomes:UP000037939}; RN [1] {ECO:0000313|EMBL:KPC52671.1, ECO:0000313|Proteomes:UP000037939} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=IGB-41 {ECO:0000313|EMBL:KPC52671.1, RC ECO:0000313|Proteomes:UP000037939}; RA Kirstahler P., Guenther M., Grumaz C., Rupp S., Zibek S., Sohn K.; RT "Draft genome sequence of the Amantichitinum ursilacus IGB-41, a new RT chitin-degrading bacterium."; RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KPC52671.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LAQT01000009; KPC52671.1; -; Genomic_DNA. DR RefSeq; WP_053938146.1; NZ_LAQT01000009.1. DR EnsemblBacteria; KPC52671; KPC52671; WG78_12525. DR PATRIC; fig|857265.3.peg.2582; -. DR Proteomes; UP000037939; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000037939}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000037939}. FT DOMAIN 198 364 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 164 191 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 367 AA; 41022 MW; DB83F4FC5DAD754C CRC64; MFDRHKGGDR AVLVCLDFGE PDYRDGQEEF VQLVTSAGVT PLAVVEGKRS RPDPAYFAGT GKVEEIAEAV RAQEAELVIF NHQLSPAQER NLERAMQCRV IDRTTLILDI FAQRARTAEG KLQVELAQLS HIATRLVRGW THLERQKGGI GLRGPGETQL ETDRRLLGIR VKRLKAQLET VQRQRATQRR ARERRNEFSV SIVGYTNAGK STLFNTLTKA RAYAADQLFA TLDTTSRKLF LDHEHSVVIS DTVGFIRALP HTLVAAFRAT LEETIQADLL LHVVDVNHPL REMQVAEVNK VLSEIGAERI PQLMVWNKID LKGLTPAVEP DEYGRIRAVR VSAAQGLGLD LLRGALVDSM SQPIEEQ // ID A0A0N0YKA2_9ACTN Unreviewed; 499 AA. AC A0A0N0YKA2; DT 09-DEC-2015, integrated into UniProtKB/TrEMBL. DT 09-DEC-2015, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=ADL27_46910 {ECO:0000313|EMBL:KPC83844.1}; OS Streptomyces sp. NRRL F-6602. OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae; OC Streptomyces. OX NCBI_TaxID=1609099 {ECO:0000313|EMBL:KPC83844.1, ECO:0000313|Proteomes:UP000037856}; RN [1] {ECO:0000313|EMBL:KPC83844.1, ECO:0000313|Proteomes:UP000037856} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NRRL F-6602 {ECO:0000313|EMBL:KPC83844.1, RC ECO:0000313|Proteomes:UP000037856}; RA Noorani M.; RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KPC83844.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LGKH01003780; KPC83844.1; -; Genomic_DNA. DR EnsemblBacteria; KPC83844; KPC83844; ADL27_46910. DR PATRIC; fig|1609099.3.peg.10531; -. DR Proteomes; UP000037856; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 2. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000313|EMBL:KPC83844.1}; KW Complete proteome {ECO:0000313|Proteomes:UP000037856}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900, KW ECO:0000313|EMBL:KPC83844.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000037856}. FT DOMAIN 275 440 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 499 AA; 54445 MW; 24EEE899944FDD00 CRC64; MTFSSSLPQN GQRIATNRRA DALMEEDVAL SHTLDEDRDG EQFDRSDRAA LRRVAGLSTE LEDVTEVEYR QLRLERVVLV GVWTSGTAQD AENSLAELAA LAETAGAMVL DGVIQRRDKP DAATYIGSGK ADELRDIVLE TGADTVVCDG ELTPGQLIHL EDVVKVKVVD RTALILDIFA QHAKSREGKA QVSLAQMQYM LPRLRGWGQS LSRQMGGGGS GSAGGGMATR GPGETKIETD RRRIREKMAK MRREIAEMKT GREVKRQDRR RNRVPSVAIA GYTNAGKSSL LNRLTGAGVL VENALFATLD PTVRKAETPS GRAYTLADTV GFVRHLPHHL VEAFRSTMEE VGDADLILHV VDGAHPAPEE QLAAVREVIR DVGAADVPEI VVVNKADAAD PLVLQRLLRA EKHALTVSAR TGQGIDELRE LIDNELPHPS VELEVLLPYT EGKLVSRVHS QGEVLSEEHT EHGTLLKARV HEELAAELRA FQPMAAARP // ID A0A0N0YSG5_9ACTN Unreviewed; 132 AA. AC A0A0N0YSG5; DT 09-DEC-2015, integrated into UniProtKB/TrEMBL. DT 09-DEC-2015, sequence version 1. DT 11-MAY-2016, entry version 4. DE SubName: Full=ATP-binding protein {ECO:0000313|EMBL:KPC88234.1}; DE Flags: Fragment; GN ORFNames=ADL27_41560 {ECO:0000313|EMBL:KPC88234.1}; OS Streptomyces sp. NRRL F-6602. OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae; OC Streptomyces. OX NCBI_TaxID=1609099 {ECO:0000313|EMBL:KPC88234.1, ECO:0000313|Proteomes:UP000037856}; RN [1] {ECO:0000313|EMBL:KPC88234.1, ECO:0000313|Proteomes:UP000037856} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NRRL F-6602 {ECO:0000313|EMBL:KPC88234.1, RC ECO:0000313|Proteomes:UP000037856}; RA Noorani M.; RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KPC88234.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LGKH01003127; KPC88234.1; -; Genomic_DNA. DR EnsemblBacteria; KPC88234; KPC88234; ADL27_41560. DR Proteomes; UP000037856; Unassembled WGS sequence. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF13167; GTP-bdg_N; 1. PE 4: Predicted; KW ATP-binding {ECO:0000313|EMBL:KPC88234.1}; KW Complete proteome {ECO:0000313|Proteomes:UP000037856}; KW Nucleotide-binding {ECO:0000313|EMBL:KPC88234.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000037856}. FT DOMAIN 44 131 GTP-bdg_N. {ECO:0000259|Pfam:PF13167}. FT NON_TER 1 1 {ECO:0000313|EMBL:KPC88234.1}. FT NON_TER 132 132 {ECO:0000313|EMBL:KPC88234.1}. SQ SEQUENCE 132 AA; 14246 MW; 131291E592B0A3F1 CRC64; ALRRVAGLST ELEDVTEVEY RQLRLERVVL VGVWTSGTAE DADRSLAELA ALAETAGALV LDGVVQRRDK PDPATYIGSG KAQELYDIVR DSGADTVVCD GELSPGQLIH LEDVVKVKVV DRTALILDIF AQ // ID A0A0N0ZDF3_9BURK Unreviewed; 404 AA. AC A0A0N0ZDF3; DT 09-DEC-2015, integrated into UniProtKB/TrEMBL. DT 09-DEC-2015, sequence version 1. DT 07-JUN-2017, entry version 10. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=ADM96_33115 {ECO:0000313|EMBL:KPD15427.1}; OS Burkholderia sp. ST111. OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Burkholderia. OX NCBI_TaxID=1682204 {ECO:0000313|EMBL:KPD15427.1, ECO:0000313|Proteomes:UP000037921}; RN [1] {ECO:0000313|EMBL:KPD15427.1, ECO:0000313|Proteomes:UP000037921} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ST111 {ECO:0000313|EMBL:KPD15427.1, RC ECO:0000313|Proteomes:UP000037921}; RA Thijs S., Bottos E.M., Van Hamme J.D., Gkorezis P., Rineau F., RA Vangronsveld J.; RT "Burkholderia sycomorum strain ST111, a rhizosphere-inhabiting RT bacterium with TNT-detoxification abilities and potential in RT rhizoremediation."; RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KPD15427.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LGIO01000050; KPD15427.1; -; Genomic_DNA. DR EnsemblBacteria; KPD15427; KPD15427; ADM96_33115. DR PATRIC; fig|1682204.3.peg.7579; -. DR Proteomes; UP000037921; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000037921}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000037921}. FT DOMAIN 205 376 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 171 198 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 404 AA; 44383 MW; 099E60CF1ECFE3AA CRC64; MAITPGRLIL IPSNLINAAL VGIDFGKIDF EASLEELSLL AQSAGANPLV TLTGRRSSPD AKMFVGSGKA EELRLACEAN DIELVIFNHA LAPAQQRNLE QALNRRVIDR TSLILDIFAQ RARSHEGKLQ VELAQLQYLS TRLIRAWTHL ERQKGGIGLR GPGETQLETD RRLIGERIKA LKTRLEKLRR QHGTQRRARS RNQTMSVSLV GYTNAGKSTL FNALTKAQAY AADQLFATLD TTSRRVYLGD EAGQVVVSDT VGFIRELPHQ LVAAFRATLE ETIHADLLLH VVDASSAVRL DQIDQVNEVL HAIGADTIRQ VLVFNKIDAV PELAARGDAV ERDEYGNISR VFLSARTGQG LDTLRAAIAE IATAEPLSET LVDLSEEDRS AAPREDRKVS ELGH // ID A0A0N1BG11_9SPHN Unreviewed; 435 AA. AC A0A0N1BG11; DT 09-DEC-2015, integrated into UniProtKB/TrEMBL. DT 09-DEC-2015, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=IP68_10370 {ECO:0000313|EMBL:KPF75022.1}; OS Blastomonas sp. AAP25. OC Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales; OC Sphingomonadaceae; Blastomonas. OX NCBI_TaxID=1523416 {ECO:0000313|EMBL:KPF75022.1, ECO:0000313|Proteomes:UP000037930}; RN [1] {ECO:0000313|EMBL:KPF75022.1, ECO:0000313|Proteomes:UP000037930} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=AAP25 {ECO:0000313|EMBL:KPF75022.1, RC ECO:0000313|Proteomes:UP000037930}; RA Zeng Y., Feng F., Liu Y., Koblizek M.; RT "Novel Diversity of Limnic Aerobic Anoxygenic Phototrophic Bacteria as RT Revealed by High-throughput Strain Identification and Genome RT Sequencing."; RL Submitted (AUG-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KPF75022.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LJHP01000011; KPF75022.1; -; Genomic_DNA. DR RefSeq; WP_054134911.1; NZ_LJHP01000011.1. DR EnsemblBacteria; KPF75022; KPF75022; IP68_10370. DR PATRIC; fig|1523416.3.peg.439; -. DR Proteomes; UP000037930; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000037930}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000037930}. FT DOMAIN 206 385 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 172 199 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 435 AA; 47907 MW; FC0DEF586957C0CA CRC64; MNDPHALDFV RGTRAVIAYP DLGRRGAVDS DARLEEARGL ALAIGISVCA SHAFRIRTAR PATLFGGGQV DIIAASLEDE KAELLIVDGS LSAIQQRNLE ERLKVKVIDR TGLILEIFGE RAATAEGRLQ VELAHLDYQA GRLVRSWTHL ERQRGGFGFL GGPGETQIEA DRRMIRDRMA KLRRELEQVK RTRGLHRERR QKAPWPVIAL VGYTNAGKST LFNRLTQAGV MAEDLLFATL DPTMRAIRLD GVEKVILSDT VGFVSDLPTE LVAAFRATLE EVLSADLVIH VRDMAHPDAQ MQAESVETIL TDLGLVIDPA LAEQGLATPL IEAWNKWDIL DEDACAFLTE TMPDDRTVCP ISALTGEGVS DLLRAASAAL VISHRIHDVN LPRHDGQRLA WLHAHGEVLT SDEKGDELAL SVRLSDKDWG RFQAL // ID A0A0N1BUU8_9PROT Unreviewed; 439 AA. AC A0A0N1BUU8; DT 09-DEC-2015, integrated into UniProtKB/TrEMBL. DT 09-DEC-2015, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=IP70_09305 {ECO:0000313|EMBL:KPF86454.1}; OS alpha proteobacterium AAP38. OC Bacteria; Proteobacteria; Alphaproteobacteria. OX NCBI_TaxID=1523418 {ECO:0000313|EMBL:KPF86454.1, ECO:0000313|Proteomes:UP000037884}; RN [1] {ECO:0000313|EMBL:KPF86454.1, ECO:0000313|Proteomes:UP000037884} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=AAP38 {ECO:0000313|EMBL:KPF86454.1, RC ECO:0000313|Proteomes:UP000037884}; RA Zeng Y., Feng F., Liu Y., Koblizek M.; RT "Novel Diversity of Limnic Aerobic Anoxygenic Phototrophic Bacteria as RT Revealed by High-throughput Strain Identification and Genome RT Sequencing."; RL Submitted (AUG-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KPF86454.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LJHR01000009; KPF86454.1; -; Genomic_DNA. DR RefSeq; WP_054167449.1; NZ_LJHR01000009.1. DR EnsemblBacteria; KPF86454; KPF86454; IP70_09305. DR PATRIC; fig|1523418.3.peg.5154; -. DR Proteomes; UP000037884; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000037884}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000037884}. FT DOMAIN 206 376 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 439 AA; 48763 MW; 16F86E78F0058922 CRC64; MSNHEGRGSS TRALVLHPVL PEDRNDARGP ESRLDEAVGL AAAIDLEVAY ARAIRVTRPR PATLLGTGAV EEVATLIKEA EIGLVIVDQS LTPIQQRNLE RDWKAKVIDR TGLILEIFGK RARTREGQLQ VELAALTYQR SRLVRSWTHL ERQRGGFGFL GGPGESQIEM DRRLISDRIV KLKGELEEVR RTRGLHRKAR EKVPYPVVAL VGYTNAGKST LFNRMAGADV FAKDLLFATL DPTMRSIMLP SNRKIILSDT VGFISDLPHG LVEAFRATLE EVMAADIILH VRDVSHPDTE AQKADVESVL KGLGIEVDTD ERVMEVLNKL DRLAEEDQQT LLRQARRNGG IAISALTGDG LDTLFDAIDR RMVAGREVVE FDIDVSDGAA IAWLYGKGEV LDRQDDETLA RLRVGLDPAD LARFLDRFPY RAREQALAS // ID A0A0N1CUY0_9MICO Unreviewed; 515 AA. AC A0A0N1CUY0; DT 09-DEC-2015, integrated into UniProtKB/TrEMBL. DT 09-DEC-2015, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=AEQ27_14175 {ECO:0000313|EMBL:KPG79290.1}; OS Frigoribacterium sp. RIT-PI-h. OC Bacteria; Actinobacteria; Micrococcales; Microbacteriaceae; OC Frigoribacterium. OX NCBI_TaxID=1690245 {ECO:0000313|EMBL:KPG79290.1, ECO:0000313|Proteomes:UP000037934}; RN [1] {ECO:0000313|EMBL:KPG79290.1, ECO:0000313|Proteomes:UP000037934} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=RIT-PI-h {ECO:0000313|EMBL:KPG79290.1, RC ECO:0000313|Proteomes:UP000037934}; RA Tran P.N., Lee Y.P., Gan H.M., Savka M.A.; RT "Whole genome sequencing of endophytes isolated from poison ivy RT (Toxicodendron radicans)."; RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KPG79290.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LHOZ01000092; KPG79290.1; -; Genomic_DNA. DR RefSeq; WP_054147245.1; NZ_LHOZ01000092.1. DR EnsemblBacteria; KPG79290; KPG79290; AEQ27_14175. DR PATRIC; fig|1690245.3.peg.575; -. DR Proteomes; UP000037934; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 2. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000037934}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}. FT DOMAIN 291 456 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 515 AA; 55904 MW; 8ECF7BA97EF96682 CRC64; MTDHTTTPFD SERNDQPDDV VARVLDRAAQ RASGYTVFSP AQAIQTRSLH DDGGSDGDQS ERDDRQALRR VAGLSTELQD VTEVEYRQLR LENVVLIGVY SQGSMSDAEN SLRELAALAE TAGAVVLDGL LQRRSNPDPS TYLGKGKAEE LRGTVAALGA DTVIADTELA PSQRRALEDV VKVKVIDRTA VILDIFSQHA KSREGKAQVE LAQLEYLLPR LRGWGESMSR QAGGQVGGAG AGMGSRGPGE TKIELDRRRI HTRMARLRKQ IKEMKPARDA KRANRDRNEV PTVAIAGYTN AGKSSLLNRL TSAGVLVENA LFATLDATVR KSVTADGRPF TYADTVGFVR NLPHQLVEAF RSTLEEVEAS DVIVHVVDGS HPDPAAQLAT VRDVIAEVDG RDIAEIVVFN KSDLVDDDQR LVLLGLEPTA VFVSARTGEG IDELLDRIAA VLPEPEIELD LLVPYDRGDV VSHLHDSGRI VSTDYEEEGT RVHARVYPSD VAGLTPYVAP VGVGR // ID A0A0N1ERQ4_9GAMM Unreviewed; 429 AA. AC A0A0N1ERQ4; DT 09-DEC-2015, integrated into UniProtKB/TrEMBL. DT 09-DEC-2015, sequence version 1. DT 30-AUG-2017, entry version 13. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=ADS77_02855 {ECO:0000313|EMBL:KPH65224.1}; OS Pseudoalteromonas porphyrae. OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales; OC Pseudoalteromonadaceae; Pseudoalteromonas. OX NCBI_TaxID=187330 {ECO:0000313|EMBL:KPH65224.1, ECO:0000313|Proteomes:UP000037848}; RN [1] {ECO:0000313|EMBL:KPH65224.1, ECO:0000313|Proteomes:UP000037848} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=UCD-SED14 {ECO:0000313|EMBL:KPH65224.1, RC ECO:0000313|Proteomes:UP000037848}; RA Coil D.A., Jospin G., Lee R.D., Eisen J.A.; RT "Draft Genome Sequence of Pseudoalteromonas porphyrae UCD-SED14."; RL Submitted (AUG-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KPH65224.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LHPH01000002; KPH65224.1; -; Genomic_DNA. DR RefSeq; WP_054452864.1; NZ_LHPH01000002.1. DR EnsemblBacteria; KPH65224; KPH65224; ADS77_02855. DR PATRIC; fig|187330.3.peg.610; -. DR Proteomes; UP000037848; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000037848}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000037848}. FT DOMAIN 198 365 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 429 AA; 48575 MW; 2BAE7615B7D216AF CRC64; MFDRYKAGEQ AVLVHIDFPK EGDREDLHEL EMLVSSAGVS SLAVVQGSRQ SPHPKLFVGT GKAEEIAEIV KIHNADVVIF NHQLRPSQER NLERVCQCRV LDRTTLILDI FAQRARTHEG KLQVELAQLR HMSTRLIRGW THLERQKGGI GLRGPGETQL ETDRRLLRVR IQSIRARLEK VAVQREQGRR ARNRNEIPTV SLVGYTNAGK STLFNRITNS NVYAADQLFA TLDPTLRKLE IDDVGSIILA DTVGFIRHLP HDLVAAFKAT LTETREADLQ LHVVDVADER RKENIEQVQS VLKEIEADEV PQLLVYNKID ALEDVSPRID RDDEGVPIRV WLSAHSGAGC ELLSEAISEL LAKKMFAKTL KLAPQYGRLR AALFNLNAVH EEAFDEQGQW LLTTRLPVVE WNKLKKEFGP EIDSFILLN // ID A0A0N1F006_9GAMM Unreviewed; 449 AA. AC A0A0N1F006; DT 09-DEC-2015, integrated into UniProtKB/TrEMBL. DT 09-DEC-2015, sequence version 1. DT 05-JUL-2017, entry version 12. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=ADS77_03885 {ECO:0000313|EMBL:KPH65036.1}; OS Pseudoalteromonas porphyrae. OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales; OC Pseudoalteromonadaceae; Pseudoalteromonas. OX NCBI_TaxID=187330 {ECO:0000313|EMBL:KPH65036.1, ECO:0000313|Proteomes:UP000037848}; RN [1] {ECO:0000313|EMBL:KPH65036.1, ECO:0000313|Proteomes:UP000037848} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=UCD-SED14 {ECO:0000313|EMBL:KPH65036.1, RC ECO:0000313|Proteomes:UP000037848}; RA Coil D.A., Jospin G., Lee R.D., Eisen J.A.; RT "Draft Genome Sequence of Pseudoalteromonas porphyrae UCD-SED14."; RL Submitted (AUG-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KPH65036.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LHPH01000003; KPH65036.1; -; Genomic_DNA. DR RefSeq; WP_054453115.1; NZ_LHPH01000003.1. DR EnsemblBacteria; KPH65036; KPH65036; ADS77_03885. DR PATRIC; fig|187330.3.peg.1823; -. DR Proteomes; UP000037848; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000037848}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000037848}. FT DOMAIN 229 394 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 190 217 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 449 AA; 49839 MW; 6225A0B722DA082B CRC64; MQLTAKPSLP NALLISISTP QFKGDEATES LAELARLVTT LGFKVVGTQS QKQSSTQKVN VLGSGKLAEI AHLTGNKGMV EDELADDLLD EVPLTEISSE IPSDELDFTC ADVVVFDCDL TPSQLRNVEN QLGVEVFDRT GIIIEIFSRH ARTKTAKLQV EIARLNYVAP RLRETSTGDK ERQMGKGAGE TTLELNRRKV RDQLAELKRE LVSVQDVMMD RRTQRSELFS VALIGYTNAG KSSMMRAITG SDVEGENKLF ATLDTTVRAL YPITQPRILV SDTVGFIKKL PHDLVASFHS TLAEAHDASL LLYVVDASDP SFRSQLDVVH KVLAEVGVEG SKKLLVLNKS DQLSIEQQQS LMDEFPDAMM TSTRNPDDIS KLHKYIIDIA QEDMIEEEVV IPYTAKGIVG EIRSSMSVVK EEYEYSHIKL TVRSSAIDLE RLKKRMLNL // ID A0A0N1GQG0_9ACTN Unreviewed; 497 AA. AC A0A0N1GQG0; DT 09-DEC-2015, integrated into UniProtKB/TrEMBL. DT 09-DEC-2015, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=OV320_8467 {ECO:0000313|EMBL:KPI25262.1}; OS Actinobacteria bacterium OV320. OC Bacteria; Actinobacteria. OX NCBI_TaxID=1592329 {ECO:0000313|EMBL:KPI25262.1, ECO:0000313|Proteomes:UP000037870}; RN [1] {ECO:0000313|EMBL:KPI25262.1, ECO:0000313|Proteomes:UP000037870} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=OV320 {ECO:0000313|EMBL:KPI25262.1, RC ECO:0000313|Proteomes:UP000037870}; RA Brown S.D., Utturkar S.M., Klingeman D.M., Pelletier D.; RT "Draft genome sequences for four actinobacteria strains OK006 OK074 RT OV450 and OV320."; RL Submitted (AUG-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KPI25262.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LJCX01000030; KPI25262.1; -; Genomic_DNA. DR RefSeq; WP_054243680.1; NZ_LJCX01000030.1. DR EnsemblBacteria; KPI25262; KPI25262; OV320_8467. DR PATRIC; fig|1592329.3.peg.7906; -. DR Proteomes; UP000037870; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 2. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000037870}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}. FT DOMAIN 275 440 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 497 AA; 54117 MW; F1A49D4A4D4970BF CRC64; MTSSSSPSQD TQRVTNAYPE GLRADALMEE DVAWSHEIDG DRDGDQFDRS ERAALRRVAG LSTELEDVTE VEYRQLRLER VVLVGVWTTG TAQDADNSLA ELAALAETAG ALVLDGVIQR RDKPDAATYI GSGKAQELRD IVLETGADTV ICDGELSPGQ LIHLEDVVKV KVIDRTALIL DIFAQHAKSR EGKAQVALAQ MQYMLPRLRG WGQSLSRQMG GGKGGGLATR GPGETKIETD RRRIREKMAK MRREIAEMKT GREIKRQERK RHKVPSVAIA GYTNAGKSSL LNRLTGAGVL VENSLFATLD PTVRRAETPS GRLYTLADTV GFVRHLPHHL VEAFRSTMEE VGESDLILHV VDGSHPNPEE QLAAVREVVR DVGATGVPEI VVINKADAAD PLTLQRLMRI EKRSIAVSAR TGQGIEELLA LIDNELPRPS VEVEALVPYT HGGLVARAHT EGEVISAEHT AEGTLLKVRV HEELAADLAP YVPAPLG // ID A0A0N1L4A7_9SPHN Unreviewed; 445 AA. AC A0A0N1L4A7; DT 09-DEC-2015, integrated into UniProtKB/TrEMBL. DT 09-DEC-2015, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=IP65_06345 {ECO:0000313|EMBL:KPF55671.1}; OS Novosphingobium sp. AAP1. OC Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales; OC Sphingomonadaceae; Novosphingobium. OX NCBI_TaxID=1523413 {ECO:0000313|EMBL:KPF55671.1, ECO:0000313|Proteomes:UP000037880}; RN [1] {ECO:0000313|EMBL:KPF55671.1, ECO:0000313|Proteomes:UP000037880} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=AAP1 {ECO:0000313|EMBL:KPF55671.1, RC ECO:0000313|Proteomes:UP000037880}; RA Zeng Y., Feng F., Liu Y., Koblizek M.; RT "Novel Diversity of Limnic Aerobic Anoxygenic Phototrophic Bacteria as RT Revealed by High-throughput Strain Identification and Genome RT Sequencing."; RL Submitted (AUG-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KPF55671.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LJHO01000002; KPF55671.1; -; Genomic_DNA. DR RefSeq; WP_028658439.1; NZ_LJHO01000002.1. DR EnsemblBacteria; KPF55671; KPF55671; IP65_06345. DR PATRIC; fig|1523413.3.peg.1983; -. DR Proteomes; UP000037880; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000037880}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000037880}. FT DOMAIN 216 392 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 175 209 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 445 AA; 48808 MW; A7BB670F33C6A77B CRC64; MSTFEFGRNA GDIEGEVTRG ARAIVVLPDI RQRGGLGEDA EARLEEGQGL ARAIGIEVVD AFIVPIRAVR PGTLFGEGQV ERLAVSATQN EAELVIIDGA LSAIQQRNLE DKLKRKVIDR TGLILEIFGE RAATAEGRLQ VELAHLDYQA GRLVRSWTHL ERQRGGFGFL GGPGETQIEA DRRMIRNRMA RLRRELEQVR RTRGLHRERR QRAPWPVIAL VGYTNAGKST LFNRLTGAAV MAEDLLFATL DPTMRAIRMP GVEKAILSDT VGFISDLPTQ LVAAFRATLE EVTAADVIVH VRDIANPAAA QQKAEVEEIL TDLGVIGEGG SEIPIIEAWN KWDLLAEDER AMREAMIAHG VPEQKVVPIS AMTGEGTDTL LSVLSDMLTG NAQVLELTVP VSDGQRLAWL HAHGEVLREE PNEDQTALRL SVRLSLADIG RFTTL // ID A0A0N4TPT8_BRUPA Unreviewed; 609 AA. AC A0A0N4TPT8; DT 09-DEC-2015, integrated into UniProtKB/TrEMBL. DT 08-JUN-2016, sequence version 2. DT 10-MAY-2017, entry version 9. DE SubName: Full=Uncharacterized protein {ECO:0000313|WBParaSite:BPAG_0001057801-mRNA-1}; OS Brugia pahangi (Filarial nematode worm). OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Spirurida; OC Filarioidea; Onchocercidae; Brugia. OX NCBI_TaxID=6280 {ECO:0000313|Proteomes:UP000038020, ECO:0000313|WBParaSite:BPAG_0001057801-mRNA-1}; RN [1] {ECO:0000313|Proteomes:UP000038020, ECO:0000313|WBParaSite:BPAG_0001057801-mRNA-1} RP NUCLEOTIDE SEQUENCE. RG Helminth Genomes Consortium; RL Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|WBParaSite:BPAG_0001057801-mRNA-1} RP IDENTIFICATION. RG WormBaseParasite; RL Submitted (APR-2016) to UniProtKB. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR WBParaSite; BPAG_0001057801-mRNA-1; BPAG_0001057801-mRNA-1; BPAG_0001057801. DR Proteomes; UP000038020; Genome Assembly. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR CDD; cd01878; HflX; 1. DR InterPro; IPR008584; DUF866_euk. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR Pfam; PF05907; DUF866; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000038020}; KW Reference proteome {ECO:0000313|Proteomes:UP000038020}. FT DOMAIN 251 414 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 609 AA; 69545 MW; CEDD81B2AD0E5CF2 CRC64; MTFSRNFAKI FVPLYSGRRF CTMIPEGAMQ MTDEFNIISK SYGIQSIAPG VQRILLIHPR LRRGRFFDLN PERAKLQLEE AVALVNTLPN FKVMETTAVS TDRSTKKKRL WGSGRIQRII ALKEKISATA LMIDVDILSP KQQAELTSIF RTPIYDRYNI VLLIFKIFAK TKEAKLQIQL AEIPYIRQRL LSMYELHVDP SLLHLDTSEK SKAERLEVLR YREQHLRKCL KAAVEEKVNL RIGEAQKNIR TVVAVVGYTN AGKSSLIKRL TGRNLYVEDR LFATLDTSLH VFRLPSGLPI LFADTIGFIS NLPTQLLASF QATLNHVANA DLLLHVEDVS NPDYLTQRNV VMKTLSALKI RNELLKSVIR VGNKIDKLCR LPPNESNTYF VSCADGRGFV ELLAAIDKRV LAISGVTIRR LKLRPHSEAF SYLCKYSFLV GQPIPSEDNN YLLCNPIIAL QLKANMVNVT SLQPMGDWSK FRWHLKEPAH WQYVVEEEKF NMPGSRGVAN ILGKCKLCSR VNSLEIIKDS FQPYTSSDDY SELIKFDCRG LEPTDFDPRS GWQAIGIESA TVFENIDLTE KEWVDYDEKA AQPTEINEIQ CRFVFCRKQ // ID A0A0N4U0J1_DRAME Unreviewed; 470 AA. AC A0A0N4U0J1; DT 09-DEC-2015, integrated into UniProtKB/TrEMBL. DT 09-DEC-2015, sequence version 1. DT 07-JUN-2017, entry version 7. DE SubName: Full=Uncharacterized protein {ECO:0000313|WBParaSite:DME_0000007401-mRNA-1}; OS Dracunculus medinensis (Guinea worm). OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Spirurida; OC Dracunculoidea; Dracunculidae; Dracunculus. OX NCBI_TaxID=318479 {ECO:0000313|Proteomes:UP000038040, ECO:0000313|WBParaSite:DME_0000007401-mRNA-1}; RN [1] {ECO:0000313|Proteomes:UP000038040, ECO:0000313|WBParaSite:DME_0000007401-mRNA-1} RP NUCLEOTIDE SEQUENCE. RG Helminth Genomes Consortium; RL Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|WBParaSite:DME_0000007401-mRNA-1} RP IDENTIFICATION. RG WormBaseParasite; RL Submitted (FEB-2017) to UniProtKB. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR WBParaSite; DME_0000007401-mRNA-1; DME_0000007401-mRNA-1; DME_0000007401. DR Proteomes; UP000038040; Genome Assembly. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR CDD; cd01878; HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000038040}; KW Reference proteome {ECO:0000313|Proteomes:UP000038040}. FT DOMAIN 228 391 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 470 AA; 53854 MW; 1C84A1B92F6DB6B4 CRC64; MARIVFRRFC TLKVDKICLQ QEFNIVKQCF GAQGFFGATH RVMVVHPKVR WGKHSTSLLT SPELQLNEAI SLVNTLPYLR VTSSSIVGAD YSTKKKNMWA KGRIEKLKEQ LRNDRVTAIM INVDVLSPEQ QRHFYSVFGI PIFDRFNVVL NIFKHYAKTK EAILQIKLAE IPYIRYFIFH QFHQTDNFYP SDHCEMLRLR EHSLRKKLKA IMEKNNNLTK GQENKKVATI AVVGYTNVGK SSFIKLLTGK ALFVEDRLFA TLDSSTHFCR LPSGTPIYLT DTIGFISNLP INLFASFQAT LSHVINADLL IHIEDVSHPG RFAQRESVLK TLSNLKIRQS LLDSMIIVGN KVDKVSSIID KESNMHYISC LTGAGIPELI STIDQNIISI KRKVLRHLKL RPGSNAWYYL YKNSFLFGKS VPSNDNNFLH CKTFMDDEEF RLFEIKFSLS KHTKNDSKSP LSSFGISNFV // ID A0A0N4VE66_ENTVE Unreviewed; 646 AA. AC A0A0N4VE66; DT 09-DEC-2015, integrated into UniProtKB/TrEMBL. DT 09-DEC-2015, sequence version 1. DT 12-APR-2017, entry version 5. DE SubName: Full=Uncharacterized protein {ECO:0000313|WBParaSite:EVEC_0000896601-mRNA-1}; OS Enterobius vermicularis (Human pinworm). OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Oxyurida; OC Oxyuroidea; Oxyuridae; Enterobius. OX NCBI_TaxID=51028 {ECO:0000313|Proteomes:UP000038041, ECO:0000313|WBParaSite:EVEC_0000896601-mRNA-1}; RN [1] {ECO:0000313|Proteomes:UP000038041, ECO:0000313|WBParaSite:EVEC_0000896601-mRNA-1} RP NUCLEOTIDE SEQUENCE. RG Helminth Genomes Consortium; RL Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|WBParaSite:EVEC_0000896601-mRNA-1} RP IDENTIFICATION. RG WormBaseParasite; RL Submitted (FEB-2017) to UniProtKB. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR WBParaSite; EVEC_0000896601-mRNA-1; EVEC_0000896601-mRNA-1; EVEC_0000896601. DR Proteomes; UP000038041; Genome Assembly. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR InterPro; IPR008584; DUF866_euk. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR Pfam; PF05907; DUF866; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 4: Predicted; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000038041}; KW Reference proteome {ECO:0000313|Proteomes:UP000038041}. FT DOMAIN 267 394 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 243 267 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 646 AA; 73315 MW; 12EE892EAA12F284 CRC64; MTLQLLNLGS NRIISVLYRR NNHITKLITG RYSTLSATGH FSLDTNNDDV KNNLSATEDE FGILSSFPTG HHVMVVHPKI RWGRHSAAAS TTPELQLEEA VALVKTIPKF TVSKLVIVYF NCFLPCLIMV FLQDCPSVIV GTDYNTNKKR IWGEGRVQKL VEAKELYRAT ALMINVDMLS PVQQVELLSV FGVPVFDRYN IALLIFKIFA RTKDAWLQIQ LASIPYLRKD KFDALRLYEH EIRKKIRASV EEKRSEIENR KNKLASTTIA VVGYTNVGKS SLIKRLTGKT IYVKDRLFAT LDAATYLSRL PSGSLVYFAD TIGFISNLPT YLFASFEATL SHVTTADLVL FVEDMSHPDR IAQKETVLET LRRLNIRPEV MDSIIFVGNK VDKLLSLPHD PSIIYISCLS GFGFSQLVAD IDKVGRVKRL LKLKPGSDVL KYLFAGSFLT ADPIPTPDGN HLLCTFSMND SEFANYSISA MPFIALELKA DLENIDELQP KPDWTDFHWH LKIKCTNCGE EKDHWHYVAA NVRETVDMGR AGKVNFVEKC KLCGRQNTLA IIQDSFKPYM IERNGEFQPV LKFDCRGIEP TDFDPRVGVW WARCTDSEAV FDDIDLSEKE WADYDEKAQC AVEIKELFSR FVLSKK // ID A0A0N4X841_HAEPC Unreviewed; 319 AA. AC A0A0N4X841; DT 09-DEC-2015, integrated into UniProtKB/TrEMBL. DT 09-DEC-2015, sequence version 1. DT 10-MAY-2017, entry version 6. DE SubName: Full=Uncharacterized protein {ECO:0000313|WBParaSite:HPLM_0002053301-mRNA-1}; OS Haemonchus placei (Barber's pole worm). OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida; OC Strongylida; Trichostrongyloidea; Haemonchidae; Haemonchinae; OC Haemonchus. OX NCBI_TaxID=6290 {ECO:0000313|Proteomes:UP000038042, ECO:0000313|WBParaSite:HPLM_0002053301-mRNA-1}; RN [1] {ECO:0000313|Proteomes:UP000038042, ECO:0000313|WBParaSite:HPLM_0002053301-mRNA-1} RP NUCLEOTIDE SEQUENCE. RG Helminth Genomes Consortium; RL Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|WBParaSite:HPLM_0002053301-mRNA-1} RP IDENTIFICATION. RG WormBaseParasite; RL Submitted (FEB-2017) to UniProtKB. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR WBParaSite; HPLM_0002053301-mRNA-1; HPLM_0002053301-mRNA-1; HPLM_0002053301. DR Proteomes; UP000038042; Genome Assembly. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR CDD; cd01878; HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000038042}; KW Reference proteome {ECO:0000313|Proteomes:UP000038042}. FT DOMAIN 152 316 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 319 AA; 35759 MW; A517DB64D70218CF CRC64; MGVDYNTKRK GVWGTGQLEV LVNMKAKSRV TALMVNVDML SPVQQRELYN IFHVPIYDRY NIVLSIFKHY AKTPEAHLQI QLAEIPYIRN RLHYVNKYHS DPGMLHIERQ PERASVDEFE VLRLREQSLR KKLQAVMDKN TGKAMEETRD AAMVAVVGYT NSGKTSLVKC LTGAASLDPK DRLFATLDTT RHLARLPSGR KVVFTDTIGF LSDLPIHLLA AFQATLSHVV LADVIIHIRD ISNPDWPAQS EDVDNTLKEI GLPPNRLNDV IMVDNKIDVN GAPRTSAPSA LRISCKTSEG VENLIAKVDE VSEFGTIFS // ID A0A0N4ZYJ5_PARTI Unreviewed; 465 AA. AC A0A0N4ZYJ5; DT 09-DEC-2015, integrated into UniProtKB/TrEMBL. DT 09-DEC-2015, sequence version 1. DT 12-APR-2017, entry version 5. DE SubName: Full=Uncharacterized protein {ECO:0000313|WBParaSite:PTRK_0001386200.1}; OS Parastrongyloides trichosuri (Possum-specific nematode worm). OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida; OC Panagrolaimoidea; Strongyloididae; Parastrongyloides. OX NCBI_TaxID=131310 {ECO:0000313|Proteomes:UP000038045, ECO:0000313|WBParaSite:PTRK_0001386200.1}; RN [1] {ECO:0000313|Proteomes:UP000038045, ECO:0000313|WBParaSite:PTRK_0001386200.1} RP NUCLEOTIDE SEQUENCE. RG Helminth Genomes Consortium; RL Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|WBParaSite:PTRK_0001386200.1} RP IDENTIFICATION. RG WormBaseParasite; RL Submitted (FEB-2017) to UniProtKB. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR WBParaSite; PTRK_0001386200.1; PTRK_0001386200.1; PTRK_0001386200. DR Proteomes; UP000038045; Genome Assembly. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000038045}; KW Reference proteome {ECO:0000313|Proteomes:UP000038045}. FT DOMAIN 230 402 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 465 AA; 52788 MW; 1CD6C6A823E3330C CRC64; MHDDTIDIGF NLSTSLSTQH SFLVVHPKIR WGQNVSPPDE RNDELQLEEA ISLVKTIPGF SVSQSVIVGT DYTTKKKQIW GQGRIDSLIK IKAALRVSAI MVNVEMLTPL QQTTLFEIFQ VPIYDRYNIV LAIFKHFAKT KLAHYQIQLA ELPYIKHRLH YLESNKVNGD ILHVGDVTRA LSKTGLDRKE LLRLREQVLR KRIKDSIEST KHGIEEQRIR YEKKNVNTPL TVAVVGYTNV GKTNLIKTLT GSSQLQPENK LFATLDTTIH PLVLPSKSNI FIADTIGFIS SLPVGLFESF SATLMHATSA NLLIHVFDLS HPDVFAQKKN VMKTLIEMKF PSKLIENMIH VGNKIDIISE EKKDELYKSG ILSENDLVIS SKTGYGVNEL ILKIDKCVMK INNSHIRRFK LKPESKIVSY LYENGLVTSE PVVSECGKYL IYDTCLNENQ FNKLKKRMGS IKKKQ // ID A0A0N5AXZ0_9BILA Unreviewed; 650 AA. AC A0A0N5AXZ0; DT 09-DEC-2015, integrated into UniProtKB/TrEMBL. DT 08-JUN-2016, sequence version 2. DT 12-APR-2017, entry version 8. DE SubName: Full=Uncharacterized protein {ECO:0000313|WBParaSite:SMUV_0000982501-mRNA-1}; OS Syphacia muris. OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Oxyurida; OC Oxyuroidea; Oxyuridae; Syphacia. OX NCBI_TaxID=451379 {ECO:0000313|Proteomes:UP000046393, ECO:0000313|WBParaSite:SMUV_0000982501-mRNA-1}; RN [1] {ECO:0000313|Proteomes:UP000046393, ECO:0000313|WBParaSite:SMUV_0000982501-mRNA-1} RP NUCLEOTIDE SEQUENCE. RG Helminth Genomes Consortium; RL Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|WBParaSite:SMUV_0000982501-mRNA-1} RP IDENTIFICATION. RG WormBaseParasite; RL Submitted (APR-2016) to UniProtKB. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR WBParaSite; SMUV_0000982501-mRNA-1; SMUV_0000982501-mRNA-1; SMUV_0000982501. DR Proteomes; UP000046393; Genome Assembly. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR CDD; cd01878; HflX; 1. DR InterPro; IPR008584; DUF866_euk. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR Pfam; PF05907; DUF866; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000046393}; KW Reference proteome {ECO:0000313|Proteomes:UP000046393}. FT DOMAIN 266 429 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 650 AA; 74039 MW; 939ADE75032624EE CRC64; MNTFNWVVIT LLRCVIVNLP AALFLQNVSD NLIRQFSKAI LLKLQKALSV NDVLGGKTVT DGNSDCISSN FIDDNDTQNG RISIKDNFKN GHRLLVVHPK IRWGKHSASA LTTTEHQVEE AVALVKTIPN FSVANTVVVG TDYSTISKRI WGTGRIERLV EEKEKCRATA VMINVAILSP MQQVEMSRTF RTPVFDRYNI TLLIFKLYAR TKDAWLQIEL ASIPYLRCNK SEFLRIYEHT IQKKITASVE EKRDTILSLK QKRAALSVAV VGYTNAGKSS LIKRLTGRDL YVEDRLFATL DTSEFFCRLP SGHPIYLADT IGFISDLPTY LFASFRATLS CVEVADLLIV VEDMSDPNFL AQRETVLKTL LDLHVKDEVI SNIIFVGNKI DKLSCLPKDV NNTIFVSCVD GTGFSELISQ IDKLGGLVKR ILKIRPDSEA FDYLLKGSFL IDKPVPSPDG NYIMCTFNMN EADFAKFSSR FNIKKRKRKP IIALEVKAEL ERLDELQPKP DWRTFRWYLK CRCSNCGEEP KIWHFVIPNE TITFGKSDVN FLEKCKICGR INSLVVLMDS FEPYTAKMEG EFQAIIKFDC RGLEPTDFDP RGQWWARCTE SGAIFSNIDL TEREWADYDE KVQCCVEVKE FTTRFVQVKK // ID A0A0N5BRY9_STREA Unreviewed; 494 AA. AC A0A0N5BRY9; DT 09-DEC-2015, integrated into UniProtKB/TrEMBL. DT 09-DEC-2015, sequence version 1. DT 12-APR-2017, entry version 6. DE SubName: Full=Uncharacterized protein {ECO:0000313|WBParaSite:SPAL_0000863400.1}; OS Strongyloides papillosus (Intestinal threadworm). OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida; OC Panagrolaimoidea; Strongyloididae; Strongyloides. OX NCBI_TaxID=174720 {ECO:0000313|Proteomes:UP000046392, ECO:0000313|WBParaSite:SPAL_0000863400.1}; RN [1] {ECO:0000313|Proteomes:UP000046392, ECO:0000313|WBParaSite:SPAL_0000863400.1} RP NUCLEOTIDE SEQUENCE. RG Helminth Genomes Consortium; RL Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|WBParaSite:SPAL_0000863400.1} RP IDENTIFICATION. RG WormBaseParasite; RL Submitted (FEB-2017) to UniProtKB. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR WBParaSite; SPAL_0000863400.1; SPAL_0000863400.1; SPAL_0000863400. DR Proteomes; UP000046392; Genome Assembly. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000046392}; KW Reference proteome {ECO:0000313|Proteomes:UP000046392}. FT DOMAIN 260 432 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 494 AA; 56068 MW; D94B79352F36B95F CRC64; MLKFVSLLPS KTFRRSLLYC RYFCSNNGEE GDSLLADVDL NMPSVPYVQH SFMVIHPKIR WGRNATPPKE KNDELQVEEA IALVKTVPGF SISQSVIVGT DYTTKKKHIW GQGRVEDLLK LKVSSRVSAL MINVDQITPL QQTELYNIFR VPIYDRYNIV LRIFKLYAKT KLAHYQIQLA EIPYIKNRLH YLDNSDSNSD VLQITDAVNA LAKSGLDRKE ALRLREHALR KRIKSSIEST KNEIAEKKLR QDKKNAGNSL VVAIVGYTNV GKTTFIKRIT GAPQLNPEDK LFATLDTTIH PFLLPSRNSV FIADTIGFMA SLPVGLFESF SATLMHATSA DLLVHLIDLS HPDVFAQKKN VLKTLIDLKF PQKLIDTMIC VGNKLDKISD DDKYKLIESG VLDKNDSVIS STSGYGIDDL ILKIDKTIMN INNSRIRRFK LKPESKLISY FYENNLVTTE PVVSECGKYL IFDICLNDGQ LNKLKKKMNF MVKQ // ID A0A0N5CZY3_THECL Unreviewed; 658 AA. AC A0A0N5CZY3; DT 09-DEC-2015, integrated into UniProtKB/TrEMBL. DT 09-DEC-2015, sequence version 1. DT 10-MAY-2017, entry version 7. DE SubName: Full=Uncharacterized protein {ECO:0000313|WBParaSite:TCLT_0000607801-mRNA-1}; OS Thelazia callipaeda (Oriental eyeworm) (Parasitic nematode). OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Spirurida; OC Thelazioidea; Thelaziidae; Thelazia. OX NCBI_TaxID=103827 {ECO:0000313|Proteomes:UP000046394, ECO:0000313|WBParaSite:TCLT_0000607801-mRNA-1}; RN [1] {ECO:0000313|Proteomes:UP000046394, ECO:0000313|WBParaSite:TCLT_0000607801-mRNA-1} RP NUCLEOTIDE SEQUENCE. RG Helminth Genomes Consortium; RL Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|WBParaSite:TCLT_0000607801-mRNA-1} RP IDENTIFICATION. RG WormBaseParasite; RL Submitted (FEB-2017) to UniProtKB. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR WBParaSite; TCLT_0000607801-mRNA-1; TCLT_0000607801-mRNA-1; TCLT_0000607801. DR Proteomes; UP000046394; Genome Assembly. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR CDD; cd01878; HflX; 1. DR InterPro; IPR008584; DUF866_euk. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR Pfam; PF05907; DUF866; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000046394}; KW Reference proteome {ECO:0000313|Proteomes:UP000046394}. FT DOMAIN 225 388 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 658 AA; 76221 MW; 2AA67D2D73ED1213 CRC64; MQSVRNLCIK QSEEVVKMND EFNIISKSYG VRDVLPGCHR VLLIHPRLRR GRFFDLNPTK IKLQLEEATA LVNTLPNFRV IQTVCVNTDR STEKKRLWGE GRIERVISLK EEIAATALMI DVKILSPRQQ VELSEIFRVP VYDRYNIVLL IFKMFAKTKE AKLQIQLAEI PYISLSVNVA LKCIFREEKL EILRYREHHL RKCLKAAVEE KVNLRIGEAR KNIRTVVAVV GYTNAGKSSL IKRLTGRDLY VEDRLFATLD TSLHLYRLPS GLPILFADTI GFISNLPSEL LASFQATLNH VSNADLLLHV EDVSNPDYLA QRDVVLKTLL ALRIRNDLIE SMIRVGNKID KLDQLPADES NTYFVSCTDG RGLVELLTAV DKRVLQMRGA VIRRLKLRPH SKAIPYLYKY SFIVGQPTPS EDNNYLLCNL QESETHFRDI MPLIALQLKA NMVNLTELQP AGDWTKFRWH LKIYKFYPIS VMMMERTKIP RNLVEIFNKL KSNVTFGTFI FISYIYSLQF KCTNCGEESK NWKYITEKYL YFEIFKDRYE VSGNRGTANL FEKCKLCARM NSVEIVKDSL QPYTDIGNFE TLVKFDCRGL EPIAFEPRVR WKAVSTKSSL VFEDVDLIDK EWVDYDEKAA EPVEISEMDC RFVLCRKE // ID A0A0N5E0D9_TRIMR Unreviewed; 516 AA. AC A0A0N5E0D9; DT 09-DEC-2015, integrated into UniProtKB/TrEMBL. DT 09-DEC-2015, sequence version 1. DT 07-JUN-2017, entry version 8. DE SubName: Full=Uncharacterized protein {ECO:0000313|WBParaSite:TMUE_s0126000800}; OS Trichuris muris (Mouse whipworm). OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia; OC Trichocephalida; Trichuridae; Trichuris. OX NCBI_TaxID=70415 {ECO:0000313|Proteomes:UP000046395, ECO:0000313|WBParaSite:TMUE_s0126000800}; RN [1] {ECO:0000313|Proteomes:UP000046395} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Edinburgh {ECO:0000313|Proteomes:UP000046395}; RA Hoang H.T., Killian M.L., Madson D.M., Arruda P.H.E., Sun D., RA Schwartz K.J., Yoon K.; RL Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Proteomes:UP000046395} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Edinburgh {ECO:0000313|Proteomes:UP000046395}; RA Foth B.J., Tsai I.J., Reid A.J., Bancroft A.J., Nichol S., Tracey A., RA Holroyd N., Cotton J.A., Stanley E.J., Zarowiecki M., Liu J.Z., RA Huckvale T., Cooper P.J., Grencis R.K., Berriman M.; RT "The whipworm genome and dual-species transcriptomics of an intimate RT host-pathogen interaction."; RL Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases. RN [3] {ECO:0000313|WBParaSite:TMUE_s0126000800} RP NUCLEOTIDE SEQUENCE. RC STRAIN=Edinburgh {ECO:0000313|WBParaSite:TMUE_s0126000800}; RG Helminth Genomes Consortium; RL Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases. RN [4] {ECO:0000313|WBParaSite:TMUE_s0126000800} RP IDENTIFICATION. RG WormBaseParasite; RL Submitted (FEB-2017) to UniProtKB. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR WBParaSite; TMUE_s0126000800; TMUE_s0126000800; TMUE_s0126000800. DR Proteomes; UP000046395; Unassembled WGS sequence. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR CDD; cd01878; HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000046395}; KW Reference proteome {ECO:0000313|Proteomes:UP000046395}. FT DOMAIN 282 448 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 516 AA; 57864 MW; 87BDF09A539F0053 CRC64; MHPVWMYSAR ISMYTIWLTV KNAGHTIETI SRSLLLAGRP FSRNSSEGIG MTATDDDEDT LSTRKDLRTL QSCLDLPQLD ISHRLFVIQP KLPTPELRRL ATTNEHLELE AVQLVKSVPG WGVYGVHDSF VKVSPRAKLP FGSGTLEVLK AAIRKSSDCT GIFLNMDRLS PLQHKTLYSV FGIPVFDRFT VALQIFKLYA NSKEAKIQAA LAELKYLKVH VKSYTAGIVQ KQFPKSLMPV QVDWKKTEEV ISRREVKLKE KLKAVAAQRT LLRQNAQRRR FPLVAVVGYT NCGKTSLIRC LSENANLSGE DRFFATLDVT THVGKLPCRL PVLYADTVGF FSDLPMDLMP SFNSTLEEIT YADLVLHVID RSNPNWRFQR QSVARTLDNL AAACGARISP VEVWNKSDKF EMESDEERPK SMIVISCLTR DGMSKLLALI EDRILTTTAY KRFLLRIPIT GGYLSLLYSI GSVVATETLP TGDQMCVSLV TQQHKVDKLL KTHPDAIQVM SGPSTA // ID A0A0N7A183_9MICO Unreviewed; 512 AA. AC A0A0N7A183; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 07-JUN-2017, entry version 16. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=NI26_05410 {ECO:0000313|EMBL:AIV41389.1}; OS Curtobacterium sp. MR_MD2014. OC Bacteria; Actinobacteria; Micrococcales; Microbacteriaceae; OC Curtobacterium. OX NCBI_TaxID=1561023 {ECO:0000313|EMBL:AIV41389.1, ECO:0000313|Proteomes:UP000069933}; RN [1] {ECO:0000313|Proteomes:UP000069933} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MR_MD2014 {ECO:0000313|Proteomes:UP000069933}; RA Mariita R.M., Bhatgnagar S., Hanselmann K., Hossain M.J., Dawson S.C., RA Korlach J., Boitano M., Liles M.R., Moss A.G., Leadbetter J.R., RA Newman D.K.; RT "Isolation and characterization of species affiliated with family RT Actinomycetaceae."; RL Submitted (OCT-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP009755; AIV41389.1; -; Genomic_DNA. DR RefSeq; WP_066657961.1; NZ_CP009755.1. DR EnsemblBacteria; AIV41389; AIV41389; NI26_05410. DR KEGG; cum:NI26_05410; -. DR PATRIC; fig|1561023.3.peg.1127; -. DR KO; K03665; -. DR Proteomes; UP000069933; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 2. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000069933}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000069933}. FT DOMAIN 288 453 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 512 AA; 55596 MW; E9F4D2D5E36A3584 CRC64; MTETTMNDGR SDDSAEGVVE RVLRNAETRA TSAIFAPAQA IQTRSVDEHG WSGDGDQYER EDRAALRRVT GLSTELEDVT EVEYRQLRLE RVVLIGVYPQ GDAQDAENSL RELAALAETA GAVVLDGLLQ RRPNPDPATY LGKGKAEELA MVVKATGADT VVADTELAPS QRRALEDVVK VKVIDRTAVI LDIFSQHATT REGKAQVELA QLQYLLPRLR GWGESMSRQA GGQVSGGAGM GSRGPGETKI ELDRRRINTR MSKLRRQIAG FRPAREAKRA DRHRNEVPSV AIAGYTNAGK SSLLNRLTSA GVLVQNQLFA TLDATVRRTE SSAGREFTFV DTVGFVRNLP HQLVEAFRST LEEVGEADVI VHVVDGSHPD PAAQLATVRD VMGDVGARDI PEVVAFNKAD LIDEAQRLVL VGLVPDAVFV SARTGEGVPE LLAAIEARLP EPDVELTVVI PYDRGDLVSS LHDAGAVETT DYVEDGTRLR VRVFQRQVAE LDPYVVTPVA TA // ID A0A0N7FUK6_9ACTN Unreviewed; 466 AA. AC A0A0N7FUK6; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 07-JUN-2017, entry version 12. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=ACH46_09105 {ECO:0000313|EMBL:ALG84623.1}; OS Gordonia sp. QH-11. OC Bacteria; Actinobacteria; Corynebacteriales; Gordoniaceae; Gordonia. OX NCBI_TaxID=1136941 {ECO:0000313|EMBL:ALG84623.1, ECO:0000313|Proteomes:UP000063789}; RN [1] {ECO:0000313|EMBL:ALG84623.1, ECO:0000313|Proteomes:UP000063789} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=QH-11 {ECO:0000313|EMBL:ALG84623.1, RC ECO:0000313|Proteomes:UP000063789}; RA Jin D., Kong X., Bai Z.; RT "Complete genome sequence and metabolic analysis of phthalate RT degradation pathway in Gordonia sp. QH-11."; RL Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP011853; ALG84623.1; -; Genomic_DNA. DR RefSeq; WP_062392619.1; NZ_CP011853.1. DR EnsemblBacteria; ALG84623; ALG84623; ACH46_09105. DR KEGG; goq:ACH46_09105; -. DR PATRIC; fig|1136941.3.peg.1857; -. DR KO; K03665; -. DR Proteomes; UP000063789; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 2. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000313|EMBL:ALG84623.1}; KW Complete proteome {ECO:0000313|Proteomes:UP000063789}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900, KW ECO:0000313|EMBL:ALG84623.1}. FT DOMAIN 244 413 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 466 AA; 50259 MW; B976FFE7CFE25D1E CRC64; MTELTNETPT TGELQLDERA SLQRVVGLST ELQDITEVEQ RQLRLEQVVL VGVWLSGSAA AAEASMAELA ALAETAGSTV LDALIQRRSK PDPATYIGSG KADELRQVVV ATGADTVICD GELTPAQLTA LEKVVKVKVV DRTALILDIF AQHATSREGK AQVALAQMEY MMPRLRGWGE SMSRQAGGRA GSNGGVGLRG PGETKIETDR RRIRERMAKI RKEIRGMKTA RTVKRAARRR GGVPGLTVVG YTNAGKSSLV NAMTGAGVLV QDALFATLDP TTRRAELADG HEVVFTDTVG FVRHLPTQLV EAFRSTLEEA MEADLLVHVV DGADPFPGNQ ISAVRQVLSD VLAEEKLPAP PEMLVINKID AVDGITMAAL RAEYPDAQFV SARTGEGLDD LFRAITEFLQ RDDVDAVLQI PFARGEVIAR LHQQAHVLDT DHNAEGTRVH VRMPSALAAE LSDLVV // ID A0A0N7HBV5_9ARCH Unreviewed; 363 AA. AC A0A0N7HBV5; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 07-JUN-2017, entry version 9. DE SubName: Full=GTPase HflX {ECO:0000313|EMBL:ALI36184.1}; GN Name=hflX_2 {ECO:0000313|EMBL:ALI36184.1}; GN ORFNames=NMY3_01982 {ECO:0000313|EMBL:ALI36184.1}; OS Candidatus Nitrocosmicus oleophilus. OC Archaea; Thaumarchaeota; Nitrososphaeria; Nitrososphaerales; OC Nitrososphaeraceae; Candidatus Nitrosocosmicus. OX NCBI_TaxID=1353260 {ECO:0000313|EMBL:ALI36184.1, ECO:0000313|Proteomes:UP000058925}; RN [1] {ECO:0000313|EMBL:ALI36184.1, ECO:0000313|Proteomes:UP000058925} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MY3 {ECO:0000313|EMBL:ALI36184.1, RC ECO:0000313|Proteomes:UP000058925}; RA Jung M.-Y., Rhee S.-K.; RT "Niche specialization of a soil ammonia-oxidizing archaeon, Candidatus RT Nitrosocosmicus oleophilus."; RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP012850; ALI36184.1; -; Genomic_DNA. DR EnsemblBacteria; ALI36184; ALI36184; NMY3_01982. DR KEGG; taa:NMY3_01982; -. DR KO; K03665; -. DR Proteomes; UP000058925; Chromosome. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000058925}; KW Reference proteome {ECO:0000313|Proteomes:UP000058925}. FT DOMAIN 188 360 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 363 AA; 41156 MW; E36E2E567A579A8F CRC64; MYSEGRKAIL ITYPNQFALS EARGLAESVG YSILEVISQK NITRSRFGVG KGKAEEIKER VAALKPDVII YDEILKPSQQ YNLARLCKIE IVDREKLILE IFLNRAVTNE SKIQVKLAQL KYDIVRVKEK ARLAKLGEQP GFYGLGKYDA DVHILDIKRR TTLLKKKLQA EERKRALHRI QRLSSSIPLI SLTGYTSAGK TSLFNILTNE NKETSTKLFT TLTTFTRSSQ IEGRKVLVSD TIGFISKLPP YMIEAFKSTL SELNYANVIL LIIDFTDDVP IIKKKLMSSL EILSKLQIPF QKCILVLNKI DMVKNNEIMN KMNELNVTEN IDHIIPISAH LGYNLPRLKK LISMQVADLP STS // ID A0A0N7I437_9MICO Unreviewed; 506 AA. AC A0A0N7I437; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 07-JUN-2017, entry version 12. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=AOA12_14435 {ECO:0000313|EMBL:ALJ21031.1}; OS Microbacterium sp. No. 7. OC Bacteria; Actinobacteria; Micrococcales; Microbacteriaceae; OC Microbacterium. OX NCBI_TaxID=1714373 {ECO:0000313|EMBL:ALJ21031.1, ECO:0000313|Proteomes:UP000059097}; RN [1] {ECO:0000313|EMBL:ALJ21031.1, ECO:0000313|Proteomes:UP000059097} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=No. 7 {ECO:0000313|EMBL:ALJ21031.1, RC ECO:0000313|Proteomes:UP000059097}; RA Ohtsubo Y., Nagata Y., Numata M., Tsuchikane K., Hosoyama A., RA Yamazoe A., Tsuda M., Fujita N., Kawai F.; RT "Complete genome sequence of a polypropylene glycol-degrading strain RT Microbacterium sp. No. 7."; RL Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP012697; ALJ21031.1; -; Genomic_DNA. DR RefSeq; WP_054683993.1; NZ_CP012697.1. DR EnsemblBacteria; ALJ21031; ALJ21031; AOA12_14435. DR KEGG; mio:AOA12_14435; -. DR PATRIC; fig|1714373.3.peg.2965; -. DR KO; K03665; -. DR Proteomes; UP000059097; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000059097}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000059097}. FT DOMAIN 287 452 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 506 AA; 54822 MW; E9DABFD801D82BDE CRC64; MTDTTPDTAT DTTEIDPVDR VLSRAETRAG MRVFGAAQAL QDESTVAYDD TDGDQWDREE RAALRRVPGL STELDDVTEV EYRQLRLENV VLAGVYPQGS QEDAENSLRE LAALAETAGA VVLDGVLQRR PHPDPATYIG RGKAQELADM VAALGADTVI ADTELAPSQR RALEDVVKVK VIDRTTVILD IFSQHAKSRE GKAQVELAQL EYLLPRLRGW GDSMSRQAGG QVGAGGAGMG SRGPGETKIE LDRRRIRTRM AQLRRQLRDF APAREAKRAE RKRNTIPAVA IAGYTNAGKS SLLNRLTRAG VLVENALFAT LDTSVRRTET SDGRVYTLTD TVGFVRNLPH QLVEAFRSTL EEVGEADVIV HVVDGSHPDP AAQLATVRDV IGDVGARDVP EIVVFNKADL LDDDARLVLR GLAPHALFVS SRTGEGVDEL RETIERTLPL PAVEVRAVVP YDRGELVSAV HEHGIILSQE HGADGTALHA HVPAVLAGRL APFVVG // ID A0A0N7JE76_9SPHI Unreviewed; 396 AA. AC A0A0N7JE76; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 07-JUN-2017, entry version 13. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=AQ505_01130 {ECO:0000313|EMBL:ALL04218.1}; OS Pedobacter sp. PACM 27299. OC Bacteria; Bacteroidetes; Sphingobacteriia; Sphingobacteriales; OC Sphingobacteriaceae; Pedobacter. OX NCBI_TaxID=1727164 {ECO:0000313|EMBL:ALL04218.1, ECO:0000313|Proteomes:UP000062859}; RN [1] {ECO:0000313|EMBL:ALL04218.1, ECO:0000313|Proteomes:UP000062859} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=PAMC 27299 {ECO:0000313|EMBL:ALL04218.1, RC ECO:0000313|Proteomes:UP000062859}; RA Millard Andrew; RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP012996; ALL04218.1; -; Genomic_DNA. DR RefSeq; WP_062546481.1; NZ_CP012996.1. DR EnsemblBacteria; ALL04218; ALL04218; AQ505_01130. DR KEGG; pep:AQ505_01130; -. DR KO; K03665; -. DR Proteomes; UP000062859; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000062859}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000062859}. FT DOMAIN 204 385 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 396 AA; 45371 MW; 9C120EFCE8037ED0 CRC64; MGKQKYFDTA LKPERAVLVG VIRQGEKPEE TKEYLDELAF LVDTAGGVVT HIFTQKMEKP DRSTFVGTGK LEEIAAYVKS EEIDLVVFDD ELSPSQLRNI ERELQVKVLD RSNLILDIFA GRAQTAQART QVELAQLQYL LPRLTRLWTH LERQKGGIGM RGPGETQIES DRRMILEKIA LLKERLKLID KQNETQRKNR SELIRVALVG YTNVGKSTIM NMLSKSEVFA ENKLFATLDT TVRKVVIENV PFLLSDTVGF IRKLPHHLIE CFKSTLDEVR EANVLIHVVD ISHPNFEDQI NVVNETLKDL GARDKPTIML FNKIDAYVSP EVDLENGEKS TLTIEEFEHS WMAANNAPAM FISALHKENL EEFKQLLYDK VKALHTERYP YDKLLY // ID A0A0N7JHH9_9CAUL Unreviewed; 444 AA. AC A0A0N7JHH9; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 07-JUN-2017, entry version 12. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=AQ619_08815 {ECO:0000313|EMBL:ALL13442.1}; OS Caulobacter henricii. OC Bacteria; Proteobacteria; Alphaproteobacteria; Caulobacterales; OC Caulobacteraceae; Caulobacter. OX NCBI_TaxID=69395 {ECO:0000313|EMBL:ALL13442.1, ECO:0000313|Proteomes:UP000056905}; RN [1] {ECO:0000313|EMBL:ALL13442.1, ECO:0000313|Proteomes:UP000056905} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CB4 {ECO:0000313|EMBL:ALL13442.1, RC ECO:0000313|Proteomes:UP000056905}; RA Scott D., Ely B.; RT "Conservation of the essential genome among Caulobacter and RT Brevundimonas species."; RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP013002; ALL13442.1; -; Genomic_DNA. DR RefSeq; WP_062146458.1; NZ_CP013002.1. DR EnsemblBacteria; ALL13442; ALL13442; AQ619_08815. DR KEGG; chq:AQ619_08815; -. DR KO; K03665; -. DR Proteomes; UP000056905; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000056905}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000056905}. FT DOMAIN 213 383 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 444 AA; 49039 MW; 2D915CBE63754A6E CRC64; MSKSSKSVDH AAPILKAFVI HPVRPLRGPA AALARDPQSR LEEAVGLAVA LDLNVVETAI APLRVVTPAT LFGKGKIEEF AAICEVEKID VAVFDDQLTP VQQRNLERGL NVKVVDRTGL ILEIFARRAR TREGKLQVEL ARLDYERSRL VRTWTHLERQ RGGTGNTGGP GETQIELDRR LIADHILKLK RELEEVRRTR TLHRKARKKV PYPTVALVGY TNAGKSTLFN RLTEAEVLAK DMLFATLDPT LRTVKLPDGR PAILSDTVGF ISDLPHELVE AFRATLEEVQ EADVVLHVRD IANPDSQAQA RDVESVLAEL GVTFDEGKTV VEVWNKFDLV AQDEREAIEG GARRAEASPV SAVTGEGCQA LLKRIAGLID DSPPIAIRLS ATEGEALAWI YRNGRVMTRE DEAEGGVMIV ARLDPQALGR FERQFPEAFV MVTN // ID A0A0N8GH58_9BACI Unreviewed; 421 AA. AC A0A0N8GH58; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=AM506_07170 {ECO:0000313|EMBL:KPL60378.1}; OS Bacillus vietnamensis. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus. OX NCBI_TaxID=218284 {ECO:0000313|EMBL:KPL60378.1, ECO:0000313|Proteomes:UP000050398}; RN [1] {ECO:0000313|EMBL:KPL60378.1, ECO:0000313|Proteomes:UP000050398} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=UCD-SED5 {ECO:0000313|EMBL:KPL60378.1, RC ECO:0000313|Proteomes:UP000050398}; RA Lee R.D., Jospin G., Lang J.M., Coil D.A., Eisen J.A.; RT "Draft Genome Sequence of Bacillus vietnamensis UCD-SED5."; RL Submitted (AUG-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KPL60378.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LIXZ01000004; KPL60378.1; -; Genomic_DNA. DR RefSeq; WP_060671802.1; NZ_LIXZ01000004.1. DR EnsemblBacteria; KPL60378; KPL60378; AM506_07170. DR PATRIC; fig|218284.4.peg.2937; -. DR Proteomes; UP000050398; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000050398}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000050398}. FT DOMAIN 198 366 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 157 184 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 421 AA; 48188 MW; 3365F4D45E675901 CRC64; MEERLKAIAI GVNTKDKNND FEYSILELKG LADARQIDVV GELTQNLPRP NHVHYIGKGK IDELLPLIEE WDADVLITND ELSPSQIRVL EEKLDVRVMD RTMLILDIFA ERAKTREAQL QVEVAQLQYM LPRLVGRRES LGRQGGGSGL ANRGAGETKL ELDRRRIEEK ITALNKELDS LVDLRTTQRK QRKKSEIPVV SLVGYTNAGK STTMNAFVET FHPNENKQVF EKDMLFATLE TSVRNITLPD KKEFLLTDTV GFVNKLPHQL VKAFRSTLEE VLEADLIIHV VDYSDPHHEK LMNVTDKTLE GIGVGDIPVI YAFNKAELVE GEVPRVEKDR IYLSAKKRIG MDELLHVVKS YIFKDYKKCQ MLIPFDKGHL ISYFNEQANV VETEYEESGT KLTLECKVSD FEKYQQYIVH E // ID A0A0N8GQC4_9CHLR Unreviewed; 458 AA. AC A0A0N8GQC4; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=SE15_07765 {ECO:0000313|EMBL:KPL83306.1}; OS Thermanaerothrix daxensis. OC Bacteria; Chloroflexi; Anaerolineae; Anaerolineales; Anaerolineaceae; OC Thermanaerothrix. OX NCBI_TaxID=869279 {ECO:0000313|EMBL:KPL83306.1, ECO:0000313|Proteomes:UP000050544}; RN [1] {ECO:0000313|EMBL:KPL83306.1, ECO:0000313|Proteomes:UP000050544} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=GNS-1 {ECO:0000313|EMBL:KPL83306.1, RC ECO:0000313|Proteomes:UP000050544}; RA Hemp J., Ward L.M., Pace L.A., Fischer W.W.; RT "Whole genome sequence of Thermanaerothrix daxensis DSM 23592."; RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KPL83306.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LGKO01000004; KPL83306.1; -; Genomic_DNA. DR RefSeq; WP_054521724.1; NZ_LGKO01000004.1. DR EnsemblBacteria; KPL83306; KPL83306; SE15_07765. DR PATRIC; fig|869279.4.peg.2283; -. DR Proteomes; UP000050544; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000050544}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000050544}. FT DOMAIN 219 385 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 178 215 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 458 AA; 51448 MW; 9D998E57D7E01B2B CRC64; MSPKIPEPTG FPRERAFLVG VEIRSEPSPL SMEDSLAELR LLAQTADLEV VGEAYQRLDR PHPDTLIGKG KVEEIKVLLE ETAADVVIFD TELSPRHQRE LEEQFGNQVR VLDRTALILD IFARHAHTRE GILQVELAFY EYRLPRLTRA WTNLAQQTGG GGGRTGSQGG VGLRGPGETQ LEVDRREIRR RIAFLKRELE KVRAHRQRYR QQRRKSQVPV ISLVGYTNAG KSTLLNRLAR AQVYVADQLF ATLDPTTRRV ELPGGHIVLF TDTVGFIQKL PTQLVAAFRA TLEEITESDL LVHVLDVTHP NAVEQWKVVQ QTLEEIGAGA IPVITALNKI DRLPNPSAIQ ALSETFLHSV PISALTGEGI PELLRVIETA LFEDYSPMTV HIPYTEGHMI SLFHEHGKVE RVTHHDGYVT IRGLLPGRLI ARFQPFTRRI KTVTQPDNVH EPVDLSDS // ID A0A0N8H3N5_9FLAO Unreviewed; 403 AA. AC A0A0N8H3N5; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=I595_3047 {ECO:0000313|EMBL:KPM31068.1}; OS Croceitalea dokdonensis DOKDO 023. OC Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales; OC Flavobacteriaceae; Croceitalea. OX NCBI_TaxID=1300341 {ECO:0000313|EMBL:KPM31068.1, ECO:0000313|Proteomes:UP000050280}; RN [1] {ECO:0000313|EMBL:KPM31068.1, ECO:0000313|Proteomes:UP000050280} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DOKDO 023 {ECO:0000313|EMBL:KPM31068.1, RC ECO:0000313|Proteomes:UP000050280}; RA Kwon S.-K., Lee H.K., Kwak M.-J., Kim J.F.; RT "Genome sequence of the marine flavobacterium Croceitalea dokdonensis RT DOKDO 023 that contains proton- and sodium-pumping rhodopsins."; RL Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KPM31068.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LDJX01000006; KPM31068.1; -; Genomic_DNA. DR RefSeq; WP_054560032.1; NZ_LDJX01000006.1. DR EnsemblBacteria; KPM31068; KPM31068; I595_3047. DR PATRIC; fig|1300341.3.peg.3199; -. DR Proteomes; UP000050280; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000050280}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000050280}. FT DOMAIN 200 385 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 403 AA; 46703 MW; 9991FE3F8631263C CRC64; MLEKKTTEYE KSVLIGIINQ EQDKTKVEEY LDELEFLTYT AGGEVLKRFV QRMDVPNPKT LLGSGKIEEV AAYVKENDIG SAIFDDELSP AQQRNIEKLL RCKIIDRTSL ILDIFAQRAQ TSYARTQVEL AQYQYLLPRL TGLWTHLERQ KGGIGMRGPG ETEIETDRRI VRDRISLLKK KLTKIDRQME TQRGNRGALV RVALVGYTNV GKSTLMNVIS KSEVFAENKL FATLDTTVRK VVLGNLPFLL SDTVGFIRKL PTQLVESFKS TLDEVREADL LLHVVDISHP QFEEHIASVN KILDEIESAD KSTIMVFNKI DMYHPETIDE DDLVTQKTKI HFTLEEWRQT WYHKLGDRAL FISALNKENL DDFRKRVYNE VRDIHVTRFP YNNFLYPEHL DEY // ID A0A0N8K630_9RHOB Unreviewed; 437 AA. AC A0A0N8K630; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 07-JUN-2017, entry version 10. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:KPP87793.1}; GN ORFNames=HLUCCO07_02885 {ECO:0000313|EMBL:KPP87793.1}; OS Rhodobacteraceae bacterium HLUCCO07. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae. OX NCBI_TaxID=1666914 {ECO:0000313|EMBL:KPP87793.1, ECO:0000313|Proteomes:UP000050369}; RN [1] {ECO:0000313|EMBL:KPP87793.1, ECO:0000313|Proteomes:UP000050369} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=HLUCCO07 {ECO:0000313|EMBL:KPP87793.1}; RA Nelson W.C., Romine M.F., Lindemann S.R.; RT "Identification and resolution of microdiversity through metagenomic RT sequencing of parallel consortia."; RL Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KPP87793.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LJSU01000009; KPP87793.1; -; Genomic_DNA. DR EnsemblBacteria; KPP87793; KPP87793; HLUCCO07_02885. DR PATRIC; fig|1666914.4.peg.2784; -. DR Proteomes; UP000050369; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000050369}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000050369}. FT DOMAIN 216 386 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 437 AA; 48411 MW; 51C03C4CD33C1B54 CRC64; MSAETDGDTH ETQARLTRAW VLHPDIRSDP KPAHGRRDPA RALEEAVSLA EALPGLEVVG QEVVRLPRPH PGLLFGTGKI EELKARIEAA EVELVLVDGP VSPVQQRNLE KKWGVKLLDR TGLILEIFSD RAATREGVLQ VEMAALSYQR TRLVRAWTHL ERQRGGLGFV GGPGETQIEA DRRAIDEQLV RLRRQLAKVV KTRDLHRKAR AKVPYPIVAL VGYTNAGKST LFNRLTGSDV MVKDMLFATL DPTMRRVQLP DGGPEVILSD TVGFISDLPT ELVAAFRATL EEVLAADLIV HVRDISHPET REQAEDVEAI LASLGVARET PQIEVWNKID LLDEGARTAA VNAAARDENV VALSAVTGQG VEDLLARIAE RLGGVRHESR VVLPFSQGRK RAWLHAEGVV EHEEETEDGH ALTLLWTDRQ EQRFRDL // ID A0A0N8KAD5_9ALTE Unreviewed; 432 AA. AC A0A0N8KAD5; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 30-AUG-2017, entry version 12. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:KPP99833.1}; GN ORFNames=HLUCCO03_16015 {ECO:0000313|EMBL:KPP99833.1}; OS Marinobacter sp. HL-58. OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales; OC Alteromonadaceae; Marinobacter. OX NCBI_TaxID=1479237 {ECO:0000313|EMBL:KPP99833.1, ECO:0000313|Proteomes:UP000050516}; RN [1] {ECO:0000313|EMBL:KPP99833.1, ECO:0000313|Proteomes:UP000050516} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=HL-58 {ECO:0000313|EMBL:KPP99833.1}; RA Nelson W.C., Romine M.F., Lindemann S.R.; RT "Identification and resolution of microdiversity through metagenomic RT sequencing of parallel consortia."; RL Submitted (AUG-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KPP99833.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LIHP01000010; KPP99833.1; -; Genomic_DNA. DR RefSeq; WP_027832737.1; NZ_JMLY01000001.1. DR EnsemblBacteria; KPP99833; KPP99833; HLUCCO03_16015. DR PATRIC; fig|1479237.4.peg.1457; -. DR Proteomes; UP000050516; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000050516}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000050516}. FT DOMAIN 198 365 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 432 AA; 49020 MW; D4608EC96B6B8E9B CRC64; MFERPDVGER AILVHIEFSS HEESEDLGEF RELVWSAGVE PVGVVTGSRK QPSPRLFVGE GKLEEIRDAV AANEADVVLF NHALSPSQER NIERELQCRV LDRTGVILDI FAQRARTHEG KLQVELAQLE HMSTRLVRGW THLERQKGGI GLRGPGETQL ETDRRLLRER IKSIHRRLEK VRKQRNQGRR ARKRADIPTV SLVGYTNAGK STLFNRITSS TVYAADQLFA TLDPTLRRLE LPDIGPVVMA DTVGFIRHLP HKLVEAFRAT LEETTEASLL LHIIDCHDDR REENMEQVEE VLAEIGADEI PVLQVFNKID LLDNFEPRIE RNEDGVPVRV WVSAVTGAGL DGLFDTIVER LAEDVIHHFV VLGPADGKLR ALLHQAGSVL SEDHRDNGDS VVEVRLQYRD WSQLLSRAGM QEKDVKFEER RI // ID A0A0N8KDE4_9RHOB Unreviewed; 443 AA. AC A0A0N8KDE4; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 07-JUN-2017, entry version 10. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:KPQ08306.1}; GN ORFNames=HLUCCA12_00445 {ECO:0000313|EMBL:KPQ08306.1}; OS Rhodobacteraceae bacterium HLUCCA12. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae. OX NCBI_TaxID=1666916 {ECO:0000313|EMBL:KPQ08306.1, ECO:0000313|Proteomes:UP000050476}; RN [1] {ECO:0000313|EMBL:KPQ08306.1, ECO:0000313|Proteomes:UP000050476} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=HLUCCA12 {ECO:0000313|EMBL:KPQ08306.1}; RA Nelson W.C., Romine M.F., Lindemann S.R.; RT "Identification and resolution of microdiversity through metagenomic RT sequencing of parallel consortia."; RL Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KPQ08306.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LJSV01000001; KPQ08306.1; -; Genomic_DNA. DR EnsemblBacteria; KPQ08306; KPQ08306; HLUCCA12_00445. DR PATRIC; fig|1666916.3.peg.1851; -. DR Proteomes; UP000050476; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000050476}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000050476}. FT DOMAIN 212 383 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 443 AA; 48212 MW; 89822AD5C472C5A1 CRC64; MSAQDGDTTT ATGRAPTRAL VLHPDIRGTD TARDPEGALA EAMALARALP GIALIDGQVV RLPRPHPGHL FGSGKVAELK ARIEADEIEL VLVDGPVSPV QQRNLEREWS VKLLDRTGLI LEIFADRART REGVLQVELA ALSYQRTRLV RAWTHLERQR GGLGFVGGPG ETQIEADRRA IDTQMVRLRR QLEKVAKTRE LHRAARRRVP YPVVALVGYT NAGKSTLFNR MTGAAVMAKD MLFATLDPTM RAVVLPGGLE VILSDTVGFI SDLPTQLVAA FRATLEEVLE ADLIVHVRDI AHPETEAQAA DVESILADLG VAQSVPRIEV WNKIDLLPAD DPLLTVAARR DTVYPASALT GAGLETVFAA ITAALDDERH ETVLDLAYDQ GRARAWLFSE GVVLDEEPGD TGSTIRVNWT ARQRRRFESL LAPDAADGQG ADD // ID A0A0N8KEF3_9RHIZ Unreviewed; 464 AA. AC A0A0N8KEF3; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 07-JUN-2017, entry version 12. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:KPQ11178.1}; GN ORFNames=HLUCCO17_07285 {ECO:0000313|EMBL:KPQ11178.1}; OS Rhizobiales bacterium HL-109. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales. OX NCBI_TaxID=1653334 {ECO:0000313|EMBL:KPQ11178.1, ECO:0000313|Proteomes:UP000050497}; RN [1] {ECO:0000313|EMBL:KPQ11178.1, ECO:0000313|Proteomes:UP000050497} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=HL-109 {ECO:0000313|EMBL:KPQ11178.1}; RA Nelson W.C., Romine M.F., Lindemann S.R.; RT "Identification and resolution of microdiversity through metagenomic RT sequencing of parallel consortia."; RL Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KPQ11178.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LJSX01000009; KPQ11178.1; -; Genomic_DNA. DR RefSeq; WP_074445351.1; NZ_FMBM01000002.1. DR EnsemblBacteria; KPQ11178; KPQ11178; HLUCCO17_07285. DR PATRIC; fig|1653334.4.peg.2532; -. DR Proteomes; UP000050497; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000050497}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000050497}. FT DOMAIN 230 404 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 189 216 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 464 AA; 51381 MW; 72C4FBCE212E9938 CRC64; MSTPDSPIGE GFTPEPDTDV SAGTRTLVVG PYVSRKQRAL PDGAPAAAEN LRPFEARLDE ACGLAAAIDL DVVEVHLTTF PAPRPSTYLG KGKVEEVKLL VAAKDITLVV MDCALSPVQQ RNLERTFGAK VIDRTGLILE IFGRRARTRE GTLQVELAHL AYQKSRLVRS WTHLERQRGG YGFLGGPGET QIEADRRQIQ ERMTRIEKEL EGVTRTRGLH RASRRRVPYP IVAFVGYTNV GKSTLFNRMT RAEVMAQDML FATLDPTSRA VALPHGEKAI LSDTVGFISD LPTMLVAAFR ATLEDVIEAD ILLHVRDVSH GETEAQAADV ESVLRDLDVD PSDTARIIEV WNKADLLDAP DRERLATRAA RLPEEARPAL VSALTGEGID ALLQTIEDRI ARGRPQYHVL LDPADGQNLN WLYENAEVMG RDDRDAAIAM RVRVAPEKEP RLLRRFPKAR RSKG // ID A0A0N8KFS4_9RHOB Unreviewed; 432 AA. AC A0A0N8KFS4; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:KPQ14946.1}; GN ORFNames=HLUCCA09_02495 {ECO:0000313|EMBL:KPQ14946.1}; OS Rhodobacteraceae bacterium HLUCCA09. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae. OX NCBI_TaxID=1666915 {ECO:0000313|EMBL:KPQ14946.1, ECO:0000313|Proteomes:UP000053417}; RN [1] {ECO:0000313|EMBL:KPQ14946.1, ECO:0000313|Proteomes:UP000053417} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=HLUCCA09 {ECO:0000313|EMBL:KPQ14946.1}; RA Nelson W.C., Romine M.F., Lindemann S.R.; RT "Identification and resolution of microdiversity through metagenomic RT sequencing of parallel consortia."; RL Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KPQ14946.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LJNT01000055; KPQ14946.1; -; Genomic_DNA. DR EnsemblBacteria; KPQ14946; KPQ14946; HLUCCA09_02495. DR PATRIC; fig|1666915.4.peg.2198; -. DR Proteomes; UP000053417; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000053417}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000053417}. FT DOMAIN 212 381 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 432 AA; 47366 MW; 0641BE8234A39075 CRC64; MRSGGGRPAF ETDRPVTRAL VLHPDVPGDT ARRDPQARLD EAVALAQALP GLEVAGADVV ALREARPGTL FGPGKVDEIG ARVAADEIGL VLVDGPVTPV QQRNLERAWK TKLLDRTGLI LEIFADRAAT REGVLQVELA ALSYQRTRLV RAWTHLERQR GGLGFVGGPG ETQIEADRRA LDEAILRLRR QLDKVQKTRT LHREARAKVP FPVVALVGYT NAGKSTLFNR LTGAEVMAED MLFATLDPTM RGVELATGAK VILSDTVGFI SELPTQLVAA FRATLEEVLE ADLILHVRDV SHRESAAQAE DVEAILHELG VADETPRLEL WNKVDRLDGE ARATAEAIAA RRDDVLLMSA ATGEGVPEVV AAVTEVLDGA REDAVLELAF ADGRKRAWLH ENRVVTEERQ GEKGWRLSVR WTPRQRDAFH RL // ID A0A0N8KIX9_9SPHN Unreviewed; 205 AA. AC A0A0N8KIX9; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 08-JUN-2016, entry version 6. DE SubName: Full=GTP-binding protein HflX {ECO:0000313|EMBL:KPQ23786.1}; DE Flags: Fragment; GN Name=hflX {ECO:0000313|EMBL:KPQ23786.1}; GN ORFNames=HLUCCX21_05725 {ECO:0000313|EMBL:KPQ23786.1}; OS Porphyrobacter sp. HL-46. OC Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales; OC Erythrobacteraceae; Porphyrobacter. OX NCBI_TaxID=1479239 {ECO:0000313|EMBL:KPQ23786.1, ECO:0000313|Proteomes:UP000054043}; RN [1] {ECO:0000313|EMBL:KPQ23786.1, ECO:0000313|Proteomes:UP000054043} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=HL-46 {ECO:0000313|EMBL:KPQ23786.1}; RA Nelson W.C., Romine M.F., Lindemann S.R.; RT "Identification and resolution of microdiversity through metagenomic RT sequencing of parallel consortia."; RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KPQ23786.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LLEX01000246; KPQ23786.1; -; Genomic_DNA. DR EnsemblBacteria; KPQ23786; KPQ23786; HLUCCX21_05725. DR Proteomes; UP000054043; Unassembled WGS sequence. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. PE 4: Predicted; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000054043}; KW Reference proteome {ECO:0000313|Proteomes:UP000054043}. FT DOMAIN 25 111 GTP-bdg_N. {ECO:0000259|Pfam:PF13167}. FT DOMAIN 114 193 GTP-bdg_M. {ECO:0000259|Pfam:PF16360}. FT COILED 158 192 {ECO:0000256|SAM:Coils}. FT NON_TER 205 205 {ECO:0000313|EMBL:KPQ23786.1}. SQ SEQUENCE 205 AA; 23217 MW; 3D3EAF2AE65B9561 CRC64; MTRGARALVL CPDIRALRYD LDAAERLAEA EGLAGAIGLA IVHAAILPVR QMQPNTLFGS GQVENIAVWC EQYEAELVIV DGALTPIQQR NLEDRLKRKV IDRTGLILEI FGERAATAEG RLQVELAHLD YQQSRLVRSW THLERQRGGF GFLGGPGETQ IEADRRMIRQ RMARLRRELE QVRKTRTLHR ERRGRAPWPI IALVG // ID A0A0N8W5S5_9SPHI Unreviewed; 398 AA. AC A0A0N8W5S5; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=AQF98_07355 {ECO:0000313|EMBL:KQC01515.1}; OS Pedobacter sp. Hv1. OC Bacteria; Bacteroidetes; Sphingobacteriia; Sphingobacteriales; OC Sphingobacteriaceae; Pedobacter. OX NCBI_TaxID=1740090 {ECO:0000313|EMBL:KQC01515.1, ECO:0000313|Proteomes:UP000050543}; RN [1] {ECO:0000313|EMBL:KQC01515.1, ECO:0000313|Proteomes:UP000050543} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Hv1 {ECO:0000313|EMBL:KQC01515.1, RC ECO:0000313|Proteomes:UP000050543}; RA Ott B.M., Beka L., Graf J., Rio R.; RT "Draft Genome Sequence of a Pedobacter sp. Strain Hv1, an Isolate From RT Medicinal Leech Mucosal Castings."; RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KQC01515.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LLWP01000003; KQC01515.1; -; Genomic_DNA. DR RefSeq; WP_055131280.1; NZ_LLWP01000003.1. DR EnsemblBacteria; KQC01515; KQC01515; AQF98_07355. DR Proteomes; UP000050543; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000050543}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000050543}. FT DOMAIN 204 387 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 398 AA; 45507 MW; F2E9390F22355DDA CRC64; MGKQKYYDTA LKQERAVLVG VITPGEKPEQ TKEYLDELAF LVDTAGGAVE KVFTQKMLKP DRATFVGTGK LEEIQAYVKA EEIDMVVFDD ELSPSQLRNI ERELQVKILD RSNLILDIFA GRAQTAQAKT QVELAQLQYL LPRLTRLWTH LERQKGGIGM RGPGETQIES DRRMILEKIS LLKERLKLID RQNETQRKNR GQLIRVALVG YTNVGKSTIM NMLSKSDVFA ENKLFATLDT TVRKVVIENL PFLLSDTVGF IRKLPHHLVE CFKSTLDEVR EADVLIHVVD VSHPNFEDQI HTVNETLNDL GARDKDTIMI FNKIDAYVTP AADEFNEEEE TGPLTLADFK KSWMAHHNAP AIFISATKKE NVEEFKQLLY DKVKSLHTVR YPYDKLLY // ID A0A0N8WA76_9EURY Unreviewed; 365 AA. AC A0A0N8WA76; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 12-APR-2017, entry version 6. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:KQC13923.1}; DE Flags: Fragment; GN ORFNames=APR56_04700 {ECO:0000313|EMBL:KQC13923.1}; OS Methanosaeta sp. SDB. OC Archaea; Euryarchaeota; Methanomicrobia; Methanosarcinales; OC Methanosaetaceae; Methanosaeta. OX NCBI_TaxID=1735328 {ECO:0000313|EMBL:KQC13923.1, ECO:0000313|Proteomes:UP000051107}; RN [1] {ECO:0000313|EMBL:KQC13923.1, ECO:0000313|Proteomes:UP000051107} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SDB {ECO:0000313|EMBL:KQC13923.1}; RA Wawrik B., Marks C.R., Davidova I.A., Mcinerney M.J., Pruitt S., RA Duncan K., Suflita J.M., Callaghan A.V.; RT "Metagenomic Analysis of a Methanogenic Paraffin-Utilizing RT Consortium."; RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KQC13923.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LKUG01000934; KQC13923.1; -; Genomic_DNA. DR Proteomes; UP000051107; Unassembled WGS sequence. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000051107}. FT DOMAIN 144 310 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 103 130 {ECO:0000256|SAM:Coils}. FT NON_TER 1 1 {ECO:0000313|EMBL:KQC13923.1}. SQ SEQUENCE 365 AA; 41128 MW; DBF1178A8C6B09B4 CRC64; TFIGTGSARD LSRRCREAGI TEIIFSEDLS PAQLRNLEDA SGVEVRDRTE LILVIFAQRA QTREASLQVE LARLEYLLPR LGGAWRHLSR QKGGMLGTRD AGEKQIELDR RLARNRIHAL KKEMETVRRQ RFTQRKSRRQ AGAPVVSIIG YTNSGKSTLL NALTSAGVRS ENRLFATLDP VTRKAALPSG RKVLFSDTVG FIRNLPPHLI DSFRATLEEV AEADLLLEVL DISHPRIRER KRVVEEVLKE LGADRTPMVV ALNKIDLVRD PYLVRESSGR FAGAVPISAR KGKGLDRLLE EVERKLPSAR RSYRLLIPQN RPELVAALHR DGRVLKVDYH PKDIYLEVMI EERALGEAGR YILGA // ID A0A0N9HZW3_9PSEU Unreviewed; 473 AA. AC A0A0N9HZW3; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 07-JUN-2017, entry version 12. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=AOZ06_14155 {ECO:0000313|EMBL:ALG07905.1}; OS Kibdelosporangium phytohabitans. OC Bacteria; Actinobacteria; Pseudonocardiales; Pseudonocardiaceae; OC Kibdelosporangium. OX NCBI_TaxID=860235 {ECO:0000313|EMBL:ALG07905.1, ECO:0000313|Proteomes:UP000063699}; RN [1] {ECO:0000313|EMBL:ALG07905.1, ECO:0000313|Proteomes:UP000063699} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=KLBMP1111 {ECO:0000313|EMBL:ALG07905.1, RC ECO:0000313|Proteomes:UP000063699}; RA Qin S., Xing K.; RT "Genome sequencing of Kibdelosporangium phytohabitans."; RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP012752; ALG07905.1; -; Genomic_DNA. DR RefSeq; WP_054289815.1; NZ_CP012752.1. DR EnsemblBacteria; ALG07905; ALG07905; AOZ06_14155. DR KEGG; kphy:AOZ06_14155; -. DR KO; K03665; -. DR Proteomes; UP000063699; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000313|EMBL:ALG07905.1}; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000063699}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900, KW ECO:0000313|EMBL:ALG07905.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000063699}. FT DOMAIN 246 415 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 205 232 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 473 AA; 51353 MW; B9E6D429D7B6AA87 CRC64; MTEDYAEELV STGDLELEDR SALRRVAGLS TELSDITEVE YRQLRLERVV LVGVWTEGTA EQADASLTEL SRLAETAGSE VLEGLIQRRD RPDPATYVGS GKVDEIFQTV LATGADTVIC DGELSPGQLR QLEARLKVKV IDRTALILDI FAQHARSKEG KAQVELAQLQ YLLPRLRGWG ESLSRQAGGR AGGGNGGVGL RGPGETKLET DRRRIRAKIS KLRREIAAMS AVRETKRGRR VANEVPSVAI AGYTNAGKSS LLNAITGAGV LVEDALFATL DATTRRTQTP DGRTYTLTDT VGFVRHLPHQ LIEAFRSTLD EVADADLLVH VVDGSDDNPE WQVNAVREVL NEIVERNDTT MPPEVLVVNK IDAADELQLA RLRHLLPGAL FVSAHKGSGL DELREHLATA LPRPDVEVDV LVPYARGELV ARVHREGEVL AERHTPEGTQ LHARVNGDLA GALGQFASNG APA // ID A0A0N9UUG7_SPHMC Unreviewed; 451 AA. AC A0A0N9UUG7; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 07-JUN-2017, entry version 12. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=AN936_08920 {ECO:0000313|EMBL:ALH80486.1}; OS Sphingopyxis macrogoltabida (Sphingomonas macrogoltabidus). OC Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales; OC Sphingomonadaceae; Sphingopyxis. OX NCBI_TaxID=33050 {ECO:0000313|EMBL:ALH80486.1, ECO:0000313|Proteomes:UP000058074}; RN [1] {ECO:0000313|EMBL:ALH80486.1, ECO:0000313|Proteomes:UP000058074} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=EY-1 {ECO:0000313|EMBL:ALH80486.1, RC ECO:0000313|Proteomes:UP000058074}; RX PubMed=26634754; RA Ohtsubo Y., Nagata Y., Numata M., Tsuchikane K., Hosoyama A., RA Yamazoe A., Tsuda M., Fujita N., Kawai F.; RT "Complete Genome Sequence of Polypropylene Glycol- and Polyethylene RT Glycol-Degrading Sphingopyxis macrogoltabida Strain EY-1."; RL Genome Announc. 3:0-0(2015). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP012700; ALH80486.1; -; Genomic_DNA. DR RefSeq; WP_054587842.1; NZ_CP012700.1. DR EnsemblBacteria; ALH80486; ALH80486; AN936_08920. DR KEGG; smag:AN936_08920; -. DR PATRIC; fig|33050.5.peg.1853; -. DR KO; K03665; -. DR Proteomes; UP000058074; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 2. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000058074}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000058074}. FT DOMAIN 206 387 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 172 199 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 451 AA; 49285 MW; A49946D0C461ED8C CRC64; MNDDIGEVTR GAAALLVVPE WHGQRLSRDL DARVEEAKGL AIAIGLVVVA AHPIRLRQTR AATLLGVGQI DAIKPDIAAH DVQVVIVDAP LTAIQQRNLE TAFGAKVIDR TGLILEIFGE RAATAEGRLQ VELAHLDYQA GRLVRSWTHL ERQRGGFGFL GGPGETQIEA DRRMIRDRMA RIRRQLEDAR RTRQLQRAKR QRAPWPVIAL VGYTNAGKST FFNRLTGSDV MAEDMLFATL DPTMREIGLP GIDKAILSDT VGFVSDLPTQ LVAAFRATLE EVTTADLIVH VRDIVHPDSE AQYDDVRAIL DSLGVNGAQD GEGGGDAPDA IPQIEIWNKI DTADPERRAA IAEMAARRPD VALISAVTGE GVDAARILMT SQLTAQHQTL RIFLGFDQGD AMAWLHARGE VLSDEVQGKG HLLTVRLDPA DRARFERLWP ARPDSTSAPT P // ID A0A0N9W4I3_9GAMM Unreviewed; 439 AA. AC A0A0N9W4I3; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 07-JUN-2017, entry version 12. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=AOY20_06805 {ECO:0000313|EMBL:ALH96685.1}; OS Acinetobacter equi. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Moraxellaceae; Acinetobacter. OX NCBI_TaxID=1324350 {ECO:0000313|EMBL:ALH96685.1, ECO:0000313|Proteomes:UP000064939}; RN [1] {ECO:0000313|EMBL:ALH96685.1, ECO:0000313|Proteomes:UP000064939} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=114 {ECO:0000313|EMBL:ALH96685.1, RC ECO:0000313|Proteomes:UP000064939}; RX PubMed=26620413; RA Poppel M.T., Skiebe E., Laue M., Bergmann H., Ebersberger I., Garn T., RA Fruth A., Baumgardt S., Busse H.J., Wilharm G.; RT "Acinetobacter equi sp. nov. isolated from horse faeces."; RL Int. J. Syst. Evol. Microbiol. 0:0-0(2015). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP012808; ALH96685.1; -; Genomic_DNA. DR RefSeq; WP_054582554.1; NZ_CP012808.1. DR EnsemblBacteria; ALH96685; ALH96685; AOY20_06805. DR KEGG; aei:AOY20_06805; -. DR KO; K03665; -. DR Proteomes; UP000064939; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000064939}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000064939}. FT DOMAIN 195 360 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 439 AA; 49206 MW; E9634A972E17584B CRC64; MQQRDGERVI LISVSVQMLE DLDADEFALL AKSAGAEILQ HLHVARIKPD AKYFIGSGKT EEIAALVEEL DANLVIFDHS LTPAQVRNLE QIMKCRVVDR TELILDIFAL RARTYEGKLQ VELAQLHHLS SRLIRSRGTL DSQKGGIGLR GPGETLLETD RRLLKIRMGQ LKARLDKVKQ TRMQGRVARQ KAAIPTVSLV GYTNAGKSTL FNILANSDVY AADQLFATLD PTLRRLDWDG IGQLVLADTV GFVRNLSHSL VESFKATLEE TLEATLLLHV IDSSSPEMLE QIEAVEKVLN EIGADVPIIR VYNKIDQSQE EAKIIYANEH QPERVYLSAH TGQGLNLLKQ AVHESLVGQI QCFDVLLKPA YGKLRTQLYA LNVIQSEKYD DEGNLHLKVM MAPHKIEQLI KKAHLPLDEI LGEKAKIFHP ALEEFEIKD // ID A0A0N9YUV1_9ARCH Unreviewed; 374 AA. AC A0A0N9YUV1; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 07-JUN-2017, entry version 9. DE SubName: Full=GTPase HflX {ECO:0000313|EMBL:ALI34252.1}; GN Name=hflX_1 {ECO:0000313|EMBL:ALI34252.1}; GN ORFNames=NMY3_00038 {ECO:0000313|EMBL:ALI34252.1}; OS Candidatus Nitrocosmicus oleophilus. OC Archaea; Thaumarchaeota; Nitrososphaeria; Nitrososphaerales; OC Nitrososphaeraceae; Candidatus Nitrosocosmicus. OX NCBI_TaxID=1353260 {ECO:0000313|EMBL:ALI34252.1, ECO:0000313|Proteomes:UP000058925}; RN [1] {ECO:0000313|EMBL:ALI34252.1, ECO:0000313|Proteomes:UP000058925} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MY3 {ECO:0000313|EMBL:ALI34252.1, RC ECO:0000313|Proteomes:UP000058925}; RA Jung M.-Y., Rhee S.-K.; RT "Niche specialization of a soil ammonia-oxidizing archaeon, Candidatus RT Nitrosocosmicus oleophilus."; RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP012850; ALI34252.1; -; Genomic_DNA. DR EnsemblBacteria; ALI34252; ALI34252; NMY3_00038. DR KEGG; taa:NMY3_00038; -. DR KO; K03665; -. DR Proteomes; UP000058925; Chromosome. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000058925}; KW Reference proteome {ECO:0000313|Proteomes:UP000058925}. FT DOMAIN 189 307 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 374 AA; 42847 MW; 6383C42E0712978D CRC64; MHQANIILVT YPEDFAIEEA KSLVESMPEY KVVKVFTQKY LNRAKYGMGF GKAEEIKQFV SQAGNIEKIF VDEHLGAKQI FNLEELIEIP IIDRERLILD IFYSRATTNE SKLQIQLAEI QYKMPRVREN AKLMSKSNER VGKGGMGEYI VDVQFRDLKR QMGFVKEKLK DANLKRHEYR KQRLRKGMFI VSLVGYTSSG KTTLFNLLTK ENKETSANLF TTLSTTTRSL DNSSNIDNKG DVDVLVVDTV GFISRLPHYM IDAFKSTLEE SLEADLIFFL IDCSENLEDI GKKYSSCWNV LEELKIDKSK LHIVLTKVET TKSDKIQEIM KYMDDSIDKI AISSKSGYGI HKLRNLIASK KAHVKDEHSK LAPS // ID A0A0N9ZMJ7_9RHOB Unreviewed; 431 AA. AC A0A0N9ZMJ7; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 07-JUN-2017, entry version 13. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=IMCC12053_588 {ECO:0000313|EMBL:ALI54536.1}; OS Celeribacter marinus. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae; Celeribacter. OX NCBI_TaxID=1397108 {ECO:0000313|EMBL:ALI54536.1, ECO:0000313|Proteomes:UP000064920}; RN [1] {ECO:0000313|EMBL:ALI54536.1, ECO:0000313|Proteomes:UP000064920} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=IMCC 12053 {ECO:0000313|EMBL:ALI54536.1, RC ECO:0000313|Proteomes:UP000064920}; RA Wang D.B., Wang M.; RL Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP012023; ALI54536.1; -; Genomic_DNA. DR RefSeq; WP_062215547.1; NZ_FOSM01000008.1. DR EnsemblBacteria; ALI54536; ALI54536; IMCC12053_588. DR KEGG; cmar:IMCC12053_588; -. DR PATRIC; fig|1397108.4.peg.608; -. DR KO; K03665; -. DR Proteomes; UP000064920; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000064920}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000064920}. FT DOMAIN 207 380 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 431 AA; 48417 MW; A6D2DC2204B59A2F CRC64; MGDYYDHEVE PTRAWVIHPD ITSDRGRRDA QPRLDEAVAL AAALPNIEVQ GAEIVRLPKT HPAALFGKGK IQELKERIQA SDVELVLVDG PVTPVQQRNL EKEWKVKLLD RTGLILEIFS DRARTREGVL QVEMAALSYQ RTRLVRAWTH LERQRGGLGF VGGPGETQIE ADRRAIDDHL NRLRKQLARV IKTRELHRAS RAKIPFPIVA LVGYTNAGKS TFFNTVTGAD VFVKDMLFAT LDPTMRQLRL ETAHGGDRDI ILSDTVGFIS NLPTQLVASF RATLEEVLDA DLILHVRDIS ADETEDQKTD VLKILSDLGI KENAPMIEVW NKIDKLDDEA RLARLERAEA DNNVFAISAV TGEGVKSLLD AVSAYFEEDK IEREIVVPFS EGKKRAWLFA EGVVLGEAAS EEGYVLTVLW TPRQEKQFRE M // ID A0A0P0CVZ4_9BACT Unreviewed; 399 AA. AC A0A0P0CVZ4; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 07-JUN-2017, entry version 13. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=DC20_05565 {ECO:0000313|EMBL:ALI98537.1}; OS Rufibacter tibetensis. OC Bacteria; Bacteroidetes; Cytophagia; Cytophagales; Hymenobacteraceae; OC Rufibacter. OX NCBI_TaxID=512763 {ECO:0000313|EMBL:ALI98537.1, ECO:0000313|Proteomes:UP000061382}; RN [1] {ECO:0000313|EMBL:ALI98537.1, ECO:0000313|Proteomes:UP000061382} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=1351 {ECO:0000313|EMBL:ALI98537.1, RC ECO:0000313|Proteomes:UP000061382}; RA Dai J.; RT "Complete genome sequence of Rufibacter tibetensis strain 1351t, a RT radiation-resistant bacterium from tibet plateau."; RL Submitted (AUG-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP012643; ALI98537.1; -; Genomic_DNA. DR RefSeq; WP_062542922.1; NZ_CP012643.1. DR EnsemblBacteria; ALI98537; ALI98537; DC20_05565. DR KEGG; rti:DC20_05565; -. DR PATRIC; fig|512763.3.peg.1234; -. DR KO; K03665; -. DR Proteomes; UP000061382; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000061382}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}. FT DOMAIN 204 387 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 399 AA; 45844 MW; BA63E1F74C8808D1 CRC64; MKNQLHITAK EQETAVLVAV PEYRQTDEKT KEYLDELAFL TETVGAKALK RFVQKLDKPD MRTYVGKGKL EEIVAYVKEH KVDMVIFDDD LSPSQVRNLE RELEVKIIDR SLLILDIFAL RAQTATARAQ VELAQYRYLL PRLTNMWTHL SRQKGGGVAM RGPGETEIET DRRIVRDKIT LLKEKLEKFE KQNFEQRKSR SGIVRVSLVG YTNVGKSTIM NLLTKADVFA ENKLFATVDA TVRKVVVENI PFLLSDTVGF IRKLPTKLIE SFKTTLDEIR ESDLLLHVVD VSHSSFEEHI GVVNDTLKDI QSADKPVILV FNKTDLYLEQ REQELKEHNP EALPDINELK SSYMAKQHTP AIFISATNRA NIDELRQTLL DHVSKIHYER YPNNAPQEQ // ID A0A0P0D6I5_9FLAO Unreviewed; 403 AA. AC A0A0P0D6I5; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 30-AUG-2017, entry version 13. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=APS56_11655 {ECO:0000313|EMBL:ALJ05739.1}; OS Algibacter alginicilyticus. OC Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales; OC Flavobacteriaceae; Algibacter. OX NCBI_TaxID=1736674 {ECO:0000313|EMBL:ALJ05739.1, ECO:0000313|Proteomes:UP000057981}; RN [1] {ECO:0000313|EMBL:ALJ05739.1, ECO:0000313|Proteomes:UP000057981} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=HZ-22 {ECO:0000313|Proteomes:UP000057981}; RA Millard Andrew; RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP012898; ALJ05739.1; -; Genomic_DNA. DR RefSeq; WP_054728291.1; NZ_CP012898.1. DR EnsemblBacteria; ALJ05739; ALJ05739; APS56_11655. DR KEGG; ahz:APS56_11655; -. DR PATRIC; fig|1736674.3.peg.2389; -. DR KO; K03665; -. DR Proteomes; UP000057981; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000057981}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000057981}. FT DOMAIN 200 385 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 403 AA; 46604 MW; 73877CEF658AA9E3 CRC64; MLEKKDISLE KAVLIGVITK EQDEDKSKEY LDELEFLTFT AGGYAVKRFT QKMDMPNPKT FIGTGKMDDV RRYIEENDIT TAIFDDELSA AQERNISKIL NVKVLDRTNL ILDIFAQRAQ TSYARTQVEL AQCEYLLPRL RGMWTHLERQ KGGIGMRGPG ETEIETDRRI VRDKIALLKE KIKTIDKQMA VQRGNRGAMV RVALVGYTNV GKSTLMNVIS KSDVFAENKL FATLDTTVRK VVIQNLPFLL SDTVGFIRKL PTQLVDSFKS TLDEVREADL LLHVVDISHP NFEEHIDSVN KILGEIKSSD KPTIMVFNKI DAYQPEPYKE EDLEIERSSE HYSLEEWKKT WMNKIGNNAL FISALNKENL EDFKKRVYDE VREIHITRFP YNHFLYPDYD DTM // ID A0A0P0GEA1_9BACT Unreviewed; 423 AA. AC A0A0P0GEA1; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 07-JUN-2017, entry version 12. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:ALJ56232.1}; GN ORFNames=AMD24_00036 {ECO:0000313|EMBL:ALJ56232.1}; OS Candidatus Xiphinematobacter sp. Idaho Grape. OC Bacteria; Verrucomicrobia; Spartobacteria; OC Candidatus Xiphinematobacter. OX NCBI_TaxID=1704307 {ECO:0000313|EMBL:ALJ56232.1, ECO:0000313|Proteomes:UP000062177}; RN [1] {ECO:0000313|EMBL:ALJ56232.1, ECO:0000313|Proteomes:UP000062177} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Idaho Grape {ECO:0000313|EMBL:ALJ56232.1, RC ECO:0000313|Proteomes:UP000062177}; RX PubMed=26362082; DOI=10.1093/gbe/evv176; RA Brown A.M., Howe D.K., Wasala S.K., Peetz A.B., Zasada I.A., RA Denver D.R.; RT "Comparative Genomics of a Plant-Parasitic Nematode Endosymbiont RT Suggest a Role in Nutritional Symbiosis."; RL Genome Biol. Evol. 7:2727-2746(2015). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP012665; ALJ56232.1; -; Genomic_DNA. DR RefSeq; WP_062100141.1; NZ_CP012665.1. DR EnsemblBacteria; ALJ56232; ALJ56232; AMD24_00036. DR KEGG; xii:AMD24_00036; -. DR PATRIC; fig|1704307.3.peg.32; -. DR KO; K03665; -. DR Proteomes; UP000062177; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000062177}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000062177}. FT DOMAIN 201 367 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 160 187 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 423 AA; 47518 MW; 8E7153E4A337A0DA CRC64; MYLTSSSHRE RALLVGSCRG SALWDIAESL DELCQLASSA GIQVVETCIQ RLERPTAPFY IGKGKAREIA QQCSKKQASS IIFDDELSPA QGRNLEYITN CKVLDRTQLI LDIFAQRART REGCLQIELA QLQYLLPRLT RMWLHLSRQT GGIGTRGPGE TQLEADRRRV QERIAKLERE LAAVRKNRFI QRGGRLKKNW PVAALIGYTN AGKSSLFNRL TGSEVITEDK LFATLDPTTR QVLLPSRQKV LLIDTVGFIR KLPYTLIDAF KATLEETQLA DLLIHVVDLS HPGYYEQMAA VDSTIKELGV GGKQVVLVFN KVDCVRNPEL IQTQLRRYPG SVAVSAYTGI GIDAFLQQLE MDLSTWRLKV EYQIPLAESA LLAELHRGGC VSSAYYKDEF ALVTAYISPA LRQRFLSFEV THQ // ID A0A0P0M8J3_9BURK Unreviewed; 395 AA. AC A0A0P0M8J3; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:ALK88471.1}; GN ORFNames=L63ED372_01260 {ECO:0000313|EMBL:ALK88471.1}; OS Limnohabitans sp. 63ED37-2. OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Comamonadaceae; Limnohabitans. OX NCBI_TaxID=1678128 {ECO:0000313|EMBL:ALK88471.1, ECO:0000313|Proteomes:UP000059510}; RN [1] {ECO:0000313|EMBL:ALK88471.1, ECO:0000313|Proteomes:UP000059510} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=63ED37-2 {ECO:0000313|EMBL:ALK88471.1, RC ECO:0000313|Proteomes:UP000059510}; RA Ahn J.-H., Kim S.B.; RT "Limnohabitans sp. 2 strains."; RL Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP011774; ALK88471.1; -; Genomic_DNA. DR EnsemblBacteria; ALK88471; ALK88471; L63ED372_01260. DR KEGG; lih:L63ED372_01260; -. DR PATRIC; fig|1678128.3.peg.1247; -. DR KO; K03665; -. DR Proteomes; UP000059510; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000059510}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000059510}. FT DOMAIN 200 373 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 395 AA; 43777 MW; 85154F4F8E4A8D49 CRC64; MSETKSNQVA PTLLVGVDFG LPHFDGELQE LGLLAESGGL KPVARLTCKR KAPDPALFVG SGKADEIKEL ALMHGAVEVL FDQALSPAQQ RNLERHIGLP VNDRTLLILE IFGQRARSHE GKLQVELARQ QYLSTRLVRR WSHLERQSGG IGMRGGPGET QIELDRRMIN DSIKRIKERL VKVKKQRNTQ RRQRERRDTF NISLVGYTNA GKSTLFNALV KARAYAADQL FATLDTTTRQ LYLGEAGRSV SLSDTVGFIR DLPHGLVEAF QATLQEATEA DLLLHVVDAA NPDFPEQMAE VQKVLAEIGA SQVPQLLVFN KLDSLPAERY PLQMQDQYEL DGHAVTRVFL SARSGEGLPL LRSTLADIVK AALPAAESPE PDPRDLDREY PGDLP // ID A0A0P0MG21_9BURK Unreviewed; 391 AA. AC A0A0P0MG21; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:ALK92225.1}; GN ORFNames=L103DPR2_01827 {ECO:0000313|EMBL:ALK92225.1}; OS Limnohabitans sp. 103DPR2. OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Comamonadaceae; Limnohabitans. OX NCBI_TaxID=1678129 {ECO:0000313|EMBL:ALK92225.1, ECO:0000313|Proteomes:UP000063254}; RN [1] {ECO:0000313|EMBL:ALK92225.1, ECO:0000313|Proteomes:UP000063254} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=103DPR2 {ECO:0000313|EMBL:ALK92225.1, RC ECO:0000313|Proteomes:UP000063254}; RA Ahn J.-H., Kim S.B.; RT "Limnohabitans sp. 2 strains."; RL Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP011834; ALK92225.1; -; Genomic_DNA. DR EnsemblBacteria; ALK92225; ALK92225; L103DPR2_01827. DR KEGG; lim:L103DPR2_01827; -. DR PATRIC; fig|1678129.3.peg.1822; -. DR KO; K03665; -. DR Proteomes; UP000063254; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000063254}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000063254}. FT DOMAIN 194 367 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 391 AA; 43625 MW; 59D0716BF7D3E9A6 CRC64; MDSTPALLVG VDFGLPHFDG ELDELSQLAL TAGMQPVAKI TCKRKAPDAA LFVGSGKADE IKFMAEQMGA REILFDQSLS PAQQRNLERH MGLPVNDRTL LILEIFAQRA RSHEGKLQVE LARLQYLSTR LVRRWSHLER QRGGIGTRGG PGETQIELDR RMISDAIKRT KERLTKVKKQ RSTQRRQRDR RNAFNVSLVG YTNAGKSTLF NALVKARAYA ADQLFATLDT TTRQLYLGEA GRSASVSDTV GFIRDLPHGL IDAFQATLQE AADADLLIHV VDASNPNFPE QMTEVQRVLH EIGADHVPQW LVFNKIDNLP PERCPLAFQD EYEVDGQALT RIFVSAQSGE GLPLLRQWLA QEVMKDSAEP TPATDPRFAL DNFGENSDDL P // ID A0A0P0N4T3_9CREN Unreviewed; 370 AA. AC A0A0P0N4T3; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 07-JUN-2017, entry version 10. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=Pyrde_1219 {ECO:0000313|EMBL:ALL01267.1}; OS Pyrodictium delaneyi. OC Archaea; Crenarchaeota; Thermoprotei; Desulfurococcales; OC Pyrodictiaceae; Pyrodictium. OX NCBI_TaxID=1273541 {ECO:0000313|EMBL:ALL01267.1, ECO:0000313|Proteomes:UP000058613}; RN [1] {ECO:0000313|EMBL:ALL01267.1, ECO:0000313|Proteomes:UP000058613} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Su06 {ECO:0000313|EMBL:ALL01267.1, RC ECO:0000313|Proteomes:UP000058613}; RA Jung J.-H., Lin J., Holden J.F., Park C.-S.; RT "Complete genome sequence of hyperthermophilic archaeon Pyrodictium RT delaneyi Su06."; RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP013011; ALL01267.1; -; Genomic_DNA. DR EnsemblBacteria; ALL01267; ALL01267; Pyrde_1219. DR KEGG; pdl:Pyrde_1219; -. DR PATRIC; fig|1273541.4.peg.1304; -. DR KO; K03665; -. DR Proteomes; UP000058613; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000058613}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}. FT DOMAIN 188 366 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 154 181 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 370 AA; 41772 MW; BF96FF2EEAE9AD3E CRC64; MKRALLALPR RLTSWEEREA YALLETAGYT VVDVVRYRPI SRSRLFSKAK LEELAEKAKP LRGDEEARII VYDELRPREY FRIVREARVD AIDRTLLILE IFALHAGSRE AKLQIELARL KHQLPVIKEA IRLAKMRELP GFLGPGGYAV DAYYRYMVSR IARIRRELQE LRRRREIERA KRRSAGLPHV AIVGYASAGK TTLFNKISGE KKPVGPEYFT TISPKVKATS FDGLRFAVVD TVGFISRIPP EIIEAFHSTL EEAAYADLIL YVLDVSEDEY VMTEKLSEGL DTLRRIGVVD RPMIIAANKV DLVRDRSDLE RVLNLIEAMA ESVYPGLQGV IPVSAATSEG LGRLLCRVAT LLRGTAGSMC // ID A0A0P0S9W9_9PSEU Unreviewed; 500 AA. AC A0A0P0S9W9; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 07-JUN-2017, entry version 12. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=AD017_05065 {ECO:0000313|EMBL:ALL80736.1}; OS Pseudonocardia sp. EC080619-01. OC Bacteria; Actinobacteria; Pseudonocardiales; Pseudonocardiaceae; OC Pseudonocardia. OX NCBI_TaxID=1096856 {ECO:0000313|EMBL:ALL80736.1, ECO:0000313|Proteomes:UP000066228}; RN [1] {ECO:0000313|EMBL:ALL80736.1, ECO:0000313|Proteomes:UP000066228} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=EC080619-01 {ECO:0000313|EMBL:ALL80736.1, RC ECO:0000313|Proteomes:UP000066228}; RX PubMed=26535611; DOI=10.1021/jacs.5b09794; RA Van Arnam E.B., Sit C.S.; RT "A Rebeccamycin Analog Provides Plasmid-Encoded Niche Defense."; RL J. Am. Chem. Soc. 137:14272-14274(2015). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP012184; ALL80736.1; -; Genomic_DNA. DR RefSeq; WP_060573200.1; NZ_CP012184.1. DR EnsemblBacteria; ALL80736; ALL80736; AD017_05065. DR KEGG; pecq:AD017_05065; -. DR PATRIC; fig|1096856.3.peg.1064; -. DR KO; K03665; -. DR Proteomes; UP000066228; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 2. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000313|EMBL:ALL80736.1}; KW Complete proteome {ECO:0000313|Proteomes:UP000066228}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900, KW ECO:0000313|EMBL:ALL80736.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000066228}. FT DOMAIN 254 423 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 500 AA; 53603 MW; 5DFE04C437F46508 CRC64; MTEAHTAAVP STSAGSAVPS AGELDLEERS SLRRIHGLST ELTDITEVEY RRLQLERVVL VGVWTEGSAE QADASLAELA RLAETAGSEV LDGLVQRRST PDPATFIGSG KVDELSTVVR ATGADTVICD GELSPGQLRQ LEERLKVKVI DRTALILDIF AQHARSRDGK AQVELAQLSY LLPRLRGWGE ALSRQVGGRA AGGVGIGGRG PGETKIELDR RRIRARMSKL RREIGAMRQV RETQRGNRTR NEVPSVAIVG YTNAGKSSLL NQLTDAGVLV QDSLFATLDP TTRRSETPDG RAYTLTDTVG FVRHLPHQLV EAFRSTLEEA ARADLLVHVV DGSDPLPDDQ IAAVRQVLVE IGEEQGGTMP RELLVINKVD AAGDLALARL RHAQPEAVFV SAHDGSGIGK LRDRIAELLP RPEYEVDLLL PYTEGALVAR LHDEGEILAE EHTGEGTRVR ARVGPELGTA VLPYAVGGTA TVPADTDPAG TDLPATAAGH // ID A0A0P0UQQ7_9GAMM Unreviewed; 436 AA. AC A0A0P0UQQ7; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 07-JUN-2017, entry version 14. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:BAS67339.1}; GN ORFNames=BSEPE_0325 {ECO:0000313|EMBL:BAS67339.1}; OS endosymbiont of Bathymodiolus septemdierum str. Myojin knoll. OC Bacteria; Proteobacteria; Gammaproteobacteria; OC sulfur-oxidizing symbionts. OX NCBI_TaxID=1303921 {ECO:0000313|EMBL:BAS67339.1, ECO:0000313|Proteomes:UP000067399}; RN [1] {ECO:0000313|EMBL:BAS67339.1, ECO:0000313|Proteomes:UP000067399} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Myojin Knoll {ECO:0000313|EMBL:BAS67339.1, RC ECO:0000313|Proteomes:UP000067399}; RA Fujiwara Y., Takai K., Uematsu K., Tsuchida S., Hunt J.C., RA Hashimoto J.; RT "Phylogenetic characterization of endosymbionts in three hydrothermal RT vent mussels: influence on host distributions."; RL Mar. Ecol. Prog. Ser. 208:147-155(2000). RN [2] {ECO:0000313|EMBL:BAS67339.1, ECO:0000313|Proteomes:UP000067399} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Myojin Knoll {ECO:0000313|EMBL:BAS67339.1, RC ECO:0000313|Proteomes:UP000067399}; RX PubMed=26418631; DOI=10.1038/ismej.2015.176; RA Ikuta T., Takaki Y., Nagai Y., Shimamura S., Tsuda M., Kawagucci S., RA Aoki Y., Inoue K., Teruya M., Satou K., Teruya K., Shimoji M., RA Tamotsu H., Hirano T., Maruyama T., Yoshida T.; RT "Heterogeneous composition of key metabolic gene clusters in a vent RT mussel symbiont population."; RL ISME J. 10:990-1001(2016). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AP013042; BAS67339.1; -; Genomic_DNA. DR RefSeq; WP_066043134.1; NZ_AP013042.1. DR EnsemblBacteria; BAS67339; BAS67339; BSEPE_0325. DR KEGG; ebh:BSEPE_0325; -. DR KO; K03665; -. DR Proteomes; UP000067399; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000067399}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000067399}. FT DOMAIN 205 372 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 436 AA; 48951 MW; 522F4108DAD95EDD CRC64; MELFDKQKDA VGQGERTLLV YVELPNNRHI HNGMDEFAEL ASSSGLSVLK NLKVSRNNAK AKHFIGSGKV EELAELVKEL ELDLVIFSAE LSPSQERNLE ADLKCQVMDR TGLILDIFSL RASSFEGKLQ VELAQLRHLS TRLVRGWTHL ERQKGGIGMR GPGETQLETD KRLIAVRIKN ITKRLDKVHK QRDLGRKSRI KNELPMVALA GYTNAGKSTL FNTITKAEVF ANDQLFATLD STIRRVILPA SGEAVIADTV GFIQNLPHDL VAAFKSTLEE TSQANVLLHV VDAADEYNIE KIEQVQEIIT DIGADKVPSI LVMNKIDCVE NLEPRLDRDE NGRIFRVWIS AQTGDGIDLL YQALAEQLSG MMTRAKIQID VKSAYIRSEI HNIGYIHNEK VDDFGQWVLE INVTHHYLSK ILSLKGVTLL WEQKAQ // ID A0A0P1C1X0_9CYAN Unreviewed; 541 AA. AC A0A0P1C1X0; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=apha_03503 {ECO:0000313|EMBL:CEJ48417.1}; OS Chrysosporum ovalisporum. OC Bacteria; Cyanobacteria; Nostocales; Aphanizomenonaceae; Chrysosporum. OX NCBI_TaxID=75695 {ECO:0000313|EMBL:CEJ48417.1, ECO:0000313|Proteomes:UP000051809}; RN [1] {ECO:0000313|EMBL:CEJ48417.1, ECO:0000313|Proteomes:UP000051809} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=UAM-MAO {ECO:0000313|EMBL:CEJ48417.1, RC ECO:0000313|Proteomes:UP000051809}; RA Zhu J., Qi W., Song R.; RL Submitted (NOV-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CDHJ01000309; CEJ48417.1; -; Genomic_DNA. DR EnsemblBacteria; CEJ48417; CEJ48417; apha_03503. DR Proteomes; UP000051809; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000051809}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000051809}. FT DOMAIN 368 538 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 327 361 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 541 AA; 59618 MW; 706CD801733E425B CRC64; MCAYLNRRGQ VIRVGVGTPR QTQIPPLELP RYGAERLSGI RCIATNLKAE PPNEGALTAM GLQRLDALVV LNITGTGFTR RGGGSTGYVK ETYLAHLVSN NNHPLSTSPS GISEKLSREA SCKDNSPADE LALYSRVSPP MSLDMLCQQD FIELVEGLEA EFQRQFVAQE VAADHDRVII VGLMTDSTSV QRFQDTISEL ARLVDTAGGD VLQTLQQKRS RIHPQTVVGE GKVQEIALTA QTLGANLVVF DRDLSPAQVR NLERKIGIRV VDRTEVILDI FAQRAQSRAG KLQVELAQLG YMMPRLSGRG LDMSRLGGGI GTRGPGETKL ETERRAIQKR ISRLQQEVNQ LQAHRSRLRQ RRQHQEVPSV ALVGYTNAGK STLLNALTNA EVYTADQLFA TLDPTTRRLV ISHGESGETQ EILLTDTVGF IHELPASLRD AFRATLEEVT EADALLHLVD LSHPAWLSHI RSVREILAQM PVTPGPALVI FNKIDQVDSA TLALAREEFP LAVFISASQR LGLETLRQRL TQLIQYAVDC R // ID A0A0P1FH40_9RHOB Unreviewed; 424 AA. AC A0A0P1FH40; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 07-JUN-2017, entry version 13. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:CUH53562.1}; GN ORFNames=SHM7688_03016 {ECO:0000313|EMBL:CUH53562.1}; OS Shimia marina. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae. OX NCBI_TaxID=321267 {ECO:0000313|EMBL:CUH53562.1, ECO:0000313|Proteomes:UP000054823}; RN [1] {ECO:0000313|EMBL:CUH53562.1, ECO:0000313|Proteomes:UP000054823} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CECT 7688 {ECO:0000313|EMBL:CUH53562.1, RC ECO:0000313|Proteomes:UP000054823}; RG Swine Surveillance; RL Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CYPW01000027; CUH53562.1; -; Genomic_DNA. DR RefSeq; WP_058240710.1; NZ_CYPW01000027.1. DR EnsemblBacteria; CUH53562; CUH53562; SHM7688_03016. DR Proteomes; UP000054823; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000054823}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000054823}. FT DOMAIN 203 373 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 424 AA; 47076 MW; 0880AF86477A7E31 CRC64; MEHDTQVTRA WVLHPDITSA EQRREASFAL EEAISLAAAL PELEVVGSNV VRLSKAQPGK LFGSGKIEEL KALFKANEVE LVLIDGPVTP VQQRNLEKEW KVKLLDRTGL ILEIFSDRAR TREGVLQVEM AALSYQRTRL VRAWTHLERQ RGGLGFVGGP GETQIEADRR AIDDQLVRLR RQLAKVVKTR ELHRKARAKV PFPIVALVGY TNAGKSTLFN RVTGADVMAK DMLFATLDPT MRAVELPNNG PEVILSDTVG FISDLPTQLV AAFRATLEEV LAADLVLHVR DIAHPETEHQ AEDVRSILET LGMSEETPQI EVWNKIDLLD ADDREAVVAR AEREEGIFAV SAVSGQGLDD MFAAIAKALA SEKTREVLSL SFSEGKARAW LFKEGVVEAE TQTDEGFEIE VLWSAKQRAQ YQTL // ID A0A0P1FP73_THAGE Unreviewed; 425 AA. AC A0A0P1FP73; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 07-JUN-2017, entry version 13. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:CUH62902.1}; GN ORFNames=TG4357_00365 {ECO:0000313|EMBL:CUH62902.1}; OS Thalassobius gelatinovorus (Ruegeria gelatinovora). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae; Thalassobius. OX NCBI_TaxID=53501 {ECO:0000313|EMBL:CUH62902.1, ECO:0000313|Proteomes:UP000051587}; RN [1] {ECO:0000313|EMBL:CUH62902.1, ECO:0000313|Proteomes:UP000051587} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CECT 4357 {ECO:0000313|EMBL:CUH62902.1, RC ECO:0000313|Proteomes:UP000051587}; RG Swine Surveillance; RL Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CYSA01000005; CUH62902.1; -; Genomic_DNA. DR RefSeq; WP_058261174.1; NZ_FOFW01000003.1. DR EnsemblBacteria; CUH62902; CUH62902; TG4357_00365. DR Proteomes; UP000051587; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000051587}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000051587}. FT DOMAIN 204 374 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 425 AA; 47824 MW; 2DA18E3EB39794CE CRC64; METHEREATR AWVLHPDLKS DAKRRPAPDA LAEAVALAAA LPDLEVVGAE SVRLQRPHPG LLFGTGKIEE LKARIQAAEV DLVLIDGPVS PVQQRNLEKK WDVKLLDRTG LILEIFSDRA RTREGVLQVE MAALKYQRTR LVRAWTHLER QRGGLGFVGG PGETQIEADR RAIDEQLVRL RRQLDKVVKT RELHRSARAK VPFPVVALVG YTNAGKSTLF NRLTGAEVMA KDMLFATLDP TMRRVDLPEG GPEVILSDTV GFISDLPTEL VASFRATLEE VLSANLILHV RDISHPETEN QCRNVLEIME SLGTDPDVPV LELWNKIDLL PEDQRSALQQ RAAREDRVFT LSAITGEGIP ELMQAITDQL ANETHLSEVT LKFSDGRKRA WLFDQDIVET ENQTETGFDL TVRWTARQEK RFRDL // ID A0A0P1G5T1_9RHOB Unreviewed; 424 AA. AC A0A0P1G5T1; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 05-JUL-2017, entry version 14. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:CUH76951.1}; GN ORFNames=TRN7648_01213 {ECO:0000313|EMBL:CUH76951.1}; OS Tropicibacter naphthalenivorans. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae; Tropicibacter. OX NCBI_TaxID=441103 {ECO:0000313|EMBL:CUH76951.1, ECO:0000313|Proteomes:UP000054935}; RN [1] {ECO:0000313|EMBL:CUH76951.1, ECO:0000313|Proteomes:UP000054935} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CECT 7648 {ECO:0000313|EMBL:CUH76951.1, RC ECO:0000313|Proteomes:UP000054935}; RG Swine Surveillance; RL Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CYSE01000002; CUH76951.1; -; Genomic_DNA. DR RefSeq; WP_058246737.1; NZ_FWXX01000002.1. DR EnsemblBacteria; CUH76951; CUH76951; TRN7648_01213. DR Proteomes; UP000054935; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000054935}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000054935}. FT DOMAIN 204 373 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 424 AA; 47388 MW; F69C9D6562885A6A CRC64; MNEHETHVTR AWVLHPDIKS DRGRRDAHMA LEEAVSLAHA LPDLEVIGSE VVSLPKPHAG MLFGSGKIAE LKTRIKDAEV ELVLVDGPVT PVQQRNLEKE WGVKLLDRTG LILEIFSDRA ATREGVLQVE MAHLSYQRTR LVRAWTHLER QRGGLGFVGG PGETQIEADR RAIDEQLVRL RRQLDKVVKT RELHRKARAK VPYPIVALVG YTNAGKSTLF NRLTGADVMA KDMLFATLDP TMRRVQLPTG ADVILSDTVG FISDLPTELV AAFRATLEEV LAADVIVHVR DISHPETEEQ ARDVTTILDS LGVDEQTTQL ELWNKVDRLD LDTADALRAR ASRDDGTFVT SALSGEGLDA FLDAVTHALG EEKRRDQLVL PYDEGRKRAW LFQKGLVEEE TQDEDGFHLT LSWSAKDRAQ FESL // ID A0A0P1GY64_9RHOB Unreviewed; 423 AA. AC A0A0P1GY64; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 07-JUN-2017, entry version 13. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:CUH82221.1}; GN ORFNames=TRM7557_03817 {ECO:0000313|EMBL:CUH82221.1}; OS Tropicibacter multivorans. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae; Tropicibacter. OX NCBI_TaxID=928856 {ECO:0000313|EMBL:CUH82221.1, ECO:0000313|Proteomes:UP000052022}; RN [1] {ECO:0000313|EMBL:CUH82221.1, ECO:0000313|Proteomes:UP000052022} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CECT 7557 {ECO:0000313|EMBL:CUH82221.1, RC ECO:0000313|Proteomes:UP000052022}; RG Swine Surveillance; RL Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CYSD01000043; CUH82221.1; -; Genomic_DNA. DR RefSeq; WP_058291789.1; NZ_FOMC01000005.1. DR EnsemblBacteria; CUH82221; CUH82221; TRM7557_03817. DR Proteomes; UP000052022; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000052022}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000052022}. FT DOMAIN 203 372 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 423 AA; 47330 MW; FA8AA5B32B809EA0 CRC64; MEHERKRTRA WVLHPDIKSD RARRDPEAAR AEAVSLAAAL PDLDVIGSNV VRLPKAHPGM LFGSGKIDEL AAILKAEEIE LVLIDGPVSP VQQRNLEKAW KVKLLDRTGL ILEIFSDRAR TREGVLQVEM AALSYQRTRL VRAWTHLERQ RGGLGFVGGP GETQIEADRR AIDEQLVRLR RQLEKVVKTR TLHRAARAKV PYPIVALVGY TNAGKSTLFN RLTGAEVMAK DMLFATLDPT MRRVVLPDGP EVILSDTVGF ISDLPTELVA AFRATLEEVL AADVILHVRD ISHEETENQA KDVEAILASL GVDEHRPQIE VWNKLDQLSD EEAEACRQRA DRLDDLHAIS ALTGEGLDPL LEDIATKLQG VRREEVLTLG FSQGRERAWL FKQDVVQSED QSEEGFVLTV LWTDKQKAKF EAL // ID A0A0P1H8K2_9RHOB Unreviewed; 425 AA. AC A0A0P1H8K2; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 05-JUL-2017, entry version 13. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:CUH83157.1}; GN ORFNames=TM5383_00340 {ECO:0000313|EMBL:CUH83157.1}; OS Thalassobius mediterraneus. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae; Thalassobius. OX NCBI_TaxID=340021 {ECO:0000313|EMBL:CUH83157.1, ECO:0000313|Proteomes:UP000051681}; RN [1] {ECO:0000313|EMBL:CUH83157.1, ECO:0000313|Proteomes:UP000051681} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CECT 8383 {ECO:0000313|EMBL:CUH83157.1, RC ECO:0000313|Proteomes:UP000051681}; RG Swine Surveillance; RL Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CYSF01000002; CUH83157.1; -; Genomic_DNA. DR RefSeq; WP_058317321.1; NZ_FTNX01000008.1. DR EnsemblBacteria; CUH83157; CUH83157; TM5383_00340. DR Proteomes; UP000051681; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000051681}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000051681}. FT DOMAIN 204 374 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 425 AA; 47677 MW; 113E84CA86CF4AA0 CRC64; METHERIATR AWVLHPDLKS DKNRREADYA LAEAISLAAA LPDLEVVGST KVPLPRAHPG YLFGSGKIEE LKQLLKENEV ELVLIDGPVT PVQQRNLEKA WKVKLLDRTG LILEIFSDRA RTREGVLQVE MAALSYQRTR LVRAWTHLER QRGGLGFVGG PGETQIEADR RAIDEQLVRL RRQLDKVVKT RELHRAARAK VPFPVVALVG YTNAGKSTLF NHLTGADVMA KDMLFATLDP TMRRVDLPDN GPEVIMSDTV GFISDLPTEL VASFRATLEE VLSANLILHV RDISHSETEG QAKNVLSIMD SLGVGKDTPV LEVWNKIDLL DDDNRAALNE RADREEDIFA ISAITGEGQT KLLDAVKAKL ASETHESQIS LTFAEGRKRA WLFQEDLVLE EEQTESGFDL TVRWTARQEK RFRDL // ID A0A0P1HNF9_9RHOB Unreviewed; 423 AA. AC A0A0P1HNF9; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 07-JUN-2017, entry version 12. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:CUH88391.1}; GN ORFNames=PH5382_02327 {ECO:0000313|EMBL:CUH88391.1}; OS Phaeobacter sp. CECT 5382. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae; Phaeobacter. OX NCBI_TaxID=1712645 {ECO:0000313|EMBL:CUH88391.1, ECO:0000313|Proteomes:UP000050782}; RN [1] {ECO:0000313|EMBL:CUH88391.1, ECO:0000313|Proteomes:UP000050782} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CECT 5382 {ECO:0000313|EMBL:CUH88391.1, RC ECO:0000313|Proteomes:UP000050782}; RG Swine Surveillance; RL Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CYSG01000009; CUH88391.1; -; Genomic_DNA. DR RefSeq; WP_058334521.1; NZ_CYSG01000009.1. DR EnsemblBacteria; CUH88391; CUH88391; PH5382_02327. DR Proteomes; UP000050782; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000050782}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000050782}. FT DOMAIN 203 372 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 423 AA; 47261 MW; A4270F1DC256D5F6 CRC64; MEHDRIRTRA WVLHPDIKSD HGRRPAEPAL AEGVALAEAL PDLDVIGSSV VRLPKAHAGM LFGSGKIEEL KAIFQGEEID LVLIDGPVSP VQQRNLEKAW KVKILDRTGL ILEIFSDRAR TREGVLQVEM AALSYQRTRL VRAWTHLERQ RGGLGFVGGP GETQIEADRR AIDEHLVRLR RQLEKVVKTR TLHRAARAKI PYPIVALVGY TNAGKSTLFN RLTGAEVMVK DMLFATLDPT MRRVELPDGP EIILSDTVGF ISDLPTELVA AFRATLEEVL AADVILHVRD ISHDESQNQA NDVKAILTSL GVDENRAQIE VWNKLDQLPE DVAEARRQRA AREEGIHAIS ALTGEGIDGL LDDIAIKLQG VRHLEELTLS FAQGKQRAWL FSQDLVISEE QTEDGFQLTV RWTDRQKAQF KAL // ID A0A0P1I6A3_9RHOB Unreviewed; 423 AA. AC A0A0P1I6A3; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 07-JUN-2017, entry version 12. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:CUJ93130.1}; GN ORFNames=PH7735_01562 {ECO:0000313|EMBL:CUJ93130.1}; OS Phaeobacter sp. CECT 7735. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae; Phaeobacter. OX NCBI_TaxID=1715693 {ECO:0000313|EMBL:CUJ93130.1, ECO:0000313|Proteomes:UP000051870}; RN [1] {ECO:0000313|EMBL:CUJ93130.1, ECO:0000313|Proteomes:UP000051870} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CECT 7735 {ECO:0000313|EMBL:CUJ93130.1, RC ECO:0000313|Proteomes:UP000051870}; RG Swine Surveillance; RL Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CYTW01000001; CUJ93130.1; -; Genomic_DNA. DR RefSeq; WP_058310679.1; NZ_CYTW01000001.1. DR EnsemblBacteria; CUJ93130; CUJ93130; PH7735_01562. DR Proteomes; UP000051870; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000051870}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000051870}. FT DOMAIN 203 372 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 423 AA; 47182 MW; 2E4043C03B880A46 CRC64; MEHDAQVTRA WVLHPDIYGA NQRREASFAL EEAVSLADAL AEIEVVGSTV VRLPKAHAGM LFGSGKIEEL KGLFEANDVE LVLIDGPVTP VQQRNLEKAW KVKLLDRTGL ILEIFSDRAR TREGVLQVEM AALSYQRTRL VRAWTHLERQ RGGLGFVGGP GETQIEADRR AIDDQLVRLR RQLAKVVKTR ELHRKARAKV PFPIVALVGY TNAGKSTLFN YVTGADVMAK DMLFATLDPT MRAVHLPDGP EVILSDTVGF ISDLPTELVA SFRATLEEVL AADLILHVRD IAHPDSEVQA KDVEDILTSL GVGTGTKQLE IWNKIDLLDD ERREAMNTRA ARDDEIFAIS AVTGEGLEDL FAAITTALDA KRTEEDLHLE FSQGKHRAWL FKEGVVENET QDEDGFHLRV RWTARQARKF EGL // ID A0A0P1INQ3_9RHOB Unreviewed; 423 AA. AC A0A0P1INQ3; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 07-JUN-2017, entry version 12. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:CUJ88063.1}; GN ORFNames=RUE5091_00642 {ECO:0000313|EMBL:CUJ88063.1}; OS Ruegeria sp. CECT 5091. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae; Ruegeria. OX NCBI_TaxID=1715692 {ECO:0000313|EMBL:CUJ88063.1, ECO:0000313|Proteomes:UP000051260}; RN [1] {ECO:0000313|EMBL:CUJ88063.1, ECO:0000313|Proteomes:UP000051260} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CECT 5091 {ECO:0000313|EMBL:CUJ88063.1, RC ECO:0000313|Proteomes:UP000051260}; RG Swine Surveillance; RL Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CYUD01000002; CUJ88063.1; -; Genomic_DNA. DR RefSeq; WP_058280440.1; NZ_CYUD01000002.1. DR EnsemblBacteria; CUJ88063; CUJ88063; RUE5091_00642. DR Proteomes; UP000051260; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000051260}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000051260}. FT DOMAIN 203 372 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 423 AA; 47447 MW; C291DB66AC8BCF19 CRC64; MEHDRTQTRA WVLHPEIKSD EQRRVPEPAL EEAVALAAAL PDLDVIGSEI VRLPRAQPGL LFGSGKIEEL AERLHDHEIE LVLIDGPVSP VQQRNLEKAW KVKILDRTGL ILEIFSDRAR TREGVLQVEM AALSYQRTRL VRAWTHLERQ RGGLGFVGGP GETQIEADRR AIDEQLVRLR RQLQKVVKTR TLHRAARAKV PYPIVALVGY TNAGKSTLFN RLTGAEVMAK DMLFATLDPT MRRVELPDGP EVILSDTVGF ISNLPTELVA AFRATLEEVL GADLVVHVRD ISHEDTEAQA QDVETILTSL GLDEDRPRLE VWNKIDLVND DEREAAFKRA DRDPSVFAIS AVTGEGVEPL LAEIATKLQG ARHQETLSLD FAEGNKRAWL FRQDVVRSEQ QTEDGFEITV LWTDRQAAQF ATL // ID A0A0P1IP77_9RHOB Unreviewed; 424 AA. AC A0A0P1IP77; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 10-MAY-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:CUK25335.1}; GN ORFNames=TA5114_01133 {ECO:0000313|EMBL:CUK25335.1}; OS Thalassobius sp. CECT 5114. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae; Thalassobius. OX NCBI_TaxID=1715690 {ECO:0000313|EMBL:CUK25335.1, ECO:0000313|Proteomes:UP000051184}; RN [1] {ECO:0000313|EMBL:CUK25335.1, ECO:0000313|Proteomes:UP000051184} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CECT 5114 {ECO:0000313|EMBL:CUK25335.1, RC ECO:0000313|Proteomes:UP000051184}; RG Swine Surveillance; RL Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CYUE01000012; CUK25335.1; -; Genomic_DNA. DR EnsemblBacteria; CUK25335; CUK25335; TA5114_01133. DR Proteomes; UP000051184; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000051184}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000051184}. FT DOMAIN 204 373 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 424 AA; 47077 MW; B370CB0F991B855B CRC64; MMEHETHVTR AWVLRPEVKS ADQKRDASSA LEEAVSLAAA LPNLEVVGAD VVRLQKIQPG KLFGSGKIEE LAAKLKAEEV ELVLIDGPVT PVQQRNLEKE WKVKLLDRTG LILEIFSDRA RTREGVLQVE MAALSYQRTR LVRAWTHLER QRGGLGFVGG PGETQIEADR RAIDDQLVRL RRQLAKVVKT RELHRGARAK VPYPIVALVG YTNAGKSTLF NRVTGAEVLA KDMLFATLDP TMRRLELTDG PEVILSDTVG FISDLPTELV AAFRATLEEV LAADIILHVR DISHPESDNQ AEDVHTILTQ LGVSEDIPQL EVWNKIDLLE EDDIAAMHAK AARADDIYSI SAITGEGIDL LLAEVTKRLQ GDVKVEVLNL PFSAGKERAW LFAENIVEDE TQTDTGFDIT VKWTPRQAAK FKSL // ID A0A0P4UPF3_9CYAN Unreviewed; 506 AA. AC A0A0P4UPF3; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=NIES2104_17110 {ECO:0000313|EMBL:GAP95191.1}; OS Leptolyngbya sp. NIES-2104. OC Bacteria; Cyanobacteria; Synechococcales; Leptolyngbyaceae; OC Leptolyngbya. OX NCBI_TaxID=1552121 {ECO:0000313|EMBL:GAP95191.1, ECO:0000313|Proteomes:UP000052243}; RN [1] {ECO:0000313|EMBL:GAP95191.1, ECO:0000313|Proteomes:UP000052243} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NIES-2104 {ECO:0000313|EMBL:GAP95191.1, RC ECO:0000313|Proteomes:UP000052243}; RX PubMed=26494835; DOI=10.1093/dnares/dsv022; RA Shimura Y., Hirose Y., Misawa N., Osana Y., Katoh H., Yamaguchi H., RA Kawachi M.; RT "Comparison of the terrestrial cyanobacterium Leptolyngbya sp. NIES- RT 2104 and the freshwater Leptolyngbya boryana PCC 6306 genomes."; RL DNA Res. 22:403-412(2015). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:GAP95191.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BBWW01000001; GAP95191.1; -; Genomic_DNA. DR EnsemblBacteria; GAP95191; GAP95191; NIES2104_17110. DR Proteomes; UP000052243; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000052243}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000052243}. FT DOMAIN 334 504 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 293 327 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 506 AA; 56292 MW; 1E9C4899DFAC0034 CRC64; MNRRGQVIRV GVGTLRQTQI PMLELPRYGA ERLCGIRCIA TQLKQDPPGE SMLTVMALQR LDAYVALTLT GGGFERRGGG ATGYVRGAYL AHLVPHPEAN WTISPPLSLD IVAEQDFLAL VEGLEEEFRR EYVAQQVDRD HDQVLIVGIQ TDDQSPQVFK TGIQELARLV ETAGGEVLQT MSQKRPRPHP QTVVGEGKVQ EITLAAQTVG ANLIVFDRDL SPAQIRNLEM QIGIRIVDRT EVILDIFAQR AQSGAGKLQV ELAQLEYMLP RLTGRGQAMS RLGGGIGTRG PGETKLETER RSIQRRITRL QREVNQLQAH RARLRQRRQH EEVPSIAVVG YTNAGKSTLL NALTNAEVYT ADQLFATLDP TTRRLTVSDL ETYKNTELLL TDTVGFIHEL PPSLMDAFRA TLEEVTEADA LLHVVDLSHP AWQSQIRAVM QILSEMPITP GPALLAFNKI DQVDAERLAI AREEFPQAAF ISANERLGLE TLRQRLCQLV RYAMTN // ID A0A0P4V3P4_9CYAN Unreviewed; 554 AA. AC A0A0P4V3P4; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 07-JUN-2017, entry version 12. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=NIES2104_46830 {ECO:0000313|EMBL:GAP98130.1}; OS Leptolyngbya sp. NIES-2104. OC Bacteria; Cyanobacteria; Synechococcales; Leptolyngbyaceae; OC Leptolyngbya. OX NCBI_TaxID=1552121 {ECO:0000313|EMBL:GAP98130.1, ECO:0000313|Proteomes:UP000052243}; RN [1] {ECO:0000313|EMBL:GAP98130.1, ECO:0000313|Proteomes:UP000052243} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NIES-2104 {ECO:0000313|EMBL:GAP98130.1, RC ECO:0000313|Proteomes:UP000052243}; RX PubMed=26494835; DOI=10.1093/dnares/dsv022; RA Shimura Y., Hirose Y., Misawa N., Osana Y., Katoh H., Yamaguchi H., RA Kawachi M.; RT "Comparison of the terrestrial cyanobacterium Leptolyngbya sp. NIES- RT 2104 and the freshwater Leptolyngbya boryana PCC 6306 genomes."; RL DNA Res. 22:403-412(2015). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:GAP98130.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BBWW01000001; GAP98130.1; -; Genomic_DNA. DR RefSeq; WP_059000239.1; NZ_BBWW01000001.1. DR EnsemblBacteria; GAP98130; GAP98130; NIES2104_46830. DR Proteomes; UP000052243; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000052243}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000052243}. FT DOMAIN 377 547 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 336 373 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 554 AA; 62472 MW; B2B93E3AE19C48ED CRC64; MATVYGQLQG IRSTHIKQIE KLYDTRFASD SLITSEFAEQ LAALSHLIHQ PICCYVNRRG QVLRVGIGTP MQTRLPESEL PRRSRDRFSG IRCTVAQFQP PDTSAFIAML RQRLDAIVVL TLQDKSIKQS YLLHLVPDID QPWQVESMSL KTLIEQDADQ LIEDWEKDIQ DAGFDLSQTV EFDHDRALLV GLQTDKMSDQ RFQDSIDELT RLVESAKGEV LGVVQQKRSH PHPQTVIGQG KVEELTLEAQ RLGANVIVFN QDISATQARN LEAQIGLRVV DRTEVILDIF AQRARSQAGK LQVELAQLEY TLPRLRGRGQ DMSRLGAGIG TRGPGETKLE TERRTIQRKI TQLQQEVNQL QAHRARLRQQ RDRQDSPTIA LVGYTNAGKS TLLNVLTRAE VYTADQLFAT LDPTTRRLTI TDPNTHDRKN LLLTDTVGFI HDLPPALMDA FRATLEEVTE SEALLHVLDL SHPAWEQHLQ SVNTVLSELP ATPPDAVLVF NKIDRVKPET LSQVQQSYPD AIFISATERM GLEELEQRLL KLVDTLTVSE TSVQ // ID A0A0P6GN08_9CRUS Unreviewed; 507 AA. AC A0A0P6GN08; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 07-JUN-2017, entry version 7. DE SubName: Full=GTP-binding protein {ECO:0000313|EMBL:JAN62562.1}; DE SubName: Full=Putative GTP-binding protein 6 {ECO:0000313|EMBL:KZS19448.1}; GN ORFNames=APZ42_014342 {ECO:0000313|EMBL:KZS19448.1}; OS Daphnia magna. OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Crustacea; Branchiopoda; OC Diplostraca; Cladocera; Anomopoda; Daphniidae; Daphnia. OX NCBI_TaxID=35525 {ECO:0000313|EMBL:JAN62562.1}; RN [1] {ECO:0000313|EMBL:JAN62562.1} RP NUCLEOTIDE SEQUENCE. RA Gilbert D.G.; RT "EvidentialGene: Evidence-directed Construction of Complete mRNA RT Transcriptomes without Genomes."; RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:KZS19448.1, ECO:0000313|Proteomes:UP000076858} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Xinb3 {ECO:0000313|EMBL:KZS19448.1, RC ECO:0000313|Proteomes:UP000076858}; RC TISSUE=Complete organism {ECO:0000313|EMBL:KZS19448.1}; RA Gilbert D.G., Choi J.-H., Mockaitis K., Colbourne J., Pfrender M.; RT "EvidentialGene: Evidence-directed Construction of Genes on Genomes."; RL Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GDIQ01032175; JAN62562.1; -; Transcribed_RNA. DR EMBL; LRGB01000389; KZS19448.1; -; Genomic_DNA. DR Proteomes; UP000076858; Unassembled WGS sequence. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR CDD; cd01878; HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000076858}; KW Reference proteome {ECO:0000313|Proteomes:UP000076858}. FT DOMAIN 283 444 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 507 AA; 57292 MW; 55A31E346D242A79 CRC64; MTVNLIRCGS VIIRMTTCSS NQNLSALLKS PRHASLCVRS LTGDRKSEDD YFKLELCSEE NNQDNHDYKD LVHRMHLFPG IRNQVVIVQP FVKWGPKKNE LTTPDLMLEE AKALIDSLPN WKCIDTLKVP VESLEKKNVF GSGQFESLQK KIVKNPNISA VFVNVNLLRG IQRKELTTAF RVPIYDRYSI VLQIFKERAK TREAKLQVAF AEIPYLRSCL VGLQKGSKGD GRGSATIVGD GESYYDSKLH LLERRELKIK KELEKMHKKR ALLKYERKKR EFPVVAIVGY TNSGKTTLIK SLTGDSNMQP QDGLFATLDV TVHAFKLPCN LTVLLVDTVG FISNIPLNLI AAFKATLNDA MDADMIIHLQ DASHPDKENQ IAAVNDTLKQ LNIDSAKPIF QVENKIDKIR PENVSASCLQ ISAQYGTGLE EMIELIQTKL LEVTNHKLLR LMVPSGSSEY SWLHKEATVV DYSHTENPQY LILDVLITPT VFGKLRSNYP DIRILNK // ID A0A0P6SSP7_9STRE Unreviewed; 412 AA. AC A0A0P6SSP7; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 07-JUN-2017, entry version 13. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=AKK44_03620 {ECO:0000313|EMBL:KPJ22745.1}; OS Streptococcus phocae. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=119224 {ECO:0000313|EMBL:KPJ22745.1, ECO:0000313|Proteomes:UP000049578}; RN [1] {ECO:0000313|EMBL:KPJ22745.1, ECO:0000313|Proteomes:UP000049578} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51973 {ECO:0000313|EMBL:KPJ22745.1, RC ECO:0000313|Proteomes:UP000049578}; RA Avendano-Herrera R.; RT "Genome sequence of Streptococcus phocae subsp. phocae ATCC 51973T RT isolated from liver specimen obtained from seal."; RL Submitted (AUG-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KPJ22745.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LHQM01000010; KPJ22745.1; -; Genomic_DNA. DR RefSeq; WP_054278548.1; NZ_LHQM01000010.1. DR EnsemblBacteria; KPJ22745; KPJ22745; AKK44_03620. DR PATRIC; fig|119224.3.peg.253; -. DR Proteomes; UP000049578; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000049578}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}. FT DOMAIN 199 359 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 412 AA; 46547 MW; 1621728421425EBD CRC64; MIETQVNRER AILVGVALQT TDNFDMSMAE LANLAKTAGA DVVDTFTQKR DRYDSKTFIG SGKLDDIKAV VEANEIDTVI VNNRLTARQN ANLEAALEVK VIDRMQLILD IFAMRARSHE GKLQVHLAQL NYLLPRLVGQ GVMLSRQAGG IGSRGPGESQ LELNRRSIRQ QIIEIERQLA VVAKNRQTVR DRRVSSDTFK VGLIGYTNAG KSTIMNVLTD NKQYEANELF ATLDATTKQL YLQNQYQATL TDTVGFIQDL PTELVAAFKS TLEESRHVDL LLHVIDASDP NHSEHEKVVL DILSDLDMLD IPRLAIYNKM DLADGLTATA FPNVRISASD KQSKDVLRRL IIDQIRDIFE PFSIKVHQDK AYKLYALNKI ALLDNYRFDD ETEDISGYIS PENKWRLDEF YD // ID A0A0P6W0E2_9BACI Unreviewed; 418 AA. AC A0A0P6W0E2; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=AM506_14830 {ECO:0000313|EMBL:KPL58796.1}; OS Bacillus vietnamensis. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus. OX NCBI_TaxID=218284 {ECO:0000313|EMBL:KPL58796.1, ECO:0000313|Proteomes:UP000050398}; RN [1] {ECO:0000313|EMBL:KPL58796.1, ECO:0000313|Proteomes:UP000050398} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=UCD-SED5 {ECO:0000313|EMBL:KPL58796.1, RC ECO:0000313|Proteomes:UP000050398}; RA Lee R.D., Jospin G., Lang J.M., Coil D.A., Eisen J.A.; RT "Draft Genome Sequence of Bacillus vietnamensis UCD-SED5."; RL Submitted (AUG-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KPL58796.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LIXZ01000012; KPL58796.1; -; Genomic_DNA. DR RefSeq; WP_060673274.1; NZ_LIXZ01000012.1. DR EnsemblBacteria; KPL58796; KPL58796; AM506_14830. DR PATRIC; fig|218284.4.peg.1148; -. DR Proteomes; UP000050398; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000050398}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000050398}. FT DOMAIN 199 361 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 418 AA; 47873 MW; 48595F4C84B0EA67 CRC64; MLKNENREKV ILVGCQLDDD DVRFQYSLTE LAELTATAQG QIAATLFQKR DRIHPSTYIG KGKVEELVLL EEQFEADIII FNDELSPSQI RNLSKELKGR VIDRTQLILD IFAQRARSRE GKLQVELAQL QYLLPRLIGQ GASLSRLGGG IGTRGPGETK LESDRRHIHK RIDDIKKQLQ TIVDHRERYR GRRKRNKTFQ IALVGYTNAG KSTMFNRMSM ADSYEENQLF ATLDPMTRKM PLPSGYSTLL TDTVGFIQDL PTTLVAAFRS TLEEVKEADL LLHVVDSSNP DYSQHEKTVE SLLKDLDMDG LQQLTVYNKR DEMDPEFVPD TESDCILISA LNEEDRGKLL IKIEEIVKNH MIPYHVFVPV NEGKILSQLK SETILRKLEF REVNQVYEMT GFHLEDHPIA GSIKKFRK // ID A0A0P6WH90_9SPHN Unreviewed; 439 AA. AC A0A0P6WH90; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 05-JUL-2017, entry version 12. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=SZ64_05375 {ECO:0000313|EMBL:KPL67589.1}; OS Erythrobacter sp. SG61-1L. OC Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales; OC Erythrobacteraceae; Erythrobacter. OX NCBI_TaxID=1603897 {ECO:0000313|EMBL:KPL67589.1, ECO:0000313|Proteomes:UP000049978}; RN [1] {ECO:0000313|EMBL:KPL67589.1, ECO:0000313|Proteomes:UP000049978} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SG61-1L {ECO:0000313|EMBL:KPL67589.1, RC ECO:0000313|Proteomes:UP000049978}; RA Palumuru S., Dellas N., Pearce S.L., Warden A.C., Oakeshott J.G., RA Pandey G.; RT "Phylogenetic and kinetic characterization of a suite of RT dehydrogenases from a newly isolated bacterium, strain SG51-1L, that RT catalyze the turnover of guaiacylglycerol-beta-guaiacyl ether RT stereoisomers."; RL Appl. Environ. Microbiol. 0:0-0(2015). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KPL67589.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JXQC01000003; KPL67589.1; -; Genomic_DNA. DR EnsemblBacteria; KPL67589; KPL67589; SZ64_05375. DR PATRIC; fig|1603897.4.peg.977; -. DR Proteomes; UP000049978; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000049978}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000049978}. FT DOMAIN 209 384 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 439 AA; 48647 MW; 6AC5FADA455E5459 CRC64; MSFTDELAGE VTRGARAIVV CPDIRGQRRS EEPEARLEEA KGLALAIGIV VAEAFIVPIR DVRAATLFGE GQIERIATAC TLEEAELVIV DGALSAIQQR NLEEKLKRKV IDRTGLILEI FGERAATAEG RLQVELAHLD YQQSRLVRSW THLERQRGGF GFLGGPGETQ IEADRRMIRT RMGRLRKELD QVRKTRALHR ERRGKAPWPV IALVGYTNAG KSTLFNRVTG ADVMAEDLLF ATLDPTMRAI RLPGVEKAIL SDTVGFISDL PTQLVAAFRA TLEEVTAADI IVHVRDMANP ANGTQKTQVL EILADLGVID GEGGESRISI VEAWNKWDLL DDERRKELGE VAQGEERIVP ISAATGLGLE TLFELLGKQL TENAKTYEFV LPVSDGQRLA WLHAHGEVLA EQQVETEEGA RMRMMVRLTP KEFGRYSSL // ID A0A0P6WK32_9RHIZ Unreviewed; 514 AA. AC A0A0P6WK32; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 05-JUL-2017, entry version 12. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=ABB55_25205 {ECO:0000313|EMBL:KPL55119.1}; OS Prosthecomicrobium hirschii. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Hyphomicrobiaceae; Prosthecomicrobium. OX NCBI_TaxID=665126 {ECO:0000313|EMBL:KPL55119.1, ECO:0000313|Proteomes:UP000048984}; RN [1] {ECO:0000313|EMBL:KPL55119.1, ECO:0000313|Proteomes:UP000048984} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=16 {ECO:0000313|EMBL:KPL55119.1, RC ECO:0000313|Proteomes:UP000048984}; RA Jackson K.R., Lunt B.L., Fisher J.N.B., Gardner A.V., Bailey M.E., RA Deus L.M., Earl A.S., Gibby P.D., Hartmann K.A., Liu J.E., Manci A.M., RA Nielsen D.A., Solomon M.B., Breakwell D.P., Burnett S.H., Grose J.H.; RL Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:KPL55119.1, ECO:0000313|Proteomes:UP000048984} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=16 {ECO:0000313|EMBL:KPL55119.1, RC ECO:0000313|Proteomes:UP000048984}; RA Daniel J., Givan S.A., Brun Y.V., Brown P.J.; RT "Draft Genome Sequence of Prosthecomicrobium hirschii ATCC 27832."; RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KPL55119.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LJYW01000001; KPL55119.1; -; Genomic_DNA. DR EnsemblBacteria; KPL55119; KPL55119; ABB55_25205. DR Proteomes; UP000048984; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000048984}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000048984}. FT DOMAIN 276 451 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 235 269 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 514 AA; 56142 MW; 5E6356C4757FFEE8 CRC64; MTRKRAGGGS GSGPGDDANR TGIGPQAGQA PVPPDETAFD SDTSDIDPIE STGRRSTGRA PQSRLAEAVR AIVVVPVRTD IRERAEPSET GETPRPQRSV AARREEAVGL AAAIDLDVVE GLVVRLSQPR PATLIGQGKV DEIKASVEAN GVGLVIVDHP LSPIQQRNLE KAWNAKVLDR TGLILEIFGE RARTREGRLQ VELAHLNYQK SRLVRSWTHL ERQRGGFGFL GGPGETQIEA DRRVITERIA KLEKELEGVT RTRALHRKTR KKVPHPVVAL VGYTNAGKST LFNRLTDAGV FAKDLLFATL DPTLRRVRLP HGGEMILSDT VGFVSDLPTH LVAAFRATLE EVIEADLILH VRDIAHEDTL AQARDVEDVL RQLGVDPRDP QRMIEVLNKI DLLDPEYREK LVAEGQRAQA DGLVTIPASA ATGEGLDRLL GLIEERLNRD RSSFRLSLPP TEGELIAWLH RSTEVLARTD GAEAVTLQVR VPDKALDLFR SRAGRFITGA GAKA // ID A0A0P6XD13_9CHLR Unreviewed; 447 AA. AC A0A0P6XD13; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 07-JUN-2017, entry version 12. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=AC812_15080 {ECO:0000313|EMBL:KPL73112.1}; OS Bellilinea caldifistulae. OC Bacteria; Chloroflexi; Anaerolineae; Anaerolineales; Anaerolineaceae; OC Bellilinea. OX NCBI_TaxID=360411 {ECO:0000313|EMBL:KPL73112.1, ECO:0000313|Proteomes:UP000050514}; RN [1] {ECO:0000313|EMBL:KPL73112.1, ECO:0000313|Proteomes:UP000050514} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=GOMI-1 {ECO:0000313|EMBL:KPL73112.1, RC ECO:0000313|Proteomes:UP000050514}; RA Hemp J., Ward L.M., Pace L.A., Fischer W.W.; RT "Draft genome of Bellilinea caldifistulae DSM 17877."; RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KPL73112.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LGHJ01000021; KPL73112.1; -; Genomic_DNA. DR RefSeq; WP_061917220.1; NZ_LGHJ01000021.1. DR EnsemblBacteria; KPL73112; KPL73112; AC812_15080. DR PATRIC; fig|360411.5.peg.1796; -. DR Proteomes; UP000050514; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000050514}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000050514}. FT DOMAIN 219 385 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 178 215 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 447 AA; 50106 MW; 86D979B67603CA3A CRC64; MAKKIAEPTQ TPRERAILVG VDLIGDPGLL PLEDSLAELA LLADTAEVEV LGEVTQRLDK PNPDTFIGSG KVEEIKMLVE ETQADLVIFD TELSPRHQRE LEERFGEQVR VIDRTALILD IFARHASTRE GILQVELAYY EYRLPRLTRV WTHLARQTGG GGGRTGSTGG VGLRGPGETQ LEVDRREIRR RIARLKEELE KVRAHRQRYR EQRRRSNIPI VALVGYTNAG KSTLLNSLAR AEVYVADQLF ATLDPTTRRV ELPAGHTVLF TDTVGFIQKL PTQLIAAFRA TLEEITEADL LVHVLDVTHP NAWEQWKAVQ QTLLDIGCEN IPTITALNKV DRISDTEAIR KALGQFTSSV AISAKTGEGL PNLLREVENI LFENFAPVTV YIPYREGQLI AQFHEFGKVE ESQPFGEYIK IKGSLPGRLL NAYRPYLKRP TPAKSEV // ID A0A0P6XRE7_9CHLR Unreviewed; 449 AA. AC A0A0P6XRE7; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 07-JUN-2017, entry version 13. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=ADN01_06930 {ECO:0000313|EMBL:KPL85097.1}; OS Levilinea saccharolytica. OC Bacteria; Chloroflexi; Anaerolineae; Anaerolineales; Anaerolineaceae; OC Levilinea. OX NCBI_TaxID=229921 {ECO:0000313|EMBL:KPL85097.1, ECO:0000313|Proteomes:UP000050501}; RN [1] {ECO:0000313|EMBL:KPL85097.1, ECO:0000313|Proteomes:UP000050501} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=KIBI-1 {ECO:0000313|EMBL:KPL85097.1, RC ECO:0000313|Proteomes:UP000050501}; RA Hemp J., Ward L.M., Pace L.A., Fischer W.W.; RT "Genome sequence of Levilinea saccharolytica DSM 16555."; RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KPL85097.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LGCM01000027; KPL85097.1; -; Genomic_DNA. DR RefSeq; WP_062418583.1; NZ_LGCM01000027.1. DR EnsemblBacteria; KPL85097; KPL85097; ADN01_06930. DR PATRIC; fig|229921.5.peg.2275; -. DR Proteomes; UP000050501; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000050501}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000050501}. FT DOMAIN 219 385 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 178 215 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 449 AA; 49829 MW; 2BBBDE45796EEB20 CRC64; MAKKIPEPTK APQSRAFLVG VEFRGEQTIL PLEESLEELA LLAKTAGLEV VGELTQRLDH PNPETYIGAG KVEELQMLVE ETLAEVVIFD SELSPRHLRE LEERLGPNVQ VSDRTALILE IFAQHASTRE GILQVELAQY EYRLPRLTRA WTHLARQAGG GGGRTGSTGG VGLRGPGETQ LEVDRREIRK RISNLKAELE KVREHRQRYR AQRKRNQVPV VALVGYTNAG KSTLLNTLAR SEVYVANQLF ATLDPTTRRV DLPGSHTVLF TDTVGFIQKL PTQLVAAFRA TLEEISEADL LVHVVDITHP SAQAQWQSVM ATLEEIGAGS IPVLTVFNKI DRLKDPSVLE AASAAIGNTL PISGLTGQGL PDFVRTLETM LYETLTPVHV HLPYQQGQLI SMFHEHGQIS RVEHVRGGVQ IQGFIPGRML TRFQPFQVKK KPEAEESEE // ID A0A0P6XX72_9CHLR Unreviewed; 447 AA. AC A0A0P6XX72; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 07-JUN-2017, entry version 12. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=ADN00_00950 {ECO:0000313|EMBL:KPL81121.1}; OS Ornatilinea apprima. OC Bacteria; Chloroflexi; Anaerolineae; Anaerolineales; Anaerolineaceae; OC Ornatilinea. OX NCBI_TaxID=1134406 {ECO:0000313|EMBL:KPL81121.1, ECO:0000313|Proteomes:UP000050417}; RN [1] {ECO:0000313|EMBL:KPL81121.1, ECO:0000313|Proteomes:UP000050417} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=P3M-1 {ECO:0000313|EMBL:KPL81121.1, RC ECO:0000313|Proteomes:UP000050417}; RA Hemp J., Ward L.M., Pace L.A., Fischer W.W.; RT "Genome sequence of Ornatilinea apprima DSM 23815."; RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KPL81121.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LGCL01000002; KPL81121.1; -; Genomic_DNA. DR RefSeq; WP_075061075.1; NZ_LGCL01000002.1. DR EnsemblBacteria; KPL81121; KPL81121; ADN00_00950. DR PATRIC; fig|1134406.4.peg.3588; -. DR Proteomes; UP000050417; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000050417}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000050417}. FT DOMAIN 219 385 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 185 212 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 447 AA; 49623 MW; 6F50A896A10C89D0 CRC64; MAKKSTETTD RPKERAFLVG VEIRSEEHLL SLEDSLEELS LLADTAGLVV VGEATQRLDR PYANTYIGSG KVEEIKALVE DCLAEVVIFD NELSPRHLRE LEKEFGTAVR IIDRTALILD IFALHANTRE GALQVELAQY EYRLPRLTRA WTHLARQAGG GGGRSGSVGG VGLRGPGETQ LEVDRREIGR RISNLKSELE KIRAHRSRYR ANRRRSQIPV IALVGYTNAG KSTLLNRLSN AGVYVADQLF ATLDPTTRRV ELPGGQVVLF TDTVGFIQKL PTQLIAAFRA TLEEIAEADL VLHIVDITHV NALAQWNAVQ LTLKEIGADQ IPALTVLNKI DRLPDPQAAM QVLQNFPDAL AISALKGQGI DELLALVQKR LYEELLPISV RIPYTEGQLI SLFHESGQVE RIEHQRGSVM IDGSIPGRYI TRYMPFIHSG DLEPEEE // ID A0A0P7AF01_9SPHN Unreviewed; 449 AA. AC A0A0P7AF01; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=AAJ72_08200 {ECO:0000313|EMBL:KPM25601.1}; OS Citromicrobium sp. RCC1885. OC Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales; OC Sphingomonadaceae; Citromicrobium. OX NCBI_TaxID=1647104 {ECO:0000313|EMBL:KPM25601.1, ECO:0000313|Proteomes:UP000050479}; RN [1] {ECO:0000313|EMBL:KPM25601.1, ECO:0000313|Proteomes:UP000050479} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=RCC1885 {ECO:0000313|EMBL:KPM25601.1, RC ECO:0000313|Proteomes:UP000050479}; RA Zheng Q., Liu Y., Lin W., Jiao N.; RT "A comprehensive comparison of genomes of Citromicrobium spp. RT strains."; RL Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KPM25601.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LBLY01000001; KPM25601.1; -; Genomic_DNA. DR RefSeq; WP_054524385.1; NZ_LBLY01000001.1. DR EnsemblBacteria; KPM25601; KPM25601; AAJ72_08200. DR PATRIC; fig|1647104.3.peg.1690; -. DR Proteomes; UP000050479; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000050479}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000050479}. FT DOMAIN 208 387 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 174 201 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 449 AA; 49083 MW; 379212CD06999356 CRC64; MFEDDLQGEV TRGARALVIC PDIRGQIHDL PAEERLAEAV GLAHAIGIEV AESYIQPIRD VRPATLFGAG QVEQIGTQAE LAEAELIIVD GALTAIQQRT LEEKLARKVI DRTGLILEIF GERAATAEGR LQVELAHLDY QASRLVRSWT HLERQRGGYG FLGGPGETQI EADRRMIRTR MARLRRDLEQ VKKTRALHRE RRTRAPWPVI ALVGYTNAGK STIFNRLTGA DVMAEDLLFA TLDPTMRAIS LPAVEKAILS DTVGFISDLP TQLVAAFRAT LEEVTNADLI LHVRDIANPA SAAQKTQVLE VLRGLGVVSG GEEGEEPVSS IPMLEVWNKW DLLADDARED LAARAAEDDG VVPLSAETGF NMDALETRIG DALTREASVC EFVLPTSAGR EIAWLHAHGD VLEEEELPAG EGGAPRYRLL VRLGPKERGQ FESFGVSSS // ID A0A0P7BMU6_9BACT Unreviewed; 419 AA. AC A0A0P7BMU6; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=AFM12_19100 {ECO:0000313|EMBL:KPM46643.1}; OS Leadbetterella sp. JN14-9. OC Bacteria; Bacteroidetes; Cytophagia; Cytophagales; Cytophagaceae; OC Leadbetterella. OX NCBI_TaxID=1605367 {ECO:0000313|EMBL:KPM46643.1, ECO:0000313|Proteomes:UP000050454}; RN [1] {ECO:0000313|EMBL:KPM46643.1, ECO:0000313|Proteomes:UP000050454} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=JN14-9 {ECO:0000313|EMBL:KPM46643.1, RC ECO:0000313|Proteomes:UP000050454}; RA Liu Y., Du J., Shao Z.; RT "The draft genome sequence of Leadbetterella sp. JN14-9."; RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KPM46643.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LGTQ01000016; KPM46643.1; -; Genomic_DNA. DR RefSeq; WP_055151969.1; NZ_LGTQ01000016.1. DR EnsemblBacteria; KPM46643; KPM46643; AFM12_19100. DR PATRIC; fig|1605367.3.peg.1261; -. DR Proteomes; UP000050454; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000050454}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000050454}. FT DOMAIN 205 391 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 419 AA; 48066 MW; 8752A8735E8CE128 CRC64; MLNTPLISTS KKKEKCVLVG LISQNQNKEK TEEYLDELAF LAKTAGLKTM KVFEQRLPTP DNKTFVGKGK LEEIRTWIDI NPVDAIIFDD DLSPSQVRNL EANFKDIKVL DRSLLILNIF SQRAKTDQAK KQVELAQYQY LYPRLTRMWT HLSKQKGGVG MRGPGEKELE TDKRIVRDRI TFLKKKLEKI DKQSMTRRKE RNRLVRVALV GYTNVGKSTL MQVLAKADVF AENKLFATID STVRKLVLGN IPFLLTDTVG FIRKLPTTLI ESFKSTLDEI READILLHVV DISHPSFEEH IDVVNQTLTD IGASDKPTIL VFNKLDLYQP ESEEGLDDHL ATEEDLQKNL ARLKSSYLSK NTENVVFLSA TEKENIAELR SILLKTLGEK HFDIYPNWDP KQNPLYDWQG EVNWEESEG // ID A0A0P7DXB2_9GAMM Unreviewed; 456 AA. AC A0A0P7DXB2; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=AOG28_15710 {ECO:0000313|EMBL:KPM75734.1}; OS Cobetia sp. UCD-24C. OC Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales; OC Halomonadaceae; Cobetia. OX NCBI_TaxID=1716176 {ECO:0000313|EMBL:KPM75734.1, ECO:0000313|Proteomes:UP000050261}; RN [1] {ECO:0000313|EMBL:KPM75734.1, ECO:0000313|Proteomes:UP000050261} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=UCD-24C {ECO:0000313|EMBL:KPM75734.1, RC ECO:0000313|Proteomes:UP000050261}; RA Krusor M., Coil D.A., Lang J.M., Eisen J.A., Alexiev A.; RT "Draft Genome of Cobetia sp. UCD-24C."; RL Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KPM75734.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LJTD01000013; KPM75734.1; -; Genomic_DNA. DR RefSeq; WP_052384759.1; NZ_LJTD01000013.1. DR EnsemblBacteria; KPM75734; KPM75734; AOG28_15710. DR PATRIC; fig|1716176.3.peg.1171; -. DR Proteomes; UP000050261; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000050261}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000050261}. FT DOMAIN 199 365 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 456 AA; 51311 MW; 2379A2B94570F470 CRC64; MFFERPEAGE TAVLVHVNFR DEKEREDAGE LLELVRSAGA VPATLIEGSR PRPDSRTFIG EGKLEEVQEA LAVHEAELVI FNHSLSPSQQ RNLEATLKCR VIDRTGLILD IFAQRARTHE GKLQVELAQL EYMSTRLVRG WTHLERQKGG IGLRGPGETQ LETDRRLLRA RIKSIHKRLE KVHKQRDQNR RARARAEIPS LSLVGYTNAG KSTLFNALTT SEVYAADQLF ATLDPTLRRL ELEDVGPAVL ADTVGFIRHL PHKLVEAFQA TLQEAAEADL LVHVIDAADP ENDRNTEQVN HVLSEIDAGD VPRLLVMNKI DRLDMAPRIE RDGFGRPLAV WLSARDGKGL DLLMQAFAEL LSDNVISMQL TLGPAKSRLR AGLHELDAVK DEQYDEQGNA LLDIRLEKRD FLQLLSHLGE SPEDYLGGEH DDREAWQREL SAERAEKHRV SVTHKS // ID A0A0P7GAM0_9MICC Unreviewed; 522 AA. AC A0A0P7GAM0; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 07-JUN-2017, entry version 12. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=AO716_08755 {ECO:0000313|EMBL:KPN17996.1}; OS Arthrobacter sp. Edens01. OC Bacteria; Actinobacteria; Micrococcales; Micrococcaceae; Arthrobacter. OX NCBI_TaxID=1732020 {ECO:0000313|EMBL:KPN17996.1, ECO:0000313|Proteomes:UP000054460}; RN [1] {ECO:0000313|EMBL:KPN17996.1, ECO:0000313|Proteomes:UP000054460} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Edens01 {ECO:0000313|EMBL:KPN17996.1, RC ECO:0000313|Proteomes:UP000054460}; RA Couger M.B.; RT "Draft Genome of Arthrobacter sp. strain Edens01."; RL Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KPN17996.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LKIU01000005; KPN17996.1; -; Genomic_DNA. DR RefSeq; WP_055240470.1; NZ_LKIU01000005.1. DR EnsemblBacteria; KPN17996; KPN17996; AO716_08755. DR Proteomes; UP000054460; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 2. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000054460}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000054460}. FT DOMAIN 301 466 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 522 AA; 56740 MW; B7B041558568D35D CRC64; MTINNSRPAA GSTPTDLKPE EIQGVIDRIL AKDDAAAAKQ SVTPAGGFRG QAQALSAQEA EHSDFDGDQQ DLQDRRALRR VAGLSTELED VTEVEYRQLR LERVVLAGLW SEGTAADAEN SLRELAALAE TAGSEVLDGM IQRRLKPDPG TFLGSGKAQE LKDVVMATGA DTVIVDSELS PSQRRGLEDI VKVKVIDRTA LILDIFAQHA KSREGKAQVE LAQLEYLLPR LRGWGESMSR QAGGQVGSAG AGMGSRGPGE TKIELDRRKI RTRMAKLRRE IAGMKPARET KRANRQRNQI PSVAIAGYTN AGKSSLLNRL TDAGVLVENA LFATLDPTIR RAETPDGLGY TLADTVGFVR SLPTQLVEAF RSTLEEVADA DLILHVVDAS HPDPEGQIAA VRSVLADVDA RRIPEIIVLN KADAADPFVI ERLRQREPRT VVVSARTGEG IEELLQAISE GIPRPGVELD LMVPYERGDV VSRLHSQDAE ILSLEHEESG TRMRVKVRDS LAPELEPFLN HA // ID A0A0P7I3C6_9EURY Unreviewed; 346 AA. AC A0A0P7I3C6; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 07-JUN-2017, entry version 6. DE SubName: Full=GTP-binding protein HflX {ECO:0000313|EMBL:KPN31450.1}; GN Name=hflX_2 {ECO:0000313|EMBL:KPN31450.1}; GN ORFNames=SY89_02197 {ECO:0000313|EMBL:KPN31450.1}; OS Halolamina pelagica. OC Archaea; Euryarchaeota; Halobacteria; Haloferacales; Halorubraceae. OX NCBI_TaxID=699431 {ECO:0000313|EMBL:KPN31450.1, ECO:0000313|Proteomes:UP000050535}; RN [1] {ECO:0000313|Proteomes:UP000050535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CDK2 {ECO:0000313|Proteomes:UP000050535}; RA Hoang H.T., Killian M.L., Madson D.M., Arruda P.H.E., Sun D., RA Schwartz K.J., Yoon K.; RL Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KPN31450.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LGUC01000001; KPN31450.1; -; Genomic_DNA. DR EnsemblBacteria; KPN31450; KPN31450; SY89_02197. DR PATRIC; fig|699431.3.peg.2257; -. DR Proteomes; UP000050535; Unassembled WGS sequence. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000050535}; KW Reference proteome {ECO:0000313|Proteomes:UP000050535}. FT DOMAIN 219 346 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 346 AA; 38067 MW; FE31ED53F01828F7 CRC64; MVRHRWGTLP YRTLQDSPHA ETDAERTNSA EHSRTDIEDA DRTAIVVARD PEDPDTTEIE RLAAAATYAV VDAVTQRREE DSQYNVGRGK AEELARRVVE TEPDAVLFDA ELTPGQYSSL TALLPDGVRI IDRHRLVLDI FEDGAGDKAA RLQVELAKLR YERPRVRETE ERTHMQRAAE TGSQLVDIEK RIRTVERKLD ALGDRASDRR AERRAQGFDL VAIAGYTNAG KSTLLHRLAD DLSIAGLAPD HDDIDGVAEV ADRLFKTLET TTRRATIDGR RVLLTDTVGL VDGVPHDLVA SFSATLDAVA DSDAALLVVD ASDPVAAMRS KLRVSLAEID APGVSY // ID A0A0P7IUC2_9RHOB Unreviewed; 428 AA. AC A0A0P7IUC2; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=AKJ29_09775 {ECO:0000313|EMBL:KPN62502.1}; OS Aliiroseovarius crassostreae. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae; Aliiroseovarius. OX NCBI_TaxID=154981 {ECO:0000313|EMBL:KPN62502.1, ECO:0000313|Proteomes:UP000050471}; RN [1] {ECO:0000313|EMBL:KPN62502.1, ECO:0000313|Proteomes:UP000050471} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CV919-312 {ECO:0000313|EMBL:KPN62502.1, RC ECO:0000313|Proteomes:UP000050471}; RA Kessner L., Spinard E., Nelson D.; RT "Draft genome sequence of Aliiroseovarius crassostreae CV919-312TSm, RT the causative agent of Roseovarius Oyster Disease (formerly Juvenile RT Oyster Disease)."; RL Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KPN62502.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LKBA01000019; KPN62502.1; -; Genomic_DNA. DR RefSeq; WP_055192262.1; NZ_LKBA01000019.1. DR EnsemblBacteria; KPN62502; KPN62502; AKJ29_09775. DR Proteomes; UP000050471; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000050471}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000050471}. FT DOMAIN 207 377 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 166 200 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 428 AA; 47544 MW; F4C02FDA4E7FC30E CRC64; MTDLVEQESL PTRAWVLHPE LTSDRARRTA GPALEEAVSL AAALPHLVVE GAEIVRISRP HPGHLFGSGK IEELKARLQA AEVELVLIDG PVSPVQQRNL EKLWKVKILD RTGLILEIFS DRARTREGVL QVEMAALSYQ RTRLVRAWTH LERQRGGLGF VGGPGETQIE ADRRAIDDQL NRLRKQLEKV VKTRELHRAA RAKVPFPIVA LVGYTNAGKS TLFNRLTGAD VLAKDMLFAT LDPTMRNIEL PGSGRKVILS DTVGFISDLP TQLVAAFRAT LEEVLAADLI LHVRDISSEN TDEQAADVEK IMEDLGVDEN TPSLEVWNKT DLLDPEDADA RRREAARNDD VFTLSAITGE GFEELLEAVE TRLASPRETT DVDLAFSQGK QRAWLFSQGV VDAEEQTETG WSLTVTWTER QKAEYAAL // ID A0A0P7VA17_9RHOB Unreviewed; 442 AA. AC A0A0P7VA17; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 07-JUN-2017, entry version 12. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:KPP82886.1}; GN ORFNames=HLUCCA04_02100 {ECO:0000313|EMBL:KPP82886.1}; OS Oceanicaulis sp. HLUCCA04. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Hyphomonadaceae; Oceanicaulis. OX NCBI_TaxID=1666904 {ECO:0000313|EMBL:KPP82886.1, ECO:0000313|Proteomes:UP000054338}; RN [1] {ECO:0000313|EMBL:KPP82886.1, ECO:0000313|Proteomes:UP000054338} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=HLUCCA04 {ECO:0000313|EMBL:KPP82886.1}; RA Nelson W.C., Romine M.F., Lindemann S.R.; RT "Identification and resolution of microdiversity through metagenomic RT sequencing of parallel consortia."; RL Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KPP82886.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LJSH01000001; KPP82886.1; -; Genomic_DNA. DR EnsemblBacteria; KPP82886; KPP82886; HLUCCA04_02100. DR PATRIC; fig|1666904.3.peg.1241; -. DR Proteomes; UP000054338; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000054338}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000054338}. FT DOMAIN 202 378 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 168 195 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 442 AA; 48602 MW; 8EB4CA3396E3F13E CRC64; MTETARPTDS ALIIHPLPPG TDASRADARL EEAIGLTIAL GLEAREGFIE PVRKLEAGTF FGKGKLETLH ERIQALGVQA VIIDAALSPV QQRNLEKRWQ VKVIDRTGLI LEIFAERART REGTLQVELA RLTYERSRLV RTWTHLERQR GGGGFLAGPG ETQIETDRRL LATKMAKLRR ELEQVKRTRA LHRTRRQAAP WPSIALVGYT NAGKSTLFNR LTAAGVLAKD MPFATLDPTV RGVRLPSGRR VLVSDTVGFI TDLPTELIAA FRATLEEVRE ADILVHIRDL SDPDHEGRKA DVESVLTALD CGPAHGQPLI EAWNKIDRLD DEARDEMVWA ARMAAGKSRV AVHPVSAVTG EGVAQLLEAI DAALGREDHR ISVELEPGQD EVSAWLHEHG EVVSEKRNSK TGKLRIEARL AGPDAGRFRA KFGALLNDGA DA // ID A0A0P7W6K8_9RHOB Unreviewed; 435 AA. AC A0A0P7W6K8; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 05-JUL-2017, entry version 12. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:KPP95668.1}; GN ORFNames=HLUCCA05_03110 {ECO:0000313|EMBL:KPP95668.1}; OS Roseibaca calidilacus. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae; Roseibaca. OX NCBI_TaxID=1666912 {ECO:0000313|EMBL:KPP95668.1, ECO:0000313|Proteomes:UP000050413}; RN [1] {ECO:0000313|EMBL:KPP95668.1, ECO:0000313|Proteomes:UP000050413} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=HL-91 {ECO:0000313|EMBL:KPP95668.1}; RA Nelson W.C., Romine M.F., Lindemann S.R.; RT "Identification and resolution of microdiversity through metagenomic RT sequencing of parallel consortia."; RL Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KPP95668.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LJSG01000002; KPP95668.1; -; Genomic_DNA. DR EnsemblBacteria; KPP95668; KPP95668; HLUCCA05_03110. DR PATRIC; fig|1666912.4.peg.1777; -. DR Proteomes; UP000050413; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000050413}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000050413}. SQ SEQUENCE 435 AA; 47773 MW; 5BB4D50A7B49BAF4 CRC64; MIDLTELGGE GGKRLTRAFV LHPELKSKPG SREPEDALAE AMALAHALPG LEVVGGQVVR LPRAHPGQLF GKGKLEELRQ ALEADEIDLV LIDGPVSPVQ QRNLEKAWNV KLLDRTGLIL EIFADRAATR EGVLQVELAA LSYQRTRLVR AWTHLERQRG GLGFVGGPGE TQIEADRRAI DEQMTRLRRQ LDKVAKTREL HRAARRKVPY PVVALVGYTN AGKSTLFNRL TGANVMAKDM LFATLDPTMR AVRLPTGKDI ILSDTVGFIS ELPTLLVAAF RATLEEVLEA DLILHVRDIA HPATAAQAAD VAHVLAALGV DDEIPRIDLW NKADQLDEAT RLQVDRQAQR AEGVFVGSAL TGAGLDALFA AITAQLDDVR HHDTVTVPHS DGRLRAWLYG QGVVESEAQG ETETVLSVHW SDRQQARFRA LRDRT // ID A0A0P7WFM4_9BACT Unreviewed; 429 AA. AC A0A0P7WFM4; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 07-JUN-2017, entry version 10. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:KPP98685.1}; GN ORFNames=HLUCCA01_09810 {ECO:0000313|EMBL:KPP98685.1}; OS Bacteroidetes bacterium HLUCCA01. OC Bacteria; Bacteroidetes. OX NCBI_TaxID=1666909 {ECO:0000313|EMBL:KPP98685.1, ECO:0000313|Proteomes:UP000050310}; RN [1] {ECO:0000313|EMBL:KPP98685.1, ECO:0000313|Proteomes:UP000050310} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=HLUCCA01 {ECO:0000313|EMBL:KPP98685.1}; RA Nelson W.C., Romine M.F., Lindemann S.R.; RT "Identification and resolution of microdiversity through metagenomic RT sequencing of parallel consortia."; RL Submitted (AUG-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KPP98685.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LIHN01000007; KPP98685.1; -; Genomic_DNA. DR EnsemblBacteria; KPP98685; KPP98685; HLUCCA01_09810. DR PATRIC; fig|1666909.3.peg.175; -. DR Proteomes; UP000050310; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000050310}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000050310}. FT DOMAIN 210 375 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 178 205 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 429 AA; 48638 MW; 7B08C5A4242A77A7 CRC64; MASSNSTDTY LIEQTAITKE RALLVGLYGQ QTPRTKAEEY LEELALLTDT AGGTVLYKVI QNRDKPHIGT YVGKGKLEEL KALIKAESID IIIFDDDLTP TQTRNIERET EIKVLDRSGL ILDIFASRAK SSTAKTQVEL AQLQYILPRL TRMWTHLSRQ KGGIGTKGPG ETQIETDRRI IKTRIATLRE KLEKLEKQRA TQRQGREKHP RVALVGYTNA GKSSLMNTLV EAGVLAEDRL FATLDSTMRR LEIGNRILLL SDTVGFIRKL PHNLVESFKS TLDEIREADL LLHVVDAASP YFEEYIQVVR QTLKEIGAED KNELLVFNKV DLLEEPYQFN ALQSDYPEAL CVSAHRGIGM EQLREALVEQ TAGDLEIHTL RIPVSNSRAI AYIHENADVE MLNYQEDVAE IRFEMHRKYA GKLMAMLHY // ID A0A0P7X1T9_9TELE Unreviewed; 539 AA. AC A0A0P7X1T9; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 07-JUN-2017, entry version 7. DE SubName: Full=Putative GTP-binding protein 6 {ECO:0000313|EMBL:KPP68100.1}; DE Flags: Fragment; GN ORFNames=Z043_113244 {ECO:0000313|EMBL:KPP68100.1}; OS Scleropages formosus (Asian bonytongue). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Osteoglossocephala; OC Osteoglossomorpha; Osteoglossiformes; Osteoglossidae; Scleropages. OX NCBI_TaxID=113540 {ECO:0000313|EMBL:KPP68100.1, ECO:0000313|Proteomes:UP000034805}; RN [1] {ECO:0000313|EMBL:KPP68100.1, ECO:0000313|Proteomes:UP000034805} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Aro1 {ECO:0000313|EMBL:KPP68100.1}; RA Tan M.H., Gan H.M., Croft L.J., Austin C.M.; RT "The genome of the Asian arowana (Scleropages formosus)."; RL Submitted (AUG-2015) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KPP68100.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JARO02004669; KPP68100.1; -; Genomic_DNA. DR Proteomes; UP000034805; Unassembled WGS sequence. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR CDD; cd01878; HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000034805}; KW Reference proteome {ECO:0000313|Proteomes:UP000034805}. FT DOMAIN 317 481 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT NON_TER 1 1 {ECO:0000313|EMBL:KPP68100.1}. SQ SEQUENCE 539 AA; 60847 MW; 140A45899373EE43 CRC64; SRLRDYHFLG TPPKSCVQYR KEKQKGFTRP PRERGALRRL GHWTPVVSSL SSTGLLNLNR TFSSTVCKLK RKKHSAEEEG VQGGADVDED FDILEDSEVE ELFQQQHIPT KVGSEDHRVL VVHPDVKWGS KKPQLTTAEL MMAEAVGLVN TLQNWTVLDK VILSTKAPDR RTIFGKGNFK ILTERIKGKP QITAVFVNVE RLSPVSEREL EEAWGVKVLD RYSVVLHIFR CNARTKEAKL QISLAEIPLL RSRLKDEVAK LDQQGGGSRY IMGSGETFME VQQRLLKERE LKIRSALEKL RKKRQLLRSQ RKSREFPVVS VMGYTNCGKT TLIKALTGDV KLQPRDQLFA TLDVTVHGGQ LPSRMTVLYV DTIGFLSQLP HQLIDSFSAT LEDVAHSDLI VHVRDISHPE TLNQKVNVLN VLKNLQIPEC LMNSIVEVHN KIDLVDNYEQ SEPDAVPVSA LKEQGLEELK QRIEAAIVKS TGKHILTVKV ELSSAQLSWL YKEATVQEVD VVADEGTALV KVIISNAAYG RYRKLFQTN // ID A0A0P7YHV1_9RHOB Unreviewed; 439 AA. AC A0A0P7YHV1; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 07-JUN-2017, entry version 10. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:KPQ14334.1}; GN ORFNames=HLUCCO18_15350 {ECO:0000313|EMBL:KPQ14334.1}; OS Rhodobacteraceae bacterium HLUCCO18. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae. OX NCBI_TaxID=1666917 {ECO:0000313|EMBL:KPQ14334.1, ECO:0000313|Proteomes:UP000050333}; RN [1] {ECO:0000313|EMBL:KPQ14334.1, ECO:0000313|Proteomes:UP000050333} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=HLUCCO18 {ECO:0000313|EMBL:KPQ14334.1}; RA Nelson W.C., Romine M.F., Lindemann S.R.; RT "Identification and resolution of microdiversity through metagenomic RT sequencing of parallel consortia."; RL Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KPQ14334.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LJSY01000043; KPQ14334.1; -; Genomic_DNA. DR EnsemblBacteria; KPQ14334; KPQ14334; HLUCCO18_15350. DR PATRIC; fig|1666917.4.peg.2595; -. DR Proteomes; UP000050333; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000050333}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000050333}. FT DOMAIN 214 383 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 439 AA; 48372 MW; 50CCBAEA9FB3AD22 CRC64; MTAGDEGHTT DRTDDRAPMR TMVLHPDIQT DRDRRDPGAA LEEAVALAAA LPDLEIRGAD VVRLPRAHAG MLFGSGKIEE LKQRIEDADV GLVLIDGVVT PVQQRNLEKA WGCKLLDRTG LILEIFADRA RTREGVLQVE LAALSYQRTR LVRAWTHLER QRGGLGFVGG PGETQIEADR RAIDEAITRL RRQLAKVAKT RGLHRAARAK VPFPVVALVG YTNAGKSTLF NRLTGAEVLA KDMLFATLDP TMRAVRLPDG TEVILSDTVG FISDLPTQLV AAFRATLEEV LDADLILHVR DIAHPQTTEQ AEDVARILED LGVAETTPQL EVWNKIDLLP AAERETRRTE AARRDSVFAI SALTGEGLDP FLSAVAELVS EPRHRTVLTL PHSDGRRRAW LFERGIVEAE DSEGETTRLT VRWTDREAQA FRALGEGGS // ID A0A0P7YK62_9RHOB Unreviewed; 412 AA. AC A0A0P7YK62; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 07-JUN-2017, entry version 10. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:KPP91061.1}; GN ORFNames=HLUCCA08_14075 {ECO:0000313|EMBL:KPP91061.1}; OS Rhodobacteraceae bacterium HLUCCA08. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae. OX NCBI_TaxID=1666913 {ECO:0000313|EMBL:KPP91061.1, ECO:0000313|Proteomes:UP000050293}; RN [1] {ECO:0000313|EMBL:KPP91061.1, ECO:0000313|Proteomes:UP000050293} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=HLUCCA08 {ECO:0000313|EMBL:KPP91061.1}; RA Nelson W.C., Romine M.F., Lindemann S.R.; RT "Identification and resolution of microdiversity through metagenomic RT sequencing of parallel consortia."; RL Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KPP91061.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LJSF01000009; KPP91061.1; -; Genomic_DNA. DR EnsemblBacteria; KPP91061; KPP91061; HLUCCA08_14075. DR PATRIC; fig|1666913.4.peg.441; -. DR Proteomes; UP000050293; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000050293}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000050293}. FT DOMAIN 192 360 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 412 AA; 45507 MW; 28D8B2BD6BD7F3E4 CRC64; MIHPDIRSDR ARRAAAPALE EAVSLAMALP DLQVVGAETV GLPRVHPGAL FGPGKIDELK ARLTADEVEL VLIDGPVSPV QQRNLEKAWE VKLLDRTGLI LEIFSDRART REGVLQVEMA ALSYQRTRLV RAWTHLERQR GGLGFVGGPG ETQIEADRRA IDEQLVRLRR QLDKVVKTRA LHRAARAKVP FPVVALVGYT NAGKSTLFNR LTGAEVMARD MLFATLDPTM RKVRLGTGDN VILSDTVGFI SDLPTQLVAA FRATLEEVLE ADVICHVRDI SHPQSEEQSD EVLSILSDLG VAEDIPVIEV WNKIDRVDPE TATALRARAA RSDDIHAVSA LTGQGIAPLL DRVSEVLGAP RERDEVLVPF ADGRRRAWLH DQGVVVQETA EDDGHRIVVD WTKRQKDRFL GL // ID A0A0P7YWG4_9CYAN Unreviewed; 501 AA. AC A0A0P7YWG4; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:KPQ35221.1}; GN ORFNames=HLUCCA11_11050 {ECO:0000313|EMBL:KPQ35221.1}; OS Phormidesmis priestleyi Ana. OC Bacteria; Cyanobacteria; Synechococcales; Leptolyngbyaceae; OC Phormidesmis. OX NCBI_TaxID=1666911 {ECO:0000313|EMBL:KPQ35221.1, ECO:0000313|Proteomes:UP000050465}; RN [1] {ECO:0000313|EMBL:KPQ35221.1, ECO:0000313|Proteomes:UP000050465} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Ana {ECO:0000313|EMBL:KPQ35221.1}; RA Nelson W.C., Romine M.F., Lindemann S.R.; RT "Identification and resolution of microdiversity through metagenomic RT sequencing of parallel consortia."; RL Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KPQ35221.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LJZR01000013; KPQ35221.1; -; Genomic_DNA. DR EnsemblBacteria; KPQ35221; KPQ35221; HLUCCA11_11050. DR PATRIC; fig|1666911.3.peg.424; -. DR Proteomes; UP000050465; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000050465}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000050465}. FT DOMAIN 328 498 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 287 321 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 501 AA; 55087 MW; 3492107C5FAB53D3 CRC64; MIRVGVGSPH KTQIPVLELP RYGAERLCGI RCIATQLKVE PPSHSVLTAM AIQRLDAVAL LTLTGTGFKR KGGGATGYIR EGYLAHLVPH PEVQWEVSDP LTLDELDQQD FLDLAEGLEE EFRRVFVAQQ VDADHDRVII VGLMTDKMTD QSFENGLEEV ARLVETAGGD VLQVMTQKRS RPHPRTVIGS GRLDDVVLAV QTLGANLIVC DRDLSPAQIR NIEAQVGVRV VDRTELILDI FAQRAKSGAG KLQVELAQLE YQLPRLTGRG QAMSRLGGGI GTRGPGETKL ETERRAIQKR ISRLQKEVDG LQAHRARMRQ QRQHQSVPSV AIIGYTNAGK STLLNRLTNS DIYAADQLFA TLDPTTRKIS IAEDDTVEIK SLVLTDTVGF IQDLPPALMD AFRATLEEVT EADALIHVVD ASHHAWQDHI RSVMGLLAQM PIAPGPILLV FNKLDEADTD TLELAKDEYP QAVFISAVNN LGLDTLKQKI IQLVDYAVVN S // ID A0A0P7Z2H0_9GAMM Unreviewed; 436 AA. AC A0A0P7Z2H0; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 30-AUG-2017, entry version 12. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:KPQ25629.1}; GN ORFNames=HLUCCA13_03690 {ECO:0000313|EMBL:KPQ25629.1}; OS Halomonas sp. HL-48. OC Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales; OC Halomonadaceae; Halomonas. OX NCBI_TaxID=1479235 {ECO:0000313|EMBL:KPQ25629.1, ECO:0000313|Proteomes:UP000050569}; RN [1] {ECO:0000313|EMBL:KPQ25629.1, ECO:0000313|Proteomes:UP000050569} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=HL-48 {ECO:0000313|EMBL:KPQ25629.1}; RA Nelson W.C., Romine M.F., Lindemann S.R.; RT "Identification and resolution of microdiversity through metagenomic RT sequencing of parallel consortia."; RL Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KPQ25629.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LJZS01000003; KPQ25629.1; -; Genomic_DNA. DR RefSeq; WP_027335345.1; NZ_KK366039.1. DR EnsemblBacteria; KPQ25629; KPQ25629; HLUCCA13_03690. DR PATRIC; fig|1479235.4.peg.1707; -. DR Proteomes; UP000050569; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000050569}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000050569}. FT DOMAIN 199 365 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 436 AA; 49012 MW; AD84653B631566CC CRC64; MFFERPEAGE TAVLVHVDFQ DEQAREDPGE FLELVRSAGA EPATLLTASR HRPDPRSFIG SGKLEELRAL LAAHEAELVI FNHGLSPSQQ RNLERELKCR VLDRTGLILD IFAQRARTHE GKLQVELAQL EYVSTRLIRG WTHLERQKGG IGLRGPGETQ LETDRRLLRG RIKSIHKRLD KVRSQREQNR RARARAEIHS VSLVGYTNAG KSTLFNALTQ SDVYAADQLF ATLDPTLRRL EIEDVGPVVM ADTVGFIRHL PHKLVEAFQA TLQEAAEATL LVHVIDAADP DRELNVEQVE RVLEEIGADD VPVLKVMNKI DILDSAPRIE RDGEGLPEVV WLSAQQGKGL DLLHQALTER LAGDVIGFSL TLSPEQGKLR AGLHELNAVR EEAFDEQGRS VLDVRLPRRD FNQLMAQLGE RANTYLPAEL RETKEW // ID A0A0P8B5H4_9GAMM Unreviewed; 427 AA. AC A0A0P8B5H4; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 30-AUG-2017, entry version 14. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:KPQ03345.1}; GN ORFNames=HLUCCO02_11770 {ECO:0000313|EMBL:KPQ03345.1}; OS Idiomarinaceae bacterium HL-53. OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales; OC Idiomarinaceae. OX NCBI_TaxID=1298881 {ECO:0000313|EMBL:KPQ03345.1, ECO:0000313|Proteomes:UP000053932}; RN [1] {ECO:0000313|EMBL:KPQ03345.1, ECO:0000313|Proteomes:UP000053932} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=HL-53 {ECO:0000313|EMBL:KPQ03345.1}; RA Nelson W.C., Romine M.F., Lindemann S.R.; RT "Identification and resolution of microdiversity through metagenomic RT sequencing of parallel consortia."; RL Submitted (AUG-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KPQ03345.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LIHO01000010; KPQ03345.1; -; Genomic_DNA. DR RefSeq; WP_072154151.1; NZ_LN899469.1. DR EnsemblBacteria; KPQ03345; KPQ03345; HLUCCO02_11770. DR PATRIC; fig|1298881.4.peg.2437; -. DR Proteomes; UP000053932; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000053932}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000053932}. SQ SEQUENCE 427 AA; 48048 MW; ED0AFB2EEFE288DE CRC64; MFDRYEGGEQ AVLVHVNFVA ESAREDLEEL KLLVSSAGVS IGGVVTGARN APDARLFVGS GKAEEIAALV KALNADVVIF NHALSPSQER NLERVFECRV IDRTGLILDI FAQRARTHEG KLQVELAQLR HISTRLIRGW THLERQKGGI GLRGPGETQL ETDRRLLRER IKNILRRLGK VEKQREQGRR SRKRAEIPTL ALVGYTNAGK STLFNTLTEA DVYAADQLFA TLDPTLRKFD LGDIGPVIFA DTVGFIRHLP HDLVAAFKAT LTETRDADLL IHVVDSFDER RDENQREVNS VLEEIGAHEV PQLLVFNKLD LMEGVTSKID YNDEGVPERV WLSAQTGEGI ELLKQALHER LAPKMVETTL RVPPAEGKLR SRLYAMQCVQ GEQANEVGDM LISVRMPDIE WQRLKKQFGE RLEKFIN // ID A0A0P8D5Q2_9CYAN Unreviewed; 539 AA. AC A0A0P8D5Q2; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 07-JUN-2017, entry version 12. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:KPQ31313.1}; GN ORFNames=HLUCCO16_22070 {ECO:0000313|EMBL:KPQ31313.1}; OS Phormidium sp. OSCR. OC Bacteria; Cyanobacteria; Oscillatoriophycideae; Oscillatoriales; OC Oscillatoriaceae; Phormidium. OX NCBI_TaxID=1666905 {ECO:0000313|EMBL:KPQ31313.1, ECO:0000313|Proteomes:UP000050461}; RN [1] {ECO:0000313|EMBL:KPQ31313.1, ECO:0000313|Proteomes:UP000050461} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=OSCR {ECO:0000313|EMBL:KPQ31313.1}; RA Nelson W.C., Romine M.F., Lindemann S.R.; RT "Identification and resolution of microdiversity through metagenomic RT sequencing of parallel consortia."; RL Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KPQ31313.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LJZT01000183; KPQ31313.1; -; Genomic_DNA. DR EnsemblBacteria; KPQ31313; KPQ31313; HLUCCO16_22070. DR PATRIC; fig|1666905.3.peg.811; -. DR Proteomes; UP000050461; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000050461}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000050461}. FT DOMAIN 369 539 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 328 362 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 539 AA; 59282 MW; 8A653A06A6C37136 CRC64; MYHQRLPGDR LTTPEFAQRL AAISTDLGKP VSAYLNRRGQ VIRVGVGSPR QTQIPPLELP RYGASRLSGI RCIATQLKRD EPGTATLTAM AIQRLDALIC LTLTGSGFQR RGGGETGYVH RTYLAHLVPN PSEASWTVSE EMTLEAIAQQ DFLDLVEALE GEFEREFVGQ SVDSDGDRVL LVGLRTQNTS ETEFEEHLAE VVRLVDTAGG VVLQTIQQGR SRPHPQTVIG SGKVDELALA VQTLGANLVV FDRDLSPAQV RNLEKRLGVR VVDRTEVILD IFAQRAQSRA GKLQVELAQL EYSLPRLTGQ GQKMSRLGGG IGTRGPGETQ LETERRAISQ RISRLQREVT NLQAHRARMR QQRQAQEVPS IALVGYTNAG KSTLLNVLAN SEIYTADQLF ATLDPTTRRL SIQEDVTHTV HQLVLTDTVG FIHELPPALV DAFRATLEEV TEADALLHVV DLSHAAWQNQ IHSVMGILAE MPITPGPILL VFNKIDAVDG DTLELAKEEY PQATFISATA GFGLATLRQR LLQLVEYAR // ID A0A0P8W8V7_9CLOT Unreviewed; 610 AA. AC A0A0P8W8V7; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:KPU45103.1}; GN ORFNames=OXPF_15840 {ECO:0000313|EMBL:KPU45103.1}; OS Oxobacter pfennigii. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Oxobacter. OX NCBI_TaxID=36849 {ECO:0000313|EMBL:KPU45103.1, ECO:0000313|Proteomes:UP000050326}; RN [1] {ECO:0000313|EMBL:KPU45103.1, ECO:0000313|Proteomes:UP000050326} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 3222 {ECO:0000313|EMBL:KPU45103.1, RC ECO:0000313|Proteomes:UP000050326}; RA Poehlein A., Bengelsdorf F.R., Schiel-Bengelsdorf B., Duerre P., RA Daniel R.; RT "Genome sequence of Oxobacter pfennigii DSM 3222."; RL Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KPU45103.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LKET01000028; KPU45103.1; -; Genomic_DNA. DR RefSeq; WP_054874640.1; NZ_LKET01000028.1. DR EnsemblBacteria; KPU45103; KPU45103; OXPF_15840. DR PATRIC; fig|36849.3.peg.1674; -. DR Proteomes; UP000050326; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000050326}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000050326}. FT DOMAIN 379 555 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 338 372 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 610 AA; 67689 MW; 4F9082330252F6B2 CRC64; MRVNGNVTGI KDSYLERLDG LYDINVSIEE LISSEILDVM AEVTSAINKE ISVFINRRGK VVDVSIGDFA TVSLPIISFR RGNRRLSGVR CIHTHPGGNG NLSEVDISAL INLRLDCIAA AGIEGSKVTN VYTGYLYPVE GALTEKYNIL GPYDLNTILS INILNVIKEI EKHIIADTAS VTEDERKERV LLIGLNTPDG MGSDEDLLDE LSELAEASGA EVAGKILQKR SKVDTAYYIG SGKAMEVSLV TQSYDIDTVI FDDELSGAQV RNLEETIGAK VIDRTTLILD IFASRALTME GKLQVELAQL KYRLPRLIGL GKVLSRTGGG IGTRGPGEKK LEVDRRHIRE RINELEKGLN EVKKNREIQR AKRMSNSIPI VSLIGYTNSG KSTLRNRLAH DFQTDSQVKK EDVLEADMLF ATLDPTTRSI KLPNGREILV SDTVGFIRKL PHDLVDAFRA TLEEVAYSDL LIHVVDASAP NAHEQIKAVN NVLGQLNALD KPTILALNKV DKIEFADGLN LLYENHENVA EISALYGTGI EDLISMIEQR LYDKLKKVEI RLPYDKMGLK SYLYKECTVL SEEYDEIAAV ITVETDEATI EKYRDYIAFE // ID A0A0P9CFC1_9ARCH Unreviewed; 373 AA. AC A0A0P9CFC1; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=JI55_00075 {ECO:0000313|EMBL:KPU81570.1}; OS Nitrosopumilus sp. PRT-SC01. OC Archaea; Thaumarchaeota; Nitrosopumilales; Nitrosopumilaceae; OC Nitrosopumilus. OX NCBI_TaxID=1527301 {ECO:0000313|EMBL:KPU81570.1, ECO:0000313|Proteomes:UP000054200}; RN [1] {ECO:0000313|EMBL:KPU81570.1, ECO:0000313|Proteomes:UP000054200} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=PRT-SC01 {ECO:0000313|EMBL:KPU81570.1}; RA Leon Zayas R.I., Novotny M., Podell S., Shepard C.M., Berkenpas E., RA Nikolenko S., Pevzner P., Lasken R.S., Bartlett D.H.; RT "Microbial Metabolic Properties Below 8,000 Meters Depth Within the RT Puerto Rico Trench Inferred From Single Cell Genomes."; RL Submitted (AUG-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KPU81570.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JPUE01000002; KPU81570.1; -; Genomic_DNA. DR EnsemblBacteria; KPU81570; KPU81570; JI55_00075. DR PATRIC; fig|1527301.3.peg.15; -. DR Proteomes; UP000054200; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000054200}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000054200}. FT DOMAIN 184 355 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 373 AA; 42580 MW; A3F7E9CC2B53F58C CRC64; MNSAILITYD KEDAINEAKG LCDAAGYQIV HTITAKFLQK RKYGMSGGVL EELEELSEKL RPDVIVFDEI LKPSQNYNIA SVLHREVLDR EALILEIFES RASSAESKLQ VKLAQLRYEM SRAKEKVRLS NMGEQPGFMG IGKFEVDVYY NDIKHRMQTV RSKLEKAGKQ RELHRQGRKR MGFKIISLAG YTSSGKTTLF NKMTGETKAE GKELFTTLST TMRRVTINQE PFLISDTVGF ISKLPAYMID AFKSTLEELK HTDIIIVVID IADSLIELKK KFASCMRTLS ELEIEKDRMI YVLNKIDLLK NEEIEQKIDI LNLTENKKYI SLSAKTGKNV NQLKELIRDI MKSQNSPKFE KNLLEGVEKA FGN // ID A0A0P9EJQ9_9ARCH Unreviewed; 387 AA. AC A0A0P9EJQ9; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 07-JUN-2017, entry version 12. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:KPV63234.1}; GN ORFNames=AOA66_0956 {ECO:0000313|EMBL:KPV63234.1}; OS Candidatus Bathyarchaeota archaeon BA2. OC Archaea; Candidatus Bathyarchaeota. OX NCBI_TaxID=1700836 {ECO:0000313|EMBL:KPV63234.1, ECO:0000313|Proteomes:UP000050284}; RN [1] {ECO:0000313|EMBL:KPV63234.1, ECO:0000313|Proteomes:UP000050284} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BA2 {ECO:0000313|EMBL:KPV63234.1}; RX PubMed=26494757; DOI=10.1126/science.aac7745; RA Evans P.N., Parks D.H., Chadwick G.L., Robbins S.J., Orphan V.J., RA Golding S.D., Tyson G.W.; RT "Methane metabolism in the archaeal phylum Bathyarchaeota revealed by RT genome-centric metagenomics."; RL Science 350:434-438(2015). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KPV63234.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LIHK01000024; KPV63234.1; -; Genomic_DNA. DR EnsemblBacteria; KPV63234; KPV63234; AOA66_0956. DR KEGG; barb:AOA66_0956; -. DR PATRIC; fig|1700836.3.peg.11; -. DR KO; K03665; -. DR Proteomes; UP000050284; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000050284}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000050284}. FT DOMAIN 155 325 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 77 104 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 387 AA; 43527 MW; 4E61F8107F9050F1 CRC64; MGSFEQIRKP DPRHQIGSGK TKELAELVRK NGVEKTIFDN ELTPVQAYNL AKATGVEAID RFQLILEIFA RRASTAEANL QIQLARLRYE LSRAKERVRL ARMEEQPGFM GLGAYEVDVY YEAVKRQTHS IQDKLKKKQR KRRLHRDRRL ELGFSSVSLA GYTNAGKSSL FNVLAEETVP VDSGLFTTLS TTTRAVVLSK RRVLLTDTVG FIDRLPLTLI QAFHSTLEET IFSDLILLVV DASESDEDIE RKLSCCLDTI QKIGAAGIPI VTAFNKIDLL QDNEIQRKAE VLKNVAPNPV FISALHGTNT DLLKQEMISR LESYVKGSFS LPITDESMSF ISWLFGRVDV HDVKYKGDSM GVIFEAIPWF ADRVKGRVEQ LGGTFNA // ID A0A0P9FSS7_9ARCH Unreviewed; 887 AA. AC A0A0P9FSS7; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 07-JUN-2017, entry version 10. DE SubName: Full=GTPase HflX {ECO:0000313|EMBL:KPV61435.1}; GN Name=hflX {ECO:0000313|EMBL:KPV61435.1}; GN ORFNames=AOA65_2252 {ECO:0000313|EMBL:KPV61435.1}; OS Candidatus Bathyarchaeota archaeon BA1. OC Archaea; Candidatus Bathyarchaeota. OX NCBI_TaxID=1700835 {ECO:0000313|EMBL:KPV61435.1, ECO:0000313|Proteomes:UP000050312}; RN [1] {ECO:0000313|EMBL:KPV61435.1, ECO:0000313|Proteomes:UP000050312} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BA1 {ECO:0000313|EMBL:KPV61435.1}; RX PubMed=26494757; DOI=10.1126/science.aac7745; RA Evans P.N., Parks D.H., Chadwick G.L., Robbins S.J., Orphan V.J., RA Golding S.D., Tyson G.W.; RT "Methane metabolism in the archaeal phylum Bathyarchaeota revealed by RT genome-centric metagenomics."; RL Science 350:434-438(2015). CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KPV61435.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LIHJ01000089; KPV61435.1; -; Genomic_DNA. DR EnsemblBacteria; KPV61435; KPV61435; AOA65_2252. DR KEGG; barc:AOA65_2252; -. DR PATRIC; fig|1700835.3.peg.859; -. DR KO; K03665; -. DR Proteomes; UP000050312; Unassembled WGS sequence. DR GO; GO:0004519; F:endonuclease activity; IEA:InterPro. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR GO; GO:0016539; P:intein-mediated protein splicing; IEA:InterPro. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR028992; Hedgehog/Intein_dom. DR InterPro; IPR003586; Hint_dom_C. DR InterPro; IPR003587; Hint_dom_N. DR InterPro; IPR027434; Homing_endonucl. DR InterPro; IPR006142; INTEIN. DR InterPro; IPR030934; Intein_C. DR InterPro; IPR004042; Intein_endonuc. DR InterPro; IPR004860; LAGLIDADG_2. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF14528; LAGLIDADG_3; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00379; INTEIN. DR SMART; SM00305; HintC; 1. DR SMART; SM00306; HintN; 1. DR SUPFAM; SSF51294; SSF51294; 2. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF55608; SSF55608; 1. DR PROSITE; PS51705; G_HFLX; 1. DR PROSITE; PS50818; INTEIN_C_TER; 1. DR PROSITE; PS50819; INTEIN_ENDONUCLEASE; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000050312}; KW Reference proteome {ECO:0000313|Proteomes:UP000050312}. FT DOMAIN 377 508 DOD-type homing endonuclease. FT {ECO:0000259|PROSITE:PS50819}. FT DOMAIN 644 668 INTEIN_C_TER. FT {ECO:0000259|PROSITE:PS50818}. FT DOMAIN 668 825 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 887 AA; 101694 MW; 4B8ACE44AD62DE82 CRC64; MKELAELINK NGIERTIFNN ELKPFQAYNL AKATGIEAVD RFQLILEIFA RRASTTEAKL QIQLARLRYE LARAKERVKL AKMGEQPGFM GLGAYKVDVY YETVKRQIHS IQDKLRRIRK KRRLHRARRL ELGFPLSTLA GYTNAGKSIP HHELVLALTS SDSGLIPIGR IFQNHSKSEI YQHGAYEYIK ASDIHVLCFN ENLKLNWVKP TALIRHKAPS VLYKVVTGTG REALTTGHHS LFTFKNGVIV PTPVKDLKIG DRIAIPKRLP ESQILVKEIN IINYLKDRDY GLYIGNVKKL LNEALIRLGK KRTLEILGVK RVNWKKDVLV TRLFRFLELM QRANIHFNPA ELWIACKTHR ETMLPGVVPV TKELMRLLGY FTSEGGYDLN RVVFSNKDPR LQEDIINLCL KVFRLKPCQS SRQLRILFTS KPLRVLFEHI LGLHGGSENK NVPSLIWQMP LSHIAEFLRG YFSGDAGESS IEGRMIEATT KSRCLAVELV YLLLFFGIVS SKRMKVVKES TYWRIFIHSN DLEKFVNYIG FIQEEKNSLI RKYINERRIL SKRDTFSVKE IIPLLKELYK RDKRAGLMCA AYWRRKNIGR QRIHRLLRIF DREETCKGLR CLIDSDIFWD KISVIKKVKN EDTYVYDFDI NPTQNFIGGT GGVFLHNSTL FNALAEEAVP VDPSLFTTIS TTTRAVDVFG KKVLLTDTVG FIDRLPLTLI EAFHSTLEET IFSDLILLVV DVSEPHDDVG RKVNCCLDTI QKIGASGIPI ITALNKIDLL SEGELQHEEE LLKGVAPNRV PVSALYKTNI DLLKQGMAQH FRNYVQAMFS VPITDESMSF LSWLFSRADI RDIKYEGDSV KVVFESVPWF ADKVKGRVEQ FSGIFNT // ID A0A0Q0HAP0_9GAMM Unreviewed; 439 AA. AC A0A0Q0HAP0; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 30-AUG-2017, entry version 12. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:KPZ70155.1}; GN ORFNames=AN944_02539 {ECO:0000313|EMBL:KPZ70155.1}; OS Shewanella sp. P1-14-1. OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales; OC Shewanellaceae; Shewanella. OX NCBI_TaxID=1723761 {ECO:0000313|EMBL:KPZ70155.1, ECO:0000313|Proteomes:UP000050414}; RN [1] {ECO:0000313|EMBL:KPZ70155.1, ECO:0000313|Proteomes:UP000050414} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=P1-14-1 {ECO:0000313|EMBL:KPZ70155.1, RC ECO:0000313|Proteomes:UP000050414}; RA Millard Andrew; RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KPZ70155.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LKTL01000015; KPZ70155.1; -; Genomic_DNA. DR RefSeq; WP_055024961.1; NZ_LKTL01000015.1. DR EnsemblBacteria; KPZ70155; KPZ70155; AN944_02539. DR PATRIC; fig|1723761.3.peg.2601; -. DR Proteomes; UP000050414; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000050414}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000050414}. FT DOMAIN 198 364 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 164 191 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 439 AA; 49615 MW; 420AD1DFEBA94F23 CRC64; MFDRYEAGET AVLVHIDFSD DDRREDITEL QLLVESAGAR SVGVITGSRR SPDRKFFVGT GKVEELAAMV AATEANVVIF NHALSPAQER NLEQICECRV LDRTALILDI FAQRARTHEG KLQVELAQLR HMSTRLIRGW THLERQKGGI GMRGPGETQL ETDRRLLRGR IKSINRRLEK VDKQREQSRR SRKRSDLSTV SLVGYTNAGK STLFNALTTS EVYAADQLFA TLDPTLRKLD LPDGAVILAD TVGFIRHLPH DLVAAFKATL QETRQADLLL HVVDCADENM TENFDQVQNV LEEIEADTIP QLVVCNKIDL LEDFVPRIDY DDEGMPERVW VSAQKQIGFE LLLQAVNEHI GEVIVEHTLK IPATAGHYLG QFYRLDAIQQ KEYDDLGNCI LSVRLSDANW RRLTKQSQGE LETFIFETSQ EDSEVSVTC // ID A0A0Q0UJY4_9CORY Unreviewed; 508 AA. AC A0A0Q0UJY4; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 07-JUN-2017, entry version 12. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:KQB86559.1}; GN ORFNames=Clow_00767 {ECO:0000313|EMBL:KQB86559.1}; OS Corynebacterium lowii. OC Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae; OC Corynebacterium. OX NCBI_TaxID=1544413 {ECO:0000313|EMBL:KQB86559.1, ECO:0000313|Proteomes:UP000050488}; RN [1] {ECO:0000313|EMBL:KQB86559.1, ECO:0000313|Proteomes:UP000050488} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NML 130206 {ECO:0000313|EMBL:KQB86559.1, RC ECO:0000313|Proteomes:UP000050488}; RA Bernard K., Pacheco A.L., Mcdougall C., Burtx T., Weibe D., Tyler S., RA Olson A.B., Cnockaert M., Eguchi H., Kuwahara T., Nakayama-Imaohji H., RA Boudewijins M., Van Hoecke F., Bernier A.-M., Vandamme P.; RT "Corynebacteirum lowii and Corynebacterium oculi species nova, derived RT from human clinical disease and and emended description of RT Corynebacterium mastiditis."; RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KQB86559.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LKEV01000002; KQB86559.1; -; Genomic_DNA. DR EnsemblBacteria; KQB86559; KQB86559; Clow_00767. DR PATRIC; fig|1544413.3.peg.768; -. DR Proteomes; UP000050488; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000050488}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000050488}. FT DOMAIN 274 450 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 233 260 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 508 AA; 55002 MW; CDD0E67D004C2F46 CRC64; MKNPMDSTDS HDDLLAQAFA GSGADGGASI SGDEPTVGDL DLSERNSLRR VNRQTTIHAE EQADGYEVEY RKLRLERVIL VGVWTQGTLA EVEATMNELA ALAETAGAEV VEMLYQRRDK PDSGTYVGSG KVEELRDIVA ATGADTVICD GELNPGQLVA LENALNTKVI DRTMLILDIF AQHAKSKEGK AQVSLAQMEY LITRVRGWGG NLSRQAGGRA GSNGGVGLRG PGETKIEADR RRLRADMARL RKELAAMKTS REIKRSRRSA SLTPKIAIAG YTNAGKSSLI NALTGAGVLV EDALFATLDP TTRKAQLADG RSIIFTDTVG FVRHLPTQLV EAFKSTLEEV LDADLMLHVV DGSDPFPLKQ IQAVNHVIAD IVKETGTPAP PEVIVVNKVD IADSLALAEL RHVIEDVVFV SAATGEGIGE LESRIELFLN TLDSHVLLEV PFTRGDVVSR VHEFGTILGE EYTDSGTRLD VRLPRQLAEE LREFEVAVGP HETAEERP // ID A0A0Q0VP61_9BACT Unreviewed; 429 AA. AC A0A0Q0VP61; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 12-APR-2017, entry version 9. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=APR54_03520 {ECO:0000313|EMBL:KQC09901.1}; OS Candidatus Cloacimonas sp. SDB. OC Bacteria; Candidatus Cloacimonetes; Candidatus Cloacimonas. OX NCBI_TaxID=1732214 {ECO:0000313|EMBL:KQC09901.1, ECO:0000313|Proteomes:UP000052007}; RN [1] {ECO:0000313|EMBL:KQC09901.1, ECO:0000313|Proteomes:UP000052007} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SDB {ECO:0000313|EMBL:KQC09901.1}; RA Wawrik B., Marks C.R., Davidova I.A., Mcinerney M.J., Pruitt S., RA Duncan K., Suflita J.M., Callaghan A.V.; RT "Methanogenic Paraffin-Utilizing Consortium."; RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KQC09901.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LKUH01000174; KQC09901.1; -; Genomic_DNA. DR Proteomes; UP000052007; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000052007}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000052007}. FT DOMAIN 195 364 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 429 AA; 49785 MW; A564E8C3270E37C4 CRC64; MPDRDKVILV GVYTGDISRE YYDETMLELQ KLADTAGVDV VKTYVQILPR PNTATYIGSG KIKEISSYAH NHQVYTLIFN NNLSPSQSRN ISDQTRCNVV DRTELILDIF ATHARTKQSR IQVELAQLEY SYTKLKRMWK HLSRIQGGIG FRGPGETQIE TDRREIRKKV QILKKKVKDI ENNSLVKRKK RNKIISISLV GYTNTGKSTL FNLLTSEQRY AEDQLFATLD SLTRVIRINS EENLVLTDTI GFIRNLPHRL VASFHSTLLE VIEADLLMHI VDLSRPNLYE YIEAVDKVLK ELKVLDKSIL MVFNKCDLVA GPYFTFLKRQ LLHEYPDSVF ISARTGEGMD QLNSKLQEFV GKYKNLLTLE IPYEMQNLIS FIYKVGEVME RKEKDDYTIL LTARIPRHFI KGIRQQIDDF KFLQYINKK // ID A0A0Q0XHI8_9FLAO Unreviewed; 403 AA. AC A0A0Q0XHI8; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=AAY42_11965 {ECO:0000313|EMBL:KQC30506.1}; OS Flagellimonas sp. DK169. OC Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales; OC Flavobacteriaceae; Flagellimonas. OX NCBI_TaxID=1547436 {ECO:0000313|EMBL:KQC30506.1, ECO:0000313|Proteomes:UP000050827}; RN [1] {ECO:0000313|EMBL:KQC30506.1, ECO:0000313|Proteomes:UP000050827} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DK169 {ECO:0000313|EMBL:KQC30506.1, RC ECO:0000313|Proteomes:UP000050827}; RA Kwon Y.M., Kim S.-J.; RT "Complete genome of flavobacterium."; RL Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KQC30506.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LCTZ01000002; KQC30506.1; -; Genomic_DNA. DR RefSeq; WP_055395501.1; NZ_LCTZ01000002.1. DR EnsemblBacteria; KQC30506; KQC30506; AAY42_11965. DR PATRIC; fig|1547436.3.peg.2472; -. DR Proteomes; UP000050827; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000050827}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000050827}. FT DOMAIN 200 385 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 403 AA; 46519 MW; F0B983F5E5257912 CRC64; MLEKKVTDYE KAVLIGVISK DQDETKVTEY LDELEFLTYT AGGEVSCRFT QRMEIPNPKT LIGSGKMEEV EKYVKANDIG SVIFDDELSP AQQRNIEKQL RCKIIDRTSL ILDIFAQRAQ TSYARTQVEL AQYQYLLPRL TGLWTHLERQ KGGIGMRGPG ETEIETDRRI VRDRISLLKK KLTKIDRQME TQRGNRGALV RVALVGYTNV GKSTLMNVIS KSDVFAENKL FATLDTTVRK VVIGNLPFLL SDTVGFIRKL PTQLVESFKS TLDEVREADL LLHVVDISHP NFEEHIASVN KILDEIKSAD KKTIMVFNKI DQYEAEVIEE DDLVTEPTKA HFTIEDWKNT WMEKIGDRAL FISALNKENL DEFRKRVYDE VRDIHVTRFP YNNFLYPEHL DQY // ID A0A0Q1A2Q3_9RHOB Unreviewed; 424 AA. AC A0A0Q1A2Q3; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=AL073_04175 {ECO:0000313|EMBL:KQB98099.1}; OS Loktanella sp. 1ANDIMAR09. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae; Loktanella. OX NCBI_TaxID=1700845 {ECO:0000313|EMBL:KQB98099.1, ECO:0000313|Proteomes:UP000050370}; RN [1] {ECO:0000313|EMBL:KQB98099.1, ECO:0000313|Proteomes:UP000050370} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=1ANDIMAR09 {ECO:0000313|EMBL:KQB98099.1, RC ECO:0000313|Proteomes:UP000050370}; RA Mas-Llado M., Nogales B., Bosch R.; RT "Draft genome sequence of Loktanella sp. 1ANDIMAR09."; RL Submitted (AUG-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KQB98099.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LIGP01000001; KQB98099.1; -; Genomic_DNA. DR RefSeq; WP_055292862.1; NZ_LIGP01000001.1. DR EnsemblBacteria; KQB98099; KQB98099; AL073_04175. DR PATRIC; fig|1700845.4.peg.865; -. DR Proteomes; UP000050370; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000050370}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000050370}. FT DOMAIN 204 373 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 163 190 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 424 AA; 47153 MW; 05C866EF0A6D3345 CRC64; MLAHDRPVTR AWVLHPELKN DQNRRAAEPA LAEGLALAAA LPNLDVIGGT IVRLPKIQPG KLFGKGKIAE LKQVFHDAEI ELVLIDGPVT PVQQRNLEKE WGVKLLDRTG LILEIFSDRA RTSEGVLQVE MAALSYQRTR LVRAWTHLER QRGGLGFVGG PGETQIEADR RAIDEQLNRL RKQLAKVVKT RELHRASRAK VPFPIVALVG YTNAGKSTLF NRLTGAEVFA KDMLFATLDP TMRKIVLPTG DEIIMSDTVG FISDLPTELV AAFRATLEEV LDADLIVHVR DISHEQTEEQ AQDVRAILQS LGVADEAPII EVWNKTDLLE GDARDAVLTQ AARMDDLYAI SAVTGEGLDT LLAAIPDKLK DPRSEEKLTL TFAEGRKRAW LFDAGIVTDE VQTETGYDLT VFWTQLQKER FVRL // ID A0A0Q1ABZ5_9BACT Unreviewed; 426 AA. AC A0A0Q1ABZ5; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 12-APR-2017, entry version 9. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=APR54_01795 {ECO:0000313|EMBL:KQC06396.1}; OS Candidatus Cloacimonas sp. SDB. OC Bacteria; Candidatus Cloacimonetes; Candidatus Cloacimonas. OX NCBI_TaxID=1732214 {ECO:0000313|EMBL:KQC06396.1, ECO:0000313|Proteomes:UP000052007}; RN [1] {ECO:0000313|EMBL:KQC06396.1, ECO:0000313|Proteomes:UP000052007} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SDB {ECO:0000313|EMBL:KQC06396.1}; RA Wawrik B., Marks C.R., Davidova I.A., Mcinerney M.J., Pruitt S., RA Duncan K., Suflita J.M., Callaghan A.V.; RT "Methanogenic Paraffin-Utilizing Consortium."; RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KQC06396.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LKUH01000390; KQC06396.1; -; Genomic_DNA. DR Proteomes; UP000052007; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000052007}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000052007}. FT DOMAIN 200 365 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 426 AA; 48638 MW; 31828947849BEE69 CRC64; MSDKNKAILI GICTDNRIHE EKKASLQELQ KLADTAGVET VGRRIQNRES PDKRFYAGKG FLAEIIREMS EKNAGLLIFD NELSPSQGRN IEQEFEISVT DRTEVILKIF QEHAQTKEAR LQVRLAELQY QLPRLKRLWG HLDRVKGQAT GSSGTARGMG EKQIEVDKRL IRIEISRLKR EIAKIYRQKE TQRKQREKIR KVCLVGYTNA GKSTLFNQLT QAGVLVEDKL FATLDTTTRK LELDKGRDMI ISDTVGFIAN LPHHLVASFR ATLKDVVDAD LLLHVVDASD ENFSKNRQEV LQVLEQIGAD EIDQVLILNK MDITDKVILN SLLKTYPDSI TVSAARGEKM EELLETIDAR LHEARKRVLF IPHQKQRILS HLYELGKIVE MEYEEKGVKI TAVLNKEDLP EFEKYIISPG LKSDSK // ID A0A0Q1B6M1_9EURY Unreviewed; 420 AA. AC A0A0Q1B6M1; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 10-MAY-2017, entry version 9. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=APR56_06185 {ECO:0000313|EMBL:KQC12618.1}; OS Methanosaeta sp. SDB. OC Archaea; Euryarchaeota; Methanomicrobia; Methanosarcinales; OC Methanosaetaceae; Methanosaeta. OX NCBI_TaxID=1735328 {ECO:0000313|EMBL:KQC12618.1, ECO:0000313|Proteomes:UP000051107}; RN [1] {ECO:0000313|EMBL:KQC12618.1, ECO:0000313|Proteomes:UP000051107} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SDB {ECO:0000313|EMBL:KQC12618.1}; RA Wawrik B., Marks C.R., Davidova I.A., Mcinerney M.J., Pruitt S., RA Duncan K., Suflita J.M., Callaghan A.V.; RT "Metagenomic Analysis of a Methanogenic Paraffin-Utilizing RT Consortium."; RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KQC12618.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LKUG01001073; KQC12618.1; -; Genomic_DNA. DR Proteomes; UP000051107; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000051107}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}. FT DOMAIN 188 357 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 420 AA; 47296 MW; 27E76851282E202F CRC64; MNRAKTAVLL FREDPRDEPH PEKMAELLGL AEAADYRVLG EISQRRGRDR RFQLGRGKIA EAASLSPDRL IFNDPLSPGQ VFNITKEFEV GAMDRFNLIL EIFASRASTR EAKLQVELAR LSYEAPFVRT IESLKRLSER PGYRGSGSYD VSMYRDIRGR MAKIRTELRA VEETGERRRE RRRKLGFDLV ALAGYTNAGK STLFNRLAEE TVTAKDQPFT TLSPTTRAVA VRERRFLLTD TVGFIDDLPL FLIKAFRSTL AEIVEADLVL LVVDLSDPPE VLREKLVSCH QTLWDCGCYA SIVSVLNKVD RISPEDALER YELMRDLAPN PVFISAREGD GLEGLLDQIA EKLPLLEMFE IHLPSTEAGM GQLSRLYDVA DPIEVKYGKE IEVLLRGRRE IVARALKGAG KPNMSPLAEG // ID A0A0Q1BCD6_9DELT Unreviewed; 360 AA. AC A0A0Q1BCD6; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 10-MAY-2017, entry version 9. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=APR63_13160 {ECO:0000313|EMBL:KQC14959.1}; OS Desulfuromonas sp. SDB. OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfuromonadales; OC Desulfuromonadaceae; Desulfuromonas. OX NCBI_TaxID=1735325 {ECO:0000313|EMBL:KQC14959.1, ECO:0000313|Proteomes:UP000051310}; RN [1] {ECO:0000313|EMBL:KQC14959.1, ECO:0000313|Proteomes:UP000051310} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SDB {ECO:0000313|EMBL:KQC14959.1}; RA Wawrik B., Marks C.R., Davidova I.A., Mcinerney M.J., Pruitt S., RA Duncan K., Suflita J.M., Callaghan A.V.; RT "Metagenomic Analysis of a Methanogenic Paraffin-Utilizing RT Consortium."; RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KQC14959.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LKUE01000035; KQC14959.1; -; Genomic_DNA. DR Proteomes; UP000051310; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000051310}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000051310}. FT DOMAIN 193 355 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 154 181 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 360 AA; 40561 MW; DBC77BFC7BA0989E CRC64; MEKYIAVGLS SYIKTDQEKI KILLDELKIL IKTLGSEITE SFFQSRISPD PKYFIGSGKL TEIKQCAHQL NLQGIIFVNE ISPSQIRNIE DFTELKIITR RDVILDIFAR HASSQLAKAE VEMAQLKHIS SRLVGSTSHL SRLGGGIGTR GPGEKKLEMD RRNIQKRMKT LTKTLEKNKK ALQVQRKRRK NVYQISLVGY TNAGKSTLLN ALTKSKVLVA NQLFSTIDTT TRKLASPYNS IPIILSDTVG FILDLPPELI DSFQATLDEV VQADLRLIVI DLSDPLYEIK LTSVEKTLKR LNCLDLPKFY VYNKIDTSSV SQYPNEADNF YVSARTGEGL DNLKNALIET AKFKQQCPHP // ID A0A0Q1FV20_9DELT Unreviewed; 547 AA. AC A0A0Q1FV20; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 12-APR-2017, entry version 8. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=APR62_09240 {ECO:0000313|EMBL:KQC11687.1}; OS Smithella sp. SDB. OC Bacteria; Proteobacteria; Deltaproteobacteria; Syntrophobacterales; OC Syntrophaceae; Smithella. OX NCBI_TaxID=1735324 {ECO:0000313|EMBL:KQC11687.1, ECO:0000313|Proteomes:UP000051978}; RN [1] {ECO:0000313|EMBL:KQC11687.1, ECO:0000313|Proteomes:UP000051978} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SDB {ECO:0000313|EMBL:KQC11687.1}; RA Wawrik B., Marks C.R., Davidova I.A., Mcinerney M.J., Pruitt S., RA Duncan K., Suflita J.M., Callaghan A.V.; RT "Metagenomic Analysis of a Methanogenic Paraffin-Utilizing RT Consortium."; RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KQC11687.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LKUC01000004; KQC11687.1; -; Genomic_DNA. DR Proteomes; UP000051978; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000051978}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000051978}. FT DOMAIN 377 542 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 547 AA; 61797 MW; F542A8205A8638A1 CRC64; MNKIFGNTTG LRVAQIKQIE RLGRRGMPPE NIITNDLARQ LASISREINR QIGLLINRKG EISSIIVGDH KSILIPDLER FRSSSTRFRG LRLIHTHLNS EELSDEDLTD LSHLRLDLIG ALEVCEDGSP GVLNWAHLVP ENPAGDYWLI MTPEEPHRLK INFLSFIQAL EDEFTKKQRV RKIDAAEKAI LLRVEKNPLT GAEASLAELA QLARTCGVEV FDSIVQYRPQ PDPKFMVGKG KLLAIDLRAS QIGANMLIFD HELTPAQARS ISNFTGLKII DRTQVILDIF ARRAHSREGK IQVELAQLRY RLPRLMHMDT SLSRLAGGIG GTGPGETKLE IDRRRIRERI HHLEKDLKAI TKSRRQRYSK REKIGLPIIS IVGYTNAGKS TLLNTLTKST VLVEDKLFAT LDTKSARLRF PKDTEAIITD TVGFIRNLPE ELFTAFRATL DELLDANILL HVIDVSNSQF EDQIDAVEKI LEELEINDKP TIRVLNKSDR VTDKEMLQNL CRRLDAFAVS ALDKKTLFGL MEKIEALLSG NHSFSVR // ID A0A0Q2UDI7_MYCGO Unreviewed; 478 AA. AC A0A0Q2UDI7; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=AO501_32280 {ECO:0000313|EMBL:KQH78656.1}; OS Mycobacterium gordonae. OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae; OC Mycobacterium. OX NCBI_TaxID=1778 {ECO:0000313|EMBL:KQH78656.1, ECO:0000313|Proteomes:UP000051677}; RN [1] {ECO:0000313|EMBL:KQH78656.1, ECO:0000313|Proteomes:UP000051677} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CTRI 14-8773 {ECO:0000313|EMBL:KQH78656.1, RC ECO:0000313|Proteomes:UP000051677}; RA Ustinova V., Smirnova T., Blagodatskikh K., Varlamov D., Larionova E., RA Chernousova L.; RT "Mycobacterium gordonae draft genome assembly."; RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KQH78656.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LKTM01000179; KQH78656.1; -; Genomic_DNA. DR RefSeq; WP_055578404.1; NZ_LKTM01000179.1. DR EnsemblBacteria; KQH78656; KQH78656; AO501_32280. DR Proteomes; UP000051677; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000313|EMBL:KQH78656.1}; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000051677}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900, KW ECO:0000313|EMBL:KQH78656.1}. FT DOMAIN 254 423 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 213 247 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 478 AA; 51621 MW; FB5B2F1FEA556683 CRC64; MKNSESFPEF ADRTGPEPST GELALEDRSA LRRVVGLSTE LTDISEVEYR QLRLERVVLV GVWTEGTSAD NQASLAELAA LAETAGSQVL EGLIQRRDRP DPSTYIGSGK AQELREVVLA TGADTVICDG ELSPAQLTAL EKAVKVKVID RTALILDIFA QHATSREGKA QVSLAQMEYM LPRLRGWGES MSRQAGGRAG GSGGGVGLRG PGETKIETDR RRIRERMSKL KREIRAMKQV RDTQRSRRLH ADMPSIAIVG YTNAGKSSVL NALTGAGVLV QDALFATLEP TTRRTEFDDG RPFVLTDTVG FVRHLPTQLV EAFRSTLEEV VDADLLVHVV DGSDVNPLAQ ISAVRQVISD VVADHGAEAP PELVVVNKTD AAGDLMLARL RHELPGAVFV SARTGDGIDA LRRRMAELAV PTDTAVDVVI PYDRGDLVAR VHSDGRVHQA DHQADGTRIQ ARVPVALAAA LRQFGSDT // ID A0A0Q2Y8C2_9RHOB Unreviewed; 425 AA. AC A0A0Q2Y8C2; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=AN189_04340 {ECO:0000313|EMBL:KQI69631.1}; OS Loktanella sp. 3ANDIMAR09. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae; Loktanella. OX NCBI_TaxID=1225657 {ECO:0000313|EMBL:KQI69631.1, ECO:0000313|Proteomes:UP000051463}; RN [1] {ECO:0000313|EMBL:KQI69631.1, ECO:0000313|Proteomes:UP000051463} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=3ANDIMAR09 {ECO:0000313|EMBL:KQI69631.1, RC ECO:0000313|Proteomes:UP000051463}; RA Mas-Llado M., Nogales B., Bosch R.; RT "Draft genome sequence of Loktanella sp. 3ANDIMAR09."; RL Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KQI69631.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LJAK01000002; KQI69631.1; -; Genomic_DNA. DR RefSeq; WP_056031576.1; NZ_LJAK01000002.1. DR EnsemblBacteria; KQI69631; KQI69631; AN189_04340. DR PATRIC; fig|1225657.3.peg.888; -. DR Proteomes; UP000051463; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000051463}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000051463}. FT DOMAIN 204 373 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 425 AA; 46991 MW; B6234F9F8589FC93 CRC64; MLEHDRPITR AYVLHPDLKT DRTRRAADPA LEEAVSLAAA LPDLQVVGAE VVRLPKLLPG TLFGKGKIAE LKDRMKAEEV ELVLIDGHVT PVQQRNLEKA WDVKLLDRTG LILEIFSDRA RTAEGVLQVE MAALSYQRTR LVRAWTHLER QRGGLGFVGG PGETQIEADR RAIDMQLQAL KRQLEKVVKT RTLHRAARAK VPYPIVALVG YTNAGKSTLF NRLTGADVFA KDMLFATLDP TMRQIELPEG DKIIMSDTVG FISDLPTELV AAFRATLEEV LDADLIVHVR DISHPQTEEQ SKDVMAILTS LGVADDAPLL EVWNKIDRLP SDDHDGIVTQ AARTEDIFAI SAITGEGLDP LLDAISEVLK DPRTADQLTL GFGAGKARAW LFDQGVVTGE RQTEDGYVID VFWTQTQASR FGKLD // ID A0A0Q3KPY1_9BRAD Unreviewed; 461 AA. AC A0A0Q3KPY1; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=ARD30_02550 {ECO:0000313|EMBL:KQK31779.1}, GN SAMN05660750_01302 {ECO:0000313|EMBL:SKB57082.1}; OS Bosea thiooxidans. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Bradyrhizobiaceae; Bosea. OX NCBI_TaxID=53254 {ECO:0000313|EMBL:KQK31779.1, ECO:0000313|Proteomes:UP000051562}; RN [1] {ECO:0000313|EMBL:KQK31779.1, ECO:0000313|Proteomes:UP000051562} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CGMCC 9174 {ECO:0000313|EMBL:KQK31779.1, RC ECO:0000313|Proteomes:UP000051562}; RA Wang X.; RT "Draft genome of Bosea thiooxidans."; RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:SKB57082.1, ECO:0000313|Proteomes:UP000190130} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 9653 {ECO:0000313|EMBL:SKB57082.1, RC ECO:0000313|Proteomes:UP000190130}; RA Peterson S.W.; RL Submitted (FEB-2017) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LMAR01000012; KQK31779.1; -; Genomic_DNA. DR EMBL; FUYX01000003; SKB57082.1; -; Genomic_DNA. DR RefSeq; WP_055726982.1; NZ_LMAR01000012.1. DR EnsemblBacteria; KQK31779; KQK31779; ARD30_02550. DR Proteomes; UP000051562; Unassembled WGS sequence. DR Proteomes; UP000190130; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000051562}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000051562}. FT DOMAIN 227 401 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 461 AA; 50881 MW; 4BA2D59A743BDEA3 CRC64; MAASRDNEQE RAAPKPLDEI ERDIAANTRA YVVGPYLQKR GVAADANQRS FAARLDEAAG LAAAIDLTVV EPVQVLLTAL RPATYLGKGK VEELAERIKL EEIGLVVMDC ALSPVQQRNL EKAFGCKVID RTGLILEIFG RRARTKEGAL QVELAHLNYQ KSRLVRSWTH LERQRGGFGF LGGPGETQIE ADRRIIQERM SKIERDLEQV KRTRSLHRAS RKRVPYPIVA LVGYTNAGKS TLFNRLTSAE VLAQDMLFAT LDPTARAIKL PHGARIMLSD TVGFISDLPT QLVAAFRATL EDAIEADVLL HVRDVAHEDT QAQAADVQAI LRDLGINPDD GQRVIEVWNK ADLLDPAERE RQLGIASLRP AEARPVLVSA LTGEGIERLT RAIETRIAHS RPVYSLALAP GDGKSLAWLH ANGEILRRED AEDGSLQLIV RLPPEREGAF SARFPEAIRQ S // ID A0A0Q3RYF7_9BACI Unreviewed; 423 AA. AC A0A0Q3RYF7; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=AN959_11780 {ECO:0000313|EMBL:KQL35016.1}; OS Psychrobacillus sp. FJAT-21963. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; OC Psychrobacillus. OX NCBI_TaxID=1712028 {ECO:0000313|EMBL:KQL35016.1, ECO:0000313|Proteomes:UP000051878}; RN [1] {ECO:0000313|EMBL:KQL35016.1, ECO:0000313|Proteomes:UP000051878} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=FJAT-21963 {ECO:0000313|EMBL:KQL35016.1, RC ECO:0000313|Proteomes:UP000051878}; RA Liu B., Wang J., Zhu Y., Liu G., Chen Q., Chen Z., Lan J., Che J., RA Ge C., Shi H., Pan Z., Liu X.; RT "Genome sequencing project for genomic taxonomy and phylogenomics of RT Bacillus-like bacteria."; RL Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KQL35016.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LJIY01000004; KQL35016.1; -; Genomic_DNA. DR RefSeq; WP_056830968.1; NZ_LJIY01000004.1. DR EnsemblBacteria; KQL35016; KQL35016; AN959_11780. DR PATRIC; fig|1712028.3.peg.3930; -. DR Proteomes; UP000051878; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000051878}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000051878}. FT DOMAIN 200 368 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 159 193 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 423 AA; 48226 MW; D797692B68337FD5 CRC64; MDELLEKAIV VAVNLQSDEH FEYELEELHN LAKALNVEVV GEVTQNLERV TSSHYVGTGK VEEIKNFYEE AGANLVIFND ELSPSQIRNL EKELECKVID RTMLILDIFA RRAKSNEAQM QVELAQLQYM LPRLVGLRAS LGRQGGGTGG GFKNRGAGET KLELDRRKIE DQIAKLKREL EHVKDQRETQ RKQRKKNAIP VVSLVGYTNA GKSTIMNQLL HKIGQEESKQ VFEKDMLFAT LETSVRQIKL QDQKEFLLTD TVGFVSKLPH HLVKAFRSTL EEARNANLLL HVVDVSNEEH RYMMEVTNET LHAVGVEDVP TIYVYNKSDL AELKYPHVSG NNIWISAKEG TGLDELLELI KKHIFSNYVQ CSLLVPFDRG DIVSYLNEHA SIMSTSYEEE GTLVKVELKQ SDYNRFLEFV YAE // ID A0A0Q3TET1_9BACI Unreviewed; 419 AA. AC A0A0Q3TET1; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=AN964_02995 {ECO:0000313|EMBL:KQL52600.1}; OS Bacillus shackletonii. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus. OX NCBI_TaxID=157838 {ECO:0000313|EMBL:KQL52600.1, ECO:0000313|Proteomes:UP000051888}; RN [1] {ECO:0000313|EMBL:KQL52600.1, ECO:0000313|Proteomes:UP000051888} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=LMG 18435 {ECO:0000313|EMBL:KQL52600.1, RC ECO:0000313|Proteomes:UP000051888}; RA Liu B., Wang J., Zhu Y., Liu G., Chen Q., Chen Z., Lan J., Che J., RA Ge C., Shi H., Pan Z., Liu X.; RT "Genome sequencing project for genomic taxonomy and phylogenomics of RT Bacillus-like bacteria."; RL Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KQL52600.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LJJC01000004; KQL52600.1; -; Genomic_DNA. DR RefSeq; WP_055738295.1; NZ_LJJC01000004.1. DR EnsemblBacteria; KQL52600; KQL52600; AN964_02995. DR PATRIC; fig|157838.3.peg.661; -. DR Proteomes; UP000051888; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000051888}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000051888}. FT DOMAIN 198 366 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 157 184 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 419 AA; 47646 MW; 2381E6705CE64AA6 CRC64; MMAEREKAIL VGANLGTQQN FDYSMEELAN LTAACEMEVT GIITQNLQRI NKSHYIGTGK IKEIIALLAA TNARTVIFND ELSPSHIRNL EKELECRVID RTILILDIFA ERAKTKEAQL QVEVAKLQYM LPRLIGLRES LGRQGGGSGL KNRGSGETKL ELDRRKIEEK ITTLNKELEV LVSHRQTQRK RRRKNNLPVV SLVGYTNAGK STIMNAMVEL YNPAANKQVF EKDMLFATLE TSVRNIPLPD AKSFLLTDTV GFVDKLPHHL VKAFRSTLEE VAESDLLIHV VDYSNPNHKQ MMDITEQTLK AIGVEDIPTI YAYNKADLLE IELPAVQHNT VYLSAKQRIG IMELVEMIRQ QIFKNYVQCE MLIPYDQGNI VSYFNKNAEI LSTSYENEGT KLLMECRTAD FEKYQEYVV // ID A0A0Q3U381_9BACI Unreviewed; 422 AA. AC A0A0Q3U381; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=AN960_09750 {ECO:0000313|EMBL:KQL39244.1}; OS Bacillus sp. FJAT-25509. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus. OX NCBI_TaxID=1712029 {ECO:0000313|EMBL:KQL39244.1, ECO:0000313|Proteomes:UP000050831}; RN [1] {ECO:0000313|EMBL:KQL39244.1, ECO:0000313|Proteomes:UP000050831} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=FJAT-25509 {ECO:0000313|EMBL:KQL39244.1, RC ECO:0000313|Proteomes:UP000050831}; RA Liu B., Wang J., Zhu Y., Liu G., Chen Q., Chen Z., Lan J., Che J., RA Ge C., Shi H., Pan Z., Liu X.; RT "Genome sequencing project for genomic taxonomy and phylogenomics of RT Bacillus-like bacteria."; RL Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KQL39244.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LJIZ01000016; KQL39244.1; -; Genomic_DNA. DR RefSeq; WP_056470283.1; NZ_LJIZ01000016.1. DR EnsemblBacteria; KQL39244; KQL39244; AN960_09750. DR PATRIC; fig|1712029.3.peg.2182; -. DR Proteomes; UP000050831; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000050831}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000050831}. FT DOMAIN 199 361 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 422 AA; 48619 MW; BBD7AF31EC9415C3 CRC64; MSNELREKAI LVGCQLQNVD DDRFNYSMDE LASLTKTANG EVVLITTQKR TKYHPALYIG TGKLEELEAA IAELEPDVVI FNNELTPSQI RNLSARLEKR VIDRTQLILD IFAQRAKTKE GKLQVELAQL QYLMPRLVGQ GTELSRLGGG IGTRGPGETK LESDRRHIRK RIDDIKQQLN IVVEHRKRYR ERRKKNEMFH ISLVGYTNAG KSTLFNRLTK SDVYEQDLLF ATLDPTTRKF VLSNGMTTLL TDTVGFIQDL PTALIAAFRS TLEEATEADF ILHVVDASHE NYKSHEVTVS KLLNDLDVKN IPILTVYNKI DQVHEDFVPS PSEGFIEMSA LNEDDLSKLR YRIEFECKQY MEHFEAFVPA YEGKLIHEIK KLTMIESINF NEDAEIYQIS GYVFKEHSIY DTVKRYRIYK EQ // ID A0A0Q3URC9_AMAAE Unreviewed; 479 AA. AC A0A0Q3URC9; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 10-MAY-2017, entry version 7. DE SubName: Full=Putative GTP-binding protein 6 {ECO:0000313|EMBL:KQK77458.1}; GN ORFNames=AAES_127698 {ECO:0000313|EMBL:KQK77458.1}; OS Amazona aestiva (Blue-fronted Amazon parrot). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda; OC Coelurosauria; Aves; Neognathae; Psittaciformes; Psittacidae; Amazona. OX NCBI_TaxID=12930 {ECO:0000313|EMBL:KQK77458.1, ECO:0000313|Proteomes:UP000051836}; RN [1] {ECO:0000313|EMBL:KQK77458.1, ECO:0000313|Proteomes:UP000051836} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=FVVF132 {ECO:0000313|EMBL:KQK77458.1}; RA Millard Andrew; RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KQK77458.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LMAW01002756; KQK77458.1; -; Genomic_DNA. DR Proteomes; UP000051836; Unassembled WGS sequence. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR CDD; cd01878; HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 4: Predicted; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000051836}; KW Reference proteome {ECO:0000313|Proteomes:UP000051836}. FT DOMAIN 252 416 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 17 40 {ECO:0000256|SAM:Coils}. FT COILED 218 241 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 479 AA; 53828 MW; CB0A4EA913A27E66 CRC64; MGRNGRRLGL GNPGPSTSEE EEEEEEEEED EDEAELEELL GPSPLAAEPG VQRVVVVHPA VKWGPKKSPL TTAELQIAEA VALVDTLQNW TVLDKIIIPT KNPDKKLIFG KGNFQVLTEK IKKLPQVTAV FLNVERISSL TKKELEDAWG VKVFDRYTVV LHIFRCNART KEAKLQIALA EVPLLRSNLK NEVSQLDQQR GGSRYIMGSG ETFMETQYRI LKEKELKIRN ALEKLRRKRS LLRTQRKKRE FPIISVMGYT NCGKTTLIKA LTGEAGIQPR DQLFATLDIT AHAGYLPSHM AVIYVDTIGF LTDLPHNLVE SFSATLEEVV YSDLIVHVRD ITHPETILQK ATVLSVLKNL NLPSHLLDSM VEVHNKVDLI ERYKPTEXNA LAVSALRGQG LEELKEEIEK KILTVTGKKI LTVNINLEGP QLSWLYKEAT VQEVEVMPEE GTARVKVIIG NSAFGKYKSL FPNSKIYMP // ID A0A0Q3WYY0_9BACI Unreviewed; 416 AA. AC A0A0Q3WYY0; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=AN964_14280 {ECO:0000313|EMBL:KQL54546.1}; OS Bacillus shackletonii. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus. OX NCBI_TaxID=157838 {ECO:0000313|EMBL:KQL54546.1, ECO:0000313|Proteomes:UP000051888}; RN [1] {ECO:0000313|EMBL:KQL54546.1, ECO:0000313|Proteomes:UP000051888} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=LMG 18435 {ECO:0000313|EMBL:KQL54546.1, RC ECO:0000313|Proteomes:UP000051888}; RA Liu B., Wang J., Zhu Y., Liu G., Chen Q., Chen Z., Lan J., Che J., RA Ge C., Shi H., Pan Z., Liu X.; RT "Genome sequencing project for genomic taxonomy and phylogenomics of RT Bacillus-like bacteria."; RL Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KQL54546.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LJJC01000004; KQL54546.1; -; Genomic_DNA. DR RefSeq; WP_055740324.1; NZ_LJJC01000004.1. DR EnsemblBacteria; KQL54546; KQL54546; AN964_14280. DR PATRIC; fig|157838.3.peg.3177; -. DR Proteomes; UP000051888; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000051888}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000051888}. FT DOMAIN 198 359 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 416 AA; 47490 MW; 419EDA687E981995 CRC64; MTEIIKEKAI LVGCSLHDNE ERFQYSMEEL ASLTETAHGQ VVTMVSQKRE RIDSSTYIGK GKVEEIKRME EELETDLVIF NDELSPSQLR NLSNILNGRV IDRTQLILDI FAGRARSKEG KLQVELAQLQ YLLPRLIGQG TELSRLGGGI GTRGPGETKL ESDRRHIRRR ISEIKNQLET IVSHRERYRE RRKKNKTFQL ALVGYTNAGK STLFNRLSSA DSFEENLLFA TLDPLTRKVI LPSGYTALLT DTVGFIQDLP TTLIAAFSST LEEVKEADIL LHIVDASNPD YHNHEKTVHK LLEELEMDHL PQLTVYNKMD ERHPDFVPTA ENHIMISALR IEDRQLLKQK IEEAAIQIMV PYHVLIPSTE GKILAQLKVE TILRELVFLE EAQIYRCKGF AIADHPVLGL LEQYQQ // ID A0A0Q4B8H8_9BACE Unreviewed; 398 AA. AC A0A0Q4B8H8; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 07-JUN-2017, entry version 10. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=AL399_06200 {ECO:0000313|EMBL:KQM08662.1}; OS Candidatus Bacteroides periocalifornicus. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae; OC Bacteroides. OX NCBI_TaxID=1702214 {ECO:0000313|EMBL:KQM08662.1, ECO:0000313|Proteomes:UP000054172}; RN [1] {ECO:0000313|EMBL:KQM08662.1, ECO:0000313|Proteomes:UP000054172} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=12B {ECO:0000313|EMBL:KQM08662.1}; RA McLean J.S., Kelley S.; RT "Candidatus Bacteriodes Periocalifornicus."; RL Submitted (AUG-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KQM08662.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LIIK01000027; KQM08662.1; -; Genomic_DNA. DR PATRIC; fig|1702214.3.peg.516; -. DR Proteomes; UP000054172; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000054172}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000054172}. FT DOMAIN 201 386 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 398 AA; 44932 MW; 052AED39712934B3 CRC64; MAIDLSQPAP EAVIIVGVHT PDRQSYTTNE YLDELEFLVQ TAGGACVQRF IQQLPAPDSR TYIGSGKVLE VKAAVAEHEA GLVVFDDELS PTQQRNLEKE LECKVVDRTN LILDIFAQRA RTAYAKKQVE LAQYQYLLPR LAGLWTHLER QRGGIGMRGP GEREIETDRR IVRDRISKLK GELAQIDRQM ATQRQTRGQL VRVALVGYTN VGKSTIMNLL GKADVLAENK LFATLDTTVR RVSTEGGLPY LLSDTVGFIR KLPTQLIESF KSTLDEVREA DLLVHVVDIS HPRFQEQIAT VNETLRDLKV SEKPQLLVFN KIDAYRPAER EEYDLTPRAP ETFTLQELQA TWMNRDGANT VFISARTGEN LEGLKSELTR LVKGIQLERY PWSTGGWE // ID A0A0Q4BA99_9SPHN Unreviewed; 448 AA. AC A0A0Q4BA99; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 05-JUL-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=ASE49_13770 {ECO:0000313|EMBL:KQM13054.1}; OS Novosphingobium sp. Leaf2. OC Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales; OC Sphingomonadaceae; Novosphingobium. OX NCBI_TaxID=1735670 {ECO:0000313|EMBL:KQM13054.1, ECO:0000313|Proteomes:UP000050893}; RN [1] {ECO:0000313|EMBL:KQM13054.1, ECO:0000313|Proteomes:UP000050893} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Leaf2 {ECO:0000313|EMBL:KQM13054.1, RC ECO:0000313|Proteomes:UP000050893}; RA Millard Andrew; RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:KQM13054.1, ECO:0000313|Proteomes:UP000050893} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Leaf2 {ECO:0000313|EMBL:KQM13054.1, RC ECO:0000313|Proteomes:UP000050893}; RA Vorholt J.; RT "Functional overlap of the Arabidopsis leaf and root microbiotas."; RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KQM13054.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LMJY01000022; KQM13054.1; -; Genomic_DNA. DR EnsemblBacteria; KQM13054; KQM13054; ASE49_13770. DR Proteomes; UP000050893; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000050893}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000050893}. FT DOMAIN 206 392 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 448 AA; 49196 MW; 3D0053405A95AD1B CRC64; MNDETTGEVT RGARALVAYP QMRGRRDLDT EARLEEARGL ALAIGLEVVD ALAIVIREPR AGTLFGEGQI QNIATACEQN EAELVIVDGS LTAIQQRNLE DKLKRKVIDR TGLILEIFGE RAATAEGRLQ VELAHLDYQA GRLVRSWTHL ERQRGGFGFL GGPGETQIEA DRRLIRDRMA KIRRELEQVR RTRGLHRDRR EKAPWPVIAL VGYTNAGKST LFNRLTGANV MAENLLFATL DPTMRAIRLP GLEKAILSDT VGFISDLPTQ LVAAFRATLE EVTAADVIVH VRDIANPDTD SQKRQVLAVL ADLGVASADG ETLEEGEGSD TKPIPIIEVW NKWDILPPDQ AQLLKDAMAH RHDETIAAVS ALTGEGCEAL LDLASRTLTQ DAKVHTFVIP AADGQRLAFL HARGEVISEK DAGTGQNGPE LRLDVRLSQR EFGRFGSL // ID A0A0Q4CN68_9SPHN Unreviewed; 428 AA. AC A0A0Q4CN68; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 30-AUG-2017, entry version 18. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=ASE58_10255 {ECO:0000313|EMBL:KQM27314.1}; OS Sphingomonas sp. Leaf9. OC Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales; OC Sphingomonadaceae; Sphingomonas. OX NCBI_TaxID=1735674 {ECO:0000313|EMBL:KQM27314.1, ECO:0000313|Proteomes:UP000051210}; RN [1] {ECO:0000313|EMBL:KQM27314.1, ECO:0000313|Proteomes:UP000051210} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Leaf9 {ECO:0000313|EMBL:KQM27314.1, RC ECO:0000313|Proteomes:UP000051210}; RA Millard Andrew; RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:KQM27314.1, ECO:0000313|Proteomes:UP000051210} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Leaf9 {ECO:0000313|EMBL:KQM27314.1, RC ECO:0000313|Proteomes:UP000051210}; RA Vorholt J.; RT "Functional overlap of the Arabidopsis leaf and root microbiotas."; RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KQM27314.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LMKC01000003; KQM27314.1; -; Genomic_DNA. DR RefSeq; WP_055820640.1; NZ_LMKC01000003.1. DR EnsemblBacteria; KQM27314; KQM27314; ASE58_10255. DR Proteomes; UP000051210; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000051210}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}. FT DOMAIN 208 377 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 428 AA; 47166 MW; 8918B5045F3F5167 CRC64; MSNGFDRDAQ EFTRGAAAIV VLPDMGGSAR DADARLEETA GLALAIGVDV RHRVPFRVRA PKPATLIGSG QVDQLTQMVR DEDLQLAVFD AALTPVQQRN LETALGCKVI DRTGLILEIF GERARTAEGR LQVELAHLDY QAGRLVRSWT HLERQRGGFG FLGGPGETQI EADRRLIRDR MARLRRELDG VSRTRTLHRD RRQRAPWPVV ALVGYTNAGK STLFNRLTGA EVMAENLLFA TLDPTLRQVS LPGIDKAILS DTVGFVSDLP TQLVAAFKAT LEEVVSADLL IHVRDVAHPD TAAQASDVEA VLKEIGVDDT TPRIEAWNKL DLLSEDDRIE MLGEAAHRED IVALSALTGE GVDRLIRTVG GRLTEGHRRY RIALAPEDGA SAAWLHAHGE VTDHWIDDDH AVYDVRLAPA DYDRFLTR // ID A0A0Q4FY05_9SPHN Unreviewed; 432 AA. AC A0A0Q4FY05; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=ASE75_06565 {ECO:0000313|EMBL:KQM65884.1}; OS Sphingomonas sp. Leaf17. OC Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales; OC Sphingomonadaceae; Sphingomonas. OX NCBI_TaxID=1735683 {ECO:0000313|EMBL:KQM65884.1, ECO:0000313|Proteomes:UP000051777}; RN [1] {ECO:0000313|EMBL:KQM65884.1, ECO:0000313|Proteomes:UP000051777} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Leaf17 {ECO:0000313|EMBL:KQM65884.1, RC ECO:0000313|Proteomes:UP000051777}; RA Millard Andrew; RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:KQM65884.1, ECO:0000313|Proteomes:UP000051777} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Leaf17 {ECO:0000313|EMBL:KQM65884.1, RC ECO:0000313|Proteomes:UP000051777}; RA Vorholt J.; RT "Functional overlap of the Arabidopsis leaf and root microbiotas."; RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KQM65884.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LMKL01000004; KQM65884.1; -; Genomic_DNA. DR RefSeq; WP_055930810.1; NZ_LMKL01000004.1. DR EnsemblBacteria; KQM65884; KQM65884; ASE75_06565. DR Proteomes; UP000051777; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000051777}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000051777}. FT DOMAIN 208 377 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 432 AA; 47344 MW; 38918D9024529917 CRC64; MSTGFERDRG EFARGTRAIV VLPDQGDAQR DADARLAETA GLAMAIGVDV ADRIAFRVRQ AKPATLIGKG QCEQLAALVR MEDAGLVVFD ASLTPVQQRN LEKELETKVI DRTGLILEIF GERAATAEGR LQVELAHLDY QAGRLVRSWT HLERQRGGFG FLGGPGETQI EADRRLIRDR MARLRKELEQ VSRTRGLHRD RRQRAPWPVI ALVGYTNAGK STLFNRLTGA SVMAEDLLFA TLDPTLRQIS LPGVDKAILS DTVGFVSDLP TQLVAAFKAT LEEVVSADLL IHVRDIAHPD TEAQRADVEA VLAEIGVSET TPRFEVWNKL DLLGEDDAIE MRGHADHRDD VVAISALDGQ GMEALVTQVA ARLTAAHRRY TIMLDASDGA GAAWLHAHGE VLGQESDDLS TAYDVRLSEE DFARFNQRSA AS // ID A0A0Q4GRW0_9BURK Unreviewed; 376 AA. AC A0A0Q4GRW0; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=ASE76_06575 {ECO:0000313|EMBL:KQM75772.1}; OS Xylophilus sp. Leaf220. OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Xylophilus. OX NCBI_TaxID=1735686 {ECO:0000313|EMBL:KQM75772.1, ECO:0000313|Proteomes:UP000051325}; RN [1] {ECO:0000313|EMBL:KQM75772.1, ECO:0000313|Proteomes:UP000051325} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Leaf220 {ECO:0000313|EMBL:KQM75772.1, RC ECO:0000313|Proteomes:UP000051325}; RA Millard Andrew; RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:KQM75772.1, ECO:0000313|Proteomes:UP000051325} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Leaf220 {ECO:0000313|EMBL:KQM75772.1, RC ECO:0000313|Proteomes:UP000051325}; RA Vorholt J.; RT "Functional overlap of the Arabidopsis leaf and root microbiotas."; RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KQM75772.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LMKO01000012; KQM75772.1; -; Genomic_DNA. DR RefSeq; WP_055839301.1; NZ_LMKO01000012.1. DR EnsemblBacteria; KQM75772; KQM75772; ASE76_06575. DR Proteomes; UP000051325; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000051325}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000051325}. FT DOMAIN 186 359 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 376 AA; 41347 MW; 7CBE3A5130B896D6 CRC64; MGVDLGQPHF DGDLEELGLL AETAGLKPVA RVAAKRKAPD AALFVGSGKA DEIRMLAEQH GAVEILFDQA LSPAQQRNLE RHIGLPVSDR TFLILEIFAQ RARSHEGKLQ VELARLQYLS TRLVRRWSHL ERQRGGIGTR GGPGETQIEL DRRMIGDSIK RIKDRLLKVK RQQGTQRRQR ERRDVFNISL VGYTNAGKST LFNTLVKARA YAADQLFATL DTTTRQLYLA DAQRSVSLSD TVGFIRDLPH GLIDAFQATL REAVDADLLM HVVDASNPAF PEQMEQVQRV LAEIGAGDIP QLLVFNKLDA IAPEQAPRQI VDTFELDGLQ VPRIFTSAQE GLGIAELRAA LAAAVTSQHP AAMPPAGDTP LPDPTD // ID A0A0Q4HDQ0_9MICO Unreviewed; 507 AA. AC A0A0Q4HDQ0; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=ASE68_12115 {ECO:0000313|EMBL:KQM83846.1}; OS Agromyces sp. Leaf222. OC Bacteria; Actinobacteria; Micrococcales; Microbacteriaceae; Agromyces. OX NCBI_TaxID=1735688 {ECO:0000313|EMBL:KQM83846.1, ECO:0000313|Proteomes:UP000050813}; RN [1] {ECO:0000313|EMBL:KQM83846.1, ECO:0000313|Proteomes:UP000050813} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Leaf222 {ECO:0000313|EMBL:KQM83846.1, RC ECO:0000313|Proteomes:UP000050813}; RA Millard Andrew; RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:KQM83846.1, ECO:0000313|Proteomes:UP000050813} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Leaf222 {ECO:0000313|EMBL:KQM83846.1, RC ECO:0000313|Proteomes:UP000050813}; RA Vorholt J.; RT "Functional overlap of the Arabidopsis leaf and root microbiotas."; RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KQM83846.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LMKQ01000001; KQM83846.1; -; Genomic_DNA. DR RefSeq; WP_055858864.1; NZ_LMKQ01000001.1. DR EnsemblBacteria; KQM83846; KQM83846; ASE68_12115. DR Proteomes; UP000050813; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 2. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000050813}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000050813}. FT DOMAIN 284 449 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 507 AA; 54246 MW; 5852328A5CD223B1 CRC64; MNEAEDHPTD DAVERVLRTA DSAASVARFG AGEATSIMRT DAAGGSSTDG DQFEREDRAA LRRVAGLSTE LEDVTEVEYR QLRLENVVLI GVYSQGSQAD ADNSMRELAA LAETAGARVL DGLLQRRPHP DPSTYLGKGK AEDLRHVVAA VGADTVIADT ELAPSQRRAL EDVVKVKVID RTAVILDIFS QHAKSREGKA QVELAQLEYL LPRLRGWGES MSRQAGGQVG GAGAGMGSRG PGETKIELDR RRIHTRMAKL RKQIVGMKPA RDAKRANRRR NAIPSVAIAG YTNAGKSSLL NRITGAGLLV ENALFATLDA TVRRNTTADG RIYTIADTVG FVRNLPHQLV EAFRSTLEEV GDSDLIVHVV DAAHPDPAGQ IATVRDVIGD VGARDIPELI VFNKADLVGP EERLVLRGLA PDAVFASART GEGIDEVLAA ITRMLPDPAV EIDLLVPYDR GDVVSLLHET GRVISVDYVD EGTRVRAFAS PEQAAQLAGF AAASAAV // ID A0A0Q4JCW0_9SPHN Unreviewed; 444 AA. AC A0A0Q4JCW0; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 07-JUN-2017, entry version 10. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=ASE85_17020 {ECO:0000313|EMBL:KQN08627.1}; OS Sphingobium sp. Leaf26. OC Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales; OC Sphingomonadaceae; Sphingobium. OX NCBI_TaxID=1735693 {ECO:0000313|EMBL:KQN08627.1, ECO:0000313|Proteomes:UP000051336}; RN [1] {ECO:0000313|EMBL:KQN08627.1, ECO:0000313|Proteomes:UP000051336} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Leaf26 {ECO:0000313|EMBL:KQN08627.1, RC ECO:0000313|Proteomes:UP000051336}; RA Millard Andrew; RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:KQN08627.1, ECO:0000313|Proteomes:UP000051336} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Leaf26 {ECO:0000313|EMBL:KQN08627.1, RC ECO:0000313|Proteomes:UP000051336}; RA Vorholt J.; RT "Functional overlap of the Arabidopsis leaf and root microbiotas."; RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KQN08627.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LMKV01000002; KQN08627.1; -; Genomic_DNA. DR RefSeq; WP_056684736.1; NZ_LMKV01000002.1. DR EnsemblBacteria; KQN08627; KQN08627; ASE85_17020. DR Proteomes; UP000051336; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0016810; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds; IEA:InterPro. DR CDD; cd01878; HflX; 1. DR Gene3D; 2.30.40.10; -; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR011059; Metal-dep_hydrolase_composite. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 2. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000051336}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000051336}. FT DOMAIN 209 390 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 444 AA; 48764 MW; ED3AC070F0416D71 CRC64; MAIFNRDSDD EVARGARAVV VHAETHNADR RDSDARLEEA RGLALAIGID VRAAQAFRVR DRKPATLFGS GQVDQIATLA RQEEAELIIV DNSLSPVQQS NLEKACEAKV IDRTGLILEI FGERAATNEG RLQVELAHLD YQAGRLVRSW THLERQRGGF GFLGGPGETQ IEADRRMIRD RMAKIRRELD QVTRTRGLHR ARRQRAPWPV IALVGYTNAG KSTLFNRMTG ATVMAEDLLF ATLDPTMRQI ALPGLDKAIL SDTVGFVSDL PTQLIAAFRA TLEEVLSADL IVHVRDIAHA DSEAQRDDVL DVLGELGVAG EAALDRGEGE PAPPPILEAW NKLDLLNEED AAIVRETAAR RDDVVILSAL TGEGVDLLQR TISDRMTRGA KVYGLRIPVS DGATLAWLHE HGEVLSTMVE GEESRIDVRL SDAAFARYSK RAKG // ID A0A0Q4KX33_9SPHN Unreviewed; 434 AA. AC A0A0Q4KX33; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=ASE86_08420 {ECO:0000313|EMBL:KQN26165.1}; OS Sphingomonas sp. Leaf33. OC Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales; OC Sphingomonadaceae; Sphingomonas. OX NCBI_TaxID=1736215 {ECO:0000313|EMBL:KQN26165.1, ECO:0000313|Proteomes:UP000051455}; RN [1] {ECO:0000313|EMBL:KQN26165.1, ECO:0000313|Proteomes:UP000051455} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Leaf33 {ECO:0000313|EMBL:KQN26165.1, RC ECO:0000313|Proteomes:UP000051455}; RA Millard Andrew; RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:KQN26165.1, ECO:0000313|Proteomes:UP000051455} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Leaf33 {ECO:0000313|EMBL:KQN26165.1, RC ECO:0000313|Proteomes:UP000051455}; RA Vorholt J.; RT "Functional overlap of the Arabidopsis leaf and root microbiotas."; RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KQN26165.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LMLB01000001; KQN26165.1; -; Genomic_DNA. DR RefSeq; WP_056424560.1; NZ_LMLB01000001.1. DR EnsemblBacteria; KQN26165; KQN26165; ASE86_08420. DR Proteomes; UP000051455; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000051455}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000051455}. FT DOMAIN 208 377 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 434 AA; 47058 MW; 8C96E471E5040C0E CRC64; MSTGFDRDQE DFARGARAVV VLPDQGNAAR DAEARLEETA GLALAIGVEV AHKIAYRVRA PKPATLIGSG QVEQLAEMVK ADDLSLAVFD AGLTPVQQRN LETSLGCKVI DRTGLILEIF GERARTAEGR LQVELAHLDY QAGRLVRSWT HLERQRGGFG FLGGPGETQI EADRRLIRDR MARLRRELDQ VSRTRGLHRE RRQRAPWPVI ALVGYTNAGK STLFNRLSGS AVMAENLLFA TLDPTLRQIS LPGVDKAILS DTVGFVSELP TQLVAAFKAT LEEVVSADLL VHVRDVAHPD SAAQKADVEA VLAEIGVEEA IPRIEAWNKL DLLDGDARDD LLVEASRRDD VVPISALTGE GVDDLLATVS ALLTAGHRRY TITLDAGDGA GAAWLHQHGD VVSQSIDGAR ASYDVRLSPK DHDRFMARAE ADGA // ID A0A0Q4LBG3_9SPHN Unreviewed; 430 AA. AC A0A0Q4LBG3; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 05-JUL-2017, entry version 12. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=ASF00_06410 {ECO:0000313|EMBL:KQN30386.1}; OS Sphingomonas sp. Leaf34. OC Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales; OC Sphingomonadaceae; Sphingomonas. OX NCBI_TaxID=1736216 {ECO:0000313|EMBL:KQN30386.1, ECO:0000313|Proteomes:UP000051932}; RN [1] {ECO:0000313|EMBL:KQN30386.1, ECO:0000313|Proteomes:UP000051932} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Leaf34 {ECO:0000313|EMBL:KQN30386.1, RC ECO:0000313|Proteomes:UP000051932}; RA Millard Andrew; RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:KQN30386.1, ECO:0000313|Proteomes:UP000051932} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Leaf34 {ECO:0000313|EMBL:KQN30386.1, RC ECO:0000313|Proteomes:UP000051932}; RA Vorholt J.; RT "Functional overlap of the Arabidopsis leaf and root microbiotas."; RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KQN30386.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LMLC01000002; KQN30386.1; -; Genomic_DNA. DR RefSeq; WP_055875973.1; NZ_LMLC01000002.1. DR EnsemblBacteria; KQN30386; KQN30386; ASF00_06410. DR GeneID; 29952866; -. DR Proteomes; UP000051932; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000051932}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000051932}. FT DOMAIN 208 377 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 174 201 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 430 AA; 47359 MW; 0BECCA82A88FB882 CRC64; MSSGFERDRD EFTRGTRAIV VLPDQGDASR DVDARLAETA GLAAAIGVEV VERIAYRVRQ LKPATLIGSG QVELLATQVR MEEAGLVVFD ASLSPIQQRN LEKALGTKVI DRTGLILEIF GERAATAEGR LQVELAHLDY QAGRLVRSWT HLERQRGGFG FLGGPGETQI EADRRLIRDR MARLKRELEQ VSRTRGLHRE RRQRAPWPVI ALVGYTNAGK STLFNRLTGA DVMAEDLLFA TLDPTLRQIQ LPGIDKAILS DTVGFVSDLP TQLVAAFKAT LEEVVSADLL VHIRDIAHPD TEAQRADVES VLSEIGVDEN TPRFEVWNKL DLLDAETHDE IAAQAANRDD VVAISALSGE GVGMLIAQVA AKLTGAHRRY RITLDATDGA GAAWLHAHGE VLDSEDDELE TTYDVRLSET DYDRFTRRDA // ID A0A0Q4N0L2_9GAMM Unreviewed; 427 AA. AC A0A0Q4N0L2; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 30-AUG-2017, entry version 12. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=ASF13_03595 {ECO:0000313|EMBL:KQN57889.1}; OS Erwinia sp. Leaf53. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; OC Erwiniaceae; Erwinia. OX NCBI_TaxID=1736225 {ECO:0000313|EMBL:KQN57889.1, ECO:0000313|Proteomes:UP000050856}; RN [1] {ECO:0000313|EMBL:KQN57889.1, ECO:0000313|Proteomes:UP000050856} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Leaf53 {ECO:0000313|EMBL:KQN57889.1, RC ECO:0000313|Proteomes:UP000050856}; RA Millard Andrew; RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:KQN57889.1, ECO:0000313|Proteomes:UP000050856} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Leaf53 {ECO:0000313|EMBL:KQN57889.1, RC ECO:0000313|Proteomes:UP000050856}; RA Vorholt J.; RT "Functional overlap of the Arabidopsis leaf and root microbiotas."; RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KQN57889.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LMLK01000012; KQN57889.1; -; Genomic_DNA. DR RefSeq; WP_056235407.1; NZ_LMLK01000012.1. DR EnsemblBacteria; KQN57889; KQN57889; ASF13_03595. DR Proteomes; UP000050856; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000050856}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000050856}. FT DOMAIN 198 365 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 427 AA; 48096 MW; 72C8B6905CBE1FE7 CRC64; MFDRYDAGEH AVLVHIYFTQ DRDMEDLQEF ESLVSSAGVE ALRVVTGSRK APLPKYFVGE GKAAEIAEAV KESGATVVLF DHALTPAQER NLEALCQCRV IDRTGLILDI FAQRARTHEG KLQVELAQLR HLATRLVRGW THLERQKGGI GLRGPGETQL ETDRRLLRNR ITLILSRLSR VEKQREQGRQ ARNKADVPTV SLVGYTNAGK STLFNRLTSA DVYAADQLFA TLDPTLRRVD VADVGEVVLA DTVGFIRHLP HDLVAAFKAT LQETREATLL LHVIDAADVR LEENIEAVNV VLEEIESDQI PSLLVMNKID MLDGFEPRID RDEENRPIRV WLSAQTGVGL PLLFQALTER LAGEIAQVDL RLPPEAGRLR SRFYQLHAIE KEWNEEDGSV GMHVRMPIVD WRRLCKQEPT LANYIVN // ID A0A0Q4RPR7_9BACL Unreviewed; 430 AA. AC A0A0Q4RPR7; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=ASF12_00020 {ECO:0000313|EMBL:KQO17137.1}; OS Paenibacillus sp. Leaf72. OC Bacteria; Firmicutes; Bacilli; Bacillales; Paenibacillaceae; OC Paenibacillus. OX NCBI_TaxID=1736234 {ECO:0000313|EMBL:KQO17137.1, ECO:0000313|Proteomes:UP000051722}; RN [1] {ECO:0000313|EMBL:KQO17137.1, ECO:0000313|Proteomes:UP000051722} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Leaf72 {ECO:0000313|EMBL:KQO17137.1, RC ECO:0000313|Proteomes:UP000051722}; RA Millard Andrew; RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:KQO17137.1, ECO:0000313|Proteomes:UP000051722} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Leaf72 {ECO:0000313|EMBL:KQO17137.1, RC ECO:0000313|Proteomes:UP000051722}; RA Vorholt J.; RT "Functional overlap of the Arabidopsis leaf and root microbiotas."; RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KQO17137.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LMLV01000001; KQO17137.1; -; Genomic_DNA. DR RefSeq; WP_056028060.1; NZ_LMLV01000001.1. DR EnsemblBacteria; KQO17137; KQO17137; ASF12_00020. DR Proteomes; UP000051722; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000051722}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000051722}. FT DOMAIN 208 372 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 430 AA; 47890 MW; 70935BF73988987A CRC64; MREKTHDTQT DIQDRAILVT LVTQQIKRGS SDPEHSLQEL VKLAETAGVE VLTTLTQNRE KPDTKWFIGK GKAEELRLVA DEMGATTAIF DQELSGAQVR NLEEMLDVKI VDRTQLILDI FAQRAGTREG NIQVELAQLS YLLPRLSGHG KNLSRLGGGI GTRGPGESKL ETDRRHIRGR ISDLKAQLDE VVRHRHLYRE RRKKSGIIQV ALVGYTNAGK STLLRQLTDA DVYVENQLFA TLDPTSRTLE LPNGREVILT DTVGFIQNLP HDLVAAFRAT LEEVNEADLV LHVVDSSSPM RDEQMAVVDR ILNDLGAAGK PTLTIYNKID LCSPEEAYTL RSGGDSLIIN AYKEADLKLL CDTIQEKLMG DTIVFALPAS RGDLIALAYR TGEVIEQEVD GEEGELLRLT IQLSKQDYEV NGHRLHPYIV // ID A0A0Q4V681_9MICO Unreviewed; 493 AA. AC A0A0Q4V681; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 05-JUL-2017, entry version 12. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=ASF23_09530 {ECO:0000313|EMBL:KQO63207.1}; OS Curtobacterium sp. Leaf261. OC Bacteria; Actinobacteria; Micrococcales; Microbacteriaceae; OC Curtobacterium. OX NCBI_TaxID=1736311 {ECO:0000313|EMBL:KQO63207.1, ECO:0000313|Proteomes:UP000050821}; RN [1] {ECO:0000313|EMBL:KQO63207.1, ECO:0000313|Proteomes:UP000050821} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Leaf261 {ECO:0000313|EMBL:KQO63207.1, RC ECO:0000313|Proteomes:UP000050821}; RA Millard Andrew; RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:KQO63207.1, ECO:0000313|Proteomes:UP000050821} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Leaf261 {ECO:0000313|EMBL:KQO63207.1, RC ECO:0000313|Proteomes:UP000050821}; RA Vorholt J.; RT "Functional overlap of the Arabidopsis leaf and root microbiotas."; RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KQO63207.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LMMJ01000008; KQO63207.1; -; Genomic_DNA. DR EnsemblBacteria; KQO63207; KQO63207; ASF23_09530. DR Proteomes; UP000050821; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 2. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000050821}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000050821}. FT DOMAIN 269 434 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 493 AA; 53534 MW; 520B8D28D9F8681C CRC64; MLRNADSRAS VSSVFAPAQA IQTRDVDQTG WQGDGDQFDR DDRAALRRVA GLSTELEDVT EVEYRQLRLE NVILIGVYAQ GDAQDAENSL RELAALAETA GAVVLDGLLQ RRPHPDPSTY LGRGKAEELR MAVAAVGADT VIADTELAPS QRRALEDVVK VKVIDRTAVI LDIFSQHAKS REGKAQVELA QLEYLLPRLR GWGESMSRQA GGQVGGAGAG MGSRGPGETK IELDRRRIHT RMAKLRRQIA GFKPAREAKR AERTRNEVPS VAIAGYTNAG KSSLLNRLTS AGVLVQNQLF ATLDATVRRT ESAKGRPYTF SDTVGFVRNL PHQLVEAFRS TLEEVGDSDV IVHVVDGSHP DPVSQLATVR DVIGDVGARE IPEIVAFNKA DLIDADQRLV LVGLEPDAVF VSARTGEGIE DLLRAIEARL PEPDVALTLV VPYDHGEVVS KLHDEGAVES TEYVPEGTRV SVRVFRRQVA DLAPYVADVV QPA // ID A0A0Q4X8E4_9RHIZ Unreviewed; 470 AA. AC A0A0Q4X8E4; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=ASF28_14820 {ECO:0000313|EMBL:KQP07265.1}; OS Methylobacterium sp. Leaf99. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Methylobacteriaceae; Methylobacterium. OX NCBI_TaxID=1736251 {ECO:0000313|EMBL:KQP07265.1, ECO:0000313|Proteomes:UP000052050}; RN [1] {ECO:0000313|EMBL:KQP07265.1, ECO:0000313|Proteomes:UP000052050} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Leaf99 {ECO:0000313|EMBL:KQP07265.1, RC ECO:0000313|Proteomes:UP000052050}; RA Millard Andrew; RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:KQP07265.1, ECO:0000313|Proteomes:UP000052050} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Leaf99 {ECO:0000313|EMBL:KQP07265.1, RC ECO:0000313|Proteomes:UP000052050}; RA Vorholt J.; RT "Functional overlap of the Arabidopsis leaf and root microbiotas."; RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KQP07265.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LMMU01000008; KQP07265.1; -; Genomic_DNA. DR RefSeq; WP_056094637.1; NZ_LMMU01000008.1. DR EnsemblBacteria; KQP07265; KQP07265; ASF28_14820. DR Proteomes; UP000052050; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000052050}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000052050}. FT DOMAIN 231 407 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 470 AA; 51482 MW; 7CCD96AA488DB2A5 CRC64; MTETMTPGEA RLQAMAAPEG DIAAATHTLV VGPYLGRVAQ RSAGGVHSAE ILRSNEARLD EASGLAAAIE LDVVEAIFAP VQRIRPSTYL GKGRVEELAG VIKAREIGLV VMDCALSPVQ QRNLEKEFGC KVIDRTGLIL EIFGRRASTR EGTLQVEHAH LAYQRSRLVR SWTHLERQRG GFGFLGGPGE TQIEADRRMI QERMTKIERE LDGVTRTRGL HRQGRARVPY PIVALVGYTN AGKSTLFNAL TKAQVMAQDM LFATLDPTAR ATKLPHGETV ILSDTVGFIS ELPTSLIAAF RATLEDVIEA DILLHVRDVS HGDSEAQAED VGAVLRELGI ETSATRIIEV WNKADLLDAD ERTRLLNLSA QGRTDRDSDA PVLVSALTGE GLAALTSRIE ARIARQRSTF AVVLPPEDGA SLHWLYENGE VLDRREEEGG TMHLAFRIAP EKEPRFLNRF AGARRLNRVG // ID A0A0Q4XI09_9RHIZ Unreviewed; 469 AA. AC A0A0Q4XI09; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 30-AUG-2017, entry version 13. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=ASF26_05210 {ECO:0000313|EMBL:KQP09410.1}; OS Methylobacterium sp. Leaf93. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Methylobacteriaceae; Methylobacterium. OX NCBI_TaxID=1736249 {ECO:0000313|EMBL:KQP09410.1, ECO:0000313|Proteomes:UP000052062}; RN [1] {ECO:0000313|EMBL:KQP09410.1, ECO:0000313|Proteomes:UP000052062} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Leaf93 {ECO:0000313|EMBL:KQP09410.1, RC ECO:0000313|Proteomes:UP000052062}; RA Millard Andrew; RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:KQP09410.1, ECO:0000313|Proteomes:UP000052062} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Leaf93 {ECO:0000313|EMBL:KQP09410.1, RC ECO:0000313|Proteomes:UP000052062}; RA Vorholt J.; RT "Functional overlap of the Arabidopsis leaf and root microbiotas."; RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KQP09410.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LMMS01000012; KQP09410.1; -; Genomic_DNA. DR RefSeq; WP_026175814.1; NZ_LMMS01000012.1. DR EnsemblBacteria; KQP09410; KQP09410; ASF26_05210. DR Proteomes; UP000052062; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000052062}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000052062}. FT DOMAIN 230 406 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 469 AA; 51231 MW; CD5CB2B56444870B CRC64; MTQMTTPGEA RLQAMAAPEG EIAAATHTLV IGPYLTRSAA PRTGGGPADV SRSSEARIDE AAGLAVAIEL DVTEAIIAPV SRIRPSTYLG KGRVEELAGR IKAEEIGLVV MDCALSPVQQ RNLEKAFGCK VIDRTGLILE IFGRRASTRE GTLQVEHAHL AYQRSRLVRS WTHLERQRGG FGFLGGPGET QIEADRRMIQ ERMTKIEREL DSVTRTRGLH RESRARVPYP IVALVGYTNA GKSTLFNALT KAEVMAKDML FATLDPTARA TKLPHGETVI LSDTVGFISE LPTALIAAFR ATLEDVIEAD ILLHVRDVSH VDSEAQAEDV GDVLRELGIE TTAERIIEVW NKADLLDDSE RTRLLNLSAQ GRNDRDSDVP ILVSALTGEG LAALSGRIEA RIAKRRSTFA VTLAPEDGAA LNWLYENAEV LDRRAEEAGT IHLAIRVAPE KEPRFLNRFA SARKLSRAD // ID A0A0Q4Y432_9BURK Unreviewed; 396 AA. AC A0A0Q4Y432; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=ASF43_00145 {ECO:0000313|EMBL:KQP22383.1}; OS Pseudorhodoferax sp. Leaf267. OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Comamonadaceae. OX NCBI_TaxID=1736316 {ECO:0000313|EMBL:KQP22383.1, ECO:0000313|Proteomes:UP000051560}; RN [1] {ECO:0000313|EMBL:KQP22383.1, ECO:0000313|Proteomes:UP000051560} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Leaf267 {ECO:0000313|EMBL:KQP22383.1, RC ECO:0000313|Proteomes:UP000051560}; RA Millard Andrew; RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:KQP22383.1, ECO:0000313|Proteomes:UP000051560} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Leaf267 {ECO:0000313|EMBL:KQP22383.1, RC ECO:0000313|Proteomes:UP000051560}; RA Vorholt J.; RT "Functional overlap of the Arabidopsis leaf and root microbiotas."; RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KQP22383.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LMMV01000001; KQP22383.1; -; Genomic_DNA. DR RefSeq; WP_056174989.1; NZ_LMMV01000001.1. DR EnsemblBacteria; KQP22383; KQP22383; ASF43_00145. DR Proteomes; UP000051560; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000051560}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000051560}. FT DOMAIN 202 375 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 396 AA; 43941 MW; 5BA31C06037EC769 CRC64; MTDTSPVDRA TASAILVGVD FGLPHFDQEL EELGLLAQTA GLVPVARITC KRKAPDAALF IGTGKAEEIK LLAQMHGASE VLFDQSLSPA QQRNLERVLE LPVNDRTMLI LTIFSQRARS HEGKLQVELA RLQYLSTRLV RRWSHLERQR GGIGTRGGPG ERQIELDRRM IGESIKRTRE RLSKVVRQRG TQRRQRERRD AFTISLVGYT NAGKSSLFNA LVKARAYAAD QLFATLDTTT RQLYLGEAGR SVSLSDTVGF IRDLPHGLVD AFRATLQEAA DADLLLHVVD ASNPHHPEQM EEVRRVLADI GADTVPMLLV FNKLDALDEA QRPLQLTDSM VVDGTTLDRV FLSAQTGEGM AQLRAELGRR AQQLDHVGLD SPGYHEADPR FGTITR // ID A0A0Q5ASD3_9MICO Unreviewed; 512 AA. AC A0A0Q5ASD3; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 07-JUN-2017, entry version 10. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=ASF46_10380 {ECO:0000313|EMBL:KQQ07806.1}; OS Rathayibacter sp. Leaf296. OC Bacteria; Actinobacteria; Micrococcales; Microbacteriaceae; OC Rathayibacter. OX NCBI_TaxID=1736327 {ECO:0000313|EMBL:KQQ07806.1, ECO:0000313|Proteomes:UP000050868}; RN [1] {ECO:0000313|EMBL:KQQ07806.1, ECO:0000313|Proteomes:UP000050868} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Leaf296 {ECO:0000313|EMBL:KQQ07806.1, RC ECO:0000313|Proteomes:UP000050868}; RA Millard Andrew; RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:KQQ07806.1, ECO:0000313|Proteomes:UP000050868} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Leaf296 {ECO:0000313|EMBL:KQQ07806.1, RC ECO:0000313|Proteomes:UP000050868}; RA Vorholt J.; RT "Functional overlap of the Arabidopsis leaf and root microbiotas."; RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KQQ07806.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LMNR01000002; KQQ07806.1; -; Genomic_DNA. DR RefSeq; WP_056867569.1; NZ_LMNR01000002.1. DR EnsemblBacteria; KQQ07806; KQQ07806; ASF46_10380. DR Proteomes; UP000050868; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 2. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000050868}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000050868}. FT DOMAIN 287 452 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 512 AA; 54897 MW; CD3EAA5AE31D37CD CRC64; MTEDLNETDT TEAVDVVSRV LANAQSRSAG YSRFVAGGAQ ALQTSGHEGE DSDGEQFDRA DRQALRRVAG LSTELEDVTE VEYRQLRLEN VVLIGVYSQG SLEDAENSLH ELAALAETAG ATVLDGLLQR RPHPDPSTYL GKGKAQELAG VVAALGADTV VADTELAPSQ RRALEDVVKV KVIDRTAVIL DIFSQHAKSR EGKAQVELAQ LEYLLPRLRG WGESMSRQAG GQVGAGAGMG SRGPGETKIE LDRRRIHTRM ARLRKQITAM KPAREAKRAN RKRNAVPSVA IAGYTNAGKS SLLNRMTHAG VLVENSLFAT LDATVRKAQT ADGRLYTFAD TVGFVRALPH QLVEAFRSTL EEVADSDIIV HVVDGSHPDP AGQIATVRDV IGEVGARGIP EIIAFNKSDL VDEGTRLVLR GLAPDAVFVS ARTGEGIDEL QARIAEILPE PDVEIDLLVP YDRGDVVSHL HRSGRILATE YVDGGTRVQA LVHQDLAGSL AEFAAPAAAV EA // ID A0A0Q5C500_9MICO Unreviewed; 511 AA. AC A0A0Q5C500; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=ASF54_10470 {ECO:0000313|EMBL:KQQ26460.1}; OS Frondihabitans sp. Leaf304. OC Bacteria; Actinobacteria; Micrococcales; Microbacteriaceae; OC Frondihabitans. OX NCBI_TaxID=1736329 {ECO:0000313|EMBL:KQQ26460.1, ECO:0000313|Proteomes:UP000051456}; RN [1] {ECO:0000313|EMBL:KQQ26460.1, ECO:0000313|Proteomes:UP000051456} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Leaf304 {ECO:0000313|EMBL:KQQ26460.1, RC ECO:0000313|Proteomes:UP000051456}; RA Millard Andrew; RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:KQQ26460.1, ECO:0000313|Proteomes:UP000051456} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Leaf304 {ECO:0000313|EMBL:KQQ26460.1, RC ECO:0000313|Proteomes:UP000051456}; RA Vorholt J.; RT "Functional overlap of the Arabidopsis leaf and root microbiotas."; RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KQQ26460.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LMNV01000003; KQQ26460.1; -; Genomic_DNA. DR RefSeq; WP_055962509.1; NZ_LMNV01000003.1. DR EnsemblBacteria; KQQ26460; KQQ26460; ASF54_10470. DR Proteomes; UP000051456; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 2. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000051456}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000051456}. FT DOMAIN 293 458 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 511 AA; 55652 MW; E279C283FB6384C9 CRC64; MTEHSTTEEK GAERDDVVDR ILSNASSRAG LSVFSPAQAI QTQGLDTRGD GTGDDHHDGD QFDREDRQAL RRVAGLSTEL QDVTEVEYRQ LRLENVVLIG VYSQGSLGDA ENSLRELAAL AETAGAVVLD GLLQRRPNPD PSTYLGSGKA LELKNTVLAL GADTVIADTE LAPSQRRALE DVVKVKVIDR TAVILDIFSQ HATSREGKAQ VELAQLEYLL PRLRGWGDSM SRQAGGQVGG AGAGMGSRGP GETKIELDRR RIHTRMAILR KKIKEMKPAR VAKRANRVRN TVPSVAIAGY TNAGKSSLLN RLTRAGVLVE NALFATLDAT VRKSSTDDGR PFTYSDTVGF VRNLPHQLVE AFRSTLEEVQ DSDIIVHVVD GSHPDPAAQL ATVREVISEV DGRDIPEVVV FNKSDLIDES QRLVLQGMVP DAIFVSARTG AGIDELRARI AELLPRPEVE LDLLVPFDRG DVVSRIHEIG RVVDVEYVAE GTRVTARVYS QDAPTLQEFA H // ID A0A0Q5CIP3_9BURK Unreviewed; 406 AA. AC A0A0Q5CIP3; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=ASF61_16435 {ECO:0000313|EMBL:KQQ31927.1}; OS Duganella sp. Leaf126. OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Oxalobacteraceae; Duganella. OX NCBI_TaxID=1736266 {ECO:0000313|EMBL:KQQ31927.1, ECO:0000313|Proteomes:UP000051032}; RN [1] {ECO:0000313|EMBL:KQQ31927.1, ECO:0000313|Proteomes:UP000051032} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Leaf126 {ECO:0000313|EMBL:KQQ31927.1, RC ECO:0000313|Proteomes:UP000051032}; RA Millard Andrew; RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:KQQ31927.1, ECO:0000313|Proteomes:UP000051032} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Leaf126 {ECO:0000313|EMBL:KQQ31927.1, RC ECO:0000313|Proteomes:UP000051032}; RA Vorholt J.; RT "Functional overlap of the Arabidopsis leaf and root microbiotas."; RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KQQ31927.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LMNW01000035; KQQ31927.1; -; Genomic_DNA. DR RefSeq; WP_056160496.1; NZ_LMNW01000035.1. DR EnsemblBacteria; KQQ31927; KQQ31927; ASF61_16435. DR Proteomes; UP000051032; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000051032}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000051032}. FT DOMAIN 190 357 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 156 183 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 406 AA; 44504 MW; DA881A399F322FE0 CRC64; MRAALVGIDF GQGDFAASVE ELQLLARSAG AEPVTTITAK RAAPDPAYFV GSGKADEIGQ AVLDERIEIV IFNHALSPAQ QRNLEKRLNI RVLDRTSLIL DIFAQRAASH EGKLQVELAQ LQHLATRLIR GWTHLERQKG GIGLRGPGET QLETDRRLIG ERVKALRARL AKLRKQHETQ RRSRGRSQTF SVSLVGYTNA GKSTLFNTVT KAGVYVADQL FATLDTTSRR VYMGQEVGNV VISDTVGFVR ELPHQLVAAF RATLEETIHA DLLLHVVDAS SPVRMEQIEQ VNLVLKEIGA DHIPQILVWN KIDAAGLEPS VERDEYAKIS RVFLSARTGA GVDLLREAIV EWAKAAPGAR LNQAYAVDAE DDEPDEEDET QEPDASGSDD DSSTSRSSLT THVGSH // ID A0A0Q5CWG8_9RHIZ Unreviewed; 452 AA. AC A0A0Q5CWG8; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 07-JUN-2017, entry version 13. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=ASG19_10900 {ECO:0000313|EMBL:KQQ36878.1}; OS Rhizobium sp. Leaf306. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium. OX NCBI_TaxID=1736330 {ECO:0000313|EMBL:KQQ36878.1, ECO:0000313|Proteomes:UP000052122}; RN [1] {ECO:0000313|EMBL:KQQ36878.1, ECO:0000313|Proteomes:UP000052122} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Leaf306 {ECO:0000313|EMBL:KQQ36878.1, RC ECO:0000313|Proteomes:UP000052122}; RA Millard Andrew; RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:KQQ36878.1, ECO:0000313|Proteomes:UP000052122} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Leaf306 {ECO:0000313|EMBL:KQQ36878.1, RC ECO:0000313|Proteomes:UP000052122}; RA Vorholt J.; RT "Functional overlap of the Arabidopsis leaf and root microbiotas."; RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KQQ36878.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LMNX01000002; KQQ36878.1; -; Genomic_DNA. DR RefSeq; WP_062456405.1; NZ_LMNX01000002.1. DR EnsemblBacteria; KQQ36878; KQQ36878; ASG19_10900. DR Proteomes; UP000052122; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000052122}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000052122}. FT DOMAIN 214 386 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 173 207 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 452 AA; 49885 MW; E65659E03CD23FA7 CRC64; MRAVVIVPVL KQSRTRSGQG DATATPVPSR PAAPQRSNEA RLEEATGLAR AIDLEIAEGM IVTVGQPRPA TLMGTGKIEE IKALLDEKDA GLVIVDHPLT PVQQRNLEKE WGAKVIDRTG LILEIFGRRA STKEGTLQVD LAHLNYQKGR LVRSWTHLER QRGGAGFMGG PGETQIEADR RQLQDKIIKL ERELEQVVRT RQLHRAKRRK VPHPIVALVG YTNAGKSTLF NRITGAGVLA EDMLFATLDP TLRRMKLPHG RTVIMSDTVG FISDLPTHLV AAFRATLEEV LEADLVLHVR DMSDPDNAAQ SADVLRILAD LGIDEKESEK RIIEVWNKID RLDPESHDAL FERAQGRANI MAVSAITGEG VEALLDEVSN RLSGVLTEAE IVIPADKLAL VSWVYGNAVV SEREDNEDGS VTLVVKLTDR QASELERRLG NGAKSDKEEW ER // ID A0A0Q5E611_9MICO Unreviewed; 506 AA. AC A0A0Q5E611; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 05-JUL-2017, entry version 12. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=ASF68_13445 {ECO:0000313|EMBL:KQQ50580.1}; OS Plantibacter sp. Leaf314. OC Bacteria; Actinobacteria; Micrococcales; Microbacteriaceae; OC Plantibacter. OX NCBI_TaxID=1736333 {ECO:0000313|EMBL:KQQ50580.1, ECO:0000313|Proteomes:UP000051200}; RN [1] {ECO:0000313|EMBL:KQQ50580.1, ECO:0000313|Proteomes:UP000051200} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Leaf314 {ECO:0000313|EMBL:KQQ50580.1, RC ECO:0000313|Proteomes:UP000051200}; RA Millard Andrew; RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:KQQ50580.1, ECO:0000313|Proteomes:UP000051200} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Leaf314 {ECO:0000313|EMBL:KQQ50580.1, RC ECO:0000313|Proteomes:UP000051200}; RA Vorholt J.; RT "Functional overlap of the Arabidopsis leaf and root microbiotas."; RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KQQ50580.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LMOB01000002; KQQ50580.1; -; Genomic_DNA. DR EnsemblBacteria; KQQ50580; KQQ50580; ASF68_13445. DR Proteomes; UP000051200; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 2. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000051200}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000051200}. FT DOMAIN 279 444 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 506 AA; 54131 MW; A6367F0D00B68A42 CRC64; MADPDDVVAR VLTSAASRSS GYTLFGSGAA ALQTSDTTGG SSDDGEQFDR EDRQALRRVA GLSTELEDVT EVEYRQLRLE NVVIIGVYPQ GALHDAENSL RELAALAETA GAVVLDGLLQ RKPHPDPSTY LGRGKAQELK AIVQALGADT VIADTELAPS QRRALEDAVG VKVIDRTAVI LDIFSQHAKS REGKAQVELA QLEYLLPRLR GWGESMSRQA GGQVGGAGAG MGSRGPGETK IELDRRRIHT RMAKLRKSIT AMKPAREAKR ANRRRNTVPS VAIAGYTNAG KSSLLNRITK AGVLVENSLF ATLDATVRRN ETADGREYTL ADTVGFVRNL PHQLVEAFRS TLEEVADSDV IVHVVDAAHP DPAGQIATVR DVIGEVGARH IPELVVFNKA DLVDDGQLLV LRGLVPDAVF VSARTGVGID ELMERIEALI PSPSNEVNVL VPFDRGDLVT LLHERGKVLS TDYDERGTIV HALVGAEVAA ALAPFAEILP APAVTS // ID A0A0Q5HFU5_9RHIZ Unreviewed; 456 AA. AC A0A0Q5HFU5; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 05-JUL-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=ASF65_16640 {ECO:0000313|EMBL:KQQ89917.1}; OS Aureimonas sp. Leaf324. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Aurantimonadaceae; Aureimonas. OX NCBI_TaxID=1736336 {ECO:0000313|EMBL:KQQ89917.1, ECO:0000313|Proteomes:UP000050862}; RN [1] {ECO:0000313|EMBL:KQQ89917.1, ECO:0000313|Proteomes:UP000050862} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Leaf324 {ECO:0000313|EMBL:KQQ89917.1, RC ECO:0000313|Proteomes:UP000050862}; RA Millard Andrew; RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:KQQ89917.1, ECO:0000313|Proteomes:UP000050862} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Leaf324 {ECO:0000313|EMBL:KQQ89917.1, RC ECO:0000313|Proteomes:UP000050862}; RA Vorholt J.; RT "Functional overlap of the Arabidopsis leaf and root microbiotas."; RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KQQ89917.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LMOH01000003; KQQ89917.1; -; Genomic_DNA. DR EnsemblBacteria; KQQ89917; KQQ89917; ASF65_16640. DR Proteomes; UP000050862; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000050862}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000050862}. FT DOMAIN 210 384 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 169 203 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 456 AA; 50278 MW; 4038B8B710D92DD5 CRC64; MEHERVPTRA AVFVPVVRQR NPADDVSEAV RRGDEERLVE AEGLALAIEL DVVARGIIPV SKIQPATLIG SGKVEELAGL IAAEKIGLVI VDHPLTPVQQ RNLEKELNAK VLDRTGLILE IFGRRARTKE GRLQVELAHL NYQRGRLVRS WTHLERQRGG AGFLGGPGET QIESDRRQLQ EKIKRLEKEL DQVRRTRSLH RAKRKKAPHP IVALVGYTNA GKSTLFNKVT GAEVLAKDLL FATLDPTLRR INLPHGTEVI FSDTVGFISD LPTHLVAAFR ATLEEVVEAD IVLHVRDIAN PDTAAQAADV RKILADLEID ADDPEHVIEV WNKADRLDEQ ARAQVELSAA SHPRGQAVHI VSALTGENVP ALLADIEGRI AGLAEPVSLT VPADALGILP WVYDNSVVRE REDLEDGSVQ LSIDLTRAAR SDLLRLKHRH PTMQIEGLPA LEEVDD // ID A0A0Q5I0R3_9BURK Unreviewed; 408 AA. AC A0A0Q5I0R3; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=ASF77_01280 {ECO:0000313|EMBL:KQQ96663.1}; OS Massilia sp. Leaf139. OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Oxalobacteraceae; Massilia. OX NCBI_TaxID=1736272 {ECO:0000313|EMBL:KQQ96663.1, ECO:0000313|Proteomes:UP000051760}; RN [1] {ECO:0000313|EMBL:KQQ96663.1, ECO:0000313|Proteomes:UP000051760} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Leaf139 {ECO:0000313|EMBL:KQQ96663.1, RC ECO:0000313|Proteomes:UP000051760}; RA Millard Andrew; RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:KQQ96663.1, ECO:0000313|Proteomes:UP000051760} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Leaf139 {ECO:0000313|EMBL:KQQ96663.1, RC ECO:0000313|Proteomes:UP000051760}; RA Vorholt J.; RT "Functional overlap of the Arabidopsis leaf and root microbiotas."; RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KQQ96663.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LMOJ01000001; KQQ96663.1; -; Genomic_DNA. DR RefSeq; WP_056333278.1; NZ_LMOJ01000001.1. DR EnsemblBacteria; KQQ96663; KQQ96663; ASF77_01280. DR Proteomes; UP000051760; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000051760}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000051760}. FT DOMAIN 199 366 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 408 AA; 44225 MW; 6AA10C71C436C2DB CRC64; MADAPGTNST RAVLVGVDFG AVDFTASLEE LALLASSAGA EPIDTITAKR NAPDPAYFVG SGKADEIGVA AKAQGAELVI FNHALSPAQQ RNLERRLELR IIDRTSLILD IFAQRAQSHE GKLQVELAQL QHLATRLIRG WTHLERQKGG IGLRGPGETQ LETDRRLIGE RVKALRARLT KLRKQHETQR RARGRNNTFS VSLVGYTNAG KSTLFNTLTK AGVYVANQLF ATLDTTSRRL YLGDATGSVV ISDTVGFVRE LPHQLVAAFR ATLEETIHAD VLLHVVDGSS PTRMEQIEQV NEVLREIGAD HIPQILVWNK IDMADLQPGV ERDEHDKISR VFISARNGAG LDLLRDAIVE AAGSAASSRT HGAPGSSPEN EEQDDAALAL QYDEAGESNP TSTHVGPH // ID A0A0Q5L377_9BURK Unreviewed; 391 AA. AC A0A0Q5L377; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=ASF94_09525 {ECO:0000313|EMBL:KQR44903.1}; OS Acidovorax sp. Leaf160. OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Comamonadaceae; Acidovorax. OX NCBI_TaxID=1736280 {ECO:0000313|EMBL:KQR44903.1, ECO:0000313|Proteomes:UP000051403}; RN [1] {ECO:0000313|EMBL:KQR44903.1, ECO:0000313|Proteomes:UP000051403} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Leaf160 {ECO:0000313|EMBL:KQR44903.1, RC ECO:0000313|Proteomes:UP000051403}; RA Millard Andrew; RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:KQR44903.1, ECO:0000313|Proteomes:UP000051403} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Leaf160 {ECO:0000313|EMBL:KQR44903.1, RC ECO:0000313|Proteomes:UP000051403}; RA Vorholt J.; RT "Functional overlap of the Arabidopsis leaf and root microbiotas."; RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KQR44903.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LMOV01000025; KQR44903.1; -; Genomic_DNA. DR RefSeq; WP_056668226.1; NZ_LMOV01000025.1. DR EnsemblBacteria; KQR44903; KQR44903; ASF94_09525. DR Proteomes; UP000051403; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000051403}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000051403}. FT DOMAIN 202 375 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 391 AA; 43077 MW; D31CBF676CD727B8 CRC64; MSSSDKPASP ATPVVLVGVD FGLPHFDGEL EELGLLAETA GLTPVARLVA KRKAPDAALF VGSGKAEEIQ VLAQMHGAVE VLFDQALSPA QQRNLERVLN LPVSDRTFLI LEIFAQRARS HEGKLQVELA KLQYLSTRLV RRWSHLERQR GGIGTRGGPG ETQIELDRRM IGDAIKRTKE RLVKVKRQRS TQRRQRDRRD TFNVSLVGYT NAGKSTLFNA LVKARAYAAD QLFATLDTTT RQLYLADAGR LISISDTVGF IRDLPHGLVD AFQATLQEAI DADLLLHVVD ASNPAFPEQI AQVQRVLAEI GAQDIPQLLV FNKLDAMSPE ARPTAARDVL EMDGVFVPRI FLSAQSGEGL PLLRQQLAAE LLKERDEMTP DLAAELKRDD G // ID A0A0Q5L8R1_9MICO Unreviewed; 515 AA. AC A0A0Q5L8R1; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 07-JUN-2017, entry version 10. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=ASF82_08140 {ECO:0000313|EMBL:KQR43612.1}; OS Frigoribacterium sp. Leaf164. OC Bacteria; Actinobacteria; Micrococcales; Microbacteriaceae; OC Frigoribacterium. OX NCBI_TaxID=1736282 {ECO:0000313|EMBL:KQR43612.1, ECO:0000313|Proteomes:UP000051005}; RN [1] {ECO:0000313|EMBL:KQR43612.1, ECO:0000313|Proteomes:UP000051005} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Leaf164 {ECO:0000313|EMBL:KQR43612.1, RC ECO:0000313|Proteomes:UP000051005}; RA Millard Andrew; RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:KQR43612.1, ECO:0000313|Proteomes:UP000051005} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Leaf164 {ECO:0000313|EMBL:KQR43612.1, RC ECO:0000313|Proteomes:UP000051005}; RA Vorholt J.; RT "Functional overlap of the Arabidopsis leaf and root microbiotas."; RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KQR43612.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LMOX01000003; KQR43612.1; -; Genomic_DNA. DR RefSeq; WP_056056207.1; NZ_LMOX01000003.1. DR EnsemblBacteria; KQR43612; KQR43612; ASF82_08140. DR Proteomes; UP000051005; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 2. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000051005}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000051005}. FT DOMAIN 291 456 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 515 AA; 55586 MW; 6D33C1E36D6BC8C1 CRC64; MTDTPSTPLD AEQGDQLPDD VVARVLERAA ARSSAYTVFS PAQAIQTRSL ADAGSDGEQL DRDDRAALRR VGGLSTELED VTEVEYRQLR LENVVLIGVW SQGSLGDAEN SLRELAALAE TAGAVVLDGL LQRRPNPDPS TYLGKGKAEE LRQTVAALGA DTVIADTELA PSQRRALEDV VKVKVIDRTA VILDIFSQHA KSREGKAQVE LAQLEYLLPR LRGWGESMSR QAGGQVGGAG AGMGSRGPGE TKIELDRRRI HTRMARLRRQ IKEMKPARDA KRANRDRNEV PSVAIAGYTN AGKSSLLNRL TSAGVLVENA LFATLDATVR KSTTPDGRPF TYVDTVGFVR NLPHQLVEAF RSTLEEVAAS DVIVHVVDGS HPDPAAQLAT VRQVISEVDG HDIAEVVVFN KADLVDADQR LVLQGLEPSA VFVSARTGEG VDELLDRVAG LLPEPEVEVD LLVPYDRGEV VAHLHDAGRV VSTDYEEAGT RLHARVYPSD VAALAPFVQP AVARR // ID A0A0Q5M9D9_9MICO Unreviewed; 503 AA. AC A0A0Q5M9D9; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=ASF88_05885 {ECO:0000313|EMBL:KQR54326.1}; OS Leifsonia sp. Leaf336. OC Bacteria; Actinobacteria; Micrococcales; Microbacteriaceae; Leifsonia. OX NCBI_TaxID=1736341 {ECO:0000313|EMBL:KQR54326.1, ECO:0000313|Proteomes:UP000050966}; RN [1] {ECO:0000313|EMBL:KQR54326.1, ECO:0000313|Proteomes:UP000050966} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Leaf336 {ECO:0000313|EMBL:KQR54326.1, RC ECO:0000313|Proteomes:UP000050966}; RA Millard Andrew; RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:KQR54326.1, ECO:0000313|Proteomes:UP000050966} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Leaf336 {ECO:0000313|EMBL:KQR54326.1, RC ECO:0000313|Proteomes:UP000050966}; RA Vorholt J.; RT "Functional overlap of the Arabidopsis leaf and root microbiotas."; RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KQR54326.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LMOZ01000001; KQR54326.1; -; Genomic_DNA. DR RefSeq; WP_055915462.1; NZ_LMOZ01000001.1. DR EnsemblBacteria; KQR54326; KQR54326; ASF88_05885. DR Proteomes; UP000050966; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 2. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000050966}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000050966}. FT DOMAIN 285 450 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 503 AA; 54725 MW; DB8B1BC9DDDD3112 CRC64; MTERTEFDEQ TTDDVVARVL ATEQDKASVT LFGRGAQALQ DDHTDGGNHD GEQFDREERA ALRRVSGLST ELEDVTEVEY RQLRLENVVL IGVYSQGTLQ DAENSLRELA ALAETAGAAV LDGLLQRRPH PDPSTYLGRG KAEELAGVVR ALGADTVIAD TELAPSQRRA LEDVVKVKVI DRTAVILDIF SQHAKSREGK AQVELAQLEY LLPRLRGWGE SMSRQAGGQV GGAGAGMGSR GPGETKIELD RRRIHSRMAK LRKQIAGFKP AREAKRANRN RNSVPSVAIA GYTNAGKSSL LNRVTKAGVL VENALFATLD ATVRRSVTAD GRLYTLADTV GFVRNLPHQL VEAFRSTLEE VADSDVILHV VDGSHPDPAS QLATVRDVIG EVGAREIPEI VVFNKSDLIP ADDRLVLRGL EPGAIFASAR TGEGIDEVLA AIARLLPDPS VEVELVVPYD RGDLISALHE RGRVLATEYV EDGTRVRARI MPEYQAVFEP FEV // ID A0A0Q5MMW9_9MICO Unreviewed; 514 AA. AC A0A0Q5MMW9; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=ASF89_14170 {ECO:0000313|EMBL:KQR62462.1}; OS Frigoribacterium sp. Leaf172. OC Bacteria; Actinobacteria; Micrococcales; Microbacteriaceae; OC Frigoribacterium. OX NCBI_TaxID=1736285 {ECO:0000313|EMBL:KQR62462.1, ECO:0000313|Proteomes:UP000051720}; RN [1] {ECO:0000313|EMBL:KQR62462.1, ECO:0000313|Proteomes:UP000051720} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Leaf172 {ECO:0000313|EMBL:KQR62462.1, RC ECO:0000313|Proteomes:UP000051720}; RA Millard Andrew; RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:KQR62462.1, ECO:0000313|Proteomes:UP000051720} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Leaf172 {ECO:0000313|EMBL:KQR62462.1, RC ECO:0000313|Proteomes:UP000051720}; RA Vorholt J.; RT "Functional overlap of the Arabidopsis leaf and root microbiotas."; RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KQR62462.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LMPB01000005; KQR62462.1; -; Genomic_DNA. DR RefSeq; WP_055794920.1; NZ_LMPB01000005.1. DR EnsemblBacteria; KQR62462; KQR62462; ASF89_14170. DR Proteomes; UP000051720; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 2. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000051720}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000051720}. FT DOMAIN 290 455 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 514 AA; 55759 MW; 46BCC5CCD26299DA CRC64; MTDLPTNPLD AERSEQGDDV VARVLDRAAS RASAYTVFSP AQAIQTRSLH DSGSDGDQFD RDDRQALRRV AGLSTELEDV TEVEYRQLRL ENVVLIGVYS QGSLADAENS LRELAALAET AGAVVLDGLL QRRPNPDPST YLGSGKAEEL RMTVAALGAD TVIADTELAP SQRRALEDVV KVKVIDRTAV ILDIFSQHAK SREGKAQVEL AQLEYLLPRL RGWGDSMSRQ AGGQVGGAGA GMGSRGPGET KIELDRRRIH TRMARLRRQI KEMKPARDAK RANRDRNEVP SVAIAGYTNA GKSSLLNRLT SAGVLVENAL FATLDATVRK STTTDGRPFT YSDTVGFVRN LPHQLVEAFR STLEEVAASD VIVHVVDGSH PDPTAQLATV RQVVSEVDGA GITEIVVFNK SDLVDPDQRL VLQGLVPDAV FVSARTGEGI DELLERIAGS LPTPDVELEL LVPYDRGDVV SQLHDSGRVV ESSYEEEGTR VHARVYPSDV AWLTPFVSRA AVSR // ID A0A0Q5NZG6_9BURK Unreviewed; 426 AA. AC A0A0Q5NZG6; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=ASG35_16850 {ECO:0000313|EMBL:KQR74451.1}; OS Burkholderia sp. Leaf177. OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Burkholderia. OX NCBI_TaxID=1736287 {ECO:0000313|EMBL:KQR74451.1, ECO:0000313|Proteomes:UP000051826}; RN [1] {ECO:0000313|EMBL:KQR74451.1, ECO:0000313|Proteomes:UP000051826} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Leaf177 {ECO:0000313|EMBL:KQR74451.1, RC ECO:0000313|Proteomes:UP000051826}; RA Millard Andrew; RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:KQR74451.1, ECO:0000313|Proteomes:UP000051826} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Leaf177 {ECO:0000313|EMBL:KQR74451.1, RC ECO:0000313|Proteomes:UP000051826}; RA Vorholt J.; RT "Functional overlap of the Arabidopsis leaf and root microbiotas."; RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KQR74451.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LMPF01000024; KQR74451.1; -; Genomic_DNA. DR RefSeq; WP_056363908.1; NZ_LMPF01000024.1. DR EnsemblBacteria; KQR74451; KQR74451; ASG35_16850. DR Proteomes; UP000051826; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000051826}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000051826}. FT DOMAIN 206 377 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 172 199 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 426 AA; 46874 MW; A13860DC0274FC1E CRC64; MNLLIHRSLQ NENINLINAA LVGVDFGKID FDASLEELSL LAQSAGAHPA VTLTGRRSSP DAKMFVGSGK VEELRLACVA NDVELVIFNH ALAPAQQRNL ETALELRVID RTSLILDIFA QRARSHEGKL QVELAQLQYL STRLIRAWTH LERQKGGIGL RGPGETQLET DRRLIGERIK ALKARLAKLQ RQHGTQRRQR ERNRTTSVSL VGYTNAGKST LFNALTKAQA YAADQLFATL DTTSRRVYLG EEAGQAVVSD TVGFIRDLPH QLVAAFRATL EETVQADLLL HVVDASSMVR LDQIEEVNKV LSSIGAEGVP QILVFNKIDA VPELAARNDP VERDEYGNIL RVFLSARTGQ GLDALRAAIA EFAASEPKDN NEYTELPDGT IVPESMDSTS DDGTTLPEDH RSADESEDRK VPEHGH // ID A0A0Q5PAR2_9SPHN Unreviewed; 430 AA. AC A0A0Q5PAR2; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=ASG07_04760 {ECO:0000313|EMBL:KQR83937.1}; OS Sphingomonas sp. Leaf343. OC Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales; OC Sphingomonadaceae; Sphingomonas. OX NCBI_TaxID=1736345 {ECO:0000313|EMBL:KQR83937.1, ECO:0000313|Proteomes:UP000051323}; RN [1] {ECO:0000313|EMBL:KQR83937.1, ECO:0000313|Proteomes:UP000051323} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Leaf343 {ECO:0000313|EMBL:KQR83937.1, RC ECO:0000313|Proteomes:UP000051323}; RA Millard Andrew; RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:KQR83937.1, ECO:0000313|Proteomes:UP000051323} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Leaf343 {ECO:0000313|EMBL:KQR83937.1, RC ECO:0000313|Proteomes:UP000051323}; RA Vorholt J.; RT "Functional overlap of the Arabidopsis leaf and root microbiotas."; RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KQR83937.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LMPG01000010; KQR83937.1; -; Genomic_DNA. DR RefSeq; WP_055843403.1; NZ_LMPG01000010.1. DR EnsemblBacteria; KQR83937; KQR83937; ASG07_04760. DR Proteomes; UP000051323; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000051323}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000051323}. FT DOMAIN 208 377 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 430 AA; 47200 MW; A9DE808B9A0FE914 CRC64; MNTGFDRDRD DVVRGARAIV VLPDRGDSTR DVEARLEECA GLAAAIGLEV VDRAALRVRT PRPATLIGSG QMEELATRVT MEDAALVVFD AALTPVQQRN LETGLSAKVI DRTGLILEIF GERAATAEGR LQVELAHLDY QAGRLVRSWT HLERQRGGFG FLGGPGETQI EADRRMIRDR MARLRRELDQ VSRTRGLHRD RRQRAPWPVI ALVGYTNAGK STLFNRLTGA HVMAENLLFA TLDPTLRQIS LPGIDKAILS DTVGFVSDLP TQLVAAFKAT LEEVVSADLL IHVRDIAHPD TEAQRADVEA VLEEIGVTAS TPRFEAWNKL DLLDDDRRAD ALQQAARRSD VMVISALTGE GVDRLSTAVA GRLTEGHHRY TISLDSTDGA GAAWLHANGE VLAQATADDA TTFDVRLSEE DYARFNRRFA // ID A0A0Q5Q7E4_9FLAO Unreviewed; 411 AA. AC A0A0Q5Q7E4; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=ASG01_05540 {ECO:0000313|EMBL:KQR95308.1}; OS Chryseobacterium sp. Leaf180. OC Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales; OC Flavobacteriaceae; Chryseobacterium. OX NCBI_TaxID=1736289 {ECO:0000313|EMBL:KQR95308.1, ECO:0000313|Proteomes:UP000051405}; RN [1] {ECO:0000313|EMBL:KQR95308.1, ECO:0000313|Proteomes:UP000051405} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Leaf180 {ECO:0000313|EMBL:KQR95308.1, RC ECO:0000313|Proteomes:UP000051405}; RA Millard Andrew; RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:KQR95308.1, ECO:0000313|Proteomes:UP000051405} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Leaf180 {ECO:0000313|EMBL:KQR95308.1, RC ECO:0000313|Proteomes:UP000051405}; RA Vorholt J.; RT "Functional overlap of the Arabidopsis leaf and root microbiotas."; RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KQR95308.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LMPJ01000001; KQR95308.1; -; Genomic_DNA. DR RefSeq; WP_055861068.1; NZ_LMPJ01000001.1. DR EnsemblBacteria; KQR95308; KQR95308; ASG01_05540. DR Proteomes; UP000051405; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000051405}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000051405}. FT DOMAIN 200 384 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 411 AA; 47700 MW; 844C5B96B80F1C94 CRC64; MLEKKQHSYE KVILVGVVTQ HQDEEKLQEY MDELEFLAFT AGATTDRRFT QKLTQPDSKT FVGSGKAQEI KEYIKENEIG TVIFDDELSP SQLKNLEKEM EVKILDRTNL ILDIFAQRAQ TSYARTQVEL AQYQYLLPRL SKMWSHLDKQ KGGIGMRGPG ETEIETDRRI IRDRITLLKD KLKTIDKQMA TQRNNRGKVV RVALVGYTNV GKSTLMNALS KSDVFAENKL FATLDTTVRK TVIGNLPFLL TDTVGFIRKL PTQLVESFKS TLDEVREADL LIHVVDISHH SFEDHIESVN QILMEINAHQ KPMIMVFNKI DDFNYEKKDE DDLTPGSSRN ISLDEWKKTW MAKSKFPTVF ISALTKENFP EMKKLIYDEV MKIHISRFPY NDFLFEYFEN DEEEAQNDES Q // ID A0A0Q5R158_9ACTN Unreviewed; 468 AA. AC A0A0Q5R158; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 05-JUL-2017, entry version 12. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=ASG12_10385 {ECO:0000313|EMBL:KQR99033.1}; OS Williamsia sp. Leaf354. OC Bacteria; Actinobacteria; Corynebacteriales; Williamsiaceae; OC Williamsia. OX NCBI_TaxID=1736349 {ECO:0000313|EMBL:KQR99033.1, ECO:0000313|Proteomes:UP000051980}; RN [1] {ECO:0000313|EMBL:KQR99033.1, ECO:0000313|Proteomes:UP000051980} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Leaf354 {ECO:0000313|EMBL:KQR99033.1, RC ECO:0000313|Proteomes:UP000051980}; RA Millard Andrew; RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:KQR99033.1, ECO:0000313|Proteomes:UP000051980} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Leaf354 {ECO:0000313|EMBL:KQR99033.1, RC ECO:0000313|Proteomes:UP000051980}; RA Vorholt J.; RT "Functional overlap of the Arabidopsis leaf and root microbiotas."; RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KQR99033.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LMPL01000002; KQR99033.1; -; Genomic_DNA. DR EnsemblBacteria; KQR99033; KQR99033; ASG12_10385. DR Proteomes; UP000051980; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000313|EMBL:KQR99033.1}; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000051980}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900, KW ECO:0000313|EMBL:KQR99033.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000051980}. FT DOMAIN 245 414 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 204 231 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 468 AA; 51128 MW; 3D0E427FACC2F8BD CRC64; MTEQFRRRTP TTGELQLDER SSLQRVPGLS TELTDVTEVE YRQLRLERVV LVGVWTDGNA STAEARMAEL AALAETAGSE ILDAVMQRRD RPDPATYIGS GKAHELREVV LATGADTVIC DGELTPAQLN ALEKVVKVKV IDRTALILDI FAQHATSREG KAQVALAQME YMIPRLRGWG ESMSRQAGGR AGSNGGVGLR GPGETKIETD RRRIRERMAK LRREIRGMKT ARTVSRSGRR RSSVPAVTIA GYTNAGKSSL INAMTGSGVL VQNALFATLD PTTRRATLDD GREVVFTDTV GFVRHLPTQL VEAFRSTLEE VVDADLVLHV VDASDPLPMD QISTVRTVID EVVRSEKATA PPEILVVNKI DAADPLTLAA LRGEFSDAVF VSAVTGEGLD ELFDRVRDVI GRDDVEMSVL VPYSRGDLVS RIHAHGDVLE TEHRDDGTYM RVKVPAALAG DLVDIAWR // ID A0A0Q5RHQ0_9SPHN Unreviewed; 431 AA. AC A0A0Q5RHQ0; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=ASG11_11835 {ECO:0000313|EMBL:KQS04854.1}; OS Sphingomonas sp. Leaf357. OC Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales; OC Sphingomonadaceae; Sphingomonas. OX NCBI_TaxID=1736350 {ECO:0000313|EMBL:KQS04854.1, ECO:0000313|Proteomes:UP000051080}; RN [1] {ECO:0000313|EMBL:KQS04854.1, ECO:0000313|Proteomes:UP000051080} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Leaf357 {ECO:0000313|EMBL:KQS04854.1, RC ECO:0000313|Proteomes:UP000051080}; RA Millard Andrew; RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:KQS04854.1, ECO:0000313|Proteomes:UP000051080} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Leaf357 {ECO:0000313|EMBL:KQS04854.1, RC ECO:0000313|Proteomes:UP000051080}; RA Vorholt J.; RT "Functional overlap of the Arabidopsis leaf and root microbiotas."; RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KQS04854.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LMPM01000001; KQS04854.1; -; Genomic_DNA. DR RefSeq; WP_055779362.1; NZ_LMPM01000001.1. DR EnsemblBacteria; KQS04854; KQS04854; ASG11_11835. DR Proteomes; UP000051080; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000051080}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000051080}. FT DOMAIN 209 378 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 431 AA; 47253 MW; 65D67D311DA890D4 CRC64; MSTTGFERDK DEFARGARCV VVFPEHGISS RDVAARLEET AGLAMAIGVV VADKVSYRVR AARPATLIGS GQVEMLAATV RMEEADLVVF DAALTPVQQR NLEKELGAKV IDRTGLILEI FGERAATAEG RLQVELAHLD YQAGRLVRSW THLERQRGGF GFLGGPGETQ IEADRRLIRD RMARLKKELE QVSRTRGLHR DRRQRAPWPV IALVGYTNAG KSTLFNRLTG ADVMAEDLLF ATLDPTLRQI SLPGVDKAIL SDTVGFVSEL PTQLVAAFKA TLEEVISADL LIHVRDIAHP DTMAQRDDVE AVLRDIGVDD TTPRIEAWNK LDLLDENDRV ELLGEAERRE DVVAISALSG EGVAVLLHTI ASLLTAGHRR YAITLDAGDG AGAAWLHAHG EVLAQDVAGD TASYDVRMAP RDYERFLQRG E // ID A0A0Q5SPX5_9BACT Unreviewed; 412 AA. AC A0A0Q5SPX5; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=ASG33_23730 {ECO:0000313|EMBL:KQS24767.1}; OS Dyadobacter sp. Leaf189. OC Bacteria; Bacteroidetes; Cytophagia; Cytophagales; Cytophagaceae; OC Dyadobacter. OX NCBI_TaxID=1736295 {ECO:0000313|EMBL:KQS24767.1, ECO:0000313|Proteomes:UP000051810}; RN [1] {ECO:0000313|EMBL:KQS24767.1, ECO:0000313|Proteomes:UP000051810} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Leaf189 {ECO:0000313|EMBL:KQS24767.1, RC ECO:0000313|Proteomes:UP000051810}; RA Millard Andrew; RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:KQS24767.1, ECO:0000313|Proteomes:UP000051810} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Leaf189 {ECO:0000313|EMBL:KQS24767.1, RC ECO:0000313|Proteomes:UP000051810}; RA Vorholt J.; RT "Functional overlap of the Arabidopsis leaf and root microbiotas."; RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KQS24767.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LMPS01000008; KQS24767.1; -; Genomic_DNA. DR RefSeq; WP_056291441.1; NZ_LMPS01000008.1. DR EnsemblBacteria; KQS24767; KQS24767; ASG33_23730. DR Proteomes; UP000051810; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000051810}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000051810}. FT DOMAIN 207 393 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 412 AA; 47300 MW; 7D8B8518BA6091B9 CRC64; MIDKKKFHST AVQPETAVLV AVSTQKQNVE KTKEYLEELA FLATTLGVET VRTFTQNLER PDTRTYTGKG KLEEIQTFIK ANPVDMVIYD DDLTPSQVRN LEAEFTDIKV IDRSLLILAI FAMRAQTAQS KLQVELAQYQ YMYPRLTRLW THLSRQSGAG VGMRGPGETE LETDRRIVKD RIAFLKEKLE KVDKQSITRR KERDRLVRVA IVGYTNVGKS TLMRSLSKAD VFAENRLFAT VDSTVRKVNM ENIPFLLTDT VGFIRKLPTT LIESFKSTLD EVREADILMH VVDISHPSFE EHLDVVNKTL EEIGAANKPS ILVFNKIDLY KPSFHEEEEN EDEGVMLQET VLEQLKKSYI SDKAEHVVFI SAEKKENIEE LRNTLFSLVK EKHFSIYPNW LDLGYTAVQT EE // ID A0A0Q5TXV0_9SPHI Unreviewed; 396 AA. AC A0A0Q5TXV0; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=ASG14_02465 {ECO:0000313|EMBL:KQS41358.1}; OS Pedobacter sp. Leaf194. OC Bacteria; Bacteroidetes; Sphingobacteriia; Sphingobacteriales; OC Sphingobacteriaceae; Pedobacter. OX NCBI_TaxID=1736297 {ECO:0000313|EMBL:KQS41358.1, ECO:0000313|Proteomes:UP000051708}; RN [1] {ECO:0000313|EMBL:KQS41358.1, ECO:0000313|Proteomes:UP000051708} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Leaf194 {ECO:0000313|EMBL:KQS41358.1, RC ECO:0000313|Proteomes:UP000051708}; RA Millard Andrew; RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:KQS41358.1, ECO:0000313|Proteomes:UP000051708} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Leaf194 {ECO:0000313|EMBL:KQS41358.1, RC ECO:0000313|Proteomes:UP000051708}; RA Vorholt J.; RT "Functional overlap of the Arabidopsis leaf and root microbiotas."; RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KQS41358.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LMPU01000001; KQS41358.1; -; Genomic_DNA. DR RefSeq; WP_056869471.1; NZ_LMPU01000001.1. DR EnsemblBacteria; KQS41358; KQS41358; ASG14_02465. DR Proteomes; UP000051708; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR018247; EF_Hand_1_Ca_BS. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS00018; EF_HAND_1; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000051708}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}. FT DOMAIN 204 384 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 396 AA; 45146 MW; 8CC9E365BAA235ED CRC64; MGKQKFYDTA IKQERAILVG VITPGEKEEQ TKEYLDELAF LVETAGGMVE KNFTQKMLKP ERATFVGTGK LEEIKAYVKS EEIDTVVFDD ELSPSQLRNI DRELGVKVLD RSNLILDIFA SRAQTAQAKT QVELAQLQYV LPRLTGMWTH LERQKGGIGM RGPGETQIES DRRIILNKIS LLKERLRNID KQNETQRKNR GELIRVALVG YTNVGKSTIM NMLSKSEVFA ENKLFATLDT TVRKVVIENL PFLLSDTVGF IRKLPHHLVE CFKSTLDEVR EADILIHVVD VSHPNFEDQI HIVNETLKDI GAIDKDMILV FNKIDAYVSP EVEDEDGDGK LTIEDFKKSW MSHGKVPVLF ISATERENIE EFKTLLYDKV KAAHVARYPY DSNLLY // ID A0A0Q5V0Q2_9FLAO Unreviewed; 409 AA. AC A0A0Q5V0Q2; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=ASG38_16110 {ECO:0000313|EMBL:KQS52661.1}; OS Flavobacterium sp. Leaf359. OC Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales; OC Flavobacteriaceae; Flavobacterium. OX NCBI_TaxID=1736351 {ECO:0000313|EMBL:KQS52661.1, ECO:0000313|Proteomes:UP000051024}; RN [1] {ECO:0000313|EMBL:KQS52661.1, ECO:0000313|Proteomes:UP000051024} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Leaf359 {ECO:0000313|EMBL:KQS52661.1, RC ECO:0000313|Proteomes:UP000051024}; RA Millard Andrew; RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:KQS52661.1, ECO:0000313|Proteomes:UP000051024} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Leaf359 {ECO:0000313|EMBL:KQS52661.1, RC ECO:0000313|Proteomes:UP000051024}; RA Vorholt J.; RT "Functional overlap of the Arabidopsis leaf and root microbiotas."; RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KQS52661.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LMPW01000002; KQS52661.1; -; Genomic_DNA. DR RefSeq; WP_056066949.1; NZ_LMPW01000002.1. DR EnsemblBacteria; KQS52661; KQS52661; ASG38_16110. DR Proteomes; UP000051024; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000051024}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000051024}. FT DOMAIN 200 386 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 409 AA; 47437 MW; 0D88FF76A2432BDE CRC64; MLEKETIKFE KTVVVGIVTQ HQNEEKLNEY LDELEFLTFT AGGEVVKRFS QKMERPNPKT FLGTGKMDEI HHYVKEHNIN TVIFDDELSP SQQKNITKIL NCKVLDRTNL ILDIFAQRAE TSYARTQVEL AQCQYLLPRL SGMWTHLERQ KGGIGMRGPG ETEIETDRRI VRDRIALLKD KIKVIDKQMS VQRSNRGAMV RVALVGYTNV GKSTLMNVIS KSEVFVENKL FATLDTTVRK VVIKNLPFLL SDTVGFIRKL PTQLVESFKS TLDEVREADL LLHVVDISHP DFEDHIDSVN QILADIKSAD KPTIMVFNKI DSYKHLTIDA DDLITEKTTK HYTLEEWKDT WMSRMGKDRA LFISALNKEN FEEFREKVYE AVREIHITRF PYNKFLYPDY KEAPEDKND // ID A0A0Q5V7X9_9CAUL Unreviewed; 436 AA. AC A0A0Q5V7X9; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=ASG17_09685 {ECO:0000313|EMBL:KQS56620.1}; OS Brevundimonas sp. Leaf363. OC Bacteria; Proteobacteria; Alphaproteobacteria; Caulobacterales; OC Caulobacteraceae; Brevundimonas. OX NCBI_TaxID=1736353 {ECO:0000313|EMBL:KQS56620.1, ECO:0000313|Proteomes:UP000051182}; RN [1] {ECO:0000313|EMBL:KQS56620.1, ECO:0000313|Proteomes:UP000051182} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Leaf363 {ECO:0000313|EMBL:KQS56620.1, RC ECO:0000313|Proteomes:UP000051182}; RA Millard Andrew; RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:KQS56620.1, ECO:0000313|Proteomes:UP000051182} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Leaf363 {ECO:0000313|EMBL:KQS56620.1, RC ECO:0000313|Proteomes:UP000051182}; RA Vorholt J.; RT "Functional overlap of the Arabidopsis leaf and root microbiotas."; RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KQS56620.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LMPZ01000002; KQS56620.1; -; Genomic_DNA. DR RefSeq; WP_056103390.1; NZ_LMPZ01000002.1. DR EnsemblBacteria; KQS56620; KQS56620; ASG17_09685. DR Proteomes; UP000051182; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000051182}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000051182}. FT DOMAIN 205 379 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 436 AA; 48395 MW; 97E3789BA7855270 CRC64; MTKLIDHTVP LIRAIVIHPD GRSDSPRSAE GRLEEAVGLA RALDLDVRAE EIVRLRKTTP ATLFGAGKVD ELAALVRAAE AEAVVIDDAL TPVQQRNLEK AFDAKVIDRT GLILEIFGRR ARTREGRLQV ELARLDYERS RLVRTWTHLE RQRGGTGSTG GPGETQIELD RRLIADRIVK LKTELEEVRR TRGLHRKQRQ KAPFPTIALV GYTNAGKSTL FNRLTGSEVM AKDLLFATLD TTQRTIRLPQ GRPAIIADTV GFISDLPHEL VESFRATLEE VAEADLILHV RDISSPDTGA EAQDVEAVLA QIPAIEGRPR RILEVWNKAD RLDDDAREDV QAQAARPDRD PQAAVVSAWT GQGIETLRQT IAGLIDDDPE TELLLQPDQG EALAWLYANG RVTARDTDDD GRIRLTVRLH PAAMGRLERL YPTLIA // ID A0A0Q5VCJ8_9ACTN Unreviewed; 502 AA. AC A0A0Q5VCJ8; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 05-JUL-2017, entry version 12. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=ASG36_21230 {ECO:0000313|EMBL:KQS54168.1}; OS Geodermatophilus sp. Leaf369. OC Bacteria; Actinobacteria; Geodermatophilales; Geodermatophilaceae; OC Geodermatophilus. OX NCBI_TaxID=1736354 {ECO:0000313|EMBL:KQS54168.1, ECO:0000313|Proteomes:UP000051830}; RN [1] {ECO:0000313|EMBL:KQS54168.1, ECO:0000313|Proteomes:UP000051830} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Leaf369 {ECO:0000313|EMBL:KQS54168.1, RC ECO:0000313|Proteomes:UP000051830}; RA Millard Andrew; RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:KQS54168.1, ECO:0000313|Proteomes:UP000051830} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Leaf369 {ECO:0000313|EMBL:KQS54168.1, RC ECO:0000313|Proteomes:UP000051830}; RA Vorholt J.; RT "Functional overlap of the Arabidopsis leaf and root microbiotas."; RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KQS54168.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LMQA01000007; KQS54168.1; -; Genomic_DNA. DR EnsemblBacteria; KQS54168; KQS54168; ASG36_21230. DR Proteomes; UP000051830; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000313|EMBL:KQS54168.1}; KW Complete proteome {ECO:0000313|Proteomes:UP000051830}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900, KW ECO:0000313|EMBL:KQS54168.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000051830}. FT DOMAIN 281 445 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 502 AA; 53722 MW; 665C886F880769A6 CRC64; MTTAQNRAVL EDAVARADKA AVTPLPTETA GDSRPAPRGQ WDEPDETTGS YVKEERGALR RVAGLSTELT DVTEVEYRQL RLERVVLVGV WTEGTAKDAD RSLVELAALA QTAGSEVLEA VSQRRDKPDA GTYVGSGKAA EIREIVAATG ADTVICDGEL TPGQLNQLEK ILKVKVVDRT ALILDIFAQH ATSREGKAQV ELAQMQYMLP RLRGWGESLS RQAGGRVAGG GGIGTRGPGE TKIETDRRRI RARVSKLRKE IAGMATARAT QRSGRDRNQT PSVAIAGYTN AGKSSLLNQL TDAGVLVQDA LFATLDPTVR RAEMPDGRDY TLTDTVGFVR HLPHQLIDAF RSTLEEVAAA DLLVHVVDGS DPDPLGQIDA VHVVLAEIDA ASVPELIVVN KIDAMDDEDV LALRQALPGA QWVSAATGEG MAELRDVIAA RLPHPDVDVD VLVPFDRGDL VSRVHQDGEV LSEDFSADGT RLHARVDGAL AAALEEFTAP VA // ID A0A0Q5VQU3_9RHIZ Unreviewed; 440 AA. AC A0A0Q5VQU3; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 07-JUN-2017, entry version 13. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=ASG39_15275 {ECO:0000313|EMBL:KQS63260.1}; OS Rhizobium sp. Leaf371. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium. OX NCBI_TaxID=1736355 {ECO:0000313|EMBL:KQS63260.1, ECO:0000313|Proteomes:UP000052161}; RN [1] {ECO:0000313|EMBL:KQS63260.1, ECO:0000313|Proteomes:UP000052161} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Leaf371 {ECO:0000313|EMBL:KQS63260.1, RC ECO:0000313|Proteomes:UP000052161}; RA Millard Andrew; RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:KQS63260.1, ECO:0000313|Proteomes:UP000052161} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Leaf371 {ECO:0000313|EMBL:KQS63260.1, RC ECO:0000313|Proteomes:UP000052161}; RA Vorholt J.; RT "Functional overlap of the Arabidopsis leaf and root microbiotas."; RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KQS63260.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LMQB01000027; KQS63260.1; -; Genomic_DNA. DR RefSeq; WP_062596506.1; NZ_LMQB01000027.1. DR EnsemblBacteria; KQS63260; KQS63260; ASG39_15275. DR Proteomes; UP000052161; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000052161}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000052161}. FT DOMAIN 203 375 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 162 196 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 440 AA; 49144 MW; 68AE9D576DAAB01D CRC64; MRALVIVPVV KKTGRQQAEQ PHSVRTDEAR LEETIGLARA IDLSVVQGLV VPIAQPKPGT LLGSGKIEEI GQLLDAQDAG LVIVDHPLTP VQQRNLEKEW NAKVIDRTGL ILEIFGRRAS TKEGTLQVDL AHLNYQKGRL VRSWTHLERQ RGGAGFMGGP GETQIEADRR QLQDKIIKLE KELEQVRRTR QLHRSKRRKV PHPIVALVGY TNAGKSTLFN RITGAGVLAE DMLFATLDPT LRRMKLPQGR TVILSDTVGF ISDLPTHLVA AFRATLEEVL EADLILHVRD VSDPDHAAQS DDVERILEDL GIDEKARSER LLEVWNKIDR LEEEPHAAML EKAAHTPNTV TVSAVTGEGV DALMQEINRR LSGVMMETTV TLPVDRLQLL PWLYEHAIVD QREDLEDGSI RLDLRLTETE AGELDRRLGQ GPKPAAEDWH // ID A0A0Q5YPC9_9RHIZ Unreviewed; 452 AA. AC A0A0Q5YPC9; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=ASG40_14315 {ECO:0000313|EMBL:KQT07494.1}; OS Methylobacterium sp. Leaf399. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Methylobacteriaceae; Methylobacterium. OX NCBI_TaxID=1736364 {ECO:0000313|EMBL:KQT07494.1, ECO:0000313|Proteomes:UP000052067}; RN [1] {ECO:0000313|EMBL:KQT07494.1, ECO:0000313|Proteomes:UP000052067} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Leaf399 {ECO:0000313|EMBL:KQT07494.1, RC ECO:0000313|Proteomes:UP000052067}; RA Millard Andrew; RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:KQT07494.1, ECO:0000313|Proteomes:UP000052067} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Leaf399 {ECO:0000313|EMBL:KQT07494.1, RC ECO:0000313|Proteomes:UP000052067}; RA Vorholt J.; RT "Functional overlap of the Arabidopsis leaf and root microbiotas."; RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KQT07494.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LMQK01000034; KQT07494.1; -; Genomic_DNA. DR RefSeq; WP_055889504.1; NZ_LMQK01000034.1. DR EnsemblBacteria; KQT07494; KQT07494; ASG40_14315. DR Proteomes; UP000052067; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000052067}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000052067}. FT DOMAIN 213 389 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 452 AA; 49312 MW; B2A56679F082BB68 CRC64; MAAPEGEIAA ATHTLVIGPY LARTASGGSR SEASRATDAR LDEAVGLAAA IELDVVEAIC LSLPRIRPST YLGKGRVEEL AGVIKAREIG LVVMDCALSP VQQRNLEKEL GAKVIDRTGL ILEIFGRRAS TREGRLQVEH AHLAYQKSRL VRSWTHLERQ RGGFGFLGGP GETQIEADRR MIQERMTRIE RDLDGVTRTR GLHRQGRARV PYPIVALVGY TNAGKSTLFN TLTKAEVMAQ DMLFATLDPT ARATRLPHGE TVILSDTVGF ISDLPTSLIA AFRATLEDVI EADILLHVRD ISHGDSEAQA EDVGGVLREL GIETSADRII EVWNKADLLD EDERNRLLNL TGTGRSDRDS GAPVLVSAVT GEGMAALTSR IEARIAKSRS TFAVVLSPED GGALHWLYEN AEVLDRREEE GGTIHLAIRI APEKEPRFLN RFDGARRLSR AG // ID A0A0Q5ZC27_9BURK Unreviewed; 394 AA. AC A0A0Q5ZC27; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=ASG30_07440 {ECO:0000313|EMBL:KQT10639.1}; OS Ramlibacter sp. Leaf400. OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Comamonadaceae; Ramlibacter. OX NCBI_TaxID=1736365 {ECO:0000313|EMBL:KQT10639.1, ECO:0000313|Proteomes:UP000051173}; RN [1] {ECO:0000313|EMBL:KQT10639.1, ECO:0000313|Proteomes:UP000051173} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Leaf400 {ECO:0000313|EMBL:KQT10639.1, RC ECO:0000313|Proteomes:UP000051173}; RA Millard Andrew; RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:KQT10639.1, ECO:0000313|Proteomes:UP000051173} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Leaf400 {ECO:0000313|EMBL:KQT10639.1, RC ECO:0000313|Proteomes:UP000051173}; RA Vorholt J.; RT "Functional overlap of the Arabidopsis leaf and root microbiotas."; RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KQT10639.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LMQL01000010; KQT10639.1; -; Genomic_DNA. DR RefSeq; WP_055896127.1; NZ_LMQL01000010.1. DR EnsemblBacteria; KQT10639; KQT10639; ASG30_07440. DR Proteomes; UP000051173; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000051173}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000051173}. FT DOMAIN 200 378 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 394 AA; 43354 MW; 9A74A63DA32D0DC6 CRC64; MSDSQARPAA PTILVGVDLG LPHFDAELQE LGELARTAGL EPVARMTAKR KAPDAALFVG RGKADEIKAL AEETGATEVL FDQSLSPGQQ RNLERHLGLP VNDRTLLILE IFAQRARSHE GKLQVELARL QYVSTRLVRR WSHLERQTGG AGVRGGPGEK QIELDRRMIG DAIKRTRDRL DKVKKQRHTQ RRQRERQGAF NISLVGYTNA GKSTLFNALV KAQAYAADQL FATLDTTTRR MYLDDVEGGS GGRSVSLSDT VGFIRDLPHG LIDAFQATLQ EATDADLLLH VVDAANPHHP EQIAEVQRVL HEIGADQVPQ LLVFNKLDAL DPSQRPRLRS DVFELEGAPV RRVFVSSRTA DGLPTLRQEL AGRAAEAARP QSLQTSPELH DTAA // ID A0A0Q6AH95_9BRAD Unreviewed; 458 AA. AC A0A0Q6AH95; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 07-JUN-2017, entry version 12. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=ASG57_02140 {ECO:0000313|EMBL:KQT29446.1}; OS Bradyrhizobium sp. Leaf396. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Bradyrhizobiaceae; Bradyrhizobium. OX NCBI_TaxID=1736363 {ECO:0000313|EMBL:KQT29446.1, ECO:0000313|Proteomes:UP000051536}; RN [1] {ECO:0000313|EMBL:KQT29446.1, ECO:0000313|Proteomes:UP000051536} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Leaf396 {ECO:0000313|EMBL:KQT29446.1, RC ECO:0000313|Proteomes:UP000051536}; RA Millard Andrew; RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:KQT29446.1, ECO:0000313|Proteomes:UP000051536} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Leaf396 {ECO:0000313|EMBL:KQT29446.1, RC ECO:0000313|Proteomes:UP000051536}; RA Vorholt J.; RT "Functional overlap of the Arabidopsis leaf and root microbiotas."; RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KQT29446.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LMQJ01000001; KQT29446.1; -; Genomic_DNA. DR RefSeq; WP_024341778.1; NZ_LMQJ01000001.1. DR EnsemblBacteria; KQT29446; KQT29446; ASG57_02140. DR Proteomes; UP000051536; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000051536}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}. FT DOMAIN 225 399 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 184 211 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 458 AA; 50562 MW; FA2357E2F58EF929 CRC64; MEPRNFGGDA DRPRSAGAHT GRVLVIGPYL RVRGGGADAQ SESHAMRDVE ARLDEAAGLA RAIDLVVADA IIAPVGQIRP ATYIGKGKVE EIAGLIKTLE VELVVMDCAL SPIQQRNLEK EWQAKVLDRT GLILEIFGRR AKTREGSLQV ELAHLNYQRS RLVRSWTHLE RQRGGFGFMG GPGETQIEAD RRLIQERISK LESELKKVQA TRRLHRAGRQ RVPYRVVALV GYTNAGKSTL FNRLTRADVQ AADMLFATLD PTLRALNLPH GGKAMLSDTV GFISNLPTQL VAAFRATLEE VLEADVILHV RDISHEDAEA QQSDVDAVLR QLGINPDDSG RIIEVWNKID RFAPEQREEL LNIAARRPED HPAMLVSAVS GEGIDALLAA IEQRLAAKRT TLDLSIDATD GAGISWLHRN AEVLSKELHD GRFDMTVRVD ETKRDIVVSR FDAVPHAT // ID A0A0Q6B823_9PROT Unreviewed; 446 AA. AC A0A0Q6B823; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 30-AUG-2017, entry version 12. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=ASG34_09050 {ECO:0000313|EMBL:KQT41711.1}; OS Methylophilus sp. Leaf416. OC Bacteria; Proteobacteria; Betaproteobacteria; Nitrosomonadales; OC Methylophilaceae; Methylophilus. OX NCBI_TaxID=1736373 {ECO:0000313|EMBL:KQT41711.1, ECO:0000313|Proteomes:UP000050891}; RN [1] {ECO:0000313|EMBL:KQT41711.1, ECO:0000313|Proteomes:UP000050891} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Leaf416 {ECO:0000313|EMBL:KQT41711.1, RC ECO:0000313|Proteomes:UP000050891}; RA Millard Andrew; RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:KQT41711.1, ECO:0000313|Proteomes:UP000050891} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Leaf416 {ECO:0000313|EMBL:KQT41711.1, RC ECO:0000313|Proteomes:UP000050891}; RA Vorholt J.; RT "Functional overlap of the Arabidopsis leaf and root microbiotas."; RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KQT41711.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LMQS01000003; KQT41711.1; -; Genomic_DNA. DR RefSeq; WP_055829717.1; NZ_LMQS01000003.1. DR EnsemblBacteria; KQT41711; KQT41711; ASG34_09050. DR Proteomes; UP000050891; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000050891}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000050891}. FT DOMAIN 220 390 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 446 AA; 49785 MW; C4DEE16344F65323 CRC64; MQSEVKEPIR YAVVAAVQLP NVSDIEFEAS LSELRELAKT LGYKIVNTFV QKRTSFDTTG YLGIGKREEI RDYVSIESAE DESQSLDAQL PIIEAVLVDH EISPAQARNL EIEVGCEVMD RTMVILEIFH RNARSRAARA QVEIARLGYM APRLREAAKL AGPQGRQRSG AGGRGAGESH TELDRRKIRD RIADLQQEII VMDGERRTQR ARRQERQTMA SVALVGYTNA GKSTLMRALT GSEVLVANKL FATLDTTVRA LYPESVPRVL VSDTVGFIKN LPHGLVASFK STLDEALDAS LLLHVIDASD PGFERQLEVT DKVLEEIEAD DVPRIRVFNK IDYVGDATAQ AECDAALRLK YPDCIVMSAR RPDEVAALRQ KLVDFFQQDL VEAEIFVPWS AQQLRGKIYS TCQVVSERSE DDGTFFTVRG EANDIDSLRE QLTQLE // ID A0A0Q6BLF7_9PROT Unreviewed; 375 AA. AC A0A0Q6BLF7; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 30-AUG-2017, entry version 12. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=ASG34_00735 {ECO:0000313|EMBL:KQT43361.1}; OS Methylophilus sp. Leaf416. OC Bacteria; Proteobacteria; Betaproteobacteria; Nitrosomonadales; OC Methylophilaceae; Methylophilus. OX NCBI_TaxID=1736373 {ECO:0000313|EMBL:KQT43361.1, ECO:0000313|Proteomes:UP000050891}; RN [1] {ECO:0000313|EMBL:KQT43361.1, ECO:0000313|Proteomes:UP000050891} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Leaf416 {ECO:0000313|EMBL:KQT43361.1, RC ECO:0000313|Proteomes:UP000050891}; RA Millard Andrew; RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:KQT43361.1, ECO:0000313|Proteomes:UP000050891} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Leaf416 {ECO:0000313|EMBL:KQT43361.1, RC ECO:0000313|Proteomes:UP000050891}; RA Vorholt J.; RT "Functional overlap of the Arabidopsis leaf and root microbiotas."; RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KQT43361.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LMQS01000001; KQT43361.1; -; Genomic_DNA. DR RefSeq; WP_055825302.1; NZ_LMQS01000001.1. DR EnsemblBacteria; KQT43361; KQT43361; ASG34_00735. DR Proteomes; UP000050891; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000050891}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000050891}. FT DOMAIN 199 365 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 158 192 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 375 AA; 41855 MW; FF6CD198E264E54C CRC64; MFDRPSGGDA VVLVSVNFGD ADYEESLQEL RHLAGTAGLN ISATLEGKRQ SPDPKFFIGS GKADELKALM ATYESKVAAF NHDLSPSQQR NLEKFLEARV VDRTGLILDI FAQRAQSHEG KLQVELAQLE HLSTRLVRGW THLERQKGGI GVRGGPGETQ LELDRRMLRV RVKQLRERLE KLKQQRGMQR RARKRSNLMT VSLVGYTNAG KSTLFNRLTH SGVYAADQLF ATLDTTSRKM YLPEGYPVVL SDTVGFIKHL PTTLIEAFGA TLEEASQADL LLHIVDVASP NRDNQIEQVN IVLNEIGASQ VTQIVVLNQI DRMGMSPGID RDEYGNIRTV RVSAMDGTGI EDLRQALLEH QQHLKKLSTE ERAYV // ID A0A0Q6C2X9_9RHIZ Unreviewed; 433 AA. AC A0A0Q6C2X9; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=ASG43_07415 {ECO:0000313|EMBL:KQT49013.1}; OS Aureimonas sp. Leaf454. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Aurantimonadaceae; Aureimonas. OX NCBI_TaxID=1736381 {ECO:0000313|EMBL:KQT49013.1, ECO:0000313|Proteomes:UP000051585}; RN [1] {ECO:0000313|EMBL:KQT49013.1, ECO:0000313|Proteomes:UP000051585} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Leaf454 {ECO:0000313|EMBL:KQT49013.1, RC ECO:0000313|Proteomes:UP000051585}; RA Millard Andrew; RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:KQT49013.1, ECO:0000313|Proteomes:UP000051585} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Leaf454 {ECO:0000313|EMBL:KQT49013.1, RC ECO:0000313|Proteomes:UP000051585}; RA Vorholt J.; RT "Functional overlap of the Arabidopsis leaf and root microbiotas."; RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KQT49013.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LMQT01000019; KQT49013.1; -; Genomic_DNA. DR RefSeq; WP_056505794.1; NZ_LMQT01000019.1. DR EnsemblBacteria; KQT49013; KQT49013; ASG43_07415. DR Proteomes; UP000051585; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000051585}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000051585}. FT DOMAIN 196 370 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 155 189 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 433 AA; 47242 MW; E040ACAC2BA06F48 CRC64; MLREHESRDE AGTAVVRRGD EQRLEEALGL AAAIDLEIVA SGVIQVSKAK PATLIGSGKV EEMKGVVAAE EIGLVIFDHP LTPVQQRNLE KELGAKVLDR TGLILEIFGR RARTKEGRLQ VDLAHLNYQK GRLVRSWTHL ERQRGGAGFL GGPGETQIES DRRQLQEKIK RLEKELEAVR RTRTLHRAKR KKAPHPVIAL VGYTNAGKST LFNTITGAGV LAQDLLFATL DPTLRRISLP HGTDVILSDT VGFISDLPTH LVAAFRATLE EVIEAELILH VRDMSDPDAS AQAADVNKIL RDLDIDTGDA DHVVEVWNKV DRLDEAGREV LKTAADTHGA GQGVFLVSAL TGEGIPALLT DIESRIAGQL GSITMTVPSD GLGLLPWLYD NANVRSRTDL EDGGVELVAD MTSQARDELR RLAEQRYPGL QLG // ID A0A0Q6D7M0_9RHIZ Unreviewed; 466 AA. AC A0A0Q6D7M0; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 05-JUL-2017, entry version 13. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=ASG52_01650 {ECO:0000313|EMBL:KQT61614.1}; OS Methylobacterium sp. Leaf456. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Methylobacteriaceae; Methylobacterium. OX NCBI_TaxID=1736382 {ECO:0000313|EMBL:KQT61614.1, ECO:0000313|Proteomes:UP000050829}; RN [1] {ECO:0000313|EMBL:KQT61614.1, ECO:0000313|Proteomes:UP000050829} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Leaf456 {ECO:0000313|EMBL:KQT61614.1, RC ECO:0000313|Proteomes:UP000050829}; RA Millard Andrew; RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:KQT61614.1, ECO:0000313|Proteomes:UP000050829} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Leaf456 {ECO:0000313|EMBL:KQT61614.1, RC ECO:0000313|Proteomes:UP000050829}; RA Vorholt J.; RT "Functional overlap of the Arabidopsis leaf and root microbiotas."; RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KQT61614.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LMQV01000001; KQT61614.1; -; Genomic_DNA. DR RefSeq; WP_056238108.1; NZ_LMQV01000001.1. DR EnsemblBacteria; KQT61614; KQT61614; ASG52_01650. DR GeneID; 32609997; -. DR Proteomes; UP000050829; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000050829}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}. FT DOMAIN 229 403 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 466 AA; 50938 MW; 5C0C8B1A56DE8E85 CRC64; MTELQTPGEA RLQQQAAPEG EIAASTRTLV VGPYLTRAGQ RLAPGQPENI RSDDARLDEA VGLAAAIELD VAQAIGVHVQ RPRPSTYLGK GRVEEMAGLV KADEIGLVVM DCALSPVQQR NLEKAWGTKV IDRTGLILEI FGRRASTREG TLQVEHAHLA YQKSRLVRSW THLERQRGGF GFLGGPGETQ IEADRRMIQE RMTKIERDLD AVTRTRGLHR KSRARVPYPI IALVGYTNAG KSTLFNALTK AEVKAQDMLF ATLDPTARAT KLPHGETVIL SDTVGFISDL PTSLIAAFRA TLEDVIEADI LLHVRDVSHG DTQAQAEDVE QVLRELGIEA DAERIVEVWN KADLLDEGER TRLLNLAAAH RGAGPAPILV SALTGEGLPA LSERIEGQVA RARSTFALTL PPEDGAALNW LYENAEVLDR QAEDSGEIAL TIRIAPEKEP RFLNRFEAAR KVASPQ // ID A0A0Q6EQH0_9RHIZ Unreviewed; 448 AA. AC A0A0Q6EQH0; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=ASG54_09305 {ECO:0000313|EMBL:KQT79476.1}; OS Aureimonas sp. Leaf460. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Aurantimonadaceae; Aureimonas. OX NCBI_TaxID=1736384 {ECO:0000313|EMBL:KQT79476.1, ECO:0000313|Proteomes:UP000051159}; RN [1] {ECO:0000313|EMBL:KQT79476.1, ECO:0000313|Proteomes:UP000051159} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Leaf460 {ECO:0000313|EMBL:KQT79476.1, RC ECO:0000313|Proteomes:UP000051159}; RA Millard Andrew; RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:KQT79476.1, ECO:0000313|Proteomes:UP000051159} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Leaf460 {ECO:0000313|EMBL:KQT79476.1, RC ECO:0000313|Proteomes:UP000051159}; RA Vorholt J.; RT "Functional overlap of the Arabidopsis leaf and root microbiotas."; RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KQT79476.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LMQY01000009; KQT79476.1; -; Genomic_DNA. DR RefSeq; WP_056692155.1; NZ_LMQY01000009.1. DR EnsemblBacteria; KQT79476; KQT79476; ASG54_09305. DR Proteomes; UP000051159; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000051159}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}. FT DOMAIN 212 386 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 171 205 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 448 AA; 49065 MW; 5297C03B008CD43D CRC64; MEHKPVATRA GVFVPVLREF EGRGEDPATA VVRRGDEQRL AEAVGLAAAI DLEIAATGII QVSKARPATL IGSGKVEEMK AIVEAEEIGL VIFDHPLTPV QQRNLEKELG AKVLDRTGLI LEIFGRRART KEGRLQVELA HLNYQKGRLV RSWTHLERQR GGAGFLGGPG ETQIESDRRQ LQEKIKRLEK ELEAVRRTRT LHRAKRKKAP HPIIALVGYT NAGKSTLFNT ITGAGVLAQD LLFATLDPTL RRISLPHGTD VIMSDTVGFI SDLPTHLVAS FRATLEEVIE AEIILHIRDM SDPDASAQAA DVNKILRDLD IDTGDADHVI EVWNKVDKLD EAGREVLRTA AETHTGGQGV FLVSALTGEG IPALLTDIEK RIAGQLGGVT LLVPPEDLSL LSWLYENANV RSRVDQDDGA VELVADMTVQ AKDELRRLVE RHPGLTLS // ID A0A0Q6F141_9RHIZ Unreviewed; 447 AA. AC A0A0Q6F141; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 05-JUL-2017, entry version 12. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=ASG48_13055 {ECO:0000313|EMBL:KQT83588.1}; OS Aurantimonas sp. Leaf443. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Aurantimonadaceae; Aurantimonas. OX NCBI_TaxID=1736378 {ECO:0000313|EMBL:KQT83588.1, ECO:0000313|Proteomes:UP000051458}; RN [1] {ECO:0000313|EMBL:KQT83588.1, ECO:0000313|Proteomes:UP000051458} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Leaf443 {ECO:0000313|EMBL:KQT83588.1, RC ECO:0000313|Proteomes:UP000051458}; RA Millard Andrew; RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:KQT83588.1, ECO:0000313|Proteomes:UP000051458} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Leaf443 {ECO:0000313|EMBL:KQT83588.1, RC ECO:0000313|Proteomes:UP000051458}; RA Vorholt J.; RT "Functional overlap of the Arabidopsis leaf and root microbiotas."; RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KQT83588.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LMRD01000009; KQT83588.1; -; Genomic_DNA. DR EnsemblBacteria; KQT83588; KQT83588; ASG48_13055. DR Proteomes; UP000051458; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000051458}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000051458}. FT DOMAIN 209 383 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 168 202 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 447 AA; 48891 MW; 075FCCDE8123EBC2 CRC64; MATRAGVFVP VFKQRPSGED GGQGVSDIHR RADEARLQEA IGLAAAIDLQ IVASGLVSGA RPKPATLIGS GKVEELKAVV ASEEIGLVIF DHPLTPVQQR NLEKELNCKV LDRTGLILEI FGRRARTKEG SLQVELAHLN YQRGRLVRSW THLERQRGGA GFLGGPGETQ IESDRRQLQD KIKRLEKELE QVRRTRTLHR AKRKKAPHPV VALVGYTNAG KSTLFNRLTG ADVLAKDLLF ATLDPTLRRL TLPHGTEAMI SDTVGFISDL PTHLVAAFRA TLEEVIEAEI VLHVRDMADA DTQAQAEDVR KILRDLDIDP DDTDHVIEIW NKVDRLDEAD RANLDLQRAG LPRNATAHVV SALTGEGVEA LLADIESRIA GDVGAVELAL EPDSLSLVPW VYENASIVSR EDREDGGVSL TVEMTTQALA ELRRLSEANA GLSVRTG // ID A0A0Q6FI81_9ACTN Unreviewed; 504 AA. AC A0A0Q6FI81; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=ASG49_04230 {ECO:0000313|EMBL:KQT94125.1}; OS Marmoricola sp. Leaf446. OC Bacteria; Actinobacteria; Propionibacteriales; Nocardioidaceae; OC Marmoricola. OX NCBI_TaxID=1736379 {ECO:0000313|EMBL:KQT94125.1, ECO:0000313|Proteomes:UP000051542}; RN [1] {ECO:0000313|EMBL:KQT94125.1, ECO:0000313|Proteomes:UP000051542} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Leaf446 {ECO:0000313|EMBL:KQT94125.1, RC ECO:0000313|Proteomes:UP000051542}; RA Millard Andrew; RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:KQT94125.1, ECO:0000313|Proteomes:UP000051542} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Leaf446 {ECO:0000313|EMBL:KQT94125.1, RC ECO:0000313|Proteomes:UP000051542}; RA Vorholt J.; RT "Functional overlap of the Arabidopsis leaf and root microbiotas."; RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KQT94125.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LMRF01000001; KQT94125.1; -; Genomic_DNA. DR RefSeq; WP_056537450.1; NZ_LMRF01000001.1. DR EnsemblBacteria; KQT94125; KQT94125; ASG49_04230. DR Proteomes; UP000051542; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000313|EMBL:KQT94125.1}; KW Complete proteome {ECO:0000313|Proteomes:UP000051542}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900, KW ECO:0000313|EMBL:KQT94125.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000051542}. FT DOMAIN 286 451 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 504 AA; 54614 MW; 80E67A2678A83495 CRC64; MTNASEPFDL AQELADTATW DEEPTEPRRP EVATAPAPTT PETSWPDERE QTTGEQDLAA RHQLRRVAGL STELEDISEV EYRQLRLERV VLVGVWTQGS VADAENSMAE LALLAETAGS TVLDALYQRR DSPDPATYIG RGKVEGLAEI VKASGADTVI CDGELAPSQL RNLEDKVKVK VVDRTALILD IFAQHAKSRE GQAQVELAQL NYMKQRLRGW GGNLSRQAGG RVAGGAGIGG RGPGETKIET DRRRINTKIA KLRRDLTHMK TTRDTKRSGR KRHEIPSVAI AGYTNAGKSS LLNRLTDAGV LVEDSLFATL DPTTRRTETG DGRVYTMSDT VGFVRHLPHQ LVEAFRSTLE EVADSDLIVH VVDGSHPDPE GQLAAVREVL AEIGADKVPE LVAINKADVA DPLVVARLRQ REPHSVVVSA RTGEGVAEAL AAIESELPKP AVEVSVLLPY DRGDLLSKVH EHGEVISLEH TGDGTQLKAR VNEVLAGELA AYPG // ID A0A0Q6FN88_9RHIZ Unreviewed; 441 AA. AC A0A0Q6FN88; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 05-JUL-2017, entry version 13. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=ASG68_12885 {ECO:0000313|EMBL:KQT95596.1}; OS Rhizobium sp. Leaf453. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium. OX NCBI_TaxID=1736380 {ECO:0000313|EMBL:KQT95596.1, ECO:0000313|Proteomes:UP000050939}; RN [1] {ECO:0000313|EMBL:KQT95596.1, ECO:0000313|Proteomes:UP000050939} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Leaf453 {ECO:0000313|EMBL:KQT95596.1, RC ECO:0000313|Proteomes:UP000050939}; RA Millard Andrew; RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:KQT95596.1, ECO:0000313|Proteomes:UP000050939} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Leaf453 {ECO:0000313|EMBL:KQT95596.1, RC ECO:0000313|Proteomes:UP000050939}; RA Vorholt J.; RT "Functional overlap of the Arabidopsis leaf and root microbiotas."; RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KQT95596.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LMRG01000026; KQT95596.1; -; Genomic_DNA. DR EnsemblBacteria; KQT95596; KQT95596; ASG68_12885. DR Proteomes; UP000050939; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000050939}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}. FT DOMAIN 205 377 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 164 198 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 441 AA; 48787 MW; BC8C7378E2D01039 CRC64; MRAVVIVPVL KKTGKQSADI IAATSTRSDE SRLEETIGLA RAIDLDVVHG MIVPVAQPKP GTLLGSGKIE EIGHLLSEHN AGLVIIDHPL TPVQQRNLEK EWNGKVIDRT GLILEIFGRR ASTKEGTLQV ELAHLNYQKG RLVRSWTHLE RQRGGAGFMG GPGETQIEAD RRLLQDKIIK LEKELEQVRR TRQLHRAKRK KVPHPIVALV GYTNAGKSTL FNRITGAGVL AEDMLFATLD PTLRRMKLPH GRMVILSDTV GFISDLPIHL VAAFRATLEE VLEADLILHV RDFSDPDNAV QAQDVIGILD DLGIDEKARS ERILEVWNKI DLLGEEAHIS LVQKAENSES TVAVSAVTGE GVDHLLNEIN KRLSGVLTET TVVLPPNKLQ LLSWIYEHTM VDGREDMEDG SVSLDLRMTP NEADELDRRL GNGPKAAAQD W // ID A0A0Q6KIN6_9SPHN Unreviewed; 430 AA. AC A0A0Q6KIN6; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=ASG67_06305 {ECO:0000313|EMBL:KQU55731.1}; OS Sphingomonas sp. Leaf339. OC Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales; OC Sphingomonadaceae; Sphingomonas. OX NCBI_TaxID=1736343 {ECO:0000313|EMBL:KQU55731.1, ECO:0000313|Proteomes:UP000051371}; RN [1] {ECO:0000313|EMBL:KQU55731.1, ECO:0000313|Proteomes:UP000051371} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Leaf339 {ECO:0000313|EMBL:KQU55731.1, RC ECO:0000313|Proteomes:UP000051371}; RA Millard Andrew; RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:KQU55731.1, ECO:0000313|Proteomes:UP000051371} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Leaf339 {ECO:0000313|EMBL:KQU55731.1, RC ECO:0000313|Proteomes:UP000051371}; RA Vorholt J.; RT "Functional overlap of the Arabidopsis leaf and root microbiotas."; RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KQU55731.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LMRS01000012; KQU55731.1; -; Genomic_DNA. DR RefSeq; WP_056527977.1; NZ_LMRS01000012.1. DR EnsemblBacteria; KQU55731; KQU55731; ASG67_06305. DR Proteomes; UP000051371; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000051371}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000051371}. FT DOMAIN 208 377 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 430 AA; 47052 MW; 3880F00A6581EAFF CRC64; MSTGFDRDRD EFARGARALV VLPDRGDSSR DANARLDECA GLAAAIGLDV VDRIAVRVRQ PRPATLIGSG QMAELATRVT MEEASLVVVD AALTPVQQRN LETGLGAKVI DRTGLILEIF GERAATAEGR LQVELAHLDY QAGRLVRSWT HLERQRGGFG FLGGPGETQI EADRRMIRDR MARLRRELEQ VSRTRGLHRD RRQRAPWPVI ALVGYTNAGK STLFNRLTGA DVMAENLLFA TLDPTLRQIA LPGLDKAILS DTVGFVSDLP TQLVAAFKAT LEEVVSADLL IHVRDIAHPD TEAQRADVET VLTEIGVADA TPRFEVWNKL DLLDQDGRED AMGDAERRGN VMAISALTGE GVDDMVQAVA AKLTEGHRRH TITLPASDGA SAAWLHAHGE VIDQRTEGDD AVYEVRLGEG DYARFSRRFS // ID A0A0Q6KJ12_9BRAD Unreviewed; 462 AA. AC A0A0Q6KJ12; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=ASG72_14535 {ECO:0000313|EMBL:KQU51013.1}; OS Bosea sp. Leaf344. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Bradyrhizobiaceae; Bosea. OX NCBI_TaxID=1736346 {ECO:0000313|EMBL:KQU51013.1, ECO:0000313|Proteomes:UP000050986}; RN [1] {ECO:0000313|EMBL:KQU51013.1, ECO:0000313|Proteomes:UP000050986} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Leaf344 {ECO:0000313|EMBL:KQU51013.1, RC ECO:0000313|Proteomes:UP000050986}; RA Millard Andrew; RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:KQU51013.1, ECO:0000313|Proteomes:UP000050986} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Leaf344 {ECO:0000313|EMBL:KQU51013.1, RC ECO:0000313|Proteomes:UP000050986}; RA Vorholt J.; RT "Functional overlap of the Arabidopsis leaf and root microbiotas."; RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KQU51013.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LMRT01000014; KQU51013.1; -; Genomic_DNA. DR RefSeq; WP_056713548.1; NZ_LMRT01000014.1. DR EnsemblBacteria; KQU51013; KQU51013; ASG72_14535. DR Proteomes; UP000050986; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000050986}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000050986}. FT DOMAIN 228 402 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 462 AA; 50779 MW; 6BD358D7DB296101 CRC64; MAGKSRGGET PAAKPLDEIE RDIAANTRAY VVGPYVQRRS PAAASDTNQR SFAARLDEAV GLAAAIDLTV VEPIQVLLTA LRPATYLGKG KVEELAERIR IEEIGLVVMD CALSPVQQRN LEKAFGCKVI DRTGLILEIF GRRARTREGA LQVELAHLNY QKSRLVRSWT HLERQRGGFG FLGGPGETQI EADRRIIQER MSKIERDLDS VKRTRSLHRA SRKRVPYPVV ALVGYTNAGK STLFNRLTSA EVLAQDMLFA TLDPTARAIK LPHGARIMLS DTVGFISDLP TQLVAAFRAT LEDAIEADVL LHVRDVSHED TQAQAADVQA ILRDLGIDPD DGQRVIEVWN KSDLLDGPER ERQLGLAALK PEASRPVLVS ALTGDGIARL TDAIESRIAR SRPVYRLRLD PGDGQSLAWL HANGEILARE DAEDGALDLL VRLPPEREGA FGARFAQAIR QE // ID A0A0Q6LRJ0_9RHIZ Unreviewed; 443 AA. AC A0A0Q6LRJ0; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=ASC75_06960 {ECO:0000313|EMBL:KQU70129.1}; OS Aminobacter sp. Root100. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Phyllobacteriaceae; Aminobacter. OX NCBI_TaxID=1736420 {ECO:0000313|EMBL:KQU70129.1, ECO:0000313|Proteomes:UP000051834}; RN [1] {ECO:0000313|EMBL:KQU70129.1, ECO:0000313|Proteomes:UP000051834} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Root100 {ECO:0000313|EMBL:KQU70129.1, RC ECO:0000313|Proteomes:UP000051834}; RA Millard Andrew; RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:KQU70129.1, ECO:0000313|Proteomes:UP000051834} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Root100 {ECO:0000313|EMBL:KQU70129.1, RC ECO:0000313|Proteomes:UP000051834}; RA Vorholt J.; RT "Functional overlap of the Arabidopsis leaf and root microbiotas."; RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KQU70129.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LMCL01000023; KQU70129.1; -; Genomic_DNA. DR RefSeq; WP_055977678.1; NZ_LMCL01000023.1. DR EnsemblBacteria; KQU70129; KQU70129; ASC75_06960. DR Proteomes; UP000051834; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000051834}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000051834}. FT DOMAIN 212 385 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 171 198 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 443 AA; 48761 MW; 77CFB68E26BF477D CRC64; MGGDKAPTRA IVIVPVLTRQ PKGDDDSARP RLQRSAEARH DEAVGLTRAI DLEPVHTAIV TLNDPRPATL LGTGKVEEFA EIVKERGAEL VIVDHPLTPV QQRNLEKEMN AKVLDRTGLI LEIFGRRART KEGTLQVELA HLNYQKGRLV RSWTHLERQR GGAGFLGGPG ETQIESDRRA LQEKIIKLKK ELETVVRTRD LHRAKRRKVP FPVVAIVGYT NAGKSTLFNR LTGAAVLAEN MLFATLDPTL RRVRLPHGTP IILSDTVGFI SDLPTHLIAA FRATLEEVVE ADLVIHLRDI SDPDTAAQAD DVERILSDLG VDAADTDRVV EVWNKIDQLD EGNRERLLSD SVDGRKTPPI AISAITGEGL SALTGLIEQR VSGELESIDV TLEPSQLGQI DWLYRNGDVV SRTDNDDGSV SMTLKATASA RDEIAAKILR NKR // ID A0A0Q6PKV2_9MICO Unreviewed; 501 AA. AC A0A0Q6PKV2; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 05-JUL-2017, entry version 12. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=ASC63_14945 {ECO:0000313|EMBL:KQV05281.1}; OS Leifsonia sp. Root112D2. OC Bacteria; Actinobacteria; Micrococcales; Microbacteriaceae; Leifsonia. OX NCBI_TaxID=1736426 {ECO:0000313|EMBL:KQV05281.1, ECO:0000313|Proteomes:UP000051914}; RN [1] {ECO:0000313|EMBL:KQV05281.1, ECO:0000313|Proteomes:UP000051914} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Root112D2 {ECO:0000313|EMBL:KQV05281.1, RC ECO:0000313|Proteomes:UP000051914}; RA Millard Andrew; RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:KQV05281.1, ECO:0000313|Proteomes:UP000051914} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Root112D2 {ECO:0000313|EMBL:KQV05281.1, RC ECO:0000313|Proteomes:UP000051914}; RA Vorholt J.; RT "Functional overlap of the Arabidopsis leaf and root microbiotas."; RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KQV05281.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LMCU01000002; KQV05281.1; -; Genomic_DNA. DR EnsemblBacteria; KQV05281; KQV05281; ASC63_14945. DR Proteomes; UP000051914; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 2. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000051914}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000051914}. FT DOMAIN 280 445 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 501 AA; 54087 MW; 27867004C8009C72 CRC64; MSETDVVARV LQNAAARASG YSLFSTGAQA LQGDAGAENP EGDHDGQQLD REERAALRRV AGLSTELEDV TEVEYRQLRL ENVVLIGVYS QGSQADAENS MRELAALAET AGAVVLDGLL QRRPHPDPST YLGRGKAQEL QSLVASLGAD TVIADTELAP SQRRALEDVV KVKVIDRTAV ILDIFSQHAK SREGKAQVEL AQLEYLLPRL RGWGESMSRQ AGGQVGGAGA GMGSRGPGET KIELDRRRIH TRMAKLRKQI VGFKPAREAK RANRRRNAVP SVAIAGYTNA GKSSLLNRIT KAGVLVENAL FATLDATVRK SVTADGRLYT LTDTVGFVRN LPHQLVEAFR STLEEVADSD LIVHVVDASH PDPASQLTTV RDVIGEVGAR DIPELVVFNK ADLVTDDDRL VLRGLEPNAV FVSARTGEGV DDVLAAIARL LPDPSIEIDV VIPYDRGDLV AALHERGRVL ETEYVAAGTR IRALMMPEYE SVFTAFASAT H // ID A0A0Q6RBH7_9MICO Unreviewed; 518 AA. AC A0A0Q6RBH7; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 07-JUN-2017, entry version 10. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=ASC54_07605 {ECO:0000313|EMBL:KQV26916.1}; OS Yonghaparkia sp. Root332. OC Bacteria; Actinobacteria; Micrococcales; Microbacteriaceae; OC Yonghaparkia. OX NCBI_TaxID=1736516 {ECO:0000313|EMBL:KQV26916.1, ECO:0000313|Proteomes:UP000051768}; RN [1] {ECO:0000313|EMBL:KQV26916.1, ECO:0000313|Proteomes:UP000051768} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Root332 {ECO:0000313|EMBL:KQV26916.1, RC ECO:0000313|Proteomes:UP000051768}; RA Millard Andrew; RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:KQV26916.1, ECO:0000313|Proteomes:UP000051768} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Root332 {ECO:0000313|EMBL:KQV26916.1, RC ECO:0000313|Proteomes:UP000051768}; RA Vorholt J.; RT "Functional overlap of the Arabidopsis leaf and root microbiotas."; RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KQV26916.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LMCX01000001; KQV26916.1; -; Genomic_DNA. DR RefSeq; WP_055898139.1; NZ_LMCX01000001.1. DR EnsemblBacteria; KQV26916; KQV26916; ASC54_07605. DR Proteomes; UP000051768; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000051768}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000051768}. FT DOMAIN 297 462 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 518 AA; 56186 MW; B66B20C3B89FE520 CRC64; MSDQTTAPGA DEPREVPIGD DAEEDAVARV LAHADSRARS VSLHGGRASA LQDDDSYLSD RDGDQFDRED RAALRRVRGL STELDDVTEV EYRQLRLENV VLIGVYSGGS IADAENSLRE LAALAETAGA VVLDGLLQRR PHPDPSTYLG KGKAAELALI VAELGADTVI ADTELAPSQR RALEDVVKVK VIDRTAVILD IFSQHAKSRE GKAQVELAQL EYLLPRLRGW GESMSRQAGG QVGSAGAGMG SRGPGETKME LDRRRIHTRM AKLRKQIKGF APARAAKRAN RDRYTVPSVA IAGYTNAGKS SLLNRITRAG VLVENALFAT LDATVRKSST PDGRPFTLAD TVGFVRNLPH QLVEAFRSTL EEIAESDVIV HVVDGAHPDP AAQIATVRNV IGEVEARHLP EIIAFNKADL LDDDARLVLR GLEPTAVFVS AKTGEGIDEL RARIAELLPN PEVELELLIP FERGELVALL HERGRVISTD YDERGTRVHA FLDPQFTGPF EPFVVVGA // ID A0A0Q6SYD0_9RHIZ Unreviewed; 442 AA. AC A0A0Q6SYD0; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=ASC86_19315 {ECO:0000313|EMBL:KQV42486.1}; OS Rhizobium sp. Root1212. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium. OX NCBI_TaxID=1736429 {ECO:0000313|EMBL:KQV42486.1, ECO:0000313|Proteomes:UP000052066}; RN [1] {ECO:0000313|EMBL:KQV42486.1, ECO:0000313|Proteomes:UP000052066} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Root1212 {ECO:0000313|EMBL:KQV42486.1, RC ECO:0000313|Proteomes:UP000052066}; RA Millard Andrew; RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:KQV42486.1, ECO:0000313|Proteomes:UP000052066} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Root1212 {ECO:0000313|EMBL:KQV42486.1, RC ECO:0000313|Proteomes:UP000052066}; RA Vorholt J.; RT "Functional overlap of the Arabidopsis leaf and root microbiotas."; RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KQV42486.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LMDA01000003; KQV42486.1; -; Genomic_DNA. DR RefSeq; WP_056318798.1; NZ_LMDA01000003.1. DR EnsemblBacteria; KQV42486; KQV42486; ASC86_19315. DR Proteomes; UP000052066; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000052066}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000052066}. FT DOMAIN 206 378 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 165 199 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 442 AA; 48588 MW; 691B78CBB451ADCF CRC64; MRALVIVPVL KKAGRQAAAD IVAPTTTRSD ESRLEEAIGL ALAIDLTVVQ GLIVPIAQPK PGTLLGTGKI EEIGHLLSEH NAGLVIVDHP LTPVQQRNLE KEWNAKVIDR TGLILEIFGR RASTKEGTLQ VELAHLNYQK GRLVRSWTHL ERQRGGAGFL GGPGETQIEA DRRLLQEKIL RLERELEQVR RTRQLHRAKR KKVPHPIVAL VGYTNAGKST LFNRITGAGV LAEDMLFATL DPTLRRMKLP AGRTVILSDT VGFISDLPTH LVAAFRATLE EVLEADLVLH VRDLSDPDNP AQASDVLRIL ADLGIDEKEG ATRIIEVWNK IDLLEPEARE ALVQKAATSK NTVAVSAFTG EGVDKLLGEI NTRLSGVMTE CTVVLATDKL QLLPWIYEHT IVDGREDMED GSVSLDLRLT AAESVELDRR LGNGPKPQVD DW // ID A0A0Q6VDJ3_9ACTN Unreviewed; 459 AA. AC A0A0Q6VDJ3; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 05-JUL-2017, entry version 12. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=ASC61_18585 {ECO:0000313|EMBL:KQV76843.1}; OS Aeromicrobium sp. Root344. OC Bacteria; Actinobacteria; Propionibacteriales; Nocardioidaceae; OC Aeromicrobium. OX NCBI_TaxID=1736521 {ECO:0000313|EMBL:KQV76843.1, ECO:0000313|Proteomes:UP000051702}; RN [1] {ECO:0000313|EMBL:KQV76843.1, ECO:0000313|Proteomes:UP000051702} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Root344 {ECO:0000313|EMBL:KQV76843.1, RC ECO:0000313|Proteomes:UP000051702}; RA Millard Andrew; RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:KQV76843.1, ECO:0000313|Proteomes:UP000051702} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Root344 {ECO:0000313|EMBL:KQV76843.1, RC ECO:0000313|Proteomes:UP000051702}; RA Vorholt J.; RT "Functional overlap of the Arabidopsis leaf and root microbiotas."; RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KQV76843.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LMDH01000001; KQV76843.1; -; Genomic_DNA. DR EnsemblBacteria; KQV76843; KQV76843; ASC61_18585. DR Proteomes; UP000051702; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 2. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000313|EMBL:KQV76843.1}; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000051702}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900, KW ECO:0000313|EMBL:KQV76843.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000051702}. FT DOMAIN 241 406 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 200 234 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 459 AA; 49919 MW; 5E20433593775CF1 CRC64; MTEQVGSTEG LELEERNSLR RVANLRTELE DITEVEYRQL RLERVVLVGV WTEGTAEDAD NSLAELKLLA ETAGSEVLDA LIQRRQKPDP ATYIGSGKVE DLRAAVVATG ADTIICDGAL APSQLRNLED RCKVKVVDRT ALILDIFAQH AKSKEGKAQV ELAQLQYQTQ RLRGWGGNLS RQAGGQAAGG EGIGGRGPGE TKLETDRRRI QMKMTKLRRE LKELGKARET KKANRKRHEI PSVSIAGYTN AGKSSLLNRL TDAGVLVEDA LFATLDPTTR RTQTSDGRVY TMSDTVGFVR NLPHQLVEAF RSTLEEIAES DLILHVVDGS HPDPGGQIAA VRSVLADVDA LDVPEIIVIN KADAADPLVI KNLLAREPHA VVVSARTGEG IDELLSAIEA DLPQPATHVD VLLPYARGDL LNQIHTQGEI ESLDHESDGT HVVARVHGQL ASELEPYAV // ID A0A0Q6W255_9BURK Unreviewed; 393 AA. AC A0A0Q6W255; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=ASD15_08205 {ECO:0000313|EMBL:KQV85093.1}; OS Massilia sp. Root351. OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Oxalobacteraceae; Massilia. OX NCBI_TaxID=1736522 {ECO:0000313|EMBL:KQV85093.1, ECO:0000313|Proteomes:UP000051876}; RN [1] {ECO:0000313|EMBL:KQV85093.1, ECO:0000313|Proteomes:UP000051876} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Root351 {ECO:0000313|EMBL:KQV85093.1, RC ECO:0000313|Proteomes:UP000051876}; RA Millard Andrew; RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:KQV85093.1, ECO:0000313|Proteomes:UP000051876} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Root351 {ECO:0000313|EMBL:KQV85093.1, RC ECO:0000313|Proteomes:UP000051876}; RA Vorholt J.; RT "Functional overlap of the Arabidopsis leaf and root microbiotas."; RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KQV85093.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LMDJ01000012; KQV85093.1; -; Genomic_DNA. DR RefSeq; WP_057155942.1; NZ_LMDJ01000012.1. DR EnsemblBacteria; KQV85093; KQV85093; ASD15_08205. DR Proteomes; UP000051876; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000051876}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000051876}. FT DOMAIN 190 357 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 156 183 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 393 AA; 43158 MW; 2D85530908625BC5 CRC64; MRAALVGVDF GQGDFAASVE ELMLLARSAG ADPVTTITGK RSSPDAAYFV GSGKADEIGF AVQDLKLEIV IFNHALSPAQ QRNLEKRLQV RVLDRTSLIL DIFAQRAQSH EGKLQVELAQ LQHLATRLIR GWTHLERQKG GIGLRGPGET QLETDRRLIG ERVKALRARL AKLRKQHETQ RRSRGRSQTF SVSLVGYTNA GKSTLFNAMT KAGVYVADQL FATLDTTSRR VYMGEEVGNV VVSDTVGFVR ELPHQLVAAF RATLEETIHA DLLLHVVDAA SPVRMEQIEQ VNLVLREIGA DHIPQILVWN KIDAAGLEPA VERDEYAKIS RVFTSARTGA GLDLLRSAIT EAAKAAPGKA YLYEAPDEEP DLHDEDQDPD SDGHSTFTQV GSH // ID A0A0Q6XY12_9MICO Unreviewed; 518 AA. AC A0A0Q6XY12; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=ASC66_16755 {ECO:0000313|EMBL:KQW04088.1}; OS Leifsonia sp. Root4. OC Bacteria; Actinobacteria; Micrococcales; Microbacteriaceae; Leifsonia. OX NCBI_TaxID=1736525 {ECO:0000313|EMBL:KQW04088.1, ECO:0000313|Proteomes:UP000051360}; RN [1] {ECO:0000313|EMBL:KQW04088.1, ECO:0000313|Proteomes:UP000051360} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Root4 {ECO:0000313|EMBL:KQW04088.1, RC ECO:0000313|Proteomes:UP000051360}; RA Millard Andrew; RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:KQW04088.1, ECO:0000313|Proteomes:UP000051360} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Root4 {ECO:0000313|EMBL:KQW04088.1, RC ECO:0000313|Proteomes:UP000051360}; RA Vorholt J.; RT "Functional overlap of the Arabidopsis leaf and root microbiotas."; RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KQW04088.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LMDN01000005; KQW04088.1; -; Genomic_DNA. DR RefSeq; WP_055842270.1; NZ_LMDN01000005.1. DR EnsemblBacteria; KQW04088; KQW04088; ASC66_16755. DR Proteomes; UP000051360; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 2. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000051360}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}. FT DOMAIN 293 458 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 518 AA; 55605 MW; D84D0819E5F66099 CRC64; MTDALNAAND TAATADGPSD DVVARVLASA ESRSSAYSLF SSGAQALQTE VGADSIGDGE QLDREDRKAL RRVPGLSTEL EDVTEVEYRQ LRLENVVLIG IYAQGSQDDA ENSMREMAAL AETAGATVLD GLLQRRAHPD PSTFLGRGKA AELAAIVQAL GADTVIADTE LAPSQRRALE DVVKVKVIDR TAVILDIFSQ HAKSREGKAQ VELAQLEYLL PRLRGWGESM SRQAGGQVGG AGAGMGSRGP GETKIELDRR RIHTRMSKLR KQIAAMKPAR EAKRANRRRN SVPSVAIAGY TNAGKSSILN RITHAGVLVE NSLFATLDAT VRKNTTADGR IYTLADTVGF VRNLPHQLVE AFRSTLEEIA DSDVIVHVVD GSHPDPASQI ATVRDVVGEV GARGITELVV FNKADLIDDD TRLVLRGLEP RAIFASARTG EGIDEILAAI SEMLPDPSLE IELIVPYDRG DLISLLHEKG RVISTEYVED GTLVHARISQ DLEAQFAEFR VPAGAIGA // ID A0A0Q6Z4F0_9BRAD Unreviewed; 461 AA. AC A0A0Q6Z4F0; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=ASC80_07165 {ECO:0000313|EMBL:KQW23084.1}; OS Afipia sp. Root123D2. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Bradyrhizobiaceae; Afipia. OX NCBI_TaxID=1736436 {ECO:0000313|EMBL:KQW23084.1, ECO:0000313|Proteomes:UP000051348}; RN [1] {ECO:0000313|EMBL:KQW23084.1, ECO:0000313|Proteomes:UP000051348} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Root123D2 {ECO:0000313|EMBL:KQW23084.1, RC ECO:0000313|Proteomes:UP000051348}; RA Millard Andrew; RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:KQW23084.1, ECO:0000313|Proteomes:UP000051348} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Root123D2 {ECO:0000313|EMBL:KQW23084.1, RC ECO:0000313|Proteomes:UP000051348}; RA Vorholt J.; RT "Functional overlap of the Arabidopsis leaf and root microbiotas."; RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KQW23084.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LMDP01000001; KQW23084.1; -; Genomic_DNA. DR RefSeq; WP_056294418.1; NZ_LMDP01000001.1. DR EnsemblBacteria; KQW23084; KQW23084; ASC80_07165. DR Proteomes; UP000051348; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000051348}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000051348}. FT DOMAIN 226 400 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 461 AA; 51237 MW; B244D7EAE17E03B1 CRC64; MEPRTFDGGA DRPGSARGET TGRVLVIGPY KRLRRGDADS QASAHTVRNP EARLEEAVGL ARAIDLTVTE AIITPLNDIR PATYLGKGKV EEIVGLIKAH HADLVVMDCA LSPIQQRNLE KEWNAKVLDR TGLILEIFGR RAKTKEGALQ VELAHLNYQR SRLVRSWTHL ERQRGGFGFL GGPGETQIEA DRRLIGERIV RIENEIKKVQ ATRRLHRAGR QRVPYRVVAL VGYTNAGKST LFNRLTRADV QAADMLFATL DPTLRALTLP HGGKAMLSDT VGFISDLPTM LVAAFRATLE EVIEADVILH VRDISHENAE AQQRDVDTIL RQLNIDPDNG HRILEVWNKI DRFDVDEREN LARIAARRPP ERPAFLVSAE TGEGIEALLA AIEGLLAATR ITLDLSIDAS DGSGISWLHR NSEVLDKHLE DGRFVMTVRV DETKRDTAIG RFGAVPRRPP D // ID A0A0Q7AQP8_9BURK Unreviewed; 420 AA. AC A0A0Q7AQP8; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 05-JUL-2017, entry version 12. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=ASC76_18855 {ECO:0000313|EMBL:KQW36702.1}; OS Rhizobacter sp. Root404. OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Rhizobacter. OX NCBI_TaxID=1736528 {ECO:0000313|EMBL:KQW36702.1, ECO:0000313|Proteomes:UP000051611}; RN [1] {ECO:0000313|EMBL:KQW36702.1, ECO:0000313|Proteomes:UP000051611} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Root404 {ECO:0000313|EMBL:KQW36702.1, RC ECO:0000313|Proteomes:UP000051611}; RA Millard Andrew; RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:KQW36702.1, ECO:0000313|Proteomes:UP000051611} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Root404 {ECO:0000313|EMBL:KQW36702.1, RC ECO:0000313|Proteomes:UP000051611}; RA Vorholt J.; RT "Functional overlap of the Arabidopsis leaf and root microbiotas."; RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KQW36702.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LMDS01000005; KQW36702.1; -; Genomic_DNA. DR EnsemblBacteria; KQW36702; KQW36702; ASC76_18855. DR Proteomes; UP000051611; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000051611}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000051611}. FT DOMAIN 207 381 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 173 200 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 420 AA; 45966 MW; 4FAE87A435694B54 CRC64; MSSTDSTAPK GLDNPARAIL VGVDFGRGKA FDDTLDELAL LAESAGDIAV ERVIARRKAP DAALFVGSGK ADEIKALVQA HQADAVLFDQ ALSPAQQRNL EKHLGVAVAD RTMLILEIFG ERAQSHEGKL QVELARLQYL STRLVRRWSH LERQSGGIGM RGGPGEAQIE LDRRMIGERI KAVKKQLERV KKQRSTQRRS RERNQTFRVS LVGYTNAGKS TLFNVLVNAK AYAADQLFAT LDTTTRQLHL DGVSRSISLS DTVGFIRELP HKLIEAFEAT LQEANDADLL LHVVDCASPV LAEQMAEVER VLAEIGAADI PQVLVFNKLD RLEDTQRPRE LRDVLELGAG RRVPRVFVSS RTGEGLPLLR QILTEAIGGT LEGFLNSREA APSDIRLSHA ADDEGEPTDP APSAPHHTLA // ID A0A0Q7BRV0_9ACTN Unreviewed; 494 AA. AC A0A0Q7BRV0; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=ASC77_09930 {ECO:0000313|EMBL:KQW49017.1}; OS Nocardioides sp. Root1257. OC Bacteria; Actinobacteria; Propionibacteriales; Nocardioidaceae; OC Nocardioides. OX NCBI_TaxID=1736439 {ECO:0000313|EMBL:KQW49017.1, ECO:0000313|Proteomes:UP000051939}; RN [1] {ECO:0000313|EMBL:KQW49017.1, ECO:0000313|Proteomes:UP000051939} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Root1257 {ECO:0000313|EMBL:KQW49017.1, RC ECO:0000313|Proteomes:UP000051939}; RA Millard Andrew; RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:KQW49017.1, ECO:0000313|Proteomes:UP000051939} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Root1257 {ECO:0000313|EMBL:KQW49017.1, RC ECO:0000313|Proteomes:UP000051939}; RA Vorholt J.; RT "Functional overlap of the Arabidopsis leaf and root microbiotas."; RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KQW49017.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LMDV01000008; KQW49017.1; -; Genomic_DNA. DR RefSeq; WP_056152717.1; NZ_LMDV01000008.1. DR EnsemblBacteria; KQW49017; KQW49017; ASC77_09930. DR Proteomes; UP000051939; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 2. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000313|EMBL:KQW49017.1}; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000051939}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900, KW ECO:0000313|EMBL:KQW49017.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000051939}. FT DOMAIN 276 441 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 242 269 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 494 AA; 53874 MW; C08B6FC72DA155B9 CRC64; MTNAHEIDPA FNLDTELEDT DDWDDDDFES GYSGADPEED PTTGAMELAE RHQLRRVAGL RTELEDITEV EYRQLRLERV VLVGVWTEGT TEDAENSMAE LALLAETAGS EVLEAIYQRR QSPDPATYVG RGKVEGIAEI VQATGADTVI CDGELAPSQL RNLEDKLKVK VVDRTALILD IFAQHAKSGE AQAQTELAQL NYMKQRLRGW GGNLSRQAGG RVAGGAGIGS RGPGETKIEN DRRRINTKIA KLRRDLREMK GTRDTKRQER QRNHIPSVTI AGYTNAGKST LLNRLTGAGV LVEDALFATL DPTTRRTTTA DGRVYTMSDT VGFVRHLPHQ LVEAFRSTLE EVAESDLVLH VVDGSHPDPE GQIAAVREVF AEIGATKVPE LIVINKGDLA DPMVLARLQR NEPHSVVVSA KTGEGIADAL AQIEGELPRP GVEFKALLPY ERGDLINRLH QQGEIASMEH TGDGTIVVGR ANADLAGELA AYAV // ID A0A0Q7DG31_9CAUL Unreviewed; 438 AA. AC A0A0Q7DG31; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=ASC73_05705 {ECO:0000313|EMBL:KQW71597.1}; OS Phenylobacterium sp. Root1277. OC Bacteria; Proteobacteria; Alphaproteobacteria; Caulobacterales; OC Caulobacteraceae; Phenylobacterium. OX NCBI_TaxID=1736442 {ECO:0000313|EMBL:KQW71597.1, ECO:0000313|Proteomes:UP000051150}; RN [1] {ECO:0000313|EMBL:KQW71597.1, ECO:0000313|Proteomes:UP000051150} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Root1277 {ECO:0000313|EMBL:KQW71597.1, RC ECO:0000313|Proteomes:UP000051150}; RA Millard Andrew; RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:KQW71597.1, ECO:0000313|Proteomes:UP000051150} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Root1277 {ECO:0000313|EMBL:KQW71597.1, RC ECO:0000313|Proteomes:UP000051150}; RA Vorholt J.; RT "Functional overlap of the Arabidopsis leaf and root microbiotas."; RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KQW71597.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LMDZ01000004; KQW71597.1; -; Genomic_DNA. DR RefSeq; WP_056018840.1; NZ_LMDZ01000004.1. DR EnsemblBacteria; KQW71597; KQW71597; ASC73_05705. DR Proteomes; UP000051150; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000051150}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000051150}. FT DOMAIN 207 378 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 438 AA; 48506 MW; C2121C5E2C6A9D0C CRC64; MTSKSIEREA PPQGALVIHP QRDGRDSARS SQARLDEAVG LALALDLEIR DAIIAPLRKR TPATLFGSGK VDEIGELCFQ LKVDVAVVDD ALTPVQQRNL EKAWQVKVMD RTGMILEIFA RRARTREGIL QVELARLSYE RSRLVRTWTH LERQRGGFGV MGGPGETQIE TDRRLLAEKI GKLKRELVEV RRTRNLQRGA RQRHPFPAVA LVGYTNAGKS TLFNRLTKAD VMAADMLFAT LDPTLRMLDL PDGRPAILSD TVGFISDLPH ELVESFRATL EEVKEADVIL HVRDIASEET EAEAEDVRTV LNRLGIDVAE RNVIEVWNKA DLLEPEVRED VAGDARRHHP PAVMVSAASG EGCEALLAAI ARLVDDAPPV SVRLTAADGA AVAWLYRHGR VMDRFDEEDG GVRIAVRLNA QALGQFEQQF PKADLTAL // ID A0A0Q7EAJ5_9RHIZ Unreviewed; 460 AA. AC A0A0Q7EAJ5; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 05-JUL-2017, entry version 12. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=ASC89_07090 {ECO:0000313|EMBL:KQW81569.1}; OS Devosia sp. Root413D1. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Hyphomicrobiaceae; Devosia. OX NCBI_TaxID=1736531 {ECO:0000313|EMBL:KQW81569.1, ECO:0000313|Proteomes:UP000051002}; RN [1] {ECO:0000313|EMBL:KQW81569.1, ECO:0000313|Proteomes:UP000051002} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Root413D1 {ECO:0000313|EMBL:KQW81569.1, RC ECO:0000313|Proteomes:UP000051002}; RA Millard Andrew; RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:KQW81569.1, ECO:0000313|Proteomes:UP000051002} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Root413D1 {ECO:0000313|EMBL:KQW81569.1, RC ECO:0000313|Proteomes:UP000051002}; RA Vorholt J.; RT "Functional overlap of the Arabidopsis leaf and root microbiotas."; RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KQW81569.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LMEA01000007; KQW81569.1; -; Genomic_DNA. DR EnsemblBacteria; KQW81569; KQW81569; ASC89_07090. DR Proteomes; UP000051002; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000051002}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000051002}. FT DOMAIN 222 397 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 181 215 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 460 AA; 50351 MW; 6966F373B6739E6F CRC64; MSDDFDDEAA RKGGPQAFID QRSAPTRVGL VIPDVRGRAT THSIEARKAE FEGLASAIRV EIVFSEIAKV REIKPATFIG GGHVEEIAKR VKEEEIELLL VDTALHPIQQ RNLEKETGAK VLDRTGLILE IFGERAATRE GVLQVELAHL NYQKSRLVRS WTHLERQRGS GGFGFMGGPG ETQLESDRRQ LQDRIKMLEE RIEKVRQTRG QQKGRRDAVP FQVVALVGYT NAGKSSIFNA LTGAGVFAKD LLFATLDTTV RKIGLPHGRE VMLSDTVGFV SDLPTDLIAA FRATLEEVLE AHVILHVRDV ANPDHAAQAQ DVLKVLEELG MSAETTPIIE VWNKVDLLGR DADGSYPALA TLSPLGKVAA SVPVSAQTGE GLDRLLDTIE KVLAGQGRTY RVLVPHTAGA DVGWLYGHAE IIGKDEPDEN GQVYEVRVEA RHKNAFTERF AGRIEGSDAA // ID A0A0Q7EHP4_9CAUL Unreviewed; 433 AA. AC A0A0Q7EHP4; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=ASC65_03805 {ECO:0000313|EMBL:KQW83777.1}; OS Brevundimonas sp. Root1279. OC Bacteria; Proteobacteria; Alphaproteobacteria; Caulobacterales; OC Caulobacteraceae; Brevundimonas. OX NCBI_TaxID=1736443 {ECO:0000313|EMBL:KQW83777.1, ECO:0000313|Proteomes:UP000050923}; RN [1] {ECO:0000313|EMBL:KQW83777.1, ECO:0000313|Proteomes:UP000050923} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Root1279 {ECO:0000313|EMBL:KQW83777.1, RC ECO:0000313|Proteomes:UP000050923}; RA Millard Andrew; RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:KQW83777.1, ECO:0000313|Proteomes:UP000050923} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Root1279 {ECO:0000313|EMBL:KQW83777.1, RC ECO:0000313|Proteomes:UP000050923}; RA Vorholt J.; RT "Functional overlap of the Arabidopsis leaf and root microbiotas."; RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KQW83777.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LMEB01000004; KQW83777.1; -; Genomic_DNA. DR RefSeq; WP_056449708.1; NZ_LMEB01000004.1. DR EnsemblBacteria; KQW83777; KQW83777; ASC65_03805. DR Proteomes; UP000050923; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000050923}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000050923}. FT DOMAIN 206 380 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 433 AA; 47973 MW; 3490AC1B8609E51B CRC64; MGTQLIDHAV PLIRAVVIHP DGRSESSRLA TERLEEAVGL ARALDLDIRA EEIVRVRKPV PATLFGSGKV DELAALVRAA EAEAVVVDDD LTPVQQRNLE KAWECKVIDR TGLILEIFGR RARTKEGRLQ VELARLDYER SRLVRTWTHL ERQRGGTGST GGPGETQIEL DRRLIADRIV KLKGELEEVR RTRGLHRKAR KKVPFPTVAL VGYTNAGKST LFNRLTGSEV LAKDLLFATL DTTQRTIRLP QGRPAIVADT VGFISDLPHE LVESFRATLE EVGEADLILH VRDIASPDSE AQAKDVEAVL KQIPTVEGKV RRVLEVWNKT DLLDDDAREA VLGQAERLRA QGQAVAVSAW TGEGIEPLRE TIAALIDDDP ETEVVLQPHQ GDALAWLYAN GRVTGRETDD EGRTHVVVRL HPAALGRFER QFG // ID A0A0Q7ITX8_9RHIZ Unreviewed; 451 AA. AC A0A0Q7ITX8; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=ASD04_01500 {ECO:0000313|EMBL:KQX42672.1}; OS Devosia sp. Root436. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Hyphomicrobiaceae; Devosia. OX NCBI_TaxID=1736537 {ECO:0000313|EMBL:KQX42672.1, ECO:0000313|Proteomes:UP000051058}; RN [1] {ECO:0000313|EMBL:KQX42672.1, ECO:0000313|Proteomes:UP000051058} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Root436 {ECO:0000313|EMBL:KQX42672.1, RC ECO:0000313|Proteomes:UP000051058}; RA Millard Andrew; RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:KQX42672.1, ECO:0000313|Proteomes:UP000051058} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Root436 {ECO:0000313|EMBL:KQX42672.1, RC ECO:0000313|Proteomes:UP000051058}; RA Vorholt J.; RT "Functional overlap of the Arabidopsis leaf and root microbiotas."; RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KQX42672.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LMEM01000001; KQX42672.1; -; Genomic_DNA. DR RefSeq; WP_056251503.1; NZ_LMEM01000001.1. DR EnsemblBacteria; KQX42672; KQX42672; ASD04_01500. DR Proteomes; UP000051058; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000051058}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000051058}. FT DOMAIN 220 389 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 188 215 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 451 AA; 49044 MW; 90A7F8F52B164F68 CRC64; MTEFDDDAAA QRGGPQAFID QRAQPTRAGL VVPDVRNQLS RHSIEARKAE FEGLAGAIRL DIVFSEVFKV REIKPATFIG GGHTEALAAR VKADKIDLLL VDAALTAIQQ RNLETETGAK VLDRTALILE IFGERAATRE GVLQVELAHL NYQKGRLVRS WTHLERQRGS GGTGFMGGPG ETQIESDRRQ IMDRIVLLED RLEKVKKTRA QQRQQRDGTP IVALVGYTNA GKSSLFNALT GAGVFAKDLL FATLDTTVRK LALPHGRDIM LSDTVGFVAD LPTDLVAAFR ATLEEVLDAD VILHARDIAN PDHMAQAHDV LKVLADLGVS AETTPIIEVW NKIDLVSEDA VVGIVPVGKV AAVVQASAMT GQGLDTIKLA VEKALGEKSR TYHVHVPHTA GADIGWLHAH SEIVSRDEPT EQGSGFVVRV EPRHKTAFLE RFNGRIESSD A // ID A0A0Q7K0Q3_9ACTN Unreviewed; 490 AA. AC A0A0Q7K0Q3; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 05-JUL-2017, entry version 12. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=ASD06_10910 {ECO:0000313|EMBL:KQX63635.1}; OS Angustibacter sp. Root456. OC Bacteria; Actinobacteria; Kineosporiales; Kineosporiaceae. OX NCBI_TaxID=1736539 {ECO:0000313|EMBL:KQX63635.1, ECO:0000313|Proteomes:UP000051170}; RN [1] {ECO:0000313|EMBL:KQX63635.1, ECO:0000313|Proteomes:UP000051170} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Root456 {ECO:0000313|EMBL:KQX63635.1, RC ECO:0000313|Proteomes:UP000051170}; RA Millard Andrew; RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:KQX63635.1, ECO:0000313|Proteomes:UP000051170} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Root456 {ECO:0000313|EMBL:KQX63635.1, RC ECO:0000313|Proteomes:UP000051170}; RA Vorholt J.; RT "Functional overlap of the Arabidopsis leaf and root microbiotas."; RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KQX63635.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LMER01000018; KQX63635.1; -; Genomic_DNA. DR EnsemblBacteria; KQX63635; KQX63635; ASD06_10910. DR Proteomes; UP000051170; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 2. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000051170}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000051170}. FT DOMAIN 272 437 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 490 AA; 53458 MW; CDF71BC1EF773058 CRC64; MNRTANAARL QQAELEPLDD LDAPHDDGGY DGDHDGGYDG DQLDLQDRQA LRRVAGLSTE LADVTEVEYR QLRLERVVLA GVFTGDVEDG ENSMRELAAL AETAGSQVLD ALMQRREQPD PGTFLGSGKA RELRDIVVAS GADTVICDGE LSPSQRRALE DVVKVKVIDR TALILDIFAQ HAKSREGKAQ VELAQLEYLL PRLRGWGESM SRQAGGRVAG GEGIGSRGPG ETKIELDRRR IRTRVAKLRR QIAGMKTARD VGRHDRKRHA VPSVAIAGYT NAGKSSLLNR LTGAGVLVEN ALFATLDPTV RRAETTDGRE YTLADTVGFV RHLPHQLVEA FRSTLEEVAD SDLVLHVVDA SHPDPEGQIQ AVREVLADVD AHNVPELIVL NKADAADPEV IARLRSRERS LVVVSARTGQ GLEELRTRID DLLPRPDVEV EVLVPYDRGD LVSRIHADGE VLAERHLAEG THLRAKVMPA LAGELTAFTA // ID A0A0Q7KIY6_9ACTN Unreviewed; 470 AA. AC A0A0Q7KIY6; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=ASD10_10155 {ECO:0000313|EMBL:KQX75504.1}; OS Aeromicrobium sp. Root472D3. OC Bacteria; Actinobacteria; Propionibacteriales; Nocardioidaceae; OC Aeromicrobium. OX NCBI_TaxID=1736540 {ECO:0000313|EMBL:KQX75504.1, ECO:0000313|Proteomes:UP000050971}; RN [1] {ECO:0000313|EMBL:KQX75504.1, ECO:0000313|Proteomes:UP000050971} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Root472D3 {ECO:0000313|EMBL:KQX75504.1, RC ECO:0000313|Proteomes:UP000050971}; RA Millard Andrew; RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:KQX75504.1, ECO:0000313|Proteomes:UP000050971} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Root472D3 {ECO:0000313|EMBL:KQX75504.1, RC ECO:0000313|Proteomes:UP000050971}; RA Vorholt J.; RT "Functional overlap of the Arabidopsis leaf and root microbiotas."; RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KQX75504.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LMET01000001; KQX75504.1; -; Genomic_DNA. DR RefSeq; WP_056607884.1; NZ_LMET01000001.1. DR EnsemblBacteria; KQX75504; KQX75504; ASD10_10155. DR Proteomes; UP000050971; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 2. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000313|EMBL:KQX75504.1}; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000050971}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900, KW ECO:0000313|EMBL:KQX75504.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000050971}. FT DOMAIN 250 415 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 209 243 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 470 AA; 51026 MW; 2F57F40CBED12B3A CRC64; MTEPTTGPTT TSQPQGTEGL DLEERHSLRR VVNLRTELED ITEVEYRQLR LERVVLVGVW TEGTVEDAEN SMAELKLLAE TAGSEVLDAL IQRRQKPDPS TYIGSGKVED LRATVEATGA DTIICDGALA PSQLRNLEDK CKVKVVDRTA LILDIFAQHA KSKEGKAQVE LAQLQYQTQR LRGWGGNLSR QAGGQAAGGE GIGGRGPGET KLETDRRRIQ MKMTKLRREL KELGKARETK KGNRQRHEIP SVSIAGYTNA GKSSLLNRLT DAGVLVENAL FATLDPTTRR TQTSDGRVYT LSDTVGLVRN LPHQLVEAFR STLEEIAESD LILHVVDGSD PDPEGQIAAV RQVILEAGAA EVPEIIVINK ADAADPLVVK QLLVREPHAV VVSARTGEGV DELLSAIEAD LPQPASHVDV LLPYARGDLL NQIHVQGEIE SLDHEADGTH VVARVNGALA NELEPFAVEA // ID A0A0Q7P1F5_9RHIZ Unreviewed; 441 AA. AC A0A0Q7P1F5; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 05-JUL-2017, entry version 13. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=ASD32_16950 {ECO:0000313|EMBL:KQY40087.1}; OS Rhizobium sp. Root483D2. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium. OX NCBI_TaxID=1736545 {ECO:0000313|EMBL:KQY40087.1, ECO:0000313|Proteomes:UP000051333}; RN [1] {ECO:0000313|EMBL:KQY40087.1, ECO:0000313|Proteomes:UP000051333} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Root483D2 {ECO:0000313|EMBL:KQY40087.1, RC ECO:0000313|Proteomes:UP000051333}; RA Millard Andrew; RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:KQY40087.1, ECO:0000313|Proteomes:UP000051333} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Root483D2 {ECO:0000313|EMBL:KQY40087.1, RC ECO:0000313|Proteomes:UP000051333}; RA Vorholt J.; RT "Functional overlap of the Arabidopsis leaf and root microbiotas."; RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KQY40087.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LMFB01000013; KQY40087.1; -; Genomic_DNA. DR EnsemblBacteria; KQY40087; KQY40087; ASD32_16950. DR Proteomes; UP000051333; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000051333}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}. FT DOMAIN 205 377 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 164 198 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 441 AA; 48923 MW; AF4BB40E87E497E5 CRC64; MRAVVIVPVL KKTGRQNAEI IAATSTRSDE SRLEETIGLA LAIDLEVVHG AIVPIAQPKP GTLLGSGKIE EIGHLLSEHN AGLVIIDHPL TPVQQRNLEK EWNCKVIDRT GLILEIFGRR ASTKEGTLQV ELAHLNYQKG RLVRSWTHLE RQRGGAGFMG GPGETQIEAD RRLLQEKIVK LEKELEQVRR TRQLHRAKRK KVPHPIVALV GYTNAGKSTL FNRITGAGVL AEDMLFATLD PTLRRMKLPH GRMVMLSDTV GFISDLPTHL VAAFRATLEE VLEADLILHV RDLADPDNQV QSQDVLRILT DLGIDEKARS ERIIEVWNKV DLLDADAHES LVQKAEHSEN TVAVSAVTGE GVDHLLDEIN KRLSGVLMEC NVVLPASKLQ LLSWVYEHTL VDGREDLEDG SVSLDLRMTP SEAEELERRL GNGPKAAAQD W // ID A0A0Q7PL25_9GAMM Unreviewed; 448 AA. AC A0A0Q7PL25; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=ASD14_03785 {ECO:0000313|EMBL:KQY51811.1}; OS Lysobacter sp. Root494. OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales; OC Xanthomonadaceae; Lysobacter. OX NCBI_TaxID=1736549 {ECO:0000313|EMBL:KQY51811.1, ECO:0000313|Proteomes:UP000051738}; RN [1] {ECO:0000313|EMBL:KQY51811.1, ECO:0000313|Proteomes:UP000051738} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Root494 {ECO:0000313|EMBL:KQY51811.1, RC ECO:0000313|Proteomes:UP000051738}; RA Millard Andrew; RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:KQY51811.1, ECO:0000313|Proteomes:UP000051738} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Root494 {ECO:0000313|EMBL:KQY51811.1, RC ECO:0000313|Proteomes:UP000051738}; RA Vorholt J.; RT "Functional overlap of the Arabidopsis leaf and root microbiotas."; RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KQY51811.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LMFH01000005; KQY51811.1; -; Genomic_DNA. DR RefSeq; WP_056129263.1; NZ_LMFH01000005.1. DR EnsemblBacteria; KQY51811; KQY51811; ASD14_03785. DR Proteomes; UP000051738; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000051738}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000051738}. FT DOMAIN 199 374 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 158 192 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 448 AA; 49010 MW; 82AD1E957A64853B CRC64; MFERSRKGEH ALLIQPHAGG PPDEGLMEEF ADLARSAGAT VAALLTARID RPNPATLVGS GKLEEMKAAA DASGADLILV NFALSPGQER NLEKALQRRV VDRTGLILDI FSQRAQSAEG KLQVELAQLK HMATRLVRGW THLERQRGGA IGLRGPGETQ LETDRRLLQK RLEQLQKRLD KVEVQRTQMR RARMRSELPR IALVGYTNAG KSTLFNALTG AAAYAADQLF ATLDPTVRRI ALPGGGAVLA DTVGFVRDLP HELVAAFRST LSEAREADLL LHVVDAADPL REERIRQVDD VLADIGAGDL PQLLVFNKID RLEREGDSGE GWSAPEPRHD HPAEGRQRVW VSAQLGLGLD LLRKALAEVL ELRHVAGEVR LPSQAARLHA RLHAIGAIRG EKHDEQGWLL QVDMAIADAQ KLYVQAHGEA LRPLLEAAGA LEDETAGW // ID A0A0Q7QAX3_9ACTN Unreviewed; 466 AA. AC A0A0Q7QAX3; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 05-JUL-2017, entry version 12. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=ASD11_07995 {ECO:0000313|EMBL:KQY60707.1}; OS Aeromicrobium sp. Root495. OC Bacteria; Actinobacteria; Propionibacteriales; Nocardioidaceae; OC Aeromicrobium. OX NCBI_TaxID=1736550 {ECO:0000313|EMBL:KQY60707.1, ECO:0000313|Proteomes:UP000051970}; RN [1] {ECO:0000313|EMBL:KQY60707.1, ECO:0000313|Proteomes:UP000051970} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Root495 {ECO:0000313|EMBL:KQY60707.1, RC ECO:0000313|Proteomes:UP000051970}; RA Millard Andrew; RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:KQY60707.1, ECO:0000313|Proteomes:UP000051970} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Root495 {ECO:0000313|EMBL:KQY60707.1, RC ECO:0000313|Proteomes:UP000051970}; RA Vorholt J.; RT "Functional overlap of the Arabidopsis leaf and root microbiotas."; RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KQY60707.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LMFJ01000001; KQY60707.1; -; Genomic_DNA. DR EnsemblBacteria; KQY60707; KQY60707; ASD11_07995. DR Proteomes; UP000051970; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 2. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000313|EMBL:KQY60707.1}; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000051970}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900, KW ECO:0000313|EMBL:KQY60707.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000051970}. FT DOMAIN 250 415 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 209 243 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 466 AA; 50856 MW; 2D3761FCEE04E91F CRC64; MTEQTERPST EPARREEVGL DLEERNSLRR VASLRTELED ITEVEYRQLR LERVVLVGVW TEGSAEDAEN SLTELKALAE TAGSEVLDAL LQRRQKPDAA TYIGSGKVEE LREAVEASGA DTIICDGELA PSQMRNLEDR VKVKCVDRTA LILDIFAQHA KSAEGKAQVE LAQLQYQTQR LRGWGGNLSR QAGGRAAGGE GIGGRGPGET KLETDRRRIQ NKMAKLRREL KGLRTTRDIK RAQRRRNAVP GVAIAGYTNA GKSSLLNQLT DAGVLVEDAL FATLDPTTRR TQTSDGRVYT LSDTVGFVRH LPHQIVEAFR STLEEVADAD LVLHVVDGSH PDPQGQIAAV REVFAEVGAT QVPEIVVINK ADAADPLVIK QLLAAEPHAV VVSARTGQGI DELLLAIEAD LPRPAVRVEV VVPYERGDLL NQVHETGEIE SIEHEGDGTH VVARVSDDLA HQLQGL // ID A0A0Q7QMG6_9CAUL Unreviewed; 437 AA. AC A0A0Q7QMG6; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=ASD25_15135 {ECO:0000313|EMBL:KQY65026.1}; OS Brevundimonas sp. Root1423. OC Bacteria; Proteobacteria; Alphaproteobacteria; Caulobacterales; OC Caulobacteraceae; Brevundimonas. OX NCBI_TaxID=1736462 {ECO:0000313|EMBL:KQY65026.1, ECO:0000313|Proteomes:UP000051815}; RN [1] {ECO:0000313|EMBL:KQY65026.1, ECO:0000313|Proteomes:UP000051815} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Root1423 {ECO:0000313|EMBL:KQY65026.1, RC ECO:0000313|Proteomes:UP000051815}; RA Millard Andrew; RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:KQY65026.1, ECO:0000313|Proteomes:UP000051815} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Root1423 {ECO:0000313|EMBL:KQY65026.1, RC ECO:0000313|Proteomes:UP000051815}; RA Vorholt J.; RT "Functional overlap of the Arabidopsis leaf and root microbiotas."; RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KQY65026.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LMFL01000078; KQY65026.1; -; Genomic_DNA. DR RefSeq; WP_055830673.1; NZ_LMFL01000078.1. DR EnsemblBacteria; KQY65026; KQY65026; ASD25_15135. DR Proteomes; UP000051815; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000051815}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000051815}. FT DOMAIN 210 384 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 437 AA; 48477 MW; 5353C2D60A5AC0F4 CRC64; MTTKHIDHAV PLIRAVVIHP ERSDSGAGDS SRQSVERLEE AVGLARALDL DVRGEEIVRI RKVTPATLFG SGKVEELAAL VRAAEAEAVV VDDDLSPVQQ RNLEKAWDCK VIDRTGLILE IFGRRARTKE GRLQVELARL DYEKSRLVRT WTHLERQRGG TGSTGGPGET QIELDRRLIA DRIVKLKVEL DEVRRTRGLH RKQRQKVPFP TIALVGYTNA GKSTLFNRLT GSEVFAKDLL FATLDTTQRT IRLPQGRPAI VADTVGFISD LPHELVESFR ATLEEVGEAD LILHVRDIAS ADSEAQAKDV EAVLKQIETP EGKTRRVLEV WNKIDLLADD VREAVLGQAE RLSREGKAVA VSAWTGEGIE PLRQAIAGLI DDDPETELVL DPSQGEALAW LYENGRVTGR ETDDQGRTHV VVRLHPAALG RFERQFG // ID A0A0Q7RIW8_9CAUL Unreviewed; 427 AA. AC A0A0Q7RIW8; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=ASD25_11450 {ECO:0000313|EMBL:KQY75558.1}; OS Brevundimonas sp. Root1423. OC Bacteria; Proteobacteria; Alphaproteobacteria; Caulobacterales; OC Caulobacteraceae; Brevundimonas. OX NCBI_TaxID=1736462 {ECO:0000313|EMBL:KQY75558.1, ECO:0000313|Proteomes:UP000051815}; RN [1] {ECO:0000313|EMBL:KQY75558.1, ECO:0000313|Proteomes:UP000051815} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Root1423 {ECO:0000313|EMBL:KQY75558.1, RC ECO:0000313|Proteomes:UP000051815}; RA Millard Andrew; RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:KQY75558.1, ECO:0000313|Proteomes:UP000051815} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Root1423 {ECO:0000313|EMBL:KQY75558.1, RC ECO:0000313|Proteomes:UP000051815}; RA Vorholt J.; RT "Functional overlap of the Arabidopsis leaf and root microbiotas."; RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KQY75558.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LMFL01000045; KQY75558.1; -; Genomic_DNA. DR RefSeq; WP_056621371.1; NZ_LMFL01000045.1. DR EnsemblBacteria; KQY75558; KQY75558; ASD25_11450. DR Proteomes; UP000051815; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000051815}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000051815}. FT DOMAIN 197 371 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 427 AA; 47464 MW; A2F8472496B0E960 CRC64; MTTKHIDHAV PLIRAVVIHP DGRSESSRLA EERLEEAVGL ARALDLDVRA EEIVRIRKPT PATLFGTGKV EELAALVRAA EAEAVVVDDD LSPVQQRNLE KAWDCKVIDR TGLILEIFGR RARTKEGRLQ VELARLDYEK SRLVRTWTHL ERQRGGTGST GGPGETQIEL DRLKVELDEV RRTRGLHRKQ RQKVPFPTIA LVGYTNAGKS TLFNRLTGSE VFAKDLLFAT LDTTQRTIRL PQGRPAIVAD TVGFISDLPH ELVESFRATL EEVGEADLIL HVRDIASPDS DAQSKDVEAV LKQIPTPEGK TRRVLEVWNK TDLLAEDVRD AVLGQAERLR AQGKAVAVSA WTGEGIEPLR DTIASLIDDD PETELVLLPS QGEALAWLYE NGRVTGRETD DEGRTHVVVR LHPAALGRFE RQFQTAT // ID A0A0Q7SKR1_9BURK Unreviewed; 394 AA. AC A0A0Q7SKR1; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 05-JUL-2017, entry version 12. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=ASD35_14070 {ECO:0000313|EMBL:KQY88671.1}; OS Pelomonas sp. Root1444. OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Comamonadaceae; Pelomonas. OX NCBI_TaxID=1736464 {ECO:0000313|EMBL:KQY88671.1, ECO:0000313|Proteomes:UP000051648}; RN [1] {ECO:0000313|EMBL:KQY88671.1, ECO:0000313|Proteomes:UP000051648} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Root1444 {ECO:0000313|EMBL:KQY88671.1, RC ECO:0000313|Proteomes:UP000051648}; RA Millard Andrew; RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:KQY88671.1, ECO:0000313|Proteomes:UP000051648} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Root1444 {ECO:0000313|EMBL:KQY88671.1, RC ECO:0000313|Proteomes:UP000051648}; RA Vorholt J.; RT "Functional overlap of the Arabidopsis leaf and root microbiotas."; RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KQY88671.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LMFP01000003; KQY88671.1; -; Genomic_DNA. DR EnsemblBacteria; KQY88671; KQY88671; ASD35_14070. DR Proteomes; UP000051648; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000051648}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000051648}. FT DOMAIN 190 366 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 156 183 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 394 AA; 42909 MW; EAE80F4EF0C5B516 CRC64; MGVDFGRQSA KQGFDESLDE LALLAESAGD TPVAKVIARR AAPDAALFVG SGKADEIKLL VQAHQAHTVL FDQAISPAQQ RNLERVLGVP VADRTALILE IFAARAQSHE GKLQVELARL QYLATRLVRR WSHLERQSGG IGMRGGPGEA QIELDRRMID DRIKKTKERL KQVQKQRSTQ RRSRSRNGVF KVSLVGYTNA GKSTLFNALT KARAYAANQL FATLDTTTRS LYLEQAGASV SLSDTVGFIR DLPHKLVEAF RATLQEAADA DLLLHVVDAA SPVLEEQMIE VERVLAEIGA ADVPQILVYN KQDLLADDQR PREIVDAVLR NAGGTGPTPR VFVSAIDGGG LAELRQLIAT AMQTQPLIPD ERDPRFDAGP PDSEPSSSED PSQA // ID A0A0Q7T9D0_9MICO Unreviewed; 511 AA. AC A0A0Q7T9D0; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=ASD19_09200 {ECO:0000313|EMBL:KQY97091.1}; OS Microbacterium sp. Root53. OC Bacteria; Actinobacteria; Micrococcales; Microbacteriaceae; OC Microbacterium. OX NCBI_TaxID=1736553 {ECO:0000313|EMBL:KQY97091.1, ECO:0000313|Proteomes:UP000051407}; RN [1] {ECO:0000313|EMBL:KQY97091.1, ECO:0000313|Proteomes:UP000051407} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Root53 {ECO:0000313|EMBL:KQY97091.1, RC ECO:0000313|Proteomes:UP000051407}; RA Millard Andrew; RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:KQY97091.1, ECO:0000313|Proteomes:UP000051407} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Root53 {ECO:0000313|EMBL:KQY97091.1, RC ECO:0000313|Proteomes:UP000051407}; RA Vorholt J.; RT "Functional overlap of the Arabidopsis leaf and root microbiotas."; RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KQY97091.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LMFR01000024; KQY97091.1; -; Genomic_DNA. DR RefSeq; WP_055993317.1; NZ_LMFR01000024.1. DR EnsemblBacteria; KQY97091; KQY97091; ASD19_09200. DR Proteomes; UP000051407; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 2. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000051407}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000051407}. FT DOMAIN 292 457 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 511 AA; 55333 MW; 6BBE661230DC09DF CRC64; MTDTTTPDPD TDGVVGQAEP DLVDRVLSRA EARTGARVFG AAQALQDATT TGEGTADGEQ WDREERAALR RVGGLSTELE DVTEVEYRQL RLENVVLVGV YSQGSLTDAE NSLRELAALA ETAGAVVLDG VLQRRPHPDP ATYIGRGKAD ELKDIVAAVG ADTVIADTEL APSQRRALED VVKVKVIDRT TVILDIFSQH AKSREGKAQV ELAQLEYLLP RLRGWGDSMS RQAGGQVGAG GAGMGSRGPG ETKIELDRRR IRTRMAQLRR QIRDFAPARE AKRGERKRNT IPSVAIAGYT NAGKSSLLNR LTSAGVLVEN ALFATLDATV RRSETSDGRV YTIADTVGFV RNLPHQLVEA FRSTLEEVAD ADVILHVVDA HHPDPAGQLQ TVRDVMGDVG ARDIHEIVVF NKADLVDDDT RLVLRGLEPN AVFVSSRSGE GIDELRAAIE AALPMPEVEI RALVPYDRGE LISAIHEQGH LLERSHEEGG TLVHAHVSER LAAALEPFRV A // ID A0A0Q7TVP8_9RHIZ Unreviewed; 450 AA. AC A0A0Q7TVP8; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 05-JUL-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=ASD45_09375 {ECO:0000313|EMBL:KQZ01049.1}; OS Pseudolabrys sp. Root1462. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Xanthobacteraceae; Pseudolabrys. OX NCBI_TaxID=1736466 {ECO:0000313|EMBL:KQZ01049.1, ECO:0000313|Proteomes:UP000051186}; RN [1] {ECO:0000313|EMBL:KQZ01049.1, ECO:0000313|Proteomes:UP000051186} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Root1462 {ECO:0000313|EMBL:KQZ01049.1, RC ECO:0000313|Proteomes:UP000051186}; RA Millard Andrew; RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:KQZ01049.1, ECO:0000313|Proteomes:UP000051186} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Root1462 {ECO:0000313|EMBL:KQZ01049.1, RC ECO:0000313|Proteomes:UP000051186}; RA Vorholt J.; RT "Functional overlap of the Arabidopsis leaf and root microbiotas."; RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KQZ01049.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LMFS01000001; KQZ01049.1; -; Genomic_DNA. DR EnsemblBacteria; KQZ01049; KQZ01049; ASD45_09375. DR Proteomes; UP000051186; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000051186}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000051186}. FT DOMAIN 223 396 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 189 216 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 450 AA; 49059 MW; 1F64875169DA8CBF CRC64; MEARERDKGT DTLTPSGSGS GRAIVIEPWV RMPGGRGAAH LADTRTPEAR LEEAMGLARA IDLDVVEGAL VPLQAIKPAT YVGSGKVDEM AGLVKSHEAS VVIMDCPISP VQQKNLEKAW NAKVIDRTGL ILEIFGRRAR TKEGALQVEH AHLTYQKGRL VRSWTHLERQ RGGGAFLGGP GETQIESDRR MLSDKIMRIE AELEKVKRTR KLHRDSRKRV PYPIVALVGY TNAGKSTLFN RVTAASVLSA DMLFATLDPT LRAIDLPRGT RIILSDTVGF ISDLPTMLVA AFRATLEEVI EADIILHVRD MSHEDTGAQS ADVAKVLGEL GIEATDRRII EVWNKIDALD ADGRDRILNL AGRQPSDRAP VVVSALTGEG IDGLLTAIET RLGESHQTLT VSLDASDGAG LSWLYRHAEV LDNRTDDNGQ MEVTVRATPD KAAQVRAKFL // ID A0A0Q7UIS6_9MICO Unreviewed; 509 AA. AC A0A0Q7UIS6; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=ASD23_15810 {ECO:0000313|EMBL:KQZ07352.1}; OS Agromyces sp. Root1464. OC Bacteria; Actinobacteria; Micrococcales; Microbacteriaceae; Agromyces. OX NCBI_TaxID=1736467 {ECO:0000313|EMBL:KQZ07352.1, ECO:0000313|Proteomes:UP000051559}; RN [1] {ECO:0000313|EMBL:KQZ07352.1, ECO:0000313|Proteomes:UP000051559} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Root1464 {ECO:0000313|EMBL:KQZ07352.1, RC ECO:0000313|Proteomes:UP000051559}; RA Millard Andrew; RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:KQZ07352.1, ECO:0000313|Proteomes:UP000051559} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Root1464 {ECO:0000313|EMBL:KQZ07352.1, RC ECO:0000313|Proteomes:UP000051559}; RA Vorholt J.; RT "Functional overlap of the Arabidopsis leaf and root microbiotas."; RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KQZ07352.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LMFU01000003; KQZ07352.1; -; Genomic_DNA. DR RefSeq; WP_056013548.1; NZ_LMFU01000003.1. DR EnsemblBacteria; KQZ07352; KQZ07352; ASD23_15810. DR Proteomes; UP000051559; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000051559}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000051559}. FT DOMAIN 286 451 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 509 AA; 54864 MW; 4DE37425768ECA31 CRC64; MNDAEQNSAD DAVERVLKGA ETKAGVTRFG SDSAEALMSP DSVDLFGSDT DGEQYDREAR AGLRRVGGLS TELEDVTEVE YRQLRLENVV LIGVYSQGSQ DEAENSMREL AALAETAGAR VLDGVLQRRP HPDPSTYLGR GKVDELRHIV ASLGADTVVA DTELAPSQRR ALEDAIKVKV IDRTAVILDI FSQHAKSREG KAQVELAQLE YLLPRLRGWG ESMSRQAGGQ VGGAGAGMGS RGPGETKIEL DRRRIHSRMA KLRKQIANMK PAREAKRANR KRNAVPSVAI AGYTNAGKSS ILNRITGAGV LVENALFATL DATVRRNTTA DGRVYTIADT VGFVRNLPHQ LVEAFRSTLE EVGDSDLIVH VVDAAHPDPA GQIATVRDVI GEVGARDIPE LIVFNKADLV TPEDRLVLRG LEPGAIFASA RTGEGIPEVL EAIARMMPDP AVEIDLLVPY DRGDVVSTLH ETGRVLSIEY DEDGTRVRAL ASPELAGQLE EFSATSAGR // ID A0A0Q7WUK9_9RHIZ Unreviewed; 461 AA. AC A0A0Q7WUK9; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 07-JUN-2017, entry version 12. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=ASD44_05915 {ECO:0000313|EMBL:KQZ36171.1}; OS Mesorhizobium sp. Root554. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Phyllobacteriaceae; Mesorhizobium. OX NCBI_TaxID=1736557 {ECO:0000313|EMBL:KQZ36171.1, ECO:0000313|Proteomes:UP000054487}; RN [1] {ECO:0000313|EMBL:KQZ36171.1, ECO:0000313|Proteomes:UP000054487} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Root554 {ECO:0000313|EMBL:KQZ36171.1, RC ECO:0000313|Proteomes:UP000054487}; RA Millard Andrew; RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:KQZ36171.1, ECO:0000313|Proteomes:UP000054487} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Root554 {ECO:0000313|EMBL:KQZ36171.1, RC ECO:0000313|Proteomes:UP000054487}; RA Vorholt J.; RT "Functional overlap of the Arabidopsis leaf and root microbiotas."; RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KQZ36171.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LMGA01000001; KQZ36171.1; -; Genomic_DNA. DR RefSeq; WP_056109775.1; NZ_LMGA01000001.1. DR EnsemblBacteria; KQZ36171; KQZ36171; ASD44_05915. DR Proteomes; UP000054487; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000054487}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000054487}. FT DOMAIN 229 401 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 188 222 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 461 AA; 50397 MW; EABBC07E477A946F CRC64; MQKDTDAGRG TRGASGTGNG EKARTRALVI VPVLNRATHD EDDRSRPRLA RSAQARLDEA VGLARAIDLD PVNVSVVTVN DPRPATLLGS GKVAEFADIV KETHAELAIV DHPLTPVQQR NLEKELNVKV LDRTGLILEI FGERARTKEG TLQVELAHLN YQKGRLVRSW THLERQRGGA GFLGGPGETQ IEADRRVLQD KIVKLKRELE TVRRTRDLHR AKRRKVPFPV VAIVGYTNAG KSTLFNRLTG AGVLAEDMLF ATLDPTLRRL RLPHGTPVIL SDTVGFISDL PTHLVAAFRA TLEEVVEADL VLHLRDISDP DTAAQAEDVE RILADLGVDV GDGDRVVEVW NKIDQLDAGS RERLLETGNE PGKSPVAISA ITGEGLDALM ALIETRVSGE LRSVEITLAP AQMRFLDWIY RNSEVVTRTD NDDGSVSLSL KVTDTAREEI DGRLSGRKGG G // ID A0A0Q7YFJ4_9RHIZ Unreviewed; 446 AA. AC A0A0Q7YFJ4; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 07-JUN-2017, entry version 12. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=ASD54_06655 {ECO:0000313|EMBL:KQZ54968.1}; OS Rhizobium sp. Root149. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium. OX NCBI_TaxID=1736473 {ECO:0000313|EMBL:KQZ54968.1, ECO:0000313|Proteomes:UP000051907}; RN [1] {ECO:0000313|EMBL:KQZ54968.1, ECO:0000313|Proteomes:UP000051907} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Root149 {ECO:0000313|EMBL:KQZ54968.1, RC ECO:0000313|Proteomes:UP000051907}; RA Millard Andrew; RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:KQZ54968.1, ECO:0000313|Proteomes:UP000051907} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Root149 {ECO:0000313|EMBL:KQZ54968.1, RC ECO:0000313|Proteomes:UP000051907}; RA Vorholt J.; RT "Functional overlap of the Arabidopsis leaf and root microbiotas."; RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KQZ54968.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LMGD01000012; KQZ54968.1; -; Genomic_DNA. DR RefSeq; WP_062554410.1; NZ_LMGD01000012.1. DR EnsemblBacteria; KQZ54968; KQZ54968; ASD54_06655. DR Proteomes; UP000051907; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000051907}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000051907}. FT DOMAIN 208 380 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 167 201 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 446 AA; 49707 MW; 195CB9037381B0CB CRC64; MRALVLVPVL KQARSAASGP SDTATPAPRR SDEARLEEAM GLARAIDLTI ARGLIIPVSQ PKPATLIGTG KIEEIKALLD ENDCGLVIVD HPLTPVQQRN LEKEWQAKVI DRTGLILEIF GRRASTKEGT LQVDLAHLNY QKGRLVRSWT HLERQRGGAG FMGGPGETQI EADRRLLQER ILKLERELEQ VVRTRQLHRA KRRKVPHPIV ALVGYTNAGK STLFNRITGA GVLAENMLFA TLDPTLRRMK LPHGRTVILS DTVGFISDLP THLVAAFRAT LEEVLEADLI LHVRDMSDPD NGAQSADVLR ILDDLGIDEK ERSERIIEVW NKIDRLEPEA HEAVAERALG RENVMAVSAI SGEGVDRLMD EISRRLAGVV TETTVVLPPE KLSLISWIYE NAMVDQREDR EDGSVAFDLR LSEQQANALE RKLGVFPVAE KEDWER // ID A0A0Q7YK93_9SPHN Unreviewed; 448 AA. AC A0A0Q7YK93; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 30-AUG-2017, entry version 17. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=ASD67_21555 {ECO:0000313|EMBL:KQZ61766.1}; OS Sphingopyxis sp. Root1497. OC Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales; OC Sphingomonadaceae; Sphingopyxis. OX NCBI_TaxID=1736474 {ECO:0000313|EMBL:KQZ61766.1, ECO:0000313|Proteomes:UP000051141}; RN [1] {ECO:0000313|EMBL:KQZ61766.1, ECO:0000313|Proteomes:UP000051141} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Root1497 {ECO:0000313|EMBL:KQZ61766.1, RC ECO:0000313|Proteomes:UP000051141}; RA Millard Andrew; RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:KQZ61766.1, ECO:0000313|Proteomes:UP000051141} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Root1497 {ECO:0000313|EMBL:KQZ61766.1, RC ECO:0000313|Proteomes:UP000051141}; RA Vorholt J.; RT "Functional overlap of the Arabidopsis leaf and root microbiotas."; RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KQZ61766.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LMGF01000005; KQZ61766.1; -; Genomic_DNA. DR RefSeq; WP_056351431.1; NZ_LMGF01000005.1. DR EnsemblBacteria; KQZ61766; KQZ61766; ASD67_21555. DR Proteomes; UP000051141; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000051141}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}. FT DOMAIN 206 388 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 172 199 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 448 AA; 48826 MW; 0DB1156363457F3B CRC64; MSDNDDEVTR GATAVLIVPE WHSQRLSRDL DARAEEAKGL ALAIGLEVVA VFPLRLRQTR AATLIGVGQI DAIKAEVGEG AAQLVIVDAA LTAIQQRNLE TAFGTKVIDR TGLILEIFGE RAATAEGRLQ VELAHLDYQA GRLVRSWTHL ERQRGGFGFL GGPGETQIEA DRRMIRNRMA RIRRSLEDAK RTRQLQRAKR QRAPWPVVAL VGYTNAGKST FFNRLTGSDV MAEDMLFATL DPTMREIRLP GIDKAILSDT VGFVSDLPTE LVAAFRATLE EVTTADLIVH VRDIAHPDSE AQYADVVAIL NSLGVNGPQD GGEGGADAPA VIPQIEIWNK IDTADSDERA AIEEMAARRS DVAVISAVSG EGVEAARTLM ASQLTALHRI ERIFLGYDHG EAAAWLHARG EVLGDEPQEN GHVLTVRLDP ADKARFERLW PARTAPTP // ID A0A0Q7ZC80_9ACTN Unreviewed; 502 AA. AC A0A0Q7ZC80; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=ASD66_18960 {ECO:0000313|EMBL:KQZ67074.1}; OS Nocardioides sp. Root151. OC Bacteria; Actinobacteria; Propionibacteriales; Nocardioidaceae; OC Nocardioides. OX NCBI_TaxID=1736475 {ECO:0000313|EMBL:KQZ67074.1, ECO:0000313|Proteomes:UP000051274}; RN [1] {ECO:0000313|EMBL:KQZ67074.1, ECO:0000313|Proteomes:UP000051274} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Root151 {ECO:0000313|EMBL:KQZ67074.1, RC ECO:0000313|Proteomes:UP000051274}; RA Millard Andrew; RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:KQZ67074.1, ECO:0000313|Proteomes:UP000051274} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Root151 {ECO:0000313|EMBL:KQZ67074.1, RC ECO:0000313|Proteomes:UP000051274}; RA Vorholt J.; RT "Functional overlap of the Arabidopsis leaf and root microbiotas."; RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KQZ67074.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LMGG01000007; KQZ67074.1; -; Genomic_DNA. DR RefSeq; WP_056682069.1; NZ_LMGG01000007.1. DR EnsemblBacteria; KQZ67074; KQZ67074; ASD66_18960. DR Proteomes; UP000051274; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 2. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000313|EMBL:KQZ67074.1}; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000051274}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900, KW ECO:0000313|EMBL:KQZ67074.1}. FT DOMAIN 284 449 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 250 277 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 502 AA; 54751 MW; 4D0E7466DD003BDD CRC64; MTNASEDFSL DAELAETDTW DDDDFESGYA DEGADELVST EGPDPEELTT GEQDLAERHA LRRVAGLRTE LEDITEVEYR QLRLERVVLV GVWTEGSIED AENSMAELAL LAETAGSEVL DNVYQRRQKP DPATYIGRGK VEGLREIVAA NGADTVILDG DLAPSQLRNL EDKLKVKAID RTALILDIFA QHAKSREGQA QVELAQLSYM KQRLRGWGGN LSRQAGGRVG ADGGGIGGRG PGETKIETDR RRINTKIAKL RRELKAMKGT RDTKRAERQR HAIPSVAIAG YTNAGKSSLL NKLTDAGVLV EDSLFATLDP TTRRTTTADG RIYTMSDTVG FVRHLPHQLV EAFRSTLEEV ADSDLILHVV DGSHPDPEGQ IAAVREVLAD IDASKVPELI VINKADAADP MVLARLRQRE KHSVVVSAKT GEGIAEALAL VEAELPRPGV EFTALLPYER GDLINRLHQR GEIETLEHTA EGTLVKGRAH EDLAGELAAY AV // ID A0A0Q8BJQ8_9RHIZ Unreviewed; 445 AA. AC A0A0Q8BJQ8; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 05-JUL-2017, entry version 13. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=ASD64_17025 {ECO:0000313|EMBL:KQZ96519.1}; OS Mesorhizobium sp. Root157. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Phyllobacteriaceae; Mesorhizobium. OX NCBI_TaxID=1736477 {ECO:0000313|EMBL:KQZ96519.1, ECO:0000313|Proteomes:UP000053761}; RN [1] {ECO:0000313|EMBL:KQZ96519.1, ECO:0000313|Proteomes:UP000053761} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Root157 {ECO:0000313|EMBL:KQZ96519.1, RC ECO:0000313|Proteomes:UP000053761}; RA Millard Andrew; RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:KQZ96519.1, ECO:0000313|Proteomes:UP000053761} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Root157 {ECO:0000313|EMBL:KQZ96519.1, RC ECO:0000313|Proteomes:UP000053761}; RA Vorholt J.; RT "Functional overlap of the Arabidopsis leaf and root microbiotas."; RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KQZ96519.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LMGJ01000006; KQZ96519.1; -; Genomic_DNA. DR EnsemblBacteria; KQZ96519; KQZ96519; ASD64_17025. DR Proteomes; UP000053761; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000053761}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000053761}. FT DOMAIN 211 384 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 170 204 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 445 AA; 48864 MW; 278A0B736103A4DE CRC64; MDGAKAPTRA VVIVPVVTRG AAADDAIRSR PMRSAEARHD EAVGLTRAID LEPVHSAVVT VNDPRPATLL GSGKVTEFAD IVKEKDAELV IVDHPLTPVQ QRNLEKEMNV KVLDRTGLIL EIFGERARTK EGTLQVELAH LNYQKGRLVR SWTHLERQRG GAGFLGGPGE TQIEADRRAL QEKIVKLKRE LETVRRTRDL HRAKRKKVPF PVIAIVGYTN AGKSTLFNRL TGAGVLAEDM LFATLDPTLR RLRLPHGTPV ILSDTVGFIS DLPTHLIAAF RATLEEVVEA DLVIHLRDIS DPDTAAQAED VERILADLGV DAKDDRRVIE VWNKIDLLDE GNRTRLLDEA QGRAGTKPIA ISAITGEGFE ALKETIEARV SGELAPLTVT LAPSQLGLVD WLYRNGEVTG RTDNEDGGVT IELSATKSAR DEIQSRLRQG NSRKQ // ID A0A0Q8BJY3_9RHIZ Unreviewed; 442 AA. AC A0A0Q8BJY3; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 07-JUN-2017, entry version 13. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=ASD74_06660 {ECO:0000313|EMBL:KQZ96922.1}; OS Rhizobium sp. Root564. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium. OX NCBI_TaxID=1736563 {ECO:0000313|EMBL:KQZ96922.1, ECO:0000313|Proteomes:UP000052141}; RN [1] {ECO:0000313|EMBL:KQZ96922.1, ECO:0000313|Proteomes:UP000052141} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Root564 {ECO:0000313|EMBL:KQZ96922.1, RC ECO:0000313|Proteomes:UP000052141}; RA Millard Andrew; RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:KQZ96922.1, ECO:0000313|Proteomes:UP000052141} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Root564 {ECO:0000313|EMBL:KQZ96922.1, RC ECO:0000313|Proteomes:UP000052141}; RA Vorholt J.; RT "Functional overlap of the Arabidopsis leaf and root microbiotas."; RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KQZ96922.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LMGN01000011; KQZ96922.1; -; Genomic_DNA. DR RefSeq; WP_062425343.1; NZ_LMGN01000011.1. DR EnsemblBacteria; KQZ96922; KQZ96922; ASD74_06660. DR Proteomes; UP000052141; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000052141}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000052141}. FT DOMAIN 204 376 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 163 197 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 442 AA; 48904 MW; 74CD6DAA4F802E48 CRC64; MRAVVLVPQL KQQRDHREAT ATAPLRSMEA KLEEAKGLAL AIDLTVTQGL IVPVSQPRPA TLFGTGKIEE IGHLLDETDA GLVIVDHPLT PVQQRNLEKQ WNSKVIDRTG LILEIFGRRA STKEGTLQVD LAHLNYQKGR LVRSWTHLER QRGGAGFMGG PGETQIEADR RLLQDRIVRL ERELEQVVRT RQLHRAKRRK VPHPIVALVG YTNAGKSTLF NRITGAGVLA EDMLFATLDP TLRRMKLPHG RTVILSDTVG FISDLPTHLV AAFRATLEEV LEADLVLHVR DMSDPDNAAQ AGDVMRILGD LGIDEKVAEE RIIEVWNKVD RLEPEAHDAI MQKAEGRANV RAVSALTGEG VDALMDDVSV RLSGVLTETT IVLSVDQLQL LSWVYDNAIV DGREDREDGS VALDIRLSGE QGAALERKLG LGAKTQSEDW ER // ID A0A0Q8CJ52_9MICO Unreviewed; 521 AA. AC A0A0Q8CJ52; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=ASD61_16725 {ECO:0000313|EMBL:KRA09346.1}; OS Leifsonia sp. Root60. OC Bacteria; Actinobacteria; Micrococcales; Microbacteriaceae; Leifsonia. OX NCBI_TaxID=1736567 {ECO:0000313|EMBL:KRA09346.1, ECO:0000313|Proteomes:UP000051073}; RN [1] {ECO:0000313|EMBL:KRA09346.1, ECO:0000313|Proteomes:UP000051073} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Root60 {ECO:0000313|EMBL:KRA09346.1, RC ECO:0000313|Proteomes:UP000051073}; RA Millard Andrew; RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:KRA09346.1, ECO:0000313|Proteomes:UP000051073} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Root60 {ECO:0000313|EMBL:KRA09346.1, RC ECO:0000313|Proteomes:UP000051073}; RA Vorholt J.; RT "Functional overlap of the Arabidopsis leaf and root microbiotas."; RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KRA09346.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LMGR01000002; KRA09346.1; -; Genomic_DNA. DR RefSeq; WP_055825300.1; NZ_LMGR01000002.1. DR EnsemblBacteria; KRA09346; KRA09346; ASD61_16725. DR Proteomes; UP000051073; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 2. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000051073}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000051073}. FT DOMAIN 285 450 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 521 AA; 56347 MW; 61EBFB81770D5811 CRC64; MTEPDTTMPD DDVVARVLAS AEQRAGYTIF AGSAQALQDD EGRAHRVDSD GDQFDREDRQ ALRRVAGLST ELEDVTEVEY RQLRLENVVL IGVYPQGSQT EAENSIRELA ALAETAGATV LDGLLQRRPH PDPSTYLGSG KARELAGIVA SLGADTVIAD TELAPSQRRA LEDIVKVKVI DRTAVILDIF SQHATSREGK AQVELAQLEY LLPRLRGWGE SMSRQAGGQV GGAGAGMGSR GPGETKIELD RRRIHTRMAK LRKSIAAMKP AREAKRANRK RNTVPSVAIA GYTNAGKSSL VNRITKAGLL VENALFATLD ATVRRNTTED GRLYTIADTV GFVRNLPHQL VEAFRSTLEE VADSDLILHV VDASHPDPAG QIQTVRDVIG EVEARHIPEL VVFNKSDLVS DDDRLVLRGL EPNAVFVSAR SGEGIDELLR KIAEMLPDPS VEVELLIPYS RGELVSSLHV RGRVIATEHT EHGTAVRALV HPEFAAQLAE FIVPAGALTV GTLPADALPA V // ID A0A0Q8DVM4_9ACTN Unreviewed; 494 AA. AC A0A0Q8DVM4; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=ASD81_17270 {ECO:0000313|EMBL:KRA31214.1}; OS Nocardioides sp. Root614. OC Bacteria; Actinobacteria; Propionibacteriales; Nocardioidaceae; OC Nocardioides. OX NCBI_TaxID=1736571 {ECO:0000313|EMBL:KRA31214.1, ECO:0000313|Proteomes:UP000051699}; RN [1] {ECO:0000313|EMBL:KRA31214.1, ECO:0000313|Proteomes:UP000051699} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Root614 {ECO:0000313|EMBL:KRA31214.1, RC ECO:0000313|Proteomes:UP000051699}; RA Millard Andrew; RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:KRA31214.1, ECO:0000313|Proteomes:UP000051699} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Root614 {ECO:0000313|EMBL:KRA31214.1, RC ECO:0000313|Proteomes:UP000051699}; RA Vorholt J.; RT "Functional overlap of the Arabidopsis leaf and root microbiotas."; RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KRA31214.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LMGV01000007; KRA31214.1; -; Genomic_DNA. DR RefSeq; WP_056713205.1; NZ_LMGV01000007.1. DR EnsemblBacteria; KRA31214; KRA31214; ASD81_17270. DR Proteomes; UP000051699; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 2. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000313|EMBL:KRA31214.1}; KW Complete proteome {ECO:0000313|Proteomes:UP000051699}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900, KW ECO:0000313|EMBL:KRA31214.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000051699}. FT DOMAIN 276 442 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 494 AA; 53528 MW; D1717FB08EB24881 CRC64; MTNHAEDFSL DSALRATEGW DDPDNDTFES GYAPASADEP TAGDMDLAAR HELRRVAGLR TELEDISEVE YRQLRLERVV LVGVWTEGTV QDHENAMAEL ALLAETAGSE VLDAIYQRRQ SPDPATYIGR GKVEGLAEIV QASGADTVIC DGELAPSQLR NLEDRVKVKV VDRTALILDI FAQHAKSAEG QAQVELAQLS YMKQRLRGWG GNLSRQAGGR VGADGAGIGG RGPGETKIET DRRRINDKIA KLRRDLKVMK GTRDTKRQER RRNHIPSVAI AGYTNAGKSS LLNRLTGAGV LVEDSLFATL DPTTRRTTTA DGRVFTMSDT VGFVRHLPHQ LVEAFRSTLE EVADADLIVH VVDGSHPDPE GQLNAVRAVL ADIDAGDVPE LVVINKVDAA DPLVIDRLLR REPHSIAVSA HTGEGIKEAL ALIEGDLPRP QVAFSALVPY ARGDLIDRIH RDGEIATIEH TADGSHVTGR TSEALAGELA DYAV // ID A0A0Q8EXW8_9GAMM Unreviewed; 446 AA. AC A0A0Q8EXW8; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=ASD77_11475 {ECO:0000313|EMBL:KRA52297.1}; OS Pseudoxanthomonas sp. Root65. OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales; OC Xanthomonadaceae; Pseudoxanthomonas. OX NCBI_TaxID=1736576 {ECO:0000313|EMBL:KRA52297.1, ECO:0000313|Proteomes:UP000051430}; RN [1] {ECO:0000313|EMBL:KRA52297.1, ECO:0000313|Proteomes:UP000051430} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Root65 {ECO:0000313|EMBL:KRA52297.1, RC ECO:0000313|Proteomes:UP000051430}; RA Millard Andrew; RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:KRA52297.1, ECO:0000313|Proteomes:UP000051430} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Root65 {ECO:0000313|EMBL:KRA52297.1, RC ECO:0000313|Proteomes:UP000051430}; RA Vorholt J.; RT "Functional overlap of the Arabidopsis leaf and root microbiotas."; RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KRA52297.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LMHA01000002; KRA52297.1; -; Genomic_DNA. DR RefSeq; WP_055941635.1; NZ_LMHA01000002.1. DR EnsemblBacteria; KRA52297; KRA52297; ASD77_11475. DR Proteomes; UP000051430; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000051430}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000051430}. FT DOMAIN 199 376 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 158 192 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 446 AA; 49050 MW; C4AD52A88304841F CRC64; MFERSRKGEH ALLIQPHAGG RPDDGLTEEF SDLARSAGAT VAALLTARID RPNPSTLIGS GKLEEVKAAA DATGADLILV NFPLSPGQER NLEKFLERRV LDRTGLILDI FAQRARSHEG KLQVELAQLR HMATRLVRGW THLERQRGGS IGLRGPGETQ LETDRRLLQK RVEQLQKRLE KVEVQRTQMR RARVRSELPR VALVGYTNAG KSTLFNVLTG AEAYAADQLF ATLDPTVRRI DLPGGAVVLA DTVGFVRDLP HELVAAFRST LSEAREADLL LHVIDAADPH REERIAQVDE VLQEIGAGDL PQMLVFNKID RIDGAAPRHD QPDPGVDAGD APSAGMGRER VWLSARDGQG IDLLKGALAQ RLGFQRVRGE LHLPANSARL RSRLHALGAV LAEDFEENGW RVTLDLALAD AQRLASQAGG HPLEALLPQT EREDWQ // ID A0A0Q8LFW9_9MICO Unreviewed; 509 AA. AC A0A0Q8LFW9; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=ASD93_07700 {ECO:0000313|EMBL:KRB36002.1}; OS Microbacterium sp. Root180. OC Bacteria; Actinobacteria; Micrococcales; Microbacteriaceae; OC Microbacterium. OX NCBI_TaxID=1736483 {ECO:0000313|EMBL:KRB36002.1, ECO:0000313|Proteomes:UP000050802}; RN [1] {ECO:0000313|EMBL:KRB36002.1, ECO:0000313|Proteomes:UP000050802} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Root180 {ECO:0000313|EMBL:KRB36002.1, RC ECO:0000313|Proteomes:UP000050802}; RA Millard Andrew; RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:KRB36002.1, ECO:0000313|Proteomes:UP000050802} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Root180 {ECO:0000313|EMBL:KRB36002.1, RC ECO:0000313|Proteomes:UP000050802}; RA Vorholt J.; RT "Functional overlap of the Arabidopsis leaf and root microbiotas."; RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KRB36002.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LMHS01000003; KRB36002.1; -; Genomic_DNA. DR RefSeq; WP_056121054.1; NZ_LMHS01000003.1. DR EnsemblBacteria; KRB36002; KRB36002; ASD93_07700. DR Proteomes; UP000050802; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000050802}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000050802}. FT DOMAIN 287 452 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 509 AA; 54919 MW; 6610A8EEB0AD6B03 CRC64; MTDTTTPQST DETPVDPVDR VLARADARSG VRVFGAAQAL QDEATTGSGD TDGDQWDREE RAALRRVPGL STELEDVTEV EYRQLRLENV VLVGVHPQGE QEDAENSLRE LSALAETAGA VVLDGVLQRR PHPDPATYVG RGKAQELRDI VAAVGADTVI ADTELAPSQR RALEDVVKVK VIDRTTVILD IFSQHAKSRE GKAQVELAQL EYLLPRLRGW GDSMSRQAGG QVGAGGAGMG SRGPGETKIE LDRRRIRTRM AQLRRQIRDF APARDAKRAE RKRHTIPSVA IAGYTNAGKS SLLNRLTSAG VLVENALFAT LDATVRRSET TDGRVYTLTD TVGFVRNLPH QLVEAFRSTL EEVGGSDVIV HVVDGSHPDP AAQLATVRDV IGDVGGRDIP ELVVFNKADL VDEDTRLVLR GLEPKALFAS SRTGEGIEEL RAAIEAALPL PAVELEVLVP YDRGDLVSAI HEQGMILSQA HEAGGTAVHA RVGEHLAARL APFLLARPS // ID A0A0Q8MUD8_9RHIZ Unreviewed; 444 AA. AC A0A0Q8MUD8; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 07-JUN-2017, entry version 12. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=ASE04_07135 {ECO:0000313|EMBL:KRB52991.1}; OS Rhizobium sp. Root708. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium. OX NCBI_TaxID=1736592 {ECO:0000313|EMBL:KRB52991.1, ECO:0000313|Proteomes:UP000051238}; RN [1] {ECO:0000313|EMBL:KRB52991.1, ECO:0000313|Proteomes:UP000051238} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Root708 {ECO:0000313|EMBL:KRB52991.1, RC ECO:0000313|Proteomes:UP000051238}; RA Millard Andrew; RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:KRB52991.1, ECO:0000313|Proteomes:UP000051238} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Root708 {ECO:0000313|EMBL:KRB52991.1, RC ECO:0000313|Proteomes:UP000051238}; RA Vorholt J.; RT "Functional overlap of the Arabidopsis leaf and root microbiotas."; RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KRB52991.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LMHV01000034; KRB52991.1; -; Genomic_DNA. DR RefSeq; WP_056819553.1; NZ_LMHV01000034.1. DR EnsemblBacteria; KRB52991; KRB52991; ASE04_07135. DR Proteomes; UP000051238; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000051238}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000051238}. FT DOMAIN 206 378 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 165 199 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 444 AA; 49013 MW; 2A1F982562C4268B CRC64; MRATVIVPVL KQARGGRSAS DAAPVATRTP ESRLEEATGL AQAIDLDVVH GAIVPVNDPR PATLMGTGKI EEIKATLDVN DSGLVIVDHP LTPVQQRNLE KEWNAKVIDR TGLILEIFGR RASTKEGTLQ VDLAHLNYQK GRLVRSWTHL ERQRGGGGFM GGPGETQIEA DRRMLQDRII KLERELEQVV RTRQLHRAKR RKVPHPIVAL VGYTNAGKST LFNRITGAGV LAEDMLFATL DPTLRRMKLP HGRTVILSDT VGFISNLPTH LVAAFRATLE EVLEADLILH VRDMADVDNQ AQSADVLRIL KDLGIDEEEG DKRIIEVWNK IDRLEPEDHD AIVNKASGSE NVVALSAVSG EGVDALMDEI SRRLSGVLTE ATVRLPVDKL ALLPWLYDHA IVDSREDNED GSITLDVRLS EAEAVELERR LGNGAKSAKE DWER // ID A0A0Q8P7M3_9ACTN Unreviewed; 502 AA. AC A0A0Q8P7M3; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=ASE03_27330 {ECO:0000313|EMBL:KRB69478.1}; OS Kitasatospora sp. Root187. OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae; OC Kitasatospora. OX NCBI_TaxID=1736486 {ECO:0000313|EMBL:KRB69478.1, ECO:0000313|Proteomes:UP000051829}; RN [1] {ECO:0000313|EMBL:KRB69478.1, ECO:0000313|Proteomes:UP000051829} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Root187 {ECO:0000313|EMBL:KRB69478.1, RC ECO:0000313|Proteomes:UP000051829}; RA Millard Andrew; RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:KRB69478.1, ECO:0000313|Proteomes:UP000051829} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Root187 {ECO:0000313|EMBL:KRB69478.1, RC ECO:0000313|Proteomes:UP000051829}; RA Vorholt J.; RT "Functional overlap of the Arabidopsis leaf and root microbiotas."; RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KRB69478.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LMHX01000017; KRB69478.1; -; Genomic_DNA. DR RefSeq; WP_057229415.1; NZ_LMHX01000017.1. DR EnsemblBacteria; KRB69478; KRB69478; ASE03_27330. DR Proteomes; UP000051829; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000313|EMBL:KRB69478.1}; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000051829}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900, KW ECO:0000313|EMBL:KRB69478.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000051829}. FT DOMAIN 280 445 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 239 273 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 502 AA; 54859 MW; C2C4C12D2C1EF095 CRC64; MRLTSTFESR SNSDSQGKRL SDLRAEALMD EDLAANDEGF DRYDGEQYDR SERAALRRVA GLSTELQDVT EVEYRQLRLE RVVLVGVWTD GTVEEAENSM AELAALAETA GSEVLDGVIQ RRDKPDPATY IGSGKARELR DIVASTGADT VVCDGELTPG QLIQLEDVVK VKVVDRTALI LDIFAQHAKS REGKAQVSLA QMQYMLPRLR GWGASLSRQM GGGGSGSSGG GMATRGPGET KIETDRRRIR EKMAKLRREI VDMKKGRDTK RQERRRNQVP SVAIAGYTNA GKSSILNRLT GAGVLVENSL FATLDPTVRR AQTPSGRVYT LADTVGFVRH LPHHLVEAFR STMEEVAEAD LILHVVDGSH PEPETQLAAV REVIVSVDAQ NVREVVVINK ADAADPLVLQ RLLRREPHAI VVSARTGLGM EELLQLIDSE LPRPAIEVQA LIPYTRGDLV SRVHAEGEPI STEHTGEGTL LHAKVAAELA AELEKYAVVT QG // ID A0A0Q8PWL2_9ACTN Unreviewed; 502 AA. AC A0A0Q8PWL2; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 07-JUN-2017, entry version 14. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=ASE01_07255 {ECO:0000313|EMBL:KRB77967.1}; OS Nocardioides sp. Root190. OC Bacteria; Actinobacteria; Propionibacteriales; Nocardioidaceae; OC Nocardioides. OX NCBI_TaxID=1736488 {ECO:0000313|EMBL:KRB77967.1, ECO:0000313|Proteomes:UP000050886}; RN [1] {ECO:0000313|EMBL:KRB77967.1, ECO:0000313|Proteomes:UP000050886} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Root190 {ECO:0000313|EMBL:KRB77967.1, RC ECO:0000313|Proteomes:UP000050886}; RA Millard Andrew; RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:KRB77967.1, ECO:0000313|Proteomes:UP000050886} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Root190 {ECO:0000313|EMBL:KRB77967.1, RC ECO:0000313|Proteomes:UP000050886}; RA Vorholt J.; RT "Functional overlap of the Arabidopsis leaf and root microbiotas."; RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KRB77967.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LMIA01000008; KRB77967.1; -; Genomic_DNA. DR RefSeq; WP_056749692.1; NZ_LMIA01000008.1. DR EnsemblBacteria; KRB77967; KRB77967; ASE01_07255. DR Proteomes; UP000050886; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 2. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000313|EMBL:KRB77967.1}; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000050886}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900, KW ECO:0000313|EMBL:KRB77967.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000050886}. FT DOMAIN 284 446 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 243 270 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 502 AA; 54811 MW; 50B15CF76BF5918C CRC64; MTNHAEDFTL AAALRATEGW DDPDDLVDPD NPDDTWESGY AADDPEDLTT GEMDLAARHE LRRVAGLRTE LEDITEVEYR QLRLERVVLV GVWTEGSIQD VENAMAELAL LAETAGSEVL DAIYQRRQTP DPATYIGRGK VEGLREIVQA SGADTVICDG ELAPSQLRNL EDRVKVKVVD RTALILDIFA QHAKSKEGQA QVELAQLSYM KQRLRGWGGN LSRQAGGRVG ADGGGIGGRG PGETKIETDR RRINDKIAKL RRELKLMKGT RDTKRQGRRR HEIPSVAIAG YTNAGKSSLL NRLTGAGVLV EDSLFATLDP TTRRTQTSDG RIYTMSDTVG FVRHLPHQLV EAFRSTLEEV ADADLIVHVV DGSHPDPEGQ LAAVREVLAD IDASKIPELV VINKIDAADP LVVDRIRRRE PHSVAVSAHT GEGIAEAIAA IENDLPRPRV EFTALVPYAR GDLIDRIHKD GEISEIEHTA DGTHISGRAT EALAGELAAY AV // ID A0A0Q8QV75_9SPHN Unreviewed; 438 AA. AC A0A0Q8QV75; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=ASE00_03550 {ECO:0000313|EMBL:KRB85849.1}; OS Sphingomonas sp. Root710. OC Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales; OC Sphingomonadaceae; Sphingomonas. OX NCBI_TaxID=1736594 {ECO:0000313|EMBL:KRB85849.1, ECO:0000313|Proteomes:UP000051854}; RN [1] {ECO:0000313|EMBL:KRB85849.1, ECO:0000313|Proteomes:UP000051854} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Root710 {ECO:0000313|EMBL:KRB85849.1, RC ECO:0000313|Proteomes:UP000051854}; RA Millard Andrew; RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:KRB85849.1, ECO:0000313|Proteomes:UP000051854} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Root710 {ECO:0000313|EMBL:KRB85849.1, RC ECO:0000313|Proteomes:UP000051854}; RA Vorholt J.; RT "Functional overlap of the Arabidopsis leaf and root microbiotas."; RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KRB85849.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LMIB01000001; KRB85849.1; -; Genomic_DNA. DR RefSeq; WP_056377800.1; NZ_LMIB01000001.1. DR EnsemblBacteria; KRB85849; KRB85849; ASE00_03550. DR Proteomes; UP000051854; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000051854}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000051854}. FT DOMAIN 209 387 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 175 202 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 438 AA; 47598 MW; 12F1CDA393731121 CRC64; MSVFNREDDD GLSRGAKALV ALPERAGDSQ RSAEARLDEA AGLAAAIGVD VVEKLAFRLR DPKPATLFGS GQVDQIATAA RMGEAELIIV DAALTPIQQR NLEKATEAKV IDRTGLILEI FGERAATAEG RLQVELAHLD YQAGRLVRSW THLERQRGGF GFLGGPGETQ IEADRRLIRD RMAKLRRELE QVRRTRGLHR ARRQRAPWPV IALVGYTNAG KSTLFNRMTG AKVMAEDLLF ATLDPTMRQI TLPGIDKAIL SDTVGFVSDL PTQLVAAFRA TLEEVTGADI ILHVRDIAHP DSDAQAADVL TVLGEIGVGP RAPESEGGDG APIIEVWNKV DMLDPETHAA TEAEAERRED VVTLSALTGE GVDTLRRVVS ERLSTGNRVR TLPVLLSDGA AMAWLHANGE VIGQEIEGGR MIVEVRLSDK DLARFEAR // ID A0A0Q8R1J2_9SPHN Unreviewed; 438 AA. AC A0A0Q8R1J2; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=ASE22_10360 {ECO:0000313|EMBL:KRB90705.1}; OS Sphingomonas sp. Root720. OC Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales; OC Sphingomonadaceae; Sphingomonas. OX NCBI_TaxID=1736595 {ECO:0000313|EMBL:KRB90705.1, ECO:0000313|Proteomes:UP000051570}; RN [1] {ECO:0000313|EMBL:KRB90705.1, ECO:0000313|Proteomes:UP000051570} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Root720 {ECO:0000313|EMBL:KRB90705.1, RC ECO:0000313|Proteomes:UP000051570}; RA Millard Andrew; RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:KRB90705.1, ECO:0000313|Proteomes:UP000051570} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Root720 {ECO:0000313|EMBL:KRB90705.1, RC ECO:0000313|Proteomes:UP000051570}; RA Vorholt J.; RT "Functional overlap of the Arabidopsis leaf and root microbiotas."; RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KRB90705.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LMID01000011; KRB90705.1; -; Genomic_DNA. DR RefSeq; WP_056359221.1; NZ_LMID01000011.1. DR EnsemblBacteria; KRB90705; KRB90705; ASE22_10360. DR Proteomes; UP000051570; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000051570}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000051570}. FT DOMAIN 209 387 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 175 202 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 438 AA; 47496 MW; 5C73F4D8879463D8 CRC64; MSVFNRDEDD GLSRGARALV ALPERSGDNS RSAEARLDEA AGLAAAIGVD VVEKLAFKLR DPKPATLFGS GQVEQIATAA RMGEAELVIV DAALTPIQQR NLEKAIEAKV IDRTGLILEI FGERAATAEG RLQVELAHLD YQAGRLVRSW THLERQRGGF GFLGGPGETQ IEADRRLIRD RMAKLRRELE QVRRTRGLHR ARRQRAPWPV IALVGYTNAG KSTLFNRMTG AKVMAEDLLF ATLDPTMRQI SLPGIDKAIL SDTVGFVSDL PTQLVAAFRA TLEEVTGADI ILHVRDIAHP DSDAQATDVL TVLGEIGVGP KAPDGEAGEG APIFEVWNKI DMLDPETRAA TEAEAARRDD VVTLSALTGD GVEDLRRAVS DRLSTGNRVR TLTVSLSDGA ALAWLHAHGE VIGQEVEGET MIVEVRLSDS DLARFEAR // ID A0A0Q8RKR8_9BURK Unreviewed; 381 AA. AC A0A0Q8RKR8; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=ASE26_02210 {ECO:0000313|EMBL:KRC03669.1}; OS Duganella sp. Root198D2. OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Oxalobacteraceae; Duganella. OX NCBI_TaxID=1736489 {ECO:0000313|EMBL:KRC03669.1, ECO:0000313|Proteomes:UP000051728}; RN [1] {ECO:0000313|EMBL:KRC03669.1, ECO:0000313|Proteomes:UP000051728} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Root198D2 {ECO:0000313|EMBL:KRC03669.1, RC ECO:0000313|Proteomes:UP000051728}; RA Millard Andrew; RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:KRC03669.1, ECO:0000313|Proteomes:UP000051728} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Root198D2 {ECO:0000313|EMBL:KRC03669.1, RC ECO:0000313|Proteomes:UP000051728}; RA Vorholt J.; RT "Functional overlap of the Arabidopsis leaf and root microbiotas."; RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KRC03669.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LMIC01000001; KRC03669.1; -; Genomic_DNA. DR RefSeq; WP_055931609.1; NZ_LMIC01000001.1. DR EnsemblBacteria; KRC03669; KRC03669; ASE26_02210. DR Proteomes; UP000051728; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000051728}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000051728}. FT DOMAIN 190 357 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 156 183 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 381 AA; 42102 MW; 6303587A3E169098 CRC64; MRAALVGVDF GQGDFAASIE ELMLLARSAG AEPVTTITGK RSAPDAAYFV GSGKADEIGH AVRDYKLEIV IFNHALSPAQ QRNLEKRLNV RVLDRTSLIL DIFAQRAQSH EGKVQVELAQ LQHLATRLVR GWTHLERQKG GIGLRGPGET QLETDRRLLG ERVKMLRAKL AKLRKQHETQ RRARGRNHTF SVSLVGYTNA GKSTLFNSLT KAGVYVADQL FATLDTTSRR VYMGEEIGNV VLSDTVGFVR ELPHQLVAAF RATLEETIHA DLLLHVVDGA SPSRMEQIEQ VNLVLREIGA DHIPQILVWN KIDAAGLEPA VERNEYDKIS RVFISARTGE GLNLLRDAIC EAARDEQEAL ANPKEEVAPD SILTFTQVGS H // ID A0A0Q8UXK3_9MICO Unreviewed; 513 AA. AC A0A0Q8UXK3; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 05-JUL-2017, entry version 12. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=ASE16_13755 {ECO:0000313|EMBL:KRC49989.1}; OS Leifsonia sp. Root227. OC Bacteria; Actinobacteria; Micrococcales; Microbacteriaceae; Leifsonia. OX NCBI_TaxID=1736496 {ECO:0000313|EMBL:KRC49989.1, ECO:0000313|Proteomes:UP000051819}; RN [1] {ECO:0000313|EMBL:KRC49989.1, ECO:0000313|Proteomes:UP000051819} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Root227 {ECO:0000313|EMBL:KRC49989.1, RC ECO:0000313|Proteomes:UP000051819}; RA Millard Andrew; RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:KRC49989.1, ECO:0000313|Proteomes:UP000051819} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Root227 {ECO:0000313|EMBL:KRC49989.1, RC ECO:0000313|Proteomes:UP000051819}; RA Vorholt J.; RT "Functional overlap of the Arabidopsis leaf and root microbiotas."; RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KRC49989.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LMIO01000003; KRC49989.1; -; Genomic_DNA. DR EnsemblBacteria; KRC49989; KRC49989; ASE16_13755. DR Proteomes; UP000051819; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 2. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000051819}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000051819}. FT DOMAIN 291 456 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 513 AA; 55277 MW; D6191BD6C1CE541D CRC64; MSTEETPTAD QPTDTSRDAD VVARVLAAAE SRAGMTLFGG GAQALQTEHT DDAGHDGEQF EREERAALRR VSGLSTELED VTEVEYRQLR LENVVLIGVY SQGSLQDAEN SIRELAALAE TAGAVVLDGL LQRRPHPDPS TYLGKGKAQE LAGVVAALGA DTVIADTELA PSQRRALEDV VKVKVIDRTA VILDIFSQHA KSREGKAQVE LAQLEYLLPR LRGWGESMSR QAGGQVGGAG AGMGSRGPGE TKIELDRRRI HTRMAKLRKQ IAGFKPAREA KRANRNRNAV PSVAIAGYTN AGKSSLLNRI TKAGVLVENA LFATLDATVR KSVTADGRLY TLADTVGFVR NLPHQLVEAF RSTLEEVAES DVIVHVVDGS HPDPASQLAT VRDVIGEVGA RELPEIVVFN KSDLITPDDR LVLRGLEPGA IFASARTGEG IDEILAAIAR LLPDHSVEVD LVVPYDRGDL ISALHERGRV VSTEYVEDGT RVRARVMPEY LSVFEAFAVE PTA // ID A0A0Q8VQ67_9ACTN Unreviewed; 503 AA. AC A0A0Q8VQ67; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 07-JUN-2017, entry version 10. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=ASE19_01025 {ECO:0000313|EMBL:KRC59637.1}; OS Nocardioides sp. Root79. OC Bacteria; Actinobacteria; Propionibacteriales; Nocardioidaceae; OC Nocardioides. OX NCBI_TaxID=1736600 {ECO:0000313|EMBL:KRC59637.1, ECO:0000313|Proteomes:UP000051414}; RN [1] {ECO:0000313|EMBL:KRC59637.1, ECO:0000313|Proteomes:UP000051414} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Root79 {ECO:0000313|EMBL:KRC59637.1, RC ECO:0000313|Proteomes:UP000051414}; RA Millard Andrew; RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:KRC59637.1, ECO:0000313|Proteomes:UP000051414} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Root79 {ECO:0000313|EMBL:KRC59637.1, RC ECO:0000313|Proteomes:UP000051414}; RA Vorholt J.; RT "Functional overlap of the Arabidopsis leaf and root microbiotas."; RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KRC59637.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LMIP01000001; KRC59637.1; -; Genomic_DNA. DR RefSeq; WP_056896704.1; NZ_LMIP01000001.1. DR EnsemblBacteria; KRC59637; KRC59637; ASE19_01025. DR Proteomes; UP000051414; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 2. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000313|EMBL:KRC59637.1}; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000051414}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900, KW ECO:0000313|EMBL:KRC59637.1}. FT DOMAIN 285 450 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 244 278 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 503 AA; 54684 MW; 6874C01F13CAF71C CRC64; MTNHAEDFSL AAALRATEGW DDPEDLVDEL EADDESADTG FVSGYADDPT TGDLDLVERH ELRRVAGLRT ELEDITEVEY RQLRLERVVL VGVWTEGSIA DIENAMAELA LLAETAGSEV LDAIYQRRQS PDPATYIGRG KVEGLREIVQ ATGADTVICD GELAPSQLRN LEDKVKVKVV DRTALILDIF AQHAKSKEGQ AQVELAQLSY MKQRLRGWGG NLSRQAGGRV GADGGGIGGR GPGETKIETD RRRINDKIAK LRRELKVMKG TRDTKRQERR RNEIPSVAIA GYTNAGKSSL LNRLTGAGVL VEDALFATLD PTTRRTTTSD GRVFTMSDTV GFVRHLPHQL VEAFRSTLEE VADADLIVHV VDGSHPDPEG QLTAVREVLA EIEAGDIPEL VIINKVDAAD PLVVDRVLRR EPHAIAVSAH TGEGIDRAIA AIEADLPRPR VEFTALVPYA RGDLIDRIHK DGEITTLEHT ADGTQVSGRA TEALAGELAA YAV // ID A0A0Q8XIQ5_9SPHN Unreviewed; 430 AA. AC A0A0Q8XIQ5; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=ASE13_07345 {ECO:0000313|EMBL:KRC82138.1}; OS Sphingomonas sp. Root241. OC Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales; OC Sphingomonadaceae; Sphingomonas. OX NCBI_TaxID=1736501 {ECO:0000313|EMBL:KRC82138.1, ECO:0000313|Proteomes:UP000051629}; RN [1] {ECO:0000313|EMBL:KRC82138.1, ECO:0000313|Proteomes:UP000051629} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Root241 {ECO:0000313|EMBL:KRC82138.1, RC ECO:0000313|Proteomes:UP000051629}; RA Millard Andrew; RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:KRC82138.1, ECO:0000313|Proteomes:UP000051629} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Root241 {ECO:0000313|EMBL:KRC82138.1, RC ECO:0000313|Proteomes:UP000051629}; RA Vorholt J.; RT "Functional overlap of the Arabidopsis leaf and root microbiotas."; RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KRC82138.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LMIV01000001; KRC82138.1; -; Genomic_DNA. DR RefSeq; WP_056613119.1; NZ_LMIV01000001.1. DR EnsemblBacteria; KRC82138; KRC82138; ASE13_07345. DR Proteomes; UP000051629; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000051629}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000051629}. FT DOMAIN 208 377 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 430 AA; 47496 MW; A02B2D775D667E39 CRC64; MSTGFDRDAD EFSRGARAIV VYPEMGGSSR DAEARLEETA GLAAAIGVEV REKVAVKLRQ PKPGTLIGSG QVDAIAETVR DQELQLAVFD AALTPVQQRN LETALGCKVI DRTGLILEIF GERARTAEGR LQVELAHLDY QAGRLVRSWT HLERQRGGFG FLGGPGETQI EADRRLIRDR MARLRKELDQ VSRTRTLHRD RRQRAPWPVI ALVGYTNAGK STLFNRLTGS DVMAEDLLFA TLDPTLRQIS LPGIDKAILS DTVGFVSELP TQLVAAFKAT LEEVVSADLL IHVRDIAHPD SEAQRADVEK VLSEIGVAEA TPRFEAWNKL DLLDGERRAQ LLEDAGKRDD VMPISAVTGE GVDTLIETVA ARLTEGHRRY TIALDPADGA GAAWLHQHGE VIEQRVEGPQ SVYEVRMAPR DYERFETRRA // ID A0A0Q9CJP8_9CELL Unreviewed; 507 AA. AC A0A0Q9CJP8; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 30-AUG-2017, entry version 17. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=ASE38_19305 {ECO:0000313|EMBL:KRD41700.1}; OS Cellulomonas sp. Root930. OC Bacteria; Actinobacteria; Micrococcales; Cellulomonadaceae; OC Cellulomonas. OX NCBI_TaxID=1736609 {ECO:0000313|EMBL:KRD41700.1, ECO:0000313|Proteomes:UP000051941}; RN [1] {ECO:0000313|EMBL:KRD41700.1, ECO:0000313|Proteomes:UP000051941} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Root930 {ECO:0000313|EMBL:KRD41700.1, RC ECO:0000313|Proteomes:UP000051941}; RA Millard Andrew; RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:KRD41700.1, ECO:0000313|Proteomes:UP000051941} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Root930 {ECO:0000313|EMBL:KRD41700.1, RC ECO:0000313|Proteomes:UP000051941}; RA Vorholt J.; RT "Functional overlap of the Arabidopsis leaf and root microbiotas."; RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KRD41700.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LMJI01000002; KRD41700.1; -; Genomic_DNA. DR RefSeq; WP_056093335.1; NZ_LMJI01000002.1. DR EnsemblBacteria; KRD41700; KRD41700; ASE38_19305. DR Proteomes; UP000051941; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 2. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000051941}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}. FT DOMAIN 285 451 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 507 AA; 54415 MW; 4FB4B724F54F1057 CRC64; MTDAQHTTSQ TEDTPTARSA QEVADDVVAR VLARAGSTLH AGATVHSSYD GDQLDLEERT SLRRVAGLST ELEDVTEVEY RQLRLEKVVL VGVWGSGTVT DAEISLRELA QLAETAGSQV LDGLLQRRQK PDPGTYLGSG KAAELATLVA AVGADTVVVD GELAPSQRRA LEDIVRVKVV DRTALILDIF AQHAKSREGK AQVELAQLEY LLPRLRGWGD SMSRQAGGQV GGAAAGMGSR GPGETKIELD RRRIRNRMAK LRREIAAMEP GRVTKRASRK KHAIPSVAIA GYTNAGKSSL LNRITHAGVL VENALFATLD PTVRRAETVD GRIYTLADTV GFVRALPHQL VEAFRSTLEE VADADLILHV VDASHPDPEG QIAAVRHVFA DIPGAMDVPE IIVLNKADVA TPEAIARLRS REVHSIVVSA HSGEGIEELQ ALIADQLPRP GVSVDLVVPY HRGDLISRVH EHGDIQTEDH TADGTAIRAR VDAGLAAELE AAAQPRP // ID A0A0Q9CNR4_9CELL Unreviewed; 510 AA. AC A0A0Q9CNR4; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=ASE27_06170 {ECO:0000313|EMBL:KRD40467.1}; OS Oerskovia sp. Root918. OC Bacteria; Actinobacteria; Micrococcales; Cellulomonadaceae; Oerskovia. OX NCBI_TaxID=1736607 {ECO:0000313|EMBL:KRD40467.1, ECO:0000313|Proteomes:UP000051694}; RN [1] {ECO:0000313|EMBL:KRD40467.1, ECO:0000313|Proteomes:UP000051694} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Root918 {ECO:0000313|EMBL:KRD40467.1, RC ECO:0000313|Proteomes:UP000051694}; RA Millard Andrew; RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:KRD40467.1, ECO:0000313|Proteomes:UP000051694} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Root918 {ECO:0000313|EMBL:KRD40467.1, RC ECO:0000313|Proteomes:UP000051694}; RA Vorholt J.; RT "Functional overlap of the Arabidopsis leaf and root microbiotas."; RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KRD40467.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LMJG01000011; KRD40467.1; -; Genomic_DNA. DR RefSeq; WP_056648802.1; NZ_LMJG01000011.1. DR EnsemblBacteria; KRD40467; KRD40467; ASE27_06170. DR Proteomes; UP000051694; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 2. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000051694}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000051694}. FT DOMAIN 289 455 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 510 AA; 54846 MW; B61C1514AFE19312 CRC64; MTQTPANPTP ETSPETVERP ERDIAGDVVA RVLARAGTAR AEGGTQHSVY DGEQLELAER TALRRVANLS TELEDVTEVE YRQLRLEKVV LVGLYTGSGD AAAAEAEVSL RELAALAETA GSQVLDGVLQ RRQKPDPGTY LGSGKAAELA AVVAATGADT VVIDGELAPS QRRALEDIVK VKVVDRTALI LDIFAQHAKS REGKAQVELA QLEYLLPRLR GWGESMSRQA GGQVGGAGAG MGSRGPGETK IELDRRRIRD RMTKLRREIA AMAPARETKR SSRKRHAIPS VAIAGYTNAG KSSLLNALTG AGVLVENALF ATLDPTVRRA QTEDGRVYTL ADTVGFVRAL PHQLVEAFRS TLEEVGQADL LLHVVDASHP DPEGQIAAVR HVLADIPGID QVLEVVVLNK VDIADPDVVA RIRGRERRTI VVSAHTGQGI DDLLQLISDE LPRPDVSVDL VVPYHRGDLV NRVHLTGEID LEEHVETGTR LLARVDEGLA LELHAVAVRA // ID A0A0Q9D205_9RHIZ Unreviewed; 441 AA. AC A0A0Q9D205; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 07-JUN-2017, entry version 12. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=ASE60_20055 {ECO:0000313|EMBL:KRD48871.1}; OS Ensifer sp. Root278. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Rhizobiaceae; Sinorhizobium/Ensifer group; Ensifer. OX NCBI_TaxID=1736509 {ECO:0000313|EMBL:KRD48871.1, ECO:0000313|Proteomes:UP000051719}; RN [1] {ECO:0000313|EMBL:KRD48871.1, ECO:0000313|Proteomes:UP000051719} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Root278 {ECO:0000313|EMBL:KRD48871.1, RC ECO:0000313|Proteomes:UP000051719}; RA Millard Andrew; RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:KRD48871.1, ECO:0000313|Proteomes:UP000051719} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Root278 {ECO:0000313|EMBL:KRD48871.1, RC ECO:0000313|Proteomes:UP000051719}; RA Vorholt J.; RT "Functional overlap of the Arabidopsis leaf and root microbiotas."; RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KRD48871.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LMJJ01000044; KRD48871.1; -; Genomic_DNA. DR RefSeq; WP_057255688.1; NZ_LMJJ01000044.1. DR EnsemblBacteria; KRD48871; KRD48871; ASE60_20055. DR Proteomes; UP000051719; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000051719}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000051719}. FT DOMAIN 205 377 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 164 198 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 441 AA; 48755 MW; 525960A9440A5277 CRC64; MRAVVIVPVL KKTGRQSADI LSTTTTRTDE SRLEEATGLA MAIDLEVVHG AIVPVSQPKP GTLLGSGKIE EIGHILVELD AGLVIVDHPL TPVQQRNLEK EWNAKVIDRT GLILEIFGRR ASTKEGTLQV DLAHLNYQKG RLVRSWTHLE RQRGGGGFMG GPGETQIEAD RRLLQDRIVK LERELEQVRR TRQLHRSKRK KVPHPIVALV GYTNAGKSTL FNRMTGAGVL AEDMLFATLD PTLRRLKLPH GRMVILSDTV GFISDLPTHL VAAFRATLEE VLEADLILHV RDLSDPDNQA QASDVLRILA DLGIDEKEAS ERLIEVWNKI DRLDTESREA LQSKAATSGN TVAVSAITGE GVDELLGEIG RRLSGVLTEC TVVLGIDQLQ LLPWVYQHAI VDGREDLEDG RVSLELRLTE NEAADLERRL GNGPKPVEED W // ID A0A0Q9EHR6_9GAMM Unreviewed; 435 AA. AC A0A0Q9EHR6; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=ASE45_12675 {ECO:0000313|EMBL:KRD67609.1}; OS Lysobacter sp. Root96. OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales; OC Xanthomonadaceae; Lysobacter. OX NCBI_TaxID=1736612 {ECO:0000313|EMBL:KRD67609.1, ECO:0000313|Proteomes:UP000050805}; RN [1] {ECO:0000313|EMBL:KRD67609.1, ECO:0000313|Proteomes:UP000050805} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Root96 {ECO:0000313|EMBL:KRD67609.1, RC ECO:0000313|Proteomes:UP000050805}; RA Millard Andrew; RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:KRD67609.1, ECO:0000313|Proteomes:UP000050805} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Root96 {ECO:0000313|EMBL:KRD67609.1, RC ECO:0000313|Proteomes:UP000050805}; RA Vorholt J.; RT "Functional overlap of the Arabidopsis leaf and root microbiotas."; RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KRD67609.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LMJN01000003; KRD67609.1; -; Genomic_DNA. DR RefSeq; WP_055901095.1; NZ_LMJN01000003.1. DR EnsemblBacteria; KRD67609; KRD67609; ASE45_12675. DR Proteomes; UP000050805; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000050805}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000050805}. FT DOMAIN 199 364 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 158 192 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 435 AA; 47726 MW; 31551D87C23D227E CRC64; MFERSRKGEH ALLIQPHAGG PPEEGLLEEF ADLAKSAGAT VAAVLTARID RPNAAMLIGS GKLAEVKAAA DATGADLILV NHPLSPGQER NLERALERRV VDRTGLILDI FSQRAHSAEG KLQVELAQLK HMATRLVRGW THLERQRGGS IGLRGPGETQ LETDRRLLQK RLEQLQKRLD KVEVQRTQMR RARVRSELPR VALVGYTNAG KSTLFNALTG AEAYAADQLF ATLDPTVRRI ELSGGGVVLA DTVGFVRDLP HELVAAFRST LSESREADLL IHVIDAADPL RDERVAQVDS VLQEIGAGDL PQLLVFNKID RLDGLQPRID RPGEGHTRVW LSAREGRGLD LLRTALAEAL ELRHVAGRLR VPSQAARLRA RLHELGAVRN ELADEHGWEL EVDLAIADAQ RLFAQPHGEP LRSLLESVAV PDDLA // ID A0A0Q9HTD5_9BRAD Unreviewed; 460 AA. AC A0A0Q9HTD5; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=ASE63_06515 {ECO:0000313|EMBL:KRE05957.1}; OS Bosea sp. Root381. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Bradyrhizobiaceae; Bosea. OX NCBI_TaxID=1736524 {ECO:0000313|EMBL:KRE05957.1, ECO:0000313|Proteomes:UP000050937}; RN [1] {ECO:0000313|EMBL:KRE05957.1, ECO:0000313|Proteomes:UP000050937} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Root381 {ECO:0000313|EMBL:KRE05957.1, RC ECO:0000313|Proteomes:UP000050937}; RA Millard Andrew; RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:KRE05957.1, ECO:0000313|Proteomes:UP000050937} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Root381 {ECO:0000313|EMBL:KRE05957.1, RC ECO:0000313|Proteomes:UP000050937}; RA Vorholt J.; RT "Functional overlap of the Arabidopsis leaf and root microbiotas."; RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KRE05957.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LMJT01000023; KRE05957.1; -; Genomic_DNA. DR RefSeq; WP_056804429.1; NZ_LMJT01000023.1. DR EnsemblBacteria; KRE05957; KRE05957; ASE63_06515. DR Proteomes; UP000050937; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000050937}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000050937}. FT DOMAIN 226 400 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 460 AA; 50548 MW; A1EE7F1828C1C0F5 CRC64; MGARSDADEA RAATKPLDAI EREIAANTRA FVVGPYLQRR GAADANQRSF AARLDEAVGL AAAIDLTVVE PIQVMLTALR PATYLGTGKV EEIAERIKLE EIGLVVMDCA LSPVQQRNLE KAFGCKVIDR TGLILEIFGR RARTKEGALQ VELAHLNYQK SRLVRSWTHL ERQRGGFGFL GGPGETQIEA DRRIIQERMT KIERDLESVK RTRSLHRASR KRVPYPVVAL VGYTNAGKST LFNRLTSAEV LAQDMLFATL DPTARAIKLP HGARIMLSDT VGFISDLPTQ LVAAFRATLE DAIEADVLLH VRDVAHEDTQ AQAADVQAIL RDLGIDPDDG QRVIEVWNKS DLLDAAERER QLGLAGLKPD ASRPVLVSAL TGDGVGRLTD SIEARIALRR PVYRVLLAPG DGKSLAWLHA NGEILHREDA EDGELSLEVR LPPEREGAFA ARFPQAQRLN // ID A0A0Q9I8X2_9BRAD Unreviewed; 453 AA. AC A0A0Q9I8X2; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 05-JUL-2017, entry version 12. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=ASE66_21135 {ECO:0000313|EMBL:KRE13398.1}; OS Bosea sp. Root483D1. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Bradyrhizobiaceae; Bosea. OX NCBI_TaxID=1736544 {ECO:0000313|EMBL:KRE13398.1, ECO:0000313|Proteomes:UP000051771}; RN [1] {ECO:0000313|EMBL:KRE13398.1, ECO:0000313|Proteomes:UP000051771} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Root483D1 {ECO:0000313|EMBL:KRE13398.1, RC ECO:0000313|Proteomes:UP000051771}; RA Millard Andrew; RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:KRE13398.1, ECO:0000313|Proteomes:UP000051771} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Root483D1 {ECO:0000313|EMBL:KRE13398.1, RC ECO:0000313|Proteomes:UP000051771}; RA Vorholt J.; RT "Functional overlap of the Arabidopsis leaf and root microbiotas."; RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KRE13398.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LMJW01000022; KRE13398.1; -; Genomic_DNA. DR EnsemblBacteria; KRE13398; KRE13398; ASE66_21135. DR Proteomes; UP000051771; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000051771}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000051771}. FT DOMAIN 219 393 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 453 AA; 49806 MW; 4C06B726B50EE8BE CRC64; MGISIDAAEH ALAADTRAFV VGPYLARHAA SRAATADENQ RNHAARLDEA FGLASAIDLQ IVEAIPVVLT ALRPATYLGK GKVEELSERV KIEEIGLVVM DCALSPVQQR NLEKTFGCKV IDRTGLILEI FGRRARTREG ALQVELAHLN YQKSRLVRSW THLERQRGGF GFLGGPGETQ IEADRRIIQE RMTKIERDLD SVKRTRSLHR ASRKRVPYPV VALVGYTNAG KSTLFNRLTS AEVLAQDMLF ATLDPTARAL KLPHGARIML SDTVGFISEL PTQLVAAFRA TLEDAIEADV LLHVRDVSHE DTQAQAADVQ GILRDLGIDP EDGDRVIEVW NKADLLSGEE RERQGALTAL KPGASRPVLV SALTGEGMER LTDAIEQRIA RARPVYRLIL EPGDGKSLAW LHANGEILER EDAEDGALSL LVRLPPEREG TFGARFPQAE RIG // ID A0A0Q9JB22_9MICO Unreviewed; 509 AA. AC A0A0Q9JB22; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=ASG80_05850 {ECO:0000313|EMBL:KRE26302.1}; OS Agromyces sp. Soil535. OC Bacteria; Actinobacteria; Micrococcales; Microbacteriaceae; Agromyces. OX NCBI_TaxID=1736390 {ECO:0000313|EMBL:KRE26302.1, ECO:0000313|Proteomes:UP000051793}; RN [1] {ECO:0000313|EMBL:KRE26302.1, ECO:0000313|Proteomes:UP000051793} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Soil535 {ECO:0000313|EMBL:KRE26302.1, RC ECO:0000313|Proteomes:UP000051793}; RA Millard Andrew; RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:KRE26302.1, ECO:0000313|Proteomes:UP000051793} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Soil535 {ECO:0000313|EMBL:KRE26302.1, RC ECO:0000313|Proteomes:UP000051793}; RA Vorholt J.; RT "Functional overlap of the Arabidopsis leaf and root microbiotas."; RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KRE26302.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LMRW01000012; KRE26302.1; -; Genomic_DNA. DR RefSeq; WP_056730789.1; NZ_LMRW01000012.1. DR EnsemblBacteria; KRE26302; KRE26302; ASG80_05850. DR Proteomes; UP000051793; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 2. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000051793}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000051793}. FT DOMAIN 286 451 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 509 AA; 54709 MW; 4744EB9FE00FF9F8 CRC64; MNEAEQRTAD DAVERVLRSA ESRAGVARFG AGDASAIQRE WSDAAGGDST DGEQYDREER AALRRVSGLS TELEDVTEVE YRQLRLENVV LIGVYSQGAQ DDAENSLREL AALAETAGAR VLDGLLQRRP NPDPSTYLGS GKAEELRHIV AALGADTVIA DTELAPSQRR ALEDVVKVKV IDRTAVILDI FSQHAKSREG KAQVELAQLE YLLPRLRGWG ESMSRQAGGQ VGGTGAGMGS RGPGETKIEL DRRRIHSRMA RLRKQIAGMK PAREAKRANR RRHAVPSVAI AGYTNAGKSS LLNRITGAGV LVENALFATL DATVRRNTTA DGRVYTIADT VGFVRNLPHQ LVEAFRSTLE EVGGADLIVH VVDAAHPDPA GQIATVRDVI GEVGARDIPE LVVFNKSDLV SPEERLVLRG LEPNAVFASA RTGEGVPEVL AAIGRMLPDP AVEVDLLVPY DRGDVVSTLH ETGRVLSVRY VEEGTRIRAL ASPEQAAQLA EFAAASVPA // ID A0A0Q9JBU5_9BACL Unreviewed; 429 AA. AC A0A0Q9JBU5; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=ASG81_27145 {ECO:0000313|EMBL:KRE25048.1}; OS Paenibacillus sp. Soil522. OC Bacteria; Firmicutes; Bacilli; Bacillales; Paenibacillaceae; OC Paenibacillus. OX NCBI_TaxID=1736388 {ECO:0000313|EMBL:KRE25048.1, ECO:0000313|Proteomes:UP000051180}; RN [1] {ECO:0000313|EMBL:KRE25048.1, ECO:0000313|Proteomes:UP000051180} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Soil522 {ECO:0000313|EMBL:KRE25048.1, RC ECO:0000313|Proteomes:UP000051180}; RA Millard Andrew; RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:KRE25048.1, ECO:0000313|Proteomes:UP000051180} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Soil522 {ECO:0000313|EMBL:KRE25048.1, RC ECO:0000313|Proteomes:UP000051180}; RA Vorholt J.; RT "Functional overlap of the Arabidopsis leaf and root microbiotas."; RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KRE25048.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LMRV01000099; KRE25048.1; -; Genomic_DNA. DR RefSeq; WP_056642036.1; NZ_LMRV01000099.1. DR EnsemblBacteria; KRE25048; KRE25048; ASG81_27145. DR Proteomes; UP000051180; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000051180}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000051180}. FT DOMAIN 208 374 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 429 AA; 47779 MW; 8F09D469C51C0668 CRC64; MSEKTFDTNP NMTEKAILVS LVTSNDKRYG GDPEMSLQEL VQLTETAGVE VLTTITQNKE TADSKWFIGK GKVEEVKALA DELGATTAIF DQELSGAQVR NLEESLDLKI VDRTQLILDI FAGRAKTREG IIQVELAQLS YLLPRLSGQS KNLSRLGGGI GTRGPGETKL ETDRRHIRDR IFDLKTLLEE VVRHRKLHRE RRKKSGVIQV ALVGYTNAGK STLLRELTQA DVYVENQLFA TLDPTSRTLE LPNGREVVIT DTVGFIQNLP HDLVAAFRAT LEEVCEADLV LHVIDSSSPM RDEQIAVVNK ILGDLGAADK PYVMVYNKKD MCINNGTLAD LPITSGDNLV ISAYEADDLE LLKQTIQDKL SGDTLTFLVP AERGDLIALA YRSGEVINQE VEEELLRLTV QVSKQEYEQH GQRLKQYME // ID A0A0Q9KLT0_9MICO Unreviewed; 483 AA. AC A0A0Q9KLT0; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 05-JUL-2017, entry version 12. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=ASG73_09865 {ECO:0000313|EMBL:KRE38121.1}; OS Janibacter sp. Soil728. OC Bacteria; Actinobacteria; Micrococcales; Intrasporangiaceae; OC Janibacter. OX NCBI_TaxID=1736393 {ECO:0000313|EMBL:KRE38121.1, ECO:0000313|Proteomes:UP000051572}; RN [1] {ECO:0000313|EMBL:KRE38121.1, ECO:0000313|Proteomes:UP000051572} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Soil728 {ECO:0000313|EMBL:KRE38121.1, RC ECO:0000313|Proteomes:UP000051572}; RA Millard Andrew; RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:KRE38121.1, ECO:0000313|Proteomes:UP000051572} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Soil728 {ECO:0000313|EMBL:KRE38121.1, RC ECO:0000313|Proteomes:UP000051572}; RA Vorholt J.; RT "Functional overlap of the Arabidopsis leaf and root microbiotas."; RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KRE38121.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LMRZ01000004; KRE38121.1; -; Genomic_DNA. DR EnsemblBacteria; KRE38121; KRE38121; ASG73_09865. DR Proteomes; UP000051572; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 2. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000051572}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000051572}. FT DOMAIN 263 428 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 483 AA; 52573 MW; 78CA2FAFC4F40EED CRC64; MDATIDRVLS RRAQALADDD GFVDGGTYDG DQLDREERSA LRRVQGLSTE LEDITEVEYR QLRLERVVLA AVWTQGSVED AENSMRELAA LAETAGSEVL EGVLQRRQNP DPGTYLGSGK ALELRDIVVA QGADTVVCDT ELSPSQRRAL EDVVKVKVID RTALILDIFA QHAQSREGRA QVELAQLQYL LPRLRGWGES MSRQAGGQAA GGQGMGSRGP GETKIELDRR RINTRIAKLK RDIAGMKTHR DTKRSSRRSN GTPSVVIAGY TNAGKSTLLN RLTHAGVLVD NQLFATLDTT VRRSETVDGR EFTLADTVGF VRELPPQLVE AFRSTLEEVG EADLLLHVVD GSHPDPEGQI SAVRGVLAEV DATDVKEVIV INKADAADPE VIDRILLHEK HSLAVSARTG KGIPELLTLI AEELPKPDID VEVLVPYARG DLISRLHDEA EILSEDHVAE GTRVAARVHP DLASELTPFA AAG // ID A0A0Q9KPF2_9MICO Unreviewed; 496 AA. AC A0A0Q9KPF2; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=ASG74_00695 {ECO:0000313|EMBL:KRE43405.1}; OS Knoellia sp. Soil729. OC Bacteria; Actinobacteria; Micrococcales; Intrasporangiaceae; Knoellia. OX NCBI_TaxID=1736394 {ECO:0000313|EMBL:KRE43405.1, ECO:0000313|Proteomes:UP000051965}; RN [1] {ECO:0000313|EMBL:KRE43405.1, ECO:0000313|Proteomes:UP000051965} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Soil729 {ECO:0000313|EMBL:KRE43405.1, RC ECO:0000313|Proteomes:UP000051965}; RA Millard Andrew; RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:KRE43405.1, ECO:0000313|Proteomes:UP000051965} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Soil729 {ECO:0000313|EMBL:KRE43405.1, RC ECO:0000313|Proteomes:UP000051965}; RA Vorholt J.; RT "Functional overlap of the Arabidopsis leaf and root microbiotas."; RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KRE43405.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LMSA01000001; KRE43405.1; -; Genomic_DNA. DR RefSeq; WP_056137935.1; NZ_LMSA01000001.1. DR EnsemblBacteria; KRE43405; KRE43405; ASG74_00695. DR Proteomes; UP000051965; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 2. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000051965}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000051965}. FT DOMAIN 278 443 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 496 AA; 53847 MW; 70426ECE51861F34 CRC64; MTARHHIFSG QADALSDDAY DDDGFVIDDE GDDSASSAPS ALYDGDQLER EERAALRRVA GLSTELEDIS EVEYRQLRLE RVVLASVWSE GSLVDAENSM RELAALAETA GAEVLDGVMQ RRQKPDTATY LGKGKAEELH DIVVAEGADT VICDSELAPS QRRALEDVVK VKVIDRTALI LDIFAQHAKS REGKAQVELA QLQYLLPRLR GWGESMSRQA GGQAAGGQGM GSRGPGETKI ELDRRRINTR VAKLKREIAG MKVHRDTKRG SRRANAIPSV AIAGYTNAGK SSILNRLTGA GVLVQNQLFA TLDPTVRRGE TPDGREFTFT DTVGFVRALP HQLVEAFRST LEEVAESDLL LHVVDGSHPD PEGQISAVRS VLADVDATDV KEVIVVNKSD IADPEVMDRL LRNEKHVIAV SARTGEGMDA LVRLIAEELP QPDISVDVLV PYDRGDLVSR LHEEGEILAS EHVGEGTRVT AKVNADLAAE LTAYKA // ID A0A0Q9L3M3_9BACL Unreviewed; 421 AA. AC A0A0Q9L3M3; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=ASG81_07220 {ECO:0000313|EMBL:KRE48108.1}; OS Paenibacillus sp. Soil522. OC Bacteria; Firmicutes; Bacilli; Bacillales; Paenibacillaceae; OC Paenibacillus. OX NCBI_TaxID=1736388 {ECO:0000313|EMBL:KRE48108.1, ECO:0000313|Proteomes:UP000051180}; RN [1] {ECO:0000313|EMBL:KRE48108.1, ECO:0000313|Proteomes:UP000051180} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Soil522 {ECO:0000313|EMBL:KRE48108.1, RC ECO:0000313|Proteomes:UP000051180}; RA Millard Andrew; RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:KRE48108.1, ECO:0000313|Proteomes:UP000051180} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Soil522 {ECO:0000313|EMBL:KRE48108.1, RC ECO:0000313|Proteomes:UP000051180}; RA Vorholt J.; RT "Functional overlap of the Arabidopsis leaf and root microbiotas."; RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KRE48108.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LMRV01000030; KRE48108.1; -; Genomic_DNA. DR RefSeq; WP_056631157.1; NZ_LMRV01000030.1. DR EnsemblBacteria; KRE48108; KRE48108; ASG81_07220. DR Proteomes; UP000051180; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000051180}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000051180}. FT DOMAIN 198 366 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 157 191 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 421 AA; 47733 MW; B0EE9D5E2ACD39D6 CRC64; MEQPQQKAII VGVQLQNQTD FSYSMEELRN LAAACYIEVV DELSQKAARI NPSHYIGTGK IQELLALLEA HDAHVVIFND ELSPSQIRNL EAALERTVID RTILILDIFA ERAKTREAQL QVEVARLQYM LPRLVGLRAS LGRQGGGAGL KNRGAGETKL ELDRRRIEER ITALQAELDK LVARRQIQRK QRQKNEVPVV CLVGYTNTGK SSLMNALLEK CNPGTNKLVF AQDMLFATLE TSVRSIELQD NKSFLLTDTV GFVSQLPHHL VKAFRSTLEE VAEADLLVHV VDYSHEDYEQ LVSVTNDTLK ELGAHHIPTI YAYNKCDLTE HAYPAVQDDK IYLSAKKKSG LDELISLIRG HIFDDYMECE LLIPFSQGRL VAYFNEHAHV QSTDYEPEGT RMKLECRVAD FERYRNEVIV L // ID A0A0Q9LVV7_9MICO Unreviewed; 489 AA. AC A0A0Q9LVV7; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=ASG70_12480 {ECO:0000313|EMBL:KRE53887.1}; OS Phycicoccus sp. Soil748. OC Bacteria; Actinobacteria; Micrococcales; Intrasporangiaceae; OC Phycicoccus. OX NCBI_TaxID=1736397 {ECO:0000313|EMBL:KRE53887.1, ECO:0000313|Proteomes:UP000051855}; RN [1] {ECO:0000313|EMBL:KRE53887.1, ECO:0000313|Proteomes:UP000051855} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Soil748 {ECO:0000313|EMBL:KRE53887.1, RC ECO:0000313|Proteomes:UP000051855}; RA Millard Andrew; RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:KRE53887.1, ECO:0000313|Proteomes:UP000051855} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Soil748 {ECO:0000313|EMBL:KRE53887.1, RC ECO:0000313|Proteomes:UP000051855}; RA Vorholt J.; RT "Functional overlap of the Arabidopsis leaf and root microbiotas."; RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KRE53887.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LMSC01000009; KRE53887.1; -; Genomic_DNA. DR RefSeq; WP_056884658.1; NZ_LMSC01000009.1. DR EnsemblBacteria; KRE53887; KRE53887; ASG70_12480. DR Proteomes; UP000051855; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 2. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000051855}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000051855}. FT DOMAIN 271 436 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 489 AA; 53372 MW; 2220735B42976D64 CRC64; MTPRSDIFDF RAAALAEETA TPRTGGDLGP QDGQGFDGDQ YDREERAALR RVAGLSTELE DVTEVEYRQL RLERVVLAAV WTEGTAEDAD NSLRELAALA ETAGSTVLAG LVQRRDRPDT GTYLGSGKAQ ELRDVVIAEG ADTVICDTEL TPSQRRALED VVKVKVIDRT ALILDIFAQH AKSKEGKAQV ELAQLQYLLP RLRGWGESMS RQAGGQAAGG QGMGSRGPGE TKIELDRRRI NTRMAKLRRE IKEMKTSRDT RRLSRKAHEV PSVAIAGYTN AGKSSLLNRL TGAGVLVENQ LFATLDPTVR RAETEDGRLY TLADTVGFVR QLPTQLVEAF RSTLEEVADA DLLLHVVDGS HPDPEGQISA VRAVLADVDA ADVKEVVVVN KADAADPEVL DRLRRHEKHC IVVSARTGAG LAELRALIAD ELPRPDIDVE VLLPYDRGDL VSRLHEEAEV LSSEHTERGT HVKARVHPEL ASELADFAA // ID A0A0Q9M6Y7_9MICC Unreviewed; 525 AA. AC A0A0Q9M6Y7; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=ASG92_20260 {ECO:0000313|EMBL:KRE61879.1}; OS Arthrobacter sp. Soil736. OC Bacteria; Actinobacteria; Micrococcales; Micrococcaceae; Arthrobacter. OX NCBI_TaxID=1736395 {ECO:0000313|EMBL:KRE61879.1, ECO:0000313|Proteomes:UP000051775}; RN [1] {ECO:0000313|EMBL:KRE61879.1, ECO:0000313|Proteomes:UP000051775} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Soil736 {ECO:0000313|EMBL:KRE61879.1, RC ECO:0000313|Proteomes:UP000051775}; RA Millard Andrew; RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:KRE61879.1, ECO:0000313|Proteomes:UP000051775} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Soil736 {ECO:0000313|EMBL:KRE61879.1, RC ECO:0000313|Proteomes:UP000051775}; RA Vorholt J.; RT "Functional overlap of the Arabidopsis leaf and root microbiotas."; RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KRE61879.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LMSB01000014; KRE61879.1; -; Genomic_DNA. DR RefSeq; WP_056627834.1; NZ_LMSB01000014.1. DR EnsemblBacteria; KRE61879; KRE61879; ASG92_20260. DR Proteomes; UP000051775; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000051775}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000051775}. FT DOMAIN 304 469 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 525 AA; 56755 MW; E44D4053165466FA CRC64; MTSQQNSGSE PAAQDMSPEE IQAVIDRILA KDVPAKNAAP GSGAGAGSRA VFGKAQAISR LDEEHSLFDG DQQDLEERRA LRRTAGLSTE LEDVTEVEYR QLRLERVVLA GLWTEGTLAD AENSLRELAA LAETAGSEVL DGLVQRRAKP DPGTFLGSGK ALELKDVVMS TGADTVVVDA ELAPSQRRGL EDIVKVKVID RTALILDIFA QHAKSREGKA QVELAQLEYL LPRLRGWGES MSRQAGGQVG GAGAGMGSRG PGETKIELDR RRIRTRMAKL RREIAAMKPA RETKRANRRR NAVPSVAIAG YTNAGKSSLL NRLTDAGVLV ENALFATLDP TVRKTETADG LGYTLADTVG FVRSLPTQLV EAFRSTLEEV ADADLILHIV DVSHPDPEGQ IAAVRSVFAE VDARKVPEII VLNKADAADP FVVERLKQRE PRHVVVSART GQGIPELLKA ISESIPRPSV KLELLVPYHR GDLISRLHDS DAEILSLDHE EGGTRAVVMV REGLAAELES FISND // ID A0A0Q9MBL6_9BACL Unreviewed; 442 AA. AC A0A0Q9MBL6; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=ASL11_24965 {ECO:0000313|EMBL:KRE59490.1}; OS Paenibacillus sp. Soil750. OC Bacteria; Firmicutes; Bacilli; Bacillales; Paenibacillaceae; OC Paenibacillus. OX NCBI_TaxID=1736398 {ECO:0000313|EMBL:KRE59490.1, ECO:0000313|Proteomes:UP000051252}; RN [1] {ECO:0000313|EMBL:KRE59490.1, ECO:0000313|Proteomes:UP000051252} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Soil750 {ECO:0000313|EMBL:KRE59490.1, RC ECO:0000313|Proteomes:UP000051252}; RA Millard Andrew; RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:KRE59490.1, ECO:0000313|Proteomes:UP000051252} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Soil750 {ECO:0000313|EMBL:KRE59490.1, RC ECO:0000313|Proteomes:UP000051252}; RA Vorholt J.; RT "Functional overlap of the Arabidopsis leaf and root microbiotas."; RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KRE59490.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LMSD01000034; KRE59490.1; -; Genomic_DNA. DR RefSeq; WP_056620899.1; NZ_LMSD01000034.1. DR EnsemblBacteria; KRE59490; KRE59490; ASL11_24965. DR Proteomes; UP000051252; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000051252}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000051252}. FT DOMAIN 208 372 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 442 AA; 49840 MW; 3866D4A7564720B6 CRC64; MKTTSHMVEK EIDDRAVLVS LITQKQKKNE LLAEYSLQEL VKLAETAGVQ VLDTMTQNKE AKDTKWFIGK GKVEELKLML EELGGNTAIF DQELSGAQVR NLEAALDVKI IDRTQLILDI FAQRAKTREG IIQVELAQLS YLLPRLSGQG KNLSRLGGGI GTRGPGESKL ETDRRHIRGR IDELKAQLEE VVRHRTLHRE RRKKSGVFQV ALVGYTNAGK STLLKQLTQA DVYIENQLFA TLDPTSRTMI LPSGKEIVLT DTVGFIQNLP HDLVASFRAT LEEANEADLI LHVVDSSTDM RGEQMRVVGE VLEQLGAHQK EQITVFNKID LISKEERELL SDQGEFMKVS AYTPEDLERL RITIEDKLMG DSKEFRIPAN KGDVIALMYR IGEVLETDVD GEDMIFKVRV NKEDYVKQAY LLVDYDQSSA KPEQDENEGE SN // ID A0A0Q9MLB2_9MICO Unreviewed; 486 AA. AC A0A0Q9MLB2; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=ASG78_05715 {ECO:0000313|EMBL:KRE62514.1}; OS Tetrasphaera sp. Soil756. OC Bacteria; Actinobacteria; Micrococcales; Intrasporangiaceae; OC Tetrasphaera. OX NCBI_TaxID=1736399 {ECO:0000313|EMBL:KRE62514.1, ECO:0000313|Proteomes:UP000051616}; RN [1] {ECO:0000313|EMBL:KRE62514.1, ECO:0000313|Proteomes:UP000051616} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Soil756 {ECO:0000313|EMBL:KRE62514.1, RC ECO:0000313|Proteomes:UP000051616}; RA Millard Andrew; RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:KRE62514.1, ECO:0000313|Proteomes:UP000051616} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Soil756 {ECO:0000313|EMBL:KRE62514.1, RC ECO:0000313|Proteomes:UP000051616}; RA Vorholt J.; RT "Functional overlap of the Arabidopsis leaf and root microbiotas."; RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KRE62514.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LMSE01000002; KRE62514.1; -; Genomic_DNA. DR RefSeq; WP_055811704.1; NZ_LMSE01000002.1. DR EnsemblBacteria; KRE62514; KRE62514; ASG78_05715. DR Proteomes; UP000051616; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 2. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000051616}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000051616}. FT DOMAIN 268 433 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 486 AA; 52974 MW; A17BB817B5069D7B CRC64; MTARDFLSGR AEALADAPLD DSGFVLDDDA LTYDGDQLDR EERASLRRVA GLSTELEDVT EVEYRQLRLE RVVLAAVWCE GTAEDAENSM RELAALAETA GSEVLAGVVQ RRANPDPATY LGKGKAAELR DIVVAEGADT VICDTELAPS QRRALEDVVK VKVIDRTALI LDIFAQHAKS REGKAQVELA QLQYLLPRLR GWGESMSRQA GGQAAGGQGM GSRGPGETKI ELDRRRINTR MAKLRREIKD MKTVRDTKRG GRKANQVPSV AIAGYTNAGK SSLLNRLTGA GVLVENQLFA TLDPTVRRAE TPDGRLYTLA DTVGFVRQLP HQLVEAFRST LEEVAEADLL LHVVDGSHPD PEGQISAVRS VLSDVEATDV KEVIVINKAD LADPEVIDRL RRHEKHSIVV SARTGEGMEQ LRALIGDELP QPDIDVDVLV PYDRGDLVSR VHETGEVLTS EHVAEGTRLT ARVDAELADD LSSYAV // ID A0A0Q9NDC6_9MICC Unreviewed; 521 AA. AC A0A0Q9NDC6; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=ASG77_19560 {ECO:0000313|EMBL:KRE76512.1}; OS Arthrobacter sp. Soil762. OC Bacteria; Actinobacteria; Micrococcales; Micrococcaceae; Arthrobacter. OX NCBI_TaxID=1736401 {ECO:0000313|EMBL:KRE76512.1, ECO:0000313|Proteomes:UP000051715}; RN [1] {ECO:0000313|EMBL:KRE76512.1, ECO:0000313|Proteomes:UP000051715} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Soil762 {ECO:0000313|EMBL:KRE76512.1, RC ECO:0000313|Proteomes:UP000051715}; RA Millard Andrew; RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:KRE76512.1, ECO:0000313|Proteomes:UP000051715} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Soil762 {ECO:0000313|EMBL:KRE76512.1, RC ECO:0000313|Proteomes:UP000051715}; RA Vorholt J.; RT "Functional overlap of the Arabidopsis leaf and root microbiotas."; RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KRE76512.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LMSG01000006; KRE76512.1; -; Genomic_DNA. DR RefSeq; WP_056342924.1; NZ_LMSG01000006.1. DR EnsemblBacteria; KRE76512; KRE76512; ASG77_19560. DR Proteomes; UP000051715; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 2. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000051715}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000051715}. FT DOMAIN 300 465 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 521 AA; 56666 MW; 9518B27EFBF7F915 CRC64; MTSQPNPGSD PAAQDMSPEE IQAVIDRILA KDVPARNVTA ADGDKGVFGR AQAISRLDDE HTSYDGDQQD REERRALKRV AGLSTELEDV TEVEYRQLRL ERVVLAGLWS EGTLADAENS LRELAALAET AGSEVLDGMV QRRAKPDPGT FLGSGKALEL KEIVMATGAD TVVVDAELAP SQRRSLEDIV KVKVIDRTAL ILDIFAQHAK SREGKAQVEL AQLEYLLPRL RGWGESMSRQ AGGQVGGAGA GMGSRGPGET KIELDRRRIR TRMAKLRREI AAMKPARETK RANRRRNSVP SVAIAGYTNA GKSSLLNRLT DAGVLVENAL FATLDPTVRK AETSDGLGYT LADTVGFVRS LPTQLVEAFR STLEEVADAD LILHVVDVSH PDPEGQIAAV RKVFSEVDAR KVPEIIVLNK ADAADPFVVE RLKQREPRHV VVSARTGQGI AELLRAISDG IPRPGVKLEL LIPYDRGDLI SKLHETDAEI LSLDHGEHGT RALVMVREGL AAELESFINH D // ID A0A0Q9PW28_9GAMM Unreviewed; 433 AA. AC A0A0Q9PW28; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=ASG87_05045 {ECO:0000313|EMBL:KRE89684.1}; OS Frateuria sp. Soil773. OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales; OC Rhodanobacteraceae; Frateuria. OX NCBI_TaxID=1736407 {ECO:0000313|EMBL:KRE89684.1, ECO:0000313|Proteomes:UP000051919}; RN [1] {ECO:0000313|EMBL:KRE89684.1, ECO:0000313|Proteomes:UP000051919} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Soil773 {ECO:0000313|EMBL:KRE89684.1, RC ECO:0000313|Proteomes:UP000051919}; RA Millard Andrew; RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:KRE89684.1, ECO:0000313|Proteomes:UP000051919} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Soil773 {ECO:0000313|EMBL:KRE89684.1, RC ECO:0000313|Proteomes:UP000051919}; RA Vorholt J.; RT "Functional overlap of the Arabidopsis leaf and root microbiotas."; RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KRE89684.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LMSL01000039; KRE89684.1; -; Genomic_DNA. DR RefSeq; WP_056006422.1; NZ_LMSL01000039.1. DR EnsemblBacteria; KRE89684; KRE89684; ASG87_05045. DR Proteomes; UP000051919; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000051919}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000051919}. FT DOMAIN 200 366 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 433 AA; 46958 MW; 11045C3E8CD4BCD0 CRC64; MFDRQKKGER AVLVLPHSRG EGDAARRAAE FAELVKSAGA EVLGSIAARV EAPNPRYYIG TGKADEVAEM ARALEADLVL VDHLLTPVQE RNLEKHLGIR VVDRAGLILD IFAQRARSHE GKLEVELAQL KHLATRLVRG WTHLDAQRGG AIGNRGPGET QLETDRRLLA ERVKMLTKRL EKVQTQRGQQ RRARLRNTVP RVALVGYTNA GKSTLFNALT AGAVYAADQL FATLDPTVRR LDDLACGPAV VADTVGFIRE LPHDLVAAFR GTLAEARDAD LLLHVCDAAD EERERLRGVV DQVLDEIDAG DLPQLQVMNK IDLAGSEPRI VRDGEGCPVQ VWLSAATGAG LDLLRQALGE LLGGERVQSE LQLPLSAGRL HARLRAAGAI ASEDVDEHGW RLRIDAPRSV IAPLRGGSSA EADLLRGLLG PAE // ID A0A0Q9QID3_9ACTN Unreviewed; 522 AA. AC A0A0Q9QID3; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=ASG76_01335 {ECO:0000313|EMBL:KRE97396.1}; OS Nocardioides sp. Soil774. OC Bacteria; Actinobacteria; Propionibacteriales; Nocardioidaceae; OC Nocardioides. OX NCBI_TaxID=1736408 {ECO:0000313|EMBL:KRE97396.1, ECO:0000313|Proteomes:UP000051100}; RN [1] {ECO:0000313|EMBL:KRE97396.1, ECO:0000313|Proteomes:UP000051100} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Soil774 {ECO:0000313|EMBL:KRE97396.1, RC ECO:0000313|Proteomes:UP000051100}; RA Millard Andrew; RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:KRE97396.1, ECO:0000313|Proteomes:UP000051100} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Soil774 {ECO:0000313|EMBL:KRE97396.1, RC ECO:0000313|Proteomes:UP000051100}; RA Vorholt J.; RT "Functional overlap of the Arabidopsis leaf and root microbiotas."; RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KRE97396.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LMSM01000001; KRE97396.1; -; Genomic_DNA. DR RefSeq; WP_056598883.1; NZ_LMSM01000001.1. DR EnsemblBacteria; KRE97396; KRE97396; ASG76_01335. DR Proteomes; UP000051100; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 2. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000313|EMBL:KRE97396.1}; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000051100}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900, KW ECO:0000313|EMBL:KRE97396.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000051100}. FT DOMAIN 304 469 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 270 297 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 522 AA; 56875 MW; 95CE873E37E39FCA CRC64; MTNAPDYPTS DFTLRDALDA TRGWDDEVIE LDGDLDTDDS ATDADDGFES GYADDESYDD WDDADPEELT VGAQELAERH ALRRVASLRT ELEDITEVEY RQLRLEKVVL VGVWTGGTVT DAENSMAELA ALAETAGSEV LEAVFQRRQS PDPATFIGRG KVEAIREIVQ ATGADTVICD GELAPSQLRN LEDKIKVKVV DRTALILDIF AQHAKSKEGQ AQVELAQLQY MKQRLRGWGG NLSRQAGGRA AGGDGIGGRG PGETKIETDR RRINTKIAKL RRELKEMRGT REVKRQSRRR NHIPSVAIAG YTNAGKSSLL NRLTDAGVLV EDALFATLDP TTRRTTTSDG RVYTMSDTVG FVRHLPHGLV EAFRSTLEEV ADSDLLLHVV DGSHPDPEGQ IAAVREVLAE IGATKVPEVI VINKADAADP LVISRLRARE PHSVVVSAKT GEGISEALAT IESELPRPQV EFDVLLPYER GDLVNRIHQE AEIGSMEHTG DGTLVVGRAN ADLAGELAAY SR // ID A0A0Q9QWH9_9MICC Unreviewed; 521 AA. AC A0A0Q9QWH9; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 07-JUN-2017, entry version 12. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=ASH00_10605 {ECO:0000313|EMBL:KRF04918.1}; OS Arthrobacter sp. Soil782. OC Bacteria; Actinobacteria; Micrococcales; Micrococcaceae; Arthrobacter. OX NCBI_TaxID=1736410 {ECO:0000313|EMBL:KRF04918.1, ECO:0000313|Proteomes:UP000053496}; RN [1] {ECO:0000313|EMBL:KRF04918.1, ECO:0000313|Proteomes:UP000053496} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Soil782 {ECO:0000313|EMBL:KRF04918.1, RC ECO:0000313|Proteomes:UP000053496}; RA Millard Andrew; RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:KRF04918.1, ECO:0000313|Proteomes:UP000053496} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Soil782 {ECO:0000313|EMBL:KRF04918.1, RC ECO:0000313|Proteomes:UP000053496}; RA Vorholt J.; RT "Functional overlap of the Arabidopsis leaf and root microbiotas."; RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KRF04918.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LMSO01000009; KRF04918.1; -; Genomic_DNA. DR RefSeq; WP_056548438.1; NZ_LMSO01000009.1. DR EnsemblBacteria; KRF04918; KRF04918; ASH00_10605. DR Proteomes; UP000053496; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 2. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000053496}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000053496}. FT DOMAIN 300 465 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 521 AA; 56785 MW; B908204EAAFAAF41 CRC64; MTTHNGAPAT PEPEMGPDEI QAVIDRILAK DPASSSNGSQ RRFGSGPGGR AQALSDLDEE HTGYDGEQQD REERRALRRV AGLSTELEDV TEVEYRQLRL ERVVLAGIWG EGTVDDAENS LRELAALAET AGSEVLDGII QRRLKPDPGT FLGAGKAEEL KNIVMATGAD TVVVDSELAP SQRRGLEDIV KVKVIDRTAL ILDIFAQHAK SREGKAQVEL AQLEYLLPRL RGWGDSMSRQ AGGQVGGAGA GMGSRGPGET KIELDRRKIR TRMAKLRREI AGMKPARETK RANRRRHEVP SVAIAGYTNA GKSSLLNRMT DAGVLVENAL FATLDPTIRR AQTPDGLEFT LADTVGFVRS LPTQLVEAFR STLEEVADAD LILHVVDASH PDPEGQIAAV RDVLTEVDAR KVPEIVVLNK ADAADPFVLE RLRQREPRHA IVSARTGQGI EELLELISQS IPRPSVKLTL LVPYQRGDIV SRLHQPDAEI LGLEHVEDGT RVEVMVREGL AAELEPFITH G // ID A0A0Q9R6U5_9BACL Unreviewed; 441 AA. AC A0A0Q9R6U5; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=ASG93_17885 {ECO:0000313|EMBL:KRF10799.1}; OS Paenibacillus sp. Soil787. OC Bacteria; Firmicutes; Bacilli; Bacillales; Paenibacillaceae; OC Paenibacillus. OX NCBI_TaxID=1736411 {ECO:0000313|EMBL:KRF10799.1, ECO:0000313|Proteomes:UP000051948}; RN [1] {ECO:0000313|EMBL:KRF10799.1, ECO:0000313|Proteomes:UP000051948} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Soil787 {ECO:0000313|EMBL:KRF10799.1, RC ECO:0000313|Proteomes:UP000051948}; RA Millard Andrew; RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:KRF10799.1, ECO:0000313|Proteomes:UP000051948} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Soil787 {ECO:0000313|EMBL:KRF10799.1, RC ECO:0000313|Proteomes:UP000051948}; RA Vorholt J.; RT "Functional overlap of the Arabidopsis leaf and root microbiotas."; RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KRF10799.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LMSP01000047; KRF10799.1; -; Genomic_DNA. DR RefSeq; WP_056839002.1; NZ_LMSP01000047.1. DR EnsemblBacteria; KRF10799; KRF10799; ASG93_17885. DR Proteomes; UP000051948; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000051948}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000051948}. FT DOMAIN 208 372 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 441 AA; 49875 MW; 6C0CB33ED6AF85A2 CRC64; MKTTSHMVEK EIDDRAVLVS LVTQKQKKNE LLAEYSLQEL VKLAETAGVL VLETLTQNKE TKDSKWFIGK GKVEELKVLL EELGGNTAIF DQELSGAQVR NLEAALDVKI IDRTQLILDI FAQRAKTREG IIQVELAQLS YLLPRLSGQG KNLSRLGGGI GTRGPGESKL ETDRRHIRGR IDELKAQLEE VVRHRTLHRE RRKKTGVFQV ALVGYTNAGK STLLKQLTQA DVYIENQLFA TLDPTSRTME LPSGKEIVLT DTVGFIQNLP HDLVASFRAT LEEANEADLI LHVVDSSTDM RNEQMRVVAE VLEELGAHQK EQLTIFNKID LCLQEDREML STEGEFLKIS AYNPDDLERL RIAIQEKLMG ESKEFRIPAD KGDIISLMYR IGDVLETDVD GEDMLFKVRV NKDDYVKLAY QLVAYDQHAQ QEAQDIEGEI Y // ID A0A0Q9S9U0_9ACTN Unreviewed; 496 AA. AC A0A0Q9S9U0; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=ASG90_20315 {ECO:0000313|EMBL:KRF19776.1}; OS Nocardioides sp. Soil797. OC Bacteria; Actinobacteria; Propionibacteriales; Nocardioidaceae; OC Nocardioides. OX NCBI_TaxID=1736413 {ECO:0000313|EMBL:KRF19776.1, ECO:0000313|Proteomes:UP000050845}; RN [1] {ECO:0000313|EMBL:KRF19776.1, ECO:0000313|Proteomes:UP000050845} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Soil797 {ECO:0000313|EMBL:KRF19776.1, RC ECO:0000313|Proteomes:UP000050845}; RA Millard Andrew; RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:KRF19776.1, ECO:0000313|Proteomes:UP000050845} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Soil797 {ECO:0000313|EMBL:KRF19776.1, RC ECO:0000313|Proteomes:UP000050845}; RA Vorholt J.; RT "Functional overlap of the Arabidopsis leaf and root microbiotas."; RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KRF19776.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LMSR01000005; KRF19776.1; -; Genomic_DNA. DR RefSeq; WP_057322689.1; NZ_LMSR01000005.1. DR EnsemblBacteria; KRF19776; KRF19776; ASG90_20315. DR Proteomes; UP000050845; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro. DR CDD; cd01878; HflX; 1. DR Gene3D; 3.50.50.60; -; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR023753; FAD/NAD-binding_dom. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 2. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000313|EMBL:KRF19776.1}; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000050845}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900, KW ECO:0000313|EMBL:KRF19776.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000050845}. FT DOMAIN 278 443 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 244 271 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 496 AA; 54060 MW; 2CDBD25084231814 CRC64; MTNASEDFSL DAELAETDAW DDDDFESGYA DDVVSADGPD PELTTGEQDL AERHALRRVA GLRTELEDIT EVEYRQLRLE RVVLVGVWTE GTPEDAENSM AELALLAETA GSEVLDNVYQ RRQKPDPATY IGRGKVDGLR EIVQATGADT VILDGDLAPS QLRNLEDKLK VKAIDRTALI LDIFAQHAKS KEGQAQVELA QLNYMKQRLR GWGGNLSRQA GGQAAGGEGI GGRGPGETKI ETDRRRINTK IAKLRRELKA MKGTRDTKRS ERQRNAIPSV AIAGYTNAGK SSLLNRLTDA GVLVEDSLFA TLDPTTRRTT TADGRIYTMS DTVGFVRHLP HQLVEAFRST LEEVADADLI LHVVDGSHPD PEGQITAVRE VFADIEASKV PELIVINKAD AADPMVLARL RAREPHSVVV SAKTGEGIRE ALALVESELP RPSVAFSALL PYERGDLINK LHQQGEIETL EHTAEGSLVK GRAHEGLADE LAAYAV // ID A0A0Q9SGN2_9MICO Unreviewed; 483 AA. AC A0A0Q9SGN2; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=ASG91_15535 {ECO:0000313|EMBL:KRF22803.1}; OS Phycicoccus sp. Soil802. OC Bacteria; Actinobacteria; Micrococcales; Intrasporangiaceae; OC Phycicoccus. OX NCBI_TaxID=1736414 {ECO:0000313|EMBL:KRF22803.1, ECO:0000313|Proteomes:UP000050906}; RN [1] {ECO:0000313|EMBL:KRF22803.1, ECO:0000313|Proteomes:UP000050906} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Soil802 {ECO:0000313|EMBL:KRF22803.1, RC ECO:0000313|Proteomes:UP000050906}; RA Millard Andrew; RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:KRF22803.1, ECO:0000313|Proteomes:UP000050906} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Soil802 {ECO:0000313|EMBL:KRF22803.1, RC ECO:0000313|Proteomes:UP000050906}; RA Vorholt J.; RT "Functional overlap of the Arabidopsis leaf and root microbiotas."; RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KRF22803.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LMSS01000006; KRF22803.1; -; Genomic_DNA. DR RefSeq; WP_056923540.1; NZ_LMSS01000006.1. DR EnsemblBacteria; KRF22803; KRF22803; ASG91_15535. DR Proteomes; UP000050906; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 2. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000050906}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000050906}. FT DOMAIN 265 430 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 483 AA; 52578 MW; AAE67C06B95F6E16 CRC64; MTLKRSDIFD LKATALASED EFLPRDGAGY DGDQYDREDR AALRRVAGLS TELEDITEVE YRQLRLERVV LAAVWTEGTA EDADNSMREL AALAETAGST VLAGLVQRRA KPDTGTYLGS GKAVELRDIV IAEGADTVIC DTELTPSQRR ALEDVVKVKV IDRTALILDI FAQHAKSKEG KAQVELAQLQ YLLPRLRGWG ESMSRQAGGQ AAGGQGMGSR GPGETKIELD RRRINTRMAK LRREIKEMKT SRDTRRLSRK ANEVPSVAIA GYTNAGKSSL LNRLTGAGVL VENQLFATLD PTVRRAETED GRLYTLADTV GFVRQLPTQL VEAFRSTLEE VGDADLLLHV VDGSHPDPEG QISAVRAVLA DVDAASVREV IVVNKADAAD PEVLDRIQRH EKHSIVVSAR TGAGIEELRT LIAEELPRPT IDVEVLVPYD RGDLVSRLHQ EAEVLSSEHT GTGTLVKARV HADLAGELAA FAA // ID A0A0Q9T5N4_9BACL Unreviewed; 419 AA. AC A0A0Q9T5N4; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=ASG93_26315 {ECO:0000313|EMBL:KRF34583.1}; OS Paenibacillus sp. Soil787. OC Bacteria; Firmicutes; Bacilli; Bacillales; Paenibacillaceae; OC Paenibacillus. OX NCBI_TaxID=1736411 {ECO:0000313|EMBL:KRF34583.1, ECO:0000313|Proteomes:UP000051948}; RN [1] {ECO:0000313|EMBL:KRF34583.1, ECO:0000313|Proteomes:UP000051948} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Soil787 {ECO:0000313|EMBL:KRF34583.1, RC ECO:0000313|Proteomes:UP000051948}; RA Millard Andrew; RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:KRF34583.1, ECO:0000313|Proteomes:UP000051948} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Soil787 {ECO:0000313|EMBL:KRF34583.1, RC ECO:0000313|Proteomes:UP000051948}; RA Vorholt J.; RT "Functional overlap of the Arabidopsis leaf and root microbiotas."; RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KRF34583.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LMSP01000010; KRF34583.1; -; Genomic_DNA. DR RefSeq; WP_056832082.1; NZ_LMSP01000010.1. DR EnsemblBacteria; KRF34583; KRF34583; ASG93_26315. DR Proteomes; UP000051948; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000051948}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000051948}. FT DOMAIN 198 366 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 157 191 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 419 AA; 47933 MW; 2F5155C8943E6202 CRC64; MEQLKEKAII VGVHILNHPN FAYSMEELKN LAAACHIEVV GQLNQKVTRV VPSHYIGTGK IQELSQLITE RNASVVICND ELSPSQIRNL ESSLACKIID RTILILDIFA ERAQTREAQL QVEVARLQYM LPRLVGLRES LGRQGGGAGL KNRGSGETKL ELDRRKIEDR ITALQSELEK LVARRQTQRK QRRKNEVPVI CLVGYTNAGK SSLMNAMIEL YNPQAHKQVF VKDMLFATLE TSVRNVNLPD SKSFLLTDTV GFVSQLPHHL VKAFRSTLEE VAEADLLIHV VDIANPEYEQ HIDVTNETLK VLRADRIPMI FAYNKSDLTE HAYPLLKDDF VYLSAQQKRG IEELTQLIRE HIFQNYMECE IVIPYEQGRL VAYFNEHAHV HSTNYEPNGT RLKLECRVSD FEQYRDDFL // ID A0A0Q9TBJ8_9ACTN Unreviewed; 508 AA. AC A0A0Q9TBJ8; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=ASG94_06255 {ECO:0000313|EMBL:KRF36989.1}; OS Nocardioides sp. Soil805. OC Bacteria; Actinobacteria; Propionibacteriales; Nocardioidaceae; OC Nocardioides. OX NCBI_TaxID=1736416 {ECO:0000313|EMBL:KRF36989.1, ECO:0000313|Proteomes:UP000051356}; RN [1] {ECO:0000313|EMBL:KRF36989.1, ECO:0000313|Proteomes:UP000051356} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Soil805 {ECO:0000313|EMBL:KRF36989.1, RC ECO:0000313|Proteomes:UP000051356}; RA Millard Andrew; RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:KRF36989.1, ECO:0000313|Proteomes:UP000051356} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Soil805 {ECO:0000313|EMBL:KRF36989.1, RC ECO:0000313|Proteomes:UP000051356}; RA Vorholt J.; RT "Functional overlap of the Arabidopsis leaf and root microbiotas."; RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KRF36989.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LMSU01000001; KRF36989.1; -; Genomic_DNA. DR RefSeq; WP_056925472.1; NZ_LMSU01000001.1. DR EnsemblBacteria; KRF36989; KRF36989; ASG94_06255. DR Proteomes; UP000051356; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 2. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000313|EMBL:KRF36989.1}; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000051356}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900, KW ECO:0000313|EMBL:KRF36989.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000051356}. FT DOMAIN 290 455 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 256 283 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 508 AA; 55495 MW; 6E1BA4C4416337CA CRC64; MTNAPDFSLD AELDATRAWD DDSEGSDGSD WESGYADEEI LSADGPDPEE ADDLTTGEQD LVARHALRRV AGLRTELEDI TEVEYRQLRL ERVVLVGVWI DGTVTDAENS MAELALLAET AGSEVLDAIY QRRTKPDPAT YIGRGKVEGL REIVQATGAD TVILDGDLAP SQLRNLEDKL KVKAIDRTAL ILDIFAQHAK SKEGQAQVEL AQLQYMKQRL RGWGGNLSRQ AGGRVGADGG GIGGRGPGET KIETDRRRIN TKIAKLRREL KDLKGTRETM RQERSRNHIP SVSIAGYTNA GKSSLLNRLT DAGVLVEDSL FATLDPTTRR TTTRDGRIYT MSDTVGFVRH LPHQLVEAFR STLEEVAESD LILHVVDGSH PDPEGQLAAV REVFAEIHAD KVPELVIINK ADAADPLVLA RLRAREPHSV VVSARTGEGI EDVLSAVEAD LPRPTVEFSV LLPYERGDLI NRLHQEGEMT SLEHTADGSL VSGRANADLA GELEPYAV // ID A0A0Q9Y4B1_9BACI Unreviewed; 423 AA. AC A0A0Q9Y4B1; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=ACA30_20905 {ECO:0000313|EMBL:KRG12098.1}; OS Virgibacillus soli. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Virgibacillus. OX NCBI_TaxID=480284 {ECO:0000313|EMBL:KRG12098.1, ECO:0000313|Proteomes:UP000050957}; RN [1] {ECO:0000313|EMBL:KRG12098.1, ECO:0000313|Proteomes:UP000050957} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=PL205 {ECO:0000313|EMBL:KRG12098.1, RC ECO:0000313|Proteomes:UP000050957}; RA Gaiero J., Nicol R., Habash M.; RT "Genome sequencing project of Virgibacillus soli PL205."; RL Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KRG12098.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LGPD01000050; KRG12098.1; -; Genomic_DNA. DR RefSeq; WP_057988951.1; NZ_LGPD01000050.1. DR EnsemblBacteria; KRG12098; KRG12098; ACA30_20905. DR PATRIC; fig|480284.4.peg.4606; -. DR Proteomes; UP000050957; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000050957}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000050957}. FT DOMAIN 205 366 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 423 AA; 48544 MW; 37B1E3B8E2663E8D CRC64; MRKRGKYLQK PGKEKVIIVG SQTIESDLHF QYSMSELESL VSTAQGETIA SLTQKQEKLH PSTYIGKGKL EELQHLEEEL EPDLTIFNDE LSPSQQRNLQ DRLNSKVLDR TQLILDIFAQ RARSKEGKLQ VELAQLQYLL PRLAGQGILL SRLGGGIGTR GPGETKLESD RRHIRRRIDE IKRQLQVVVH HRERYRERRR RNKAFQIAIV GYTNAGKSTL FNRLSTAQAF EENQLFATLD PLTRKLVLPS GYNAILTDTV GFIQELPTTL IAAFRSTLEE VRDADLLLHV VDSSNPDFDN HENTVLHLLK ELEMDHLPQL IVYNKSDQIT PEFVPRSGEH FIMSAFSDTD RQKLKQIIEK MATENMDYYH VVVPSDEGRL LSVLKNDTIL REFIFLEEEQ SYKCKGYVLK DHPVNAALKL YGV // ID A0A0Q9YEX9_9BACI Unreviewed; 422 AA. AC A0A0Q9YEX9; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=ACA30_05125 {ECO:0000313|EMBL:KRG15726.1}; OS Virgibacillus soli. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Virgibacillus. OX NCBI_TaxID=480284 {ECO:0000313|EMBL:KRG15726.1, ECO:0000313|Proteomes:UP000050957}; RN [1] {ECO:0000313|EMBL:KRG15726.1, ECO:0000313|Proteomes:UP000050957} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=PL205 {ECO:0000313|EMBL:KRG15726.1, RC ECO:0000313|Proteomes:UP000050957}; RA Gaiero J., Nicol R., Habash M.; RT "Genome sequencing project of Virgibacillus soli PL205."; RL Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KRG15726.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LGPD01000008; KRG15726.1; -; Genomic_DNA. DR RefSeq; WP_057982898.1; NZ_LGPD01000008.1. DR EnsemblBacteria; KRG15726; KRG15726; ACA30_05125. DR PATRIC; fig|480284.4.peg.1099; -. DR Proteomes; UP000050957; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000050957}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000050957}. FT DOMAIN 196 363 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 162 189 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 422 AA; 47879 MW; AECAC60C446EFAC1 CRC64; MERKAIIVGV NRQQALENFT YSMEELVNLA TACHISVIGE IAQNLQHFDK TYYIGSGKVE ELQALIAELE ANIVVFDDEL SPSQIRNLEE KLDCEVIDRT MLILEIFASR AKTKESQLQV EIARLNYMLP RLVGSRESLG RQGGGAGLKN RGAGETKLEL DRRKIEMKIS ALSKELEQLV ARRKIQRKQR HKNEIPVVSL VGYTNAGKST LMNTMLNNHQ ADQEKQVFEK DMLFATLETA VRKIDLPGNK SFLLTDTVGF INKLPHHLVK AFRSTLEEVM EADLLVHVID YSNPYHEEQK TLTNQVLQEM GVENIPVLYA YNKADKVDGP FPSQENSVYI AAKTGEGIEE FTKLLSEQIF QDYLQCDLFI PYTDGAVISY FNEHSQILAT RYEEEGTAFT VECKKADAEK FQQYVRKAEA AD // ID A0A0Q9YG88_9COXI Unreviewed; 433 AA. AC A0A0Q9YG88; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:KRG19557.1}; GN ORFNames=CC99x_00569 {ECO:0000313|EMBL:KRG19557.1}; OS Candidatus Berkiella cookevillensis. OC Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales; OC Coxiellaceae; Candidatus Berkiella. OX NCBI_TaxID=437022 {ECO:0000313|EMBL:KRG19557.1, ECO:0000313|Proteomes:UP000051494}; RN [1] {ECO:0000313|EMBL:KRG19557.1, ECO:0000313|Proteomes:UP000051494} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CC99 {ECO:0000313|EMBL:KRG19557.1, RC ECO:0000313|Proteomes:UP000051494}; RA Mehari Y.T., Arivett B.A., Farone A.L., Gunderson J.H., Farone M.B.; RT "Draft Genome Sequences of Two Novel Amoeba-resistant Intranuclear RT Bacteria, Candidatus Berkiella cookevillensis and Candidatus Berkiella RT aquae."; RL Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KRG19557.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LKHV01000002; KRG19557.1; -; Genomic_DNA. DR RefSeq; WP_057623454.1; NZ_LKHV01000002.1. DR EnsemblBacteria; KRG19557; KRG19557; CC99x_00569. DR PATRIC; fig|1590042.3.peg.587; -. DR Proteomes; UP000051494; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000051494}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000051494}. FT DOMAIN 198 369 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 433 AA; 48255 MW; EFBD032858AC4ACD CRC64; MFERPKSGER AVLVHLTFPH ISESSDSAEF AELAMAAGAE PVAKIFGRRP APDPKFFIGK GKLEEIKSAL AAFDAALIIF NHELSPAQER NVERETRCRV LSRTGLILDI FAQRARTFEG KLQVELAQLN HMSTRLVRGW THLERQKGGI GLRGPGETQL ESDRRLLRRR VEFIKQRLDK VKVSREQSRR ARTRQAIPTI SLVGYTNAGK STLFNALTGA HVLVANQLFA TLDPTLRAIE LPEIGKVILA DTVGFVSQLP HGLVDAFRAT LEEVAQSALL IHVVDAHDDK RDEHIHQVNL VLNEIGADDL QQIVVMNKSD LDESFTHGEN EDQGNLNNYP PHQIATSALT GQGLEQLLLA IQKALSQETV IGWIQVAANE GKMRALFYQN HAVVEELPQE DGGFNMKIKV SGIKWRQMCQ VFTELSSKLQ NIP // ID A0A0Q9YIP0_9COXI Unreviewed; 436 AA. AC A0A0Q9YIP0; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 07-JUN-2017, entry version 12. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:KRG20571.1}; GN ORFNames=HT99x_02302 {ECO:0000313|EMBL:KRG20571.1}; OS Candidatus Berkiella aquae. OC Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales; OC Coxiellaceae; Candidatus Berkiella. OX NCBI_TaxID=295108 {ECO:0000313|EMBL:KRG20571.1, ECO:0000313|Proteomes:UP000051497}; RN [1] {ECO:0000313|EMBL:KRG20571.1, ECO:0000313|Proteomes:UP000051497} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=HT99 {ECO:0000313|EMBL:KRG20571.1, RC ECO:0000313|Proteomes:UP000051497}; RA Mehari Y.T., Arivett B.A., Farone A.L., Gunderson J.H., Farone M.B.; RT "Draft Genome Sequences of Two Novel Amoeba-resistant Intranuclear RT Bacteria, Candidatus Berkiella cookevillensis and Candidatus Berkiella RT aquae."; RL Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KRG20571.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LKAJ01000010; KRG20571.1; -; Genomic_DNA. DR RefSeq; WP_075066924.1; NZ_LKAJ01000010.1. DR EnsemblBacteria; KRG20571; KRG20571; HT99x_02302. DR PATRIC; fig|1590043.3.peg.2351; -. DR Proteomes; UP000051497; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000051497}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000051497}. FT DOMAIN 198 368 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 436 AA; 48879 MW; 5BF843BBE7C3CD9B CRC64; MFERPGRGER AVLVHVTFRR QSEQADLQEL GELAFAAGVT TVAKITTQRD KPDPKHYIGQ GKLAEILDAV SLHEAEVVIF NHELSPSQER NVERFVKCRV LSRTGLILDI FAQRARTFEG KLQVELAQLE HLSTRLVRGW THLERQKGGI GLRGPGETQL ETDRRLIRDR IMAIQKRLDK VRQQRGQSRH ARTRAEIPTI ALVGYTNAGK STLFNALTGA HVFVANQLFA TLDPTLRAIE LTGIGKVVLA DTVGFIRQLP HTLVDAFRAT LEETSQAHLL LHVVDAHDEK FEEHMHEVNQ VLADIGANDV SQLTVFNKAD LLVGQGFQSG DCERDKDGKI TKIWVSAQTK EGLDLLREAL QGRLSIETIE GSVYLAPEQG QLRSQLFALQ AVLEEKDLSE GGWKIKIKTT KYHWEKLCQQ YAGLASVFQG KDKKRG // ID A0A0Q9ZE25_9FLAO Unreviewed; 406 AA. AC A0A0Q9ZE25; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=APR42_08760 {ECO:0000313|EMBL:KRG27834.1}; OS Salegentibacter mishustinae. OC Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales; OC Flavobacteriaceae; Salegentibacter. OX NCBI_TaxID=270918 {ECO:0000313|EMBL:KRG27834.1, ECO:0000313|Proteomes:UP000051643}; RN [1] {ECO:0000313|EMBL:KRG27834.1, ECO:0000313|Proteomes:UP000051643} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=KCTC 12263 {ECO:0000313|EMBL:KRG27834.1, RC ECO:0000313|Proteomes:UP000051643}; RA Lin W., Zheng Q.; RT "Draft genome sequence of Salegentibacter mishustinae KCTC 12263."; RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KRG27834.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LKTP01000034; KRG27834.1; -; Genomic_DNA. DR RefSeq; WP_057482506.1; NZ_LKTP01000034.1. DR EnsemblBacteria; KRG27834; KRG27834; APR42_08760. DR Proteomes; UP000051643; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000051643}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000051643}. FT DOMAIN 200 385 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 406 AA; 47174 MW; 7F644216C94D788C CRC64; MIEKTDLTHE KAVLIGIVTK EQGHDKLKEY LDELEFLTYT AGGEVIKRFS QNMDKPNPKT FIGTGKMNEL KEFVDENDVG TAIFDDELSP AQQKNIEKIL KCKVLDRTTL ILDIFAQRAQ TSYARTQVEL AQYEYLLPRL AGMWTHLERQ RGGIGMRGPG ETEIETDRRI VRDKISLLKK KLETIDKQME VQRGNRGQLV RVALVGYTNV GKSTLMNTIS KSEVFAENKL FATLDTTVRK VVIRNLPFLL TDTVGFIRKL PTQLVESFKS TLDEVREADL LLHVVDISHP NFEDHIESVN QIMSEIKSID KPTIMVFNKI DQYEAEEIED DDLMTERTKA HYTLKEWKQT WMNKMGDNVL FISALNKENM EDFRRKVYEA VRKIHITRFP YNNFLYPEYD KYGEEK // ID A0A0R0AYP6_9GAMM Unreviewed; 438 AA. AC A0A0R0AYP6; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=ARC20_04945 {ECO:0000313|EMBL:KRG46663.1}; OS Stenotrophomonas panacihumi. OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales; OC Xanthomonadaceae; Stenotrophomonas. OX NCBI_TaxID=676599 {ECO:0000313|EMBL:KRG46663.1, ECO:0000313|Proteomes:UP000051802}; RN [1] {ECO:0000313|EMBL:KRG46663.1, ECO:0000313|Proteomes:UP000051802} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=JCM 16536 {ECO:0000313|EMBL:KRG46663.1, RC ECO:0000313|Proteomes:UP000051802}; RA Patil P.P., Midha S., Patil P.B.; RT "Genome sequencing and analysis of members of genus RT Stenotrophomonas."; RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KRG46663.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LLXU01000053; KRG46663.1; -; Genomic_DNA. DR RefSeq; WP_057644443.1; NZ_LLXU01000053.1. DR EnsemblBacteria; KRG46663; KRG46663; ARC20_04945. DR Proteomes; UP000051802; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000051802}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000051802}. FT DOMAIN 199 369 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 158 192 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 438 AA; 48279 MW; 59062EB980D1607B CRC64; MFDRSKRGEH ALLIQTHAGG PAEEDVLEEF VDLAKSAGAT VAATLTARID KPSPSTLIGS GKLEEVKAAA DATGADLVLV NHSLSPVQER NLERALQRRV IDRTGLILDI FAQRAHSHEG KLQVELAQLR HLATRLVRGW THLERQRGGS IGLRGPGETQ LETDRRLLQK RVEQLQKRLE KVEVQRTQMR RARVRSELPR IALVGYTNAG KSTLFNALTG AEAYAADQLF ATLDPTVRRI ALPGGNVILA DTVGFVRDLP HELVAAFRST LSEAREADLL LHVVDAADPL REDRIRQVDE VLQAVGAGEL PQLLVFNKID RIEGADVRHD AQDGVPDQAR RERVWISARD GRGLELLQRV LGQRLGLQHV TGSLRLPPSA GRLRSRLHAL EVVQGEQADE EGWLLEVDIP IAEAERLAAS RDGAPIRALL PEPPAEEW // ID A0A0R0BRK9_9GAMM Unreviewed; 436 AA. AC A0A0R0BRK9; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=ABB25_04060 {ECO:0000313|EMBL:KRG59707.1}; OS Stenotrophomonas koreensis. OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales; OC Xanthomonadaceae; Stenotrophomonas. OX NCBI_TaxID=266128 {ECO:0000313|EMBL:KRG59707.1, ECO:0000313|Proteomes:UP000051254}; RN [1] {ECO:0000313|EMBL:KRG59707.1, ECO:0000313|Proteomes:UP000051254} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 17805 {ECO:0000313|EMBL:KRG59707.1, RC ECO:0000313|Proteomes:UP000051254}; RA Patil P.P., Midha S., Patil P.B.; RT "Genome sequencing and analysis of members of genus RT Stenotrophomonas."; RL Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KRG59707.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LDJH01000006; KRG59707.1; -; Genomic_DNA. DR RefSeq; WP_057664043.1; NZ_LDJH01000006.1. DR EnsemblBacteria; KRG59707; KRG59707; ABB25_04060. DR PATRIC; fig|266128.3.peg.2467; -. DR Proteomes; UP000051254; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000051254}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000051254}. FT DOMAIN 198 368 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 157 191 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 436 AA; 47893 MW; CC3A1CA354D24B2C CRC64; MFDRSKRGEH ALLIQPHAGK LEEDVLEEFV DLARSAGASI AATITARIDR PNPSILIGSG KLEEVRAAAD ATEADLILVN HALSPVQERN LERALGRRVI DRTGLILDIF AQRAHSHEGK LQVELAQLRH IATRLVRGWT HLERQRGGSI GLRGPGETQL ETDRRLLQKR VDQLQKRLEK VEVQRTQMRR ARVRSEMPRV ALVGYTNAGK STLFNALAGA QAYAADQLFA TLDPTVRRVG IPGGNVVLAD TVGFVRDLPH ELVAAFRSTL SEAREADLLL HVVDAADPHR QERIAQVDEV LAEVGAGELP QLLVYNKIDR IDGAQPRHDA QDGIADPARR ERVWLSARDG IGLDLLTAAL GARLGFTRIR GQVVLPPSAG RLHARLHALG GIVDEQYTDE GWVLEIDLPR SEAEKLAGSA DGGPLRPLIP QPEPEW // ID A0A0R0C7T0_9GAMM Unreviewed; 436 AA. AC A0A0R0C7T0; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 07-JUN-2017, entry version 13. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=ABB26_04730 {ECO:0000313|EMBL:KRG65126.1}; OS Stenotrophomonas humi. OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales; OC Xanthomonadaceae; Stenotrophomonas. OX NCBI_TaxID=405444 {ECO:0000313|EMBL:KRG65126.1, ECO:0000313|Proteomes:UP000050864}; RN [1] {ECO:0000313|EMBL:KRG65126.1, ECO:0000313|Proteomes:UP000050864} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 18929 {ECO:0000313|EMBL:KRG65126.1, RC ECO:0000313|Proteomes:UP000050864}; RA Patil P.P., Midha S., Patil P.B.; RT "Genome sequencing and analysis of members of genus RT Stenotrophomonas."; RL Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KRG65126.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LDJI01000009; KRG65126.1; -; Genomic_DNA. DR RefSeq; WP_057632440.1; NZ_LDJI01000009.1. DR EnsemblBacteria; KRG65126; KRG65126; ABB26_04730. DR PATRIC; fig|405444.3.peg.3656; -. DR Proteomes; UP000050864; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000050864}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}. FT DOMAIN 198 368 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 157 191 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 436 AA; 48428 MW; 4BB279D707C75B4A CRC64; MFDRSKKGEH ALLIQPHVGR MEEDVLEEFT DLARSAGASI AATLTARMDR PNPSTLIGSG KLDEVKAAAD ATGADLVLVN HQLSPVQERN LERFLERRVI DRTGLILDIF AQRAHSHEGK LQVELAQLRH MATRLVRGWT HLERQRGGAI GLRGPGETQL ETDRRLLQKR VEQLQKRLEK VEVQRTQMRR ARVRSEMPRV ALVGYTNAGK STLFNALTGA DAYAADQLFA TLDPTVRRIM LPGGNAMLAD TVGFVRNLPH ELVAAFRSTL SEAREADFLL HLVDAADPLR EERIAQVDEV LEAVGAGGLP QLLVFNKIDR IEGADVRHDA QDGVPDESRR ERVWISARDG RGLELLQSVL GKRLGLQHVT GTVRLPPSAG RLRSRLHQLE VVRSEQVDEE GWLIEVDLPI AEAEKLAASA EGAIIRALLP EPEPEW // ID A0A0R0C9P0_9GAMM Unreviewed; 436 AA. AC A0A0R0C9P0; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 30-AUG-2017, entry version 12. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=ABB28_17300 {ECO:0000313|EMBL:KRG66333.1}; OS Stenotrophomonas chelatiphaga. OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales; OC Xanthomonadaceae; Stenotrophomonas. OX NCBI_TaxID=517011 {ECO:0000313|EMBL:KRG66333.1, ECO:0000313|Proteomes:UP000051386}; RN [1] {ECO:0000313|EMBL:KRG66333.1, ECO:0000313|Proteomes:UP000051386} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 21508 {ECO:0000313|EMBL:KRG66333.1, RC ECO:0000313|Proteomes:UP000051386}; RA Patil P.P., Midha S., Patil P.B.; RT "Genome sequencing and analysis of members of genus RT Stenotrophomonas."; RL Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KRG66333.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LDJK01000114; KRG66333.1; -; Genomic_DNA. DR RefSeq; WP_057687589.1; NZ_LDJK01000114.1. DR EnsemblBacteria; KRG66333; KRG66333; ABB28_17300. DR PATRIC; fig|517011.3.peg.216; -. DR Proteomes; UP000051386; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000051386}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000051386}. FT DOMAIN 198 368 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 157 191 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 436 AA; 48109 MW; E77A27C2BB8F2C02 CRC64; MFDRSKKGEN ALLIQPHFGK LEEDVLEEFG DLARSAGASI AATITARIDR PNPSTLIGSG KLEEVKAAAD ATGADLILVN HALSPGQERN LEKILERRVI DRTGLILDIF AQRAHSHDGK LQVELAQLRH MSTRLIRGWT HLERQRGGSI GLRGPGETQL ETDRRLLQKR VEQLQKRLEK VEVQRTQMRR ARLRSELPRV ALVGYTNAGK STLFNSLTGA EAYAADQLFA TLDPTVRRIA LPGGNVVLAD TVGFVRDLPH DLVAAFRSTL SEAREADFLL HIVDAADPHR EERIAQVDEV LTAIGAGDLP QLLVFNKIDR IEGAEVRHDG HDGVPDASRR ERVWISARDG RGLDVLEAAL GKRLGLQHVT GELRLPPSQG RLRARLHQLE VVRAETADED GWLLQVEIPI AEAEKLAAGD DGGPIQALLP EKLPEW // ID A0A0R0CVR1_9GAMM Unreviewed; 434 AA. AC A0A0R0CVR1; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=ABB29_08615 {ECO:0000313|EMBL:KRG69841.1}; OS Pseudoxanthomonas dokdonensis. OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales; OC Xanthomonadaceae; Pseudoxanthomonas. OX NCBI_TaxID=344882 {ECO:0000313|EMBL:KRG69841.1, ECO:0000313|Proteomes:UP000052052}; RN [1] {ECO:0000313|EMBL:KRG69841.1, ECO:0000313|Proteomes:UP000052052} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 21858 {ECO:0000313|EMBL:KRG69841.1, RC ECO:0000313|Proteomes:UP000052052}; RA Patil P.P., Midha S., Patil P.B.; RT "Genome sequencing and analysis of members of genus RT Stenotrophomonas."; RL Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KRG69841.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LDJL01000008; KRG69841.1; -; Genomic_DNA. DR RefSeq; WP_057658218.1; NZ_LDJL01000008.1. DR EnsemblBacteria; KRG69841; KRG69841; ABB29_08615. DR PATRIC; fig|344882.3.peg.3079; -. DR Proteomes; UP000052052; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000052052}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000052052}. FT DOMAIN 199 364 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 158 192 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 434 AA; 47928 MW; 86917CE499A0C101 CRC64; MFERSRKGEH ALLIQPYSGG PPDEGASEEF TDLARSAGAS IAALLTARID RPNPATLIGS GKLEEVKAAA DATGADLILV NFPLSPGQER NLEKHLQRRV LDRTGLILDI FAQRARSHEG KLQVELAQLR HMATRLVRGW THLERQRGGS IGLRGPGETQ LETDRRLLQK RVEQLQKRLE KVEVQRTQMR RARVRSELPR VALVGYTNAG KSTLFNALTG ADAYAADQLF ATLDPTVRRV DLSGGSVVLA DTVGFVRDLP HELVAAFRST LSEAREADLL LHVIDAADPV RNDRIGQVDE VLQEIGAGDI PQILVFNKID RIEGAQPRRD QPSEGRERVW LSARDNLGLD LLQAVLAERL GMQRVRGALH LPSRAARLHA RLHALGAIRA ESHNDEGWQL DIDMALADAQ RLAAQADGHL LEPLLPAQEN EPWQ // ID A0A0R0E066_9GAMM Unreviewed; 436 AA. AC A0A0R0E066; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 30-AUG-2017, entry version 12. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=ABB34_08400 {ECO:0000313|EMBL:KRG84770.1}; OS Stenotrophomonas daejeonensis. OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales; OC Xanthomonadaceae; Stenotrophomonas. OX NCBI_TaxID=659018 {ECO:0000313|EMBL:KRG84770.1, ECO:0000313|Proteomes:UP000050940}; RN [1] {ECO:0000313|EMBL:KRG84770.1, ECO:0000313|Proteomes:UP000050940} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=JCM 16244 {ECO:0000313|EMBL:KRG84770.1, RC ECO:0000313|Proteomes:UP000050940}; RA Patil P.P., Midha S., Patil P.B.; RT "Genome sequencing and analysis of members of genus RT Stenotrophomonas."; RL Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KRG84770.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LDJP01000048; KRG84770.1; -; Genomic_DNA. DR RefSeq; WP_057640863.1; NZ_LDJP01000048.1. DR EnsemblBacteria; KRG84770; KRG84770; ABB34_08400. DR PATRIC; fig|659018.3.peg.1627; -. DR Proteomes; UP000050940; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000050940}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000050940}. FT DOMAIN 198 368 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 157 191 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 436 AA; 48388 MW; 218962CBF1CD15DF CRC64; MFDRSKKGEH ALLIQPHFGR LEEDVLEEFT DLARSAGAGI AATVTARIDR PNPSTLIGSG KLDEVKAAAE ATGADLVLVN HPLTPVQERN LERFLERRVI DRTGLILDIF AQRAHSHEGK LQVELAQLRH LATRLVRGWT HLERQRGGSI GLRGPGETQL ETDRRLLQKR VEQLQKRLEK VEVQRTQMRR ARVRSEMPRV ALVGYTNAGK STLFNALTGA GAYAADQLFA TLDPTVRRIA LPGGNAMLAD TVGFVRDLPH ELVAAFRSTL SEAREADFLL HLVDAADPLR EERIAQVDEV LEAVGAGELP QLLVFNKIDR IEGADVRHDA QDGVPDEARR ERVWISARDG RGLELLQSVL GKRLGLQHVT GSVRLPPEAG RLRSRLHQLE VIRSEQADEE GWLVEVDIPI AEAEKLAAGA DGQVIRALLP EREPEW // ID A0A0R0E246_9GAMM Unreviewed; 436 AA. AC A0A0R0E246; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 07-JUN-2017, entry version 14. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:ALJ27876.1}; GN ORFNames=ABB33_13110 {ECO:0000313|EMBL:KRG83779.1}, GN AOT14_14780 {ECO:0000313|EMBL:ALJ27876.1}; OS Stenotrophomonas acidaminiphila. OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales; OC Xanthomonadaceae; Stenotrophomonas. OX NCBI_TaxID=128780 {ECO:0000313|EMBL:KRG83779.1, ECO:0000313|Proteomes:UP000050958}; RN [1] {ECO:0000313|EMBL:ALJ27876.1, ECO:0000313|Proteomes:UP000061010} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ZAC14D2_NAIMI4_2 {ECO:0000313|EMBL:ALJ27876.1, RC ECO:0000313|Proteomes:UP000061010}; RX PubMed=26659678; RA Vinuesa P., Ochoa-Sanchez L.E.; RT "Complete Genome Sequencing of Stenotrophomonas acidaminiphila RT ZAC14D2_NAIMI4_2, a Multidrug-Resistant Strain Isolated from Sediments RT of a Polluted River in Mexico, Uncovers New Antibiotic Resistance RT Genes and a Novel Class-II Lasso Peptide Biosynthesis Gene Cluster."; RL Genome Announc. 3:e01433-15(2015). RN [2] {ECO:0000313|EMBL:KRG83779.1, ECO:0000313|Proteomes:UP000050958} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=JCM 13310 {ECO:0000313|EMBL:KRG83779.1, RC ECO:0000313|Proteomes:UP000050958}; RA Patil P.P., Midha S., Patil P.B.; RT "Genome sequencing and analysis of members of genus RT Stenotrophomonas."; RL Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP012900; ALJ27876.1; -; Genomic_DNA. DR EMBL; LDJO01000042; KRG83779.1; -; Genomic_DNA. DR RefSeq; WP_054664789.1; NZ_LDJO01000042.1. DR EnsemblBacteria; ALJ27876; ALJ27876; AOT14_14780. DR EnsemblBacteria; KRG83779; KRG83779; ABB33_13110. DR KEGG; sacz:AOT14_14780; -. DR PATRIC; fig|128780.6.peg.1487; -. DR KO; K03665; -. DR Proteomes; UP000050958; Unassembled WGS sequence. DR Proteomes; UP000061010; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000050958, KW ECO:0000313|Proteomes:UP000061010}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}. FT DOMAIN 198 368 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 157 191 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 436 AA; 48447 MW; EFC5DD1F6DFC1DCA CRC64; MFDRSKRGEH ALLIQPHSGR LEEDVLEEFT DLARSAGASI AATVTARIDR PNPSTLIGSG KLDEVKAMAD ATGADLVLVN HALTPVQERN LERFLERRVI DRTGLILDIF AQRAHSHEGK LQVELAQLRH LATRLVRGWT HLERQRGGSI GLRGPGETQL ETDRRLLQKR VEQLQKRLEK VEVQRTQMRR ARVRSEMPRV ALVGYTNAGK STLFNALTGA GAYAADQLFA TLDPTVRRIA LPGGNAMLAD TVGFVRDLPH ELVAAFRSTL SEAREADFLL HLVDAADPLR EERIAQVDEV LEAVGAGELP QLLVFNKIDR IEGAEVRHDA QDGVPDEARR ERVWISARDG RGLDLLQSVL GKRLGLQHVT GRVRLPPSAG RLRSRLHQLE VIRSEQADEE GWLIEVDIPI AEAEKLAAGA DGQVIRALLP EREPEW // ID A0A0R0LJ89_9PROT Unreviewed; 421 AA. AC A0A0R0LJ89; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 07-JUN-2017, entry version 10. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:KRH78846.1}; GN ORFNames=FERRO_18440 {ECO:0000313|EMBL:KRH78846.1}; OS Ferrovum sp. JA12. OC Bacteria; Proteobacteria; Betaproteobacteria; Ferrovales; Ferrovaceae; OC Ferrovum. OX NCBI_TaxID=1356299 {ECO:0000313|EMBL:KRH78846.1, ECO:0000313|Proteomes:UP000050960}; RN [1] {ECO:0000313|EMBL:KRH78846.1, ECO:0000313|Proteomes:UP000050960} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=JA12 {ECO:0000313|EMBL:KRH78846.1, RC ECO:0000313|Proteomes:UP000050960}; RA Poehlein A., Ullrich S.R., Tischler J.S., Schloemann M., Muehling M., RA Daniel R.; RT "Genome sequence of the acidophilic iron oxidising Ferrovum strain RT JA12."; RL Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KRH78846.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LJWX01000002; KRH78846.1; -; Genomic_DNA. DR EnsemblBacteria; KRH78846; KRH78846; FERRO_18440. DR PATRIC; fig|1356299.4.peg.1852; -. DR Proteomes; UP000050960; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000050960}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000050960}. FT DOMAIN 226 393 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 421 AA; 47409 MW; E979661558185BDC CRC64; MSDNGPLVGR GRKSSNTHLA QESGSLEQED VYLGRLDHAL LVHIQIDSER SKNNPQELTL LSQTAGLHVD ELITGKRPKP DPATFIGSGK IEEIRQKLRH HEAGLVVFDH EITPIQERNL AHALKARVID RTGLILDIFA QRARSHEGQL QVELAQLERL STRLVRGWTH LERQKGGIGL RGPGETQLET DRRLLSKRVK LLKDRLDKVR KSHRVQRQSR SRAGLLRVSF VGYTNAGKST LFNRLTHAKA YVADQLFATL DTTTRRVYID GIGQMVLSDT VGFIQHLPHT LVAAFKATLD ETIESDLLLH VVDAADKNRD LHQESVNQVL KDIGADHIPQ VLVLNKIDQL VDWQAGLIRD PYGTIEEVHL SAMNGQGMEF IRQAFVERIN DLMQKEDTSI TLDKDLILNY GNQDTKLDRT A // ID A0A0R0MRN3_9BURK Unreviewed; 394 AA. AC A0A0R0MRN3; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=AO057_11155 {ECO:0000313|EMBL:KRI00860.1}; OS Curvibacter sp. PAE-UM. OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Comamonadaceae; Curvibacter. OX NCBI_TaxID=1714344 {ECO:0000313|EMBL:KRI00860.1, ECO:0000313|Proteomes:UP000051912}; RN [1] {ECO:0000313|EMBL:KRI00860.1, ECO:0000313|Proteomes:UP000051912} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=PAE-UM {ECO:0000313|EMBL:KRI00860.1, RC ECO:0000313|Proteomes:UP000051912}; RA Ma D.; RT "The whole genome sequence of a typical ultramicrobacteria PAE-UM from RT river sediment."; RL Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KRI00860.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LKCX01000016; KRI00860.1; -; Genomic_DNA. DR RefSeq; WP_057675872.1; NZ_KQ483358.1. DR EnsemblBacteria; KRI00860; KRI00860; AO057_11155. DR Proteomes; UP000051912; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000051912}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000051912}. FT DOMAIN 200 373 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 394 AA; 43715 MW; 846A9E5A3A972E97 CRC64; MTVLSDQHPA STILVGVDFG LPHFDGELEE LGLLAETAGL HPVGRITCKR KAPDAALFVG SGKAEEIKLL AQQLGASEIL FDQSLSPAQQ RNLERTLELP VNDRTLLILE IFAQRARSHE GKLQVELARL QYLSTRLVRR WSHLERQTGG AGVRGGPGEK QIELDRRMIA ESIKRTKERL HKVKRQRQTQ RRQRERRDAY NISLVGYTNA GKSTLFNSLV KARAYAADQL FATLDTTTRQ LYLGEAGRSV SLSDTVGFIR DLPHGLIDAF QATLQEAVDA DLLLHVVDAA NPNFPEQIAE VQRVLAEIGA EHIPQVLVFN KLDALGPERR PERVQDSYEL DGQAVPRIFV SARDGEGLPA LRQLLAQRVI ASTTVAPEEA EIEADFPDNH ASPF // ID A0A0R1GSW3_9LACO Unreviewed; 425 AA. AC A0A0R1GSW3; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 07-JUN-2017, entry version 12. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=FD07_GL000345 {ECO:0000313|EMBL:KRK37087.1}; OS Lactobacillus parabrevis ATCC 53295. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; OC Lactobacillus. OX NCBI_TaxID=1267003 {ECO:0000313|EMBL:KRK37087.1, ECO:0000313|Proteomes:UP000051176}; RN [1] {ECO:0000313|EMBL:KRK37087.1, ECO:0000313|Proteomes:UP000051176} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 53295 {ECO:0000313|EMBL:KRK37087.1, RC ECO:0000313|Proteomes:UP000051176}; RX PubMed=26415554; DOI=10.1038/ncomms9322; RA Sun Z., Harris H.M., McCann A., Guo C., Argimon S., Zhang W., Yang X., RA Jeffery I.B., Cooney J.C., Kagawa T.F., Liu W., Song Y., Salvetti E., RA Wrobel A., Rasinkangas P., Parkhill J., Rea M.C., O'Sullivan O., RA Ritari J., Douillard F.P., Paul Ross R., Yang R., Briner A.E., RA Felis G.E., de Vos W.M., Barrangou R., Klaenhammer T.R., RA Caufield P.W., Cui Y., Zhang H., O'Toole P.W.; RT "Expanding the biotechnology potential of lactobacilli through RT comparative genomics of 213 strains and associated genera."; RL Nat. Commun. 6:8322-8322(2015). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KRK37087.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AZCZ01000013; KRK37087.1; -; Genomic_DNA. DR RefSeq; WP_020089043.1; NZ_KB911375.1. DR PATRIC; fig|1267003.4.peg.374; -. DR Proteomes; UP000051176; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000051176}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}. FT DOMAIN 202 366 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 425 AA; 47029 MW; 074A9F2119108E87 CRC64; MEETPRTPVI TIGLNAGQAT FNYSMTELRN LVEANNMTVA EEIQQSLTKP NPGTYFGTGK VEELAQIVAD DGVDIIIVND ELTPSQIRNL ENGTKARIID RTGLILEIFA NRAQSREAKL QVQLAMLQYQ LPRLHTSASQ RLDQQTGSGG GGGFTNRGSG ESQTEMSRRT IQRSINHVNH ELKEITQAAA TQRQQRERNE LPSVALVGYT NAGKSTLMNA LVREFGKSED KQVFVKDMLF ATLDTSVRQL VFPDQKKMLL SDTVGFVSQL PTQLVKAFRS TLAEAASADL LVQVVDYADP NREAMMATTE KTLEEIGVTD VPMITVFNKA DLTEASYPSR VGDQLILSAK DSDSIAMLVK AMKEKVFHNY VTANFLVPFS DGEIVSYLNE NANVLDTNYE AEGTALKVEL QQADFDRFKK FVVTE // ID A0A0R1H9U9_9LACO Unreviewed; 424 AA. AC A0A0R1H9U9; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=FC07_GL003013 {ECO:0000313|EMBL:KRK40721.1}; OS Lactobacillus bifermentans DSM 20003. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; OC Lactobacillus. OX NCBI_TaxID=1423726 {ECO:0000313|EMBL:KRK40721.1, ECO:0000313|Proteomes:UP000051461}; RN [1] {ECO:0000313|EMBL:KRK40721.1, ECO:0000313|Proteomes:UP000051461} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 20003 {ECO:0000313|EMBL:KRK40721.1, RC ECO:0000313|Proteomes:UP000051461}; RX PubMed=26415554; DOI=10.1038/ncomms9322; RA Sun Z., Harris H.M., McCann A., Guo C., Argimon S., Zhang W., Yang X., RA Jeffery I.B., Cooney J.C., Kagawa T.F., Liu W., Song Y., Salvetti E., RA Wrobel A., Rasinkangas P., Parkhill J., Rea M.C., O'Sullivan O., RA Ritari J., Douillard F.P., Paul Ross R., Yang R., Briner A.E., RA Felis G.E., de Vos W.M., Barrangou R., Klaenhammer T.R., RA Caufield P.W., Cui Y., Zhang H., O'Toole P.W.; RT "Expanding the biotechnology potential of lactobacilli through RT comparative genomics of 213 strains and associated genera."; RL Nat. Commun. 6:8322-8322(2015). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KRK40721.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AZDA01000005; KRK40721.1; -; Genomic_DNA. DR RefSeq; WP_057903377.1; NZ_AZDA01000005.1. DR EnsemblBacteria; KRK40721; KRK40721; FC07_GL003013. DR PATRIC; fig|1423726.3.peg.3127; -. DR Proteomes; UP000051461; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000051461}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000051461}. FT DOMAIN 199 369 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 424 AA; 47137 MW; 054A75E7A0152E44 CRC64; MLNEAPNVLI GGVNLQATNF DYEVQELAEL VKANGMTVVG EVFQNLERIN AGTYFGVGKI DEIKGLAAEK NAEFLVLNDE LTPAQMSNLD QALPDVKIMD RTGLILAIFA NRAHSREAQL QVQIAQLRYR LPRLRVGGQA NLMQQGGGPG FANRGSGETK LELNQRTIKH HIAQIRKELA QLDVAQATKR QQRDKQELPT VALVGYTNAG KSTTMNGLLQ LFDEAPSKQV FEKDMLFATL DTSVREIHLP SHQKFLLSDT VGFVSKLPTQ LIKAFRSTLA EAAQADLLVQ VIDYSDPNYE QMVQVTEQTL AELDIHDIPM IYAYNKADLR PDTKFPQVNS EHDLIYSAND PASLQQLSDL ITKLLFADHQ VLTYLVPYAD GKWVDYLNEH ASVQSQDYDA TGTKIVASVT PIDAQRLAQF EVTD // ID A0A0R1HQA0_9LACO Unreviewed; 431 AA. AC A0A0R1HQA0; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=FC96_GL001135 {ECO:0000313|EMBL:KRK48816.1}; OS Lactobacillus kimchicus JCM 15530. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; OC Lactobacillus. OX NCBI_TaxID=1302272 {ECO:0000313|EMBL:KRK48816.1, ECO:0000313|Proteomes:UP000050911}; RN [1] {ECO:0000313|EMBL:KRK48816.1, ECO:0000313|Proteomes:UP000050911} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=JCM 15530 {ECO:0000313|EMBL:KRK48816.1, RC ECO:0000313|Proteomes:UP000050911}; RX PubMed=26415554; DOI=10.1038/ncomms9322; RA Sun Z., Harris H.M., McCann A., Guo C., Argimon S., Zhang W., Yang X., RA Jeffery I.B., Cooney J.C., Kagawa T.F., Liu W., Song Y., Salvetti E., RA Wrobel A., Rasinkangas P., Parkhill J., Rea M.C., O'Sullivan O., RA Ritari J., Douillard F.P., Paul Ross R., Yang R., Briner A.E., RA Felis G.E., de Vos W.M., Barrangou R., Klaenhammer T.R., RA Caufield P.W., Cui Y., Zhang H., O'Toole P.W.; RT "Expanding the biotechnology potential of lactobacilli through RT comparative genomics of 213 strains and associated genera."; RL Nat. Commun. 6:8322-8322(2015). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KRK48816.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AZCX01000002; KRK48816.1; -; Genomic_DNA. DR RefSeq; WP_056942014.1; NZ_AZCX01000002.1. DR EnsemblBacteria; KRK48816; KRK48816; FC96_GL001135. DR PATRIC; fig|1302272.5.peg.1143; -. DR Proteomes; UP000050911; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000050911}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000050911}. FT DOMAIN 202 370 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 168 195 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 431 AA; 47676 MW; 9A076B6AF55363EA CRC64; MAEIETEPVI TIGLNTGETD YDYSMAELDA LCEANALAVV ETVTQNLNRP VAATYFGSGK VDELATIVLD TGATMVVAND ELTPSQIRNL EAVVKVPVMD RTGLILAIFS NRAQSREAKL QVELASLQYQ MPRLHTAASQ RLDQQTGTSA GGGFTNRGAG EGQRELNRRV LQRQINHIRH ELKDVNKAAE TKRQQRERVQ LPNVALIGYT NAGKSTIMNA LIKRFGVNED KQVMVKNMLF ATLDTSVRQL QFDDAKKLLL SDTVGFVSKL PTTLVEAFKS TLYEAANADL LVQVVDYSSD NRDDMMTTTM DTLHEIGVPD LPMVTVFNKA DLTETDYPFR TGDDLIISAN DEASINLLVD VIKEKVFKDY VTATFLVPFD KGDVVSYLND HASVLATEYE ATGTLIKAEV TTIDFHRFSD YLVEDRDSAN N // ID A0A0R1HQL6_9LACO Unreviewed; 424 AA. AC A0A0R1HQL6; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=FC66_GL001234 {ECO:0000313|EMBL:KRK45586.1}; OS Lactobacillus algidus DSM 15638. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; OC Lactobacillus. OX NCBI_TaxID=1423719 {ECO:0000313|EMBL:KRK45586.1, ECO:0000313|Proteomes:UP000051450}; RN [1] {ECO:0000313|EMBL:KRK45586.1, ECO:0000313|Proteomes:UP000051450} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 15638 {ECO:0000313|EMBL:KRK45586.1, RC ECO:0000313|Proteomes:UP000051450}; RX PubMed=26415554; DOI=10.1038/ncomms9322; RA Sun Z., Harris H.M., McCann A., Guo C., Argimon S., Zhang W., Yang X., RA Jeffery I.B., Cooney J.C., Kagawa T.F., Liu W., Song Y., Salvetti E., RA Wrobel A., Rasinkangas P., Parkhill J., Rea M.C., O'Sullivan O., RA Ritari J., Douillard F.P., Paul Ross R., Yang R., Briner A.E., RA Felis G.E., de Vos W.M., Barrangou R., Klaenhammer T.R., RA Caufield P.W., Cui Y., Zhang H., O'Toole P.W.; RT "Expanding the biotechnology potential of lactobacilli through RT comparative genomics of 213 strains and associated genera."; RL Nat. Commun. 6:8322-8322(2015). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KRK45586.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AZDI01000006; KRK45586.1; -; Genomic_DNA. DR RefSeq; WP_057974293.1; NZ_AZDI01000006.1. DR EnsemblBacteria; KRK45586; KRK45586; FC66_GL001234. DR PATRIC; fig|1423719.4.peg.1255; -. DR Proteomes; UP000051450; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000051450}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000051450}. FT DOMAIN 203 333 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 424 AA; 47512 MW; F1FCDB806D632776 CRC64; MKETYSTEIP VIDVFIAGIE KQRENLDYTM SELAALVEAN NMHAVEDIRQ KLDRPTAALY FGKGKAEEFK TESEAQGVKI LVVNDELSPT QIRNLEAASG MEVMDRTGLI LAIFASRAQS REAKLQVQMA QLQYQLPRLR GMQAKLDQQS GGAGLANRGA GETKIELDRR VIENRITHIK KDLAEMDKEE STRRKQRDKS GIPTVALVGY TNSGKSTTMN GLLRLIGQDE DKQVFEKNML FATLDTSVRN IQFEDKKQIL LSDTVGFVSK LPHQLVKAFR TTLAEAAQAD LLIQVIDVAD KHAEEMIQTT EETLKAIGVE NIPMIYAYNK ADLADIAYPT FSDDKFTYSA RDEASLNQLV DIIKKNVFKD NEIMTVLIPF DKGQLVDLIN EKATILETTY EESGTKLKID APKIIANQVQ EYIV // ID A0A0R1IXH1_9LACO Unreviewed; 430 AA. AC A0A0R1IXH1; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=FC72_GL000842 {ECO:0000313|EMBL:KRK63957.1}; OS Lactobacillus tucceti DSM 20183. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; OC Lactobacillus. OX NCBI_TaxID=1423811 {ECO:0000313|EMBL:KRK63957.1, ECO:0000313|Proteomes:UP000050929}; RN [1] {ECO:0000313|EMBL:KRK63957.1, ECO:0000313|Proteomes:UP000050929} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 20183 {ECO:0000313|EMBL:KRK63957.1, RC ECO:0000313|Proteomes:UP000050929}; RX PubMed=26415554; DOI=10.1038/ncomms9322; RA Sun Z., Harris H.M., McCann A., Guo C., Argimon S., Zhang W., Yang X., RA Jeffery I.B., Cooney J.C., Kagawa T.F., Liu W., Song Y., Salvetti E., RA Wrobel A., Rasinkangas P., Parkhill J., Rea M.C., O'Sullivan O., RA Ritari J., Douillard F.P., Paul Ross R., Yang R., Briner A.E., RA Felis G.E., de Vos W.M., Barrangou R., Klaenhammer T.R., RA Caufield P.W., Cui Y., Zhang H., O'Toole P.W.; RT "Expanding the biotechnology potential of lactobacilli through RT comparative genomics of 213 strains and associated genera."; RL Nat. Commun. 6:8322-8322(2015). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KRK63957.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AZDG01000019; KRK63957.1; -; Genomic_DNA. DR EnsemblBacteria; KRK63957; KRK63957; FC72_GL000842. DR PATRIC; fig|1423811.3.peg.854; -. DR Proteomes; UP000050929; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000050929}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Hydrolase {ECO:0000313|EMBL:KRK63957.1}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Protease {ECO:0000313|EMBL:KRK63957.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000050929}. FT DOMAIN 206 380 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 430 AA; 48595 MW; 499D88A9943C29E2 CRC64; MPPGGSMKEL NNTKERVIVA GVSHLQPDFE YTMEELASLV EANNMEVADT IKQKADSVSA KTYFGSGKVT EIKEIANADD VKTIVLNDEL TPSQIRNLEK ETKLSFMDRT ELILQVFSNR AHTKQAKLQV EIAKLQYQLP RIHPSGNPLD QQSASGGLAN RGAGETKLEL DRRVIRKRIT YLKDQLKTVD KTINVQSRKR TNTTMPLVSL VGYTNAGKST TMNGLLNFNK EDSDDRKVFE KDMLFATLDT SVRKIDLEDN TSFLLSDTVG FVSKLPHNLI ESFKTTLKEA KDADLLVQVI DVSDEHWRNM LEVTEKTLKE VGVKDKPMIY AFNKADLKPD QVFPSIEGDN IYYSALDKKS IDTLVDLIKK KLYANFKMTN LLIPYDKQKV AEKVLRNSQI IKKEFLNEGS SITANLSPDE LNEYSEFIKE // ID A0A0R1JHR7_9LACO Unreviewed; 426 AA. AC A0A0R1JHR7; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=FD02_GL000034 {ECO:0000313|EMBL:KRK70853.1}; OS Lactobacillus nasuensis JCM 17158. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; OC Lactobacillus. OX NCBI_TaxID=1291734 {ECO:0000313|EMBL:KRK70853.1, ECO:0000313|Proteomes:UP000051804}; RN [1] {ECO:0000313|EMBL:KRK70853.1, ECO:0000313|Proteomes:UP000051804} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=JCM 17158 {ECO:0000313|EMBL:KRK70853.1, RC ECO:0000313|Proteomes:UP000051804}; RX PubMed=26415554; DOI=10.1038/ncomms9322; RA Sun Z., Harris H.M., McCann A., Guo C., Argimon S., Zhang W., Yang X., RA Jeffery I.B., Cooney J.C., Kagawa T.F., Liu W., Song Y., Salvetti E., RA Wrobel A., Rasinkangas P., Parkhill J., Rea M.C., O'Sullivan O., RA Ritari J., Douillard F.P., Paul Ross R., Yang R., Briner A.E., RA Felis G.E., de Vos W.M., Barrangou R., Klaenhammer T.R., RA Caufield P.W., Cui Y., Zhang H., O'Toole P.W.; RT "Expanding the biotechnology potential of lactobacilli through RT comparative genomics of 213 strains and associated genera."; RL Nat. Commun. 6:8322-8322(2015). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KRK70853.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AZDJ01000030; KRK70853.1; -; Genomic_DNA. DR RefSeq; WP_056951512.1; NZ_AZDJ01000030.1. DR EnsemblBacteria; KRK70853; KRK70853; FD02_GL000034. DR PATRIC; fig|1291734.4.peg.37; -. DR Proteomes; UP000051804; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000051804}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000051804}. FT DOMAIN 200 370 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 159 186 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 426 AA; 47109 MW; 730008A436D4D5A0 CRC64; MQDNQPQSEL VLIAGISRGQ DNFDYSMTEL TELAKAHGDT VVADVRQNLD RAIGATYFGK GKVDEIAELA RANDATTVII NDELSPSQLR NLNKLIGLHV IDRTQLILDI FADRAKSKAA KTQVEIAQLQ YALPRLHPSA NKLDQQGGGG GLANRGAGET KLEMDKRVLN KRIARLRREL KEADVGAQVR RVQRDTNAVP VVALVGYTNA GKSTTMNGLL DLYADHPETK QVFEKDMLFA TLDTSVRQLT LPDNRKFLLS DTVGFVSKLP HHLIDAFKAT LAEAANADLL IQVVDYSDPH YPEMMQITEQ TLKTIGIHDI PMITAYNKAD KRPDTHYPEL NGDQFIYSAQ DPASLHQLAR LITKHIFADA ETHTYLIPFS EGQLVDFMNR ETAVSATDYT DDGTRITATV NAAQAGRLAQ YLVTES // ID A0A0R1KBW5_9LACO Unreviewed; 426 AA. AC A0A0R1KBW5; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 07-JUN-2017, entry version 12. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=FD03_GL000725 {ECO:0000313|EMBL:KRK81133.1}; OS Lactobacillus nodensis DSM 19682 = JCM 14932 = NBRC 107160. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; OC Lactobacillus. OX NCBI_TaxID=1423775 {ECO:0000313|EMBL:KRK81133.1, ECO:0000313|Proteomes:UP000051248}; RN [1] {ECO:0000313|EMBL:KRK81133.1, ECO:0000313|Proteomes:UP000051248} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 19682 {ECO:0000313|EMBL:KRK81133.1, RC ECO:0000313|Proteomes:UP000051248}; RX PubMed=26415554; DOI=10.1038/ncomms9322; RA Sun Z., Harris H.M., McCann A., Guo C., Argimon S., Zhang W., Yang X., RA Jeffery I.B., Cooney J.C., Kagawa T.F., Liu W., Song Y., Salvetti E., RA Wrobel A., Rasinkangas P., Parkhill J., Rea M.C., O'Sullivan O., RA Ritari J., Douillard F.P., Paul Ross R., Yang R., Briner A.E., RA Felis G.E., de Vos W.M., Barrangou R., Klaenhammer T.R., RA Caufield P.W., Cui Y., Zhang H., O'Toole P.W.; RT "Expanding the biotechnology potential of lactobacilli through RT comparative genomics of 213 strains and associated genera."; RL Nat. Commun. 6:8322-8322(2015). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KRK81133.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AZDZ01000001; KRK81133.1; -; Genomic_DNA. DR RefSeq; WP_025023317.1; NZ_BCWC01000006.1. DR EnsemblBacteria; KRK81133; KRK81133; FD03_GL000725. DR PATRIC; fig|1423775.4.peg.741; -. DR Proteomes; UP000051248; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000051248}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000051248}. FT DOMAIN 200 370 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 426 AA; 48126 MW; 5681A315646A7534 CRC64; MENTINAKER VIVAGVSHKQ LDFDYTMEEL GSLVEANNME VADVIKQNVD SVSAKTYFGS GKVTEIKEIA NADDVTTIVL NDELTPSQIR NLEKETKLSF MDRTELILQV FSNRAHTRQA KLQVEIAKLQ YQLPRIHPSG NPLDQQSSSG GLANRGAGET KLELDRRVIR KRITYLKDQL KTVDKTINVQ SRRRTNTSLP LVSLVGYTNA GKSTTMNGLL NFNKEDSDDR KVFEKDMLFA TLDTSVRKID LEDNTSFLLS DTVGFVSKLP HNLIESFKTT LKEAKDADLL VQVIDVSDEH WKNMLEVTEN TLREVGVTGK PMIYAFNKAD LKPDQVFPTI EGDNIYYSAL DDSSIQKLVE LIKMKLYSGY QTVDLLIPYD KQKLTEQLLK NAQIISKEFT NDGSLLKANL SPDELERYEQ FVQVNA // ID A0A0R1LVP8_9LACO Unreviewed; 425 AA. AC A0A0R1LVP8; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=FD04_GL001883 {ECO:0000313|EMBL:KRK97025.1}; OS Lactobacillus odoratitofui DSM 19909 = JCM 15043. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; OC Lactobacillus. OX NCBI_TaxID=1423776 {ECO:0000313|EMBL:KRK97025.1, ECO:0000313|Proteomes:UP000051160}; RN [1] {ECO:0000313|EMBL:KRK97025.1, ECO:0000313|Proteomes:UP000051160} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 19909 {ECO:0000313|EMBL:KRK97025.1, RC ECO:0000313|Proteomes:UP000051160}; RX PubMed=26415554; DOI=10.1038/ncomms9322; RA Sun Z., Harris H.M., McCann A., Guo C., Argimon S., Zhang W., Yang X., RA Jeffery I.B., Cooney J.C., Kagawa T.F., Liu W., Song Y., Salvetti E., RA Wrobel A., Rasinkangas P., Parkhill J., Rea M.C., O'Sullivan O., RA Ritari J., Douillard F.P., Paul Ross R., Yang R., Briner A.E., RA Felis G.E., de Vos W.M., Barrangou R., Klaenhammer T.R., RA Caufield P.W., Cui Y., Zhang H., O'Toole P.W.; RT "Expanding the biotechnology potential of lactobacilli through RT comparative genomics of 213 strains and associated genera."; RL Nat. Commun. 6:8322-8322(2015). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KRK97025.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AZEE01000030; KRK97025.1; -; Genomic_DNA. DR RefSeq; WP_056948839.1; NZ_AZEE01000030.1. DR EnsemblBacteria; KRK97025; KRK97025; FD04_GL001883. DR PATRIC; fig|1423776.4.peg.1906; -. DR Proteomes; UP000051160; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000051160}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000051160}. FT DOMAIN 202 370 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 425 AA; 47472 MW; F6A308797A618353 CRC64; MENSELVPVI NIGLNTGRYN FDYAMEELKA LSQANNMTVI ETIVQNLSQP IAGTYFGTGK VEELRDVVVD TGAEIVVAND ELTPSQIRNL ENVVKVPVMD RTGLILAIFA NRAQSREAKL QVELAKLQYQ MPRLHTAMNQ RLDQQTGTSA GGGFTNRGAG EAQVELNRRT IQRQINHVRH ELKEVNKSAE VKRQQRERVQ LPNVALIGYT NAGKSTIMNE LIKRFGMNDD KQVMVKNMLF ATLDTSVRQL QFEDTKKLLL SDTVGFVSQL PTTLVEAFKS TLYEAANADL LVQVVDYSSP NRIDMMSTTK QTLNEIGVPD LPMVTVYNKA DLTDSDYPSR AGDEIVVSAK DPASIDLLVD VIREKVFKNY VKATFLIPFD RGDLVSYLNE HASVTGTDYL ADGTQLDAEV TDIDFQRLQK FVVEK // ID A0A0R1M8C6_9LACO Unreviewed; 419 AA. AC A0A0R1M8C6; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 07-JUN-2017, entry version 12. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=FC81_GL002071 {ECO:0000313|EMBL:KRL00539.1}; OS Lactobacillus capillatus DSM 19910. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; OC Lactobacillus. OX NCBI_TaxID=1423731 {ECO:0000313|EMBL:KRL00539.1, ECO:0000313|Proteomes:UP000051621}; RN [1] {ECO:0000313|EMBL:KRL00539.1, ECO:0000313|Proteomes:UP000051621} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 19910 {ECO:0000313|EMBL:KRL00539.1, RC ECO:0000313|Proteomes:UP000051621}; RX PubMed=26415554; DOI=10.1038/ncomms9322; RA Sun Z., Harris H.M., McCann A., Guo C., Argimon S., Zhang W., Yang X., RA Jeffery I.B., Cooney J.C., Kagawa T.F., Liu W., Song Y., Salvetti E., RA Wrobel A., Rasinkangas P., Parkhill J., Rea M.C., O'Sullivan O., RA Ritari J., Douillard F.P., Paul Ross R., Yang R., Briner A.E., RA Felis G.E., de Vos W.M., Barrangou R., Klaenhammer T.R., RA Caufield P.W., Cui Y., Zhang H., O'Toole P.W.; RT "Expanding the biotechnology potential of lactobacilli through RT comparative genomics of 213 strains and associated genera."; RL Nat. Commun. 6:8322-8322(2015). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KRL00539.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AZEF01000042; KRL00539.1; -; Genomic_DNA. DR RefSeq; WP_057746145.1; NZ_AZEF01000042.1. DR EnsemblBacteria; KRL00539; KRL00539; FC81_GL002071. DR PATRIC; fig|1423731.3.peg.2128; -. DR Proteomes; UP000051621; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000051621}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000051621}. FT DOMAIN 194 365 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 419 AA; 47183 MW; E6552BD58AE1716A CRC64; MIKVIIAGIE NQQSNFDYLM QELAELAYAN NMQVVADIRQ GLQRPVAATY LGKGKIEELS RLAEVKGAEM LILNDELSPT QIRNLEKETA LAVLDRTELI LEIFSSRART KEAQLQVEIA RLKYKLPRLR TSSNEKLDQQ SSGGSLANRG AGETKLEINR RTIQKRIAQL SRDLKNLDKE QEIQSSSRRE SGLPSVALVG YTNSGKSTTM NGLLNLLSDT DIPPAKQVMT KDMLFATLDT SVRKLRFQDK REFLLSDTVG FVSKLPHNLV KAFQSTLAEV KNADLLLHVV DLSDKHSAEM VKVTTETLKE LGVENTPTIY AFNKADKTDS RYPVIEGQQI TYSARDAKSL HALADLIKRV LFKDYKTHKY FISFEQGRYL EKINQLALVT DTTYNENGAI ITAEISPAQE EYFARFLTE // ID A0A0R1MBP4_9LACO Unreviewed; 417 AA. AC A0A0R1MBP4; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 07-JUN-2017, entry version 10. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=FD46_GL000401 {ECO:0000313|EMBL:KRL05655.1}; OS Lactobacillus oeni DSM 19972. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; OC Lactobacillus. OX NCBI_TaxID=1423777 {ECO:0000313|EMBL:KRL05655.1, ECO:0000313|Proteomes:UP000051686}; RN [1] {ECO:0000313|EMBL:KRL05655.1, ECO:0000313|Proteomes:UP000051686} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 19972 {ECO:0000313|EMBL:KRL05655.1, RC ECO:0000313|Proteomes:UP000051686}; RX PubMed=26415554; DOI=10.1038/ncomms9322; RA Sun Z., Harris H.M., McCann A., Guo C., Argimon S., Zhang W., Yang X., RA Jeffery I.B., Cooney J.C., Kagawa T.F., Liu W., Song Y., Salvetti E., RA Wrobel A., Rasinkangas P., Parkhill J., Rea M.C., O'Sullivan O., RA Ritari J., Douillard F.P., Paul Ross R., Yang R., Briner A.E., RA Felis G.E., de Vos W.M., Barrangou R., Klaenhammer T.R., RA Caufield P.W., Cui Y., Zhang H., O'Toole P.W.; RT "Expanding the biotechnology potential of lactobacilli through RT comparative genomics of 213 strains and associated genera."; RL Nat. Commun. 6:8322-8322(2015). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KRL05655.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AZEH01000020; KRL05655.1; -; Genomic_DNA. DR RefSeq; WP_057895399.1; NZ_AZEH01000020.1. DR EnsemblBacteria; KRL05655; KRL05655; FD46_GL000401. DR PATRIC; fig|1423777.3.peg.422; -. DR Proteomes; UP000051686; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000051686}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000051686}. FT DOMAIN 194 362 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 160 187 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 417 AA; 46528 MW; BAE76172A9B68557 CRC64; MTRAIIAGIE NQQKNFSYLM KELAQLAEAN GMETVADFSQ KIDKPIAATY LGKGKIEEIA KAAQHYDAQY LILNDELSPT QIRNLEKETA LSVLDRTELI LEIFSNRAHT KEAQLQVEIA RLKYQLPRLR SSSAISMDQQ SAGSSAANRG AGETKLELNR RTIQHRIAFL NRELKAIEKE YDVKSKSRRE SEVPRVALVG YTNAGKSTTL NGLISLLGGE EKQMVFEKDM LFATLDTSVR KLTFSDNKTF LLSDTVGFVN KLPHTLIEAF KSTLAEVREA DLLIQVVDIS DESSKEMIET TNRTLEEIGA ANKPMIYAYN KADKAGIDFP SIEGLQITYS AKEKSSLQQL AGLIKGFLFK GYKTYTYLIP YTQGSYLEKL NVHANVLATD YTPDGSKVTA EVSPRQAGYY AKFLVKS // ID A0A0R1MTD0_9LACO Unreviewed; 434 AA. AC A0A0R1MTD0; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=FD09_GL000923 {ECO:0000313|EMBL:KRL10777.1}; OS Lactobacillus perolens DSM 12744. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; OC Lactobacillus. OX NCBI_TaxID=1423792 {ECO:0000313|EMBL:KRL10777.1, ECO:0000313|Proteomes:UP000051330}; RN [1] {ECO:0000313|EMBL:KRL10777.1, ECO:0000313|Proteomes:UP000051330} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 12744 {ECO:0000313|EMBL:KRL10777.1, RC ECO:0000313|Proteomes:UP000051330}; RX PubMed=26415554; DOI=10.1038/ncomms9322; RA Sun Z., Harris H.M., McCann A., Guo C., Argimon S., Zhang W., Yang X., RA Jeffery I.B., Cooney J.C., Kagawa T.F., Liu W., Song Y., Salvetti E., RA Wrobel A., Rasinkangas P., Parkhill J., Rea M.C., O'Sullivan O., RA Ritari J., Douillard F.P., Paul Ross R., Yang R., Briner A.E., RA Felis G.E., de Vos W.M., Barrangou R., Klaenhammer T.R., RA Caufield P.W., Cui Y., Zhang H., O'Toole P.W.; RT "Expanding the biotechnology potential of lactobacilli through RT comparative genomics of 213 strains and associated genera."; RL Nat. Commun. 6:8322-8322(2015). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KRL10777.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AZEC01000014; KRL10777.1; -; Genomic_DNA. DR RefSeq; WP_057821983.1; NZ_AZEC01000014.1. DR EnsemblBacteria; KRL10777; KRL10777; FD09_GL000923. DR PATRIC; fig|1423792.3.peg.943; -. DR Proteomes; UP000051330; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000051330}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000051330}. FT DOMAIN 205 373 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 434 AA; 48388 MW; 1C15C1BB9509FFA1 CRC64; MNEITTQTIS TIIVGLDMQQ PDFTYTMTEL GELVAAAGMT VVGQMTQRSD RPDPATYFGK GKVEEIAERA RATDAPIVVV NSDLSPSQTR NLEKAMKLSV MDRTELILRI FASRARSREA KLQVGIAKEE YALPRIHPSS NPLDQQGGGR GNSGGATANR GTGETQLELD KRVIKKRITH MRHELKEIMR AQDTRRDRRI HQALPSVALV GYTNAGKSTT MNSMLQQFGL ADKQVFVKNQ LFATLDTSVR KIQLPTNRHF LLSDTVGFVS HLPHHLVESF KATLKEAADA DLLIQVVDFA DPHYKEMMET TEQTLDAIGV KNIPMLTVYN KADLRPDTHY PDREGNTLTL SATDPKSIQM LADTLDELLF KDYQDTTLLV PFTKGDIVNY LRDNTEVKNE HYTDEGTAIT TILGPIDRSK FAAYIQTNPV PTKA // ID A0A0R1PCU8_9LACO Unreviewed; 425 AA. AC A0A0R1PCU8; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=FD27_GL000259 {ECO:0000313|EMBL:KRL27986.1}; OS Lactobacillus frumenti DSM 13145. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; OC Lactobacillus. OX NCBI_TaxID=1423746 {ECO:0000313|EMBL:KRL27986.1, ECO:0000313|Proteomes:UP000051445}; RN [1] {ECO:0000313|EMBL:KRL27986.1, ECO:0000313|Proteomes:UP000051445} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 13145 {ECO:0000313|EMBL:KRL27986.1, RC ECO:0000313|Proteomes:UP000051445}; RX PubMed=26415554; DOI=10.1038/ncomms9322; RA Sun Z., Harris H.M., McCann A., Guo C., Argimon S., Zhang W., Yang X., RA Jeffery I.B., Cooney J.C., Kagawa T.F., Liu W., Song Y., Salvetti E., RA Wrobel A., Rasinkangas P., Parkhill J., Rea M.C., O'Sullivan O., RA Ritari J., Douillard F.P., Paul Ross R., Yang R., Briner A.E., RA Felis G.E., de Vos W.M., Barrangou R., Klaenhammer T.R., RA Caufield P.W., Cui Y., Zhang H., O'Toole P.W.; RT "Expanding the biotechnology potential of lactobacilli through RT comparative genomics of 213 strains and associated genera."; RL Nat. Commun. 6:8322-8322(2015). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KRL27986.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AZER01000013; KRL27986.1; -; Genomic_DNA. DR RefSeq; WP_057748986.1; NZ_AZER01000013.1. DR EnsemblBacteria; KRL27986; KRL27986; FD27_GL000259. DR PATRIC; fig|1423746.3.peg.266; -. DR Proteomes; UP000051445; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000051445}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000051445}. FT DOMAIN 202 371 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 425 AA; 48208 MW; 91E6616812A58963 CRC64; METNIQTEEQ VLISGLNTEQ EDFDYSMREL AELAQANHME VVGQVSQAID RPNPATYFGS GKVEELKERV FNDHVHTLIT NDELTPSQLR NLENELGCRV LDRTALILEI FAERAKSKEA KLQVQIAQLQ YRLPRLQTSA NQRLDQQTGG GSGFTNRGSG ETQLEMDRRT IQRSINHLRH ELSAIDRSEE VKRKQREKSN IPTAALVGYT NAGKSTIMNG LVRRYGAVED KTVFEKDMLF ATLDTSVRQL HLPDQKRFLL SDTVGFVSKL PTHLVESFKS TLAEAASADL LIQVIDVSDP HYEEMMKTTS KTLKQIGIEN IPMIYVFNKA DKTEMEYPVM EGDDRIIISA KQSESLDLLT SVIRKHLFKD YVEAKMLVPF KDGAVVSYFN EHTNILNTEY QSSGTLLTLE LSAEDYAKYE KYAVK // ID A0A0R1QFG6_9LACO Unreviewed; 436 AA. AC A0A0R1QFG6; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 07-JUN-2017, entry version 12. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=FD29_GL000736 {ECO:0000313|EMBL:KRL43591.1}; OS Lactobacillus mindensis DSM 14500. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; OC Lactobacillus. OX NCBI_TaxID=1423770 {ECO:0000313|EMBL:KRL43591.1, ECO:0000313|Proteomes:UP000050872}; RN [1] {ECO:0000313|EMBL:KRL43591.1, ECO:0000313|Proteomes:UP000050872} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 14500 {ECO:0000313|EMBL:KRL43591.1, RC ECO:0000313|Proteomes:UP000050872}; RX PubMed=26415554; DOI=10.1038/ncomms9322; RA Sun Z., Harris H.M., McCann A., Guo C., Argimon S., Zhang W., Yang X., RA Jeffery I.B., Cooney J.C., Kagawa T.F., Liu W., Song Y., Salvetti E., RA Wrobel A., Rasinkangas P., Parkhill J., Rea M.C., O'Sullivan O., RA Ritari J., Douillard F.P., Paul Ross R., Yang R., Briner A.E., RA Felis G.E., de Vos W.M., Barrangou R., Klaenhammer T.R., RA Caufield P.W., Cui Y., Zhang H., O'Toole P.W.; RT "Expanding the biotechnology potential of lactobacilli through RT comparative genomics of 213 strains and associated genera."; RL Nat. Commun. 6:8322-8322(2015). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KRL43591.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AZEZ01000076; KRL43591.1; -; Genomic_DNA. DR EnsemblBacteria; KRL43591; KRL43591; FD29_GL000736. DR PATRIC; fig|1423770.3.peg.757; -. DR Proteomes; UP000050872; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000050872}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}. FT DOMAIN 208 378 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 436 AA; 49078 MW; 3A4223316BF2B3C4 CRC64; MPPGGFMKDS KLTFEKTRVI VAGVSHLQPD FEYTMQELAA LVEANNMEVA DTIIQNANTV SGATYFGSGK VTEIKEIANA DDVQIIVLND ELTPSQIRNL EKETKLSFMD RTELILQVFS NRAQTKQAKL QVEIAKMQYQ LPRIHPSGNP LDQQSASGGL ANRGAGESKL ELDRRVIRKR ITALRNELKT VDQTVDVQSK RRTNTSLPLV SLVGYTNAGK STTMNGILNF NKEDSQDRKV FEKNMLFATL DTSVRRIDLA DNSSFLLSDT VGFVSKLPHN LVESFKTTLQ EAQNADLLIQ VIDVSDEHWR NMIEVTEKTL KEVGVVDKPM IYAFNKADLK PGQQFPTIEG DNIYYSAIDK DSIEKLVDLI KIKVFNNFKE TTLLIPYNEQ KVAEEILRNS QVIKKEFTND GSLITANLSP NELEKFNKYI QTEMSN // ID A0A0R1QHZ6_9LACO Unreviewed; 424 AA. AC A0A0R1QHZ6; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=FD01_GL001152 {ECO:0000313|EMBL:KRL44413.1}; OS Lactobacillus manihotivorans DSM 13343 = JCM 12514. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; OC Lactobacillus. OX NCBI_TaxID=1423769 {ECO:0000313|EMBL:KRL44413.1, ECO:0000313|Proteomes:UP000051790}; RN [1] {ECO:0000313|EMBL:KRL44413.1, ECO:0000313|Proteomes:UP000051790} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 13343 {ECO:0000313|EMBL:KRL44413.1, RC ECO:0000313|Proteomes:UP000051790}; RX PubMed=26415554; DOI=10.1038/ncomms9322; RA Sun Z., Harris H.M., McCann A., Guo C., Argimon S., Zhang W., Yang X., RA Jeffery I.B., Cooney J.C., Kagawa T.F., Liu W., Song Y., Salvetti E., RA Wrobel A., Rasinkangas P., Parkhill J., Rea M.C., O'Sullivan O., RA Ritari J., Douillard F.P., Paul Ross R., Yang R., Briner A.E., RA Felis G.E., de Vos W.M., Barrangou R., Klaenhammer T.R., RA Caufield P.W., Cui Y., Zhang H., O'Toole P.W.; RT "Expanding the biotechnology potential of lactobacilli through RT comparative genomics of 213 strains and associated genera."; RL Nat. Commun. 6:8322-8322(2015). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KRL44413.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AZEU01000155; KRL44413.1; -; Genomic_DNA. DR RefSeq; WP_056963846.1; NZ_AZEU01000155.1. DR EnsemblBacteria; KRL44413; KRL44413; FD01_GL001152. DR PATRIC; fig|1423769.4.peg.1244; -. DR Proteomes; UP000051790; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000051790}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000051790}. FT DOMAIN 199 369 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 424 AA; 47407 MW; ABBE1F26CB43E5C6 CRC64; MQENILQPEK VLVTGISRGR EDFDYTMTEL VELAKANNYD VVGELRQNLD RSTAAFYFGS GKVEEIRELA DAYDATTVLV NDELSPSQLR NLERETKHHI VDRTQLILEI FANRAQSKTA KMQVEIAQLQ YALPRLHPSA NKLDQQGGGG VANRGAGETK LEMDKRVLNK RIARLRRELK DADVGEEVRR AKRTDKELPT VALVGYTNAG KSTTMNGLLE KFADHPETKQ VFEKDMLFAT LDTSVRQITL PNNRKFLLSD TVGFVSKLPH TLVDAFKATL AEAASADLLI QVVDYADPHY PDMMQVTEKT LDSIGIHDIP MIVAYNKADL KAGTVFPEVN GDDLIYSARD AASLDKLTEL IQSHLFAQDV TNQYLIPFDK GQVVDFINRE TSVENTDYTE NGTLITTTVN PIQAGQLRDY LVEA // ID A0A0R1RE47_9LACO Unreviewed; 424 AA. AC A0A0R1RE47; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 07-JUN-2017, entry version 12. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=FC70_GL000889 {ECO:0000313|EMBL:KRL55293.1}, GN LACOL_0408 {ECO:0000313|EMBL:CUS25716.1}; OS Lactobacillus oligofermentans DSM 15707 = LMG 22743. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; OC Lactobacillus. OX NCBI_TaxID=1423778 {ECO:0000313|EMBL:KRL55293.1, ECO:0000313|Proteomes:UP000051697}; RN [1] {ECO:0000313|EMBL:KRL55293.1, ECO:0000313|Proteomes:UP000051697} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 15707 {ECO:0000313|EMBL:KRL55293.1, RC ECO:0000313|Proteomes:UP000051697}; RX PubMed=26415554; DOI=10.1038/ncomms9322; RA Sun Z., Harris H.M., McCann A., Guo C., Argimon S., Zhang W., Yang X., RA Jeffery I.B., Cooney J.C., Kagawa T.F., Liu W., Song Y., Salvetti E., RA Wrobel A., Rasinkangas P., Parkhill J., Rea M.C., O'Sullivan O., RA Ritari J., Douillard F.P., Paul Ross R., Yang R., Briner A.E., RA Felis G.E., de Vos W.M., Barrangou R., Klaenhammer T.R., RA Caufield P.W., Cui Y., Zhang H., O'Toole P.W.; RT "Expanding the biotechnology potential of lactobacilli through RT comparative genomics of 213 strains and associated genera."; RL Nat. Commun. 6:8322-8322(2015). RN [2] {ECO:0000313|EMBL:CUS25716.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=LACOL {ECO:0000313|EMBL:CUS25716.1}; RA Millard Andrew; RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LN898144; CUS25716.1; -; Genomic_DNA. DR EMBL; AZFE01000031; KRL55293.1; -; Genomic_DNA. DR RefSeq; WP_057889845.1; NZ_AZFE01000031.1. DR EnsemblBacteria; KRL55293; KRL55293; FC70_GL000889. DR PATRIC; fig|1423778.4.peg.922; -. DR Proteomes; UP000051697; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000051697}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000051697}. FT DOMAIN 202 371 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 424 AA; 47399 MW; 5B0E330B378E40E7 CRC64; MDTMPPIESV IIAGLNNSQT SFEYSMNELA ELVKANNMEV KDKLVQNLDR PNAATYFGKG KVEELAEAAR AADVHTIVTN DELSPSQIRN LEAATGARLL DRTALILEIF AKRAQSKEAK LQVEIAQLKY RLPRLRTSAN QSLDQQTGAG GGSFTNRGSG ETKLEMNRRT IENSIAHLRG ELDEINKSAV TRRQQRIKNE MPMVALVGYT NAGKSTVMNG LVRNYGVDED KQVFEKDMLF ATLDTSVRRL TLPDQKEFLL SDTVGFVSKL PHNLVESFKS TLAEASQADL LLQVIDYSDP HHQEMMKTTA DTLEAIGIKD IPMINIFNKA DKMEISYPTM EGENQIIMSA IQPESLDMLT DLIKKIIFKD FVTTTLLIPF TEGNVVAYLN EKANVINTDY VANGTQIEVE LSTNDYKRYA KYEL // ID A0A0R1RI43_9LACO Unreviewed; 426 AA. AC A0A0R1RI43; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=FD35_GL000754 {ECO:0000313|EMBL:KRL53925.1}; OS Lactobacillus rossiae DSM 15814. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; OC Lactobacillus. OX NCBI_TaxID=1114972 {ECO:0000313|EMBL:KRL53925.1, ECO:0000313|Proteomes:UP000051999}; RN [1] {ECO:0000313|EMBL:KRL53925.1, ECO:0000313|Proteomes:UP000051999} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 15814 {ECO:0000313|EMBL:KRL53925.1, RC ECO:0000313|Proteomes:UP000051999}; RX PubMed=26415554; DOI=10.1038/ncomms9322; RA Sun Z., Harris H.M., McCann A., Guo C., Argimon S., Zhang W., Yang X., RA Jeffery I.B., Cooney J.C., Kagawa T.F., Liu W., Song Y., Salvetti E., RA Wrobel A., Rasinkangas P., Parkhill J., Rea M.C., O'Sullivan O., RA Ritari J., Douillard F.P., Paul Ross R., Yang R., Briner A.E., RA Felis G.E., de Vos W.M., Barrangou R., Klaenhammer T.R., RA Caufield P.W., Cui Y., Zhang H., O'Toole P.W.; RT "Expanding the biotechnology potential of lactobacilli through RT comparative genomics of 213 strains and associated genera."; RL Nat. Commun. 6:8322-8322(2015). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KRL53925.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AZFF01000013; KRL53925.1; -; Genomic_DNA. DR RefSeq; WP_017260950.1; NZ_AZFF01000013.1. DR EnsemblBacteria; KRL53925; KRL53925; FD35_GL000754. DR PATRIC; fig|1114972.6.peg.757; -. DR Proteomes; UP000051999; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000051999}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000051999}. FT DOMAIN 204 372 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 426 AA; 47326 MW; 55DCDD86C9409576 CRC64; MDETAIAPKE VIIAGLNTGA GNFEYSMEEL ANLVAANNMI VKEEVRQKLE RPHPGTYFGK GKITELAEIV ASENVDTIVT NDELTASQIR NIESATKASV LDRTALILDI FANRAQTREA KLQVQIAQLQ YQLPRLHTSV NQRLDQQTGA GGGGGFTNRG AGETQQEMDR RTINNQIKHL KGELTDITKA ADTQRTQREK NGLPTVALVG YTNAGKSTTM NGLVRKYGLN EDKQVFEKNM LFATLDTSVR QINLPDQKQF LLSDTVGFVS KLPHGLVEAF RSTLAEAANA DLLIQVVDYS DPNSEKMMKT TNEALKAIGV TDIPMIVAFN KADKTEAKYP SREGMQLVYS ARDDASLDEL ITMIREQVFK NYQTVTLLIP FDQGNILNFL NEKAHILETE YVAEGTKITV ELTDESAQRF EKYRVN // ID A0A0R1RZZ1_9LACO Unreviewed; 426 AA. AC A0A0R1RZZ1; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=FC69_GL001220 {ECO:0000313|EMBL:KRL62009.1}; OS Lactobacillus fuchuensis DSM 14340 = JCM 11249. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; OC Lactobacillus. OX NCBI_TaxID=1423747 {ECO:0000313|EMBL:KRL62009.1, ECO:0000313|Proteomes:UP000051264}; RN [1] {ECO:0000313|EMBL:KRL62009.1, ECO:0000313|Proteomes:UP000051264} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 14340 {ECO:0000313|EMBL:KRL62009.1, RC ECO:0000313|Proteomes:UP000051264}; RX PubMed=26415554; DOI=10.1038/ncomms9322; RA Sun Z., Harris H.M., McCann A., Guo C., Argimon S., Zhang W., Yang X., RA Jeffery I.B., Cooney J.C., Kagawa T.F., Liu W., Song Y., Salvetti E., RA Wrobel A., Rasinkangas P., Parkhill J., Rea M.C., O'Sullivan O., RA Ritari J., Douillard F.P., Paul Ross R., Yang R., Briner A.E., RA Felis G.E., de Vos W.M., Barrangou R., Klaenhammer T.R., RA Caufield P.W., Cui Y., Zhang H., O'Toole P.W.; RT "Expanding the biotechnology potential of lactobacilli through RT comparative genomics of 213 strains and associated genera."; RL Nat. Commun. 6:8322-8322(2015). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KRL62009.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AZEX01000002; KRL62009.1; -; Genomic_DNA. DR RefSeq; WP_025082739.1; NZ_BAMJ01000006.1. DR EnsemblBacteria; KRL62009; KRL62009; FC69_GL001220. DR PATRIC; fig|1423747.3.peg.1245; -. DR Proteomes; UP000051264; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000051264}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}. FT DOMAIN 200 370 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 426 AA; 47757 MW; 5FB7E2E61B4F358C CRC64; MKDTTPQPKR VLVTGVSKRQ DNFDYTMIEL GELAKANNLN VVGEVRQNVD QANHATYFGK GKVQEIKEQA IADDVDIILI NDELSPSQIR NLEKELGISI LDRTQLILEI FANRAQTKEA QLQVAIAEAK YQLPRLHPSD NKLDQQNGGG GGTNRGTGET QLELDRRLID KRITKLKGEL AKIDQQQATQ RQQRDKNPVP VVALVGYTNA GKSTTMNRIL QRLSPDTPEK QVFEKNMLFA TLDTSVREIT LPNQQKFLLS DTVGFVSKLP HHLVQAFKAT LAEAAGADLL IHVVDYSDPN YLNMMQTTQE TLESLGIKDI PMIEAYNKAD LKPDTRYPEI DGTQLVFSAR DEVSIDALID LIDKQLFGQY PIIDFLIPYT EGQAVTYLSD HVNILEQSYE EDGTHIKAQI NPDLLGPVQK YTMTTD // ID A0A0R1SAI5_9LACO Unreviewed; 427 AA. AC A0A0R1SAI5; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=FC85_GL000267 {ECO:0000313|EMBL:KRL65438.1}; OS Lactobacillus diolivorans DSM 14421. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; OC Lactobacillus. OX NCBI_TaxID=1423739 {ECO:0000313|EMBL:KRL65438.1, ECO:0000313|Proteomes:UP000052013}; RN [1] {ECO:0000313|EMBL:KRL65438.1, ECO:0000313|Proteomes:UP000052013} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 14421 {ECO:0000313|EMBL:KRL65438.1, RC ECO:0000313|Proteomes:UP000052013}; RX PubMed=26415554; DOI=10.1038/ncomms9322; RA Sun Z., Harris H.M., McCann A., Guo C., Argimon S., Zhang W., Yang X., RA Jeffery I.B., Cooney J.C., Kagawa T.F., Liu W., Song Y., Salvetti E., RA Wrobel A., Rasinkangas P., Parkhill J., Rea M.C., O'Sullivan O., RA Ritari J., Douillard F.P., Paul Ross R., Yang R., Briner A.E., RA Felis G.E., de Vos W.M., Barrangou R., Klaenhammer T.R., RA Caufield P.W., Cui Y., Zhang H., O'Toole P.W.; RT "Expanding the biotechnology potential of lactobacilli through RT comparative genomics of 213 strains and associated genera."; RL Nat. Commun. 6:8322-8322(2015). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KRL65438.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AZEY01000068; KRL65438.1; -; Genomic_DNA. DR RefSeq; WP_057864852.1; NZ_AZEY01000068.1. DR EnsemblBacteria; KRL65438; KRL65438; FC85_GL000267. DR PATRIC; fig|1423739.3.peg.280; -. DR Proteomes; UP000052013; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000052013}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000052013}. FT DOMAIN 203 371 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 427 AA; 47866 MW; 8DA74CB8561A897F CRC64; MDLTDNLTPV VTIGLNRNSN SFDYSMTELN NLVEANNMKV VESLVQKLDK PDPATYFGKG KIEELTQVVI DDGVNTIVAN DELSPSQIRN IEKNTKARII DRTGLILEIF ANRAQSREAK LQVELAKLKY QLPRLHTSAS QRLDQQTGTS SGGGFTNRGA GESQYELNRR TLEKRITHVN AELKESSKAD LTKRKQRDRS ETPTVALVGY TNAGKSTVMN GMINLYGENE DKQVMVKNML FATLDTSVRK LTLPDQKRFL LSDTVGFVSQ LPHQLVQAFK STLAEAASAD LLIQVVDYSD PHRELMMKTT EETLAEIGIT NVPMIVALNK ADKLEVQYPN REGDNLIMSA NDEDSLKELT TMIKEKIFKD YQTLSLLIPF DKGDVVSYLN DNTNILKTDY RDDGTVIKAE LKDVDAKRFA KYVLTTD // ID A0A0R1UBX3_9LACO Unreviewed; 421 AA. AC A0A0R1UBX3; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=FC46_GL001512 {ECO:0000313|EMBL:KRL90902.1}; OS Lactobacillus kalixensis DSM 16043. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; OC Lactobacillus. OX NCBI_TaxID=1423763 {ECO:0000313|EMBL:KRL90902.1, ECO:0000313|Proteomes:UP000051036}; RN [1] {ECO:0000313|EMBL:KRL90902.1, ECO:0000313|Proteomes:UP000051036} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 16043 {ECO:0000313|EMBL:KRL90902.1, RC ECO:0000313|Proteomes:UP000051036}; RX PubMed=26415554; DOI=10.1038/ncomms9322; RA Sun Z., Harris H.M., McCann A., Guo C., Argimon S., Zhang W., Yang X., RA Jeffery I.B., Cooney J.C., Kagawa T.F., Liu W., Song Y., Salvetti E., RA Wrobel A., Rasinkangas P., Parkhill J., Rea M.C., O'Sullivan O., RA Ritari J., Douillard F.P., Paul Ross R., Yang R., Briner A.E., RA Felis G.E., de Vos W.M., Barrangou R., Klaenhammer T.R., RA Caufield P.W., Cui Y., Zhang H., O'Toole P.W.; RT "Expanding the biotechnology potential of lactobacilli through RT comparative genomics of 213 strains and associated genera."; RL Nat. Commun. 6:8322-8322(2015). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KRL90902.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AZFM01000005; KRL90902.1; -; Genomic_DNA. DR RefSeq; WP_057797547.1; NZ_AZFM01000005.1. DR EnsemblBacteria; KRL90902; KRL90902; FC46_GL001512. DR PATRIC; fig|1423763.3.peg.1536; -. DR Proteomes; UP000051036; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000051036}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}. FT DOMAIN 199 368 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 421 AA; 47418 MW; 0EF0E863B3856068 CRC64; MIDNQSKKTK AFIAGVNLND PNFEYYMTEL ANLTEANNME VVGRAQQNAE KVVVGTYFGL GKINEIKAMA QGLKAKVLII NDELTPVQIR NLEKLTKLRV IDRTELILEI FSSRARTKQA KLQVQLARLQ YELPRLHPSE NNLDQQRGGG FNNRGAGESK LELNRRTIGK QISAIKKELK AVASQEELKS ARRNQNHIPK VALVGYTNAG KSTTMNGLLK TFTDEKPDKQ VFVKNMLFAT LDTSVRRIDM DNNFSFILSD TVGFISKLPH NLVESFKATL QEAKDADLLV NVVDSSDPNM IQMIRTTQEV LNEIGVKDIP MITAYNKADK TDRNYPQIEG NDILYSAIDE KSIKLLADLI TKRVFSDYES FNLKLPLAAG RDLAYLHEHA QVTKEDYEDD GIMITANISP SDQAKFKQYL V // ID A0A0R1UTP3_9LACO Unreviewed; 426 AA. AC A0A0R1UTP3; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=FC21_GL001065 {ECO:0000313|EMBL:KRL95018.1}; OS Lactobacillus equigenerosi DSM 18793 = JCM 14505. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; OC Lactobacillus. OX NCBI_TaxID=1423742 {ECO:0000313|EMBL:KRL95018.1, ECO:0000313|Proteomes:UP000051084}; RN [1] {ECO:0000313|EMBL:KRL95018.1, ECO:0000313|Proteomes:UP000051084} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 18793 {ECO:0000313|EMBL:KRL95018.1, RC ECO:0000313|Proteomes:UP000051084}; RX PubMed=26415554; DOI=10.1038/ncomms9322; RA Sun Z., Harris H.M., McCann A., Guo C., Argimon S., Zhang W., Yang X., RA Jeffery I.B., Cooney J.C., Kagawa T.F., Liu W., Song Y., Salvetti E., RA Wrobel A., Rasinkangas P., Parkhill J., Rea M.C., O'Sullivan O., RA Ritari J., Douillard F.P., Paul Ross R., Yang R., Briner A.E., RA Felis G.E., de Vos W.M., Barrangou R., Klaenhammer T.R., RA Caufield P.W., Cui Y., Zhang H., O'Toole P.W.; RT "Expanding the biotechnology potential of lactobacilli through RT comparative genomics of 213 strains and associated genera."; RL Nat. Commun. 6:8322-8322(2015). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KRL95018.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AZGC01000026; KRL95018.1; -; Genomic_DNA. DR RefSeq; WP_056995518.1; NZ_AZGC01000026.1. DR EnsemblBacteria; KRL95018; KRL95018; FC21_GL001065. DR PATRIC; fig|1423742.4.peg.1107; -. DR Proteomes; UP000051084; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000051084}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000051084}. FT DOMAIN 202 371 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 426 AA; 47945 MW; C09529FD0123636A CRC64; MENTAQPIDQ IIIIGLDKGS PDFSYSMDEL RELAAANHME VLDQLIQPLD RPNAATYFGK GKVEELANLA AALNATTIVA NDELSPSQIK NLTDATKVRV IDRTALILEI FAQRAKSKEA KIQVEIAQLQ YRLPRLRTAS NITLDQQSGG GAGMSNRGAG ETQMELDRRV IKRHISHLRN ELKEIQRSED TKRVQRDKSQ IPTAALVGYT NAGKSTIMNQ FVNRYGISAD KQVFEKDMLF ATLDTSVRQL TFNDQKRFLL SDTVGFVSKL PTTLVEAFKS TLAEAAHADL LIQVIDYSDP HYKEMMATTE KTLAQIGITD IPMIYVFNKA DRTEFEYPLM EGEDRVIISA RDDDSIDLLE QVIRRHLFKD YVTTTLLIPF TDGQVVSYLN EHCNILNTSY EADGTKLEVE IANADLPRFE QYMVVD // ID A0A0R1V054_9LACO Unreviewed; 417 AA. AC A0A0R1V054; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 07-JUN-2017, entry version 12. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=FD50_GL001966 {ECO:0000313|EMBL:KRL97018.1}; OS Lactobacillus satsumensis DSM 16230 = JCM 12392. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; OC Lactobacillus. OX NCBI_TaxID=1423801 {ECO:0000313|EMBL:KRL97018.1, ECO:0000313|Proteomes:UP000051166}; RN [1] {ECO:0000313|EMBL:KRL97018.1, ECO:0000313|Proteomes:UP000051166} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 16230 {ECO:0000313|EMBL:KRL97018.1, RC ECO:0000313|Proteomes:UP000051166}; RX PubMed=26415554; DOI=10.1038/ncomms9322; RA Sun Z., Harris H.M., McCann A., Guo C., Argimon S., Zhang W., Yang X., RA Jeffery I.B., Cooney J.C., Kagawa T.F., Liu W., Song Y., Salvetti E., RA Wrobel A., Rasinkangas P., Parkhill J., Rea M.C., O'Sullivan O., RA Ritari J., Douillard F.P., Paul Ross R., Yang R., Briner A.E., RA Felis G.E., de Vos W.M., Barrangou R., Klaenhammer T.R., RA Caufield P.W., Cui Y., Zhang H., O'Toole P.W.; RT "Expanding the biotechnology potential of lactobacilli through RT comparative genomics of 213 strains and associated genera."; RL Nat. Commun. 6:8322-8322(2015). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KRL97018.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AZFQ01000054; KRL97018.1; -; Genomic_DNA. DR RefSeq; WP_056961848.1; NZ_AZFQ01000054.1. DR EnsemblBacteria; KRL97018; KRL97018; FD50_GL001966. DR PATRIC; fig|1423801.4.peg.2010; -. DR Proteomes; UP000051166; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000051166}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}. FT DOMAIN 194 362 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 160 187 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 417 AA; 47006 MW; B433E98027AD7892 CRC64; MTRAFIAGIE NQQKNFPYLM KELAQLVAAN NLEVVADFSQ KLTKPVAATY LGKGKIQEIA EAVDHYQAEY LILNDELSPT QIRNLEKETS LKVLDRTELI LEIFSNRART KEAQLQVEIA RLKYQLPRLR GSITARLDQQ SASSTSANRG AGETKLELNR RTIQHRIDFL RRELKSIEKE YDIKSKSRRA SAIPRVALVG YTNAGKSTTM NGLISLLAGD KKQLVLEKDM LFATLDTSVR RLTYPDNKTF LLSDTVGFVS KLPHNLVEAF KSTLAEVREA DLLIQVIDVS DENSKEMVAT TEQTLEEIGA ADKPMIYAYN KADQAGITFP SVEGLQLTYS AREHSSIEQL AAMIKQFLFK DYRTFTYLIP YTQGSYLERL NVQANVLSTD YTEDGSKVTA EVSPRQADYY ARFLVKG // ID A0A0R1VRV8_9LACO Unreviewed; 415 AA. AC A0A0R1VRV8; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=FC89_GL001257 {ECO:0000313|EMBL:KRM05555.1}; OS Lactobacillus ghanensis DSM 18630. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; OC Lactobacillus. OX NCBI_TaxID=1423750 {ECO:0000313|EMBL:KRM05555.1, ECO:0000313|Proteomes:UP000051451}; RN [1] {ECO:0000313|EMBL:KRM05555.1, ECO:0000313|Proteomes:UP000051451} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 18630 {ECO:0000313|EMBL:KRM05555.1, RC ECO:0000313|Proteomes:UP000051451}; RX PubMed=26415554; DOI=10.1038/ncomms9322; RA Sun Z., Harris H.M., McCann A., Guo C., Argimon S., Zhang W., Yang X., RA Jeffery I.B., Cooney J.C., Kagawa T.F., Liu W., Song Y., Salvetti E., RA Wrobel A., Rasinkangas P., Parkhill J., Rea M.C., O'Sullivan O., RA Ritari J., Douillard F.P., Paul Ross R., Yang R., Briner A.E., RA Felis G.E., de Vos W.M., Barrangou R., Klaenhammer T.R., RA Caufield P.W., Cui Y., Zhang H., O'Toole P.W.; RT "Expanding the biotechnology potential of lactobacilli through RT comparative genomics of 213 strains and associated genera."; RL Nat. Commun. 6:8322-8322(2015). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KRM05555.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AZGB01000018; KRM05555.1; -; Genomic_DNA. DR RefSeq; WP_057872000.1; NZ_AZGB01000018.1. DR EnsemblBacteria; KRM05555; KRM05555; FC89_GL001257. DR PATRIC; fig|1423750.3.peg.1286; -. DR Proteomes; UP000051451; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000051451}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000051451}. FT DOMAIN 194 362 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 153 180 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 415 AA; 46568 MW; 760A1E34E314A443 CRC64; MTEIIIAGLN LHTADFDYSM AEFANLAQAA EMHVLAQLTQ AADHPISGTY FGRGKADEFA AAVAANQADA LLVNDQLSPT QLRNLEEIVK VPVIDRTELI LEIFSRRART KRAKLQVEIA RLKYQLPRLR ISGFNKLDQQ SSGSQSANRG AGETQHELTK RTLQQRINQL QHQLQEIAKE NLTQSRARQR SGLPLVAFVG YTNAGKSTTF NGLLNLFGEK TANRNLVKDQ LFATLDTSIR RLNFKDNKSF LISDTVGFIN DLPADLLEAF KTTLETVNEA DLLIQVIDIS QPEYKKMMAA TEKTLKQIGA GSIPMLYAYN KADKLHLTYP LSEGGQLTYS AVDQTSLIKL TALIKQQLFG NYQQFEYLIP FQASRFLEEF NQQANILETH YTAEGTLLKA EVSPQMAQKF TRFQQ // ID A0A0R1VUG5_9LACO Unreviewed; 431 AA. AC A0A0R1VUG5; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=FC15_GL001713 {ECO:0000313|EMBL:KRM09069.1}; OS Lactobacillus concavus DSM 17758. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; OC Lactobacillus. OX NCBI_TaxID=1423735 {ECO:0000313|EMBL:KRM09069.1, ECO:0000313|Proteomes:UP000051315}; RN [1] {ECO:0000313|EMBL:KRM09069.1, ECO:0000313|Proteomes:UP000051315} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 17758 {ECO:0000313|EMBL:KRM09069.1, RC ECO:0000313|Proteomes:UP000051315}; RX PubMed=26415554; DOI=10.1038/ncomms9322; RA Sun Z., Harris H.M., McCann A., Guo C., Argimon S., Zhang W., Yang X., RA Jeffery I.B., Cooney J.C., Kagawa T.F., Liu W., Song Y., Salvetti E., RA Wrobel A., Rasinkangas P., Parkhill J., Rea M.C., O'Sullivan O., RA Ritari J., Douillard F.P., Paul Ross R., Yang R., Briner A.E., RA Felis G.E., de Vos W.M., Barrangou R., Klaenhammer T.R., RA Caufield P.W., Cui Y., Zhang H., O'Toole P.W.; RT "Expanding the biotechnology potential of lactobacilli through RT comparative genomics of 213 strains and associated genera."; RL Nat. Commun. 6:8322-8322(2015). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KRM09069.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AZFX01000059; KRM09069.1; -; Genomic_DNA. DR RefSeq; WP_057824747.1; NZ_AZFX01000059.1. DR EnsemblBacteria; KRM09069; KRM09069; FC15_GL001713. DR PATRIC; fig|1423735.3.peg.1781; -. DR Proteomes; UP000051315; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000051315}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000051315}. FT DOMAIN 203 374 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 169 196 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 431 AA; 48479 MW; CA51D39046417DC5 CRC64; MTEIINLQPE KERVIIGGLS HKTANFDYTM NELKELARAD NMEVVDRVVQ NLDKMEAATY FGKGKVVEIA ELAAGLDVKV LVINDELSPS QIANLEKQTK MRIIDRTELI LEIFADRAKT REAKTQVEIA KLQYELPRVH PSANSLDQQH GGGGLANRGS GETQMELDKR VIRKRISELK QNLLTLEKSA ETQRERRQQS GLPKVALVGY TNAGKSTTMN QLLAAFDQLD ADKKQVFEKD MLFATLDTSV RTIQLPNKQK FLLSDTVGFV SHLPHNLVAS FKSTLAEAAD ADLLIHVVDY SDPHYREMME TTTQTLQEIG ITNLPTIIAF NKADLRADTN YPEVVGNDLI YSAKDPASIE KLAELIKKRI FADYQSVELL IPFADARVLA DLEAHTNVFE KDYTEAGTRV KVVLDPVRHN KYQKFVLKEK V // ID A0A0R1VVU8_9LACO Unreviewed; 428 AA. AC A0A0R1VVU8; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=FD16_GL001600 {ECO:0000313|EMBL:KRM09634.1}; OS Lactobacillus suebicus DSM 5007 = KCTC 3549. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; OC Lactobacillus. OX NCBI_TaxID=1423807 {ECO:0000313|EMBL:KRM09634.1, ECO:0000313|Proteomes:UP000051820}; RN [1] {ECO:0000313|EMBL:KRM09634.1, ECO:0000313|Proteomes:UP000051820} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 5007 {ECO:0000313|EMBL:KRM09634.1, RC ECO:0000313|Proteomes:UP000051820}; RX PubMed=26415554; DOI=10.1038/ncomms9322; RA Sun Z., Harris H.M., McCann A., Guo C., Argimon S., Zhang W., Yang X., RA Jeffery I.B., Cooney J.C., Kagawa T.F., Liu W., Song Y., Salvetti E., RA Wrobel A., Rasinkangas P., Parkhill J., Rea M.C., O'Sullivan O., RA Ritari J., Douillard F.P., Paul Ross R., Yang R., Briner A.E., RA Felis G.E., de Vos W.M., Barrangou R., Klaenhammer T.R., RA Caufield P.W., Cui Y., Zhang H., O'Toole P.W.; RT "Expanding the biotechnology potential of lactobacilli through RT comparative genomics of 213 strains and associated genera."; RL Nat. Commun. 6:8322-8322(2015). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KRM09634.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AZGF01000038; KRM09634.1; -; Genomic_DNA. DR RefSeq; WP_010621566.1; NZ_BACO01000021.1. DR EnsemblBacteria; KRM09634; KRM09634; FD16_GL001600. DR PATRIC; fig|1423807.3.peg.1640; -. DR Proteomes; UP000051820; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000051820}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}. FT DOMAIN 204 373 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 428 AA; 47718 MW; D249A22789E4E629 CRC64; MDTQPITEPV IIAGLNLSNQ ENDFDYSMEE LANLVEANEM KVSDKMVQSL DRPNAATYFG KGKVEELAEL VAATNVATIV TNDELSPSQI RNLEEATKAR VMDRTALILE IFAKRAQSKE AKLQVEIAQL QYRLPRLKTS ANQRLDQQTG AGGGSFTNRG SGETKLEMNR RTIQNAITHL RGELAELNKS SETQRQQRDK RGIPTAALVG YTNAGKSTIM NGLVREFGID DEKQVFEKNM LFATLDTSVR QLTLPDQKQF LLSDTVGFVS KLPTHLVEAF KSTLAEAANA DLLIQVIDYS DPHYQEMMQT TENTLKEIGI KDIPMILVFN KADKMEVQFP TMDGDDQIIM SARDETSLSM LAGVVKTHLF TDYVTTTLLV PFANGDVVSY LNEHADIKET DYLADGTKLV VELSSSDLQR FEKFVVEE // ID A0A0R1WXH0_9LACO Unreviewed; 420 AA. AC A0A0R1WXH0; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=FC40_GL001505 {ECO:0000313|EMBL:KRM19654.1}; OS Lactobacillus hayakitensis DSM 18933 = JCM 14209. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; OC Lactobacillus. OX NCBI_TaxID=1423755 {ECO:0000313|EMBL:KRM19654.1, ECO:0000313|Proteomes:UP000051054}; RN [1] {ECO:0000313|EMBL:KRM19654.1, ECO:0000313|Proteomes:UP000051054} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 18933 {ECO:0000313|EMBL:KRM19654.1, RC ECO:0000313|Proteomes:UP000051054}; RX PubMed=26415554; DOI=10.1038/ncomms9322; RA Sun Z., Harris H.M., McCann A., Guo C., Argimon S., Zhang W., Yang X., RA Jeffery I.B., Cooney J.C., Kagawa T.F., Liu W., Song Y., Salvetti E., RA Wrobel A., Rasinkangas P., Parkhill J., Rea M.C., O'Sullivan O., RA Ritari J., Douillard F.P., Paul Ross R., Yang R., Briner A.E., RA Felis G.E., de Vos W.M., Barrangou R., Klaenhammer T.R., RA Caufield P.W., Cui Y., Zhang H., O'Toole P.W.; RT "Expanding the biotechnology potential of lactobacilli through RT comparative genomics of 213 strains and associated genera."; RL Nat. Commun. 6:8322-8322(2015). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KRM19654.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AZGD01000037; KRM19654.1; -; Genomic_DNA. DR RefSeq; WP_025021792.1; NZ_BAML01000002.1. DR EnsemblBacteria; KRM19654; KRM19654; FC40_GL001505. DR PATRIC; fig|1423755.3.peg.1595; -. DR Proteomes; UP000051054; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000051054}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000051054}. FT DOMAIN 198 366 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 164 191 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 420 AA; 47476 MW; B25B48D8F92A3967 CRC64; MTVPVIISGL ETENENFEYT MSELSALCEA NDMEVVQQIS QKLEHPVAAT YFGKGKAEEI FHEGELHEVE TLIVNDELTP TQLRNLEDIT EMRVVDRTAL ILEIFASRAH TKEAKLQVQI AKLQYQLPRL RTSSINKMDQ QTAGNAGGGY TNRGSGETKM ELNRRVIEKR INNLSKELKE IEANQETQSK LRDKSGIKTV ALVGYTNAGK STTMNGLLKM LGQDPEKEVF EKDMLFATLD TSVRKLKFND NKEILLSDTV GFVSKLPHQL VKAFRTTLYE ASKADLLIQV IDGADEHAKE MIETTTSTLK EIGVTDIPMI YAYNKADLAQ IPYPIMEGDQ LTYSARDQKS LELLINVIKE KLFDDYQTHT YLLPFSEGRY LEVLNQEANI LRTEYLAEGT KLEVEVNPIL AAKLKQFQID // ID A0A0R1XEX6_9LACO Unreviewed; 424 AA. AC A0A0R1XEX6; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 07-JUN-2017, entry version 10. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=FD32_GL001683 {ECO:0000313|EMBL:KRM28679.1}; OS Lactobacillus panis DSM 6035. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; OC Lactobacillus. OX NCBI_TaxID=1423782 {ECO:0000313|EMBL:KRM28679.1, ECO:0000313|Proteomes:UP000051412}; RN [1] {ECO:0000313|EMBL:KRM28679.1, ECO:0000313|Proteomes:UP000051412} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 6035 {ECO:0000313|EMBL:KRM28679.1, RC ECO:0000313|Proteomes:UP000051412}; RX PubMed=26415554; DOI=10.1038/ncomms9322; RA Sun Z., Harris H.M., McCann A., Guo C., Argimon S., Zhang W., Yang X., RA Jeffery I.B., Cooney J.C., Kagawa T.F., Liu W., Song Y., Salvetti E., RA Wrobel A., Rasinkangas P., Parkhill J., Rea M.C., O'Sullivan O., RA Ritari J., Douillard F.P., Paul Ross R., Yang R., Briner A.E., RA Felis G.E., de Vos W.M., Barrangou R., Klaenhammer T.R., RA Caufield P.W., Cui Y., Zhang H., O'Toole P.W.; RT "Expanding the biotechnology potential of lactobacilli through RT comparative genomics of 213 strains and associated genera."; RL Nat. Commun. 6:8322-8322(2015). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KRM28679.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AZGM01000039; KRM28679.1; -; Genomic_DNA. DR RefSeq; WP_047769031.1; NZ_LDPB01000092.1. DR EnsemblBacteria; KRM28679; KRM28679; FD32_GL001683. DR PATRIC; fig|1423782.4.peg.1750; -. DR Proteomes; UP000051412; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000051412}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}. FT DOMAIN 202 371 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 424 AA; 47666 MW; 911D2701BC3893C5 CRC64; MDNNIQKDEQ VIIAGLDTGQ EDYDYSMTEL AELAQANHMD VVQRVDQVID RPNPATYFGT GKVAEIAEVA ATNDATTIIT NDELSPSQLR NLEEEVGCRI LDRTALILEI FANRAQTKEA KLQVQIAELQ YRLPRLQTSA SQRLDQQTGG GSGFTNRGAG ETKLEMDRRT IQHQISHLRH ELADIDKSEA TKRKQRAKSN IPTAALVGYT NAGKSTIMNG LVRRYGAVED KTVFEKNMLF ATLDTSVRRL TLPSKKDFLL SDTVGFVSKL PTNLVKSFRS TLAEAANADL LIQVIDYSDP HYEEMMHTTE QTLKQIGIEN IPMINVFNKA DKTEIEFPVL EGDDQVVISA KQPESLDLLV NVIRKHLFKD YVQVKLLLPF AEGQLVSYLN EHTNILNTEY RTDGTLLTVE MSPQEAQRFT KYEV // ID A0A0R1XGD1_9LACO Unreviewed; 433 AA. AC A0A0R1XGD1; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=FC91_GL001174 {ECO:0000313|EMBL:KRM29010.1}; OS Lactobacillus harbinensis DSM 16991. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; OC Lactobacillus. OX NCBI_TaxID=1122147 {ECO:0000313|EMBL:KRM29010.1, ECO:0000313|Proteomes:UP000050949}; RN [1] {ECO:0000313|EMBL:KRM29010.1, ECO:0000313|Proteomes:UP000050949} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 16991 {ECO:0000313|EMBL:KRM29010.1, RC ECO:0000313|Proteomes:UP000050949}; RX PubMed=26415554; DOI=10.1038/ncomms9322; RA Sun Z., Harris H.M., McCann A., Guo C., Argimon S., Zhang W., Yang X., RA Jeffery I.B., Cooney J.C., Kagawa T.F., Liu W., Song Y., Salvetti E., RA Wrobel A., Rasinkangas P., Parkhill J., Rea M.C., O'Sullivan O., RA Ritari J., Douillard F.P., Paul Ross R., Yang R., Briner A.E., RA Felis G.E., de Vos W.M., Barrangou R., Klaenhammer T.R., RA Caufield P.W., Cui Y., Zhang H., O'Toole P.W.; RT "Expanding the biotechnology potential of lactobacilli through RT comparative genomics of 213 strains and associated genera."; RL Nat. Commun. 6:8322-8322(2015). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KRM29010.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AZFW01000020; KRM29010.1; -; Genomic_DNA. DR RefSeq; WP_027827798.1; NZ_AZFW01000020.1. DR EnsemblBacteria; KRM29010; KRM29010; FC91_GL001174. DR PATRIC; fig|1122147.4.peg.1214; -. DR Proteomes; UP000050949; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000050949}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000050949}. FT DOMAIN 205 373 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 433 AA; 48096 MW; 833602C100871041 CRC64; MQDTTIQTIP TIIAGLDRQQ ADFDYTMTEL GELVTAAGMT VSSKVTQRAD HIDAATYFGK GKVEEMAAQA RGEDVPIIVV NDDLTPSQTR NLEKITKLSV MDRTELILRI FSSRARTREA KLQVAIAREE YALPRVHPSA NPLDQQGGGR GASGGATANR GAGETQLELD KRVIRKRITH MRNELKEIMR AQDTRRDRRI HQALPSVALV GYTNAGKSTT MNGMLQQYGL TDKQVMVKNQ LFATLDTSVR KLQLPNHRHF LLSDTVGFVS HLPHHLVESF KATLAEARDA DLLIQVVDFA DPHYREMMAT TEETLNAIGV KDIPMLTVYN KADLRSDTHY PDREGMTLTL SATDPNSIRL LGQTLNELLY KDYVTTDLLV PFTKGDVVNY LRDNTEVKSE HYTDDGTAVT AVLGPIDRGR FAEYVQAAVA AAK // ID A0A0R1Y7G9_9LACO Unreviewed; 426 AA. AC A0A0R1Y7G9; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=FD34_GL001026 {ECO:0000313|EMBL:KRM37749.1}; OS Lactobacillus pontis DSM 8475. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; OC Lactobacillus. OX NCBI_TaxID=1423794 {ECO:0000313|EMBL:KRM37749.1, ECO:0000313|Proteomes:UP000051085}; RN [1] {ECO:0000313|EMBL:KRM37749.1, ECO:0000313|Proteomes:UP000051085} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 8475 {ECO:0000313|EMBL:KRM37749.1, RC ECO:0000313|Proteomes:UP000051085}; RX PubMed=26415554; DOI=10.1038/ncomms9322; RA Sun Z., Harris H.M., McCann A., Guo C., Argimon S., Zhang W., Yang X., RA Jeffery I.B., Cooney J.C., Kagawa T.F., Liu W., Song Y., Salvetti E., RA Wrobel A., Rasinkangas P., Parkhill J., Rea M.C., O'Sullivan O., RA Ritari J., Douillard F.P., Paul Ross R., Yang R., Briner A.E., RA Felis G.E., de Vos W.M., Barrangou R., Klaenhammer T.R., RA Caufield P.W., Cui Y., Zhang H., O'Toole P.W.; RT "Expanding the biotechnology potential of lactobacilli through RT comparative genomics of 213 strains and associated genera."; RL Nat. Commun. 6:8322-8322(2015). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KRM37749.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AZGO01000012; KRM37749.1; -; Genomic_DNA. DR RefSeq; WP_057805974.1; NZ_AZGO01000012.1. DR EnsemblBacteria; KRM37749; KRM37749; FD34_GL001026. DR PATRIC; fig|1423794.3.peg.1050; -. DR Proteomes; UP000051085; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000051085}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000051085}. FT DOMAIN 202 371 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 426 AA; 47739 MW; 94FD972EE9C4E65D CRC64; MDTNIQSDEL VIITGLDTGQ EDYDYSMVEL AELAQANHMD VVQRVDQVID RPNPATYFGK GKVQEIGDVA AANHATTIIT NDELTPSQLR NLEEETSCRI LDRTALILEI FATRAQTKEA KLQVQIAELQ YRLPRLQTSA SQRLDQQTGG GSGFTNRGAG ETKLEMDRRT IQYQITHLRH ELAAIAKSEK TKRKQRAKSE IPTAALVGYT NSGKSTIMNG LVKRYGRVED KTVFEKDMLF ATLDTSVRRM ALPGQKEFLL SDTVGFVSKL PTQLVESFKS TLAEAANADL LIQVIDYSDP HYEEMMATTR KTLKQIGIHD IPMVNVFNKA DKTEIEFPVL EGDDQIVISA KQGASLELLV DVIRKHLFKD YVQAKLLVPF ADGQVVSYLN EHSNILDTEY QNDGTLLTVE AAPQDYQRFA KYEVKS // ID A0A0R1YBL2_9LACO Unreviewed; 427 AA. AC A0A0R1YBL2; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 07-JUN-2017, entry version 10. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=FC39_GL000912 {ECO:0000313|EMBL:KRM39911.1}; OS Lactobacillus hamsteri DSM 5661 = JCM 6256. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; OC Lactobacillus. OX NCBI_TaxID=1423754 {ECO:0000313|EMBL:KRM39911.1, ECO:0000313|Proteomes:UP000051223}; RN [1] {ECO:0000313|EMBL:KRM39911.1, ECO:0000313|Proteomes:UP000051223} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 5661 {ECO:0000313|EMBL:KRM39911.1, RC ECO:0000313|Proteomes:UP000051223}; RX PubMed=26415554; DOI=10.1038/ncomms9322; RA Sun Z., Harris H.M., McCann A., Guo C., Argimon S., Zhang W., Yang X., RA Jeffery I.B., Cooney J.C., Kagawa T.F., Liu W., Song Y., Salvetti E., RA Wrobel A., Rasinkangas P., Parkhill J., Rea M.C., O'Sullivan O., RA Ritari J., Douillard F.P., Paul Ross R., Yang R., Briner A.E., RA Felis G.E., de Vos W.M., Barrangou R., Klaenhammer T.R., RA Caufield P.W., Cui Y., Zhang H., O'Toole P.W.; RT "Expanding the biotechnology potential of lactobacilli through RT comparative genomics of 213 strains and associated genera."; RL Nat. Commun. 6:8322-8322(2015). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KRM39911.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AZGI01000030; KRM39911.1; -; Genomic_DNA. DR EnsemblBacteria; KRM39911; KRM39911; FC39_GL000912. DR PATRIC; fig|1423754.3.peg.939; -. DR Proteomes; UP000051223; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000051223}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}. FT DOMAIN 205 374 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 427 AA; 47909 MW; 777CA3D47E11C4E8 CRC64; MKVGGFMIDN QPKKTKAFIA GVNLKDPNFD YYMTELANLT EANNMEVVGQ AYQNLENIVA GTYFGVGKIN EIKAMAHGLK AKVLILNDEL SPVQIRNLEK LTKLRVIDRT ELILEIFASR AQTKQAKLQV QLARLQYELP RLHPSENNLD QQRGGGFANR GAGESKLEMN RRTIGKQISA IKKELKAVES QEEIKATRRN QSRIPKVALV GYTNAGKSTT MNGLLKVFAG ENADKQVFVK NMLFATLDTS VRRIDMKDNF SFILSDTVGF ISKLPHNLVE SFKATLQEAK DADLLINVVD ASDPNMIQMI RTTQQVLNEI GVKGIPMITA YNKADKTERN FPQIEGDDIL YSAIDDKSIK MLADLIVKRV FANYNKVNLK LPLTDGKLIA YLHDRANVLT EDYKDDGVYV TANVAPDDQA RFKKYEI // ID A0A0R1YGW2_9LACO Unreviewed; 429 AA. AC A0A0R1YGW2; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 07-JUN-2017, entry version 10. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=FD40_GL001311 {ECO:0000313|EMBL:KRM41473.1}; OS Lactobacillus amylophilus DSM 20533 = JCM 1125. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; OC Lactobacillus. OX NCBI_TaxID=1423721 {ECO:0000313|EMBL:KRM41473.1, ECO:0000313|Proteomes:UP000051230}; RN [1] {ECO:0000313|EMBL:KRM41473.1, ECO:0000313|Proteomes:UP000051230} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 20533 {ECO:0000313|EMBL:KRM41473.1, RC ECO:0000313|Proteomes:UP000051230}; RX PubMed=26415554; DOI=10.1038/ncomms9322; RA Sun Z., Harris H.M., McCann A., Guo C., Argimon S., Zhang W., Yang X., RA Jeffery I.B., Cooney J.C., Kagawa T.F., Liu W., Song Y., Salvetti E., RA Wrobel A., Rasinkangas P., Parkhill J., Rea M.C., O'Sullivan O., RA Ritari J., Douillard F.P., Paul Ross R., Yang R., Briner A.E., RA Felis G.E., de Vos W.M., Barrangou R., Klaenhammer T.R., RA Caufield P.W., Cui Y., Zhang H., O'Toole P.W.; RT "Expanding the biotechnology potential of lactobacilli through RT comparative genomics of 213 strains and associated genera."; RL Nat. Commun. 6:8322-8322(2015). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KRM41473.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AYYS01000029; KRM41473.1; -; Genomic_DNA. DR EnsemblBacteria; KRM41473; KRM41473; FD40_GL001311. DR PATRIC; fig|1423721.4.peg.1344; -. DR Proteomes; UP000051230; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000051230}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000051230}. FT DOMAIN 198 372 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 429 AA; 47697 MW; 44002DB0277A941F CRC64; MIIGGVNKGE PNFDYYMREL AQLSAANNME VVGRVDQNLE RLVAATYFGS GKVAEIGTLA QESGATHLVL NDELSPTQIR NLERETKLHV VDRTELILEI FSNRAKTKQA KLQVALARLQ YELPRLHTAE NSGLDQQRGS GTGGSGGGGL ANRGSGETKL ELNRRTLGKQ IAMIKEELQE ISRSEATRRK ERNESALPQV ALVGYTNAGK STTMNSLLQL FGQGEDHEKK AKKQVFEKDM LFATLDTSVR RIDLASNFSF LLSDTVGFIS KLPHKLVESF KATLQEVRDA DLLIHVVDVS DENHKEMVET TNAVLKELGV LETPTIIAYN KADETVREYP SMDGDDLFYS AKDEQSMQLL SQLITKKLFA DYQVRTLRLP LTAGKDLAYL HAKAEILTED YTSDGVTVEA RLSPTDQKRL ESFTVNVQE // ID A0A0R1ZE89_9LACO Unreviewed; 422 AA. AC A0A0R1ZE89; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 07-JUN-2017, entry version 10. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=FC64_GL000344 {ECO:0000313|EMBL:KRM52594.1}; OS Lactobacillus aviarius subsp. araffinosus DSM 20653. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; OC Lactobacillus. OX NCBI_TaxID=1423820 {ECO:0000313|EMBL:KRM52594.1, ECO:0000313|Proteomes:UP000051291}; RN [1] {ECO:0000313|EMBL:KRM52594.1, ECO:0000313|Proteomes:UP000051291} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 20653 {ECO:0000313|EMBL:KRM52594.1, RC ECO:0000313|Proteomes:UP000051291}; RX PubMed=26415554; DOI=10.1038/ncomms9322; RA Sun Z., Harris H.M., McCann A., Guo C., Argimon S., Zhang W., Yang X., RA Jeffery I.B., Cooney J.C., Kagawa T.F., Liu W., Song Y., Salvetti E., RA Wrobel A., Rasinkangas P., Parkhill J., Rea M.C., O'Sullivan O., RA Ritari J., Douillard F.P., Paul Ross R., Yang R., Briner A.E., RA Felis G.E., de Vos W.M., Barrangou R., Klaenhammer T.R., RA Caufield P.W., Cui Y., Zhang H., O'Toole P.W.; RT "Expanding the biotechnology potential of lactobacilli through RT comparative genomics of 213 strains and associated genera."; RL Nat. Commun. 6:8322-8322(2015). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KRM52594.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AYYZ01000017; KRM52594.1; -; Genomic_DNA. DR RefSeq; WP_057906488.1; NZ_AYYZ01000017.1. DR EnsemblBacteria; KRM52594; KRM52594; FC64_GL000344. DR PATRIC; fig|1423820.4.peg.344; -. DR Proteomes; UP000051291; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000051291}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000051291}. FT DOMAIN 198 328 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 164 191 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 422 AA; 47617 MW; 607A5CCA55AF1B39 CRC64; MKSVIIGGIE NEQINFDYTM TELANLAAAD NMEVVGEVRQ NIEKPVSATY FGKGKVDEIT RQAEMLDAEA LIVNDELLPT QIRNLEKETG LDIIDRTALI LDIFASRAHT RVAKLQVKIA QLQYQLPRIR TASINKMDQQ TAGGNTGGGF TNRGTGETQI ELNRRVIQKQ ISSLRKELKE VQRDNETQRK KRKKSDIKSV ALVGYTNAGK STTMNNVLDL LEINDSKRVF EKDMLFATLD TYVRKIVLPD KKSFILSDTV GFVSKLPHQL VEAFKSTLQE ATEADLLIQV IDISDPNYRQ MIKTTEKTLT EIGVDGIPMI YAFNKADKAG IPYPSVEGNQ FTYCARDQKS IEMLLGILKK ELFKDYETET FLIPFQDGRY LDLLNKEANI KKTDYQADGT LITAEVAPKL KQQLARYIVD ED // ID A0A0R1ZVX0_9LACO Unreviewed; 423 AA. AC A0A0R1ZVX0; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=FD44_GL000184 {ECO:0000313|EMBL:KRM59025.1}; OS Lactobacillus malefermentans DSM 5705 = KCTC 3548. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; OC Lactobacillus. OX NCBI_TaxID=1122149 {ECO:0000313|EMBL:KRM59025.1, ECO:0000313|Proteomes:UP000051712}; RN [1] {ECO:0000313|EMBL:KRM59025.1, ECO:0000313|Proteomes:UP000051712} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 5705 {ECO:0000313|EMBL:KRM59025.1, RC ECO:0000313|Proteomes:UP000051712}; RX PubMed=26415554; DOI=10.1038/ncomms9322; RA Sun Z., Harris H.M., McCann A., Guo C., Argimon S., Zhang W., Yang X., RA Jeffery I.B., Cooney J.C., Kagawa T.F., Liu W., Song Y., Salvetti E., RA Wrobel A., Rasinkangas P., Parkhill J., Rea M.C., O'Sullivan O., RA Ritari J., Douillard F.P., Paul Ross R., Yang R., Briner A.E., RA Felis G.E., de Vos W.M., Barrangou R., Klaenhammer T.R., RA Caufield P.W., Cui Y., Zhang H., O'Toole P.W.; RT "Expanding the biotechnology potential of lactobacilli through RT comparative genomics of 213 strains and associated genera."; RL Nat. Commun. 6:8322-8322(2015). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KRM59025.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AZGJ01000011; KRM59025.1; -; Genomic_DNA. DR RefSeq; WP_010619484.1; NZ_BACN01000027.1. DR EnsemblBacteria; KRM59025; KRM59025; FD44_GL000184. DR PATRIC; fig|1122149.3.peg.186; -. DR Proteomes; UP000051712; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000051712}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}. FT DOMAIN 202 370 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 168 198 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 423 AA; 46981 MW; EB5E6FBFFDA1AE36 CRC64; MSESSSPKAI AIGLNTGQQD FDYSMEELSA LAAANNVDIV ETVTQNLDRP VAGTYFGTGK VEELKDIVID DEVEMVIAND ELSPSQIRNL EGVINVAVID RTGLILQIFA DRAQSREAKL QVQLAKLQYQ LPRLHTSASQ RLDQQTGTSS GGGFTNRGAG ESQIELNRRV IERQINHVRQ ELKEISKSEE TKRQQRERQG LPMIALVGYT NAGKSTIMNA LVRQFGTSEE KQVFEKNMLF ATLDTSVRQL TFGDQKKLLL SDTVGFVAHL PTHLIEAFKS TLYEAANADL LIQVVDAADP NRDSMMATTM KTLEDIGVPN LPMIVAYNKA DLTDVSFPSR EGENLTMSAR DDASIALLID MIREKVFKNY VTADFLIPFA NGDVVSYFNE NANVLSTEYV ADGSKMKVEL TRTDYDRFEK FVV // ID A0A0R1ZWG4_9LACO Unreviewed; 442 AA. AC A0A0R1ZWG4; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=FC18_GL000701 {ECO:0000313|EMBL:KRM56169.1}; OS Lactobacillus sharpeae JCM 1186 = DSM 20505. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; OC Lactobacillus. OX NCBI_TaxID=1291052 {ECO:0000313|EMBL:KRM56169.1, ECO:0000313|Proteomes:UP000051679}; RN [1] {ECO:0000313|EMBL:KRM56169.1, ECO:0000313|Proteomes:UP000051679} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 20505 {ECO:0000313|EMBL:KRM56169.1, RC ECO:0000313|Proteomes:UP000051679}; RX PubMed=26415554; DOI=10.1038/ncomms9322; RA Sun Z., Harris H.M., McCann A., Guo C., Argimon S., Zhang W., Yang X., RA Jeffery I.B., Cooney J.C., Kagawa T.F., Liu W., Song Y., Salvetti E., RA Wrobel A., Rasinkangas P., Parkhill J., Rea M.C., O'Sullivan O., RA Ritari J., Douillard F.P., Paul Ross R., Yang R., Briner A.E., RA Felis G.E., de Vos W.M., Barrangou R., Klaenhammer T.R., RA Caufield P.W., Cui Y., Zhang H., O'Toole P.W.; RT "Expanding the biotechnology potential of lactobacilli through RT comparative genomics of 213 strains and associated genera."; RL Nat. Commun. 6:8322-8322(2015). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KRM56169.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AYYO01000009; KRM56169.1; -; Genomic_DNA. DR EnsemblBacteria; KRM56169; KRM56169; FC18_GL000701. DR PATRIC; fig|1291052.5.peg.716; -. DR Proteomes; UP000051679; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000051679}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Hydrolase {ECO:0000313|EMBL:KRM56169.1}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Protease {ECO:0000313|EMBL:KRM56169.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000051679}. FT DOMAIN 215 387 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 442 AA; 48830 MW; BFBBADAC5B4BBDFD CRC64; MEHIMTENKP LTATTQTRNA LISGITKRQD NFDYTMTELG ELAKAAGYAV VADVRQKADF PTGATYFGKG KVEEIREAAV LHEADVIIVN DELSPSQLRN LEKQIKRRVV DRTQLILDIF GTRARSKQAK MQVEIAQLRY ALPRLRNQSA GFDQQGGGST GGGGAALANR GSGETQLEMD KRILTKRISH IKHELIEEEQ SEQTRSSQRT ASDIPTVALV GYTNAGKSTT MNGLLSLYAD RPEDKQVFEK NMLFATLDTS VRRIELPGNR QFLLSDTVGF VGKLPTKLVD SFKATLAEAK NADLLIHVVD FADQHYPEMM QVTEKTLRDI GIAEDVPVIE AYNKADLRGD ATAFPEVNGN QLVYSARDDA SLQQLAAMIE ERIFADQVTA TYLIPFTDGA AVNYINSVAK VDQTDYNETG TLITATMSKA QAVKVQQYIV EE // ID A0A0R2A301_9LACO Unreviewed; 427 AA. AC A0A0R2A301; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=FC26_GL001619 {ECO:0000313|EMBL:KRM61544.1}; OS Lactobacillus vaccinostercus DSM 20634. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; OC Lactobacillus. OX NCBI_TaxID=1423813 {ECO:0000313|EMBL:KRM61544.1, ECO:0000313|Proteomes:UP000051733}; RN [1] {ECO:0000313|EMBL:KRM61544.1, ECO:0000313|Proteomes:UP000051733} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 20634 {ECO:0000313|EMBL:KRM61544.1, RC ECO:0000313|Proteomes:UP000051733}; RX PubMed=26415554; DOI=10.1038/ncomms9322; RA Sun Z., Harris H.M., McCann A., Guo C., Argimon S., Zhang W., Yang X., RA Jeffery I.B., Cooney J.C., Kagawa T.F., Liu W., Song Y., Salvetti E., RA Wrobel A., Rasinkangas P., Parkhill J., Rea M.C., O'Sullivan O., RA Ritari J., Douillard F.P., Paul Ross R., Yang R., Briner A.E., RA Felis G.E., de Vos W.M., Barrangou R., Klaenhammer T.R., RA Caufield P.W., Cui Y., Zhang H., O'Toole P.W.; RT "Expanding the biotechnology potential of lactobacilli through RT comparative genomics of 213 strains and associated genera."; RL Nat. Commun. 6:8322-8322(2015). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KRM61544.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AYYY01000025; KRM61544.1; -; Genomic_DNA. DR RefSeq; WP_057778790.1; NZ_AYYY01000025.1. DR EnsemblBacteria; KRM61544; KRM61544; FC26_GL001619. DR PATRIC; fig|1423813.3.peg.1646; -. DR Proteomes; UP000051733; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000051733}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000051733}. FT DOMAIN 204 334 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 427 AA; 47278 MW; 1413DD10259CD8BF CRC64; MDTQPTTEPV IIAGLNLANQ QVDFDYSMEE LANLIEANEM TVADRLVQSL DRPNAATYFG KGKVEELAEL ITATGVQTVV TNDELSPSQI RNLEENTTAR ILDRTALILE IFAKRAKSRE AKLQVEIAQL QYRLPRLKTS ANQRLDQQTG AGGGSFTNRG AGETKLEMNR RTIQNAITHL RGELAELNKS ATTQRQQRAK SGIPTAALVG YTNAGKSTIM NGLVRMFGID DDKQVFEKNM LFATLDTSVR QLTLPDQKQF LLSDTVGFVS KLPTHLVQAF KSTLAEAANA DLLIQVIDYS DPHYQEMMAT TAATLKEIGI EDIPMILVFN KADKMEVQFP VMDGDDQVVL SARDEQSLGM LVGVIKSHLF TNYVTVELLI PFADGEVVSY LNDHAHILST DYLATGTQLK VELSATDQQR FAKYQQQ // ID A0A0R2ABK6_9LACO Unreviewed; 418 AA. AC A0A0R2ABK6; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=FC14_GL001817 {ECO:0000313|EMBL:KRM64541.1}; OS Lactobacillus agilis DSM 20509. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; OC Lactobacillus. OX NCBI_TaxID=1423718 {ECO:0000313|EMBL:KRM64541.1, ECO:0000313|Proteomes:UP000051008}; RN [1] {ECO:0000313|EMBL:KRM64541.1, ECO:0000313|Proteomes:UP000051008} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 20509 {ECO:0000313|EMBL:KRM64541.1, RC ECO:0000313|Proteomes:UP000051008}; RX PubMed=26415554; DOI=10.1038/ncomms9322; RA Sun Z., Harris H.M., McCann A., Guo C., Argimon S., Zhang W., Yang X., RA Jeffery I.B., Cooney J.C., Kagawa T.F., Liu W., Song Y., Salvetti E., RA Wrobel A., Rasinkangas P., Parkhill J., Rea M.C., O'Sullivan O., RA Ritari J., Douillard F.P., Paul Ross R., Yang R., Briner A.E., RA Felis G.E., de Vos W.M., Barrangou R., Klaenhammer T.R., RA Caufield P.W., Cui Y., Zhang H., O'Toole P.W.; RT "Expanding the biotechnology potential of lactobacilli through RT comparative genomics of 213 strains and associated genera."; RL Nat. Commun. 6:8322-8322(2015). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KRM64541.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AYYP01000030; KRM64541.1; -; Genomic_DNA. DR RefSeq; WP_056976656.1; NZ_AYYP01000030.1. DR EnsemblBacteria; KRM64541; KRM64541; FC14_GL001817. DR PATRIC; fig|1423718.3.peg.1889; -. DR Proteomes; UP000051008; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000051008}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000051008}. FT DOMAIN 196 364 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 155 189 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 418 AA; 46864 MW; CEED19F87688267E CRC64; MNTIIAGIEN NQANFDYTME ELAALASADN LTVVKEIRQK LEQPVAATYF GKGKAEEIKT ASEIYDAQLL VVNDELTPTQ IRNLETITNL TILDRTALIL EIFASRARTK EAKLQVQIAK LQYQLPRLQT GKKDQLDQQT AGNAGGGYTN RGAGETKLEL NRRVIQKRIS NLRKELKELT KNHAVQRQQR QKNQLKTVAL VGYTNAGKST TMNQILALTG AKQSKQVFEK DMLFATLDTA VRKISLDDKK EFLLSDTVGF VSKLPHQLVK SFRATLEEAA QADLLIQVID GADEHAKEMI ATTEATLKEI GVTDIPMIYA YNKADKSQLT YPVAEGNQIT YSARQVESIE LLLELIKKEL FKDYEEHTYL IPYDQGRYLD LLNQQASISK QDYLETGYLV KAEVAPKLAG QLAQFLSE // ID A0A0R2AXY4_9LACO Unreviewed; 423 AA. AC A0A0R2AXY4; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=FC34_GL001190 {ECO:0000313|EMBL:KRM72205.1}; OS Lactobacillus brantae DSM 23927. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; OC Lactobacillus. OX NCBI_TaxID=1423727 {ECO:0000313|EMBL:KRM72205.1, ECO:0000313|Proteomes:UP000051672}; RN [1] {ECO:0000313|EMBL:KRM72205.1, ECO:0000313|Proteomes:UP000051672} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 23927 {ECO:0000313|EMBL:KRM72205.1, RC ECO:0000313|Proteomes:UP000051672}; RX PubMed=26415554; DOI=10.1038/ncomms9322; RA Sun Z., Harris H.M., McCann A., Guo C., Argimon S., Zhang W., Yang X., RA Jeffery I.B., Cooney J.C., Kagawa T.F., Liu W., Song Y., Salvetti E., RA Wrobel A., Rasinkangas P., Parkhill J., Rea M.C., O'Sullivan O., RA Ritari J., Douillard F.P., Paul Ross R., Yang R., Briner A.E., RA Felis G.E., de Vos W.M., Barrangou R., Klaenhammer T.R., RA Caufield P.W., Cui Y., Zhang H., O'Toole P.W.; RT "Expanding the biotechnology potential of lactobacilli through RT comparative genomics of 213 strains and associated genera."; RL Nat. Commun. 6:8322-8322(2015). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KRM72205.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AYZQ01000002; KRM72205.1; -; Genomic_DNA. DR RefSeq; WP_057894468.1; NZ_AYZQ01000002.1. DR EnsemblBacteria; KRM72205; KRM72205; FC34_GL001190. DR PATRIC; fig|1423727.3.peg.1209; -. DR Proteomes; UP000051672; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000051672}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000051672}. FT DOMAIN 197 368 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 423 AA; 46723 MW; 1CEAE94BF77D5369 CRC64; MQETNEKVII TGISNQQTDF DYSMTELSEL AAANSYDVVG EVRQNADRPT GATYFGKGKV EEVGETARML EATTVLVNDE LTPSQLRNLE KQLGLHVVDR TQLILDIFGN RARSKAAKTQ VEIAQLKYAL PRLHPSANRL DQQGGGGGLA NRGAGETQLE LDRRILTKRI AHLRQDLKDA DVGEEVRRAK RQSNELPVVA LVGYTNAGKS TTMNGLLDLF ADRPEDKQVF EKDMLFATLD TSVRALTLPD HRQFLLSDTV GFVSKLPHNL IDSFKATLAE AANADLLIQV VDYADPNYQE MMRITEGVLK EIGIENIPMI EAYNKADLRD DGVSFPEVDG NQIVYSARDP KSLKALTDLI TTNIFANHQT NTYLIPFSDG NIVSFINENT AVKSTDYTED GTKIVASVNA IQAGKLAKYQ IDD // ID A0A0R2AYH1_9LACO Unreviewed; 423 AA. AC A0A0R2AYH1; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=FD06_GL001248 {ECO:0000313|EMBL:KRM68227.1}; OS Lactobacillus ozensis DSM 23829 = JCM 17196. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; OC Lactobacillus. OX NCBI_TaxID=1423781 {ECO:0000313|EMBL:KRM68227.1, ECO:0000313|Proteomes:UP000052012}; RN [1] {ECO:0000313|EMBL:KRM68227.1, ECO:0000313|Proteomes:UP000052012} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 23829 {ECO:0000313|EMBL:KRM68227.1, RC ECO:0000313|Proteomes:UP000052012}; RX PubMed=26415554; DOI=10.1038/ncomms9322; RA Sun Z., Harris H.M., McCann A., Guo C., Argimon S., Zhang W., Yang X., RA Jeffery I.B., Cooney J.C., Kagawa T.F., Liu W., Song Y., Salvetti E., RA Wrobel A., Rasinkangas P., Parkhill J., Rea M.C., O'Sullivan O., RA Ritari J., Douillard F.P., Paul Ross R., Yang R., Briner A.E., RA Felis G.E., de Vos W.M., Barrangou R., Klaenhammer T.R., RA Caufield P.W., Cui Y., Zhang H., O'Toole P.W.; RT "Expanding the biotechnology potential of lactobacilli through RT comparative genomics of 213 strains and associated genera."; RL Nat. Commun. 6:8322-8322(2015). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KRM68227.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AYYQ01000029; KRM68227.1; -; Genomic_DNA. DR RefSeq; WP_056966099.1; NZ_AYYQ01000029.1. DR EnsemblBacteria; KRM68227; KRM68227; FD06_GL001248. DR PATRIC; fig|1423781.4.peg.1293; -. DR Proteomes; UP000052012; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000052012}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000052012}. FT DOMAIN 200 368 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 423 AA; 47470 MW; 0A970C5932B63B67 CRC64; MNNELLPVIT IGLNLNNERF EYSMKELSAL AFANNMQVVE ELVQKLDHPD SATYFGKGKV ELLKETATAH NVNTVVVNDE LSPSQLRNLE KKTEVKIIDR TGLILEIFAN RARTHEAKLQ VQLAKLQYQL PRLHTSASQR LDQQTGSGGG GFTNRGSGES QLELNRRVIE KSITHIKEEL KTIEKSDKTQ RKQRAKSDIP NVALVGYTNA GKSTIMNQLV QRYGENVEKQ VMVKNMLFAT LDTSVRKLVF SDQKKMLLSD TVGFVSKLPH QLIKAFRSTL SEAASADLLV QVVDESDENK QLMMETTNET LKEIGIENIP MLTIFNKADL ANESRPVRTG NSLTMAALED SSVNELVNVI KEKILKNYAT INLLIPFSDG NVVEYLNSNA NVLETKYNAE GTEIKVELPD SDLNRFEKYV IKK // ID A0A0R2BEK6_LACCL Unreviewed; 427 AA. AC A0A0R2BEK6; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=FC82_GL000039 {ECO:0000313|EMBL:KRM78013.1}; OS Lactobacillus collinoides DSM 20515 = JCM 1123. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; OC Lactobacillus. OX NCBI_TaxID=1423733 {ECO:0000313|EMBL:KRM78013.1, ECO:0000313|Proteomes:UP000051845}; RN [1] {ECO:0000313|EMBL:KRM78013.1, ECO:0000313|Proteomes:UP000051845} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 20515 {ECO:0000313|EMBL:KRM78013.1, RC ECO:0000313|Proteomes:UP000051845}; RX PubMed=26415554; DOI=10.1038/ncomms9322; RA Sun Z., Harris H.M., McCann A., Guo C., Argimon S., Zhang W., Yang X., RA Jeffery I.B., Cooney J.C., Kagawa T.F., Liu W., Song Y., Salvetti E., RA Wrobel A., Rasinkangas P., Parkhill J., Rea M.C., O'Sullivan O., RA Ritari J., Douillard F.P., Paul Ross R., Yang R., Briner A.E., RA Felis G.E., de Vos W.M., Barrangou R., Klaenhammer T.R., RA Caufield P.W., Cui Y., Zhang H., O'Toole P.W.; RT "Expanding the biotechnology potential of lactobacilli through RT comparative genomics of 213 strains and associated genera."; RL Nat. Commun. 6:8322-8322(2015). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KRM78013.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AYYR01000001; KRM78013.1; -; Genomic_DNA. DR RefSeq; WP_056995888.1; NZ_AYYR01000001.1. DR EnsemblBacteria; KRM78013; KRM78013; FC82_GL000039. DR PATRIC; fig|1423733.4.peg.40; -. DR Proteomes; UP000051845; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000051845}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000051845}. FT DOMAIN 202 370 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 427 AA; 47353 MW; E584FFB5C3C77D0D CRC64; MDNSELTPVI NIGLNTGRAN FNYGMAELAA LSTANNMNVV ERIDQSLPKP IAATYFGTGK VEELRDIVVE TGAEIVVAND ELTPSQIRNL EKVVKVPVMD RTGLILAIFA NRAQSREAKL QVQLAKLQYQ MPRLHTAANQ SLDQQTGTSA GGGFTNRGAG EAQIELSRRT VQRQINHVRH ELKEVNRSAE VKRQQREKGH LPNVALIGYT NAGKSTIMNE LIKRFGMNDD KQVMVKNMLF ATLDTSVRQL QFEDAKKLLL SDTVGFVSQL PTTLVEAFKS TLYEAANADL LVQIVDYSSN DRANMMTTTE KTLREIGVPD LPMLTVFNKA DLTDSEYPTQ AGDQLVISAN DDASIDLLVD AIKKKVFKNF VTATFLIPFD KGDVVSYLNE HASVLNTDYK AEGTEMTAEV TDIDFQRFQK YYVSSEA // ID A0A0R2BMU8_9LACO Unreviewed; 430 AA. AC A0A0R2BMU8; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=FC84_GL000605 {ECO:0000313|EMBL:KRM79906.1}; OS Lactobacillus dextrinicus DSM 20335. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; OC Lactobacillus. OX NCBI_TaxID=1423738 {ECO:0000313|EMBL:KRM79906.1, ECO:0000313|Proteomes:UP000051813}; RN [1] {ECO:0000313|EMBL:KRM79906.1, ECO:0000313|Proteomes:UP000051813} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 20335 {ECO:0000313|EMBL:KRM79906.1, RC ECO:0000313|Proteomes:UP000051813}; RX PubMed=26415554; DOI=10.1038/ncomms9322; RA Sun Z., Harris H.M., McCann A., Guo C., Argimon S., Zhang W., Yang X., RA Jeffery I.B., Cooney J.C., Kagawa T.F., Liu W., Song Y., Salvetti E., RA Wrobel A., Rasinkangas P., Parkhill J., Rea M.C., O'Sullivan O., RA Ritari J., Douillard F.P., Paul Ross R., Yang R., Briner A.E., RA Felis G.E., de Vos W.M., Barrangou R., Klaenhammer T.R., RA Caufield P.W., Cui Y., Zhang H., O'Toole P.W.; RT "Expanding the biotechnology potential of lactobacilli through RT comparative genomics of 213 strains and associated genera."; RL Nat. Commun. 6:8322-8322(2015). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KRM79906.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AYYK01000001; KRM79906.1; -; Genomic_DNA. DR RefSeq; WP_057753880.1; NZ_AYYK01000001.1. DR EnsemblBacteria; KRM79906; KRM79906; FC84_GL000605. DR PATRIC; fig|1423738.3.peg.614; -. DR Proteomes; UP000051813; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000051813}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000051813}. FT DOMAIN 206 377 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 172 199 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 430 AA; 48175 MW; 1ADE8E67883B95E0 CRC64; MSDTINLQPE KERVLIGGLN RNKTSDFDYT MTELGELAKA DNMEVVDQVI QNLDHKDAAT YFGSGKIQEI AELANGLDVH TLVINDELSP SQIANIEKET KLRIVDRTEL ILEIFADRAQ TKEAKTQVEI ARLQYELPRI HPSANSLDQQ HSGGGGGLRN RGAGETQSEL DRRVIRKRIS DLKQNLKALE KSAATQRERR QQSGLPKVAL VGYTNAGKST TMNQLLARFD QLDADKKQVF EKDMLFATLD TSVRTIQLPN KQQFLLSDTV GFVSHLPHNL VASFKSTLAE AADADLLIQV VDYSDPNYRE MMTTTTNTLN EIGIENIPMI VAYNKADLKA DTNYPEVNGD DFIYSAKDPA SIDALAKLIT KHIFAGYHTV NLLIPFSEAR ILAELEAHTS IIEKEYTEQG TQVKVVLDPI RYNKYQKFVH // ID A0A0R2C8V2_9LACO Unreviewed; 434 AA. AC A0A0R2C8V2; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=FD19_GL000996 {ECO:0000313|EMBL:KRM87490.1}; OS Lactobacillus thailandensis DSM 22698 = JCM 13996. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; OC Lactobacillus. OX NCBI_TaxID=1423810 {ECO:0000313|EMBL:KRM87490.1, ECO:0000313|Proteomes:UP000051789}; RN [1] {ECO:0000313|EMBL:KRM87490.1, ECO:0000313|Proteomes:UP000051789} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 22698 {ECO:0000313|EMBL:KRM87490.1, RC ECO:0000313|Proteomes:UP000051789}; RX PubMed=26415554; DOI=10.1038/ncomms9322; RA Sun Z., Harris H.M., McCann A., Guo C., Argimon S., Zhang W., Yang X., RA Jeffery I.B., Cooney J.C., Kagawa T.F., Liu W., Song Y., Salvetti E., RA Wrobel A., Rasinkangas P., Parkhill J., Rea M.C., O'Sullivan O., RA Ritari J., Douillard F.P., Paul Ross R., Yang R., Briner A.E., RA Felis G.E., de Vos W.M., Barrangou R., Klaenhammer T.R., RA Caufield P.W., Cui Y., Zhang H., O'Toole P.W.; RT "Expanding the biotechnology potential of lactobacilli through RT comparative genomics of 213 strains and associated genera."; RL Nat. Commun. 6:8322-8322(2015). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KRM87490.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AYZK01000002; KRM87490.1; -; Genomic_DNA. DR EnsemblBacteria; KRM87490; KRM87490; FD19_GL000996. DR PATRIC; fig|1423810.4.peg.1020; -. DR Proteomes; UP000051789; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000051789}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000051789}. FT DOMAIN 208 379 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 167 194 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 434 AA; 48036 MW; B0350BBF6C21DDA0 CRC64; MIKEDFMPET QTNAIVAGIT RRQPNFDYTM TELANLAAAN NYVVVDSVRQ NADQVVAATY FGKGKAEELG ELARLKDAQT VIVNDELTPS QLRNLEKIIG VDVVDRTQLI LDIFGTRARS KQAKTQVEIA QLRYALPRLR QRNANFDQQS AGTGAGGAGL ANRGSGETQL ELDRRRLTKR ISRLKQELAD EAKDEETRSA QRNESHLPTV ALVGYTNAGK STTMNGLLNL FAEQGEAKNV EEKDMLFATL DTSVRKIELP SNRAFLLSDT VGFVSKLPTK LVDSFKATLA EAKNADLLLH VVDYADPHYQ DMMAVTEATL ADIGIHDVPT IIIDNKADLR PDTTYPEMVG DSELIFSARD QRSLQKLAEL IEAKLFAHEE THTYLIPFSD GQVVSYINDH LKIDATEYTD AGTRITASVD ATQAGRLARY LDED // ID A0A0R2CDC6_9LACO Unreviewed; 416 AA. AC A0A0R2CDC6; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=FD21_GL001737 {ECO:0000313|EMBL:KRM89354.1}; OS Lactobacillus vini DSM 20605. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; OC Lactobacillus. OX NCBI_TaxID=1133569 {ECO:0000313|EMBL:KRM89354.1, ECO:0000313|Proteomes:UP000051576}; RN [1] {ECO:0000313|EMBL:KRM89354.1, ECO:0000313|Proteomes:UP000051576} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 20605 {ECO:0000313|EMBL:KRM89354.1, RC ECO:0000313|Proteomes:UP000051576}; RX PubMed=26415554; DOI=10.1038/ncomms9322; RA Sun Z., Harris H.M., McCann A., Guo C., Argimon S., Zhang W., Yang X., RA Jeffery I.B., Cooney J.C., Kagawa T.F., Liu W., Song Y., Salvetti E., RA Wrobel A., Rasinkangas P., Parkhill J., Rea M.C., O'Sullivan O., RA Ritari J., Douillard F.P., Paul Ross R., Yang R., Briner A.E., RA Felis G.E., de Vos W.M., Barrangou R., Klaenhammer T.R., RA Caufield P.W., Cui Y., Zhang H., O'Toole P.W.; RT "Expanding the biotechnology potential of lactobacilli through RT comparative genomics of 213 strains and associated genera."; RL Nat. Commun. 6:8322-8322(2015). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KRM89354.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AYYX01000006; KRM89354.1; -; Genomic_DNA. DR RefSeq; WP_010581151.1; NZ_AYYX01000006.1. DR EnsemblBacteria; KRM89354; KRM89354; FD21_GL001737. DR PATRIC; fig|1133569.4.peg.1881; -. DR Proteomes; UP000051576; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000051576}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000051576}. FT DOMAIN 194 326 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 416 AA; 46239 MW; 938BEDCFC33C9304 CRC64; MTKIIITGLN LKTADFDYSM QEFANLAQAA EMDVCLQLTQ TTDHPNAGTY LGSGKVAELA AAIQANQAEA LLVNAQLSPT QLRNIESLVK VPVIDRTELI LEIFSRRAQT KRAQLQVEIA RLKYQLPRLR VSGFNKLDQQ NGGGQGANRG AGETQHELTK RTLQKRITQL THQLQELATE QTTQSRARKR SGLPSVALVG YTNAGKSTTF NGLVKLFGEK TAHQVLVKDQ LFATLDTSIR RLTFPDQKAL LLSDTVGFIS QLPADLLEAF KTTLETVLDA DLLVQVVDCS HPEHQKMIAA TNQTLQEIGA DAIPMIYAYN QADKLEIAYP VTEGQQITYS AMDSRSLKML AELLKQQLFK GYQKLDYLIP YTAGKYVEEL NQQAHVLKTS YTETGTLLQA EVSPVQAQKY VRFQKH // ID A0A0R2CDX3_9LACO Unreviewed; 427 AA. AC A0A0R2CDX3; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=FC80_GL001771 {ECO:0000313|EMBL:KRM89949.1}; OS Lactobacillus cacaonum DSM 21116. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; OC Lactobacillus. OX NCBI_TaxID=1423729 {ECO:0000313|EMBL:KRM89949.1, ECO:0000313|Proteomes:UP000051131}; RN [1] {ECO:0000313|EMBL:KRM89949.1, ECO:0000313|Proteomes:UP000051131} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 21116 {ECO:0000313|EMBL:KRM89949.1, RC ECO:0000313|Proteomes:UP000051131}; RX PubMed=26415554; DOI=10.1038/ncomms9322; RA Sun Z., Harris H.M., McCann A., Guo C., Argimon S., Zhang W., Yang X., RA Jeffery I.B., Cooney J.C., Kagawa T.F., Liu W., Song Y., Salvetti E., RA Wrobel A., Rasinkangas P., Parkhill J., Rea M.C., O'Sullivan O., RA Ritari J., Douillard F.P., Paul Ross R., Yang R., Briner A.E., RA Felis G.E., de Vos W.M., Barrangou R., Klaenhammer T.R., RA Caufield P.W., Cui Y., Zhang H., O'Toole P.W.; RT "Expanding the biotechnology potential of lactobacilli through RT comparative genomics of 213 strains and associated genera."; RL Nat. Commun. 6:8322-8322(2015). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KRM89949.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AYZE01000017; KRM89949.1; -; Genomic_DNA. DR RefSeq; WP_057829807.1; NZ_AYZE01000017.1. DR EnsemblBacteria; KRM89949; KRM89949; FC80_GL001771. DR PATRIC; fig|1423729.3.peg.1798; -. DR Proteomes; UP000051131; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000051131}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000051131}. FT DOMAIN 194 362 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 427 AA; 47823 MW; 4EDDE41479337C7C CRC64; MIPVITAGIE AQQENFDYLM DELAELAKAN SMSVVADVRQ RLQKPVSATY LGKGKIAEIA EIARETNAQF LILNDELSPT QIRNLEKDAA ISVLDRTELI LEIFSNRAHS KEAQIQVEIA RLKYKMPRLR VAPDIKLDQQ SASGALANRG AGETKLELNK RTLQKRISFL SHELKEIDKE FEIKSKSRRN SDLPSVALVG YTNAGKSTTM NGLLSLFSED EKKQVFEKDM LFATLDTSVR SLSFSDNKKF LLSDTVGFVS KLPHNLIEAF KSTLAEVRDA DLLIQVIDVS DPHLKEMIST TNKTLEELEI GHKTMIYAYN KADKISLEFP TVEGLNLTYS ARDESSLQEL ASLIKKSLFP GYQKMKFLIP FTSGAYLESL NSKANVLKTE YTAKGSIVTA EVSPIQAKYY SKFSWNPDEN KTSAEEI // ID A0A0R2CZR5_9LACO Unreviewed; 425 AA. AC A0A0R2CZR5; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 07-JUN-2017, entry version 10. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=FC56_GL000861 {ECO:0000313|EMBL:KRM93196.1}; OS Lactobacillus senioris DSM 24302 = JCM 17472. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; OC Lactobacillus. OX NCBI_TaxID=1423802 {ECO:0000313|EMBL:KRM93196.1, ECO:0000313|Proteomes:UP000051256}; RN [1] {ECO:0000313|EMBL:KRM93196.1, ECO:0000313|Proteomes:UP000051256} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 24302 {ECO:0000313|EMBL:KRM93196.1, RC ECO:0000313|Proteomes:UP000051256}; RX PubMed=26415554; DOI=10.1038/ncomms9322; RA Sun Z., Harris H.M., McCann A., Guo C., Argimon S., Zhang W., Yang X., RA Jeffery I.B., Cooney J.C., Kagawa T.F., Liu W., Song Y., Salvetti E., RA Wrobel A., Rasinkangas P., Parkhill J., Rea M.C., O'Sullivan O., RA Ritari J., Douillard F.P., Paul Ross R., Yang R., Briner A.E., RA Felis G.E., de Vos W.M., Barrangou R., Klaenhammer T.R., RA Caufield P.W., Cui Y., Zhang H., O'Toole P.W.; RT "Expanding the biotechnology potential of lactobacilli through RT comparative genomics of 213 strains and associated genera."; RL Nat. Commun. 6:8322-8322(2015). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KRM93196.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AYZR01000009; KRM93196.1; -; Genomic_DNA. DR RefSeq; WP_056978629.1; NZ_AYZR01000009.1. DR EnsemblBacteria; KRM93196; KRM93196; FC56_GL000861. DR PATRIC; fig|1423802.4.peg.874; -. DR Proteomes; UP000051256; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000051256}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000051256}. FT DOMAIN 202 370 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 161 198 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 425 AA; 47207 MW; 00DE8EA0EF5F25D1 CRC64; MTEVTLTPVI TIALDLNSPN FTYAVEELNN LVEANNMEVA ETLTQKLDRS DPATYFGKGK IEELKELVIE TGVDTVIAND ELSPSQIRNI EKAIDARIID RTGLILEIFA NRAQSKEAKL QVELAKLKYQ LPRLHTSASQ RLDQQTGTSA GGGFTNRGAG ESQLELNRRT LQKRITHVQE ELKEAQKADE TKRKQRDRSE LPTVALVGYT NAGKSTIMNG LIKLFGENEE KQVLVKNMLF ATLDTSVRKL TLPDQKSFLL SDTVGFVSQL PHQLVQAFKS TLAEAANADL LVQVVDYSDP DYQLMMETTA KTLAEIGIEN RPMIVALNKA DRIEGPYPTR EGNDLIMAAT DETSLQELTS MIVELAFDDY ETKTLLIPFN RGDVISYLND NANVLSTEYL AEGTQVTVEL GGADLNRFDD FLITN // ID A0A0R2DG10_9LACO Unreviewed; 424 AA. AC A0A0R2DG10; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=FC24_GL000293 {ECO:0000313|EMBL:KRM99433.1}; OS Lactobacillus rennini DSM 20253. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; OC Lactobacillus. OX NCBI_TaxID=1423796 {ECO:0000313|EMBL:KRM99433.1, ECO:0000313|Proteomes:UP000051638}; RN [1] {ECO:0000313|EMBL:KRM99433.1, ECO:0000313|Proteomes:UP000051638} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 20253 {ECO:0000313|EMBL:KRM99433.1, RC ECO:0000313|Proteomes:UP000051638}; RX PubMed=26415554; DOI=10.1038/ncomms9322; RA Sun Z., Harris H.M., McCann A., Guo C., Argimon S., Zhang W., Yang X., RA Jeffery I.B., Cooney J.C., Kagawa T.F., Liu W., Song Y., Salvetti E., RA Wrobel A., Rasinkangas P., Parkhill J., Rea M.C., O'Sullivan O., RA Ritari J., Douillard F.P., Paul Ross R., Yang R., Briner A.E., RA Felis G.E., de Vos W.M., Barrangou R., Klaenhammer T.R., RA Caufield P.W., Cui Y., Zhang H., O'Toole P.W.; RT "Expanding the biotechnology potential of lactobacilli through RT comparative genomics of 213 strains and associated genera."; RL Nat. Commun. 6:8322-8322(2015). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KRM99433.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AYYI01000014; KRM99433.1; -; Genomic_DNA. DR RefSeq; WP_057873216.1; NZ_AYYI01000014.1. DR EnsemblBacteria; KRM99433; KRM99433; FC24_GL000293. DR PATRIC; fig|1423796.3.peg.304; -. DR Proteomes; UP000051638; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000051638}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000051638}. FT DOMAIN 199 369 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 424 AA; 47490 MW; 0DAAE67ACEB09798 CRC64; MQKIESTKVL IGGVSQNQPY FESDLAELAE LTKANNMQVV GTVRQNLDHV VTATYFGSGK LAEIKALAAE KDAQSLILND ELSPSQIRNL EQDLKLPIID RTRLILAIFA NRAKSREAKL QVQIARLQYE LPRLRIGEEA NFMQQGGGPG FANRGSGETK LEMNQRTIKN KISQLWHELK AMNVSQQTKR QQRQRTNIPT VALVGYTNAG KSTTMNGLLR LFNPDTAKTV FERDMLFATL DTSVREITLP TNQKFLLSDT VGFINKLPTQ LVKAFRSTLA EAANADLLVQ VIDFSDPHYE EMAKVTNATL RELQIADIPM IYAYNKADRK PGTQFPLQTG EHDLVYAAND QTSLKLLAEM IAKALFSDLT QVAFNIPFTE SKWVAYLNQH AHVLSQNYSA NGTQLTAEVT STDRQRLAKY VVNR // ID A0A0R2DN68_9LACO Unreviewed; 422 AA. AC A0A0R2DN68; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=FC86_GL000051 {ECO:0000313|EMBL:KRN04603.1}; OS Lactobacillus floricola DSM 23037 = JCM 16512. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; OC Lactobacillus. OX NCBI_TaxID=1423744 {ECO:0000313|EMBL:KRN04603.1, ECO:0000313|Proteomes:UP000051378}; RN [1] {ECO:0000313|EMBL:KRN04603.1, ECO:0000313|Proteomes:UP000051378} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 23037 {ECO:0000313|EMBL:KRN04603.1, RC ECO:0000313|Proteomes:UP000051378}; RX PubMed=26415554; DOI=10.1038/ncomms9322; RA Sun Z., Harris H.M., McCann A., Guo C., Argimon S., Zhang W., Yang X., RA Jeffery I.B., Cooney J.C., Kagawa T.F., Liu W., Song Y., Salvetti E., RA Wrobel A., Rasinkangas P., Parkhill J., Rea M.C., O'Sullivan O., RA Ritari J., Douillard F.P., Paul Ross R., Yang R., Briner A.E., RA Felis G.E., de Vos W.M., Barrangou R., Klaenhammer T.R., RA Caufield P.W., Cui Y., Zhang H., O'Toole P.W.; RT "Expanding the biotechnology potential of lactobacilli through RT comparative genomics of 213 strains and associated genera."; RL Nat. Commun. 6:8322-8322(2015). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KRN04603.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AYZL01000008; KRN04603.1; -; Genomic_DNA. DR RefSeq; WP_056974240.1; NZ_AYZL01000008.1. DR EnsemblBacteria; KRN04603; KRN04603; FC86_GL000051. DR PATRIC; fig|1423744.4.peg.54; -. DR Proteomes; UP000051378; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000051378}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000051378}. FT DOMAIN 200 331 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 422 AA; 47972 MW; E34118F131E6B81B CRC64; MLSNNIEKTK VVVAGVDAQK YNFDYAISEL KELVFANNMT ASATLTQKLD NPVSGTYFGK GKLEELKQLC EHKDVGTVVL NDELTPTQIR NIEKITELKV IDRTELILEI FAQRAQTKQA ILQVNLARLQ YALPRLHPSE NTLDQQRGGA GFANRGAGET KLEINRRTIQ KEITRIKRQL EEIEQTTLTQ RKDRQNSDLP KVALVGYTNA GKSSTMNALI KAFTKNQEDK AVFEKDMLFA TLDTSVRHIR LPHHREFILS DTVGFVSRLP HNLVEAFKAT LLEAKEADLI IQVVDYSDPN YREMMATTAD VLKEIDADKI PMILAFNKAD KTDTPYPQIN SDEIIYSAIE KPSILQFSDF IQKQIFKDYE IIDLKIPATD GKTLAYLQGK TEIISQEIVE TDFYIKAVIN PNDKIWLKDY LK // ID A0A0R2F4U3_9LACO Unreviewed; 425 AA. AC A0A0R2F4U3; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=FC75_GL001483 {ECO:0000313|EMBL:KRN23283.1}; OS Lactobacillus camelliae DSM 22697 = JCM 13995. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; OC Lactobacillus. OX NCBI_TaxID=1423730 {ECO:0000313|EMBL:KRN23283.1, ECO:0000313|Proteomes:UP000050865}; RN [1] {ECO:0000313|EMBL:KRN23283.1, ECO:0000313|Proteomes:UP000050865} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 22697 {ECO:0000313|EMBL:KRN23283.1, RC ECO:0000313|Proteomes:UP000050865}; RX PubMed=26415554; DOI=10.1038/ncomms9322; RA Sun Z., Harris H.M., McCann A., Guo C., Argimon S., Zhang W., Yang X., RA Jeffery I.B., Cooney J.C., Kagawa T.F., Liu W., Song Y., Salvetti E., RA Wrobel A., Rasinkangas P., Parkhill J., Rea M.C., O'Sullivan O., RA Ritari J., Douillard F.P., Paul Ross R., Yang R., Briner A.E., RA Felis G.E., de Vos W.M., Barrangou R., Klaenhammer T.R., RA Caufield P.W., Cui Y., Zhang H., O'Toole P.W.; RT "Expanding the biotechnology potential of lactobacilli through RT comparative genomics of 213 strains and associated genera."; RL Nat. Commun. 6:8322-8322(2015). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KRN23283.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AYZJ01000028; KRN23283.1; -; Genomic_DNA. DR RefSeq; WP_056989351.1; NZ_AYZJ01000028.1. DR EnsemblBacteria; KRN23283; KRN23283; FC75_GL001483. DR PATRIC; fig|1423730.4.peg.1555; -. DR Proteomes; UP000050865; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000050865}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000050865}. FT DOMAIN 199 369 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 425 AA; 47373 MW; 429AF5FF7AA20540 CRC64; MQEIPEKVII AGISRMQENF DYSMQELKEL ALARHYDVVG ESRQNLDRPT GATYFGSGKV DEVAELARAN DATTVVINDE LTPSQLRNLE KEMKLHVVDR TQLILDIFAS RAASKTAQAQ VEIAQLQYAL PRLHPSANKL DQQGGGGAGG LANRGAGETK LEMDKRVLNK RIARLRRELK DADVGEEVRR AQRKENKLPV VALVGYTNAG KSTTMNGLLD RYTDLGADKQ VFEKDMLFAT LDTSVRQISL KDNRKFLLSD TVGFVSKLPH NLIDSFKATL AEAANADLLI QVVDYHDEHY PEMMKVTSDT LKSIGIENIP MIEAYNKADL RPGTRFPEEN GNTLIYSAKD PASLDKLVQM ITARVFSDSA VHTYLIPFDK GQLVDFINRE TGVINTEYVE TGTKVKTTVN PIQAGKLRQY LVEED // ID A0A0R2FCE0_9LACO Unreviewed; 435 AA. AC A0A0R2FCE0; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=FD14_GL002653 {ECO:0000313|EMBL:KRN26193.1}; OS Lactobacillus similis DSM 23365 = JCM 2765. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; OC Lactobacillus. OX NCBI_TaxID=1423804 {ECO:0000313|EMBL:KRN26193.1, ECO:0000313|Proteomes:UP000051442}; RN [1] {ECO:0000313|EMBL:KRN26193.1, ECO:0000313|Proteomes:UP000051442} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 23365 {ECO:0000313|EMBL:KRN26193.1, RC ECO:0000313|Proteomes:UP000051442}; RX PubMed=26415554; DOI=10.1038/ncomms9322; RA Sun Z., Harris H.M., McCann A., Guo C., Argimon S., Zhang W., Yang X., RA Jeffery I.B., Cooney J.C., Kagawa T.F., Liu W., Song Y., Salvetti E., RA Wrobel A., Rasinkangas P., Parkhill J., Rea M.C., O'Sullivan O., RA Ritari J., Douillard F.P., Paul Ross R., Yang R., Briner A.E., RA Felis G.E., de Vos W.M., Barrangou R., Klaenhammer T.R., RA Caufield P.W., Cui Y., Zhang H., O'Toole P.W.; RT "Expanding the biotechnology potential of lactobacilli through RT comparative genomics of 213 strains and associated genera."; RL Nat. Commun. 6:8322-8322(2015). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KRN26193.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AYZM01000042; KRN26193.1; -; Genomic_DNA. DR EnsemblBacteria; KRN26193; KRN26193; FD14_GL002653. DR PATRIC; fig|1423804.4.peg.2866; -. DR Proteomes; UP000051442; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000051442}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}. FT DOMAIN 209 377 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 435 AA; 48386 MW; 3A09EC45F655D5C6 CRC64; MIKDGDNMDQ SELVPVLNIG LNTGRYNFDY AMAELKALSV ANNMHVVETI VQNLNQPVAG TYFGTGKVEE LRDAVIDTGA EIVVANDELT PSQIRNLEKV VEVPVMDRTG LILAIFANRA QSREAKLQVE LAKLQYQMPR LHTAMNQRLD QQTGTSAGGG FTNRGAGEAQ VELNRRTIQR QINHVRHELK NVNKSAEVKR QQRERVHLPN VALIGYTNAG KSTIMNELIK RFGMNDDKQV MVKNMLFATL DTSVRQLQFA DAKKLLLSDT VGFVSQLPTT LVEAFKSTLY EAANADLLVQ VVDYSSDNKA DMMATTRKTL TEIGVPDLPM ITVYNKADLT DTDFPSRAGD ELIVSAKDEA SIDMLVDVIK EKVFTNYVTA TFLVPFAKGD VVSYLNDHAS VLKTDYLAEG TQVTAEVTTI DFHRFEQYLV DEVKD // ID A0A0R2FTY4_9LACO Unreviewed; 424 AA. AC A0A0R2FTY4; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=IV38_GL001643 {ECO:0000313|EMBL:KRN28190.1}, GN IV40_GL001572 {ECO:0000313|EMBL:KRN30934.1}; OS Lactobacillus selangorensis. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; OC Lactobacillus. OX NCBI_TaxID=81857 {ECO:0000313|EMBL:KRN30934.1, ECO:0000313|Proteomes:UP000051645}; RN [1] {ECO:0000313|EMBL:KRN30934.1, ECO:0000313|Proteomes:UP000051645, ECO:0000313|Proteomes:UP000051751} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-66 {ECO:0000313|EMBL:KRN28190.1, RC ECO:0000313|Proteomes:UP000051751}, and RC DSM 13344 {ECO:0000313|EMBL:KRN30934.1, RC ECO:0000313|Proteomes:UP000051645}; RX PubMed=26415554; DOI=10.1038/ncomms9322; RA Sun Z., Harris H.M., McCann A., Guo C., Argimon S., Zhang W., Yang X., RA Jeffery I.B., Cooney J.C., Kagawa T.F., Liu W., Song Y., Salvetti E., RA Wrobel A., Rasinkangas P., Parkhill J., Rea M.C., O'Sullivan O., RA Ritari J., Douillard F.P., Paul Ross R., Yang R., Briner A.E., RA Felis G.E., de Vos W.M., Barrangou R., Klaenhammer T.R., RA Caufield P.W., Cui Y., Zhang H., O'Toole P.W.; RT "Expanding the biotechnology potential of lactobacilli through RT comparative genomics of 213 strains and associated genera."; RL Nat. Commun. 6:8322-8322(2015). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KRN30934.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JQAT01000004; KRN28190.1; -; Genomic_DNA. DR EMBL; JQAZ01000005; KRN30934.1; -; Genomic_DNA. DR RefSeq; WP_057770069.1; NZ_JQAZ01000005.1. DR EnsemblBacteria; KRN28190; KRN28190; IV38_GL001643. DR EnsemblBacteria; KRN30934; KRN30934; IV40_GL001572. DR PATRIC; fig|81857.3.peg.1654; -. DR Proteomes; UP000051645; Unassembled WGS sequence. DR Proteomes; UP000051751; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000051645}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Hydrolase {ECO:0000313|EMBL:KRN30934.1}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Protease {ECO:0000313|EMBL:KRN30934.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000051645}. FT DOMAIN 200 370 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 424 AA; 47230 MW; 6C1C800993141384 CRC64; MEAETNPQTR VIITGVSQRR PNFDYTMTEL GELATANDMQ VVGDLRQIAD RPIAATYFGT GKVAEIKAYA EEMDAAVILV NDELSPSQIR NLEKETGKTI IDRTQLILDI FANRAQTKQA KYQVEIAQLQ YQLPRLHPSA NRLDQQGGGG GLANRGAGET KLEMNRRVIQ KRITHLRHAL KEQEKTQETQ SQQRAKSQLP VVALVGYTNA GKSTTMNGLL KLYSEHGAEK QVFTKNMLFA TLDTSVREIT LPSHQKFLLS DTVGFVSRLP HNLVEAFKAT LSEAVNADLI IQVVDYADPN YHDMIAVTDK TLAQIGAGDI PRIDAFNKAD LRTDTPYPEI NGNEIVYSAT DKKSLAELAT LIEQKIAAQY PTLTYLFPYT DGKALSALNE HAAILKQDYQ ENGTLVTARI NPNSRDYWSK YEVD // ID A0A0R2G1R6_9LACT Unreviewed; 430 AA. AC A0A0R2G1R6; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=IV68_GL000596 {ECO:0000313|EMBL:KRN32245.1}; OS Weissella halotolerans DSM 20190. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Leuconostocaceae; OC Weissella. OX NCBI_TaxID=1123500 {ECO:0000313|EMBL:KRN32245.1, ECO:0000313|Proteomes:UP000051296}; RN [1] {ECO:0000313|EMBL:KRN32245.1, ECO:0000313|Proteomes:UP000051296} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 20190 {ECO:0000313|EMBL:KRN32245.1, RC ECO:0000313|Proteomes:UP000051296}; RX PubMed=26415554; DOI=10.1038/ncomms9322; RA Sun Z., Harris H.M., McCann A., Guo C., Argimon S., Zhang W., Yang X., RA Jeffery I.B., Cooney J.C., Kagawa T.F., Liu W., Song Y., Salvetti E., RA Wrobel A., Rasinkangas P., Parkhill J., Rea M.C., O'Sullivan O., RA Ritari J., Douillard F.P., Paul Ross R., Yang R., Briner A.E., RA Felis G.E., de Vos W.M., Barrangou R., Klaenhammer T.R., RA Caufield P.W., Cui Y., Zhang H., O'Toole P.W.; RT "Expanding the biotechnology potential of lactobacilli through RT comparative genomics of 213 strains and associated genera."; RL Nat. Commun. 6:8322-8322(2015). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KRN32245.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JQAX01000002; KRN32245.1; -; Genomic_DNA. DR RefSeq; WP_022791606.1; NZ_JQAX01000002.1. DR EnsemblBacteria; KRN32245; KRN32245; IV68_GL000596. DR PATRIC; fig|1123500.6.peg.599; -. DR Proteomes; UP000051296; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000051296}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000051296}. FT DOMAIN 207 377 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 166 205 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 430 AA; 47644 MW; 33BD7006F74A6EA6 CRC64; MAVATSEVAK EQPRVILLGL DRQDDTFEYQ MTELAELAAA NDMVVVGQIS QKMDRPNAGT YFGKGKVDEL SEAVSYYEAD MVVANDELSP SQIRNLETKT GASVIDRTAL ILDIFARRAR TRVAQLQVAI AQLQYQLPRL RTSMNVRLDQ QTGGGGGSFT SRGAGETKLE LNRRHIEHKI ADLRKELAEI EHDDQTRRSQ RLKENIKNVA LVGYTNAGKS TIMNGLVQRF GANQEKTVFE ADMLFATLET AVRKLTLPDH QSFLLSDTVG FVSHLPHGLV AAFRATLTEA AQADLLVQVV DYSDENYQAM MATTEKTLKE IGVGDVPMIT VYNKADQIAD TAYPEREGEN ALVMSAQDES SLTALVTMIE EQIFADNVEK TLLIPFDQGK VVAELNDQAV VLATDYETDG TRLRVVLSPT QVKRYQQYEG // ID A0A0R2GSQ3_9LACO Unreviewed; 427 AA. AC A0A0R2GSQ3; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=IV41_GL001043 {ECO:0000313|EMBL:KRN43906.1}; OS Lactobacillus ingluviei. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; OC Lactobacillus. OX NCBI_TaxID=148604 {ECO:0000313|EMBL:KRN43906.1, ECO:0000313|Proteomes:UP000051639}; RN [1] {ECO:0000313|EMBL:KRN43906.1, ECO:0000313|Proteomes:UP000051639} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 14792 {ECO:0000313|EMBL:KRN43906.1, RC ECO:0000313|Proteomes:UP000051639}; RX PubMed=26415554; DOI=10.1038/ncomms9322; RA Sun Z., Harris H.M., McCann A., Guo C., Argimon S., Zhang W., Yang X., RA Jeffery I.B., Cooney J.C., Kagawa T.F., Liu W., Song Y., Salvetti E., RA Wrobel A., Rasinkangas P., Parkhill J., Rea M.C., O'Sullivan O., RA Ritari J., Douillard F.P., Paul Ross R., Yang R., Briner A.E., RA Felis G.E., de Vos W.M., Barrangou R., Klaenhammer T.R., RA Caufield P.W., Cui Y., Zhang H., O'Toole P.W.; RT "Expanding the biotechnology potential of lactobacilli through RT comparative genomics of 213 strains and associated genera."; RL Nat. Commun. 6:8322-8322(2015). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KRN43906.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JQBA01000029; KRN43906.1; -; Genomic_DNA. DR RefSeq; WP_019206434.1; NZ_JQBA01000029.1. DR EnsemblBacteria; KRN43906; KRN43906; IV41_GL001043. DR PATRIC; fig|148604.4.peg.1080; -. DR Proteomes; UP000051639; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000051639}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000051639}. FT DOMAIN 204 373 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 177 200 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 427 AA; 47760 MW; 3AF0DCD1E4B99DEC CRC64; MDTTISRPER VIIIGLDNDQ PDYQYSMTEL TELAEANQME VVDRLDQALD RPNAATYFGS GKVEELAQLV AALEVPTVIA NDELSPSQLQ NLTKATGVRV IDRTALILEI FAKRAQSKEA KIQVQIAQLQ YRLPRLQTAS DQRLDQQTGS GGGGGFTNRG AGETKLEMNH RVIAKQISHL RAELKEIEKS EQTKRAQRDK AAIPTAALVG YTNAGKSTIM NHLVERYGVD ADKQVFEKDM LFATLDTSVR QLTLPDQKRF LLSDTVGFVS KLPHHLVQAF KSTLTEAAQA DLLIQVIDYS DPHYEQMIKT TETTLQQIGV ENIPMIYVFN KADRTEIEFP TMEGDDRLII SAKDGASLDL LVEAIKHHLF SDYETVDLLI PFADGQVVSY LNEHATILNT EYVSEGTKLQ VELAPKDLPR VEKYRVM // ID A0A0R2H1R0_WEIVI Unreviewed; 427 AA. AC A0A0R2H1R0; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 07-JUN-2017, entry version 10. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=IV50_GL000636 {ECO:0000313|EMBL:KRN46366.1}; OS Weissella viridescens (Lactobacillus viridescens). OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Leuconostocaceae; OC Weissella. OX NCBI_TaxID=1629 {ECO:0000313|EMBL:KRN46366.1, ECO:0000313|Proteomes:UP000051992}; RN [1] {ECO:0000313|EMBL:KRN46366.1, ECO:0000313|Proteomes:UP000051992} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 20410 {ECO:0000313|EMBL:KRN46366.1, RC ECO:0000313|Proteomes:UP000051992}; RX PubMed=26415554; DOI=10.1038/ncomms9322; RA Sun Z., Harris H.M., McCann A., Guo C., Argimon S., Zhang W., Yang X., RA Jeffery I.B., Cooney J.C., Kagawa T.F., Liu W., Song Y., Salvetti E., RA Wrobel A., Rasinkangas P., Parkhill J., Rea M.C., O'Sullivan O., RA Ritari J., Douillard F.P., Paul Ross R., Yang R., Briner A.E., RA Felis G.E., de Vos W.M., Barrangou R., Klaenhammer T.R., RA Caufield P.W., Cui Y., Zhang H., O'Toole P.W.; RT "Expanding the biotechnology potential of lactobacilli through RT comparative genomics of 213 strains and associated genera."; RL Nat. Commun. 6:8322-8322(2015). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KRN46366.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JQBM01000002; KRN46366.1; -; Genomic_DNA. DR EnsemblBacteria; KRN46366; KRN46366; IV50_GL000636. DR PATRIC; fig|1629.5.peg.641; -. DR Proteomes; UP000051992; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000051992}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000051992}. FT DOMAIN 204 373 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 170 202 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 427 AA; 47707 MW; E7DCD4BB562CB1F9 CRC64; MIENEMDEKR PVILAGLDRQ NDDFDYQMEE LANLVEANHM NPVSTVTQKL DRPNPGTYFG KGKVEALKEA VDYYQVDMVV TNDELTPSQI RNLEAGTGVT VIDRTALILD IFASRAKTKV AKLQVEIAQL QYQLPRLRTS MNVRLDQQTG GNGGSFTSRG AGETKLEMNR RHIEHQIGEL RKELAEIEAD DATRRARREK ENIKNVALIG YTNAGKSTIM NALVRRFGEN QEKTVFQADM LFATLETSVR KLNLPDKQSF LLSDTVGFVS HLPHGLVAAF KATLAEAASA DLLVQVVDYS DPNYKEMMKT TADTLKEIGV GDIPMIVVYN KADKCDGVPY PEREGDDLIL SAPEESSQDM LLDAVRQHIF SDLIEKTVLI PFDQGQVVSE LNDQATVLST EYVENGTQMQ VVLTPTQLGR FEKYVID // ID A0A0R2HLV0_9FIRM Unreviewed; 400 AA. AC A0A0R2HLV0; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=IV49_GL000279 {ECO:0000313|EMBL:KRN50269.1}; OS Kandleria vitulina DSM 20405. OC Bacteria; Firmicutes; Erysipelotrichia; Erysipelotrichales; OC Erysipelotrichaceae; Kandleria. OX NCBI_TaxID=1410657 {ECO:0000313|EMBL:KRN50269.1, ECO:0000313|Proteomes:UP000051841}; RN [1] {ECO:0000313|EMBL:KRN50269.1, ECO:0000313|Proteomes:UP000051841} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 20405 {ECO:0000313|EMBL:KRN50269.1, RC ECO:0000313|Proteomes:UP000051841}; RX PubMed=26415554; DOI=10.1038/ncomms9322; RA Sun Z., Harris H.M., McCann A., Guo C., Argimon S., Zhang W., Yang X., RA Jeffery I.B., Cooney J.C., Kagawa T.F., Liu W., Song Y., Salvetti E., RA Wrobel A., Rasinkangas P., Parkhill J., Rea M.C., O'Sullivan O., RA Ritari J., Douillard F.P., Paul Ross R., Yang R., Briner A.E., RA Felis G.E., de Vos W.M., Barrangou R., Klaenhammer T.R., RA Caufield P.W., Cui Y., Zhang H., O'Toole P.W.; RT "Expanding the biotechnology potential of lactobacilli through RT comparative genomics of 213 strains and associated genera."; RL Nat. Commun. 6:8322-8322(2015). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KRN50269.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JQBL01000011; KRN50269.1; -; Genomic_DNA. DR RefSeq; WP_031589119.1; NZ_JQBL01000011.1. DR EnsemblBacteria; KRN50269; KRN50269; IV49_GL000279. DR PATRIC; fig|1410657.5.peg.293; -. DR Proteomes; UP000051841; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000051841}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000051841}. FT DOMAIN 186 346 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 400 AA; 46554 MW; 4BD3C8485120A23F CRC64; MKAILVALKY TTDYDFDISI KELKELCRAC QIEVTHIVTQ AADPNKTTYV GIGKIKEIRH LIEDEDMVIF NEELTPLQLR NISDLLGIEV KDRTDLILRI FESRARTKEA KLQVEVARLK YELPRLAGAH EEMYSQQGGS GFRGSGEQQI EIERRHIRRH MAQVYKELRE VTKERQTQRK RRENMKVVAL VGYTNAGKST LLNLFTQKKV YSEDMLFATL ETSTRQAVLK NNRTILMSDT VGFISQLPHH LIEAFKSTLE EVKEADLILH VVDASSPYAN KQIEVTNMVL KELGVETPML YVYNKCDLEQ AEFIVPRDPY VFISAKNNLH IDKLEDEIIK IIYKDEERIT LYIPYEEGDL YKKLIRETTL IKEEFQDECI AITIEAPTYY ANKYSRYRKV // ID A0A0R2HS12_9LACT Unreviewed; 433 AA. AC A0A0R2HS12; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 05-JUL-2017, entry version 12. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=IV71_GL001397 {ECO:0000313|EMBL:KRN52349.1}; OS Fructobacillus fructosus KCTC 3544. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Leuconostocaceae; OC Fructobacillus. OX NCBI_TaxID=930946 {ECO:0000313|EMBL:KRN52349.1, ECO:0000313|Proteomes:UP000051944}; RN [1] {ECO:0000313|EMBL:KRN52349.1, ECO:0000313|Proteomes:UP000051944} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 20349 {ECO:0000313|EMBL:KRN52349.1, RC ECO:0000313|Proteomes:UP000051944}; RX PubMed=26415554; DOI=10.1038/ncomms9322; RA Sun Z., Harris H.M., McCann A., Guo C., Argimon S., Zhang W., Yang X., RA Jeffery I.B., Cooney J.C., Kagawa T.F., Liu W., Song Y., Salvetti E., RA Wrobel A., Rasinkangas P., Parkhill J., Rea M.C., O'Sullivan O., RA Ritari J., Douillard F.P., Paul Ross R., Yang R., Briner A.E., RA Felis G.E., de Vos W.M., Barrangou R., Klaenhammer T.R., RA Caufield P.W., Cui Y., Zhang H., O'Toole P.W.; RT "Expanding the biotechnology potential of lactobacilli through RT comparative genomics of 213 strains and associated genera."; RL Nat. Commun. 6:8322-8322(2015). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KRN52349.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JQBH01000008; KRN52349.1; -; Genomic_DNA. DR RefSeq; WP_010017629.1; NZ_JQBH01000008.1. DR STRING; 930946.FfruK3_010100007070; -. DR EnsemblBacteria; KRN52349; KRN52349; IV71_GL001397. DR PATRIC; fig|930946.7.peg.1449; -. DR Proteomes; UP000051944; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000051944}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000051944}. FT DOMAIN 207 380 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 433 AA; 48251 MW; 7B2893DDA4D6FAD6 CRC64; MEEKNQTAQP VRKVLLAALK QNQKQNLDYE LEELSNLARA NRLEPVETFI QSLERPNPAT YFGKGKVEEL RIAVNTYETD LIVTNDELSP SQIRNLEKAT QATVVDRTGL ILDIFAKRAQ TKVAKLQVQL ARLEYQLPRL RTSMSVSLDQ QTGAGGAGFT SRGAGETKLE QSRRRLTSEM VAIKKELAAL QKDSQTQGKK RQESAIPTVA LVGYTNAGKS TLMNQFLVRF GQGAESDQSK QVFEKDMLFA TLNTTIRQLT LSDKSKFLLS DTVGFVSKLP HHLVAAFEST LQEAATADLL LQVVDISDEH YADMMKTTEE TLARLGIKDK PMITVYNKAD KADMAFPMLD GDAAITISAR DRKSQDALLE LIESRLFADR KKVTLAIPFA DSAVTANILD EHELLAQEFN ESGSLITVKL SSEEIARYRQ YIQ // ID A0A0R2HV10_CARDV Unreviewed; 424 AA. AC A0A0R2HV10; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 07-JUN-2017, entry version 10. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=IV74_GL001412 {ECO:0000313|EMBL:KRN56299.1}; OS Carnobacterium divergens DSM 20623. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Carnobacteriaceae; OC Carnobacterium. OX NCBI_TaxID=1449336 {ECO:0000313|EMBL:KRN56299.1, ECO:0000313|Proteomes:UP000051658}; RN [1] {ECO:0000313|EMBL:KRN56299.1, ECO:0000313|Proteomes:UP000051658} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 20623 {ECO:0000313|EMBL:KRN56299.1, RC ECO:0000313|Proteomes:UP000051658}; RX PubMed=26415554; DOI=10.1038/ncomms9322; RA Sun Z., Harris H.M., McCann A., Guo C., Argimon S., Zhang W., Yang X., RA Jeffery I.B., Cooney J.C., Kagawa T.F., Liu W., Song Y., Salvetti E., RA Wrobel A., Rasinkangas P., Parkhill J., Rea M.C., O'Sullivan O., RA Ritari J., Douillard F.P., Paul Ross R., Yang R., Briner A.E., RA Felis G.E., de Vos W.M., Barrangou R., Klaenhammer T.R., RA Caufield P.W., Cui Y., Zhang H., O'Toole P.W.; RT "Expanding the biotechnology potential of lactobacilli through RT comparative genomics of 213 strains and associated genera."; RL Nat. Commun. 6:8322-8322(2015). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KRN56299.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JQBS01000032; KRN56299.1; -; Genomic_DNA. DR EnsemblBacteria; KRN56299; KRN56299; IV74_GL001412. DR PATRIC; fig|1449336.4.peg.1442; -. DR Proteomes; UP000051658; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000051658}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000051658}. FT DOMAIN 208 369 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 424 AA; 47793 MW; BDFBFCE56AD1B2FA CRC64; MFKRNVGGTM EEKLDYERVV IVGVQTNELD TNFRYSLEEL GQLTETAHGQ VVAELTQKRD RMDSKTYLGK GKIQELVHLV EETEADVVIF NHALTPSQTR NIQVEIDVKV IDRIQLILDI FAMRAQSKEG KLQVALAQLQ YLLPRLAGQG KNLSKLGGGI GTRGPGETKL ETDRRHIRSQ INDIKKTLKE TEAHRQRSRE KRNDGTTFQI GLIGYTNAGK STLLNRLTDA KTYEENQLFA TLDPLTRKMV LPSGMNVTLT DTVGFIQDLP TQLIDAFHST LEETRGVDLL LHVVDAAAEN VAGHEVTVIN LLKELNMDQI PIFTVYNKKD LLNGNFSPNL FPNSLISAKD PEDLLKLRNQ IMKQMKEVML PYEFEVAADE GNKLVQLKKE TLLESAEFQE ELNVYLVKGY AKKASKWTGG NEIQ // ID A0A0R2HZT0_9LACO Unreviewed; 426 AA. AC A0A0R2HZT0; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=IV45_GL000832 {ECO:0000313|EMBL:KRN58386.1}; OS Lactobacillus secaliphilus. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; OC Lactobacillus. OX NCBI_TaxID=396268 {ECO:0000313|EMBL:KRN58386.1, ECO:0000313|Proteomes:UP000050934}; RN [1] {ECO:0000313|EMBL:KRN58386.1, ECO:0000313|Proteomes:UP000050934} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 17896 {ECO:0000313|EMBL:KRN58386.1, RC ECO:0000313|Proteomes:UP000050934}; RX PubMed=26415554; DOI=10.1038/ncomms9322; RA Sun Z., Harris H.M., McCann A., Guo C., Argimon S., Zhang W., Yang X., RA Jeffery I.B., Cooney J.C., Kagawa T.F., Liu W., Song Y., Salvetti E., RA Wrobel A., Rasinkangas P., Parkhill J., Rea M.C., O'Sullivan O., RA Ritari J., Douillard F.P., Paul Ross R., Yang R., Briner A.E., RA Felis G.E., de Vos W.M., Barrangou R., Klaenhammer T.R., RA Caufield P.W., Cui Y., Zhang H., O'Toole P.W.; RT "Expanding the biotechnology potential of lactobacilli through RT comparative genomics of 213 strains and associated genera."; RL Nat. Commun. 6:8322-8322(2015). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KRN58386.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JQBW01000010; KRN58386.1; -; Genomic_DNA. DR RefSeq; WP_057741669.1; NZ_JQBW01000010.1. DR EnsemblBacteria; KRN58386; KRN58386; IV45_GL000832. DR PATRIC; fig|396268.3.peg.844; -. DR Proteomes; UP000050934; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000050934}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000050934}. FT DOMAIN 202 372 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 426 AA; 47928 MW; DDFEE0B602F83093 CRC64; MDNSVPHNEK VLLIGLNTGQ DDYDYSMVEL RKLAKANNME VVGRIDQPLD EPNAATYFGS GKVKQLHDLV QTTGVTTVIA NDELSPSQLK NLTDQIGVRI IDRTALILEI FAQRAKTKEA KLQVQIAQLQ YRLPRLHTAS NQVLDQQTGA GAGFANRGSG ETQIELDRRV IQRQISHLRQ ELKNVQRSEQ VKRSQRDKSS IPTAALVGYT NAGKSTIMNE LLSRFGLVKD KQVFTKDMLF ATLDTSVRQL TLPDQKRFLL SDTVGFVSKL PTHLIEAFKS TLQEAAKADL LVQVIDYSDP HRDEMIKTTE RTLSEIGIEN IPMIYVFNKA DKVDETDYPT MEGDSRVIIS AKNPESIDFL AKTIKNKLFS DYVQADLLVP FADGQVVSYL NEHTNILDTD YQTDGTRLKV ELSPEDLQRL SKYEVQ // ID A0A0R2IQ44_9LACO Unreviewed; 425 AA. AC A0A0R2IQ44; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=IV80_GL000801 {ECO:0000313|EMBL:KRN67265.1}; OS Pediococcus cellicola. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; OC Pediococcus. OX NCBI_TaxID=319652 {ECO:0000313|EMBL:KRN67265.1, ECO:0000313|Proteomes:UP000051568}; RN [1] {ECO:0000313|EMBL:KRN67265.1, ECO:0000313|Proteomes:UP000051568} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 17757 {ECO:0000313|EMBL:KRN67265.1, RC ECO:0000313|Proteomes:UP000051568}; RX PubMed=26415554; DOI=10.1038/ncomms9322; RA Sun Z., Harris H.M., McCann A., Guo C., Argimon S., Zhang W., Yang X., RA Jeffery I.B., Cooney J.C., Kagawa T.F., Liu W., Song Y., Salvetti E., RA Wrobel A., Rasinkangas P., Parkhill J., Rea M.C., O'Sullivan O., RA Ritari J., Douillard F.P., Paul Ross R., Yang R., Briner A.E., RA Felis G.E., de Vos W.M., Barrangou R., Klaenhammer T.R., RA Caufield P.W., Cui Y., Zhang H., O'Toole P.W.; RT "Expanding the biotechnology potential of lactobacilli through RT comparative genomics of 213 strains and associated genera."; RL Nat. Commun. 6:8322-8322(2015). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KRN67265.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JQBR01000002; KRN67265.1; -; Genomic_DNA. DR RefSeq; WP_057749028.1; NZ_JQBR01000002.1. DR EnsemblBacteria; KRN67265; KRN67265; IV80_GL000801. DR PATRIC; fig|319652.3.peg.810; -. DR Proteomes; UP000051568; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000051568}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000051568}. FT DOMAIN 198 367 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 157 184 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 425 AA; 47691 MW; F1F46D41A86FDC40 CRC64; MTEKVIIAGL ELPNQDLDYA MQELAALVEA NNMEATEKVI QKLDRPNPAT YFGSGKVTEL HELGTSIDVH TLVVNAELSP SQIRNLEQES KLSVIDRTGL ILEIFANRPQ SREAKLQVEI AKLNYQMPRL RTSSSQRLDQ QSAGDAGGGY TNRGAGETKL EMNRRTIQQR INNLNHELKE MTTSSAVQRK KRDQTGIPSV ALVGYTNAGK STTMNGLVHL YGKDDDKQVF EKNMLFATLD TSVRQLTFPD QKQLLLSDTV GFVSNLPHQL IKAFRSTLAE AAQADLLVQV VDVSDPHFRE MIQTTNDTLR EIGVTKVPMI VAFNKADLAG VDYPTFEGNE EITYSARDKK SLLMLTNMIK QKVFTGYREA TFLIPFSEGQ IIDYLNQHTN VLKTAYQENG TEITAELSSE DYQRYQKYLV TEVEN // ID A0A0R2JLX5_9LACT Unreviewed; 427 AA. AC A0A0R2JLX5; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=IV73_GL000564 {ECO:0000313|EMBL:KRN75399.1}; OS Weissella kandleri. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Leuconostocaceae; OC Weissella. OX NCBI_TaxID=1616 {ECO:0000313|EMBL:KRN75399.1, ECO:0000313|Proteomes:UP000051655}; RN [1] {ECO:0000313|EMBL:KRN75399.1, ECO:0000313|Proteomes:UP000051655} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 20593 {ECO:0000313|EMBL:KRN75399.1, RC ECO:0000313|Proteomes:UP000051655}; RX PubMed=26415554; DOI=10.1038/ncomms9322; RA Sun Z., Harris H.M., McCann A., Guo C., Argimon S., Zhang W., Yang X., RA Jeffery I.B., Cooney J.C., Kagawa T.F., Liu W., Song Y., Salvetti E., RA Wrobel A., Rasinkangas P., Parkhill J., Rea M.C., O'Sullivan O., RA Ritari J., Douillard F.P., Paul Ross R., Yang R., Briner A.E., RA Felis G.E., de Vos W.M., Barrangou R., Klaenhammer T.R., RA Caufield P.W., Cui Y., Zhang H., O'Toole P.W.; RT "Expanding the biotechnology potential of lactobacilli through RT comparative genomics of 213 strains and associated genera."; RL Nat. Commun. 6:8322-8322(2015). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KRN75399.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JQBP01000002; KRN75399.1; -; Genomic_DNA. DR RefSeq; WP_057754457.1; NZ_JQBP01000002.1. DR EnsemblBacteria; KRN75399; KRN75399; IV73_GL000564. DR PATRIC; fig|1616.3.peg.580; -. DR Proteomes; UP000051655; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000051655}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}. FT DOMAIN 204 373 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 427 AA; 47603 MW; F7C9BC3A0AB91E8F CRC64; MHENDDTPQV PVLLVGLDQG VSQFDYQMEE LANLAQANQM QVVGTLTQKL DRPVAATYFG KGKVDELRVA VEANEAEMVV VNDELSPSQI RNLENVTGVR IIDRTALILD IFASRAKTRL AKLQVEMAQL QYQLPRLRTS LNIRLDQQTG GGGGSFTTRG SGETKLETSR RLVEHQIAGI KKEIAEIDMD DQNRRKHRDE LLMPTVALVG YTNAGKSTIM NQLVERFGAN QSKTVFQADM LFATLETSVR KIFLPENQTI LLSDTVGFVS KLPHQLVAAF RATLAEAAQA DLLLQIVDFS DPNYQAMMDT TKHTLAEIGV KDIPMVTIYN KADRLENVQY PEAAGDGIVL SAQDATSIDY LVEVLQQKLF ADLKTYQLLV PFDQGQVVAK LNEDAIVLAT EYEPDGTLLQ VRLRSEQLPR YAKYLFE // ID A0A0R2JNA0_9LACO Unreviewed; 375 AA. AC A0A0R2JNA0; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 05-JUL-2017, entry version 12. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=IV52_GL000932 {ECO:0000313|EMBL:KRN78656.1}; OS Lactobacillus lindneri DSM 20690 = JCM 11027. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; OC Lactobacillus. OX NCBI_TaxID=1122148 {ECO:0000313|EMBL:KRN78656.1, ECO:0000313|Proteomes:UP000051565}; RN [1] {ECO:0000313|EMBL:KRN78656.1, ECO:0000313|Proteomes:UP000051565} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 20690 {ECO:0000313|EMBL:KRN78656.1, RC ECO:0000313|Proteomes:UP000051565}; RX PubMed=26415554; DOI=10.1038/ncomms9322; RA Sun Z., Harris H.M., McCann A., Guo C., Argimon S., Zhang W., Yang X., RA Jeffery I.B., Cooney J.C., Kagawa T.F., Liu W., Song Y., Salvetti E., RA Wrobel A., Rasinkangas P., Parkhill J., Rea M.C., O'Sullivan O., RA Ritari J., Douillard F.P., Paul Ross R., Yang R., Briner A.E., RA Felis G.E., de Vos W.M., Barrangou R., Klaenhammer T.R., RA Caufield P.W., Cui Y., Zhang H., O'Toole P.W.; RT "Expanding the biotechnology potential of lactobacilli through RT comparative genomics of 213 strains and associated genera."; RL Nat. Commun. 6:8322-8322(2015). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KRN78656.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JQBT01000033; KRN78656.1; -; Genomic_DNA. DR EnsemblBacteria; KRN78656; KRN78656; IV52_GL000932. DR PATRIC; fig|1122148.6.peg.956; -. DR Proteomes; UP000051565; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000051565}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000051565}. SQ SEQUENCE 375 AA; 42008 MW; 70473A13E42A1EFA CRC64; MENKPTPVIT IGLNVNNSHF DYSMEELQNL AAANHMESIE TVVQKLDHPD AGTYFGKGKI EFLAQLIQTT AADTIIANDE LSPSQIRNIE KQTNATVIDR TGLILEIFAN RAQTSEAKLQ VQMAKLKYQL PRLRTSASQR LDQQSAGGGL ANRGSGETKI ELSRRNIEHQ IDHVRRELKE IDKSHQTQSK RRKESDIKTV ALVGYTNAGK STIMNQLVKR FGENEDKRVM VKNMLFATLD TSVRDIKMAD NKHFLLSDTV GFVSDLPHQL IQAFKSTLAE AANADLLIQV VDYSDENQEL MMQTTEKTLK EIGVPNLPMI KVFNKADLAG ASFPNREGNN LIISALDSHS IDLLISVILE KLFQRLCNQN LFNSF // ID A0A0R2KPL0_9LACO Unreviewed; 416 AA. AC A0A0R2KPL0; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=IV53_GL000323 {ECO:0000313|EMBL:KRN88359.1}; OS Lactobacillus ceti DSM 22408. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; OC Lactobacillus. OX NCBI_TaxID=1122146 {ECO:0000313|EMBL:KRN88359.1, ECO:0000313|Proteomes:UP000051500}; RN [1] {ECO:0000313|EMBL:KRN88359.1, ECO:0000313|Proteomes:UP000051500} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 22408 {ECO:0000313|EMBL:KRN88359.1, RC ECO:0000313|Proteomes:UP000051500}; RX PubMed=26415554; DOI=10.1038/ncomms9322; RA Sun Z., Harris H.M., McCann A., Guo C., Argimon S., Zhang W., Yang X., RA Jeffery I.B., Cooney J.C., Kagawa T.F., Liu W., Song Y., Salvetti E., RA Wrobel A., Rasinkangas P., Parkhill J., Rea M.C., O'Sullivan O., RA Ritari J., Douillard F.P., Paul Ross R., Yang R., Briner A.E., RA Felis G.E., de Vos W.M., Barrangou R., Klaenhammer T.R., RA Caufield P.W., Cui Y., Zhang H., O'Toole P.W.; RT "Expanding the biotechnology potential of lactobacilli through RT comparative genomics of 213 strains and associated genera."; RL Nat. Commun. 6:8322-8322(2015). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KRN88359.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JQBZ01000025; KRN88359.1; -; Genomic_DNA. DR RefSeq; WP_027106338.1; NZ_JQBZ01000025.1. DR EnsemblBacteria; KRN88359; KRN88359; IV53_GL000323. DR PATRIC; fig|1122146.4.peg.334; -. DR Proteomes; UP000051500; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000051500}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000051500}. FT DOMAIN 194 362 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 160 187 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 416 AA; 46653 MW; 0D7AA802CCD293BB CRC64; MTPVIIAGIE TPHNDFTYTM EELTNLVEAN HMIAEKQVSQ KLDHPLAGSY FGSGKADEIK RLAETYDIDF LIINDELTPT QIRNLERLTN LTIIDRTALI LDIFAQRAQS KEAKLQVEIA KLQYQLPRLH TSGVEKLDQQ SAGGGMANRG AGEKKIELNR RVIEKKITRA RKELKAIAKE KETQRKARDK SGLKTVALVG YTNAGKSTTM NGLLKLTNAD EHKKVFEKDM LFATLDTSVR KLKFSDNKEI LLSDTVGFVS MLPHQLVAAF KTTLAEAAQA DLLIQVVDSS DPNAKEMIAT TNKTLQEIGV TDVPMIYAFN KADETLVNYP VITGDEITYS AKDLISLQAL SDFIKEQLFR DYQTLTYLIP FNQGHFLEDL NQNAHILKTE YVEQGTLITA NVAPELARKL HKFLQK // ID A0A0R2L3Y1_9LACO Unreviewed; 427 AA. AC A0A0R2L3Y1; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=IV55_GL001312 {ECO:0000313|EMBL:KRN96350.1}; OS Lactobacillus siliginis. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; OC Lactobacillus. OX NCBI_TaxID=348151 {ECO:0000313|EMBL:KRN96350.1, ECO:0000313|Proteomes:UP000051139}; RN [1] {ECO:0000313|EMBL:KRN96350.1, ECO:0000313|Proteomes:UP000051139} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 22696 {ECO:0000313|EMBL:KRN96350.1, RC ECO:0000313|Proteomes:UP000051139}; RX PubMed=26415554; DOI=10.1038/ncomms9322; RA Sun Z., Harris H.M., McCann A., Guo C., Argimon S., Zhang W., Yang X., RA Jeffery I.B., Cooney J.C., Kagawa T.F., Liu W., Song Y., Salvetti E., RA Wrobel A., Rasinkangas P., Parkhill J., Rea M.C., O'Sullivan O., RA Ritari J., Douillard F.P., Paul Ross R., Yang R., Briner A.E., RA Felis G.E., de Vos W.M., Barrangou R., Klaenhammer T.R., RA Caufield P.W., Cui Y., Zhang H., O'Toole P.W.; RT "Expanding the biotechnology potential of lactobacilli through RT comparative genomics of 213 strains and associated genera."; RL Nat. Commun. 6:8322-8322(2015). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KRN96350.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JQCB01000004; KRN96350.1; -; Genomic_DNA. DR RefSeq; WP_057809526.1; NZ_JQCB01000004.1. DR EnsemblBacteria; KRN96350; KRN96350; IV55_GL001312. DR PATRIC; fig|348151.3.peg.1349; -. DR Proteomes; UP000051139; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000051139}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000051139}. FT DOMAIN 205 373 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 164 191 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 427 AA; 47359 MW; B96F565B8CC56BDD CRC64; MNVAETAIAP KEVIIAGLNT GDHSFEYSMT ELANLVAANN MVVKEEIRQS LERPHPGTYF GKGKVAELSE IVASENLTTI VTNDELTSSQ IRNIETITKA TVLDRTALIL DIFANRAQTR EAKLQVQIAQ LQYQLPRLHT SVNQRLDQQT GAGGGSFTNR GAGESQLEMD RRTIKNHIKH LQEELADITK ASETQRVQRE KNGLPTVALV GYTNAGKSTT MNGLVRKYGS SDEKQVFEKN MLFATLDTSV RQITLPDQKQ FLLSDTVGFV SKLPHNLVKA FQSTLAEAAN ADLLIQVVDY ADDNSDAMMA TTNETLASIG VADIPMIVAF NKADMTDAKY PVREGKQLVY SARDDTSLEE LITMIREEVF QNYQTVTLLI PFDKGNILNF LNEKAHILST DYVAEGTKIT VELTDESAQR FSEYRVD // ID A0A0R2LCJ5_9LACO Unreviewed; 430 AA. AC A0A0R2LCJ5; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 07-JUN-2017, entry version 10. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=IV66_GL000624 {ECO:0000313|EMBL:KRN96762.1}; OS Lactobacillus pobuzihii. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; OC Lactobacillus. OX NCBI_TaxID=449659 {ECO:0000313|EMBL:KRN96762.1, ECO:0000313|Proteomes:UP000051886}; RN [1] {ECO:0000313|EMBL:KRN96762.1, ECO:0000313|Proteomes:UP000051886} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NBRC 103219 {ECO:0000313|EMBL:KRN96762.1, RC ECO:0000313|Proteomes:UP000051886}; RX PubMed=26415554; DOI=10.1038/ncomms9322; RA Sun Z., Harris H.M., McCann A., Guo C., Argimon S., Zhang W., Yang X., RA Jeffery I.B., Cooney J.C., Kagawa T.F., Liu W., Song Y., Salvetti E., RA Wrobel A., Rasinkangas P., Parkhill J., Rea M.C., O'Sullivan O., RA Ritari J., Douillard F.P., Paul Ross R., Yang R., Briner A.E., RA Felis G.E., de Vos W.M., Barrangou R., Klaenhammer T.R., RA Caufield P.W., Cui Y., Zhang H., O'Toole P.W.; RT "Expanding the biotechnology potential of lactobacilli through RT comparative genomics of 213 strains and associated genera."; RL Nat. Commun. 6:8322-8322(2015). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KRN96762.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JQCN01000064; KRN96762.1; -; Genomic_DNA. DR EnsemblBacteria; KRN96762; KRN96762; IV66_GL000624. DR PATRIC; fig|449659.4.peg.629; -. DR Proteomes; UP000051886; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000051886}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000051886}. FT DOMAIN 206 375 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 172 202 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 430 AA; 47856 MW; 93F2B82343603FC8 CRC64; MFMKMNGGKN MDGAILAGID SGQENFEYTM NELAALTQAA TIKPELTITQ KLDKPVSATY FGSGKLNEIK NAATAKSAID LIINDELTPT QLRNIEDQTN LTVIDRTALI LEIFARRAHT REAKLQVQIA SLQYRLPRLR TSSLNRFDQQ TAGSGGGFTS RGSGETQMEL NRRTIQNQIN HLRHQLKEVE QEEQTKRKAR DRSNLKTVAL VGYTNAGKST TMNGLLRLTG QDEEKQVFEK NMLFATLDTS VRKIQFADNK QILLSDTVGF VSSLPHQLVE AFKTTLSEAA QADLLIQVID ASDPHAKEMV KTTEKTLREI GVTGIPMIYA FNKADLEPQL SYPQIAGDQI TFSAQDDESL KLLIKMIKKT LFADFETKTY LIPFDEGKYL EQLNSNASIL NTDYLAKGTL ITAEVSPATA GILQKFEYSN // ID A0A0R2LS70_9LACO Unreviewed; 428 AA. AC A0A0R2LS70; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 30-AUG-2017, entry version 15. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=IV54_GL000475 {ECO:0000313|EMBL:KRO01258.1}; OS Lactobacillus paucivorans. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; OC Lactobacillus. OX NCBI_TaxID=616990 {ECO:0000313|EMBL:KRO01258.1, ECO:0000313|Proteomes:UP000051906}; RN [1] {ECO:0000313|EMBL:KRO01258.1, ECO:0000313|Proteomes:UP000051906} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 22467 {ECO:0000313|EMBL:KRO01258.1, RC ECO:0000313|Proteomes:UP000051906}; RX PubMed=26415554; DOI=10.1038/ncomms9322; RA Sun Z., Harris H.M., McCann A., Guo C., Argimon S., Zhang W., Yang X., RA Jeffery I.B., Cooney J.C., Kagawa T.F., Liu W., Song Y., Salvetti E., RA Wrobel A., Rasinkangas P., Parkhill J., Rea M.C., O'Sullivan O., RA Ritari J., Douillard F.P., Paul Ross R., Yang R., Briner A.E., RA Felis G.E., de Vos W.M., Barrangou R., Klaenhammer T.R., RA Caufield P.W., Cui Y., Zhang H., O'Toole P.W.; RT "Expanding the biotechnology potential of lactobacilli through RT comparative genomics of 213 strains and associated genera."; RL Nat. Commun. 6:8322-8322(2015). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KRO01258.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JQCA01000115; KRO01258.1; -; Genomic_DNA. DR RefSeq; WP_057878982.1; NZ_JQCA01000115.1. DR EnsemblBacteria; KRO01258; KRO01258; IV54_GL000475. DR PATRIC; fig|616990.3.peg.511; -. DR Proteomes; UP000051906; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000051906}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000051906}. FT DOMAIN 202 370 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 428 AA; 47451 MW; 53E87418302D7837 CRC64; MEETPRTPVI TIGLNAGQAT FDYSMTELKN LVEANNMTVV EEIQQSLTKP NPGTYFGTGK VEELAEIVAD DEVNIVIVND ELTPSQIRNL ENGTKARIID RTGLILEIFA NRAQSREAKL QVQLAMLQYQ LPRLHTSASQ RLDQQTGSGG GGGFTNRGSG ESQTEMSRRT IQRSINHVNH ELKEINQAAA TQRQQRERNQ LPSVALVGYT NAGKSTLMNA LVRKFGKNED KQVFVKDMLF ATLDTSVRQL VFPDQKKMLL SDTVGFVSQL PTQLVKAFRS TLAEAANADL LIQVVDYADA NKESMMATTE KTLTDIGVTD VPMITVFNKA DLTEATYPTR AGDQLVLSAL DDASLDLLVQ AIKEKVFHNY VTANFLIPFS EGEVVSYLNE HAHVLSTDYV EDGTAIKVEL QQADFDRFKK FVVTEEHS // ID A0A0R2MAL7_9LACO Unreviewed; 431 AA. AC A0A0R2MAL7; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 07-JUN-2017, entry version 13. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=IV64_GL000118 {ECO:0000313|EMBL:KRO08994.1}; OS Lactobacillus xiangfangensis. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; OC Lactobacillus. OX NCBI_TaxID=942150 {ECO:0000313|EMBL:KRO08994.1, ECO:0000313|Proteomes:UP000051783}; RN [1] {ECO:0000313|EMBL:KRO08994.1, ECO:0000313|Proteomes:UP000051783} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=LMG 26013 {ECO:0000313|EMBL:KRO08994.1, RC ECO:0000313|Proteomes:UP000051783}; RX PubMed=26415554; DOI=10.1038/ncomms9322; RA Sun Z., Harris H.M., McCann A., Guo C., Argimon S., Zhang W., Yang X., RA Jeffery I.B., Cooney J.C., Kagawa T.F., Liu W., Song Y., Salvetti E., RA Wrobel A., Rasinkangas P., Parkhill J., Rea M.C., O'Sullivan O., RA Ritari J., Douillard F.P., Paul Ross R., Yang R., Briner A.E., RA Felis G.E., de Vos W.M., Barrangou R., Klaenhammer T.R., RA Caufield P.W., Cui Y., Zhang H., O'Toole P.W.; RT "Expanding the biotechnology potential of lactobacilli through RT comparative genomics of 213 strains and associated genera."; RL Nat. Commun. 6:8322-8322(2015). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KRO08994.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JQCL01000074; KRO08994.1; -; Genomic_DNA. DR RefSeq; WP_057706737.1; NZ_JQCL01000074.1. DR EnsemblBacteria; KRO08994; KRO08994; IV64_GL000118. DR PATRIC; fig|942150.3.peg.125; -. DR Proteomes; UP000051783; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000051783}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}. FT DOMAIN 207 375 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 431 AA; 47917 MW; 8F07BCA0441C6F79 CRC64; MSETNVNQVQ EVIIAGMSKT VSNYDYAMSE LEALVEANNM HAALRIDQGL DKPNSATYFG KGKVVEIKED AEAHDLHIMV INADLTPSQV RNLEEQTGLQ IIDRTGLILE IFGTRARSKE ANLQVKIAQL QYQLPRLRTS ISNRLDQQAG AAAGGGGGFT NRGSGETQLE LNRRTIQDRI SHAKHELKEL NKDEEVRRSQ RDKAGLPNVA LVGYTNAGKS TTMNGLVRLF GKGEDKQVFE KDMLFATLDT SIRQLTFPDN KQLLLSDTVG FVSNLPHNLI NAFRSTLAEA ANADLLIQVI DYADPHYKEM MATTDKTLKE IGVTDIPMIY AYNKADLTEA NYPNQQDDQL IYAAKDEKSL QVLTQMMKDK VFKGYVTTTL LIPFSDGDVV AYLNDNANIL KTDYVADGTQ LEVELNSVDA QRYEKYVVTP A // ID A0A0R2MUQ8_9LACO Unreviewed; 422 AA. AC A0A0R2MUQ8; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=IV56_GL000471 {ECO:0000313|EMBL:KRO17145.1}; OS Lactobacillus saniviri JCM 17471 = DSM 24301. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; OC Lactobacillus. OX NCBI_TaxID=1293598 {ECO:0000313|EMBL:KRO17145.1, ECO:0000313|Proteomes:UP000050969}; RN [1] {ECO:0000313|EMBL:KRO17145.1, ECO:0000313|Proteomes:UP000050969} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 24301 {ECO:0000313|EMBL:KRO17145.1, RC ECO:0000313|Proteomes:UP000050969}; RX PubMed=26415554; DOI=10.1038/ncomms9322; RA Sun Z., Harris H.M., McCann A., Guo C., Argimon S., Zhang W., Yang X., RA Jeffery I.B., Cooney J.C., Kagawa T.F., Liu W., Song Y., Salvetti E., RA Wrobel A., Rasinkangas P., Parkhill J., Rea M.C., O'Sullivan O., RA Ritari J., Douillard F.P., Paul Ross R., Yang R., Briner A.E., RA Felis G.E., de Vos W.M., Barrangou R., Klaenhammer T.R., RA Caufield P.W., Cui Y., Zhang H., O'Toole P.W.; RT "Expanding the biotechnology potential of lactobacilli through RT comparative genomics of 213 strains and associated genera."; RL Nat. Commun. 6:8322-8322(2015). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KRO17145.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JQCE01000021; KRO17145.1; -; Genomic_DNA. DR RefSeq; WP_056992738.1; NZ_JQCE01000021.1. DR EnsemblBacteria; KRO17145; KRO17145; IV56_GL000471. DR PATRIC; fig|1293598.4.peg.504; -. DR Proteomes; UP000050969; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000050969}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Hydrolase {ECO:0000313|EMBL:KRO17145.1}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Protease {ECO:0000313|EMBL:KRO17145.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000050969}. FT DOMAIN 197 367 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 422 AA; 47287 MW; F789889B3ADA9815 CRC64; MPENNEKVLI TGISKQQPDF DYTMTELGEL AKANNYTVVG EMRQNVDRQT AATYFGSGKV DEIRQEADIL EATTVLVNDE LSPSQLRNLE KQLGRRVVDR TQLILDIFAD RARSKTAKTQ VEIAQLKYAL PRLHPSANRL DQQGGGGGFA NRGAGETQLE MDRRILTKRI AHLRQDLRDA DVGEEVRRAK RQTNQLPVVA LVGYTNAGKS TTMNGLLDLY ADRPEDKQVF EKDMLFATLD TSVRALTLPD NRQFLLSDTV GFVSKLPHNL IDSFKATLAE AANADLLIQV VDYADPNYRE MMAITEKTLK EIGIENIPMI EAYNKADKRE DTTYPEINGH QLVYSAKDPK SLKALTEMIT QLIFAEDQEK TYLVPFTDGQ IVSFINEKTA VKATDYTETG TKITTIVNAV QAGQLEKYEV TE // ID A0A0R2NJA9_9LACO Unreviewed; 422 AA. AC A0A0R2NJA9; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=IV88_GL001397 {ECO:0000313|EMBL:KRO25862.1}; OS Pediococcus argentinicus. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; OC Pediococcus. OX NCBI_TaxID=480391 {ECO:0000313|EMBL:KRO25862.1, ECO:0000313|Proteomes:UP000051249}; RN [1] {ECO:0000313|EMBL:KRO25862.1, ECO:0000313|Proteomes:UP000051249} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 23026 {ECO:0000313|EMBL:KRO25862.1, RC ECO:0000313|Proteomes:UP000051249}; RX PubMed=26415554; DOI=10.1038/ncomms9322; RA Sun Z., Harris H.M., McCann A., Guo C., Argimon S., Zhang W., Yang X., RA Jeffery I.B., Cooney J.C., Kagawa T.F., Liu W., Song Y., Salvetti E., RA Wrobel A., Rasinkangas P., Parkhill J., Rea M.C., O'Sullivan O., RA Ritari J., Douillard F.P., Paul Ross R., Yang R., Briner A.E., RA Felis G.E., de Vos W.M., Barrangou R., Klaenhammer T.R., RA Caufield P.W., Cui Y., Zhang H., O'Toole P.W.; RT "Expanding the biotechnology potential of lactobacilli through RT comparative genomics of 213 strains and associated genera."; RL Nat. Commun. 6:8322-8322(2015). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KRO25862.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JQCQ01000005; KRO25862.1; -; Genomic_DNA. DR RefSeq; WP_057798218.1; NZ_JQCQ01000005.1. DR EnsemblBacteria; KRO25862; KRO25862; IV88_GL001397. DR PATRIC; fig|480391.4.peg.1421; -. DR Proteomes; UP000051249; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000051249}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000051249}. FT DOMAIN 196 364 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 422 AA; 47141 MW; 14A42E36742A46A2 CRC64; METEQILIAG LELPGVDLEY NMDELASLVA ANNMEVVDTL TQKLEKPNAG TYFGKGKVQE LAEMATAHDV STVVLSAEVT PSQLTNLEKE TGLHLIDRTG LILEIFANRA RSKEAKLQVE LAKSQYQLAR LRTSSSQRLD QQSAGGGYTN RGTGETKLEL NRRTVRDKIT RINRELKEMS TAADVQRKQR DARDIPSVAL VGYTNTGKST TMNGLVRMFG RSDEKQVFEK DMLFATLDTS VRKLTFADQK ELILSDTVGF VSDLPHQLVK AFRSTLAEAA KADLLVQVID ISDPHYREMM ETTEKTLSEI GVTDIPMIYA FNKADRAEIA YPTLDGKEIT YSAKQLQSLE LLTSLIKKQV FNNYVEATFL IPFAEGQVVD FLNGNANVKE TTYTENGTVI TAELKDKDYN RLERYVQTPK AK // ID A0A0R2PBG5_9ACTN Unreviewed; 401 AA. AC A0A0R2PBG5; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 12-APR-2017, entry version 7. DE SubName: Full=ATP-binding protein {ECO:0000313|EMBL:KRO35292.1}; DE Flags: Fragment; GN ORFNames=ABR54_04810 {ECO:0000313|EMBL:KRO35292.1}; OS Actinobacteria bacterium BACL15 MAG-120619-bin91. OC Bacteria; Actinobacteria; ac1 cluster. OX NCBI_TaxID=1655562 {ECO:0000313|EMBL:KRO35292.1, ECO:0000313|Proteomes:UP000053274}; RN [1] {ECO:0000313|EMBL:KRO35292.1, ECO:0000313|Proteomes:UP000053274} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BACL15 MAG-120619-bin91 {ECO:0000313|EMBL:KRO35292.1}; RA Hugerth L.W., Larsson J., Alneberg J., Lindh M.V., Legrand C., RA Pinhassi J., Andersson A.; RT "Metagenome-Assembled Genomes uncover a global brackish microbiome."; RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KRO35292.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LIAM01000133; KRO35292.1; -; Genomic_DNA. DR Proteomes; UP000053274; Unassembled WGS sequence. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000313|EMBL:KRO35292.1}; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000053274}; KW Nucleotide-binding {ECO:0000313|EMBL:KRO35292.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000053274}. FT DOMAIN 177 342 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 136 170 {ECO:0000256|SAM:Coils}. FT NON_TER 1 1 {ECO:0000313|EMBL:KRO35292.1}. SQ SEQUENCE 401 AA; 43964 MW; D27AE94C42897114 CRC64; ELKALAETAG SEVLEGLIQR RDKPDPATYI GSGKVIELKQ VVMSTGADTV VCDGELSPSQ LRQLEDKLKV KVVDRTALIL DIFAQHAKSK EGKAQVELAQ IAYLLPRLRG WGDSLSRQVG GRAAGGAGIG GRGPGETKIE TDRRRIRDKM AKLRREIAEM KVSRDTKRQE RRRFNIPSVA IAGYTNAGKS SLLNKLTDAG VLVENALFAT LDPTVRKTQT SDGRVYTLSD TVGFVRHLPH QLIDAFKSTL EEVSESDLIV HVVDGSHPDP FEQIRAVRLV IDEIGGKDIP EIIAINKVDI ADPHVIMEIL RKEPNSYAFS VRTGFGIEGL LHAIENSLPR PSVEINVVIP YDRGDLVHAI HERGEIFSEQ YIAEGTSIHA RVDGGLAQKI EKSQGSEKSP Q // ID A0A0R2QPH3_9ACTN Unreviewed; 445 AA. AC A0A0R2QPH3; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 12-APR-2017, entry version 8. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=ABR78_09430 {ECO:0000313|EMBL:KRO52087.1}; OS Acidimicrobiia bacterium BACL6 MAG-120910-bin40. OC Bacteria; Actinobacteria; Acidimicrobiia. OX NCBI_TaxID=1655586 {ECO:0000313|EMBL:KRO52087.1, ECO:0000313|Proteomes:UP000050903}; RN [1] {ECO:0000313|EMBL:KRO52087.1, ECO:0000313|Proteomes:UP000050903} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BACL6 MAG-120910-bin40 {ECO:0000313|EMBL:KRO52087.1}; RA Hugerth L.W., Larsson J., Alneberg J., Lindh M.V., Legrand C., RA Pinhassi J., Andersson A.; RT "Metagenome-Assembled Genomes uncover a global brackish microbiome."; RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KRO52087.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LIBI01000144; KRO52087.1; -; Genomic_DNA. DR Proteomes; UP000050903; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000050903}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000050903}. FT DOMAIN 213 377 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 445 AA; 47966 MW; 2C1215A0F0429CBD CRC64; MSNPYQQALG RTLIDRTIRE RIVLVGVIFD GHDESETEES LDELAQLIDT AGAVEVARMT QRRDAPDSTY FIGKGKAQEL KELCLAVDSD TVVFDNELTP GQQYNLEKLL GRTAIDRTAV ILDIFAQNAH TLEGKAQVEL ALLRYKLPRL RRGISEAMSQ QGAGIGSRGP GETKLEVDRR RIQDKIAKLS RDLVDLANNR REQAKGRSRS GLGAVAIVGY TNAGKSTLLN HLTDAGVLVE NRLFATLDPT TRRLALPGGE PVLVSDTVGF VRRLPHGLVE SFKSTLEVAV LGDLLIHVVD STAVDPAGQI LAVREVLTDI GAGEVPELLV FNKADMASDV AAQLVASHPG SVAISAVTGT GIDDLLRTIG DRMRAISVVV ELLIPYDRGD IVASVHREGE VVSTANEENG MRIRARLGDA STGRLSQFVV DQSGDQADDR TVVAS // ID A0A0R2RZG0_9FLAO Unreviewed; 402 AA. AC A0A0R2RZG0; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 12-APR-2017, entry version 8. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=ABR84_04035 {ECO:0000313|EMBL:KRO67897.1}; OS Cryomorphaceae bacterium BACL21 MAG-121220-bin10. OC Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales; OC Cryomorphaceae; unclassified Cryomorphaceae. OX NCBI_TaxID=1655592 {ECO:0000313|EMBL:KRO67897.1, ECO:0000313|Proteomes:UP000051758}; RN [1] {ECO:0000313|EMBL:KRO67897.1, ECO:0000313|Proteomes:UP000051758} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BACL21 MAG-121220-bin10 {ECO:0000313|EMBL:KRO67897.1}; RA Hugerth L.W., Larsson J., Alneberg J., Lindh M.V., Legrand C., RA Pinhassi J., Andersson A.; RT "Metagenome-Assembled Genomes uncover a global brackish microbiome."; RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KRO67897.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LICC01000002; KRO67897.1; -; Genomic_DNA. DR Proteomes; UP000051758; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000051758}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000051758}. FT DOMAIN 200 385 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 402 AA; 45865 MW; 4B683E7849F3CF0F CRC64; MLERQNTDYE KVVLIGVVTR LQDEDKAAEY LDELEFLAFT AGGTVEKRFT QKLDVPHPKT FIGTGKLQEV LAFVEAQEIG TAIFDDELSP AQQKNIQKIL NCKVIDRTNL ILDIFAQRAT TSYARTQVEL AQYEYLLPRL SGMWTHLERQ RGGIGMRGPG ETEIETDRRI VRDRIALLKK KIITIDRQMS VQRGNRGSLV RIALVGYTNV GKSTLMNVIS KSDVFAENKL FATLDTTVRK VVIGNLPFLL SDTVGFIRKL PTQLVDSFKS TLDEVREADL LLHVVDISHP SFEDHIASVD QILDEIGGKG KPVLMVFNKI DAYTPEVIDP EDLVTEKTEA HYTLEDWTRT WMSRSNGDAV FISAIEKDNI ETFRKVVYDR VRNIHVTRFP YNHFLYPEEI QE // ID A0A0R2S5U9_9FLAO Unreviewed; 390 AA. AC A0A0R2S5U9; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 12-APR-2017, entry version 8. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=ABR83_07195 {ECO:0000313|EMBL:KRO70086.1}; OS Cryomorphaceae bacterium BACL18 MAG-120924-bin36. OC Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales; OC Cryomorphaceae; unclassified Cryomorphaceae. OX NCBI_TaxID=1655591 {ECO:0000313|EMBL:KRO70086.1, ECO:0000313|Proteomes:UP000051105}; RN [1] {ECO:0000313|EMBL:KRO70086.1, ECO:0000313|Proteomes:UP000051105} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BACL18 MAG-120924-bin36 {ECO:0000313|EMBL:KRO70086.1}; RA Hugerth L.W., Larsson J., Alneberg J., Lindh M.V., Legrand C., RA Pinhassi J., Andersson A.; RT "Metagenome-Assembled Genomes uncover a global brackish microbiome."; RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KRO70086.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LIBP01000373; KRO70086.1; -; Genomic_DNA. DR Proteomes; UP000051105; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000051105}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000051105}. FT DOMAIN 201 379 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 390 AA; 44193 MW; D9E38378EBD64C86 CRC64; MIDRRPRQGP ERCVLVGAVT RLQDETKANE YLDELRFLAE TAGAETVAVF SQKLDKPDPK LFLGSGKMDE IKAYLDAEEV DLVIFDDELS PSQLKNIERL FECKVMDRTN LILDIFAARA QTSYARTQVE LAQYEYLLPR LTRMWTHLER QKGGIGMRGP GETQIETDRR IIKQKIAHLK EKLSVIDRQM ATQRGNRGAL VRMALIGYTN VGKSTLMNAL SKSEVLAENK LFATLDTTVR KVVVGNLPFL LTDTVGFIRK LPTQLVESFK STLDEVREAD ILLHVVDVAH PNYEDHMESV ASILQELGCQ DTPQIVVFNK IDAWTAPTDD EGRPAGTLDE LKSAWARRTN GQCVFISALH KDQFDALRDM IYRNASTIHA VRFPFDTFLY // ID A0A0R2SI42_9ACTN Unreviewed; 481 AA. AC A0A0R2SI42; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 30-AUG-2017, entry version 17. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=ABS00_01170 {ECO:0000313|EMBL:KRO74452.1}; OS Actinobacteria bacterium BACL2 MAG-120920-bin34. OC Bacteria; Actinobacteria. OX NCBI_TaxID=1655602 {ECO:0000313|EMBL:KRO74452.1, ECO:0000313|Proteomes:UP000051188}; RN [1] {ECO:0000313|EMBL:KRO74452.1, ECO:0000313|Proteomes:UP000051188} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BACL20 MAG-120920-bin34 {ECO:0000313|EMBL:KRO74452.1}; RA Hugerth L.W., Larsson J., Alneberg J., Lindh M.V., Legrand C., RA Pinhassi J., Andersson A.; RT "Metagenome-Assembled Genomes uncover a global brackish microbiome."; RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KRO74452.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LIBS01000013; KRO74452.1; -; Genomic_DNA. DR Proteomes; UP000051188; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000313|EMBL:KRO74452.1}; KW Complete proteome {ECO:0000313|Proteomes:UP000051188}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900, KW ECO:0000313|EMBL:KRO74452.1}. FT DOMAIN 262 427 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 481 AA; 52567 MW; 47EC00822087B9FA CRC64; MAKKKELPEI EELISESQQV AAEFDSEIFI PDSFQSTQQD LSDRQALRRV IGLSTELSDI SEAEYRQLRL ERVILVGVWT EGSVKDAENS MEELAALAET AGSTVLDALI QRRDKPDPAT FIGSGKVSEL KAIVKSTGAD TVVCDGELSP SQLRNLEDKV KVKVVDRTAL ILDIFAQHAK SKEGKAQVEL AQMSYMLPRL RGWGDSLSRQ AGGIGGRGPG ETKIEVDRRR IRDKMSKLRR EIGDMKVARD TKRQERKRNS IPSVAIAGYT NAGKSSLLNR LTNAGVLVQN ALFATLDPTV RRSETSDGRT YTLSDTVGFV KHLPHDLIDA FKSTLEEVSG ADVIVHVVDG SHADPLGQIK AVRGVIADVG GAKIPEIIAL NKADIADPQV IAQVLIQEPD AYLISVHSGV GIEKLIRAIE SSLPRPRIEI RTVLPYDRGD LVSQIHEHGE ILSQEYLPEG TSLHALVDGS LAHALEKYSV N // ID A0A0R2T0M1_9GAMM Unreviewed; 431 AA. AC A0A0R2T0M1; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 30-AUG-2017, entry version 9. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=ABR85_05330 {ECO:0000313|EMBL:KRO78640.1}; OS OM182 bacterium BACL3 MAG-120619-bin3. OC Bacteria; Proteobacteria; Gammaproteobacteria; OMG group; OM182 clade. OX NCBI_TaxID=1655593 {ECO:0000313|EMBL:KRO78640.1, ECO:0000313|Proteomes:UP000051242}; RN [1] {ECO:0000313|EMBL:KRO78640.1, ECO:0000313|Proteomes:UP000051242} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BACL22 MAG-120619-bin3 {ECO:0000313|EMBL:KRO78640.1}; RA Hugerth L.W., Larsson J., Alneberg J., Lindh M.V., Legrand C., RA Pinhassi J., Andersson A.; RT "Metagenome-Assembled Genomes uncover a global brackish microbiome."; RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KRO78640.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LICD01000298; KRO78640.1; -; Genomic_DNA. DR Proteomes; UP000051242; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000051242}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000051242}. FT DOMAIN 199 366 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 431 AA; 48212 MW; 425CC1C6D8C0CEEE CRC64; MFFDRPDSGE ISLLVNLQID NDREADDIVE FEELALSAGA QPVAIITGSR RQPSPSYFVG SGKLEELQAA VASHKAEVVL FNHSLSPSQE RNLERELKCR VIDRTGLILD IFAQRARSYE GKLQVELAQL QHMSSRLKRG WTHLDRQKGG IGMRGAGETQ LEMDQRIIAQ RIKSINKALV KVRTQRDQGR RSRRRAEVPT VSLVGYTNAG KSSLFNRLTQ AETYAADQLF ATLDSTLRKV ELPNFGQAIM ADTVGFISHL PHQLVEAFRA TLEETVQADL LLHVIDAAHD YHPEFIREVE SVLSEIGAQE VPQLQVFNKI DLLPGREPEL QRNSAGKPYR VWVSAKTGAG IETLLEAVSE LLAGEMSDQL LRVAPSEAKL RSKLYAANYV ENEEITDDGH YLLRVRMPLQ EFDRIKLLGG VVIEGVRRGA E // ID A0A0R2T721_9FLAO Unreviewed; 391 AA. AC A0A0R2T721; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 12-APR-2017, entry version 8. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=ABR87_06885 {ECO:0000313|EMBL:KRO82822.1}; OS Cryomorphaceae bacterium BACL7 MAG-121220-bin83. OC Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales; OC Cryomorphaceae; unclassified Cryomorphaceae. OX NCBI_TaxID=1655595 {ECO:0000313|EMBL:KRO82822.1, ECO:0000313|Proteomes:UP000051535}; RN [1] {ECO:0000313|EMBL:KRO82822.1, ECO:0000313|Proteomes:UP000051535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BACL29 MAG-121220-bin83 {ECO:0000313|EMBL:KRO82822.1}; RA Hugerth L.W., Larsson J., Alneberg J., Lindh M.V., Legrand C., RA Pinhassi J., Andersson A.; RT "Metagenome-Assembled Genomes uncover a global brackish microbiome."; RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KRO82822.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LICF01000018; KRO82822.1; -; Genomic_DNA. DR Proteomes; UP000051535; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000051535}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000051535}. FT DOMAIN 203 380 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 391 AA; 44655 MW; 2170FBCF8EEEA1DF CRC64; MLERTSARST EPERCILIGA ITRAQPEAKS EEYLEELRFL AFTAGAETLE VFTQKLDRPD SSTFLGSGKM EEIKEYVDEN KIDLAIFDDE LSPSQLKNIE RLLEIKVMDR TNLILDIFAA RAQTSYARTQ VELAQYEYLL PRLTKMWTHL ERQKGGIGMR GPGETQIETD RRIIKQKITL LQQKLGKIDR QMATQRGNRG NLIRASLVGY TNVGKSTLMN ALGKTEVLAE NKLFATLDTT VRKIVIGNLP FLLTDTVGFI RKLPTQLIES FKSTLDEVRE ADILFHVVDI AHESYEDHMA SVDQILTEIK AHEKPILVIF NKVDAWMPEK DADGYLPRIE DFQNRWIKEL GGQCVFISAT QKGNFDSLRE SIYRAVATLH AVRFPFDTFL Y // ID A0A0R2TWJ4_9FLAO Unreviewed; 399 AA. AC A0A0R2TWJ4; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 12-APR-2017, entry version 8. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=ABR90_07630 {ECO:0000313|EMBL:KRO89579.1}; OS Cryomorphaceae bacterium BACL29 MAG-121220-bin8. OC Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales; OC Cryomorphaceae; unclassified Cryomorphaceae. OX NCBI_TaxID=1655598 {ECO:0000313|EMBL:KRO89579.1, ECO:0000313|Proteomes:UP000051665}; RN [1] {ECO:0000313|EMBL:KRO89579.1, ECO:0000313|Proteomes:UP000051665} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BACL7 MAG-121220-bin8 {ECO:0000313|EMBL:KRO89579.1}; RA Hugerth L.W., Larsson J., Alneberg J., Lindh M.V., Legrand C., RA Pinhassi J., Andersson A.; RT "Metagenome-Assembled Genomes uncover a global brackish microbiome."; RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KRO89579.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LICI01000053; KRO89579.1; -; Genomic_DNA. DR Proteomes; UP000051665; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000051665}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000051665}. FT DOMAIN 200 384 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 399 AA; 45504 MW; F9DF11C1E88206DF CRC64; MIEKNNVSLE RTVIVGVITL KQTKSVLEEY LNELSFLTFT AGGEVIKRFT QKLTSPDSKT FLGKGKMEEL AAFINTNDIN SVIFDDELTP AQQLNIEKFL KCKIVDRTGL ILDIFAQRAK TSSARNQVEL AQYQYILPRL KGLWTHLERQ KGGIGMRGPG ETEIETDRRI VRDKITLLKK KLVVIDKQMS TQRGNRGSLV RVALVGYTNV GKSTLMNSIS KAEVFAEDKL FATLDTTVRK VVIENMPFLL TDTVGFIRKL PTQLIDSFKS TLTEITEADL LIHVVDIAHP NYEDHIDSVN TILNEIGSGE KPMIMLFNKI DKYVNDKENI KDINDIDYQD KSLNTLKSSL SKKYNQKAYF ISALSKKDVR ELKTNFYKEI REIHVTRFPY NAFLYPDIT // ID A0A0R2U617_9GAMM Unreviewed; 352 AA. AC A0A0R2U617; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 12-APR-2017, entry version 6. DE SubName: Full=GTPase HflX {ECO:0000313|EMBL:KRO95007.1}; DE Flags: Fragment; GN ORFNames=ABS24_02040 {ECO:0000313|EMBL:KRO95007.1}; OS SAR92 bacterium BACL26 MAG-121220-bin70. OC Bacteria; Proteobacteria; Gammaproteobacteria; Cellvibrionales; OC Porticoccaceae; SAR92 clade. OX NCBI_TaxID=1655626 {ECO:0000313|EMBL:KRO95007.1, ECO:0000313|Proteomes:UP000051213}; RN [1] {ECO:0000313|EMBL:KRO95007.1, ECO:0000313|Proteomes:UP000051213} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BACL26 MAG-121220-bin70 {ECO:0000313|EMBL:KRO95007.1}; RA Hugerth L.W., Larsson J., Alneberg J., Lindh M.V., Legrand C., RA Pinhassi J., Andersson A.; RT "Metagenome-Assembled Genomes uncover a global brackish microbiome."; RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KRO95007.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LICA01000115; KRO95007.1; -; Genomic_DNA. DR Proteomes; UP000051213; Unassembled WGS sequence. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000051213}; KW Reference proteome {ECO:0000313|Proteomes:UP000051213}. FT DOMAIN 201 352 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT NON_TER 352 352 {ECO:0000313|EMBL:KRO95007.1}. SQ SEQUENCE 352 AA; 39059 MW; FFE81F9FA87AE0D1 CRC64; MALFFERPES GERAVLVHIK LNSESEPEDP REFEELVLAA GGDPVEFITG SRQSPSAKTF IGTGKLDEIN AVVKSTCAEL VIFNHNLSPS QERNLEAVLQ CRVLDRTGLI LDIFAQRART HEGKLQVELA QLQHLSSRLV RGWTHLERQK GGIGMRGPGE TQLESDRRMV RDRIKLIKQR LEKVRKQRGQ GRIGRQRSEI PTVSLVGYTN AGKSTLFNTL TNADVFVADQ LFATLDPTMR RLDIANIGAV IFADTVGFIS HLPHRLVEAF RATLEEAALA DLLLHVIDAG AEDRATNIVR VDEVLKEIQA NKIPSLMVYN KGDLLDDFSP RLDRDADGMP IAVWVSALAG EG // ID A0A0R2UE63_9GAMM Unreviewed; 432 AA. AC A0A0R2UE63; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 10-MAY-2017, entry version 9. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=ABS10_04595 {ECO:0000313|EMBL:KRO96098.1}; OS SAR86 cluster bacterium BACL1 MAG-120820-bin45. OC Bacteria; Proteobacteria; Gammaproteobacteria; SAR86 cluster. OX NCBI_TaxID=1655612 {ECO:0000313|EMBL:KRO96098.1, ECO:0000313|Proteomes:UP000051027}; RN [1] {ECO:0000313|EMBL:KRO96098.1, ECO:0000313|Proteomes:UP000051027} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BACL1 MAG-120820-bin45 {ECO:0000313|EMBL:KRO96098.1}; RA Hugerth L.W., Larsson J., Alneberg J., Lindh M.V., Legrand C., RA Pinhassi J., Andersson A.; RT "Metagenome-Assembled Genomes uncover a global brackish microbiome."; RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KRO96098.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LICS01000007; KRO96098.1; -; Genomic_DNA. DR Proteomes; UP000051027; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000051027}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}. FT DOMAIN 203 369 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 432 AA; 47964 MW; 8BE597D4680A6955 CRC64; MEKTLAPADL RAIIVSVDLL RSSPKESNNF NANEFLDLAQ SAGLKVEDHI FSKQNFVSAS HFITKGKVEE LKTLVTEKDI KLVLLDCDLS PSQERNLETV LCARVLDRTG LILDIFATRA QSDIGKLQVE LAQLSFLSTR LVRGWSHLER QKGGIGLRGP GETQLETDKR LVANRIKQLK KRLKTQHNQK NLNRYSRKKG ENKLVALVGY TNAGKTSLFN TLTKGGLYAA DKLFATLDTT TRKADFKSKT LSTMLFSDTV GFISNLPTKL VESFKATLDD LSSADLLLHV IDAADPESDF KIQQVNLILQ DLGVEKIPQI RVLNKTDLIP ANAIQPANEH HPEIRVSAQT GDGLDKLKAQ ISEMLFGEIV AGWICFSPTQ SAIRSKLFDS GCIIEEKMDE HGSYQSFVEI SQGMLKQFKE LDGAKSLKPI QV // ID A0A0R2VVM7_9SPHI Unreviewed; 393 AA. AC A0A0R2VVM7; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 12-APR-2017, entry version 8. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=ABR95_02285 {ECO:0000313|EMBL:KRP13852.1}; OS Sphingobacteriales bacterium BACL12 MAG-120813-bin55. OC Bacteria; Bacteroidetes; Sphingobacteriia; Sphingobacteriales. OX NCBI_TaxID=1655600 {ECO:0000313|EMBL:KRP13852.1, ECO:0000313|Proteomes:UP000050993}; RN [1] {ECO:0000313|EMBL:KRP13852.1, ECO:0000313|Proteomes:UP000050993} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BACL12 MAG-120813-bin55 {ECO:0000313|EMBL:KRP13852.1}; RA Hugerth L.W., Larsson J., Alneberg J., Lindh M.V., Legrand C., RA Pinhassi J., Andersson A.; RT "Metagenome-Assembled Genomes uncover a global brackish microbiome."; RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KRP13852.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LICN01000007; KRP13852.1; -; Genomic_DNA. DR Proteomes; UP000050993; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000050993}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000050993}. FT DOMAIN 200 382 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 393 AA; 45466 MW; E0AA00F72B7D1040 CRC64; MTETTVNKNE TCILVGLVTQ YQTTTQLDEY LDELEFLAGT AGAVTIGRFY QKLTTPDKRT YVGKGKLEEI RLFAEKHEAD MLIFDDEISP AQLRNIEEVL KMKILDRSML ILDIFASRAQ TLQAKTQVEL AQTQYLLPRL RGMWTHLDRI KGGIGMRGTG EKEIETDRRV AQQRISILKQ KLRDIDVQSQ TQRKNRGEFI RVALVGYTNV GKSTLMNTLS KSEVFAENKL FATLDTTVRK VVFDRTPFLL SDTVGFIRKL PHHLVESFKS TLDEVREADV LLHVVDIAHP AFEDHIATVN ATLEDIGARD KPVIMVFNKM DLYEQRMFDP YLKEEVKKDI LNELQQTWMQ RSNENAVFIS VTQRTNLEEL RDRILLMVVE AYKVRYPYKT DFY // ID A0A0R2WEW8_9GAMM Unreviewed; 436 AA. AC A0A0R2WEW8; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 12-APR-2017, entry version 8. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=ABS23_01005 {ECO:0000313|EMBL:KRP20030.1}; OS SAR92 bacterium BACL16 MAG-120619-bin48. OC Bacteria; Proteobacteria; Gammaproteobacteria; Cellvibrionales; OC Porticoccaceae; SAR92 clade. OX NCBI_TaxID=1655625 {ECO:0000313|EMBL:KRP20030.1, ECO:0000313|Proteomes:UP000051070}; RN [1] {ECO:0000313|EMBL:KRP20030.1, ECO:0000313|Proteomes:UP000051070} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BACL16 MAG-120619-bin48 {ECO:0000313|EMBL:KRP20030.1}; RA Hugerth L.W., Larsson J., Alneberg J., Lindh M.V., Legrand C., RA Pinhassi J., Andersson A.; RT "Metagenome-Assembled Genomes uncover a global brackish microbiome."; RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KRP20030.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LIDE01000005; KRP20030.1; -; Genomic_DNA. DR Proteomes; UP000051070; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000051070}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000051070}. FT DOMAIN 201 368 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 436 AA; 48520 MW; 1905CD8951900220 CRC64; MALFFERPDF GEKAVLVHLK LNSESEPDDP REFEELVLSA GGDPVDFLTG SRSSPHAKFF VGTGKLEEIG NAVKSSGAEL VIFNHNLSPS QERNIEAELQ CRVLDRTGLI LDIFAQRART HEGKLQVELA QLHHLSTRLV RGWTHLERQK GGIGLRGPGE TQLESDRRMV RDRIKAIQAR LVKVRNQRAQ SRQSRVRAEI PAVSLVGYTN AGKSTLFNAV TQSDVFVADQ LFATLDPTMR KIEIDEKGVV IFADTVGFIS HLPHRLVDAF RSTLEEAANS TLLLHVVDAA SEDRANSINQ VNEVLKEIDA YELPTLMVYN KIDLLEDSTA RIDYDADGQP VAVWVSALNR EGMALLIEAV TARLPGRLVH KTLHLLPEQG ALRASMYSHK AVIHEEVDDR GCINLEVKLP EMDYFRLIKA AGLKSEDLAA LYNAAR // ID A0A0R2X287_9FLAO Unreviewed; 400 AA. AC A0A0R2X287; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 12-APR-2017, entry version 9. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=ABS28_08365 {ECO:0000313|EMBL:KRP30250.1}; OS Cryomorphaceae bacterium BACL22 MAG-120619-bin32. OC Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales; OC Cryomorphaceae; unclassified Cryomorphaceae. OX NCBI_TaxID=1655630 {ECO:0000313|EMBL:KRP30250.1, ECO:0000313|Proteomes:UP000052139}; RN [1] {ECO:0000313|EMBL:KRP30250.1, ECO:0000313|Proteomes:UP000052139} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BACL3 MAG-120619-bin32 {ECO:0000313|EMBL:KRP30250.1}; RA Hugerth L.W., Larsson J., Alneberg J., Lindh M.V., Legrand C., RA Pinhassi J., Andersson A.; RT "Metagenome-Assembled Genomes uncover a global brackish microbiome."; RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KRP30250.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LIDG01000010; KRP30250.1; -; Genomic_DNA. DR Proteomes; UP000052139; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000052139}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000052139}. FT DOMAIN 200 385 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 400 AA; 46252 MW; B7BA0EE1B6F225B4 CRC64; MIDQIEAISE KVVLIGVITQ FQDESKSKEY LDELEFLTLT AGGIALKRFV QKVDKPNPKT FLGIGKLEEV RQFIDANEIG TAIFDDELTP GQLRNIEKEL NCKILDRTNL ILDIFAQRAQ TSSAKMQVEL AQNQYILPRL TRLWTHLDKQ KGGIGMRGPG ETEIETDRRI IRDKITLLKK KLLTLDIQMA VQRKNRGKMV RVALIGYTNV GKSTLMNVIS KSDVFAENKL FATLDTTVRK VVIKNIPFLM TDTVGFIRKL PTQLVESFKS TLDEVCEADL LLHVVDISHP HFEDHIDSVN SILLDIKCGD KPTLMVFNKI DAYEYQTIDE DDLMTEKGKE HYTLQDWKKT WMNEYEVESI FISALNKDNF EDFKEKVYKE VKKIHVQRFP YNDFLFEEYQ // ID A0A0R2XMT3_9BACT Unreviewed; 422 AA. AC A0A0R2XMT3; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 12-APR-2017, entry version 9. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=ABS34_03315 {ECO:0000313|EMBL:KRP37334.1}; OS Opitutaceae bacterium BACL24 MAG-120322-bin51. OC Bacteria; Verrucomicrobia; Opitutae; Opitutales; Opitutaceae. OX NCBI_TaxID=1655636 {ECO:0000313|EMBL:KRP37334.1, ECO:0000313|Proteomes:UP000054041}; RN [1] {ECO:0000313|EMBL:KRP37334.1, ECO:0000313|Proteomes:UP000054041} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BACL24 MAG-120322-bin51 {ECO:0000313|EMBL:KRP37334.1}; RA Hugerth L.W., Larsson J., Alneberg J., Lindh M.V., Legrand C., RA Pinhassi J., Andersson A.; RT "Metagenome-Assembled Genomes uncover a global brackish microbiome."; RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KRP37334.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LIDO01000022; KRP37334.1; -; Genomic_DNA. DR Proteomes; UP000054041; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000054041}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000054041}. FT DOMAIN 198 364 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 422 AA; 47464 MW; 43500A9B1A38D6AD CRC64; MVERAMLIGI TLPGRDDATT RSLLDELREL VTTLGIGIQH EVQLSIRKPQ AKFLLGTGKA EEMIEEAKAH NCDVIVLDNE LTPAQQRNWE QAADDKILVI DRQEVILDIF GKRAQTKEAV LQVELARLEY NLPRLKSAWT HLSRQRGGGS MQRDAGETQQ ELDQRMVRTQ ITRVKRELES VIQHRHVQRK KRMTVPVPTC AIVGYTNAGK SSLLNQLTNS DILVEDKLFA TLDPTSRRCP LPSGQPLIIT DTVGFVRNLP HRLVNAFKAT LEEAVVSNFL IHVLDVNSPE IEAHAETTLS VLHGLGADEK KIITVFNKID DLWSEDIRLT LSFRYPEALF VSAHTGEGIP ELLECIEAIV ESDFAQLRLL IPHDRYDLVA RLHREGGVRK EEARDDGTYI VGSVPERMLS ALHPFLLSSD EP // ID A0A0R3JV95_9CLOT Unreviewed; 604 AA. AC A0A0R3JV95; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 07-JUN-2017, entry version 10. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:KRQ87488.1}; GN ORFNames=ABG79_00826 {ECO:0000313|EMBL:KRQ87488.1}; OS Caloramator mitchellensis. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Caloramator. OX NCBI_TaxID=908809 {ECO:0000313|EMBL:KRQ87488.1, ECO:0000313|Proteomes:UP000052015}; RN [1] {ECO:0000313|EMBL:KRQ87488.1, ECO:0000313|Proteomes:UP000052015} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=VF08 {ECO:0000313|EMBL:KRQ87488.1, RC ECO:0000313|Proteomes:UP000052015}; RA Patel B.K.; RT "Draft genome sequence of a Caloramator mitchellensis, a moderate RT thermophile from the Great Artesian Basin of Australia."; RL Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KRQ87488.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LKHP01000003; KRQ87488.1; -; Genomic_DNA. DR RefSeq; WP_057977389.1; NZ_LKHP01000003.1. DR EnsemblBacteria; KRQ87488; KRQ87488; ABG79_00826. DR PATRIC; fig|908809.3.peg.835; -. DR Proteomes; UP000052015; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000052015}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000052015}. FT DOMAIN 376 547 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 335 369 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 604 AA; 67445 MW; C70BFBA705A1CCD2 CRC64; MLRGDLEGVK KLFIKELEEL FEADVDKNII ITEEIVNIIS RISWELKREI SIYINRRGKI VDIAIGDNNT VSLEEVFERR GEFGLSGVRC IHTHPGGGGE LSIVDITALV SLKFDMMVAI GVNEGKPTEF SLGVIKVEEG KLSKKAEELG PLNIKEITKL NAIEIIHDVE KDLKDKVHVV DENRKERAIL VAIGNDDLYS LEESLDELEE LVETAGAEVV YKISQKKGKI DPATYIGSGK AKEISLLRQS LMADSVIFDD QLSPAQIRNL EEIFGCKVID RTALILDIFA QRAISREGKI QVELAQLKYR LPRLTGFGAM LSRTGGGIGT RGPGEKKLEI DKRHIMRRIN DLEKELESVR GTRQLQRERR ISNEVPVVSI VGYTNAGKST LRNKLCEIAG VDKEKVLEAN MLFATLDTTT RLINLPNGKT ALVSDTVGFI RKLPHELVEA FKSTLEEILY SDLILHVVDA SNNNALAQIE VVNGVLDEIG AGDKKAILVL NKIDLASTEN IEVIRNKHKE SIEISALNEI NLDGLLKAVQ ENVFTNMIRA KLFIPYSDSK IVSYLHDNNC VENEEYAEDG FLVQVYTTED VIGRVKGYVR EYIN // ID A0A0R3MEQ6_9BRAD Unreviewed; 457 AA. AC A0A0R3MEQ6; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 07-JUN-2017, entry version 13. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=CQ14_24745 {ECO:0000313|EMBL:KRR18601.1}; OS Bradyrhizobium lablabi. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Bradyrhizobiaceae; Bradyrhizobium. OX NCBI_TaxID=722472 {ECO:0000313|EMBL:KRR18601.1, ECO:0000313|Proteomes:UP000051660}; RN [1] {ECO:0000313|EMBL:KRR18601.1, ECO:0000313|Proteomes:UP000051660} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CCBAU 23086 {ECO:0000313|EMBL:KRR18601.1, RC ECO:0000313|Proteomes:UP000051660}; RA Duran D., Rey L., Navarro A., Busquets A., Imperial J., RA Ruiz-Argueso T.; RT "Bradyrhizobium valentinum sp. nov., isolated from effective nodules RT of Lupinus mariae-josephae, a lupine endemic of basic-lime soils in RT Eastern Spain."; RL Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KRR18601.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LLYB01000103; KRR18601.1; -; Genomic_DNA. DR RefSeq; WP_057861507.1; NZ_LLYB01000103.1. DR EnsemblBacteria; KRR18601; KRR18601; CQ14_24745. DR Proteomes; UP000051660; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000051660}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000051660}. FT DOMAIN 224 398 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 457 AA; 50656 MW; 37314D908EB0EA5A CRC64; MEPFDREGSA DRPRSAAKQS GRVIVIGPYL RMRGGNADAQ ANEAVRDSEA RLEEAAGLAR AIDLTIADAL IAPISQIRPA TYLGKGKVEE ITGLIAGHNI ELVVMDCALS PIQQRNLEKA WNTKVLDRTG LILEIFGRRA KTKEGALQVE LAHLNYQRSR LVRSWTHLER QRGGFGFMGG PGETQIEADR RLIGDRITRL ENELKKVQAT RRLHRAGRQR VPYRVVALVG YTNAGKSTLF NRLTRADVQA ADMLFATLDP TLRALSLPHG GKAMLSDTVG FISNLPTQLV AAFRATLEEV LEADIILHVR DISHEDAEAQ ERDVDAVLRQ LGIDPTAGGR ILEVWNKIDR FDPEERENLR NIAARRPPER PCFLVSATSG EGINELLSAI EERLAATRTT LDLSIDASDG AGISWLHRNA EVLTKELHDG RFDMTVRVDE TKRDIVVSRF DAVPRVA // ID A0A0R3R958_9BILA Unreviewed; 265 AA. AC A0A0R3R958; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 12-APR-2017, entry version 4. DE SubName: Full=Uncharacterized protein {ECO:0000313|WBParaSite:BTMF_0001656801-mRNA-1}; OS Brugia timori. OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Spirurida; OC Filarioidea; Onchocercidae; Brugia. OX NCBI_TaxID=42155 {ECO:0000313|Proteomes:UP000050602, ECO:0000313|WBParaSite:BTMF_0001656801-mRNA-1}; RN [1] {ECO:0000313|Proteomes:UP000050602, ECO:0000313|WBParaSite:BTMF_0001656801-mRNA-1} RP NUCLEOTIDE SEQUENCE. RG Helminth Genomes Consortium; RL Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|WBParaSite:BTMF_0001656801-mRNA-1} RP IDENTIFICATION. RG WormBaseParasite; RL Submitted (FEB-2017) to UniProtKB. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR WBParaSite; BTMF_0001656801-mRNA-1; BTMF_0001656801-mRNA-1; BTMF_0001656801. DR Proteomes; UP000050602; Genome Assembly. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR Pfam; PF13167; GTP-bdg_N; 1. DR SUPFAM; SSF52540; SSF52540; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000050602}; KW Reference proteome {ECO:0000313|Proteomes:UP000050602}. FT DOMAIN 74 162 GTP-bdg_N. {ECO:0000259|Pfam:PF13167}. SQ SEQUENCE 265 AA; 30344 MW; 346712B458F5B4DC CRC64; MKNFAKIFVP LYSGRRFCTM IPEGAMQMTD EFNIISKSYG IQSIAPGVQR ILLIHPRLRR GRFFDLNPER AKLQLGEAVA LVNTLPNFKV METTAVSTDR STKKKRLWGS GRIQRIIALK EKISATALMI DVDILSPKQQ AELTSIFRTP VYDRYNIVLL IFKIFAKTKE AKLQIQLAEI PYIRQRLLSM YELHVDPSLL HLDTSEKSKA ERLEVLRYRE QHLRKCLKAA VEEKVNLRIG EAQKNIRTVV AVVGYTNAGK SSLIK // ID A0A0R3UAI5_9CEST Unreviewed; 517 AA. AC A0A0R3UAI5; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 12-APR-2017, entry version 5. DE SubName: Full=Uncharacterized protein {ECO:0000313|WBParaSite:MCOS_0000393301-mRNA-1}; OS Mesocestoides corti. OC Eukaryota; Metazoa; Platyhelminthes; Cestoda; Eucestoda; OC Cyclophyllidea; Mesocestoididae; Mesocestoides. OX NCBI_TaxID=53468 {ECO:0000313|Proteomes:UP000046399, ECO:0000313|WBParaSite:MCOS_0000393301-mRNA-1}; RN [1] {ECO:0000313|Proteomes:UP000046399, ECO:0000313|WBParaSite:MCOS_0000393301-mRNA-1} RP NUCLEOTIDE SEQUENCE. RG Helminth Genomes Consortium; RL Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|WBParaSite:MCOS_0000393301-mRNA-1} RP IDENTIFICATION. RG WormBaseParasite; RL Submitted (FEB-2017) to UniProtKB. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR WBParaSite; MCOS_0000393301-mRNA-1; MCOS_0000393301-mRNA-1; MCOS_0000393301. DR Proteomes; UP000046399; Genome Assembly. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR SUPFAM; SSF52540; SSF52540; 2. DR PROSITE; PS51705; G_HFLX; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000046399}; KW Reference proteome {ECO:0000313|Proteomes:UP000046399}. FT DOMAIN 246 346 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 517 AA; 57730 MW; FBF3464E045DE997 CRC64; LHLVERSFKC LSFCRVNVIL LSLVVRSAKL CRKLDLNVSS IDSTENGGLV VSQMAKGPDE QEARSLIDSI GGWTVENVVH MNLRSVGFNS GQFFTKGVWQ ELTQVVEDHF QPLANKSSRY QVSRPITAVF INWRRLTVNQ LIEMQKAWKC PVYDRYMLVV HLFLLRARSR EAKAQAQLAE LGVIRSRLLA ATAASTLSQP KSRSIDHLHR VLDDQERKLS AILVEEEKRK ELGRKRRREK TTNRLPTVAV IGYTNAGKTS LIRHLTRSAG MVVSPRVFAT LDVTHHAARL PPPKTSDSSG VPGLRLLMVD TIGFMADLPQ NLIAAFKATL SECLDAEIIL HVIDSSQPGW PAFAAYIERV LQESGVQARR LADLSIDTKG ATDLGERDSS SPVLIRVGNK ADLGTHIDSS VHTKLQLDVE VSCVNNTGIA ELRNLIEFAL VSGLGWSKRK LRMKQGSRAL RSFDFSWLYA NAMVLQVSSC PEDPEKLLCE VLFNDTIWSL FKSKFVASCR NNFTHCT // ID A0A0R4J0Z0_MOUSE Unreviewed; 514 AA. AC A0A0R4J0Z0; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 07-JUN-2017, entry version 12. DE SubName: Full=Putative GTP-binding protein 6 {ECO:0000313|Ensembl:ENSMUSP00000076458}; GN Name=Gtpbp6 {ECO:0000313|Ensembl:ENSMUSP00000076458, GN ECO:0000313|MGI:MGI:1306825}; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090 {ECO:0000313|Ensembl:ENSMUSP00000076458, ECO:0000313|Proteomes:UP000000589}; RN [1] {ECO:0000313|Ensembl:ENSMUSP00000076458, ECO:0000313|Proteomes:UP000000589} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000076458, RC ECO:0000313|Proteomes:UP000000589}; RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112; RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., RA She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., RA Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., RA Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J., RA Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., RA Lindblad-Toh K., Eichler E.E., Ponting C.P.; RT "Lineage-specific biology revealed by a finished genome assembly of RT the mouse."; RL PLoS Biol. 7:E1000112-E1000112(2009). RN [2] {ECO:0000213|PubMed:21183079} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001; RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R., RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.; RT "A tissue-specific atlas of mouse protein phosphorylation and RT expression."; RL Cell 143:1174-1189(2010). RN [3] {ECO:0000313|Ensembl:ENSMUSP00000076458} RP IDENTIFICATION. RC STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000076458}; RG Ensembl; RL Submitted (MAR-2016) to UniProtKB. CC -!- CAUTION: The sequence shown here is derived from an Ensembl CC automatic analysis pipeline and should be considered as CC preliminary data. {ECO:0000313|Ensembl:ENSMUSP00000076458}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AC166747; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR RefSeq; NP_660129.2; NM_145147.5. DR UniGene; Mm.86267; -. DR SMR; A0A0R4J0Z0; -. DR Ensembl; ENSMUST00000077220; ENSMUSP00000076458; ENSMUSG00000033434. DR GeneID; 107999; -. DR KEGG; mmu:107999; -. DR CTD; 8225; -. DR MGI; MGI:1306825; Gtpbp6. DR GeneTree; ENSGT00390000001397; -. DR OMA; MDTVGFM; -. DR Proteomes; UP000000589; Chromosome 5. DR ExpressionAtlas; A0A0R4J0Z0; baseline and differential. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR CDD; cd01878; HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 1: Evidence at protein level; KW Complete proteome {ECO:0000313|Proteomes:UP000000589}; KW Proteomics identification {ECO:0000213|MaxQB:A0A0R4J0Z0, KW ECO:0000213|PeptideAtlas:A0A0R4J0Z0}; KW Reference proteome {ECO:0000313|Proteomes:UP000000589}. FT DOMAIN 285 449 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 514 AA; 56448 MW; 9DCE57EE1A1D8541 CRC64; MLFLRAAVLP GFWLPRVRRV QLVRSPAVTL PSPVRTVHAG SRVWGSAWAG GGPVRGGGEE DPREDEEEEE DELLRAPPLL PLDTQRVCVL HPDVKRPAGK KPRSTAEWQV AEAAALVRAL PGWSVASTLV VPSAAPGSRL VFGKGNFQDV TEKIKGCQDI TSVFLNVERM APPTKKELES AWGLRVFDRF TLVLHIFRCN ARTREARMQL ALAEIPLLRS SVNTDSGQQD QQGWGSRYIM GSGESPTELR ARALRDRELR LRRVLERLRD KRRLMRKERV RREFPVVSVV GYTNCGKTTL IQALTGEAAL QPRDQPFATL DVTVHAGLLP SRLRILYVDT IGFLSQLPHS LIHAFSATLE DVAYSDVLVH VTDVSHPDAE LQKATVLSTL RGLHLPPALL ESALEVHSKV DLVPGYTPPC SGALAVSAIS GRGLDELKAA LEASVLRATG RQVLTLCVRL GGPQLGWLYK EAVVQQVQEL PEGDAAHVTV VITQAAYGRF RKLFPIDAPS ALPH // ID A0A0S1SEM8_9FLAO Unreviewed; 403 AA. AC A0A0S1SEM8; DT 17-FEB-2016, integrated into UniProtKB/TrEMBL. DT 17-FEB-2016, sequence version 1. DT 07-JUN-2017, entry version 12. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=SB49_11530 {ECO:0000313|EMBL:ALM08368.1}; OS Sediminicola sp. YIK13. OC Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales; OC Flavobacteriaceae; Sediminicola. OX NCBI_TaxID=1453352 {ECO:0000313|EMBL:ALM08368.1, ECO:0000313|Proteomes:UP000063759}; RN [1] {ECO:0000313|Proteomes:UP000063759} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=YIK13 {ECO:0000313|Proteomes:UP000063759}; RA Kwon Y.M., Kim S.-J.; RT "Genome sequence of Sediminicola sp. YIK13."; RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP010535; ALM08368.1; -; Genomic_DNA. DR RefSeq; WP_062056743.1; NZ_CP010535.1. DR EnsemblBacteria; ALM08368; ALM08368; SB49_11530. DR KEGG; syi:SB49_11530; -. DR PATRIC; fig|1453352.4.peg.2409; -. DR KO; K03665; -. DR Proteomes; UP000063759; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000063759}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000063759}. FT DOMAIN 200 385 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 403 AA; 46873 MW; 8B9558D9A135CA03 CRC64; MIEKKTIVYE KVVLIGVIHR EQDEIKVKEY LDELEFLTYT AGGEVSKRFV QRIDVPNPKT YIGSGKLLEV EAFVAENDIG TVVFDDELSP GQQRNIEREL RCKILDRTSL ILDIFAQRAQ TSYARTQVEL AQYEYLLPRL TGLWTHLERQ KGGIGMRGPG ETEIETDRRI VRDRIALLKK KLLKIDRQME TQRGNRGALV RVALVGYTNV GKSTLMNVIS KSEVFAEDKL FATLDTTVRK VVIGNLPFLL TDTVGFIRKL PTQLVESFKS TLDEVREADL LLHVVDISHP TFEEHIESVN KILDEIDSAD KRTIMVFNKI DQYHHETIDD DDLMTERTQK HFTLEEWEKT WMQKVGDKAI FISALNKENL DEFRKRVYDE VRDIHVTRFP YNNFLYPEQL DEY // ID A0A0S1Y110_9BORD Unreviewed; 368 AA. AC A0A0S1Y110; DT 17-FEB-2016, integrated into UniProtKB/TrEMBL. DT 17-FEB-2016, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=ASB57_12800 {ECO:0000313|EMBL:ALM83737.1}; OS Bordetella sp. N. OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Alcaligenaceae; Bordetella. OX NCBI_TaxID=1746199 {ECO:0000313|EMBL:ALM83737.1, ECO:0000313|Proteomes:UP000064621}; RN [1] {ECO:0000313|EMBL:ALM83737.1, ECO:0000313|Proteomes:UP000064621} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=N {ECO:0000313|EMBL:ALM83737.1, RC ECO:0000313|Proteomes:UP000064621}; RA Hou L.; RT "Draft genome of Bordetella sp. N."; RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP013111; ALM83737.1; -; Genomic_DNA. DR RefSeq; WP_057652583.1; NZ_CP013111.1. DR EnsemblBacteria; ALM83737; ALM83737; ASB57_12800. DR Proteomes; UP000064621; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000064621}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000064621}. FT DOMAIN 190 354 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 156 183 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 368 AA; 40386 MW; 910C1BEFB8716FFB CRC64; MRALIISVDL GNPDYVAHAE EFAMLARGAG AEIVDTIKAR RDRPDAKYFI GSGKVEEAVA LAKAHDADIV LFDHPLSPAQ QRNLEREFLL RVVDRVALIL DIFALRAKSH EGKLQVELAQ LQHLTTRLTR MWSHLERQRG GIGMRGPGES QLEMDKRMIG AKVKLLRERL DKVERQRVTQ RRARARGGVL SVSLVGYTNA GKSTLFNAVT RADAYAADQL FATLDTTTRK IWIEGAGSVV LSDTVGFIRD LPPTLIAAFR ATLEETVHAD LLLHVVDAAS PQRDEQILEV EKVLNEIGAG TIPVIMVYNK IDRVDMAPRV DRNAHGTIAR VFVSAAERAG LDALRGAIAE AGQIAGNNAS NIQTVQSE // ID A0A0S2DE92_LYSEN Unreviewed; 432 AA. AC A0A0S2DE92; DT 17-FEB-2016, integrated into UniProtKB/TrEMBL. DT 17-FEB-2016, sequence version 1. DT 05-JUL-2017, entry version 14. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:ALN56868.1}; GN ORFNames=BV903_21780 {ECO:0000313|EMBL:OPD61807.1}, GN GLE_1511 {ECO:0000313|EMBL:ALN56868.1}; OS Lysobacter enzymogenes. OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales; OC Xanthomonadaceae; Lysobacter. OX NCBI_TaxID=69 {ECO:0000313|EMBL:ALN56868.1, ECO:0000313|Proteomes:UP000061569}; RN [1] {ECO:0000313|EMBL:ALN56868.1, ECO:0000313|Proteomes:UP000061569} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C3 {ECO:0000313|EMBL:ALN56868.1, RC ECO:0000313|Proteomes:UP000061569}; RA Kobayashi D.Y.; RT "Genome sequences of Lysobacter enzymogenes strain C3 and Lysobacter RT antibioticus ATCC 29479."; RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:OPD61807.1, ECO:0000313|Proteomes:UP000190203} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=B25 {ECO:0000313|EMBL:OPD61807.1, RC ECO:0000313|Proteomes:UP000190203}; RA Hernandez I., Fernandez C.; RT "Draft genome of Lysobacter enzymogenes B25."; RL Submitted (JAN-2017) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP013140; ALN56868.1; -; Genomic_DNA. DR EMBL; MTAY01000072; OPD61807.1; -; Genomic_DNA. DR RefSeq; WP_057946836.1; NZ_MTAY01000072.1. DR EnsemblBacteria; ALN56868; ALN56868; GLE_1511. DR KEGG; lez:GLE_1511; -. DR PATRIC; fig|69.6.peg.1492; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR Proteomes; UP000061569; Chromosome. DR Proteomes; UP000190203; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000061569}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000061569}. FT DOMAIN 199 364 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 158 192 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 432 AA; 47408 MW; C05DC4EABE6FC297 CRC64; MFERSKRGEH ALLIQPHSGG APEEDLLEEF ADLARSAGAS VAAVLTARID RPNAAILIGS GKLEEVKAAA EASGADLILV NHPLSPGQER NLERALQRRV VDRTGLILDI FSQRARSAEG KLQVELAQLK HMATRLVRGW THLERQRGGS IGLRGPGETQ LETDRRLLQK RLEQLQKRLD KVEVQRTQMR RARVRSELPR VALVGYTNAG KSTLFNALTG ADAYAADQLF ATLDPTVRRI ELAGGGVVLA DTVGFVRDLP HELVAAFRST LSEAREADLL LHVIDAADPL RDERIAQVDA VLAEIGAGDL PQLLVFNKID RLDGVAPRID RPGEERHRVW LSARTGEGLA TLRDALGEAL QLRRVQGGLR IAPQDARLRA RLHDLGAVRA EQADEHGWWV EVDLAVADAQ RLFAQAHGEP LRPLLETAET PT // ID A0A0S2DTK8_9GAMM Unreviewed; 432 AA. AC A0A0S2DTK8; DT 17-FEB-2016, integrated into UniProtKB/TrEMBL. DT 17-FEB-2016, sequence version 1. DT 30-AUG-2017, entry version 13. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:ALN81802.1}; GN ORFNames=LA76x_3680 {ECO:0000313|EMBL:ALN81802.1}; OS Lysobacter antibioticus. OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales; OC Xanthomonadaceae; Lysobacter. OX NCBI_TaxID=84531 {ECO:0000313|EMBL:ALN81802.1, ECO:0000313|Proteomes:UP000060787}; RN [1] {ECO:0000313|EMBL:ALN81802.1, ECO:0000313|Proteomes:UP000060787} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=76 {ECO:0000313|EMBL:ALN81802.1, RC ECO:0000313|Proteomes:UP000060787}; RX PubMed=26597042; DOI=10.1186/s12864-015-2191-z; RA de Bruijn I., Cheng X., de Jager V., Exposito R.G., Watrous J., RA Patel N., Postma J., Dorrestein P.C., Kobayashi D., Raaijmakers J.M.; RT "Comparative genomics and metabolic profiling of the genus RT Lysobacter."; RL BMC Genomics 16:991-991(2015). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP011129; ALN81802.1; -; Genomic_DNA. DR RefSeq; WP_057918744.1; NZ_CP013141.1. DR EnsemblBacteria; ALN81802; ALN81802; LA76x_3680. DR KEGG; lab:LA76x_3680; -. DR KEGG; laq:GLA29479_840; -. DR PATRIC; fig|84531.7.peg.835; -. DR KO; K03665; -. DR Proteomes; UP000060787; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000060787}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000060787}. FT DOMAIN 199 364 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 158 192 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 432 AA; 47257 MW; 02E9E492541FE72B CRC64; MFERSRKGEH ALLIQPHAGG PPDEDLLEEF ADLARSAGAS VAAVLTARID RPNAATLIGS GKLDEVKAAA EASGADLILV NHPLSPGQER NLERFLERRV VDRTGLILDI FSQRAKSSEG KLQVELAQLK HMATRLVRGW THLERQRGGS IGLRGPGETQ LETDRRLLQK RLEQLQRRLD KVEVQRTQMR RARLRSELPR VALVGYTNAG KSTLFNAMTG AEAYAADQLF ATLDPTVRRI ELSGGAAVLA DTVGFVRDLP HGLVAAFRAT LSEAREADLL LHVIDAADPL RDERIAQVDA VLNEIGAGDL PQVLVFNKID RLDGVEPRID RPGEDSSRVW VSARDSQGLD LLRSALGEAL QLRHVAGSVR IAPQDARLRA RLHELGAVRS EQADEHGWLV EVDLAVADAQ RLFAQANGEA LRPLLEAVQA PT // ID A0A0S2EQ65_9RHIZ Unreviewed; 459 AA. AC A0A0S2EQ65; DT 17-FEB-2016, integrated into UniProtKB/TrEMBL. DT 17-FEB-2016, sequence version 1. DT 07-JUN-2017, entry version 10. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=M673_11340 {ECO:0000313|EMBL:ALN73313.1}; OS Aureimonas sp. AU20. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Aurantimonadaceae; Aureimonas. OX NCBI_TaxID=1349819 {ECO:0000313|EMBL:ALN73313.1, ECO:0000313|Proteomes:UP000060544}; RN [1] {ECO:0000313|EMBL:ALN73313.1, ECO:0000313|Proteomes:UP000060544} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=AU20 {ECO:0000313|EMBL:ALN73313.1, RC ECO:0000313|Proteomes:UP000060544}; RX PubMed=26534993; DOI=10.1073/pnas.1514326112; RA Anda M., Ohtsubo Y., Okubo T., Sugawara M., Nagata Y., Tsuda M., RA Minamisawa K., Mitsui H.; RT "Bacterial clade with the ribosomal RNA operon on a small plasmid RT rather than the chromosome."; RL Proc. Natl. Acad. Sci. U.S.A. 112:14343-14347(2015). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP006367; ALN73313.1; -; Genomic_DNA. DR EnsemblBacteria; ALN73313; ALN73313; M673_11340. DR KEGG; aua:M673_11340; -. DR PATRIC; fig|1349819.3.peg.2359; -. DR KO; K03665; -. DR Proteomes; UP000060544; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000060544}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}. FT DOMAIN 223 397 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 182 216 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 459 AA; 50702 MW; 8423F01A1BA35AF0 CRC64; MTEFDKASGS KGPIEHKQVA TRAGVFVPVL RERSRAEEGA DLVRRADEDR LIEAEGLAAA IDLHVVARGI IPVSKAQPAT LIGSGKVEEL KGLVAAEEIG LVIVDHPLTP VQQRNLEKEL NAKVLDRTGL ILEIFGRRAR TKEGRLQVEL AHLNYQRGRL VRSWTHLERQ RGGAGFLGGP GETQIEADRR QLQDKIKRLE KELDQVRKTR TLHRAKRKKT PHPVIALVGY TNAGKSTLFN TVTGADVLAK NLLFATLDPT LRRITLPHGT EVIMSDTVGF ISDLPTHLVA AFRATLEEVI EADIILHVRD MSDPDSLAQS ADVNKILKDL DVDVDDPDHV IEVWNKIDRL DESARVHLAQ TAASNAKGPS IHLASALTGE GVDALLAEIE RRIAGKAELL ELDVPSDSMT VLPWVYENSI VREREDLEDG GVHLVLDVTR QARSDLQRLG SRYPNLRID // ID A0A0S2I2T7_9BACT Unreviewed; 397 AA. AC A0A0S2I2T7; DT 17-FEB-2016, integrated into UniProtKB/TrEMBL. DT 17-FEB-2016, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:ALO16541.1}; GN ORFNames=L21SP5_02921 {ECO:0000313|EMBL:ALO16541.1}; OS Salinivirga cyanobacteriivorans. OC Bacteria; Bacteroidetes; Bacteroidia; Marinilabiliales; OC Salinivirgaceae; Salinivirga. OX NCBI_TaxID=1307839 {ECO:0000313|EMBL:ALO16541.1, ECO:0000313|Proteomes:UP000064893}; RN [1] {ECO:0000313|EMBL:ALO16541.1, ECO:0000313|Proteomes:UP000064893} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=L21-Spi-D4 {ECO:0000313|EMBL:ALO16541.1, RC ECO:0000313|Proteomes:UP000064893}; RA Spring S., Bunk B., Sproer C., Klenk H.-P.; RT "Description and complete genome sequence of a novel strain RT predominating in hypersaline microbial mats and representing a new RT family of the Bacteriodetes phylum."; RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP013118; ALO16541.1; -; Genomic_DNA. DR RefSeq; WP_057954911.1; NZ_CP013118.1. DR EnsemblBacteria; ALO16541; ALO16541; L21SP5_02921. DR KEGG; blq:L21SP5_02921; -. DR PATRIC; fig|1307839.3.peg.3067; -. DR KO; K03665; -. DR Proteomes; UP000064893; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000064893}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000064893}. FT DOMAIN 202 386 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 170 197 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 397 AA; 45773 MW; 4D875CF42D5EC7B8 CRC64; MKDIIEQKKV AETTVLVGII SQHQTEEQTE EYLNELAFLA KTAGVEPKKQ FTQKLDTPNP KTFIGSGKLN DIKNYMEEHE IDMVIFDDEL TPSQIRNIEK SIKGRVIDRT NLILDIFAQR AQTAHAKVQV ELAQYQYLLP RLAGLWTHLE RQKGGIGMRG PGEREIETDR RIIRDKIARL KDQLSKIDKQ MATQRKNRGK MVRVALVGYT NVGKSTLMNM LSKSEVFAEN KLFATLDTTV RKVVVGNLPF LMSDTVGFIR KLPTTLVEAF KSTLDEVREA DILLHVVDIS HPNHEEQIDV VETTLNEIGC TDTPTHLVFN KIDQYTYTAK EDDDLTERTR ENWTLDELQR SYMAKNNDSC IFISAKENTN IDQLKEMLYE KVKDIHTKRY PYNDFLY // ID A0A0S2JBY6_9GAMM Unreviewed; 428 AA. AC A0A0S2JBY6; DT 17-FEB-2016, integrated into UniProtKB/TrEMBL. DT 17-FEB-2016, sequence version 1. DT 30-AUG-2017, entry version 13. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=CMT41_01490 {ECO:0000313|EMBL:ALO33538.1}; OS Colwellia sp. MT41. OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales; OC Colwelliaceae; Colwellia. OX NCBI_TaxID=58049 {ECO:0000313|EMBL:ALO33538.1, ECO:0000313|Proteomes:UP000065319}; RN [1] {ECO:0000313|EMBL:ALO33538.1, ECO:0000313|Proteomes:UP000065319} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MT41 {ECO:0000313|EMBL:ALO33538.1, RC ECO:0000313|Proteomes:UP000065319}; RA Kyaw T.S., Ugalde J., Peoples L., Narasingarao P., Chastain R.A., RA Yayanos A., Methe B.A., Bartlett D.H.; RT "Distinctive Gene and Protein Characteristics of Extremely Piezophilic RT Colwellia."; RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP013145; ALO33538.1; -; Genomic_DNA. DR RefSeq; WP_058026158.1; NZ_CP013145.1. DR EnsemblBacteria; ALO33538; ALO33538; CMT41_01490. DR KEGG; com:CMT41_01490; -. DR KO; K03665; -. DR Proteomes; UP000065319; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000065319}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000065319}. FT DOMAIN 198 365 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 428 AA; 48768 MW; F71444A4A1704DCE CRC64; MFERYQAGEQ AVLVHIDFPD ESCKEDLNEF KMLVSSAGVQ ALTIVTGKRN KPDSRFFVGS GKAEEIRDAV HLVAANVILF NHSLTPSQEK NIEALCECRV IDRTTLILDI FAQRARTHEG KLQVELAQLR HMSSRLIRGW THLERQKGGI GLRGPGETQL ETDRRLLRER MVNIRKRLDK VEVQRQQGRR ARTRAELPTL SLVGYTNAGK STLFNTLTQS EVYAADKLFS TLDPTLRKMD LPGIGRVILA DTVGFIRHLP HDLVAAFKAT LTETREAELL LHVVDISDDR RSENIEQVEY VLKEIEANEV PQLVICNKID NLDDIEPRID RDEQGVPIRV WLSAQANIGI ELLFTALAER LDIEVVNHQL NIPPSAGKLR GELYKLNCIT HETFDEQGYC HLEVKMPSRE WQRLIATKYS ELVDYIVH // ID A0A0S2JGT9_9GAMM Unreviewed; 451 AA. AC A0A0S2JGT9; DT 17-FEB-2016, integrated into UniProtKB/TrEMBL. DT 17-FEB-2016, sequence version 1. DT 07-JUN-2017, entry version 12. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=CMT41_09310 {ECO:0000313|EMBL:ALO34894.1}; OS Colwellia sp. MT41. OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales; OC Colwelliaceae; Colwellia. OX NCBI_TaxID=58049 {ECO:0000313|EMBL:ALO34894.1, ECO:0000313|Proteomes:UP000065319}; RN [1] {ECO:0000313|EMBL:ALO34894.1, ECO:0000313|Proteomes:UP000065319} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MT41 {ECO:0000313|EMBL:ALO34894.1, RC ECO:0000313|Proteomes:UP000065319}; RA Kyaw T.S., Ugalde J., Peoples L., Narasingarao P., Chastain R.A., RA Yayanos A., Methe B.A., Bartlett D.H.; RT "Distinctive Gene and Protein Characteristics of Extremely Piezophilic RT Colwellia."; RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP013145; ALO34894.1; -; Genomic_DNA. DR RefSeq; WP_058027104.1; NZ_CP013145.1. DR EnsemblBacteria; ALO34894; ALO34894; CMT41_09310. DR KEGG; com:CMT41_09310; -. DR KO; K03665; -. DR Proteomes; UP000065319; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000065319}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000065319}. FT DOMAIN 231 396 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 192 226 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 451 AA; 49744 MW; 52AAD7018E0EEBC3 CRC64; MQLTAKASRT NALLISICTP DFKGDEATES LAELARLVTT LGFKVVGSQS QKQSSTKKIN VLGLGKLAEI AHLTGNKGEV NTEVEAGEVL PEEEVDETPF SDIPSDNLPF ACADVVVFDC DLSPSQLRNV ENQLGVEVFD RTGIIIEIFS RHARTKTAKL QVEIARLNYV APRLRETSCG DKERQMGKGA GETTLELNRR KVRDQLADLK RELVSVQDEM KGRRSQRAEL FCVALVGYTN AGKSSLMRAI TGSDVEGENK LFATLDTTVR ALFPISQPRI LVSDTVGFIK KLPHDLVASF HSTLAEAHDA SLLLYVVDAS DPSFRAQLDV VHGVLEEVGV EDSKKLLILN KSDQLSSEQQ QALMDEFPEA MMTSARDPAD ISKLHKYIVA IAQDEMIEEE IIVPYTANGI IGEIRSKMSV TKEEYESDHI KITVRSNAID LARLKKRMQS L // ID A0A0S2K4S5_9GAMM Unreviewed; 429 AA. AC A0A0S2K4S5; DT 17-FEB-2016, integrated into UniProtKB/TrEMBL. DT 17-FEB-2016, sequence version 1. DT 30-AUG-2017, entry version 12. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=PP2015_2828 {ECO:0000313|EMBL:ALO43313.1}; OS Pseudoalteromonas phenolica. OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales; OC Pseudoalteromonadaceae; Pseudoalteromonas. OX NCBI_TaxID=161398 {ECO:0000313|EMBL:ALO43313.1, ECO:0000313|Proteomes:UP000061457}; RN [1] {ECO:0000313|EMBL:ALO43313.1, ECO:0000313|Proteomes:UP000061457} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=KCTC 12086 {ECO:0000313|EMBL:ALO43313.1, RC ECO:0000313|Proteomes:UP000061457}; RA Zhang Y., Guo Z.; RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP013187; ALO43313.1; -; Genomic_DNA. DR RefSeq; WP_058030979.1; NZ_CP013187.1. DR EnsemblBacteria; ALO43313; ALO43313; PP2015_2828. DR KEGG; pphe:PP2015_2828; -. DR PATRIC; fig|161398.10.peg.2887; -. DR KO; K03665; -. DR Proteomes; UP000061457; Chromosome I. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000061457}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000061457}. FT DOMAIN 198 365 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 429 AA; 48525 MW; 7398861FD427341F CRC64; MFDRYEAGEQ AILVHIDFQN EGDREDLKEL EMLVSSAGVR SLAVVQGSRQ APDAKLFVGT GKAEEIAEIV KIHNADVIIF NHQLSPSQER NLESICKCRV LDRTTLILDI FAQRARTHEG KLQVELAQLR HISTRLIRGW THLERQKGGI GLRGPGETQL ETDRRLLRER IKSIRKRLEK VATVREQGRR ARSRNEVPTV SLVGYTNAGK SSLFNFVTDA EVYAADQLFA TLDPTLRKLE IDDIGPVIFA DTVGFIRHLP HDLVAAFKAT LTETREADLQ LHVIDVADNR RKENIEEVQS VLKEIEADEI PQLLVYNKID LLEDVKPRID FNDEGVPIRV WLSAQTGEGT ELLLEAISKL LAKKVFAHTL CVPPASGKLR GSLFNLNGVK QENYDEQGNW LLDVRIPQVD WERLKKEQGA NIEQFIVSD // ID A0A0S2KFX0_9GAMM Unreviewed; 422 AA. AC A0A0S2KFX0; DT 17-FEB-2016, integrated into UniProtKB/TrEMBL. DT 17-FEB-2016, sequence version 1. DT 30-AUG-2017, entry version 13. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=PS2015_2600 {ECO:0000313|EMBL:ALO47232.1}; OS Pseudohongiella spirulinae. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudohongiella. OX NCBI_TaxID=1249552 {ECO:0000313|EMBL:ALO47232.1, ECO:0000313|Proteomes:UP000065641}; RN [1] {ECO:0000313|EMBL:ALO47232.1, ECO:0000313|Proteomes:UP000065641} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=KCTC 32221 {ECO:0000313|EMBL:ALO47232.1, RC ECO:0000313|Proteomes:UP000065641}; RA Zhang Y., Guo Z.; RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP013189; ALO47232.1; -; Genomic_DNA. DR RefSeq; WP_058022641.1; NZ_CP013189.1. DR EnsemblBacteria; ALO47232; ALO47232; PS2015_2600. DR KEGG; pspi:PS2015_2600; -. DR PATRIC; fig|1249552.3.peg.2617; -. DR KO; K03665; -. DR Proteomes; UP000065641; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000065641}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000065641}. FT DOMAIN 199 366 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 422 AA; 47883 MW; FF98BF4444264543 CRC64; MFFERPEGGE SSVLVHIDLD SEREQEDPVE FEELVRSSGS EPVCFIKGSR KTPDARTFIG QGKLEEVAEA VRQHEAGLVL FNHSLSPSQE RNLEKALKCR VLDRTGLILD IFAQRARTYE GKLQVELAQL QHMVTRLKRG WTHLDRQKGG VNLRGAGETQ LELDQRMIRQ RIKNINKSLA KVRAQREQGR RSRKRAEVPI VSLVGYTNAG KSSLFNVMTE SHIYAADQLF ATLDATLRRI NVPSFGEAIL VDTVGFISHL PHKLVEAFRA TLEETSQADL LLHVVDIANE DHDYYIEQVH EVLTEIGADD IPTLQVLNKI DLLDGFESRI DRNDQGQPER VWISARDGLG IDLLLQAISE RLGHDIVNRQ LTLSPNQGKL RARLYERGAV TTEQVDDHGQ VVLSVRLPRQ DFDRLMQEDA RR // ID A0A0S2W521_9FIRM Unreviewed; 425 AA. AC A0A0S2W521; DT 17-FEB-2016, integrated into UniProtKB/TrEMBL. DT 17-FEB-2016, sequence version 1. DT 07-JUN-2017, entry version 12. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=IB211_01976c {ECO:0000313|EMBL:ALP94367.1}; OS Intestinimonas butyriciproducens. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Intestinimonas. OX NCBI_TaxID=1297617 {ECO:0000313|EMBL:ALP94367.1, ECO:0000313|Proteomes:UP000064844}; RN [1] {ECO:0000313|Proteomes:UP000064844} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=AF211 {ECO:0000313|Proteomes:UP000064844}; RA de Vos W.M., Bui N.T.P., Plugge C.M., Ritari J.; RT "A butyrogenic pathway from the amino acid lysine in a human gut RT commensal."; RL Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP011307; ALP94367.1; -; Genomic_DNA. DR RefSeq; WP_033116476.1; NZ_JPJD01000007.1. DR EnsemblBacteria; ALP94367; ALP94367; IB211_01976c. DR KEGG; ibu:IB211_01976c; -. DR PATRIC; fig|1297617.4.peg.2040; -. DR KO; K03665; -. DR Proteomes; UP000064844; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000064844}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000064844}. FT DOMAIN 210 371 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 169 203 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 425 AA; 46607 MW; 9BD9D212D9D55F59 CRC64; MTDHTTEEKI NRAVLVGLNA ACLSREENAT ESSMEELSAL LETAGGVCVG TVLQNKDAPD PRTFIGEGKA AEVKALAEAA GADMVILDNA LSPSQQRVLS EELGVAVMDR SALILDIFAQ RARTKEGRLQ VELAQYKYLL PRLTGMWGHL VRQTASGGKS PIGTRGPGET QLETDRRHIR KKIAKLEEDL EQVRRVRGVQ RERRIKNEVP VVAIVGYTNA GKSTLLNALT GSDIPANNRL FDTLDTTTRN LEISDTCTVL VSDTVGFISK LPHHLVEAFK ATLEELSFAD LLLHVIDASN PEWREQAAVV DALIRELGAE QTPRIEVFNK SDLYRGDIMP HGEDIVSISA RTGEGLDRLT SMIGDRLDGG AHRVTLRLPY DQGGVVDMLY REAKVERVEY GETIEVTAVC TAKILGQVSE FLWNG // ID A0A0S3F0P7_9SPHN Unreviewed; 441 AA. AC A0A0S3F0P7; DT 17-FEB-2016, integrated into UniProtKB/TrEMBL. DT 17-FEB-2016, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=ATN00_13935 {ECO:0000313|EMBL:ALR21228.1}; OS Sphingobium baderi. OC Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales; OC Sphingomonadaceae; Sphingobium. OX NCBI_TaxID=1332080 {ECO:0000313|EMBL:ALR21228.1, ECO:0000313|Proteomes:UP000056968}; RN [1] {ECO:0000313|EMBL:ALR21228.1, ECO:0000313|Proteomes:UP000056968} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DE-13 {ECO:0000313|EMBL:ALR21228.1, RC ECO:0000313|Proteomes:UP000056968}; RA Cheng M., Meng Q., Yang Y., Chu C., Yan X., He J., Li S.; RT "A Two-component Flavoprotein Monooxygenase System MeaXY Responsible RT for para-Hydroxylation of 2-Methyl-6-ethylaniline and 2,6- RT Diethylaniline in Sphingobium baderi DE-13."; RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP013264; ALR21228.1; -; Genomic_DNA. DR RefSeq; WP_062065740.1; NZ_CP013264.1. DR EnsemblBacteria; ALR21228; ALR21228; ATN00_13935. DR KEGG; sbd:ATN00_13935; -. DR KO; K03665; -. DR Proteomes; UP000056968; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000056968}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000056968}. FT DOMAIN 209 387 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 441 AA; 48272 MW; BC467F6D535681A7 CRC64; MATFNRDSSD EVTRGARAIV VRAETQGAER RDSDARLEEA KGLALAIGID VCAAQAFRVR DRKPATLFGS GQVDGITALA QAKQAELIIV DNALSPVQQS NLEKATSVKV IDRTGLILEI FGERAATNEG RLQVELAHLD YQAGRLVRSW THLERQRGGF GFLGGPGETQ IEADRRMIRD RMAKIRRELD QVTRTRGLHR ARRQRAPWPV IALVGYTNAG KSTLFNRLTG ADVMAQDLLF ATLDPTMRQI ALPGLDKAIL SDTVGFVSDL PTQLIAAFRA TLEEVLSADL IIHVRDIAHP DTEAQREDVM DVLRELGVTG ESAEEASDGP PLIIEAWNKL DLLDQETAAA TREIAERRND VVILSALTGE GIDTLQRTIG NLMTAGAAVH VLRVPSADGA ALAWLHEHGE VLSIRPEADE MIIEVRLSDS ALARFLKRNR T // ID A0A0S3FY65_9FLAO Unreviewed; 408 AA. AC A0A0S3FY65; DT 17-FEB-2016, integrated into UniProtKB/TrEMBL. DT 17-FEB-2016, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=ATE47_16435 {ECO:0000313|EMBL:ALR32008.1}; OS Chryseobacterium sp. IHB B 17019. OC Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales; OC Flavobacteriaceae; Chryseobacterium. OX NCBI_TaxID=1721091 {ECO:0000313|EMBL:ALR32008.1, ECO:0000313|Proteomes:UP000058667}; RN [1] {ECO:0000313|EMBL:ALR32008.1, ECO:0000313|Proteomes:UP000058667} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=IHB B 17019 {ECO:0000313|EMBL:ALR32008.1, RC ECO:0000313|Proteomes:UP000058667}; RA Swarnkar M.K., Rana A., Soni R., Shah M.A., Reshi Z.A., Singh A.K., RA Gulati A.; RT "Complete Genome Sequence of Chryseobacterium sp. IHB B 17019."; RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP013293; ALR32008.1; -; Genomic_DNA. DR RefSeq; WP_062162977.1; NZ_CP013293.1. DR EnsemblBacteria; ALR32008; ALR32008; ATE47_16435. DR KEGG; cih:ATE47_16435; -. DR KO; K03665; -. DR Proteomes; UP000058667; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000058667}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000058667}. FT DOMAIN 200 384 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 408 AA; 47589 MW; A0F001CCF757C788 CRC64; MLEKKEHNYE KAILVGVVTQ HQDEEKLQEY MDELEFLAFT AGATVDRRFT QKLTQPDSKT FIGSGKAQEI KEYVKENEIG TVIFDDELSP SQLKNLEREI EVKILDRTNL ILDIFAQRAQ TSYARTQVEL AQYQYLLPRL TRMWTHLERQ KGGIGMRGPG ETEIETDRRI IRDRISLLKD KLKTIDRQMA TQRNNRGKVV RAALVGYTNV GKSTLMNALS KSEVFAENKL FATLDTTVRK VVIGNLPFLL TDTVGFIRKL PTQLVESFKS TLDEVREADL LIHVVDISHE SFEDHIDSVN QILMEINAHQ KPMIMVFNKI DDFSYEKKDE DDLTPSTKRN ISLEEWTKTW MAKSKYPTVF ISALTKENFP EMKRMIYDEV MKIHISRFPY NDFLFEYFDN DEEEENKD // ID A0A0S3PD05_9NOSO Unreviewed; 528 AA. AC A0A0S3PD05; DT 17-FEB-2016, integrated into UniProtKB/TrEMBL. DT 17-FEB-2016, sequence version 1. DT 07-JUN-2017, entry version 12. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=NOS3756_24540 {ECO:0000313|EMBL:BAT53493.1}; OS Nostoc sp. NIES-3756. OC Bacteria; Cyanobacteria; Nostocales; Nostocaceae; Nostoc. OX NCBI_TaxID=1751286 {ECO:0000313|EMBL:BAT53493.1, ECO:0000313|Proteomes:UP000064670}; RN [1] {ECO:0000313|EMBL:BAT53493.1, ECO:0000313|Proteomes:UP000064670} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NIES-3756 {ECO:0000313|EMBL:BAT53493.1, RC ECO:0000313|Proteomes:UP000064670}; RX PubMed=26656223; DOI=10.1016/j.jbiotec.2015.12.002; RA Hirose Y., Fujisawa T., Ohtsubo Y., Katayama M., Misawa N., RA Wakazuki S., Shimura Y., Nakamura Y., Kawachi M., Yoshikawa H., RA Eki T., Kanesaki Y.; RT "Complete genome sequence of cyanobacterium Nostoc sp. NIES-3756, a RT potentially useful strain for phytochrome-based bioengineering."; RL J. Biotechnol. 218:51-52(2016). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AP017295; BAT53493.1; -; Genomic_DNA. DR RefSeq; WP_067768689.1; NZ_AP017295.1. DR EnsemblBacteria; BAT53493; BAT53493; NOS3756_24540. DR KEGG; non:NOS3756_24540; -. DR PATRIC; fig|1751286.4.peg.2576; -. DR KO; K03665; -. DR Proteomes; UP000064670; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000064670}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}. FT DOMAIN 355 525 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 314 348 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 528 AA; 58152 MW; CE2581BDA1797E94 CRC64; MCAYVNRRGQ VIRVGVGTPR QTQIPPMELP RYGAERLCGI RCISTHLKAE PPNDAALTAM AMQRLDALVV INITGTGFTR RGGGATGYVK EAYLAHLVPQ DARALTPSAA FSGSNNGQSA SWSISPPLDL DDLAQQDFLD LVEGLEEEFR REFVAQEVDA DHDRVLIVGV MTDNMSLQQF HDTVAELARL VDTAGGDVLQ TIQQKRSRIH PQTVIGEGKV QEVALTAQTL GCNLVVFDRD LSPSQVRNLE AQIGIRVVDR TEVILDIFAQ RAQSRAGKLQ VELAQLEYML PRLTGRGQAM SRLGGGIGTR GPGETKLETE RRAIQRRISR LQQEVDQLQA HRSRLRQRRQ HREVPSVALV GYTNAGKSTL LNALTNAEVY TADQLFATLD PTTRRLVIPH AETGQPQEIL ITDTVGFIHE LPASLMDAFR ATLEEVTEAD ALLHLVDLSH PAWLSHIRAV REILAQMPVT PGPALVAFNK IDQVDSATLA LAQEEFPLAV FISASQRLGL ETLRHRLGQL IEYAVDLR // ID A0A0S3QVR5_9AQUI Unreviewed; 540 AA. AC A0A0S3QVR5; DT 17-FEB-2016, integrated into UniProtKB/TrEMBL. DT 17-FEB-2016, sequence version 1. DT 07-JUN-2017, entry version 12. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:BAT72407.1}; GN ORFNames=TST_1623 {ECO:0000313|EMBL:BAT72407.1}; OS Thermosulfidibacter takaii ABI70S6. OC Bacteria; Aquificae; Aquificales. OX NCBI_TaxID=1298851 {ECO:0000313|EMBL:BAT72407.1, ECO:0000313|Proteomes:UP000063234}; RN [1] {ECO:0000313|EMBL:BAT72407.1, ECO:0000313|Proteomes:UP000063234} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ABI70S6 {ECO:0000313|EMBL:BAT72407.1, RC ECO:0000313|Proteomes:UP000063234}; RX PubMed=18319474; DOI=10.1099/ijs.0.65349-0; RA Nunoura T., Oida H., Miyazaki M., Suzuki Y.; RT "Thermosulfidibacter takaii gen. nov., sp. nov., a thermophilic, RT hydrogen-oxidizing, sulfur-reducing chemolithoautotroph isolated from RT a deep-sea hydrothermal field in the Southern Okinawa Trough."; RL Int. J. Syst. Evol. Microbiol. 58:659-665(2008). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AP013035; BAT72407.1; -; Genomic_DNA. DR RefSeq; WP_068550563.1; NZ_AP013035.1. DR EnsemblBacteria; BAT72407; BAT72407; TST_1623. DR KEGG; ttk:TST_1623; -. DR PATRIC; fig|1298851.3.peg.1701; -. DR KO; K03665; -. DR Proteomes; UP000063234; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000063234}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000063234}. FT DOMAIN 376 539 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 335 372 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 540 AA; 61503 MW; 0B3C3E29FA24415A CRC64; MARLFGELKG LQKSEIRALE RLYRRKLKDQ LLSSELARYL SQLSGEIGRQ IGLLVDRKGN ITHVIVGDRQ RIVIPDLSYF RYYPGRLKGV RCIHTHFGEK PLDEEDLTDL AMLRLDAMVV LSVEEDGLPG SVWMAYLLPP NPEGKRWDIM VWRHPSEINM NFPEFVSELE DQMLEEMALK SPKGEERAIL VSVTTASKHD AEHSMAELVR LAESAGVEVL DTVIQRVHRF NPKYLMGKGK IQELIIRALY LGASMLIFDN ELTPVQVNAI SELTDLKVID RTQLILDIFA KRAISREGKI QVELAQLRYM YPRILGKGEA MSRLAGGIGG RGPGETKLEI DRRRIRKRIQ VLEQQLEQLK RQRRERRKRR QKASVPVVSL VGYTNAGKTT LLNRLTGADA FAENKLFATL DPSNRVLWLP EVGECILTDT VGFIRNMPED LMVAFRATLE ELEDAFLIVH VVDITSPYME EEMETVEEIL RELELHLKPR LVVYNKADLL SEYERALSEK SGKLLISAKE GYGLDKLTAK ISEMLAGVAY // ID A0A0S4KVD7_9BACT Unreviewed; 574 AA. AC A0A0S4KVD7; DT 17-FEB-2016, integrated into UniProtKB/TrEMBL. DT 17-FEB-2016, sequence version 1. DT 07-JUN-2017, entry version 10. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:CUQ67759.1}; GN ORFNames=NITINOP_2787 {ECO:0000313|EMBL:CUQ67759.1}; OS Candidatus Nitrospira inopinata. OC Bacteria; Nitrospirae; Nitrospirales; Nitrospiraceae; Nitrospira. OX NCBI_TaxID=1715989 {ECO:0000313|EMBL:CUQ67759.1, ECO:0000313|Proteomes:UP000066284}; RN [1] {ECO:0000313|EMBL:CUQ67759.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ENR4 {ECO:0000313|EMBL:CUQ67759.1}; RA Jackson K.R., Lunt B.L., Fisher J.N.B., Gardner A.V., Bailey M.E., RA Deus L.M., Earl A.S., Gibby P.D., Hartmann K.A., Liu J.E., Manci A.M., RA Nielsen D.A., Solomon M.B., Breakwell D.P., Burnett S.H., Grose J.H.; RL Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LN885086; CUQ67759.1; -; Genomic_DNA. DR EnsemblBacteria; CUQ67759; CUQ67759; NITINOP_2787. DR KEGG; nio:NITINOP_2787; -. DR KO; K03665; -. DR Proteomes; UP000066284; Chromosome 1. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000066284}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000066284}. FT DOMAIN 389 553 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 348 375 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 574 AA; 64235 MW; 646E0C72422F29AC CRC64; MSEAFGERRL SIPEVRGQIA GLRPSQIAAI ERLYRRRVAA DQVLGSELAK TMSQLTLDVR RPIGVVLTRR GIVQEVIVGT DLCLTPATAA KFRAGPRSLR GLRFIRTQLH DQPLSQEAIT DLAYLRLDLI GTLSVSSEGT PGYLYLAHIL PPNGENRLCN VLGAVPFHRC AIRFDRFIEE LEAKVQAARS HQVIKNGHEA AMLVSASPRG RGEQEERLAE LAELARSAGV TVIDRVVQRT DEGHQRYLLG SGKLKEVLIR TLHQGADMVI IDQTLTPAQS RAIAEMTDIK VIDRTQLILD IFARRAHSRE GKVQVELAQL RYLLPRLSGK GADLSRLGGG IGARGPGETK LETDRRRIRD RITRLERELE LFSKQQDRRR VRRRRYGLPI VSLVGYTNAG KSTLLNQLTG SCVSAKDRLF ETLDTTSRRL RFPRDREIII TDTVGFIRDL PQELVRTFRA TLEGLREADL LLHVVDAGVT DIDMQIAAVA DIVRDLDLDE IPRVLVFNKC DRLPAQQVEL LCRRYRAIGI SALQPHTWPP LLEVIEKAAS RSIPGHQEGP STYVSQESAD LVFH // ID A0A0S4NYY3_9BURK Unreviewed; 415 AA. AC A0A0S4NYY3; DT 17-FEB-2016, integrated into UniProtKB/TrEMBL. DT 17-FEB-2016, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=BN2497_3873 {ECO:0000313|EMBL:CUI04548.1}, GN BN3177_3873 {ECO:0000313|EMBL:CUU28334.1}; OS Janthinobacterium sp. CG23_2. OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Oxalobacteraceae; Janthinobacterium. OX NCBI_TaxID=1706231 {ECO:0000313|EMBL:CUU28334.1, ECO:0000313|Proteomes:UP000052254}; RN [1] {ECO:0000313|EMBL:CUI04548.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=CG23-2 {ECO:0000313|EMBL:CUI04548.1}; RA Jackson K.R., Lunt B.L., Fisher J.N.B., Gardner A.V., Bailey M.E., RA Deus L.M., Earl A.S., Gibby P.D., Hartmann K.A., Liu J.E., Manci A.M., RA Nielsen D.A., Solomon M.B., Breakwell D.P., Burnett S.H., Grose J.H.; RL Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:CUU28334.1, ECO:0000313|Proteomes:UP000052254} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Janthinobacterium sp. CG23_25 {ECO:0000313|EMBL:CUU28334.1}; RA Zhang Y., Guo Z.; RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CYSS01000001; CUI04548.1; -; Genomic_DNA. DR EMBL; FAOS01000001; CUU28334.1; -; Genomic_DNA. DR RefSeq; WP_054263766.1; NZ_FAOS01000001.1. DR EnsemblBacteria; CUU28334; CUU28334; BN3177_3873. DR Proteomes; UP000052254; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000052254}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000052254}. FT DOMAIN 190 357 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 156 183 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 415 AA; 45084 MW; 67E8BCDC4A0F2CAF CRC64; MRAALVGIDF GAGDFNASVE ELSLLARSAG ADPITTITAK RSSPDAAYFV GSGKADEIGL ACVDQNIEIV IFNHALSPAQ QRNLEKRLNI RVLDRTSLIL DIFAQRAKSH EGKLQVELAQ LQHLATRLIR GWTHLERQKG GIGLRGPGET QLETDRRLIG ERVKALRARL AKLRKQHETQ RRSRGRSHTF SVSLVGYTNA GKSTLFNALT KAGVYVANQL FATLDTTSRR VYLGEEVGNV VMSDTVGFVR ELPHQLVAAF RATLEETIHA DLLLHVVDGA SPVRMEQIEQ VNLVLKEIGA DHIPQILVWN KIDAAGLEPA VERDEAGNIA RVFISAHTGA GLDMLREAVV EAARAAPARS HLFEEQDDAE PDDAPDGDDA DDASDPDDAD DADDADDAQD AQPAEILNST IVGPR // ID A0A0S4Q1Y6_BLAVI Unreviewed; 437 AA. AC A0A0S4Q1Y6; DT 17-FEB-2016, integrated into UniProtKB/TrEMBL. DT 17-FEB-2016, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:CUU42348.1}; GN ORFNames=BVIRIDIS_13570 {ECO:0000313|EMBL:CUU42348.1}; OS Blastochloris viridis (Rhodopseudomonas viridis). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Hyphomicrobiaceae; Blastochloris. OX NCBI_TaxID=1079 {ECO:0000313|EMBL:CUU42348.1, ECO:0000313|Proteomes:UP000065734}; RN [1] {ECO:0000313|Proteomes:UP000065734} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 19567 / DSM 133 / F {ECO:0000313|Proteomes:UP000065734}; RX PubMed=26798090; DOI=10.1128/genomeA.01520-15; RA Liu L.N., Faulkner M., Liu X., Huang F., Darby A.C., Hall N.; RT "Revised genome sequence of the purple photosynthetic bacterium RT Blastochloris viridis."; RL Genome Announc. 4:0-0(2016). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LN907867; CUU42348.1; -; Genomic_DNA. DR EnsemblBacteria; CUU42348; CUU42348; BVIRIDIS_13570. DR PATRIC; fig|1079.7.peg.1410; -. DR Proteomes; UP000065734; Chromosome I. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000065734}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000065734}. FT DOMAIN 205 379 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 437 AA; 48001 MW; 1C1258251F64100E CRC64; MAPTRAAVLV PVRSRDRSRA GAAGSTRTPD ARLDEATGLA AAIDLDVVVA TLVPLADVRP ATFLGKGKVE ELAGLIEAER IDLAYVDASL SPVQQRNLER AWKTKVIDRT ALILEIFGRR ARTREGTLQV ELAHLNYQKS RLVRSWTHLE RQRGGFGFLG GPGETQIETD RRLIGERIIS IERELEQVTR TRALHRKSRE RVPFPVVALV GYTNAGKSTL FNRLTRAEVF AENLLFATLD PTLRAVGLPH GTRIILSDTV GFISELPTTL VAAFRATLEE VIEADLILHV RDVAHIDTAA QAADVADVLG ELGIDSDDHA RIVEVWNKVD LIEGEARAQL DAEAARRPAE QQPALVSALS GEGVEALLDR IETRITAGRI TRTVSLAPED GQGLAWLYRH ADVIERSGDA ETGRTLVTVR VSPERLEEID RRFPPNP // ID A0A0S6VZ90_9BACT Unreviewed; 573 AA. AC A0A0S6VZ90; DT 17-FEB-2016, integrated into UniProtKB/TrEMBL. DT 17-FEB-2016, sequence version 1. DT 12-APR-2017, entry version 10. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=U14_02079 {ECO:0000313|EMBL:GAK50838.1}; OS Candidatus Moduliflexus flocculans. OC Bacteria. OX NCBI_TaxID=1499966 {ECO:0000313|EMBL:GAK50838.1, ECO:0000313|Proteomes:UP000030700}; RN [1] {ECO:0000313|EMBL:GAK50838.1, ECO:0000313|Proteomes:UP000030700} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Sekiguchi Y., Ohashi A., Parks D.H., Yamauchi T., Tyson G.W., RA Hugenholtz P.; RT "First genomic representation of candidate bacterial phylum KSB3 RT points to enhanced environmental sensing as a trigger of wastewater RT bulking."; RL PeerJ 3:e740-e740(2015). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; DF820456; GAK50838.1; -; Genomic_DNA. DR EnsemblBacteria; GAK50838; GAK50838; U14_02079. DR Proteomes; UP000030700; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000030700}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000030700}. FT DOMAIN 387 573 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 346 380 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 573 AA; 65608 MW; 8753FDD3F1C19DA3 CRC64; MQFVAIPPPI RKIHGNLTGL KPNQLDRLER IYRRKIPTDQ VITQELANYL TELSAEIARQ IGVLVNRKGA VEDVIIGDHR QIEIPPLGRF RAGYLRLRGL RYLHTHLADT PLSQEDLTDL ALLRFDLVGA IAVNQYGLPA KYYFAHLVPE NPDQKRWEVL APIYPGQVEM QFDEFIHALE EEFQRGREGR EVDDSRERAV LVGVSNGQRA LAEESLRELR ELADSAGLIV MDSVLQHRPK IDPKFMIGKG KLDELIIRCF QLGADMLIFD HDLTPAQNKM ISEVTELKII DRTQLILDIF AQRAHSRVGK LQVELAQLKY QLPRLGTRDD ALSRITGGIG ARGPGETKLE IDRRRARDRI RNLEKELEHL RKGRHQRRAK RQRNDVPIIS IVGYTNAGKS TLLNALTHSE VEVKNQMFAT LDPTSRRLRF PKDIEVIITD TVGFLRDLPK DLIEAFRATL EELEDADLLL HVVDISNPEF EEQIAAVQTI LEELELQEIP QLMVFNKEDL VEPRFTETVC ARYDGVSISA IQRPSLRKLV LRVQDEILRL YPSQDKYPQL KTDLRQENSV VPA // ID A0A0S6X5L0_9SPHN Unreviewed; 448 AA. AC A0A0S6X5L0; DT 17-FEB-2016, integrated into UniProtKB/TrEMBL. DT 17-FEB-2016, sequence version 1. DT 05-JUL-2017, entry version 12. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=MBENS4_3674 {ECO:0000313|EMBL:GAM06678.1}; OS Novosphingobium sp. MBES04. OC Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales; OC Sphingomonadaceae; Novosphingobium. OX NCBI_TaxID=1206458 {ECO:0000313|EMBL:GAM06678.1, ECO:0000313|Proteomes:UP000053513}; RN [1] {ECO:0000313|Proteomes:UP000053513} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MBES04 {ECO:0000313|Proteomes:UP000053513}; RA Ohta Y., Nishi S., Kobayashi K., Tsubouchi T., Iida K., Tanizaki A., RA Kurosawa K., Adachi A., Nishihara M., Sato R., Hasegawa R., Hatada Y.; RT "Draft Genome Sequence of Novosphingobium sp. Strain MBES04, Isolated RT from Sunken Wood from Suruga Bay, Japan."; RL Genome Announc. 3:e01373-14(2015). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; DF850489; GAM06678.1; -; Genomic_DNA. DR Proteomes; UP000053513; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000053513}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000053513}. FT DOMAIN 209 392 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 448 AA; 49710 MW; E0C067C5764D319B CRC64; MDDELKGEVT RGARALVVYP HMRGNRGSAD LDPEARLEEA KGLALAIGLV IADGQIIPIR EPRAGTLFGE GQIENISVAC NLHEAELVVV DGSLTAIQQR NLEEKLKRKV IDRTGLILEI FGERAATAEG RLQVELAHLD YQAGRLVRSW THLERQRGGF GFLGGPGETQ IEADRRMIRD RMGRLRRELE QVRRTRGLHR DRREKAPWPI VALVGYTNAG KSTLFNRVTG ADVMAEDLLF ATLDPTMRAV RLPGVQKAIL SDTVGFISDL PTQLVAAFRA TLEEVTAADV ILHVRDIANP DTESQKRQVL SVLSDLGVIP REDDEEEPGE EPTIPIIEVW NKWDLLSPER AEELREVIDY RSDETIIPLS AVTGEGCEHL LDVVGHGLNA DAKVYTFVLP AADGQRLAFL HARGEVLSEV ADGEDENGPR IRIEVRLAER ELGRFRAL // ID A0A0S7BM34_9CHLR Unreviewed; 445 AA. AC A0A0S7BM34; DT 17-FEB-2016, integrated into UniProtKB/TrEMBL. DT 17-FEB-2016, sequence version 1. DT 07-JUN-2017, entry version 12. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=LARV_02613 {ECO:0000313|EMBL:GAP14837.1}; OS Longilinea arvoryzae. OC Bacteria; Chloroflexi; Anaerolineae; Anaerolineales; Anaerolineaceae; OC Longilinea. OX NCBI_TaxID=360412 {ECO:0000313|EMBL:GAP14837.1, ECO:0000313|Proteomes:UP000055060}; RN [1] {ECO:0000313|EMBL:GAP14837.1, ECO:0000313|Proteomes:UP000055060} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=KOME-1 {ECO:0000313|EMBL:GAP14837.1, RC ECO:0000313|Proteomes:UP000055060}; RA Sekiguchi Y., Ohashi A., Matsuura N., Tourlousse M.D.; RT "Draft Genome Sequences of Anaerolinea thermolimosa IMO-1, Bellilinea RT caldifistulae GOMI-1, Leptolinea tardivitalis YMTK-2, Levilinea RT saccharolytica KIBI-1,Longilinea arvoryzae KOME-1, Previously RT Described as Members of the Anaerolineaceae (Chloroflexi)."; RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; DF967972; GAP14837.1; -; Genomic_DNA. DR RefSeq; WP_075074064.1; NZ_DF967972.1. DR EnsemblBacteria; GAP14837; GAP14837; LARV_02613. DR Proteomes; UP000055060; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000055060}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000055060}. FT DOMAIN 219 385 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 185 212 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 445 AA; 49453 MW; 50DCF77E946305FD CRC64; MSKRVSEPTA PPVERAFLVG VEVKSQPGLL SLEDSLSELS LLCETAGLEV VGETKQRLDT PHPNTYIGSG KVEEIRLLVE ETLSNVVVFD TELSPTHQRE LEEKLGDNVR VLDRTAIILD IFAQHANTRE GKLQVELAQY EYRLPRLTRA WTHLARQAGG GGGRTGSVGG VGLRGPGETQ LEVDRRDIHR RISALKKELE NVRAHRSRHR DQRRRTQIPV IALVGYTNAG KSTLLNHLSK ADVYVADKLF ATLDPTTRRV ELPGGHWVLM TDTVGFIQKL PTQLIAAFRA TLEEITEADL LIHLVDATHP NAHVQWDSVK ETLSAIDAGN IPMITALNKI DQLSDPEEAQ RLTTEYEDAI AISALKGAGI QNLLSSIERE LFETFVPVTV YLPFQEGQLI SLFHEQGQIA TTENTRTGVT IQGNLPGRLI ARYQPFFERP KSTEE // ID A0A0S7BQZ0_9CHLR Unreviewed; 454 AA. AC A0A0S7BQZ0; DT 17-FEB-2016, integrated into UniProtKB/TrEMBL. DT 17-FEB-2016, sequence version 1. DT 07-JUN-2017, entry version 12. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=ATC1_13674 {ECO:0000313|EMBL:GAP40695.1}; OS Flexilinea flocculi. OC Bacteria; Chloroflexi; Anaerolineae; Anaerolineales; Anaerolineaceae; OC Flexilinea. OX NCBI_TaxID=1678840 {ECO:0000313|EMBL:GAP40695.1, ECO:0000313|Proteomes:UP000053370}; RN [1] {ECO:0000313|EMBL:GAP40695.1, ECO:0000313|Proteomes:UP000053370} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=TC1 {ECO:0000313|EMBL:GAP40695.1, RC ECO:0000313|Proteomes:UP000053370}; RA Matsuura N., Tourlousse D.M., Sun L., Toyonaga M., Kuroda K., RA Ohashi A., Cruz R., Yamaguchi T., Sekiguchi Y.; RT "Draft Genome Sequence of Anaerolineae Strain TC1, a Novel Isolate RT from a Methanogenic Wastewater Treatment System."; RL Genome Announc. 3:e01104-15(2015). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; DF968181; GAP40695.1; -; Genomic_DNA. DR RefSeq; WP_062280396.1; NZ_DF968181.1. DR EnsemblBacteria; GAP40695; GAP40695; ATC1_13674. DR PATRIC; fig|1678840.3.peg.2020; -. DR Proteomes; UP000053370; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000053370}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000053370}. FT DOMAIN 219 386 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 178 212 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 454 AA; 50472 MW; DA9C61801F86E6AA CRC64; MAENILRSTN ERKERAFLVG VEIKNEPSIL SLSDSLEELA LLADTAGLEV VGETSQKLER PHASTYIGSG KVEEVAALAE ETLADIILFD NELSPRHLRE LSLRFGKSVR IIDRTTLILD IFAQHATTKE GRLQVELAQH EYRLPRLSHA WSHLERQAGG ASGRSGSAGG VGLRGPGETQ LEVDKREIRK RIAFLKKEIE KVSDHRKRYR AQRKRSQIPV VALVGYTNSG KSTLLNSLAD ADVYVADQLF ATLDPTTRRV MLPGSHLCLF TDTVGFIQKL PTQLIAAFRS TLEEINEADL LLHVIDVSHF NAAAQYESVQ ATLAEIEADH IPVISVFNKA DLLEDAEEAK QLLAETDPDA FLISAKTGQG MEALKAGIME QLYEKMLPIR VRLPFTEGAL IAQFHEQGSI DLIENFQNGV MIQGSIPGRL ITRFQNFVDK PTHQETDRPI FPED // ID A0A0S7BZP7_9BACT Unreviewed; 394 AA. AC A0A0S7BZP7; DT 17-FEB-2016, integrated into UniProtKB/TrEMBL. DT 17-FEB-2016, sequence version 1. DT 07-JUN-2017, entry version 12. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=TBC1_11249 {ECO:0000313|EMBL:GAP42120.1}; OS Lentimicrobium saccharophilum. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; OC Lentimicrobiaceae; Lentimicrobium. OX NCBI_TaxID=1678841 {ECO:0000313|EMBL:GAP42120.1, ECO:0000313|Proteomes:UP000053091}; RN [1] {ECO:0000313|Proteomes:UP000053091} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=TBC1 {ECO:0000313|Proteomes:UP000053091}; RA Tourlousse D.M., Matsuura N., Sun L., Toyonaga M., Kuroda K., RA Ohashi A., Cruz R., Yamaguchi T., Sekiguchi Y.; RT "Draft Genome Sequence of Bacteroidales Strain TBC1, a Novel Isolate RT from a Methanogenic Wastewater Treatment System."; RL Genome Announc. 3:e01168-15(2015). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; DF968182; GAP42120.1; -; Genomic_DNA. DR RefSeq; WP_062037341.1; NZ_DF968182.1. DR EnsemblBacteria; GAP42120; GAP42120; TBC1_11249. DR PATRIC; fig|1678841.3.peg.288; -. DR Proteomes; UP000053091; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000053091}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000053091}. FT DOMAIN 199 383 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 394 AA; 45110 MW; D4C2029EF9798BC4 CRC64; MIEITHITET AVLVGLITFR QDEARVHETL DELEFLFETA GGTAVKRFIQ KLEKPDTRTF VGSGKLDEIK AFITVENVGT VVFDDELSPS QLRNIEKELQ CKVLDRTTLI LDIFARRART ATARTQVELA QYQYLLPRLS RMWTHLEKQR GGIGMRGPGE KEIETDRRII RDKIALLKEK LKDIDKQKIT QRSGRERLVR VALIGYTNVG KSTLMNLLSK SDVFAENKLF ATLDTTVRKV VIDNLPFLLT DTVGFIRKLP HGLVESFKST LDELREADLL LHVVDISHPG FEDQIAVVNQ TLSEIKAGDK PVMMVFNKVD AYTFVEKDET DLSPATRENI TLDELKRTWI AKVNSPAQFI SATKKLHLEE FKNALYKTVH DIHIVRYPYN RLLY // ID A0A0S7CR70_9MICC Unreviewed; 395 AA. AC A0A0S7CR70; DT 17-FEB-2016, integrated into UniProtKB/TrEMBL. DT 17-FEB-2016, sequence version 1. DT 12-APR-2017, entry version 9. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=AHiyo1_10720 {ECO:0000313|EMBL:GAP58092.1}; OS Arthrobacter sp. Hiyo1. OC Bacteria; Actinobacteria; Micrococcales; Micrococcaceae; Arthrobacter. OX NCBI_TaxID=1588020 {ECO:0000313|EMBL:GAP58092.1, ECO:0000313|Proteomes:UP000063628}; RN [1] {ECO:0000313|EMBL:GAP58092.1, ECO:0000313|Proteomes:UP000063628} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Hiyo1 {ECO:0000313|EMBL:GAP58092.1, RC ECO:0000313|Proteomes:UP000063628}; RX PubMed=26764021; DOI=10.1186/s12864-016-2380-4; RA Hiraoka S., Machiyama A., Ijichi M., Inoue K., Oshima K., Hattori M., RA Yoshizawa S., Kogure K., Iwasaki W.; RT "Genomic and metagenomic analysis of microbes in a soil environment RT affected by the 2011 Great East Japan Earthquake tsunami."; RL BMC Genomics 17:53-53(2016). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; DF952469; GAP58092.1; -; Genomic_DNA. DR Proteomes; UP000063628; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000063628}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000063628}. FT DOMAIN 174 339 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 395 AA; 42877 MW; DA65599A9472901A CRC64; MAETAGSEVL DGIVQRRMKP DPGTFLGSGK AMELKDIVMS TGADTVVVDA ELAPSQRRGL EDIVKVKVVD RTTLILDIFA QHAKSREGKA QVELAQLEYL LPRLRGWGDS MSRQAGGQVG GAGAGMGSRG PGETKIELDR RRIRTRMAKL RREIAAMKPS RETKRANRRR NAVPSVAIAG YTNAGKSSLL NRLTDAGVLV ENALFATLDP TVRKAQTPDG IGYTLSDTVG FVRSLPTQLV EAFRSTLEEV ADADLILHVV DVSHPDPEGQ IAAVRTVFSE VDARKIPEII VLNKADAADP FVIERLKQKE PRHVVVSTRT GQGIAELLGA ISEAIPRPGV RLEVLIPYNR GELINKLHNT DAEILSLEHE EEGTRVVAMV HENLAAELES FVSNG // ID A0A0S7WMY3_9CHLR Unreviewed; 400 AA. AC A0A0S7WMY3; DT 17-FEB-2016, integrated into UniProtKB/TrEMBL. DT 17-FEB-2016, sequence version 1. DT 07-JUN-2017, entry version 10. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=AMJ38_00290 {ECO:0000313|EMBL:KPJ51512.1}; OS Dehalococcoidia bacterium DG_22. OC Bacteria; Chloroflexi; Dehalococcoidia. OX NCBI_TaxID=1703393 {ECO:0000313|EMBL:KPJ51512.1, ECO:0000313|Proteomes:UP000054105}; RN [1] {ECO:0000313|EMBL:KPJ51512.1, ECO:0000313|Proteomes:UP000054105} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DG_22 {ECO:0000313|EMBL:KPJ51512.1}; RX PubMed=25922666; DOI=10.1186/s40168-015-0077-6; RA Baker B.J., Lazar C.S., Teske A.P., Dick G.J.; RT "Genomic resolution of linkages in carbon, nitrogen, and sulfur RT cycling among widespread estuary sediment bacteria."; RL Microbiome 3:14-14(2015). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KPJ51512.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LIZQ01000005; KPJ51512.1; -; Genomic_DNA. DR PATRIC; fig|1703393.3.peg.940; -. DR Proteomes; UP000054105; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000054105}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000054105}. FT DOMAIN 207 385 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 166 200 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 400 AA; 44059 MW; 99DEF8ECF37CD9C4 CRC64; MATTGHVTAE PIERAYLVAV EIKGRGNSRW TSQSSLEELA QLALTAGASV VGRCIQRLER PTSAYYVGRG KVQELASLRH RLGYGTIIFD EELSPSQQRN LEDALQIKVL DRTALILDIF AQHARTREGA LQVELAQHEY LLPRLAGQWT HLERLEGAIG TRGPGETQLE TDRRLIRRKI QHLKRQLEEV RRQRALYRRR RARQRVPVIS LVGYTNAGKS TLMRALSGAD VLVEDKLFAT LDPVTRRVAL PQGGAFLLTD TVGFIQNLPT QLVAAFRATL EELSEASLLL HVVDITHPDA AEQAQTVEDT LADLGLADKP SITVLNKADL ICGPDGLPIE GLEDLSDVRA SLRYWRPDAL LVSAVKGWGL TDLLGRIEAA LGLGEGSEAA SWGYRVRPAG // ID A0A0S7WQY0_9BACT Unreviewed; 436 AA. AC A0A0S7WQY0; DT 17-FEB-2016, integrated into UniProtKB/TrEMBL. DT 17-FEB-2016, sequence version 1. DT 07-JUN-2017, entry version 10. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=AMJ39_07425 {ECO:0000313|EMBL:KPJ52608.1}; OS candidate division TA06 bacterium DG_24. OC Bacteria; candidate division TA06. OX NCBI_TaxID=1703770 {ECO:0000313|EMBL:KPJ52608.1, ECO:0000313|Proteomes:UP000052008}; RN [1] {ECO:0000313|EMBL:KPJ52608.1, ECO:0000313|Proteomes:UP000052008} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DG_24 {ECO:0000313|EMBL:KPJ52608.1}; RX PubMed=25922666; DOI=10.1186/s40168-015-0077-6; RA Baker B.J., Lazar C.S., Teske A.P., Dick G.J.; RT "Genomic resolution of linkages in carbon, nitrogen, and sulfur RT cycling among widespread estuary sediment bacteria."; RL Microbiome 3:14-14(2015). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KPJ52608.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LIZS01000050; KPJ52608.1; -; Genomic_DNA. DR PATRIC; fig|1703770.3.peg.1867; -. DR Proteomes; UP000052008; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000052008}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000052008}. FT DOMAIN 201 367 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 162 189 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 436 AA; 48441 MW; EFB879E110107E7D CRC64; MHPIETTTRA ERALLVGLAL SDRERWEKIE SLDELAQLAA TAGAEVAEKI LQTRRKPDPA YLIGKGKVDE LAKAAQEIPV DLLIFDEELS PAQVRNIESV TETRVVDRSE LIMDIFAIHA RSRAAKIQVE LAQLNYRLPR LVGRGVELSR LGGGIGTRGP GETKLEVDRR RIRARIAQLK RDLTSLETSR MVQRQGRGDA FRVALAGYTN AGKSTLMNAL SSAGVTVADQ LFATLDATTR QIDLGTRRDI LLTDTVGFIR HLPHHLVASF HATLEETIEA DLILHVVDVS HTAYRQQMAT VDEVLSELGC IDTSTLVVFN KIDQLEDQSC LDLIRSRYPM SVAASALTGV GIETVKARIV ALAEDMDREE VLFLPLDATK LLAQVHRDGR IIEEIFEDSR IQVRVRMDRA KLSRLQREIA DAWARAQDRP GAGEQD // ID A0A0S7X3R1_9BACT Unreviewed; 439 AA. AC A0A0S7X3R1; DT 17-FEB-2016, integrated into UniProtKB/TrEMBL. DT 17-FEB-2016, sequence version 1. DT 07-JUN-2017, entry version 9. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=AMS16_01625 {ECO:0000313|EMBL:KPJ57018.1}; OS Planctomycetes bacterium DG_58. OC Bacteria; Planctomycetes. OX NCBI_TaxID=1703415 {ECO:0000313|EMBL:KPJ57018.1, ECO:0000313|Proteomes:UP000052181}; RN [1] {ECO:0000313|EMBL:KPJ57018.1, ECO:0000313|Proteomes:UP000052181} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DG_58 {ECO:0000313|EMBL:KPJ57018.1}; RX PubMed=25922666; DOI=10.1186/s40168-015-0077-6; RA Baker B.J., Lazar C.S., Teske A.P., Dick G.J.; RT "Genomic resolution of linkages in carbon, nitrogen, and sulfur RT cycling among widespread estuary sediment bacteria."; RL Microbiome 3:14-14(2015). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KPJ57018.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LJMZ01000027; KPJ57018.1; -; Genomic_DNA. DR PATRIC; fig|1703415.3.peg.1525; -. DR Proteomes; UP000052181; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000052181}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000052181}. FT DOMAIN 203 369 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 164 191 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 439 AA; 49456 MW; DE0B6DA890B622DA CRC64; MVELKRTRLS VRREQALLLG VMLPADKHRA AKPLAELASL ARTAGARVVG EVVQQLKRFH PSTWIGRGKA QEVHDRAKSL DADVVICDGD LSPAQVRNLE KITDTKVVDR SELILDIFAT HARTKQARLQ VELAQLEYTY PRLARMWTHL SRYEGGIGTR GPGEMQLETD RRLVQRRIRD LKRELGRIDA RRQREVKSRG ECFKVGIVGY TNAGKSTLMN ALTDAGVRVE DQLFATLDTK TRRWDLGDHG EALLSDTVGF IRHLPHHLVA SFKATLEEAT LADLLLHIVD ISRADAIEQA DAVMEVLEEI GCRDKRILAV FNKVDAADDE TALHILSERF RNGVTVSALK KQGLDRLTEA VVAELQRDFA ELVVTFPSSD GRLAAFLFEK GDVLERDDQD TVTQMRVKLH RRFLADLSEH DGVEVRVSDG KEEPRAERY // ID A0A0S7X5B2_9DELT Unreviewed; 420 AA. AC A0A0S7X5B2; DT 17-FEB-2016, integrated into UniProtKB/TrEMBL. DT 17-FEB-2016, sequence version 1. DT 07-JUN-2017, entry version 10. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=AMJ42_04730 {ECO:0000313|EMBL:KPJ57395.1}; OS Deltaproteobacteria bacterium DG_8. OC Bacteria; Proteobacteria; Deltaproteobacteria. OX NCBI_TaxID=1703397 {ECO:0000313|EMBL:KPJ57395.1, ECO:0000313|Proteomes:UP000051875}; RN [1] {ECO:0000313|EMBL:KPJ57395.1, ECO:0000313|Proteomes:UP000051875} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DG_8 {ECO:0000313|EMBL:KPJ57395.1}; RX PubMed=25922666; DOI=10.1186/s40168-015-0077-6; RA Baker B.J., Lazar C.S., Teske A.P., Dick G.J.; RT "Genomic resolution of linkages in carbon, nitrogen, and sulfur RT cycling among widespread estuary sediment bacteria."; RL Microbiome 3:14-14(2015). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KPJ57395.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LIZV01000128; KPJ57395.1; -; Genomic_DNA. DR PATRIC; fig|1703397.3.peg.845; -. DR Proteomes; UP000051875; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000051875}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000051875}. FT DOMAIN 200 366 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 159 186 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 420 AA; 46918 MW; B00A87EEDE5F0709 CRC64; MDNFKHKEKA LLIGTRNGSR MEWEAEDSLE ELSRLAETAG ARVDGTIVQE LKKIDSSLFM GKGKVEEVRD LVSSHDIDLV IFDDELTSTQ QRNLEEIFNT KTIDRTGLIL DIFAQRAKSK EGKLQVELAQ LTYTLPRLTG KGVVLSRLGG GIGTRGPGET QLEVDRRRIK ERITRLKREI DKVRKVRELH RKGRRSISKL NIALIGYTNA GKSTLLNYLS HTGVLAENRL FSSLDPKVGK FSLPNSQEVF ISDTVGFINK LPHQLIAAFK ATFEEVKESD VLLHVIDMSN PHFEAQINAV NKVLEEIGVL PKKIIHVVNK IDSVTHKKMI SAWVKKLENG VAVSALTGEG IDRLLSIIEG FVATSMQRVK LKIPFDAGKT IGQILGKSKI ITKKYLDTGV IIEAEVHRTL LDSLKPYLQA // ID A0A0S7X6B4_9BACT Unreviewed; 445 AA. AC A0A0S7X6B4; DT 17-FEB-2016, integrated into UniProtKB/TrEMBL. DT 17-FEB-2016, sequence version 1. DT 07-JUN-2017, entry version 9. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=AMS15_09390 {ECO:0000313|EMBL:KPJ57981.1}; OS Planctomycetes bacterium DG_23. OC Bacteria; Planctomycetes. OX NCBI_TaxID=1703414 {ECO:0000313|EMBL:KPJ57981.1, ECO:0000313|Proteomes:UP000052166}; RN [1] {ECO:0000313|EMBL:KPJ57981.1, ECO:0000313|Proteomes:UP000052166} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DG_23 {ECO:0000313|EMBL:KPJ57981.1}; RX PubMed=25922666; DOI=10.1186/s40168-015-0077-6; RA Baker B.J., Lazar C.S., Teske A.P., Dick G.J.; RT "Genomic resolution of linkages in carbon, nitrogen, and sulfur RT cycling among widespread estuary sediment bacteria."; RL Microbiome 3:14-14(2015). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KPJ57981.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LIZR01000159; KPJ57981.1; -; Genomic_DNA. DR PATRIC; fig|1703414.3.peg.1137; -. DR Proteomes; UP000052166; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000052166}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000052166}. FT DOMAIN 202 368 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 163 197 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 445 AA; 49945 MW; D8343399127F0DCF CRC64; MVRPNRKQLS VAKERAILVG LVPPGEDWKE ELLNELASLA RTAGAVVVDK VPQVRSRIDP AYYIGKGKAA ELAQKARAAD VDTVIFDNDL SPAQVRNLEQ LTQAKVIDRS ELILDIFSTH ARTRQAKIQV ELAQLEYTLP RLRGMWTHLS RFEGGIGTRG PGEQQLEVDR RIASRRINEL KKRLKKIERR KVSEVTKRSP ELSVSLVGYT NAGKSTLMNA LTDAGMLVED KLFATLDTRT RRWVLPGGKK VLLSDTVGFI RGLPHHLIAA FRATLEEARN ADILLHIADL GSRQVLHQVA IVEEVLKNLG CKDVPTILVL NKVDIMADPV DLEILKRKYP ENVVISALTG ERLEDLRERI IDYLERGWQH FRIFCTPDDG RVLAYLYENG EVLSKSFGNE ENEFLVRLHP DYVVGLKRLN GSVRVNEWVP SGPSPSSPRS AEQSG // ID A0A0S7XE79_9BACT Unreviewed; 424 AA. AC A0A0S7XE79; DT 17-FEB-2016, integrated into UniProtKB/TrEMBL. DT 17-FEB-2016, sequence version 1. DT 07-JUN-2017, entry version 10. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=AMJ46_05525 {ECO:0000313|EMBL:KPJ60712.1}; OS Latescibacteria bacterium DG_63. OC Bacteria; Candidatus Latescibacteria. OX NCBI_TaxID=1703781 {ECO:0000313|EMBL:KPJ60712.1, ECO:0000313|Proteomes:UP000051457}; RN [1] {ECO:0000313|EMBL:KPJ60712.1, ECO:0000313|Proteomes:UP000051457} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DG_63 {ECO:0000313|EMBL:KPJ60712.1}; RX PubMed=25922666; DOI=10.1186/s40168-015-0077-6; RA Baker B.J., Lazar C.S., Teske A.P., Dick G.J.; RT "Genomic resolution of linkages in carbon, nitrogen, and sulfur RT cycling among widespread estuary sediment bacteria."; RL Microbiome 3:14-14(2015). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KPJ60712.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LJNC01000008; KPJ60712.1; -; Genomic_DNA. DR PATRIC; fig|1703781.3.peg.736; -. DR Proteomes; UP000051457; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000051457}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000051457}. FT DOMAIN 201 366 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 424 AA; 47622 MW; CD33FB221979D5B2 CRC64; MNIYTPAEDT RPERAILVGL RDSKGNETND SLKELGLLVD TAGGLVAGSL LQKRKSVSPR TFLGKGKVDE LKGLIRQHSA DVVVFDEDLS PGQVRNLEKE LGIKVVDRSE VILHIFALRA RTREARVQVE LAQLEYQLPR LTRLWKHLSR LGGGIGTRGP GETQLEVDRR RVRERIATLK KHLAGVEKER RVQRRKREDI FKVSIVGYTN AGKTTLFKAL TEAQAFVEDR LFATVDATTR RLRAERTSPV VITDTVGFIR KLPHHLVTSF RATLEEVVQA DLLVHVVDSS SSSASHQMEI VEEVLTEMGA GAKPTIVALN KTDIAEEESL QGLRYKCPLA VEISALRKHN VSSLVTRILQ AARSEKSLAT VEIPLTEKRL ISQLRRSCEF VKERMLTDKV RIQLWAGRRE LGKLTRRGFS VRTN // ID A0A0S7XN83_9BACT Unreviewed; 437 AA. AC A0A0S7XN83; DT 17-FEB-2016, integrated into UniProtKB/TrEMBL. DT 17-FEB-2016, sequence version 1. DT 07-JUN-2017, entry version 9. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=AMJ44_13675 {ECO:0000313|EMBL:KPJ63949.1}; OS candidate division WOR_1 bacterium DG_54_3. OC Bacteria; candidate division WOR-1. OX NCBI_TaxID=1703775 {ECO:0000313|EMBL:KPJ63949.1, ECO:0000313|Proteomes:UP000051861}; RN [1] {ECO:0000313|EMBL:KPJ63949.1, ECO:0000313|Proteomes:UP000051861} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DG_54_3 {ECO:0000313|EMBL:KPJ63949.1}; RX PubMed=25922666; DOI=10.1186/s40168-015-0077-6; RA Baker B.J., Lazar C.S., Teske A.P., Dick G.J.; RT "Genomic resolution of linkages in carbon, nitrogen, and sulfur RT cycling among widespread estuary sediment bacteria."; RL Microbiome 3:14-14(2015). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KPJ63949.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LIZX01000209; KPJ63949.1; -; Genomic_DNA. DR PATRIC; fig|1703775.3.peg.2050; -. DR Proteomes; UP000051861; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000051861}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000051861}. FT DOMAIN 201 375 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 437 AA; 49621 MW; 14E7DD639EC09F8B CRC64; MFEVAKLKTK EKAILVGVKL PSVSRFTLEE SLQELVLLTE TAGGEVLQTV IQERQKLNPT FFIGKGKTNQ IKSLSQRLGA NILIFDDDLT PAQVYNLEKT LDIKVIDRSW LILDIFAKRA RSKEAKVQVE LAQLKYLLPR LTRGWTHLSR QWGGIGTKGP GETQLEMDRR RVRRKILELE KGLLKIDKER SVQRRRRESI FKVTLVGYTN VGKSTLFNQL TSSSVFVEEK LFATLDSTTR LLRVSGNGKL KETAKIVITD TIGFIRKLPQ HLVASFKSTL DEVRLADLLL HVVDISHPDF LQHIAKVNQV LSELDSLDKP TIMTYNKIDK LPQAYTLNFP SASHQENGRI LVSARDDIGI GDLAERIVNF AKGDWAEAWL YVGNGNSDLL PHVYKIGIVT ESKFEKEGIR LRIKGKRENL QKIRKLNSEL KLKFLAT // ID A0A0S7XVP3_9COXI Unreviewed; 437 AA. AC A0A0S7XVP3; DT 17-FEB-2016, integrated into UniProtKB/TrEMBL. DT 17-FEB-2016, sequence version 1. DT 07-JUN-2017, entry version 9. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=AMJ43_09585 {ECO:0000313|EMBL:KPJ65948.1}; OS Coxiella sp. DG_40. OC Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales; OC Coxiellaceae; Coxiella. OX NCBI_TaxID=1703354 {ECO:0000313|EMBL:KPJ65948.1, ECO:0000313|Proteomes:UP000051153}; RN [1] {ECO:0000313|EMBL:KPJ65948.1, ECO:0000313|Proteomes:UP000051153} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DG_40 {ECO:0000313|EMBL:KPJ65948.1}; RX PubMed=25922666; DOI=10.1186/s40168-015-0077-6; RA Baker B.J., Lazar C.S., Teske A.P., Dick G.J.; RT "Genomic resolution of linkages in carbon, nitrogen, and sulfur RT cycling among widespread estuary sediment bacteria."; RL Microbiome 3:14-14(2015). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KPJ65948.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LIZW01000047; KPJ65948.1; -; Genomic_DNA. DR PATRIC; fig|1703354.3.peg.2014; -. DR Proteomes; UP000051153; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000051153}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000051153}. FT DOMAIN 211 377 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 437 AA; 48348 MW; 4FCB8A9E4D287728 CRC64; MEKMRKTLRV RKERAILVAA IQHSGSDGDD LAELTALAES AGAIVVDRFQ QKIRTINPAK YIGKGKAEQL RERVKRFKAD VVIFDNDLLP RQIRELEEII QVKVLDRSEL ILDIFATRAK TRQAKLQVEL AQLEYTYPRL TKMWSHLDSL AGAGGGTAAG TVGGIGTRGP GEQQLEIDRR LVSKRITELK RELTNIDKRR VREINGRKGL FKICLVGYTN AGKSTILNAL TNAGVFVEDR LFATLDTRTR KWNLGRGAEV LLSDTVGFVK NLPHQLVASF KATLEEAVNA DLLLHIVDVA NPDALQQIES VNKVLEEIGC GERPTLEVFN KVDIITKVGE LEMLQTLFPD AVCVSAKTGL GLERLNDVVS AKYKGAELLL RVASSQSNGK VQSFLRAHGQ IIKEQYLDGS VLIDVRLGRN QLAGLKRLGA EKIDIVS // ID A0A0S7XYV3_9COXI Unreviewed; 418 AA. AC A0A0S7XYV3; DT 17-FEB-2016, integrated into UniProtKB/TrEMBL. DT 17-FEB-2016, sequence version 1. DT 30-AUG-2017, entry version 10. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=AMJ43_03245 {ECO:0000313|EMBL:KPJ67666.1}; OS Coxiella sp. DG_40. OC Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales; OC Coxiellaceae; Coxiella. OX NCBI_TaxID=1703354 {ECO:0000313|EMBL:KPJ67666.1, ECO:0000313|Proteomes:UP000051153}; RN [1] {ECO:0000313|EMBL:KPJ67666.1, ECO:0000313|Proteomes:UP000051153} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DG_40 {ECO:0000313|EMBL:KPJ67666.1}; RX PubMed=25922666; DOI=10.1186/s40168-015-0077-6; RA Baker B.J., Lazar C.S., Teske A.P., Dick G.J.; RT "Genomic resolution of linkages in carbon, nitrogen, and sulfur RT cycling among widespread estuary sediment bacteria."; RL Microbiome 3:14-14(2015). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KPJ67666.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LIZW01000012; KPJ67666.1; -; Genomic_DNA. DR PATRIC; fig|1703354.3.peg.206; -. DR Proteomes; UP000051153; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000051153}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000051153}. FT DOMAIN 197 365 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 418 AA; 47586 MW; ADC5572D0D94788E CRC64; MQRGFTNRVV LVHIDFSNYK ISNEDIGEFH ELVKATDIEI VSLITFRSEA PRPRYFIGSG KAEEIRILVE VEKANLVIFN CILTPSQERN LERLFQCRVM DRIGLILDIF AQRARSFEGR LQVELAQLQY LSTRLIRGWS HLERQKGGIG LRGPGETQLE LDRRSITNRI KVIKKRLQKV RLGRQQARRA RQHSEIPIVS LVGYTNVGKS TLFNKLTAAD VHIADQLFAT LDPVLRRIEL SEVGPIILVD TVGFIRHLPT GLIEAFQATL EETMAGDLLL HVVDASDPLR REKIAAVNNV LQQINAQKIP QLLVYNKIDL TKDNISRINY DNFNSNPKSV KISAVTGEGL DLLLGALKIL LFGEIKEYKF TLKPSDGKLR AALYRLGTVL SEKISRDGNW QLIVRLKKQD FERLFANF // ID A0A0S7YRF6_9DELT Unreviewed; 551 AA. AC A0A0S7YRF6; DT 17-FEB-2016, integrated into UniProtKB/TrEMBL. DT 17-FEB-2016, sequence version 1. DT 07-JUN-2017, entry version 9. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=AMJ54_09090 {ECO:0000313|EMBL:KPJ77157.1}; OS Deltaproteobacteria bacterium SG8_13. OC Bacteria; Proteobacteria; Deltaproteobacteria. OX NCBI_TaxID=1703398 {ECO:0000313|EMBL:KPJ77157.1, ECO:0000313|Proteomes:UP000051346}; RN [1] {ECO:0000313|EMBL:KPJ77157.1, ECO:0000313|Proteomes:UP000051346} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SG8_13 {ECO:0000313|EMBL:KPJ77157.1}; RX PubMed=25922666; DOI=10.1186/s40168-015-0077-6; RA Baker B.J., Lazar C.S., Teske A.P., Dick G.J.; RT "Genomic resolution of linkages in carbon, nitrogen, and sulfur RT cycling among widespread estuary sediment bacteria."; RL Microbiome 3:14-14(2015). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KPJ77157.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LJNK01000027; KPJ77157.1; -; Genomic_DNA. DR PATRIC; fig|1703398.3.peg.2705; -. DR Proteomes; UP000051346; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000051346}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000051346}. FT DOMAIN 378 543 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 551 AA; 62026 MW; B7376B24BDF7CB84 CRC64; MKRLYGNTGG LKAGQLRRLE KLYRRRIPPE NAISFELAKD ISRLSGEIRR QVGLLIDRSG KIIRVLVGDH RQIVIPDVSE YRLAAGRLRG LRCMHTHING EPLTKDDLTD LALLRLDLMG VVSVEHDGQP PRIYLAHILP SSSSDQPYRL LPPFRAHETH VRCLQTVRAL EDELASVRAL HRGEGRKERA LLVSVTDAST RSDSDGLDEL RELAVSCGIT VVGNVVQHRR EADSRFLLGR GKLEELTLAV LAKGATLIIF DQELNPSQIR SITNQIDIKV IDRTMLILDI FAQRAQSREG KLQVELAQLK YLLPRLATKN TAMSRLTGGI GGRGPGETKL EINRRRTRDR IANLERSLGL VRKQRKQRRA RRSKKQLPII SIVGYTNAGK STLLNTLTKS RALVENRLFA TLDPSSRRLR FPQDIEVIIT DTVGFIKDLP RDLVVAFRAT LEELESADLL LHVIDISNPR FMDQIRSVET ILTDLQLQDI AMIRVLNKQD LVDPETARQV TRRFNGIPVS ATRSSTLLPL IEEMQGRIVQ SSSDHHPVNP A // ID A0A0S8A3V2_9GAMM Unreviewed; 435 AA. AC A0A0S8A3V2; DT 17-FEB-2016, integrated into UniProtKB/TrEMBL. DT 17-FEB-2016, sequence version 1. DT 07-JUN-2017, entry version 10. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=AMJ55_07430 {ECO:0000313|EMBL:KPJ93795.1}; OS Gammaproteobacteria bacterium SG8_15. OC Bacteria; Proteobacteria; Gammaproteobacteria. OX NCBI_TaxID=1703403 {ECO:0000313|EMBL:KPJ93795.1, ECO:0000313|Proteomes:UP000053644}; RN [1] {ECO:0000313|EMBL:KPJ93795.1, ECO:0000313|Proteomes:UP000053644} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SG8_15 {ECO:0000313|EMBL:KPJ93795.1}; RX PubMed=25922666; DOI=10.1186/s40168-015-0077-6; RA Baker B.J., Lazar C.S., Teske A.P., Dick G.J.; RT "Genomic resolution of linkages in carbon, nitrogen, and sulfur RT cycling among widespread estuary sediment bacteria."; RL Microbiome 3:14-14(2015). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KPJ93795.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LJNL01000118; KPJ93795.1; -; Genomic_DNA. DR PATRIC; fig|1703403.3.peg.502; -. DR Proteomes; UP000053644; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000053644}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000053644}. FT DOMAIN 198 365 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 435 AA; 48871 MW; 77D18A7BC45A43DC CRC64; MFDRPQNGES AVLVYANFSS RLSGEEIEEF HELAKSAGVD PVGTVTSARK IQDPRYLIGE AKAEEIRQVI AATKADVVLV DSTLTPSQER NLEKFLQCRV LDRTGLILDI FAQRATTHEG RLQVELAQLQ HLSTRLVRGW THLERQKGGI GLRGPGETQL ETDRRLVGIR IKQLKKRLEK VHKRRQQGRR ARKNADISTV SLVGYTNAGK STLFNRLTAA GVYAEDQLFA TLDPTLRRCD LGDNNAVILA DTVGFIRHLP HDLVEAFHST LEETQEADLL LHVIDASYAD YQDTIKQVNA VLKEIDASTI PQLQVFNKLD RVDGGEPRID YDEAGLPTRV WVSAQTGEGI HLLLTAIKAL CFNETIHQWI RVPVTNGRLR SKLYLQGKVL RECSDESGDL LLEVQITRRN LEAIQQKEGV VLEKEMDKQI INYCG // ID A0A0S8B382_9CHLR Unreviewed; 445 AA. AC A0A0S8B382; DT 17-FEB-2016, integrated into UniProtKB/TrEMBL. DT 17-FEB-2016, sequence version 1. DT 07-JUN-2017, entry version 9. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=AMJ56_15010 {ECO:0000313|EMBL:KPK06072.1}; OS Anaerolineae bacterium SG8_19. OC Bacteria; Chloroflexi; Anaerolineae; unclassified Anaerolineae. OX NCBI_TaxID=1703386 {ECO:0000313|EMBL:KPK06072.1, ECO:0000313|Proteomes:UP000050892}; RN [1] {ECO:0000313|EMBL:KPK06072.1, ECO:0000313|Proteomes:UP000050892} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SG8_19 {ECO:0000313|EMBL:KPK06072.1}; RX PubMed=25922666; DOI=10.1186/s40168-015-0077-6; RA Baker B.J., Lazar C.S., Teske A.P., Dick G.J.; RT "Genomic resolution of linkages in carbon, nitrogen, and sulfur RT cycling among widespread estuary sediment bacteria."; RL Microbiome 3:14-14(2015). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KPK06072.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LJNN01000216; KPK06072.1; -; Genomic_DNA. DR PATRIC; fig|1703386.3.peg.685; -. DR Proteomes; UP000050892; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000050892}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000050892}. FT DOMAIN 220 386 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 445 AA; 49084 MW; 865DDF97F94BE66A CRC64; MEVSINKQLF DIIPPREKAF LVGVELKGSR PLLSVHDSLA ELSLLAKTAG LEVVGQASQL LDRPDSATYI GSGKLEEIKA LTTELDVDVV IFDDELLPRH QRELEKTFGE EVRVLDRTAL ILDIFALHAS TREGKLQVEL AQLEYRLPRL TRMWTHLARQ AGGRAGGEGG GVGLRGPGET QLEVDRQEIG RRISTVKAEL EAVRAHRGRY RAKRKQTEIQ VVAIVGYTNS GKSTLLNQLS NADVLSADML FATLDPTTRR VTMPGGREVL FTDTVGFIQK LPTNIVAAFR ATLEEITEAD MLLHVVDVTH PHVAAQIESV EDILAELEVD HLPEIVALNK IDRLPDDVNP AAGLDLPSIA VPISAITGEG IEALLMAIEA TIEQQLEPLT VKLPYDRGDL MSLFHERGQV SSEEHLADGI MIYGRLPERL VPYFDCYRLS PDTIK // ID A0A0S8BFZ0_9PROT Unreviewed; 422 AA. AC A0A0S8BFZ0; DT 17-FEB-2016, integrated into UniProtKB/TrEMBL. DT 17-FEB-2016, sequence version 1. DT 07-JUN-2017, entry version 10. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=AMJ68_08880 {ECO:0000313|EMBL:KPK10543.1}; OS Acidithiobacillales bacterium SG8_45. OC Bacteria; Proteobacteria; Acidithiobacillia; Acidithiobacillales. OX NCBI_TaxID=1703383 {ECO:0000313|EMBL:KPK10543.1, ECO:0000313|Proteomes:UP000053136}; RN [1] {ECO:0000313|EMBL:KPK10543.1, ECO:0000313|Proteomes:UP000053136} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SG8_45 {ECO:0000313|EMBL:KPK10543.1}; RX PubMed=25922666; DOI=10.1186/s40168-015-0077-6; RA Baker B.J., Lazar C.S., Teske A.P., Dick G.J.; RT "Genomic resolution of linkages in carbon, nitrogen, and sulfur RT cycling among widespread estuary sediment bacteria."; RL Microbiome 3:14-14(2015). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KPK10543.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LJTU01000044; KPK10543.1; -; Genomic_DNA. DR PATRIC; fig|1703383.3.peg.1396; -. DR Proteomes; UP000053136; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000053136}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000053136}. FT DOMAIN 183 345 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 142 169 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 422 AA; 47891 MW; B7FB4087C312A35E CRC64; MRLPGGPDDE DLTEFRFLAE SAGAEVRGTI LGRRNRPDPA FFIGKGKAEE IQQRVETDEI ELVLVDHDLS PIQERNLEKA VGCRVLDRTG LILDIFALRA RSHEGKLQVE LAQLDRLATR LVRGWTHLER QKGGIGLRGP GETQLETDRR LMRDRIRRLN KRLEKVRNQR GLRRKNRNKI PIPTISLVGY TNAGKSTLFN RLTGASVYEA DQLFATLDPT MRRLDLAGKE QVILADTVGF IRHLPHTLVE AFKSTLEEVT EASLLIHVVD SHHPESAELM SHVNQVLKEI DADELPQIVV YNKIDLTGES PRLERDQNGA IRKVWLSART GEGTELLLRA LSEHYRKNRH FCRLHLPPAA ARLRAHLYDR VDVLAERGDG EGGFIIELTL EQRDIDWLRK QIGFEEGFLE QAQDSELAPV AS // ID A0A0S8BPB8_9PROT Unreviewed; 410 AA. AC A0A0S8BPB8; DT 17-FEB-2016, integrated into UniProtKB/TrEMBL. DT 17-FEB-2016, sequence version 1. DT 07-JUN-2017, entry version 8. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=AMJ67_17605 {ECO:0000313|EMBL:KPK13427.1}; OS Betaproteobacteria bacterium SG8_41. OC Bacteria; Proteobacteria; Betaproteobacteria. OX NCBI_TaxID=1703391 {ECO:0000313|EMBL:KPK13427.1, ECO:0000313|Proteomes:UP000051544}; RN [1] {ECO:0000313|EMBL:KPK13427.1, ECO:0000313|Proteomes:UP000051544} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SG8_41 {ECO:0000313|EMBL:KPK13427.1}; RX PubMed=25922666; DOI=10.1186/s40168-015-0077-6; RA Baker B.J., Lazar C.S., Teske A.P., Dick G.J.; RT "Genomic resolution of linkages in carbon, nitrogen, and sulfur RT cycling among widespread estuary sediment bacteria."; RL Microbiome 3:14-14(2015). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KPK13427.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LJTT01000147; KPK13427.1; -; Genomic_DNA. DR PATRIC; fig|1703391.3.peg.642; -. DR Proteomes; UP000051544; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 2. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000051544}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000051544}. FT DOMAIN 184 335 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 410 AA; 45944 MW; 21E25B2B77DD789C CRC64; MREAASSRRA GRPAERALLV QLRLDGRNVD EDAEELRLLA LSAGADVRGT IFGSRQIPDA ATFVGKGKAE EIREAVAREQ TDLIVVNHEL SPAQERNLEK LVGCRVLDRT GLILDIFAQR ARSHEGKLQV ELAQLEHLAT RLVRGWTHLE RQKGGIGLRG PGETQLEVDR RLIRDRIKKL HERLFNHLTG AGVYAADQLF ATLDPTMRRL ELSGNANIIL TDTVGFVRHL PHDLVEAFKS TLEEVAEANL LLHVVDASSS ERIEQMQQVN IVLTEIAASE IPQIVIFNKI DLSGEAPHSE RDAAGRIARI WLSARTGQGV ELLRDALSEH YRRTRQLLRL HLPPAAGRLR ALLYERFDVR GEEQIESGGW RIDVELDAAK LEWLQRQAEF DPSFIVQEKP RVLAPTGSCP // ID A0A0S8C873_9PROT Unreviewed; 375 AA. AC A0A0S8C873; DT 17-FEB-2016, integrated into UniProtKB/TrEMBL. DT 17-FEB-2016, sequence version 1. DT 07-JUN-2017, entry version 9. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=AMJ67_03215 {ECO:0000313|EMBL:KPK20053.1}; OS Betaproteobacteria bacterium SG8_41. OC Bacteria; Proteobacteria; Betaproteobacteria. OX NCBI_TaxID=1703391 {ECO:0000313|EMBL:KPK20053.1, ECO:0000313|Proteomes:UP000051544}; RN [1] {ECO:0000313|EMBL:KPK20053.1, ECO:0000313|Proteomes:UP000051544} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SG8_41 {ECO:0000313|EMBL:KPK20053.1}; RX PubMed=25922666; DOI=10.1186/s40168-015-0077-6; RA Baker B.J., Lazar C.S., Teske A.P., Dick G.J.; RT "Genomic resolution of linkages in carbon, nitrogen, and sulfur RT cycling among widespread estuary sediment bacteria."; RL Microbiome 3:14-14(2015). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KPK20053.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LJTT01000007; KPK20053.1; -; Genomic_DNA. DR PATRIC; fig|1703391.3.peg.1518; -. DR Proteomes; UP000051544; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000051544}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000051544}. FT DOMAIN 198 364 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 375 AA; 41139 MW; 216D93347D1DF111 CRC64; MFDRPGTGTD AVLVGLDLGA ADYAEGLEEI QLLASSAGVM ARALVKGRRA RPDAAFFAGK GKVEEIRRVV AESGARLVIF NHELSPIQER NLERALDCRV VDRVSLILDI FAQRARTHEG KLQVELAQLE HLATRLVRGW THLERQRGGI GLRGPGETQL ETDRRLLGKR VKVLKEKLAK VRAQRTVQRR ARRRSNLLQA SLVGYTNAGK STLFNRIARA DVFAMDRLFA TLDTTTRRVH TANGAGVALS DTVGFIRRLP HTLVAAFRAT LEETAEASML LHVVDASSAD RAAQIAAVDQ VLAEIGAEEI PQVLVMNKID LTRLPARVER DQYGRISRVW VSAKTGDGIE GVRLALEEYV DQALAPAQIN QTAAA // ID A0A0S8CXY5_9DELT Unreviewed; 558 AA. AC A0A0S8CXY5; DT 17-FEB-2016, integrated into UniProtKB/TrEMBL. DT 17-FEB-2016, sequence version 1. DT 07-JUN-2017, entry version 9. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=AMJ61_00930 {ECO:0000313|EMBL:KPK28857.1}; OS Desulfobacterales bacterium SG8_35_2. OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfobacterales. OX NCBI_TaxID=1703401 {ECO:0000313|EMBL:KPK28857.1, ECO:0000313|Proteomes:UP000051714}; RN [1] {ECO:0000313|EMBL:KPK28857.1, ECO:0000313|Proteomes:UP000051714} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SG8_35_2 {ECO:0000313|EMBL:KPK28857.1}; RX PubMed=25922666; DOI=10.1186/s40168-015-0077-6; RA Baker B.J., Lazar C.S., Teske A.P., Dick G.J.; RT "Genomic resolution of linkages in carbon, nitrogen, and sulfur RT cycling among widespread estuary sediment bacteria."; RL Microbiome 3:14-14(2015). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KPK28857.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LJTL01000002; KPK28857.1; -; Genomic_DNA. DR PATRIC; fig|1703401.3.peg.988; -. DR Proteomes; UP000051714; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000051714}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000051714}. FT DOMAIN 382 558 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 558 AA; 62586 MW; EB4B6FB3A4207C0D CRC64; MSKVVGNTGG LKTAQLKHLE RLGKKRIAPD LIVSHEMARS MAEISHITGR QVGVLIDRSG RVDMVIVGDA RQIVIPALSG IRSSGGRLKG LRCIHTHLAG ENLTDDDLVD LLFLRLDLMG ILKIRPDGQP EKLYSAHLVP SPRDGKNWAF LEAIAPGQQS FDFNELITAL EQEFSRLQPI REVDRGKDRA ILISVVTPSR IQSRISAQES MDELVELARS DDVVVLDTVM QQRSKINPKY ILGKGKLGEI MLSALRLNAN LLLFNQELNP SQIRSITDHL ELRVIDRTQL ILDIFARRAL SREGRLQIEM AQLKYMLPRL TKRDDALSRL TGGIGGRGPG ETRLEIDRRR INDRIALLTK KLNKVSRERY QRRSRRRKKG IPVISLVGYT NAGKSTLLNT LTASEISAEN KLFATLDPTS RRLRFPKDIE VIITDTVGFI RNLPAELLQA FKATLEELYE ADMLVHVIDV SNPRFANQVA VVEKQLRELE LDNIPCLKVL NKADLVEKKF TEKQCREYGA VALSALDVKT FGPFFDAAQK IIGRLGNQAD SESRLSVN // ID A0A0S8D7I9_9BACT Unreviewed; 417 AA. AC A0A0S8D7I9; DT 17-FEB-2016, integrated into UniProtKB/TrEMBL. DT 17-FEB-2016, sequence version 1. DT 07-JUN-2017, entry version 9. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=AMS24_04965 {ECO:0000313|EMBL:KPK32104.1}; OS Chlamydiae bacterium SM23_39. OC Bacteria; Chlamydiae. OX NCBI_TaxID=1704235 {ECO:0000313|EMBL:KPK32104.1, ECO:0000313|Proteomes:UP000051986}; RN [1] {ECO:0000313|EMBL:KPK32104.1, ECO:0000313|Proteomes:UP000051986} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SM23_39 {ECO:0000313|EMBL:KPK32104.1}; RX PubMed=25922666; DOI=10.1186/s40168-015-0077-6; RA Baker B.J., Lazar C.S., Teske A.P., Dick G.J.; RT "Genomic resolution of linkages in carbon, nitrogen, and sulfur RT cycling among widespread estuary sediment bacteria."; RL Microbiome 3:14-14(2015). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KPK32104.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LJUH01000052; KPK32104.1; -; Genomic_DNA. DR PATRIC; fig|1704235.3.peg.429; -. DR Proteomes; UP000051986; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000051986}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000051986}. FT DOMAIN 198 364 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 157 198 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 417 AA; 48765 MW; 98D68E3BB97C392F CRC64; MKNRSTAILI GVYGNSRDRE ICEDHLLELE SLGKTYGLIT TYKICFFVKK KDPATLIKRG AIDKILNILN ESELFYVIFD DEISPTQQRN LEKELKKTVI DRTELILGVF DKHAKTKEAK IQISLAQARY QLPRLKRLWT HLERQRMKGG YLKGMGERQL EVDKRILKSE ISKLKKRLKE IEKKRATQRK KRIREENLIF SIVGYTNSGK STLLNALTKA DVLVEDKLFS TLDTTTKRFI LPNKQKILFI DTVGFIRKLP HDLIASFKST LEEIVYSDVL INVIDLSDKN VFEKIESSLD VLKKLKVEDK PIIYVFNKID KVKDHSLIKK LKERYPTSVK ISALKKIGFD DFLKIIMDSI KFKIKKFKLK IPQNEVKLIN ELIEKGNITS KKYKDNYLFL EVEIPKTLFY KIERFII // ID A0A0S8D8U3_9PROT Unreviewed; 345 AA. AC A0A0S8D8U3; DT 17-FEB-2016, integrated into UniProtKB/TrEMBL. DT 17-FEB-2016, sequence version 1. DT 07-JUN-2017, entry version 7. DE SubName: Full=GTP-binding protein HflX {ECO:0000313|EMBL:KPK32209.1}; DE Flags: Fragment; GN ORFNames=AMJ66_06975 {ECO:0000313|EMBL:KPK32209.1}; OS Betaproteobacteria bacterium SG8_40. OC Bacteria; Proteobacteria; Betaproteobacteria. OX NCBI_TaxID=1703389 {ECO:0000313|EMBL:KPK32209.1, ECO:0000313|Proteomes:UP000051602}; RN [1] {ECO:0000313|EMBL:KPK32209.1, ECO:0000313|Proteomes:UP000051602} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SG8_40 {ECO:0000313|EMBL:KPK32209.1}; RX PubMed=25922666; DOI=10.1186/s40168-015-0077-6; RA Baker B.J., Lazar C.S., Teske A.P., Dick G.J.; RT "Genomic resolution of linkages in carbon, nitrogen, and sulfur RT cycling among widespread estuary sediment bacteria."; RL Microbiome 3:14-14(2015). CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KPK32209.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LJTS01000103; KPK32209.1; -; Genomic_DNA. DR PATRIC; fig|1703389.3.peg.115; -. DR Proteomes; UP000051602; Unassembled WGS sequence. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000051602}; KW Reference proteome {ECO:0000313|Proteomes:UP000051602}. FT DOMAIN 171 337 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT NON_TER 1 1 {ECO:0000313|EMBL:KPK32209.1}. SQ SEQUENCE 345 AA; 37708 MW; DA336E365757CBDB CRC64; EEMLRLADSA GVQVLGVVKG RRQRPDAATF AGKGKVEELA ALVSAQQANL VIFNHDLSPA QQRNLEQRTH VRVVDRTSLI LDIFAQRARS HEGKLQVELA QLDHLATRLV RGWTHLERQK GGIGLRGPGE TQLETDRRLL AKRVRVLRSK LEAVSRQRMT QRRARSRGNT LSVSLVGYTN AGKSTLFNRL TRGDAYAADQ LFATLDTTSR RLGTTGNRTI VLSDTVGFIR DLPHTLVAAF RATLEETVRA DLLLHVVDAA SPVRDSQIAQ VNKVLADIGA DRVPQIIVYN KIDLAGLPPG VERDACGKIR AVRVSAATGA GIAELRALYN EFQSATEPVT SLALA // ID A0A0S8DQ25_9GAMM Unreviewed; 438 AA. AC A0A0S8DQ25; DT 17-FEB-2016, integrated into UniProtKB/TrEMBL. DT 17-FEB-2016, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=AMJ69_08570 {ECO:0000313|EMBL:KPK38389.1}; OS Gammaproteobacteria bacterium SG8_47. OC Bacteria; Proteobacteria; Gammaproteobacteria. OX NCBI_TaxID=1703406 {ECO:0000313|EMBL:KPK38389.1, ECO:0000313|Proteomes:UP000054199}; RN [1] {ECO:0000313|EMBL:KPK38389.1, ECO:0000313|Proteomes:UP000054199} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SG8_47 {ECO:0000313|EMBL:KPK38389.1}; RX PubMed=25922666; DOI=10.1186/s40168-015-0077-6; RA Baker B.J., Lazar C.S., Teske A.P., Dick G.J.; RT "Genomic resolution of linkages in carbon, nitrogen, and sulfur RT cycling among widespread estuary sediment bacteria."; RL Microbiome 3:14-14(2015). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KPK38389.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LJTV01000083; KPK38389.1; -; Genomic_DNA. DR PATRIC; fig|1703406.3.peg.2155; -. DR Proteomes; UP000054199; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000054199}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000054199}. FT DOMAIN 197 364 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 438 AA; 48938 MW; EF45E3814565EFEE CRC64; MFERPKSGER AVLVHIDLPG ADHDSLDEFY DLAVSAGAEP VASVTGARKL PEPKYFVGSG KAEEIKECVA RESAQVVLVD HGLSPAQERN LERLLNCRVL DRTGLILDIF AQRARSHEGK LQVELAQLRH LSTRLVRGWS HLERQKGGIG LRGPGETQLE SDRRLIGGRI KQLNKRLEKV SRQRGQSRRA RRRAQLTTVS LVGYTNAGKS TLFNQLTATS VYAADQLFAT LDPTLRRVAL PSGEPIVLAD TVGFIRQLPH DLVAAFRSTL QETQEAHLLL HVIDASHEHR DELIEHVNGV LNEIEADDVP QLEVYNKIDL IADAEPHIDY DQAGRPIRVW LSARTGAGLD LLLQAVEEHL RQDWLTVSLR LPPEEGRLRA LLFERNLVEH EETDAEGGAL LILCLTRAGL EKLRNEYPHI DHWLSSESEH TTRLAVAG // ID A0A0S8E7H7_9BACT Unreviewed; 438 AA. AC A0A0S8E7H7; DT 17-FEB-2016, integrated into UniProtKB/TrEMBL. DT 17-FEB-2016, sequence version 1. DT 07-JUN-2017, entry version 10. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=AMJ65_03345 {ECO:0000313|EMBL:KPK44336.1}; OS Phycisphaerae bacterium SG8_4. OC Bacteria; Planctomycetes; Phycisphaerae. OX NCBI_TaxID=1703409 {ECO:0000313|EMBL:KPK44336.1, ECO:0000313|Proteomes:UP000051853}; RN [1] {ECO:0000313|EMBL:KPK44336.1, ECO:0000313|Proteomes:UP000051853} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SG8_4 {ECO:0000313|EMBL:KPK44336.1}; RX PubMed=25922666; DOI=10.1186/s40168-015-0077-6; RA Baker B.J., Lazar C.S., Teske A.P., Dick G.J.; RT "Genomic resolution of linkages in carbon, nitrogen, and sulfur RT cycling among widespread estuary sediment bacteria."; RL Microbiome 3:14-14(2015). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KPK44336.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LJTR01000036; KPK44336.1; -; Genomic_DNA. DR PATRIC; fig|1703409.3.peg.2732; -. DR Proteomes; UP000051853; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000051853}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000051853}. FT DOMAIN 211 377 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 438 AA; 47971 MW; 8C2A7B30552639B3 CRC64; MEKFRETLRV RKERAILVGA ILRGGDGGDD LAELTALAES AGALVVDKFQ QKIRTIKAST YIGKGKADRL AGRVKRFGAD VVIFDNDLSP GQIRELEEIV EIKVLDRSEL ILDIFATRAK TRQAKLQVAL AQLEYTYPRL TRMWSHLDTV AGAGGGTAAG AVGGIGTRGT GEQQLEIDRR LVNKRITELK RELAGIDQRR IREIDARRGL FKLCLVGYTN AGKSTLLNNL TDAGVPVEDR LFATLDTRTR KWVLSGGIDV LISDTVGFVN NLPHQLVASF KATLEEAVNA DLLLHVIDAA SPEALKQIES VNSVLEEIGC SDKPVLEVLN KADVVRKISD LETLQTLYPD AVCISAKTGF GIDSLSEAVM AKYKGNILLL RVTCKQSNGK VQSFLRAHGR ILDAQYSNSS VLIDAQLGRN QLPGLKRLHP ENIEIVRE // ID A0A0S8ECQ4_9BACT Unreviewed; 395 AA. AC A0A0S8ECQ4; DT 17-FEB-2016, integrated into UniProtKB/TrEMBL. DT 17-FEB-2016, sequence version 1. DT 07-JUN-2017, entry version 5. DE SubName: Full=GTP-binding protein HflX {ECO:0000313|EMBL:KPK46216.1}; DE Flags: Fragment; GN ORFNames=AMK74_01015 {ECO:0000313|EMBL:KPK46216.1}; OS Nitrospira bacterium SM23_35. OC Bacteria; Nitrospirae. OX NCBI_TaxID=1704026 {ECO:0000313|EMBL:KPK46216.1, ECO:0000313|Proteomes:UP000051169}; RN [1] {ECO:0000313|EMBL:KPK46216.1, ECO:0000313|Proteomes:UP000051169} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SM23_35 {ECO:0000313|EMBL:KPK46216.1}; RX PubMed=25922666; DOI=10.1186/s40168-015-0077-6; RA Baker B.J., Lazar C.S., Teske A.P., Dick G.J.; RT "Genomic resolution of linkages in carbon, nitrogen, and sulfur RT cycling among widespread estuary sediment bacteria."; RL Microbiome 3:14-14(2015). CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KPK46216.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LJUG01000007; KPK46216.1; -; Genomic_DNA. DR Proteomes; UP000051169; Unassembled WGS sequence. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 4: Predicted; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000051169}; KW Reference proteome {ECO:0000313|Proteomes:UP000051169}. FT DOMAIN 358 395 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 317 351 {ECO:0000256|SAM:Coils}. FT NON_TER 395 395 {ECO:0000313|EMBL:KPK46216.1}. SQ SEQUENCE 395 AA; 44923 MW; 08A19A7B88F13A08 CRC64; MTALERIYRR KLHREFISPE LARYLTSLSH EINRQIGILV SRSGNITHVI VGDARGIFIP ALEDYPLGRK ALRGLRLVHT HLQEEPLTQD DLTDLALLRF DLIAAMGVRH GLPGNISVAH LTPAGNEPFE ILRNENFHNF EFDFLPFIES LEEEMERIRH FNPDDRRERA ILVSVSKQPK YEQQDSVAEL DELARSSDLL VLDTVIQRPK EINPRYLMGE GKIKDLIINA LSKGATILVF DQELSPSQIK AISELTELKV IDRSQLILDI FARRAHSRDG KVQVELAQLK YRLPRLTGKG TAMSRLMGGI GGRGPGEMKL EIDRRRVRER ISLLERELRS LGEARKQRKQ KRIETGIPIV SIIGYTNAGK STLLNSLTKS YVFVEDKLFA TLDTA // ID A0A0S8EDD2_9CHLR Unreviewed; 399 AA. AC A0A0S8EDD2; DT 17-FEB-2016, integrated into UniProtKB/TrEMBL. DT 17-FEB-2016, sequence version 1. DT 07-JUN-2017, entry version 10. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=AMJ77_06675 {ECO:0000313|EMBL:KPK45914.1}; OS Dehalococcoidia bacterium SM23_28_2. OC Bacteria; Chloroflexi; Dehalococcoidia. OX NCBI_TaxID=1703396 {ECO:0000313|EMBL:KPK45914.1, ECO:0000313|Proteomes:UP000054036}; RN [1] {ECO:0000313|EMBL:KPK45914.1, ECO:0000313|Proteomes:UP000054036} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SM23_28_2 {ECO:0000313|EMBL:KPK45914.1}; RX PubMed=25922666; DOI=10.1186/s40168-015-0077-6; RA Baker B.J., Lazar C.S., Teske A.P., Dick G.J.; RT "Genomic resolution of linkages in carbon, nitrogen, and sulfur RT cycling among widespread estuary sediment bacteria."; RL Microbiome 3:14-14(2015). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KPK45914.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LJUA01000090; KPK45914.1; -; Genomic_DNA. DR PATRIC; fig|1703396.3.peg.1039; -. DR Proteomes; UP000054036; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000054036}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000054036}. FT DOMAIN 207 331 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 166 200 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 399 AA; 43832 MW; 98F6DC73E263D74E CRC64; MPATGHVTAE PKERAYLVAV EIKGRGNSRW SSQSSLDELA QLTLTAGANV VGRSVQRLER PTSAYYVGRG KVQELASLRY RLGYSTVIFD DELSPSQQRN LEDALEVKVL DRTALILDIF AQHARTREGA LQVELAQHEY LLPRLAGQWA HLERLEGAIG TRGPGETQLE TDRRLIRRKI QHLKQQIEEV RRQRALYRRR RARQGVSVIS LVGYTNAGKS TLMRALSGAN VLVEDKLFAT LDPVTRRVVL PHGGAFLLTD TVGFIQKLPT QLVAAFRATL EELSEASVLL HVVDITHPDA AEQAQTVEDT LADLSLADKP CITVLNKADL ICGPDGSPIE GLEALGEARA SLRYWRPDAL LVSAIKGWGL TDLLGRIEGA LGLGEGEAAS WAYRERSAG // ID A0A0S8F523_9GAMM Unreviewed; 442 AA. AC A0A0S8F523; DT 17-FEB-2016, integrated into UniProtKB/TrEMBL. DT 17-FEB-2016, sequence version 1. DT 30-AUG-2017, entry version 10. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=AMJ59_24705 {ECO:0000313|EMBL:KPK54588.1}; OS Gammaproteobacteria bacterium SG8_31. OC Bacteria; Proteobacteria; Gammaproteobacteria. OX NCBI_TaxID=1703405 {ECO:0000313|EMBL:KPK54588.1, ECO:0000313|Proteomes:UP000051321}; RN [1] {ECO:0000313|EMBL:KPK54588.1, ECO:0000313|Proteomes:UP000051321} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SG8_31 {ECO:0000313|EMBL:KPK54588.1}; RX PubMed=25922666; DOI=10.1186/s40168-015-0077-6; RA Baker B.J., Lazar C.S., Teske A.P., Dick G.J.; RT "Genomic resolution of linkages in carbon, nitrogen, and sulfur RT cycling among widespread estuary sediment bacteria."; RL Microbiome 3:14-14(2015). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KPK54588.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LJTI01000160; KPK54588.1; -; Genomic_DNA. DR PATRIC; fig|1703405.3.peg.5862; -. DR Proteomes; UP000051321; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000051321}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000051321}. FT DOMAIN 198 364 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 157 191 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 442 AA; 50228 MW; 7B7E3D0003934965 CRC64; MFERPKSGER AILVEVAVGE RLSQDQIDEF EELALSAGAT ICASLTGNRQ SPNPRFYIGS GKVEELGALV KEHDADLVLF NHELSPSQER NLEQQLRCRV LDRTGLILDI FAQRARSFEG KLQVELAQLE HLSTRLVRGW THLERQKGGI GLRGPGETQL ETDRRLLGQR IKQLKRKLDK VRQQRDQGRR TRRRAEVPTV SLVGYTNAGK STLFNRLTES GVYVADQLFA TLDPTLRGID LGEGQRAVLA DTVGFVRDLP HELVEAFRST LQETRDATLL LHVIDVSDPN RRDRIRQVAR VIEEIEADEV PQIEVFNKID LLDEQPRLQR DETGRPVRVW VSAQDGRGME LIIQALRERL ATDMARGRLR INADEGRLRA ALYEENAVTQ EEPDGDGGWI VDLALPRRTF LSMCRRENID AERLEDLPCA PRDRYLQSRT VA // ID A0A0S8FPC8_9GAMM Unreviewed; 442 AA. AC A0A0S8FPC8; DT 17-FEB-2016, integrated into UniProtKB/TrEMBL. DT 17-FEB-2016, sequence version 1. DT 07-JUN-2017, entry version 10. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=AMJ59_02275 {ECO:0000313|EMBL:KPK61405.1}; OS Gammaproteobacteria bacterium SG8_31. OC Bacteria; Proteobacteria; Gammaproteobacteria. OX NCBI_TaxID=1703405 {ECO:0000313|EMBL:KPK61405.1, ECO:0000313|Proteomes:UP000051321}; RN [1] {ECO:0000313|EMBL:KPK61405.1, ECO:0000313|Proteomes:UP000051321} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SG8_31 {ECO:0000313|EMBL:KPK61405.1}; RX PubMed=25922666; DOI=10.1186/s40168-015-0077-6; RA Baker B.J., Lazar C.S., Teske A.P., Dick G.J.; RT "Genomic resolution of linkages in carbon, nitrogen, and sulfur RT cycling among widespread estuary sediment bacteria."; RL Microbiome 3:14-14(2015). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KPK61405.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LJTI01000002; KPK61405.1; -; Genomic_DNA. DR PATRIC; fig|1703405.3.peg.3834; -. DR Proteomes; UP000051321; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000051321}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000051321}. FT DOMAIN 198 364 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 164 191 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 442 AA; 49689 MW; 898D596BEE894F1D CRC64; MFERPKSGER AILVQVAVGG RLSQDQIEEF EELARSAGAR ICASLAGSRQ APNPRFYIGA GKVEELRALA LAHDAELVLF NHELSPSQER NLERELQCRV LDRTGLILDI FAQRARSFEG KLQVELAQLE HLSTRLVRGW THLERQKGGI GLRGPGETQL ETDRRLLGQR IKQLNRKLDR VRQQREQGRR TRRRAEVPTV SLVGYTNAGK STLFNRLTES GVYVADQLFA TLDPTLRGVD LGEGQRAVLA DTVGFVRDLP HELVEAFRST LQETREAALL LHVIDASDSS RRDRIEQVEQ VIEEIGADEV PQVQVFNKID LVNEQPRLQR DEWGRPVRVW ASAADGRGMD LILQALRERL AEDVARGKIH LTSAEGRFRA GLYTEGGVVS EEPDGEGGWL LELALPRRRF LSLCRRERID PERLKGLPCA TGNGYLQSRT VA // ID A0A0S8FZH7_9BACT Unreviewed; 418 AA. AC A0A0S8FZH7; DT 17-FEB-2016, integrated into UniProtKB/TrEMBL. DT 17-FEB-2016, sequence version 1. DT 07-JUN-2017, entry version 9. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=AMS21_03245 {ECO:0000313|EMBL:KPK66032.1}; OS Gemmatimonas sp. SG8_38_2. OC Bacteria; Gemmatimonadetes; Gemmatimonadales; Gemmatimonadaceae; OC Gemmatimonas. OX NCBI_TaxID=1703358 {ECO:0000313|EMBL:KPK66032.1, ECO:0000313|Proteomes:UP000051763}; RN [1] {ECO:0000313|EMBL:KPK66032.1, ECO:0000313|Proteomes:UP000051763} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SG8_38_2 {ECO:0000313|EMBL:KPK66032.1}; RX PubMed=25922666; DOI=10.1186/s40168-015-0077-6; RA Baker B.J., Lazar C.S., Teske A.P., Dick G.J.; RT "Genomic resolution of linkages in carbon, nitrogen, and sulfur RT cycling among widespread estuary sediment bacteria."; RL Microbiome 3:14-14(2015). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KPK66032.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LJTP01000020; KPK66032.1; -; Genomic_DNA. DR PATRIC; fig|1703358.3.peg.2153; -. DR Proteomes; UP000051763; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000051763}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000051763}. FT DOMAIN 186 355 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 147 174 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 418 AA; 46035 MW; 03F8C0FA63FCDA21 CRC64; MSAPDQGSSR QDAEEHLSEL ASLTGTAGAE VVATIQQQIQ SPHPAYYIGT GKVVELRSAV QESGASLVIF DEDLSPVQGQ KLEQELGVRV MDRTELIIDI FALRARSAEA KAQVELAQLQ YLMPRLKRMW NHLSRIRGGI GLRGPGETQL ETDRRTIRRK ISDLKRRLEK VARQRETERK GRAGEFRAAL VGYTNAGKSS ILAGLSGSEL FVEDCLFATL DPATRVVDLG DDYHALVTDT VGFIRKLPHD LVASFRATLE EANEADVLCH VVDVAHGHWE EQYEVVESVI SDLQFNPKSR LVVFNKVDRI THAEQSAIED RASALLGSHV FTSTVEAGGL ETLRTTLRET IREQWPLVSL TIPASAGGLL AELYREGEVL AREEQGAHIR ITVRLPIDVL GRLAAREEVA VFDAPPAA // ID A0A0S8GS78_9BACT Unreviewed; 143 AA. AC A0A0S8GS78; DT 17-FEB-2016, integrated into UniProtKB/TrEMBL. DT 17-FEB-2016, sequence version 1. DT 11-MAY-2016, entry version 4. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:KPK75871.1}; DE Flags: Fragment; GN ORFNames=AMS25_17995 {ECO:0000313|EMBL:KPK75871.1}; OS Gemmatimonas sp. SM23_52. OC Bacteria; Gemmatimonadetes; Gemmatimonadales; Gemmatimonadaceae; OC Gemmatimonas. OX NCBI_TaxID=1703359 {ECO:0000313|EMBL:KPK75871.1, ECO:0000313|Proteomes:UP000051975}; RN [1] {ECO:0000313|EMBL:KPK75871.1, ECO:0000313|Proteomes:UP000051975} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SM23_52 {ECO:0000313|EMBL:KPK75871.1}; RX PubMed=25922666; DOI=10.1186/s40168-015-0077-6; RA Baker B.J., Lazar C.S., Teske A.P., Dick G.J.; RT "Genomic resolution of linkages in carbon, nitrogen, and sulfur RT cycling among widespread estuary sediment bacteria."; RL Microbiome 3:14-14(2015). CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KPK75871.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LJUM01000218; KPK75871.1; -; Genomic_DNA. DR Proteomes; UP000051975; Unassembled WGS sequence. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000051975}; KW Reference proteome {ECO:0000313|Proteomes:UP000051975}. FT DOMAIN 27 114 GTP-bdg_N. {ECO:0000259|Pfam:PF13167}. FT DOMAIN 116 142 GTP-bdg_M. {ECO:0000259|Pfam:PF16360}. FT NON_TER 143 143 {ECO:0000313|EMBL:KPK75871.1}. SQ SEQUENCE 143 AA; 15990 MW; A4C4943B40517AFF CRC64; MEVEAPQERV VLLSAPSQRV SRQEARDHLT ELVSLADTAG ATVVATAQQT LQAPHPAYYI GTGKVEQLRS LVSESAASLV IFDEDLTPIQ GQKLEEMLGV RVMDRTELII DIFALRARTA EAKMQVELAQ LEYLMPRLRR MWS // ID A0A0S8GTL8_9BACT Unreviewed; 444 AA. AC A0A0S8GTL8; DT 17-FEB-2016, integrated into UniProtKB/TrEMBL. DT 17-FEB-2016, sequence version 1. DT 07-JUN-2017, entry version 9. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=AMJ79_08145 {ECO:0000313|EMBL:KPK76121.1}; OS Phycisphaerae bacterium SM23_30. OC Bacteria; Planctomycetes; Phycisphaerae. OX NCBI_TaxID=1703411 {ECO:0000313|EMBL:KPK76121.1, ECO:0000313|Proteomes:UP000051901}; RN [1] {ECO:0000313|EMBL:KPK76121.1, ECO:0000313|Proteomes:UP000051901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SM23_30 {ECO:0000313|EMBL:KPK76121.1}; RX PubMed=25922666; DOI=10.1186/s40168-015-0077-6; RA Baker B.J., Lazar C.S., Teske A.P., Dick G.J.; RT "Genomic resolution of linkages in carbon, nitrogen, and sulfur RT cycling among widespread estuary sediment bacteria."; RL Microbiome 3:14-14(2015). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KPK76121.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LJUC01000091; KPK76121.1; -; Genomic_DNA. DR PATRIC; fig|1703411.3.peg.56; -. DR Proteomes; UP000051901; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000051901}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000051901}. FT DOMAIN 212 377 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 173 207 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 444 AA; 49624 MW; 0F646F455E2D433D CRC64; MENKRNTLKV GQETALLVNV ALPDSDIDPV DSLDELAALA EAVDAVVVDR VVQRRPHPHP AHYVGHGKAQ EIALRAQHYG ANTIIFDNDL SPAQIRELET ITHCKVIDRS ELILDIFATR ARTHEAKLQV ELAQLQYTYP RLTRMWSHLD TVVGAAAAAA GAVGGIGTRG PGEKQLEIDR RLVQKRLAQL RRQINQIDRR KQRQVRSRSE NFTVSLVGYT NAGKSTLLNL LTGSEAYVEH KLFATLDTKT ARWILDRDIS VLLSDTVGFI RNLPHHLVAS FQATLEEAIH ADLLLHVVDA SHPQADQQLQ AAHKVLEEIH CHKKDILLVL NKIDRRPNPT IDTMMTLYPE AIPVSARKGL GIEKLAEAVT YRVTGEKLRL RISCNQTDGH IPNFLRAHGA IISEDYTDSR ITLEAYLGRR QLPNLKRLKP HTCQIISNPA PDST // ID A0A0S8HBK4_9BACT Unreviewed; 420 AA. AC A0A0S8HBK4; DT 17-FEB-2016, integrated into UniProtKB/TrEMBL. DT 17-FEB-2016, sequence version 1. DT 07-JUN-2017, entry version 9. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=AMS25_04740 {ECO:0000313|EMBL:KPK81860.1}; OS Gemmatimonas sp. SM23_52. OC Bacteria; Gemmatimonadetes; Gemmatimonadales; Gemmatimonadaceae; OC Gemmatimonas. OX NCBI_TaxID=1703359 {ECO:0000313|EMBL:KPK81860.1, ECO:0000313|Proteomes:UP000051975}; RN [1] {ECO:0000313|EMBL:KPK81860.1, ECO:0000313|Proteomes:UP000051975} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SM23_52 {ECO:0000313|EMBL:KPK81860.1}; RX PubMed=25922666; DOI=10.1186/s40168-015-0077-6; RA Baker B.J., Lazar C.S., Teske A.P., Dick G.J.; RT "Genomic resolution of linkages in carbon, nitrogen, and sulfur RT cycling among widespread estuary sediment bacteria."; RL Microbiome 3:14-14(2015). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KPK81860.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LJUM01000022; KPK81860.1; -; Genomic_DNA. DR PATRIC; fig|1703359.3.peg.1268; -. DR Proteomes; UP000051975; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000051975}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000051975}. FT DOMAIN 188 357 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 156 183 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 420 AA; 46756 MW; 31C7EB805858C4A8 CRC64; MLLSAPSRSV SRQEARDHLT ELVSLADTAG ATIVATVQQP LQAPHPAYYI GTGKVEQLRS LSTESAASLV IFDEDLTPVQ GQKLEEMLGV RVMDRTELII DIFALRARTA EAKMQVEVAQ LEYLMPRLRR MWSHLSRIRG GIGLRGPGET QLETDRRIIR SKIRELKRRL EKVARQRATE RKGRAGEFRV ALVGYTNAGK SSILAALSGS DLFIEDRLFA TLDPATRAVD LGEGFQALVT DTVGFIRKLP HHLVASFRAT LEEANEADLL CHVVDVAHPR WEDQHEVVEG VVAELQLNAK RRLVAFNKVD RLTHAEQAAI EQRAGVLVDP HVFTSTLEPD GLDALRATLR RLIREQWRTV VLSIPASAGS VLAEVYREGE VLTREERGIS IQMTARLPLY VLGRLRTRED VAIFEAPPAA // ID A0A0S8HFF1_9BACT Unreviewed; 443 AA. AC A0A0S8HFF1; DT 17-FEB-2016, integrated into UniProtKB/TrEMBL. DT 17-FEB-2016, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=AMJ81_06845 {ECO:0000313|EMBL:KPK83983.1}; OS Phycisphaerae bacterium SM23_33. OC Bacteria; Planctomycetes; Phycisphaerae. OX NCBI_TaxID=1703412 {ECO:0000313|EMBL:KPK83983.1, ECO:0000313|Proteomes:UP000054531}; RN [1] {ECO:0000313|EMBL:KPK83983.1, ECO:0000313|Proteomes:UP000054531} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SM23_33 {ECO:0000313|EMBL:KPK83983.1}; RX PubMed=25922666; DOI=10.1186/s40168-015-0077-6; RA Baker B.J., Lazar C.S., Teske A.P., Dick G.J.; RT "Genomic resolution of linkages in carbon, nitrogen, and sulfur RT cycling among widespread estuary sediment bacteria."; RL Microbiome 3:14-14(2015). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KPK83983.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LJUF01000096; KPK83983.1; -; Genomic_DNA. DR PATRIC; fig|1703412.3.peg.764; -. DR Proteomes; UP000054531; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000054531}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000054531}. FT DOMAIN 213 379 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 443 AA; 49267 MW; 7D1D9829715CE7F6 CRC64; MSEAKRTQFT VQQERALLVS VILPDSDADL HDPLGELRSL ARTAGAKVVD EAVARRSSIQ PGLYLGRGKA EEIAGRARQN RVDVVLFDND LSPAQIRDLE KIIDRKVLDR SEVILDIFAA HARTREARLQ VELAQLEYTY PRLRRMWTHL ERVAGGATTA AAAVGGIGTR GPGEKQIETD RRLVRRRVAQ LRRRIAAIDR RRQREVRSRR ESFQICLVGY TNAGKSTLMN LLTGAGMPVA DQLFATLDTR TRRWNLGEGH EALLSDTVGF ISHLPHHLIA SFRATLEEAI GAELLLHVAD AAHPRVAEQI RAVQEVLGEL GCGEKDQLLL LNKIDLISDP TVLRVLSERH ADAIALSAAT GENAEKLVEA VLERVRGRRV SVTIQADYTN GRLMQYLSRY AQVGDRSYEG RSVQLEATLG EKHVEVLRTF GAEVRIRAES ESS // ID A0A0S8HSV7_9BACE Unreviewed; 397 AA. AC A0A0S8HSV7; DT 17-FEB-2016, integrated into UniProtKB/TrEMBL. DT 17-FEB-2016, sequence version 1. DT 07-JUN-2017, entry version 9. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=AMS27_00235 {ECO:0000313|EMBL:KPK88217.1}; OS Bacteroides sp. SM23_62_1. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae; OC Bacteroides. OX NCBI_TaxID=1703353 {ECO:0000313|EMBL:KPK88217.1, ECO:0000313|Proteomes:UP000051265}; RN [1] {ECO:0000313|EMBL:KPK88217.1, ECO:0000313|Proteomes:UP000051265} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SM23_62_1 {ECO:0000313|EMBL:KPK88217.1}; RX PubMed=25922666; DOI=10.1186/s40168-015-0077-6; RA Baker B.J., Lazar C.S., Teske A.P., Dick G.J.; RT "Genomic resolution of linkages in carbon, nitrogen, and sulfur RT cycling among widespread estuary sediment bacteria."; RL Microbiome 3:14-14(2015). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KPK88217.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LJUQ01000001; KPK88217.1; -; Genomic_DNA. DR PATRIC; fig|1703353.3.peg.1545; -. DR Proteomes; UP000051265; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000051265}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000051265}. FT DOMAIN 202 386 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 170 197 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 397 AA; 45837 MW; 1429C25C97B4C2D6 CRC64; MHEPVITKPK IETAILIGVV DNSNDEQLVR EYLDELAFLA ITAGVEPVGR FTQKLEYPNP RTFVGTGKLQ EIRDFVIKKK IDLVIFDDEL SASQIRNIER ELNCRILDRT NLILDIFATR AKTAHAKTQV ELAQYQYLLP RLAGLWTHLE RQRGGIGLRG PGETEIETDR RVIRDRIAKL KDDLEKIDIQ KKTQRQNRGK MVRVALVGYT NVGKSTLMNV LSKSDVFAED KLFATLDTTV RKVVVENLPF LISDTVGFIR KLPHSLVESF KSTLDEVRES DILLHVVDIS HPNFEEQVEI VQQTLYEINA NDKPVILVFN KIDAFHYILK EFDDLTPLTK ENLSLEDLKR TWMARCNGTC VFISAKHKEN IETIKDLLYE KVKEIHIQRY PYDDFLY // ID A0A0S8IB50_9DELT Unreviewed; 565 AA. AC A0A0S8IB50; DT 17-FEB-2016, integrated into UniProtKB/TrEMBL. DT 17-FEB-2016, sequence version 1. DT 07-JUN-2017, entry version 9. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=AMJ94_03595 {ECO:0000313|EMBL:KPK93258.1}; OS Deltaproteobacteria bacterium SM23_61. OC Bacteria; Proteobacteria; Deltaproteobacteria. OX NCBI_TaxID=1703399 {ECO:0000313|EMBL:KPK93258.1, ECO:0000313|Proteomes:UP000051218}; RN [1] {ECO:0000313|EMBL:KPK93258.1, ECO:0000313|Proteomes:UP000051218} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SM23_61 {ECO:0000313|EMBL:KPK93258.1}; RX PubMed=25922666; DOI=10.1186/s40168-015-0077-6; RA Baker B.J., Lazar C.S., Teske A.P., Dick G.J.; RT "Genomic resolution of linkages in carbon, nitrogen, and sulfur RT cycling among widespread estuary sediment bacteria."; RL Microbiome 3:14-14(2015). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KPK93258.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LJUR01000020; KPK93258.1; -; Genomic_DNA. DR PATRIC; fig|1703399.3.peg.3159; -. DR Proteomes; UP000051218; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000051218}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000051218}. FT DOMAIN 379 543 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 338 365 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 565 AA; 63942 MW; DC09D986E68BE108 CRC64; MQKIFGNTLG LKPSQTRKIL ALYRRRVPPQ RVVTPELARA LTELSQDSNR QLALLIDRGG NVRYVIVGGP AGIWIPDLSA YRLGSGPRLR GLRCVHTHLK GESLSHDDLT DLALLRFDLM AAIGVLPSGL PGDIFLANLM PMNEKGKSWR CWDPLPLASL DVDALEIIQA LEGEFRRSQK VREAGDRRDR AILVHASSAP RWAIEDSLSE LADLADSAGV LVLEKLSQRR NQFHPRFLVG REKLTDLSIR AFQQGADLLI FDQELNPNQM RSITDLTELR VIDRTQLILD IFAQRAHTRE GKLKVELAQL KYLLPRLTTE DSGLSRLTGG IGSRGPGETK LEVDRRKVRE RIHRLTKEME GVNRSREVRR LQREKNQMPV ISIVGYTNAG KSTLLNALTK SRIHVENKLF ATLDPTTRRL RFPREREAII TDTVGFLRDL PKDLMDAFRA TLEELRDADL LLHVVDMSHP RFEDQMAAVE KILEELELKQ IPLLRVFNKA DRLDLETAQR ISRAFNAVCI SALKPETFPP LLEKMEVVFP RPKNGILPSP TSHEFPMDSP VPEPV // ID A0A0S8IHA9_9CHLR Unreviewed; 437 AA. AC A0A0S8IHA9; DT 17-FEB-2016, integrated into UniProtKB/TrEMBL. DT 17-FEB-2016, sequence version 1. DT 07-JUN-2017, entry version 9. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=AMJ88_00560 {ECO:0000313|EMBL:KPK95466.1}; OS Anaerolineae bacterium SM23_ 63. OC Bacteria; Chloroflexi; Anaerolineae; unclassified Anaerolineae. OX NCBI_TaxID=1703387 {ECO:0000313|EMBL:KPK95466.1, ECO:0000313|Proteomes:UP000051685}; RN [1] {ECO:0000313|EMBL:KPK95466.1, ECO:0000313|Proteomes:UP000051685} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SM23_ 63 {ECO:0000313|EMBL:KPK95466.1}; RX PubMed=25922666; DOI=10.1186/s40168-015-0077-6; RA Baker B.J., Lazar C.S., Teske A.P., Dick G.J.; RT "Genomic resolution of linkages in carbon, nitrogen, and sulfur RT cycling among widespread estuary sediment bacteria."; RL Microbiome 3:14-14(2015). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KPK95466.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LJUS01000001; KPK95466.1; -; Genomic_DNA. DR PATRIC; fig|1703387.3.peg.3850; -. DR Proteomes; UP000051685; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000051685}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000051685}. FT DOMAIN 218 384 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 437 AA; 48670 MW; DB9BEA81C21460CD CRC64; MTKVTLPTKL PTERAFLVGF ELPDEQRLVS IQDSLEELKL LSLTAGLVVV GETSQRLKRL NPKTLLGSGK IEEIKTLVKE TVADIVLFDD ELSPRHQREL ERFFGDEVRV VDRSALILDI FAQHANTREG SLQVELAQYE YRLPRLTRAW THLARQAGGG GGRAGSVGGV GLRGPGETQL EVDRRDIGRR IAHLREQLEK VRAHRGRYRA RRKRAAIPTV ALVGYTNAGK STLLNRLSNA NVLVADKLFA TLDPTTRRVE LPEGREVLFT DTVGFIQKLP TTLVAAFQAT LEEIAEADLL LHIVDITHPN AKAQALAVRA TLDEIEVIDI PMVTALNKID LLPDPTSSLD RVDEFERAVP ISALTGEGIP TLLSSIEFEL YQSMSQVKVL LPYKAGRLIS LFHEQGRIDE IQHNENAVMI EGRIPTRLAS HYTDYQI // ID A0A0S8IJS8_9BACT Unreviewed; 421 AA. AC A0A0S8IJS8; DT 17-FEB-2016, integrated into UniProtKB/TrEMBL. DT 17-FEB-2016, sequence version 1. DT 07-JUN-2017, entry version 9. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=AMJ95_12510 {ECO:0000313|EMBL:KPK96732.1}; OS Omnitrophica WOR_2 bacterium SM23_72. OC Bacteria; Candidatus Omnitrophica. OX NCBI_TaxID=1703777 {ECO:0000313|EMBL:KPK96732.1, ECO:0000313|Proteomes:UP000051899}; RN [1] {ECO:0000313|EMBL:KPK96732.1, ECO:0000313|Proteomes:UP000051899} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SM23_72 {ECO:0000313|EMBL:KPK96732.1}; RX PubMed=25922666; DOI=10.1186/s40168-015-0077-6; RA Baker B.J., Lazar C.S., Teske A.P., Dick G.J.; RT "Genomic resolution of linkages in carbon, nitrogen, and sulfur RT cycling among widespread estuary sediment bacteria."; RL Microbiome 3:14-14(2015). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KPK96732.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LJUU01000080; KPK96732.1; -; Genomic_DNA. DR PATRIC; fig|1703777.3.peg.787; -. DR Proteomes; UP000051899; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000051899}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000051899}. FT DOMAIN 197 363 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 156 183 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 421 AA; 47574 MW; 15838FC98F960075 CRC64; MAMEKCLLVT IELRTEKDKW PRQDIARELE ELVKTANGQP IEQIFCAREK PTPDLFIGKG KAQEIALLCQ DEDIGTVIFS HDLSGTQQRN LEEEIGKKTI DRTQLILDIF SHHAHSPEGN MQVELAQLEY LLPRLVGKGI MLSRLGGGIG TRGPGEQKLE VDRRRIRERI TKLKQDLQHL TNHRRVIRKK RKEEAIPCLA LVGYTNAGKS TLLNALTGAG QYVKDSLFTT LDPLARRMNT PFGARVVVSD TVGFLHNLPH HLIEAFHTTL EEVVEADLLI HVLDASHSRI QEHNRAVITV LKQLNCENKP LITALNKIDL LEDKAWLSWL KEKFSDSVCI SAKTGQNLGE LLKEIDSFIE PKLTKVLLSV PLNKMSIIGF LYRQGKVIKA EYGEERVKVE VNIAKNLLDN LLINKEVKVI N // ID A0A0S8IKB4_9BACT Unreviewed; 439 AA. AC A0A0S8IKB4; DT 17-FEB-2016, integrated into UniProtKB/TrEMBL. DT 17-FEB-2016, sequence version 1. DT 07-JUN-2017, entry version 9. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=AMK75_07385 {ECO:0000313|EMBL:KPK97617.1}; OS Planctomycetes bacterium SM23_65. OC Bacteria; Planctomycetes. OX NCBI_TaxID=1704030 {ECO:0000313|EMBL:KPK97617.1, ECO:0000313|Proteomes:UP000052185}; RN [1] {ECO:0000313|EMBL:KPK97617.1, ECO:0000313|Proteomes:UP000052185} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SM23_65 {ECO:0000313|EMBL:KPK97617.1}; RX PubMed=25922666; DOI=10.1186/s40168-015-0077-6; RA Baker B.J., Lazar C.S., Teske A.P., Dick G.J.; RT "Genomic resolution of linkages in carbon, nitrogen, and sulfur RT cycling among widespread estuary sediment bacteria."; RL Microbiome 3:14-14(2015). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KPK97617.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LJUT01000193; KPK97617.1; -; Genomic_DNA. DR PATRIC; fig|1704030.3.peg.1610; -. DR Proteomes; UP000052185; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000052185}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000052185}. FT DOMAIN 203 369 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 164 191 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 439 AA; 49486 MW; 7C574A34BB976B7D CRC64; MVELKRTRLS VRREQALLLG VMLPADKHRA TKPLAELASL ARTAGARVVG EVVQQLKRFH PSTWIGRGKA QEVHDRAKSL DADVVICDGD LSPAQVRNLE KITDTKVVDR SELILDIFAT HARTKQARLQ VELAQLEYTY PRLARMWTHL SRYEGGIGTR GPGEMQLETD RRLVQRRIRD LKRELGRIDA RRQREVKSRG ECFKVGIVGY TNAGKSTLMN ALTDAGVRVE DQLFATLDTK TRRWDLGDHG EALLSDTVGF IRHLPHHLVA SFKATLEEAT LADLLLHIVD ISRADAIEQA DAVMEVLEEI GCRDKRILAV FNKVDAADDE TALHILSERF RNGVTVSALK KQGLDRLTEA VVAELQRDFA ELVVTFPSSD GRLAAFLFEK GDVLERDDQD TVTQMRVKLH RRFLADLSEH DGVEVRVSDG KEEPRAERY // ID A0A0S8IQR9_9BACT Unreviewed; 409 AA. AC A0A0S8IQR9; DT 17-FEB-2016, integrated into UniProtKB/TrEMBL. DT 17-FEB-2016, sequence version 1. DT 07-JUN-2017, entry version 9. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=AMJ95_01310 {ECO:0000313|EMBL:KPK98932.1}; OS Omnitrophica WOR_2 bacterium SM23_72. OC Bacteria; Candidatus Omnitrophica. OX NCBI_TaxID=1703777 {ECO:0000313|EMBL:KPK98932.1, ECO:0000313|Proteomes:UP000051899}; RN [1] {ECO:0000313|EMBL:KPK98932.1, ECO:0000313|Proteomes:UP000051899} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SM23_72 {ECO:0000313|EMBL:KPK98932.1}; RX PubMed=25922666; DOI=10.1186/s40168-015-0077-6; RA Baker B.J., Lazar C.S., Teske A.P., Dick G.J.; RT "Genomic resolution of linkages in carbon, nitrogen, and sulfur RT cycling among widespread estuary sediment bacteria."; RL Microbiome 3:14-14(2015). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KPK98932.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LJUU01000004; KPK98932.1; -; Genomic_DNA. DR PATRIC; fig|1703777.3.peg.1696; -. DR Proteomes; UP000051899; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000051899}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000051899}. FT DOMAIN 185 351 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 144 171 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 409 AA; 46057 MW; 4318BED736658587 CRC64; MNSEKDSWSL EDVAFELEEL TATCGAEAVD NITCACDKPT PNFFIGRGKV EELADAAREK YVDTLIFSHD LSGTQQRNLE DIIGKKTLDR TQLILDIFAR HAKSPEGKTQ VELAQLQYLL PRLVGKGIIL SRLGGGIGTR GPGEQKLEVD RRRIRKRIDK LKDDLKHLHQ HRCVMRKRRL EFALPTVALV GYTNAGKSTL LNALTNAGQL VGDSLFTTLD PLSEGMQLPN GEKIVISDTV GFLHRLPHHL IEAFKATLEE VVVADLLIHV LDVSAPGVHE HKQAVYDVLR KLQVGEKPII TALNKIDNLE DALGLERLKR DFANPVTISA LRKQNLDVLL EKIQNHFSDR MEYLEIKIPH SRMDLVDLFH QQGKIEDIKY LQSGIRISLH LPKIIASKLF HNKEIEKIC // ID A0A0S8IWA8_9BACT Unreviewed; 437 AA. AC A0A0S8IWA8; DT 17-FEB-2016, integrated into UniProtKB/TrEMBL. DT 17-FEB-2016, sequence version 1. DT 07-JUN-2017, entry version 9. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=AMJ91_03055 {ECO:0000313|EMBL:KPL00821.1}; OS candidate division Zixibacteria bacterium SM23_73_3. OC Bacteria. OX NCBI_TaxID=1703427 {ECO:0000313|EMBL:KPL00821.1, ECO:0000313|Proteomes:UP000051398}; RN [1] {ECO:0000313|EMBL:KPL00821.1, ECO:0000313|Proteomes:UP000051398} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SM23_73_3 {ECO:0000313|EMBL:KPL00821.1}; RX PubMed=25922666; DOI=10.1186/s40168-015-0077-6; RA Baker B.J., Lazar C.S., Teske A.P., Dick G.J.; RT "Genomic resolution of linkages in carbon, nitrogen, and sulfur RT cycling among widespread estuary sediment bacteria."; RL Microbiome 3:14-14(2015). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KPL00821.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LJUX01000018; KPL00821.1; -; Genomic_DNA. DR PATRIC; fig|1703427.3.peg.764; -. DR Proteomes; UP000051398; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000051398}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000051398}. FT DOMAIN 201 375 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 162 189 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 437 AA; 49752 MW; 29859F0978D815B3 CRC64; MFEVAKLRTK EKAILVGVKL PSVNRFSVQE SLQELALLTE TAGGEVLDTV LQERQKLNPA FFVGKGKTDQ IKNLSQRLGA NIIIFDDDLT PAQVYNLEKN LDIKVIDRSW LILDIFAKRA KSKEAQVQVE LAQLKYLLPR LTRGWTHLSR QWGGIGTKGP GETQLEMDKR RVNKKIQELE KSLLKIDKER SVQRKRREDI FKVTLVGYTN VGKSTLFNQL TSSSAFVEEK LFATLDSTTR LLKVTDNGKL KEGVKIVITD TIGFIRKLPH HLIASFKSTL DEVKLADLLL HVVDISHPDF LQHINKVNQV LSELGSLDKL TLFIYNKIDK LSGKYPFNLS PYSEQKDDEL LVSAQNQIGI SDLAERIAEF AKGEWAEAWL YLRDGDSELL PCVYKIGIVT ESRFEKEGIR LKIRGKKENL QKIRKFSSGL KLKFLVF // ID A0A0S8JFC3_9BACT Unreviewed; 422 AA. AC A0A0S8JFC3; DT 17-FEB-2016, integrated into UniProtKB/TrEMBL. DT 17-FEB-2016, sequence version 1. DT 07-JUN-2017, entry version 9. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=AMJ86_05155 {ECO:0000313|EMBL:KPL07227.1}; OS bacterium SM23_57. OC Bacteria. OX NCBI_TaxID=1703763 {ECO:0000313|EMBL:KPL07227.1, ECO:0000313|Proteomes:UP000051603}; RN [1] {ECO:0000313|EMBL:KPL07227.1, ECO:0000313|Proteomes:UP000051603} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SM23_57 {ECO:0000313|EMBL:KPL07227.1}; RX PubMed=25922666; DOI=10.1186/s40168-015-0077-6; RA Baker B.J., Lazar C.S., Teske A.P., Dick G.J.; RT "Genomic resolution of linkages in carbon, nitrogen, and sulfur RT cycling among widespread estuary sediment bacteria."; RL Microbiome 3:14-14(2015). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KPL07227.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LJUN01000099; KPL07227.1; -; Genomic_DNA. DR PATRIC; fig|1703763.3.peg.1029; -. DR Proteomes; UP000051603; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000051603}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000051603}. FT DOMAIN 196 362 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 422 AA; 47598 MW; F83ECE4432885E6B CRC64; MADQKERVLL IALRRKGVSD WEVDDHLDEL AQLADTAGAQ VMGRFTQRLA KPDPATFLGK GKVRELVGEV RNRSVNSVVF DDDLAPAQVR NLEKELDVKV LDRSGVILDI FARRARSREA RTQVELAQLN YLLPRLTRRW GHLSRQIGGI GVRGPGETQL EVDKRLVRER IAKLSKELVK IEKGRQVRRR RRESMFRAAI VGYTNAGKST LLNALTGAEA FVEDRLFATL DSTTRKLALT PQTSILLTDT VGFIRKLPHH LVASFRSTLE ETVQADLLMH VIDISHPQFR TQMKTVKSVL RELGLEERPR LFVFNKVDQL QEGAALEWAR KSYPNAVFIS ALLGIRISHL VQRLSDIVLQ EYVEGDLAIP IDKGDLVAKL YQLAEVLDID QRDGALHIRF RTHQATLDHV LSLIGSGNTT KP // ID A0A0S8JR05_9BACE Unreviewed; 397 AA. AC A0A0S8JR05; DT 17-FEB-2016, integrated into UniProtKB/TrEMBL. DT 17-FEB-2016, sequence version 1. DT 07-JUN-2017, entry version 9. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=AMS26_20730 {ECO:0000313|EMBL:KPL11115.1}; OS Bacteroides sp. SM23_62. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae; OC Bacteroides. OX NCBI_TaxID=1703352 {ECO:0000313|EMBL:KPL11115.1, ECO:0000313|Proteomes:UP000050819}; RN [1] {ECO:0000313|EMBL:KPL11115.1, ECO:0000313|Proteomes:UP000050819} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SM23_62 {ECO:0000313|EMBL:KPL11115.1}; RX PubMed=25922666; DOI=10.1186/s40168-015-0077-6; RA Baker B.J., Lazar C.S., Teske A.P., Dick G.J.; RT "Genomic resolution of linkages in carbon, nitrogen, and sulfur RT cycling among widespread estuary sediment bacteria."; RL Microbiome 3:14-14(2015). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KPL11115.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LJUP01000276; KPL11115.1; -; Genomic_DNA. DR PATRIC; fig|1703352.3.peg.2287; -. DR Proteomes; UP000050819; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000050819}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000050819}. FT DOMAIN 202 386 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 170 197 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 397 AA; 45750 MW; C639D39EB9AC8279 CRC64; MPEPLITTPK PETAILIGII DQYQDAVTVE EYLQELAFLT ETAGAIPEKT FVQKLAYPDP RTFVGSGKLL EIREYVAMND TDLVIFDDEL TPSQLRNIER ELNCRILDRT NLILDIFARR AKTAHAKTQV ELAQYEYLLP RLTRMWTHLE RQRGGIGLRG PGETEIETDR RIIRDKIAKL KEDLKRIDKQ KSVQRKNRGK MVRVALVGYT NVGKSTLMNV VSKSDIFAEN KLFATLDTTI RKVVIGNLPF LLSDTVGFIR KLPHTLVESF KSTLDEVRES DILLHVVDIS HPNFEEQIDI VNQTLLEIDA RHKPTYIVFN KIDAFRYVAK DEDDLGPYTS ENMSLDDLKK SWMAKSNGAC VFISAKKLEN IQEIRDLLYD KVKEIHARRY PYDDFLY // ID A0A0S8K7W2_9BACT Unreviewed; 431 AA. AC A0A0S8K7W2; DT 17-FEB-2016, integrated into UniProtKB/TrEMBL. DT 17-FEB-2016, sequence version 1. DT 07-JUN-2017, entry version 9. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=AMJ92_10155 {ECO:0000313|EMBL:KPL17991.1}; OS candidate division Zixibacteria bacterium SM23_81. OC Bacteria. OX NCBI_TaxID=1703428 {ECO:0000313|EMBL:KPL17991.1, ECO:0000313|Proteomes:UP000051415}; RN [1] {ECO:0000313|EMBL:KPL17991.1, ECO:0000313|Proteomes:UP000051415} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SM23_81 {ECO:0000313|EMBL:KPL17991.1}; RX PubMed=25922666; DOI=10.1186/s40168-015-0077-6; RA Baker B.J., Lazar C.S., Teske A.P., Dick G.J.; RT "Genomic resolution of linkages in carbon, nitrogen, and sulfur RT cycling among widespread estuary sediment bacteria."; RL Microbiome 3:14-14(2015). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KPL17991.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LJUY01000045; KPL17991.1; -; Genomic_DNA. DR PATRIC; fig|1703428.3.peg.1780; -. DR Proteomes; UP000051415; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000051415}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000051415}. FT DOMAIN 201 368 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 431 AA; 48898 MW; D9F9539900F1B851 CRC64; MYKTQQNNAR EKALLVAVKL PHSDGWPPED TLQELALLAD TAGADVLDTI IQARKQLDPA TLIGEGKVVQ IAQRVQQLDA NLVIFDDDLT PAQARNLERT IDVKILDRSA LILDIFARRA KSKEAKTQVE LAQLKYLLPR LTRQWTHLSR QEGGIGTRGP GETQLEVDRR RIRKRIADLS VALKRIAERR EVRRKRRKGE FTVALVGYTN TGKSTLLNAL SQADVYTENK LFATLDPTTR TVHLNGEKKV LITDTVGLIR KLPHHLIASF HSTLEELAAV DLLLHIVDLS HEMFAEQMKT VQEVLEQLGA HTRPLLLVFN KIDKISHLPK LPLRLEREYP QAVFISALQG TGFKQLSQGI LRHFQQQMLE LSLNLSLSNA KLLSQIYSVG EVLERHDLPK GVSLRVRLRW EDAHRLQKKL SLLPLRNPHL K // ID A0A0S8KHE7_9BACT Unreviewed; 144 AA. AC A0A0S8KHE7; DT 17-FEB-2016, integrated into UniProtKB/TrEMBL. DT 17-FEB-2016, sequence version 1. DT 08-JUN-2016, entry version 5. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:KPL21303.1}; DE Flags: Fragment; GN ORFNames=AMJ75_10250 {ECO:0000313|EMBL:KPL21303.1}; OS Phycisphaerae bacterium SM1_79. OC Bacteria; Planctomycetes; Phycisphaerae. OX NCBI_TaxID=1703410 {ECO:0000313|EMBL:KPL21303.1, ECO:0000313|Proteomes:UP000053139}; RN [1] {ECO:0000313|EMBL:KPL21303.1, ECO:0000313|Proteomes:UP000053139} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SM1_79 {ECO:0000313|EMBL:KPL21303.1}; RX PubMed=25922666; DOI=10.1186/s40168-015-0077-6; RA Baker B.J., Lazar C.S., Teske A.P., Dick G.J.; RT "Genomic resolution of linkages in carbon, nitrogen, and sulfur RT cycling among widespread estuary sediment bacteria."; RL Microbiome 3:14-14(2015). CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KPL21303.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LJVF01000148; KPL21303.1; -; Genomic_DNA. DR Proteomes; UP000053139; Unassembled WGS sequence. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000053139}; KW Reference proteome {ECO:0000313|Proteomes:UP000053139}. FT DOMAIN 27 112 GTP-bdg_N. {ECO:0000259|Pfam:PF13167}. FT DOMAIN 115 144 GTP-bdg_M. {ECO:0000259|Pfam:PF16360}. FT NON_TER 144 144 {ECO:0000313|EMBL:KPL21303.1}. SQ SEQUENCE 144 AA; 16368 MW; BEFEC3EAF998D0CE CRC64; MEKLRQTLRV RKERAILVAA VPDGGDDLAE LAALAESAGA VVVDRFQQRI RTINPSTYIG KGKAEQLRAR VRQSKADVVI FDNDLSPGQI RELEKIIEIK VLDRSELILD IFSTRAKTRQ AKLQVELAQL EYTYPRLARM WSHL // ID A0A0S8KNE6_9CHLR Unreviewed; 434 AA. AC A0A0S8KNE6; DT 17-FEB-2016, integrated into UniProtKB/TrEMBL. DT 17-FEB-2016, sequence version 1. DT 07-JUN-2017, entry version 9. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=AMJ93_04975 {ECO:0000313|EMBL:KPL23328.1}; OS Anaerolineae bacterium SM23_84. OC Bacteria; Chloroflexi; Anaerolineae; unclassified Anaerolineae. OX NCBI_TaxID=1703388 {ECO:0000313|EMBL:KPL23328.1, ECO:0000313|Proteomes:UP000052016}; RN [1] {ECO:0000313|EMBL:KPL23328.1, ECO:0000313|Proteomes:UP000052016} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SM23_84 {ECO:0000313|EMBL:KPL23328.1}; RX PubMed=25922666; DOI=10.1186/s40168-015-0077-6; RA Baker B.J., Lazar C.S., Teske A.P., Dick G.J.; RT "Genomic resolution of linkages in carbon, nitrogen, and sulfur RT cycling among widespread estuary sediment bacteria."; RL Microbiome 3:14-14(2015). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KPL23328.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LJUZ01000052; KPL23328.1; -; Genomic_DNA. DR PATRIC; fig|1703388.3.peg.182; -. DR Proteomes; UP000052016; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000052016}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000052016}. FT DOMAIN 215 381 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 174 211 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 434 AA; 47769 MW; E29F9D2FCEDB9BD2 CRC64; MARRSAPAEA PTERAYLVGA QVKGATYPLR LEDSLCELAQ LARTAGVEVV GQIQQRLEAI SPATYIGKGK VAELGVLAQE LDLDTVIFDD ELSPNQQRNL EEALGVKVID RTALILDIFA KHARTREGAL QVELAQYVYR LPRLTRAWTH LARQAGGSAG RGGIGGVGLR GPGESQLETD RRIINQRIAQ LKKELESVRR HRKQYRRHRE NQGLPVVSLV GYTNAGKSTL LNTLTDAGVV TTDMLFATLD PVTRRLILPG GKEVLLTDTV GFIQKLPTQL VAAFRATLEE INEADLILHV VDITHINVRE QARTVEQVLN EIGANRKPVL VALNKVDLLS EPEKAQRIAT QYPKAVAISA LYGWGLDDLL ATIESMLAQQ MARLRVHIPY AANELVALFH KHGVVVHEHH GQTGITIEGK LPSNLMGRFE PYLA // ID A0A0S8KTW8_9BACE Unreviewed; 397 AA. AC A0A0S8KTW8; DT 17-FEB-2016, integrated into UniProtKB/TrEMBL. DT 17-FEB-2016, sequence version 1. DT 07-JUN-2017, entry version 10. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=AMS23_05005 {ECO:0000313|EMBL:KPL25321.1}; OS Bacteroides sp. SM1_62. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae; OC Bacteroides. OX NCBI_TaxID=1703351 {ECO:0000313|EMBL:KPL25321.1, ECO:0000313|Proteomes:UP000054347}; RN [1] {ECO:0000313|EMBL:KPL25321.1, ECO:0000313|Proteomes:UP000054347} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SM1_62 {ECO:0000313|EMBL:KPL25321.1}; RX PubMed=25922666; DOI=10.1186/s40168-015-0077-6; RA Baker B.J., Lazar C.S., Teske A.P., Dick G.J.; RT "Genomic resolution of linkages in carbon, nitrogen, and sulfur RT cycling among widespread estuary sediment bacteria."; RL Microbiome 3:14-14(2015). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KPL25321.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LJVC01000090; KPL25321.1; -; Genomic_DNA. DR PATRIC; fig|1703351.3.peg.265; -. DR Proteomes; UP000054347; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000054347}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000054347}. FT DOMAIN 202 386 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 170 197 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 397 AA; 45750 MW; C639D39EB9AC8279 CRC64; MPEPLITTPK PETAILIGII DQYQDAVTVE EYLQELAFLT ETAGAIPEKT FVQKLAYPDP RTFVGSGKLL EIREYVAMND TDLVIFDDEL TPSQLRNIER ELNCRILDRT NLILDIFARR AKTAHAKTQV ELAQYEYLLP RLTRMWTHLE RQRGGIGLRG PGETEIETDR RIIRDKIAKL KEDLKRIDKQ KSVQRKNRGK MVRVALVGYT NVGKSTLMNV VSKSDIFAEN KLFATLDTTI RKVVIGNLPF LLSDTVGFIR KLPHTLVESF KSTLDEVRES DILLHVVDIS HPNFEEQIDI VNQTLLEIDA RHKPTYIVFN KIDAFRYVAK DEDDLGPYTS ENMSLDDLKK SWMAKSNGAC VFISAKKLEN IQEIRDLLYD KVKEIHARRY PYDDFLY // ID A0A0S8KXD5_9PROT Unreviewed; 439 AA. AC A0A0S8KXD5; DT 17-FEB-2016, integrated into UniProtKB/TrEMBL. DT 17-FEB-2016, sequence version 1. DT 07-JUN-2017, entry version 10. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=AMJ72_12385 {ECO:0000313|EMBL:KPL26603.1}; OS Acidithiobacillales bacterium SM1_46. OC Bacteria; Proteobacteria; Acidithiobacillia; Acidithiobacillales. OX NCBI_TaxID=1703384 {ECO:0000313|EMBL:KPL26603.1, ECO:0000313|Proteomes:UP000052054}; RN [1] {ECO:0000313|EMBL:KPL26603.1, ECO:0000313|Proteomes:UP000052054} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SM1_46 {ECO:0000313|EMBL:KPL26603.1}; RX PubMed=25922666; DOI=10.1186/s40168-015-0077-6; RA Baker B.J., Lazar C.S., Teske A.P., Dick G.J.; RT "Genomic resolution of linkages in carbon, nitrogen, and sulfur RT cycling among widespread estuary sediment bacteria."; RL Microbiome 3:14-14(2015). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KPL26603.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LJVB01000146; KPL26603.1; -; Genomic_DNA. DR PATRIC; fig|1703384.3.peg.960; -. DR Proteomes; UP000052054; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000052054}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000052054}. FT DOMAIN 204 370 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 439 AA; 48730 MW; BBBE9672E6E69AB9 CRC64; MTRFYPTASE VETFLLVELR LPRESARQAQ LRLAELERLV ESTGGLVAES DTVTLRRVDP GYFLSQRRCA QIAARIAELG VTGVVFDAPL SPAQSRNLEQ ICTVKVLDRT AVILDIFARR ARTHEGRLQV ELAQLRYLLP RLTGRGREMS RLGGGIGTRG PGETQLETDR RRILARIGQL QKAIEAIRRH RGPQRRRRLR TALPTAAIVG YTNAGKSTLI NRLTGSSIFT ADQLFATLDP TTRALVLPHG IRLAVIDTVG FIRDLPSSLA VAFRATLEEM NYADLLVEIV DISSPNRTEE LNTTERVLAD LGLGGMARIL VWNKIDQLDG VPARDVQTPS GHPQVEVSAL TGEGIEALLL EIERLLTGDY VLDTFLISYD QLEQLSELHR RAQIVSERYE ESGLRVTARV PPDMATRLSR YQVSGDEDRP SESVGTLPT // ID A0A0S8L4F8_9PROT Unreviewed; 424 AA. AC A0A0S8L4F8; DT 17-FEB-2016, integrated into UniProtKB/TrEMBL. DT 17-FEB-2016, sequence version 1. DT 07-JUN-2017, entry version 9. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=AMJ72_04625 {ECO:0000313|EMBL:KPL28224.1}; OS Acidithiobacillales bacterium SM1_46. OC Bacteria; Proteobacteria; Acidithiobacillia; Acidithiobacillales. OX NCBI_TaxID=1703384 {ECO:0000313|EMBL:KPL28224.1, ECO:0000313|Proteomes:UP000052054}; RN [1] {ECO:0000313|EMBL:KPL28224.1, ECO:0000313|Proteomes:UP000052054} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SM1_46 {ECO:0000313|EMBL:KPL28224.1}; RX PubMed=25922666; DOI=10.1186/s40168-015-0077-6; RA Baker B.J., Lazar C.S., Teske A.P., Dick G.J.; RT "Genomic resolution of linkages in carbon, nitrogen, and sulfur RT cycling among widespread estuary sediment bacteria."; RL Microbiome 3:14-14(2015). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KPL28224.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LJVB01000027; KPL28224.1; -; Genomic_DNA. DR PATRIC; fig|1703384.3.peg.1180; -. DR Proteomes; UP000052054; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000052054}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000052054}. FT DOMAIN 183 349 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 424 AA; 47547 MW; D78383C80AC3955E CRC64; MRLDGRNVDE DAEELRLLAL SAGADVRGTI FGSRQIPDAA TFVGKGKAEE IREAVAREQT DLIVVNHELS PAQERNLEKL VGCRVLDRTG LILDIFAQRA RSHEGKLQVE LAQLEHLATR LVRGWTHLER QKGGIGLRGP GETQLEVDRR LIRDRIKKLH ERLAQVTVQR RSRRRARERV PIPTVSLVGY TNAGKSSLFN HLTGAGVYAA DQLFATLDPT MRRLELSGNA NIILTDTVGF VRHLPHDLVE AFKSTLEEVA EANLLLHVVD ASSSERIEQM QQVNIVLTEI AASEIPQIVI FNKIDLSGEA PHSERDAAGR IARIWLSART GQGVELLRDA LSEHYRRTRQ LLRLHLPPAA GRLRALLYER FDVRGEEQIE SGGWRIDVEL DAAKLEWLQR QAEFDPSFIV QEKPRVLAPT GSCP // ID A0A0S9BXH4_9MICC Unreviewed; 522 AA. AC A0A0S9BXH4; DT 17-FEB-2016, integrated into UniProtKB/TrEMBL. DT 17-FEB-2016, sequence version 1. DT 30-AUG-2017, entry version 17. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=ASE96_14575 {ECO:0000313|EMBL:KQN86099.1}; OS Arthrobacter sp. Leaf69. OC Bacteria; Actinobacteria; Micrococcales; Micrococcaceae; Arthrobacter. OX NCBI_TaxID=1736232 {ECO:0000313|EMBL:KQN86099.1, ECO:0000313|Proteomes:UP000051467}; RN [1] {ECO:0000313|EMBL:KQN86099.1, ECO:0000313|Proteomes:UP000051467} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Leaf69 {ECO:0000313|EMBL:KQN86099.1, RC ECO:0000313|Proteomes:UP000051467}; RA Millard Andrew; RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:KQN86099.1, ECO:0000313|Proteomes:UP000051467} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Leaf69 {ECO:0000313|EMBL:KQN86099.1, RC ECO:0000313|Proteomes:UP000051467}; RA Vorholt J.; RT "Functional overlap of the Arabidopsis leaf and root microbiotas."; RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KQN86099.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LMLR01000014; KQN86099.1; -; Genomic_DNA. DR RefSeq; WP_056432383.1; NZ_LMLR01000014.1. DR EnsemblBacteria; KQN86099; KQN86099; ASE96_14575. DR Proteomes; UP000051467; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 2. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000051467}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}. FT DOMAIN 301 466 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 522 AA; 56553 MW; 005A4676E8D1297B CRC64; MTSQPNTGPE SAAQDMSPAE IQAVIDRILA KDTPARKAAP AAGEPAPVLG KAQAISRLDE EHSTFDGDQQ DLEERHALRR TAGLSTELED VTEVEYRQLR LERVVLAGLW TEGTLADAEN SLRELAALAE TAGSEVLDGI VQRRQKPDPG TFLGSGKAQE LKDIVMSTGA DTVVVDAELA PSQRRSLEDI VKVKVIDRTA LILDIFAQHA KSREGKAQVE LAQLEYLLPR LRGWGDSMSR QAGGQVGGAG AGMGSRGPGE TKIELDRRRI RTRMAKLRRE IAAMKPARET KRANRRRNSV PSVAIAGYTN AGKSSLLNRL TDAGVLVENA LFATLDPTVR KAETSDGLGY TLADTVGFVR SLPTQLVEAF RSTLEEVADA DLILHVVDVS HPDPEGQIAA VRKVFSEVDA RKVPEIIVLN KADAADPFVV ERLKQREPRH VVVSARTGAG IPELLKAISE GIPRPSVKLE LMIPYNRGDL LSKLHEADAE ILSLNHEEAG TRAVVMVREG FAAELDSFIS ND // ID A0A0S9CHC1_9SPHN Unreviewed; 430 AA. AC A0A0S9CHC1; DT 17-FEB-2016, integrated into UniProtKB/TrEMBL. DT 17-FEB-2016, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=ASE95_10650 {ECO:0000313|EMBL:KQN93034.1}; OS Sphingomonas sp. Leaf231. OC Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales; OC Sphingomonadaceae; Sphingomonas. OX NCBI_TaxID=1736301 {ECO:0000313|EMBL:KQN93034.1, ECO:0000313|Proteomes:UP000051427}; RN [1] {ECO:0000313|EMBL:KQN93034.1, ECO:0000313|Proteomes:UP000051427} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Leaf231 {ECO:0000313|EMBL:KQN93034.1, RC ECO:0000313|Proteomes:UP000051427}; RA Millard Andrew; RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:KQN93034.1, ECO:0000313|Proteomes:UP000051427} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Leaf231 {ECO:0000313|EMBL:KQN93034.1, RC ECO:0000313|Proteomes:UP000051427}; RA Vorholt J.; RT "Functional overlap of the Arabidopsis leaf and root microbiotas."; RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KQN93034.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LMLS01000002; KQN93034.1; -; Genomic_DNA. DR RefSeq; WP_056635414.1; NZ_LMLS01000002.1. DR EnsemblBacteria; KQN93034; KQN93034; ASE95_10650. DR Proteomes; UP000051427; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000051427}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000051427}. FT DOMAIN 208 377 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 174 201 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 430 AA; 47027 MW; 59398F5DA746F7D8 CRC64; MSTGFDRDRD EFTRGARAIV VYPDLGGSSR DADARLEETA GLAGAIGVVV VDRVALRVRT PRAATLIGSG QIEELAARAR MEDAGLVVFD GNLTPIQQRN LETALEAKVI DRTGLILEIF GERAATAEGR LQVELAHLDY QSGRLVRSWT HLERQRGGFG FLGGPGETQI EADRRLIRDR MARLRRELEQ VTRTRGLHRE RRQRAPWPVI ALVGYTNAGK STLFNRLTGA HVMAEDLLFA TLDPTLRQIS LPGIDKAILS DTVGFVSELP TQLVAAFKAT LEEVVSADLL VHVRDVAHPD SAAQKADVEA VLAEVGVTDE TPVIEAWNKL DLIGGDTRED LLAEAQRRDD VVAISALTGE GVEALVRQVA ELLTQGHQRY ALSLDAGDGA AAAWLHAHGE VLDSHVEDAK VVYHVRMSPA DHERFLTREH // ID A0A0S9CYF8_9MICC Unreviewed; 525 AA. AC A0A0S9CYF8; DT 17-FEB-2016, integrated into UniProtKB/TrEMBL. DT 17-FEB-2016, sequence version 1. DT 07-JUN-2017, entry version 12. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=ASF21_13625 {ECO:0000313|EMBL:KQN98682.1}; OS Arthrobacter sp. Leaf234. OC Bacteria; Actinobacteria; Micrococcales; Micrococcaceae; Arthrobacter. OX NCBI_TaxID=1736303 {ECO:0000313|EMBL:KQN98682.1, ECO:0000313|Proteomes:UP000053418}; RN [1] {ECO:0000313|EMBL:KQN98682.1, ECO:0000313|Proteomes:UP000053418} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Leaf234 {ECO:0000313|EMBL:KQN98682.1, RC ECO:0000313|Proteomes:UP000053418}; RA Millard Andrew; RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:KQN98682.1, ECO:0000313|Proteomes:UP000053418} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Leaf234 {ECO:0000313|EMBL:KQN98682.1, RC ECO:0000313|Proteomes:UP000053418}; RA Vorholt J.; RT "Functional overlap of the Arabidopsis leaf and root microbiotas."; RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KQN98682.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LMLU01000008; KQN98682.1; -; Genomic_DNA. DR RefSeq; WP_055772480.1; NZ_LMLU01000008.1. DR EnsemblBacteria; KQN98682; KQN98682; ASF21_13625. DR Proteomes; UP000053418; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 2. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000053418}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000053418}. FT DOMAIN 304 469 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 525 AA; 57204 MW; 0A4BE63E17E3A7AD CRC64; MTTNNGHSTG ADMGPEEIQA VIDRILASDE AAVAKTKAGT WEQAAAPTEK TWRSRALALS DGDETSDADG DQQDLAERRA LRRVAGLSTE LEDVTEVEYR QLRLERVVLA GLWSEGTAQD AENSLQELAA LAETAGSEVL DGIVQRRLKP DPGTFLGSGK AQELKDIVQA TGADTVIVDS ELSPSQRRGL EDIVKVKVID RTALILDIFA QHAKSREGKA QVELAQLEYL LPRLRGWGES MSRQAGGQVG SAGAGMGSRG PGETKIELDR RKIRTRMAKL RREIAAMKPA RETKRSNRRR NQVPSVAIAG YTNAGKSSLL NRLTDAGVLV ENALFATLDP TIRRTETPDG IGYTLADTVG FVRSLPTQLI EAFRSTLEEV ADSDLILHVV DASHPDPEGQ IAAVRAVLTE VEARNVPEII VLNKADAADP FVIERLRQRE PRSVVVSART GAGLTELRQL ISTSIPRPGV KLDLMVPYEH GEIVSRLHEE DAEILGMEHV DEGTRLEVMV REGLAAELEP YVRHE // ID A0A0S9NDV3_9BURK Unreviewed; 394 AA. AC A0A0S9NDV3; DT 17-FEB-2016, integrated into UniProtKB/TrEMBL. DT 17-FEB-2016, sequence version 1. DT 05-JUL-2017, entry version 12. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=ASF44_07800 {ECO:0000313|EMBL:KQP43506.1}; OS Pseudorhodoferax sp. Leaf274. OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Comamonadaceae. OX NCBI_TaxID=1736318 {ECO:0000313|EMBL:KQP43506.1, ECO:0000313|Proteomes:UP000051759}; RN [1] {ECO:0000313|EMBL:KQP43506.1, ECO:0000313|Proteomes:UP000051759} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Leaf274 {ECO:0000313|EMBL:KQP43506.1, RC ECO:0000313|Proteomes:UP000051759}; RA Millard Andrew; RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:KQP43506.1, ECO:0000313|Proteomes:UP000051759} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Leaf274 {ECO:0000313|EMBL:KQP43506.1, RC ECO:0000313|Proteomes:UP000051759}; RA Vorholt J.; RT "Functional overlap of the Arabidopsis leaf and root microbiotas."; RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KQP43506.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LMNA01000012; KQP43506.1; -; Genomic_DNA. DR EnsemblBacteria; KQP43506; KQP43506; ASF44_07800. DR Proteomes; UP000051759; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000051759}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000051759}. FT DOMAIN 199 372 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 394 AA; 43729 MW; 63F5C12BD84A4262 CRC64; MPVADAAAAS AILVGVDFGL PHFDAELEEL GLLAQTAGLQ PVARVTCKRK APDAALFIGN GKAEEIKLLA RMHKATEVLF DQALSPAQQR NLERALELPV NDRTMLILTI FSQRARSHEG KLQVELARLQ YLSTRLVRRW SHLERQRGGI GTRGGPGERQ IELDRRMIGE SIKRTRERLS KVVRQRGTQR RQRERRDAFT ISLVGYTNAG KSSLFNAMVK ARAYAADQLF ATLDTTTRQL YLGEAGRSVS LSDTVGFIRD LPHGLVDAFR ATLQEAADAD LLLHVIDASN PHHPEQMEEV RRVLTDIGAD EVPMLLVFNK LDALTPEQRP LQLADTVEVD GRQIGRVFVS ARTGEGMPAL RAELARRAEQ LAPARAPDSP EYDEADPRFG TIVR // ID A0A0S9PYK8_9ACTN Unreviewed; 459 AA. AC A0A0S9PYK8; DT 17-FEB-2016, integrated into UniProtKB/TrEMBL. DT 17-FEB-2016, sequence version 1. DT 05-JUL-2017, entry version 12. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=ASF47_19735 {ECO:0000313|EMBL:KQP62748.1}; OS Nocardioides sp. Leaf285. OC Bacteria; Actinobacteria; Propionibacteriales; Nocardioidaceae; OC Nocardioides. OX NCBI_TaxID=1736322 {ECO:0000313|EMBL:KQP62748.1, ECO:0000313|Proteomes:UP000051495}; RN [1] {ECO:0000313|EMBL:KQP62748.1, ECO:0000313|Proteomes:UP000051495} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Leaf285 {ECO:0000313|EMBL:KQP62748.1, RC ECO:0000313|Proteomes:UP000051495}; RA Millard Andrew; RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:KQP62748.1, ECO:0000313|Proteomes:UP000051495} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Leaf285 {ECO:0000313|EMBL:KQP62748.1, RC ECO:0000313|Proteomes:UP000051495}; RA Vorholt J.; RT "Functional overlap of the Arabidopsis leaf and root microbiotas."; RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KQP62748.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LMNH01000006; KQP62748.1; -; Genomic_DNA. DR EnsemblBacteria; KQP62748; KQP62748; ASF47_19735. DR Proteomes; UP000051495; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 2. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000313|EMBL:KQP62748.1}; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000051495}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900, KW ECO:0000313|EMBL:KQP62748.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000051495}. FT DOMAIN 231 396 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 197 224 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 459 AA; 49830 MW; FFB1300AD9F87324 CRC64; MDLAERHQLR RVASLRTELE DITEVEYRQL RLERVVLVGV WTEGTTQDAE NSMAELALLA ETAGSEVLDA IYQRRQSPDP ATYVGRGKVE GLKEIVAATG ADTVICDGEL APSQLRNLED RLKVKVVDRT ALILDIFAQH AKSKEGQAQT ELAQLNYMKQ RLRGWGGNLS RQAGGRVAAG AGIGGRGPGE TKIETDRRRI NTKIAKLRRE LKEMKGTRDT KRADRKRHQI PAVAIAGYTN AGKSSLLNRL TSAGVLVEDS LFATLDPTTR RTTTSDGRVY TMSDTVGFVR HLPHQLVESF RSTLEEVADA DLLLHVVDGS HPDPEGQLAA VREVLAEIDA GDVPELVVIN KADAADPMVI ARLRAREPHS VVVSARTGEG IAEALAVIEA ELPHPEVAFE ALLPYDRGDL VNRLHQEGEI DSIEHTADGS LVRGRATEAL AGELAPYLLD AGVGTATIG // ID A0A0S9RCC8_9ACTN Unreviewed; 473 AA. AC A0A0S9RCC8; DT 17-FEB-2016, integrated into UniProtKB/TrEMBL. DT 17-FEB-2016, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=ASF37_01870 {ECO:0000313|EMBL:KQP79782.1}; OS Aeromicrobium sp. Leaf289. OC Bacteria; Actinobacteria; Propionibacteriales; Nocardioidaceae; OC Aeromicrobium. OX NCBI_TaxID=1736324 {ECO:0000313|EMBL:KQP79782.1, ECO:0000313|Proteomes:UP000051640}; RN [1] {ECO:0000313|EMBL:KQP79782.1, ECO:0000313|Proteomes:UP000051640} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Leaf289 {ECO:0000313|EMBL:KQP79782.1, RC ECO:0000313|Proteomes:UP000051640}; RA Millard Andrew; RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:KQP79782.1, ECO:0000313|Proteomes:UP000051640} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Leaf289 {ECO:0000313|EMBL:KQP79782.1, RC ECO:0000313|Proteomes:UP000051640}; RA Vorholt J.; RT "Functional overlap of the Arabidopsis leaf and root microbiotas."; RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KQP79782.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LMNK01000001; KQP79782.1; -; Genomic_DNA. DR RefSeq; WP_056578839.1; NZ_LMNK01000001.1. DR EnsemblBacteria; KQP79782; KQP79782; ASF37_01870. DR Proteomes; UP000051640; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 2. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000313|EMBL:KQP79782.1}; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000051640}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900, KW ECO:0000313|EMBL:KQP79782.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000051640}. FT DOMAIN 257 422 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 216 250 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 473 AA; 51224 MW; 1A67F1FD8AF7756B CRC64; MSRSTPTPGP DVDAESQRAT EGAHEGLELA ERQSLRRVAG LRTELEDITE VEYRQLRLER VVLVGVWTDG SAEDAENSLA ELKLLAETAG SEVLDALLQR RQRPDAATFI GSGKVEELTA AVQATGADTI ICDGELAPSQ LRNLEDRTKV KVVDRTALIL DIFAQHAKSA EGKAQVELAQ LQYQTQRLRG WGGNLSRQAG GRAAGGEGIG GRGPGETKLE TDRRRIQAKM AKLRRELKAL RTTRDIKKAQ RRRNAVPAVV IAGYTNAGKS SLLNRLTGAG VLVEDALFAT LDPTTRKTQA SDGRVYTMSD TVGFVRHLPH QLVEAFRSTL EEVAESDLVL HVVDASHPDP EGQIAAVREV FAEIDATGVP EIIVLNKADA ADPMMVNQLL AREPHAVLVS ARTGQGIDEL LAAVEADLPR PEARVDVVVP YDRGDLLSLV HQTGEIETLD HASDGTHLVA RVSDELAHQL NEL // ID A0A0T0PUA9_9SPHN Unreviewed; 430 AA. AC A0A0T0PUA9; DT 17-FEB-2016, integrated into UniProtKB/TrEMBL. DT 17-FEB-2016, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=ASG29_11910 {ECO:0000313|EMBL:KQT32477.1}; OS Sphingomonas sp. Leaf412. OC Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales; OC Sphingomonadaceae; Sphingomonas. OX NCBI_TaxID=1736370 {ECO:0000313|EMBL:KQT32477.1, ECO:0000313|Proteomes:UP000051178}; RN [1] {ECO:0000313|EMBL:KQT32477.1, ECO:0000313|Proteomes:UP000051178} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Leaf412 {ECO:0000313|EMBL:KQT32477.1, RC ECO:0000313|Proteomes:UP000051178}; RA Millard Andrew; RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:KQT32477.1, ECO:0000313|Proteomes:UP000051178} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Leaf412 {ECO:0000313|EMBL:KQT32477.1, RC ECO:0000313|Proteomes:UP000051178}; RA Vorholt J.; RT "Functional overlap of the Arabidopsis leaf and root microbiotas."; RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KQT32477.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LMQP01000003; KQT32477.1; -; Genomic_DNA. DR RefSeq; WP_055984108.1; NZ_LMQP01000003.1. DR EnsemblBacteria; KQT32477; KQT32477; ASG29_11910. DR Proteomes; UP000051178; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000051178}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000051178}. FT DOMAIN 208 377 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 174 201 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 430 AA; 46766 MW; 9DB6571FEE23704B CRC64; MSTGFERDRD EFSRGAKAVV VYPDLGGSAR DADSRLAETA GLAAAIGIEV VDRIAVKVRS PKAATLMGSG QVEEIATRAR MEDATLVVID GALTPIQQRN LETALAVKVI DRTGLILEIF GERAATAEGR LQVELAHLDY QSGRLVRSWT HLERQRGGFG FLGGPGETQI EADRRLIRDR MARLKRELEQ VTRTRGLHRE RRQRAPWPVV ALVGYTNAGK STLFNRLTGS DVMAEDLLFA TLDPTLRQIS LPGIDKAILS DTVGFVSELP TQLVAAFKAT LEEVVSADLL VHVRDVAHPD SAAQKADVEA VLAEVGVSET TPRIEAWNKL DLLDGDARED LLVEAMHRDD VAVLSALTGE GVDALVRRLG DLLTGGHVRY TVSLDAGDGA GAAWLHAHGE VLDREVEDDR AVYEVRMSPG DYDRFLTRGA // ID A0A0T1WJV2_9MYCO Unreviewed; 465 AA. AC A0A0T1WJV2; DT 17-FEB-2016, integrated into UniProtKB/TrEMBL. DT 17-FEB-2016, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=ASD37_04885 {ECO:0000313|EMBL:KQY09721.1}; OS Mycobacterium sp. Root135. OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae; OC Mycobacterium. OX NCBI_TaxID=1736457 {ECO:0000313|EMBL:KQY09721.1, ECO:0000313|Proteomes:UP000051127}; RN [1] {ECO:0000313|EMBL:KQY09721.1, ECO:0000313|Proteomes:UP000051127} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Root135 {ECO:0000313|EMBL:KQY09721.1, RC ECO:0000313|Proteomes:UP000051127}; RA Millard Andrew; RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:KQY09721.1, ECO:0000313|Proteomes:UP000051127} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Root135 {ECO:0000313|EMBL:KQY09721.1, RC ECO:0000313|Proteomes:UP000051127}; RA Vorholt J.; RT "Functional overlap of the Arabidopsis leaf and root microbiotas."; RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KQY09721.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LMEZ01000001; KQY09721.1; -; Genomic_DNA. DR RefSeq; WP_056548636.1; NZ_LMEZ01000001.1. DR EnsemblBacteria; KQY09721; KQY09721; ASD37_04885. DR Proteomes; UP000051127; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 2. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000313|EMBL:KQY09721.1}; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000051127}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900, KW ECO:0000313|EMBL:KQY09721.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000051127}. FT DOMAIN 242 411 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 201 228 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 465 AA; 50126 MW; 9333AA7D023C5312 CRC64; MTTPRLPSTG ELDLDDRSAL RRVAGLSTEL TDVTEVEYRQ LRLERVVLVG VWTDGTAADA DASMAELAAL AETAGSEVLE GMVQRRDKPD AGTYIGSGKA KELRDVVVAT GADTVICDGE LTPGQLNALE KAVKVKVVDR TALILDIFAQ HATSAEGKAQ VAFAQMEYML PRLRGWGESM SRQGGGAGGS GGGVGTRGPG ETKIETDRRR IRERMSKLRR EIKDMKKIRD TQRGRRLRSD AASIAIVGYT NAGKSSLLNA LTGAGVLVEN ALFATLEPTT RRGHLEDGRP FVLTDTVGFV RHLPTQLVEA FRSTLEEVVD AELLIHVIDG SDVNPLAQVN AVREVVNEVV REYDIAPPPE LLVVNKTDAA TGFGLAQLRR ALPDAVFVSA HTGDGLDQLR SRMSEMVEPT DLTVDVTIPY DRGELIARMH AEGRVDATEH TETGTRMKAR VPAALAAALA DFVTL // ID A0A0T1WV96_9RHIZ Unreviewed; 440 AA. AC A0A0T1WV96; DT 17-FEB-2016, integrated into UniProtKB/TrEMBL. DT 17-FEB-2016, sequence version 1. DT 05-JUL-2017, entry version 12. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=ASD31_10090 {ECO:0000313|EMBL:KQY14590.1}; OS Rhizobium sp. Root482. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium. OX NCBI_TaxID=1736543 {ECO:0000313|EMBL:KQY14590.1, ECO:0000313|Proteomes:UP000052057}; RN [1] {ECO:0000313|EMBL:KQY14590.1, ECO:0000313|Proteomes:UP000052057} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Root482 {ECO:0000313|EMBL:KQY14590.1, RC ECO:0000313|Proteomes:UP000052057}; RA Millard Andrew; RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:KQY14590.1, ECO:0000313|Proteomes:UP000052057} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Root482 {ECO:0000313|EMBL:KQY14590.1, RC ECO:0000313|Proteomes:UP000052057}; RA Vorholt J.; RT "Functional overlap of the Arabidopsis leaf and root microbiotas."; RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KQY14590.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LMFA01000021; KQY14590.1; -; Genomic_DNA. DR EnsemblBacteria; KQY14590; KQY14590; ASD31_10090. DR Proteomes; UP000052057; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000052057}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000052057}. FT DOMAIN 204 376 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 163 197 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 440 AA; 48752 MW; A77C2EEC034906E1 CRC64; MRALVIVPVL KKTGRQTQEP VATSTRSDDS RLQETIGLAL AIDLEVVHGM IVPVAQPKPG TLLGTGKIEE IGHLLSEHDA GLVIVDHPLT PVQQRNLEKE WNCKVIDRTG LILEIFGRRA STKEGTLQVD LAHLNYQKGR LVRSWTHLER QRGGAGFMGG PGETQIEADR RLLQDKIVKL EKELEQVRRT RQLHRAKRKK VPHPIVALVG YTNAGKSTLF NRITGAGVLA EDMLFATLDP TLRRMKLPHG RMVMLSDTVG FISDLPTHLV AAFRATLEEV LEADLILHVR DLSDPDNQVQ AQDVLRILTD LGIDEKARSE RLIEVWNKID LLDTETREGL VQKAENTENS AAVSAVTGEG VAELLDEIGK RLSGVMTECT VVLSAEKLQL LPWVYEHAIV DGRDDLEDGS VSLDLRLAPS EAEELERRLG NGPKAAPQDW // ID A0A0T2KRZ3_9MICO Unreviewed; 505 AA. AC A0A0T2KRZ3; DT 17-FEB-2016, integrated into UniProtKB/TrEMBL. DT 17-FEB-2016, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=ASD65_18465 {ECO:0000313|EMBL:KRA22455.1}; OS Microbacterium sp. Root61. OC Bacteria; Actinobacteria; Micrococcales; Microbacteriaceae; OC Microbacterium. OX NCBI_TaxID=1736570 {ECO:0000313|EMBL:KRA22455.1, ECO:0000313|Proteomes:UP000051216}; RN [1] {ECO:0000313|EMBL:KRA22455.1, ECO:0000313|Proteomes:UP000051216} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Root61 {ECO:0000313|EMBL:KRA22455.1, RC ECO:0000313|Proteomes:UP000051216}; RA Millard Andrew; RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:KRA22455.1, ECO:0000313|Proteomes:UP000051216} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Root61 {ECO:0000313|EMBL:KRA22455.1, RC ECO:0000313|Proteomes:UP000051216}; RA Vorholt J.; RT "Functional overlap of the Arabidopsis leaf and root microbiotas."; RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KRA22455.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LMGU01000002; KRA22455.1; -; Genomic_DNA. DR RefSeq; WP_056226234.1; NZ_LMGU01000002.1. DR EnsemblBacteria; KRA22455; KRA22455; ASD65_18465. DR Proteomes; UP000051216; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000051216}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000051216}. FT DOMAIN 287 452 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 505 AA; 54532 MW; C71F3203E92DEC87 CRC64; MTESTTPMST DETPVDPVDR VLARADAHSG VRVFGAAQAL QDETTVTRAD SDGAQWDREE RAALRRVPGL STELEDVTEV EYRQLRLENV VLVGVHPQGE QTDAENSLRE LAALAETAGA VVLDAVLQRR PHPDPATYIG RGKADELRSI VAALGADTVI ADTELAPSQR RALEDVVKVK VIDRTTVILD IFSQHAKSRE GKAQVELAQL EYLLPRLRGW GDSMSRQAGG QVGAGGAGMG SRGPGETKIE LDRRRIRTKM AILRRQIRDY GPAREAKRAE RKRNTIPSVA IAGYTNAGKS SLLNRLTSAG VLVENALFAT LDATVRRAEA SDGRVYTLTD TVGFVRNLPH QLVEAFRSTL EEVADADVIV HVVDAAHPDP AAQLQTVRDV MGDVGARDIP ELVVFNKADL VDDDTRLVLR GLEPKALFAS SRSGEGIDEL RAAIEAALPL PAVEVRAIVP YDRGDLVSAA HGSGHIVSQT HEAEGTALHA FVSERLAAEL APYRV // ID A0A0T2QF41_9SPHN Unreviewed; 441 AA. AC A0A0T2QF41; DT 17-FEB-2016, integrated into UniProtKB/TrEMBL. DT 17-FEB-2016, sequence version 1. DT 05-JUL-2017, entry version 12. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=ASD76_04780 {ECO:0000313|EMBL:KRA83372.1}; OS Altererythrobacter sp. Root672. OC Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales; OC Erythrobacteraceae; Altererythrobacter. OX NCBI_TaxID=1736584 {ECO:0000313|EMBL:KRA83372.1, ECO:0000313|Proteomes:UP000051125}; RN [1] {ECO:0000313|EMBL:KRA83372.1, ECO:0000313|Proteomes:UP000051125} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Root672 {ECO:0000313|EMBL:KRA83372.1, RC ECO:0000313|Proteomes:UP000051125}; RA Millard Andrew; RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:KRA83372.1, ECO:0000313|Proteomes:UP000051125} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Root672 {ECO:0000313|EMBL:KRA83372.1, RC ECO:0000313|Proteomes:UP000051125}; RA Vorholt J.; RT "Functional overlap of the Arabidopsis leaf and root microbiotas."; RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KRA83372.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LMHH01000001; KRA83372.1; -; Genomic_DNA. DR EnsemblBacteria; KRA83372; KRA83372; ASD76_04780. DR Proteomes; UP000051125; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000051125}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000051125}. FT DOMAIN 210 387 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 441 AA; 48676 MW; 28DB036DB557486C CRC64; MIVDDEFEGE VTRGARALVV CPDIRRKGRQ AEDPEARLEE AKGLAMAIGI VVAEAFIIPV RDVRAATLFG EGQIERIATA CEQDQAELVI IDGALSAIQQ RNLEEKLKRK VIDRTGLILE IFGERAATAE GRLQVELAHL DYQQSRLVRS WTHLERQRGG FGFLGGPGET QIEADRRLIR ARMGKLRRDL EQVRKTRALH RERRGRAPWP VIALVGYTNA GKSTLFNRMT GADVMAEDLL FATLDPAMRA VRLPGIDKAI LSDTVGFISD LPTQLVAAFR ATLEEVTAAD LIVHVRDMAN PDNSAQKGQV LHVLEDLGVV GAEESGEGGS IPILEAWNKL DLLDPNQRED LLDAAEENPD VVLISAHTGE GVEALEARVA SLLTEGHRRY RLELPLSDGA GAAWLHQNGE VLEHGIEGDR AWYEVRLSPG DMDRFKARER A // ID A0A0T2YBF6_9BURK Unreviewed; 394 AA. AC A0A0T2YBF6; DT 17-FEB-2016, integrated into UniProtKB/TrEMBL. DT 17-FEB-2016, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=ASE11_17020 {ECO:0000313|EMBL:KRB96285.1}; OS Hydrogenophaga sp. Root209. OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Comamonadaceae; Hydrogenophaga. OX NCBI_TaxID=1736490 {ECO:0000313|EMBL:KRB96285.1, ECO:0000313|Proteomes:UP000050889}; RN [1] {ECO:0000313|EMBL:KRB96285.1, ECO:0000313|Proteomes:UP000050889} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Root209 {ECO:0000313|EMBL:KRB96285.1, RC ECO:0000313|Proteomes:UP000050889}; RA Millard Andrew; RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:KRB96285.1, ECO:0000313|Proteomes:UP000050889} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Root209 {ECO:0000313|EMBL:KRB96285.1, RC ECO:0000313|Proteomes:UP000050889}; RA Vorholt J.; RT "Functional overlap of the Arabidopsis leaf and root microbiotas."; RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KRB96285.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LMIE01000033; KRB96285.1; -; Genomic_DNA. DR RefSeq; WP_056277689.1; NZ_LMIE01000033.1. DR EnsemblBacteria; KRB96285; KRB96285; ASE11_17020. DR Proteomes; UP000050889; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000050889}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000050889}. FT DOMAIN 202 375 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 394 AA; 42782 MW; 528D15C9CFD0E9E8 CRC64; MKSSETSSTP TPSVILVGVD FGTPHFDAPL EELGLLAQTA GYTVADRVTC KRRAPDPALF VGSGKADEIK LLAQSTGASE VLFDQSLSPA QQRNLERHLG MPVNDRTLLI LEIFAQRARS HEGKLQVELA RLQYLSTRLV RRWSHLERQS GGIGMRGGPG ETQIELDRRM IGDSIKRTKE RLEKVKKQRA TQRRQRERRD TFSISLVGYT NAGKSSLFNG LVKARAYAAD QLFATLDTTT RQLYLGEAGR SVSLSDTVGF IRDLPHGLVD AFAATLQEAA DADLLLHVVD ASNASHLEQI ASVMGVLKDI GADQVPQVLV FNKLDAMDEA VHPHALSDQM ELDGQPVPRI YVSAKTGEGL PALRALLAAQ VTNLNGGQGP MAPGAFPEME SPVS // ID A0A0T5NZK8_9RHOB Unreviewed; 425 AA. AC A0A0T5NZK8; DT 17-FEB-2016, integrated into UniProtKB/TrEMBL. DT 17-FEB-2016, sequence version 1. DT 07-JUN-2017, entry version 10. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=XM53_00800 {ECO:0000313|EMBL:KRS14305.1}; OS Roseovarius atlanticus. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae; Roseovarius. OX NCBI_TaxID=1641875 {ECO:0000313|EMBL:KRS14305.1, ECO:0000313|Proteomes:UP000051295}; RN [1] {ECO:0000313|EMBL:KRS14305.1, ECO:0000313|Proteomes:UP000051295} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=R12B {ECO:0000313|EMBL:KRS14305.1, RC ECO:0000313|Proteomes:UP000051295}; RA Li G., Lai Q., Shao Z., Yan P.; RT "The draft genome sequence of Roseovarius sp.R12b."; RL Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KRS14305.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LAXJ01000002; KRS14305.1; -; Genomic_DNA. DR RefSeq; WP_057789334.1; NZ_LAXJ01000002.1. DR EnsemblBacteria; KRS14305; KRS14305; XM53_00800. DR PATRIC; fig|1641875.4.peg.1245; -. DR Proteomes; UP000051295; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000051295}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000051295}. FT DOMAIN 204 374 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 425 AA; 46866 MW; F85C692A5CB6A268 CRC64; MTQTDVSDTR AWVLHPDIPS SDRERDPARA LEEAVSLAHA LPGLDVLGGS VVRLRDPHPG MLFSKGKLAD LKSLVEDNEV ELVLIDGPVS PVQQRNLEKQ LGVKLLDRTG LILEIFSDRA ATREGVLQVE MAALSYQRTR LVRAWTHLER QRGGLGFVGG PGETQIEADR RAIDEQLVRL RRQLDKVVKT RTLHRAARAK VPFPIVALVG YTNAGKSTLF NHLTGAEVMA KDMLFATLDP TMRKIALPGG GPEVILSDTV GFISDLPTEL VAAFRATLEE VLAADLIVHV RDISHPETEE QARDVHEILT SLGVLDTTPQ IEVWNKIDRL TPEDRTLAEN RAARLENVQL LSAITGEGMA VLSDTIIARL AGATRVETVS LGFEAGRKRA WLFEKGLVED EVQDEDGYSL TVRWNDTQKS QFDGL // ID A0A0T5P9Z3_9RHOB Unreviewed; 425 AA. AC A0A0T5P9Z3; DT 17-FEB-2016, integrated into UniProtKB/TrEMBL. DT 17-FEB-2016, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=SAMN04488031_101417 {ECO:0000313|EMBL:SFD53864.1}, GN XM52_10935 {ECO:0000313|EMBL:KRS18054.1}; OS Roseovarius indicus. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae; Roseovarius. OX NCBI_TaxID=540747 {ECO:0000313|EMBL:KRS18054.1, ECO:0000313|Proteomes:UP000051401}; RN [1] {ECO:0000313|EMBL:KRS18054.1, ECO:0000313|Proteomes:UP000051401} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=B108 {ECO:0000313|EMBL:KRS18054.1, RC ECO:0000313|Proteomes:UP000051401}; RA Li G., Lai Q., Shao Z., Yan P.; RT "The draft genome sequence of Roseovarius indicus B108T."; RL Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:SFD53864.1, ECO:0000313|Proteomes:UP000183238} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 26383 {ECO:0000313|EMBL:SFD53864.1, RC ECO:0000313|Proteomes:UP000183238}; RA de Groot N.N.; RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LAXI01000005; KRS18054.1; -; Genomic_DNA. DR EMBL; FOMY01000001; SFD53864.1; -; Genomic_DNA. DR RefSeq; WP_057816153.1; NZ_LAXI01000005.1. DR EnsemblBacteria; KRS18054; KRS18054; XM52_10935. DR PATRIC; fig|540747.5.peg.5113; -. DR Proteomes; UP000051401; Unassembled WGS sequence. DR Proteomes; UP000183238; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000051401}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000051401}. FT DOMAIN 204 374 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 425 AA; 46843 MW; 205D1A74326B85C3 CRC64; MTQTDTAATR AWVVHPDIPG DADARDPAYA LEEAVALAHA LPGLQVCGSN VVRLRQPHPG TLFSKGKLQE LQALIEAEEV ELLLVDGPVT PVQQRNLEKD LKVKLLDRTG LILEIFSDRA ATREGVLQVE MAALSYQRTR LVRAWTHLER QRGGLGFVGG PGETQIEADR RAIDEQLVRL KRQLEKVVKT RSLHRAARAK VPFPIVALVG YTNAGKSTLF NRMTGADVMA KDMLFATLDP TMRKIELPGN GPEVILSDTV GFISNLPTEL VAAFRATLEE VTAADLIVHV RDISHPESEE QAADVAAILE SLGVQKEVPQ IELWNKIDRV ETEARLVLEN RAGRSDNVYL MSAVTGEGIG DVVEAIKEEI AGVTSVEVLH LGFDDGRRRA WLFEKGLVED EAQDEDGYHL TVRWNARQAA QFEAI // ID A0A0T5ZGI1_9ARCH Unreviewed; 368 AA. AC A0A0T5ZGI1; DT 17-FEB-2016, integrated into UniProtKB/TrEMBL. DT 17-FEB-2016, sequence version 1. DT 07-JUN-2017, entry version 8. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=XU09_C0003G0052 {ECO:0000313|EMBL:KRT61841.1}; OS Thaumarchaeota archaeon CSP1-1. OC Archaea; Thaumarchaeota; unclassified Thaumarchaeota. OX NCBI_TaxID=1640512 {ECO:0000313|EMBL:KRT61841.1, ECO:0000313|Proteomes:UP000051388}; RN [1] {ECO:0000313|EMBL:KRT61841.1, ECO:0000313|Proteomes:UP000051388} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CSP1-1 {ECO:0000313|EMBL:KRT61841.1}; RA Hug L.A., Thomas B.C., Sharon I., Brown C.T., Sharma R., Hettich R.L., RA Wilkins M.J., Williams K.H., Singh A., Banfield J.F.; RT "Critical biogeochemical functions in the subsurface are associated RT with bacteria from new phyla and little studied lineages."; RL Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KRT61841.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LDXL01000003; KRT61841.1; -; Genomic_DNA. DR PATRIC; fig|1640512.3.peg.335; -. DR Proteomes; UP000051388; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000051388}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000051388}. FT DOMAIN 184 355 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 368 AA; 42050 MW; C332E7815AD67812 CRC64; MKTAILITYD INDSVNEALA LCDTANYRVS KIIKQDYLLR AKFGIGEGKV DEIKELIKKL RPDVIIYDEI LKPRQNYNLA SKLKIPIIDR ETLILEIFVN HAVSSESKLQ IKLAQLRYEM SRAKETVRLA KQGEQPGFLG IGKFEVDVYY NDIKHRIESI KSKLKKAGKQ RALHRQSRDR LGFKTISLAG YTSAGKTTLF NLLTGEDRQK GKELFTTLST TTRRLNIDRK AVLISDTVGF ISRLPAYMIE AFRSTLEELL YTDIVIVVVD ASDLQTELKK KFQSCTKTLN ELGVEPDKMI FALNKSDLIK PDKVIENTKY LKLDETKKWI PISAVTGENI LELKDLIGRM LELEKFEMTK KPIKAELD // ID A0A0T5ZM18_9CHLR Unreviewed; 436 AA. AC A0A0T5ZM18; DT 17-FEB-2016, integrated into UniProtKB/TrEMBL. DT 17-FEB-2016, sequence version 1. DT 07-JUN-2017, entry version 10. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=XU10_C0006G0004 {ECO:0000313|EMBL:KRT63859.1}; OS Chloroflexi bacterium CSP1-4. OC Bacteria; Chloroflexi. OX NCBI_TaxID=1640513 {ECO:0000313|EMBL:KRT63859.1, ECO:0000313|Proteomes:UP000051896}; RN [1] {ECO:0000313|EMBL:KRT63859.1, ECO:0000313|Proteomes:UP000051896} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CSP1-4 {ECO:0000313|EMBL:KRT63859.1}; RA Hug L.A., Thomas B.C., Sharon I., Brown C.T., Sharma R., Hettich R.L., RA Wilkins M.J., Williams K.H., Singh A., Banfield J.F.; RT "Critical biogeochemical functions in the subsurface are associated RT with bacteria from new phyla and little studied lineages."; RL Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KRT63859.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LDXM01000006; KRT63859.1; -; Genomic_DNA. DR PATRIC; fig|1640513.3.peg.701; -. DR Proteomes; UP000051896; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000051896}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000051896}. FT DOMAIN 206 374 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 165 192 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 436 AA; 47805 MW; 0B2010A723850CBD CRC64; MPTTSMIELA PPQERAFLVA VDTGDDPGWS AEDSLEELAA LATTAGAEVV GAEWQNRRHV DPNWYLGKGK AEELVQAKGE TGFTLLVADD ELKPNQQKAF EELLKVKVLD RSGLILDIFA QHAQTHEGRL QVELAQLEYQ LPRLTRLWTH LSRTGGGIGT RGPGETQLET DRRVIRDKIR KLKERVEVVR RQRETTARSR DRRLVPTVAI VGYTNAGKSS MLNALVGAEA AKVEDQLFAT LDPTSRAVKL GDGQSAIVTD TVGFIHKLPH QLVDAFRATL EEVNRADVLL EVVDASDRHR QEHRTTVQAV LTELGAGDKP RLVAYNKTDL IDPAATDGDR PGPAVGEAVH VSALTGYGLE TLRARLSALL AELWEDVDVA LPYAAGELLA RVRERGTVEV SYRARDVRVK GRVVPSLASE LRAAAEAWRA GARNET // ID A0A0T5ZUG9_9BACT Unreviewed; 440 AA. AC A0A0T5ZUG9; DT 17-FEB-2016, integrated into UniProtKB/TrEMBL. DT 17-FEB-2016, sequence version 1. DT 07-JUN-2017, entry version 9. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=XU11_C0008G0012 {ECO:0000313|EMBL:KRT66447.1}; OS Candidatus Dadabacteria bacterium CSP1-2. OC Bacteria; Candidatus Dadabacteria. OX NCBI_TaxID=1640508 {ECO:0000313|EMBL:KRT66447.1, ECO:0000313|Proteomes:UP000051780}; RN [1] {ECO:0000313|EMBL:KRT66447.1, ECO:0000313|Proteomes:UP000051780} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CSP1-2 {ECO:0000313|EMBL:KRT66447.1}; RA Hug L.A., Thomas B.C., Sharon I., Brown C.T., Sharma R., Hettich R.L., RA Wilkins M.J., Williams K.H., Singh A., Banfield J.F.; RT "Critical biogeochemical functions in the subsurface are associated RT with bacteria from new phyla and little studied lineages."; RL Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KRT66447.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LDXN01000008; KRT66447.1; -; Genomic_DNA. DR PATRIC; fig|1640508.3.peg.610; -. DR Proteomes; UP000051780; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000051780}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000051780}. FT DOMAIN 258 422 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 217 251 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 440 AA; 50072 MW; D14389ED2D5D5D4C CRC64; MLELKDGGIP GRFQIAHILP SNPQGEMWRI INYNDLGRVD INFEEFIRDI EHEFERSYFD SGGREEKEGV FLVGFSTKSR IEAEESVEEL KELARSAGKV VLDKTIQIRK QIDPKYLIGK GKLEEIILKA KQVGADTLIF DVELTPTQVR AISEETNLSV MDRTQLILDI FAERAKTSEG KIQVQLAQLR YMLPRLTGRG VELSKLGGGI GTRGPGEQKL EEQRRRLRER IGHLEKQIEE LSRRREHTRK QRRETGIPTV TLIGYTNVGK STLFNALTRS GVTVENKLFS TLNPTTRKLM LPSGREILLT DTVGFIRNLP KELVKAFRAT LEELGGSSLL IHVADASDPL VEEKIYSVEK ILDESGYSSI PRFIVFNKMD SSSKEVIDMF LKVFNAPLIS ALNKDNLTVF LQRLDVEIEK LTFYKQKEES SSNYLREIKV // ID A0A0T6A8J1_9BACT Unreviewed; 379 AA. AC A0A0T6A8J1; DT 17-FEB-2016, integrated into UniProtKB/TrEMBL. DT 17-FEB-2016, sequence version 1. DT 07-JUN-2017, entry version 10. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:KRT71254.1}; GN ORFNames=XU15_C0001G0005 {ECO:0000313|EMBL:KRT71254.1}; OS candidate division NC10 bacterium CSP1-5. OC Bacteria; candidate division NC10. OX NCBI_TaxID=1640516 {ECO:0000313|EMBL:KRT71254.1, ECO:0000313|Proteomes:UP000051123}; RN [1] {ECO:0000313|EMBL:KRT71254.1, ECO:0000313|Proteomes:UP000051123} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CSP1-5 {ECO:0000313|EMBL:KRT71254.1}; RA Hug L.A., Thomas B.C., Sharon I., Brown C.T., Sharma R., Hettich R.L., RA Wilkins M.J., Williams K.H., Singh A., Banfield J.F.; RT "Critical biogeochemical functions in the subsurface are associated RT with bacteria from new phyla and little studied lineages."; RL Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KRT71254.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LDXR01000001; KRT71254.1; -; Genomic_DNA. DR PATRIC; fig|1640516.3.peg.5; -. DR Proteomes; UP000051123; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000051123}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000051123}. FT DOMAIN 201 366 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 379 AA; 41713 MW; A0ADFE646FA9580A CRC64; MNAVFAPQRE VAVLIGLRRP HQSRWDAEDS LEELAQLAIS AGATPAFRVL QERSLPNPRT LIGPGKAEEV RAICEEGVDL VIFDDDLTGS QQRNLEGVLG RKVVDRTGLI LDIFAQRARS REGKLQVELA QLKYLLPRLT GHGVELSQLG GGIGTRGPGE TQLEVDRRRI RRRIVKIEEG LEKVRRHRAL LRRGRQKQAL LTAAFVGYTN AGKSSLLNAL THAALPVADK FFATLDPTVR KVIVPGGRVI LLSDTVGFIR KLPHQLVAAF KATLEEVRAS DFLLHVIDIS HPDWQNQSQA VMAVLGELGA AAKPLINVYN KVDKLPHPEA VAFLARRPRS VVVSARTGAG LDDLKYAMAE TLKTVEDATA VARDERRRP // ID A0A0T6AHI1_9DELT Unreviewed; 374 AA. AC A0A0T6AHI1; DT 17-FEB-2016, integrated into UniProtKB/TrEMBL. DT 17-FEB-2016, sequence version 1. DT 07-JUN-2017, entry version 10. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=XU12_C0002G0022 {ECO:0000313|EMBL:KRT74579.1}; OS Deltaproteobacteria bacterium CSP1-8. OC Bacteria; Proteobacteria; Deltaproteobacteria. OX NCBI_TaxID=1640514 {ECO:0000313|EMBL:KRT74579.1, ECO:0000313|Proteomes:UP000051991}; RN [1] {ECO:0000313|EMBL:KRT74579.1, ECO:0000313|Proteomes:UP000051991} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CSP1-8 {ECO:0000313|EMBL:KRT74579.1}; RA Hug L.A., Thomas B.C., Sharon I., Brown C.T., Sharma R., Hettich R.L., RA Wilkins M.J., Williams K.H., Singh A., Banfield J.F.; RT "Critical biogeochemical functions in the subsurface are associated RT with bacteria from new phyla and little studied lineages."; RL Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KRT74579.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LDXO01000002; KRT74579.1; -; Genomic_DNA. DR PATRIC; fig|1640514.3.peg.286; -. DR Proteomes; UP000051991; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000051991}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000051991}. FT DOMAIN 205 365 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 374 AA; 40666 MW; 433CF76681084157 CRC64; MTIPGSKSAE RAWLVWARRK KRPVPGVPPP ADPLGELKSL VEAAGGIVAG IHSQALSSEH PATLIGSGTV EHLKETVREH GVDLVVFQNL LRPNQQANLE RELGVKVLDR REVILDIFAR RARSREGKLQ IELAQLSFRL ARLIGGRRDL SRLGGGIGTR GPGEKKLEED RRRIRTHIRQ IERELATVRR TRTLHYRRRR EVGFPVVALV GYTNAGKSTL FNRITGADVF VAEQLFATLD PTARRFSLPG GGAAILVDTV GFIHDLPDEI REAFLATLEG IGEADLLVHV ADGISEMMEE NISSVEKILS GLGFSGKPRI LAINKSDLTG EAGHCPPGAI RISAATGSGI PGLLKQVEGG LWLHRSANGS TRRG // ID A0A0T6LZQ9_9ACTN Unreviewed; 505 AA. AC A0A0T6LZQ9; DT 17-FEB-2016, integrated into UniProtKB/TrEMBL. DT 17-FEB-2016, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=AQ490_01535 {ECO:0000313|EMBL:KRV51465.1}; OS Streptomyces vitaminophilus. OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae; OC Streptomyces. OX NCBI_TaxID=76728 {ECO:0000313|EMBL:KRV51465.1, ECO:0000313|Proteomes:UP000050867}; RN [1] {ECO:0000313|EMBL:KRV51465.1, ECO:0000313|Proteomes:UP000050867} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 31673 {ECO:0000313|EMBL:KRV51465.1, RC ECO:0000313|Proteomes:UP000050867}; RA Graham D.E., Mahan K.M., Klingeman D.M., Hettich R.L., Parry R.J.; RT "Draft genome sequence of pyrrolomycin-producing Streptomyces RT vitaminophilus."; RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KRV51465.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LLZU01000001; KRV51465.1; -; Genomic_DNA. DR RefSeq; WP_026219980.1; NZ_LLZU01000001.1. DR EnsemblBacteria; KRV51465; KRV51465; AQ490_01535. DR Proteomes; UP000050867; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000313|EMBL:KRV51465.1}; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000050867}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900, KW ECO:0000313|EMBL:KRV51465.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000050867}. FT DOMAIN 283 448 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 242 269 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 505 AA; 54873 MW; EA4D24E94C2E6A16 CRC64; MTSVLYPSHP NSGDKGAAAG KRGGRLPEDL RAEALMDDEF SHADEWDGEQ FDRTDRAALR RVVGLSTELE DVTEVEYRQL RLERVVLVGV WTSGTVEDAE NSLAELAALA ETAGSLVLDG VIQRRDKPDP ATYIGSGKAQ ELRDIVEATG ADTVVCDGEL TPGQLIHLED VVKVKVVDRT ALILDIFAQH AKSREGKAQV SLAQMQYMLP RLRGWGQSLS RQMGGGGSGS SGGGMATRGP GETKIETDRR RINQKMARLR REIAAMKTGR DLKRRERRQN RVPSVAIAGY TNAGKSSLLN RLTGAGVLVE NALFATLDPT VRRAQTPSGR VHTLADTVGF VRHLPHDLVE AFRSTMEEVA DADLILHVVD GAHAEPEAQL ATVREVIREV GASEVPEIVV INKADAADPE VLRRLLRLEP HAVAVSARTG EGIEELRARV DAELPRPSTE VEALVPFTRG DLVSRLHVEG ELLLEEHTAD GTRIRAMVDE LLASALAPYA VATQR // ID A0A0T6UJD0_9PSED Unreviewed; 433 AA. AC A0A0T6UJD0; DT 17-FEB-2016, integrated into UniProtKB/TrEMBL. DT 17-FEB-2016, sequence version 1. DT 30-AUG-2017, entry version 12. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=AO726_18935 {ECO:0000313|EMBL:KRW57737.1}; OS Pseudomonas sp. TTU2014-080ASC. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=1729724 {ECO:0000313|EMBL:KRW57737.1, ECO:0000313|Proteomes:UP000051864}; RN [1] {ECO:0000313|EMBL:KRW57737.1, ECO:0000313|Proteomes:UP000051864} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=TTU2014-080ASC {ECO:0000313|EMBL:KRW57737.1, RC ECO:0000313|Proteomes:UP000051864}; RA Webb H.E., Bugarel M., Den Bakker H.C., Nightingale K., Granier S.A., RA Loneragan G.H.; RT "Carbapenem-non-susceptible Bacteria Recovered from the Faeces of RT Dairy Cattle."; RL Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KRW57737.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LKKK01000015; KRW57737.1; -; Genomic_DNA. DR RefSeq; WP_058069688.1; NZ_LKKK01000015.1. DR EnsemblBacteria; KRW57737; KRW57737; AO726_18935. DR Proteomes; UP000051864; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000051864}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000051864}. FT DOMAIN 199 366 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 165 192 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 433 AA; 48710 MW; 5C45593456EADAFD CRC64; MFFERHEGGD RAILVHLDGQ NSEASEDPQE FQELALSAGA ETVAFFSIPS NKLAAKYLIG TGKVEELREQ VKATEADLVI FNHVLTPSQE RNLERAFECR VLDRTGLILD IFAQRARTHE GKLQVELAQL DHMSTRLVRG WTHLERQKGG IGLRGPGETQ LETDRRLLRV RMRQIKQKLE KVRSQREQAR RGRQRADIPS VSLVGYTNAG KSTLFNALTT SEVYAADQLF ATLDPTLRRL ELDDLGPVVL ADTVGFIRHL PHKLVEAFRA TLEESSNSDL LLHVIDSHEP ERDQQIEQVL AVLGEIGAHE LPILEVYNKL DLLEGVEPQI QRDANGKPQR VWLSARDGRG LPLLRQAIAE LLGNDLFVGT LQLPQRMGRL RAQLFSLGAV QRESHADDGS SLLEVRLPTT ELNRLVSREG FSPPDFIEQH TLQ // ID A0A0T7BVN9_9CYAN Unreviewed; 595 AA. AC A0A0T7BVN9; DT 17-FEB-2016, integrated into UniProtKB/TrEMBL. DT 17-FEB-2016, sequence version 1. DT 05-JUL-2017, entry version 14. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=IJ00_19645 {ECO:0000313|EMBL:AKG23192.1}; OS Calothrix sp. 336/3. OC Bacteria; Cyanobacteria; Nostocales; Rivulariaceae; Calothrix. OX NCBI_TaxID=1337936 {ECO:0000313|EMBL:AKG23192.1, ECO:0000313|Proteomes:UP000065745}; RN [1] {ECO:0000313|EMBL:AKG23192.1, ECO:0000313|Proteomes:UP000065745} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=336/3 {ECO:0000313|EMBL:AKG23192.1, RC ECO:0000313|Proteomes:UP000065745}; RX PubMed=25614574; RA Isojarvi J., Shunmugam S., Sivonen K., Allahverdiyeva Y., Aro E.M., RA Battchikova N.; RT "Draft genome sequence of calothrix strain 336/3, a novel h2-producing RT cyanobacterium isolated from a finnish lake."; RL Genome Announc. 3:0-0(2015). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP011382; AKG23192.1; -; Genomic_DNA. DR EnsemblBacteria; AKG23192; AKG23192; IJ00_19645. DR KEGG; calh:IJ00_19645; -. DR KO; K03665; -. DR Proteomes; UP000065745; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000065745}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000065745}. FT DOMAIN 421 591 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 380 414 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 595 AA; 65621 MW; B0E822DBE1C4A620 CRC64; MHLGEPGNWS KMPIETIFGN LHGLKTSQMK QLQRLYHQRI PGDRVTTPEF SQRLAAISTE INLPVCAYLN RRGQVIRVGV GTPRQTQIPP VELPRYGAER LSGIRCIATQ LKPEPPNDGA LTAMAIQRLD ALVVLNITGS GFQRRGGGAT GYVKEAYLAH LTTQESQALI ASLTGNNTET NLPSVASWQV SAPMSLDDLS QQDFIDLVEA LEADFSREFV AQEVDTSSDR VVIVGVMTDE GKTLQFQDTL AELARLVDTA GGGVLQTIWQ KRSRIHPQTV VGEGKVQEIA LTAQTLGANL IVFDRDLSPS QIRNLEAHIG IRVIDRTEVI LDIFAQRAQS RAGKLQVELA QLEYMLPRLT GRGQAMSRLG GGIGTRGPGE TKLETERRAI QRRISRLQQE VNQLQAHRAR LRQRRQHREV PSVALVGYTN AGKSTLLNAL TNAEVYTADQ LFATLDPTTR RLVIPHGNIP GSQEILITDT VGFIHELPAS LMDAFRATLE EVTESDALLH LVDLSHPAWL SHIRSVRDIL AQMPITPGPA LVVFNKIDEV NSETLEQARE EFPLAIFISA SHRLGLETLR QRLSQLIEYV LGGGQ // ID A0A0T7Q2S6_BORPT Unreviewed; 376 AA. AC A0A0T7Q2S6; DT 17-FEB-2016, integrated into UniProtKB/TrEMBL. DT 17-FEB-2016, sequence version 1. DT 12-APR-2017, entry version 10. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:CFT88058.1}; GN ORFNames=ERS005128_00355 {ECO:0000313|EMBL:CFT88058.1}; OS Bordetella pertussis. OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Alcaligenaceae; Bordetella. OX NCBI_TaxID=520 {ECO:0000313|EMBL:CFT88058.1, ECO:0000313|Proteomes:UP000047656}; RN [1] {ECO:0000313|EMBL:CFT88058.1, ECO:0000313|Proteomes:UP000047656} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=B161 {ECO:0000313|EMBL:CFT88058.1, RC ECO:0000313|Proteomes:UP000047656}; RA Murphy D.; RL Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CGFF01000021; CFT88058.1; -; Genomic_DNA. DR EnsemblBacteria; CFT88058; CFT88058; ERS005128_00355. DR Proteomes; UP000047656; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000047656}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000047656}. FT DOMAIN 198 362 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 376 AA; 41221 MW; AAE97E2A12A8FA90 CRC64; MRALIISVDL GNPDYPAHAE EFAMLAKGAG AEIVGTLTAR RDRPDAKFFI GSGKVEEGVA MAGALLADII LFDQPLSPAQ QRNLEREFNL RVVDRVALIL DIFALRAKSH EGKLQVELAQ LQHLATRLTR MWSHLERQRG XXXXXXXXXX XMRGPGEAQL EMDRRMIGAK VKVLRERLDR VERQRVTQRR ARARGGALSV SLVGYTNAGK STLFNAMTRA GAYAADQLFA TLDTTTRRIW IDGAGSVVLS DTVGFIRDLP HNLIAAFRAT LEETVYADLL LHVVDAASAQ RDEQIAEVDK VLAEIGAAQI PTILVYNKID RAGLEPRVDR DAHGTIARVF VSATERAGLD ALRGAIAEIG QIVGNNVSNH QTLQSE // ID A0A0T7RSH9_SALET Unreviewed; 426 AA. AC A0A0T7RSH9; DT 17-FEB-2016, integrated into UniProtKB/TrEMBL. DT 17-FEB-2016, sequence version 1. DT 30-AUG-2017, entry version 17. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:CFW72904.1}; GN ORFNames=ERS008215_01915 {ECO:0000313|EMBL:CFW72904.1}; OS Salmonella enterica subsp. enterica serovar Bovismorbificans. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; OC Enterobacteriaceae; Salmonella. OX NCBI_TaxID=58097 {ECO:0000313|EMBL:CFW72904.1, ECO:0000313|Proteomes:UP000048853}; RN [1] {ECO:0000313|EMBL:CFW72904.1, ECO:0000313|Proteomes:UP000048853} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=A31126 {ECO:0000313|EMBL:CFW72904.1, RC ECO:0000313|Proteomes:UP000048853}; RA Murphy D.; RL Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CGIA01000005; CFW72904.1; -; Genomic_DNA. DR RefSeq; WP_000460338.1; NZ_MZFY01000001.1. DR ProteinModelPortal; A0A0T7RSH9; -. DR EnsemblBacteria; CFW72904; CFW72904; ERS008215_01915. DR Proteomes; UP000048853; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000048853}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Hydrolase {ECO:0000313|EMBL:CFW72904.1}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Protease {ECO:0000313|EMBL:CFW72904.1}. FT DOMAIN 198 365 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 164 191 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 426 AA; 48262 MW; 229CAE358920A78F CRC64; MFDRYDAGEQ AVLVHIYFSQ DKDMEDLQEF ESLVSSAGVE AMQVITGSRK APHPKYFVGE GKAVEIAEAV KATGAAVVLF DHALSPAQER NLERLCECRV IDRTGLILDI FAQRARTHEG KLQVELAQLR HLATRLVRGW THLERQKGGI GLRGPGETQL ETDRRLLRNR IVQIQSRLEK VEKQREQGRQ SRIKADVPTV SLVGYTNAGK STLFNQITEA RVYAADQLFA TLDPTLRRID VADVGETVLA DTVGFIRHLP HDLVAAFKAT LQETRQATLL LHVVDAADVR VQENIEAVNT VLEEIDAHEI PTLMVMNKID MLDDFEPRID RDEENKPIRV WLSAQSGVGI PQLFQALTER LSGEVAQHTL RLPPQEGRLR SRFYQLQAIE KEWMEEDGSV SLQVRMPIVD WRRLCKQEPA LIEYVI // ID A0A0T9LC14_9GAMM Unreviewed; 426 AA. AC A0A0T9LC14; DT 17-FEB-2016, integrated into UniProtKB/TrEMBL. DT 17-FEB-2016, sequence version 1. DT 30-AUG-2017, entry version 12. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:CNE77328.1}; GN ORFNames=ERS137967_02490 {ECO:0000313|EMBL:CNE77328.1}; OS Yersinia nurmii. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; OC Yersiniaceae; Yersinia. OX NCBI_TaxID=685706 {ECO:0000313|EMBL:CNE77328.1, ECO:0000313|Proteomes:UP000040578}; RN [1] {ECO:0000313|EMBL:CNE77328.1, ECO:0000313|Proteomes:UP000040578} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=type strain: CIP110231 {ECO:0000313|Proteomes:UP000040578}; RA Murphy D.; RL Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CPYD01000009; CNE77328.1; -; Genomic_DNA. DR RefSeq; WP_049599277.1; NZ_CPYD01000009.1. DR EnsemblBacteria; CNE77328; CNE77328; ERS137967_02490. DR Proteomes; UP000040578; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000040578}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}. FT DOMAIN 198 365 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 426 AA; 47864 MW; 9F40990718E3A555 CRC64; MFDRYEAGEQ AVLVHIYFSQ DKDTENLSEF ESLVSSAGVE ALQIVTGSRK APHPKYFVGE GKAEEIADAV KASGASVVLF DHALSAAQER NLERLCECRV IDRTGLILDI FAQRARTHEG KLQVELAQLR HIATRLVRGW THLERQKGGI GLRGPGETQL ETDRRLLRDR ISLILNRLER VAKQREQNRR ARNRAEIPTV SLVGYTNAGK SSLFNRITSA DVYAADKLFA TLDPTLRRIN VADVGDTVLA DTVGFIRHLP HDLVAAFKAT LQETRQASLL LHVIDAADSR VSENVAAVDT VLAEIEADEI PTLLVMNKID MLDDFEPRID RNEENLPVRV WLSAETGAGI PLLFQALTER LSGEIAHYEL SLPPQAGRLR SRFYQLQAIE KEWIEEGGHI GMVVRLPIVE WRRLCKQEQE LIDYVV // ID A0A0U1A2N6_9MYCO Unreviewed; 496 AA. AC A0A0U1A2N6; DT 17-FEB-2016, integrated into UniProtKB/TrEMBL. DT 17-FEB-2016, sequence version 1. DT 30-AUG-2017, entry version 12. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX_1 {ECO:0000313|EMBL:CPW00971.1}; GN Synonyms=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=ERS075544_01723 {ECO:0000313|EMBL:CPW00971.1}; OS Mycobacterium abscessus. OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae; OC Mycobacterium. OX NCBI_TaxID=36809 {ECO:0000313|EMBL:CPW00971.1, ECO:0000313|Proteomes:UP000038470}; RN [1] {ECO:0000313|EMBL:CPW00971.1, ECO:0000313|Proteomes:UP000038470} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=PAP053 {ECO:0000313|EMBL:CPW00971.1, RC ECO:0000313|Proteomes:UP000038470}; RA Murphy D.; RL Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CSXB01000002; CPW00971.1; -; Genomic_DNA. DR EnsemblBacteria; CPW00971; CPW00971; ERS075544_01723. DR Proteomes; UP000038470; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000038470}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}. FT DOMAIN 276 445 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 235 269 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 496 AA; 53009 MW; F1E7A22EE1C01D86 CRC64; MVKSRTNGGA ALAPADNSDA FDEPRVGASV ASMRTTYETP TDGELVLEDR AALKRVAGLS TELADVTEVE YRQLRLERVV LVGVWTEGTS QEAEASMTEL AALAETAGSE VLEGLIQRRQ KPDPATYIGS GKAIELREIV LATGADTVIC DGELSPAQLV ALEKAVKVKV IDRTALILDI FAQHATSREG KAQVSLAQME YMLPRLRGWG ESMSRQAGGR AGGAGGGVGT RGPGETKIET DRRRIRERMS KLRREIRDMK KVRDTKRSRR LEGDVPSVAI VGYTNAGKSS LLNAITGAGV LVQDALFATL EPTTRRGTFD DGREFVITDT VGFVRHLPTQ LVEAFRSTLE EVADADLLVH VVDGSDMAPL AQIEAVRTVI GEVVADHDAS AAPELLVINK VDAAGDLALA QLRRALPKAL FVSAHTGEGI ATLREAIAEA VPRGDVPVDV VIPYERGDLV ARIHTEGQVQ STEHLADGTR VVGRVPRALA AVLTAL // ID A0A0U1ANK3_9MYCO Unreviewed; 413 AA. AC A0A0U1ANK3; DT 17-FEB-2016, integrated into UniProtKB/TrEMBL. DT 17-FEB-2016, sequence version 1. DT 30-AUG-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX_2 {ECO:0000313|EMBL:CPW37084.1}; GN Synonyms=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=ERS075544_05292 {ECO:0000313|EMBL:CPW37084.1}; OS Mycobacterium abscessus. OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae; OC Mycobacterium. OX NCBI_TaxID=36809 {ECO:0000313|EMBL:CPW37084.1, ECO:0000313|Proteomes:UP000038470}; RN [1] {ECO:0000313|EMBL:CPW37084.1, ECO:0000313|Proteomes:UP000038470} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=PAP053 {ECO:0000313|EMBL:CPW37084.1, RC ECO:0000313|Proteomes:UP000038470}; RA Murphy D.; RL Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CSXB01000014; CPW37084.1; -; Genomic_DNA. DR ProteinModelPortal; A0A0U1ANK3; -. DR EnsemblBacteria; CPW37084; CPW37084; ERS075544_05292. DR Proteomes; UP000038470; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000038470}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}. FT DOMAIN 196 354 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 413 AA; 47021 MW; 37464CC3DA31BEEB CRC64; MTTHEKVILV GVETEKNYQT FSASMEELAN LTETANGEVV FVLTQKRPQV DRQTVIGKGK LEELIQLTDA YEADLVIFNH ELTPRQNQLL SEALAVRVID RVQLILDIFA LRARSKEGKL QVELAQLDYL LPRLAGQGKQ LSRLGGGIGT RGPGETKLES DRRHIRNKIL GIRRELKEVT AHRERSRQKR QNSELFQIGL IGYTNAGKST ILNMLTTAGT YSEDQLFATL DPLTKKWQLP QGMEVTLTDT VGFIQDLPTQ LIEAFQSTLE ESRTMDLLLH VVDASAPDRL QHERTVQTLM KELALENIPC LTVYNKRDQV DSKEFVPTLF PNVLISTKIS EDKERLVQAI RAQMMELLEP YQLEISPTDG QLLSELRRMT LMISEEYAEN ENRYIVKGFA KKKSKWLAES EKE // ID A0A0U1L3U7_9FIRM Unreviewed; 597 AA. AC A0A0U1L3U7; DT 17-FEB-2016, integrated into UniProtKB/TrEMBL. DT 17-FEB-2016, sequence version 1. DT 07-JUN-2017, entry version 12. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=SpAn4DRAFT_0833 {ECO:0000313|EMBL:CQR74371.1}; OS Sporomusa sp. An4. OC Bacteria; Firmicutes; Negativicutes; Selenomonadales; Sporomusaceae; OC Sporomusa. OX NCBI_TaxID=411922 {ECO:0000313|EMBL:CQR74371.1, ECO:0000313|Proteomes:UP000049855}; RN [1] {ECO:0000313|EMBL:CQR74371.1, ECO:0000313|Proteomes:UP000049855} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Sporomusa ovata strain An4 {ECO:0000313|EMBL:CQR74371.1}; RA Murphy D.; RL Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CTRP01000014; CQR74371.1; -; Genomic_DNA. DR RefSeq; WP_021170372.1; NZ_CTRP01000014.1. DR EnsemblBacteria; CQR74371; CQR74371; SpAn4DRAFT_0833. DR Proteomes; UP000049855; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000049855}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000049855}. FT DOMAIN 376 541 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 597 AA; 66003 MW; 29A72ACF6F339C76 CRC64; MPEIYGEKNG LKKTIIENLE QLYEYTVPFG QTITDELAQA MRAIAEQLNK EIAVYINRRG NVVQVAVGDT KTVPLPETDG RRALNRLSGI RCIHTHPGGD SQLSSVDLAS LKKMRFDIMV ALAVRENVLE FSLGFISGHC PDSYEVQTVG PLSLAEFVQI DLNYLTNQIE QLLETKDVSS TIGQTEKALL VGIERQGEWD VNDSLSELAQ LAETAGAEVS GSVWQKRSRA DAALYIGRGK VQEISLIRQE LGVNVIIFDD ELSPAQQRNL EQALGVKVID RSALILDIFA QRAHSHEGKL QVELAQLKYN LPRLGGQGLV LSRLGGGIGT RGPGETKLEV DRRRIRTRIS DIEKAIENLK SHRSLHRERR QASEIPTIAL VGYTNAGKSS LLNKLTAAEV LAEDKLFATL DPTTRRSKLP GGQEILLTDT VGFIQKLPHQ LIAAFRGTLE EVVQADLLLH VIDASHPQFE KQSIAVYQVL KELGADTKPV ITVFNKIDKI DNEYVIERML RRTDSIAVSA VAGTHIDKLL AMIEGSIKAT SIDARLIIPY DDSGFMAKLY AVATVNSVEY QAEGIYVSAS LSPEYWERFK KYVVGDV // ID A0A0U1NHQ0_9RHOB Unreviewed; 428 AA. AC A0A0U1NHQ0; DT 17-FEB-2016, integrated into UniProtKB/TrEMBL. DT 17-FEB-2016, sequence version 1. DT 05-JUL-2017, entry version 12. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:CRK74257.1}; GN ORFNames=NIG5292_00284 {ECO:0000313|EMBL:CRK74257.1}; OS Nereida ignava. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae; Nereida. OX NCBI_TaxID=282199 {ECO:0000313|EMBL:CRK74257.1, ECO:0000313|Proteomes:UP000048949}; RN [1] {ECO:0000313|EMBL:CRK74257.1, ECO:0000313|Proteomes:UP000048949} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CECT 5292 {ECO:0000313|EMBL:CRK74257.1, RC ECO:0000313|Proteomes:UP000048949}; RA Syromyatnikov M.Y., Popov V.N.; RL Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CVQV01000002; CRK74257.1; -; Genomic_DNA. DR EnsemblBacteria; CRK74257; CRK74257; NIG5292_00284. DR Proteomes; UP000048949; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000048949}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000048949}. FT DOMAIN 208 377 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 428 AA; 47512 MW; CB10C6DC048B906E CRC64; MSTEHFETET PNTRAWVIHP DIKSDRDRRE ANDALAEAIA LGEALPNLDV EGGTVVSLPK VHAGMLFGKG KIEELRVMFN DNDIELVLVD GPVTPVQQRN LEKAWGVKLL DRTGLILEIF SDRARTREGV LQVEMAHLAY QRTRLVRAWT HLERQRGGLG FVGGPGETQI EADRRAIDDQ MGRLRKQLEK VVKTRALHRA ARAKVPFPVV ALVGYTNAGK STLFNRVTGA DVFAKDMLFA TLDPTMRRLE IEDGPEIILS DTVGFISDLP TQLVAAFRAT LEEVLDADLI LHVRDISHPE TENQARDVMT ILADLGVAET APMIEVWNKI DLLDDSARDG AIETASRSDT LHVVSALTGQ GLDDLLAAVS QTLTPDLHME TLNVPYANGK GRAWLFEEGV IEEESADETG YIFKVKWTAR QAKKFRDL // ID A0A0U1PZX0_9BURK Unreviewed; 384 AA. AC A0A0U1PZX0; DT 17-FEB-2016, integrated into UniProtKB/TrEMBL. DT 17-FEB-2016, sequence version 1. DT 05-JUL-2017, entry version 12. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=AAV94_07350 {ECO:0000313|EMBL:KKW68074.1}; OS Lampropedia cohaerens. OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Comamonadaceae; Lampropedia. OX NCBI_TaxID=1610491 {ECO:0000313|EMBL:KKW68074.1, ECO:0000313|Proteomes:UP000050580}; RN [1] {ECO:0000313|EMBL:KKW68074.1, ECO:0000313|Proteomes:UP000050580} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CT6 {ECO:0000313|EMBL:KKW68074.1, RC ECO:0000313|Proteomes:UP000050580}; RA Tripathi C., Rani P., Mahato N.K., Lal R.; RT "Draft genome sequence of Lampropedia sp. CT6, isolated from the RT microbial mat of a hot water spring, located at Manikaran, India."; RL Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KKW68074.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LBNQ01000023; KKW68074.1; -; Genomic_DNA. DR EnsemblBacteria; KKW68074; KKW68074; AAV94_07350. DR PATRIC; fig|1610491.3.peg.1561; -. DR Proteomes; UP000050580; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000050580}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000050580}. FT DOMAIN 186 359 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 152 179 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 384 AA; 42621 MW; 702A968BB97C65F8 CRC64; MGVDFGGAHF DHELQELGLL AQTAGLAPCD RIVVKRKFPD AALFIGKGKA EEIKALALGH GASEVIFDQA LSPAQQRNLE RVLELPVYDR TFLILEIFAQ RARSHEGKLQ VELARLQYLS TRLVRRWSHL ERQRGGIGAR GGPGETQIEL DRRMIGDAIK RVRERLRKLE KQRHTQRRQR HRNNVFSISL VGYTNAGKSS LFNALVKARA YAADQLFATL DTTTRQLFLQ EAGASVSISD TVGFIRDLPH GLVEAFKATL QEAVDADLLL HVVDASNPHF PEQIGEVMQV LQDIGAGDVP QLLVFNKIDA LEAQQQPRQP VDFMEVDGRQ VPRVFISAHT GQGLDALRAQ LAQRWQANHA DVGEVSPTAA ATYEHAEKPP AKPL // ID A0A0U1QSA7_9BACL Unreviewed; 416 AA. AC A0A0U1QSA7; DT 17-FEB-2016, integrated into UniProtKB/TrEMBL. DT 17-FEB-2016, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=SINU_01515 {ECO:0000313|EMBL:KLI03685.1}; OS Sporolactobacillus inulinus CASD. OC Bacteria; Firmicutes; Bacilli; Bacillales; Sporolactobacillaceae; OC Sporolactobacillus. OX NCBI_TaxID=1069536 {ECO:0000313|EMBL:KLI03685.1, ECO:0000313|Proteomes:UP000035553}; RN [1] {ECO:0000313|EMBL:KLI03685.1, ECO:0000313|Proteomes:UP000035553} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CASD {ECO:0000313|EMBL:KLI03685.1, RC ECO:0000313|Proteomes:UP000035553}; RX PubMed=21952540; DOI=10.1128/JB.05934-11; RA Yu B., Su F., Wang L., Xu K., Zhao B., Xu P.; RT "Draft genome sequence of Sporolactobacillus inulinus strain CASD, an RT efficient D-lactic acid-producing bacterium with high-concentration RT lactate tolerance capability."; RL J. Bacteriol. 193:5864-5865(2011). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KLI03685.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFVQ02000018; KLI03685.1; -; Genomic_DNA. DR RefSeq; WP_047034767.1; NZ_AFVQ02000018.1. DR EnsemblBacteria; KLI03685; KLI03685; SINU_01515. DR Proteomes; UP000035553; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000035553}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000035553}. FT DOMAIN 194 354 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 416 AA; 46226 MW; D6F59A1B9C3FA906 CRC64; MEHVILAACQ LPHQSDEHFQ SSLDELEALA KTAGGEVIAV VTQKRAKIDA ATYIGSGKVQ EIAALAKQLE ANTVIFNSEL SPAQQGRLGA LLSAKVLDRT QLILDIFAVR ARSREGKLQV ELAQLKYLLP RLSGIGQSLS RLGGGIGTRG PGETKLESDR RYIRSRMKDI SHQLNAVVSH RQRYRERRLL NNQCQIVLVG YTNAGKSTLF NQLTEMQTYA ENKLFATLDP LTRKMNLPNG FTCLLSDTVG FIQQLPTQLI AAFRSTLEEV TGAQLIVHVL DASSPDVAEH EKTVCKLLRE LEADDLPMLT VYNKKDLLQT PFIVPKGALL VSARDINDRK RILEAIESQI MQQMVPFHTK IRASEGKLLS SIKLNAILKK QTFDQKAQMY EIEGFVYPET SIAAKLNQHQ GSADKE // ID A0A0U2M4G0_9BACL Unreviewed; 440 AA. AC A0A0U2M4G0; DT 16-MAR-2016, integrated into UniProtKB/TrEMBL. DT 16-MAR-2016, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=IJ22_21220 {ECO:0000313|EMBL:ALS22496.1}; OS Paenibacillus naphthalenovorans. OC Bacteria; Firmicutes; Bacilli; Bacillales; Paenibacillaceae; OC Paenibacillus. OX NCBI_TaxID=162209 {ECO:0000313|EMBL:ALS22496.1, ECO:0000313|Proteomes:UP000061660}; RN [1] {ECO:0000313|Proteomes:UP000061660} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=32O-Y {ECO:0000313|Proteomes:UP000061660}; RA Butler R.III., Wang J., Stark B.C., Pombert J.-F.; RT "Complete genome sequences of two moderately thermophilic RT Paenibacillus species."; RL Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP013652; ALS22496.1; -; Genomic_DNA. DR RefSeq; WP_062408740.1; NZ_CP013652.1. DR EnsemblBacteria; ALS22496; ALS22496; IJ22_21220. DR KEGG; pnp:IJ22_21220; -. DR PATRIC; fig|162209.4.peg.2250; -. DR KO; K03665; -. DR Proteomes; UP000061660; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000061660}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000061660}. FT DOMAIN 209 373 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 168 195 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 440 AA; 49452 MW; FE386001E19A8FE1 CRC64; MKKTSYEVMP NAQEKAILVS LVTAEQKMRE AYDPEFSLSE LASLAETAKV QVLGSLTQNK EYADSKWFIG RGKAEELKAM IEETGANTAI FDQELSGAQV RNLEQFLDVK IIDRTQLILD IFAQRAKTRE GIIQVELAQL TYLLPRLYGQ GKNLSRLGGG IGTRGPGETK LETDRRHIRN RISELKRQLQ EVVRHRSLHR ERRKKSGVYQ AALVGYTNAG KSTLLRQLTH ADVYVENQLF ATLDPTSRSL KLPNGLEIVV TDTVGFIQNL PHDLVAAFRA TLEEVCEADL ILHIVDSSSK MMAAQMQVVD QVLEELGAHG KDRITVFNKI DLCPPEQADM LTTEGEFLKI SAFREEDLLR LKERIEVRMT GGSRSFRIPA DKGDMISLVY RIGEVLENEV DGSDMLFKVR VNHKAFDKIG YMLAAYDAVR PAEGEQGRDV // ID A0A0U2MA10_9BACL Unreviewed; 421 AA. AC A0A0U2MA10; DT 16-MAR-2016, integrated into UniProtKB/TrEMBL. DT 16-MAR-2016, sequence version 1. DT 07-JUN-2017, entry version 12. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=IJ21_00010 {ECO:0000313|EMBL:ALS25456.1}; OS Paenibacillus sp. 32O-W. OC Bacteria; Firmicutes; Bacilli; Bacillales; Paenibacillaceae; OC Paenibacillus. OX NCBI_TaxID=1695218 {ECO:0000313|EMBL:ALS25456.1, ECO:0000313|Proteomes:UP000059673}; RN [1] {ECO:0000313|Proteomes:UP000059673} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=32O-W {ECO:0000313|Proteomes:UP000059673}; RA Butler R.III., Wang J., Stark B.C., Pombert J.-F.; RT "Complete genome sequences of two moderately thermophilic RT Paenibacillus species."; RL Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP013653; ALS25456.1; -; Genomic_DNA. DR RefSeq; WP_062489139.1; NZ_CP013653.1. DR EnsemblBacteria; ALS25456; ALS25456; IJ21_00010. DR KEGG; pow:IJ21_00010; -. DR PATRIC; fig|1695218.3.peg.1; -. DR KO; K03665; -. DR Proteomes; UP000059673; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000059673}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000059673}. FT DOMAIN 198 366 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 157 191 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 421 AA; 48060 MW; BB3A458185FD6EA9 CRC64; MKQQQQQAVI VGVHLPERTD FASSMEELRS LAEACQVQVV DELSQKAVRI NPSHYIGTGK LQELAALLEA YEEAFVIFND ELSPSQIRNL EAALKRKVID RTMLILDIFA ERAKTREAQL QVEVAQLQYM LPRLVGLRAS LGRQGGGAGL RNRGAGETKL ELDRRRIEER IAALQNELEK LVARRQVQRK QRRKNDIPVV CLVGYTNTGK SSLMNALVER YNPQPEKQVL ARDMLFATLE TSVRSIELPD RKSFLLTDTV GFVSGLPHHL VKAFRSTLEE VAEADLLIHV VDFSNPDHEK QIEVTNDTLR ELGADHIPMI YAFNKLDITE HPYPQVQDGS VYLSVRERKG IDELVGMIRE QIFSSYVQRE IVIPYDQGRL VAYFNEHAHV QETSYEPEGT RLRLECKAAD YEKYRAHFIE L // ID A0A0U2VC70_9CREN Unreviewed; 365 AA. AC A0A0U2VC70; DT 16-MAR-2016, integrated into UniProtKB/TrEMBL. DT 16-MAR-2016, sequence version 1. DT 07-JUN-2017, entry version 10. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=EYM_03850 {ECO:0000313|EMBL:ALU11698.1}; OS Ignicoccus islandicus DSM 13165. OC Archaea; Crenarchaeota; Thermoprotei; Desulfurococcales; OC Desulfurococcaceae; Ignicoccus. OX NCBI_TaxID=940295 {ECO:0000313|EMBL:ALU11698.1, ECO:0000313|Proteomes:UP000060778}; RN [1] {ECO:0000313|EMBL:ALU11698.1, ECO:0000313|Proteomes:UP000060778} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 13165 {ECO:0000313|EMBL:ALU11698.1, RC ECO:0000313|Proteomes:UP000060778}; RA Podar M.; RT "Comparative genomics of Ignicoccus."; RL Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP006867; ALU11698.1; -; Genomic_DNA. DR EnsemblBacteria; ALU11698; ALU11698; EYM_03850. DR KEGG; iis:EYM_03850; -. DR PATRIC; fig|940295.4.peg.744; -. DR KO; K03665; -. DR Proteomes; UP000060778; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000060778}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000060778}. FT DOMAIN 186 365 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 151 178 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 365 AA; 41407 MW; 316DD8A44239AD83 CRC64; MDRKVILVAC TRSDNFEETL ALCHTANLKV VDVLNFCKKP DPGFYLTKGK LKELKEMVEK DSLNAIVIDT QLKPSQYYRL QRELGVEVID RVMLILKIFE LHSGSKEAKL QTELARLKYE LSISKEYIRR KKLGEQVHFL GPGEYAAEYL IKAFHRKIKK IENELEKVKK RRMTQKLSRR RSLSAPEVAV TGYTCAGKTA LINALSKSNL MEGPEMFTTI TPKHVKVRRN GWEVVLIDTV GFIESVPPQL IEAFHATLAE VTYSDAILLV IDSSEEEGRV INKTLSSLET LSEIDAIDKP LVVALNKIDI ARDWKSKMEV LEELLKEYYP WSFSIVPVSA RAQLNLNLLL DVLKGVVTKT ASNSV // ID A0A0U2VI69_9LACT Unreviewed; 413 AA. AC A0A0U2VI69; DT 16-MAR-2016, integrated into UniProtKB/TrEMBL. DT 16-MAR-2016, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=NY10_679 {ECO:0000313|EMBL:ALV21297.1}; OS Carnobacterium sp. CP1. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Carnobacteriaceae; OC Carnobacterium. OX NCBI_TaxID=1564681 {ECO:0000313|EMBL:ALV21297.1, ECO:0000313|Proteomes:UP000064734}; RN [1] {ECO:0000313|EMBL:ALV21297.1, ECO:0000313|Proteomes:UP000064734} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CP1 {ECO:0000313|EMBL:ALV21297.1, RC ECO:0000313|Proteomes:UP000064734}; RA Chen J., Yang J., Zhu S., Zhang D., Xiong S.; RT "Whole genome Sequence of Carnobacterium sp. strain CP1 Isolated from RT Amanda bay, East Antarctic."; RL Submitted (FEB-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP010796; ALV21297.1; -; Genomic_DNA. DR RefSeq; WP_058918637.1; NZ_CP010796.1. DR EnsemblBacteria; ALV21297; ALV21297; NY10_679. DR KEGG; carc:NY10_679; -. DR PATRIC; fig|1564681.3.peg.679; -. DR KO; K03665; -. DR Proteomes; UP000064734; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000064734}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000064734}. FT DOMAIN 199 360 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 413 AA; 46855 MW; 58733390DD62D8B2 CRC64; METKKEQEKV VLVGVQTNET DQDFAYSLNE LAQLTETALG KVVGELTQKR ERFDPRTFLG KGKLEELGHL VEESAADVVI FNHALTPGQT RNIQEVIDVK IIDRIQLILD IFAMRAQSKE GKLQVELAQL QYMLPRLAGQ GINLSRLGGG IGTRGPGETK LETDRRHIRD QISDIKRTLK ETEKHRDRNR IQRKESGTFQ IGLMGYTNAG KSTLLNKLTQ AETYEENQLF ATLDPLTRKL VLPSGMNVTL TDTVGFIQDL PTELIEAFQS TLEETRNVDL LLHVVDSSAE NMAGHEKTVM QLLKELKMDH IPMLTVYNKK DLVDGMFFPS LYPNVWISAK EPADIAVLLE EITNHMREIM VPYQIEVNAA EGHKLVRLKQ ETLLLSETYD EEKNVYIVRG YANKESKWIG ESH // ID A0A0U2VXY4_9BACL Unreviewed; 433 AA. AC A0A0U2VXY4; DT 16-MAR-2016, integrated into UniProtKB/TrEMBL. DT 16-MAR-2016, sequence version 1. DT 07-JUN-2017, entry version 12. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=IJ21_25270 {ECO:0000313|EMBL:ALS27923.1}; OS Paenibacillus sp. 32O-W. OC Bacteria; Firmicutes; Bacilli; Bacillales; Paenibacillaceae; OC Paenibacillus. OX NCBI_TaxID=1695218 {ECO:0000313|EMBL:ALS27923.1, ECO:0000313|Proteomes:UP000059673}; RN [1] {ECO:0000313|Proteomes:UP000059673} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=32O-W {ECO:0000313|Proteomes:UP000059673}; RA Butler R.III., Wang J., Stark B.C., Pombert J.-F.; RT "Complete genome sequences of two moderately thermophilic RT Paenibacillus species."; RL Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP013653; ALS27923.1; -; Genomic_DNA. DR RefSeq; WP_062492898.1; NZ_CP013653.1. DR EnsemblBacteria; ALS27923; ALS27923; IJ21_25270. DR KEGG; pow:IJ21_25270; -. DR PATRIC; fig|1695218.3.peg.2688; -. DR KO; K03665; -. DR Proteomes; UP000059673; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000059673}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000059673}. FT DOMAIN 208 375 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 433 AA; 47893 MW; 3BF535538B0547C3 CRC64; MRQTTYETNT LVQDRAVLVS LITPEIRRGS ADPEHSLQEL VNLAETAGVD VAATVTQHRD APDSKWFVGK GKVEELKAIG DERGANTFIF DQELSGAQVR NLEEALDAKI IDRTQLILDI FAQRAKTREG IIQVELAQLS YLLPRLSGQG RNLSRLGGGI GTRGPGETKL ETDRRHIRER IADLKRQLSD VVRHRKLHRE RRRKNGVVQV ALVGYTNAGK STLLRELTSA DVLVENRLFA TLDPTSRMLT LPSGKEVLLT DTVGFIQNLP HDLVAAFRAT LEEVNEADLL LHVIDCSSPM REEQMRVVGS ILSELGAADK PQLTIFNKKD LCGGAGAASF GLLPSDSDTM LISAYDAEDL ARLRQKIQDK LAGDTRTFAL PAERGDLIAL AYRIGEVVDR ETAGDKLLLK VELNKQDFEV LGGPLHEYLE QRP // ID A0A0U2YU74_9BACL Unreviewed; 423 AA. AC A0A0U2YU74; DT 16-MAR-2016, integrated into UniProtKB/TrEMBL. DT 16-MAR-2016, sequence version 1. DT 07-JUN-2017, entry version 13. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=AUC31_07930 {ECO:0000313|EMBL:ALS75150.1}; OS Planococcus rifietoensis. OC Bacteria; Firmicutes; Bacilli; Bacillales; Planococcaceae; OC Planococcus. OX NCBI_TaxID=200991 {ECO:0000313|EMBL:ALS75150.1, ECO:0000313|Proteomes:UP000067683}; RN [1] {ECO:0000313|EMBL:ALS75150.1, ECO:0000313|Proteomes:UP000067683} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=M8 {ECO:0000313|EMBL:ALS75150.1, RC ECO:0000313|Proteomes:UP000067683}; RA See-Too W.S.; RT "Complete genome of Planococcus rifietoensis type strain M8."; RL Submitted (JAN-2016) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP013659; ALS75150.1; -; Genomic_DNA. DR RefSeq; WP_058381857.1; NZ_CP013659.2. DR EnsemblBacteria; ALS75150; ALS75150; AUC31_07930. DR KEGG; prt:AUC31_07930; -. DR KO; K03665; -. DR Proteomes; UP000067683; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000067683}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000067683}. FT DOMAIN 200 368 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 159 193 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 423 AA; 47892 MW; 1B61941EF79DCC45 CRC64; MEQLIEKAII VGVQLQKDTH FEYSMEELRN LAEALGVEVV GELHQNLDRV NPAHYVGTGK VDEAKMLYEE ADANLIIFND ELSPSQIRNL EEELECKVID RTMLILDIFS RRARTREAQV QVELAQLQYM LPRLVGLRAS LGRQGGASSG GLANRGAGET KLELDRRKIE DQITKLRREL DQVKEQRTTQ RKQRLKKGMP VVSLVGYTNA GKSTIMNSLL SKTGQDEDKQ VFEKDMLFAT LDTSIRQIRL EDNKTFLLSD TVGFVSRLPH HLVKAFRSTL EEARNADLLL HVVDVSNDEH DYMMEVTDAT LQEVGVENVP TLYVYNKSDL AGVVYPRKSA DAVWISAKEG AGLDELVESI RERLFANHVM CRMEIPFGRG DVVAYLNDHA SIKETEYGEE GTLITVELSR ADYDRYEQFV VGK // ID A0A0U3B4N3_9ALTE Unreviewed; 430 AA. AC A0A0U3B4N3; DT 16-MAR-2016, integrated into UniProtKB/TrEMBL. DT 16-MAR-2016, sequence version 1. DT 30-AUG-2017, entry version 12. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=AT746_18335 {ECO:0000313|EMBL:ALT00033.1}; OS Lacimicrobium alkaliphilum. OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales; OC Alteromonadaceae; Lacimicrobium. OX NCBI_TaxID=1526571 {ECO:0000313|EMBL:ALT00033.1, ECO:0000313|Proteomes:UP000068447}; RN [1] {ECO:0000313|EMBL:ALT00033.1, ECO:0000313|Proteomes:UP000068447} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=YelD216 {ECO:0000313|EMBL:ALT00033.1, RC ECO:0000313|Proteomes:UP000068447}; RA Kim S.-G., Lee Y.-J.; RT "Complete genome of Lacimicrobium alkaliphilum KCTC 32984."; RL Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP013650; ALT00033.1; -; Genomic_DNA. DR RefSeq; WP_062483403.1; NZ_CP013650.1. DR EnsemblBacteria; ALT00033; ALT00033; AT746_18335. DR KEGG; lal:AT746_18335; -. DR KO; K03665; -. DR Proteomes; UP000068447; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000068447}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000068447}. FT DOMAIN 198 365 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 430 AA; 48415 MW; 20FCC17CB8F80985 CRC64; MFDRYEAGEQ AVLVHIDFPD ENSKEDLHEL QLLVSSAGVN AIDLVTGSRA TPSARYFVGS GKAEEIAQAV KANDADVVIF NHALSPSQER NLESVCKCRV LDRTGLILDI FAQRARTHEG KLQVELAQLR HISTRLIRGW THLERQKGGI GLRGPGETQL ETDRRLLRAR ITHILQRLKK VQKQREQSRR ARNRAEMPTL SLVGYTNAGK STLFNTITSA GVYAADQLFA TLDPTLRKIQ LQDVGPAILA DTVGFIRHLP HDLVAAFKAT LQETQQAELL LHVVDYADEQ RLDNIDQVNI VLDEIDAGEV PQLMICNKID QLDNIQPHID RDEEGRPVRV WVSAQKGLGI ELLFQAISES IGRNMVQYSL RIPPKEGKLR GALYRMQCIS DESYAEDGDW LVDVRMPAKD WYQLEKHLAS DLATYVINKH // ID A0A0U3FA20_9STRE Unreviewed; 412 AA. AC A0A0U3FA20; DT 16-MAR-2016, integrated into UniProtKB/TrEMBL. DT 16-MAR-2016, sequence version 1. DT 30-AUG-2017, entry version 17. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=AU077_05885 {ECO:0000313|EMBL:ALT81080.1}; OS Streptococcus gallolyticus. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=315405 {ECO:0000313|EMBL:ALT81080.1, ECO:0000313|Proteomes:UP000067067}; RN [1] {ECO:0000313|EMBL:ALT81080.1, ECO:0000313|Proteomes:UP000067067} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ICDDRB-NRC-S1 {ECO:0000313|EMBL:ALT81080.1, RC ECO:0000313|Proteomes:UP000067067}; RA Alam Sarker S., Sultana S., Moine D., Descombes P., Charton F., RA Bourdin G., McCallin S., Ngom-Bru C., Neville T., Akter M., Huq S., RA Qadri F., Talukdar K., Delley M., Loiseau C., Deng Y., Kassam M., RA Berger B.; RT "Oral Phage Therapy of Acute Bacterial Diarrhea in Children from RT Bangladesh with Two Coliphage Preparations."; RL Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP013688; ALT81080.1; -; Genomic_DNA. DR RefSeq; WP_058621743.1; NZ_CP013688.1. DR EnsemblBacteria; ALT81080; ALT81080; AU077_05885. DR Proteomes; UP000067067; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000067067}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}. FT DOMAIN 199 359 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 165 192 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 412 AA; 47185 MW; B0751BC86B4F10CC CRC64; MIETSKRQER VILLGVELPE TENFEMSMEE LASLAKTAGA EVVSSYRQKR EKYDSKSLIG SGKLAEIKAI VEADEIDTVI VNDRLTPRQN VNLEVELGVK VIDRMQLILD IFAMRARSHE GKLQVHLAQL KYMLPRLVGQ GVMLSRQAGG IGSRGPGESQ LELNRRSIRH QISDIERQLK VVEKNRETGR DKRTESQVFK IGLIGYTNAG KSTIMNILTN DKQYEADELF ATLDATTKQI YLQNQFQVTL TDTVGFIQNL PTELVAAFKS TLEESRNVDL LLHVIDASDP NHAEHEKVVL NLLKELDMLD IPRLAVYNKM DVAEHLVATT FPNVRISARD KDARTLLRRL LINEIREIFE PFSIRVHQSQ AYKLYELNKI ALLDHYDFAQ EYETITGYIN PKNKWRLEEF YD // ID A0A0U3FV20_9RHOB Unreviewed; 431 AA. AC A0A0U3FV20; DT 16-MAR-2016, integrated into UniProtKB/TrEMBL. DT 16-MAR-2016, sequence version 1. DT 05-JUL-2017, entry version 13. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=APZ00_18180 {ECO:0000313|EMBL:ALV30206.1}; OS Pannonibacter phragmitetus. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae; Pannonibacter. OX NCBI_TaxID=121719 {ECO:0000313|EMBL:ALV30206.1, ECO:0000313|Proteomes:UP000064921}; RN [1] {ECO:0000313|EMBL:ALV30206.1, ECO:0000313|Proteomes:UP000064921} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=31801 {ECO:0000313|EMBL:ALV30206.1, RC ECO:0000313|Proteomes:UP000064921}; RA Ming D., Wang M., Zhou Y., Jiang T., Hu S.; RT "The world's first case of liver abscess caused by Pannonibacter RT phragmitetus."; RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP013068; ALV30206.1; -; Genomic_DNA. DR EnsemblBacteria; ALV30206; ALV30206; APZ00_18180. DR KEGG; pphr:APZ00_18180; -. DR KO; K03665; -. DR Proteomes; UP000064921; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000064921}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000064921}. FT DOMAIN 201 371 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 160 194 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 431 AA; 47667 MW; B96C6CF9EA5A767D CRC64; MVIEPVLPER LPKGFEGTPP PTRTPEARLE EAVGLCAAIE LEIVSASIAR IHTPRPATLL GPGKVEEIAR AAEEGDVDVV VIDHALTPIQ QRNLEKAMKT KVIDRTGLIL EIFGARARTK EGRLQVDLAH LTWQKSRLVR SWTHLERQRG GVGFMGGPGE TQIEADRRQI QDKIMRLERE LEQVRRTRDL HRKKRKKIPQ PVIALVGYTN AGKSTLFNRL TQSDVFAKDL LFATLDPTLR RIRLPHGREV ILSDTVGFIS ELPTHLVAAF RATLEEVLEA DLILHVRDIS HEDSDAQSVD VGRTLADLGV NPQTGAPVVE VWNKIDNLDP ERRAKLLEAN GPEGAIALSA LTGDGIPALL SRIEAFMAVG DDRFELALPV TEGELLAGLY QMGEVLERVD GEEVIELTVR ISDKQKGPFR SRYGAYISGA D // ID A0A0U3HA16_9MICC Unreviewed; 541 AA. AC A0A0U3HA16; DT 16-MAR-2016, integrated into UniProtKB/TrEMBL. DT 16-MAR-2016, sequence version 1. DT 07-JUN-2017, entry version 12. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=AS188_08500 {ECO:0000313|EMBL:ALU39781.1}; OS Kocuria flava. OC Bacteria; Actinobacteria; Micrococcales; Micrococcaceae; Kocuria. OX NCBI_TaxID=446860 {ECO:0000313|EMBL:ALU39781.1, ECO:0000313|Proteomes:UP000057181}; RN [1] {ECO:0000313|EMBL:ALU39781.1, ECO:0000313|Proteomes:UP000057181} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=HO-9041 {ECO:0000313|EMBL:ALU39781.1, RC ECO:0000313|Proteomes:UP000057181}; RA Zhou M., Dai J.; RT "Complete Genome Sequence of Kocuria flava strain HO-9041."; RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP013254; ALU39781.1; -; Genomic_DNA. DR RefSeq; WP_058858490.1; NZ_CP013254.1. DR EnsemblBacteria; ALU39781; ALU39781; AS188_08500. DR KEGG; kfv:AS188_08500; -. DR KO; K03665; -. DR Proteomes; UP000057181; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 2. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000057181}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000057181}. FT DOMAIN 311 476 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 541 AA; 59253 MW; 5480B74BFF88384B CRC64; MTQSHPTPAD RSAGAEHAPE GLSRQELEDV VERVLARARA RGAAAEPTTE DETDGTGVLT GRARELAEPG TGHGEHDGEQ QDLEERRALR RVAGLSTELE DVTELEYRQL RLERVVLAGL WTEGTLEEAE NSLRELAALA ETAGSEVLDG IVQRRLKPDP ATYLGSGKAR ELRDIVAATG ADTVIVDSEL APSQRRGLED VVKVKVIDRT GLILDIFAQH AKSKEGKAQV ELAQLEYMLP RLRGWGESLS RQAGGRAAAG EGIGSRGPGE TKIELDRRRI RARMAKLRRE IAAMKPARET KRLNRRRNAV PSVAIAGYTN AGKSSLLNRL TDAGVLVENA LFATLDPTVR RAQTPDGIGY TLSDTVGFVR SLPTQLVEAF RSTLEEVADA DLILHVVDAS HPDPEGQIRA VRQVFTDIDA QNIPEIIVLN KVDAADPFVV ERIRQRERSV VVVSARTGEG IDRLRQRISE SIPRPQTVLD LVVPYRRGDV VSRLHEWDAE ILRTEHLAEG THLLVKVRDE LAAELAEFVP EHAPAFGAES A // ID A0A0U3J064_9FLAO Unreviewed; 403 AA. AC A0A0U3J064; DT 16-MAR-2016, integrated into UniProtKB/TrEMBL. DT 16-MAR-2016, sequence version 1. DT 07-JUN-2017, entry version 12. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=AUW17_12070 {ECO:0000313|EMBL:ALU75940.1}; OS Tenacibaculum dicentrarchi. OC Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales; OC Flavobacteriaceae; Tenacibaculum. OX NCBI_TaxID=669041 {ECO:0000313|EMBL:ALU75940.1, ECO:0000313|Proteomes:UP000061908}; RN [1] {ECO:0000313|EMBL:ALU75940.1, ECO:0000313|Proteomes:UP000061908} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=AY7486TD {ECO:0000313|EMBL:ALU75940.1, RC ECO:0000313|Proteomes:UP000061908}; RX PubMed=26893432; RA Grothusen H., Castillo A., Henriquez P., Navas E., Bohle H., Araya C., RA Bustamante F., Bustos P., Mancilla M.; RT "First Complete Genome Sequence of Tenacibaculum dicentrarchi, an RT Emerging Bacterial Pathogen of Salmonids."; RL Genome Announc. 4:e01756-15(2016). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP013671; ALU75940.1; -; Genomic_DNA. DR RefSeq; WP_058886079.1; NZ_CP013671.1. DR EnsemblBacteria; ALU75940; ALU75940; AUW17_12070. DR KEGG; tdi:AUW17_12070; -. DR KO; K03665; -. DR Proteomes; UP000061908; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000061908}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000061908}. FT DOMAIN 200 385 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 403 AA; 46143 MW; D332251C9A48C295 CRC64; MEETREEIIE KAVLIGIITQ KQNEKQSDEY LDELEFLTLT AGGVAVKRFV QKMEKPNPKT FLGTGKLEEV RMYIASKGIS IAIFDDELSP AQLRNIENEL GCKVLDRTNL ILDIFAGRAQ TSSAKAQVEL AQCQYLLPRL TRLWTHLDKQ KGGIGMRGPG ETEIETDRRI IRDKITLLKK KLSTIDRQMA VQRKNRGKMV RVALVGYTNV GKSTLMNVIS KSDVFAENKL FATLDTTVRK VVIKNIPFLM TDTVGFIRKL PTQLVESFKS TLDEVREADL LLHVVDICHP NFEDHIASVN KILDEIGASN KPILMVFNKI DAYTHDTIDE DDLITEKSKN HYTLDDWKNT WMNDLGEESL FISALNKDNL EDFKEKVYKS VKKIHIERFP YNNFLYEDDL PIE // ID A0A0U3MEP3_9BURK Unreviewed; 420 AA. AC A0A0U3MEP3; DT 16-MAR-2016, integrated into UniProtKB/TrEMBL. DT 16-MAR-2016, sequence version 1. DT 05-JUL-2017, entry version 12. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=RD2015_1495 {ECO:0000313|EMBL:ALV05980.1}; OS Roseateles depolymerans. OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Roseateles. OX NCBI_TaxID=76731 {ECO:0000313|EMBL:ALV05980.1, ECO:0000313|Proteomes:UP000060699}; RN [1] {ECO:0000313|EMBL:ALV05980.1, ECO:0000313|Proteomes:UP000060699} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=KCTC 42856 {ECO:0000313|EMBL:ALV05980.1, RC ECO:0000313|Proteomes:UP000060699}; RA Kim K.M.; RT "Complete genome of Roseateles depolymerans KCTC 42856."; RL Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP013729; ALV05980.1; -; Genomic_DNA. DR EnsemblBacteria; ALV05980; ALV05980; RD2015_1495. DR KEGG; rdp:RD2015_1495; -. DR PATRIC; fig|76731.3.peg.1526; -. DR KO; K03665; -. DR Proteomes; UP000060699; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000060699}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000060699}. FT DOMAIN 207 385 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 173 200 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 420 AA; 46226 MW; F6A4320E597852AF CRC64; MNSQDPTHQS PPPEAARAIL VGVDLGRGEP FDPTLDELAL LAESAGDTPV ARIVAKRKAP DAALFVGSGK ADEIKLMVQA HAAHTVLFDQ AISPAQQRNL ERHLGVPVAD RTALILEIFA ARAQSFEGKL QVELARLQYL ATRLVRRWSH LERQSGGIGM RGGPGERQIE LDRRMIDDRI KTIKERLKKV ERQRSTQRRA RARNGVFRVS LVGYTNAGKS TLFNALTKAR TYAANQLFAT LDTTTRSLYL EEAGSSVSLS DTVGFIRDLP HKLVEAFKAT LQEAADADLL LHVVDAASPV LTEQMEEVER VLAEIGAQHI PQILVYNKLD LLEPTQRPRE MQDWLPRLGG EHGGQRLPRI FVSAAGGEGL DLLRSRIAAL MQASPVPETW DPDFKSDELP QDLTQDLPAP KDASGHDPGE // ID A0A0U3PZH9_9ACTN Unreviewed; 497 AA. AC A0A0U3PZH9; DT 16-MAR-2016, integrated into UniProtKB/TrEMBL. DT 16-MAR-2016, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=AS200_13070 {ECO:0000313|EMBL:ALV32876.1}; OS Streptomyces sp. CdTB01. OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae; OC Streptomyces. OX NCBI_TaxID=1725411 {ECO:0000313|EMBL:ALV32876.1, ECO:0000313|Proteomes:UP000068029}; RN [1] {ECO:0000313|EMBL:ALV32876.1, ECO:0000313|Proteomes:UP000068029} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CdTB01 {ECO:0000313|EMBL:ALV32876.1, RC ECO:0000313|Proteomes:UP000068029}; RA Tian Y., Zhou G., Yang H., Lu X.; RT "Complete genome sequence of the Streptomyces sp. strain CdTB01, a RT bacterium tolerant to cadmium."; RL Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP013743; ALV32876.1; -; Genomic_DNA. DR RefSeq; WP_058922554.1; NZ_CP013743.1. DR EnsemblBacteria; ALV32876; ALV32876; AS200_13070. DR KEGG; scx:AS200_13070; -. DR KO; K03665; -. DR Proteomes; UP000068029; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 2. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000313|EMBL:ALV32876.1}; KW Complete proteome {ECO:0000313|Proteomes:UP000068029}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900, KW ECO:0000313|EMBL:ALV32876.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000068029}. FT DOMAIN 275 440 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 497 AA; 54365 MW; 5A8D41236C370CC6 CRC64; MTSSSSPSQD TQRFAHSYAE GLRADALMEE DVAWSHEIDG DRDGEQFDRS ERAALRRVAG LSTELEDVTE VEYRQLRLER VVLVGVWTSG TAQDADNSLA ELAALAETAG ALVLDGVIQR RSEPDAATYI GSGKAVELRD IVLETGADTV ICDGELSPGQ LIHLEDVVKV KVIDRTALIL DIFAQHAKSR EGKAQVALAQ MQYMLPRLRG WGQSLSRQMG GGKGGGLATR GPGETKIETD RRRIREKMAK MRREIADMKT GREIKRQERK RNKVPSVAIA GYTNAGKSSL LNRLTGAGVL VENALFATLD PTVRRAETPS GRLYTLADTV GFVRHLPHHL VEAFRSTMEE VGESDLILHV VDGSHPNPEE QLAAVREVIR DVGAIDVPEI VVINKADAAD PLTLQRLMRI EKRSIAVSAR TGQGIQELLA LIDNELPRPS EEIEALVPYT HGKLVARAHD EGEVISAEHT PEGTLLKARV HEELAADLQP YVPVPTV // ID A0A0U3RQR6_9MICC Unreviewed; 519 AA. AC A0A0U3RQR6; DT 16-MAR-2016, integrated into UniProtKB/TrEMBL. DT 16-MAR-2016, sequence version 1. DT 05-JUL-2017, entry version 12. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=MB46_03945 {ECO:0000313|EMBL:ALV47393.1}; OS Arthrobacter sp. A3. OC Bacteria; Actinobacteria; Micrococcales; Micrococcaceae; Arthrobacter. OX NCBI_TaxID=595593 {ECO:0000313|EMBL:ALV47393.1, ECO:0000313|Proteomes:UP000055883}; RN [1] {ECO:0000313|EMBL:ALV47393.1, ECO:0000313|Proteomes:UP000055883} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=A3 {ECO:0000313|EMBL:ALV47393.1, RC ECO:0000313|Proteomes:UP000055883}; RA Shamseldin A., Moawad H., Abd El-Rahim W.M., Sadowsky M.J.; RL Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP013745; ALV47393.1; -; Genomic_DNA. DR EnsemblBacteria; ALV47393; ALV47393; MB46_03945. DR KEGG; arw:MB46_03945; -. DR KO; K03665; -. DR Proteomes; UP000055883; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000055883}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000055883}. FT DOMAIN 298 463 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 519 AA; 56383 MW; 63876C80AB79A9EA CRC64; MSVAEIEAVI DRILAKDVAA SRAVSEDADE EAQDPYQGVP STRPLAGQAQ AVSSLKLQHS IFDGDQSELA ERNALRRKAS HSTELEDVSE VEYRQLRLER VVLAGLWSQG TMADAENSLR ELAALAETAG SEVLDGLVQR RAKPDPATYL GTGKAQELKD IVHATGADTV IIDGNLAPSQ RRTLEEVVKV KVIDRTALIL DIFAQHAKSR EGRAQVELAQ MEYLLPRLRG WGESMSRQAG GRVGAAGGGI GSRGPGETKM ELDRRKIRTR MAKLRREIAA MRPARETKRA NRKRNSVPSV AIAGYTNAGK SSLLNRLTDA GVLVENALFA TLDPTVRKTE TADGLGYTLV DTVGFVRSLP TQLVEAFRST LEEVADADLI LHIVDASHPD PEGQISAVRT VFAEVGALQI PEIIILNKAD IADPFVIERL RQHESRTVVV SARTGAGIDE LLEAISEAIP HPSVTLTLLI PYDRGDVLNK LHRTDAEIIS LEHGEHGTLA TVRVREDLAA EVEPFVQHA // ID A0A0U4AUC5_9BACT Unreviewed; 390 AA. AC A0A0U4AUC5; DT 16-MAR-2016, integrated into UniProtKB/TrEMBL. DT 16-MAR-2016, sequence version 1. DT 05-JUL-2017, entry version 15. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=AUC43_02680 {ECO:0000313|EMBL:ALW87189.1}; OS Hymenobacter sedentarius. OC Bacteria; Bacteroidetes; Cytophagia; Cytophagales; Hymenobacteraceae; OC Hymenobacter. OX NCBI_TaxID=1411621 {ECO:0000313|EMBL:ALW87189.1, ECO:0000313|Proteomes:UP000059542}; RN [1] {ECO:0000313|EMBL:ALW87189.1, ECO:0000313|Proteomes:UP000059542} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DG5B {ECO:0000313|EMBL:ALW87189.1, RC ECO:0000313|Proteomes:UP000059542}; RA Shamseldin A., Moawad H., Abd El-Rahim W.M., Sadowsky M.J.; RL Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP013909; ALW87189.1; -; Genomic_DNA. DR EnsemblBacteria; ALW87189; ALW87189; AUC43_02680. DR KEGG; hyg:AUC43_02680; -. DR KO; K03665; -. DR Proteomes; UP000059542; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000059542}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000059542}. FT DOMAIN 188 379 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 156 183 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 390 AA; 43891 MW; CCE2741BF012E338 CRC64; MLVSVPPRRQ SEAQTTEYLD ELAFLIETAG ATATKRFVQR LEKPDIRTYV GEGKLAEIKA WVQHEGTSMV VFDDDLSPSQ LRNLEAELLV KIVDRSLLIL DIFALRAKSA TSRTQVELAQ YQYLLPRLTG LWTHLDKQRG GVGMKGPGET EIETDRRIVR DRIAFLKEKL EDLDKQAHTQ RKTRGGSIRV ALVGYTNVGK STLMNVLGKA DVFAENKLFA TVDATTRKIV LDQTPFLLSD TVGFIRKLPT KLIESFKSTL DEIREADLLL HVVDISHPGF EEQIQVVNDT LSDIGAADKP VLLVFNKIDQ YKQDDAQHDP FGEVLDAEDD GTAPRPPLAQ LQATYMAKLH DPVVFVSAQE RTNLEELREL LAKRVAALHQ QRYPYQAANY // ID A0A0U4E348_9BACI Unreviewed; 411 AA. AC A0A0U4E348; DT 16-MAR-2016, integrated into UniProtKB/TrEMBL. DT 16-MAR-2016, sequence version 1. DT 07-JUN-2017, entry version 12. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=AOX59_03185 {ECO:0000313|EMBL:ALX47692.1}; OS Lentibacillus amyloliquefaciens. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Lentibacillus. OX NCBI_TaxID=1472767 {ECO:0000313|EMBL:ALX47692.1, ECO:0000313|Proteomes:UP000050331}; RN [1] {ECO:0000313|EMBL:ALX47692.1, ECO:0000313|Proteomes:UP000050331} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=LAM0015 {ECO:0000313|EMBL:ALX47692.1, RC ECO:0000313|Proteomes:UP000050331}; RA Wang J.-L., He M.-X.; RT "Complete genome sequence of strain Lentibacillus amyloliquefaciens RT LAM0015T isolated from saline sediment."; RL Submitted (JAN-2016) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP013862; ALX47692.1; -; Genomic_DNA. DR RefSeq; WP_068441730.1; NZ_CP013862.1. DR EnsemblBacteria; ALX47692; ALX47692; AOX59_03185. DR KEGG; lao:AOX59_03185; -. DR KO; K03665; -. DR Proteomes; UP000050331; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000050331}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000050331}. FT DOMAIN 195 356 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 411 AA; 46871 MW; 7040EAE8ACD6B230 CRC64; MPEKVLVIAV KMPEDNDERF NSSLDELKSL SHTAGATVEK AMIQNRKRLH PAYYIGEGKM EEIKEVAEDL EADLIISNDE LSAGQLRNLT DRIGVHVIDR SQLILDIFAQ RARTKEGKLQ VELAQLEYTL PRLRGRGEEM SRLGAGIGTR GPGETKLETD QRHIRKRIDD IKRQLNQVVK QREQYRKRRK LNDAFQIAIV GYTNAGKSTL FNRLAKSDAQ VENQLFATLD PLTRQIQLPF GFQTLITDTV GFIQDLPTSL IAAFKSTLEE VTEADFILHV VDAANPDLEQ HQQTVDRLLT DLGANTIPKL VVYNKKDRLE TDFIPMQHPN ILISATEQND IGRVLEKIED TLKNEWDAYT VSIAPDEGKL LHRLEKETIV TYRSFQEESR KYSVAGYIRQ HHPLRGLVKE N // ID A0A0U4GLH5_9MICO Unreviewed; 502 AA. AC A0A0U4GLH5; DT 16-MAR-2016, integrated into UniProtKB/TrEMBL. DT 16-MAR-2016, sequence version 1. DT 07-JUN-2017, entry version 12. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=AB663_002222 {ECO:0000313|EMBL:ALX66819.1}; OS Microbacterium sp. XT11. OC Bacteria; Actinobacteria; Micrococcales; Microbacteriaceae; OC Microbacterium. OX NCBI_TaxID=367477 {ECO:0000313|EMBL:ALX66819.1, ECO:0000313|Proteomes:UP000065197}; RN [1] {ECO:0000313|EMBL:ALX66819.1, ECO:0000313|Proteomes:UP000065197} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=XT11 {ECO:0000313|EMBL:ALX66819.1, RC ECO:0000313|Proteomes:UP000065197}; RA Yang F., Li L., Yang M., Guo X., Hou Y., Chen X., Li X.; RT "Draft genome sequence of a xanthan-degrading Microbacterium sp. RT strain XT11 with the potential for xantho-oligosaccharides RT production."; RL Submitted (JAN-2016) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP013859; ALX66819.1; -; Genomic_DNA. DR RefSeq; WP_067198828.1; NZ_CP013859.1. DR EnsemblBacteria; ALX66819; ALX66819; AB663_002222. DR KEGG; mix:AB663_002222; -. DR PATRIC; fig|367477.3.peg.2216; -. DR KO; K03665; -. DR Proteomes; UP000065197; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 2. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000313|EMBL:ALX66819.1}; KW Complete proteome {ECO:0000313|Proteomes:UP000065197}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900, KW ECO:0000313|EMBL:ALX66819.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000065197}. FT DOMAIN 282 447 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 502 AA; 54413 MW; 318A25163F6ECB9E CRC64; MTETTPSHDG EAIERVLANA EKRTEVRVFG AAQALQDEAT AAHGTADGEQ WDLEDRHALR RVAGLSTELE DVTEVEYRQL RLENVVLVGV YPQGAQEDAE NSLRELAALA ETAGAVVLDG VLQRRPHPDA ATYIGRGKAQ ELKDIVAATG ADTVIADTEL APSQRRALED VVKVKVIDRT TVILDIFSQH AKSREGKAQV ELAQLEYLLP RLRGWGESMS RQAGGQVGAG GAGMGSRGPG ETKIELDRRR IRTRMAQLRR QIRDFAPARE AKRAERRRNT IPSVAIAGYT NAGKSSLLNA LTSAGVLVEN ALFATLDATV RRSETSDGRV FTLTDTVGFV RNLPHQLVEA FRSTLEEVGD ADVILHVVDG SHPDPAGQLQ TVRDVMGDVG VRDMPEIVVF NKADLIDDDE RLVLRGLEPK AHFVSSRSGE GIAELRAAIE EALPKPAVEV HAVVPYDRGD LVAAIHETGM LLSVEHREQG TAVHARVSER LAADLAPFAT TP // ID A0A0U4W2A1_9GAMM Unreviewed; 427 AA. AC A0A0U4W2A1; DT 16-MAR-2016, integrated into UniProtKB/TrEMBL. DT 16-MAR-2016, sequence version 1. DT 30-AUG-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=ATY27_09785 {ECO:0000313|EMBL:ALZ76029.1}; OS Rheinheimera sp. F8. OC Bacteria; Proteobacteria; Gammaproteobacteria; Chromatiales; OC Chromatiaceae; Rheinheimera. OX NCBI_TaxID=1763998 {ECO:0000313|EMBL:ALZ76029.1, ECO:0000313|Proteomes:UP000059499}; RN [1] {ECO:0000313|Proteomes:UP000059499} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=F8 {ECO:0000313|Proteomes:UP000059499}; RA Schuster A.K., Szewzyk U.; RT "Draft genome sequence of Rheinheimera sp. F8, a biofilm-forming RT strain which produces large amounts of extracellular DNA."; RL Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP013656; ALZ76029.1; -; Genomic_DNA. DR EnsemblBacteria; ALZ76029; ALZ76029; ATY27_09785. DR Proteomes; UP000059499; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000059499}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000059499}. FT DOMAIN 197 363 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 427 AA; 48099 MW; C84EFF7BD7086857 CRC64; MFDLHQPAEQ AILVHITFPQ EHAREDLDEL RMLVSSAGVH AATVVTGPRQ TIDARLFVGS GKAQEIAAAV QQYSADVIIF NHSLSPAQTR NLERLCQCKV IDRTTLILDI FAQRARSFEG KLQVELAQLK HLASRLIRGF DNERQKGGIG LRGPGETALE TDRRLLRDRI SALMQRLDKV SRQRETGRKA RQRAEVPVVS LVGYTNAGKS TLFNKLTQAD VYAADQLFAT LDPTLRQVRF PDFGALIFAD TVGFIRHLPH DLVAAFKSTL QETREADLQL HVIDVSDARL EDNIAQVQHV LHEIEADDLP QLRVYNKIDR AEQEPRIEFD EYGVPQAVYI SAQNGVGLDL LSRAIVARLS DRYLTMQLRL PPDTLNWRAK LHEAGCVRQE LFDEDGNCLL HIQLSLALWE RLNKQSQALL QSCVLTT // ID A0A0U5AF34_9EURY Unreviewed; 435 AA. AC A0A0U5AF34; DT 16-MAR-2016, integrated into UniProtKB/TrEMBL. DT 16-MAR-2016, sequence version 1. DT 07-JUN-2017, entry version 12. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:CQH57733.1}; GN ORFNames=HHUB_2590 {ECO:0000313|EMBL:CQH57733.1}; OS Halobacterium hubeiense. OC Archaea; Euryarchaeota; Halobacteria; Halobacteriales; OC Halobacteriaceae; Halobacterium. OX NCBI_TaxID=1407499 {ECO:0000313|EMBL:CQH57733.1, ECO:0000313|Proteomes:UP000066737}; RN [1] {ECO:0000313|Proteomes:UP000066737} RP NUCLEOTIDE SEQUENCE. RC STRAIN=JI20-1 {ECO:0000313|Proteomes:UP000066737}; RX PubMed=26628271; DOI=10.1111/1462-2920.13130; RA Jaakkola S.T., Pfeiffer F., Ravantti J.J., Guo Q., Liu Y., Chen X., RA Ma H., Yang C., Oksanen H.M., Bamford D.H.; RT "The complete genome of a viable archaeum isolated from 123-million- RT year-old rock salt."; RL Environ. Microbiol. 18:565-579(2016). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LN831302; CQH57733.1; -; Genomic_DNA. DR RefSeq; WP_059057024.1; NZ_LN831302.1. DR EnsemblBacteria; CQH57733; CQH57733; Hhub_2590. DR GeneID; 26659225; -. DR KEGG; hhb:Hhub_2590; -. DR KO; K03665; -. DR Proteomes; UP000066737; Chromosome I. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000066737}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000066737}. FT DOMAIN 192 375 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 158 188 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 435 AA; 48610 MW; AC9F047BFD0134D7 CRC64; MTGTTTKTAV VAKRVDDGEA DTAEIRELVR AAGYEVGGEV TQTRTADPAL QLGEGKVEEL AALVAETDAE RVVFDNRLGP YQTYNLGKQL PENTEVVDRF RLILDIFGQR ANTRKAQLQV ELAELRYELP RAEAKTSLAK RDERPGFMGL GEYDESREQD IKAQISRIRD ELANIEKTEQ QRRETRRESG FELVALAGYT NAGKSTLLRR LADDLDVDEN EQLHPDLDTT AESQDKLFTT LGTTTRRLDM DRRDVLLTDT VGFISDLPHW LVESFKSTLE SVYQADLVLL VVDASESIDE IREKLVTSHD TLYERNEAPI VTVFNKVDKV GDDELAEKME ALSALAPDPI AVSGKEGINL AALRERIDAE LPPRERETLV LPMTDETMSV VSWVHDHAHV RDVDYGDEQV VVDFEALPTV VEKSRAKASD LVAEA // ID A0A0U5B4F1_9BACT Unreviewed; 581 AA. AC A0A0U5B4F1; DT 16-MAR-2016, integrated into UniProtKB/TrEMBL. DT 16-MAR-2016, sequence version 1. DT 07-JUN-2017, entry version 12. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=THC_0534 {ECO:0000313|EMBL:BAU22928.1}; OS Caldimicrobium thiodismutans. OC Bacteria; Thermodesulfobacteria; Thermodesulfobacteriales; OC Thermodesulfobacteriaceae; Caldimicrobium. OX NCBI_TaxID=1653476 {ECO:0000313|EMBL:BAU22928.1, ECO:0000313|Proteomes:UP000068196}; RN [1] {ECO:0000313|Proteomes:UP000068196} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=TF1 {ECO:0000313|Proteomes:UP000068196}; RA Kojima H., Umezawa K., Fukui M.; RT "Caldimicrobium thiodismutans sp. nov., a sulfur-disproportionating RT bacterium isolated from a hot spring."; RL Int. J. Syst. Evol. Microbiol. 0:0-0(2016). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AP014945; BAU22928.1; -; Genomic_DNA. DR EnsemblBacteria; BAU22928; BAU22928; THC_0534. DR KEGG; cthi:THC_0534; -. DR PATRIC; fig|1653476.3.peg.550; -. DR KO; K03665; -. DR Proteomes; UP000068196; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000068196}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000068196}. FT DOMAIN 392 562 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 351 385 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 581 AA; 66813 MW; 2293AD29818A094E CRC64; MSRVVYGNLQ GLKPSEIRRL ERLYYRKIHP EVIFSSDLAW ELAELSFLLN RQIGILINRT GEIEYVIVGT FNQIEIPELK GYRESLARLK GLRLIHTHLI KNGKGSGLDQ DDLLDLAFLR LDLIGALEVN EKGEPGKIHL AHILPHAGFF SQALSDREDQ FFFFFKPKYV WDLRENFLEL IKALEDEFEK IKPLKNVKEK EDRALLIFVK EPQDLDWEER LKELKELAKT AGVTVVGEII QKRTILDPRY VIGKGKLIEV MIQAMRNKAN LLIFDRELTP SQVRALTEVT DLRVIDRTQL ILDIFAQRAK TKEGKIQVEM AQLRYALPRL RAKDDAFSRL TGGIGGRGPG ETKLEIDKRR IKDKMSRLER ELARISAERD LRRKRRKKLD YKIVALIGYT NAGKTTLLNT LSKSNYLAED KLFATLDPVT KAVRTQKGHI FLLTDTVGFI RDLPEELKKA FKATLEELYN ADLLLHLVDI SHPNWENHIQ AVENILEEMD LLNFPRLIVF NKIDLLNKRE DLSPNFILRL LNQYNGVGIS AMTGEGLDQL ISHIESLLFK EESSIVVEIP SEKVLTSHLS A // ID A0A0U5GRG3_9GAMM Unreviewed; 426 AA. AC A0A0U5GRG3; DT 16-MAR-2016, integrated into UniProtKB/TrEMBL. DT 16-MAR-2016, sequence version 1. DT 30-AUG-2017, entry version 14. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:CUU25330.1}; GN ORFNames=EM595_3099 {ECO:0000313|EMBL:CUU25330.1}; OS Erwinia gerundensis. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; OC Erwiniaceae; Erwinia. OX NCBI_TaxID=1619313 {ECO:0000313|EMBL:CUU25330.1, ECO:0000313|Proteomes:UP000059419}; RN [1] {ECO:0000313|EMBL:CUU25330.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=E_g_EM595 {ECO:0000313|EMBL:CUU25330.1}; RA Zhang Y., Guo Z.; RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LN907827; CUU25330.1; -; Genomic_DNA. DR RefSeq; WP_067433997.1; NZ_LN907827.1. DR EnsemblBacteria; CUU25330; CUU25330; EM595_3099. DR KEGG; ege:EM595_3099; -. DR PATRIC; fig|1619313.3.peg.3217; -. DR KO; K03665; -. DR Proteomes; UP000059419; Chromosome 1. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000059419}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000059419}. FT DOMAIN 198 365 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 426 AA; 47823 MW; 277D417BA7C0887C CRC64; MFDRYDAGEQ AVLVHIYFSQ DKNTEDLQEF ETLVSSAGVE ALCVVTGSRK SPHPKYFVGE GKAVEIADAV KSSGASVVLF DHALTPAQER NLERLCECRV IDRTGLILDI FAQRARTHEG KLQVELAQLR HLATRLVRGW THLERQKGGI GLRGPGETQL ETDRRLLRNR ISQILSRLER VEKQRDQGRQ SRAKADVPTV SLVGYTNAGK STLFNAITSA DVYVADQLFA TLDPTLRRLD VADVGDVVLA DTVGFIRHLP HDLVAAFKAT LQETRQATLL LHVIDASDVR MGENIEAVQT VLEEIEADEI PALLVMNKID ALDEFEPRID RNDENYPVRV WVSAQTGAGL PLLFQALTER LAGEIAQYDL RLPPEAGRLR SRFYQLQAIE KEWNEEDGSV GLHVRMPIVD WRRLCKQEPS VTDYIV // ID A0A0U9I2S6_9THEO Unreviewed; 413 AA. AC A0A0U9I2S6; DT 16-MAR-2016, integrated into UniProtKB/TrEMBL. DT 16-MAR-2016, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=TSYNT_1137 {ECO:0000313|EMBL:GAQ24152.1}; OS Tepidanaerobacter syntrophicus. OC Bacteria; Firmicutes; Clostridia; Thermoanaerobacterales; OC Thermoanaerobacteraceae; Tepidanaerobacter. OX NCBI_TaxID=224999 {ECO:0000313|EMBL:GAQ24152.1, ECO:0000313|Proteomes:UP000062160}; RN [1] {ECO:0000313|Proteomes:UP000062160} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=JL {ECO:0000313|Proteomes:UP000062160}; RA Sekiguchi Y., Ohashi A., Matsuura N., Tourlousse M.D.; RT "Draft genome sequence of Tepidanaerobacter syntrophicus strain JL."; RL Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; DF976995; GAQ24152.1; -; Genomic_DNA. DR RefSeq; WP_059031258.1; NZ_BCMU01000001.1. DR Proteomes; UP000062160; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000062160}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000062160}. FT DOMAIN 194 359 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 413 AA; 45445 MW; F218742114DC9AC4 CRC64; MISTENKSTK ALLLGMLNDI SDEDSFKELK LLAETAGVEV VGEAVQKRNK IDPAYYVGKG KAEEVAQAVK TLGANAVICD DELSPVQIRN LEDLTGVQII DRTMLILDIF AQRAKTSEGK IQVELAQLQY MMPRLTGKGI ELSQEGGGIG TRGPGETKLE TDRRHIRRRI HHLKEELEDI QKSRKIITQS RAYPVISLIG YTNAGKSTLM NALTNAGVKT GDRLFETLDT TTRGLILPDG RKVLLSDTVG FIRKLPHQLV DAFRATLEEV KEADLLIHVA DGSSPTVEED IAVVNSVLKE LGIEKTPIII AINKIDITGD TAIFIEGYNK DSTIGISALT GKNLDKLLDA ICRMLPSNRR KAELLIPYDN ASALNEIHQN SAISETEYLD EGVKIKGEID IAKLKKYEKY IIG // ID A0A0V0QL99_PSEPJ Unreviewed; 951 AA. AC A0A0V0QL99; DT 16-MAR-2016, integrated into UniProtKB/TrEMBL. DT 16-MAR-2016, sequence version 1. DT 10-MAY-2017, entry version 10. DE SubName: Full=p-loop containing nucleoside triphosphate hydrolase {ECO:0000313|EMBL:KRX02833.1}; GN ORFNames=PPERSA_04036 {ECO:0000313|EMBL:KRX02833.1}; OS Pseudocohnilembus persalinus (Ciliate). OC Eukaryota; Alveolata; Ciliophora; Intramacronucleata; OC Oligohymenophorea; Scuticociliatia; Philasterida; Pseudocohnilembidae; OC Pseudocohnilembus. OX NCBI_TaxID=266149 {ECO:0000313|EMBL:KRX02833.1, ECO:0000313|Proteomes:UP000054937}; RN [1] {ECO:0000313|EMBL:KRX02833.1, ECO:0000313|Proteomes:UP000054937} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=36N120E {ECO:0000313|EMBL:KRX02833.1}; RX PubMed=26486372; DOI=10.1038/srep15470; RA Xiong J., Wang G., Cheng J., Tian M., Pan X., Warren A., Jiang C., RA Yuan D., Miao W.; RT "Genome of the facultative scuticociliatosis pathogen RT Pseudocohnilembus persalinus provides insight into its virulence RT through horizontal gene transfer."; RL Sci. Rep. 5:15470-15470(2015). CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KRX02833.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LDAU01000151; KRX02833.1; -; Genomic_DNA. DR EnsemblProtists; KRX02833; KRX02833; PPERSA_04036. DR Proteomes; UP000054937; Unassembled WGS sequence. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW. DR CDD; cd01878; HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000054937}; KW Hydrolase {ECO:0000313|EMBL:KRX02833.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000054937}. FT DOMAIN 688 859 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 951 AA; 110281 MW; D2AF3C8043496F73 CRC64; MEQIDENQIP KESQQSKYKI QQQPLNECEE FADYIVTSMQ ICENNNFVLF EQKEGEKPLD LRHCIMVFFF EKNDEKKWVV GEVGDIGEGP QIMFYLMDIP ENSKDFGIVN NKLFFPNRDD IKLKEIIDHV NKNLAGKYYL LVRDNCYTLA HLVGQKFCQD YKGEAMKWCN DTILRTGKIS VVKTGHIIYN GGKKLAEQGF IEGKKLVENA PELLNQGLKT GKSISHSPTL KINQPQQQNL NFSISFYFGS KKSKNLKNQF HRKKATKEVL DYSKNLNYEE KQQEALEKQN VKCLVLHPVG YPNKGAEIEL YLAEEAIGLT KSLGWGVSKG PYWQEEFTEN IQKQFDEKQK ISDRKRREEW LREEAVLKGL SNEQYKELYE KEFGQDDQDV ESKQDESEWK QLAKSDVKDG DYIYTPAFKG VYYNGGLVVD LSSSDESDGD MFSEWGNELL RQSFAKSCLI RVRKVSSKNY LNRGKLHEIG TFIKNNDINA VYFNTELSTI QNRNLEKYLL QVVNGKEDEK FFNKSSIAYR NGGHSSDSEL SDSQIDPQHH ENYVQQFDRK LRVFDRYTMI LQIFAKRART QLAKLQIEYT FLNFLRTKLM REGGNTFSYM YNIFQGDLMQ AEQVNLEVVS AKSRLSKGIM TGGGETQLEL QRRLIGEKQA EIQGKIKKLQ SNAEFARKRK QAQLSSVPVI ALIGYTNAGK SALMNSIIKQ EVVESKDLLF QTLSTTSRKI RLISGQQAIL LDTIGFVSNL PHDLVESFKT TLQEVEYADL VLHVRDISHP QTEEQKKTVL KVLKQLNFDQ EFYTKKMVEV WNKIDLIKNE VDYENASVQD YPIVPISAKY KTNVDKLIET VEGKVNFIQG KRKYKLIHGI EKHGERTKWL FQNANITKIE NEKYDYTNVT KEFPYGTVTI EIILDDIQYR RYGLNFGIKD QRELDDQYQS PKKKGMPPPE W // ID A0A0V0RL38_9BILA Unreviewed; 503 AA. AC A0A0V0RL38; DT 16-MAR-2016, integrated into UniProtKB/TrEMBL. DT 16-MAR-2016, sequence version 1. DT 07-JUN-2017, entry version 7. DE SubName: Full=Putative GTP-binding protein 6 {ECO:0000313|EMBL:KRX15193.1}; DE Flags: Fragment; GN Name=gtpbp6 {ECO:0000313|EMBL:KRX15193.1}; GN ORFNames=T07_1288 {ECO:0000313|EMBL:KRX15193.1}; OS Trichinella nelsoni. OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia; OC Trichocephalida; Trichinellidae; Trichinella. OX NCBI_TaxID=6336 {ECO:0000313|EMBL:KRX15193.1, ECO:0000313|Proteomes:UP000054630}; RN [1] {ECO:0000313|EMBL:KRX15193.1, ECO:0000313|Proteomes:UP000054630} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ISS37 {ECO:0000313|EMBL:KRX15193.1}; RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.; RT "Evolution of Trichinella species and genotypes."; RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KRX15193.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JYDL01000138; KRX15193.1; -; Genomic_DNA. DR Proteomes; UP000054630; Unassembled WGS sequence. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR SUPFAM; SSF52540; SSF52540; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000054630}; KW Reference proteome {ECO:0000313|Proteomes:UP000054630}. FT DOMAIN 110 197 GTP-bdg_N. {ECO:0000259|Pfam:PF13167}. FT NON_TER 1 1 {ECO:0000313|EMBL:KRX15193.1}. SQ SEQUENCE 503 AA; 57702 MW; 58C32116E0465B49 CRC64; LLNQQFHLLL CFHLQINGFV CDHPTLPMAV RIFIRQIQHT PISYKRLNSS KSIHKDDDLP AVLPLEDYRD LQRKLDVPLQ GVKKALFVLQ PKVPKPDLLR LATSNESLEQ EALQLVKSVP GWNVAGVYER YVKVNRSRPS ILGKGTIEEL ISYFTNLHHR DGVFLNVARL TPIQHFYLSC AFKMPVYDRY TVALQIFKHY AISKEAKLQA ALAELAYMKE RLQPYINGEI DLKEAVKLGA LQMKMPDKKR RKLLDEQEIA IRGKLDKLKT QRHYLRQNTR RKQCPMIAVI GYTNAEDRRI SSEDRFFATL DVTVHHGQLP CRLDVLYADT VGFFSDLPMG LMPCFDATME EIACSVDALL HVVDRSHESW LSQRLIVVHN LNKLNVEHVI EVWNKCDKLN EIPNSTASQA LLISCLNGEG IDDLKMQIER EILNLCSFHH VTLEVPITGD YINQLYNVAA VKQAVPSEDG QKMLISAVLR PYQLESFLKN YDCVKVLPVK DKE // ID A0A0V0RLI5_9BILA Unreviewed; 487 AA. AC A0A0V0RLI5; DT 16-MAR-2016, integrated into UniProtKB/TrEMBL. DT 16-MAR-2016, sequence version 1. DT 07-JUN-2017, entry version 8. DE SubName: Full=Putative GTP-binding protein 6 {ECO:0000313|EMBL:KRX15194.1}; DE Flags: Fragment; GN Name=gtpbp6 {ECO:0000313|EMBL:KRX15194.1}; GN ORFNames=T07_1288 {ECO:0000313|EMBL:KRX15194.1}; OS Trichinella nelsoni. OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia; OC Trichocephalida; Trichinellidae; Trichinella. OX NCBI_TaxID=6336 {ECO:0000313|EMBL:KRX15194.1, ECO:0000313|Proteomes:UP000054630}; RN [1] {ECO:0000313|EMBL:KRX15194.1, ECO:0000313|Proteomes:UP000054630} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ISS37 {ECO:0000313|EMBL:KRX15194.1}; RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.; RT "Evolution of Trichinella species and genotypes."; RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KRX15194.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JYDL01000138; KRX15194.1; -; Genomic_DNA. DR Proteomes; UP000054630; Unassembled WGS sequence. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR CDD; cd01878; HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000054630}; KW Reference proteome {ECO:0000313|Proteomes:UP000054630}. FT DOMAIN 260 420 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT NON_TER 1 1 {ECO:0000313|EMBL:KRX15194.1}. SQ SEQUENCE 487 AA; 55777 MW; 9D1754EF1895FCD5 CRC64; LPMAVRIFIR QIQHTPISYK RLNSSKSIHK DDDLPAVLPL EDYRDLQRKL DVPLQGVKKA LFVLQPKVPK PDLLRLATSN ESLEQEALQL VKSVPGWNVA GVYERYVKVN RSRPSILGKG TIEELISYFT NLHHRDGVFL NVARLTPIQH FYLSCAFKMP VYDRYTVALQ IFKHYAISKE AKLQAALAEL AYMKERLQPY INGEIDLKEA VKLGALQMKM PDKKRRKLLD EQEIAIRGKL DKLKTQRHYL RQNTRRKQCP MIAVIGYTNA GKSTLIHQLT EDRRISSEDR FFATLDVTVH HGQLPCRLDV LYADTVGFFS DLPMGLMPCF DATMEEIACS DLVLHVVDRS HESWLSQRLI VVHNLNKLNV EHVIEVWNKC DKLNEIPNST ASQALLISCL NGEGIDDLKM QIEREILNLC SFHHVTLEVP ITGDYINQLY NVAAVKQAVP SEDGQKMLIS AVLRPYQLES FLKNYDCVKV LPVKDKE // ID A0A0V0TT44_9BILA Unreviewed; 524 AA. AC A0A0V0TT44; DT 16-MAR-2016, integrated into UniProtKB/TrEMBL. DT 16-MAR-2016, sequence version 1. DT 07-JUN-2017, entry version 7. DE SubName: Full=Putative GTP-binding protein 6 {ECO:0000313|EMBL:KRX42205.1}; DE Flags: Fragment; GN Name=gtpbp6 {ECO:0000313|EMBL:KRX42205.1}; GN ORFNames=T05_1955 {ECO:0000313|EMBL:KRX42205.1}; OS Trichinella murrelli. OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia; OC Trichocephalida; Trichinellidae; Trichinella. OX NCBI_TaxID=144512 {ECO:0000313|EMBL:KRX42205.1, ECO:0000313|Proteomes:UP000055048}; RN [1] {ECO:0000313|EMBL:KRX42205.1, ECO:0000313|Proteomes:UP000055048} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ISS417 {ECO:0000313|EMBL:KRX42205.1}; RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.; RT "Evolution of Trichinella species and genotypes."; RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KRX42205.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JYDJ01000150; KRX42205.1; -; Genomic_DNA. DR Proteomes; UP000055048; Unassembled WGS sequence. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR SUPFAM; SSF52540; SSF52540; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000055048}; KW Reference proteome {ECO:0000313|Proteomes:UP000055048}. FT DOMAIN 131 218 GTP-bdg_N. {ECO:0000259|Pfam:PF13167}. FT NON_TER 1 1 {ECO:0000313|EMBL:KRX42205.1}. SQ SEQUENCE 524 AA; 60165 MW; 86E91EFEB3F3DA6A CRC64; LFVTIVCHLK HFIAKLIHNS CRACVTRMQQ SIYYKIQIYI LDLSATLPMA VRIFIRQIQH TPISYNRLNS SKSIHKDDDL PAVLPLEDYR DLQRKLDVPL QGVRKALFVL QPKVPKPDLL RLATSNESLE QEALQLVKSV PGWNVAGVYE RYVKVNRSRL SILGKGTIEE LISYFTNLHH RDGVFLNVAR LTPIQHFYLS CAFKMPVYDR YTVALQIFKH YAISKEAKLQ AALAELAYMK ERLQPYINGE IDLKEAVKLG ALQMKMPDKK RRKLLDEQEI AIRGKLDKLK TQRHYLRQNT RRKQCPMIAV IGYTNAEDRR ISSEDRFFAT LDVTVHHGQL PCRLDVLYAD TVGFFSDLPM GLMPCFDATM EEIACSVDAL LHVVDRSHES WLSQRLIVVH NLNKLNVEHV IEVWNKCDKL NEIPNSTASQ ALLISCLNGE GIDELKMQIE REILSLCSFH HVTLEVPITG DYINQLYNVA AVKQAVPSED GQKMLISAVL RPYQLESFLK NYDCVKVLPV KDKE // ID A0A0V0UWM8_9BILA Unreviewed; 510 AA. AC A0A0V0UWM8; DT 16-MAR-2016, integrated into UniProtKB/TrEMBL. DT 16-MAR-2016, sequence version 1. DT 07-JUN-2017, entry version 6. DE SubName: Full=Putative GTP-binding protein 6 {ECO:0000313|EMBL:KRX55676.1}; GN Name=gtpbp6 {ECO:0000313|EMBL:KRX55676.1}; GN ORFNames=T09_11540 {ECO:0000313|EMBL:KRX55646.1}, GN T09_12373 {ECO:0000313|EMBL:KRX55676.1}; OS Trichinella sp. T9. OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia; OC Trichocephalida; Trichinellidae; Trichinella. OX NCBI_TaxID=181606 {ECO:0000313|EMBL:KRX55676.1, ECO:0000313|Proteomes:UP000054681}; RN [1] {ECO:0000313|EMBL:KRX55676.1, ECO:0000313|Proteomes:UP000054681} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ISS409 {ECO:0000313|EMBL:KRX55676.1}; RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.; RT "Evolution of Trichinella species and genotypes."; RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KRX55676.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JYDN01000140; KRX55646.1; -; Genomic_DNA. DR EMBL; JYDN01000140; KRX55676.1; -; Genomic_DNA. DR Proteomes; UP000054681; Unassembled WGS sequence. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR SUPFAM; SSF52540; SSF52540; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000054681}; KW Reference proteome {ECO:0000313|Proteomes:UP000054681}. FT DOMAIN 118 204 GTP-bdg_N. {ECO:0000259|Pfam:PF13167}. SQ SEQUENCE 510 AA; 58538 MW; C5837A9C5E934ECC CRC64; MYSTRLLNQQ FHLLLCFHLQ INGFVCNHHL SATLPMAVRI FIRQIQHTPI SYNRLNSSKS IHKDDDLPAV LPLEDYRDLQ RKLDVPLQGV RKALFVLQPK VPKPDLLRLA TSNESLEQEA LQLVKSVPGW NVAGVYERYV KVNRSKLSIL GKGTIEELIS YFNLHHRDGV FLNVARLTPI QHFYLSCAFK MPVYDRYTVA LQIFKHYAIS KEAKLQAALA ELAYMKERLQ PYINGEINLK EAVKLGALQM KMPDKKRRKL LDEQEIAIRG KLDKLKTQRH YLRQNTRRKQ CPMIAVIGYT NAEDRRISSE DRFFATLDVT VHHGQLPCRL DVLYADTVGF FSDLPMGLMP CFDATMEEIA CSVDALLHVV DRSHESWLSQ RLIVVHNLNK LNVEHVIEVW NKCDKLNEIP NSTASQALLI SCLNGEGIDE LKMQIEREIL SLCSFHHVTL EVPITGDYIN QLYNVAAVKQ AVPSEDGQKM LISAVLRPYQ LESFLKNYDC VKVLPVKDKE // ID A0A0V0WE90_9BILA Unreviewed; 524 AA. AC A0A0V0WE90; DT 16-MAR-2016, integrated into UniProtKB/TrEMBL. DT 16-MAR-2016, sequence version 1. DT 07-JUN-2017, entry version 6. DE SubName: Full=Putative GTP-binding protein 6 {ECO:0000313|EMBL:KRX73911.1}; DE Flags: Fragment; GN Name=gtpbp6 {ECO:0000313|EMBL:KRX73911.1}; GN ORFNames=T06_11209 {ECO:0000313|EMBL:KRX73911.1}; OS Trichinella sp. T6. OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia; OC Trichocephalida; Trichinellidae; Trichinella. OX NCBI_TaxID=92179 {ECO:0000313|EMBL:KRX73911.1, ECO:0000313|Proteomes:UP000054673}; RN [1] {ECO:0000313|EMBL:KRX73911.1, ECO:0000313|Proteomes:UP000054673} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ISS34 {ECO:0000313|EMBL:KRX73911.1}; RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.; RT "Evolution of Trichinella species and genotypes."; RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KRX73911.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JYDK01000161; KRX73911.1; -; Genomic_DNA. DR Proteomes; UP000054673; Unassembled WGS sequence. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR SUPFAM; SSF52540; SSF52540; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000054673}; KW Reference proteome {ECO:0000313|Proteomes:UP000054673}. FT DOMAIN 131 218 GTP-bdg_N. {ECO:0000259|Pfam:PF13167}. FT NON_TER 1 1 {ECO:0000313|EMBL:KRX73911.1}. SQ SEQUENCE 524 AA; 60171 MW; 9EB0BE38A6E94A71 CRC64; LFVTIVCHLK HFIAKLIHNS CRACVTRMQQ SIYYKIQIYI LDFSATLPMA VRIFIRQIQH ASISYNRLNS SKSIHKDDDL PAVLPLEDYR DLQRKLDVPL QGVRKALFVL QPKVPKPDLL RLATSNESLE QEALQLVKSV PGWNVAGVYE RYVKVNRSRL SILGKGTIEE LISYFTNLHH RDGVFLNVAR LTPIQHFYLS CAFKMPVYDR YTVALQIFKH YAISKEAKLQ AALAELAYMK ERLQPYINGE IDLKEAVKLG ALQMKMPDKK RRKLLDEQEI AIRGKLDKLK IQRHYLRQNT RRKQCPMIAV IGYTNAEDRR ISSEDRFFAT LDVTVHHGQL PCRLDVLYAD TVGFFSDLPM GLMPCFDATM EEIACSVDAL LHVVDRSHES WLSQRLIVVH NLNKLNVEHV IEVWNKCDKL NEIPNSTASQ ALLISCLNGE GIDELKMQIE REILSLCSFH HVTLEVPITG DYINQLYNVA AVKQAVPSED GQKMLISAVL RPYQLESFLK NYDCVKVLPV KDKE // ID A0A0V0ZZT0_9BILA Unreviewed; 503 AA. AC A0A0V0ZZT0; DT 16-MAR-2016, integrated into UniProtKB/TrEMBL. DT 16-MAR-2016, sequence version 1. DT 07-JUN-2017, entry version 7. DE SubName: Full=Putative GTP-binding protein 6 {ECO:0000313|EMBL:KRY17710.1}; GN Name=gtpbp6 {ECO:0000313|EMBL:KRY17710.1}; GN ORFNames=T12_12682 {ECO:0000313|EMBL:KRY17710.1}; OS Trichinella patagoniensis. OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia; OC Trichocephalida; Trichinellidae; Trichinella. OX NCBI_TaxID=990121 {ECO:0000313|EMBL:KRY17710.1, ECO:0000313|Proteomes:UP000054783}; RN [1] {ECO:0000313|EMBL:KRY17710.1, ECO:0000313|Proteomes:UP000054783} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ISS2496 {ECO:0000313|EMBL:KRY17710.1}; RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.; RT "Evolution of Trichinella species and genotypes."; RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KRY17710.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JYDQ01000057; KRY17710.1; -; Genomic_DNA. DR Proteomes; UP000054783; Unassembled WGS sequence. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR SUPFAM; SSF52540; SSF52540; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000054783}; KW Reference proteome {ECO:0000313|Proteomes:UP000054783}. FT DOMAIN 115 202 GTP-bdg_N. {ECO:0000259|Pfam:PF13167}. SQ SEQUENCE 503 AA; 57891 MW; D8C2CE88F764265B CRC64; MYSTRLLNQQ FHLLLCFHLQ INGFVCDHPT LPMAVRIFIR QIQHTPISYN RLNSSKSIHK DDDLPAVLPL EDYRDLQRKL DVPLQGVRKA LFVLQPKVPK PDLLRLATSN ESLEQEALQL VKSVPGWNVA GVYERYVKVN RSRLSILGKG TIEELISYFT NLHHRDGVFL NVARLTPIQH FYLSCAFKMP VYDRYTVALQ IFKHYAISKE AKLQAALAEL AYMKERLQPY INGEIDLKEA VKLGALQMKM PDKKRRKLLD EQEIAIREKL DKLKTQRHYL RQNTRRKQCP MIAVIGYTNA EDRRISSEDR FFATLDVTVH HGQLPCRLDV LYADTVGFFS DLPMGLMPCF DATMEEIACS VDAHRSHESW LSQRLIVVHN LNKLNVEHVI EVWNKCDKLN EIPNSTASQA LLISCLNGEG IDELKMEIER EILSLCSFHH VTLEVPITGD YINQLYNVAA VKQAVPSEDG QKMLISAVLR PYQLESFLKN YDCVKVLPVK DKE // ID A0A0V1CMP7_TRIBR Unreviewed; 497 AA. AC A0A0V1CMP7; DT 16-MAR-2016, integrated into UniProtKB/TrEMBL. DT 16-MAR-2016, sequence version 1. DT 07-JUN-2017, entry version 7. DE SubName: Full=Putative GTP-binding protein 6 {ECO:0000313|EMBL:KRY50300.1}; GN Name=gtpbp6 {ECO:0000313|EMBL:KRY50300.1}; GN ORFNames=T03_14650 {ECO:0000313|EMBL:KRY50300.1}; OS Trichinella britovi (Parasitic roundworm). OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia; OC Trichocephalida; Trichinellidae; Trichinella. OX NCBI_TaxID=45882 {ECO:0000313|EMBL:KRY50300.1, ECO:0000313|Proteomes:UP000054653}; RN [1] {ECO:0000313|EMBL:KRY50300.1, ECO:0000313|Proteomes:UP000054653} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ISS120 {ECO:0000313|EMBL:KRY50300.1}; RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.; RT "Evolution of Trichinella species and genotypes."; RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KRY50300.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JYDI01000153; KRY50300.1; -; Genomic_DNA. DR Proteomes; UP000054653; Unassembled WGS sequence. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR SUPFAM; SSF52540; SSF52540; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000054653}; KW Reference proteome {ECO:0000313|Proteomes:UP000054653}. FT DOMAIN 104 191 GTP-bdg_N. {ECO:0000259|Pfam:PF13167}. SQ SEQUENCE 497 AA; 57110 MW; 583D27959767C4F4 CRC64; MQQSIYYKIQ IYILDLSATL PMAVRIFIRQ IQHTPISYNR LYSSKSIHKD DDLPAVLPLE DYRDLQRQLD VPLQGVRKAL FVLQPKIPKP DLLRLATSNE SLEQEALQLV KSVPGWNVAG VYERYVKVNR SRLSILGKGT TEELISYFTN LHHRDGVFLN VARLTPIQHF YLSCAFKMPV YDRYTVALQI FKHYAISKEA KLQAALAELA YMKERLQPYI NGEIDLKEAV KLGALQMKMP DKKRRKLLDE QEIAIRGKLD KLKTQRHYLR QNTRRKQCPM IAVIGYTNAE DRRISSEDRF FATLDVTVHH GQLPCRLDVL YADTVGFFSD LPMGLMPCFD ATMEEIACSV DALLHVVDRS HESWLSQRLI VVHNLNKLNV EHVIEVWNKC DKLNEIPNST ASQALLISCL NGEGIDELKM QIEREILSLC SFHHVTLEVP ITGDYINQLY NVAAVKQAVP SEDGQKMLIS AVLRPYQLES FLKNYDCVKV LPVKDKE // ID A0A0V1HJE5_9BILA Unreviewed; 487 AA. AC A0A0V1HJE5; DT 16-MAR-2016, integrated into UniProtKB/TrEMBL. DT 16-MAR-2016, sequence version 1. DT 07-JUN-2017, entry version 8. DE SubName: Full=Putative GTP-binding protein 6 {ECO:0000313|EMBL:KRZ10585.1}; DE Flags: Fragment; GN Name=gtpbp6 {ECO:0000313|EMBL:KRZ10585.1}; GN ORFNames=T11_4301 {ECO:0000313|EMBL:KRZ10585.1}; OS Trichinella zimbabwensis. OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia; OC Trichocephalida; Trichinellidae; Trichinella. OX NCBI_TaxID=268475 {ECO:0000313|EMBL:KRZ10585.1, ECO:0000313|Proteomes:UP000055024}; RN [1] {ECO:0000313|EMBL:KRZ10585.1, ECO:0000313|Proteomes:UP000055024} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ISS1029 {ECO:0000313|EMBL:KRZ10585.1}; RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.; RT "Evolution of Trichinella species and genotypes."; RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KRZ10585.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JYDP01000058; KRZ10585.1; -; Genomic_DNA. DR Proteomes; UP000055024; Unassembled WGS sequence. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR CDD; cd01878; HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000055024}; KW Reference proteome {ECO:0000313|Proteomes:UP000055024}. FT DOMAIN 260 420 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT NON_TER 1 1 {ECO:0000313|EMBL:KRZ10585.1}. SQ SEQUENCE 487 AA; 55810 MW; 74A7CCF7A8DD2A93 CRC64; LPMAVRIFIR QIQHTPISYN RLNSSKSFHE DDDLPAVLPL EDYRDLQRKL DVPLQGVKKA LFVLQPKVPK PDLLRLATSN ESLEQEALQL VKSVPGWSVA GVFERYVKVN RSRPSILGKG TIEELISYFT NLHHREGVFL NVARLTPIQH FYLSCAFKMP VYDRYTVALQ IFKHYAISKE AKLQAALAEL AYMKERLQPY VKGEIDLKEA IKLGAFQIKM PDKKRRKLLD EQEIAIRGKL DKLKTQRHYL RQNTRRKQCP MIAVIGYTNA GKSTLIHQLT EDRRISSEDR FFATLDVTVH HGQLPCRLDV LYADTVGFFS DLPMGLMPCF EATMEEIACS DLVLHVVDRS HESWLSQRLI VVNNLNKLNV EHVIEVWNKC DKLNEIPNST ASQALLISCL NGEGIDELKM QIEREILNLC NFRHVSLEVP ITGDYINQLY NVAAVKQAVP SEDGQKMLIS AVLRPHQLES FLKNYDCVKV LPVKDQE // ID A0A0V1L0J5_9BILA Unreviewed; 510 AA. AC A0A0V1L0J5; DT 16-MAR-2016, integrated into UniProtKB/TrEMBL. DT 16-MAR-2016, sequence version 1. DT 07-JUN-2017, entry version 7. DE SubName: Full=Putative GTP-binding protein 6 {ECO:0000313|EMBL:KRZ53064.1}; GN Name=gtpbp6 {ECO:0000313|EMBL:KRZ53064.1}; GN ORFNames=T02_16370 {ECO:0000313|EMBL:KRZ53064.1}; OS Trichinella nativa. OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia; OC Trichocephalida; Trichinellidae; Trichinella. OX NCBI_TaxID=6335 {ECO:0000313|EMBL:KRZ53064.1, ECO:0000313|Proteomes:UP000054721}; RN [1] {ECO:0000313|EMBL:KRZ53064.1, ECO:0000313|Proteomes:UP000054721} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ISS10 {ECO:0000313|EMBL:KRZ53064.1}; RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.; RT "Evolution of Trichinella species and genotypes."; RL Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KRZ53064.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JYDW01000175; KRZ53064.1; -; Genomic_DNA. DR Proteomes; UP000054721; Unassembled WGS sequence. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR SUPFAM; SSF52540; SSF52540; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000054721}; KW Reference proteome {ECO:0000313|Proteomes:UP000054721}. FT DOMAIN 118 205 GTP-bdg_N. {ECO:0000259|Pfam:PF13167}. SQ SEQUENCE 510 AA; 58570 MW; 1F054D89242B1A64 CRC64; MYSTRLLNKQ FHLLLCFHLQ INGFVCDHHL SATLPMAVRI FIRQIQHASI SYNRLNSSKS IHKDDDLPAV LPLEDYRDLQ RKLDVPLQGV RKALFVLQPK VPKPDLLRLA TSNESLEQEA LQLVKSVPGW NVAGVYERYV KVNRSRLSIL GKGTIEELIS YFTNLHHRDG VFLNVARLTP IQHFYLSCAF KMPVYDRYTV ALQIFKHYAI SKEAKLQAAL AELAYMKERL QPYINGEIDL KEAVKLGALQ MKMPDKKRRK LLDEQEIAIR GKLDKLKIQR HYLRQNTRRK QCPMIAVIGY TNAEDRRISS EDRFFATLDV TVHHGQLPCR LDVLYADTVG FFSDLPMGLM PCFDATMEEI ACSDLVLHVV DRSHESWLSQ RLIVVHNLNK LNVEHVIEVW NKCDKLNEIP NSTASQALLI SCLNGEGIDE LKMQIEREIL SLCSFHHVTL EVPITGDYIN QLYNVAAVKQ AVPSEDGQKM LISAVLRPYQ LESFLKNYDC VKVLPVKDKE // ID A0A0V1L128_9BILA Unreviewed; 520 AA. AC A0A0V1L128; DT 16-MAR-2016, integrated into UniProtKB/TrEMBL. DT 16-MAR-2016, sequence version 1. DT 07-JUN-2017, entry version 8. DE SubName: Full=Putative GTP-binding protein 6 {ECO:0000313|EMBL:KRZ53063.1}; GN Name=gtpbp6 {ECO:0000313|EMBL:KRZ53063.1}; GN ORFNames=T02_16370 {ECO:0000313|EMBL:KRZ53063.1}; OS Trichinella nativa. OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia; OC Trichocephalida; Trichinellidae; Trichinella. OX NCBI_TaxID=6335 {ECO:0000313|EMBL:KRZ53063.1, ECO:0000313|Proteomes:UP000054721}; RN [1] {ECO:0000313|EMBL:KRZ53063.1, ECO:0000313|Proteomes:UP000054721} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ISS10 {ECO:0000313|EMBL:KRZ53063.1}; RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.; RT "Evolution of Trichinella species and genotypes."; RL Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KRZ53063.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JYDW01000175; KRZ53063.1; -; Genomic_DNA. DR Proteomes; UP000054721; Unassembled WGS sequence. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR CDD; cd01878; HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000054721}; KW Reference proteome {ECO:0000313|Proteomes:UP000054721}. FT DOMAIN 293 453 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 520 AA; 59649 MW; 7173AEAE93B0122F CRC64; MYSTRLLNKQ FHLLLCFHLQ INGFVCDHHL SATLPMAVRI FIRQIQHASI SYNRLNSSKS IHKDDDLPAV LPLEDYRDLQ RKLDVPLQGV RKALFVLQPK VPKPDLLRLA TSNESLEQEA LQLVKSVPGW NVAGVYERYV KVNRSRLSIL GKGTIEELIS YFTNLHHRDG VFLNVARLTP IQHFYLSCAF KMPVYDRYTV ALQIFKHYAI SKEAKLQAAL AELAYMKERL QPYINGEIDL KEAVKLGALQ MKMPDKKRRK LLDEQEIAIR GKLDKLKIQR HYLRQNTRRK QCPMIAVIGY TNAGKSTLIH QLTEDRRISS EDRFFATLDV TVHHGQLPCR LDVLYADTVG FFSDLPMGLM PCFDATMEEI ACSDLVLHVV DRSHESWLSQ RLIVVHNLNK LNVEHVIEVW NKCDKLNEIP NSTASQALLI SCLNGEGIDE LKMQIEREIL SLCSFHHVTL EVPITGDYIN QLYNVAAVKQ AVPSEDGQKM LISAVLRPYQ LESFLKNYDC VKVLPVKDKE // ID A0A0V1MYY7_9BILA Unreviewed; 521 AA. AC A0A0V1MYY7; DT 16-MAR-2016, integrated into UniProtKB/TrEMBL. DT 16-MAR-2016, sequence version 1. DT 07-JUN-2017, entry version 8. DE SubName: Full=Putative GTP-binding protein 6 {ECO:0000313|EMBL:KRZ77000.1}; GN Name=gtpbp6 {ECO:0000313|EMBL:KRZ77000.1}; GN ORFNames=T10_6088 {ECO:0000313|EMBL:KRZ77000.1}; OS Trichinella papuae. OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia; OC Trichocephalida; Trichinellidae; Trichinella. OX NCBI_TaxID=268474 {ECO:0000313|EMBL:KRZ77000.1, ECO:0000313|Proteomes:UP000054843}; RN [1] {ECO:0000313|EMBL:KRZ77000.1, ECO:0000313|Proteomes:UP000054843} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ISS1980 {ECO:0000313|EMBL:KRZ77000.1}; RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.; RT "Evolution of Trichinella species and genotypes."; RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KRZ77000.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JYDO01000023; KRZ77000.1; -; Genomic_DNA. DR Proteomes; UP000054843; Unassembled WGS sequence. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR CDD; cd01878; HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000054843}; KW Reference proteome {ECO:0000313|Proteomes:UP000054843}. FT DOMAIN 294 454 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 521 AA; 59605 MW; BFF722FFDE6264C1 CRC64; MIHCTGDSCK ACGTRIQQSI YYKIQIYIFD LSATLPMAVR IFIRQIQHTP ISYNRLNSSK SFHEDDDLPA VLPLEDYRDL QRKLDVPLQG VKKALFVLQP KVPKPDLLRL ATSNESLEQE ALQLVKSVPG WSVAGVFERY VKVNRSRPSI LGTGTIEELI SYFTNLHHRE GVFLNVARLT PIQHFYLSCA FKMPVYDRYT VALQIFKHYA ISKEAKLQAA LAELAYMKER LQPYVKGEID LKEAIKLGAF QIKMPDKKRR KLLDEQEIAI RGKLDKLKTQ RHYLRQNTRR KQCPVIAVIG YTNAGKSTLI HQLTEDRRIS SEDRFFATLD VTVHHGQLPC RLDVLYADTV GFFSDLPMGL MPCFEATMEE IACSDLVLHV VDRSHESWLS QRLIVVNNLN KLNVEHVIEV WNKCDKLNEI PNSTASQALL ISCLNGEGID ELKMQIEREI LNLCNFRHVS LEVPITGDYI NQLYNVAAVK QAVPSEDGQK MLISAVLRPH QLESFLKNYD CVKVLPVKDQ E // ID A0A0V1NN78_9BILA Unreviewed; 524 AA. AC A0A0V1NN78; DT 16-MAR-2016, integrated into UniProtKB/TrEMBL. DT 16-MAR-2016, sequence version 1. DT 07-JUN-2017, entry version 7. DE SubName: Full=Putative GTP-binding protein 6 {ECO:0000313|EMBL:KRZ85409.1}; DE Flags: Fragment; GN Name=gtpbp6 {ECO:0000313|EMBL:KRZ85409.1}; GN ORFNames=T08_8417 {ECO:0000313|EMBL:KRZ85409.1}; OS Trichinella sp. T8. OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia; OC Trichocephalida; Trichinellidae; Trichinella. OX NCBI_TaxID=92180 {ECO:0000313|EMBL:KRZ85409.1, ECO:0000313|Proteomes:UP000054924}; RN [1] {ECO:0000313|EMBL:KRZ85409.1, ECO:0000313|Proteomes:UP000054924} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ISS272 {ECO:0000313|EMBL:KRZ85409.1}; RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.; RT "Evolution of Trichinella species and genotypes."; RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KRZ85409.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JYDM01000143; KRZ85409.1; -; Genomic_DNA. DR Proteomes; UP000054924; Unassembled WGS sequence. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR SUPFAM; SSF52540; SSF52540; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000054924}; KW Reference proteome {ECO:0000313|Proteomes:UP000054924}. FT DOMAIN 131 218 GTP-bdg_N. {ECO:0000259|Pfam:PF13167}. FT NON_TER 1 1 {ECO:0000313|EMBL:KRZ85409.1}. SQ SEQUENCE 524 AA; 60165 MW; 86E91EFEB3F3DA6A CRC64; LFVTIVCHLK HFIAKLIHNS CRACVTRMQQ SIYYKIQIYI LDLSATLPMA VRIFIRQIQH TPISYNRLNS SKSIHKDDDL PAVLPLEDYR DLQRKLDVPL QGVRKALFVL QPKVPKPDLL RLATSNESLE QEALQLVKSV PGWNVAGVYE RYVKVNRSRL SILGKGTIEE LISYFTNLHH RDGVFLNVAR LTPIQHFYLS CAFKMPVYDR YTVALQIFKH YAISKEAKLQ AALAELAYMK ERLQPYINGE IDLKEAVKLG ALQMKMPDKK RRKLLDEQEI AIRGKLDKLK TQRHYLRQNT RRKQCPMIAV IGYTNAEDRR ISSEDRFFAT LDVTVHHGQL PCRLDVLYAD TVGFFSDLPM GLMPCFDATM EEIACSVDAL LHVVDRSHES WLSQRLIVVH NLNKLNVEHV IEVWNKCDKL NEIPNSTASQ ALLISCLNGE GIDELKMQIE REILSLCSFH HVTLEVPITG DYINQLYNVA AVKQAVPSED GQKMLISAVL RPYQLESFLK NYDCVKVLPV KDKE // ID A0A0V1QVQ3_9FLAO Unreviewed; 403 AA. AC A0A0V1QVQ3; DT 16-MAR-2016, integrated into UniProtKB/TrEMBL. DT 16-MAR-2016, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=I600_2136 {ECO:0000313|EMBL:KSA12703.1}; OS Maribacter dokdonensis DSW-8. OC Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales; OC Flavobacteriaceae; Maribacter. OX NCBI_TaxID=1300346 {ECO:0000313|EMBL:KSA12703.1, ECO:0000313|Proteomes:UP000053333}; RN [1] {ECO:0000313|EMBL:KSA12703.1, ECO:0000313|Proteomes:UP000053333} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSW-8 {ECO:0000313|EMBL:KSA12703.1, RC ECO:0000313|Proteomes:UP000053333}; RA Wang D.B., Wang M.; RL Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KSA12703.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LDPE01000002; KSA12703.1; -; Genomic_DNA. DR RefSeq; WP_058104467.1; NZ_LDPE01000002.1. DR EnsemblBacteria; KSA12703; KSA12703; I600_2136. DR PATRIC; fig|1300346.8.peg.2160; -. DR Proteomes; UP000053333; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000053333}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000053333}. FT DOMAIN 200 385 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 403 AA; 46834 MW; 1585249AB747EBD5 CRC64; MIEKKSIDYE KAVLIGIINK EQNEEKVTEY LDELEFLTYT AGGEVTKRFV QRMDVPNPKT LIGSGKMEEV ERYVQENEIG SVIFDDELSP AQQRNIEKIL RCKIIDRTSL ILDIFAQRAQ TSYARTQVEL AQYEYLLPRL TGLWTHLERQ KGGIGMRGPG ETEIETDRRI VRDRITLLKK KLAKIDRQME TQRGNRGALV RVALVGYTNV GKSTLMNVIS KSDVFAENKL FATLDTTVRK VVLGNLPFLL SDTVGFIRKL PTQLVESFKS TLDEVREADL LLHIVDISHP QFEEHIDSVN NILSDIKSSD KKTIMVFNKI DQYEHETIDE DDLVTERTGR HFTINDWKHT WMEKVGDRAI FISALNKENL DEFRKRVYDE VRDIHVTRFP YNNFLYPEHL DEY // ID A0A0V2F9M2_CAUVI Unreviewed; 450 AA. AC A0A0V2F9M2; DT 16-MAR-2016, integrated into UniProtKB/TrEMBL. DT 16-MAR-2016, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=AS593_04615 {ECO:0000313|EMBL:KSB89181.1}; OS Caulobacter vibrioides (Caulobacter crescentus). OC Bacteria; Proteobacteria; Alphaproteobacteria; Caulobacterales; OC Caulobacteraceae; Caulobacter. OX NCBI_TaxID=155892 {ECO:0000313|EMBL:KSB89181.1, ECO:0000313|Proteomes:UP000053705}; RN [1] {ECO:0000313|EMBL:KSB89181.1, ECO:0000313|Proteomes:UP000053705} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=T5M6 {ECO:0000313|EMBL:KSB89181.1, RC ECO:0000313|Proteomes:UP000053705}; RA Wang Y., Zheng S., Rensing C., Kot W., Wang G.; RT "Genome sequence of Se Oxidizing Caulobacter vibrioides T5M6."; RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KSB89181.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LNIY01000095; KSB89181.1; -; Genomic_DNA. DR RefSeq; WP_058348900.1; NZ_LNIY01000095.1. DR EnsemblBacteria; KSB89181; KSB89181; AS593_04615. DR Proteomes; UP000053705; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000053705}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000053705}. FT DOMAIN 218 388 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 450 AA; 49715 MW; 1C74969FAF641C40 CRC64; MSKSTSKSPD GLIDHADPIL RAFVIHPVRP ARGQAALEAR DPKARLEEAV GLAIALDLDV VETAIAPLRA VTPATLFGSG KVQEFKAVCE VEEIDVAVFD DQLTPVQQRN LERGLGVKVV DRTGLILEIF ARRARTREGK LQVELARLDY ERSRLVRTWT HLERQRGGTG NTGGPGETQI ELDRRLIAGT IGKLKRELEE VRRTRTLHRS ARKKVPYPTV ALVGYTNAGK STLFNRLTNA EVVAQDMLFA TLDPTLRTVK LPDGRPAILS DTVGFISDLP HELVEAFRAT LEEVQEADVV LHVRDVANPD TDAQARDVQA VLAELKVTAD DGKTVVEVWN KIDLVDGEER EILEGRARRV DASPVSAVTG EGCVELLRRV GGLIDDTPPM ALRLSPADGE ALAWIYRNGR VVEREDKEDG EVRLVARMDP QALGRFERQF PTVWVMPIGE // ID A0A0V7ZQW8_9CYAN Unreviewed; 583 AA. AC A0A0V7ZQW8; DT 16-MAR-2016, integrated into UniProtKB/TrEMBL. DT 16-MAR-2016, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=BC008_18805 {ECO:0000313|EMBL:KST64864.1}, GN BC008_28110 {ECO:0000313|EMBL:KST67056.1}; OS Mastigocoleus testarum BC008. OC Bacteria; Cyanobacteria; Nostocales; Hapalosiphonaceae; Mastigocoleus. OX NCBI_TaxID=371196 {ECO:0000313|EMBL:KST67056.1, ECO:0000313|Proteomes:UP000053372}; RN [1] {ECO:0000313|EMBL:KST67056.1, ECO:0000313|Proteomes:UP000053372} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BC008 {ECO:0000313|EMBL:KST67056.1, RC ECO:0000313|Proteomes:UP000053372}; RA Guida B.S., Garcia-Pichel F.; RT "Draft Genome of the Euendolithic (true boring) Cyanobacterium RT Mastigocoleus testarum strain BC008."; RL Genome Announc. 0:0-0(2015). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KST67056.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LMTZ01000116; KST64864.1; -; Genomic_DNA. DR EMBL; LMTZ01000091; KST67056.1; -; Genomic_DNA. DR RefSeq; WP_058183746.1; NZ_LMTZ01000116.1. DR EnsemblBacteria; KST64864; KST64864; BC008_18805. DR EnsemblBacteria; KST67056; KST67056; BC008_28110. DR Proteomes; UP000053372; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000053372}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000053372}. FT DOMAIN 410 580 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 369 406 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 583 AA; 64226 MW; 3E7ED3D9B7834F74 CRC64; MPIETIFGNL QGLKPSQLKQ LRRLYHQRIP GDRITTPEFA QRLAAVSTEI NKPVCAYLNR RGQVIRVGVG TPRQTQIPLM ELPRYGAERL SGIRCIATQL KPEASSDAAL TSMALQRLDA LVVMNVTASG FKKRGGAASG YVKEAYLAHL TPQDSRILTA TQGGGNISTS DYSPPSWSIS PPMSLDMLGK QDFMDLVEGL EEEFRREYTA LDVDSDHERV LIVGIMTGDL SSQEFQDTLA EIARLVDTAG GDVVQMLQQK RNRVHPQTVV GEGKVQEIAL AAQTLGANLV VFDRDLSPAQ VRNLEAQIGV RVVDRTEVIL DIFAQRAQSG AGKLQVELAQ LEYMLPRLTG RGQAMSRLGG GIGTRGPGET KLETERRAIQ RRITRLQKEV NQLQAHRERL RQRRQNQGVP TVSIVGYTNA GKSTLLNALT NAEVYTADQL FATLDPTTRR LTVPHAVSGD RQEILLTDTV GFIHELPASL VDAFRATLEE VTEADALVHL VDLSHAAWLN QVRSVREILK QMPVTPGPAI VVFNKIDQAN SETLALAREE FPMAVFISAD KRLGLENLRQ RLGQLINYAV SSQ // ID A0A0V8HKE6_9BACI Unreviewed; 436 AA. AC A0A0V8HKE6; DT 16-MAR-2016, integrated into UniProtKB/TrEMBL. DT 16-MAR-2016, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=AS034_10930 {ECO:0000313|EMBL:KSU62989.1}; OS Bacillus enclensis. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus. OX NCBI_TaxID=1402860 {ECO:0000313|EMBL:KSU62989.1, ECO:0000313|Proteomes:UP000053625}; RN [1] {ECO:0000313|EMBL:KSU62989.1, ECO:0000313|Proteomes:UP000053625} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SGD-1123 {ECO:0000313|EMBL:KSU62989.1, RC ECO:0000313|Proteomes:UP000053625}; RX PubMed=24174310; DOI=10.1007/s10482-013-0066-3; RA Dastager S.G., Mawlankar R., Tang S.K., Srinivasan K., Ramana V.V., RA Shouche Y.S.; RT "Bacillus enclensis sp. nov., isolated from sediment sample."; RL Antonie Van Leeuwenhoek 105:199-206(2014). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KSU62989.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LNQI01000003; KSU62989.1; -; Genomic_DNA. DR RefSeq; WP_058298738.1; NZ_KQ758483.1. DR EnsemblBacteria; KSU62989; KSU62989; AS034_10930. DR Proteomes; UP000053625; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000053625}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000053625}. FT DOMAIN 212 374 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 436 AA; 50008 MW; 7D9C34119FBF18F3 CRC64; MEFIQLIQKK EGRLLQRDVK EKILLTGCQL DEDDLRFQYS MKELEELAKT AQGEVMAVLS QKRDRIDPGT YIGKGKVDEL KALEEQFDPD IIIFNDELSP SQVRNLSKIL DARVIDRTQL ILDIFAQRAR SREGKLQVEL AQLQYLLPRL IGKGTSLSRL GGGIGTRGPG ETKLESDRRH IHRRIDDIKK QLQTIVEHRE RYRERRKKNN TFQAALVGYT NAGKSTLFNR LSTAESYEEN QLFATLDPMT RKMALPSGYF TLLTDTVGFI QDLPTSLIAA FRSTLEEVKE ADLLLHVVDS SNPDYHQHEE TVQSLLEELG MDGMPMLTVY NKRDIIHPEF VPVSGANQIL ISAIDSEDRR QLLLRIEDMV KKQMDKYQVQ VPSNEGKVLS QLKNDTILLN LYFDEDTQLY EAEGYHLKDH QISGSIKKFQ KQKGSK // ID A0A0V8HQ51_9BACI Unreviewed; 421 AA. AC A0A0V8HQ51; DT 16-MAR-2016, integrated into UniProtKB/TrEMBL. DT 16-MAR-2016, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=AS034_00720 {ECO:0000313|EMBL:KSU64702.1}; OS Bacillus enclensis. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus. OX NCBI_TaxID=1402860 {ECO:0000313|EMBL:KSU64702.1, ECO:0000313|Proteomes:UP000053625}; RN [1] {ECO:0000313|EMBL:KSU64702.1, ECO:0000313|Proteomes:UP000053625} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SGD-1123 {ECO:0000313|EMBL:KSU64702.1, RC ECO:0000313|Proteomes:UP000053625}; RX PubMed=24174310; DOI=10.1007/s10482-013-0066-3; RA Dastager S.G., Mawlankar R., Tang S.K., Srinivasan K., Ramana V.V., RA Shouche Y.S.; RT "Bacillus enclensis sp. nov., isolated from sediment sample."; RL Antonie Van Leeuwenhoek 105:199-206(2014). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KSU64702.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LNQI01000001; KSU64702.1; -; Genomic_DNA. DR RefSeq; WP_058298049.1; NZ_KQ758482.1. DR EnsemblBacteria; KSU64702; KSU64702; AS034_00720. DR Proteomes; UP000053625; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000053625}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000053625}. FT DOMAIN 198 367 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 157 191 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 421 AA; 47837 MW; C909F17E426337E5 CRC64; MEERLRAIAV GVNTKEKGED FEYNMLELKG LAEARRIDVL AEMTQNLPKR NHVHYIGKGK IDELLPLIEE MEADVLIAND ELSPSQIRVL EEKLDIRVMD RTMLILDIFA ERAQTREAQL QVEVAQLQYM LPRLIGRRES LGRQGGGSGL ANRGAGETKL ELDRRRIEDN ITALNKELEA LVDLRKTQRK QRKKSGIPVV SLVGYTNAGK STTMNALLET FNSGENKQVF EKDMLFATLD TSVRNITLPD NKSFLLTDTV GFVNKLPHHL VKAFRSTLEE VAEADLIVQV VDYSDPHHET MMEVTNKTLD DIGVGGIPMV YAFNKAELVD EESVGSVVND RIYLSAKQRK GIDELIDVIK GHIFKDYKKC DMLIPFSQGQ LISYFNEHAN VLHTEYEENG TKLTMECRSS DFEKYREYVV Q // ID A0A0V8JER7_9BACI Unreviewed; 412 AA. AC A0A0V8JER7; DT 16-MAR-2016, integrated into UniProtKB/TrEMBL. DT 16-MAR-2016, sequence version 1. DT 07-JUN-2017, entry version 12. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=AS030_06420 {ECO:0000313|EMBL:KSU85152.1}; OS Fictibacillus enclensis. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Fictibacillus. OX NCBI_TaxID=1017270 {ECO:0000313|EMBL:KSU85152.1, ECO:0000313|Proteomes:UP000054099}; RN [1] {ECO:0000313|EMBL:KSU85152.1, ECO:0000313|Proteomes:UP000054099} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NIO-1003 {ECO:0000313|EMBL:KSU85152.1, RC ECO:0000313|Proteomes:UP000054099}; RX PubMed=24343101; DOI=10.1007/s10482-013-0097-9; RA Dastager S.G., Mawlankar R., Srinivasan K., Tang S.K., Lee J.C., RA Ramana V.V., Shouche Y.S.; RT "Fictibacillus enclensis sp. nov., isolated from marine sediment."; RL Antonie Van Leeuwenhoek 105:461-469(2014). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KSU85152.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LNQN01000001; KSU85152.1; -; Genomic_DNA. DR RefSeq; WP_061969623.1; NZ_KQ758617.1. DR EnsemblBacteria; KSU85152; KSU85152; AS030_06420. DR Proteomes; UP000054099; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000054099}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000054099}. FT DOMAIN 202 363 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 412 AA; 46509 MW; B0A098822A61B403 CRC64; MEDTTHSQQE KAILVGCQLP GQTDERFFYS MEELESLTKT AQGQAVATVT QKRDRYDAST FIGKGKIEEI VALEEELEAD LIIFNDELTP AQNRNLSRYF EARIIDRTQL ILDIFATRAR SREGKLQVEL AQLQYILPRL AGIGASLSRL GGGIGTRGPG ETKLEQDRRH IRTKITDIKR QLEDIVHHRE RYRERRKENQ AIQAALVGYT NAGKSTLFNG LTRADSYEEN LLFATLDPLT RKMHLPSGLQ VLVTDTVGFI QDLPTSLIAA FRSTLEEVRE ADVLIHVIDG SSEDRGQHEE TVLSILKELG AASIPMVTVF NKKDQFNEGF IPAAATSISI SAFETEDVQR LKEVIETEMK KQMDYYHIFV PASEGKTLSM LKTTTILMEQ KFEEENQAYE CKGYALPSTK LQ // ID A0A0V8JS52_9BACI Unreviewed; 416 AA. AC A0A0V8JS52; DT 16-MAR-2016, integrated into UniProtKB/TrEMBL. DT 16-MAR-2016, sequence version 1. DT 05-JUL-2017, entry version 13. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=AS180_00300 {ECO:0000313|EMBL:KSU89876.1}; OS Bacillus sp. SGD-V-76. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus. OX NCBI_TaxID=1414648 {ECO:0000313|EMBL:KSU89876.1, ECO:0000313|Proteomes:UP000053681}; RN [1] {ECO:0000313|EMBL:KSU89876.1, ECO:0000313|Proteomes:UP000053681} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SGD-V-76 {ECO:0000313|EMBL:KSU89876.1, RC ECO:0000313|Proteomes:UP000053681}; RA Dastager S.G., Mawlankar R.; RT "Bacillus caseinolyticus sp nov."; RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KSU89876.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LNQP01000001; KSU89876.1; -; Genomic_DNA. DR EnsemblBacteria; KSU89876; KSU89876; AS180_00300. DR Proteomes; UP000053681; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000053681}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000053681}. FT DOMAIN 197 358 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 156 190 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 416 AA; 47663 MW; FE6C956DFA580593 CRC64; MKQELERVIL VGCQLHDDDE RFEYSMDELA SLTETAQGEV LVRLSQKRDR IHPATYIGKG KVEELVALEE ELEPDLIVFN DELSPSQIRN LSSQLEARII DRTQLILDIF AQRAQTKEGK LQVELAQLNY LLPRLVGQGT ALSRLGGGIG TRGPGETKLE SDRRHIRRKI DEIKRQLKTV VSHRERYRER RKRNHVYQIA IVGYTNAGKS TLFNRLTEAG IYEENQLFAT LDPTTRQYTM PSGLTALLTD TVGFIQDLPT TLVAAFRSTL EEVTEADFIL HVVDSGNPDY HNHEQTVHKL LAELDVEDIP MLTVYNKRDV KHELFVPTTP ASVLISAFNK EDLALLGTKI QDEMKKEMEY FHLFIPSDEG KLLAELKTVA LVDSLKFNEE KEKYECRGYI AKEHPIYKQL RMIEES // ID A0A0V8QD30_9FIRM Unreviewed; 416 AA. AC A0A0V8QD30; DT 16-MAR-2016, integrated into UniProtKB/TrEMBL. DT 16-MAR-2016, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=ASU35_12745 {ECO:0000313|EMBL:KSV58485.1}; OS Acetivibrio ethanolgignens. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Ruminococcaceae; OC Acetivibrio. OX NCBI_TaxID=290052 {ECO:0000313|EMBL:KSV58485.1, ECO:0000313|Proteomes:UP000054874}; RN [1] {ECO:0000313|EMBL:KSV58485.1, ECO:0000313|Proteomes:UP000054874} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ACET-33324 {ECO:0000313|EMBL:KSV58485.1, RC ECO:0000313|Proteomes:UP000054874}; RA Zou Y., Xue W., Luo G., Lv M.; RT "Butyribacter intestini gen. nov., sp. nov., a butyric acid-producing RT bacterium of the family Lachnospiraceae isolated from the human RT faeces."; RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KSV58485.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LNAM01000170; KSV58485.1; -; Genomic_DNA. DR RefSeq; WP_058353278.1; NZ_LNAM01000170.1. DR EnsemblBacteria; KSV58485; KSV58485; ASU35_12745. DR Proteomes; UP000054874; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000054874}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000054874}. FT DOMAIN 202 367 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 168 198 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 416 AA; 46535 MW; 0E600E19EBD278F4 CRC64; MTQLHEIKEQ EERVILLGVA TQENDDTEES LEELSELAKT AGAVTVAKVI QNRESVHPGT YIGKGKIKEV RELMDELSAT GVVCDDELSP AQLKNLENEL DTKVIDRTVM ILDIFAKRAS TREGKIQVEL AQLKYRSSRL VGLRSSLSRL GGGIGTRGPG EKKLEMDRRL IRDRIGQLNK ELSEVKQARE TARKQRSKNP VPVIAIVGYT NAGKSTLLNT LTGAGVLEED KLFATLDPTT RNLQLESGQQ ILLTDTVGFI RKLPHHLIDA FRSTLEEAKY ADVILHVVDA SNPQAYAQMH IVYETLRNLG VKDKSVITAF NKQDKLEDTE TILKDFKADK TVKIAAKTGL GLGNLLNTIE EVLREQKVYI EKSYPYNEAG KLQVIRKYGQ LLSEEYREDG IYIKAYVPKE VYNSLG // ID A0A0V8RW08_PYROC Unreviewed; 372 AA. AC A0A0V8RW08; DT 16-MAR-2016, integrated into UniProtKB/TrEMBL. DT 16-MAR-2016, sequence version 1. DT 07-JUN-2017, entry version 9. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=CF15_05060 {ECO:0000313|EMBL:KSW12138.1}; OS Pyrodictium occultum. OC Archaea; Crenarchaeota; Thermoprotei; Desulfurococcales; OC Pyrodictiaceae; Pyrodictium. OX NCBI_TaxID=2309 {ECO:0000313|EMBL:KSW12138.1, ECO:0000313|Proteomes:UP000053352}; RN [1] {ECO:0000313|EMBL:KSW12138.1, ECO:0000313|Proteomes:UP000053352} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=PL-19 {ECO:0000313|EMBL:KSW12138.1, RC ECO:0000313|Proteomes:UP000053352}; RA Utturkar S., Huber H., Leptihn S., Brown S., Stetter K.O., Podar M.; RT "Genome sequence of Pyrodictium occultum PL-19, a marine RT hyperthermophilic archaeon isolated from Volcano, Italy."; RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KSW12138.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LNTB01000001; KSW12138.1; -; Genomic_DNA. DR EnsemblBacteria; KSW12138; KSW12138; CF15_05060. DR OMA; FNNHAHV; -. DR Proteomes; UP000053352; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000053352}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000053352}. FT DOMAIN 188 366 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 372 AA; 41393 MW; A39F1398B2B587D0 CRC64; MKRAILALPR SMEGWEEREA YALVETAGYR VEGVVRYRPV SRSRLFSRAK LEEIAASARG LRDDEEARII VYDELKPREY FRVVREAGVE AIDRTLLILE IFALHAGSRE AKLQIELARL RHRLPLVKEA IRLAKMRELP GFLGPGGYAV DAYYRYMVSR IARIRRELQR LRERRGLERR KRRSAGLPHV AIVGYASAGK TTLFNMLSGE AKPVGPEYFT TVSPKVKAVG VDGLRFAVVD TVGLISRIPP EIIEAFHSTL EEAAEADLIL YVLDVSEEEH VLAEKLSEGL DTLRRIGVID KPMVIAANKM DLVSDRSELD RVLRLVEAMA SSVYPGLQGV IPVSAATGEG LGRLLCRLST LLRGTAGSTC SG // ID A0A0V8T968_9CELL Unreviewed; 496 AA. AC A0A0V8T968; DT 16-MAR-2016, integrated into UniProtKB/TrEMBL. DT 16-MAR-2016, sequence version 1. DT 07-JUN-2017, entry version 12. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=ATM99_09640 {ECO:0000313|EMBL:KSW29172.1}; OS Cellulomonas sp. B6. OC Bacteria; Actinobacteria; Micrococcales; Cellulomonadaceae; OC Cellulomonas. OX NCBI_TaxID=1295626 {ECO:0000313|EMBL:KSW29172.1, ECO:0000313|Proteomes:UP000054319}; RN [1] {ECO:0000313|EMBL:KSW29172.1, ECO:0000313|Proteomes:UP000054319} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=B6 {ECO:0000313|EMBL:KSW29172.1, RC ECO:0000313|Proteomes:UP000054319}; RA Piccinni F.E., Campos E.; RT "Draft Genome Sequence of Cellulolytic and Xylanolytic Cellulomonas RT strain Isolated from Decaying Forest Soil."; RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KSW29172.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LNTD01000072; KSW29172.1; -; Genomic_DNA. DR RefSeq; WP_062102108.1; NZ_LNTD01000072.1. DR EnsemblBacteria; KSW29172; KSW29172; ATM99_09640. DR Proteomes; UP000054319; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 2. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000054319}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000054319}. FT DOMAIN 275 441 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 496 AA; 53131 MW; 20432FAF4E57C4F5 CRC64; MTPQASARSA QEVADDVVAR VLARAGTALQ AGGTDHTAFD GDQLDLEERT SLRRVANLST ELEDVTEVEY RQLRLEKVVL VGLWGAGTAE EAEISLRELA ALAETAGSQV MDGLLQRRRT PDPGTFLGSG KAAELATVVA AVGADTVVVD GELAPSQRRA LEDVVKVKVV DRTALILDIF AQHAKSREGK AQVELAQLEY LLPRLRGWGE SMSRQAGGQV GGAGAGMGSR GPGETKIELD RRRIRNRMAK LRREIAAMAP ARETKRASRR RNAIPSVAIA GYTNAGKSSL LNRLTHAGVL VENALFATLD PTVRRAETTD GRVYTLADTV GFVRALPHQL VEAFRSTLEE VADADLILHV VDAAHPDPEG QIAAVRHVFA DIPGAMDVPE IIVLNKADLA SPEAVARLRS REVHSVVVSA HTGEGVAELQ ELIADQLPRP GVSVDLVVPY SRGDLVSRVH EHGDIDHEEH TPDGTLLRAR VDEGLAAELE AASRTA // ID A0A0W0GJ99_9CHLR Unreviewed; 307 AA. AC A0A0W0GJ99; DT 16-MAR-2016, integrated into UniProtKB/TrEMBL. DT 16-MAR-2016, sequence version 1. DT 07-JUN-2017, entry version 10. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=DEALK_14820 {ECO:0000313|EMBL:KTB48636.1}; OS Dehalogenimonas alkenigignens. OC Bacteria; Chloroflexi; Dehalococcoidia; Dehalogenimonas. OX NCBI_TaxID=1217799 {ECO:0000313|EMBL:KTB48636.1, ECO:0000313|Proteomes:UP000053947}; RN [1] {ECO:0000313|EMBL:KTB48636.1, ECO:0000313|Proteomes:UP000053947} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=IP3-3 {ECO:0000313|EMBL:KTB48636.1, RC ECO:0000313|Proteomes:UP000053947}; RA Key T.A., Richmond D.P., Bowman K.S., Cho Y.-J., Chun J., RA da Costa M.S., Rainey F.A., Moe W.M.; RT "Genome sequence of the organohalide-respiring Dehalogenimonas RT alkenigignens type strain (IP3-3T)."; RL Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KTB48636.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LFDV01000002; KTB48636.1; -; Genomic_DNA. DR EnsemblBacteria; KTB48636; KTB48636; DEALK_14820. DR PATRIC; fig|1217799.6.peg.1530; -. DR Proteomes; UP000053947; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000053947}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000053947}. FT DOMAIN 122 299 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 81 115 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 307 AA; 34697 MW; 297F18A1C27D0ACC CRC64; MAIFDDELTP AQQRTLEDFL KVKVIDRAAL ILDIFARHAK TMEGKLQVEL AQYQYLLPRL AGQWSHLERL GGGIGTRGPG ESQLESDKRL LQQRISKLKD NIDRVSRQRN LYRNTRRARG IPVIAIVGYT NSGKSSLLNA LTKSNVQAEN KLFATLDPTT RRIGLPDNRQ FLLTDTVGFI KKLPPTIIKA FRATLEEIVD STLLIHVIDI NSPNAVEQCQ TVEQILNDLG LGEKPRITVF NKIDLLPELK GRVNEPNRLS MLDDFLQFQP SNTVLTSATR RWGLKNLLET IGRYLPEPYR SEEGSVS // ID A0A0W0R157_9GAMM Unreviewed; 415 AA. AC A0A0W0R157; DT 16-MAR-2016, integrated into UniProtKB/TrEMBL. DT 16-MAR-2016, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=Lade_2086 {ECO:0000313|EMBL:KTC64792.1}; OS Legionella adelaidensis. OC Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales; OC Legionellaceae; Legionella. OX NCBI_TaxID=45056 {ECO:0000313|EMBL:KTC64792.1, ECO:0000313|Proteomes:UP000054859}; RN [1] {ECO:0000313|EMBL:KTC64792.1, ECO:0000313|Proteomes:UP000054859} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=1762-AUS-E {ECO:0000313|EMBL:KTC64792.1, RC ECO:0000313|Proteomes:UP000054859}; RA Burstein D., Amaro F., Zusman T., Lifshitz Z., Cohen O., Gilbert J.A., RA Pupko T., Shuman H.A., Segal G.; RT "Identification of large and diverse effector repertoires of 38 RT Legionella species."; RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KTC64792.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LNKA01000019; KTC64792.1; -; Genomic_DNA. DR RefSeq; WP_058463134.1; NZ_LNKA01000019.1. DR EnsemblBacteria; KTC64792; KTC64792; Lade_2086. DR PATRIC; fig|45056.6.peg.2156; -. DR Proteomes; UP000054859; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000054859}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000054859}. FT DOMAIN 198 363 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 415 AA; 46923 MW; 193049C3741E0C9C CRC64; MFERPKGGER AILVQIALPD LNKEEALAEF KELAKAADAE VIDCVLSSRS VPEPKYFVGL GKAEEIRMMV QEHEAELVLV NHELSPSQER NLERLIQCRV VDRSGLILDI FAQRARTFEG KLQVELAQLQ HLSTRLVRGW THLERQKGGI GLRGPGETQL ETDRRLLRDR IRSINKRLEK VKRSRDQNRR ARIKSALPNV SLVGYTNAGK SSLFNALTGE KIFAANLLFA TLDPTMRKIE LPGSGDAILT DTVGFIRDLP HQLVNAFHAT LEETLESDLL LHVIDIADKN WRDHVQAVEE VLKEIGADKV KRIQVFNKID LQEGWKAKVE FQDDQAKVWV SATTGEGLDL LLQAIAQQLE GILLEETIIL SPAEAKTRAK LYAMNAVLTE KNLENGDWEL LIRITKEEKR KLFNS // ID A0A0W0SNQ3_9GAMM Unreviewed; 423 AA. AC A0A0W0SNQ3; DT 16-MAR-2016, integrated into UniProtKB/TrEMBL. DT 16-MAR-2016, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:KTC84931.1}; GN ORFNames=Lbru_1146 {ECO:0000313|EMBL:KTC84931.1}; OS Legionella brunensis. OC Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales; OC Legionellaceae; Legionella. OX NCBI_TaxID=29422 {ECO:0000313|EMBL:KTC84931.1, ECO:0000313|Proteomes:UP000054742}; RN [1] {ECO:0000313|EMBL:KTC84931.1, ECO:0000313|Proteomes:UP000054742} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43878 {ECO:0000313|EMBL:KTC84931.1, RC ECO:0000313|Proteomes:UP000054742}; RA Burstein D., Amaro F., Zusman T., Lifshitz Z., Cohen O., Gilbert J.A., RA Pupko T., Shuman H.A., Segal G.; RT "Genomic analysis of 38 Legionella species identifies large and RT diverse effector repertoires."; RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KTC84931.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LNXV01000008; KTC84931.1; -; Genomic_DNA. DR RefSeq; WP_058441383.1; NZ_LNXV01000008.1. DR EnsemblBacteria; KTC84931; KTC84931; Lbru_1146. DR PATRIC; fig|29422.6.peg.1204; -. DR Proteomes; UP000054742; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000054742}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000054742}. FT DOMAIN 198 363 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 423 AA; 47693 MW; 44924BCF1F97B259 CRC64; MFERPQGGER AILVQLALPG VDAEKALVEF KELALSAQAE IMTCVTGARS TPEAKYYVGL GKAEEIKQQV LAHKAELVLV NHELSPSQER NLERLLECRV VDRSGLILDI FAQRARTFEG KLQVELAQLQ HLSTRLVRGW THLERQKGGI GLRGPGETQL ETDRRLLRER IKSINKRLEK VRRSRDQNRR ARQKAALPTV SLVGYTNAGK STLFNALTGE HIYAANQLFA TLDPTMRKLE LPGAASVILT DTVGFIRDLP HQLIEAFRAT LEETQEADLL LHVIDVSDPH WRDMVFAVEQ VLEELGANDI PMIQVFNKID QQEGWDAKID RQEDGYKVWL SAKTGAGLDL LCQAIATQLQ GAIIEEEILL APEQAKLRAT LYEMDAVLSE KIEEEGGWRL KIKLTQEQRR RVFGNQAKNY TPN // ID A0A0W0TMW2_9GAMM Unreviewed; 424 AA. AC A0A0W0TMW2; DT 16-MAR-2016, integrated into UniProtKB/TrEMBL. DT 16-MAR-2016, sequence version 1. DT 30-AUG-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:KTC96924.1}; GN ORFNames=Lfee_1836 {ECO:0000313|EMBL:KTC96924.1}; OS Legionella feeleii. OC Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales; OC Legionellaceae; Legionella. OX NCBI_TaxID=453 {ECO:0000313|EMBL:KTC96924.1, ECO:0000313|Proteomes:UP000054698}; RN [1] {ECO:0000313|EMBL:KTC96924.1, ECO:0000313|Proteomes:UP000054698} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=WO-44C {ECO:0000313|EMBL:KTC96924.1, RC ECO:0000313|Proteomes:UP000054698}; RA Burstein D., Amaro F., Zusman T., Lifshitz Z., Cohen O., Gilbert J.A., RA Pupko T., Shuman H.A., Segal G.; RT "Genomic analysis of 38 Legionella species identifies large and RT diverse effector repertoires."; RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KTC96924.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LNYB01000080; KTC96924.1; -; Genomic_DNA. DR EnsemblBacteria; KTC96924; KTC96924; Lfee_1836. DR PATRIC; fig|453.4.peg.2015; -. DR Proteomes; UP000054698; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000054698}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000054698}. FT DOMAIN 200 365 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 424 AA; 47705 MW; 73C1D0E3BA7BF89F CRC64; MQLFERPQGG ERAILVQLAL PGVDAGTALA EFKELAVSAQ AEVLACVLGT RAAPEAKYYV GLGKAEEIQH LVKEHQAELV LVNHELSPSQ ERNLERLFQC RVVDRSGLIL DIFAQRARTF EGKLQVELAQ LQHLSTRLVR GWTHLERQKG GIGLRGPGET QLETDRRLLR ERIRSIHKRL EKVRRSRDQN RRARRKLAMP TVSLVGYTNA GKSTLFNALT GEQIYVADQL FATLDPTMRK LELPGAASAI LTDTVGFIRD LPHHLIEAFR ATLEETQEAD LLLHVIDISD PHWRDTVFAV QQVLDELEVK DIPIIQVFNK IDQQEGWQPK LDRQEEGYKV WVSAKTGVGL DLLREAIATQ LQGDIIEEEI RLAASAAKLR AQLYQLGAVL SETTSEEGGW QLKVRLTETQ KSRLFPAMDD TKSS // ID A0A0W0U5V3_9GAMM Unreviewed; 406 AA. AC A0A0W0U5V3; DT 16-MAR-2016, integrated into UniProtKB/TrEMBL. DT 16-MAR-2016, sequence version 1. DT 07-JUN-2017, entry version 10. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=Lgee_0586 {ECO:0000313|EMBL:KTD03036.1}; OS Legionella geestiana. OC Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales; OC Legionellaceae; Legionella. OX NCBI_TaxID=45065 {ECO:0000313|EMBL:KTD03036.1, ECO:0000313|Proteomes:UP000054785}; RN [1] {ECO:0000313|EMBL:KTD03036.1, ECO:0000313|Proteomes:UP000054785} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 49504 {ECO:0000313|EMBL:KTD03036.1, RC ECO:0000313|Proteomes:UP000054785}; RA Burstein D., Amaro F., Zusman T., Lifshitz Z., Cohen O., Gilbert J.A., RA Pupko T., Shuman H.A., Segal G.; RT "Genomic analysis of 38 Legionella species identifies large and RT diverse effector repertoires."; RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KTD03036.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LNYC01000014; KTD03036.1; -; Genomic_DNA. DR EnsemblBacteria; KTD03036; KTD03036; Lgee_0586. DR PATRIC; fig|45065.4.peg.627; -. DR Proteomes; UP000054785; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000054785}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000054785}. FT DOMAIN 185 350 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 406 AA; 44602 MW; 818549934AD05F85 CRC64; MQMALPDVDA LSALAEFGEL ARSAGAVVVG TVTSQRVRPE AKYCIGEGKA LEIQALMAET DANLVLVNHE LSPSQTRNLE RLLGARVIDR SGLILDIFAR RARTFEGKLQ VELAQLEHLS TRLVRGWTHL ERQKGGIGLR GPGETQLETD RRLLRARIRV IRERLEKVRK SRDQNRRARE KAALPTVSLV GYTNAGKSTL FNALTGASTH AANQLFATLD PNMRSLELRG AGTVILADTV GFIRDLPHQL VAAFRATLEE TVLADLLLHV IDASDANWRE HVNAVNAVLT EAGAIDIPMI LVFNKTDLRE GWDIKSAPGD LPPKVWLSAK TGEGLDLLAT LMSTALFGAA KEEEWVLAPE DARLRARLYA LNAVLKESTT EEGGWRLLVR LSPAARERLL QVRPPA // ID A0A0W0VCN4_9GAMM Unreviewed; 422 AA. AC A0A0W0VCN4; DT 16-MAR-2016, integrated into UniProtKB/TrEMBL. DT 16-MAR-2016, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=Ljor_2172 {ECO:0000313|EMBL:KTD17866.1}; OS Legionella jordanis. OC Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales; OC Legionellaceae; Legionella. OX NCBI_TaxID=456 {ECO:0000313|EMBL:KTD17866.1, ECO:0000313|Proteomes:UP000055035}; RN [1] {ECO:0000313|EMBL:KTD17866.1, ECO:0000313|Proteomes:UP000055035} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BL-540 {ECO:0000313|EMBL:KTD17866.1, RC ECO:0000313|Proteomes:UP000055035}; RA Burstein D., Amaro F., Zusman T., Lifshitz Z., Cohen O., Gilbert J.A., RA Pupko T., Shuman H.A., Segal G.; RT "Genomic analysis of 38 Legionella species identifies large and RT diverse effector repertoires."; RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KTD17866.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LNYJ01000011; KTD17866.1; -; Genomic_DNA. DR RefSeq; WP_058471582.1; NZ_LNYJ01000011.1. DR EnsemblBacteria; KTD17866; KTD17866; Ljor_2172. DR PATRIC; fig|456.5.peg.2328; -. DR Proteomes; UP000055035; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000055035}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000055035}. FT DOMAIN 198 363 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 422 AA; 47737 MW; 91AA4AFA3C702E37 CRC64; MFERPQGGER AILVQLALPE IDAEKALEEF KELAISAQAE VVGCVLGRRS TPEAKYYVGL GKAEEIQQQV QALQADLVLV NHELSPSQER NLERLFQCRV VDRSGLILDI FAQRARTFEG KLQVELAQLQ HLSTRLVRGW THLERQKGGI GLRGPGETQL ETDRRLLRER IRSINKRLEK VRKSRDQNRR ARKKAAMPTV SLVGYTNAGK STLFNALTGE QIYAANQLFA TLDPTMRKTE LPGATSVILA DTVGFIRDLP HQLIEAFRAT LEETQEADLL LHVIDISDPH WREMAAAVGQ VLLELGVQDI PIIQVFNKID QQEGWQAKID LQDGAYKVWL SAKTGEGLDL LREAITKQLQ GGILEEEIVL TPQDAKLRSE LYAIHAVLDE KIEEDGWRLT IKLTKEQKQK LFLKESREQK HS // ID A0A0W0VFC8_9GAMM Unreviewed; 417 AA. AC A0A0W0VFC8; DT 16-MAR-2016, integrated into UniProtKB/TrEMBL. DT 16-MAR-2016, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=Llan_2397 {ECO:0000313|EMBL:KTD18794.1}; OS Legionella lansingensis. OC Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales; OC Legionellaceae; Legionella. OX NCBI_TaxID=45067 {ECO:0000313|EMBL:KTD18794.1, ECO:0000313|Proteomes:UP000054869}; RN [1] {ECO:0000313|EMBL:KTD18794.1, ECO:0000313|Proteomes:UP000054869} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 49751 {ECO:0000313|EMBL:KTD18794.1, RC ECO:0000313|Proteomes:UP000054869}; RA Burstein D., Amaro F., Zusman T., Lifshitz Z., Cohen O., Gilbert J.A., RA Pupko T., Shuman H.A., Segal G.; RT "Genomic analysis of 38 Legionella species identifies large and RT diverse effector repertoires."; RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KTD18794.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LNYI01000057; KTD18794.1; -; Genomic_DNA. DR RefSeq; WP_028372502.1; NZ_LNYI01000057.1. DR EnsemblBacteria; KTD18794; KTD18794; Llan_2397. DR PATRIC; fig|45067.4.peg.2517; -. DR Proteomes; UP000054869; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000054869}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000054869}. FT DOMAIN 198 363 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 417 AA; 47321 MW; D0EF42EE86254E3C CRC64; MFERPQGGER AILVQLALPE VDTEQALAEF KELAVSAQAE IVAVVLGARS NPEVKYYVGM GKAEEIQQQV QIHHADLVLV NHELSPSQER NLERLLQCRV VDRSGLILDI FAQRARTFEG KLQVELAQLQ HLSTRLIRGW THLERQKGGI GLRGPGETQL ETDRRLLRER IKSINKRLEK VRRSRDQNRR ARKKAAMPTV SLVGYTNAGK STLFNALTGE HIYAADQLFA TLDPTMRKIE LPGSTPVILA DTVGFIRDLP HQLIEAFRAT LEETEEADLL LHVIDVSDPH WRDMASAVEQ VLQELGVNDI PIIQVFNKID QQKGWEAKID QQDDIYKVWL SAKTGAGLNL LREAIAKQLQ GAISEEEIWL GPEKAKLRST LYNIDAVLNE RTEDGGWRLK IKLTHEQKQR LFPKKYI // ID A0A0W0VNN2_9GAMM Unreviewed; 433 AA. AC A0A0W0VNN2; DT 16-MAR-2016, integrated into UniProtKB/TrEMBL. DT 16-MAR-2016, sequence version 1. DT 07-JUN-2017, entry version 10. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=Llon_0941 {ECO:0000313|EMBL:KTD21776.1}; OS Legionella londiniensis. OC Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales; OC Legionellaceae; Legionella. OX NCBI_TaxID=45068 {ECO:0000313|EMBL:KTD21776.1, ECO:0000313|Proteomes:UP000054997}; RN [1] {ECO:0000313|EMBL:KTD21776.1, ECO:0000313|Proteomes:UP000054997} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 49505 {ECO:0000313|EMBL:KTD21776.1, RC ECO:0000313|Proteomes:UP000054997}; RA Burstein D., Amaro F., Zusman T., Lifshitz Z., Cohen O., Gilbert J.A., RA Pupko T., Shuman H.A., Segal G.; RT "Genomic analysis of 38 Legionella species identifies large and RT diverse effector repertoires."; RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KTD21776.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LNYK01000014; KTD21776.1; -; Genomic_DNA. DR EnsemblBacteria; KTD21776; KTD21776; Llon_0941. DR PATRIC; fig|45068.5.peg.1018; -. DR Proteomes; UP000054997; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000054997}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000054997}. FT DOMAIN 206 371 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 433 AA; 48494 MW; 07D534F436BA212D CRC64; MCFLRVDILF ERPEGGERAV LVQLALPGID AERALAEFKE LAVSAGAEIQ GTVCGARAVP EPKYFVGAGK AEEIRQQVLA YEAELVLVNH ELSPSQERNL ERLLQCRVVD RTGLILDIFA RRARTFEGKL QVELAQLQHL STRLVRGWTH LERQKGGIGL RGPGETQLET DRRLLRERIK TIHQRLEKVR KSRDQSRQAR RKASLPTVAL VGYTNAGKST LFNKLTGAQL FAANQLFATL DPTMRRLDLP GSQPVILADT VGFIRDLPHQ LIDAFHATLE ETKEADLLLQ VIDISDLNWR EQALSVDKVL HEIGADKIPK IQVFNKIDLQ EGWQAKLDCQ EESCKVWISA QTGAGLDLLR TAVIQMLHGA VFEEEVELSP NEGKLRAKLY ELDAVLGEKA LAEGGWRLLI RISRDKKQEL FHGKGPEKTN PNG // ID A0A0W0WJR2_9GAMM Unreviewed; 414 AA. AC A0A0W0WJR2; DT 16-MAR-2016, integrated into UniProtKB/TrEMBL. DT 16-MAR-2016, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=Lisr_0383 {ECO:0000313|EMBL:KTD32573.1}; OS Legionella israelensis. OC Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales; OC Legionellaceae; Legionella. OX NCBI_TaxID=454 {ECO:0000313|EMBL:KTD32573.1, ECO:0000313|Proteomes:UP000054761}; RN [1] {ECO:0000313|EMBL:KTD32573.1, ECO:0000313|Proteomes:UP000054761} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Bercovier 4 {ECO:0000313|EMBL:KTD32573.1, RC ECO:0000313|Proteomes:UP000054761}; RA Burstein D., Amaro F., Zusman T., Lifshitz Z., Cohen O., Gilbert J.A., RA Pupko T., Shuman H.A., Segal G.; RT "Genomic analysis of 38 Legionella species identifies large and RT diverse effector repertoires."; RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KTD32573.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LNYH01000012; KTD32573.1; -; Genomic_DNA. DR RefSeq; WP_058500774.1; NZ_LNYH01000012.1. DR EnsemblBacteria; KTD32573; KTD32573; Lisr_0383. DR PATRIC; fig|454.4.peg.403; -. DR Proteomes; UP000054761; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000054761}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000054761}. FT DOMAIN 198 363 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 414 AA; 46606 MW; F9C042E25037A43B CRC64; MFERWQGGER AILVQLGLPG IDSEKALAEF EELARSANAE IMGIIRGARA TPEVKYYVGL GKAKEIQEQV AALNADLVLV NHELSPSQER NLERLLQCRV VDRSGLILDI FAQRARTFEG KLQVELAQLQ HLSTRLVRGW THLERQKGGI GLRGPGETQL ETDRRLLRER IKSIHKRLEK VRRSRDQSRQ ARRKAALSTV SLVGYTNAGK STLFNALTHE KIYVANQLFA TLDPTMRKLE LPGSSDAILV DTVGFIRELP HHLIEAFRAT LEETQEADLL LHVIDISDPN WRDTVQSVQQ VLAELKVDDI PLIQVFNKID LQEGWESKVD YTGQYVKVWV SAATGAGLDL LKGVIAEQLH GQIVIEKIVL SPGEAKLRAR LYELGAVLDE SINESGEWLL TIRLTRAQKE RLFS // ID A0A0W0WQB2_9GAMM Unreviewed; 416 AA. AC A0A0W0WQB2; DT 16-MAR-2016, integrated into UniProtKB/TrEMBL. DT 16-MAR-2016, sequence version 1. DT 30-AUG-2017, entry version 12. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=Lmor_1900 {ECO:0000313|EMBL:KTD34503.1}; OS Legionella moravica. OC Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales; OC Legionellaceae; Legionella. OX NCBI_TaxID=39962 {ECO:0000313|EMBL:KTD34503.1, ECO:0000313|Proteomes:UP000054985}; RN [1] {ECO:0000313|EMBL:KTD34503.1, ECO:0000313|Proteomes:UP000054985} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43877 {ECO:0000313|EMBL:KTD34503.1, RC ECO:0000313|Proteomes:UP000054985}; RA Burstein D., Amaro F., Zusman T., Lifshitz Z., Cohen O., Gilbert J.A., RA Pupko T., Shuman H.A., Segal G.; RT "Genomic analysis of 38 Legionella species identifies large and RT diverse effector repertoires."; RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KTD34503.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LNYN01000020; KTD34503.1; -; Genomic_DNA. DR RefSeq; WP_028382946.1; NZ_LNYN01000020.1. DR EnsemblBacteria; KTD34503; KTD34503; Lmor_1900. DR PATRIC; fig|39962.5.peg.2084; -. DR Proteomes; UP000054985; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000054985}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}. FT DOMAIN 198 363 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 416 AA; 46638 MW; C1F48246D905ABB4 CRC64; MFERPQGGER AILVQLALPG VDAEKALAEF EELALSAQAE ILDCVLGTRA TPDAKYYLGK GKAEEISQLV KALDAELVLV NHELSPSQER NLERLFECRV VDRSGLILDI FAQRARTFEG KLQVELAQLQ HLSTRLVRGW THLERQKGGI GLRGPGETQL ETDRRLLRER IRYINKRLEK VRCSRDQNRQ ARKKADMATV SLVGYTNAGK STLFNALTGE NIYAANQLFA TLDPTMRKLE LPGSLPVILA DTVGFIRDLP HHLVEAFRAT LEETQQANLL IHVIDISDPH WRDTVFAVQK VLDEIGVSDI PVIQVFNKID LQEGWEPKID CNEGSCKVWL SAATGQGLEL LKEAIAAQLH GAVLIEYIIL NSAQAKLRAQ LYQLGAVLSE SINEEGDWQL KIRITVDQKQ RLLHHS // ID A0A0W0WVZ6_9GAMM Unreviewed; 421 AA. AC A0A0W0WVZ6; DT 16-MAR-2016, integrated into UniProtKB/TrEMBL. DT 16-MAR-2016, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=Lnau_1473 {ECO:0000313|EMBL:KTD36489.1}; OS Legionella nautarum. OC Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales; OC Legionellaceae; Legionella. OX NCBI_TaxID=45070 {ECO:0000313|EMBL:KTD36489.1, ECO:0000313|Proteomes:UP000054725}; RN [1] {ECO:0000313|EMBL:KTD36489.1, ECO:0000313|Proteomes:UP000054725} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 49506 {ECO:0000313|EMBL:KTD36489.1, RC ECO:0000313|Proteomes:UP000054725}; RA Burstein D., Amaro F., Zusman T., Lifshitz Z., Cohen O., Gilbert J.A., RA Pupko T., Shuman H.A., Segal G.; RT "Genomic analysis of 38 Legionella species identifies large and RT diverse effector repertoires."; RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KTD36489.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LNYO01000013; KTD36489.1; -; Genomic_DNA. DR RefSeq; WP_058504479.1; NZ_LNYO01000013.1. DR EnsemblBacteria; KTD36489; KTD36489; Lnau_1473. DR PATRIC; fig|45070.6.peg.1544; -. DR Proteomes; UP000054725; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000054725}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000054725}. FT DOMAIN 198 363 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 421 AA; 47032 MW; D4BD838EABBB15CA CRC64; MFERPQSGER AILVQLALPG VDAEKALAEF KELALSAQAE VLACVVGARA TPEAKYYVGL GKAEEIQQLV EEHDAELVLV NHELSPSQER NLERLLQCRV IDRSGLILDI FAQRARTFEG KLQVELAQLQ HISTRLIRGW THLERQKGGI GLRGPGETQL ETDRRLLRER IKSINKRLEK VRRSRDQNRR ARQKAAMPTV SLVGYTNAGK STLFNALTGE HIYVADQLFA TLDPTMRKVE LPGAGAIILA DTVGFIRDLP HQLVEAFRAT LEETAEADLL LQVIDISDPN WREMVFSVQQ VLAEIGVSEI PTIQVFNKID AQENWLPKMD QQEDGAKVWL SAKSGAGLDL LSEAIATQLH GKISEETLSL KPSEAKLRAK LYQLDAVLQE VPSDEGGWHL KVKLTQAQKK RLFPLENKSA E // ID A0A0W0XMK9_9GAMM Unreviewed; 424 AA. AC A0A0W0XMK9; DT 16-MAR-2016, integrated into UniProtKB/TrEMBL. DT 16-MAR-2016, sequence version 1. DT 30-AUG-2017, entry version 12. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=Lrub_2678 {ECO:0000313|EMBL:KTD45881.1}; OS Legionella rubrilucens. OC Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales; OC Legionellaceae; Legionella. OX NCBI_TaxID=458 {ECO:0000313|EMBL:KTD45881.1, ECO:0000313|Proteomes:UP000054608}; RN [1] {ECO:0000313|EMBL:KTD45881.1, ECO:0000313|Proteomes:UP000054608} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=WA-270A-C2 {ECO:0000313|EMBL:KTD45881.1, RC ECO:0000313|Proteomes:UP000054608}; RA Burstein D., Amaro F., Zusman T., Lifshitz Z., Cohen O., Gilbert J.A., RA Pupko T., Shuman H.A., Segal G.; RT "Genomic analysis of 38 Legionella species identifies large and RT diverse effector repertoires."; RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KTD45881.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LNYT01000022; KTD45881.1; -; Genomic_DNA. DR RefSeq; WP_058532634.1; NZ_LNYT01000022.1. DR EnsemblBacteria; KTD45881; KTD45881; Lrub_2678. DR PATRIC; fig|458.5.peg.2792; -. DR Proteomes; UP000054608; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000054608}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000054608}. FT DOMAIN 198 363 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 424 AA; 47586 MW; 99EC9EC0B7923952 CRC64; MFERPQGGER AILVQLALPG VDAGRALEEF KELAVSAQAD VIACVTGARA TPEARYYVGL GKAEEIQELV QAEQAELVLV NHELSPSQER NLERLFQCRV VDRSGLILDI FAQRARTFEG KLQVELAQLQ HISTRLIRGW THLERQKGGI GLRGPGETQL ETDRRLLRER IKYINKRLEK VRRSRDQNRR ARQKAALKTV SLVGYTNAGK STLFNALTGG HSYAADQLFA TLDPTMRKLD IPGSSPIILA DTVGFIRDLP HDLVEAFRAT LEETAEADLL LHVIDIADPN WRDTVFAVQQ VLKEIGVDDI PVIQVFNKID QHEDWQPKLD MQDDNCKVWL SAKTGEGLDL LIKAIATLLH GDIIEETVSL GPDQAKLRAQ LYQMGAVKDE VSQEEGGWQL TITMTQSQKE RLFTPKSDNL EPEY // ID A0A0W0Y4V1_9GAMM Unreviewed; 416 AA. AC A0A0W0Y4V1; DT 16-MAR-2016, integrated into UniProtKB/TrEMBL. DT 16-MAR-2016, sequence version 1. DT 30-AUG-2017, entry version 12. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:KTD51977.1}; GN ORFNames=Lqui_0821 {ECO:0000313|EMBL:KTD51977.1}; OS Legionella quinlivanii. OC Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales; OC Legionellaceae; Legionella. OX NCBI_TaxID=45073 {ECO:0000313|EMBL:KTD51977.1, ECO:0000313|Proteomes:UP000054618}; RN [1] {ECO:0000313|EMBL:KTD51977.1, ECO:0000313|Proteomes:UP000054618} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CDC#1442-AUS-E {ECO:0000313|EMBL:KTD51977.1, RC ECO:0000313|Proteomes:UP000054618}; RA Burstein D., Amaro F., Zusman T., Lifshitz Z., Cohen O., Gilbert J.A., RA Pupko T., Shuman H.A., Segal G.; RT "Genomic analysis of 38 Legionella species identifies large and RT diverse effector repertoires."; RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KTD51977.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LNYS01000006; KTD51977.1; -; Genomic_DNA. DR RefSeq; WP_058506915.1; NZ_LNYS01000006.1. DR EnsemblBacteria; KTD51977; KTD51977; Lqui_0821. DR PATRIC; fig|45073.5.peg.868; -. DR Proteomes; UP000054618; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000054618}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000054618}. FT DOMAIN 198 363 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 416 AA; 46768 MW; 86F65C7C6AFC7BAF CRC64; MFERPKAGER AILVQLALPG LNAERALQEF KELATSAKAE VVAVITGSRA VPEAKYYVGL GKAEEIQQQV EEHKAELVLV NHELSPSQER NLERLLQCRV VDRSGLILDI FAQRARTFEG KLQVELAQLQ HLSTRLVRGW THLERQKGGI GLRGPGETQL ETDRRLLRER IRYINKRLEK VRRSRDQNRR ARQKAEMPTV SLVGYTNAGK STLFNALTGE QIYAANQLFA TLDPTMRKVD LPGSGSIILA DTVGFIRDLP HQLVEAFRAT LEETQEADLL LHVVDIADPI WRENVAAVEQ VLAEIEVDDI PIIQVFNKID QQEGWTPRVD QQAEGSKVWL SAKTGIGLDG LREAIAIHLH GQVTDEMLRL APDQAKLRAS LYQLNAVKSE SINEDGSWEL NVRLTKAQRA ALFNKQ // ID A0A0W0Z4V3_9GAMM Unreviewed; 418 AA. AC A0A0W0Z4V3; DT 16-MAR-2016, integrated into UniProtKB/TrEMBL. DT 16-MAR-2016, sequence version 1. DT 30-AUG-2017, entry version 12. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=Lsha_0577 {ECO:0000313|EMBL:KTD64146.1}; OS Legionella shakespearei DSM 23087. OC Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales; OC Legionellaceae; Legionella. OX NCBI_TaxID=1122169 {ECO:0000313|EMBL:KTD64146.1, ECO:0000313|Proteomes:UP000054600}; RN [1] {ECO:0000313|EMBL:KTD64146.1, ECO:0000313|Proteomes:UP000054600} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 49655 {ECO:0000313|EMBL:KTD64146.1, RC ECO:0000313|Proteomes:UP000054600}; RA Burstein D., Amaro F., Zusman T., Lifshitz Z., Cohen O., Gilbert J.A., RA Pupko T., Shuman H.A., Segal G.; RT "Genomic analysis of 38 Legionella species identifies large and RT diverse effector repertoires."; RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KTD64146.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LNYW01000019; KTD64146.1; -; Genomic_DNA. DR RefSeq; WP_018576728.1; NZ_LNYW01000019.1. DR EnsemblBacteria; KTD64146; KTD64146; Lsha_0577. DR PATRIC; fig|1122169.6.peg.666; -. DR Proteomes; UP000054600; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000054600}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000054600}. FT DOMAIN 198 363 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 418 AA; 46542 MW; AF38560104424CDC CRC64; MFERPQGGER AILVQLALPG VDAEKALAEF EELALSANAE ILDCVLGARA TPDAKYYVGK GKADEIAQLV KAFDAELVLV NHELSPSQER NLERLFQCRV VDRSGLILDI FAQRARTFEG KLQVELAQLQ HLSTRLIRGW THLERQKGGI GLRGPGETQL ETDRRLLRER IKSINKRLEK VRSSREQNRQ SRRKASMPTV SLVGYTNAGK STLFNALTGE NIYVADQLFA TLDPTMRKLE LPGAAAAILA DTVGFIRDLP HDLVEAFRAT LEETQQADLL LHVIDISDPH WRDTVFSVQQ VLDELGVDSI PIVQVFNKID LHEGWEPKVE LNEGSCKVWI SAATGLGLTL LKETIASQLH GVVLVEDIVI KATQAKLRAQ LYQLGAVLTE TITEEGNWLL KIRITQAQKQ RLFSLPAA // ID A0A0W0ZA62_LEGSP Unreviewed; 425 AA. AC A0A0W0ZA62; DT 16-MAR-2016, integrated into UniProtKB/TrEMBL. DT 16-MAR-2016, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:KTD65996.1}; GN ORFNames=Lspi_0285 {ECO:0000313|EMBL:KTD65996.1}; OS Legionella spiritensis. OC Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales; OC Legionellaceae; Legionella. OX NCBI_TaxID=452 {ECO:0000313|EMBL:KTD65996.1, ECO:0000313|Proteomes:UP000054877}; RN [1] {ECO:0000313|EMBL:KTD65996.1, ECO:0000313|Proteomes:UP000054877} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Mt.St.Helens-9 {ECO:0000313|EMBL:KTD65996.1, RC ECO:0000313|Proteomes:UP000054877}; RA Burstein D., Amaro F., Zusman T., Lifshitz Z., Cohen O., Gilbert J.A., RA Pupko T., Shuman H.A., Segal G.; RT "Genomic analysis of 38 Legionella species identifies large and RT diverse effector repertoires."; RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KTD65996.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LNYX01000003; KTD65996.1; -; Genomic_DNA. DR RefSeq; WP_058482233.1; NZ_LNYX01000003.1. DR EnsemblBacteria; KTD65996; KTD65996; Lspi_0285. DR PATRIC; fig|452.5.peg.318; -. DR Proteomes; UP000054877; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000054877}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000054877}. FT DOMAIN 198 363 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 425 AA; 47593 MW; B321E9A7B0875A52 CRC64; MFERPQGGER AVLVQLALPG IDAGKALAEF QELALSANAE VMTCISGSRA TPEAKYFVGL GKAEEIQAAV KHHQAELVLV NHELSPSQER NLERLLQCRV VDRSGLILDI FAQRARTFEG KLQVELAQLQ HLSTRLVRGW THLERQKGGI GLRGPGETQL ETDRRLLRDR IKYINKRLEK VRRSRDQNRR ARRKASLCTV SLVGYTNAGK STLFNALTAG HSYVADQLFA TLDPTMRKLD LPGSSPVILA DTVGFIRDLP HHLVEAFRAT LEETEQADLL LHVIDISDLD WRDNVFAVEQ VLNEIGVDKL PVIQVFNKID QQPDWQAKLN QQENGCKVWV SAKTGAGLDL LVKAIATELH GVIIEETILV EARNAKLRAQ LYQSGAVVSE YVDDKGDWQM TIRLTQAQKR RLFQEPMIHG DEGEG // ID A0A0W0ZT78_9GAMM Unreviewed; 422 AA. AC A0A0W0ZT78; DT 16-MAR-2016, integrated into UniProtKB/TrEMBL. DT 16-MAR-2016, sequence version 1. DT 30-AUG-2017, entry version 12. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:KTD72395.1}; GN ORFNames=Ltuc_0242 {ECO:0000313|EMBL:KTD72395.1}; OS Legionella tucsonensis. OC Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales; OC Legionellaceae; Legionella. OX NCBI_TaxID=40335 {ECO:0000313|EMBL:KTD72395.1, ECO:0000313|Proteomes:UP000054693}; RN [1] {ECO:0000313|EMBL:KTD72395.1, ECO:0000313|Proteomes:UP000054693} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 49180 {ECO:0000313|EMBL:KTD72395.1, RC ECO:0000313|Proteomes:UP000054693}; RA Burstein D., Amaro F., Zusman T., Lifshitz Z., Cohen O., Gilbert J.A., RA Pupko T., Shuman H.A., Segal G.; RT "Genomic analysis of 38 Legionella species identifies large and RT diverse effector repertoires."; RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KTD72395.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LNZA01000001; KTD72395.1; -; Genomic_DNA. DR RefSeq; WP_058519545.1; NZ_LNZA01000001.1. DR EnsemblBacteria; KTD72395; KTD72395; Ltuc_0242. DR PATRIC; fig|40335.7.peg.250; -. DR Proteomes; UP000054693; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000054693}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000054693}. FT DOMAIN 198 363 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 422 AA; 47627 MW; B7A0869D3D050D55 CRC64; MFERPQGGER AVLVQLALPG VDADKALQEF EELALSAKAE ILDCVLGTRA TPDAKYYIGK GKAEEIAQRV KALDAELVLV NHELSPSQER NLERLFECRV VDRSGLILDI FAQRARTFEG KLQVELAQLQ HLSTRLIRGW THLERQKGGI GLRGPGETQL ETDRRLLRER IKYINKRLEK VRSSRDQNRQ ARRKASLLTV SLVGYTNAGK STLFNTLTGE SIYVADQLFA TLDPTMRQLN LPGSSSVILT DTVGFIRDLP HQLIEAFRAT LEETQQADLL LHVIDISDVH WRDNVFSVQC VLDELGVHDI PIIQVFNKID LKEGWKAKID YQEENCKVWI SAAANLGLDL LKEAISTQLH GAVFIENVVL KATQAKLRAQ LYELGSVLSE SHNEKGDWLL KIRITQAQKQ RLFASENSYR EG // ID A0A0W1A567_9GAMM Unreviewed; 419 AA. AC A0A0W1A567; DT 16-MAR-2016, integrated into UniProtKB/TrEMBL. DT 16-MAR-2016, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=Lwal_2220 {ECO:0000313|EMBL:KTD76498.1}; OS Legionella waltersii. OC Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales; OC Legionellaceae; Legionella. OX NCBI_TaxID=66969 {ECO:0000313|EMBL:KTD76498.1, ECO:0000313|Proteomes:UP000054729}; RN [1] {ECO:0000313|EMBL:KTD76498.1, ECO:0000313|Proteomes:UP000054729} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51914 {ECO:0000313|EMBL:KTD76498.1, RC ECO:0000313|Proteomes:UP000054729}; RA Burstein D., Amaro F., Zusman T., Lifshitz Z., Cohen O., Gilbert J.A., RA Pupko T., Shuman H.A., Segal G.; RT "Genomic analysis of 38 Legionella species identifies large and RT diverse effector repertoires."; RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KTD76498.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LNZB01000051; KTD76498.1; -; Genomic_DNA. DR RefSeq; WP_058480851.1; NZ_LNZB01000051.1. DR EnsemblBacteria; KTD76498; KTD76498; Lwal_2220. DR PATRIC; fig|66969.6.peg.2413; -. DR Proteomes; UP000054729; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000054729}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000054729}. FT DOMAIN 198 363 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 419 AA; 46836 MW; E3FB7C0999BDA168 CRC64; MFERPQGGER AVLVQLALPG VDAGKALDEF KELALSANAE VLDCVTGSRA TPDAKYYVGK GKAEDISLLV KSLNAELVLV NHELSPSQER NLEKLFECRV VDRSGLILDI FAQRARTFEG KLQVELAQLQ HLSTRLVRGW THLERQKGGI GLRGPGETQL ETDRRLLRDR IRYINKRLEK VRCSRDQNRQ ARKKAALATV SLVGYTNAGK STLFNVLTGD DSFVADQLFA TLDPTMRKLE LPGSAAVILA DTVGFIRDLP HHLVEAFRAT LEETQQADLL LHVIDVSDPN WRENVFSVQK VLDELGVNDI PIIQVFNKID RHEGWLPKVD YTEDSCKVWI SASKGLGLDL LKEAIAAQLH GQILIEDIVV QSTEAKLRAQ LYQLGAVLSE TITDTGDWHL RIRITAQQKQ RLFPLGSQK // ID A0A0W1AE94_9GAMM Unreviewed; 414 AA. AC A0A0W1AE94; DT 16-MAR-2016, integrated into UniProtKB/TrEMBL. DT 16-MAR-2016, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=Lwor_1185 {ECO:0000313|EMBL:KTD79671.1}; OS Legionella worsleiensis. OC Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales; OC Legionellaceae; Legionella. OX NCBI_TaxID=45076 {ECO:0000313|EMBL:KTD79671.1, ECO:0000313|Proteomes:UP000054662}; RN [1] {ECO:0000313|EMBL:KTD79671.1, ECO:0000313|Proteomes:UP000054662} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 49508 {ECO:0000313|EMBL:KTD79671.1, RC ECO:0000313|Proteomes:UP000054662}; RA Burstein D., Amaro F., Zusman T., Lifshitz Z., Cohen O., Gilbert J.A., RA Pupko T., Shuman H.A., Segal G.; RT "Genomic analysis of 38 Legionella species identifies large and RT diverse effector repertoires."; RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KTD79671.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LNZC01000012; KTD79671.1; -; Genomic_DNA. DR RefSeq; WP_058493000.1; NZ_LNZC01000012.1. DR EnsemblBacteria; KTD79671; KTD79671; Lwor_1185. DR PATRIC; fig|45076.6.peg.1293; -. DR Proteomes; UP000054662; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000054662}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000054662}. FT DOMAIN 198 363 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 414 AA; 46295 MW; 52039A5DBF2E97CE CRC64; MFERPQGGER AILVQLALPG VDAEKALAEF RELALSAHAE LIDCVVGTRA TPDAKYYLGK GKAEEVCELV KALDADLVLV NHELSPSQER NLERLFECRV VDRSGLILDI FAQRARTFEG KLQVELAQLQ HLSTRLVRGW THLERQKGGI GLRGPGETQL ETDRRLLRER IRYINNRLEK VRCSRDQNRQ ARKKADMATV SLVGYTNAGK STLFNALTGE SIYAANQLFA TLDPTMRKLE LPGSMPVILA DTVGFIRDLP HHLVEAFRAT LEETQQANLL IHVIDISDPH WRDTVFAVQK VLDELGVSDI PLIQVFNKID VQEGWAPKMD LNEGACKVWL SAATGQGLDL LKEAIAAQLY GCVLIEDVII KSTQAKLRAQ LYQLGSVISE SINAEGDWEL KIRITANQKQ RLFS // ID A0A0W1DV48_9SPHN Unreviewed; 446 AA. AC A0A0W1DV48; DT 16-MAR-2016, integrated into UniProtKB/TrEMBL. DT 16-MAR-2016, sequence version 1. DT 07-JUN-2017, entry version 13. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=ATE67_04955 {ECO:0000313|EMBL:KTE21984.1}; OS Sphingopyxis sp. H050. OC Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales; OC Sphingomonadaceae; Sphingopyxis. OX NCBI_TaxID=1759072 {ECO:0000313|EMBL:KTE21984.1, ECO:0000313|Proteomes:UP000053439}; RN [1] {ECO:0000313|EMBL:KTE21984.1, ECO:0000313|Proteomes:UP000053439} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=H050 {ECO:0000313|EMBL:KTE21984.1, RC ECO:0000313|Proteomes:UP000053439}; RA Zhang Y., Guo Z.; RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KTE21984.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LNRZ01000002; KTE21984.1; -; Genomic_DNA. DR RefSeq; WP_058815513.1; NZ_LNRZ01000002.1. DR EnsemblBacteria; KTE21984; KTE21984; ATE67_04955. DR Proteomes; UP000053439; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000053439}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}. FT DOMAIN 206 386 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 172 199 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 446 AA; 49306 MW; 02007575B31FC5EC CRC64; MIDSEGEVTR GAAALLVVPE WHSQRLPRDL DARVEEAKGL ALAIGLDVVA AHPLRLRQTR AATLLGVGQI EAIKPDIAAH GVQLVIVDAP LTPIQQRNLE TEFGAKVIDR TGLILEIFGE RAATAEGRLQ VELAHLDYQA GRLVRSWTHL ERQRGGFGFL GGPGETQIEA DRRMIRNRMA RIRKQLEDAR RTRQLQRSKR QRAPWPVIAL VGYTNAGKST FFNRLTGSDV MAEDLLFATL DPTMREIRLP GIDKAILSDT VGFVSDLPTE LVAAFRATLE EVTTADLIVH VRDIVHPDSD AQYDDVRAIL ESLGVNGSQN GEGEDTADAV PQIEIWNKID TADPDRRVQI EEMAARRLDV AVISAVTGEG VEVARTLMAS QLTAQHRVER IFLGFDQGEA MAWLHARGEV LSDEVDGEGH MLTVRLDPAD RARFERLWPL RSAPTP // ID A0A0W1KMM4_9ACTO Unreviewed; 443 AA. AC A0A0W1KMM4; DT 16-MAR-2016, integrated into UniProtKB/TrEMBL. DT 16-MAR-2016, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX_1 {ECO:0000313|EMBL:KTF04798.1}; GN Synonyms=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=AQZ59_00098 {ECO:0000313|EMBL:KTF04798.1}; OS Trueperella bernardiae. OC Bacteria; Actinobacteria; Actinomycetales; Actinomycetaceae; OC Trueperella. OX NCBI_TaxID=59561 {ECO:0000313|EMBL:KTF04798.1, ECO:0000313|Proteomes:UP000054404}; RN [1] {ECO:0000313|EMBL:KTF04798.1, ECO:0000313|Proteomes:UP000054404} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=LCDC 89-0504 {ECO:0000313|EMBL:KTF04798.1, RC ECO:0000313|Proteomes:UP000054404}; RA Bernier A.-M., Bernard K.; RT "Draft Genome Sequence of the Type Strain Trueperella bernardiae LCDC RT 89-0504T, Isolated from Blood Culture."; RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KTF04798.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LNIZ01000001; KTF04798.1; -; Genomic_DNA. DR EnsemblBacteria; KTF04798; KTF04798; AQZ59_00098. DR PATRIC; fig|59561.3.peg.98; -. DR Proteomes; UP000054404; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000054404}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000054404}. FT DOMAIN 222 387 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 443 AA; 48057 MW; CAE8F6E896556F90 CRC64; MRRVEGLSTE LTDVTEVEYR QLRLERVVLI GVVDDDMKAG EESLRELAAL ATTAGSQVLD GALQRRPHPD PATYFGSGKA RELAELVAAT GADTVIADSE LSPSQRRALE DIVKVKVVDR TALILDIFAQ HAKSREGKAQ VELAQLEYLL PRLRGWGESM SRQAGGRVAS GEGIGSRGPG ETKIELDRRR IHRRMAKLRK DIAHMGNARQ TKRAARRKNR TPSVVVVGYT NAGKSSLMNV LTGAGVLVEN ALFATLDPTV RRALTRDGRE YTLTDTVGFV RNLPTQLVEA FRSTLEEAAD ADVLLHVVDA AHDDPVAQVD AVHEVLADVD GALDVPELIV LSKVDIADPV TVATLRSRFP DAMVVSAVTG EGIEELRTRI EELLPHPQVA VDVVIPYDRG DLVSRIHEDG EILHESHEEA GTHMVARVNP DVAAAVEALG GQA // ID A0A0W1QFH6_9SPHN Unreviewed; 430 AA. AC A0A0W1QFH6; DT 16-MAR-2016, integrated into UniProtKB/TrEMBL. DT 16-MAR-2016, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=ATB93_18195 {ECO:0000313|EMBL:KTF67259.1}; OS Sphingomonas sp. WG. OC Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales; OC Sphingomonadaceae; Sphingomonas. OX NCBI_TaxID=1592629 {ECO:0000313|EMBL:KTF67259.1, ECO:0000313|Proteomes:UP000052965}; RN [1] {ECO:0000313|EMBL:KTF67259.1, ECO:0000313|Proteomes:UP000052965} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=WG {ECO:0000313|EMBL:KTF67259.1, RC ECO:0000313|Proteomes:UP000052965}; RA Li H., Feng Z., Sun Y., Jiao X., Zhou W., Zhu H.; RT "Draft Genome Sequence of Sphingomonas sp. WG, a welan gum producing RT strain."; RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KTF67259.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LNOS01000094; KTF67259.1; -; Genomic_DNA. DR RefSeq; WP_019369923.1; NZ_LNOS01000094.1. DR EnsemblBacteria; KTF67259; KTF67259; ATB93_18195. DR Proteomes; UP000052965; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000052965}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000052965}. FT DOMAIN 208 378 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 174 201 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 430 AA; 47597 MW; B4CE5691237C6864 CRC64; MSTGFERDPD EFARGARALV VYPDMGGSSR DAEARLEETA GLAAAIGVDV VERVAVRLRQ PKPGTLIGSG QVEALAETVR DGELQLAVFD AALTPVQQRN LETALGCKVI DRTGLILEIF GERARTAEGR LQVELAHLDY QAGRLVRSWT HLERQRGGFG FLGGPGETQI EADRRLIRDR MARLRRELDQ VSRTRTLHRD RRQRAPWPVV ALVGYTNAGK STLFNRLTGA EVMAENLLFA TLDPTLRQIS LPGIDKAILS DTVGFVSELP TQLVAAFKAT LEEVVSADLL IHVRDIAHPD TEAQRADVEK VLQEIGVSEQ TPRFEAWNKL DLLDEEQREE ALAMAARRTD EVRVISALNG EGVDALVEAV AGRLTEGHRR YTLRLDPADG AAAAWLHQHG DVIGQHIEDE QAVYEVRMAP RDYERFVTRG // ID A0A0W1R9X5_9EURY Unreviewed; 440 AA. AC A0A0W1R9X5; DT 16-MAR-2016, integrated into UniProtKB/TrEMBL. DT 16-MAR-2016, sequence version 1. DT 07-JUN-2017, entry version 10. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=AUR64_11215 {ECO:0000313|EMBL:KTG10155.1}; OS Haloprofundus marisrubri. OC Archaea; Euryarchaeota; Halobacteria; Haloferacales; Haloferacaceae; OC Haloprofundus. OX NCBI_TaxID=1514971 {ECO:0000313|EMBL:KTG10155.1, ECO:0000313|Proteomes:UP000054387}; RN [1] {ECO:0000313|EMBL:KTG10155.1, ECO:0000313|Proteomes:UP000054387} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SB9 {ECO:0000313|EMBL:KTG10155.1, RC ECO:0000313|Proteomes:UP000054387}; RA Zhang G., Stingl U., Rashid M.; RT "Haloprofundus marisrubri gen. nov., sp. nov., an extremely halophilic RT archaeon isolated from the Discovery deep brine-seawater interface in RT the Red Sea."; RL Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KTG10155.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LOPU01000018; KTG10155.1; -; Genomic_DNA. DR RefSeq; WP_058581510.1; NZ_LOPU01000018.1. DR EnsemblBacteria; KTG10155; KTG10155; AUR64_11215. DR Proteomes; UP000054387; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000054387}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000054387}. FT DOMAIN 199 387 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 440 AA; 48604 MW; B1556BFAA42EAE35 CRC64; MQQRTSDNDQ SAIVAKRTEP SEAAGKTAEI EALADAAGYD VVETVTQTRH EDATYQFGRG KAEALGRRLA ESDIDTIVFD NPLSPQQAYS LGELLPDSVA IVDRYRLILD IFAEQAGTTE AQLQVRLAEL RYELPRVKME IRLETEAANE RRTRGGMDEK EHRRVLDLRE RIQRVEAKLD GVDTVGADRR RNHRAAGRDI VALAGYTNAG KSTLLQRLAA DLELGDNDAR HADESETAAA EDCLFKTLDT TTRRGELDGR EVLLTDTVGF VRDLPHWLVE SFESTLSVSH RADVVVLVVD ASDAPDEVDA KLDASLDTLD DADGVILPVL NKVDRLSADE LTARRRLVED RVSEVDAATD PVAVSATDAT NLDRLRSAIR RELPTECLSL VLPNTGKTQA FVSWAHDHGR VPDIDYDAES VTLTFEGRPE LVERAEARVD // ID A0A0W1RAZ9_9EURY Unreviewed; 435 AA. AC A0A0W1RAZ9; DT 16-MAR-2016, integrated into UniProtKB/TrEMBL. DT 16-MAR-2016, sequence version 1. DT 05-JUL-2017, entry version 12. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=AUR64_12505 {ECO:0000313|EMBL:KTG10535.1}; OS Haloprofundus marisrubri. OC Archaea; Euryarchaeota; Halobacteria; Haloferacales; Haloferacaceae; OC Haloprofundus. OX NCBI_TaxID=1514971 {ECO:0000313|EMBL:KTG10535.1, ECO:0000313|Proteomes:UP000054387}; RN [1] {ECO:0000313|EMBL:KTG10535.1, ECO:0000313|Proteomes:UP000054387} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SB9 {ECO:0000313|EMBL:KTG10535.1, RC ECO:0000313|Proteomes:UP000054387}; RA Zhang G., Stingl U., Rashid M.; RT "Haloprofundus marisrubri gen. nov., sp. nov., an extremely halophilic RT archaeon isolated from the Discovery deep brine-seawater interface in RT the Red Sea."; RL Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KTG10535.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LOPU01000018; KTG10535.1; -; Genomic_DNA. DR EnsemblBacteria; KTG10535; KTG10535; AUR64_12505. DR Proteomes; UP000054387; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000054387}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000054387}. FT DOMAIN 190 373 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 106 133 {ECO:0000256|SAM:Coils}. FT COILED 156 186 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 435 AA; 48504 MW; FA4D99749DBE013A CRC64; MPEDGTAVVA KRVDSGSADL GEITELARAA GYSVVGELTQ SREEDPAYEF GEGKVDELAA LVRRSDADTL VIDNRLGPYQ TYNIGQKLPE GVEVVDRFTL ILDIFGQRAQ TRKAQLQVEL AELRYELPRA EAKASLAKRD ERPGFMGLGE YDESRERDIK AQIANIKQEL DAIADKEETR REQRRESGFD LVALAGYTNA GKSTLLRRLA AELDVDENED LHPDLEATAE SEDRLFTTLG TTTRRAETGK RNVLLTDTVG FVSNLPHWLV ESFKSTLDSV YRADLVLLVV DASESVEEMR EKLVTSHDTL YERNEAPIVT VLNKIDRIDD DELEEKKAAL TALAPNPVAV SGKTGENVEK LQARVESELP AWERERLMMP LVDDTMSVVS WIHDHGHVET EEYDDDHVLV EFEARPAIVE QARAKAADLT PVESA // ID A0A0W1RUR1_9GAMM Unreviewed; 450 AA. AC A0A0W1RUR1; DT 16-MAR-2016, integrated into UniProtKB/TrEMBL. DT 16-MAR-2016, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=AUR63_09675 {ECO:0000313|EMBL:KTG17402.1}; OS Halothiobacillus sp. XI15. OC Bacteria; Proteobacteria; Gammaproteobacteria; Chromatiales; OC Halothiobacillaceae; Halothiobacillus. OX NCBI_TaxID=1766620 {ECO:0000313|EMBL:KTG17402.1, ECO:0000313|Proteomes:UP000053033}; RN [1] {ECO:0000313|Proteomes:UP000053033} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=XI15 {ECO:0000313|Proteomes:UP000053033}; RA Zhang G., Stingl U., Rashid M.; RT "Haloferax marisrubri sp. nov., isolated from the Discovery deep RT brine-seawater interface in the Red Sea."; RL Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KTG17402.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LOPX01000004; KTG17402.1; -; Genomic_DNA. DR RefSeq; WP_058574593.1; NZ_LOPX01000004.1. DR EnsemblBacteria; KTG17402; KTG17402; AUR63_09675. DR Proteomes; UP000053033; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000053033}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000053033}. FT DOMAIN 201 368 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 167 194 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 450 AA; 50307 MW; 865087477B29019B CRC64; MEFFERHKGG ERAVLLHVEQ RALDSNEDLS EFRELVRSAG AEILAESTVN RQTPDPRLFI GKGKAEELAE MVAAHEAELV IVNAQLSPSQ ERNLEALVKC RVLDRTGLIL DIFAQRARSH EGKLQVELAQ LNHLSTRLVR GWTHLERQRG GSIGLRGPGE TQLEMDRRLL GGRIKQLKER IARVRRQRAE GRKGRQQSDV PTVALVGYTN AGKSTLFNAL TVAESFAANQ LFATLDTTLR RVEMNPQLTV VFADTVGFIR HLPHELVSAF RSTLEETLEA DLLLHVVDAS SPERDRQIED VEAVLEEIGA GKLPMLTVMN KIDRLEDGAV RVDRDATEAP TRVWVSAKES LGLDELREAL GERLEPSTVS RRLFIPMADG RLYAMLQGEG GVVSEDVDES GWHLEIVLPV ARWGQLLKKE PTLAEMVLDA PPTPEPEPFE QVLAERAERH // ID A0A0W1SRP4_9GAMM Unreviewed; 430 AA. AC A0A0W1SRP4; DT 16-MAR-2016, integrated into UniProtKB/TrEMBL. DT 16-MAR-2016, sequence version 1. DT 30-AUG-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=AUR68_12815 {ECO:0000313|EMBL:KTG28982.1}; OS Idiomarina sp. H105. OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales; OC Idiomarinaceae; Idiomarina. OX NCBI_TaxID=1766622 {ECO:0000313|EMBL:KTG28982.1, ECO:0000313|Proteomes:UP000054149}; RN [1] {ECO:0000313|EMBL:KTG28982.1, ECO:0000313|Proteomes:UP000054149} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=H105 {ECO:0000313|EMBL:KTG28982.1, RC ECO:0000313|Proteomes:UP000054149}; RA Zhang G., Stingl U., Rashid M.; RT "The draft genome sequence of Idiomarina sp., isolated from Erba RT brine-seawater interface of Red Sea."; RL Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KTG28982.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LOPZ01000035; KTG28982.1; -; Genomic_DNA. DR EnsemblBacteria; KTG28982; KTG28982; AUR68_12815. DR Proteomes; UP000054149; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000054149}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}. FT DOMAIN 198 364 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 430 AA; 48072 MW; 5E105A787F41B6C4 CRC64; MFDRYEGGDY AILVHVDFPT EVNREDLSEL KLLANSSGVE TRGVITTSRG SPTPKYFVGS GKAEEIAEQV KALDANIVIF NHALSPTQER NLEAICKCRV LDRTGLILDI FAQRARTHEG KLQVELAQLR HISTRLVRGW THLERQKGGI GLRGPGETQL ETDRRLIRGR IKNILRRLEK VQKQREQGRR ARQKAEIPTV SLVGYTNAGK STLFNQLTEA GVYAADQLFA TLDPTLRKLT IEDVGDLILA DTVGFIRHLP HDLVAAFKAT LQETQEADLL LHVVDVADDQ QQSNIDQVTE VLEEIDAGDV PQLIICNKID QIDGAKPRID YEDGKPVRVW VSAQEGIGVE LILEALTQLL GPQMMDATLK IPPSMGKLRG TLYELNSVTS EDVDENGQLA LHVRLSSVDW QRLKKRFDSN LDELIVQKNN // ID A0A0W1SS55_9GAMM Unreviewed; 436 AA. AC A0A0W1SS55; DT 16-MAR-2016, integrated into UniProtKB/TrEMBL. DT 16-MAR-2016, sequence version 1. DT 30-AUG-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=AUR68_27630 {ECO:0000313|EMBL:KTG29122.1}; OS Idiomarina sp. H105. OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales; OC Idiomarinaceae; Idiomarina. OX NCBI_TaxID=1766622 {ECO:0000313|EMBL:KTG29122.1, ECO:0000313|Proteomes:UP000054149}; RN [1] {ECO:0000313|EMBL:KTG29122.1, ECO:0000313|Proteomes:UP000054149} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=H105 {ECO:0000313|EMBL:KTG29122.1, RC ECO:0000313|Proteomes:UP000054149}; RA Zhang G., Stingl U., Rashid M.; RT "The draft genome sequence of Idiomarina sp., isolated from Erba RT brine-seawater interface of Red Sea."; RL Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KTG29122.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LOPZ01000033; KTG29122.1; -; Genomic_DNA. DR EnsemblBacteria; KTG29122; KTG29122; AUR68_27630. DR Proteomes; UP000054149; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000054149}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}. FT DOMAIN 199 365 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 436 AA; 49016 MW; 546E72739CB110F0 CRC64; MFFERPEAGE TAVLVHVDFY DEQAREDPGE FLELVRSAGA EPATLLTASR QRPDSRTFIG SGKLDELRAM LAAHQAELVI FNHSLSPSQQ RNLEKELKCR VLDRTGLILD IFAQRARTHE GKLQVELAQL EYMSTRLIRG WTHLERQKGG IGLRGPGETQ LETDRRLLRG RIKSIHKRLD KVRSQREQNR RARARAEIHS VSLVGYTNAG KSTLFNALTS AEVYAADQLF ATLDPTLRRL EIEDVGPVVM ADTVGFIRHL PHKLVEAFQA TLQEAAEATL LVHVIDAADP DRELNVEQVD NVLKEIGADS VPVLKVMNKI DKLDSAPRIE RDGHGVPEVV WLSAQQGHGL DLLHEALTER LANDVIGFSL TLSPEQGKLR AGLHELNAVR EESFDEQGRS VLDVRLPRRD FNQLMAQLGE RANTYLPEAL RESDEW // ID A0A0W7WCB9_9MICO Unreviewed; 524 AA. AC A0A0W7WCB9; DT 16-MAR-2016, integrated into UniProtKB/TrEMBL. DT 16-MAR-2016, sequence version 1. DT 05-JUL-2017, entry version 12. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=AUL38_05585 {ECO:0000313|EMBL:KUF08304.1}; OS Leucobacter sp. G161. OC Bacteria; Actinobacteria; Micrococcales; Microbacteriaceae; OC Leucobacter. OX NCBI_TaxID=663704 {ECO:0000313|EMBL:KUF08304.1, ECO:0000313|Proteomes:UP000053012}; RN [1] {ECO:0000313|EMBL:KUF08304.1, ECO:0000313|Proteomes:UP000053012} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=G161 {ECO:0000313|EMBL:KUF08304.1, RC ECO:0000313|Proteomes:UP000053012}; RA Ge S., Dong X.; RT "High quality draft genome sequence of Leucobacter sp. G161, a RT distinct and effective chromium reducer."; RL Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KUF08304.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LOHP01000017; KUF08304.1; -; Genomic_DNA. DR EnsemblBacteria; KUF08304; KUF08304; AUL38_05585. DR Proteomes; UP000053012; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000053012}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000053012}. FT DOMAIN 306 471 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 113 140 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 524 AA; 56980 MW; AD7B8FB30B100D9F CRC64; MTGDAAVSKT PAPDTATESA DTTNDPLERV LRRASGVGAS VIRDLSEAQA LGSSTHDELD ADDHGIQMDR EDRASLTRVA GLSTELEDVT DVEYRQLRLE NVVLIGIYSS SRTQSAQDAL EEAENSLREL AALAETAGAT VLDGVLQRRA NPDPATYLGK GKAQELAELV QALGADTVIA DDELGPSQRR VLEDVVNAKV IDRTTVILDI FSQHAKSREG KAQVELAQLE YLLPRLRGWG ESMSRQAGGQ VGAAGAGMGS RGPGETKIEL DRRRINTRMA RLRKQIAEFA PAREAKRANR KRGEVPSVAI AGYTNAGKSS LLNRLTGTQE LVQNQLFATL DTAVRHAETT DGRTFTYVDT VGFVRNLPHQ LVEAFRSTFE EVGDADVILH VVDGSHPDPE AQLATVREVI AEVDAQAIPE VVVFNKADLI DDSRRMLLHG LAPDGVFVSA RTGEGIEELK ARIDAALPTP DREVTVVVPY DRGDLVAELH ERNRILELDY VEEGTRVRAL VTPEMFSKLD DFLV // ID A0A0W7WP99_9RHOB Unreviewed; 418 AA. AC A0A0W7WP99; DT 16-MAR-2016, integrated into UniProtKB/TrEMBL. DT 16-MAR-2016, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=AVJ23_01005 {ECO:0000313|EMBL:KUF12340.1}; OS Ponticoccus sp. SJ5A-1. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae; Ponticoccus. OX NCBI_TaxID=1685382 {ECO:0000313|EMBL:KUF12340.1, ECO:0000313|Proteomes:UP000054396}; RN [1] {ECO:0000313|EMBL:KUF12340.1, ECO:0000313|Proteomes:UP000054396} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SJ5A-1 {ECO:0000313|EMBL:KUF12340.1, RC ECO:0000313|Proteomes:UP000054396}; RA Shamseldin A., Moawad H., Abd El-Rahim W.M., Sadowsky M.J.; RL Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KUF12340.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LPXO01000001; KUF12340.1; -; Genomic_DNA. DR RefSeq; WP_058860287.1; NZ_LPXO01000001.1. DR EnsemblBacteria; KUF12340; KUF12340; AVJ23_01005. DR Proteomes; UP000054396; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000054396}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000054396}. FT DOMAIN 197 366 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 418 AA; 46658 MW; 55D1F39FD9F36355 CRC64; MTRAWVLHPD IKSDPDRRDA PMALDEAVSL AHALPDLEVV GHEVVPLPRP QPGMLFGSGK IAELAERLKA AEVELVLVDG PVTPVQQRNL EKEWKVKLLD RTGLILEIFS DRAATREGVL QVEMAHLSYQ RTRLVRAWTH LERQRGGLGF VGGPGETQIE ADRRAIDEQL VRLRRQLDKV VRTRDLHRKA RAKVPYPIVA LVGYTNAGKS TLFNRLTGAE VMAKDMLFAT LDPTMRKVTL PTGADVILSD TVGFISDLPT ELVAAFRATL EEVLAADVVV HVRDISHPET DEQAADVRAI LESLGVAEET AQIELWNKID LLDADEAEAL RLRATREDGV FVVSALTGQG LDEMLQAVTR ALGEERRREE LVLGYDEGRK RAWLFERGLV EGEQQGEDGF RLQLNWSARD RARFASMD // ID A0A0W7WRC0_9ACTN Unreviewed; 496 AA. AC A0A0W7WRC0; DT 16-MAR-2016, integrated into UniProtKB/TrEMBL. DT 16-MAR-2016, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=AT728_34145 {ECO:0000313|EMBL:KUF13147.1}; OS Streptomyces silvensis. OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae; OC Streptomyces. OX NCBI_TaxID=1765722 {ECO:0000313|EMBL:KUF13147.1, ECO:0000313|Proteomes:UP000054804}; RN [1] {ECO:0000313|EMBL:KUF13147.1, ECO:0000313|Proteomes:UP000054804} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 53525 {ECO:0000313|EMBL:KUF13147.1, RC ECO:0000313|Proteomes:UP000054804}; RA Johnston C.W., Li Y., Magarvey N.A.; RT "Draft genome sequence of Streptomyces silvensis ATCC 53525, a RT producer of novel hormone antagonists."; RL Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KUF13147.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LOCL01000082; KUF13147.1; -; Genomic_DNA. DR RefSeq; WP_058852620.1; NZ_LOCL01000082.1. DR EnsemblBacteria; KUF13147; KUF13147; AT728_34145. DR Proteomes; UP000054804; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 2. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000313|EMBL:KUF13147.1}; KW Complete proteome {ECO:0000313|Proteomes:UP000054804}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900, KW ECO:0000313|EMBL:KUF13147.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000054804}. FT DOMAIN 275 440 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 496 AA; 53888 MW; 93C7EF1637FE4DE6 CRC64; MTSSSSPSQD AQSFAQNYPE GLRADALMEE DVAWSHEIDG ARDGDQLDRS ERAALRRVAG LSTELEDVTE VEYRQLRLER VVLVGVWTSG TVDDAENSLA ELAALAETAG AHVLDGVIQR RDKPDPATYI GSGKALELRD IVLETGADTV VCDGELSPGQ LIHLEDVVKV KVVDRTALIL DIFAQHAKSR EGKAQVALAQ MQYMLPRLRG WGQSLSRQMG GGGGGGMATR GPGETKIETD RRRIREKMAK MRREIAEMKT GREIKRQERK RNKVPSVAIA GYTNAGKSSL LNRLTGAGVL VENALFATLD PTVRRAETPS GRLYTLADTV GFVRHLPHHL VEAFRSTMEE VGESDLILHV VDGSHPAPEE QLAAVREVIR DVGATDVPEI VVINKADAAD PLVVQRLLRT QKHAIVVSAR TGAGIEELLA LIDAELPRPE VEIEALVPYT HGKLVSRAHA DGEVLSEEHT AEGTLLKARV HEELAAELAP FVPAAH // ID A0A0W7Z353_9BURK Unreviewed; 399 AA. AC A0A0W7Z353; DT 16-MAR-2016, integrated into UniProtKB/TrEMBL. DT 16-MAR-2016, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=AS359_07300 {ECO:0000313|EMBL:KUF41752.1}; OS Acidovorax sp. 12322-1. OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Comamonadaceae; Acidovorax. OX NCBI_TaxID=1705602 {ECO:0000313|EMBL:KUF41752.1, ECO:0000313|Proteomes:UP000053300}; RN [1] {ECO:0000313|EMBL:KUF41752.1, ECO:0000313|Proteomes:UP000053300} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=12322-1 {ECO:0000313|EMBL:KUF41752.1, RC ECO:0000313|Proteomes:UP000053300}; RA Ming D., Wang M., Hu S., Zhou Y., Jiang T.; RT "Complete genome sequence of a multi-drug resistant strain Acidovorax RT sp. 12322-1."; RL Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KUF41752.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LPXH01000019; KUF41752.1; -; Genomic_DNA. DR RefSeq; WP_054066408.1; NZ_LPXH01000019.1. DR EnsemblBacteria; KUF41752; KUF41752; AS359_07300. DR Proteomes; UP000053300; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000053300}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000053300}. FT DOMAIN 202 375 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 168 195 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 399 AA; 44139 MW; BFE3336B70505CF0 CRC64; MSASSSSSPD ATPVVLVGVD FGLPHFDAEL EELGLLAQTA GLDPVARITC KRKTPDAALF VGSGKAEEIR MLAQMHGAQE VLFDQALSPA QQRNLEKYMQ MPVNDRTLLI LEIFAQRARS HEGKLQVELA RLQYISTRLV RRWTHLERQM GGIGGRGGPG EKQIELDRRM IAEAIKRTKD KLQKVKKQRQ TQRRQRERRD VFNISLVGYT NAGKSTLFNA LVKARAYAAD QLFATLDTTT RQLYLTEAQR SVSLSDTVGF IRDLPHGLVE AFQATLQEAV DADLLLHVVD ASNETFPEQM DQVRKVLGEI GALDIPQILV FNKLDALPDG RKPVQLQDTY DVDGVAVPRV FVSARSGEGL TQLRQMLADA VLSSKGAADA SQEDESLQLP PISPEEDDD // ID A0A0W8EKN6_9BACT Unreviewed; 426 AA. AC A0A0W8EKN6; DT 16-MAR-2016, integrated into UniProtKB/TrEMBL. DT 16-MAR-2016, sequence version 1. DT 05-JUL-2017, entry version 10. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=ASU33_08000 {ECO:0000313|EMBL:KUG08926.1}; OS Solirubrum puertoriconensis. OC Bacteria; Bacteroidetes; Cytophagia; Cytophagales. OX NCBI_TaxID=1751427 {ECO:0000313|EMBL:KUG08926.1, ECO:0000313|Proteomes:UP000054223}; RN [1] {ECO:0000313|EMBL:KUG08926.1, ECO:0000313|Proteomes:UP000054223} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC1A {ECO:0000313|EMBL:KUG08926.1, RC ECO:0000313|Proteomes:UP000054223}; RA Cuebas-Irizarry M.F., Montalvo-Rodriguez R.; RT "Solirubrum puertoriconensis gen. nov. an environmental bacteria RT isolated in Puerto Rico."; RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KUG08926.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LNAL01000006; KUG08926.1; -; Genomic_DNA. DR EnsemblBacteria; KUG08926; KUG08926; ASU33_08000. DR Proteomes; UP000054223; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 2. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000054223}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000054223}. FT DOMAIN 208 405 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 426 AA; 48424 MW; 96D0593F39E408AA CRC64; MLAKGNKTAT YETALEAEKA VLVAVPDKRE DDAIITESLD ELAFLTETAG TVPIKRFVQK LEKPDIRTFV GSGKLEEIKA YVQHAGATTV IFDDDLSPSQ LRNLEKELKV KILDRTLLIL DIFALRAKTA TARTQVELAQ YQYLLPRLTG LWTHLERQRG GVGMRGPGER EIETDRRVVR DRISLLKDQL KDFDKQSQTQ RKSRTGIVRV AFVGYTNVGK STLMNLLSRA DVFAENKLFA TVDSTVRKVV LENVPFLLSD TVGFIRKLPT RLIESFKSTL DEIREADLLL HVVDISHPMF EEHIQVVNDT LKDIGAADKR TILVFNKIDQ YSTDVDIAQH LHDVEPDHDE DVVSREEHQH RPSLEQLKSS YMARLHDPVI FVSAQERVNI DELREMVARH VRTLYEQQYP GHAPFADLSA YTAEAE // ID A0A0W8I5V9_9MICO Unreviewed; 516 AA. AC A0A0W8I5V9; DT 16-MAR-2016, integrated into UniProtKB/TrEMBL. DT 16-MAR-2016, sequence version 1. DT 30-AUG-2017, entry version 13. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=AVL62_02405 {ECO:0000313|EMBL:KUG53648.1}; OS Serinicoccus chungangensis. OC Bacteria; Actinobacteria; Micrococcales; Intrasporangiaceae; OC Serinicoccus. OX NCBI_TaxID=767452 {ECO:0000313|EMBL:KUG53648.1, ECO:0000313|Proteomes:UP000054837}; RN [1] {ECO:0000313|EMBL:KUG53648.1, ECO:0000313|Proteomes:UP000054837} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CD08_5 {ECO:0000313|EMBL:KUG53648.1, RC ECO:0000313|Proteomes:UP000054837}; RA Chander A.M., Kaur G., Nair G.R., Dhawan D.K., Kochhar R.K., RA Mayilraj S., Bhadada S.K.; RT "Serinicoccus chungangenesis strain CD08_5 genome sequencing and RT assembly."; RL Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KUG53648.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LQBL01000028; KUG53648.1; -; Genomic_DNA. DR RefSeq; WP_058891657.1; NZ_LQBL01000028.1. DR EnsemblBacteria; KUG53648; KUG53648; AVL62_02405. DR Proteomes; UP000054837; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 2. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000054837}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000054837}. FT DOMAIN 295 463 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 516 AA; 56219 MW; D8524FABBC4A1915 CRC64; MTAPRTDPTG TDGGRLLDRR AEALIDDDAI DLHEGDWGSW GQTPEGTDPG VHGDLDRDGD QLDREERAAL RRVAGLSTEL EDVTEVEYRQ LRLERVVLAS VWEDNGQTTL EDAENSLREL AALAETAGST VLDGVIQRRQ KPDPATYLGS GKAAQLREIV AAEGADTVVC DGELGPSQRR ALEDVVKVKV IDRTALILDI FAQHAKSKEG RAQVELAQLQ YLLPRLRGWG ESMSRQAGGR VAGGEGIGSR GPGETKIELD RRRINTRIAR LRREITAMKT VRDTKRSSRR SHRVPSVAIV GYTNAGKSSL LNRLTGAGVL VQNQLFATLD PTVRRTESEE GRTYTLSDTV GFVKRLPHQL VEAFRSTLEE AADADVLLHV VDGSHPDPEG QVDAVHAVLA EIDEGSALKI PEIVAVNKAD LADPEVLDRL RRAYPRVVVV SAKTGAGVPE LLEAVEAALP RPEILVDVLL PYDRGDLVAR LYDEGEILAE EHTAEGTRVE AKVDPDLHGH LSDYAV // ID A0A0W8JA78_9VIBR Unreviewed; 429 AA. AC A0A0W8JA78; DT 16-MAR-2016, integrated into UniProtKB/TrEMBL. DT 16-MAR-2016, sequence version 1. DT 30-AUG-2017, entry version 12. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=VRK_37870 {ECO:0000313|EMBL:KUI97125.1}; OS Vibrio sp. MEBiC08052. OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; OC Vibrionaceae; Vibrio. OX NCBI_TaxID=1761910 {ECO:0000313|EMBL:KUI97125.1, ECO:0000313|Proteomes:UP000054473}; RN [1] {ECO:0000313|EMBL:KUI97125.1, ECO:0000313|Proteomes:UP000054473} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MEBiC08052 {ECO:0000313|EMBL:KUI97125.1, RC ECO:0000313|Proteomes:UP000054473}; RA Kim Y.J., Lee J.-H., Kwon K.K.; RT "Genome sequence of Vibrio sp. MEBiC08052."; RL Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KUI97125.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LQIY01000035; KUI97125.1; -; Genomic_DNA. DR RefSeq; WP_059122866.1; NZ_KQ947476.1. DR EnsemblBacteria; KUI97125; KUI97125; VRK_37870. DR PATRIC; fig|1761910.3.peg.3843; -. DR Proteomes; UP000054473; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000054473}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000054473}. FT DOMAIN 198 365 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 429 AA; 48751 MW; 701A51539B262C6C CRC64; MFDRYEAGER AVLVHINFTQ EGEWEDLSEC EMLVSSAGVT TLQVITGSRQ APHPKYYVGE GKAQEIAQAV MQTEAEVVIF NHALSPAQER NLEQLCQCRV IDRTGLILDI FAQRARTHEG KLQVELAQLR HLSTRLVRGW THLERQKGGI GLRGPGETQL ETDRRLLRER IKAILRRLEK VAKQREQGRR ARNRAEVPTI SLVGYTNAGK STLFNCITEA GVYAADQLFA TLDPTLRRIQ LEDVGNAILA DTVGFIRHLP HDLVAAFKAT LQETQEADIL LHVVDASDER FRDNIRAVDD VLAEIEADEV PVLLVMNKID NMESQQPRIE RDDEGVPRIV WVSAMEGLGI DLLFQALTER LAGQIVQYQL CIPPEHQGRM RSFFFKNRSI LQESYDQQGN LLISIRMQQA DWSRLEKREH AVLCDFIVT // ID A0A0X1T5K1_PSEAA Unreviewed; 436 AA. AC A0A0X1T5K1; DT 13-APR-2016, integrated into UniProtKB/TrEMBL. DT 13-APR-2016, sequence version 1. DT 30-AUG-2017, entry version 12. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=AWM79_19620 {ECO:0000313|EMBL:AMB87384.1}; OS Pseudomonas agarici. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=46677 {ECO:0000313|EMBL:AMB87384.1, ECO:0000313|Proteomes:UP000063229}; RN [1] {ECO:0000313|EMBL:AMB87384.1, ECO:0000313|Proteomes:UP000063229} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NCPPB 2472 {ECO:0000313|EMBL:AMB87384.1, RC ECO:0000313|Proteomes:UP000063229}; RA McClelland M., Jain A., Saraogi P., Mendelson R., Westerman R., RA SanMiguel P., Csonka L.; RL Submitted (JAN-2016) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP014135; AMB87384.1; -; Genomic_DNA. DR RefSeq; WP_017133327.1; NZ_FOAR01000009.1. DR EnsemblBacteria; AMB87384; AMB87384; AWM79_19620. DR Proteomes; UP000063229; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000063229}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000063229}. FT DOMAIN 199 366 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 436 AA; 49333 MW; 3ACA167E3DCA5445 CRC64; MFFERHGGGE RTVLVHLEGQ DPEAREDPQE FQELALSAGA ETVAFFNVPR HRPTAKYLIG TGKVEELRDL VKAEQVDIVI FNHILTPSQE RNLERAFECR VLDRTGLILD IFAQRARTHE GKLQVELAQL EHMSTRLVRG WTHLERQKGG IGLRGPGETQ LETDRRLLRV RLRQIKSRLE KVRSQREQSR RGRKRADIPT VSLVGYTNAG KSTLFNAVTE SDVYAADQLF ATLDPTLRRL DLEDLGPVVL ADTVGFIRHL PHKLVEAFRA TLEESSNSDL LLHVIDAAEP DRMLQIEQVM VVLGEIGAQD LPILEVYNKL DLLEGVEPQI QRAEDGKPQR VWLSARDGIG LELLEQAIAE LLGSDLFVGT LHLPQRFARL RAQFFELGAV QKEEHDEEGA CLLSVRLPRA ELNRMVSRAG MTPAEFIEQH TLQYKA // ID A0A0X1TKP3_9FIRM Unreviewed; 421 AA. AC A0A0X1TKP3; DT 13-APR-2016, integrated into UniProtKB/TrEMBL. DT 13-APR-2016, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=AT726_06490 {ECO:0000313|EMBL:AMC08584.1}; OS Turicibacter sp. H121. OC Bacteria; Firmicutes; Erysipelotrichia; Erysipelotrichales; OC Erysipelotrichaceae; Turicibacter. OX NCBI_TaxID=1712675 {ECO:0000313|EMBL:AMC08584.1, ECO:0000313|Proteomes:UP000057144}; RN [1] {ECO:0000313|Proteomes:UP000057144} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=H121 {ECO:0000313|Proteomes:UP000057144}; RA Shamseldin A., Moawad H., Abd El-Rahim W.M., Sadowsky M.J.; RL Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP013476; AMC08584.1; -; Genomic_DNA. DR RefSeq; WP_055275505.1; NZ_CP013476.1. DR EnsemblBacteria; AMC08584; AMC08584; AT726_06490. DR KEGG; tur:AT726_06490; -. DR KO; K03665; -. DR Proteomes; UP000057144; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000057144}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000057144}. FT DOMAIN 196 364 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 155 182 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 421 AA; 47441 MW; C3AAF04A380A6E4B CRC64; MEEIIQRAIL VGVDLNNDKN FDYSVEELKN LAEACSVQVV GVLTQKLERV NPACYIGTGK VDEVALLVEQ NDANLVIFND ELSPSQIRNL EHGLQCKVID RTILILDIFA SRAKTREAQL QVEVAQLKYM MPRLIGLNAS LSRQAGGIGS KGPGEKKLEL DRRRIEEQVH KLNKELDSLV LARQNQRKLR KRNSTPVVAL VGYTNAGKST TMNALLTVSN AQSEKSVFEK NMLFATLETS TRHIQLPDNK QFLLTDTVGF VSKLPHQLVK AFRSTLEEVT EADLLLHVVD LSHPEFQTQI EITNKVLDEL GVKETPMVYV YNKADLVEDE FTPSTKEAVR ISAKNLTNID TLIDCIKSHI FQHYVKASFL IPYDRGNLVS YLNEHANVFD TEYLENGTLI TVECSEHDAH RLAEYKVKPL N // ID A0A0X3RX61_9ACTN Unreviewed; 496 AA. AC A0A0X3RX61; DT 13-APR-2016, integrated into UniProtKB/TrEMBL. DT 13-APR-2016, sequence version 1. DT 07-JUN-2017, entry version 10. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=ADL25_35830 {ECO:0000313|EMBL:KUJ35596.1}; OS Streptomyces sp. NRRL F-5122. OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae; OC Streptomyces. OX NCBI_TaxID=1609098 {ECO:0000313|EMBL:KUJ35596.1, ECO:0000313|Proteomes:UP000054048}; RN [1] {ECO:0000313|EMBL:KUJ35596.1, ECO:0000313|Proteomes:UP000054048} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NRRL F-5122 {ECO:0000313|EMBL:KUJ35596.1, RC ECO:0000313|Proteomes:UP000054048}; RA Millard Andrew; RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KUJ35596.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LMWH01000266; KUJ35596.1; -; Genomic_DNA. DR RefSeq; WP_059132085.1; NZ_LMWH01000266.1. DR EnsemblBacteria; KUJ35596; KUJ35596; ADL25_35830. DR Proteomes; UP000054048; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 2. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000313|EMBL:KUJ35596.1}; KW Complete proteome {ECO:0000313|Proteomes:UP000054048}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900, KW ECO:0000313|EMBL:KUJ35596.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000054048}. FT DOMAIN 274 439 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 496 AA; 54255 MW; 4DAE2BE0E5B335AF CRC64; MTSSSSSSQD TKRIAHTYPE GLRADALMEE DVAWSHEIDG ERDGDQFDRS ERAALRRVAG LSTELEDVTE VEYRQLRLER VVLVGVWTSG TVQDAENSLA ELAALAETAG AIVLDGVIQR RDKPDAATYI GSGKALELRD IVIETGADTV ICDGELSPGQ LIHLEDVVKV KVIDRTALIL DIFAQHAKSR EGKAQVALAQ MQYMLPRLRG WGQSLSRQMG GGSGGLATRG PGETKIETDR RRIREKMAKM RREIAEMKTG REIKRQERRR HKVPSVAIAG YTNAGKSSLL NRLTGAGVLV ENALFATLDP TVRRAETPSG RLYTLADTVG FVRHLPHHLV EAFRSTMEEV GDSDLILHVV DGSHPVPEEQ LAAVREVIRD VGATDVPEIV VINKADAADP LVLQRLLRTE KRALAVSART GKGIQELLAL LDNELPRPSV EIEALVPYTH GRLVARAHSE GDVISEEHTP EGTLLKARVH EELAAELAPY APAPAF // ID A0A0X3SYG7_9ACTN Unreviewed; 496 AA. AC A0A0X3SYG7; DT 13-APR-2016, integrated into UniProtKB/TrEMBL. DT 13-APR-2016, sequence version 1. DT 07-JUN-2017, entry version 9. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=ACZ90_17075 {ECO:0000313|EMBL:KUJ68597.1}; OS Streptomyces albus subsp. albus. OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae; OC Streptomyces. OX NCBI_TaxID=67257 {ECO:0000313|EMBL:KUJ68597.1, ECO:0000313|Proteomes:UP000054175}; RN [1] {ECO:0000313|EMBL:KUJ68597.1, ECO:0000313|Proteomes:UP000054175} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NRRL B-2513 {ECO:0000313|EMBL:KUJ68597.1, RC ECO:0000313|Proteomes:UP000054175}; RA Millard Andrew; RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KUJ68597.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LMWG01001113; KUJ68597.1; -; Genomic_DNA. DR EnsemblBacteria; KUJ68597; KUJ68597; ACZ90_17075. DR Proteomes; UP000054175; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 2. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000313|EMBL:KUJ68597.1}; KW Complete proteome {ECO:0000313|Proteomes:UP000054175}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900, KW ECO:0000313|EMBL:KUJ68597.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000054175}. FT DOMAIN 275 440 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 496 AA; 54194 MW; DB73496617B15F09 CRC64; MTYSSSLPQE RQRLADSLRA DALMEEDVAW SQEIDEERDG DQYDRSERAA LRRVAGLSTE LEDVTEVEYR QLRLERVVLV GVWTSGTIQD AENSLAELAA LAETAGALVL DGVTQRRDKP DPATYIGSGK AQELRDIVLE SGADTVVCDG ELSPGQLIHL EDVVKVKVVD RTALILDIFA QHAKSREGKA QVSLAQMQYM LPRLRGWGQS LSRQMGGGGS GSSGGGMATR GPGETKIETD RRRIREKMAK MRREIAEMKT GREIKRQERR RNKVPSVAIA GYTNAGKSSL LNRLTGAGVL VENALFATLD PTVRRAETPS GRVYTLADTV GFVRHLPHHL VEAFRSTMEE VGDSDLILHV VDGAHPVPEE QLAAVREVIR EVGAVDVPEI VVINKADAAD PLVLQRLLRV EKHSIAVSAR SGQGIEELLA LIDQELPRPE VEVSALVPYT HGKLVARAHA EGEVLSEEHT GEGTLLKARV HQELAAELQP FVPASA // ID A0A0X3TCU8_9GAMM Unreviewed; 433 AA. AC A0A0X3TCU8; DT 13-APR-2016, integrated into UniProtKB/TrEMBL. DT 13-APR-2016, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=AVO41_06945 {ECO:0000313|EMBL:KUJ72156.1}; OS Thiomicrospira sp. WB1. OC Bacteria; Proteobacteria; Gammaproteobacteria; Thiotrichales; OC Piscirickettsiaceae; Thiomicrospira. OX NCBI_TaxID=1685380 {ECO:0000313|EMBL:KUJ72156.1, ECO:0000313|Proteomes:UP000053531}; RN [1] {ECO:0000313|EMBL:KUJ72156.1, ECO:0000313|Proteomes:UP000053531} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=WB1 {ECO:0000313|EMBL:KUJ72156.1, RC ECO:0000313|Proteomes:UP000053531}; RA Shamseldin A., Moawad H., Abd El-Rahim W.M., Sadowsky M.J.; RL Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KUJ72156.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LQBN01000002; KUJ72156.1; -; Genomic_DNA. DR RefSeq; WP_068584660.1; NZ_LQBN01000002.1. DR EnsemblBacteria; KUJ72156; KUJ72156; AVO41_06945. DR Proteomes; UP000053531; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000053531}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000053531}. FT DOMAIN 201 370 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 160 194 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 433 AA; 48428 MW; 72E0363799D4FFA6 CRC64; MELFGKLERQ QLDRAVLVHV DFYHESDREE LDELYELVDS AGADVQTLIT AKRDKPDPKY FVGKGKVDEI QSAIASTEAD VVIVNHALSP AQERNLSDQL KIQVLDRVGL ILDIFAQRAR SHEGKLQVEL AQLKRMATRL VKGWTHLDRQ GGIGARGPGE TQLETDRRLV QGKIKQLEAR IEKVRKQRQL GRQSRKKSDL PTVAIVGYTN AGKSTLFNWL TQAHVYAEDR LFATLDSTLR KVHLPGAGPV IFADTVGFIR HIPHDLVAAF RSTLEETSEA DLLIHLVDVA DPHRAEKMAD VAEVIEEVGA ADVPQLVVFN KIDRLEPPAN EPKVRHGEDG LPCEIWISAA KESGLSLLSD AIGAHFHGRY QTVSLTLDVT AGKRRSELYQ LGTILEESFD EAGHSCFRMH VTDQESRQIQ QWPEILAYQV VSS // ID A0A0X3U5C7_9RHOB Unreviewed; 423 AA. AC A0A0X3U5C7; DT 13-APR-2016, integrated into UniProtKB/TrEMBL. DT 13-APR-2016, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=AVO44_01475 {ECO:0000313|EMBL:KUJ81976.1}; OS Ruegeria sp. ZGT108. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae; Ruegeria. OX NCBI_TaxID=1685378 {ECO:0000313|EMBL:KUJ81976.1, ECO:0000313|Proteomes:UP000053690}; RN [1] {ECO:0000313|EMBL:KUJ81976.1, ECO:0000313|Proteomes:UP000053690} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ZGT108 {ECO:0000313|EMBL:KUJ81976.1, RC ECO:0000313|Proteomes:UP000053690}; RA Shamseldin A., Moawad H., Abd El-Rahim W.M., Sadowsky M.J.; RL Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KUJ81976.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LQBP01000001; KUJ81976.1; -; Genomic_DNA. DR RefSeq; WP_068331573.1; NZ_LQBP01000001.1. DR EnsemblBacteria; KUJ81976; KUJ81976; AVO44_01475. DR Proteomes; UP000053690; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000053690}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}. FT DOMAIN 203 372 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 423 AA; 47278 MW; 865A03FC2C205B91 CRC64; MEHDRMHTRA WVLHPEIKSD EQRRVPGPAL EEAVALAAAL PDLDVIGSEI VRLQRAQPGL LFGSGKIEEL AERLHDNKIE LVLIDGPVTP VQQRNLEKAW KVKILDRTGL ILEIFSDRAR TREGVLQVEM AALSYQRTRL VRAWTHLERQ RGGLGFVGGP GETQIEADRR AIDEQLVRLR RQLQKVVKTR TLHRAARAKV PYPIVALVGY TNAGKSTLFN RLTGAKVMAK DMLFATLDPT MRRVELPDGP EVILSDTVGF ISNLPTELVA AFRATLEEVL GADIIIHVRD ISHEDTEAQA QDVEAILTSL GVDDERPRLD VWNKIDLLND EEREAALKRA DRDPAIFAIS AVTGEGVEPL LAEIAAKLQG ARHEEVLSLD FAEGNKRAWL FRQDVVRSEK QTDDGFQITV LWTDKQAAQF AGL // ID A0A0X3UBD4_9GAMM Unreviewed; 437 AA. AC A0A0X3UBD4; DT 13-APR-2016, integrated into UniProtKB/TrEMBL. DT 13-APR-2016, sequence version 1. DT 30-AUG-2017, entry version 12. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=AVO43_09930 {ECO:0000313|EMBL:KUJ82870.1}; OS Microbulbifer sp. ZGT114. OC Bacteria; Proteobacteria; Gammaproteobacteria; Cellvibrionales; OC Microbulbiferaceae; Microbulbifer. OX NCBI_TaxID=1685377 {ECO:0000313|EMBL:KUJ82870.1, ECO:0000313|Proteomes:UP000054457}; RN [1] {ECO:0000313|EMBL:KUJ82870.1, ECO:0000313|Proteomes:UP000054457} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ZGT114 {ECO:0000313|EMBL:KUJ82870.1, RC ECO:0000313|Proteomes:UP000054457}; RA Shamseldin A., Moawad H., Abd El-Rahim W.M., Sadowsky M.J.; RL Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KUJ82870.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LQBR01000003; KUJ82870.1; -; Genomic_DNA. DR RefSeq; WP_067084340.1; NZ_LQBR01000003.1. DR EnsemblBacteria; KUJ82870; KUJ82870; AVO43_09930. DR Proteomes; UP000054457; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000054457}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000054457}. FT DOMAIN 199 366 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 158 192 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 437 AA; 48772 MW; 9B3B0510CAC45CC8 CRC64; MFFERPKSGE LAVLVHLDLS AIDSPEDPRE FEELALSAGA DPVTFIFGQR ATPDPKTFVG RGKLEEIQAA VREHDAQLVI FDHILSPSQE RNIERELKCR VLDRTGLILD IFAQRARTHE GKLQVELAQL RHMSTRLVRG WTHLERQKGG IGLRGPGETQ LETDRRLLRA RIDSIEKRLE KVRRQREQGR RARSRAEVAT VSLVGYTNAG KSTLFNRLTD AGVYVKDQLF ATLDPTMRRV ELPNVGAMIL ADTVGFVSHL PHRLVEAFRA TLEEASNASL LLHVVDAAAE DRLTLMEEVQ EVLTEIGAGE LPQLLVYNKI DLLQDREPGI DRDEHGMPRA VWLSAVTGEG CDLLVEAIAE RLGEEMVSGH LVVAPEQGRL RAQLHEINAV RDERYLDDGA CELALTLPRG DLERLLAPYK ESATSPLWQP DSAADAG // ID A0A0X3UUM2_9ACTN Unreviewed; 468 AA. AC A0A0X3UUM2; DT 13-APR-2016, integrated into UniProtKB/TrEMBL. DT 13-APR-2016, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=ADL15_13715 {ECO:0000313|EMBL:KUL35817.1}; OS Actinoplanes awajinensis subsp. mycoplanecinus. OC Bacteria; Actinobacteria; Micromonosporales; Micromonosporaceae; OC Actinoplanes. OX NCBI_TaxID=135947 {ECO:0000313|EMBL:KUL35817.1, ECO:0000313|Proteomes:UP000053244}; RN [1] {ECO:0000313|EMBL:KUL35817.1, ECO:0000313|Proteomes:UP000053244} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NRRL B-16712 {ECO:0000313|EMBL:KUL35817.1, RC ECO:0000313|Proteomes:UP000053244}; RA Millard Andrew; RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KUL35817.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LLZH01000097; KUL35817.1; -; Genomic_DNA. DR RefSeq; WP_067689384.1; NZ_LLZH01000097.1. DR EnsemblBacteria; KUL35817; KUL35817; ADL15_13715. DR Proteomes; UP000053244; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 2. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000313|EMBL:KUL35817.1}; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000053244}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900, KW ECO:0000313|EMBL:KUL35817.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000053244}. FT DOMAIN 250 415 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 209 236 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 468 AA; 50979 MW; F424D6AB5A8279D1 CRC64; MRNTYQAPVL DEPDLTSGDL ELAERHSLRR VAGLSTELTD VTEVEYRQLR LERVVLVGVW TGGSVEDADN SLAELAALAE TAGSQVLEGL IQRRSQPDAA TFIGRGKVDE LRDVVVATGA DTVICDGELS PSQLRKLEQQ IKVKVVDRTA LILDIFAQHA KSKEGKAQVE LAQLQYLLPR LRGWGDSLSR QGGGSGGSGG GVGTRGPGET KLETDRRRIN TRISRLRREI KAMRTMRDTK RSRRSASGVP GVAIAGYTNA GKSSLLNRLT QAGVLVEDAL FATLDPTTRR AAAEDGRVYT LSDTVGFVRH LPHHIVEAFR STLEEVAMAD LVVHVVDGAH PDPEGQVSAV REVLGEVGAD KISELLVINK MDAADEETVL RLKRAWPDAV FVSARSGAGI PELQAAIAER LPRPAVDLRI LLPYDRGDLV ARVHRTGQVL QSRHLDDGTE LQVRVDERLA AELESYRC // ID A0A0X3VLU9_9ACTN Unreviewed; 497 AA. AC A0A0X3VLU9; DT 13-APR-2016, integrated into UniProtKB/TrEMBL. DT 13-APR-2016, sequence version 1. DT 30-AUG-2017, entry version 16. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=ADL12_03410 {ECO:0000313|EMBL:KUL45590.1}; OS Streptomyces regalis. OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae; OC Streptomyces. OX NCBI_TaxID=68262 {ECO:0000313|EMBL:KUL45590.1, ECO:0000313|Proteomes:UP000053923}; RN [1] {ECO:0000313|EMBL:KUL45590.1, ECO:0000313|Proteomes:UP000053923} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NRRL 3151 {ECO:0000313|EMBL:KUL45590.1, RC ECO:0000313|Proteomes:UP000053923}; RA Millard Andrew; RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KUL45590.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LLZG01000012; KUL45590.1; -; Genomic_DNA. DR RefSeq; WP_062698306.1; NZ_LLZG01000012.1. DR EnsemblBacteria; KUL45590; KUL45590; ADL12_03410. DR Proteomes; UP000053923; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 2. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000313|EMBL:KUL45590.1}; KW Complete proteome {ECO:0000313|Proteomes:UP000053923}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900, KW ECO:0000313|EMBL:KUL45590.1}. FT DOMAIN 275 440 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 497 AA; 54400 MW; 1DA978543A86349A CRC64; MTSSSSFSQD TQRFAHTHPE GLRADALMEE DVAWSHEIDG ERDGDQFDRS ERAALRRVAG LSTELEDVTE VEYRQLRLER VVLVGVWTTG SAQDAENSLA ELAALAETAG ALVLDGVIQR RDKPDAATYI GSGKADELRD IVLETGADTV ICDGELSPGQ LIHLEDVVKV KVIDRTALIL DIFAQHAKSR EGKAQVALAQ MQYMLPRLRG WGQSLSRQMG GGKGGGLATR GPGETKIETD RRRIREKMAK MRREIAEMKT GRDIQRQVRR RNKVPSVAIA GYTNAGKSSL LNRLTGAGVL VENALFATLD PTVRRAETPG GRHYTLADTV GFVRHLPHHL VEAFRSTMEE VGDSDLILHV VDGSHPNPEE QLAAVREVIR DVGATDVPEI VVINKADAAD PLTLQRLMRI EKRSIAVSAR TGRGIDELLA LIDNELPRPS VEIEALVPYT HGKLVARAHT EGEVISEEHT PEGTLLKVRV HEELAADLTP YVPAATA // ID A0A0X3W635_9ACTN Unreviewed; 495 AA. AC A0A0X3W635; DT 13-APR-2016, integrated into UniProtKB/TrEMBL. DT 13-APR-2016, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=ADL22_05340 {ECO:0000313|EMBL:KUL52361.1}; OS Streptomyces sp. NRRL F-4489. OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae; OC Streptomyces. OX NCBI_TaxID=1609095 {ECO:0000313|EMBL:KUL52361.1, ECO:0000313|Proteomes:UP000053256}; RN [1] {ECO:0000313|EMBL:KUL52361.1, ECO:0000313|Proteomes:UP000053256} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NRRL F-4489 {ECO:0000313|EMBL:KUL52361.1, RC ECO:0000313|Proteomes:UP000053256}; RA Millard Andrew; RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KUL52361.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LLZI01000035; KUL52361.1; -; Genomic_DNA. DR RefSeq; WP_066974239.1; NZ_LLZI01000035.1. DR EnsemblBacteria; KUL52361; KUL52361; ADL22_05340. DR Proteomes; UP000053256; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 2. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000313|EMBL:KUL52361.1}; KW Complete proteome {ECO:0000313|Proteomes:UP000053256}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900, KW ECO:0000313|EMBL:KUL52361.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000053256}. FT DOMAIN 275 440 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 495 AA; 54110 MW; C4E33ADAD362CDCE CRC64; MTSSSSLPQD RQRLAESLRA DALMEEDVAW SHEIDGERDG DQYDRSDRAA LRRVAGLSTE LEDVTEVEYR QLRLERVVLV GVWTSGTVQD AENSLAELAA LAETAGALVL DGVIQRREKP DPATYIGSGK ALELRDIVLE SGADTVVCDG ELSPGQLIHL EDVVKVKVVD RTALILDIFA QHAKSREGKA QVSLAQMQYM LPRLRGWGQS LSRQMGGGGS GSAGGGMATR GPGETKIETD RRRIREKMAK MRREIAEMKT GRDVKRQERR RNKIPSVAIA GYTNAGKSSL LNRLTGAGVL VENALFATLD PTVRRAETPS GRLYTLADTV GFVRHLPHHL VEAFRSTMEE VADADLILHV VDGSHPVPEE QLAAVREVIR DVGATDVPEI VVVNKADAAD PLTLQRLLRQ EKRALVVSAR TGEGIAELRE LLDAELPRPR VEIEVLVPYT QGALVSRAHA EGEVLSEEHT AEGTVLKARV HEELAAEFRP FVPAA // ID A0A0X3WJR8_9ACTN Unreviewed; 496 AA. AC A0A0X3WJR8; DT 13-APR-2016, integrated into UniProtKB/TrEMBL. DT 13-APR-2016, sequence version 1. DT 07-JUN-2017, entry version 10. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=ADL30_11990 {ECO:0000313|EMBL:KUL57103.1}; OS Streptomyces sp. NRRL S-1521. OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae; OC Streptomyces. OX NCBI_TaxID=1609100 {ECO:0000313|EMBL:KUL57103.1, ECO:0000313|Proteomes:UP000053420}; RN [1] {ECO:0000313|EMBL:KUL57103.1, ECO:0000313|Proteomes:UP000053420} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NRRL S-1521 {ECO:0000313|EMBL:KUL57103.1, RC ECO:0000313|Proteomes:UP000053420}; RA Millard Andrew; RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KUL57103.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LLZK01000144; KUL57103.1; -; Genomic_DNA. DR RefSeq; WP_062773692.1; NZ_LLZK01000144.1. DR EnsemblBacteria; KUL57103; KUL57103; ADL30_11990. DR Proteomes; UP000053420; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 2. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000313|EMBL:KUL57103.1}; KW Complete proteome {ECO:0000313|Proteomes:UP000053420}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900, KW ECO:0000313|EMBL:KUL57103.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000053420}. FT DOMAIN 275 440 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 496 AA; 54035 MW; 819C43572FCD9C12 CRC64; MTSSSSPSQD VQSFAQNYPE GLRADALMEE DVAWSHEIDG ERDGDQLDRS ERAALRRVAG LSTELEDVTE VEYRQLRLER VVLVGVWTSG TVDDAENSLA ELAALAETAG ALVLDGVVQR RDKPDPATYI GSGKALELRD IVLETGADTV VCDGELSPGQ LIHLEDVVKV KVVDRTALIL DIFAQHAKSR EGKAQVALAQ MQYMLPRLRG WGQSLSRQMG GGGGGGMATR GPGETKIETD RRRIREKMAK MRREIAEMKT GRDIKRQERR RNKVPSVAIA GYTNAGKSSL LNRLTGAGVL VENALFATLD PTVRRAETPG GRLYTLADTV GFVRHLPHHL VEAFRSTMEE VADSDLILHV VDGSHPVPEE QLAAVREVIR DVGATEVPEI VVINKADAAD PLVLQRLLRN EKHAIAVSAR TGAGIDELLA LIDVELPRPE VEIEALVPYT HGQLVSRAHA EGEVLSEEHT GEGTLLKARV HEELAAELNP YVPAAH // ID A0A0X3XWS0_9ACTN Unreviewed; 497 AA. AC A0A0X3XWS0; DT 13-APR-2016, integrated into UniProtKB/TrEMBL. DT 13-APR-2016, sequence version 1. DT 07-JUN-2017, entry version 10. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=ADL34_05900 {ECO:0000313|EMBL:KUL79066.1}; OS Streptomyces sp. NRRL WC-3605. OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae; OC Streptomyces. OX NCBI_TaxID=1609103 {ECO:0000313|EMBL:KUL79066.1, ECO:0000313|Proteomes:UP000052945}; RN [1] {ECO:0000313|EMBL:KUL79066.1, ECO:0000313|Proteomes:UP000052945} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NRRL WC-3605 {ECO:0000313|EMBL:KUL79066.1, RC ECO:0000313|Proteomes:UP000052945}; RA Millard Andrew; RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KUL79066.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LLZN01000035; KUL79066.1; -; Genomic_DNA. DR RefSeq; WP_062673298.1; NZ_LLZN01000035.1. DR EnsemblBacteria; KUL79066; KUL79066; ADL34_05900. DR Proteomes; UP000052945; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000313|EMBL:KUL79066.1}; KW Complete proteome {ECO:0000313|Proteomes:UP000052945}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900, KW ECO:0000313|EMBL:KUL79066.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000052945}. FT DOMAIN 275 440 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 497 AA; 54182 MW; E30BB397E43C7B89 CRC64; MTSSSSFSQD SKRLAHTHPD GLRADALMEE DVAWSHEIDG DRDGDQFDRS DRAALRRVAG LSTELEDVTE VEYRQLRLER VVLVGVWTSG TVQDAENSLA ELAALAETAG ALVLDGVIQR RDKPDAATYI GSGKAQELRD IVLDTGADTV ICDGELSPGQ LIHLEDVVKV KVIDRTALIL DIFAQHAKSR EGKAQVALAQ MQYMLPRLRG WGQSLSRQMG GGKGGGLATR GPGETKIETD RRRIREKMAK MRREIAEMKT GRDIQRQSRR RNKVPSVAIA GYTNAGKSSL LNRLTGAGVL VENALFATLD PTVRRAETPS GRLYTLADTV GFVRHLPHHL VEAFRSTMEE VGDSDLILHV VDGSHPNPEE QLAAVREVIR DVGATGVPEI VVINKADAAD PLTLQRLLRI EKRSIAVSAR TGQGIAELLA LIDNELPRPS VEVEALVPYT HGKLVARAHT EGEVISEEHT PEGTLLKVRV HEELAADLAP YMPTPAG // ID A0A0X3YBZ9_9GAMM Unreviewed; 431 AA. AC A0A0X3YBZ9; DT 13-APR-2016, integrated into UniProtKB/TrEMBL. DT 13-APR-2016, sequence version 1. DT 30-AUG-2017, entry version 12. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=AR688_13570 {ECO:0000313|EMBL:KUM54345.1}; OS Rheinheimera sp. EpRS3. OC Bacteria; Proteobacteria; Gammaproteobacteria; Chromatiales; OC Chromatiaceae; Rheinheimera. OX NCBI_TaxID=1712383 {ECO:0000313|EMBL:KUM54345.1, ECO:0000313|Proteomes:UP000054239}; RN [1] {ECO:0000313|EMBL:KUM54345.1, ECO:0000313|Proteomes:UP000054239} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=RS3 {ECO:0000313|EMBL:KUM54345.1, RC ECO:0000313|Proteomes:UP000054239}; RA Zhang Y., Guo Z.; RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KUM54345.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LNQS01000001; KUM54345.1; -; Genomic_DNA. DR RefSeq; WP_068228491.1; NZ_LNQS01000001.1. DR EnsemblBacteria; KUM54345; KUM54345; AR688_13570. DR Proteomes; UP000054239; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000054239}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}. FT DOMAIN 198 364 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 157 191 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 431 AA; 48377 MW; 4C1354FAA629C5C2 CRC64; MSDISVVPEQ AILVHVNFSQ QHVSEDLTEL KLLVSSAGVQ TVQVVTASRS APDAKFFVGS GKADEIAALV EETGADVVIF NHALSPAQTR NLERLCLTRV IDRTTLILDI FAQRARTFEG KLQVELAQLQ HLASRLVRGW DSLDRQKGGI GLRGPGETQL ETDRRLLRER VKALQTRLAK LTKQREQGRR ARQRSEVPVV SVVGYTNAGK STLFNRITKA DVYAADQLFA TLDPTLRKLK LKGVGEIILA DTVGFIRHLP HDLVAAFKST LQETRDADLQ LHVVDLSDPR KDDNMQQVDL VLQEIDADQL PQLVVYNKID LLQQLPRIEY NEYKQPVAVY LSAVSGAGVD LLAQAVSQLL SERYLDITLL LPPEQMQWRA RFHQQHSIEQ EQFDAEGNCH LQLRLSESVW NRSVKQSHGQ LENYVVSQPV I // ID A0A0X7B8U4_9FLAO Unreviewed; 415 AA. AC A0A0X7B8U4; DT 13-APR-2016, integrated into UniProtKB/TrEMBL. DT 13-APR-2016, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:KVV13571.1}; GN ORFNames=AP058_02936 {ECO:0000313|EMBL:KVV13571.1}; OS Flavobacterium sp. TAB 87. OC Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales; OC Flavobacteriaceae; Flavobacterium. OX NCBI_TaxID=1729581 {ECO:0000313|EMBL:KVV13571.1, ECO:0000313|Proteomes:UP000059935}; RN [1] {ECO:0000313|EMBL:KVV13571.1, ECO:0000313|Proteomes:UP000059935} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=TAB87 {ECO:0000313|EMBL:KVV13571.1, RC ECO:0000313|Proteomes:UP000059935}; RA Millard Andrew; RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KVV13571.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LLWK01000038; KVV13571.1; -; Genomic_DNA. DR RefSeq; WP_066312401.1; NZ_LLWK01000038.1. DR EnsemblBacteria; KVV13571; KVV13571; AP058_02936. DR PATRIC; fig|1729581.3.peg.3032; -. DR Proteomes; UP000059935; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000059935}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000059935}. FT DOMAIN 200 386 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 415 AA; 48087 MW; E0BA65D805E99EDB CRC64; MLEKEILNFE RTAVVGVVTQ SQSEEKLNEY LDELEFLTFT AGGEVIKRFW QKMDKPNPKT FLGTGKIEEI NLFVKENEIS TLIFDDELSP SQQKNISKII DCKILDRTNL ILDIFAQRAE TSYARTQVEL AQCIYLLPRL SGLWTHLERQ KGGIGMRGPG ETEIETDRRI VRDRISLLKE KIKSIDRQMG VQRSNRGAMV RVALVGYTNV GKSTLMNAVG KSDVFVENKL FATLDTTVRK VVIKNLPFLL SDTVGFIRKL PTQLVDSFKS TLDEVREADL LLHIVDISHP DFEDHIASVN QILQDIKAND KPVIMVFNKI DSFKHLTIDE DDLMTERTPR HYTLEEWKST WMSRVGEENA LFISATNKEN FEEFRERVYE AVRHIHITRF PYNKFLYPDY KDAIEKEDKD EEEIE // ID A0A0X8BYT1_9PSED Unreviewed; 433 AA. AC A0A0X8BYT1; DT 13-APR-2016, integrated into UniProtKB/TrEMBL. DT 13-APR-2016, sequence version 1. DT 30-AUG-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=APT63_17825 {ECO:0000313|EMBL:AMA47324.1}; OS Pseudomonas monteilii. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=76759 {ECO:0000313|EMBL:AMA47324.1, ECO:0000313|Proteomes:UP000065993}; RN [1] {ECO:0000313|EMBL:AMA47324.1, ECO:0000313|Proteomes:UP000065993} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=USDA-ARS-USMARC-56711 {ECO:0000313|EMBL:AMA47324.1, RC ECO:0000313|Proteomes:UP000065993}; RA Harhay G.P., Harhay D.M., Smith T.P.L., Bono J.L., Heaton M.P., RA Clawson M.L., Chitko-Mckown C.G., Capik S.F., DeDonder K.D., RA Apley M.D., Lubbers B.V., White B.J., Larson R.L.; RT "Annotation of Achromobacter piechaudii USDA-ARS-USMARC-56711."; RL Submitted (JAN-2016) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP013997; AMA47324.1; -; Genomic_DNA. DR RefSeq; WP_060395121.1; NZ_CP013997.1. DR EnsemblBacteria; AMA47324; AMA47324; APT63_17825. DR Proteomes; UP000065993; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000065993}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}. FT DOMAIN 199 366 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 165 192 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 433 AA; 48816 MW; FBE8CAE77AB72F27 CRC64; MFFERHGGGE RALLVHLEGQ NPEAREDPQE FQELALSAGA DIVALANVAR HQPTAKYLIG SGKVEELRDL VKTQEADLVI FNHTLTPSQE RNLERVFECR VLDRTGLILD IFAQRARTHE GKLQVELAQL EHMSTRLVRG WTHLERQKGG IGLRGPGETQ LETDRRLLRV RLRQIKARLE KVRSQREQAR RGRRRADIPS VSLVGYTNAG KSTLFNALTQ SEVYAADQLF ATLDPTLRRL QLDDLGPIVL ADTVGFIRHL PHKLVEAFRA TLEESSNSDL LLHVIDAHEP ERMEQIEQVL AVLGEIGAEG LPILEVYNKL DLLEDVEPQI QRDPDGKPER VWVSARDGRG LELVGQAIAE LLGDDLFVGT LRLEQQLSRL RAQFFELGAV QSEEHDEEGS SLLAVRLPRV ELNRLVSRAG LEPEAFLEQH TLQ // ID A0A0X8CR00_9BACL Unreviewed; 423 AA. AC A0A0X8CR00; DT 13-APR-2016, integrated into UniProtKB/TrEMBL. DT 13-APR-2016, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:AMA61906.1}; GN ORFNames=ASO14_244 {ECO:0000313|EMBL:AMA61906.1}; OS Kurthia sp. 11kri321. OC Bacteria; Firmicutes; Bacilli; Bacillales; Planococcaceae; Kurthia. OX NCBI_TaxID=1750719 {ECO:0000313|EMBL:AMA61906.1, ECO:0000313|Proteomes:UP000058129}; RN [1] {ECO:0000313|EMBL:AMA61906.1, ECO:0000313|Proteomes:UP000058129} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=11kri321 {ECO:0000313|EMBL:AMA61906.1, RC ECO:0000313|Proteomes:UP000058129}; RA Zhang Y., Guo Z.; RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP013217; AMA61906.1; -; Genomic_DNA. DR RefSeq; WP_068450483.1; NZ_CP013217.1. DR EnsemblBacteria; AMA61906; AMA61906; ASO14_244. DR KEGG; kur:ASO14_244; -. DR PATRIC; fig|1750719.3.peg.236; -. DR KO; K03665; -. DR Proteomes; UP000058129; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000058129}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000058129}. FT DOMAIN 200 368 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 159 193 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 423 AA; 48350 MW; A48847EF840D98A4 CRC64; MDQIIEKAIL VGVNLRHDPH FEYSMEELAN LAEALNVEVV GVITQNLERV TASHYVGTGK IDEVRSLYEA MDANLVIFDD ELSPAQIRNL EKDLDCKVID RTMLILDIFA RRAKTKEAQM QVEIAQLQYM LPRLVGMYNS LSRQGGATGG GFANRGAGET KLELDRRKIE EQITKLRRDL EVVKEQRETQ RKQRRKNNIP VVSLVGYTNA GKSTIMNQLL ARTSDEEHKQ VFEKDMLFAT LETSVRQIEL EDRKKFLLTD TVGFVSKLPH HLVKAFRSTL EEARDADLLL HVVDVSNEDH EYMMEVTNKT LQAVGVEGVP TIYVYNKADC TEITYPYVNQ NRIWLSARDG KGLDELIGMI RSEVFSDYVT LRVCIPYDRG DLVSFLNEKA SIKETAYEED GTHLKVEVRL EHEPKLKPFI ITE // ID A0A0X8D371_9BACL Unreviewed; 419 AA. AC A0A0X8D371; DT 13-APR-2016, integrated into UniProtKB/TrEMBL. DT 13-APR-2016, sequence version 1. DT 07-JUN-2017, entry version 10. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=ACH33_09120 {ECO:0000313|EMBL:AMA73003.1}; OS Aneurinibacillus sp. XH2. OC Bacteria; Firmicutes; Bacilli; Bacillales; Paenibacillaceae; OC Aneurinibacillus group; Aneurinibacillus. OX NCBI_TaxID=1450761 {ECO:0000313|EMBL:AMA73003.1, ECO:0000313|Proteomes:UP000065566}; RN [1] {ECO:0000313|EMBL:AMA73003.1, ECO:0000313|Proteomes:UP000065566} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Xh2 {ECO:0000313|EMBL:AMA73003.1, RC ECO:0000313|Proteomes:UP000065566}; RA Millard Andrew; RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:AMA73003.1, ECO:0000313|Proteomes:UP000065566} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Xh2 {ECO:0000313|EMBL:AMA73003.1, RC ECO:0000313|Proteomes:UP000065566}; RA Zhang Z., Qiao N., Zhang Y., Xiao Z., Jing L., Zhao J.-Y.; RT "Draft genome of the novel themophilic polyhydroxyalkanoates producer RT Aneurinibacillus sp. XH2 (CCTCC M 2013550) isolated from Gudao RT oilfield in China."; RL Submitted (JAN-2016) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP014140; AMA73003.1; -; Genomic_DNA. DR RefSeq; WP_057898738.1; NZ_CP014140.1. DR EnsemblBacteria; AMA73003; AMA73003; ACH33_09120. DR KEGG; anx:ACH33_09120; -. DR KO; K03665; -. DR Proteomes; UP000065566; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000065566}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000065566}. FT DOMAIN 200 362 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 419 AA; 47522 MW; 85C37E36D98FC571 CRC64; MVDEQKTEQA ILIGCYKKHG DQRRFELSME ELAELTRTAQ AEVIASLTQE RNQIDARLYV GKGKVEEINQ LALELKADLV IFNDELTPMQ IRNLEQAIEC KVIDRTQLIL DIFAQRAHSR EGKLQVELAQ LQYRLPRLTG KGAGLSRLGA GIGTRGPGET KLETDRRHIR RRISEIEHQL AEVKRHRLLY RERRKKNEVF QAALVGYTNA GKSTILNRLT GAGVLEEDKL FATLDPTSRR VRLPGGEEII MTDTVGFIQD LPHQLVAAFR STLEEAAEAD VIVQIVDASH PDHQIHMEVV DSVLTELGAG MIPRLTVFNK MDVVAEAPIA PVTGEVLYIS AHRPEDIKRL LMVIEAHIKS RYARYTLRLP TIRGDLYALV RRNLHIVHEN ISEDGMYYEL QVEGRNVTQL SPELLQFII // ID A0A0X8E214_9MICO Unreviewed; 523 AA. AC A0A0X8E214; DT 13-APR-2016, integrated into UniProtKB/TrEMBL. DT 13-APR-2016, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=AWU67_08805 {ECO:0000313|EMBL:AMB58945.1}; OS Microterricola viridarii. OC Bacteria; Actinobacteria; Micrococcales; Microbacteriaceae; OC Microterricola. OX NCBI_TaxID=412690 {ECO:0000313|EMBL:AMB58945.1, ECO:0000313|Proteomes:UP000058305}; RN [1] {ECO:0000313|EMBL:AMB58945.1, ECO:0000313|Proteomes:UP000058305} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ERGS5:02 {ECO:0000313|EMBL:AMB58945.1, RC ECO:0000313|Proteomes:UP000058305}; RA Kumar R., Singh D., Swarnkar M.K.; RT "First complete genome sequence of a species in the genus RT Microterricola, an extremophilic cold active enzyme producing strain RT ERGS5:02 isolated from Sikkim Himalaya."; RL Submitted (JAN-2016) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP014145; AMB58945.1; -; Genomic_DNA. DR RefSeq; WP_067227987.1; NZ_CP014145.1. DR EnsemblBacteria; AMB58945; AMB58945; AWU67_08805. DR KEGG; mvd:AWU67_08805; -. DR KO; K03665; -. DR Proteomes; UP000058305; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 2. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000058305}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000058305}. FT DOMAIN 298 463 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 523 AA; 55896 MW; F7B3FD99555748F9 CRC64; MTDASNTTND STGTDALESD DVVARVLASA DARAAGGAHF SSGIFSSGAQ ALQTEAGAAA SSDGEQLDRE DRNALRRVPS LSTELEDVTE VEYRQLRLEN VVLIGIYMQG SVDDAENSMR ELAALAETAG ATVLDGLLQR RPNPDPSTFL GSGKARELAG IVQALGADTV IADTELAPSQ RRALEDVVKV KVIDRTAVIL DIFSQHAKSR EGKAQVELAQ LQYLLPRLRG WGDSMSRQAG GQVGGAGAGM GSRGPGETKI ELDRRRIHTR MSKLRKQIAA MKPAREAKRA NRRRNSVPSV AIAGYTNAGK SSILNRITHA GVLVENSLFA TLDATVRKNT TSDGRIYTLA DTVGFVRNLP HQLVEAFRST LEEVADSDLI VHVVDGSHPD PASQIATVRD VIGEVGARGI PELIVFNKSD LIDDDARLVL RGLEPRAIFA SARSGEGIDE LLATIGEMLP DPSLAIELVV PYDRGDLISL LHEKGRVIST EYVEDGTLVR ARIASDLESL FAPFRAPAGA LEA // ID A0A0X8F9E2_9LACT Unreviewed; 392 AA. AC A0A0X8F9E2; DT 13-APR-2016, integrated into UniProtKB/TrEMBL. DT 13-APR-2016, sequence version 1. DT 05-JUL-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=AWM71_00250 {ECO:0000313|EMBL:AMB93179.1}; OS Aerococcus christensenii. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Aerococcaceae; OC Aerococcus. OX NCBI_TaxID=87541 {ECO:0000313|EMBL:AMB93179.1, ECO:0000313|Proteomes:UP000060400}; RN [1] {ECO:0000313|Proteomes:UP000060400} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CCUG28831 {ECO:0000313|Proteomes:UP000060400}; RA Carkaci D., Dargis R., Nielsen X.C., Skovgaard O., Fuursted K., RA Christensen J.J.; RT "Six Aerococcus type strain genome sequencing and assembly using RT PacBio and Illumina Hiseq."; RL Submitted (JAN-2016) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP014159; AMB93179.1; -; Genomic_DNA. DR EnsemblBacteria; AMB93179; AMB93179; AWM71_00250. DR KEGG; acg:AWM71_00250; -. DR KO; K03665; -. DR Proteomes; UP000060400; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000060400}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000060400}. FT DOMAIN 176 340 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 135 169 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 392 AA; 44324 MW; CFD60EFA5DCE0168 CRC64; MKRQVQELQS LVETAGGEVV CTLMQARPQI DGRTVIGKGK LKALKDLVGS LEADLVVFYQ ELTHTQNRNL QEALEVGVID RVQLILDIFA QRAQSKEGKL QVALAQSQYL LPRLAGQGKS LSRLGGGIGS RGPGETQLEQ DRRFLRKKIQ KIKQDLKQVE KHRQVARKNR TSSFVFRVGL MGYTNAGKST LLTGLTSADT YQADQLFATL TPLTRHFQFS NQCLVSVTDT VGFIQDLPPL VIDAFHSTLE ESRQVDLLLI VVDSSSPYAK EQEEVVNQLL IDLHMQEIPR LYLYNKTDYL PISQEVPLTY SRPFLKLSAK SKSDIERLKE AIADQIKRAY TPFSGWVAPE ELSSWLKCRS SLYLESVHFD QGHNAYRLKG YRPPTFQLPR DF // ID A0A0X8FCA2_9LACT Unreviewed; 406 AA. AC A0A0X8FCA2; DT 13-APR-2016, integrated into UniProtKB/TrEMBL. DT 13-APR-2016, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=AWM72_07980 {ECO:0000313|EMBL:AMB94698.1}; OS Aerococcus sanguinicola. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Aerococcaceae; OC Aerococcus. OX NCBI_TaxID=119206 {ECO:0000313|EMBL:AMB94698.1, ECO:0000313|Proteomes:UP000069912}; RN [1] {ECO:0000313|Proteomes:UP000069912} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CCUG43001 {ECO:0000313|Proteomes:UP000069912}; RA Carkaci D., Dargis R., Nielsen X.C., Skovgaard O., Fuursted K., RA Christensen J.J.; RT "Six Aerococcus type strain genome sequencing and assembly using RT PacBio and Illumina Hiseq."; RL Submitted (JAN-2016) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP014160; AMB94698.1; -; Genomic_DNA. DR RefSeq; WP_067976003.1; NZ_CP014160.1. DR EnsemblBacteria; AMB94698; AMB94698; AWM72_07980. DR KEGG; asan:AWM72_07980; -. DR KO; K03665; -. DR Proteomes; UP000069912; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000069912}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000069912}. FT DOMAIN 194 356 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 153 187 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 406 AA; 45672 MW; 0EED584F8FD760F1 CRC64; MQEVIAVLLE DKSETDQDFQ MRLEECQELI KTAGGKLVAT LTQSRDHPDP RTYIGQGKLA ELKSLAETLS ADLIIFYDAL SPSQVRNIEA ALDWPVIDRV QLILDIFTLR AHSKEAKLQV ALVQNEYLLP RLAGQGLALS RLAGGIGTRG PGESQLERNR RTLRDDISRI KKQLKEAEKH REISRDRRTS SSRFKIGLVG YTNAGKSTIL NGLTQADTYE EDQLFATLTP LTRSFSLENG FQMTLTDTVG FIQDLPPMVI DAFHSTLEES RDVDLLLIVI DASSTYAKAQ EKTVCQLLDD LDMLKIPHLF VYNKMDQVET ADFVSPSSPY VAISARSPQG IKKLEEGIIT QIQSIYDYFE IDLPSQEASQ FLGQADSLYI ESFIFDEEKN TYLVKGYKRP QSKISH // ID A0A0X8FK97_9LACT Unreviewed; 399 AA. AC A0A0X8FK97; DT 13-APR-2016, integrated into UniProtKB/TrEMBL. DT 13-APR-2016, sequence version 1. DT 07-JUN-2017, entry version 13. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=AWM75_02090 {ECO:0000313|EMBL:AMB98855.1}; OS Aerococcus urinaehominis. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Aerococcaceae; OC Aerococcus. OX NCBI_TaxID=128944 {ECO:0000313|EMBL:AMB98855.1, ECO:0000313|Proteomes:UP000062260}; RN [1] {ECO:0000313|Proteomes:UP000062260} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CCUG42038B {ECO:0000313|Proteomes:UP000062260}; RA Carkaci D., Dargis R., Nielsen X.C., Skovgaard O., Fuursted K., RA Christensen J.J.; RT "Six Aerococcus type strain genome sequencing and assembly using RT PacBio and Illumina Hiseq."; RL Submitted (JAN-2016) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP014163; AMB98855.1; -; Genomic_DNA. DR RefSeq; WP_067977648.1; NZ_FNHJ01000007.1. DR EnsemblBacteria; AMB98855; AMB98855; AWM75_02090. DR KEGG; auh:AWM75_02090; -. DR KO; K03665; -. DR Proteomes; UP000062260; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000062260}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000062260}. FT DOMAIN 194 356 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 153 187 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 399 AA; 45351 MW; C81A009C588C8EA8 CRC64; MERVIAVYVQ TPDVDDRRLD MQLEELSELV RTAGGQLKKT IIQKRDRYDN RTLVGKGKVA EIKAMADAHE ADLVVFYQPL SPSQGRNIQE ELDMPVIDRV QLILDIFAQH ASSKEGKLQV ALAQNEYLLP RLAGQGTSLS RLGGGIGTRG PGETKLEMDR RVLRHEIQKI KRELKAVEDH RQRTRLKRQD SPTFQIALFG YTNVGKSTIL NQISAGGAQE DNKLFATLTP LTRQFDLENK FKLTITDTVG FIQDLPPQVI DAFHSTLEES RDVDLMLIVI DASSPYASEQ QEVVLDLLAE LEMNQTPHLF VYNKMDLVDE GQDHLFRPPY VAISARDETG MNKLKAAIIE QIKTIYQPFK MKVAPAEIGN WIAKQDYIYI ADMSFDDDEQ VYWLSGYRR // ID A0A0X8G6V0_9FLAO Unreviewed; 403 AA. AC A0A0X8G6V0; DT 13-APR-2016, integrated into UniProtKB/TrEMBL. DT 13-APR-2016, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=Lupro_07805 {ECO:0000313|EMBL:AMC11162.1}; OS Lutibacter profundi. OC Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales; OC Flavobacteriaceae; Lutibacter. OX NCBI_TaxID=1622118 {ECO:0000313|EMBL:AMC11162.1, ECO:0000313|Proteomes:UP000059672}; RN [1] {ECO:0000313|EMBL:AMC11162.1, ECO:0000313|Proteomes:UP000059672} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=LP1 {ECO:0000313|EMBL:AMC11162.1, RC ECO:0000313|Proteomes:UP000059672}; RA Wissuwa J., Le Moine Bauer S., Stokke R., Dahle H., Steen I.H.; RT "Complete genome sequence of Lutibacter profundus strain LP1."; RL Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP013355; AMC11162.1; -; Genomic_DNA. DR RefSeq; WP_068208328.1; NZ_CP013355.1. DR EnsemblBacteria; AMC11162; AMC11162; Lupro_07805. DR KEGG; lut:Lupro_07805; -. DR PATRIC; fig|1622118.3.peg.1613; -. DR KO; K03665; -. DR Proteomes; UP000059672; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000059672}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000059672}. FT DOMAIN 200 385 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 403 AA; 46641 MW; C220F072A143576F CRC64; MIEEKKVTSE KIVLIGVVTQ HQDEEQSNEY LNELEFLTLT AGGVAVKRFT QKLEIPNPKT FIGTGKLDEV KQYMEANNIE TAIFDDELSA SQLRNIEKVL DCKVLDRTSL ILDIFARRAQ TSYARTQVEL AQCQYLLPRL TRLWTHLERQ KGGIGLRGPG ETEIETDRRI IRDKITLLKK KLKVIDKQMA VQRKNRGKMV RVALVGYTNV GKSTLMNVVS KSDVFAENKL FATLDTTVRK VVIKNIPFLL TDTVGFIRKL PTQLVESFKS TLDEVREADL LLHIVDISHP NFEEHIASVN KILDEIKSAN KPTIMVFNKI DVYQHETIDS DDLVTKKTKE HYTLAEWEKT WMNKLDNNCL FISALNKENL ENFKEKVFKE VKKIHITRFP YNDFLYEEYK EID // ID A0A0X8GKQ6_9BURK Unreviewed; 374 AA. AC A0A0X8GKQ6; DT 13-APR-2016, integrated into UniProtKB/TrEMBL. DT 13-APR-2016, sequence version 1. DT 07-JUN-2017, entry version 10. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=VN23_04655 {ECO:0000313|EMBL:AMC33941.1}; OS Janthinobacterium sp. B9-8. OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Oxalobacteraceae; Janthinobacterium. OX NCBI_TaxID=1236179 {ECO:0000313|EMBL:AMC33941.1, ECO:0000313|Proteomes:UP000069577}; RN [1] {ECO:0000313|EMBL:AMC33941.1, ECO:0000313|Proteomes:UP000069577} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=B9-8 {ECO:0000313|EMBL:AMC33941.1, RC ECO:0000313|Proteomes:UP000069577}; RA Xu X., Jin W., Wu Q., Jiang L., Huang H.; RT "The whole genome sequence of Janthinbacterium sp. B9-8, a bacterium RT isolated from low temperature sewage."; RL Submitted (JAN-2016) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP014222; AMC33941.1; -; Genomic_DNA. DR RefSeq; WP_046349896.1; NZ_CP014222.1. DR EnsemblBacteria; AMC33941; AMC33941; VN23_04655. DR KEGG; jab:VN23_04655; -. DR KO; K03665; -. DR Proteomes; UP000069577; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000069577}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000069577}. FT DOMAIN 198 364 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 374 AA; 41913 MW; C99C1E0392099EFA CRC64; MFERHKGGDR AILVCLDFGE LDYQDGVEEF VQLVESAGAN ILATVEGKRS RPDRAYFAGT GKVQEIAEIV RAHEAELVIF NHQLSPSQER NLEKVLQCRV VDRTTLILDI FAQRARTAEG KLQVELAQLS HISTRLIRGW THLERQKGGI GMRGPGESQL ETDRRLLGTR VKRLKDQLAT VQKQRATQRR SRERNRQFSV AIVGYTNAGK SSLFNALTKS KIYVADQLFA TLDTTSRKLY LDPENSIVLS DTVGFIRQLP HTLVAAFHAT LEETIQADLL LHVVDINHPL RDMQIIEVNK VLSEIGAERI PQLMVNNKID LRDMPASVDH DEYGRICAVR LSATQGIGLD ALRAALLEAL SHPLKTAELT NESK // ID A0A0X8GZF2_9FIRM Unreviewed; 361 AA. AC A0A0X8GZF2; DT 13-APR-2016, integrated into UniProtKB/TrEMBL. DT 13-APR-2016, sequence version 1. DT 05-JUL-2017, entry version 12. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=AOC36_04540 {ECO:0000313|EMBL:AMC93264.1}; OS Erysipelothrix larvae. OC Bacteria; Firmicutes; Erysipelotrichia; Erysipelotrichales; OC Erysipelotrichaceae; Erysipelothrix. OX NCBI_TaxID=1514105 {ECO:0000313|EMBL:AMC93264.1, ECO:0000313|Proteomes:UP000063781}; RN [1] {ECO:0000313|EMBL:AMC93264.1, ECO:0000313|Proteomes:UP000063781} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=LV19 {ECO:0000313|EMBL:AMC93264.1, RC ECO:0000313|Proteomes:UP000063781}; RA Lim S., Kim B.-C.; RT "Erysipelothrix larvae sp. LV19 isolated from the larval gut of the RT rhinoceros beetle, Trypoxylus dichotomus."; RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP013213; AMC93264.1; -; Genomic_DNA. DR EnsemblBacteria; AMC93264; AMC93264; AOC36_04540. DR KEGG; erl:AOC36_04540; -. DR KO; K03665; -. DR Proteomes; UP000063781; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000063781}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000063781}. FT DOMAIN 198 299 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 164 191 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 361 AA; 41262 MW; B0AAB9014D4E59B8 CRC64; MTQKDKVLAV IIAQGNNAFE IEEDRQEFLG LAKACEMEVE AEASFKLKSP NAVTYFGDGN VQMVANVVQD SDYDAVIINV GLTGNQIKNL QERFKCTVLD KNMVLLQIFS KRAQSAESKA RVEIANLNYM MSRMVGSYDD LGRQSGRGSG KNRGLGETKL ELDRRHVRKR INLLKKKIEQ FEKQRETQRS RRVNNTDLKV ALVGYTNVGK SSLMNVLLSN DTKNVLEQDM VFASLDTTSR QIYNGDSSFI LHDTVGYIEN LPKALYPAFQ STRDEIMDAD LILHVIDRSH PFYERQEQVI EDYLKSMQVE DVPVWKVYNK IDRLDEIFMS TPTVHFISTK DHQGIESLKA CIHEFSNRSF H // ID A0A0X8HC47_9GAMM Unreviewed; 440 AA. AC A0A0X8HC47; DT 13-APR-2016, integrated into UniProtKB/TrEMBL. DT 13-APR-2016, sequence version 1. DT 07-JUN-2017, entry version 12. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:AMC99922.1}; GN ORFNames=LOKO_00841 {ECO:0000313|EMBL:AMC99922.1}; OS Halomonas chromatireducens. OC Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales; OC Halomonadaceae; Halomonas. OX NCBI_TaxID=507626 {ECO:0000313|EMBL:AMC99922.1, ECO:0000313|Proteomes:UP000063387}; RN [1] {ECO:0000313|EMBL:AMC99922.1, ECO:0000313|Proteomes:UP000063387} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=AGD 8-3 {ECO:0000313|EMBL:AMC99922.1, RC ECO:0000313|Proteomes:UP000063387}; RA Wen L., He K., Yang H.; RL Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP014226; AMC99922.1; -; Genomic_DNA. DR RefSeq; WP_066445440.1; NZ_CP014226.1. DR EnsemblBacteria; AMC99922; AMC99922; LOKO_00841. DR KEGG; hco:LOKO_00841; -. DR PATRIC; fig|507626.3.peg.834; -. DR KO; K03665; -. DR Proteomes; UP000063387; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000063387}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000063387}. FT DOMAIN 199 365 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 440 AA; 49516 MW; B66B70EFD8795DB3 CRC64; MFFERPDAGE TAVLVHVDFQ DEREREDPGE FLELVRSAGA EPATLLSGSR QRPDSRTFIG SGKVEELRET LSVHGAELVI FNHALSPSQE RNLEQVLKCR VLDRTGLILD IFAQRARTHE GKLQVELAQL EYMSTRLVRG WTHLERQKGG IGLRGPGETQ LETDRRLLRA RIKAIHKRLD KVRTQRAQNR RARARAEIPS VSLVGYTNAG KSTLFNALTE SKVYTADQLF ATLDPTLRRL EIGDVGPVVL ADTVGFIRHL PHKLVEAFQA TLQEASEATL LVHVIDAADP DRERNISEVE GVLNEIGALD VPMLKVMNKI DLLDSAPRIE RDGQGRPEVV WVSAQEGRGL DLLEEALSEC LADDVIDFSL TLSPEQGRLR AGLHELGAVR EEHFEEPDGR VGLKVRLPRR DFLQLMSRLD ERAEDYLPPE LCERPVWEAR // ID A0A0X8JHB0_9ACTO Unreviewed; 516 AA. AC A0A0X8JHB0; DT 13-APR-2016, integrated into UniProtKB/TrEMBL. DT 13-APR-2016, sequence version 1. DT 07-JUN-2017, entry version 12. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=AXF14_12600 {ECO:0000313|EMBL:AMD88622.1}; OS Actinomyces radicidentis. OC Bacteria; Actinobacteria; Actinomycetales; Actinomycetaceae; OC Actinomyces. OX NCBI_TaxID=111015 {ECO:0000313|EMBL:AMD88622.1, ECO:0000313|Proteomes:UP000065220}; RN [1] {ECO:0000313|EMBL:AMD88622.1, ECO:0000313|Proteomes:UP000065220} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CCUG 36733 {ECO:0000313|EMBL:AMD88622.1, RC ECO:0000313|Proteomes:UP000065220}; RA Wen L., He K., Yang H.; RL Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP014228; AMD88622.1; -; Genomic_DNA. DR RefSeq; WP_067944448.1; NZ_CP014228.1. DR EnsemblBacteria; AMD88622; AMD88622; AXF14_12600. DR KEGG; ard:AXF14_12600; -. DR KO; K03665; -. DR Proteomes; UP000065220; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 2. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000065220}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000065220}. FT DOMAIN 287 453 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 516 AA; 55089 MW; 98894DA9380D45FE CRC64; MPSPEDIVSR ILSRTGTALA STAGEHERRD VVDAGALERE ARAGTRRVAS LSTELEDVSE VEYRQIRLEK VVLVGLELPT AHAGTTGPAG ARHGSAVELA DAQDAETSLA ELAALAETAG SQVLDALIQK RDHPDPATYL GSGKAKELAE MVSAHGADTV IVDGELAPSQ RRALEDVVKV KVVDRTALIL DIFAQHAKSR EGKAQVELAQ LEYLLPRLRG WGDSMSRQAG GRVAGGQGIG SRGPGETKIE LDRRRIRDRM AKLRREIKAM APSREVKRGS RRRGPIPSVA IAGYTNAGKS SLMNRLTDAG LMVQDALFAT LDPTVRKAET SDGRVYTLTD TVGFVRNLPH ELIEAFRSTL EEVAGADLVL HVVDAAHPDP LSQVAAVREV LADIPGALDV PELIVLNKAD LADPVTLAAL RTRLPGALTV SAYTGEGLDE LRARIDEMLP RPDVQVDVVV PYSRGDLVSR VHADGEIDAV EYVEAGTRVR ARVDAPLAAE LEAADVAGGS DDETRA // ID A0A0X8JN64_9DELT Unreviewed; 538 AA. AC A0A0X8JN64; DT 13-APR-2016, integrated into UniProtKB/TrEMBL. DT 13-APR-2016, sequence version 1. DT 07-JUN-2017, entry version 12. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=AXF15_00850 {ECO:0000313|EMBL:AMD91808.1}; OS Desulfomicrobium orale DSM 12838. OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfovibrionales; OC Desulfomicrobiaceae; Desulfomicrobium. OX NCBI_TaxID=888061 {ECO:0000313|EMBL:AMD91808.1, ECO:0000313|Proteomes:UP000063964}; RN [1] {ECO:0000313|EMBL:AMD91808.1, ECO:0000313|Proteomes:UP000063964} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 12838 {ECO:0000313|EMBL:AMD91808.1, RC ECO:0000313|Proteomes:UP000063964}; RA Wen L., He K., Yang H.; RL Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP014230; AMD91808.1; -; Genomic_DNA. DR RefSeq; WP_066602025.1; NZ_CP014230.1. DR EnsemblBacteria; AMD91808; AMD91808; AXF15_00850. DR KEGG; doa:AXF15_00850; -. DR KO; K03665; -. DR Proteomes; UP000063964; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000063964}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000063964}. FT DOMAIN 379 538 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 338 365 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 538 AA; 59080 MW; 9264C7E034DB70B1 CRC64; MSSKPLGSLT GLKPSQITAL SRLYNRRFPG LGGFTADQAK ELALLSRGMG RQIGVLVNRK GVPVMVIAGE QDSILIPELS RHREAQSRLS GLRLLHTHLD SSLLTQEDLM DMAFLRLDAV CVLTVSPEGT PGACQIAHLL PPNADELPYM VHPPRIWDEV DFDFDASARA LEDELARTGQ SVASTAREGS AILVSVGAAP RSVQERSLAE LAELAVTAGL DVAGEVVQRV PRVNPKLILG RGKLAELEVL ALQKNASVLV FDQELSPTQQ RNLSQITERK VLDRTQLILD IFAQHARTKE GKLQVEMAQL KYMMPRLVGQ NRALSRLMGG IGGRGPGESK LEMDRRKIRE RLAQLKTELA GVRRHRAATR GRRDKAGLPV VSLVGYTNAG KSTLLNTLTR SDVLAENRLF ATLDPTSRRL RFPEDREIIL TDTVGFIRHL PEDLREAFMA TLEELQGADL LVHVADASHP EMDQQLEAVE AILRDLKLDG IPRILALNKT DLAPDPSALA FAHPQAVFIS AIHRPSLTPL VERIKSLL // ID A0A0X8R3K3_9SPHN Unreviewed; 443 AA. AC A0A0X8R3K3; DT 13-APR-2016, integrated into UniProtKB/TrEMBL. DT 13-APR-2016, sequence version 1. DT 07-JUN-2017, entry version 12. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:AMG74579.1}; GN ORFNames=SGRAN_2211 {ECO:0000313|EMBL:AMG74579.1}; OS Sphingopyxis granuli. OC Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales; OC Sphingomonadaceae; Sphingopyxis. OX NCBI_TaxID=267128 {ECO:0000313|EMBL:AMG74579.1, ECO:0000313|Proteomes:UP000058599}; RN [1] {ECO:0000313|EMBL:AMG74579.1, ECO:0000313|Proteomes:UP000058599} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=TFA {ECO:0000313|EMBL:AMG74579.1, RC ECO:0000313|Proteomes:UP000058599}; RX PubMed=26847793; DOI=10.1186/s12864-016-2411-1; RA Garcia-Romero I., Perez-Pulido A.J., Gonzalez-Flores Y.E., RA Reyes-Ramirez F., Santero E., Floriano B.; RT "Genomic analysis of the nitrate-respiring Sphingopyxis granuli RT (formerly Sphingomonas macrogoltabida) strain TFA."; RL BMC Genomics 17:93-93(2016). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP012199; AMG74579.1; -; Genomic_DNA. DR RefSeq; WP_067106593.1; NZ_CP012199.1. DR EnsemblBacteria; AMG74579; AMG74579; SGRAN_2211. DR KEGG; sgi:SGRAN_2211; -. DR PATRIC; fig|267128.3.peg.2338; -. DR KO; K03665; -. DR Proteomes; UP000058599; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 2. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000058599}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000058599}. FT DOMAIN 207 389 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 173 200 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 443 AA; 48446 MW; 46D04614C4C29A51 CRC64; MDDAAQGEVT RGAAAVLVVP EWHGQGLSRD LDARVAEAKG LALAIGLDVV AVHPLRLRQT RAATLIGAGQ IEAIKPGIAE NAAQLVIVDA ALTAIQQRNL ETEFGAKVID RTGLILEIFG ERAATAEGRL QVELAHLDYQ AGRLVRSWTH LERQRGGFGF LGGPGETQIE ADRRMIRNRM ARIRRQLDDA RRTRQLQRAK RQRAPWPVIA LVGYTNAGKS TFFNRLTGSD VMAEDMLFAT LDPTMREIRL PGIDKAILSD TVGFVSDLPT ELVAAFRATL EEVTTADLIV HVRDIVHPDT DAQYADVRAI LDSLGVNEAG GGEGDGEDRA RPIAQIEIWN KIDTADPERR AEIEAMAARR PDVAPISAAT GEGVEAARVL MAAELTARHE LLRVRLRFDQ GEAMAWLHAR GEVLADEPQG DGHLLTVRLD PADRARFERL WGA // ID A0A0X8VAJ7_CLOPR Unreviewed; 425 AA. AC A0A0X8VAJ7; DT 13-APR-2016, integrated into UniProtKB/TrEMBL. DT 13-APR-2016, sequence version 1. DT 07-JUN-2017, entry version 12. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:AMJ42062.1}; GN ORFNames=CPRO_25140 {ECO:0000313|EMBL:AMJ42062.1}; OS [Clostridium] propionicum DSM 1682. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Lachnospiraceae; OC Tyzzerella. OX NCBI_TaxID=991789 {ECO:0000313|EMBL:AMJ42062.1, ECO:0000313|Proteomes:UP000068026}; RN [1] {ECO:0000313|Proteomes:UP000068026} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=X2 {ECO:0000313|Proteomes:UP000068026}; RA McClelland M., Jain A., Saraogi P., Mendelson R., Westerman R., RA SanMiguel P., Csonka L.; RL Submitted (JAN-2016) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP014223; AMJ42062.1; -; Genomic_DNA. DR RefSeq; WP_066052277.1; NZ_FQUA01000003.1. DR EnsemblBacteria; AMJ42062; AMJ42062; CPRO_25140. DR KEGG; cpro:CPRO_25140; -. DR PATRIC; fig|991789.3.peg.2688; -. DR KO; K03665; -. DR Proteomes; UP000068026; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000068026}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}. SQ SEQUENCE 425 AA; 47215 MW; 2CF03BE8809F95E6 CRC64; MARDLHDTAD LEERVILFAV EPDERNSRST METEACLDEL EELVRTAGAV AVARSIQRRE RVHPGHYLGK GKIEELKMMV DAYGASGVVC DDELSPAQLK NLERLLETKV MDRTIVILDI FAGRAISGEG KIQVELAQLK YRLSRLTGMG ASMSRLGGGI GTRGPGEKKL ETDRRYIKDR IAELNSAAKE IQTHRELLRS QRGKKGTPVV SLVGYTNAGK STLINKLTDA GVLAEDKLFA TLDTTTRKVE LPNGSEILLT DTVGFIQKLP HHLVQAFRAT LEELKYADIL LHVVDASNSN RQEQMQVVYK TLEDLGCGDT PVITVFNKMD REVELPLPMD TKAREIAQVS AFTGDGLNGM LGMVENLLKS FRKSMVALVP YTEGGLIGWV HGRCEIIREE HTPEGVLLEV YVNEESANRL EKYKQ // ID A0A0X8WQB6_9CYAN Unreviewed; 587 AA. AC A0A0X8WQB6; DT 13-APR-2016, integrated into UniProtKB/TrEMBL. DT 13-APR-2016, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:BAU40413.1}; GN ORFNames=O77CONTIG1_00210 {ECO:0000313|EMBL:BAU40413.1}; OS Leptolyngbya sp. O-77. OC Bacteria; Cyanobacteria; Synechococcales; Leptolyngbyaceae; OC Leptolyngbya. OX NCBI_TaxID=1080068 {ECO:0000313|EMBL:BAU40413.1, ECO:0000313|Proteomes:UP000057790}; RN [1] {ECO:0000313|EMBL:BAU40413.1, ECO:0000313|Proteomes:UP000057790} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=O-77 {ECO:0000313|EMBL:BAU40413.1, RC ECO:0000313|Proteomes:UP000057790}; RA Tran K.T., Nguyen T.N., Yoon K-S., Ogo S.; RT "Complete genome sequence of Leptolyngbya sp. O-77."; RL Submitted (JAN-2016) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AP017367; BAU40413.1; -; Genomic_DNA. DR EnsemblBacteria; BAU40413; BAU40413; O77CONTIG1_00210. DR KEGG; let:O77CONTIG1_00210; -. DR PATRIC; fig|1080068.3.peg.245; -. DR KO; K03665; -. DR Proteomes; UP000057790; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000057790}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000057790}. FT DOMAIN 391 561 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 350 384 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 587 AA; 64693 MW; 19172C9154E67EEC CRC64; MPIETIFGNL QGLKPSQIKQ LQRLYHQRLP GDRLTTPEFA QRLAAVSTEI GQPVCAYINR RGQVIRVGVG TLRQTQIPPQ DLPRYGAERL SGIRCVATKF KPEPPSSAAL TAMALQRLDA LVLLVMTGEG FERRGGGATG YIREAYLAHL IPHPEANWTV SPPLSLDRVS QQDFLELTEG LESEFRREFV AQQVEVDHDR ALLVGIMTDN LSAQQFQAGL EELARLVETA GGDVVQVLSQ KRAHPHPQTV VGEGKVQEIA LAAQTVGANL IVFDRDLSPA QVRNLEAQIG VRVVDRTEVI LDIFAQRAQT GAGKLQVELA QLEYTMPRLI GRGRDMSRLG GGIGTRGPGE TKLETERRAI QRRIARLQQE VNQIQAHRAR LRQRRQHRDV PSVAVVGYTN AGKSTLLNAL TNAEVYTADQ LFATLDPTSR RLVVTDAETQ EPVELVLTDT VGFIHDLPPS LVDAFRATLE EVTEADALLH LVDLSHPAWQ SQIRSVMKIL SEMPITPGPA LLVFNKIDQV DGDTLALAQS EFPQALFISA GDRLGLGTLR QRLLQLVHYA VSMNAEMGEL PASDSPAQQS RRSYDFP // ID A0A100W3T9_9MYCO Unreviewed; 466 AA. AC A0A100W3T9; DT 13-APR-2016, integrated into UniProtKB/TrEMBL. DT 13-APR-2016, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=RMCB_5199 {ECO:0000313|EMBL:GAS91103.1}; OS Mycobacterium brisbanense. OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae; OC Mycobacterium; Mycobacterium fortuitum complex. OX NCBI_TaxID=146020 {ECO:0000313|EMBL:GAS91103.1, ECO:0000313|Proteomes:UP000069620}; RN [1] {ECO:0000313|Proteomes:UP000069620} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=JCM15654 {ECO:0000313|Proteomes:UP000069620}; RA Katahira K., Gotou Y., Iida K., Ogura Y., Hayashi T.; RT "Draft genome sequence of five rapidly growing Mycobacterium RT species."; RL Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:GAS91103.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BCSX01000045; GAS91103.1; -; Genomic_DNA. DR RefSeq; WP_062831074.1; NZ_BCSX01000045.1. DR Proteomes; UP000069620; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000069620}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000069620}. FT DOMAIN 243 412 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 202 236 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 466 AA; 50199 MW; 818E8FBF5D7EEDB8 CRC64; MTYPQTPSTG ELALQDRASL RRVAGLSTEL TDVSEVEYRQ LRLERVVLVG VWTDGSSADA DASLAELAAL AETAGSEVLE GLIQRRDKPD PSTYIGSGKA AELREVVVAT GADTVICDGE LSPAQLNSLE KVVKVKVIDR TALILDIFAQ HATSREGKAQ VSLAQMEYML PRLRGWGESM SRQAGGRAGG AGGGVGTRGP GETKIETDRR RIRERMSKLR REIRDMKKVR DTQRSRRLTS DVASVAIVGY TNAGKSSLLN ALTGAGVLVE NALFATLEPT SRRGEFDDGR PFVLTDTVGF VRHLPTQLVE AFRSTLEEVV DADLLVHVVD GSDANPLAQI SAVRQVIGEV IAEHDGRRAP ELLVVNKIDA TGDLALAQLR RALPDAVFVS AHSGDGLDRL RQRMGELVEP TDTMVDVTIP YERGDLVAKL HAEGRIDATE HGADGTRIKA RVPVPLAASL GEFATF // ID A0A100Y4A2_9ACTN Unreviewed; 497 AA. AC A0A100Y4A2; DT 13-APR-2016, integrated into UniProtKB/TrEMBL. DT 13-APR-2016, sequence version 1. DT 07-JUN-2017, entry version 10. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=ATE80_18085 {ECO:0000313|EMBL:KUH37441.1}; OS Streptomyces kanasensis. OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae; OC Streptomyces. OX NCBI_TaxID=936756 {ECO:0000313|EMBL:KUH37441.1, ECO:0000313|Proteomes:UP000054011}; RN [1] {ECO:0000313|EMBL:KUH37441.1, ECO:0000313|Proteomes:UP000054011} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ZX01 {ECO:0000313|EMBL:KUH37441.1, RC ECO:0000313|Proteomes:UP000054011}; RA Zhang G., Han L., Feng J., Zhang X.; RT "Genome-wide analysis reveals the secondary metabolome in Streptomyces RT kanasensis ZX01."; RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KUH37441.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LNSV01000046; KUH37441.1; -; Genomic_DNA. DR RefSeq; WP_058943262.1; NZ_LNSV01000046.1. DR EnsemblBacteria; KUH37441; KUH37441; ATE80_18085. DR Proteomes; UP000054011; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 2. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000313|EMBL:KUH37441.1}; KW Complete proteome {ECO:0000313|Proteomes:UP000054011}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900, KW ECO:0000313|EMBL:KUH37441.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000054011}. FT DOMAIN 276 441 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 497 AA; 53967 MW; FEE930E81A7A8F02 CRC64; MTSSSSPSQD EQSSAELNRA ESLRADALME EDVAWSYEID GERDGEQLDR SERAALRRVA GLSTELEDVT EVEYRQLRLE RVVLVGVWTS GTVQDAENSL AELAALAETA GALVLDGVIQ RRDKPDPATY IGSGKAEELR DIVLETGADT VVCDGELSPG QLIHLEDVVK VKVVDRTALI LDIFAQHAKS REGKAQVALA QMQYMLPRLR GWGQSLSRQM GGGGGGGMAT RGPGETKIET DRRRIREKMA KMRREIAEMK TGRDIKRQER RRNKVPSVAI AGYTNAGKSS LLNRLTGAGV LVENALFATL DPTVRRAETP SGRLYTLVDT VGFVRHLPHH LVEAFRSTME EVGESDLILH VVDGAHPAPE EQLAAVREVI RDVGATNVRE IVVVNKADAA DPLVLQRLLR VEKHAIAVSA RTGAGIAELL ALIDAELPRP EVEIEALVPY TQGGLVSRVH AEGEVLSEEH TADGTLIKAR VHSELAALLA PFSPVTA // ID A0A100YV97_9ACTN Unreviewed; 446 AA. AC A0A100YV97; DT 13-APR-2016, integrated into UniProtKB/TrEMBL. DT 13-APR-2016, sequence version 1. DT 07-JUN-2017, entry version 10. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=AUL39_04755 {ECO:0000313|EMBL:KUH58325.1}; OS Olsenella scatoligenes. OC Bacteria; Actinobacteria; Coriobacteriia; Coriobacteriales; OC Atopobiaceae; Olsenella. OX NCBI_TaxID=1299998 {ECO:0000313|EMBL:KUH58325.1, ECO:0000313|Proteomes:UP000054078}; RN [1] {ECO:0000313|EMBL:KUH58325.1, ECO:0000313|Proteomes:UP000054078} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SK9K4 {ECO:0000313|EMBL:KUH58325.1, RC ECO:0000313|Proteomes:UP000054078}; RA Li X., Borg B., Canibe N.; RT "Draft Genome Sequence of Olsenella scatoligenes SK9K4T; a Producer of RT 3-Methylindole- (skatole) and 4-Methylphenol- (p-cresol) Isolated from RT Pig Feces."; RL Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KUH58325.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LOJF01000009; KUH58325.1; -; Genomic_DNA. DR RefSeq; WP_059054255.1; NZ_LOJF01000009.1. DR EnsemblBacteria; KUH58325; KUH58325; AUL39_04755. DR Proteomes; UP000054078; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000054078}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000054078}. FT DOMAIN 211 376 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 177 204 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 446 AA; 49193 MW; C9EA072ABB78507D CRC64; MARFEPTSTA PVRERAILVG VDFGKNDDWT LEESMAELGR LAETDGADVV FTLTQRLDAP VPRTFIGKGK VEELVSYVRN LDADVVIFDD ELTPSQQSNL EKIVGEPVKI IDRTALILDI FGVHATTREG RLQVQLAQLQ YVLPRLRGMW SHLVGEQTRG GIGSRFGQGE SQLEVDRRLV RKRISTLRDE LARLETRREV QSKARWDSGV YRVALAGYTN AGKSTLLNAL TGSEVYVRDE LFATLDPTTR SIELEEGRKV TLTDTVGFIQ KLPTTLVEAF KSTLAEVRAA DLILLVADAS DSGVERQVRA VRSVLDEIGA SQIPSVLVLN KCDLLTPEAF SDLQASHPDA VTISAREGTG LSGLLYRVAR EASRGDATVT VLVPFSKGIL MKMVHERCQV IREVYTEKGL LATVSASERM RSTLAPYVVP DENFEPWGST APTPRQ // ID A0A101CZA6_9RHOB Unreviewed; 423 AA. AC A0A101CZA6; DT 13-APR-2016, integrated into UniProtKB/TrEMBL. DT 13-APR-2016, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=AVO45_03720 {ECO:0000313|EMBL:KUJ86082.1}; OS Ruegeria sp. ZGT118. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae; Ruegeria. OX NCBI_TaxID=1685379 {ECO:0000313|EMBL:KUJ86082.1, ECO:0000313|Proteomes:UP000053791}; RN [1] {ECO:0000313|EMBL:KUJ86082.1, ECO:0000313|Proteomes:UP000053791} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ZGT118 {ECO:0000313|EMBL:KUJ86082.1, RC ECO:0000313|Proteomes:UP000053791}; RA Shamseldin A., Moawad H., Abd El-Rahim W.M., Sadowsky M.J.; RL Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KUJ86082.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LQBQ01000001; KUJ86082.1; -; Genomic_DNA. DR RefSeq; WP_068344534.1; NZ_LQBQ01000001.1. DR EnsemblBacteria; KUJ86082; KUJ86082; AVO45_03720. DR Proteomes; UP000053791; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000053791}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000053791}. FT DOMAIN 203 372 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 423 AA; 47348 MW; FB207BE5930FFBA7 CRC64; MEHDRVRTRA WVLHPDIKTD QDRRLPEPAL EEAVALAAAL PDLDVIGAEI VRLSRAQPGL LFGSGKIEEL GARFKENEIE LVLIDGPVTP VQQRNLEREW KVKILDRTGL ILEIFSDRAR TREGVLQVEM AALSYQRTRL VRAWTHLERQ RGGLGFVGGP GETQIEADRR AIDEQLVRLR RQLQKVVKTR TLHRAARAKV PYPIVALVGY TNAGKSTLFN RLTGAEVMAK DMLFATLDPT MRRVQLPDGP EVILSDTVGF VSNLPTELVA AFRATLEEVL GADLIVHVRD ISHPETEAQA KDVETILASL GVGEDRARLE VWNKIDLLPE EERTAAIARA DRDPKVFAIS AVTGVGVQPL LEAIAEKLQG VRHEETLHLG FGDGRKRAWL FEQDVVQDEN QTEDGFEITV LWTPRQQAKF AKL // ID A0A101D5X1_9GAMM Unreviewed; 436 AA. AC A0A101D5X1; DT 13-APR-2016, integrated into UniProtKB/TrEMBL. DT 13-APR-2016, sequence version 1. DT 30-AUG-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:KUJ89454.1}; GN ORFNames=XD36_0077 {ECO:0000313|EMBL:KUJ89454.1}; OS Halomonas sp. 54_146. OC Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales; OC Halomonadaceae; Halomonas. OX NCBI_TaxID=1635257 {ECO:0000313|EMBL:KUJ89454.1, ECO:0000313|Proteomes:UP000053192}; RN [1] {ECO:0000313|EMBL:KUJ89454.1, ECO:0000313|Proteomes:UP000053192} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=54_146 {ECO:0000313|EMBL:KUJ89454.1}; RA Hu P., Tom L., Singh A., Thomas B.C., Baker B.J., Piceno Y.M., RA Andersen G.L., Banfield J.F.; RT "Genome-resolved metagenomic analysis reveals roles for candidate RT phyla and other microbial community members in biogeochemical RT transformations in oil reservoirs."; RL MBio 7:e01669-15(2015). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KUJ89454.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LGEN01000001; KUJ89454.1; -; Genomic_DNA. DR PATRIC; fig|1635257.4.peg.80; -. DR Proteomes; UP000053192; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000053192}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}. FT DOMAIN 199 365 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 436 AA; 48981 MW; EC546608DF37B91D CRC64; MFFERPDAGE TAVLVHVDFH DEQKREDPGE FLELVRSAGA EPATLLTASR HRPDSRTFIG SGKLEELRAL LAAHAAELVI FNHSLSPSQE RNVEQELKCR VLDRTGLILD IFAQRARTHE GKLQVELAQL EYMSTRLVRG WTHLERQKGG IGLRGPGETQ LETDRRLLRG RIKSIHKRLD KVRSQRDQNR RARARAEIHS VSLVGYTNAG KSTLFNALTN AEVYAADQLF ATLDPTLRRL EIEDVGPVVL ADTVGFIRHL PHKLVEAFQA TLQEASEATL LVHVIDAADP DRELNVEQVD LVLKEIGADD VPVLKVMNKI DKLDSAPRIE RDGQGVPEVV WLSAQQGQGL ELLHEALTER LANDVIGFSL TLSPEQGKLR AGLHELNAVR EEAFDEQGHS VLDVRLPRRD FNQLMAQLGE RSNTYLPKAL RETDEW // ID A0A101DI39_9DELT Unreviewed; 477 AA. AC A0A101DI39; DT 13-APR-2016, integrated into UniProtKB/TrEMBL. DT 13-APR-2016, sequence version 1. DT 07-JUN-2017, entry version 10. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=XD41_1027 {ECO:0000313|EMBL:KUJ95965.1}; OS Desulfonauticus sp. 38_4375. OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfovibrionales; OC Desulfohalobiaceae; Desulfonauticus. OX NCBI_TaxID=1635258 {ECO:0000313|EMBL:KUJ95965.1, ECO:0000313|Proteomes:UP000053839}; RN [1] {ECO:0000313|EMBL:KUJ95965.1, ECO:0000313|Proteomes:UP000053839} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=38_4375 {ECO:0000313|EMBL:KUJ95965.1}; RA Hu P., Tom L., Singh A., Thomas B.C., Baker B.J., Piceno Y.M., RA Andersen G.L., Banfield J.F.; RT "Genome-resolved metagenomic analysis reveals roles for candidate RT phyla and other microbial community members in biogeochemical RT transformations in oil reservoirs."; RL MBio 7:e01669-15(2015). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KUJ95965.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LGER01000022; KUJ95965.1; -; Genomic_DNA. DR PATRIC; fig|1635258.3.peg.2191; -. DR Proteomes; UP000053839; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000053839}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000053839}. FT DOMAIN 315 477 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 274 311 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 477 AA; 54331 MW; 0BE1F9E7113ADAFB CRC64; MVIVGDNRGI LIPFLEKVRH NQSRLSGLRL LHTHLKEQEL DQEDLMDMIF LRLDSIEVLT VSEEGYPKSY AYAHILPANK QEQMYSISSL LPWDQADFNP KEVIKSLEEE LERTSAKTSE VLEENRALLI SVDSAPKKEQ EATLEELKAL AQTAGLEVRG FFIQQVKKVN PAHILSKNKL AELEVLALQK GASILVFASE LSPSQLRNLT NITERKVIDR TQLILDIFAQ HAQSRAGKLQ VEMAQLKYTL PRLIKQNRAL SRLTGGIGGR GPGETKLELD RRKIRTRLNK IEEELNQIKK QRKTARSLRE KSEIPIVALI GYTNVGKSTL LNTLTKSQVL AQNKLFATLD PTSKKMRYPQ DREIVFTDTV GFIKNLPQEL KEAFSATLEE LYPAHLLLHV ADASHPHLAK QIQAVENILK DLELQDKPKI LILNKWDKLE EESKNFLANQ YPQAVKISAL HKEGLEELMQ IIFRKLF // ID A0A101E940_9FIRM Unreviewed; 431 AA. AC A0A101E940; DT 13-APR-2016, integrated into UniProtKB/TrEMBL. DT 13-APR-2016, sequence version 1. DT 07-JUN-2017, entry version 10. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=XD50_0052 {ECO:0000313|EMBL:KUK11585.1}; OS Clostridia bacterium 41_269. OC Bacteria; Firmicutes; Clostridia. OX NCBI_TaxID=1635275 {ECO:0000313|EMBL:KUK11585.1, ECO:0000313|Proteomes:UP000053409}; RN [1] {ECO:0000313|EMBL:KUK11585.1, ECO:0000313|Proteomes:UP000053409} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=41_269 {ECO:0000313|EMBL:KUK11585.1}; RA Hu P., Tom L., Singh A., Thomas B.C., Baker B.J., Piceno Y.M., RA Andersen G.L., Banfield J.F.; RT "Genome-resolved metagenomic analysis reveals roles for candidate RT phyla and other microbial community members in biogeochemical RT transformations in oil reservoirs."; RL MBio 7:e01669-15(2015). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KUK11585.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LGEZ01000001; KUK11585.1; -; Genomic_DNA. DR PATRIC; fig|1635275.3.peg.53; -. DR Proteomes; UP000053409; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000053409}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000053409}. FT DOMAIN 206 370 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 431 AA; 48275 MW; 93073ABC32DA83D0 CRC64; MSGFLDAVGK EEGKRALLVT LQLPGDSKEK IEISLEELKG LVETAGCTAV GYEVQKRDSP CASLFLGKGK ALELEERRKA GEFDMLVFNH DLSPTQQRNL EDIIQCPIID RTTLILDIFA QRAKTKEAKL QVELAQLQYR LPRLTGRGTA LNRLGGGIGT RGPGLTKLEV DRRKIRDRIA YITRELKKIE KHRRLIRKRR LSRDVPVVAL TGYTNVGKST LHDVLSGSGT YADDRLFATL DSTARKVVPK CGEPYVLIDT VGFIRDLPPK LVAAFRSTLE ELQYSDLLLH VVDSTSKDID QEIELVEKVL GELEVLEKPR ILVFNKIDKI KGTLPKVSHG AQKEVYISAL KGIGIEELNK VIQEEISRDR EEMEVFISYE KFEILDLVYK EGVVLEQKPQ ENGIFLKVVL KKAAAGKIKK ELGEKTSTSS V // ID A0A101F8L6_9FIRM Unreviewed; 420 AA. AC A0A101F8L6; DT 13-APR-2016, integrated into UniProtKB/TrEMBL. DT 13-APR-2016, sequence version 1. DT 07-JUN-2017, entry version 9. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=XD63_0342 {ECO:0000313|EMBL:KUK32464.1}; OS Thermoanaerobacterales bacterium 50_218. OC Bacteria; Firmicutes; Clostridia; Thermoanaerobacterales. OX NCBI_TaxID=1635288 {ECO:0000313|EMBL:KUK32464.1, ECO:0000313|Proteomes:UP000053634}; RN [1] {ECO:0000313|EMBL:KUK32464.1, ECO:0000313|Proteomes:UP000053634} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=50_218 {ECO:0000313|EMBL:KUK32464.1}; RA Hu P., Tom L., Singh A., Thomas B.C., Baker B.J., Piceno Y.M., RA Andersen G.L., Banfield J.F.; RT "Genome-resolved metagenomic analysis reveals roles for candidate RT phyla and other microbial community members in biogeochemical RT transformations in oil reservoirs."; RL MBio 7:e01669-15(2015). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KUK32464.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LGFL01000004; KUK32464.1; -; Genomic_DNA. DR PATRIC; fig|1635288.3.peg.838; -. DR Proteomes; UP000053634; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000053634}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000053634}. FT DOMAIN 194 354 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 160 190 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 420 AA; 48284 MW; C1F40A625B30CAF0 CRC64; MKKGIICYLA TREDQEEINY DLAELRELLR NIGIEVCEVV VQRRRPNLLY LFGEGKIREV RELVKKEGIE AVVFNLELSP RQVRALEDLF GEGVEVWDRT QVILEIFRHR ARSREGKIQV ELARLSYLYP RILGLGGVLS RLGGGIGTRG PGETKLEVLR RAVRRRIHDL KEELAEVRKN RELLRKHRKE EGLPVVSLVG YTNAGKSTLL NALCRPKEKV LVEDRLFATL DPVSRRLRLP SGRIALLTDT VGFVKDLPQK LKAAFMATLE ELLEADLLLH VIDLASPCLD RQIEAVEEIL EEMKLYDRPI IKVYNKIDAY EGPLPADGLA VSALYGTNLD SLLTAVDEKL FREQEATLVL PYQHMGEFSR FREHLEVVEE QYLPEGVHLR VRGRSAELQR FLKRVEEKKQ KKTLYVNRLV // ID A0A101FRE6_9FIRM Unreviewed; 407 AA. AC A0A101FRE6; DT 13-APR-2016, integrated into UniProtKB/TrEMBL. DT 13-APR-2016, sequence version 1. DT 07-JUN-2017, entry version 9. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=XD69_0139 {ECO:0000313|EMBL:KUK41819.1}; OS Clostridia bacterium 62_21. OC Bacteria; Firmicutes; Clostridia. OX NCBI_TaxID=1635276 {ECO:0000313|EMBL:KUK41819.1, ECO:0000313|Proteomes:UP000067139}; RN [1] {ECO:0000313|EMBL:KUK41819.1, ECO:0000313|Proteomes:UP000067139} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=62_21 {ECO:0000313|EMBL:KUK41819.1}; RX PubMed=26787827; RA Hu P., Tom L., Singh A., Thomas B.C., Baker B.J., Piceno Y.M., RA Andersen G.L., Banfield J.F.; RT "Genome-Resolved Metagenomic Analysis Reveals Roles for Candidate RT Phyla and Other Microbial Community Members in Biogeochemical RT Transformations in Oil Reservoirs."; RL MBio 7:0-0(2016). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KUK41819.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LGFR01000007; KUK41819.1; -; Genomic_DNA. DR PATRIC; fig|1635276.4.peg.692; -. DR Proteomes; UP000067139; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000067139}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000067139}. FT DOMAIN 193 353 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 159 186 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 407 AA; 46141 MW; 99680B794C004588 CRC64; MKSGLICYLA VDEDDEEVRY DVVEMKELAL NIGIRVVDVV MQRRRPDPNY LLGEGKVLEV RERVYREQIA AVIFNRELSP RQIMRLEDLL EDVEVWDRTQ VILEIFRRRA QSREGKIQVE LARLTYLYPR MLGLGEVLSR LGGGIGTRGP GETKLEVLRR AVRRRIYLLQ RELQEVRQNR ELLRRHRSRA ALPVVSLVGY TNAGKSTLLN ALALSEHKVL VKDQLFATLD PVSRRIRLPS GREAILTDTV GFIKELPPKL KEAFAATLEE LLAADLLLHV IDLTSPCMET QVRAVESLLA ELKLCDRPLI KVYNKIDCYD GPLPADGVAV SALLGTNLPL LLQRIEAALA PWEEAVLTVP FARLGEVARA GDRLQILAEE YLPEGVRFSL RGDPVVLQKL ERRLKAE // ID A0A101FYF9_9CHLR Unreviewed; 438 AA. AC A0A101FYF9; DT 13-APR-2016, integrated into UniProtKB/TrEMBL. DT 13-APR-2016, sequence version 1. DT 07-JUN-2017, entry version 9. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=XD73_0326 {ECO:0000313|EMBL:KUK46800.1}; OS Anaerolinea thermophila. OC Bacteria; Chloroflexi; Anaerolineae; Anaerolineales; Anaerolineaceae; OC Anaerolinea. OX NCBI_TaxID=167964 {ECO:0000313|EMBL:KUK46800.1, ECO:0000313|Proteomes:UP000064249}; RN [1] {ECO:0000313|EMBL:KUK46800.1, ECO:0000313|Proteomes:UP000064249} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=46_16 {ECO:0000313|EMBL:KUK46800.1}; RX PubMed=26787827; RA Hu P., Tom L., Singh A., Thomas B.C., Baker B.J., Piceno Y.M., RA Andersen G.L., Banfield J.F.; RT "Genome-Resolved Metagenomic Analysis Reveals Roles for Candidate RT Phyla and Other Microbial Community Members in Biogeochemical RT Transformations in Oil Reservoirs."; RL MBio 7:0-0(2016). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KUK46800.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LGFU01000007; KUK46800.1; -; Genomic_DNA. DR PATRIC; fig|167964.4.peg.272; -. DR Proteomes; UP000064249; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000064249}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000064249}. FT DOMAIN 219 385 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 178 212 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 438 AA; 49091 MW; BDA8DBA2D3B43AA2 CRC64; MAKNLVLSTT PPREKAILVG IECATENSLL SMESSLEELY LLSDTAGVEV VGELTQKLDK PNPSTFIGSG KVNELKELVS VLQADMVIFD EELNPRNFRE LEEQLPEGTK VIDRTGLILD IFAQHANTSE GKLQVQLAQY EYLYPRLTRA WTHLVRQAGG GAGRTGSVGG VGLRGPGETQ LEVDRRKIRE QISALKNELD KVQDHRQQTR LKRKKANMPL IAMVGYTNAG KSTLLNRLTK ADVYVADQLF ATLDPTTRKL WLSDGKEVLI TDTVGFIQKL PHQLVAAFRA TMEDIVEADL LLHVVDISNP DAYAQWQSVI QTLIEIKADD IPMLTILNKC DKKVEESEIN RNFPQFQNAV RISAKTGLGM EDLQVRIKEN LYDATMSISV KIPYKQMNLI NLFHQSGLVE NVVNEVDYTS INGKIPARLY RLFTPYKV // ID A0A101GJ61_9BACT Unreviewed; 385 AA. AC A0A101GJ61; DT 13-APR-2016, integrated into UniProtKB/TrEMBL. DT 13-APR-2016, sequence version 1. DT 07-JUN-2017, entry version 9. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=XD81_0860 {ECO:0000313|EMBL:KUK59428.1}; OS Bacteroidetes bacterium 38_7. OC Bacteria; Bacteroidetes. OX NCBI_TaxID=1635292 {ECO:0000313|EMBL:KUK59428.1, ECO:0000313|Proteomes:UP000053999}; RN [1] {ECO:0000313|EMBL:KUK59428.1, ECO:0000313|Proteomes:UP000053999} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=38_7 {ECO:0000313|EMBL:KUK59428.1}; RA Hu P., Tom L., Singh A., Thomas B.C., Baker B.J., Piceno Y.M., RA Andersen G.L., Banfield J.F.; RT "Genome-resolved metagenomic analysis reveals roles for candidate RT phyla and other microbial community members in biogeochemical RT transformations in oil reservoirs."; RL MBio 7:e01669-15(2015). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KUK59428.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LGGC01000092; KUK59428.1; -; Genomic_DNA. DR PATRIC; fig|1635292.3.peg.726; -. DR Proteomes; UP000053999; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000053999}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000053999}. FT DOMAIN 199 372 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 385 AA; 44146 MW; 4E440F205EC4584E CRC64; MIESITKKES AVVVGLITPE QSVDKSREYL DELEFLADTA GAVVKKRFVQ RLPYPDPKTF VGKGKLNEIF NYVTDNHIDI IIFDDELSAS QLRNLSMELP CKILDRNNLI LDIFARRART ADAITQVELA QYEYMLPRLT RMWTHLEKQR GGIGLRGPGE KEIETDRRLI RKRIALLKSQ LEQIDQIKQT QRKSRSSLVR VALVGYTNVG KSTIMNLLSK SSVFAEDKLF ATLDTTVRRV VIDQTPFLLS DTVGFIRKLP HSLIESFKST LDEVREADIM LHVADVSHPA LEEQIDVVKQ TLMEIGAAEK IMITLLNKAD LLEQQTSFGF ISNSFPRWII DNNQPCLLIS ATKQQGTQDL KDMLVEEVRC IYRHRYPYKT RYDDL // ID A0A101H5C7_9CHLR Unreviewed; 443 AA. AC A0A101H5C7; DT 13-APR-2016, integrated into UniProtKB/TrEMBL. DT 13-APR-2016, sequence version 1. DT 07-JUN-2017, entry version 9. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=XD89_0303 {ECO:0000313|EMBL:KUK70700.1}; OS Anaerolineae bacterium 49_20. OC Bacteria; Chloroflexi; Anaerolineae; unclassified Anaerolineae. OX NCBI_TaxID=1641376 {ECO:0000313|EMBL:KUK70700.1, ECO:0000313|Proteomes:UP000053481}; RN [1] {ECO:0000313|EMBL:KUK70700.1, ECO:0000313|Proteomes:UP000053481} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=49_20 {ECO:0000313|EMBL:KUK70700.1}; RA Hu P., Tom L., Singh A., Thomas B.C., Baker B.J., Piceno Y.M., RA Andersen G.L., Banfield J.F.; RT "Genome-resolved metagenomic analysis reveals roles for candidate RT phyla and other microbial community members in biogeochemical RT transformations in oil reservoirs."; RL MBio 7:e01669-15(2015). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KUK70700.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LGGK01000015; KUK70700.1; -; Genomic_DNA. DR PATRIC; fig|1641376.4.peg.808; -. DR Proteomes; UP000053481; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000053481}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000053481}. FT DOMAIN 218 384 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 177 211 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 443 AA; 49040 MW; F0E219747375EEDA CRC64; MKENYSNLTE KETGILVGVQ VGSPTGQSLS LEDSLAELEL LAETAGVEVV GTLTQQLATI NPRTFIGSGK VEELKLLANE LGVQMVIFDD ELSPRHQREL ERVLGESIKV IDRTALILDI FALHARTYEG MLQVELAQLE YRLPRLTHAW IHLERQAGGG GGRAGGVGGV GLRGPGEKQL ELDRREIKAR ISRIKDELKK VQEQRSQHRA HRRKTNIPVV ALVGYTNAGK STLMNSLTHA GILVADQLFA TLDPTTRQLG LPNGQTILLT DTVGFIQKLP TQLIAAFRAT LEEITEADLL VHLVDAAHEN AIEQKRTVLK TLHDIGAGDL PILTVFNKID LLDESAREER RQIADPQTIF ISAKTGEGFD GLLAAIEKEL VSQYTQIRVL LPFEQGQLRS LFHERGKVQH TESTADGIRM SGYLPKELVS FFEPYQVKPE KNK // ID A0A101H9Z4_9FIRM Unreviewed; 408 AA. AC A0A101H9Z4; DT 13-APR-2016, integrated into UniProtKB/TrEMBL. DT 13-APR-2016, sequence version 1. DT 07-JUN-2017, entry version 10. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=XD91_1024 {ECO:0000313|EMBL:KUK72887.1}; OS Clostridiales bacterium 38_11. OC Bacteria; Firmicutes; Clostridia; Clostridiales. OX NCBI_TaxID=1641393 {ECO:0000313|EMBL:KUK72887.1, ECO:0000313|Proteomes:UP000053314}; RN [1] {ECO:0000313|EMBL:KUK72887.1, ECO:0000313|Proteomes:UP000053314} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=38_11 {ECO:0000313|EMBL:KUK72887.1}; RA Hu P., Tom L., Singh A., Thomas B.C., Baker B.J., Piceno Y.M., RA Andersen G.L., Banfield J.F.; RT "Genome-resolved metagenomic analysis reveals roles for candidate RT phyla and other microbial community members in biogeochemical RT transformations in oil reservoirs."; RL MBio 7:e01669-15(2015). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KUK72887.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LGGM01000038; KUK72887.1; -; Genomic_DNA. DR PATRIC; fig|1641393.3.peg.1291; -. DR Proteomes; UP000053314; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000053314}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000053314}. FT DOMAIN 194 360 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 153 180 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 408 AA; 46307 MW; 9EE836901170DD1F CRC64; MIEKCVIAGV KIKQSRTDID YEMEELKQLV EASGGIVEYS VVQEKDNYTA STYLGKGKVE EIRVLCEEVE ATLVVVNDEL TGSQINNLEK MLNVRVIDRT MLILDIFALR AKTKESKLQV ELAQLKYTMP RLKGKGIEMS KLGGGIGTRG PGEKKLETDR RHIENNIHEI EKQLKKAKTV REVNRKSRLK NNVPVIAVVG YTNAGKSTLI NSLLNLYGVE KDKEVFVYDM LFATLTTENR KLRILDKYEA VITDTVGFIS KLPTKLVESF KSTLEEINYS DIIIHLMDVT NKDLNVQKDT TDEILKEIKA TDIPVIEVYN KIDKTDISFD DSQGIYISAK TGLNIGKLVE RILLLLYGAS KTYTARLSYS DHAKLSFLEN NTNIIEREYL EAGINVVFET REKMYEKL // ID A0A101I599_9BACT Unreviewed; 377 AA. AC A0A101I599; DT 13-APR-2016, integrated into UniProtKB/TrEMBL. DT 13-APR-2016, sequence version 1. DT 07-JUN-2017, entry version 9. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=XE01_0141 {ECO:0000313|EMBL:KUK88958.1}; OS Synergistales bacterium 58_81. OC Bacteria; Synergistetes; Synergistia; Synergistales. OX NCBI_TaxID=1635274 {ECO:0000313|EMBL:KUK88958.1, ECO:0000313|Proteomes:UP000054873}; RN [1] {ECO:0000313|EMBL:KUK88958.1, ECO:0000313|Proteomes:UP000054873} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=58_81 {ECO:0000313|EMBL:KUK88958.1}; RA Hu P., Tom L., Singh A., Thomas B.C., Baker B.J., Piceno Y.M., RA Andersen G.L., Banfield J.F.; RT "Genome-resolved metagenomic analysis reveals roles for candidate RT phyla and other microbial community members in biogeochemical RT transformations in oil reservoirs."; RL MBio 7:e01669-15(2015). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KUK88958.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LGGV01000003; KUK88958.1; -; Genomic_DNA. DR PATRIC; fig|1635274.3.peg.115; -. DR Proteomes; UP000054873; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000054873}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000054873}. FT DOMAIN 200 370 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 159 193 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 377 AA; 40891 MW; 5787C02F3040D24B CRC64; MIDLRQLSSR KAFLVALDED DSLDVPGSLE ELSLLLGNLG ITTTGISIQR RSRPDPGSFI GSGKAELVGA EARDLGAGLI VVNGSLSPGQ AAALGRLTGL TVWDRPLVIM KIFEDRAQTG EAKLQIELAR CRYEIPFLKG LGLQMSRPGG GVGTRGPGET EFERHRRKLE RRIREINRKI EAIRERRKDQ RKHRARAGLA TVALTGYTNS GKSTLLRRLS GDTDLPVANK LFSTLDPFIR RVRLPGGAPV LFTDTVGFIR DLPPDLVAAF SATLEEVAAA DLVILVADQS SVRYEEDVEV VEEVLASIGA GTVPRIIALN KIDRIGPETA ETIRALAVRS GDRVIPISAL RGDNIPELLT VVEDMLFMGR GKECASC // ID A0A101ID99_9BACT Unreviewed; 96 AA. AC A0A101ID99; DT 13-APR-2016, integrated into UniProtKB/TrEMBL. DT 13-APR-2016, sequence version 1. DT 08-JUN-2016, entry version 3. DE SubName: Full=GTPase HflX {ECO:0000313|EMBL:KUK92640.1}; DE Flags: Fragment; GN ORFNames=XE05_1358 {ECO:0000313|EMBL:KUK92640.1}; OS Thermotogales bacterium 46_20. OC Bacteria; Thermotogae; Thermotogales. OX NCBI_TaxID=1635293 {ECO:0000313|EMBL:KUK92640.1, ECO:0000313|Proteomes:UP000054930}; RN [1] {ECO:0000313|EMBL:KUK92640.1, ECO:0000313|Proteomes:UP000054930} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=46_20 {ECO:0000313|EMBL:KUK92640.1}; RA Hu P., Tom L., Singh A., Thomas B.C., Baker B.J., Piceno Y.M., RA Andersen G.L., Banfield J.F.; RT "Genome-resolved metagenomic analysis reveals roles for candidate RT phyla and other microbial community members in biogeochemical RT transformations in oil reservoirs."; RL MBio 7:e01669-15(2015). CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KUK92640.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LGGZ01000098; KUK92640.1; -; Genomic_DNA. DR Proteomes; UP000054930; Unassembled WGS sequence. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF13167; GTP-bdg_N; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000054930}; KW Reference proteome {ECO:0000313|Proteomes:UP000054930}. FT DOMAIN 15 96 GTP-bdg_N. {ECO:0000259|Pfam:PF13167}. FT NON_TER 96 96 {ECO:0000313|EMBL:KUK92640.1}. SQ SEQUENCE 96 AA; 10266 MW; 9F24E2F267430119 CRC64; MLVGYLKAES NALSSSIEEM EMLSRTAGFL IAETVTQCID SPGYVTYLGS GKIESVASLI SKSNAEAVIT RHNLKPAQVS TLEKTLGTSV LDRTQL // ID A0A101IMX5_9CHLR Unreviewed; 444 AA. AC A0A101IMX5; DT 13-APR-2016, integrated into UniProtKB/TrEMBL. DT 13-APR-2016, sequence version 1. DT 07-JUN-2017, entry version 9. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=XE06_0093 {ECO:0000313|EMBL:KUK98147.1}; OS Anaerolinaceae bacterium 46_22. OC Bacteria; Chloroflexi; Anaerolineae; Anaerolineales; Anaerolineaceae. OX NCBI_TaxID=1635294 {ECO:0000313|EMBL:KUK98147.1, ECO:0000313|Proteomes:UP000054480}; RN [1] {ECO:0000313|EMBL:KUK98147.1, ECO:0000313|Proteomes:UP000054480} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=46_22 {ECO:0000313|EMBL:KUK98147.1}; RA Hu P., Tom L., Singh A., Thomas B.C., Baker B.J., Piceno Y.M., RA Andersen G.L., Banfield J.F.; RT "Genome-resolved metagenomic analysis reveals roles for candidate RT phyla and other microbial community members in biogeochemical RT transformations in oil reservoirs."; RL MBio 7:e01669-15(2015). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KUK98147.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LGHA01000005; KUK98147.1; -; Genomic_DNA. DR PATRIC; fig|1635294.3.peg.612; -. DR Proteomes; UP000054480; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000054480}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000054480}. FT DOMAIN 217 383 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 183 210 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 444 AA; 49182 MW; 46BA2EA3767E1321 CRC64; MTKLIDTTAP QEKALLIGVS LFSDKNLLSL EDSLDELSLL AETAGVEVME TITQNLNTPN PKTFIGSGKV EEVKILAQEL GADMVIFDNV LSPRHQRELE EALGESIRVI DRTALILDIF AQHANTSEGG LQVELAQYEY RLPRLTRAWT HLARQAGGGG GRAGGVGGVG LRGPGETQLE VDRRIISRRI EFLKEELEKV RAHRSRYRQR RKKTRIPVIA LVGYTNAGKS TLLNRLASSD VYVADQLFAT LDPTTRRVEL PGGQAVLFTD TVGFIQKLPT ELVAAFRATL EEISDADVLL HVVDITHRNA SAQAKSVQET LIDIGAGDIP MVTAFNKIDL LKDPEAAVDN LEEFSGTFPI SARTGQGIDA LLSAIESELF ETYIELDVFI PYQEGQLISK LHEFGQVHEV ENLEEGTRIK GLIPRRFMHQ FEPYFMPDPD DDEL // ID A0A101K375_9BRAD Unreviewed; 449 AA. AC A0A101K375; DT 13-APR-2016, integrated into UniProtKB/TrEMBL. DT 13-APR-2016, sequence version 1. DT 07-JUN-2017, entry version 9. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=DK26_05300 {ECO:0000313|EMBL:KUL96678.1}; OS Bosea sp. WAO. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Bradyrhizobiaceae; Bosea. OX NCBI_TaxID=406341 {ECO:0000313|EMBL:KUL96678.1, ECO:0000313|Proteomes:UP000053994}; RN [1] {ECO:0000313|EMBL:KUL96678.1, ECO:0000313|Proteomes:UP000053994} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=WAO {ECO:0000313|EMBL:KUL96678.1, RC ECO:0000313|Proteomes:UP000053994}; RA Xiang T., Song Y., Huang L., Wang B., Wu P.; RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:KUL96678.1, ECO:0000313|Proteomes:UP000053994} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=WAO {ECO:0000313|EMBL:KUL96678.1, RC ECO:0000313|Proteomes:UP000053994}; RA Walczak A.B., Yee N., Young L.Y.; RT "Draft genome sequence of Bosea species strain WAO an arsenite and RT sulfide oxidizer isolated from a pyrite rock outcrop in New Jersey."; RL Submitted (JAN-2016) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KUL96678.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JXTJ01000004; KUL96678.1; -; Genomic_DNA. DR EnsemblBacteria; KUL96678; KUL96678; DK26_05300. DR PATRIC; fig|406341.6.peg.3004; -. DR Proteomes; UP000053994; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000053994}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000053994}. FT DOMAIN 215 389 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 449 AA; 49443 MW; 701E452783324975 CRC64; MDAAEHAVAA GTRAFVIGPY LARQAPGRAI AADENQRSYA ARLDEAIGLA GAIDLQVVEA IQVMLSALRP ATYLGKGKVE ELAERVKLEE IGLVVMDCAL SPVQQRNLEK AFGCKVIDRT GLILEIFGRR ARTREGTLQV ELAHLNYQKS RLVRSWTHLE RQRGGFGFLG GPGETQIEAD RRVIQERMTK IERDLETVKR TRSLHRASRK RVPYPIVALV GYTNAGKSTL FNRLTSAEVL AQDMLFATLD PTARALKLPH GAKILLSDTV GFISDLPTQL IAAFRATLED AIEADVLLHV RDVSHEDTQA QATDVRAILR DLGIDPEDGR RVIEVWNKAD LLEDAERERQ AALAELKPEA TRPVLVSALT GEGMARLTDA IEARIAKSRP VYRLVLAPGD GKSLAWLHAN GEILTRSDGE DGALSLLVRL PPEREGAFTA RFPEAERER // ID A0A101KPU1_RHILI Unreviewed; 462 AA. AC A0A101KPU1; DT 13-APR-2016, integrated into UniProtKB/TrEMBL. DT 13-APR-2016, sequence version 1. DT 05-JUL-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=AU467_05965 {ECO:0000313|EMBL:KUM24662.1}; OS Rhizobium loti (Mesorhizobium loti). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Phyllobacteriaceae; Mesorhizobium. OX NCBI_TaxID=381 {ECO:0000313|EMBL:KUM24662.1, ECO:0000313|Proteomes:UP000053176}; RN [1] {ECO:0000313|EMBL:KUM24662.1, ECO:0000313|Proteomes:UP000053176} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=UFLA 01-765 {ECO:0000313|EMBL:KUM24662.1, RC ECO:0000313|Proteomes:UP000053176}; RA Rangel W.M., Thijs S., Longatti S.M., Moreira F.M., Weyens N., RA Vangronsveld J., Van Hamme J.D., Bottos E.M., Rineau F.; RT "Draft genome sequence of Mesorhizobium sp. UFLA 01-765, a RT multitolerant efficient symbiont and plant-growth promoting strain RT isolated from Zn-mining soil using Leucaena leucocephala as a trap RT plant."; RL Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KUM24662.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LPWA01000131; KUM24662.1; -; Genomic_DNA. DR RefSeq; WP_059188552.1; NZ_LPWA01000131.1. DR EnsemblBacteria; KUM24662; KUM24662; AU467_05965. DR Proteomes; UP000053176; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000053176}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000053176}. FT DOMAIN 231 403 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 462 AA; 50591 MW; 5F66B7575B487279 CRC64; MAREKDADRS VRGKQGHQLG PEAKDPTRAV VIVPVLTRLP RSDDDSSRPR LSRSADARHD EAVGLASAID LNPVHTAVVT VTDPRPATLL GSGKVAEFAD IVKERKAELV IVDHPLTPVQ QRNLEKELNA KVLDRTGLIL EIFGERARTK EGTLQVELAH LNYQKGRLVR SWTHLERQRG GAGFLGGPGE TQIESDRRIL QDKITKLKHE LETVRRTRDL HRAKRKKVPF PVVAIVGYTN AGKSTLFNRM TGAGVLAEDM LFATLDPTLR RVRLPHGTPI ILSDTVGFIS DLPTHLVAAF RATLEEVVEA DLVLHLRDIS DPDTAAQAED VERILGDLGV DAADTGRVIE VWNKIDLLDE GNRERLLAES AGGKAPPIAI SAATGEGIDA LKALIETRVS GELETMTVTL SPAELGQVDW LYRNGDVVSR ADNEDGSVTI SLTATHSARQ EIESRLHRRN HG // ID A0A101NWI9_9ACTN Unreviewed; 497 AA. AC A0A101NWI9; DT 13-APR-2016, integrated into UniProtKB/TrEMBL. DT 13-APR-2016, sequence version 1. DT 07-JUN-2017, entry version 12. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=AQI95_34165 {ECO:0000313|EMBL:KUN00558.1}; OS Streptomyces yokosukanensis. OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae; OC Streptomyces. OX NCBI_TaxID=67386 {ECO:0000313|EMBL:KUN00558.1, ECO:0000313|Proteomes:UP000053127}; RN [1] {ECO:0000313|EMBL:KUN00558.1, ECO:0000313|Proteomes:UP000053127} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 40224 {ECO:0000313|EMBL:KUN00558.1, RC ECO:0000313|Proteomes:UP000053127}; RA Ruckert C., Winkler A., Kalinowski J., Kampfer P., Glaeser S.; RT "Draft genome sequence of Streptomyces yokosukanensis DSM 40224, type RT strain for the species Streptomyces yokosukanensis."; RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KUN00558.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LMWN01000048; KUN00558.1; -; Genomic_DNA. DR RefSeq; WP_067133125.1; NZ_KQ948222.1. DR EnsemblBacteria; KUN00558; KUN00558; AQI95_34165. DR Proteomes; UP000053127; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000313|EMBL:KUN00558.1}; KW Complete proteome {ECO:0000313|Proteomes:UP000053127}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900, KW ECO:0000313|EMBL:KUN00558.1}. FT DOMAIN 275 440 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 497 AA; 54324 MW; 4C654E2D650ADAFB CRC64; MTSSSSPSQD TQRLAHAYPE GLRADALMEE DVAWSYEIDG DRDGDQFDRS ERAALRRVVG LSTELEDVTE VEYRQLRLER VVLVGVWTTG TAQDADNSLA ELAALAETAG ALVLDGVVQR RDKPDAATYI GSGKALELRD IVVESGADTV ICDGELSPGQ LIQLEDVVKV KVIDRTALIL DIFAQHAKSR EGKAQVALAQ MQYMLPRLRG WGQSLSRQMG GGKGGGLATR GPGETKIETD RRRIREKMAK MRREIAEMKT GREIKRQERR RNKVPSVAIA GYTNAGKSSL LNRLTGAGVL VENALFATLD PTVRRAETPS GRLYTLADTV GFVRHLPHHL VEAFRSTMEE VGDADLIVHV VDGSHPVPEE QLAAVREVIR DVGATDVPEI VVINKADAAD PLVLQRLLRV EKRSIVVSAR TGQGIDELLA LIDNELPRPS VEIEALVPYT HGRLVARAHT EGEVISEEHT AEGTLLKVRV HEELAVDLAP YTPVPAV // ID A0A101QNU8_9ACTN Unreviewed; 497 AA. AC A0A101QNU8; DT 13-APR-2016, integrated into UniProtKB/TrEMBL. DT 13-APR-2016, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=AQJ30_35015 {ECO:0000313|EMBL:KUN33156.1}; OS Streptomyces longwoodensis. OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae; OC Streptomyces. OX NCBI_TaxID=68231 {ECO:0000313|EMBL:KUN33156.1, ECO:0000313|Proteomes:UP000053271}; RN [1] {ECO:0000313|EMBL:KUN33156.1, ECO:0000313|Proteomes:UP000053271} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 41677 {ECO:0000313|EMBL:KUN33156.1, RC ECO:0000313|Proteomes:UP000053271}; RA Ruckert C., Winkler A., Kalinowski J., Kampfer P., Glaeser S.; RT "Draft genome sequence of Streptomyces longwoodensis DSM 41677, type RT strain for the species Streptomyces longwoodensis."; RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KUN33156.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LMWS01000058; KUN33156.1; -; Genomic_DNA. DR RefSeq; WP_067241920.1; NZ_KQ948567.1. DR EnsemblBacteria; KUN33156; KUN33156; AQJ30_35015. DR Proteomes; UP000053271; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 2. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000313|EMBL:KUN33156.1}; KW Complete proteome {ECO:0000313|Proteomes:UP000053271}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900, KW ECO:0000313|EMBL:KUN33156.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000053271}. FT DOMAIN 275 440 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 497 AA; 54142 MW; 71C6783B01063096 CRC64; MTSSSSPSQD TKRFAHAYPE GLRADALMEE DVAWSHEIDG ERDGDQFDRS ERAALRRVAG LSTELEDVTE VEYRQLRLER VVLVGVWTSG TVQDADNSLA ELAALAETAG ALVLDGVIQR RDKPDAATYI GSGKAGELRD IVLETGADTV ICDGELSPGQ LIHLEDVVKV KVIDRTALIL DIFAQHAKSR EGKAQVALAQ MQYMLPRLRG WGQSLSRQMG GGKGGGLATR GPGETKIETD RRRIREKMAK MRREIAEMKT GREVQRQVRR RNKVPSVAIA GYTNAGKSSL LNRLTGAGVL VENALFATLD PTVRRAETPS GRLYTLADTV GFVRHLPHHL VEAFRSTMEE VGDADLILHV VDGSHPNPEE QLLAVREVIR DVGATGVPEI VVINKADAAD PLTLQRLLRV EKRSIAVSAR TGQGIAELLG LIDNELPRPS VEIEALVPYT HGKLVARAHT EGEVISEEHT AEGTLLKARV HEELAADLAP YVPAQAL // ID A0A101SKM5_9ACTN Unreviewed; 497 AA. AC A0A101SKM5; DT 13-APR-2016, integrated into UniProtKB/TrEMBL. DT 13-APR-2016, sequence version 1. DT 30-AUG-2017, entry version 16. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=AQJ64_42065 {ECO:0000313|EMBL:KUN75473.1}; OS Streptomyces griseoruber. OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae; OC Streptomyces. OX NCBI_TaxID=1943 {ECO:0000313|EMBL:KUN75473.1, ECO:0000313|Proteomes:UP000052982}; RN [1] {ECO:0000313|EMBL:KUN75473.1, ECO:0000313|Proteomes:UP000052982} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 40281 {ECO:0000313|EMBL:KUN75473.1, RC ECO:0000313|Proteomes:UP000052982}; RA Ruckert C., Winkler A., Kalinowski J., Kampfer P., Glaeser S.; RT "Draft genome sequence of Streptomyces griseoruber DSM 40281, type RT strain for the species Streptomyces griseoruber."; RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KUN75473.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LMWW01000078; KUN75473.1; -; Genomic_DNA. DR RefSeq; WP_055637346.1; NZ_LIQS01000488.1. DR EnsemblBacteria; KUN75473; KUN75473; AQJ64_42065. DR GeneID; 32312927; -. DR Proteomes; UP000052982; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 2. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000313|EMBL:KUN75473.1}; KW Complete proteome {ECO:0000313|Proteomes:UP000052982}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900, KW ECO:0000313|EMBL:KUN75473.1}. FT DOMAIN 275 440 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 497 AA; 54228 MW; 3940DCFAF7D13A53 CRC64; MTSSSSSSQD TKRFAHAYPE GLRADALMEE DVAWSHEIDG ERDGDQFDRS ERAALRRVAG LSTELEDVTE VEYRQLRLER VVLVGVWTSG TAQDADNSLA ELAALAETAG ALVLDGVIQR RDKPDAATYI GSGKADELRD IVIETGADTV ICDGELSPGQ LIHLEDVVKV KVIDRTALIL DIFAQHAKSR EGKAQVALAQ MQYMLPRLRG WGQSLSRQMG GGKGGGLATR GPGETKIETD RRRIREKMAK MRREIAEMKT GREIKRQERK RHKVPSVAIA GYTNAGKSSL LNRLTGAGVL VENALFATLD PTVRRAETPS GRLYTLADTV GFVRHLPHHL VEAFRSTMEE VGESDLILHV VDGSHPNPEE QLAAVREVVH DVGATQVPEI VVINKADAAD PLTLQRLMRI EKRSIAVSAR TGQGIEELLA LIDNELPRPS VEIEALVPYT HGKLVARAHT EGEVISAEHT ADGTLLKARV HEELAADLAP YVPAPLA // ID A0A101SRK3_9ACTN Unreviewed; 495 AA. AC A0A101SRK3; DT 13-APR-2016, integrated into UniProtKB/TrEMBL. DT 13-APR-2016, sequence version 1. DT 07-JUN-2017, entry version 10. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=AQJ66_30220 {ECO:0000313|EMBL:KUN78920.1}; OS Streptomyces bungoensis. OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae; OC Streptomyces. OX NCBI_TaxID=285568 {ECO:0000313|EMBL:KUN78920.1, ECO:0000313|Proteomes:UP000053024}; RN [1] {ECO:0000313|EMBL:KUN78920.1, ECO:0000313|Proteomes:UP000053024} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 41781 {ECO:0000313|EMBL:KUN78920.1, RC ECO:0000313|Proteomes:UP000053024}; RA Ruckert C., Winkler A., Kalinowski J., Kampfer P., Glaeser S.; RT "Draft genome sequence of Streptomyces bungoensis DSM 41781, type RT strain for the species Streptomyces bungoensis."; RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KUN78920.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LMWX01000056; KUN78920.1; -; Genomic_DNA. DR RefSeq; WP_061928276.1; NZ_KQ948870.1. DR EnsemblBacteria; KUN78920; KUN78920; AQJ66_30220. DR Proteomes; UP000053024; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 2. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000313|EMBL:KUN78920.1}; KW Complete proteome {ECO:0000313|Proteomes:UP000053024}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900, KW ECO:0000313|EMBL:KUN78920.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000053024}. FT DOMAIN 274 439 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 495 AA; 54028 MW; 8C3201D79BEF7994 CRC64; MTSSSSPSQD TKRLAHSHPE ALRADALMEE DVAWSFEIDG ERDGDQFDRS ERAALRRVAG LSTELEDVTE VEYRQLRLER VVLVGVWTTG TSADAENSLA ELAALAETAG ALVLDGVIQR RDKPDAATYI GSGKAAELRD VVLETGADTV ICDGELSPGQ LIQLEDVVKV KVIDRTALIL DIFAQHAKSR EGKAQVALAQ MQYMLPRLRG WGQSLSRQMG GGRGGLATRG PGETKIETDR RRIREKMAKM RREIADMKTG REVKRQERRR HKVPSVAIAG YTNAGKSSLL NRLTGAGVLV ENALFATLDP TVRRAETPTG RVYTLADTVG FVRHLPHHLV EAFRSTMEEV GDSDLILHVV DGSHPVPEEQ LAAVREVIRD VGATDVPEIV VINKADAADP LVLQRLLRIE PRSIAVSART GRGIDELLAL IDNELPRPSV EIEALVPYTH GKLVARAHTE GEVLSEEHTA EGTLLKARVH EELAAELAPY TPASA // ID A0A101VI90_9PROT Unreviewed; 449 AA. AC A0A101VI90; DT 13-APR-2016, integrated into UniProtKB/TrEMBL. DT 13-APR-2016, sequence version 1. DT 10-MAY-2017, entry version 9. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=APF80_11495 {ECO:0000313|EMBL:KUO55217.1}; OS Alphaproteobacteria bacterium BRH_c36. OC Bacteria; Proteobacteria; Alphaproteobacteria. OX NCBI_TaxID=1734406 {ECO:0000313|EMBL:KUO55217.1, ECO:0000313|Proteomes:UP000053382}; RN [1] {ECO:0000313|EMBL:KUO55217.1, ECO:0000313|Proteomes:UP000053382} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BRH_c36 {ECO:0000313|EMBL:KUO55217.1}; RA Bagnoud A., Chourey K., Hettich R.L., De Bruijn I., Andersson A.F., RA Leupin O.X., Schwyn B., Bernier-Latmani R.; RT "Microbial metabolic network in the subsurface."; RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KUO55217.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LOEV01000202; KUO55217.1; -; Genomic_DNA. DR Proteomes; UP000053382; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000053382}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000053382}. FT DOMAIN 215 388 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 449 AA; 49473 MW; 34E4C3191B5BF1DE CRC64; MKRSGTLSRA LVLVPILTRT GAGDASSASH ATHSPLERLE EAIGLARAIE LEICDARTVN VASPKPGTLF GTGKVEELGH LVTDHEADLV VIDHAVTPVQ QRNLEMAWKC KVLDRTGLIL EIFGERARTR EGRLQVELAH LSYQKGRLVR AWTHLERQRG GGGGGASFVG GPGEAQIELD RRMIQNRIDA IRRDLSQVVK TRELHRAGRR KVPYPVVAIV GYTNAGKSTL FNRVTGAEVL AQDQVFATLD PTMREVKLPS GRRIILSDTV GFISNLPTML VAAFRATLEE VVEADLILHV RDISHAETEA QRRDVENVLQ GLDVDVKTAD RAMLEVWNKI DRLSPVTREE ALSAARFDDQ HPVCVSALTG EGVVELLAAI DESLGVDDTY LSLVLPPNEG QLLAWLHENA EVLQRTVVDE GDTHIRVRIA AEKRGRLLAQ LQTRQLRVE // ID A0A101VSG6_9BACT Unreviewed; 420 AA. AC A0A101VSG6; DT 13-APR-2016, integrated into UniProtKB/TrEMBL. DT 13-APR-2016, sequence version 1. DT 12-APR-2017, entry version 8. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=APF79_09345 {ECO:0000313|EMBL:KUO59967.1}; OS bacterium BRH_c32. OC Bacteria. OX NCBI_TaxID=1734400 {ECO:0000313|EMBL:KUO59967.1, ECO:0000313|Proteomes:UP000053092}; RN [1] {ECO:0000313|EMBL:KUO59967.1, ECO:0000313|Proteomes:UP000053092} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BRH_c32 {ECO:0000313|EMBL:KUO59967.1}; RA Bagnoud A., Chourey K., Hettich R.L., De Bruijn I., Andersson A.F., RA Leupin O.X., Schwyn B., Bernier-Latmani R.; RT "Microbial metabolic network in the subsurface."; RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KUO59967.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LOEU01000032; KUO59967.1; -; Genomic_DNA. DR Proteomes; UP000053092; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000053092}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000053092}. FT DOMAIN 200 326 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 420 AA; 47851 MW; 03F3F82EB04A80C1 CRC64; MIDIENKETE KAILVGVSKG LNTRRVTEEH LEELELLADT AGAETVIKFF QDRDSYDPAY FIGKGKAEEI LEYAKENNIN LVIFDDDLNP TQLRNLEKLF ERKILDRSAL ILDIFASHAK TKEAKTQVEL AQLQYMLPRL TRAWTHLSKQ LGGIGTKGPG ETQIETDRRI IRTRISKLKD TLKKIEAQHV TKSAGRQDLI NVSLVGYTNA GKSTLLNQLT GADVLAEDKL FATLDSTTRS FDLDKNKKVL LSDTVGFIRK LPPHLVASFK TTLNVVREAD LILHVIDVSN EFYEEHIEVV DETMKSLGSE TKPQIKVFNK IDLLEDKQKL EFISQHYKDS VFVSSMRGFG INSLIEKISD FYEMNYIVHT IHLKQTQGKL ISAIYELADI LESVYEEDSI VIKYRTSKEM HNKILSMLQN // ID A0A101W6F4_9FLAO Unreviewed; 403 AA. AC A0A101W6F4; DT 13-APR-2016, integrated into UniProtKB/TrEMBL. DT 13-APR-2016, sequence version 1. DT 12-APR-2017, entry version 8. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=APF83_05435 {ECO:0000313|EMBL:KUO67647.1}; OS Lutibacter sp. BRH_c52. OC Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales; OC Flavobacteriaceae; Lutibacter. OX NCBI_TaxID=1734397 {ECO:0000313|EMBL:KUO67647.1, ECO:0000313|Proteomes:UP000054346}; RN [1] {ECO:0000313|EMBL:KUO67647.1, ECO:0000313|Proteomes:UP000054346} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BRH_c52 {ECO:0000313|EMBL:KUO67647.1}; RA Bagnoud A., Chourey K., Hettich R.L., De Bruijn I., Andersson A.F., RA Leupin O.X., Schwyn B., Bernier-Latmani R.; RT "Microbial metabolic network in the subsurface."; RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KUO67647.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LOEY01000034; KUO67647.1; -; Genomic_DNA. DR Proteomes; UP000054346; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000054346}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000054346}. FT DOMAIN 200 385 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 403 AA; 46433 MW; D855F2A147366803 CRC64; MTEIIEDNIE KVVLIGLITQ YQNEEKCNEY LDELEFLTLT AGGIAVKRFV QKLETPNPKT FIGTGKLEDV RQYIEANNVG TVIFDDELKS SQLRNIEKVL NIKVLDRTNL ILDIFAARAQ TSYARTQVEL AQCEYLLPRL TRLWTHLERQ KGGIGLRGPG ETEIETDRRI IRDKISLLKK KLEIVDKQMA VQRKNRGKMV RVALVGYTNV GKSTLMNVVS KSEVFAENKL FATLDTTVRK VVIKNLPFLL TDTVGFIRKL PTQLIESFKS TLDEVREADL LLHVVDISHP NFEDHMASVN KTLAEIGSAD KPTIIVFNKI DAFTHQTIDD DDLVTEKTEM HFSLEEWKKT WMNRLDNNCV FISALNKENM EAFKEKVFDE VKKIHITRFP YNDLLYEEFE EES // ID A0A101WGG4_9FIRM Unreviewed; 588 AA. AC A0A101WGG4; DT 13-APR-2016, integrated into UniProtKB/TrEMBL. DT 13-APR-2016, sequence version 1. DT 12-APR-2017, entry version 8. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=APF77_10510 {ECO:0000313|EMBL:KUO72597.1}; OS Clostridia bacterium BRH_c25. OC Bacteria; Firmicutes; Clostridia. OX NCBI_TaxID=1734399 {ECO:0000313|EMBL:KUO72597.1, ECO:0000313|Proteomes:UP000057710}; RN [1] {ECO:0000313|EMBL:KUO72597.1, ECO:0000313|Proteomes:UP000057710} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BRH_c25 {ECO:0000313|EMBL:KUO72597.1}; RA Bagnoud A., Chourey K., Hettich R.L., De Bruijn I., Andersson A.F., RA Leupin O.X., Schwyn B., Bernier-Latmani R.; RT "Microbial metabolic network in the subsurface."; RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KUO72597.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LOES01000147; KUO72597.1; -; Genomic_DNA. DR Proteomes; UP000057710; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000057710}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000057710}. FT DOMAIN 369 534 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 328 362 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 588 AA; 65214 MW; 31F739ACD6A8AAE5 CRC64; MDNTAGIKKS LLKRLQDLKE LTVEKYQLIS EEIIAEICDI TEETGKEIAV YIDRKGAVLD VSIGDENTVI LKDYNNRRSE ESLSGVRCVH THPNGSGGLS EVDLSALKRM KFDIMAAVGV ADGIMTNGSI AFLGIDGEKQ LQTIVMGPYS MERLMKVNVL DVINEAEAGI KDIRKAGKEV DSDIERAVLV GIEDEEALDE LRELLKTAGG YEVGRMVQSK DKKDTAIFIG KGKLKELMLL SQAMDASLVV FDEELSGAQI RNLEEALGLK VIDRTQLILD IFAQRARSRE GKLQVELAQL KYMMPRLIGM GQQMSRTGGG IGTRGPGEKK LEVDRRRIRN RLNDLEKDLK EVKKQRDLQR EGRVSRKVFQ ICLVGYTNAG KSTLLNNLAE ADIYARDQLF ATLDPTTRKV TLNNSKEVLI TDTVGFIRKL PHDLVEAFKS TLEEVLYADL LIHVVDGSNP DCETQVSVVA DVLAELGADD KDTIMAINKI DKCPGKFAAA EYKDMENVVH ISASERIGLS QLLDLIEKYA GLQSKTVELL IPYAEGSVVS TIYGSANEVI EEQYREDGIY IKAEVDEISY GRLTKYAI // ID A0A101WP11_9FIRM Unreviewed; 534 AA. AC A0A101WP11; DT 13-APR-2016, integrated into UniProtKB/TrEMBL. DT 13-APR-2016, sequence version 1. DT 07-JUN-2017, entry version 9. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=APF81_16770 {ECO:0000313|EMBL:KUO76586.1}; OS Desulfosporosinus sp. BRH_c37. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Peptococcaceae; OC Desulfosporosinus. OX NCBI_TaxID=1734396 {ECO:0000313|EMBL:KUO76586.1, ECO:0000313|Proteomes:UP000053148}; RN [1] {ECO:0000313|EMBL:KUO76586.1, ECO:0000313|Proteomes:UP000053148} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BRH_c37 {ECO:0000313|EMBL:KUO76586.1}; RA Bagnoud A., Chourey K., Hettich R.L., De Bruijn I., Andersson A.F., RA Leupin O.X., Schwyn B., Bernier-Latmani R.; RT "Microbial metabolic network in the subsurface."; RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KUO76586.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LOEW01000123; KUO76586.1; -; Genomic_DNA. DR Proteomes; UP000053148; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000053148}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000053148}. FT DOMAIN 365 534 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 324 351 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 534 AA; 59202 MW; ED581B1B0E0754E3 CRC64; MDISGELSGI RASQLQELKD LSEIKTERSE LIHPEILGEL IRLTQLWNRE IAVYLSRPGT LLAAAVGRHA AVTLPPIKGR SIGKHLRCIH THPNGDSRLS PLDHSALLSL QLESMASVGV RDGLLNGIQI AYRTGENDSF IVNLSSKNWQ SFDYNDSLSS FSKGTTNINE TAAGKERAFL IALLESDQDD NEDLTELREL VRSAGVDVVG QLVQLRRYGQ SRSYLGSGKI EELVHRLQET KANVVICDDE LTPTQLRTLE TETGLKVLDR TGLILDIFAQ RAQSREGKLQ VELAQLKHLL PYLTGQGQAL SKLGAGVGSR GPGETKLELD RRRMRDRISQ LEKELKLVLQ HRDVQRRQRS RSGLPTIALV GYTNAGKTTF LKVAMEQAGN RSDIPSGENK LFATLDPLIR SIKVNSSLEI LLSDTVGFIQ KLPTQLLRAF LATLEEVQQA DILLHVVDAS HPQALQHAET VNEVLKQLGC EEKPMLTLLN KVDKVLSEDD LSELVERLPH PIELSLTRGD SLKPVWNQLS SLLT // ID A0A101WZA5_9CREN Unreviewed; 362 AA. AC A0A101WZA5; DT 13-APR-2016, integrated into UniProtKB/TrEMBL. DT 13-APR-2016, sequence version 1. DT 30-AUG-2017, entry version 12. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=AT718_06530 {ECO:0000313|EMBL:KUO81867.1}; OS Vulcanisaeta sp. JCHS_4. OC Archaea; Crenarchaeota; Thermoprotei; Thermoproteales; OC Thermoproteaceae; Vulcanisaeta. OX NCBI_TaxID=1714253 {ECO:0000313|EMBL:KUO81867.1, ECO:0000313|Proteomes:UP000054689}; RN [1] {ECO:0000313|EMBL:KUO81867.1, ECO:0000313|Proteomes:UP000054689} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Jay Z.J., Beam J.P., Kozubal M.A., Jennings R.D.E., Rusch D.B., RA Inskeep W.P.; RT "The distribution, diversity and function of predominant RT Thermoproteales in high-temperature environments of Yellowstone RT National Park."; RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KUO81867.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LOCE01000024; KUO81867.1; -; Genomic_DNA. DR EnsemblBacteria; KUO81867; KUO81867; AT718_06530. DR Proteomes; UP000054689; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000054689}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000054689}. FT DOMAIN 187 357 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 362 AA; 41742 MW; 9FD0EF5940BFDF8D CRC64; MGSKAILLVA DDIEDGKIRE FKSLAEAGDY EVLDTIIQRR RPDPRYYLGL GKLGEVEEII RSYEPDTVIT YHQLNPVQYV NLGRRLRIRV MDRVWLILEI FERRAGSKEA KLQIELTRLR LEIPRVREFI RLAKLGEQIG FYGGGEYAIE TYYRHMVRRA SHIRKELEKI RERRASLVMR RRDYGLPQVA LTGYTSAGKT TLFNRLAREN KYVDGKPFAT LDTYSRLAYF NGINAMLTDT IGFIDDLPPL LIESFYATIA EVLNSDLVLF VIDMSDEYSE FHRKFTSSLR IFMDLGVPKG KILPVLNKVD AANDSYISNK VSLVKQEFNE YVVISAKLGI GIDDLRNTIR NRLERLGLVG KD // ID A0A101X7H7_9CREN Unreviewed; 409 AA. AC A0A101X7H7; DT 13-APR-2016, integrated into UniProtKB/TrEMBL. DT 13-APR-2016, sequence version 1. DT 07-JUN-2017, entry version 9. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=AT709_00615 {ECO:0000313|EMBL:KUO86232.1}; OS Caldivirga sp. MG_3. OC Archaea; Crenarchaeota; Thermoprotei; Thermoproteales; OC Thermoproteaceae; Caldivirga. OX NCBI_TaxID=1714256 {ECO:0000313|EMBL:KUO86232.1, ECO:0000313|Proteomes:UP000054806}; RN [1] {ECO:0000313|EMBL:KUO86232.1, ECO:0000313|Proteomes:UP000054806} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Jay Z.J., Beam J.P., Kozubal M.A., Jennings R.D.E., Rusch D.B., RA Inskeep W.P.; RT "The distribution, diversity and function of predominant RT Thermoproteales in high-temperature environments of Yellowstone RT National Park."; RL Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KUO86232.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LOCB01000014; KUO86232.1; -; Genomic_DNA. DR EnsemblBacteria; KUO86232; KUO86232; AT709_00615. DR Proteomes; UP000054806; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000054806}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}. FT DOMAIN 187 356 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 409 AA; 45833 MW; 6E704AEEFC47BFD8 CRC64; MGKVAILVYV DPNPVRSKVD EFRMLAEVAG YSIKDVVVQR RAPDSRFYVG AGKLREIKGL INDGVGYLIA YHQLKPSQSF NLSRELGINV MDRVKLILEI FDSRAGDAEA KLQIRLAELR YTLPMIKEYI RLSKRGEQIG FHGLGEYGAE TYYKHALRQI ASIRRRLQAI KAMRDVHIVK RRDKGIPEVV LTGYTMAGKT TLFNRLTGEG KYIDGKAFAT LSTYSRLVNF NGKYAVVTDT VGFIDDLPPV LIESFYSTIR EIAYADLILL LIDSSDPLPE VRRKLSSSVT ILNNVGVPMS KVIPVFNKID QVNEYSTLAN LASEFNLSTP LFISAKNNIG LDSLKSRVAQ ELKDYVTVRL NLEYLDKVNS VLGHRASLMM ISDGSALINV RRIDVKVLDE NGVKYSVEG // ID A0A101X9L9_9CREN Unreviewed; 400 AA. AC A0A101X9L9; DT 13-APR-2016, integrated into UniProtKB/TrEMBL. DT 13-APR-2016, sequence version 1. DT 07-JUN-2017, entry version 9. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=AT715_06590 {ECO:0000313|EMBL:KUO87358.1}; OS Thermoproteus sp. JCHS_4. OC Archaea; Crenarchaeota; Thermoprotei; Thermoproteales; OC Thermoproteaceae; Thermoproteus. OX NCBI_TaxID=1714258 {ECO:0000313|EMBL:KUO87358.1, ECO:0000313|Proteomes:UP000054781}; RN [1] {ECO:0000313|EMBL:KUO87358.1, ECO:0000313|Proteomes:UP000054781} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Jay Z.J., Beam J.P., Kozubal M.A., Jennings R.D.E., Rusch D.B., RA Inskeep W.P.; RT "The distribution, diversity and function of predominant RT Thermoproteales in high-temperature environments of Yellowstone RT National Park."; RL Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KUO87358.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LOBZ01000025; KUO87358.1; -; Genomic_DNA. DR EnsemblBacteria; KUO87358; KUO87358; AT715_06590. DR Proteomes; UP000054781; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000054781}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}. FT DOMAIN 186 305 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 400 AA; 45608 MW; 88E235B059289E02 CRC64; MRNRALLAYV GPRDRRLGRR LAEFEALAEV AGYEVAGVVA QYGERDTRFY LGRGKLDEVA GMDFDVFVAY HELTPLQSYN LRRRLGVDVM DRVLLILKIF ERRAGGIESK LQIELASLKY QLPLVKEYLR RAKMGEQIGY MGAGEYAVDA YYRHMVSRIS HIKRRLDRMR EDRVGLMKRR RDLGVPEVVL TGYTSVGKTT LFNRLTAEHK YVDGKPFATL DTYSRRINLW GKELVLTDTI GFIEDLPPVL IESFYSTLQE VADADLVLLL VDVSDDEGEL ARELQTSLDV LSTIGVYREK ILPVLSKVDR VSLSELVEKA SIVRRHFPLF VPVSALTGFG INTLKLLLFW KTPGYAIYEA RPPIGGLMLD GKSYLPVKMG EVKRFESSSL NLYIELRRVL // ID A0A101XD95_9CREN Unreviewed; 362 AA. AC A0A101XD95; DT 13-APR-2016, integrated into UniProtKB/TrEMBL. DT 13-APR-2016, sequence version 1. DT 07-JUN-2017, entry version 9. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=AT716_02365 {ECO:0000313|EMBL:KUO89279.1}; OS Vulcanisaeta sp. MG_3. OC Archaea; Crenarchaeota; Thermoprotei; Thermoproteales; OC Thermoproteaceae; Vulcanisaeta. OX NCBI_TaxID=1714250 {ECO:0000313|EMBL:KUO89279.1, ECO:0000313|Proteomes:UP000054619}; RN [1] {ECO:0000313|EMBL:KUO89279.1, ECO:0000313|Proteomes:UP000054619} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Jay Z.J., Beam J.P., Kozubal M.A., Jennings R.D.E., Rusch D.B., RA Inskeep W.P.; RT "The distribution, diversity and function of predominant RT Thermoproteales in high-temperature environments of Yellowstone RT National Park."; RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KUO89279.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LOCH01000009; KUO89279.1; -; Genomic_DNA. DR EnsemblBacteria; KUO89279; KUO89279; AT716_02365. DR Proteomes; UP000054619; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000054619}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000054619}. FT DOMAIN 187 357 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 362 AA; 41723 MW; 3321F2533C5E35E5 CRC64; MGSKAILLVA DDIEDGKIRE FKSLAEAGDY EVLDMIIQRR RPDPRYYLGL GKLGEVEEIV RNYEPDTVIT YHQLNPVQYV NLGRRLRIRV MDRVWLILEI FERRAGSKEA KLQIELTRLR LEIPRVREFI RLAKLGEQIG FYGGGEYAIE AYYRHMVRRA SHIRKELEKI RERRASLVMR RRDYGLPQVA LTGYTSAGKT TLFNRLAREN KYVDGKPFAT LDTYSRLAYF NGVNAILTDT IGFIDDLPPL LIESFYATIA EVLNSDLVLF VIDMSDEYSE FHRKFTSSLR IFMDLGVPKG KILPVLNKVD AANDSYISNK VSLVKQEFNE YVVISAKLGI GIDDLRNTIR NRLERLGLVG KD // ID A0A101XSL9_9BACL Unreviewed; 389 AA. AC A0A101XSL9; DT 13-APR-2016, integrated into UniProtKB/TrEMBL. DT 13-APR-2016, sequence version 1. DT 07-JUN-2017, entry version 10. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=ATW55_08330 {ECO:0000313|EMBL:KUO96807.1}; OS Acidibacillus ferrooxidans. OC Bacteria; Firmicutes; Bacilli; Bacillales; Acidibacillus. OX NCBI_TaxID=1765683 {ECO:0000313|EMBL:KUO96807.1, ECO:0000313|Proteomes:UP000053557}; RN [1] {ECO:0000313|EMBL:KUO96807.1, ECO:0000313|Proteomes:UP000053557} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ITV001 {ECO:0000313|EMBL:KUO96807.1, RC ECO:0000313|Proteomes:UP000053557}; RA Dall'Agnol H., Nancucheo I., Johnson B., Oliveira R., Leite L., RA Pylro V., Nunes G.L., Tzotzos G., Fernandes G.R., Dutra J., RA Orellana S.C., Oliveira G.; RT "Draft genome sequence of Acidibacillus ferrooxidans ITV001, isolated RT from a chalcopyrite acid mine drainage site in Brazil."; RL Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KUO96807.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LPVJ01000009; KUO96807.1; -; Genomic_DNA. DR RefSeq; WP_067712699.1; NZ_LPVJ01000009.1. DR EnsemblBacteria; KUO96807; KUO96807; ATW55_08330. DR Proteomes; UP000053557; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000053557}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000053557}. FT DOMAIN 164 274 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 389 AA; 43065 MW; 91FD6279CB66E09B CRC64; MSAGADVVDE LAQQVDDKRA GTMIGKGKLE QLCDRVAAVD ADLVIFSVDL TGSQVRNLED GVNVRVIDRT QLILDLFARR AVSAEGSAQV KLAQLSYLLP RLIGSSGHLS RLGGGIGTRG PGETQLETDR RNIRREISDL RRIVEAEGER RRENRRRRKR QGVYSIGLVG YTNAGKSTLL QKLAKRFGER ESRGGNDRIF DTLDLTSRRI TYEGRTWVVT DTVGFIRALP HHLVDAFRAT LEEAVDADVL LHVVDAQDED ANAQMSTVYQ VLDNELKSVA PVITVLNKKT DALLTVHGDP SAKRVVAGDV TDEETLFKIA NAVDELLGAR VHLRLRVPSE RSDLIARAYR AGNVQNMTDE ANSFHFDLQV DSRDAFLFLP FVETAYSAE // ID A0A102DFM5_9SPHN Unreviewed; 448 AA. AC A0A102DFM5; DT 13-APR-2016, integrated into UniProtKB/TrEMBL. DT 13-APR-2016, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=AQZ49_01380 {ECO:0000313|EMBL:KUR80712.1}; OS Novosphingobium sp. FSW06-99. OC Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales; OC Sphingomonadaceae; Novosphingobium. OX NCBI_TaxID=1739113 {ECO:0000313|EMBL:KUR80712.1, ECO:0000313|Proteomes:UP000061032}; RN [1] {ECO:0000313|EMBL:KUR80712.1, ECO:0000313|Proteomes:UP000061032} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=FSW06-99 {ECO:0000313|EMBL:KUR80712.1, RC ECO:0000313|Proteomes:UP000061032}; RA Ruckert C., Winkler A., Glaeser J., Grossart H.-P., Kalinowski J., RA Glaeser S.; RT "Draft genome sequence of Novosphingobium sp. FSW06-99 (=LMG 27919), a RT Novosphingobium acidiphilum related species isolated from a surface RT water sample of the southwest basin of Lake Grosse Fuchskuhle."; RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KUR80712.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LLZQ01000001; KUR80712.1; -; Genomic_DNA. DR RefSeq; WP_067611713.1; NZ_KQ954251.1. DR EnsemblBacteria; KUR80712; KUR80712; AQZ49_01380. DR Proteomes; UP000061032; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000061032}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000061032}. FT DOMAIN 216 392 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 448 AA; 48928 MW; B56ADAB4512F4EAE CRC64; MTGFEFGRNP EDLKGEVTRG AKVLVALPDV RQKGNLGLDA ESRLEEAEGL ARAIGLDVVD SFALPIRAIR PATLFGEGQV DKIAVACEQS GADLVIVDGA LSAIQQRNLE TRLGRKVIDR TGLILEIFGE RAATAEGRLQ VELAHLDYQA GRLVRSWTHL ERQRGGFGFL GGPGETQIEA DRRLIRGRMA RIRRELDQVR RTRGLHRERR QRAPWPVIAL VGYTNAGKST LFNRLTGADV MAQDLLFATL DPTMRAIRLP AVDKAILSDT VGFISDLPTQ LVAAFRATLE EVTAADVIVH VRDVANPASA EQKREVEAIL ADLGVGGEDG PAIPIIEAWN KIDLLPPDDR AMREDLIAHD IADRPVVPIS AVTGEGVDAL IERLGVMLTG EAQTLDLTVP MHDGQKLAWL HAHGEVLLEE AAQDQQGQPA AHLRVRLTPR ELGRFYAL // ID A0A103E133_9BURK Unreviewed; 387 AA. AC A0A103E133; DT 13-APR-2016, integrated into UniProtKB/TrEMBL. DT 13-APR-2016, sequence version 1. DT 07-JUN-2017, entry version 10. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=WS67_15980 {ECO:0000313|EMBL:KVE26456.1}; OS Burkholderia sp. TSV85. OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Burkholderia; pseudomallei group. OX NCBI_TaxID=1385593 {ECO:0000313|EMBL:KVE26456.1, ECO:0000313|Proteomes:UP000062788}; RN [1] {ECO:0000313|EMBL:KVE26456.1, ECO:0000313|Proteomes:UP000062788} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=TSV85 {ECO:0000313|EMBL:KVE26456.1, RC ECO:0000313|Proteomes:UP000062788}; RA Sahl J., Keim P., Wagner D.; RT "Expanding the genomic diversity of Burkholderia species for the RT development of highly accurate diagnostics."; RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KVE26456.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LOWA01000034; KVE26456.1; -; Genomic_DNA. DR RefSeq; WP_059518271.1; NZ_LOWA01000034.1. DR EnsemblBacteria; KVE26456; KVE26456; WS67_15980. DR Proteomes; UP000062788; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000062788}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000062788}. FT DOMAIN 191 362 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 157 184 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 387 AA; 42511 MW; 1B02431365C657EE CRC64; MINAALVGID FGKTDFEASL EELSLLAASA GAHPAVTLTG RRASPDAAMF VGSGKAEELR LACEANDVEI VIFNHALAPA QQRNLERMLN RRVVDRTSLI LDIFAQRARS HEGKLQVELA QLQYLATRLI RAWTHLERQK GGIGLRGPGE TQLETDRRLI GERIKMLKSR LEKLRRQHHT QRRQRERNRT MSVSLVGYTN AGKSTLFNAL TKAQAYAADQ LFATLDTTSR RVYLGDDVGQ IVVSDTVGFI RELPHQLVAA FRATLEETIH ADLLLHVVDA SSVVRLEQIE QVNGVLHEIG ADSIRQILVF NKIDAVPELA ARGGAVERDE YGNISRVFLS ARTGQGLDAL RAAIAEIATA EHLAGAMPLI GAPAQPHEDH PVSEHGH // ID A0A106BRC8_THIDE Unreviewed; 384 AA. AC A0A106BRC8; DT 13-APR-2016, integrated into UniProtKB/TrEMBL. DT 13-APR-2016, sequence version 1. DT 30-AUG-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=ABW22_05255 {ECO:0000313|EMBL:KVW97221.1}; OS Thiobacillus denitrificans. OC Bacteria; Proteobacteria; Betaproteobacteria; Nitrosomonadales; OC Thiobacillaceae; Thiobacillus. OX NCBI_TaxID=36861 {ECO:0000313|EMBL:KVW97221.1, ECO:0000313|Proteomes:UP000064243}; RN [1] {ECO:0000313|EMBL:KVW97221.1, ECO:0000313|Proteomes:UP000064243} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=RG {ECO:0000313|EMBL:KVW97221.1, RC ECO:0000313|Proteomes:UP000064243}; RX PubMed=26712544; RA Harrold Z.R., Skidmore M.L., Hamilton T.L., Desch L., Amada K., RA van Gelder W., Glover K., Roden E.E., Boyd E.S.; RT "Aerobic and Anaerobic Thiosulfate Oxidation by a Cold-Adapted, RT Subglacial Chemoautotroph."; RL Appl. Environ. Microbiol. 82:1486-1495(2015). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KVW97221.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LDUG01000017; KVW97221.1; -; Genomic_DNA. DR RefSeq; WP_059752788.1; NZ_LDUG01000017.1. DR EnsemblBacteria; KVW97221; KVW97221; ABW22_05255. DR PATRIC; fig|36861.3.peg.515; -. DR Proteomes; UP000064243; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000064243}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000064243}. FT DOMAIN 198 364 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 384 AA; 41735 MW; FEE4883886DBABB2 CRC64; MIERHAGGER VILVALDFGT PDFAESVAEL RLLATGAGLD IQGEVQGKRS RPDAALFVGS GKADEIAALV AATEADVVIF NHELSPAQER NLERRLHCRV IDRVSLILDI FARRASSAEG KLQVELAQLQ HLSTRLVRGW THLERQRGGV GMRGPGEKQL ETDRRLIGTR VKALRERLAK LGKQRRTQRR SRARQNVLSV ALVGYTNAGK STLFNALTRA DAYAADQLFA TLDTTTRKIY LPQVGEVVLS DTVGFITRLP HDLVAAFRAT LEATAEADLL LHVIDSSSPG RERQIEAVEK VLHEIGADAV PQLRVYNKLD LTGVAPGVGR GEYGKLQSVY VSAQTGAGLE LLREALSEIL GAGRVRLEAG VPDDTSPPTE VISE // ID A0A109BMJ8_HYPSL Unreviewed; 449 AA. AC A0A109BMJ8; DT 13-APR-2016, integrated into UniProtKB/TrEMBL. DT 13-APR-2016, sequence version 1. DT 07-JUN-2017, entry version 9. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=APY04_0451 {ECO:0000313|EMBL:KWT71529.1}; OS Hyphomicrobium sulfonivorans. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Hyphomicrobiaceae; Hyphomicrobium. OX NCBI_TaxID=121290 {ECO:0000313|EMBL:KWT71529.1, ECO:0000313|Proteomes:UP000059074}; RN [1] {ECO:0000313|EMBL:KWT71529.1, ECO:0000313|Proteomes:UP000059074} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=WDL6 {ECO:0000313|EMBL:KWT71529.1, RC ECO:0000313|Proteomes:UP000059074}; RA Albers P.; RT "Transcriptomic analysis of a linuron degrading triple-species RT bacterial consortium."; RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KWT71529.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LMTR01000021; KWT71529.1; -; Genomic_DNA. DR EnsemblBacteria; KWT71529; KWT71529; APY04_0451. DR PATRIC; fig|121290.4.peg.2168; -. DR Proteomes; UP000059074; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000059074}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000059074}. FT DOMAIN 205 379 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 449 AA; 49919 MW; 85B9CD7155F84842 CRC64; MLVPDLKRSA RPLSDAATGA GRTAPLHSPH DRLEEARGLS EAIDLDVRDA MLVPVSSPRP STLFGSGKVE SLGAHIEADE IGLVIIDHPV SPIQQRNLER AWKTKVLDRT GLILEIFGRR ARTREGRLQV ELAHLSYQKS RLVRTWTHLE RQRGGYGFLG GPGEAQIELD RRMIDERIMA IRKELEVVVR TRDLHRQGRR RVPYPVVAIV GYTNAGKSTL FNRITGASVF AKHQLFATLD PTMREVRLQS GRRIILSDTV GFISDLPTML VAAFRATLEE VIEADLILHV RDISHDETES QAQDVEAVLR DLGIDTLAVD APIIEVWNKT DLLEQPKREE IESQARWSSE RPPVLVSAVT GDGIDALLGA IDARLGSGDA ELQLDIPPEG GRLLNWLYEE AEVLARETQD SGGVRVRVRV AAEKKERLLA NARRSGVEAV DVRRVSNQV // ID A0A109C8V3_9BACT Unreviewed; 549 AA. AC A0A109C8V3; DT 13-APR-2016, integrated into UniProtKB/TrEMBL. DT 13-APR-2016, sequence version 1. DT 07-JUN-2017, entry version 9. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:KWT82591.1}; GN ORFNames=ASN18_2451 {ECO:0000313|EMBL:KWT82591.1}; OS Nitrospirae bacterium HCH-1. OC Bacteria; Nitrospirae. OX NCBI_TaxID=1748249 {ECO:0000313|EMBL:KWT82591.1, ECO:0000313|Proteomes:UP000060487}; RN [1] {ECO:0000313|EMBL:KWT82591.1, ECO:0000313|Proteomes:UP000060487} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=HCH-1 {ECO:0000313|EMBL:KWT82591.1, RC ECO:0000313|Proteomes:UP000060487}; RA Zhang Y., Guo Z.; RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KWT82591.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LNQR01000086; KWT82591.1; -; Genomic_DNA. DR EnsemblBacteria; KWT82591; KWT82591; ASN18_2451. DR PATRIC; fig|1748249.3.peg.2563; -. DR Proteomes; UP000060487; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000060487}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000060487}. FT DOMAIN 374 538 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 333 367 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 549 AA; 61326 MW; 1DBF5421991D3A41 CRC64; MVVYGNTQGI KKKSVTGLEK IYRRKVPPDR IISQELARYL TELSSEINRQ LGVLITRGGT VSHVIVGDAG SIFLPELSAY PLGKKYLRGL RFVHTHLKNE PLTHDDLTDL ALLRFDYIAA IGIRDALPDR FYTAHLTANI GDKPYEINPA VNFYNDTIDF LAHIGAIEEE MGRQRPQAAD SAAEKAIIIA VSQAPKHEIE EALDELQELC ASSGIATVDR VIQRPKEINP RYLLGAGRLR DLIIDALAKG ATLLVFNENL TPSQSLAIAE LTEIKVIDRT ALILDIFARR AMSRDGKVQV ELAQLKYRLP RLTGKGTAMS RLTGGIGGRG PGEMKLEIDR RRVRDRINIL EKELEKLSMA RKQRRARRSN STLPIVSIVG YTNAGKSTLL NNLTESAAFV EDKMFATLDT STRRLRFPEE RDVIITDTVG FIKDLPRDLI TAFKATLEEL EDADTLIHLV DASNQRFEQH IQSVETILKD LGIDSKPTLL VFNKTDKIHE DELEGILRRY GAVGISAINP STFGALLETL KERVFGRRHH QEAEGTDEV // ID A0A109IGA0_9ACTN Unreviewed; 483 AA. AC A0A109IGA0; DT 13-APR-2016, integrated into UniProtKB/TrEMBL. DT 13-APR-2016, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=AWV63_25370 {ECO:0000313|EMBL:KWV30001.1}; OS Micromonospora rifamycinica. OC Bacteria; Actinobacteria; Micromonosporales; Micromonosporaceae; OC Micromonospora. OX NCBI_TaxID=291594 {ECO:0000313|EMBL:KWV30001.1, ECO:0000313|Proteomes:UP000063460}; RN [1] {ECO:0000313|EMBL:KWV30001.1, ECO:0000313|Proteomes:UP000063460} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=AM105 {ECO:0000313|EMBL:KWV30001.1, RC ECO:0000313|Proteomes:UP000063460}; RA Li Y., Zhang Z., Yang H., Zhu D.; RT "Draft genome sequence of Micromonospora rifamycinica AM105, a novel RT actinomycete isolated from mangrove sediment in the South China Sea."; RL Submitted (JAN-2016) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KWV30001.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LRMV01000191; KWV30001.1; -; Genomic_DNA. DR RefSeq; WP_067314171.1; NZ_LRMV01000191.1. DR EnsemblBacteria; KWV30001; KWV30001; AWV63_25370. DR Proteomes; UP000063460; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000313|EMBL:KWV30001.1}; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000063460}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900, KW ECO:0000313|EMBL:KWV30001.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000063460}. FT DOMAIN 255 420 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 214 248 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 483 AA; 52744 MW; 6F8F7B1AB8D2EC9F CRC64; MRDQETHTPY SDDDLDATTG EYELSERQAL RRVPGLSTEL TDVTEVEYRQ LRLERVVLVG VWTEGTQQDA DNSLTELAAL AETAGSQVLE GLVQRRGRPD PATYVGRGKV DDLGAVVLST GADTVICDGE LSPSQLRNLE QRTKVKVVDR TALILDIFAQ HAKSREGKAQ VELAQLEYLL PRLRGWGETL SRQTGGSGRG GGAGGGVGLR GPGETKLETD RRRIRHRIAR LRREIKAMKT VRQTKRARRS RNAVPAVAIA GYTNAGKSSL LNRLTGAGVL VENALFATLD PTTRRATTSD GRLYTLSDTV GFVRHLPHQI VEAFRSTLEE VAQADLVVHV VDGTHPDPEE QVRAVHEVLS EVGADRLPEL LVVNKTDAAD EESLLRLKRL WPDAVFVSAH NGRGIDGLRE AIEQRLPRPA VEVRVVLPYD RGDLVARLHR QGEVLGTVHL PEGTSLHVRV SEALAAELTP FVAVGDPAVA GSR // ID A0A109IMV2_9ACTN Unreviewed; 109 AA. AC A0A109IMV2; DT 13-APR-2016, integrated into UniProtKB/TrEMBL. DT 13-APR-2016, sequence version 1. DT 05-JUL-2017, entry version 8. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:KWV33481.1}; GN ORFNames=AWV63_06830 {ECO:0000313|EMBL:KWV33481.1}; OS Micromonospora rifamycinica. OC Bacteria; Actinobacteria; Micromonosporales; Micromonosporaceae; OC Micromonospora. OX NCBI_TaxID=291594 {ECO:0000313|EMBL:KWV33481.1, ECO:0000313|Proteomes:UP000063460}; RN [1] {ECO:0000313|EMBL:KWV33481.1, ECO:0000313|Proteomes:UP000063460} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=AM105 {ECO:0000313|EMBL:KWV33481.1, RC ECO:0000313|Proteomes:UP000063460}; RA Li Y., Zhang Z., Yang H., Zhu D.; RT "Draft genome sequence of Micromonospora rifamycinica AM105, a novel RT actinomycete isolated from mangrove sediment in the South China Sea."; RL Submitted (JAN-2016) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KWV33481.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LRMV01000021; KWV33481.1; -; Genomic_DNA. DR EnsemblBacteria; KWV33481; KWV33481; AWV63_06830. DR Proteomes; UP000063460; Unassembled WGS sequence. DR InterPro; IPR025121; GTPase_HflX_N. DR Pfam; PF13167; GTP-bdg_N; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000063460}; KW Reference proteome {ECO:0000313|Proteomes:UP000063460}. FT DOMAIN 52 103 GTP-bdg_N. {ECO:0000259|Pfam:PF13167}. SQ SEQUENCE 109 AA; 11518 MW; 9F592071FBF54A5C CRC64; MMLVGLFSAK DKQVEVKLDL LAASVEARGG RVVGRQIQRR GISRGGASRM TSPFSRRTLL GSGKADEVAD ACRSAAVAMA VFVNPLTDHQ RTVLSDLFGC PVVSGDDLA // ID A0A109LTI8_9SPHN Unreviewed; 432 AA. AC A0A109LTI8; DT 13-APR-2016, integrated into UniProtKB/TrEMBL. DT 13-APR-2016, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=AUC45_02315 {ECO:0000313|EMBL:KWV93457.1}; OS Erythrobacter sp. YT30. OC Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales; OC Erythrobacteraceae; Erythrobacter. OX NCBI_TaxID=1735012 {ECO:0000313|EMBL:KWV93457.1, ECO:0000313|Proteomes:UP000055668}; RN [1] {ECO:0000313|EMBL:KWV93457.1, ECO:0000313|Proteomes:UP000055668} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=YT30 {ECO:0000313|EMBL:KWV93457.1, RC ECO:0000313|Proteomes:UP000055668}; RA Lin W., Zheng Q.; RT "Draft genome sequence of Erythrobacter sp. YT30."; RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KWV93457.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LMAF01000001; KWV93457.1; -; Genomic_DNA. DR RefSeq; WP_067598936.1; NZ_LMAF01000001.1. DR EnsemblBacteria; KWV93457; KWV93457; AUC45_02315. DR Proteomes; UP000055668; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000055668}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000055668}. FT DOMAIN 202 376 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 168 195 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 432 AA; 47739 MW; EEDF0DDC50D3F3F4 CRC64; MDEVTRGARA LVLCPDIRSV SYDLTANERL EEAKGLALAI GVVIAHSEIF TIRQMQPNTL FGSGQVERIK TDCELHDAEL VIVDGALTPI QQRNLEEKFK RKVIDRTGLI LEIFGERAAT AEGRLQVELA HLDYQQSRLV RSWTHLERQR GGFGFLGGPG ETQIEADRRM IRQRMGRLRR ELEQVRKTRA LHRERRGRAP WPVIALVGYT NAGKSTLFNR LTGSNVMAED MLFATLDPTM RAISLLGVEK AILSDTVGFI SDLPTQLVAA FRATLEEVTG ADIICHVRDM AGEAHAAQKK QVLEVLSDLD VVDSETGQSD IPILEVWNKA DLLDKDRLAE LQDAADSTDA VLISASTGAG IDAFADRVAE MLTAAAREIT VTIPVSDGRR IAWLHAHGDV RSERDAGEGE KGPERELTVR LNPKELGQFE AL // ID A0A109LYA4_9SPHN Unreviewed; 432 AA. AC A0A109LYA4; DT 13-APR-2016, integrated into UniProtKB/TrEMBL. DT 13-APR-2016, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=ASS64_02090 {ECO:0000313|EMBL:KWV96034.1}; OS Erythrobacter sp. AP23. OC Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales; OC Erythrobacteraceae; Erythrobacter. OX NCBI_TaxID=499656 {ECO:0000313|EMBL:KWV96034.1, ECO:0000313|Proteomes:UP000058666}; RN [1] {ECO:0000313|EMBL:KWV96034.1, ECO:0000313|Proteomes:UP000058666} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=AP23 {ECO:0000313|EMBL:KWV96034.1, RC ECO:0000313|Proteomes:UP000058666}; RA Lin W., Zheng Q.; RT "Draft genome sequence of Erythrobacter sp. AP23."; RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KWV96034.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LNBY01000001; KWV96034.1; -; Genomic_DNA. DR RefSeq; WP_067689072.1; NZ_LNBY01000001.1. DR EnsemblBacteria; KWV96034; KWV96034; ASS64_02090. DR Proteomes; UP000058666; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000058666}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}. FT DOMAIN 202 377 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 432 AA; 47290 MW; 0AF5A142FBE953C4 CRC64; MGEVSRGARA LVVCPDIRGM AYDLDAQSRL AEAEGLALAI GIVIAESFVL PVRDVRPNLL FGAGQVDNIR TSCEQNEAEL VVVDGALSPI QQRNLEEKLG RKVIDRTGLI LEIFGERAAT AEGRLQVELA HLDYQQSRLV RSWTHLERQR GGFGFLGGPG ETQIEADRRM IRQRMGRLRK ELEQVRKTRG LHRERRERAP WPVVALVGYT NAGKSTLFNR LTGAGVMAED LLFATLDPTM RAIALPGVEK AILSDTVGFI SDLPTQLVAA FRATLEEVTS ADVICHVRDI SNPSTAAQKA QVLQVLRDLD VVGGEGEDAS IPILEVWNKW DRLTPEAADD LAAQVEADEH IVATSAVTGE GLDLLLERLG EMLTRNASLQ TFEVPASDGR RIAWLHAHGE VIEDVADDEG GAVRRITVRL NPKELGQFEA IG // ID A0A117KT32_9EURY Unreviewed; 407 AA. AC A0A117KT32; DT 13-APR-2016, integrated into UniProtKB/TrEMBL. DT 13-APR-2016, sequence version 1. DT 07-JUN-2017, entry version 9. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=XD46_0831 {ECO:0000313|EMBL:KUK04416.1}; OS Euryarchaeota archaeon 55_53. OC Archaea; Euryarchaeota. OX NCBI_TaxID=1635285 {ECO:0000313|EMBL:KUK04416.1, ECO:0000313|Proteomes:UP000056382}; RN [1] {ECO:0000313|EMBL:KUK04416.1, ECO:0000313|Proteomes:UP000056382} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=55_53 {ECO:0000313|EMBL:KUK04416.1}; RX PubMed=26787827; RA Hu P., Tom L., Singh A., Thomas B.C., Baker B.J., Piceno Y.M., RA Andersen G.L., Banfield J.F.; RT "Genome-Resolved Metagenomic Analysis Reveals Roles for Candidate RT Phyla and Other Microbial Community Members in Biogeochemical RT Transformations in Oil Reservoirs."; RL MBio 7:0-0(2016). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KUK04416.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LGEW01000010; KUK04416.1; -; Genomic_DNA. DR PATRIC; fig|1635285.3.peg.1085; -. DR Proteomes; UP000056382; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000056382}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000056382}. FT DOMAIN 187 353 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 103 130 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 407 AA; 46788 MW; 051E080EC80FAE7D CRC64; MVLRSEPSPQ ERQKEDYRLK ELKLLATSAG YTVARTFTQV RHWDRRYQIG YGKVRDIAEY IADEHVDKVI FYNRLSTLQL FNLSKLLGTD TMDRFHLILE IFAKRAKTRV AKLQVELASL SYELPKAREK VALSKRREHP GFMGFGNYED SYEQDIRRRM AKLREELARY AAKQHERRTR DTRKGLLRVA LCGYTNAGKS TLLNALAGGE YAVAANQLFT TLSPTTRKVK VGRRKVLITD TVGFIEDLPH FMIEAFRSTF SEIYEADLVL LVVDASEDAS SIRRKLATSH ATLFEDIADA PIITVFNKMD RVEEFDPHAF RELAPNPVMV SAKEGAGLDE LREAIDRMLP RWREHMVELP MCPSSMSRLS MLYERGVVEE ARFDDSIKIR FRACDEVASK IRKVGHG // ID A0A117KZ29_9BACT Unreviewed; 362 AA. AC A0A117KZ29; DT 13-APR-2016, integrated into UniProtKB/TrEMBL. DT 13-APR-2016, sequence version 1. DT 07-JUN-2017, entry version 9. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=XD52_0713 {ECO:0000313|EMBL:KUK14006.1}; OS bacterium 42_11. OC Bacteria. OX NCBI_TaxID=1635281 {ECO:0000313|EMBL:KUK14006.1, ECO:0000313|Proteomes:UP000053082}; RN [1] {ECO:0000313|EMBL:KUK14006.1, ECO:0000313|Proteomes:UP000053082} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=42_11 {ECO:0000313|EMBL:KUK14006.1}; RA Hu P., Tom L., Singh A., Thomas B.C., Baker B.J., Piceno Y.M., RA Andersen G.L., Banfield J.F.; RT "Genome-resolved metagenomic analysis reveals roles for candidate RT phyla and other microbial community members in biogeochemical RT transformations in oil reservoirs."; RL MBio 7:e01669-15(2015). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KUK14006.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LGFB01000064; KUK14006.1; -; Genomic_DNA. DR PATRIC; fig|1635281.3.peg.1560; -. DR Proteomes; UP000053082; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000053082}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000053082}. FT DOMAIN 192 362 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 158 185 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 362 AA; 40901 MW; 078F4B3F62BA80D5 CRC64; MKGILVSLIP PSSNAVEIEE QIEELKELFR TLGGETLAVL TQKRTPDPAF LIGRGKVEEL KKLVEDLKAD VVVFNDDLTP RQQVNLEEAL GVKVIDRTQV IIQIFARRAK TAEAKLQVEL AQLTYELTRL RGRGKELSRL GGGVGTRGPG EPEIEAERSR IRERIAVLKE KLEEIRNRRE IQRKRRKRAG VFQASIVGYT NAGKSTLLSA LSGEDVYAED KLFVTLDPLT RRVYLPSGGE ILVTDTVGFI RKLPHHLVAA FRATLEEVRE SDGLLHVVDV SSYNFFDQID AVNTVLKGLK SLDKPTIMVF NKIDKLTLEE LEGIKRRIGD RFGDKVVYIS ALKKYNLEEL YQAMERWFFS GK // ID A0A117LDP4_9BACT Unreviewed; 381 AA. AC A0A117LDP4; DT 13-APR-2016, integrated into UniProtKB/TrEMBL. DT 13-APR-2016, sequence version 1. DT 07-JUN-2017, entry version 9. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=XD68_0198 {ECO:0000313|EMBL:KUK40226.1}; OS Synergistales bacterium 54_24. OC Bacteria; Synergistetes; Synergistia; Synergistales. OX NCBI_TaxID=1635272 {ECO:0000313|EMBL:KUK40226.1, ECO:0000313|Proteomes:UP000054050}; RN [1] {ECO:0000313|EMBL:KUK40226.1, ECO:0000313|Proteomes:UP000054050} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=54_24 {ECO:0000313|EMBL:KUK40226.1}; RA Hu P., Tom L., Singh A., Thomas B.C., Baker B.J., Piceno Y.M., RA Andersen G.L., Banfield J.F.; RT "Genome-resolved metagenomic analysis reveals roles for candidate RT phyla and other microbial community members in biogeochemical RT transformations in oil reservoirs."; RL MBio 7:e01669-15(2015). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KUK40226.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LGFQ01000004; KUK40226.1; -; Genomic_DNA. DR PATRIC; fig|1635272.3.peg.1185; -. DR Proteomes; UP000054050; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000054050}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000054050}. FT DOMAIN 203 373 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 381 AA; 42579 MW; 6E72D2887041B2BD CRC64; MKRPVEIQDK NSKRALLLIL GLQEDREVEL LAGELELLLK NLGIAPAGRI LQERRSPDPA YFLGQGKIEE AKVLAEAMGA NLLVCDDPLT PSQMSNIGEL TGLEVWDRHL VIMKIFEARA RSAEAKLQVE LARCRYEIPR LKGLGLQMSR PGGGIGTRGP GETEFERHRR KLMRRVHSIR ATLENMRRQR EDRRKRRKRV GLPTVSLVGY TNSGKSTLLR RLSGDKSILV ADQLFSTLDT TVRKIVLPHG TSVLFSDTVG FIRKLPPDLI AAFQATLEEL KNADILLVVL DGTDDRWAET LKVIDETLAA IGAAKIPRII ALNKVDVLSW DVTLKIVNRL EAEGERVIPI SALRGDNIPS LLDAVEEEVR YLREGLFVKS S // ID A0A117M6C1_9BACT Unreviewed; 408 AA. AC A0A117M6C1; DT 13-APR-2016, integrated into UniProtKB/TrEMBL. DT 13-APR-2016, sequence version 1. DT 07-JUN-2017, entry version 9. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=XE03_1242 {ECO:0000313|EMBL:KUK86754.1}; OS candidate division TA06 bacterium 34_109. OC Bacteria; candidate division TA06. OX NCBI_TaxID=1635277 {ECO:0000313|EMBL:KUK86754.1, ECO:0000313|Proteomes:UP000053467}; RN [1] {ECO:0000313|EMBL:KUK86754.1, ECO:0000313|Proteomes:UP000053467} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=34_109 {ECO:0000313|EMBL:KUK86754.1}; RA Hu P., Tom L., Singh A., Thomas B.C., Baker B.J., Piceno Y.M., RA Andersen G.L., Banfield J.F.; RT "Genome-resolved metagenomic analysis reveals roles for candidate RT phyla and other microbial community members in biogeochemical RT transformations in oil reservoirs."; RL MBio 7:e01669-15(2015). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KUK86754.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LGGX01000012; KUK86754.1; -; Genomic_DNA. DR PATRIC; fig|1635277.3.peg.1735; -. DR Proteomes; UP000053467; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000053467}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000053467}. FT DOMAIN 193 355 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 408 AA; 47495 MW; 92924AF1D292356D CRC64; MQSSCIIVGT FTKSESDERI NKTIVEMKDL SSSLNMKSRE DVIQRIEKIN PAFYIGKGKV DEIKVIAENL KVDYVIFSNS LTPLQKRNLE KYLDLSVMDR TELILMIFEK NAKTTISKLE SELAKWTYLL PRLTGKGITM SQTGGGIGTR GPGEKKLEVD RRYIEKRIGI LKRKIKDYQK SIKVKSERRK NLFRVALFGY TNAGKTTIMN RLTKNNFFTD DKLFTTLDTV TRKLERYIVL TDTVGFLGDL PHEIIESFKL TIEEASDSDL KLFVVDISDQ YVDLVLDDMA KVIDQLKLNN GDIIYVFNKI DLLLHFNRID YFKDLYKNSI FISAKTGENF ELLKKVILEE FYKKLDYFEI STDDENLKKI LNYVNRYGII KDIKSDERNI IKFYIPKKYS KFIKVNFS // ID A0A117M8E3_9BACT Unreviewed; 427 AA. AC A0A117M8E3; DT 13-APR-2016, integrated into UniProtKB/TrEMBL. DT 13-APR-2016, sequence version 1. DT 07-JUN-2017, entry version 9. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=XE04_1607 {ECO:0000313|EMBL:KUK90042.1}; OS Marinimicrobia bacterium 46_43. OC Bacteria; Candidatus Marinimicrobia. OX NCBI_TaxID=1635280 {ECO:0000313|EMBL:KUK90042.1, ECO:0000313|Proteomes:UP000054945}; RN [1] {ECO:0000313|EMBL:KUK90042.1, ECO:0000313|Proteomes:UP000054945} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=46_43 {ECO:0000313|EMBL:KUK90042.1}; RA Hu P., Tom L., Singh A., Thomas B.C., Baker B.J., Piceno Y.M., RA Andersen G.L., Banfield J.F.; RT "Genome-resolved metagenomic analysis reveals roles for candidate RT phyla and other microbial community members in biogeochemical RT transformations in oil reservoirs."; RL MBio 7:e01669-15(2015). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KUK90042.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LGGY01000190; KUK90042.1; -; Genomic_DNA. DR PATRIC; fig|1635280.3.peg.555; -. DR Proteomes; UP000054945; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000054945}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000054945}. FT DOMAIN 204 370 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 165 192 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 427 AA; 48454 MW; 415C2F915880C864 CRC64; MTDVNNRNDT EKVLLVAVEL PGAGEKTERS LEELSRLTET AGGEVVDTLV QARPTLHSIH YLGKGKLQTL KNLCEELGVE TVIFDDELDP GQAKAVQKIL GDGLKVLDRS ALILDIFQQH ARTREAKTQV ALARAEYLLP RLTRQWTHLE RQAGGIGGAR RGPGETQIEI DRRLLRDQIK KLKKELEKIA LQRSTQRKFR HEFFNVALVG YTNAGKSTLM NTLTDAGVDV EDQLFKTLDT TVRKMTMPNG REVYLSDTVG FIQKLPHQLV ASFRSTLKEA ESADLLIKLV DISDPDFRRH LATIDRVLKD FEIPEKRFLT VFNKADRVPE SMNVTLVKRE YPDAVWISAK EAIGLSRLIK EIQSRMDENT IIRTVDIPHQ AGDIIAALHE HTRILSQSHE EDVTRFTLQA DRDIWAYLTK KFHLKGE // ID A0A117RZB6_9ACTN Unreviewed; 497 AA. AC A0A117RZB6; DT 13-APR-2016, integrated into UniProtKB/TrEMBL. DT 13-APR-2016, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=AQJ91_29500 {ECO:0000313|EMBL:KUO17537.1}; OS Streptomyces sp. RV15. OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae; OC Streptomyces. OX NCBI_TaxID=909626 {ECO:0000313|EMBL:KUO17537.1, ECO:0000313|Proteomes:UP000053260}; RN [1] {ECO:0000313|EMBL:KUO17537.1, ECO:0000313|Proteomes:UP000053260} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=RV15 {ECO:0000313|EMBL:KUO17537.1, RC ECO:0000313|Proteomes:UP000053260}; RA Ruckert C., Abdelmohsen U.R., Winkler A., Hentschel U., Kalinowski J., RA Kampfer P., Glaeser S.; RT "Draft genome sequence of Streptomyces sp. RV15, isolated from a RT marine sponge."; RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KUO17537.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LMXB01000074; KUO17537.1; -; Genomic_DNA. DR RefSeq; WP_067027591.1; NZ_KQ949096.1. DR EnsemblBacteria; KUO17537; KUO17537; AQJ91_29500. DR Proteomes; UP000053260; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 2. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000313|EMBL:KUO17537.1}; KW Complete proteome {ECO:0000313|Proteomes:UP000053260}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900, KW ECO:0000313|EMBL:KUO17537.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000053260}. FT DOMAIN 275 440 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 497 AA; 54299 MW; 0B2CFCF88F33A56B CRC64; MTSSSSPSQD TQSLAHTYPD GLRADALMEE DVAWSHEIDG ERDGDQFDRS ERAALRRVAG LSTELEDVTE VEYRQLRLER VVLVGVWTTG TVQDADNSLA ELAALAETAG ALVLDGVIQR RDKPDAATYI GSGKAEELRD IVLESGADTV ICDGELSPGQ LIHLEDVVKV KVIDRTALIL DIFAQHAKSR EGKAQVALAQ MQYMLPRLRG WGQSLSRQMG GGKGGGLATR GPGETKIETD RRRIREKMAK MRREIADMKT GREIKRQERK RHKVPSVAIA GYTNAGKSSL LNRLTGAGVL VENALFATLD PTVRRAETPS GRLYTLADTV GFVRHLPHHL VEAFRSTMEE VGESDLILHV VDGSHPNPEE QLAAVREVVR DVGATEVPEI VVINKADAAD PLTLQRLMRI EKRSIAVSAR TGQGITELLA LIDNELPRPS VEIEALVPYT HGRLVARAHS EGEVISEEHT PEGTLLKVRV HEELAADLTP YVPAPAA // ID A0A117S2M1_9FIRM Unreviewed; 425 AA. AC A0A117S2M1; DT 13-APR-2016, integrated into UniProtKB/TrEMBL. DT 13-APR-2016, sequence version 1. DT 12-APR-2017, entry version 8. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=APF76_09745 {ECO:0000313|EMBL:KUO48921.1}; OS Desulfitibacter sp. BRH_c19. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Peptococcaceae; OC Desulfitibacter. OX NCBI_TaxID=1734395 {ECO:0000313|EMBL:KUO48921.1, ECO:0000313|Proteomes:UP000053015}; RN [1] {ECO:0000313|EMBL:KUO48921.1, ECO:0000313|Proteomes:UP000053015} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BRH_c19 {ECO:0000313|EMBL:KUO48921.1}; RA Bagnoud A., Chourey K., Hettich R.L., De Bruijn I., Andersson A.F., RA Leupin O.X., Schwyn B., Bernier-Latmani R.; RT "Microbial metabolic network in the subsurface."; RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KUO48921.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LOER01000046; KUO48921.1; -; Genomic_DNA. DR Proteomes; UP000053015; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000053015}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000053015}. FT DOMAIN 197 371 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 157 184 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 425 AA; 47606 MW; BFD7983247BC9DAC CRC64; MEGKNERALL VSIEMPGHHL IGTEASLEEL TELARTAGAE VLGKFIQKRN KPDTTYYMGK GFAEELGLKA EELAANLIIV DEELSGTQIR NLEEITDVTV IDRTNLILDI FAQRAKSREG KLQVELAQIN YRLPRLTGMG IQLSRLAGGI GTKGPGETKL ETDRRHLKNR INDIKKQIAR ISRQRKIKRK GRNPNTPLIV LVGYTNAGKS SVRYRLLKEV PSIVTDTSNE DQGTDKLFAT LDSTIRGITL KSGREALIGD TVGFIQKIPH QLITSFKTTL DEVLEADLLL HVVDINNSFA KEQQEAVYNV LEEIGASNIK RITIYNKIDL VDLSVLPKPL DQSSYLSFSA KTGRGVAELL DLIEQELPEK KFILNVLIPF SQGKIISDLH NNCKVFEMKY TTAGTHFTVE VPAYFYPKLE YFILK // ID A0A117S880_9SPHN Unreviewed; 444 AA. AC A0A117S880; DT 13-APR-2016, integrated into UniProtKB/TrEMBL. DT 13-APR-2016, sequence version 1. DT 12-APR-2017, entry version 8. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=APF78_11685 {ECO:0000313|EMBL:KUO57125.1}; OS Sphingomonadales bacterium BRH_c3. OC Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales; OC unclassified Sphingomonadales. OX NCBI_TaxID=1734408 {ECO:0000313|EMBL:KUO57125.1, ECO:0000313|Proteomes:UP000061825}; RN [1] {ECO:0000313|EMBL:KUO57125.1, ECO:0000313|Proteomes:UP000061825} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BRH_c3 {ECO:0000313|EMBL:KUO57125.1}; RA Bagnoud A., Chourey K., Hettich R.L., De Bruijn I., Andersson A.F., RA Leupin O.X., Schwyn B., Bernier-Latmani R.; RT "Microbial metabolic network in the subsurface."; RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KUO57125.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LOET01000023; KUO57125.1; -; Genomic_DNA. DR Proteomes; UP000061825; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000061825}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000061825}. FT DOMAIN 214 388 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 180 207 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 444 AA; 49095 MW; 9FC0584DA0BAF51A CRC64; MGWRRLSFDD DLLGEVTRGA RALVLCPDIR GQSYAIDAAE RLEEACGLAL AIGVVIADAR VVPVRTMRPG TLFGSGQVEQ IQADCELHEA ELVIVDGALS PIQQRNLEEK LRRKVIDRTG LILEIFGERA VTAEGRLQVE LAHLDYQQSR LVRSWTHLER QRGGFGFLGG PGETQIEADR RMIRQRMARL RKELEQVRKT RGLHRKRRGR APWPVIALVG YTNAGKSTLF NRLTGAEVMA EDLLFATLDP TMRAIELPAV EKAILSDTVG FISDLPTQLV AAFRATLEEV TGADIILHVR DMANPAHESQ KKQVLSVLAE LGVTDDNGES TIPIIEAWNK VDLVSASRAD ELREMAALQG DALVISAQTG EGIDALLEWI GSILTKESRV VELELPASDG RRIAWLHANG EVLAEQELRG GREGPLRQFT VRLNPKQLGQ FARL // ID A0A117SBZ7_9FIRM Unreviewed; 599 AA. AC A0A117SBZ7; DT 13-APR-2016, integrated into UniProtKB/TrEMBL. DT 13-APR-2016, sequence version 1. DT 12-APR-2017, entry version 8. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=APF84_10795 {ECO:0000313|EMBL:KUO63006.1}; OS Gracilibacter sp. BRH_c7a. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Gracilibacteraceae; OC Gracilibacter. OX NCBI_TaxID=1734398 {ECO:0000313|EMBL:KUO63006.1, ECO:0000313|Proteomes:UP000053404}; RN [1] {ECO:0000313|EMBL:KUO63006.1, ECO:0000313|Proteomes:UP000053404} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BRH_c7a {ECO:0000313|EMBL:KUO63006.1}; RA Bagnoud A., Chourey K., Hettich R.L., De Bruijn I., Andersson A.F., RA Leupin O.X., Schwyn B., Bernier-Latmani R.; RT "Microbial metabolic network in the subsurface."; RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KUO63006.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LOEZ01000053; KUO63006.1; -; Genomic_DNA. DR Proteomes; UP000053404; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000053404}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000053404}. FT DOMAIN 378 542 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 599 AA; 66789 MW; 8214AFC047E7F5DD CRC64; MRVNGEIEGI KKSILEELDA LYEVRIPQNL LWTKELIEEV CQISALINRE VAIYLNRKGQ ITDVSVGDNQ TVTLAAVEGK RNSNRLSGTR CLHTHPNGSG RLSEVDISSL KILRLDAMIA VGIYNGEPRD IYIGIISEDN TYGINIMGPY YPDKDDFEIL FEYISESDQL LRQISKDHQA KERAILVGLH TRKSRELNGA NEADVSLAEL EELAKTAGAQ IVGRLMQKRD TRSSATVIGQ GKIDELRLLA QAKEADLVIF DEELTGTQQR NIEQMIGVKV LCRTGLILDI FAQRARSREG ILQVELAQLQ YQLPRLMGMG LALSRLGGGI GTRGPGETKL ETDRRRIRMR ITHLKKQLAE IRRQRGVLRG NRHKSGIPVV SIVGYTNAGK STLLNTLCDS EVLAEDKLFA TLDTTTRKLE LSNESTVLLT DTVGFIRKLP HNLLDAFKST LEEVLLSDLI LIVADASDPQ VEDHIRIVDE ILDELGAGTK PTIIALNKID LMKEDNSVIL RENRPILEIS AKSGDGLDLL KQEIENTLYN DRIEIDLEIP FSDGSTMAWL HANSKIMNIV YAEDTSLVKV ELEKELLAKV SPYRVDSGV // ID A0A117SPS4_9CREN Unreviewed; 386 AA. AC A0A117SPS4; DT 13-APR-2016, integrated into UniProtKB/TrEMBL. DT 13-APR-2016, sequence version 1. DT 07-JUN-2017, entry version 9. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=AT707_05705 {ECO:0000313|EMBL:KUO83191.1}; OS Pyrobaculum sp. JCHS_4. OC Archaea; Crenarchaeota; Thermoprotei; Thermoproteales; OC Thermoproteaceae; Pyrobaculum. OX NCBI_TaxID=1714260 {ECO:0000313|EMBL:KUO83191.1, ECO:0000313|Proteomes:UP000054943}; RN [1] {ECO:0000313|EMBL:KUO83191.1, ECO:0000313|Proteomes:UP000054943} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Jay Z.J., Beam J.P., Kozubal M.A., Jennings R.D.E., Rusch D.B., RA Inskeep W.P.; RT "The distribution, diversity and function of predominant RT Thermoproteales in high-temperature environments of Yellowstone RT National Park."; RL Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KUO83191.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LOBX01000020; KUO83191.1; -; Genomic_DNA. DR EnsemblBacteria; KUO83191; KUO83191; AT707_05705. DR Proteomes; UP000054943; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000054943}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000054943}. FT DOMAIN 186 356 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 386 AA; 43771 MW; 1FC5CBD2BEC578B9 CRC64; MRSRALLAYV GPKTLNLSYR LDEFVSLVEV AGFDVVDLMT QFGRSDTRFY LGSGRAREVA KRDFDVFIAY HSLSPLQVFN LERLFRRRAI DRVLVILSIF EKRAGSTESK LQIELARLRY ELPKVKEYLR RAKMGEQLGF MGAGEYIIDA YYRHMVKRIS TIRRKLEEVR RSRVTHIAKR KEVGVPEVVI TGYTSAGKTT LFNRLVGENK PVDGKPFATL ETYSRALDLW GKRVVLTDTI GFIDDLPPVL IESFHSTLQE VIDADTILLV VDGSEPQEEI TRKLETSLET LGEVGVDRGR IILVVNKVDK VRLGDVRHLR DLFTRYFAWF VPVSAATGFG IEALKAVLFF KVPGYSIIRS TGEDGARGLR VGNVTFIPMP SRSNRG // ID A0A117SV76_9CREN Unreviewed; 386 AA. AC A0A117SV76; DT 13-APR-2016, integrated into UniProtKB/TrEMBL. DT 13-APR-2016, sequence version 1. DT 07-JUN-2017, entry version 9. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=AT708_00395 {ECO:0000313|EMBL:KUO91818.1}; OS Pyrobaculum sp. OCT_11. OC Archaea; Crenarchaeota; Thermoprotei; Thermoproteales; OC Thermoproteaceae; Pyrobaculum. OX NCBI_TaxID=1714259 {ECO:0000313|EMBL:KUO91818.1, ECO:0000313|Proteomes:UP000054659}; RN [1] {ECO:0000313|EMBL:KUO91818.1, ECO:0000313|Proteomes:UP000054659} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Jay Z.J., Beam J.P., Kozubal M.A., Jennings R.D.E., Rusch D.B., RA Inskeep W.P.; RT "The distribution, diversity and function of predominant RT Thermoproteales in high-temperature environments of Yellowstone RT National Park."; RL Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KUO91818.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LOBY01000011; KUO91818.1; -; Genomic_DNA. DR EnsemblBacteria; KUO91818; KUO91818; AT708_00395. DR Proteomes; UP000054659; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000054659}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000054659}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 326 350 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 186 356 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 386 AA; 43732 MW; 2F7613F09E48BAF2 CRC64; MRSRALLAYV GPKTLNLSYG LDEFVSLVEV AGFDVVDLMT QFGRADTRFY LGSGKAREVA KRDFDVFIAY HSLSPLQVFN LERLFRRRVI DRVLVILSIF EKRAGSTESK LQIELARFRY ELPKVKEYLR RAKMGEQLGF MGAGEYIIDA YYRHMVKRIS TIRRKLEEVR RSRVTHIAKR KEVGVPEVVI TGYTSAGKTT LFNRLVGENK LVDGKPFATL ETYSRALDLW GKRVVLTDTI GFIDDLPPVL IESFHSTLQE VIDADTILLV VDGSEPQEEI TRKLETSVET LGEVGVDRGR IILVVNKVDR VRPGDVRHLR DLFTRYFAWF VPVSAATGFG IEALKVVLFF KVPGYSIIRS TGEDGARGLR VGNVTFIPMP SRSNRG // ID A0A117SVR3_9CREN Unreviewed; 398 AA. AC A0A117SVR3; DT 13-APR-2016, integrated into UniProtKB/TrEMBL. DT 13-APR-2016, sequence version 1. DT 07-JUN-2017, entry version 8. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=AT710_02405 {ECO:0000313|EMBL:KUO92671.1}; OS Thermocladium sp. ECH_B. OC Archaea; Crenarchaeota; Thermoprotei; Thermoproteales; OC Thermoproteaceae; Thermocladium. OX NCBI_TaxID=1714261 {ECO:0000313|EMBL:KUO92671.1, ECO:0000313|Proteomes:UP000054381}; RN [1] {ECO:0000313|EMBL:KUO92671.1, ECO:0000313|Proteomes:UP000054381} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Jay Z.J., Beam J.P., Kozubal M.A., Jennings R.D.E., Rusch D.B., RA Inskeep W.P.; RT "The distribution, diversity and function of predominant RT Thermoproteales in high-temperature environments of Yellowstone RT National Park."; RL Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KUO92671.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LOBW01000011; KUO92671.1; -; Genomic_DNA. DR EnsemblBacteria; KUO92671; KUO92671; AT710_02405. DR Proteomes; UP000054381; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000054381}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000054381}. FT DOMAIN 179 350 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 398 AA; 44636 MW; 5ADDDD504A1B7AFE CRC64; MAGIGKESKG NEFIELAKAA GYDVVDLIYQ RRFIDSRFYV GSGKVKQLKQ LIEHNGATHV ITYDRLKPSQ FNNLRKELGI NVMDRVQLIL EIFNERAGDM ESKLQVRLAG LYNQLPLLRE YVRHAKKGEQ IGFMGLGEYA IDAYYKHVLK QIATIRRKLD EXTATQANRI YRRKELGMPQ VAITGYTMAG KTTLFNLLAN EEKGIDGRPF ATLSTYSRLV SFEGKRAVLT DTIGFIDDLP PLLIKSFYAT IKEVTYADAV LLVVDISEGV DEVSRKLSVS LNIFNSLGVS MQRVLLVMNK IDLLGDAASL SSINGLASDL GLRYVKVSAK MGIGINDLKR EVSNMLXDYV RLRIVGNNVP PWIFRVGTII NADNDGLILL VNRVYVPKIM KEIKAEEL // ID A0A117V349_9SPHN Unreviewed; 446 AA. AC A0A117V349; DT 13-APR-2016, integrated into UniProtKB/TrEMBL. DT 13-APR-2016, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=AQZ50_08975 {ECO:0000313|EMBL:KUR77885.1}; OS Novosphingobium sp. Fuku2-ISO-50. OC Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales; OC Sphingomonadaceae; Novosphingobium. OX NCBI_TaxID=1739114 {ECO:0000313|EMBL:KUR77885.1, ECO:0000313|Proteomes:UP000056630}; RN [1] {ECO:0000313|EMBL:KUR77885.1, ECO:0000313|Proteomes:UP000056630} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Fuku2-ISO-50 {ECO:0000313|EMBL:KUR77885.1, RC ECO:0000313|Proteomes:UP000056630}; RA Ruckert C., Winkler A., Glaeser J., Grossart H.-P., Kalinowski J., RA Glaeser S.; RT "Draft genome sequence of Novosphingobium sp. Fuku2-ISO-50 (=DSM RT 27930), a Novosphingobium acidiphilum related species isolated from a RT surface water sample of the southwest basin of Lake Grosse RT Fuchskuhle."; RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KUR77885.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LLZR01000011; KUR77885.1; -; Genomic_DNA. DR RefSeq; WP_067745682.1; NZ_KQ954289.1. DR EnsemblBacteria; KUR77885; KUR77885; AQZ50_08975. DR Proteomes; UP000056630; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000056630}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000056630}. FT DOMAIN 214 390 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 446 AA; 48873 MW; B0C4BCDF72FB1619 CRC64; MSGFEFGRNP DDLMGEVTRG AKALVVLPDL RQKGGLDAES RLDEAKGLAR AIGLEIADAF ILPIRAVRPA TLFGEGQVDR IAVACEQSGA ELVIVDGALS AIQQRNLEDK LRRKVIDRTG LILEIFGERA ATAEGRMQVE LAHLDYQAGR LVRSWTHLER QRGGFGFLGG PGETQIEADR RLIRGRMARI RRELEQVRRT RGLHRERRHR APWPVIALVG YTNAGKSTLF NRLTGATVMA EDLLFATLDP TMRAIRLPAV DKAILSDTVG FISDLPTQLV AAFRATLEEV TAADVIVHVR DVANPASADQ KREVEAILAD LGVNAEDGPT IPIIEAWNKI DLLSPEERAM REDLIAHDVP DRPAVPISAV TGEGVDVLLE RLGALLTGEA QTLELTIPMG EGQKLAWLHA HGEILSEHDT EDAQGHPASR IRVRLTPREL GRFSSL // ID A0A120IDS0_9FIRM Unreviewed; 416 AA. AC A0A120IDS0; DT 13-APR-2016, integrated into UniProtKB/TrEMBL. DT 13-APR-2016, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=AT726_11140 {ECO:0000313|EMBL:AMC09399.1}; OS Turicibacter sp. H121. OC Bacteria; Firmicutes; Erysipelotrichia; Erysipelotrichales; OC Erysipelotrichaceae; Turicibacter. OX NCBI_TaxID=1712675 {ECO:0000313|EMBL:AMC09399.1, ECO:0000313|Proteomes:UP000057144}; RN [1] {ECO:0000313|Proteomes:UP000057144} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=H121 {ECO:0000313|Proteomes:UP000057144}; RA Shamseldin A., Moawad H., Abd El-Rahim W.M., Sadowsky M.J.; RL Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP013476; AMC09399.1; -; Genomic_DNA. DR RefSeq; WP_068759602.1; NZ_CP013476.1. DR EnsemblBacteria; AMC09399; AMC09399; AT726_11140. DR KEGG; tur:AT726_11140; -. DR KO; K03665; -. DR Proteomes; UP000057144; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000057144}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000057144}. FT DOMAIN 197 363 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 156 190 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 416 AA; 47752 MW; 9ABC68DA7545A731 CRC64; MKMIKKGIIV GININNKNNF EESIIELKNL CIACDIEIVG EMEQNLKKIN PTFYMGSGKI EELRDLIEEM NAEIIVFNNE LSASQIKNIE EEVKCSIIDR TALILDIFAN RAKTREAKLQ VEVARLQYEL PRLIGANENL GRQSGGVGTK NRGAGETKLE LDRRRIEDRI ASLNKELEIL KYQRNTQKNK RKKSSIPNVA LVGYTNAGKS SVMNVLVEKF INKEDKKVFE KNMLFATLET YVRNIKLHNN KSFLLYDTVG FVGDLPHNLV KAFRSTLEEV CDADLLVHII DISNPNYKNQ IDVTNETLSQ IGADNIPMIY VYNKIDLIDL DKLDNNKILI SAKRDIGIDR LIESICEKVF EDYIRFKLKI PYSEGKMISN IMENATILDS EYIEDGVIFN IEFSEKEYVK YKQYII // ID A0A124FGL8_9THEM Unreviewed; 423 AA. AC A0A124FGL8; DT 13-APR-2016, integrated into UniProtKB/TrEMBL. DT 13-APR-2016, sequence version 1. DT 07-JUN-2017, entry version 9. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=XD58_0974 {ECO:0000313|EMBL:KUK25046.1}; OS Thermotoga sp. 50_1627. OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=1635260 {ECO:0000313|EMBL:KUK25046.1, ECO:0000313|Proteomes:UP000063297}; RN [1] {ECO:0000313|EMBL:KUK25046.1, ECO:0000313|Proteomes:UP000063297} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=50_1627 {ECO:0000313|EMBL:KUK25046.1}; RX PubMed=26787827; RA Hu P., Tom L., Singh A., Thomas B.C., Baker B.J., Piceno Y.M., RA Andersen G.L., Banfield J.F.; RT "Genome-Resolved Metagenomic Analysis Reveals Roles for Candidate RT Phyla and Other Microbial Community Members in Biogeochemical RT Transformations in Oil Reservoirs."; RL MBio 7:0-0(2016). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KUK25046.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LGFH01000012; KUK25046.1; -; Genomic_DNA. DR PATRIC; fig|1635260.4.peg.1660; -. DR Proteomes; UP000063297; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000063297}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000063297}. FT DOMAIN 196 362 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 155 189 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 423 AA; 47531 MW; BBCFCAB572A40538 CRC64; MVRTNETVGL KKVLMLTIEN SETSCEELVN LLANIGAEVV ELIEQKREFP DSRFYLGRGK IESVAEKIAH LGIDYVVVDS ELTPVQAKNL EKLLKVPVRD RTQVILDVFA KHATTKEGKI QVELARLQYE LPRLVGEGKS LSRLGGRVGT RGPGEPKLEE RRRRIHQRIA ELRKELQELR KNREQQRKLR LDSGLATVSI VGYTNAGKSC LLATLSSDRS ITVSGKLFST LAPVVRRVKL PDGRIVLFKD TVGFIRRVPH SIIEAFKSTL EEILYSDLII LLADVSDPEV IQKVNVAIDV LSELQAEKIP RLLVFNKIDL LSKENLERLS DAYPSAIFIS ALKGEGIDLL LEEVSRLLGK SEAEREFIID AKRLHLLEKY REKITIKRSI FTDEGVVVRI RAREGMLKKL ATLLGGGMET CEG // ID A0A124FHE4_9BACT Unreviewed; 451 AA. AC A0A124FHE4; DT 13-APR-2016, integrated into UniProtKB/TrEMBL. DT 13-APR-2016, sequence version 1. DT 07-JUN-2017, entry version 9. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=XD60_0268 {ECO:0000313|EMBL:KUK27519.1}; OS Acetothermia bacterium 64_32. OC Bacteria; Candidatus Acetothermia. OX NCBI_TaxID=1635286 {ECO:0000313|EMBL:KUK27519.1, ECO:0000313|Proteomes:UP000053978}; RN [1] {ECO:0000313|EMBL:KUK27519.1, ECO:0000313|Proteomes:UP000053978} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=64_32 {ECO:0000313|EMBL:KUK27519.1}; RA Hu P., Tom L., Singh A., Thomas B.C., Baker B.J., Piceno Y.M., RA Andersen G.L., Banfield J.F.; RT "Genome-resolved metagenomic analysis reveals roles for candidate RT phyla and other microbial community members in biogeochemical RT transformations in oil reservoirs."; RL MBio 7:e01669-15(2015). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KUK27519.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LGFI01000002; KUK27519.1; -; Genomic_DNA. DR PATRIC; fig|1635286.4.peg.1196; -. DR Proteomes; UP000053978; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000053978}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000053978}. FT DOMAIN 217 388 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 451 AA; 50167 MW; 7CC59002CD7DAEC9 CRC64; MGRRPGELPL IEDYLGRRAR VYREERAILV GVLPPGRLSW EEEELMVELE ALVRTAGVRV LARVVQRRAR PDPATFVGRG KVEELAALAR DLSADVLVMG DELSPAQARN LEEATGLKVV DRTQVILDIF AQRAGTREAE LAVELAQLEY LLPRLRGWGK ALTDPGGGIG TRGPGETRLE QDRRKVKRRI QAIRRRLSDA DRVREVRRKR RRQSGVPQVA IVGYTNSGKS TLFRALTGAD VLVEDKLFAT LDARVRRMEL PQGRWALAAD TVGFIRKLPH QLIPAFRATL ESVREADLLL ITVDASSPFA LEHLETVRKV LAQIFGEAQL PPRLHVLTKL DRVSSPEQKA LLSRLGLEAV PSLAVSALLG TNMEELKEEV SLILAGHFAR VQVRIPPGRQ GVIPWLSRLG QLQGVSWKDG EGLAELTLPV ARLGRLHKAR LVVEERDRIT S // ID A0A124FNR8_9ACTN Unreviewed; 438 AA. AC A0A124FNR8; DT 13-APR-2016, integrated into UniProtKB/TrEMBL. DT 13-APR-2016, sequence version 1. DT 07-JUN-2017, entry version 9. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=XD74_0662 {ECO:0000313|EMBL:KUK48776.1}; OS Actinobacteria bacterium 66_15. OC Bacteria; Actinobacteria. OX NCBI_TaxID=1635289 {ECO:0000313|EMBL:KUK48776.1, ECO:0000313|Proteomes:UP000057652}; RN [1] {ECO:0000313|EMBL:KUK48776.1, ECO:0000313|Proteomes:UP000057652} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=66_15 {ECO:0000313|EMBL:KUK48776.1}; RX PubMed=26787827; RA Hu P., Tom L., Singh A., Thomas B.C., Baker B.J., Piceno Y.M., RA Andersen G.L., Banfield J.F.; RT "Genome-Resolved Metagenomic Analysis Reveals Roles for Candidate RT Phyla and Other Microbial Community Members in Biogeochemical RT Transformations in Oil Reservoirs."; RL MBio 7:0-0(2016). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KUK48776.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LGFV01000015; KUK48776.1; -; Genomic_DNA. DR PATRIC; fig|1635289.4.peg.384; -. DR Proteomes; UP000057652; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000057652}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000057652}. FT DOMAIN 210 374 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 438 AA; 47945 MW; 153C8F164B38605B CRC64; MARDLYEVVG DTEERAVLVG IDRARSDGWT LDDDLAELRR LVDTAGAVVA GVVTQRMDRP NPRTFIGSGK AEEVERLARE AGATMVVFDD DLSPSQQANL EGLLPQVRVI DRTQLILDIF ALHAVSHEGK LQVELARLEY VLPRLRGMWG HLEAERLGGG RGARFGAGES QLESDRRLTR KRISELKREL KHVARARATQ RASRARSGVF RIALVGYTNA GKSTLLNALT DAGVLAQDQL FATLDATTRR LDLPDGRTVT LTDTVGFINK LPHGLVEAFK STLDEVREAD LLLHVVDASH ANRDAQMAAV KVVLQEIGAS GRPQLVVYNK CDLLPAGECE RLSSAPGAVV VSGATGMGLE TLLERIATIA AQGDVPLTVT LPYDRGDLVR IAHEHGHILS EEHLPEGTRL TVVLTDEIRG RFSEYLPVHE PEPEDWET // ID A0A124HAV8_9ACTN Unreviewed; 497 AA. AC A0A124HAV8; DT 13-APR-2016, integrated into UniProtKB/TrEMBL. DT 13-APR-2016, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=AQI88_39870 {ECO:0000313|EMBL:KUM89348.1}; OS Streptomyces cellostaticus. OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae; OC Streptomyces. OX NCBI_TaxID=67285 {ECO:0000313|EMBL:KUM89348.1, ECO:0000313|Proteomes:UP000054241}; RN [1] {ECO:0000313|EMBL:KUM89348.1, ECO:0000313|Proteomes:UP000054241} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 40189 {ECO:0000313|EMBL:KUM89348.1, RC ECO:0000313|Proteomes:UP000054241}; RA Ruckert C., Winkler A., Kalinowski J., Kampfer P., Glaeser S.; RT "Draft genome sequence of Streptomyces cellostaticus DSM 40189, type RT strain for the species Streptomyces cellostaticus."; RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KUM89348.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LMWL01000092; KUM89348.1; -; Genomic_DNA. DR RefSeq; WP_067010202.1; NZ_KQ948059.1. DR EnsemblBacteria; KUM89348; KUM89348; AQI88_39870. DR Proteomes; UP000054241; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 2. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000313|EMBL:KUM89348.1}; KW Complete proteome {ECO:0000313|Proteomes:UP000054241}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900, KW ECO:0000313|EMBL:KUM89348.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000054241}. FT DOMAIN 275 440 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 497 AA; 54343 MW; 35589794A0BE4E2E CRC64; MTSSSSPSQD TKRLAHDYPE GLRADALMEE DVAWSHEIDG ERDGEQFDRS ERAALRRVAG LSTELEDVTE VEYRQLRLER VVLVGVWTTG TVQDADNSLA ELAALAETAG ALVLDGVIQR RDKPDAATYI GSGKALELRD IVLETGADTV ICDGELSPGQ LIQLEDVVKV KVIDRTALIL DIFAQHAKSR EGKAQVSLAQ MQYMLPRLRG WGQSLSRQMG GGKGGGLATR GPGETKIETD RRRIREKMAK MRREIADMKT GREIKRQERR RHKVPSVAIA GYTNAGKSSL LNRLTGAGVL VENALFATLD PTVRRAETPS GRLYTLADTV GFVRHLPHHL VEAFRSTMEE VGDSDLILHV VDGSHPVPEE QLAAVREVIR DVGATDVPEI VVINKADAAD PLVLQRLLRV EKRSIAVSAR TGQGIEELLA LIDNDLPRPS VEIEAVVPYT HGKLVARAHT EGEVISEEHT AEGTLLKVRV HEELAADLAP YVPASLA // ID A0A124IH35_9SPHN Unreviewed; 422 AA. AC A0A124IH35; DT 13-APR-2016, integrated into UniProtKB/TrEMBL. DT 13-APR-2016, sequence version 1. DT 12-APR-2017, entry version 8. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=APF82_03510 {ECO:0000313|EMBL:KUO52100.1}; OS Sphingomonadales bacterium BRH_c42. OC Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales; OC unclassified Sphingomonadales. OX NCBI_TaxID=1734407 {ECO:0000313|EMBL:KUO52100.1, ECO:0000313|Proteomes:UP000054281}; RN [1] {ECO:0000313|EMBL:KUO52100.1, ECO:0000313|Proteomes:UP000054281} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BRH_c42 {ECO:0000313|EMBL:KUO52100.1}; RA Bagnoud A., Chourey K., Hettich R.L., De Bruijn I., Andersson A.F., RA Leupin O.X., Schwyn B., Bernier-Latmani R.; RT "Microbial metabolic network in the subsurface."; RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KUO52100.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LOEX01000118; KUO52100.1; -; Genomic_DNA. DR Proteomes; UP000054281; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000054281}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000054281}. FT DOMAIN 192 367 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 422 AA; 46513 MW; 8F9EA1869AC9FBDF CRC64; MVLCPEIKGQ RHDLDGKGRL DEACGLALAI GLQIVEASLL PVRSVRANTL FGSGQVERIA ADCELHSAEL VVVDGALSAI QQRNLEEKLG RKVIDRTGLI LEIFGERAAT AEGRLQVELA HLDYQQSRLV RSWTHLERQR GGFGFLGGPG ETQIEADRRM IRQRMGRLRR ELEQVRKTRK LHRGRREKAP WPVIALVGYT NAGKSSLFNR LTGSDVMAED LLFATLDPTM RAIGLPGIEK AILSDTVGFI SDLPTQLVAA FRATLEEVTS ADLILHVRDM ANAAHSAQKK QVMAVLADLG IVDLQSGESS IPILEVWNKI DLLAPEEAQE LDRVCRERED AVAISAVTGE GIEPLLDRVS QMLTGEAREF ELLLPASDGR RIAWLHAHGE VISDEESTGT GEALRKLVVR LNPKEFGQFR SL // ID A0A125BDT4_THIDE Unreviewed; 463 AA. AC A0A125BDT4; DT 13-APR-2016, integrated into UniProtKB/TrEMBL. DT 13-APR-2016, sequence version 1. DT 30-AUG-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=ABW22_00400 {ECO:0000313|EMBL:KVW99662.1}; OS Thiobacillus denitrificans. OC Bacteria; Proteobacteria; Betaproteobacteria; Nitrosomonadales; OC Thiobacillaceae; Thiobacillus. OX NCBI_TaxID=36861 {ECO:0000313|EMBL:KVW99662.1, ECO:0000313|Proteomes:UP000064243}; RN [1] {ECO:0000313|EMBL:KVW99662.1, ECO:0000313|Proteomes:UP000064243} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=RG {ECO:0000313|EMBL:KVW99662.1, RC ECO:0000313|Proteomes:UP000064243}; RX PubMed=26712544; RA Harrold Z.R., Skidmore M.L., Hamilton T.L., Desch L., Amada K., RA van Gelder W., Glover K., Roden E.E., Boyd E.S.; RT "Aerobic and Anaerobic Thiosulfate Oxidation by a Cold-Adapted, RT Subglacial Chemoautotroph."; RL Appl. Environ. Microbiol. 82:1486-1495(2015). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KVW99662.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LDUG01000002; KVW99662.1; -; Genomic_DNA. DR RefSeq; WP_059750810.1; NZ_LDUG01000002.1. DR EnsemblBacteria; KVW99662; KVW99662; ABW22_00400. DR PATRIC; fig|36861.3.peg.1114; -. DR Proteomes; UP000064243; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000064243}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000064243}. FT DOMAIN 238 408 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 196 230 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 463 AA; 51407 MW; 56867328F260BE24 CRC64; MQNEVKEKPQ YAVVAAVQLP GVNDVEFEAS LTELRELAKT LGFTVTRTFT QKRSGFDSTA YLGVGKRQEI RRFVNSEAGD ETESDHAPQN SLHRLSTFVE GLVDDVSPDP IDVIFVDHEI SPSQARHLEK EVGCQVMDRT MVILEIFHRN ARSPAARAQV EIARLGYLAP RLREAAKLAG PQGRQRSGVG GRGAGESHTE LDKRKIRDRI AELQKEITAM DVERKTQRAR RQAHQGLASV ALVGYTNAGK STLMRALTGS EVLVANKLFA TLDTTVRSLH PESIPRVLVS DTVGFIKNLP HGLVASFKST LEEALDASLL LHVIDASDPG FERQIETTEE VLKEIDAQDV PRFRIFNKID HVGDAAAQAE REAALRAEYP GCIVMSARRP DDVAKLHKAI VAFFQQDLVE AELFLPWSAQ QLRGEIFARC EVLDERADEE GAFFRVRGEQ ETLNSLREQL GQA // ID A0A125Q8J1_9BRAD Unreviewed; 464 AA. AC A0A125Q8J1; DT 13-APR-2016, integrated into UniProtKB/TrEMBL. DT 13-APR-2016, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=AS156_01260 {ECO:0000313|EMBL:KWV54380.1}; OS Bradyrhizobium sp. BR 10303. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Bradyrhizobiaceae; Bradyrhizobium. OX NCBI_TaxID=1755647 {ECO:0000313|EMBL:KWV54380.1, ECO:0000313|Proteomes:UP000057737}; RN [1] {ECO:0000313|EMBL:KWV54380.1, ECO:0000313|Proteomes:UP000057737} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BR 10303 {ECO:0000313|EMBL:KWV54380.1, RC ECO:0000313|Proteomes:UP000057737}; RA Zelli J.E., Simoes-Araujo J.L., Barauna A.C., Silva K.; RT "Draft Genome Sequence of the Strain BR 10303 (Bradyrhizobium sp.) RT isolated from nodules of Centrolobium paraense."; RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KWV54380.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LNCU01000072; KWV54380.1; -; Genomic_DNA. DR RefSeq; WP_066508299.1; NZ_LNCU01000072.1. DR EnsemblBacteria; KWV54380; KWV54380; AS156_01260. DR Proteomes; UP000057737; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000057737}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}. FT DOMAIN 229 405 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 464 AA; 51397 MW; 7BC11D8EC19E4755 CRC64; MEPFNREGGA DRTKSRPGSA GDSNTGRVIV IGPYLRARRG DGDGQSDASV RDYEARIEEA AGLARAIDLA VVESVVAVIS QIRPATYLGK GKVEEFTGLI AGNAIELVVM DCALSPIQQR NLEKAWSTKV LDRTGLILEI FGRRAKTKEG ALQVELAHLN YQRSRLVRSW THLERQRGGF GFMGGPGETQ IEADRRLISE RITKLEGELK KVQATRRLHR AGRQRVPYRV VALVGYTNAG KSTLFNRLTR SDVQAADMLF ATLDPTLRAL NLPHGGKAML SDTVGFISNL PTQLVAAFRA TLEEVLEADI ILHVRDISHE DAEAQERDVE AVLRQLGIDP DADGGQRIIE VWNKVDRFDP DERENLRNIA ARRPPERPCF LVSAASGERI DELLSAIEDR LAAKRMTLHL SIDASDGAGI SWLHRNAEVL NKELRGERFD MTVRVDETKR DIVMSRFDAV PSGA // ID A0A125S1T7_9FLAO Unreviewed; 400 AA. AC A0A125S1T7; DT 13-APR-2016, integrated into UniProtKB/TrEMBL. DT 13-APR-2016, sequence version 1. DT 07-JUN-2017, entry version 13. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=AXF12_00695 {ECO:0000313|EMBL:AMD84181.1}; OS Capnocytophaga haemolytica. OC Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales; OC Flavobacteriaceae; Capnocytophaga. OX NCBI_TaxID=45243 {ECO:0000313|EMBL:AMD84181.1, ECO:0000313|Proteomes:UP000065822}; RN [1] {ECO:0000313|EMBL:AMD84181.1, ECO:0000313|Proteomes:UP000065822} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CCUG 32990 {ECO:0000313|EMBL:AMD84181.1, RC ECO:0000313|Proteomes:UP000065822}; RA Wen L., He K., Yang H.; RL Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP014227; AMD84181.1; -; Genomic_DNA. DR RefSeq; WP_066427694.1; NZ_FOVX01000005.1. DR EnsemblBacteria; AMD84181; AMD84181; AXF12_00695. DR KEGG; chg:AXF12_00695; -. DR KO; K03665; -. DR Proteomes; UP000065822; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000065822}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000065822}. FT DOMAIN 200 385 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 400 AA; 45640 MW; 74A4F745976180FF CRC64; MLEKTDLSYE KVVLVGIVNQ SQDEQKSKEY LDELEFLTFT AGGEVLARFT QKLDVPNPKT FIGTGKLEEV AAFVVENEVG TVVFDDELTP AQQKNIEREL KVKILDRTGL ILDIFAQRAQ TSYARTQVEL AQYEYLLPRL TGLWTHLERQ RGGIGMRGPG ETEIETDRRI VRDRIALLKK KLTAIDKQMA TQRSNRGALV RVALIGYTNV GKSTLMNVIS KSEVFAENKL FATLDTTVRK VVIENLPFLL SDTVGFIRKL PTQLVESFKS TLDEVREADL LLHVVDISHP NFEEHIASVN QILGEIGCAD KPVIMVFNKI DAYRHEVIAA DDLATERTSR HFTLEDWRAT WMQKMGADVL FISALNKENL EEFRQVVYEK VKGIHITRFP YNNFLYEKIE // ID A0A125TZB3_9GAMM Unreviewed; 432 AA. AC A0A125TZB3; DT 13-APR-2016, integrated into UniProtKB/TrEMBL. DT 13-APR-2016, sequence version 1. DT 07-JUN-2017, entry version 10. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=AZ78_5130 {ECO:0000313|EMBL:KWS01997.1}; OS Lysobacter capsici AZ78. OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales; OC Xanthomonadaceae; Lysobacter. OX NCBI_TaxID=1444315 {ECO:0000313|EMBL:KWS01997.1, ECO:0000313|Proteomes:UP000023435}; RN [1] {ECO:0000313|EMBL:KWS01997.1, ECO:0000313|Proteomes:UP000023435} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=AZ78 {ECO:0000313|EMBL:KWS01997.1, RC ECO:0000313|Proteomes:UP000023435}; RX PubMed=24762937; RA Puopolo G., Sonego P., Engelen K., Pertot I.; RT "Draft Genome Sequence of Lysobacter capsici AZ78, a Bacterium RT Antagonistic to Plant-Pathogenic Oomycetes."; RL Genome Announc. 2:0-0(2014). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KWS01997.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JAJA02000003; KWS01997.1; -; Genomic_DNA. DR RefSeq; WP_036114116.1; NZ_JAJA02000003.1. DR EnsemblBacteria; KWS01997; KWS01997; AZ78_5130. DR Proteomes; UP000023435; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000023435}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000023435}. FT DOMAIN 199 364 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 158 192 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 432 AA; 47343 MW; B8B2A8A2B00EB142 CRC64; MFERSKKGEH ALLIQPHAGG APDEDLLEEF ADLARSAGAT VAAVITARID KPNAAILIGS GKLDEVKAAA DASGADLILV NHRLSPGQER NLEKLLERRV VDRTGLILDI FSQRAHSAEG KLQVELAQLK HMSTRLIRGW THLERQRGGS IGLRGPGETQ LETDRRLLQK RLEQLQKRLD KVEVQRTQMR RARMRSELPR VALVGYTNAG KSTLFNAMTG ADAYAADQLF ATLDPTVRRI DLPGGGAVLA DTVGFVRDLP HDLVAAFRST LSEAREADLL LHVIDAADPL RDERIAQVDE VLADIGAGDL PQLLVFNKID RLDDVAPRID RPGEGKNRVW VSARDGKGLD LLREALGEAL QLRHVTGSVR IASQDARLRA RLHELGAVRS EQADEHGWVV EVDLAVTDAE RLFAQANGEA LRPLLETVQA PT // ID A0A126NT70_9BRAD Unreviewed; 463 AA. AC A0A126NT70; DT 11-MAY-2016, integrated into UniProtKB/TrEMBL. DT 11-MAY-2016, sequence version 1. DT 07-JUN-2017, entry version 10. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=AXW83_07475 {ECO:0000313|EMBL:AMJ60160.1}; OS Bosea sp. PAMC 26642. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Bradyrhizobiaceae; Bosea. OX NCBI_TaxID=1792307 {ECO:0000313|EMBL:AMJ60160.1, ECO:0000313|Proteomes:UP000061184}; RN [1] {ECO:0000313|Proteomes:UP000061184} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=PAMC 26642 {ECO:0000313|Proteomes:UP000061184}; RA Park H.; RT "Complete genome of Burkholderia sp."; RL Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP014301; AMJ60160.1; -; Genomic_DNA. DR RefSeq; WP_066611989.1; NZ_CP014301.1. DR EnsemblBacteria; AMJ60160; AMJ60160; AXW83_07475. DR KEGG; bop:AXW83_07475; -. DR KO; K03665; -. DR Proteomes; UP000061184; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000061184}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000061184}. FT DOMAIN 229 403 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 463 AA; 50923 MW; 07F2BEA0657166D7 CRC64; MSGRKGAEDG EPVAKPLDEI EREIAANTRA YVIGPYSQRR GGAGTTEANQ RSFAARLDEA VGLAAAIDLT VVEPIQVMLT AFRPATYLGK GKVEEIAERI KIEEIGLVVM DCALSPVQQR NLEKAFGCKV IDRTGLILEI FGRRARTREG TLQVELAHLN YQKSRLVRSW THLERQRGGF GFLGGPGETQ IEADRRIIQE RMTKIERDLE SVKRTRGLHR ASRKRVPYPV VALVGYTNAG KSTLFNRLTS AEVLAQDMLF ATLDPTARAL KLPHGARIML SDTVGFISDL PTQLVAAFRA TLEDAIEADV LLHVRDVSHE DTQAQAADVQ GILRDLGIDP DDGQRVVEVW NKSDLLDEAE RERQLGLAAL KPEVSRPVLV SALTGDGIGR LTDAIEVRIA KSRPVYRLML APGDGKSLAW LHANGEILDR EDAEDGALNL LVRLPPEREG AFGARFPEAE RQG // ID A0A126PGE9_9BACT Unreviewed; 408 AA. AC A0A126PGE9; DT 11-MAY-2016, integrated into UniProtKB/TrEMBL. DT 11-MAY-2016, sequence version 1. DT 05-JUL-2017, entry version 12. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=AXW84_01900 {ECO:0000313|EMBL:AMJ67973.1}; OS Hymenobacter sp. PAMC 26628. OC Bacteria; Bacteroidetes; Cytophagia; Cytophagales; Hymenobacteraceae; OC Hymenobacter. OX NCBI_TaxID=1484118 {ECO:0000313|EMBL:AMJ67973.1, ECO:0000313|Proteomes:UP000059956}; RN [1] {ECO:0000313|EMBL:AMJ67973.1, ECO:0000313|Proteomes:UP000059956} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=PAMC26628 {ECO:0000313|EMBL:AMJ67973.1, RC ECO:0000313|Proteomes:UP000059956}; RA Wen L., He K., Yang H.; RL Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP014304; AMJ67973.1; -; Genomic_DNA. DR EnsemblBacteria; AMJ67973; AMJ67973; AXW84_01900. DR Proteomes; UP000059956; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000059956}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000059956}. FT DOMAIN 199 390 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 408 AA; 45607 MW; B1140C919CBC3355 CRC64; MHATAAEHET AVLVSVPPRR QTEAQTTEYL DELAFLVETA GATATQRFVQ RLEKPDVRSY VGEGKLAEIK AYVQHEGSSM VVFDDDLSAS QLRNLEAELK VKIVDRSLLI LDIFALRAKS ATARTQVELA QYQYLLPRLT GLWTHLDRQR GGVGTKGPGE TEIETDRRIV RDRIDFLKEK LETLDKQATT RRKDRGGVVR ASLVGYTNVG KSTLMNVLGK TDVFAENKLF ATVDATTRKV VLEGTPFLLS DTVGFIRKLP TKLIESFKST LDEIREADLL LHVVDISHPN FEEQIQVVND TLLEIGAADK PLLLVFNKID QYRPDEIPDD DFAAEAAGAE RETAARPPLA QLQATYMAKL HDPVVFVSAQ TKENLDELRQ LLGQRVAALH QQRYPHLAAG EYGEYEAE // ID A0A126RN16_9SPHN Unreviewed; 443 AA. AC A0A126RN16; DT 11-MAY-2016, integrated into UniProtKB/TrEMBL. DT 11-MAY-2016, sequence version 1. DT 07-JUN-2017, entry version 10. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=K426_12970 {ECO:0000313|EMBL:AMK23527.1}; OS Sphingobium sp. TKS. OC Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales; OC Sphingomonadaceae; Sphingobium. OX NCBI_TaxID=1315974 {ECO:0000313|EMBL:AMK23527.1, ECO:0000313|Proteomes:UP000060779}; RN [1] {ECO:0000313|Proteomes:UP000060779} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=TKS {ECO:0000313|Proteomes:UP000060779}; RA Tabata M.; RT "Whole genome sequence of gamma-HCH degrading bacterium Sphingobium RT sp. TKS."; RL Submitted (APR-2013) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP005083; AMK23527.1; -; Genomic_DNA. DR RefSeq; WP_066557671.1; NZ_CP005083.1. DR EnsemblBacteria; AMK23527; AMK23527; K426_12970. DR PATRIC; fig|1315974.3.peg.2731; -. DR Proteomes; UP000060779; Chromosome 1. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0016810; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds; IEA:InterPro. DR CDD; cd01878; HflX; 1. DR Gene3D; 2.30.40.10; -; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR011059; Metal-dep_hydrolase_composite. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000060779}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}. FT DOMAIN 209 389 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 443 AA; 48234 MW; 7926FA9CFA0DBACA CRC64; MAVFNRDSAD EVSRGARAIV VRADVHGPER RDSDARLEEA RGLALAIGID VRAAQAFRVR DRKPATLFGS GQVDQIATLA RSEEAELVIV DNALSPVQQS NLEKATETKV IDRTGLILEI FGERAATNEG RLQVELAHLD YQAGRLVRSW THLERQRGGF GFLGGPGETQ IEADRRMIRD RMAKIRRELD QVTKTRGLHR ARRQRAPWPV IALVGYTNAG KSTLFNRMTG ADVMAEDLLF ATLDPTMRQI ALPGLDKAIL SDTVGFVSDL PTQLIAAFRA TLEEVLSADL IVHVRDIAHP DSDAQRDDVI DVLSELGVAG EGALEAGEGN EPPPIIEAWN KLDLLDDDAV ALAREAAARR DDVVILSALT GEGVDGLQRT ISARLTSGAQ VHQLRVSLAD GAAMAWLHEH GEVIGSQSQG DDMLVDVRLS DSALARFVKR RGN // ID A0A126T7W7_9GAMM Unreviewed; 421 AA. AC A0A126T7W7; DT 06-JUL-2016, integrated into UniProtKB/TrEMBL. DT 06-JUL-2016, sequence version 1. DT 07-JUN-2017, entry version 10. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=JT25_017085 {ECO:0000313|EMBL:AMK78177.1}; OS Methylomonas denitrificans. OC Bacteria; Proteobacteria; Gammaproteobacteria; Methylococcales; OC Methylococcaceae; Methylomonas. OX NCBI_TaxID=1538553 {ECO:0000313|EMBL:AMK78177.1, ECO:0000313|Proteomes:UP000030512}; RN [1] {ECO:0000313|EMBL:AMK78177.1, ECO:0000313|Proteomes:UP000030512} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=FJG1 {ECO:0000313|EMBL:AMK78177.1, RC ECO:0000313|Proteomes:UP000030512}; RX PubMed=25580993; DOI=10.1111/1462-2920.12772; RA Kits K.D., Klotz M.G., Stein L.Y.; RT "Methane oxidation coupled to nitrate reduction under hypoxia by the RT Gammaproteobacterium Methylomonas denitrificans, sp. nov. type strain RT FJG1."; RL Environ. Microbiol. 17:3219-3232(2015). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP014476; AMK78177.1; -; Genomic_DNA. DR RefSeq; WP_036274701.1; NZ_CP014476.1. DR EnsemblBacteria; AMK78177; AMK78177; JT25_017085. DR KEGG; mdn:JT25_017085; -. DR KO; K03665; -. DR Proteomes; UP000030512; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000030512}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000030512}. FT DOMAIN 196 363 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 421 AA; 46805 MW; 1E20D215D335B084 CRC64; MFERPDAGER AILVHLNLQA GQEDLDELKE LTKSAGAQPT HVVTGSRYRP DPKYFVGTGK VEEIRSAIIE HEANIVIVNH PLTPSQERNL EKVLEVRVVD RNGLILDIFA QRAQTFEGKL QVELAQLKHL STRLIRGWTH LERQKGGIGL RGPGETQLET DRRLLAVRIK QIQQRLGKVE KQRHQGRSKR KKAEIPTVSL VGYTNAGKST LFNTLTGADI YAADQLFATL DPTLRQLSLS NGGEIILADT VGFIRHLPHE LVAAFRSTLQ EASEADLLLH VIDAAAEDRE DTIYQVNQVL NDIDAAKIPQ LMVFNKIDLL EDVAPHIDYD ADGKPVSVWI SAQNGVGCDL LQQALSELFA SSKVIRKCYL PASQAGLKAK LFTFVKIIDE VNNDSGDCEL TIEIDRKHLG LLKGIDVHEQ V // ID A0A126V2Y9_9RHOB Unreviewed; 426 AA. AC A0A126V2Y9; DT 08-JUN-2016, integrated into UniProtKB/TrEMBL. DT 08-JUN-2016, sequence version 1. DT 07-JUN-2017, entry version 9. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=RC74_16795 {ECO:0000313|EMBL:AML52701.1}; OS Halocynthiibacter arcticus. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae; Halocynthiibacter. OX NCBI_TaxID=1579316 {ECO:0000313|EMBL:AML52701.1, ECO:0000313|Proteomes:UP000070371}; RN [1] {ECO:0000313|EMBL:AML52701.1, ECO:0000313|Proteomes:UP000070371} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=PAMC 20958 {ECO:0000313|EMBL:AML52701.1}; RA Lee Y.M., Baek K., Lee H.K., Shin S.C.; RT "Complete genome sequence of Halocynthiibacter arcticus PAMC 20958t RT from arctic marine sediment."; RL Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP014327; AML52701.1; -; Genomic_DNA. DR RefSeq; WP_039003555.1; NZ_CP014327.1. DR EnsemblBacteria; AML52701; AML52701; RC74_16795. DR KEGG; hat:RC74_16795; -. DR KO; K03665; -. DR Proteomes; UP000070371; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000070371}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000070371}. FT DOMAIN 206 375 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 165 199 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 426 AA; 48082 MW; D83416A5EA301663 CRC64; MGEEIPEKSV TPVWVLHPDL RNDRFRRDPE FALQEAVSLA EAMPETDVVG ATIVPVPKIR AGWLFGKGKT EELKQQFVET HVDLVIIDGT LTPVQQRNLE EEWNVKILDR TGLILEIFSD RARTREGVLQ VEVAALSYQR TRLVRAWTHL ERQRGGLGFV GGPGETQVEA DRRALDERIQ NLKRQLEKVV RTRALHRQSR ARVPFPVVAL VGYTNAGKST LFNRLTGANV FAKDMLFATL DPTMRSVELP SGRTIILSDT VGFISELPTQ LVASFRATLE EVLEADLILH VRDISHPLTD QQSRDVTTIM TDLGVSKETP LIEVWNKVDL LDAQEQEGIL AKSEREEAIF ATSSITGQGI EELLDAVSET LTDPKTYRDL VLPYSDGKKR AWLFSEDLVE AETQGEDGFH LKVHWTARQE KNFRDM // ID A0A126Z2P4_9MICO Unreviewed; 511 AA. AC A0A126Z2P4; DT 08-JUN-2016, integrated into UniProtKB/TrEMBL. DT 08-JUN-2016, sequence version 1. DT 07-JUN-2017, entry version 10. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=AX769_10900 {ECO:0000313|EMBL:AMM20561.1}; OS Frondihabitans sp. PAMC 28766. OC Bacteria; Actinobacteria; Micrococcales; Microbacteriaceae; OC Frondihabitans. OX NCBI_TaxID=1795630 {ECO:0000313|EMBL:AMM20561.1, ECO:0000313|Proteomes:UP000070552}; RN [1] {ECO:0000313|EMBL:AMM20561.1, ECO:0000313|Proteomes:UP000070552} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=PAMC28744 {ECO:0000313|Proteomes:UP000070552}; RA Park H.; RT "Complete genome of Frondihabitans sp."; RL Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP014513; AMM20561.1; -; Genomic_DNA. DR RefSeq; WP_066279137.1; NZ_CP014513.1. DR EnsemblBacteria; AMM20561; AMM20561; AX769_10900. DR KEGG; frp:AX769_10900; -. DR KO; K03665; -. DR Proteomes; UP000070552; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 2. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000070552}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000070552}. FT DOMAIN 293 458 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 511 AA; 55994 MW; B7134F6E3667166E CRC64; MTEDGTTSTE REQQDDVVDR ILRGSEARAG LSVFSPAQAI QTQGLTRPVD YQGTPGDDGD QFDREDRQAL RRVAGLSTEL EDVTEVEYRQ LRLENVVLIG VYSQGTLQDA ENSLRELAAL AETAGAVVLD GLLQRRPHPD PSTYLGSGKA LELKQTVMAL GADTVIADTE LAPSQRRALE DVVKVKVIDR TAVILDIFSQ HAKSREGKAQ VELAQLEYLL PRLRGWGESM SRQAGGQVGG AGAGMGSRGP GETKIELDRR RIHTRMAILR KKIKEMKPAR VAKRANRVRN TVPSVAIAGY TNAGKSSLLN RLTRAGVLVE NALFATLDAT VRKSMTDDGR PFTYSDTVGF VRNLPHQLVE AFRSTLEEVE DSDIIVHVVD GSHPDPAAQL ATVRDVITEV DGRDIPEVVV FNKSDLVDDS QRLVLQGMVP DAIFVSARTG EGIDELRARI AELLPRPEVE LDLLVPYDRG EVIARIHEIG RVVDVEYLPE GTRVTARVYP QDASGLQQFV S // ID A0A126Z7S7_9BURK Unreviewed; 390 AA. AC A0A126Z7S7; DT 08-JUN-2016, integrated into UniProtKB/TrEMBL. DT 08-JUN-2016, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=AX767_00710 {ECO:0000313|EMBL:AMM23056.1}; OS Variovorax sp. PAMC 28711. OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Comamonadaceae; Variovorax. OX NCBI_TaxID=1795631 {ECO:0000313|EMBL:AMM23056.1, ECO:0000313|Proteomes:UP000070169}; RN [1] {ECO:0000313|EMBL:AMM23056.1, ECO:0000313|Proteomes:UP000070169} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=PAMC 28711 {ECO:0000313|EMBL:AMM23056.1, RC ECO:0000313|Proteomes:UP000070169}; RA Park H.; RT "Complete genome of Variovorax sp."; RL Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP014517; AMM23056.1; -; Genomic_DNA. DR RefSeq; WP_068627909.1; NZ_CP014517.1. DR EnsemblBacteria; AMM23056; AMM23056; AX767_00710. DR KEGG; vaa:AX767_00710; -. DR KO; K03665; -. DR Proteomes; UP000070169; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000070169}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000070169}. FT DOMAIN 200 373 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 390 AA; 43129 MW; A55B46F1C48AD814 CRC64; MSELIPRQEG AAILVGVDFG LPHFDGELEE LGLLAETAGL TPVARIVCKR KAPDAALFVG SGKADEIKAL AEMHRASEVI FDQTISPAQQ RNLERQLDVA VYDRTFLILE IFAQRARSHE GKLQVELARL QYLSTRLVRR WSHLERQTGG AGVRGGPGEK QIELDRRMIG ESIKRTRERL AKVQKQRGTQ RRQRERRETY NISLVGYTNA GKSSIFNALV KARAYAADQL FATLDTTTRN LYLGDARRQV SISDTVGFIR DLPHGLVDAF KATLQEAVDA DLLIHVVDAS NPHHPEQMAE VQSVLKDIGA DAVPQLVVFN KIDALESVQR PLHLVDDMEI DGTRVPRVFL SAHTGEGVPA LRAELAQRSG SLSAQDMTLA QDAELHDAAD // ID A0A127A0G0_9MICC Unreviewed; 535 AA. AC A0A127A0G0; DT 08-JUN-2016, integrated into UniProtKB/TrEMBL. DT 08-JUN-2016, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=SA2016_1695 {ECO:0000313|EMBL:AMM32371.1}; OS Sinomonas atrocyanea. OC Bacteria; Actinobacteria; Micrococcales; Micrococcaceae; Sinomonas. OX NCBI_TaxID=37927 {ECO:0000313|EMBL:AMM32371.1, ECO:0000313|Proteomes:UP000070134}; RN [1] {ECO:0000313|EMBL:AMM32371.1, ECO:0000313|Proteomes:UP000070134} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=KCTC 3377 {ECO:0000313|EMBL:AMM32371.1, RC ECO:0000313|Proteomes:UP000070134}; RA Kim K.M.; RT "Complete genome of Sinomonas atrocyanea KCTC 3377."; RL Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP014518; AMM32371.1; -; Genomic_DNA. DR RefSeq; WP_066497282.1; NZ_CP014518.1. DR EnsemblBacteria; AMM32371; AMM32371; SA2016_1695. DR KEGG; satk:SA2016_1695; -. DR PATRIC; fig|37927.3.peg.1745; -. DR KO; K03665; -. DR Proteomes; UP000070134; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 2. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000070134}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000070134}. FT DOMAIN 314 479 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 535 AA; 57990 MW; CE5391C56FADBFB3 CRC64; MTDEQHTTGS SRAAGGSDAP QDLSPADIQA VIDRILAKEE AATAKGSRAD QRSERPRGAL GDGRALAISD VETEHGDYDG DQQDLAERRA LRRVAGLSTE LEDITEVEYR QLRLERVVLA GLWSEGTLED AENSLRELAA LAETAGSEVL DGVVQRRQKP DAGTFLGSGK ALELRDIVAA TGADTVVVDS ELSPSQRRGL EDIVKVKVID RTALILDIFA QHAKSREGKA QVELAQLEYL LPRLRGWGES MSRQAGGRVG AAGGGIGSRG PGETKIELDR RRIRTRMAKL RREIAGMKPA RETKRANRKR NEVPSVAIAG YTNAGKSSLL NRLTDAGVLV QNALFATLDP TVRRAETPDG LPYTLADTVG FVRSLPTQLV EAFRSTLEEV ADADLILHVV DASHPDPEGQ IAAVRAVLAD VDARKVPEII VLNKADAADP FVLERLRQRE PRHVVVSART GQGIAELKEA ISDAIPRPDV ALTILVPYSR GDILNRLHTS SAEIRSLEHV ESGTRVEVVV REEFAAELEP FVVHD // ID A0A127AQY5_9DELT Unreviewed; 488 AA. AC A0A127AQY5; DT 08-JUN-2016, integrated into UniProtKB/TrEMBL. DT 08-JUN-2016, sequence version 1. DT 07-JUN-2017, entry version 9. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=HS1_001959 {ECO:0000313|EMBL:AMM41751.1}; OS Candidatus Desulfofervidus auxilii. OC Bacteria; Proteobacteria; Deltaproteobacteria; OC Candidatus Desulfofervidaceae; Candidatus Desulfofervidus. OX NCBI_TaxID=1621989 {ECO:0000313|EMBL:AMM41751.1, ECO:0000313|Proteomes:UP000070560}; RN [1] {ECO:0000313|EMBL:AMM41751.1, ECO:0000313|Proteomes:UP000070560} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=HS1 {ECO:0000313|EMBL:AMM41751.1, RC ECO:0000313|Proteomes:UP000070560}; RA Krukenberg V., Richter M., Wegener G.; RT "Candidatus Desulfofervidus auxilii, a hydrogenotrophic sulfate- RT reducing bacterium involved in the thermophilic anaerobic oxidation of RT methane."; RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP013015; AMM41751.1; -; Genomic_DNA. DR EnsemblBacteria; AMM41751; AMM41751; HS1_001959. DR PATRIC; fig|1621989.3.peg.2098; -. DR Proteomes; UP000070560; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000070560}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000070560}. FT DOMAIN 315 479 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 274 301 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 488 AA; 55454 MW; FFC830314B004074 CRC64; MVVGDQKGIL LPDLSRYRSG LTRLRGLRCL HTHLIEEGLN EEDLTDLALL RLDLMGTIVM DERGIPRYYH LAHLLPVNEN GCGWRVLKPI SYGHLQIKFD QLISALEEEF QRVQKAHSIK ENKDKAILIH VANSGEKTEP ETSLTELSEL ANTAGVEIVD KVVQKRRYIN PKFFIGKGKL AEVIIRALQS GANLLIFDHE LNPSQANAIA KFTDLRVIDR TQLILDIFAQ RAKSREGKIQ VEMAQLKYVL PRLVKQDASM SRLAGGIGGR GPGETKLEID RRRIKKRLHH LQKELKNIQA QRMQRRIKRR RMQLPIISII GYTNAGKSTL LNTLTKSDIL AENRLFATLD PTSRRLRFPS EKEAIITDTV GFIRNLPKEL FDAFAATLEE LYEAHLLIHL IDISNPCFPD HITSVEEILS QLQLAHIPTL RVFNKKDLVS EGYVKQQCKR YNAIAISALK SETLLPLLEE IEKILGKLAY SKVFRSAV // ID A0A127B1Y3_9BACT Unreviewed; 402 AA. AC A0A127B1Y3; DT 08-JUN-2016, integrated into UniProtKB/TrEMBL. DT 08-JUN-2016, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=TH61_08745 {ECO:0000313|EMBL:AMM51244.1}; OS Rufibacter sp. DG15C. OC Bacteria; Bacteroidetes; Cytophagia; Cytophagales; Hymenobacteraceae; OC Rufibacter. OX NCBI_TaxID=1379909 {ECO:0000313|EMBL:AMM51244.1, ECO:0000313|Proteomes:UP000070672}; RN [1] {ECO:0000313|EMBL:AMM51244.1, ECO:0000313|Proteomes:UP000070672} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DG15C {ECO:0000313|EMBL:AMM51244.1, RC ECO:0000313|Proteomes:UP000070672}; RA Kim M.K., Srinivasan S., Lee J.-J.; RT "Rufibacter sp. DG15C whole genome sequencing."; RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP010776; AMM51244.1; -; Genomic_DNA. DR RefSeq; WP_066508344.1; NZ_CP010776.1. DR EnsemblBacteria; AMM51244; AMM51244; TH61_08745. DR KEGG; rud:TH61_08745; -. DR PATRIC; fig|1379909.4.peg.1893; -. DR KO; K03665; -. DR Proteomes; UP000070672; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000070672}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000070672}. FT DOMAIN 205 388 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 402 AA; 46192 MW; AB09DF49F88EA730 CRC64; MKNTKLHVTA KEQETAVLVS VPEWRQTDEK TKEYLDELAF LTETVGAKTL KRFIQKLDKP DMRTYVGKGK LEEIVAFVKE HKVDMVIFDD ELSPSQVRNL ERELEVKIID RSLLILDIFA LRAQTATARA QVELAQYRYM LPRLTNMWTH LSRQKGGGVA MRGPGETEIE TDRRIVREKI ALLKEKLEKF DKQNYEQRKS RTGVVRVSLV GYTNVGKSTI MNLLSKSDVF AENKLFATVD ATVRKVVIDN IPFLLSDTVG FIRKLPTKLI ESFKSTLDEI READLLLHVV DVSHPSFEEH INVVNETLKD IQSADKSVIL VFNKTDLYLE KREQELKEDN PEALPEIADL KSTYMAKEHA PAIFISATNR SNIDELREVL TREVAKLHFE RYPNAGKQAE EY // ID A0A127CIH4_9RHIZ Unreviewed; 408 AA. AC A0A127CIH4; DT 08-JUN-2016, integrated into UniProtKB/TrEMBL. DT 08-JUN-2016, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=AZF01_09960 {ECO:0000313|EMBL:AMM84637.1}; OS Martelella sp. AD-3. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Aurantimonadaceae; Martelella. OX NCBI_TaxID=686597 {ECO:0000313|EMBL:AMM84637.1, ECO:0000313|Proteomes:UP000070688}; RN [1] {ECO:0000313|EMBL:AMM84637.1, ECO:0000313|Proteomes:UP000070688} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=AD-3 {ECO:0000313|EMBL:AMM84637.1, RC ECO:0000313|Proteomes:UP000070688}; RA Wen L., He K., Yang H.; RL Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP014275; AMM84637.1; -; Genomic_DNA. DR RefSeq; WP_024706885.1; NZ_CP014275.1. DR EnsemblBacteria; AMM84637; AMM84637; AZF01_09960. DR KEGG; maad:AZF01_09960; -. DR KO; K03665; -. DR Proteomes; UP000070688; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000070688}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000070688}. FT DOMAIN 181 353 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 140 174 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 408 AA; 45171 MW; 87E7ADBF2A705FBE CRC64; MSRAPESRLQ EAVGLARAIG LDVVASEIVT VNEPRPATLI GTGKIKEIDE LLDARNIGLV IVDHPLSPVQ QRNLEKEWVA KVIDRTGLIL EIFGERASTK EGRLQVELAH LNYQRGRLVR SWTHLERQRG GGGFMGGPGE TQIEADRRLL RERITKLERE LEQVVRTRKL HRSKRKKVPH PIVALVGYTN AGKSTLFNRI TGAGVLAEDM LFATLDPTLR RMKLPHGRTV ILSDTVGFIS DLPTHLVAAF RATLEEVLEA DLILHVRDMA DPARDAQSDD VLRILGELGI DEKAQNERII EVWNKLDLLE SEEHDALMAR AAASDAVMGV SAVTGEGVDA LVEKIAARLA GVLTETTITL SPDRLHLLPW IYEHAIVDAR RDLEDGSVDL DIRVPGAEAQ RLESMLAE // ID A0A127EVX8_9RHIZ Unreviewed; 456 AA. AC A0A127EVX8; DT 08-JUN-2016, integrated into UniProtKB/TrEMBL. DT 08-JUN-2016, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=RHPLAN_39720 {ECO:0000313|EMBL:AMN42404.1}; OS Rhodoplanes sp. Z2-YC6860. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Hyphomicrobiaceae; Rhodoplanes. OX NCBI_TaxID=674703 {ECO:0000313|EMBL:AMN42404.1, ECO:0000313|Proteomes:UP000070354}; RN [1] {ECO:0000313|EMBL:AMN42404.1, ECO:0000313|Proteomes:UP000070354} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=YC6860 {ECO:0000313|EMBL:AMN42404.1, RC ECO:0000313|Proteomes:UP000070354}; RA Saikia M., Chaudhari Y., Khan M., Devi D.; RL Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP007440; AMN42404.1; -; Genomic_DNA. DR RefSeq; WP_068021690.1; NZ_CP007440.1. DR EnsemblBacteria; AMN42404; AMN42404; RHPLAN_39720. DR KEGG; rhz:RHPLAN_39720; -. DR PATRIC; fig|674703.3.peg.4563; -. DR KO; K03665; -. DR Proteomes; UP000070354; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000070354}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000070354}. FT DOMAIN 226 400 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 192 219 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 456 AA; 50248 MW; A7CF73BC1A2F16F0 CRC64; MEPRRRDTQA DGLTPTGSAT GRAIVIGPYL RRPPTRGAAA RVAEQGERAP AARLEEAVGL ALAIDLDVAQ SGIVALNEIR PATYIGKGKV DEIAGLVKSL EAGIVIVDGA LSPVQQRNLE KAWNAKVLDR TGLILEIFGR RARTKEGALQ VELAHLTYQR SRLVRSWTHL ERQRGGFGFL GGPGESQIET DRRLIEERVR RIEDELEKVK KRRKLHRASR ARVPYPIAAL VGYTNAGKST LFNRLTRATV LEADMLFATL DPTLRAVELP SGMKIILSDT VGFISDLPTM LVAAFRATLE EVIEADVILH VRDVSHEDTE AQSHDVEEVL RALGIDPNDE QRLIEVWNKV DRLDEAGRTR LANLAERRPS GQRPVLVSAI TGEGAEALIA AIERRLAQRR IVLDLILDPA DGAGVSWLHR HTEVMEKSLS DDGKLAMTVR VDPDKAGAVK TKFQMH // ID A0A127F7D7_9GAMM Unreviewed; 476 AA. AC A0A127F7D7; DT 08-JUN-2016, integrated into UniProtKB/TrEMBL. DT 08-JUN-2016, sequence version 1. DT 07-JUN-2017, entry version 9. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=ACG33_04375 {ECO:0000313|EMBL:AMN46353.1}; OS Steroidobacter denitrificans. OC Bacteria; Proteobacteria; Gammaproteobacteria; Nevskiales; OC Sinobacteraceae; Steroidobacter. OX NCBI_TaxID=465721 {ECO:0000313|EMBL:AMN46353.1, ECO:0000313|Proteomes:UP000070250}; RN [1] {ECO:0000313|EMBL:AMN46353.1, ECO:0000313|Proteomes:UP000070250} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 18526 {ECO:0000313|EMBL:AMN46353.1, RC ECO:0000313|Proteomes:UP000070250}; RA Yang F.-C., Chen Y.-L., Yu C.-P., Tang S.-L., Wang P.-H., Ismail W., RA Wang C.-H., Yang C.-Y., Chiang Y.-R.; RT "A Comprehensive Approach to Explore the Metabolic and Phylogenetic RT Diversity of Bacterial Steroid Degradation in the Environment: RT Testosterone as an Example."; RL Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP011971; AMN46353.1; -; Genomic_DNA. DR EnsemblBacteria; AMN46353; AMN46353; ACG33_04375. DR KEGG; sdf:ACG33_04375; -. DR PATRIC; fig|465721.4.peg.935; -. DR KO; K03665; -. DR Proteomes; UP000070250; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000070250}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000070250}. FT DOMAIN 198 364 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 476 AA; 51675 MW; C712F30B431124BA CRC64; MFERPRSGER ALLVRIGLGA PPGEEELSEF EALARSAGAE VVGVVTGTRR APDPRLYVGS GKAQEIRTRI EAEGADLAVF DHALSPSQER NLEALLRCRV LDRTGLILDI FAQRARSFEG QLQVELAQLK HLSTRLVRGW SHLERQKGGI GLRGPGETQL ETDRRLLGKR IKTLNARLDK VITQRETTRR ERRRAEIPTV ALVGYTNAGK TTLFNRLTGA QAYAADQLFA TLDPAVRRIE LADARQALLA DTVGFVRELP HELVAAFRST LQEARQAALL LHVIDAADPN RGERIAQVNQ VLADVGAAGL AQIEVYNKAD LIGETPRVER DESGDVRRVW LSAQTGAGMP LLVAAIGDFL GPRIVRRRIV LSAGEGRARA RFFEAGAVLS ESIRADGGSE LEVSMPARAF QLLCRTEGLE SGLDAADRDI DRDIELDGAV RAAGLDTVVP GSGLDMKGPE PASLERPDAG HAVVHP // ID A0A127MEW1_9SPHN Unreviewed; 432 AA. AC A0A127MEW1; DT 11-MAY-2016, integrated into UniProtKB/TrEMBL. DT 11-MAY-2016, sequence version 1. DT 05-JUL-2017, entry version 13. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=AZE99_08090 {ECO:0000313|EMBL:AMO71812.1}; OS Sphingorhabdus sp. M41. OC Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales; OC Sphingomonadaceae; Sphingorhabdus. OX NCBI_TaxID=1806885 {ECO:0000313|EMBL:AMO71812.1, ECO:0000313|Proteomes:UP000073959}; RN [1] {ECO:0000313|EMBL:AMO71812.1, ECO:0000313|Proteomes:UP000073959} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=M41 {ECO:0000313|EMBL:AMO71812.1, RC ECO:0000313|Proteomes:UP000073959}; RA Shamseldin A., Moawad H., Abd El-Rahim W.M., Sadowsky M.J.; RL Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP014545; AMO71812.1; -; Genomic_DNA. DR EnsemblBacteria; AMO71812; AMO71812; AZE99_08090. DR KEGG; sphg:AZE99_08090; -. DR KO; K03665; -. DR Proteomes; UP000073959; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000073959}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000073959}. FT DOMAIN 207 380 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 173 200 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 432 AA; 47768 MW; 30E70AA33B0761BB CRC64; MIPFEKESLD SKSRRALIVH PDMVSLSQSE LENRLEEAVG LAAAIGLVAT ASHAFSVRKP KPATLFGSGQ VDQIRKMMEE QEASILIVDG SLSAIQQRNL EEKLDVKVID RTGLILEIFG ARAATAEGRL QVELAHLDYQ AGRLVRSWTH LERQRGGFGF LGGPGETQIE SDRRMIRDRM AKLRKDLAHL RKTRALHRER RQRAPWPVIA LVGYTNAGKS TLFNRLTGAD VFAEDLLFAT LDPTMREFPL PGYDKAILSD TVGFVSDLPT QLVAAFRATL EEVSAADIVV HVRDISHEAS DAQARDVRQI LAELGVSEEA GEGPPVIEAW NKIDKISVDD PEYSRISPPL PENVCTISAE TGAGVDTLVK LIAKTLSEGY KSERIVIAAS DGKRMAWLHE NGRVLNSEQQ GDDLLLEVEM SPRNWGRYHA LD // ID A0A127VJW6_9SPHI Unreviewed; 397 AA. AC A0A127VJW6; DT 11-MAY-2016, integrated into UniProtKB/TrEMBL. DT 11-MAY-2016, sequence version 1. DT 07-JUN-2017, entry version 12. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=AY601_4356 {ECO:0000313|EMBL:AMQ01199.1}; OS Pedobacter cryoconitis. OC Bacteria; Bacteroidetes; Sphingobacteriia; Sphingobacteriales; OC Sphingobacteriaceae; Pedobacter. OX NCBI_TaxID=188932 {ECO:0000313|EMBL:AMQ01199.1, ECO:0000313|Proteomes:UP000071561}; RN [1] {ECO:0000313|EMBL:AMQ01199.1, ECO:0000313|Proteomes:UP000071561} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=PAMC 27485 {ECO:0000313|EMBL:AMQ01199.1, RC ECO:0000313|Proteomes:UP000071561}; RA Lee J., Kim O.-S.; RT "Complete genome sequence of Pedobacter cryoconitis PAMC 27485."; RL Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP014504; AMQ01199.1; -; Genomic_DNA. DR RefSeq; WP_068404980.1; NZ_CP014504.1. DR EnsemblBacteria; AMQ01199; AMQ01199; AY601_4356. DR KEGG; pcm:AY601_4356; -. DR PATRIC; fig|188932.3.peg.4515; -. DR KO; K03665; -. DR Proteomes; UP000071561; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000071561}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000071561}. FT DOMAIN 204 386 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 397 AA; 45598 MW; 8691CF336361192E CRC64; MGKEKTYDTA VKQERAVLVG VIRPGEKPEE TKEYLDELTF LVDTAGGVVD NIFTQKMLKP DRGTFVGTGK LEEIRAYVKS EEIDMVVFDD ELSPSQLRNI ERELEVKVLD RSNLILDIFA GRAQTSQAKT QVELAQLQYL LPRLTRLWTH LERQKGGIGM RGPGETQIES DRRMILEKIS LLKGRLKLID KQNETQRKNR TELIRVALVG YTNVGKSTIM NMISKSEVFA ENKLFATLDT TVRKVVIDNL PFLLSDTVGF IRKLPHHLVE CFKSTLDEVR EADILIHVVD VSHTSFEDQI RVVNETLKDL GARDKETIVV FNKIDAYVNP EADEMNEDEK VTLTLEDFKR SWMAQHNTPS LFISALHKEN LEEFKQLLYD KVVALHTVRY PYDKLLY // ID A0A127VVH8_SPOPS Unreviewed; 423 AA. AC A0A127VVH8; DT 11-MAY-2016, integrated into UniProtKB/TrEMBL. DT 11-MAY-2016, sequence version 1. DT 07-JUN-2017, entry version 12. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=AZE41_02230 {ECO:0000313|EMBL:AMQ04879.1}; OS Sporosarcina psychrophila (Bacillus psychrophilus). OC Bacteria; Firmicutes; Bacilli; Bacillales; Planococcaceae; OC Sporosarcina. OX NCBI_TaxID=1476 {ECO:0000313|EMBL:AMQ04879.1, ECO:0000313|Proteomes:UP000071057}; RN [1] {ECO:0000313|EMBL:AMQ04879.1, ECO:0000313|Proteomes:UP000071057} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 6497 {ECO:0000313|EMBL:AMQ04879.1, RC ECO:0000313|Proteomes:UP000071057}; RA Yan W.; RT "Complete genome sequence of the Sporosarcina psychrophila DSM6497, a RT psychrophila Bacillus that can mediate the Ca2+ precipitation."; RL Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP014616; AMQ04879.1; -; Genomic_DNA. DR RefSeq; WP_067205122.1; NZ_CP014616.1. DR EnsemblBacteria; AMQ04879; AMQ04879; AZE41_02230. DR KEGG; spsy:AZE41_02230; -. DR KO; K03665; -. DR Proteomes; UP000071057; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000071057}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000071057}. FT DOMAIN 200 368 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 423 AA; 48022 MW; 9F6BCF816360FEB3 CRC64; MEFLVERAVI VGVHEQKDQH FEYAMEELKN LAKAIDVEVV GEVTQNMEKR NPSTYVGKGK MEEIQNFYEE LDANLVIFND ELSPSQIRNL ERELDCKVID RTMLILDIFV RRARTSESRM QVELAQLQYM LPRLVGLRAS LGRQGGGAGG GVQNKGAGET KLELDRRKIE DQISKLGRDL DHVKDQRETQ RKQRKKSGIP VVSIVGYTNA GKSTIMNKLL LKMDVDNAKQ VYEEDMLFAT LDTSIRKVKL EDNKEFILTD TVGFVSKLPH HLVKAFRSTL EEARDADLLL HVVDVSNSEH GYMMEVTNDT LQAVGVENVA TLNIYNKADL ADVPYPVVSD DSVWISAREG KGLDELIELI KKKIFEQYST CKLLIPFDRG DIVSYLNDKA NVKSTEYEED GTLMTVEMDI SERAKIEEFI VSH // ID A0A132AF62_SARSC Unreviewed; 487 AA. AC A0A132AF62; DT 11-MAY-2016, integrated into UniProtKB/TrEMBL. DT 11-MAY-2016, sequence version 1. DT 30-AUG-2017, entry version 13. DE SubName: Full=GTP-binding protein 6-like protein {ECO:0000313|EMBL:KPM09583.1, ECO:0000313|VectorBase:SSCA003055-PA}; GN ORFNames=QR98_0081220 {ECO:0000313|EMBL:KPM09583.1}; OS Sarcoptes scabiei (Itch mite) (Acarus scabiei). OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; OC Acari; Acariformes; Sarcoptiformes; Astigmata; Psoroptidia; OC Sarcoptoidea; Sarcoptidae; Sarcoptinae; Sarcoptes. OX NCBI_TaxID=52283 {ECO:0000313|EMBL:KPM09583.1, ECO:0000313|Proteomes:UP000070412}; RN [1] {ECO:0000313|EMBL:KPM09583.1, ECO:0000313|Proteomes:UP000070412, ECO:0000313|VectorBase:SSCA003055-PA} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Arlian Lab {ECO:0000313|EMBL:KPM09583.1}; RX PubMed=26555130; DOI=10.1186/s13071-015-1198-2; RA Rider S.D.Jr., Morgan M.S., Arlian L.G.; RT "Draft genome of the scabies mite."; RL Parasit. Vectors 8:585-585(2015). RN [2] {ECO:0000313|VectorBase:SSCA003055-PA} RP IDENTIFICATION. RG VectorBase; RL Submitted (FEB-2017) to UniProtKB. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JXLN01013770; KPM09583.1; -; Genomic_DNA. DR EnsemblMetazoa; SSCA003055-RA; SSCA003055-PA; SSCA003055. DR VectorBase; SSCA003055-RA; SSCA003055-PA; SSCA003055. DR OMA; MDTVGFM; -. DR Proteomes; UP000070412; Unassembled WGS sequence. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR CDD; cd01878; HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000070412}; KW Reference proteome {ECO:0000313|Proteomes:UP000070412}. FT DOMAIN 263 427 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 487 AA; 55897 MW; 5ABF8BFE0F551443 CRC64; MSQRKFSFNI KNNLLALKQN NLFLRSTIHY RNENDNKLDN DDPDDEKSTL LNEVLSYTCL TDLSPKNVFV ILPRNRSKKR SFEENELLLD ETKALVETIP YWRVSGSAIV SAKSLRSDYI FGKGNLESLK DYCRNQSTNG IVFGVDTLKP SQHYFFRDFL GIEVYDRFSI ILKIFRERCR TKEARIQLAM AELNYVQKNL HHLTANDFQN FSLSQSFGGN FDTFYQIKKR VIQERESQLK DKLSKITQSY AVKRKNRASL EIPTVAIVGY TNSGKTSLIK ALTNNDEIVP EDRLFATLDV TNHQITLPSK LKALLIDTIG FISDIPLTLV HCFKSTLTEI CNADLIVHVV DASHPNRSKQ IETVQNTLKE IDVPSKLIET MIEVSNKIDK VPESEIEKFD GLTISATEKI NLNELVKKIE NRIITNTDRL ALKLKVLNGG QEYGWLFKEA SVVECVPDQE DPNYALMKIL ITKSKIGRFR KLFKHEN // ID A0A132BWI0_9RHOB Unreviewed; 423 AA. AC A0A132BWI0; DT 11-MAY-2016, integrated into UniProtKB/TrEMBL. DT 11-MAY-2016, sequence version 1. DT 07-JUN-2017, entry version 10. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:KUP92556.1}; GN ORFNames=TRIHO_25260 {ECO:0000313|EMBL:KUP92556.1}; OS Rhodobacteraceae bacterium O3.65. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae. OX NCBI_TaxID=1768241 {ECO:0000313|EMBL:KUP92556.1, ECO:0000313|Proteomes:UP000068382}; RN [1] {ECO:0000313|EMBL:KUP92556.1, ECO:0000313|Proteomes:UP000068382} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=O3.65 {ECO:0000313|EMBL:KUP92556.1, RC ECO:0000313|Proteomes:UP000068382}; RA Poehlein A., Giebel H.A., Voget S., Brinkhoff T.; RT "Genome sequence of the marine Rhodobacteraceae strain O3.65, RT Candidatus Tritonibacter horizontis."; RL Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KUP92556.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LPUY01000074; KUP92556.1; -; Genomic_DNA. DR RefSeq; WP_068244059.1; NZ_LPUY01000074.1. DR EnsemblBacteria; KUP92556; KUP92556; TRIHO_25260. DR PATRIC; fig|1768241.3.peg.2647; -. DR Proteomes; UP000068382; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000068382}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000068382}. FT DOMAIN 203 372 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 423 AA; 47014 MW; 1051F795F9B115FD CRC64; MEHDRKLTRA WVLHPEIKSD QRRRPPGPAL EEAVGLAEAL PDLEVIGATV VRLPKAHAGK LFGSGKIEEL GGELKAAEIE LVLIDGSVSP VQQRNLEKAW KVKILDRTGL ILEIFSDRAR TREGVLQVEM AALSYQRTRL VRAWTHLERQ RGGLGFVGGP GETQIEADRR AIDDQLVRLR RQLDKVVKTR TLHRAARAKI PYPIVALVGY TNAGKSTLFN RLTGADVMAK DMLFATLDPT MRRVELPDGP EVIMSDTVGF ISDLPTELVA AFRATLEEVL AADVVIHVRD ISHSDTESQA RDVEKILSSL GVSDERPRLE VWNKIDQLSP EEAEACRQRA VRSDDLFATS AITGEGLPEL LADVAAKLQG ARLTEVLTLD FSQGKQRAWL FKEEIVEAEE QTETGFEITV SWTELQKSRY AAL // ID A0A132H0S3_9BACT Unreviewed; 397 AA. AC A0A132H0S3; DT 08-JUN-2016, integrated into UniProtKB/TrEMBL. DT 08-JUN-2016, sequence version 1. DT 07-JUN-2017, entry version 8. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=AUK64_753 {ECO:0000313|EMBL:KWW30398.1}; OS bacterium P201. OC Bacteria. OX NCBI_TaxID=1768112 {ECO:0000313|EMBL:KWW30398.1, ECO:0000313|Proteomes:UP000070264}; RN [1] {ECO:0000313|EMBL:KWW30398.1, ECO:0000313|Proteomes:UP000070264} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=P201 {ECO:0000313|EMBL:KWW30398.1}; RA Shamseldin A., Moawad H., Abd El-Rahim W.M., Sadowsky M.J.; RL Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KWW30398.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LPNI01000007; KWW30398.1; -; Genomic_DNA. DR PATRIC; fig|1768112.3.peg.2474; -. DR Proteomes; UP000070264; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000070264}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000070264}. FT DOMAIN 202 386 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 397 AA; 45718 MW; 2B62451AB19512CE CRC64; MGDFITYEKI PERAVLIAVA SKQQGRERTE EYLDELAFLL ETAGGVPVAR FVQPLDRPSS VTYLGSGKLE EIHQYIKAEN IEIAVIDDEL SATQARNMEQ ALECRVLDRT SLILDIFASN AHTAHAKAQV ELAQYQYLLP RLTRMWTHLE RQRGGIGMRG PGETQIETDR RLILERIALL KEKLKDIDKQ KTVQRKNRSK LVRVALVGYT NVGKSTIMNL LSKSEVYTEN KLFATLDTTV RKVVVDNLPF LLSDTVGFIR KLPHHLVESF KSTLDEVRES DILLHVVDIS HPDFEAQMEV VNQTLAELGC ADKKTIVVFN KTDAYTWEEK DPDDLTPPTK RNVSYDELKK TWMAKMNENC IFISAKNRDN YQEFRDLLYK EIRDMHAIRY PYDSFLY // ID A0A132HZ08_9BACT Unreviewed; 431 AA. AC A0A132HZ08; DT 08-JUN-2016, integrated into UniProtKB/TrEMBL. DT 08-JUN-2016, sequence version 1. DT 07-JUN-2017, entry version 8. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=F083_646 {ECO:0000313|EMBL:KWW41995.1}; OS bacterium F083. OC Bacteria. OX NCBI_TaxID=1768114 {ECO:0000313|EMBL:KWW41995.1, ECO:0000313|Proteomes:UP000070097}; RN [1] {ECO:0000313|EMBL:KWW41995.1, ECO:0000313|Proteomes:UP000070097} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=F083 {ECO:0000313|EMBL:KWW41995.1}; RA Shamseldin A., Moawad H., Abd El-Rahim W.M., Sadowsky M.J.; RL Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KWW41995.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LPNF01000004; KWW41995.1; -; Genomic_DNA. DR PATRIC; fig|1768114.3.peg.2242; -. DR Proteomes; UP000070097; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000070097}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000070097}. FT DOMAIN 232 420 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 431 AA; 49276 MW; 361CBF5607805780 CRC64; MNITNYKQNQ GKWRNSHDDV EVPEPRLSRR ERNTVDNSPQ PERAILVAVC TAQSEVERCQ ESLDELAFLL DTAGGVAVRQ VMQRLPRPDS RTYIGSGKIE EVKEFKQALD ADMLVFDDEL TPTQLRNLER DFSCRILDRT TLILDIFAKR ARTSTAKTQV ELAQLQYMLP RLTRMWTHLE RQRGGIGMRG PGETQIETDR RLITEKIVLL KERLASIDRQ KVQQRKSREA LVRVALVGYT NVGKSTLMNL ISKSDVFAEN KLFATLDTTV RKVVIGNLPF LLSDTVGFIR KLPHGLVESF KSTLDEVCEA DILIHVVDIS HPSFEQQIQS VNATLAEIGA AGKPTLLLFN KCDAFRFQPK DPDDLTPVSR DNWSLNDWEA YWQEQVAAMP DTAALFVSAH KRDGIDALRD VLYHTVRQIH SRRFPYDNFL W // ID A0A132MPW0_9ACTN Unreviewed; 510 AA. AC A0A132MPW0; DT 08-JUN-2016, integrated into UniProtKB/TrEMBL. DT 08-JUN-2016, sequence version 1. DT 07-JUN-2017, entry version 8. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=LI90_1404 {ECO:0000313|EMBL:KWW99765.1}; OS Streptomyces thermoautotrophicus. OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae; OC Streptomyces. OX NCBI_TaxID=1469144 {ECO:0000313|EMBL:KWW99765.1, ECO:0000313|Proteomes:UP000070188}; RN [1] {ECO:0000313|EMBL:KWW99765.1, ECO:0000313|Proteomes:UP000070188} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=H1 {ECO:0000313|EMBL:KWW99765.1, RC ECO:0000313|Proteomes:UP000070188}; RA MacKellar D.C., Lieber L., Norman J., Bolger A., Tobin C., RA Murray J.W., Woodward J., Friesen M., Prell J.; RT "Physiological reanalysis, assessment of diazotrophy, and genome RT sequences of multiple isolates of Streptomyces thermoautotrophicus."; RL Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KWW99765.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LAXD01000001; KWW99765.1; -; Genomic_DNA. DR EnsemblBacteria; KWW99765; KWW99765; LI90_1404. DR PATRIC; fig|1469144.10.peg.1543; -. DR Proteomes; UP000070188; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000070188}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000070188}. FT DOMAIN 288 453 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 247 284 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 510 AA; 56099 MW; 7E4008B8D1459FCD CRC64; MTGVAGGVEQ DGMTSLPHEF DSELDRRSVL DESAIDIDPT FPPETPGLED ETYEEDQLDL VERYALRRVA GLSTELTDIT EVEYRRLRLE RVVLVGVWTE GTVEDAENSL RELAALAETA GSQVLEGVIQ RRDRPDPATY IGSGKAGELR DIVRATGADT VICDGELSPA QLIHLEDVVK VKVIDRTALI LDIFAQHARS REGKAQVALA QMEYMLPRLR GWGESLSRQA GGRAGSNGGV GLRGPGETKI ETDRRRIRQR MAKLRREIAE MKKARETKRQ QRRRNEVPSV AIAGYTNAGK SSLLNRLTGA GALVENALFA TLDPTVRRAE TPGGRVFTLA DTVGFVRHLP HQLVEAFRST LEEVAGADLI LHVVDGSHPD PEAQLATVRE VFAEIGAQGI PEIVVINKAD VADPLVIDRL RRREPHSVAV SARTGRGVDE LLAAIERDLP RPSIEVEVLV PYAKGGLVSR VYDHGQVLER EDTLEGVRLR ARVTRFLAGE LEPYTLSRVE // ID A0A132PLB1_9MYCO Unreviewed; 469 AA. AC A0A132PLB1; DT 08-JUN-2016, integrated into UniProtKB/TrEMBL. DT 08-JUN-2016, sequence version 1. DT 07-JUN-2017, entry version 10. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=AFM11_17695 {ECO:0000313|EMBL:KWX22782.1}; OS Mycobacterium wolinskyi. OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae; OC Mycobacterium. OX NCBI_TaxID=59750 {ECO:0000313|EMBL:KWX22782.1, ECO:0000313|Proteomes:UP000070612}; RN [1] {ECO:0000313|EMBL:KWX22782.1, ECO:0000313|Proteomes:UP000070612} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CDC_01 {ECO:0000313|EMBL:KWX22782.1, RC ECO:0000313|Proteomes:UP000070612}; RA de Man T.J., Perry K.A., Coulliette A.D., Jensen B., Toney N.C., RA Limbago B.M., Noble-Wang J.; RT "A draft genome sequence of Mycobacterium wolinskyi."; RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KWX22782.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LGTW01000011; KWX22782.1; -; Genomic_DNA. DR RefSeq; WP_067851123.1; NZ_LGTW01000011.1. DR EnsemblBacteria; KWX22782; KWX22782; AFM11_17695. DR PATRIC; fig|59750.3.peg.894; -. DR Proteomes; UP000070612; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000313|EMBL:KWX22782.1}; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000070612}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900, KW ECO:0000313|EMBL:KWX22782.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000070612}. FT DOMAIN 246 415 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 205 232 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 469 AA; 50475 MW; 0176145A0B295F95 CRC64; MTYPEHPVAP STGELALEDR ASLRRVAGLS TELADVSEVE YRQLRLERVV LVGVWTEGSA ADADASLAEL AALAETAGSE VLEGLIQRRD KPDPSTYIGS GKAAELREVV LATGADTVIC DGELSPAQLT ALEKAVKVKV IDRTALILDI FAQHATSREG KAQVSLAQME YMLPRLRGWG ESMSRQAGGR AGGAGGGVGT RGPGETKIET DRRRIRERMA KLRREIRDMK KIRDTQRSGR RRSEIASVAI VGYTNAGKSS LLNALTGAGV LVENALFATL EPTTRRGEFE DGRPFVLTDT VGFVRHLPTQ LVEAFRSTLE EVVDADLLVH VVDGSDVNPL AQINAVRTVI NEVVAEYDIV APPELLVVNK IDAATDVGLA QLRRALPDAV FVSARTSDGL GKLRSRMAEL VPPTDTTVDV TIPYDRGDLV ARVHAEGRVD ATEHTAAGTR IKARVPVPLA AGLHEYTTF // ID A0A132T363_9MYCO Unreviewed; 482 AA. AC A0A132T363; DT 08-JUN-2016, integrated into UniProtKB/TrEMBL. DT 08-JUN-2016, sequence version 1. DT 07-JUN-2017, entry version 10. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=ASJ79_28510 {ECO:0000313|EMBL:KWX65633.1}; OS Mycobacterium sp. NAZ190054. OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae; OC Mycobacterium. OX NCBI_TaxID=1747766 {ECO:0000313|EMBL:KWX65633.1, ECO:0000313|Proteomes:UP000070146}; RN [1] {ECO:0000313|EMBL:KWX65633.1, ECO:0000313|Proteomes:UP000070146} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NAZ190054 {ECO:0000313|EMBL:KWX65633.1, RC ECO:0000313|Proteomes:UP000070146}; RA Zhang Y., Guo Z.; RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KWX65633.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LMVQ01000331; KWX65633.1; -; Genomic_DNA. DR RefSeq; WP_067959189.1; NZ_LMVQ01000331.1. DR EnsemblBacteria; KWX65633; KWX65633; ASJ79_28510. DR Proteomes; UP000070146; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000313|EMBL:KWX65633.1}; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000070146}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900, KW ECO:0000313|EMBL:KWX65633.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000070146}. FT DOMAIN 259 428 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 218 245 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 482 AA; 51850 MW; 0F7066AEF2A7CC20 CRC64; MRSDIRANLD SPMTYPEFSD DIPSVGELAL EERSALRRVA GLSTELADVS EVEYRKLRLE RVVLVGVWTE GSAADADASL AELAALAETA GSEVLEGLIQ RRDKPDPSTY IGSGKAAELR EIVLATGADT VICDGELSPA QLNALEKVVK VKVIDRTALI LDIFAQHATS REGKAQVSLA QMEYMLPRLR GWGESMSRQA GGRAGGAGGG VGTRGPGETK IETDRRRIRE RMSKLRREIR DMKQVRDTQR GRRVANDVPS VAIVGYTNAG KSSLLNALTG AGVLVENALF ATLEPTTRRG ELADGREFVL TDTVGFVRHL PTQLVEAFRS TLEEVADADL LVHVVDGSDV NPLAQINAVR QVVNDVIAET DAPPPPELLV VNKIDAADGL TLAQLRRALP GAVFVSAHTG DGLDRLQARM AEMIAPRDTV VDVTIPYDRG DLVNRVHAEG RVDAVEHTES GTRMKARVPV SLAAGLAGYA TY // ID A0A133Q3P9_STALU Unreviewed; 412 AA. AC A0A133Q3P9; DT 08-JUN-2016, integrated into UniProtKB/TrEMBL. DT 08-JUN-2016, sequence version 1. DT 07-JUN-2017, entry version 12. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=HMPREF3225_01680 {ECO:0000313|EMBL:KXA37507.1}; OS Staphylococcus lugdunensis. OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae; OC Staphylococcus. OX NCBI_TaxID=28035 {ECO:0000313|EMBL:KXA37507.1, ECO:0000313|Proteomes:UP000070063}; RN [1] {ECO:0000313|EMBL:KXA37507.1, ECO:0000313|Proteomes:UP000070063} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MJR7738 {ECO:0000313|EMBL:KXA37507.1, RC ECO:0000313|Proteomes:UP000070063}; RA Oliw E.H.; RL Submitted (JAN-2016) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KXA37507.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LRQI01000074; KXA37507.1; -; Genomic_DNA. DR RefSeq; WP_002492660.1; NZ_KQ957392.1. DR EnsemblBacteria; KXA37507; KXA37507; HMPREF3225_01680. DR PATRIC; fig|28035.7.peg.1701; -. DR Proteomes; UP000070063; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000070063}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}. FT DOMAIN 206 326 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 412 AA; 46967 MW; 6E9DA46F2D03BD23 CRC64; MVQQAAYSTQ QKRETAVLVG VNAQVDNQFD YDSTMQELQA LSQTCQLEVV SQITQNRQQV DHKYYVGKGK IDEIKAFIDL HDIDVVVAND ELTTAQSKSL NDALDVKIID RTQLILEIFA LRAKSKEGKL QVELAQLDYL LPRLQGHGKS LSRLGGGIGT RGPGETKLEM DRRHIRTRIN EIKHQLQTIV EHRERYRNKR EQNQVFQIAL VGYTNAGKSS WFNVLSGEST YEQNLLFATL DPKTRQIQLN EGFNVIITDT VGFIQKLPTT LVAAFKSTLE EAKNADILLH IVDASHPEFR SQYETVNQLI QELEMDQIPQ VVLFNKRDLC PSTMALPMSS SLSEFVSTQH HSDITKVKAL LIKQIKESLT YYSETVASSN AQRIYFLKQH TLIEEMNFNP QNNCYEVTGY RK // ID A0A133QQE5_9BACT Unreviewed; 416 AA. AC A0A133QQE5; DT 08-JUN-2016, integrated into UniProtKB/TrEMBL. DT 08-JUN-2016, sequence version 1. DT 07-JUN-2017, entry version 9. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=HMPREF3226_00072 {ECO:0000313|EMBL:KXA45105.1}; OS Prevotella corporis. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Prevotellaceae; OC Prevotella. OX NCBI_TaxID=28128 {ECO:0000313|EMBL:KXA45105.1, ECO:0000313|Proteomes:UP000070533}; RN [1] {ECO:0000313|EMBL:KXA45105.1, ECO:0000313|Proteomes:UP000070533} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MJR7716 {ECO:0000313|EMBL:KXA45105.1, RC ECO:0000313|Proteomes:UP000070533}; RA Oliw E.H.; RL Submitted (JAN-2016) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KXA45105.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LRQG01000002; KXA45105.1; -; Genomic_DNA. DR RefSeq; WP_060939941.1; NZ_KQ957185.1. DR EnsemblBacteria; KXA45105; KXA45105; HMPREF3226_00072. DR PATRIC; fig|28128.5.peg.70; -. DR Proteomes; UP000070533; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000070533}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000070533}. FT DOMAIN 216 400 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 416 AA; 47653 MW; 4A43E7758BAA1979 CRC64; MKEFVISEAK AETAVLVGLI TQEQNEAKTK EYLDELEFLA DTAGAVTVKR FTQRSGGPNM TTYVGKGKLE EIKEYISQKE DEDDPVGMVI FDDELSAKQL RNIEKELGVK ILDRTSLILD IFAMRAQTAN AKTQVELAQY RYMLPRLQRL WTHLERQGGG SGSGGGKGSV GLRGPGETQL EMDRRIILQR MSLLKQRLLE IDKQKVTQRK NRGRMVRVAL VGYTNVGKST IMNLLAKSEV FAENKLFATL DTTVRKVVLE NLPFLLADTV GFIRKLPTDL VDSFKSTLDE VREADLLLHV VDISHPDFEE QVQIVNETLK DLDCSDKPSM IIFNKIDNYE WEEKDIDDLT PATKENVSLE ELKRTWMAKM PEDCLFISAK NKENIDEFRN ILYKKVREQH VRKYPYNDFL YDIDIN // ID A0A133XJ63_9RHOO Unreviewed; 437 AA. AC A0A133XJ63; DT 08-JUN-2016, integrated into UniProtKB/TrEMBL. DT 08-JUN-2016, sequence version 1. DT 30-AUG-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=AT959_09745 {ECO:0000313|EMBL:KXB30980.1}; OS Dechloromonas denitrificans. OC Bacteria; Proteobacteria; Betaproteobacteria; Rhodocyclales; OC Azonexaceae; Dechloromonas. OX NCBI_TaxID=281362 {ECO:0000313|EMBL:KXB30980.1, ECO:0000313|Proteomes:UP000070186}; RN [1] {ECO:0000313|EMBL:KXB30980.1, ECO:0000313|Proteomes:UP000070186} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-841 {ECO:0000313|EMBL:KXB30980.1, RC ECO:0000313|Proteomes:UP000070186}; RA Yoon S., Nissen S., Park D., Sanford R.A., Loeffler F.E.; RT "Nitrous oxide reduction kinetics distinguish bacteria harboring RT typical versus atypical NosZ."; RL Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KXB30980.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LODL01000019; KXB30980.1; -; Genomic_DNA. DR RefSeq; WP_066882780.1; NZ_LODL01000019.1. DR EnsemblBacteria; KXB30980; KXB30980; AT959_09745. DR Proteomes; UP000070186; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000070186}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}. FT DOMAIN 209 379 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 174 206 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 437 AA; 48283 MW; DD66101519EF0683 CRC64; MQTEVKEKPV YAVVASVQLP QVSDIEFEAS LAELRELAKT LGYTVVRTFI QKRGSFDTTG YLGIGKRQEI EHFVNHEAEC EIEAVLVDHE ISPSQARNLE KETGCGVMDR TMVILEIFHN NARSRAAKAQ VEIARLGYMA PRLREAAKLA GPQGRQRSGV GGRGAGESHT ELDRRKIRDR IAELQLEIVA MEAERKTQRA RRQERQGLAS VALVGYTNAG KSTLMRALTG SEVLVANKLF ATLDTTVRTL HPESVPRVLV SDTVGFIKNL PHGLVASFKS TLDEALDAGL LLHVIDASDP GFERQLEVTD KVLAEIDADT VPRLRIFNKI DHVGDAAAQA ECEAALRAKY PDCVVMSARR PDEVAKLRLT IIAFFQQGLV EAELFLPWSA QQLRKDIYAS CQVLEERADE DGAFFRLRGE AEAIEGLRGQ FAQAQPG // ID A0A133XMD9_9RHOO Unreviewed; 384 AA. AC A0A133XMD9; DT 08-JUN-2016, integrated into UniProtKB/TrEMBL. DT 08-JUN-2016, sequence version 1. DT 30-AUG-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=AT959_03340 {ECO:0000313|EMBL:KXB32105.1}; OS Dechloromonas denitrificans. OC Bacteria; Proteobacteria; Betaproteobacteria; Rhodocyclales; OC Azonexaceae; Dechloromonas. OX NCBI_TaxID=281362 {ECO:0000313|EMBL:KXB32105.1, ECO:0000313|Proteomes:UP000070186}; RN [1] {ECO:0000313|EMBL:KXB32105.1, ECO:0000313|Proteomes:UP000070186} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-841 {ECO:0000313|EMBL:KXB32105.1, RC ECO:0000313|Proteomes:UP000070186}; RA Yoon S., Nissen S., Park D., Sanford R.A., Loeffler F.E.; RT "Nitrous oxide reduction kinetics distinguish bacteria harboring RT typical versus atypical NosZ."; RL Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KXB32105.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LODL01000007; KXB32105.1; -; Genomic_DNA. DR RefSeq; WP_066880586.1; NZ_LODL01000007.1. DR EnsemblBacteria; KXB32105; KXB32105; AT959_03340. DR Proteomes; UP000070186; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000070186}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}. FT DOMAIN 198 364 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 349 377 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 384 AA; 42350 MW; 087EC706D3EEAA79 CRC64; MNERPAAGER AVIVQLDFGQ PDLGDQLEEI RLLAESAGGV VAAEVCGKRQ SPDPKTFAGK GKVQEIAAML AAAEADLVIF NHELSPAQQR NLERELKCRV IDRTSLILDI FALRASSAEG KLQVELAQLE HLSTRLVRGW THLERQRGGI GMRGPGETQL ETDRRLLGKR VKLLKERLEK LSRQRGVQRR ARLRGDVLSV SLVGYTNAGK STLFNALTHA GVFAADQLFA TLDTTSRKLW IEGAGNIVIS DTVGFIRDLP HSLVDAFHAT LEAAIDADVL LHVVDSASHA RDEQMYEVNK VLDEIGARDL RQVIVWNKID LTQASPGVEL DEYAKIARVR VSARSGEGLD LLREALADFA RNKAEARKKA FADAEREAQN DYIN // ID A0A133XRI0_9BACT Unreviewed; 421 AA. AC A0A133XRI0; DT 08-JUN-2016, integrated into UniProtKB/TrEMBL. DT 08-JUN-2016, sequence version 1. DT 07-JUN-2017, entry version 10. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=HMPREF1869_01535 {ECO:0000313|EMBL:KXB33545.1}; OS Bacteroidales bacterium KA00251. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales. OX NCBI_TaxID=1497953 {ECO:0000313|EMBL:KXB33545.1, ECO:0000313|Proteomes:UP000070662}; RN [1] {ECO:0000313|EMBL:KXB33545.1, ECO:0000313|Proteomes:UP000070662} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=KA00251 {ECO:0000313|EMBL:KXB33545.1, RC ECO:0000313|Proteomes:UP000070662}; RA Oliw E.H.; RL Submitted (JAN-2016) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KXB33545.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LSCS01000098; KXB33545.1; -; Genomic_DNA. DR RefSeq; WP_066042117.1; NZ_KQ959277.1. DR EnsemblBacteria; KXB33545; KXB33545; HMPREF1869_01535. DR PATRIC; fig|1497953.3.peg.1516; -. DR Proteomes; UP000070662; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000070662}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000070662}. FT DOMAIN 216 401 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 184 211 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 421 AA; 48086 MW; F26C3C5843EA5CAB CRC64; MSIGCFCLGL LIFVKQMIEK KEIDTGKAVL VGIATPEVSD FEMTDNLDEL AFLAETASIK EEGRFVQRLD TPNGATFVGK GKLDEIADFT RQKQIDIALF DDELSPTQQR NIEKILGIPA MDRTSLILDI FARRARTAHA KTQVEMAQYQ YLLPRLTRMW THLERQRGGL NMRGPGETQL ETDRRIVLDK IARLKEELQH IDRQKEQQRK HRGKMVRVAL VGYTNVGKST LMNLLSKSTV FAENKLFATL DTTVRKVVLH NLPFLLSDTV GFIRKLPTQL VKSFKSTLDE VIEADLIIHV VDLSHPNFEQ QFNVVNETLA ELLEGEKKPT LTLFNKIDAF TYTPKEDDDL TPKQRENYSL IELQETWMAH LGDNCLFVSA ATGDGIDGLK AKLYEMVKRI HITRYPYNDF LFEDYSDLAV E // ID A0A133XS92_9ACTN Unreviewed; 440 AA. AC A0A133XS92; DT 08-JUN-2016, integrated into UniProtKB/TrEMBL. DT 08-JUN-2016, sequence version 1. DT 07-JUN-2017, entry version 10. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=HMPREF3192_01035 {ECO:0000313|EMBL:KXB33806.1}; OS Atopobium deltae. OC Bacteria; Actinobacteria; Coriobacteriia; Coriobacteriales; OC Atopobiaceae; Atopobium. OX NCBI_TaxID=1393034 {ECO:0000313|EMBL:KXB33806.1, ECO:0000313|Proteomes:UP000070675}; RN [1] {ECO:0000313|EMBL:KXB33806.1, ECO:0000313|Proteomes:UP000070675} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DNF00019 {ECO:0000313|EMBL:KXB33806.1, RC ECO:0000313|Proteomes:UP000070675}; RA Oliw E.H.; RL Submitted (JAN-2016) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KXB33806.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LSCR01000029; KXB33806.1; -; Genomic_DNA. DR RefSeq; WP_066305819.1; NZ_KQ959507.1. DR EnsemblBacteria; KXB33806; KXB33806; HMPREF3192_01035. DR PATRIC; fig|1393034.3.peg.999; -. DR Proteomes; UP000070675; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000070675}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000070675}. FT DOMAIN 218 383 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 440 AA; 48915 MW; 27880D928B900490 CRC64; MGKQGRYKPQ PTAPEKERVI LVGVSTEKDR LMGSAWTLEE SLAELARLVE TDGAQVVGRL TQNVPTPFAK TFIGSGKVDE LLGLVERLEA QVVVFDDELT PSQQANLSKC LGKSVKVIDR TALILDIFAV HATAQAGRLQ VQLAQLQYMY PRLRGMWSHF AKEQTRGGIG SRFGQGESQL EVDRRLVRKR IAKVKQDLET LNRRRAVQAK ARLASGVWRV ALAGYTNAGK STLLNALTGA EVYAKDELFA TLDPTTRSCE LSEGRKITLT DTVGFIQKLP TTLIEAFKST LLEVQNADLI LLVADAHDKQ VAAQIEAVSK VLQQINADQI PYIVVFNKID LLIDDELADL QARYPDAVYI SAQERRGLDT LSYRISQAAT QGEALITVLI PYDKTALVHM VRQQAQIIRE DYQQQGFMAT IRISQKLLEL LEPFMLENPS // ID A0A133YAE1_9FIRM Unreviewed; 399 AA. AC A0A133YAE1; DT 08-JUN-2016, integrated into UniProtKB/TrEMBL. DT 08-JUN-2016, sequence version 1. DT 07-JUN-2017, entry version 10. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=HMPREF1872_00987 {ECO:0000313|EMBL:KXB40176.1}; OS Clostridiales bacterium KA00274. OC Bacteria; Firmicutes; Clostridia; Clostridiales. OX NCBI_TaxID=1497955 {ECO:0000313|EMBL:KXB40176.1, ECO:0000313|Proteomes:UP000070080}; RN [1] {ECO:0000313|EMBL:KXB40176.1, ECO:0000313|Proteomes:UP000070080} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=KA00274 {ECO:0000313|EMBL:KXB40176.1, RC ECO:0000313|Proteomes:UP000070080}; RA Oliw E.H.; RL Submitted (JAN-2016) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KXB40176.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LSCV01000031; KXB40176.1; -; Genomic_DNA. DR RefSeq; WP_066714380.1; NZ_KQ959588.1. DR EnsemblBacteria; KXB40176; KXB40176; HMPREF1872_00987. DR PATRIC; fig|1497955.3.peg.958; -. DR Proteomes; UP000070080; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000070080}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000070080}. FT DOMAIN 219 395 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 186 213 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 399 AA; 44527 MW; 5F8C5DCF66666D2D CRC64; MANKKGANRA DSTLFAKINS LQEEAEKAIC FSVCLTTKGQ TEAIVEASLD ELSELANTAG AEVLAKIYQK RAKIDSRYYI GVGKLEEIKV LAEQVEANCL ICDDELSPAQ LRNIEEFTQM KIVDRSLLIL DIFAKRAKSS EGKLQVALAQ AKYRLPRIQF MQGFNSRLAG GIGTRGPGES LKETDRRHIQ ARINTLQQKL VELGRKRQIV REQRRKSALT IAVVGYTNAG KSSLINRLCK SDLYAEDKVF ATLDPACRHL WLEDLSCDCL LIDTVGFIRK LPHHLVEAFK STLEEAAQAD FLLLVLDVAD VQAEAELDVV LSLLEEIGAS HLPRVYVANK FDEFNYDLSQ VDSSLLAKLH ALSFDDKSLF FTSVKEQRGL NELKAALQAK LKKILQKNN // ID A0A133YAR9_9BACT Unreviewed; 414 AA. AC A0A133YAR9; DT 08-JUN-2016, integrated into UniProtKB/TrEMBL. DT 08-JUN-2016, sequence version 1. DT 07-JUN-2017, entry version 10. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=HMPREF1870_01770 {ECO:0000313|EMBL:KXB40291.1}; OS Bacteroidales bacterium KA00344. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales. OX NCBI_TaxID=1497954 {ECO:0000313|EMBL:KXB40291.1, ECO:0000313|Proteomes:UP000070254}; RN [1] {ECO:0000313|EMBL:KXB40291.1, ECO:0000313|Proteomes:UP000070254} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=KA00344 {ECO:0000313|EMBL:KXB40291.1, RC ECO:0000313|Proteomes:UP000070254}; RA Oliw E.H.; RL Submitted (JAN-2016) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KXB40291.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LSCT01000155; KXB40291.1; -; Genomic_DNA. DR RefSeq; WP_066264053.1; NZ_KQ959448.1. DR EnsemblBacteria; KXB40291; KXB40291; HMPREF1870_01770. DR PATRIC; fig|1497954.3.peg.1795; -. DR Proteomes; UP000070254; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000070254}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000070254}. FT DOMAIN 215 399 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 414 AA; 47595 MW; 06EF50CA4A690467 CRC64; MKEFVISEVK AETAVLVGLI TPQQNEAKTE EYLDELEFLA DTAGAVTVKR FTQKVGGINQ TTYVGKGKLA EIKQYIKDEE DNEREVGMVI FDDELSAKQI HNIEKELKVK ILDRTSLILD IFAMRAQTAS AKTQVELAQY RYMLPRLQRL WTHLERQAGG SGAGGKGSVG LRGPGETQLE MDRRIILQRV TLLKKRLEDI DKQKKTQRKN RGRLIRVALV GYTNVGKSTI MNLLAKSDVF AENKLFATLD TTVRKVVVQN LPFLLADTVG FIRKLPTDLV ESFKSTLDEV READMLLHVV DISHPDFEEQ IRVVNATLKD LECADKPQMI IFNKIDNYRW VEKEPDDLTP ETKENITLEE LKHTWMAKLD ENCLFISAKQ KDNIDEFRDV LYRKVRELHV QKYPYNDFLY PIMD // ID A0A133YMH3_9FIRM Unreviewed; 429 AA. AC A0A133YMH3; DT 08-JUN-2016, integrated into UniProtKB/TrEMBL. DT 08-JUN-2016, sequence version 1. DT 07-JUN-2017, entry version 10. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=HMPREF3188_01280 {ECO:0000313|EMBL:KXB44385.1}; OS Tissierellia bacterium KA00581. OC Bacteria; Firmicutes; Tissierellia. OX NCBI_TaxID=1588751 {ECO:0000313|EMBL:KXB44385.1, ECO:0000313|Proteomes:UP000070503}; RN [1] {ECO:0000313|EMBL:KXB44385.1, ECO:0000313|Proteomes:UP000070503} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=KA00581 {ECO:0000313|EMBL:KXB44385.1, RC ECO:0000313|Proteomes:UP000070503}; RA Oliw E.H.; RL Submitted (JAN-2016) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KXB44385.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LSCW01000081; KXB44385.1; -; Genomic_DNA. DR RefSeq; WP_068552466.1; NZ_KQ959659.1. DR EnsemblBacteria; KXB44385; KXB44385; HMPREF3188_01280. DR PATRIC; fig|1588751.3.peg.1260; -. DR Proteomes; UP000070503; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000070503}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000070503}. FT DOMAIN 200 374 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 173 200 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 429 AA; 49365 MW; 729587A723C99ED3 CRC64; MNRKVIAVTV NIEDDNKIVD SKKDIENKIF ELENLIEAIG DETVINITQN KDKIDKSYYI GKGKALEIKD YCQKLSADLV VFNNELTGSQ VKNLEQLIEA EVIDRTNLIL DIFNQRAKTK EAKLQVKIAK LKYTLPRLSM LRSGFSRQQG GIGTKGVGEQ QIELDRRTIS SQIASISSRL KEIQKNRNET RKKRVNSKNN IISLIGYTNA GKSTIMNKLI SYNKEENSIT KEVFVKDMLF ATLDTYVREG KLLNGQNVMY VDTVGFVSDI PHNLVESFKS TLEEIKYSNL LLHVIDISNT NVDKQIEITN EMIKELNCEQ KDVIYVFNKT DKLLDENIKL QYVNLKNKVF ISAKNDKDIV ILLKEIEKVL FSKAKNTKLL IPYDKQQLVN KILEHYIPKN VQYLDNGSMI EISLKKEDYE IYKGYEINE // ID A0A133ZKA8_9CORY Unreviewed; 509 AA. AC A0A133ZKA8; DT 08-JUN-2016, integrated into UniProtKB/TrEMBL. DT 08-JUN-2016, sequence version 1. DT 07-JUN-2017, entry version 9. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=HMPREF0307_00545 {ECO:0000313|EMBL:KXB55883.1}; OS Corynebacterium sp. DNF00584. OC Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae; OC Corynebacterium. OX NCBI_TaxID=1384076 {ECO:0000313|EMBL:KXB55883.1, ECO:0000313|Proteomes:UP000070591}; RN [1] {ECO:0000313|EMBL:KXB55883.1, ECO:0000313|Proteomes:UP000070591} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DNF00584 {ECO:0000313|EMBL:KXB55883.1, RC ECO:0000313|Proteomes:UP000070591}; RA Oliw E.H.; RL Submitted (JAN-2016) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KXB55883.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LSCZ01000007; KXB55883.1; -; Genomic_DNA. DR EnsemblBacteria; KXB55883; KXB55883; HMPREF0307_00545. DR PATRIC; fig|1384076.3.peg.530; -. DR Proteomes; UP000070591; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000070591}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000070591}. FT DOMAIN 281 452 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 509 AA; 55437 MW; BB1374D92CA1481D CRC64; MGKHMTEKEK QSHEDLLAAA FRDLAAPVHG VRPVDHGDHG DPTTGELDLA ERNSFRRVTK ATTIRAEDTT DGYEVEYRKL RLEQVVLVGV WTEGTVAEVE ATMSELAALT ETAGAEVVEA LYQKRDKPDP GTYVGSGKVK ELKDIVMATG ADTVVCDGEL TPGQLSALER ELDTKVIDRT MLILDIFAQH AKSKEGKAQV SLAQLEYLYT HTRGWGGNLS RQAGGRAGSN GGVGLRGPGE TKIETDRRRI RTQMALLRRE LKAMKTAREV KRARRGASAI PQIAIAGYTN AGKSSLINAM TGAGVLVENA LFATLDPTTR RAELADGRQV VFTDTVGFVR HLPTQLVEAF KSTLEEVLAA DIMLHVVDGS DPFPLKQIEA VNKVIYDIVR ETGEDAPPEI IVINKIDEAD PLVLAELRHV LDRDNVVYVS AKTGEGIDEL TARVELFLNA RDAHVQLLVP FTRGDVVARA HAVGTVRSES YTEDGTLLDV RLPVAVADEL KEFHVSDAA // ID A0A134AFY7_9FIRM Unreviewed; 425 AA. AC A0A134AFY7; DT 08-JUN-2016, integrated into UniProtKB/TrEMBL. DT 08-JUN-2016, sequence version 1. DT 05-JUL-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=HMPREF1863_01015 {ECO:0000313|EMBL:KXB66633.1}; OS Peptoniphilus coxii. OC Bacteria; Firmicutes; Tissierellia; Tissierellales; Peptoniphilaceae; OC Peptoniphilus. OX NCBI_TaxID=755172 {ECO:0000313|EMBL:KXB66633.1, ECO:0000313|Proteomes:UP000070442}; RN [1] {ECO:0000313|EMBL:KXB66633.1, ECO:0000313|Proteomes:UP000070442} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DNF00729 {ECO:0000313|EMBL:KXB66633.1, RC ECO:0000313|Proteomes:UP000070442}; RA Oliw E.H.; RL Submitted (JAN-2016) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KXB66633.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LSDG01000027; KXB66633.1; -; Genomic_DNA. DR EnsemblBacteria; KXB66633; KXB66633; HMPREF1863_01015. DR PATRIC; fig|755172.3.peg.974; -. DR Proteomes; UP000070442; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000070442}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000070442}. FT DOMAIN 198 368 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 425 AA; 47978 MW; CE2F597965FA066A CRC64; MEKHITERQK VITAAAWDDK SKYNEESLSE LNDLVDVAGG VVVGTATQTV RSFHPATLMG KGKLEEIRLA AETLGAELVI FDGELTGIQM REIEKVLDLP VLDRTALILD IFASRARTDV GKLQVYLAQL EYGKTHLIGK KNYSRLGGGI GTRGPGEQKL EIDRRRINDD IMRTKRKLKR AQKVRDTGRK QRERSDIPSI AIVGYTNAGK SSLMNRMLRE SSAQGKEVYV EDMPFASLDP DTRRITLPGG LAVCVTDTVG FISNLPTTLI ESFHTTLEEL KDSDLIIHMI DGSEEDEGLR YETTQKLLSD LGVRDTPIIL FVNKADKMEH KKLPFLPSEH RVLYGSVRED PSIESLYAAI EEALKSKYVK VMMAFSYGEM HLVEEIKNRF PVEAFEYTHG GVELLATLPK VYLNRYEEQI RRRYV // ID A0A135HVW1_9RHIZ Unreviewed; 464 AA. AC A0A135HVW1; DT 08-JUN-2016, integrated into UniProtKB/TrEMBL. DT 08-JUN-2016, sequence version 1. DT 07-JUN-2017, entry version 10. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=ATN84_07995 {ECO:0000313|EMBL:KXF77326.1}; OS Paramesorhizobium deserti. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Phyllobacteriaceae; Paramesorhizobium. OX NCBI_TaxID=1494590 {ECO:0000313|EMBL:KXF77326.1, ECO:0000313|Proteomes:UP000070107}; RN [1] {ECO:0000313|EMBL:KXF77326.1, ECO:0000313|Proteomes:UP000070107} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=A-3-E {ECO:0000313|EMBL:KXF77326.1, RC ECO:0000313|Proteomes:UP000070107}; RA Lv R., Yang X., Fang N., Guo J., Luo X., Peng F., Yang R., Cui Y., RA Fang C., Song Y.; RT "Draft genome sequence of Paramesorhizobium deserti A-3-E, a strain RT highly resistant to diverse beta-lactam antibiotics."; RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KXF77326.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LNTU01000012; KXF77326.1; -; Genomic_DNA. DR RefSeq; WP_068881512.1; NZ_LNTU01000012.1. DR EnsemblBacteria; KXF77326; KXF77326; ATN84_07995. DR Proteomes; UP000070107; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000070107}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000070107}. FT DOMAIN 233 407 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 464 AA; 51658 MW; 7E09F0D55C5AAEBE CRC64; MSRSKGRTTH EGDADAGFGT SAKGPTRAVV IVPILPERLQ DAGQADDVYR PQFRRSNEAR LEEAIGLARA IDLDLVYCDV VTVANPRPAT LIGSGKVEAI AEIIKREEAE LVIVDHALTP VQQRNLEKEW NAKVIDRTGL ILEIFGRRAQ TKEGALQVEL AHLNYQKGRL VRSWTHLERQ RGGGGFLGGP GETQIEADRR ILQEKILRIR RELETVVRTR TLHRQKRRKV PHPIVALVGY TNAGKSTLFN RLTGSDVLAE DMLFATLDPT LRRIRLPHGE TVILSDTVGF ISNLPTHLVA AFRATLEEVV EADLILHVRD ISDPDNAAQA EDVESILESL DIERGDVRRI LEVWNKIDLL DEAGREAALR LSAAAPEDAR PIAISAATGE GVDHLLSVIE SRISGALEHV ELELAPNDLH LLDWIYQHAS NIRRNDLEDG SLRIKADMTV SARKTLRERM KNEK // ID A0A135I436_9GAMM Unreviewed; 429 AA. AC A0A135I436; DT 08-JUN-2016, integrated into UniProtKB/TrEMBL. DT 08-JUN-2016, sequence version 1. DT 30-AUG-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=ATN88_10150 {ECO:0000313|EMBL:KXF80210.1}; OS Enterovibrio coralii. OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; OC Vibrionaceae; Enterovibrio. OX NCBI_TaxID=294935 {ECO:0000313|EMBL:KXF80210.1, ECO:0000313|Proteomes:UP000070529}; RN [1] {ECO:0000313|EMBL:KXF80210.1, ECO:0000313|Proteomes:UP000070529} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CAIM 912 {ECO:0000313|EMBL:KXF80210.1, RC ECO:0000313|Proteomes:UP000070529}; RA Gomez-Gil B., Enciso-Ibarra J.; RT "Genomic Taxonomy of the Vibrionaceae."; RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KXF80210.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LNTY01000055; KXF80210.1; -; Genomic_DNA. DR RefSeq; WP_067419440.1; NZ_LNTY01000055.1. DR EnsemblBacteria; KXF80210; KXF80210; ATN88_10150. DR Proteomes; UP000070529; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000070529}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000070529}. FT DOMAIN 198 365 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 429 AA; 48584 MW; 2E66A50787332DFC CRC64; MFDRYEAGEQ AVLVHINFTQ EGEWEDLSEF EMLVSSAGVT KLQTITGSRQ APHSKYFVGE GKALEIADAV RMTGAEIVIF NHALSPAQER NLERLVKCRV LDRTGLILDI FAQRARTHEG KLQVELAQLR HLSTRLVRGW THLERQKGGI GLRGPGETQL ETDRRLLRDR VKAILRRLDK VAKQREQGRR ARNRAEVPTV SLVGYTNAGK STLFNRITQA GVYAADQLFA TLDPTLRKID VEDVGDVILA DTVGFIRHLP HDLVAAFKAT LKETQEAQLL LHVVDASDER FRENIDAVNV VLEEIEANEV PVLLVMNKID NMEDAQPRIE RDDEGVPRVV WVSALADRGI DLLFEALTER LSGTMVNYRL RIPPAAIGRM HSKFCQLRCI LHEEYEQDGH LLIDVRLPQT DWLRLKKREG SELGDFIVS // ID A0A135VGN3_9ARCH Unreviewed; 427 AA. AC A0A135VGN3; DT 11-MAY-2016, integrated into UniProtKB/TrEMBL. DT 11-MAY-2016, sequence version 1. DT 12-APR-2017, entry version 6. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:KXH71809.1}; GN ORFNames=AM324_08105 {ECO:0000313|EMBL:KXH71809.1}; OS Candidatus Thorarchaeota archaeon SMTZ1-83. OC Archaea; Asgard group; Candidatus Thorarchaeota. OX NCBI_TaxID=1706445 {ECO:0000313|EMBL:KXH71809.1, ECO:0000313|Proteomes:UP000070043}; RN [1] {ECO:0000313|EMBL:KXH71809.1, ECO:0000313|Proteomes:UP000070043} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SMTZ1-83 {ECO:0000313|EMBL:KXH71809.1}; RX PubMed=26824177; RA Seitz K.W., Lazar C.S., Hinrichs K.U., Teske A.P., Baker B.J.; RT "Genomic reconstruction of a novel, deeply branched sediment archaeal RT phylum with pathways for acetogenesis and sulfur reduction."; RL ISME J. 0:0-0(2016). CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KXH71809.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LRSK01000220; KXH71809.1; -; Genomic_DNA. DR Proteomes; UP000070043; Unassembled WGS sequence. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR CDD; cd01878; HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000070043}; KW Reference proteome {ECO:0000313|Proteomes:UP000070043}. FT DOMAIN 195 365 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 427 AA; 47938 MW; 47296C0F8246A8EA CRC64; MTVERALLIQ RRAHNEPNLL DEFEALALTA GYSVAKSYDI VSTPSARYAI RSGKVEEIAT WIEINQPDVV LFSPRLTSGQ VFRLMERWEV EVRDRTQLIL EIFDRQARTP QAKLQIEQAR LRYELPFERH QIRMRLQKEH TGDRPIAEQI GAGEDLLNLR IHQIRKRIAV IQEKLDSISK AQGLKKRKRS KKGFLEVTLA GYTNAGKSTL HRALTGSEVE VADKLFTTLS TKSTELPLEG RKVVLTDSVG FISDLPRSLL QAFNTTLMEI GEADVIVLVV DGSDSLAEMR RKLDTCLETF TQIGVNGISS VVAVNKIDLL EEGAIQERLE IVNDESLRGV PISALKNTNL EELVQVIDSN LPSLTRYLLT LPYSDETMSL VSQLHDMSSV RNQDFAGGTV HVEVILSAEM VQKLESELPV GSLKRID // ID A0A135W7L7_9BACL Unreviewed; 423 AA. AC A0A135W7L7; DT 08-JUN-2016, integrated into UniProtKB/TrEMBL. DT 08-JUN-2016, sequence version 1. DT 07-JUN-2017, entry version 10. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=AU377_09215 {ECO:0000313|EMBL:KXH80901.1}; OS Sporosarcina sp. HYO08. OC Bacteria; Firmicutes; Bacilli; Bacillales; Planococcaceae; OC Sporosarcina. OX NCBI_TaxID=1759557 {ECO:0000313|EMBL:KXH80901.1, ECO:0000313|Proteomes:UP000070230}; RN [1] {ECO:0000313|EMBL:KXH80901.1, ECO:0000313|Proteomes:UP000070230} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=HYO08 {ECO:0000313|EMBL:KXH80901.1, RC ECO:0000313|Proteomes:UP000070230}; RA Choi I.-G., Park W.; RT "Draft genome sequences of microorganisms having biocementation RT activity."; RL Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KXH80901.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LPUT01000027; KXH80901.1; -; Genomic_DNA. DR RefSeq; WP_067407819.1; NZ_LPUT01000027.1. DR EnsemblBacteria; KXH80901; KXH80901; AU377_09215. DR Proteomes; UP000070230; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000070230}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000070230}. FT DOMAIN 200 368 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 159 193 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 423 AA; 48274 MW; CAD88616D41A83CC CRC64; MEILVERAIL VGVHEQQDEH FDYAMEELKN LADAIDVETV GVVTQSLERR HPSHYVGKGK VIEIRNVYDA TDANLIIFND ELSPSQIRNL EQELECKIID RTMLILDIFA RRARTSESKM QVELAQLQYT LPRLIGLRAS LSRQGGGTGG GFQNKGAGET KLELDRRKIE DQIAKLRRDL NHVKDQRETQ RKQRKRSGIP VVSIVGYTNA GKSTLMNRLL EKMDTDHSKQ VFEKDMLFAT LDTSIRKIKL IDNKEFILTD TVGFVSKLPH NLVQAFRSTL EEARDADLLL HVVDVSNEDY QYMVEVTNDT LHEIGVENVA MVNVYNKADL ANIMYPKVSG NTVWLSAREG NGLEELIALI KRHIFEQYVT CKLMIPYDRG EIVSHLNDKA NVKNVAYEEE GTLMTVEMDV TERDKLSEYI ISH // ID A0A136A503_9ALTE Unreviewed; 432 AA. AC A0A136A503; DT 08-JUN-2016, integrated into UniProtKB/TrEMBL. DT 08-JUN-2016, sequence version 1. DT 30-AUG-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=AX660_10070 {ECO:0000313|EMBL:KXI30313.1}; OS Paraglaciecola sp. S66. OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales; OC Alteromonadaceae; Paraglaciecola. OX NCBI_TaxID=1799789 {ECO:0000313|EMBL:KXI30313.1, ECO:0000313|Proteomes:UP000070299}; RN [1] {ECO:0000313|EMBL:KXI30313.1, ECO:0000313|Proteomes:UP000070299} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=S66 {ECO:0000313|EMBL:KXI30313.1, RC ECO:0000313|Proteomes:UP000070299}; RA Wen L., He K., Yang H.; RL Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KXI30313.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LSNE01000003; KXI30313.1; -; Genomic_DNA. DR RefSeq; WP_068374518.1; NZ_LSNE01000003.1. DR Proteomes; UP000070299; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000070299}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000070299}. FT DOMAIN 198 365 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 432 AA; 48760 MW; A073C63256352550 CRC64; MFDRYAAGEQ AVLVHVDFAD ENSREDLLEL QLLVSSAGVN AVDVVSGSRQ TPKARYFVGS GKAEEIANSV RANQADVVIF NHSLTPSQER NLEKLCQCRV LDRTGLILDI FAQRARTHEG KLQVELAQLK HMSTRLIRGW THLERQKGGI GLRGPGETQL ETDRRLLRER IKSITRRLAK VQVQREQGRR ARLRAEIPTV SLVGYTNAGK STLFNTVTQS AVYAADQLFA TLDPTLRKIQ LQDIGSAILA DTVGFIRHLP HDLIAAFKAT LQETQQADLL LHVVDYADEQ FRENTDQVNK VLEEIEADDI KQLVVCNKID RMEGVEARID RDEENVPIRV WVSAQQGLGI DLLLSAISEC LSKNMVQHTL RIPPSLSKLR GALYEMNCIA EQSYTDNGDW QVAVRMEQSD WQRLIKRSEI NLQDYIVSDN QN // ID A0A136FXM4_9PSED Unreviewed; 434 AA. AC A0A136FXM4; DT 08-JUN-2016, integrated into UniProtKB/TrEMBL. DT 08-JUN-2016, sequence version 1. DT 30-AUG-2017, entry version 14. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=AX284_08730 {ECO:0000313|EMBL:KXJ33092.1}; OS Pseudomonas sp. HUK17. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=1799359 {ECO:0000313|EMBL:KXJ33092.1, ECO:0000313|Proteomes:UP000070105}; RN [1] {ECO:0000313|EMBL:KXJ33092.1, ECO:0000313|Proteomes:UP000070105} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=HUK17 {ECO:0000313|EMBL:KXJ33092.1, RC ECO:0000313|Proteomes:UP000070105}; RA Gasc C., Richard J.-Y., Peyret P.; RT "Genome sequence of Pseudomonas psychrotolerans Strain HUK17, Isolated RT from Hexachlorocyclohexane-contaminated Soil."; RL Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KXJ33092.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LSMW01000003; KXJ33092.1; -; Genomic_DNA. DR RefSeq; WP_017642908.1; NZ_LSMW01000003.1. DR EnsemblBacteria; KXJ33092; KXJ33092; AX284_08730. DR Proteomes; UP000070105; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000070105}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000070105}. FT DOMAIN 199 367 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 165 192 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 434 AA; 49278 MW; 40F967976C873E7D CRC64; MFFERHEGGE RAILVHLEGL HPEAREDPQE FLELARSAGA ETVAFVTVNR SQPTARYLIG TGKVEELHDQ VHAHAADLVI FNHDLTPSQE RNLEKAFECR VLDRTGLILD IFAQRARTHE GKLQVELAQL EHMSTRLVRG WTHLERQKGG IGLRGPGETQ LETDRRLLRI RIRQIRQRLD KVRSQREQAR RGRRRAEIPS VSLVGYTNAG KSTLFNSLTE SGVYAANLLF ATLDPTLRRL ELPDLGPIVL ADTVGFIRHL PHKLVEAFRA TLEESSNSDL LLHVIDAHED DRQLQIEQVE AVLHEIGADE LPMLEIYNKL DLLDGVEPHI QRDDETGRPI RVWVSAREGR GLELVGQAVA ELLGEDLFVG VLRLPQRHAR LRAQLFELGV VRQDDHDDEG NILLSVRVPR AELNRLLSRA GEEPEVFIQQ HVLQ // ID A0A136GQC7_9GAMM Unreviewed; 302 AA. AC A0A136GQC7; DT 08-JUN-2016, integrated into UniProtKB/TrEMBL. DT 08-JUN-2016, sequence version 1. DT 12-APR-2017, entry version 5. DE SubName: Full=GTPase HflX {ECO:0000313|EMBL:KXJ45359.1}; DE Flags: Fragment; GN ORFNames=AXW16_04320 {ECO:0000313|EMBL:KXJ45359.1}; OS Cycloclasticus sp. Phe_18. OC Bacteria; Proteobacteria; Gammaproteobacteria; Thiotrichales; OC Piscirickettsiaceae; Cycloclasticus. OX NCBI_TaxID=1795870 {ECO:0000313|EMBL:KXJ45359.1, ECO:0000313|Proteomes:UP000070359}; RN [1] {ECO:0000313|EMBL:KXJ45359.1, ECO:0000313|Proteomes:UP000070359} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Phe_18 {ECO:0000313|EMBL:KXJ45359.1}; RA Wen L., He K., Yang H.; RL Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KXJ45359.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LSMQ01000082; KXJ45359.1; -; Genomic_DNA. DR Proteomes; UP000070359; Unassembled WGS sequence. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000070359}; KW Reference proteome {ECO:0000313|Proteomes:UP000070359}. FT DOMAIN 200 302 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT NON_TER 302 302 {ECO:0000313|EMBL:KXJ45359.1}. SQ SEQUENCE 302 AA; 34019 MW; A30748DE247B0766 CRC64; MELFDRPDTG EKALIIHLSI NESFSEDDLS EFVQLVISAN VEPVATITGS RRAPDARFFV GKGKLEEVRQ VLHETCADIV LFNHSLSPSQ QRNLEKELEV RVLDRTNLIL DIFAQRAQSF EGKLQVELAQ LQHLSTRLIR GWTHLERQKG GIGLRGPGET QLETDRRLIG QRIRQIKMRL AKVNKQRNQG RRGRQRADVP TVSLVGYTNA GKSTLFNALT NSSIYVADQL FATLDPTLRQ VKLPDYGELV LADTVGFIQD LPHELVAAFR STLQETIEAD LLLHVVDASS PNRQEQIHEV NS // ID A0A136GYB5_9GAMM Unreviewed; 456 AA. AC A0A136GYB5; DT 08-JUN-2016, integrated into UniProtKB/TrEMBL. DT 08-JUN-2016, sequence version 1. DT 30-AUG-2017, entry version 8. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=AXW13_08210 {ECO:0000313|EMBL:KXJ48384.1}; OS Alcanivorax sp. Nap_24. OC Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales; OC Alcanivoracaceae; Alcanivorax. OX NCBI_TaxID=1795868 {ECO:0000313|EMBL:KXJ48384.1, ECO:0000313|Proteomes:UP000070259}; RN [1] {ECO:0000313|EMBL:KXJ48384.1, ECO:0000313|Proteomes:UP000070259} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Nap_24 {ECO:0000313|EMBL:KXJ48384.1}; RA Wen L., He K., Yang H.; RL Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KXJ48384.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LSMO01000025; KXJ48384.1; -; Genomic_DNA. DR Proteomes; UP000070259; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000070259}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000070259}. FT DOMAIN 205 372 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 456 AA; 51156 MW; EC9B0651F804B48B CRC64; MDLFDRTEQV RTGAGEKAVL VHIDLPDALG REDLDEFHHL VTSSGVEPVV ELLGKRDRPD PALFIGSGKA EELADLVREH QADVVLFNHG LSAGQERNLE RAVKCRVLDR TGLILDIFAQ RARTHEGRLQ VELAQLQHLS TRLVRGWTHL ERQKGGIGLR GPGETQLETD RRLLRERIRS IQARLDKVRK QRAQGRRARD RSETPLISLV GYTNAGKSTL FNALTTGDVY VADKLFATLD PTLRKVRVPG VGPAILADTV GFIRHLPHRL VQAFRATLEE TVNASLLLHV TDSSVEESDA NVAAVNEVLE EIGADTVPVL HVYNKVDALE DASPHLERDE QGLPWRVWLS ARTGEGFDLL HQAIAERLAD RWVDRWLRLP PEAGRLRSRL HEAGEVREEQ AATDGGMLLR VHVNRVHFER LLREAGLREE QVRVHDPSVA ETDTPSYNPE RSHRAG // ID A0A136H2Y8_9GAMM Unreviewed; 428 AA. AC A0A136H2Y8; DT 08-JUN-2016, integrated into UniProtKB/TrEMBL. DT 08-JUN-2016, sequence version 1. DT 30-AUG-2017, entry version 8. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=AXW17_02200 {ECO:0000313|EMBL:KXJ49759.1}; OS Colwellia sp. Phe_37. OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales; OC Colwelliaceae; Colwellia. OX NCBI_TaxID=1795872 {ECO:0000313|EMBL:KXJ49759.1, ECO:0000313|Proteomes:UP000070110}; RN [1] {ECO:0000313|EMBL:KXJ49759.1, ECO:0000313|Proteomes:UP000070110} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Phe_37 {ECO:0000313|EMBL:KXJ49759.1}; RA Wen L., He K., Yang H.; RL Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KXJ49759.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LSMS01000311; KXJ49759.1; -; Genomic_DNA. DR Proteomes; UP000070110; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000070110}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000070110}. FT DOMAIN 198 365 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 164 191 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 428 AA; 48699 MW; 8A8608AC0529D8AE CRC64; MFDRYQAGEQ AILVHLDFPD DSTREDLQEF EMLVDSAGIT ALNTITGKRN TPHPKFFVGT GKAQEVADAV RMFGANIVLF NHSLSPSQEK NIEALCECRV VDRTTLILDI FAQRARTHEG KLQVELAQLR HISTRLIRGW THLERQKGGI GLRGPGETQL ETDRRLLRER MVNIRKRLEK VEKQRQQGRR ARNRAEIPTV SLVGYTNAGK STLFNKITQA DVYAADQLFA TLDPTLRKIE VEEVGRVILA DTVGFIRHLP HDLVAAFKAT LTETREAELL LHVIDIADER RSENIEQVDE VLKEIEAGDV PQLLICNKID RLDDVEPRID RDEQGLPIRV WLSAQQGVGI ELLFIALAER LGKQIIKHLL CLPPSAGKLR GQLYQLNCIT DEHYDDKGNC LLTIKLPVRE WNQLLKQDEA EIEHFIQT // ID A0A136HAG7_9GAMM Unreviewed; 418 AA. AC A0A136HAG7; DT 08-JUN-2016, integrated into UniProtKB/TrEMBL. DT 08-JUN-2016, sequence version 1. DT 12-APR-2017, entry version 7. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=AXW15_03530 {ECO:0000313|EMBL:KXJ52663.1}; OS Neptuniibacter sp. Phe_28. OC Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales; OC Neptuniibacter. OX NCBI_TaxID=1795871 {ECO:0000313|EMBL:KXJ52663.1, ECO:0000313|Proteomes:UP000070472}; RN [1] {ECO:0000313|EMBL:KXJ52663.1, ECO:0000313|Proteomes:UP000070472} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Phe_28 {ECO:0000313|EMBL:KXJ52663.1}; RA Wen L., He K., Yang H.; RL Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KXJ52663.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LSMR01000163; KXJ52663.1; -; Genomic_DNA. DR Proteomes; UP000070472; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000070472}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000070472}. FT DOMAIN 183 350 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 418 AA; 47013 MW; C8F40B6BEA05E9C3 CRC64; MNLAAAADQE SPKELEELAL SAGADPVEFL TGSLGHPNPK FFIGQGKLEE LKTLVDHHDA QVVIFNHALS PAQERNIERE IQCRVLDRTG LILDIFAQRA RTHEGKLQVE LAQLDHMSTR LVRGWTHLER QKGGIGLRGP GETQLETDRR LLRARMKSIH KRLEKVRKQR DQGRRSRKRA EVPTLSLVGY TNAGKSTLFN ALTASEVYAA DQLFATLDPT LRRIDIEDVG PAILADTVGF IRHLPHKLVE AFRATLQETI EATLLLHVID CHDDDRHEHV AEVEHVLGEI GADEVPVLEV YNKIDLLEGR EARIDRNEEG KPIRVWLSAV AGKGHELLFQ AVNELLADDV YHDSVTLQSS EGQFRARLYD SGAVLSEQMD ENGSIVLEVR IQKKDMLQIL SHLGMPQERC FPVEVNPY // ID A0A136HFM3_9GAMM Unreviewed; 455 AA. AC A0A136HFM3; DT 08-JUN-2016, integrated into UniProtKB/TrEMBL. DT 08-JUN-2016, sequence version 1. DT 10-MAY-2017, entry version 8. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=AXW17_00835 {ECO:0000313|EMBL:KXJ54150.1}; OS Colwellia sp. Phe_37. OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales; OC Colwelliaceae; Colwellia. OX NCBI_TaxID=1795872 {ECO:0000313|EMBL:KXJ54150.1, ECO:0000313|Proteomes:UP000070110}; RN [1] {ECO:0000313|EMBL:KXJ54150.1, ECO:0000313|Proteomes:UP000070110} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Phe_37 {ECO:0000313|EMBL:KXJ54150.1}; RA Wen L., He K., Yang H.; RL Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KXJ54150.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LSMS01000165; KXJ54150.1; -; Genomic_DNA. DR Proteomes; UP000070110; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000070110}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000070110}. FT DOMAIN 235 400 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 196 230 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 455 AA; 50524 MW; 775FBC1919E19DAC CRC64; MQLTAKAALN HALLISIATP EFKGDEATES LAELARLVTT LGFKVVGSQS QKLSSTKKLN VLGLGKLAEI AHLTGNKGSV EEDDFEEINE AHATDKTLTS EKLLTDIPSD NLPFACADVV VFDCDLSPSQ LRNVENQLGV EVFDRTGIII EIFSRHARTR TARLQVEIAR LNYVAPRLRE STSGNKERQM GKGAGETTLE LDRRKVRDQL AELKRELVSV QNEMKGRRTQ RAELFCVALV GYTNAGKSSM MRAITGSDVE GENKLFATLD TTVRALYPVT QPRILVSDTV GFIKKLPHDL VASFHSTLAE AHDASLLLYV VDAADPSFRT QLDVVHEVLA EVGVEDSKKL LVLNKSDQLT PEQQQALMVE FPDAMLTSTR HPADIKKLHQ YIVDVAQEEM IEDEITVPYT AKGIIGEIRA SMSVTKEDYE YEHIKLTVRS NAIDLQRLKK RMKNL // ID A0A136HTI1_9ALTE Unreviewed; 429 AA. AC A0A136HTI1; DT 08-JUN-2016, integrated into UniProtKB/TrEMBL. DT 08-JUN-2016, sequence version 1. DT 30-AUG-2017, entry version 10. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=AXW14_01340 {ECO:0000313|EMBL:KXJ58911.1}; OS Alteromonas sp. Nap_26. OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales; OC Alteromonadaceae; Alteromonas. OX NCBI_TaxID=1795869 {ECO:0000313|EMBL:KXJ58911.1, ECO:0000313|Proteomes:UP000070342}; RN [1] {ECO:0000313|EMBL:KXJ58911.1, ECO:0000313|Proteomes:UP000070342} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Nap_26 {ECO:0000313|EMBL:KXJ58911.1}; RA Wen L., He K., Yang H.; RL Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KXJ58911.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LSMP01000232; KXJ58911.1; -; Genomic_DNA. DR Proteomes; UP000070342; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000070342}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000070342}. FT DOMAIN 198 365 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 164 191 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 429 AA; 48042 MW; 4C2FAA1324664120 CRC64; MFDRYEAGEQ AVLVHVNFSD ESNKEDLSEL SLLVSSAGVD AVEVITTSRS APHAKFFVGS GKAEEIAAAV KAHDANVVIF NHALSPSQER NLEAVCKCRV LDRTGLILDI FAQRARTHEG KLQVELAQLR HISTRLIRGW THLERQKGGI GLRGPGETQL ETDRRLLRGR IKAILRRLEK VQKQREQGRR SRKRAEIPTV SLVGYTNAGK STLFNTITDS HVYAADQLFA TLDPTLRKID LKDVGPAILA DTVGFIRHLP HDLVAAFKAT LQETQEADLL LHVVDIADAK YRETMDEVNN VLEEIDAGEI QQLVICNKID KLEDVKPRIE RNDEGVPVRV WLSAQSGDGT ELLSQALTEC LGRSMVNYTL KIPPAHSRLR GVLYELNCIS SEQYDSQGDW VVDVRMPAAD WNRLEKRLEN GISEYVVHH // ID A0A136JS73_9BACT Unreviewed; 329 AA. AC A0A136JS73; DT 08-JUN-2016, integrated into UniProtKB/TrEMBL. DT 08-JUN-2016, sequence version 1. DT 07-JUN-2017, entry version 4. DE SubName: Full=GTP-binding protein HflX {ECO:0000313|EMBL:KXK00006.1}; GN ORFNames=UZ17_ACD001002280 {ECO:0000313|EMBL:KXK00006.1}; OS Acidobacteria bacterium OLB17. OC Bacteria; Acidobacteria. OX NCBI_TaxID=1617423 {ECO:0000313|EMBL:KXK00006.1, ECO:0000313|Proteomes:UP000070331}; RN [1] {ECO:0000313|EMBL:KXK00006.1, ECO:0000313|Proteomes:UP000070331} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=OLB17 {ECO:0000313|EMBL:KXK00006.1}; RA Speth D.R., In T Zandt M., Guerrero Cruz S., Dutilh B.E., Jetten M.S.; RT "Genome based microbial ecology of anammox granules in a full-scale RT wastewater treatment system."; RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KXK00006.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LLEU01000048; KXK00006.1; -; Genomic_DNA. DR PATRIC; fig|1617423.3.peg.2378; -. DR Proteomes; UP000070331; Unassembled WGS sequence. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF13167; GTP-bdg_N; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000070331}; KW Reference proteome {ECO:0000313|Proteomes:UP000070331}. FT DOMAIN 226 313 GTP-bdg_N. {ECO:0000259|Pfam:PF13167}. SQ SEQUENCE 329 AA; 36742 MW; FE5C31D8556CD7A4 CRC64; MNTEETRFTI SKVSGFTRGL KHNQLVRIER LGTRRVPASD IVSPELARQM SEISHETGRQ IGVLLNRKGQ VEYVMVGNSK QIEMPDFGRS RVSTERFRGL RCVHTHLQGE KLTQDDLTDL ALLRFDLMSI IQVEPKTGLP GMVYSAHLLP MSARAANSDG DKDASEPYQF LEPNIPSQLD TDLLELIPSL EAEMARVSAT ARIRSSGRER AILVGVTTGD IDEERESMTE LEELTISADV TVVDSFIQRR PQIDPRTVLG RGKLDDLFVR SMRLGADLLI FDTELSPAQV RSLSEATELK VIDRPQLILD IFASVPRAGK ENFRSSLPS // ID A0A136K3N4_9BACT Unreviewed; 538 AA. AC A0A136K3N4; DT 08-JUN-2016, integrated into UniProtKB/TrEMBL. DT 08-JUN-2016, sequence version 1. DT 07-JUN-2017, entry version 8. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=UZ03_NOB001001504 {ECO:0000313|EMBL:KXK04021.1}; OS Nitrospira sp. OLB3. OC Bacteria; Nitrospirae; Nitrospirales; Nitrospiraceae; Nitrospira. OX NCBI_TaxID=1617410 {ECO:0000313|EMBL:KXK04021.1, ECO:0000313|Proteomes:UP000070691}; RN [1] {ECO:0000313|EMBL:KXK04021.1, ECO:0000313|Proteomes:UP000070691} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=OLB3 {ECO:0000313|EMBL:KXK04021.1}; RA Speth D.R., In T Zandt M., Guerrero Cruz S., Jetten M.S., Dutilh B.E.; RT "Improved understanding of the partial-nitritation anammox process RT through 23 genomes representing the majority of the microbial RT community."; RL Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KXK04021.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JZQY01000034; KXK04021.1; -; Genomic_DNA. DR PATRIC; fig|1617410.3.peg.1528; -. DR Proteomes; UP000070691; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000070691}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000070691}. FT DOMAIN 352 538 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 311 338 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 538 AA; 60247 MW; 74AABF8E60CBBC65 CRC64; MPASVVITSE LARTTCQLSR EIRRPIGLLI TRRGIVDQVL IGAACVPTFE SLARFRVGPH SLRGLRLIRT DLHEEPLTQE DLTQLALLRL DLIGSLGTNE DGEPTLLHLA HLLPLNPQGQ VCQIMKPVPF HQLNFPFDVF IQSLDSELLR AETTHTVGGQ AEAAILISAS PKSRGEQEEH LEELQELAES AGVRVLDRMV QRTHEDYQRF LLGKGKLKEV VVRALQQGAD LLIFDQDLAP AQARAIAEVT DLKVIDRTQL ILDIFARRAH TREGKVQVEL AQLRYLLPRL SGHGTSLSRL GGGIGTRGPG ETKLETDRRR IRDRIAHLER ELERFARHQD QRRARRVRQA LPILSIVGYT NAGKSTLLNA LTHSRVAAQD RLFDTLDTTS RRLRFPEDRE LIVTDTVGFI RDLPKDLVGA FRTTLEELRD ADLLLHVVDA TAQDIDLQIS AVESVLRSLD LEHLPKVLVL NKCDRLSPHE RLVLCQRYRA IGISALQRET LRPLIAHLAS LLPAPSTSQD RLGEHEPNSL KLALASHD // ID A0A136L3F9_9CHLR Unreviewed; 456 AA. AC A0A136L3F9; DT 08-JUN-2016, integrated into UniProtKB/TrEMBL. DT 08-JUN-2016, sequence version 1. DT 07-JUN-2017, entry version 8. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:KXK16173.1}; GN ORFNames=UZ14_CFX002000051 {ECO:0000313|EMBL:KXK16173.1}; OS Chloroflexi bacterium OLB14. OC Bacteria; Chloroflexi. OX NCBI_TaxID=1617415 {ECO:0000313|EMBL:KXK16173.1, ECO:0000313|Proteomes:UP000070321}; RN [1] {ECO:0000313|EMBL:KXK16173.1, ECO:0000313|Proteomes:UP000070321} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=OLB14 {ECO:0000313|EMBL:KXK16173.1}; RA Speth D.R., In T Zandt M., Guerrero Cruz S., Jetten M.S., Dutilh B.E.; RT "Genome based microbial ecology of anammox granules in a full-scale RT wastewater treatment system."; RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KXK16173.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LMZR01000003; KXK16173.1; -; Genomic_DNA. DR PATRIC; fig|1617415.3.peg.54; -. DR Proteomes; UP000070321; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000070321}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000070321}. FT DOMAIN 219 385 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 456 AA; 50728 MW; BEF3CE19CF4469E9 CRC64; MAKKTPQPTT PPRERAFLVG VEIHNQHKHL SLDDSLAELA LLADTAGVDV VGELTQKLSH PHVETYIGPG KVQELLALAE ETLCDVIIFD DELSPRHQRE LEKALGLKIR VIDRTALILD IFAQHAHTKE GMLQVELAQY EYNLPRLTRA WTHLERQAGG GGGRAGSTGG VGLRGPGETQ LEVDRRDIRK RISYIKKELE KVEAHRLRYR AQRKRSRIPT VALVGYTNAG KSTLLNRLSK SDVYAADQLF ATLDPTTRRV QLPADNVALI TDTVGFIQKL PTTLIAAFHA TLEEIAEADL LLHVVDISHP NALGQFEAVQ ETLEEIGAGH IPMITALNKA DRLKDPENAK RVLQSFEKSV AISATKGTGI EDLLHLMQEE LFESYTAIHV RLPYKEGALI SLFHELGQVE RIEHERGGVM MQGRIPGRLL AQFSPFYAKS NGNKIIEIEE SDLEQI // ID A0A136L4V2_9BACT Unreviewed; 409 AA. AC A0A136L4V2; DT 08-JUN-2016, integrated into UniProtKB/TrEMBL. DT 08-JUN-2016, sequence version 1. DT 07-JUN-2017, entry version 8. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=UZ08_BCD001002912 {ECO:0000313|EMBL:KXK16697.1}; OS Bacteroidetes bacterium OLB8. OC Bacteria; Bacteroidetes. OX NCBI_TaxID=1617419 {ECO:0000313|EMBL:KXK16697.1, ECO:0000313|Proteomes:UP000070208}; RN [1] {ECO:0000313|EMBL:KXK16697.1, ECO:0000313|Proteomes:UP000070208} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=OLB8 {ECO:0000313|EMBL:KXK16697.1}; RA Speth D.R., In T Zandt M., Guerrero Cruz S., Jetten M.S., Dutilh B.E.; RT "Improved understanding of the partial-nitritation anammox process RT through 23 genomes representing the majority of the microbial RT community."; RL Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KXK16697.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JZQW01000073; KXK16697.1; -; Genomic_DNA. DR PATRIC; fig|1617419.3.peg.3346; -. DR Proteomes; UP000070208; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000070208}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000070208}. FT DOMAIN 208 390 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 409 AA; 46745 MW; F3142DF0F3539996 CRC64; MAEWNIGQKS SGLVRQKERA VLVGLVYGLQ TEDKLNDYLD ELAFLAETAG AETIKRFTQK LPHPDNRTFV GKGKAEEIRN YIEDHDIDLV IFDDDLTGKQ VNILEAMFKR KIVDRSTLIL DIFAERAQTA QAKTQVELAQ MQYLLPRLRG LWTHLERQQG GIGMRGPGEK EIETDRRIVN EKIKLLKDKL AVIDRQNTTQ RKNRSNTVRV ALVGYTNVGK STLLNALSGA DTFVENKLFA TLDTTVRKVT LNKIPFLLSD TVGFIRKLPH HLVESFKSTL DEARESDFLL HVVDLSHPGM EDQLITVQKT LHDLGAQDIP TLIVGNKIDA YKKNLFDDFL SNAEKKEILA EQLEHFQRNF PQPWIFISAY TGENLAALKS LLADKVKEIY ETKFPHQFHK EYNQNSFKQ // ID A0A136LLI9_9CHLR Unreviewed; 434 AA. AC A0A136LLI9; DT 08-JUN-2016, integrated into UniProtKB/TrEMBL. DT 08-JUN-2016, sequence version 1. DT 07-JUN-2017, entry version 8. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:KXK22530.1}; GN ORFNames=UZ15_CFX003000991 {ECO:0000313|EMBL:KXK22530.1}; OS Chloroflexi bacterium OLB15. OC Bacteria; Chloroflexi. OX NCBI_TaxID=1617416 {ECO:0000313|EMBL:KXK22530.1, ECO:0000313|Proteomes:UP000070332}; RN [1] {ECO:0000313|EMBL:KXK22530.1, ECO:0000313|Proteomes:UP000070332} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=OLB15 {ECO:0000313|EMBL:KXK22530.1}; RA Speth D.R., In T Zandt M., Guerrero Cruz S., Jetten M.S., Dutilh B.E.; RT "Genome based microbial ecology of anammox granules in a full-scale RT wastewater treatment system."; RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KXK22530.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LMZS01000050; KXK22530.1; -; Genomic_DNA. DR PATRIC; fig|1617416.3.peg.1039; -. DR Proteomes; UP000070332; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000070332}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000070332}. FT DOMAIN 212 379 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 171 205 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 434 AA; 48428 MW; C886884C5E1EDBDD CRC64; MPAEHSYELN QRPERAFLVG IGLKRSQPLL TTEESLEELA LLANTAGMEV VGQASQNLNQ IDPATLIGSG KVEEIREALI ANDIQTVIFD DELTPRHQRE LEERFGENIK VLDRSALILD IFAQHASTHE GALQVELAQY EYRLPRLTRQ WTHLSRQAGG SSSVGLRGPG ETQLEVDRRE IRHRISRLKQ ELEKVRGHRS RHRQQRNRTG IPLVALVGYT NAGKSTLLHA LSGADVYIAD QLFATLDPTT RRVDLPNGLQ ILVTDTVGFI QKLPTTLIAA FRATLEEIAE ADIILEVVDI NAQNAPGHIE TVEDTLAEID VPLVPRILVW NKADKYKGES PPELPNSHEY FDVVTISARK NTGLDKLTAA ISRAISSSLY QVKLLLPYER GDLVSQLHEL AVVHQQTAKD SGIELTVRLP ANLFDKFKQY RISG // ID A0A136LSF6_9BACT Unreviewed; 384 AA. AC A0A136LSF6; DT 08-JUN-2016, integrated into UniProtKB/TrEMBL. DT 08-JUN-2016, sequence version 1. DT 07-JUN-2017, entry version 8. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=UZ12_BCD005001967 {ECO:0000313|EMBL:KXK24562.1}; OS Bacteroidetes bacterium OLB12. OC Bacteria; Bacteroidetes. OX NCBI_TaxID=1619897 {ECO:0000313|EMBL:KXK24562.1, ECO:0000313|Proteomes:UP000070129}; RN [1] {ECO:0000313|EMBL:KXK24562.1, ECO:0000313|Proteomes:UP000070129} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=OLB12 {ECO:0000313|EMBL:KXK24562.1}; RA Speth D.R., In T Zandt M., Guerrero Cruz S., Jetten M.S., Dutilh B.E.; RT "Genome based microbial ecology of anammox granules in a full-scale RT wastewater treatment system."; RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KXK24562.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LNFR01000071; KXK24562.1; -; Genomic_DNA. DR PATRIC; fig|1619897.3.peg.2145; -. DR Proteomes; UP000070129; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR002145; CopG. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR Pfam; PF01402; RHH_1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000070129}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000070129}. FT DOMAIN 197 368 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 384 AA; 43830 MW; 7E079A4BB49C1D30 CRC64; MNAVLVALAD KDPEITREHL DELAFLAETA GIATLQRYIQ KLPQPDVRTF VGKGKLAEIK EFVVAKQIDN VIFDDDLSPS QLRNIEKELN TPARDVKCRV YDRSLLILDI FSMRAQTAQS RAQVELAMNQ YLLPRLTRMW THLERQRGGT GTRGGAGERE IETDRRNIRF RISLLKDELE KIDKQRKTQR KSRSNIMRVA LVGYTNVGKS TLMNLLSKSD VKAENKLFAT VDATVRKVVL GDIPFLLSDT VGFIRKLPHH LIESFKSTLD EVREADILLH VVDVAHPYHD NQIEVVKNTL AELGAGHIPT ILVLNKIDLL PNADVNTDDL KGYYRQHGFE HVVFISAEKK ENLSELRRIL FETVRKKHMT IYPNYVTETT QVIS // ID A0A136MH28_9BACT Unreviewed; 438 AA. AC A0A136MH28; DT 08-JUN-2016, integrated into UniProtKB/TrEMBL. DT 08-JUN-2016, sequence version 1. DT 07-JUN-2017, entry version 8. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=UZ06_CHB003001870 {ECO:0000313|EMBL:KXK33143.1}; OS Chlorobi bacterium OLB6. OC Bacteria; Chlorobi. OX NCBI_TaxID=1617413 {ECO:0000313|EMBL:KXK33143.1, ECO:0000313|Proteomes:UP000070423}; RN [1] {ECO:0000313|EMBL:KXK33143.1, ECO:0000313|Proteomes:UP000070423} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=OLB6 {ECO:0000313|EMBL:KXK33143.1}; RA Speth D.R., In T Zandt M., Guerrero Cruz S., Dutilh B.E., Jetten M.S.; RT "Genome based microbial ecology of anammox granules in a full-scale RT wastewater treatment system."; RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KXK33143.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LLZP01000046; KXK33143.1; -; Genomic_DNA. DR PATRIC; fig|1617413.3.peg.1960; -. DR Proteomes; UP000070423; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000070423}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000070423}. FT DOMAIN 204 370 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 438 AA; 48787 MW; FB15EE255EC54297 CRC64; MTAILHDIGN APRERAIIIA VVRKGADPDV VSEHLDELEL LLDTAGADVA LRMYQERDRP DGATCIGKGK LEELRGLIDD ENVQMVVFDD ELSPVQVRNL EKELNVKILD RTGVILDIFA SHARSLESRT QVELAQLEYL MPRLTRMWTH LSKQYGGVGT KGPGETQIET DRRMFRTRIQ RLKEKLAQIN VQRSVQRKGR ENITRCALVG YTNAGKSSLM RALTNADVLV EDRLFATLDT TVRSLDLPSG KRVLLSDTVG FIRKLPPQLV ASFRTTLAEA IESDIIIHVV DAAAGHSADH IMVVNETLKN IGITHHPTIL VFNKIDCITD PYALMDLQAS YPDAVFTSAL TGFNLDALTD AIQRVADTLS VTRTVCIPYS DAAYIAKLYR DSEVLLRTDD ENGTTLQVKL TPEMLATFNQ RYSQYLCDPV ICTTQPTP // ID A0A136MX04_9BACT Unreviewed; 388 AA. AC A0A136MX04; DT 08-JUN-2016, integrated into UniProtKB/TrEMBL. DT 08-JUN-2016, sequence version 1. DT 07-JUN-2017, entry version 8. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:KXK38415.1}; GN ORFNames=UZ16_OP3001000856 {ECO:0000313|EMBL:KXK38415.1}; OS Omnitrophica bacterium OLB16. OC Bacteria; Candidatus Omnitrophica. OX NCBI_TaxID=1617433 {ECO:0000313|EMBL:KXK38415.1, ECO:0000313|Proteomes:UP000070296}; RN [1] {ECO:0000313|EMBL:KXK38415.1, ECO:0000313|Proteomes:UP000070296} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=OLB16 {ECO:0000313|EMBL:KXK38415.1}; RA Speth D.R., In T Zandt M., Guerrero Cruz S., Jetten M.S., Dutilh B.E.; RT "Genome based microbial ecology of anammox granules in a full-scale RT wastewater treatment system."; RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KXK38415.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LMZT01000042; KXK38415.1; -; Genomic_DNA. DR PATRIC; fig|1617433.3.peg.925; -. DR Proteomes; UP000070296; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000070296}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000070296}. FT DOMAIN 212 377 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 388 AA; 43327 MW; 71561D22F443D051 CRC64; MAQIKSPNYH FPDRSGPKEL GTPFKKIVLV QVLPPTISGF ESEDRFEELS RLVETLDGEV VGHIVQRRPN PHREYYVGPG KADQIGSLCD QTEADTVVID GQLTPTQISH LEHETGSHIM DRTELILEIF ARRAQTAEAK LQVELAYLNY FHPRHDQSTQ KRAYRGGVRG FGESALGKKI LATRARADLL RKKIDKMKKQ TESRLRQRSD QWTVALVGYT NAGKSTLLNA LTGESLYADD RLFATLDTTT RRVFLKENRV ALFSDTVGFI RRLPHELIAS FHSTLSEALG ADLLLHVADA SALTLKAQME TVQETLQQLG ADEDRVLIAF NKVDAADPSR IEELKSHYPS AVFISAWTKA GLGDLRNAVF EYLALKARSS QNFAEAGV // ID A0A136N3X9_9BACT Unreviewed; 404 AA. AC A0A136N3X9; DT 08-JUN-2016, integrated into UniProtKB/TrEMBL. DT 08-JUN-2016, sequence version 1. DT 07-JUN-2017, entry version 8. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=UZ09_BCD002000037 {ECO:0000313|EMBL:KXK40874.1}; OS Bacteroidetes bacterium OLB9. OC Bacteria; Bacteroidetes. OX NCBI_TaxID=1617420 {ECO:0000313|EMBL:KXK40874.1, ECO:0000313|Proteomes:UP000070267}; RN [1] {ECO:0000313|EMBL:KXK40874.1, ECO:0000313|Proteomes:UP000070267} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=OLB9 {ECO:0000313|EMBL:KXK40874.1}; RA Speth D.R., In T Zandt M., Guerrero Cruz S., Jetten M.S., Dutilh B.E.; RT "Genome based microbial ecology of anammox granules in a full-scale RT wastewater treatment system."; RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KXK40874.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LNBW01000003; KXK40874.1; -; Genomic_DNA. DR PATRIC; fig|1617420.3.peg.39; -. DR Proteomes; UP000070267; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000070267}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000070267}. FT DOMAIN 211 393 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 404 AA; 46715 MW; 3062FDA3CE998516 CRC64; MSDAWKVGKE KKKGIAVEAE YCVLVGVITK EVSEAQVMEY LDELEFLAST AGAVTRKVFT QKMEHPNVKS FIGPGKLDEI KEFIDRNEDI TLAIFDDDLT GKQTGYLEEY LKVKIVDRST LILDIFAERA QTAQAKTQVE LAQMQYLLPR LRGLWTHLER QRGGIGMRGP GEQEIETDRR IVRDKISVLK KKLEKIDQQT QTQRKNRGEL IRVALVGYTN VGKSTLMNLL SKSEVFAENK LFATLDTTVR KVVWDTMPFL LSDTVGFIRK LPHHLVESFK STLDEVRESD ILVHVVDISH PQHEDHIMTV QHTLHDLGAS DRTTLMVFNK VDLYREKYFD DYLDLGTKLE IMQEIKDKFN NVYNYPNVLI SATQRENIDE LRARLTQMIA HEYTIRYPYQ VKTW // ID A0A136NCK0_9BACT Unreviewed; 396 AA. AC A0A136NCK0; DT 08-JUN-2016, integrated into UniProtKB/TrEMBL. DT 08-JUN-2016, sequence version 1. DT 07-JUN-2017, entry version 8. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=UZ11_BCD004000435 {ECO:0000313|EMBL:KXK43875.1}; OS Bacteroidetes bacterium OLB11. OC Bacteria; Bacteroidetes. OX NCBI_TaxID=1617422 {ECO:0000313|EMBL:KXK43875.1, ECO:0000313|Proteomes:UP000070496}; RN [1] {ECO:0000313|EMBL:KXK43875.1, ECO:0000313|Proteomes:UP000070496} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=OLB11 {ECO:0000313|EMBL:KXK43875.1}; RA Speth D.R., In T Zandt M., Guerrero Cruz S., Jetten M.S., Dutilh B.E.; RT "Genome based microbial ecology of anammox granules in a full-scale RT wastewater treatment system."; RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KXK43875.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LNFQ01000014; KXK43875.1; -; Genomic_DNA. DR PATRIC; fig|1617422.3.peg.479; -. DR Proteomes; UP000070496; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000070496}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000070496}. FT DOMAIN 202 384 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 170 197 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 396 AA; 45793 MW; F92A21F0443271B5 CRC64; MIEKKGTIKE QANAILVGWL PQGKSESYIQ EFLDELSFLA ETAGAKEVKR FYQKLEHPDS RTFLGKGKLE EIKKYIDTHS VDLIIFDDEL SGSQLSNIEA ILKRKIIDRS DLILDIFAIR AKTATAKVQV ELAQYQYILP RLRGMWKHLE RQGGGIGSRG PGETEIETDR RIIKDKISLL KKRLQEYDKQ AQTQRKERGE LIRVALVGYT NVGKSTLMTV LSKSDVFAEN KLFATLDTTT RKVVLERTPF LLSDTVGFIR KLPHHLVESF KSTLDEVREA DILLHVVDIS HPQFEDQIAT VNKTLHEIKA EQKLTILVFN KMDKYEQDAY DEWLADDIKS DLLNQLKNRW ENETHGLCIF ISASQKNNID ELRKILLDKV REMYGIRYPY KTVFYE // ID A0A136NHN6_9BACT Unreviewed; 471 AA. AC A0A136NHN6; DT 08-JUN-2016, integrated into UniProtKB/TrEMBL. DT 08-JUN-2016, sequence version 1. DT 07-JUN-2017, entry version 8. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:KXK45698.1}; GN ORFNames=UZ05_CHB002002440 {ECO:0000313|EMBL:KXK45698.1}; OS Chlorobi bacterium OLB5. OC Bacteria; Chlorobi. OX NCBI_TaxID=1617412 {ECO:0000313|EMBL:KXK45698.1, ECO:0000313|Proteomes:UP000070057}; RN [1] {ECO:0000313|EMBL:KXK45698.1, ECO:0000313|Proteomes:UP000070057} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=OLB5 {ECO:0000313|EMBL:KXK45698.1}; RA Speth D.R., In T Zandt M., Guerrero Cruz S., Dutilh B.E., Jetten M.S.; RT "Genome based microbial ecology of anammox granules in a full-scale RT wastewater treatment system."; RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KXK45698.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LLZO01000285; KXK45698.1; -; Genomic_DNA. DR PATRIC; fig|1617412.3.peg.2557; -. DR Proteomes; UP000070057; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000070057}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000070057}. FT DOMAIN 214 387 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 182 209 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 471 AA; 53214 MW; 27F3D979E93D7E89 CRC64; MSKLHTTHKE EEKAILVCTT IPKSSTAKTV KQRIFKEHLE ELEFLTQTAG AVVVDKVYQE RDNIDSSLFI GKGKAEEIAK KAEEEKIDLV IFENSLSPTQ IRNLEKIIKC KIVDKPALIL DIFATNARTS EAKTQVELAQ LQYMQARLTR QWTHLSKQAG GIGTRGPSGT KGPGETQIET DRRLIAARIA MLKERLKKIE EQRKTQRQQR TGFSRIALVG YTNVGKSTLL NQLTDAGVYV ENKLFATLDT STKLLKEING EKLPQPVLIS DTVGFIRNLP HDLIESFKST LAEVVEADIL LHVVDLSSES FEDQIQVVEE TLKDIGADTK PVIMVFNKVD KLVEENKHEL MFTLKEKYPE SVFISAFKGI NLSSLFDKII EMMHAEIEEL EIKIPSSNPE AYRIINRLHK DADIVSTKYL TKDIKLVVKG NKNQLKKILN GLKLDKEIIK EHKLPVKNTV PGKNNRKELP A // ID A0A136NMR6_9BACT Unreviewed; 400 AA. AC A0A136NMR6; DT 08-JUN-2016, integrated into UniProtKB/TrEMBL. DT 08-JUN-2016, sequence version 1. DT 07-JUN-2017, entry version 8. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=UZ10_BCD003000461 {ECO:0000313|EMBL:KXK47376.1}; OS Bacteroidetes bacterium OLB10. OC Bacteria; Bacteroidetes. OX NCBI_TaxID=1617421 {ECO:0000313|EMBL:KXK47376.1, ECO:0000313|Proteomes:UP000070480}; RN [1] {ECO:0000313|EMBL:KXK47376.1, ECO:0000313|Proteomes:UP000070480} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=OLB10 {ECO:0000313|EMBL:KXK47376.1}; RA Speth D.R., In T Zandt M., Guerrero Cruz S., Jetten M.S., Dutilh B.E.; RT "Genome based microbial ecology of anammox granules in a full-scale RT wastewater treatment system."; RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KXK47376.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LNBX01000015; KXK47376.1; -; Genomic_DNA. DR PATRIC; fig|1617421.3.peg.481; -. DR Proteomes; UP000070480; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000070480}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000070480}. FT DOMAIN 205 389 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 400 AA; 45628 MW; 5D1CE5EECA1AB4EE CRC64; MKEKTKFAPV GKAEESAVLI GVITRNQSEE REKEYLDELA FLAETAGAST VKIFTQNLDY PDPRTFVGSG KLNQIVEFCK ANAVTLAIFD DELTPSQLRN IEKALGIKVL DRTQLILDIF ARRARTAQAQ VQVELAQYQY LLPRLTRMWT HLEKQQGGIG TRGPGETEIE TDRRIVRDKL SKLRQRLKEI DKQNFNQRKS RGNMVRVALV GYTNVGKSTI MNLLSKSDVF AENKLFATLD TTVRKVVLEN IPFLLSDTVG FIRKLPHHLV ESFKSTLDEV READVLVHVV DISHPNFEDH IQVVNQMLAE LNAAEKPTIL VFNKIDAFTY VKKEEDDLTP ATRENLSLED LKKTWMAKGR TKSIFISAAK KENIKELREL LLEEVKQIHL QRYPNQPELG // ID A0A136P6Y4_9CHLR Unreviewed; 439 AA. AC A0A136P6Y4; DT 08-JUN-2016, integrated into UniProtKB/TrEMBL. DT 08-JUN-2016, sequence version 1. DT 07-JUN-2017, entry version 8. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:KXK54151.1}; GN ORFNames=UZ13_00417 {ECO:0000313|EMBL:KXK54151.1}; OS Chloroflexi bacterium OLB13. OC Bacteria; Chloroflexi. OX NCBI_TaxID=1617414 {ECO:0000313|EMBL:KXK54151.1, ECO:0000313|Proteomes:UP000070395}; RN [1] {ECO:0000313|EMBL:KXK54151.1, ECO:0000313|Proteomes:UP000070395} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=OLB13 {ECO:0000313|EMBL:KXK54151.1}; RA Speth D.R., In T Zandt M., Guerrero Cruz S., Jetten M.S., Dutilh B.E.; RT "Improved understanding of the partial-nitritation anammox process RT through 23 genomes representing the majority of the microbial RT community."; RL Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KXK54151.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JZRA01000016; KXK54151.1; -; Genomic_DNA. DR PATRIC; fig|1617414.3.peg.422; -. DR Proteomes; UP000070395; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000070395}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000070395}. FT DOMAIN 217 384 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 439 AA; 48434 MW; 502E8C5DC9D0B3AB CRC64; MPSMHEVVRF EAERAVLVAA MEHRSRPLMS MQDSLAELAL LASTAGIDVV GQTTQVLRQI EPATYIGSGK LEEVRDLLVA ADARVVIFDD ELSPRHQREI EERLRPSVPE VKVIDRSALI LDIFAQHAQT REGSLQVELA QYEYRLPRLT RQWTHLARQG GGKGSAAGVG LRGPGETQLE VDRREMARKI GKLKQELEIV RGHRGRQRSQ RSRSGVPVVA LVGYTNAGKS TLLNALTDAQ AFVADQLFAT LDPTTRKLEL PSGRQAVLTD TVGFIQKLPT TLIAAFRATL EEVAEADLLL HLIDVTHPNA AEHFEAVEDT LAEIDVPPIP RILVYNKADQ WHGTELPFDA QAIGYSSAVL ISAITGRGLD DLREAIDHGL ATASRTLQLR FPYNRGDLVS LAYENATVLA REDKADGVHL TARMPAVFAE QMKEHEVRS // ID A0A136PFU4_9BACT Unreviewed; 442 AA. AC A0A136PFU4; DT 08-JUN-2016, integrated into UniProtKB/TrEMBL. DT 08-JUN-2016, sequence version 1. DT 07-JUN-2017, entry version 8. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:KXK57281.1}; GN ORFNames=UZ07_CHB004000779 {ECO:0000313|EMBL:KXK57281.1}; OS Chlorobi bacterium OLB7. OC Bacteria; Chlorobi. OX NCBI_TaxID=1619898 {ECO:0000313|EMBL:KXK57281.1, ECO:0000313|Proteomes:UP000070627}; RN [1] {ECO:0000313|EMBL:KXK57281.1, ECO:0000313|Proteomes:UP000070627} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=OLB7 {ECO:0000313|EMBL:KXK57281.1}; RA Speth D.R., In T Zandt M., Guerrero Cruz S., Jetten M.S., Dutilh B.E.; RT "Genome based microbial ecology of anammox granules in a full-scale RT wastewater treatment system."; RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KXK57281.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LMYZ01000072; KXK57281.1; -; Genomic_DNA. DR PATRIC; fig|1619898.3.peg.921; -. DR Proteomes; UP000070627; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000070627}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000070627}. FT DOMAIN 205 372 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 173 200 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 442 AA; 49510 MW; 4D25C7772CD6DB9D CRC64; MTEQKLHTIV QNARERALLV GLAQGANSRE QTLEHLNELE LLVDTAGADT VLKVVQGLPR QDGAFFIGKG KAEELAEIVE EEGINLVVVD DDLSPMQARN LERVIKRKIV DRSGLILDIF AGRARSSEAR TQVELAQLQY MLPRLTRQWT HLSKQYGGIG TKGPGETQIE TDRRLIRTRI SLLREKLEKI EQQRETQRKG RSEMFKIALV GYTNAGKSTL MRELSGADVH AEDRLFATLD TTVRQIEVAN DRKALLSDTV GFIRKLPPHL VASFRSTLAE VREADLLLHV VDIASPSLME QISVVESTLA DIDASGIPTI MVFNKVDALP KGSEMLLEMN ERYPDAVMIS AMRGFNIVAL RDKLAERIES SLVERIVRAP IAKWHALARL HDHADVLEKR YDNDFVYLHI RYSPKVLDHV EHYLALAQAA TIQGIPAETE AG // ID A0A136PRA6_9ACTN Unreviewed; 484 AA. AC A0A136PRA6; DT 08-JUN-2016, integrated into UniProtKB/TrEMBL. DT 08-JUN-2016, sequence version 1. DT 07-JUN-2017, entry version 10. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=AWW66_15870 {ECO:0000313|EMBL:KXK60970.1}; OS Micromonospora rosaria. OC Bacteria; Actinobacteria; Micromonosporales; Micromonosporaceae; OC Micromonospora. OX NCBI_TaxID=47874 {ECO:0000313|EMBL:KXK60970.1, ECO:0000313|Proteomes:UP000070620}; RN [1] {ECO:0000313|EMBL:KXK60970.1, ECO:0000313|Proteomes:UP000070620} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 803 {ECO:0000313|EMBL:KXK60970.1, RC ECO:0000313|Proteomes:UP000070620}; RA Yang H., He X., Zhu D.; RT "Whole genome sequence and analysis of Micromonospora rosaria DSM 803, RT which can produce antibacterial substance rosamicin."; RL Submitted (JAN-2016) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KXK60970.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LRQV01000053; KXK60970.1; -; Genomic_DNA. DR RefSeq; WP_067366417.1; NZ_LRQV01000053.1. DR EnsemblBacteria; KXK60970; KXK60970; AWW66_15870. DR Proteomes; UP000070620; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000313|EMBL:KXK60970.1}; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000070620}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900, KW ECO:0000313|EMBL:KXK60970.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000070620}. FT DOMAIN 255 420 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 214 248 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 484 AA; 52960 MW; 39B317E89286BE96 CRC64; MRDQETFVSV EGEELDATTG ELELSERQAL RRVPGLSTEL TDVTEVEYRQ LRLERVVLVG VWTEGTVADA ENSLTELAAL AETAGSQVLE GLIQRRTRPD PATYIGRGKV EDLGAVVRSS GADTVICDGE LSPSQLRNLE QRIKVKVIDR TALILDIFAQ HAKSKEGKAQ VELAQLEYLL PRLRGWGEAL SRQAGGSGGG GGAGGGVGLR GPGETKLETD RRRIRHRIAR LRREIKSMKT VRQTKRARRA RNVVPAVAIA GYTNAGKSSL LNRLTGAGVL VENALFATLD PTTRRATTAD GRQYTLSDTV GFVRHLPHQI VEAFRSTLEE VADADLLVHV VDGAHPDPEE QVRAVREVLV EAGAERLPEL LVVNKVDAAD EETLLRLKRL WPDAVFVSAH TGRGIDELRA VVESRLPTPA VEVRAVLPYD RGDLVARVHQ YGEVLSTEHL PEGTVLHVRV DEGLAAELAP FDEDRTDRVV TAHR // ID A0A136PS58_9ACTN Unreviewed; 483 AA. AC A0A136PS58; DT 08-JUN-2016, integrated into UniProtKB/TrEMBL. DT 08-JUN-2016, sequence version 1. DT 07-JUN-2017, entry version 10. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=AWW66_15090 {ECO:0000313|EMBL:KXK61167.1}; OS Micromonospora rosaria. OC Bacteria; Actinobacteria; Micromonosporales; Micromonosporaceae; OC Micromonospora. OX NCBI_TaxID=47874 {ECO:0000313|EMBL:KXK61167.1, ECO:0000313|Proteomes:UP000070620}; RN [1] {ECO:0000313|EMBL:KXK61167.1, ECO:0000313|Proteomes:UP000070620} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 803 {ECO:0000313|EMBL:KXK61167.1, RC ECO:0000313|Proteomes:UP000070620}; RA Yang H., He X., Zhu D.; RT "Whole genome sequence and analysis of Micromonospora rosaria DSM 803, RT which can produce antibacterial substance rosamicin."; RL Submitted (JAN-2016) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KXK61167.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LRQV01000048; KXK61167.1; -; Genomic_DNA. DR RefSeq; WP_067365974.1; NZ_LRQV01000048.1. DR EnsemblBacteria; KXK61167; KXK61167; AWW66_15090. DR Proteomes; UP000070620; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000313|EMBL:KXK61167.1}; KW Complete proteome {ECO:0000313|Proteomes:UP000070620}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900, KW ECO:0000313|EMBL:KXK61167.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000070620}. FT DOMAIN 264 429 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 483 AA; 51628 MW; F9843B762F3DDE0D CRC64; MTSAAHHPRY SARADALMDD ADVRPGAEDV DGAQLDRDDR AALRRVAGLS TETTDVTEVE YRQVRLERVI LVGVWTAGTV DEAERSLAEL AALAETAGAM VLDGVIQRRD RPDPATYLGS GKARELRDLV RAAGADTVVC DGELSPAQLV RLEQVVDAKV VDRTALILDV FAQHATSREG KAQVALAQMQ YMLPRLRGWG QSLSRQMGGG GGGGGMATRG PGETKIETDR RRIHEKMARL RREIAEMRTG RELKRQERRR SSIPSVAIAG YTNAGKSSLL NRLTGAGVLV QNALFATLDP TVRRATTPAG RAYTITDTVG FVRHLPHHLV EAFRSTLEEV AEADLLLHVV DGSHPAPLEQ LAAVRAVIRD VDAGDVPELV VVNKADAATP AALAALAEAE PRHVVVSART GQGIDTLREA VGAALPHPEV QVDVLIPYTA GGLVARIHAD GEVLAEEHTA DGTVLRARVA ADLAADLDGY ART // ID A0A136Q3V7_9FIRM Unreviewed; 595 AA. AC A0A136Q3V7; DT 08-JUN-2016, integrated into UniProtKB/TrEMBL. DT 08-JUN-2016, sequence version 1. DT 07-JUN-2017, entry version 9. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=HMPREF3293_01907 {ECO:0000313|EMBL:KXK65317.1}; OS Christensenella minuta. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Christensenellaceae; OC Christensenella. OX NCBI_TaxID=626937 {ECO:0000313|EMBL:KXK65317.1, ECO:0000313|Proteomes:UP000070366}; RN [1] {ECO:0000313|EMBL:KXK65317.1, ECO:0000313|Proteomes:UP000070366} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 22607 {ECO:0000313|EMBL:KXK65317.1, RC ECO:0000313|Proteomes:UP000070366}; RA Wen L., He K., Yang H.; RL Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KXK65317.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LSZW01000062; KXK65317.1; -; Genomic_DNA. DR EnsemblBacteria; KXK65317; KXK65317; HMPREF3293_01907. DR PATRIC; fig|626937.4.peg.1885; -. DR Proteomes; UP000070366; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000070366}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000070366}. FT DOMAIN 385 545 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 351 381 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 595 AA; 65033 MW; 150CB3C2DD8421C4 CRC64; MPRCGQKAFV SGIINNMNEI HGNTAGLRSR TVEELKGLYE FKLSPQEFAS EDMLFEMARL TEVTGKEISV FLSRGGRVLD VSVGTDKSVK LPYMRVRRGS AGVSGIRAIH THPGGSPMLS NVDIGSLISS RFDAMAAVSV KDGKAAAMCV GFIGETLDQA KVTGPFRPGR IPQQALMYEI AAATERTQNL VRMHETEDAP ERAVLVGLNA LQQSMEELAR LAETAGAEVV GSVTQNRDRD RAYYIGKGKA QELSLQMSAL DADIAIMNDE LSPLETRNLE ETLGVKVVDR TMLILDIFAA HARTREGRLQ VELAQLQYTL PRLAGEGVSL SRLGGGIGTR GPGEKKIEID RRRIRRRIFE LQQEIDKVAE QRELRRTARR ENDVKEVALV GYTNAGKSSL LNALTNAGVR AEDKLFATLD PVTRRVVLPD VGETVFTDTV GFIEKLPHDL VSAFRSTLEE VTRADLLLLV TDASSPNAEG QMEVVRELLS SLHANETPKI LVMNKADRLA QVPAAGQDTV YISAKTGEGL RTLLSLVAEK LAPQLMTYCG TLGYDRGDLL ALVNRDGKDV AMDYRPDGVH VEATLPVETI KKLKS // ID A0A136WDH0_9FIRM Unreviewed; 425 AA. AC A0A136WDH0; DT 08-JUN-2016, integrated into UniProtKB/TrEMBL. DT 08-JUN-2016, sequence version 1. DT 07-JUN-2017, entry version 10. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:KXL52536.1}; GN ORFNames=CLNEO_19450 {ECO:0000313|EMBL:KXL52536.1}; OS [Clostridium] neopropionicum. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Lachnospiraceae; OC Tyzzerella. OX NCBI_TaxID=36847 {ECO:0000313|EMBL:KXL52536.1, ECO:0000313|Proteomes:UP000070539}; RN [1] {ECO:0000313|EMBL:KXL52536.1, ECO:0000313|Proteomes:UP000070539} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM-3847 {ECO:0000313|EMBL:KXL52536.1, RC ECO:0000313|Proteomes:UP000070539}; RA Poehlein A., Beck M.H., Bengelsdorf F.R., Daniel R., Duerre P.; RT "Genome sequence of Clostridium neopropionicum X4, DSM-3847."; RL Submitted (JAN-2016) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KXL52536.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LRVM01000006; KXL52536.1; -; Genomic_DNA. DR RefSeq; WP_066088129.1; NZ_LRVM01000006.1. DR EnsemblBacteria; KXL52536; KXL52536; CLNEO_19450. DR PATRIC; fig|36847.3.peg.2289; -. DR Proteomes; UP000070539; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000070539}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000070539}. FT DOMAIN 208 372 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 425 AA; 47087 MW; 11E39A87F3896C90 CRC64; MARDLHDTAD LEERVILFAV EPEERNSRSA METDACLDEL EELVRTAGAV AVARCVQKRE RVHPGHYFGK GKIEELKMML EAYDASGVVC DDELSPAQLK NLGKMLETKV MDRTIVILDI FAGRAISGEG KIQVELAQLK YRLSRLTGMG ASMSRLGGGI GTRGPGEKKL ETDRRYIKDR IAELNSAAKE IQTHRQLLRS QRGKKGTPVV SLVGYTNAGK STLINKLTDA GVLAEDKLFA TLDTTTRKVA LPNGSEILLT DTVGFIQKLP HHLVQAFRAT LEELKYADIL LHVVDASNPN RQEQMQVVYK TLDDLGCADT PVITIFNKMD RDVELPLPLD TQAREIAQIS AFTGDGLEGM LKTVENLLKS FRSSLVALVP YTEGGLMGWV HGRCEIIREE HTPEGVLLEV YVDAESANRL NKYKQ // ID A0A137SX39_9FIRM Unreviewed; 397 AA. AC A0A137SX39; DT 08-JUN-2016, integrated into UniProtKB/TrEMBL. DT 08-JUN-2016, sequence version 1. DT 07-JUN-2017, entry version 9. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=HMPREF3189_00265 {ECO:0000313|EMBL:KXO17028.1}; OS Clostridiales bacterium KA00134. OC Bacteria; Firmicutes; Clostridia; Clostridiales. OX NCBI_TaxID=1588750 {ECO:0000313|EMBL:KXO17028.1, ECO:0000313|Proteomes:UP000070500}; RN [1] {ECO:0000313|EMBL:KXO17028.1, ECO:0000313|Proteomes:UP000070500} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=KA00134 {ECO:0000313|EMBL:KXO17028.1, RC ECO:0000313|Proteomes:UP000070500}; RA Wen L., He K., Yang H.; RL Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KXO17028.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LTAF01000003; KXO17028.1; -; Genomic_DNA. DR EnsemblBacteria; KXO17028; KXO17028; HMPREF3189_00265. DR PATRIC; fig|1588750.3.peg.267; -. DR Proteomes; UP000070500; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000070500}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000070500}. FT DOMAIN 171 338 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 130 164 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 397 AA; 44809 MW; 5D23CE628E1D8D13 CRC64; MKELSELVYA AGGQVEIEVV QNMERYNPKY LIGPGKAEEI KEVCESNEID TVVFNDELSG IQLRNLSDLI KKKVVDRTNL ILDIFALRAS TYEAKLQVKM AALEYELPRL LGIKGWSRTG GGIGTRGPGE QIIETDRRRL KREIDSIRQK LEKAKQTRKT IGRERRDSNL PIVSLVGYTN AGKSTILNNL KDKQSKEVFV KDMLFATLDP SSRQATLPNK TSIIVSDTVG FVSKLPTKLI EAFKSTLEEI QYSDLILHVI DLAGEDMMLE YKTTMDILKD VGIKDKKILT VYNKKDLVDI ENVVLPSSDG DKIFISAFDE KDIRRLQDEI TRLLDLDLKK YSISLPYNSL GLLEKIKTKY CVEEIEYDEN GAKFKAIISS RTLDDIKKAG GLCIEAC // ID A0A138AQ65_9ACTN Unreviewed; 472 AA. AC A0A138AQ65; DT 08-JUN-2016, integrated into UniProtKB/TrEMBL. DT 08-JUN-2016, sequence version 1. DT 07-JUN-2017, entry version 12. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=AXK60_04795 {ECO:0000313|EMBL:KXP12539.1}; OS Tsukamurella pseudospumae. OC Bacteria; Actinobacteria; Corynebacteriales; Tsukamurellaceae; OC Tsukamurella. OX NCBI_TaxID=239498 {ECO:0000313|EMBL:KXP12539.1, ECO:0000313|Proteomes:UP000070258}; RN [1] {ECO:0000313|EMBL:KXP12539.1, ECO:0000313|Proteomes:UP000070258} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=JCM 15929 {ECO:0000313|EMBL:KXP12539.1, RC ECO:0000313|Proteomes:UP000070258}; RA Wen L., He K., Yang H.; RL Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KXP12539.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LSRF01000012; KXP12539.1; -; Genomic_DNA. DR RefSeq; WP_068570520.1; NZ_LSRF01000012.1. DR EnsemblBacteria; KXP12539; KXP12539; AXK60_04795. DR Proteomes; UP000070258; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000313|EMBL:KXP12539.1}; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000070258}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900, KW ECO:0000313|EMBL:KXP12539.1}. FT DOMAIN 250 419 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 209 243 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 472 AA; 50898 MW; 16677D8119E63BF5 CRC64; MTQTDTWEPT DAQQPTVGEL QLQERSSLRR VVGLSTELDD VTEVEYRQLR LEQVVLVGVW TEGSAAEADS SLAELKALAE TAGSVVLDGV VQRRDRPDPA TYIGSGKAHE LREVVLATGA DTVICDGELT PAQLNALEKV VKVKVIDRTA LILDIFAQHA TSREGKAQVS LAQMEYMLPR LRGWGEALSR QAGGRAGSNG GVGLRGPGET KIETDRRRIR ERMAKLRREI KGMKQARDTK RGQRRRSGVP SVAIAGYTNA GKSSLLNALT DAGVLVQNAL FATLDPTTRQ STLADGRDVV FTDTVGFVRH LPTQLVEAFR STLEEVVDAD LLLHVVDGSD PMPQRQIDAV RHVLREVAGE REATLPRELL VVNKIDAADP MVLAQLRVAL PGAVFVSAHT REGIAELLDA LTGLITAGDV EVAALLPYER GDLVARIHAE GTVVSADHEA DGTRIVARVP GALAGLLARF AQ // ID A0A139B825_9BIFI Unreviewed; 496 AA. AC A0A139B825; DT 08-JUN-2016, integrated into UniProtKB/TrEMBL. DT 08-JUN-2016, sequence version 1. DT 07-JUN-2017, entry version 8. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=AYW84_02110 {ECO:0000313|EMBL:KXS25144.1}; OS Bifidobacterium pseudocatenulatum. OC Bacteria; Actinobacteria; Bifidobacteriales; Bifidobacteriaceae; OC Bifidobacterium. OX NCBI_TaxID=28026 {ECO:0000313|EMBL:KXS25144.1, ECO:0000313|Proteomes:UP000070632}; RN [1] {ECO:0000313|Proteomes:UP000070632} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Oh S.; RT "Bifidobacterium_breve_1k.141.3."; RL Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KXS25144.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LSUM01000004; KXS25144.1; -; Genomic_DNA. DR EnsemblBacteria; KXS25144; KXS25144; AYW84_02110. DR Proteomes; UP000070632; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000070632}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000070632}. FT DOMAIN 276 442 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 496 AA; 54509 MW; E6D657E1B6036116 CRC64; MSQENDIEHS MSANDVSGVL ADQSEVLLDT NGENHFNESH DEQWQERESR NALKHVSGLG EMQDVTEVEY RKVRLERVVL VGVWSSRETT QAQAEESLRE LAALAETAGA VVCDGLLQHR IKPDAATYVG SGKARELAGI VAQEEADTIV VDDDLPPSQR RALEDATKVK VVDRTAVILD IFAQHATSRE GKAQVELAQL QYMLPRLRGW GGSLSRQAGG RAAGDAGIGS RGPGETKIEM DRRVIRSRIA KLRKQIEQMA PARDVKRGAR RRFGLPTVAV VGYTNAGKSS LTNRLTGSAE LVENALFATL DTAVRRARAK DGRQYAYVDT VGFVRRLPTQ LIEAFKSTLE EVSEADLIVH VVDGSHPDPF SQIDAVDDVL SDIDGVETIP TIIVFNKADR MDEATRERIE VLMPEAYIVS AFSGEGVDEL RMQVESMLPT PNVHVEALLP YTAGSLVSRV REYGKVINVE YRDDGMMLEA EVDDHLAAQI VEQSIG // ID A0A139BW56_9PROT Unreviewed; 382 AA. AC A0A139BW56; DT 08-JUN-2016, integrated into UniProtKB/TrEMBL. DT 08-JUN-2016, sequence version 1. DT 30-AUG-2017, entry version 10. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=AWT59_0654 {ECO:0000313|EMBL:KXS33221.1}; OS Candidatus Gallionella acididurans. OC Bacteria; Proteobacteria; Betaproteobacteria; Nitrosomonadales; OC Gallionellaceae; Gallionella. OX NCBI_TaxID=1796491 {ECO:0000313|EMBL:KXS33221.1, ECO:0000313|Proteomes:UP000070578}; RN [1] {ECO:0000313|EMBL:KXS33221.1, ECO:0000313|Proteomes:UP000070578} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ShG14-8 {ECO:0000313|EMBL:KXS33221.1}; RA Wen L., He K., Yang H.; RL Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:KXS33221.1, ECO:0000313|Proteomes:UP000070578} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ShG14-8 {ECO:0000313|EMBL:KXS33221.1}; RA Kadnikov V., Ivasenko D., Beletsky A., Mardanov A., Danilova E., RA Pimenov N., Karnachuk O., Ravin N.; RT "New uncultured bacterium of the family Gallionellaceae from acid mine RT drainage: description and reconstruction of genome based on RT metagenomic analysis of microbial community."; RL Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KXS33221.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LSLI01000009; KXS33221.1; -; Genomic_DNA. DR PATRIC; fig|1796491.3.peg.713; -. DR Proteomes; UP000070578; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000070578}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000070578}. FT DOMAIN 198 364 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 382 AA; 42429 MW; 35B1120C18D0E3EB CRC64; MQQSSAGPEA AVLVSIDFGN SDHSESLQEL RLLAETAGVR VLAIVEARRQ RPDAALFAGS GKVQEIAELV ERLEAPLVIF NHDLSPAQMR NLTAKLNTRV IDRTMLILDI FAQRAQSHEG KVQVEIAQLK YLATRLVGMN QDMGQQKHAV GARGPGETRL ELDRRKLDKR VHLLKERLEQ LTRQREVRRR ARNRHDVLSA SIVGYTNAGK STLFNRLTRA NVYVADQLFA TLDTTSRRMF TEDSGEIVLS DTVGFIRHLP HSLVAAFRST LEETIQADLL LHVVDSSNPN HDDQIAEVNK VLAEIDAAEI PQVMVFNKID MGDVPAGVER DEYGRICRVF LSAQSGAGME GLRLALTEAK TARQAAAAKE NQTNQASDEL WD // ID A0A139CBW3_9GAMM Unreviewed; 442 AA. AC A0A139CBW3; DT 08-JUN-2016, integrated into UniProtKB/TrEMBL. DT 08-JUN-2016, sequence version 1. DT 07-JUN-2017, entry version 8. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=AWU55_1282 {ECO:0000313|EMBL:KXS38691.1}; OS Halomonadaceae bacterium T82-2. OC Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales; OC Halomonadaceae. OX NCBI_TaxID=1783518 {ECO:0000313|EMBL:KXS38691.1, ECO:0000313|Proteomes:UP000070062}; RN [1] {ECO:0000313|EMBL:KXS38691.1, ECO:0000313|Proteomes:UP000070062} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=T82-2 {ECO:0000313|EMBL:KXS38691.1}; RA Wolfe R., Daly R., Wrighton K.; RT "Halomonadaceaea-1 T82 Annotated Genome."; RL Submitted (JAN-2016) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KXS38691.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LSBP01000007; KXS38691.1; -; Genomic_DNA. DR PATRIC; fig|1783518.3.peg.2656; -. DR Proteomes; UP000070062; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000070062}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000070062}. FT DOMAIN 199 365 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 442 AA; 49707 MW; 806CA3E138ED3253 CRC64; MFFERPDAGE TAVLVHIDFQ DEQEREDPGE FLELVRSAGA EPATLMQGSR RRPDPRTFIG SGKVEELREL LAIHHAELVI FNHGLSPSQE RNLERALKCR VLDRTGLILD IFAQRARTHE GKLQVELAQL EYMSTRLVRG WTHLERQKGG IGLRGPGETQ LETDRRLLRG RIKAIHKRLD KVRSQREQNR RARARAEIPS ISLVGYTNAG KSTLFNALTA SEVYAADQLF ATLDPTLRRL EIPDVGPVVM ADTVGFIRHL PHKLVEAFQA TLQEAAEATL LVHVIDCADP DREQNVAEVN KVLAEIGADT VPCLRVMNKV DLFDSAPRIE RDGHGVPEEV WLSARDGRGL ELFAQALSER LAEDLLELDL TLAPEQGRLR AGLHALDAVR DERFDEQGHT LLSIRLPRRE FLQLLARQGE NAEDYLPPEE LAPPAWADGI RD // ID A0A139CV15_9EURY Unreviewed; 417 AA. AC A0A139CV15; DT 11-MAY-2016, integrated into UniProtKB/TrEMBL. DT 11-MAY-2016, sequence version 1. DT 07-JUN-2017, entry version 9. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=AWU59_107 {ECO:0000313|EMBL:KXS45033.1}; OS Methanolobus sp. T82-4. OC Archaea; Euryarchaeota; Methanomicrobia; Methanosarcinales; OC Methanosarcinaceae; Methanolobus. OX NCBI_TaxID=1794908 {ECO:0000313|EMBL:KXS45033.1, ECO:0000313|Proteomes:UP000074030}; RN [1] {ECO:0000313|EMBL:KXS45033.1, ECO:0000313|Proteomes:UP000074030} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=T82-4 {ECO:0000313|EMBL:KXS45033.1}; RA Wolfe R., Daly R., Wrighton K.; RT "Methanolobus T82 Annotated."; RL Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KXS45033.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LSRV01000002; KXS45033.1; -; Genomic_DNA. DR PATRIC; fig|1794908.3.peg.470; -. DR Proteomes; UP000074030; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000074030}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000074030}. FT DOMAIN 191 360 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 417 AA; 47521 MW; 7DDC14D60229FADC CRC64; MKRAILVKRN DPRSEDDDNE LRLRELEELA GSAGYTVVSE LTQTRHPDPK YQVGSGKVEE LAQLVQDVEA DKIIFYNQLS TMQVYNISEI CRCEVIDKFQ LILEIFASRA TTHRSKLQVE LARLEYELPK ARAIVSILKK EERPGFMGLG GYEDSYAQDV KNRIARIKDE LRDVDRDRDS LRTFRHSKGF SLVALAGYTN AGKSTLFNML VDESKTVRNM LFTTLVPTTR SLTVQGREVL LTDTVGFIED LPHWMVDAFR STLNEIFFAD IVLLVVDCSE PVETIHRKLS VSHETMWEQL QEVEIITVFN KADLLTEEEL DDRMLSLGYL APNPVAVSAK TGFGIDALKQ EIRRHLPEWD RVQLSLPLSE EGMSTLSWLF DEGVVHNVDY DDSINIDLEA RESIISKAKS FTGKKVN // ID A0A139D276_9ALTE Unreviewed; 379 AA. AC A0A139D276; DT 11-MAY-2016, integrated into UniProtKB/TrEMBL. DT 11-MAY-2016, sequence version 1. DT 07-JUN-2017, entry version 7. DE SubName: Full=GTP-binding protein hflX {ECO:0000313|EMBL:KXS47623.1}; DE Flags: Fragment; GN ORFNames=AWU57_5457 {ECO:0000313|EMBL:KXS47623.1}; OS Marinobacter sp. T13-3. OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales; OC Alteromonadaceae; Marinobacter. OX NCBI_TaxID=1794906 {ECO:0000313|EMBL:KXS47623.1, ECO:0000313|Proteomes:UP000073748}; RN [1] {ECO:0000313|EMBL:KXS47623.1, ECO:0000313|Proteomes:UP000073748} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=T13-3 {ECO:0000313|EMBL:KXS47623.1}; RA Wolfe R., Daly R., Wrighton K.; RT "Marinobacter-3 T13 Annotated."; RL Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KXS47623.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LSRT01001098; KXS47623.1; -; Genomic_DNA. DR PATRIC; fig|1794906.3.peg.2237; -. DR Proteomes; UP000073748; Unassembled WGS sequence. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000073748}; KW Reference proteome {ECO:0000313|Proteomes:UP000073748}. FT DOMAIN 198 365 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT NON_TER 379 379 {ECO:0000313|EMBL:KXS47623.1}. SQ SEQUENCE 379 AA; 42611 MW; DDC0881BB24FB7A6 CRC64; MFERPDVGER AVLVHIDFTA HEDTEDPGEF RELVTSAGVE PVVSVTGSRK QPSPRLFVGK GKLEEIRDAV AANEADIVLF NHALSPSQER NIERELKCRV LDRTGVILDI FAQRARTHEG KLQVELAQLE HMSTRLVRGW THLERQKGGI GLRGPGETQL ETDRRLLRER IKSIHKRLEK VRKQRNQGRR ARKRADIPTV SLVGYTNAGK STLFNHITTS TVYAANQLFA TLAPTLRRLD LPDVGPVVMA DTVGFIRHLP HKLVEAFRAT LEETTQASLL LHVIDCYDGR RDENIEQVEN VLAEIGADEI PVLQVFNKID LLDDFEPRID RNEDGVPVRV WVSAVSGQGL ELLFDAIVER LAEDVVHHFV VLGPTDGKL // ID A0A139D7Y0_9FIRM Unreviewed; 409 AA. AC A0A139D7Y0; DT 08-JUN-2016, integrated into UniProtKB/TrEMBL. DT 08-JUN-2016, sequence version 1. DT 07-JUN-2017, entry version 8. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=AWL62_899 {ECO:0000313|EMBL:KXS49627.1}; OS Halanaerobium sp. T82-1. OC Bacteria; Firmicutes; Clostridia; Halanaerobiales; Halanaerobiaceae; OC Halanaerobium. OX NCBI_TaxID=1794808 {ECO:0000313|EMBL:KXS49627.1, ECO:0000313|Proteomes:UP000070487}; RN [1] {ECO:0000313|EMBL:KXS49627.1, ECO:0000313|Proteomes:UP000070487} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=T82-1 {ECO:0000313|EMBL:KXS49627.1}; RA Wolfe R., Daly R., Wrighton K.; RT "Halanaerobium-1 T82 Annotated."; RL Submitted (JAN-2016) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KXS49627.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LSBN01000028; KXS49627.1; -; Genomic_DNA. DR PATRIC; fig|1794808.3.peg.647; -. DR Proteomes; UP000070487; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000070487}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}. FT DOMAIN 189 354 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 409 AA; 46691 MW; C70BD33D4C6A8A97 CRC64; MYQIQEMQEK AVLVGLNEGE LKELQLLIET AGAKTILKMT YHDRKIDPAY YIGSGKVKEI KEAAETVAAN LIVFDNELSP VQQRNLEDKI EIKVIDRAQV ILDIFARHAH SRESKIQVEL AQLEYRLPRL QGRGIEMSRL AGGIGTRGPG ETKLEVDRRR IEKKIYRLKE NLKEIKASRE VQRSSRQDPI AALVGYTNAG KSTLMNKLTG AGSHTADKLF ATLDSTMRQL QLPVGQNIIL SDTVGFINKL PHQLIASFRT TLEEVENADI ILHLIDASNS EMEKNMRIVN KEINELVDPS CKIIKVFNKI DLVEQSKLND LKIIYPDSLF ISALKEINID TVINKLNKII SNEMIEMEID LPYSEAKWVE KIHNTAKVYE EKYQKNNIYL KVLIPKKTAL KLKKYRRES // ID A0A139DHN4_9ALTE Unreviewed; 379 AA. AC A0A139DHN4; DT 11-MAY-2016, integrated into UniProtKB/TrEMBL. DT 11-MAY-2016, sequence version 1. DT 07-JUN-2017, entry version 7. DE SubName: Full=GTP-binding protein HflX {ECO:0000313|EMBL:KXS52831.1}; DE Flags: Fragment; GN ORFNames=AWU57_2779 {ECO:0000313|EMBL:KXS52831.1}; OS Marinobacter sp. T13-3. OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales; OC Alteromonadaceae; Marinobacter. OX NCBI_TaxID=1794906 {ECO:0000313|EMBL:KXS52831.1, ECO:0000313|Proteomes:UP000073748}; RN [1] {ECO:0000313|EMBL:KXS52831.1, ECO:0000313|Proteomes:UP000073748} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=T13-3 {ECO:0000313|EMBL:KXS52831.1}; RA Wolfe R., Daly R., Wrighton K.; RT "Marinobacter-3 T13 Annotated."; RL Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KXS52831.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LSRT01000221; KXS52831.1; -; Genomic_DNA. DR PATRIC; fig|1794906.3.peg.2927; -. DR Proteomes; UP000073748; Unassembled WGS sequence. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000073748}; KW Reference proteome {ECO:0000313|Proteomes:UP000073748}. FT DOMAIN 198 365 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT NON_TER 379 379 {ECO:0000313|EMBL:KXS52831.1}. SQ SEQUENCE 379 AA; 42600 MW; 061126935F65C7CE CRC64; MFERPDVGER AVLVHIDFTA HEGTEDPGEF RELVTSAGVE PVATVTGSRK QPSPRLFVGK GKLEEIRDAV AANEADIVLF NHALSPSQER NIERELKCRV LDRTGVILDI FAQRARTHEG KLQVELAQLD HMSTRLVRGW THLERQKGGI GLRGPGETQL ETDRRLLRER IKSIHKRLEK VRKQRNQGRR ARKRADIPTV SLVGYTNAGK STLFNHITTS TVYAANQLFA TLDPTLRRLD LPDVGPVVMA DTVGFIRHLP HKLVEAFRAT LEETTQASLL LHVIDCYDSR RDENIEQVES VLAEIGADEI PVLQVFNKID LLEDFEPRID RNEDGIPVRV WVSAVSGQGL ELLFDAIVER LAEDVVHHFV VLGPTDGKL // ID A0A139NC39_9STRE Unreviewed; 412 AA. AC A0A139NC39; DT 11-MAY-2016, integrated into UniProtKB/TrEMBL. DT 11-MAY-2016, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=STRDD10_01444 {ECO:0000313|EMBL:KXT73638.1}; OS Streptococcus sp. DD10. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=1777878 {ECO:0000313|EMBL:KXT73638.1, ECO:0000313|Proteomes:UP000072050}; RN [1] {ECO:0000313|EMBL:KXT73638.1, ECO:0000313|Proteomes:UP000072050} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DD10 {ECO:0000313|EMBL:KXT73638.1, RC ECO:0000313|Proteomes:UP000072050}; RA Denapaite D., Rieger M., Koendgen S., Brueckner R., Ochigava I., RA Kappeler P., Maetz-Rensing K., Leendertz F., Hakenbeck R.; RT "Highly variable Streptococcus oralis are common among viridans RT streptococci isolated from primates."; RL Submitted (JAN-2016) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KXT73638.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LQRE01000110; KXT73638.1; -; Genomic_DNA. DR RefSeq; WP_067194323.1; NZ_KQ969161.1. DR EnsemblBacteria; KXT73638; KXT73638; STRDD10_01444. DR PATRIC; fig|1777878.3.peg.1580; -. DR Proteomes; UP000072050; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000072050}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000072050}. FT DOMAIN 199 359 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 158 192 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 412 AA; 47029 MW; C2297E7419D50CB6 CRC64; MIDTQKKQER VLLVGVELQG MEHFSMSMEE LASLAKTAGA EVVGCYRQKR EKYDSKTFVG SGKLQEIADM VDADEISTVV VNNRLTPRQN VNLEEILGIK VIDRMQLILD IFAMRARSHE GKLQVHLAQL NYLLPRLVGQ GIMLSRQAGG IGSRGPGESQ LELNRRAVRN QINEIERQLK IVEKNRETVR EKRMDSPVFK IGLIGYTNAG KSTIMNRLSS KRQYEADELF ATLDATTNSI HLEGKLQVTL TDTVGFIQDL PTELVSSFKS TLEESKHVDL LVHVIDASDP NHEEHEKTVL SIMKDLDMLE IPRLTLYNKS DKISDFTPTQ TPYTLVAAKG EKSREVLQTA IVEKIKELFV PFSIRLPFEK SYRLHDLENV AFIEDIDYEE QYQLIKGYIA PKNKWRLEEF YD // ID A0A139NKH9_9STRE Unreviewed; 415 AA. AC A0A139NKH9; DT 08-JUN-2016, integrated into UniProtKB/TrEMBL. DT 08-JUN-2016, sequence version 1. DT 07-JUN-2017, entry version 10. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=STRDD12_00641 {ECO:0000313|EMBL:KXT76304.1}; OS Streptococcus sp. DD12. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=1777880 {ECO:0000313|EMBL:KXT76304.1, ECO:0000313|Proteomes:UP000070638}; RN [1] {ECO:0000313|EMBL:KXT76304.1, ECO:0000313|Proteomes:UP000070638} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DD12 {ECO:0000313|EMBL:KXT76304.1, RC ECO:0000313|Proteomes:UP000070638}; RA Denapaite D., Rieger M., Koendgen S., Brueckner R., Ochigava I., RA Kappeler P., Maetz-Rensing K., Leendertz F., Hakenbeck R.; RT "Highly variable Streptococcus oralis are common among viridans RT streptococci isolated from primates."; RL Submitted (JAN-2016) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KXT76304.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LQRG01000008; KXT76304.1; -; Genomic_DNA. DR RefSeq; WP_066915092.1; NZ_KQ969495.1. DR EnsemblBacteria; KXT76304; KXT76304; STRDD12_00641. DR PATRIC; fig|1777880.3.peg.663; -. DR Proteomes; UP000070638; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000070638}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000070638}. FT DOMAIN 199 359 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 165 192 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 415 AA; 47364 MW; 753E9CFF168197E7 CRC64; MFETKLSPER VLLVHVVLPE SQRWEMSLAE LERLAQTAGG QVVGSVIQRK NVIDAKSFVG SGKLDQLRQE VEDNAIDTVI VNNRLSPRQN MVLEEALDCK VIDRMQLILD IFAMRARSYE GKLQVHLAQL KYLLPRLVGK GIMLSRQAGG IGSRGPGESQ LELNRRSIRH QITDIERQLK VVEKQRQQGR EQRQQSSVFK IGLIGYTNAG KSTMMNCLTQ DDQYEADELF ATLDATTKKI HIQGAFEATL TDTVGFIQDL PTELIAAFKS TLEESRDCDL LLHVVDASDP DFREQEVVVE QLLDEVDMGT IPRLTIYNKL DKVSLFAPDR FPHATLSCKA KDSHKQIKTI LVRELKHLFS PFQITCPVEE VYRLYELSRW AILDQDELGN FSETITGYIA DKNKWRLERF YDRLS // ID A0A139NTE6_9STRE Unreviewed; 416 AA. AC A0A139NTE6; DT 08-JUN-2016, integrated into UniProtKB/TrEMBL. DT 08-JUN-2016, sequence version 1. DT 07-JUN-2017, entry version 10. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=STRDD13_00143 {ECO:0000313|EMBL:KXT79123.1}; OS Streptococcus sp. DD13. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=1777881 {ECO:0000313|EMBL:KXT79123.1, ECO:0000313|Proteomes:UP000070387}; RN [1] {ECO:0000313|EMBL:KXT79123.1, ECO:0000313|Proteomes:UP000070387} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DD13 {ECO:0000313|EMBL:KXT79123.1, RC ECO:0000313|Proteomes:UP000070387}; RA Denapaite D., Rieger M., Koendgen S., Brueckner R., Ochigava I., RA Kappeler P., Maetz-Rensing K., Leendertz F., Hakenbeck R.; RT "Highly variable Streptococcus oralis are common among viridans RT streptococci isolated from primates."; RL Submitted (JAN-2016) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KXT79123.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LQRH01000008; KXT79123.1; -; Genomic_DNA. DR RefSeq; WP_067100536.1; NZ_KQ969506.1. DR EnsemblBacteria; KXT79123; KXT79123; STRDD13_00143. DR PATRIC; fig|1777881.3.peg.150; -. DR Proteomes; UP000070387; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000070387}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000070387}. FT DOMAIN 199 360 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 165 192 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 416 AA; 47126 MW; D2B66C1BFED04A93 CRC64; MIENKQEVER VLLVGVELQQ DKQMDMSMGE LARLAETAGA EVKGVYLQKR EKYDSKTFVG SGKLEEIARM VEAEDIQTVI VNNRLTPRQN ANLEEGLGVK VIDRMQLILD IFALRARSHE GKLQVHLAQL KYMLPRLVGQ GIMLSRQAGG IGSRGPGESQ LELNRRSIRH QIHDIERQLK EVEKNRTIVR ERRLDSGLFK IGLIGYTNAG KSTIMNALTE TGQYEADELF ATLDATTKLV HLGGRFQVTI TDTVGFIQDL PTELISAFKS TLEESMHVDL LLHVVDASDP YHVEEEQVVS SIIDQLDMGG IPRLVLYNKA DLVGEDFLPT QFPNVMLSAK APQAKQDLQK LLTAQLKTMF EPFELELPYT RGHLLHEIEK FALVTKSELG DESQWIQGYI PPKNKWRVEE YDERNH // ID A0A139P6W6_9STRE Unreviewed; 412 AA. AC A0A139P6W6; DT 08-JUN-2016, integrated into UniProtKB/TrEMBL. DT 08-JUN-2016, sequence version 1. DT 07-JUN-2017, entry version 8. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=STRDD11_01126 {ECO:0000313|EMBL:KXT84080.1}; OS Streptococcus sp. DD11. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=1777879 {ECO:0000313|EMBL:KXT84080.1, ECO:0000313|Proteomes:UP000070514}; RN [1] {ECO:0000313|EMBL:KXT84080.1, ECO:0000313|Proteomes:UP000070514} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DD11 {ECO:0000313|EMBL:KXT84080.1, RC ECO:0000313|Proteomes:UP000070514}; RA Denapaite D., Rieger M., Koendgen S., Brueckner R., Ochigava I., RA Kappeler P., Maetz-Rensing K., Leendertz F., Hakenbeck R.; RT "Highly variable Streptococcus oralis are common among viridans RT streptococci isolated from primates."; RL Submitted (JAN-2016) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KXT84080.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LQRF01000135; KXT84080.1; -; Genomic_DNA. DR EnsemblBacteria; KXT84080; KXT84080; STRDD11_01126. DR PATRIC; fig|1777879.3.peg.1255; -. DR Proteomes; UP000070514; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000070514}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000070514}. FT DOMAIN 199 359 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 158 192 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 412 AA; 46575 MW; 9CD42153E6885C9E CRC64; MIETEKKTER VFLVGVELAD TEHFDLSMEE LASLAKTAGA EVIGSYSQKR EKYDSRTFVG SGKLEEIRQM VEAEEISTVI VNNRLTPRQN VNLEESLGVK VIDRMQLILD IFAMRARSHE GKLQVHLAQL KYLLPRLVGQ GIMLSRQAGG IGSRGPGESQ LELNRRSVRN QIHDIERQLK AVEKNRATVR EKRLESSIFK IGLIGYTNAG KSTIMNCLTS KSQYEADELF ATLDATTKSI NLSGQLNVTL TDTVGFIQDL PTELVSSFKS TLEESRNVDL LVHVIDASDP HHEEHEKTVL DIMKDLDMLD IPRLTLYNKA DKAENFTPTL TPYSLISAKA DNSRAVLQQV LLERMKELFL PFTIRVVPAK AYKIHDLEKA AIIGKREYIN DVEAISGWIA EKNKWKLEEF YD // ID A0A139R650_9LACT Unreviewed; 427 AA. AC A0A139R650; DT 08-JUN-2016, integrated into UniProtKB/TrEMBL. DT 08-JUN-2016, sequence version 1. DT 07-JUN-2017, entry version 9. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=WEIDD23_00425 {ECO:0000313|EMBL:KXU10217.1}; OS Weissella sp. DD23. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Leuconostocaceae; OC Weissella. OX NCBI_TaxID=1777865 {ECO:0000313|EMBL:KXU10217.1, ECO:0000313|Proteomes:UP000070536}; RN [1] {ECO:0000313|EMBL:KXU10217.1, ECO:0000313|Proteomes:UP000070536} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DD23 {ECO:0000313|EMBL:KXU10217.1, RC ECO:0000313|Proteomes:UP000070536}; RA Denapaite D., Rieger M., Koendgen S., Brueckner R., Ochigava I., RA Kappeler P., Maetz-Rensing K., Leendertz F., Hakenbeck R.; RT "Highly variable Streptococcus oralis are common among viridans RT streptococci isolated from primates."; RL Submitted (JAN-2016) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KXU10217.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LQQL01000180; KXU10217.1; -; Genomic_DNA. DR EnsemblBacteria; KXU10217; KXU10217; WEIDD23_00425. DR PATRIC; fig|1777865.3.peg.560; -. DR Proteomes; UP000070536; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000070536}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}. FT DOMAIN 204 373 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 427 AA; 47492 MW; C81843D1D97EA007 CRC64; MIENELHPVR KVILAGLDRQ NAEFDYEMIE LANLAEANYM EVVGTVTQKL ERPNAATYFG KGKVEELKEA VEYYEADMVV TNDELSPSQI RNLESGTGAG IMDRTALILD IFASRAKTKV AKLQVAIAQL QYQLPRLRTS MNVRLDQQTG GGGGSFTSRG AGETKLETNR RHIEHQISLL RQELKDVEAD DQTRRARREK ESIKNVALVG YTNAGKSTIM NGLVRRYGEN QDKTVFQADM LFATLETSVR KLNLPDNQNF LLSDTVGFVS KLPHGLVAAF RATLAEAAQA DLLLQVVDYA DENYKEMMST TAKTLKEIGV GDIPMITIYN KADKIEGMSF PDRDGDTLTL SAQDDASLDM LIEVIRQHIY SDHVQTKVLI PFEQGQLVSE LNEQASVHSI DYVEAGTMMD VTLTPVQAAR FAAYVVD // ID A0A139SRE9_9BACT Unreviewed; 452 AA. AC A0A139SRE9; DT 11-MAY-2016, integrated into UniProtKB/TrEMBL. DT 11-MAY-2016, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=AXK12_02205 {ECO:0000313|EMBL:KXU37113.1}; OS Cephaloticoccus capnophilus. OC Bacteria; Verrucomicrobia; Opitutae; Opitutales; Opitutaceae; OC Cephaloticoccus. OX NCBI_TaxID=1548208 {ECO:0000313|EMBL:KXU37113.1, ECO:0000313|Proteomes:UP000071392}; RN [1] {ECO:0000313|EMBL:KXU37113.1, ECO:0000313|Proteomes:UP000071392} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CV41 {ECO:0000313|EMBL:KXU37113.1, RC ECO:0000313|Proteomes:UP000071392}; RA Wen L., He K., Yang H.; RL Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KXU37113.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LSZP01000014; KXU37113.1; -; Genomic_DNA. DR RefSeq; WP_068711030.1; NZ_LSZP01000014.1. DR EnsemblBacteria; KXU37113; KXU37113; AXK12_02205. DR Proteomes; UP000071392; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000071392}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000071392}. FT DOMAIN 210 375 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 169 196 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 452 AA; 50179 MW; 0365B4F24CA77738 CRC64; MADFLDNTPQ SDPNRCERAL LVGVHTQTMR TGEAEELLEE LRELVENLQI SVVHRELVTL RGQPKPATLL GSGRTDQIIT LAKHLDCDLI VIDESLSPAQ QRNWEKLAGI AVIDREEVIL DIFADRAQTR EAVLQIALAR MEYSLPRLAR AWTHLSRQRG KGKLGGEGET QLEQDRRLVR DRITRLRAEL VQVQKQRAVQ RSKRLRVPVP TASIVGYTNA GKSSLINALT GAEVLAADKL FATLDPTTRQ LLLRGNQKLL VTDTVGFIRR LPHRLVEAFK ATLEETIVAD FLIHTLDLAN PNFEEHHATT LGVLEELGAA DKPIITVFNK IDLATEADRS RARQLVPDAL FISAHTGEGL DALEAQCVEL IANTQGSAEL LVPHERYDVI ARLHALGHIQ AQIHDEAAGI YVRARIPLAQ TGFFKPFVLQ GEWPSELDET VEPGLSPAAA ER // ID A0A139SSW0_9BACT Unreviewed; 450 AA. AC A0A139SSW0; DT 08-JUN-2016, integrated into UniProtKB/TrEMBL. DT 08-JUN-2016, sequence version 1. DT 07-JUN-2017, entry version 10. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=AXK11_01990 {ECO:0000313|EMBL:KXU37592.1}; OS Cephaloticoccus primus. OC Bacteria; Verrucomicrobia; Opitutae; Opitutales; Opitutaceae; OC Cephaloticoccus. OX NCBI_TaxID=1548207 {ECO:0000313|EMBL:KXU37592.1, ECO:0000313|Proteomes:UP000070058}; RN [1] {ECO:0000313|EMBL:KXU37592.1, ECO:0000313|Proteomes:UP000070058} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CAG34 {ECO:0000313|EMBL:KXU37592.1, RC ECO:0000313|Proteomes:UP000070058}; RA Wen L., He K., Yang H.; RL Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KXU37592.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LSZQ01000013; KXU37592.1; -; Genomic_DNA. DR RefSeq; WP_068628735.1; NZ_LSZQ01000013.1. DR EnsemblBacteria; KXU37592; KXU37592; AXK11_01990. DR Proteomes; UP000070058; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000070058}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}. FT DOMAIN 210 375 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 450 AA; 50146 MW; F914419BB24C4AF6 CRC64; MADFLDNTPK SDSRRCERAL LVGVQTPAMR TGEAEELLDE LRELVENLQI SVVHREQVTL RGQPTPATLL GSGRTEQIIT LAKHLDCDLI VIDESLSPAQ QRNWEKLSGI AVIDREEVIL DIFADRAQTR EAVLQIALAR MEYSLPRLAR AWTHLSRQRG KGKLGGEGET QLEQDRRLVR DRITRLRAEL ALVQKQRAVQ RSKRLRVPVP TASIVGYTNA GKSSLINALT GAEVLAADKL FATLDPTTRQ LLLRGNQKLL VTDTVGFIRR LPHRLVEAFK ATLEETIVAD FLIHTLDLAN PNFEEHYATT LGVLEELGAA GKPILTVFNK IDLATEADRQ RARQLVPDAL FISAHTGEGL DTLEAHCLEL IANTQGTAEL LVPHERYDVI ARLHAIGHVQ AQVHDEETGI YVRAQIPLAQ TGFFKPFALK GEWPRSLKIT DAQFTRSTPN // ID A0A139SWB9_9GAMM Unreviewed; 436 AA. AC A0A139SWB9; DT 11-MAY-2016, integrated into UniProtKB/TrEMBL. DT 11-MAY-2016, sequence version 1. DT 30-AUG-2017, entry version 12. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=AXE65_12275 {ECO:0000313|EMBL:KXU38722.1}; OS Ventosimonas gracilis. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Ventosimonadaceae; Ventosimonas. OX NCBI_TaxID=1680762 {ECO:0000313|EMBL:KXU38722.1, ECO:0000313|Proteomes:UP000072660}; RN [1] {ECO:0000313|EMBL:KXU38722.1, ECO:0000313|Proteomes:UP000072660} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CV58 {ECO:0000313|EMBL:KXU38722.1, RC ECO:0000313|Proteomes:UP000072660}; RA Wen L., He K., Yang H.; RL Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KXU38722.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LSZO01000088; KXU38722.1; -; Genomic_DNA. DR RefSeq; WP_068388648.1; NZ_LSZO01000088.1. DR EnsemblBacteria; KXU38722; KXU38722; AXE65_12275. DR Proteomes; UP000072660; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000072660}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000072660}. FT DOMAIN 199 368 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 165 192 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 436 AA; 48934 MW; 7890483BE6F8F161 CRC64; MFFERHQGGE RAILVHLDTQ NPELSEDADE FRALATSAGA EILTFLEFPC QHPSPRFLIG SGKAEQLAQQ VKALQAELII FNHALTPSQE RNLESFCACR VIDRIGLILD IFAQRARTHE GKLQVELAQL SHLSTRLVRG WTHLERQKGG IGLRGPGETQ LESDRRLLRE RIAHIKQRLA KVRRQREQAR RRRRRAQIPT VSLVGYTNAG KSSLFNALTE GQVYAADQLF ATLDPTLRRL DIPGFGPIIL ADTVGFIRHL PHRLIEAFRA TLEESSNADL LLHVIDASGY EKEQQMEQVS AVLKEIGAGE LPLLEVCNKI DLLDDERAQP LLQRDSNGCA VRIWLSAQNG QGLDGLLKAM AERLGQDVFR GTLRLPGQAG RLRAKFFAQN AVRAEEQGDD GSTVLCVHLP QLELERLLRS EGWQPEHFLA QHELAQ // ID A0A139TI36_9FIRM Unreviewed; 408 AA. AC A0A139TI36; DT 08-JUN-2016, integrated into UniProtKB/TrEMBL. DT 08-JUN-2016, sequence version 1. DT 07-JUN-2017, entry version 10. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=HMPREF3037_01043 {ECO:0000313|EMBL:KXU51166.1}; OS Candidatus Stoquefichus sp. KLE1796. OC Bacteria; Firmicutes; Erysipelotrichia; Erysipelotrichales; OC Erysipelotrichaceae; Candidatus Stoquefichus. OX NCBI_TaxID=1574263 {ECO:0000313|EMBL:KXU51166.1, ECO:0000313|Proteomes:UP000070150}; RN [1] {ECO:0000313|EMBL:KXU51166.1, ECO:0000313|Proteomes:UP000070150} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=KLE1796 {ECO:0000313|EMBL:KXU51166.1, RC ECO:0000313|Proteomes:UP000070150}; RA Wen L., He K., Yang H.; RL Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KXU51166.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LTZJ01000048; KXU51166.1; -; Genomic_DNA. DR RefSeq; WP_066445805.1; NZ_KQ970880.1. DR EnsemblBacteria; KXU51166; KXU51166; HMPREF3037_01043. DR PATRIC; fig|1574263.3.peg.1038; -. DR Proteomes; UP000070150; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000070150}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000070150}. FT DOMAIN 190 351 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 408 AA; 47622 MW; 803C5A6B5954B17B CRC64; MKAILVGVEY DHMYYDLDIS MNELRDLSEA CHIEVKDVVI QKLSLISPKY YIGKGKVEEL KHMLDEDDIV IFNEELTPLQ VKNLTDALDV EVTDRSDLIL RIFESRAQTK EAKLQVEIAK NQYLLPRLAG MKEELYSQQG GSGFRGSGEK QIELDRRIIH RELIQAKREL AAIVKQRQTQ RQLRIRNQEK VVCLVGYTNS GKSSLLNYFT DKKVFQEDML FASLQTASRQ VKLKNHHRII MSDTVGFINQ LPHHLVQAFR STLEEVKEAD LLVHVIDSSS PYCDLQIETT LNVLEALGVK DTPMLFVYNK VDQDRYAFLQ PKEPAVFISV KEKINLDLLE DKIIELLFKD YELIELYIPY DKGEVYSQVK QAYEMIKEEY LEDGIYLSFY IDRKQIHKYQ DYIYKSIN // ID A0A139TTE4_9BACT Unreviewed; 441 AA. AC A0A139TTE4; DT 08-JUN-2016, integrated into UniProtKB/TrEMBL. DT 08-JUN-2016, sequence version 1. DT 07-JUN-2017, entry version 10. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=HMPREF3039_00901 {ECO:0000313|EMBL:KXU54936.1}; OS Akkermansia sp. KLE1798. OC Bacteria; Verrucomicrobia; Verrucomicrobiae; Verrucomicrobiales; OC Akkermansiaceae; Akkermansia. OX NCBI_TaxID=1574265 {ECO:0000313|EMBL:KXU54936.1, ECO:0000313|Proteomes:UP000070454}; RN [1] {ECO:0000313|EMBL:KXU54936.1, ECO:0000313|Proteomes:UP000070454} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=KLE1798 {ECO:0000313|EMBL:KXU54936.1, RC ECO:0000313|Proteomes:UP000070454}; RA Wen L., He K., Yang H.; RL Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KXU54936.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LTZM01000024; KXU54936.1; -; Genomic_DNA. DR RefSeq; WP_067571897.1; NZ_KQ971075.1. DR EnsemblBacteria; KXU54936; KXU54936; HMPREF3039_00901. DR PATRIC; fig|1574265.3.peg.878; -. DR Proteomes; UP000070454; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000070454}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}. FT DOMAIN 212 382 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 441 AA; 48923 MW; E4645B0B7862E658 CRC64; MFEIREKPEM VERAMLVSIY FDPSEAGEKQ AMLDELEDLV SNLGIGIVGK HLVKSRDMHA KFLCGTGKAQ EVKQLAVDCG ADCVVFDNML APSQQREWER LIDECVIDRE EVILDIFAKR ARTREATLQV ELARMQYSLP RMARMWSHLD RQGGGSGGGK GGGGAARGEG EKQIEVDRRL ARARIEAIQK ELVMVTRQRA TQRKERERQA VATAAIVGYT NAGKSSLLSL VSGSEVMARD MLFATLDTTT RKIELPNGQP LLLTDTVGFI RNLPHRLVEA FKSTLEEAVL ADFLVQVVDA SDPEAVRHYE TTLEVLGELG AGDKPMIVVL NKLDLVPEEE RAALTERLAP HFNGSLVCMS VREGQGTEDL LRACVEMLES RVRRARFLIP YTRSDLAAAM HSEGMVISTE YVEEGALVEA VLPVAFYNKV SQFLAEPSCE E // ID A0A139VLE0_MYCPH Unreviewed; 482 AA. AC A0A139VLE0; DT 08-JUN-2016, integrated into UniProtKB/TrEMBL. DT 08-JUN-2016, sequence version 1. DT 07-JUN-2017, entry version 9. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=MPHL43239_06960 {ECO:0000313|EMBL:KXW67007.1}; OS Mycobacterium phlei DSM 43239 = CCUG 21000. OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae; OC Mycobacterium. OX NCBI_TaxID=1226750 {ECO:0000313|EMBL:KXW67007.1, ECO:0000313|Proteomes:UP000070233}; RN [1] {ECO:0000313|EMBL:KXW67007.1, ECO:0000313|Proteomes:UP000070233} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 43239 \ CCUG 21000 {ECO:0000313|Proteomes:UP000070233}; RX PubMed=26941228; RA Das S., Pettersson B.M., Behra P.R., Ramesh M., Dasgupta S., RA Bhattacharya A., Kirsebom L.A.; RT "The Mycobacterium phlei genome: expectations and surprises."; RL Genome Biol. Evol. 0:0-0(2016). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KXW67007.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ANBO01000006; KXW67007.1; -; Genomic_DNA. DR EnsemblBacteria; KXW67007; KXW67007; MPHL43239_06960. DR PATRIC; fig|1226750.3.peg.1382; -. DR Proteomes; UP000070233; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000070233}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}. FT DOMAIN 258 427 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 217 251 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 482 AA; 52129 MW; 9210BBCE7199FBD1 CRC64; MRSDLRANLY SPMTYPDLPD TPSTGELALE DRSALRRVAG LSTELTDVSE VEYRQLRLER VVLVGVWTDG TVADAEASLA ELAALAETAG SEVLDGLIQR RDKPDPATYI GSGKAAELRE VVVATGADTV ICDGELSPAQ LTALEKAVKV KVIDRTALIL DIFAQHATSR EGKAQVSLAQ MEYMLPRLRG WGESMSRQAG GRAGGAGGGV GLRGPGETKI ETDRRRIRER MAKLRREIKE MKKIRDTQRS ARRSSDVAQI AIVGYTNAGK SSLLNALTGA GVLVENALFA TLEPTTRRGE FADGRPFVLT DTVGFVRHLP TQLVEAFRST LEEVVDADLL VHVVDGSDAN PLAQINAVRE VINEVIAEHD AQRAPELLVI NKIDAADELT LAQLRSALPD AVFVSARTGE GLDRLQQRIA ELIPPTDITV DVTIPYHRGD LVNKVHAEGR VDAVEHTADG TRIKARVPAG LAAGLREYTT FD // ID A0A139X6K3_9CYAN Unreviewed; 560 AA. AC A0A139X6K3; DT 11-MAY-2016, integrated into UniProtKB/TrEMBL. DT 11-MAY-2016, sequence version 1. DT 05-JUL-2017, entry version 13. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=WA1_27640 {ECO:0000313|EMBL:KYC40306.1}; OS Scytonema hofmannii PCC 7110. OC Bacteria; Cyanobacteria; Nostocales; Scytonemataceae; Scytonema. OX NCBI_TaxID=128403 {ECO:0000313|EMBL:KYC40306.1, ECO:0000313|Proteomes:UP000076925}; RN [1] {ECO:0000313|EMBL:KYC40306.1, ECO:0000313|Proteomes:UP000076925} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=PCC 7110 {ECO:0000313|EMBL:KYC40306.1, RC ECO:0000313|Proteomes:UP000076925}; RX PubMed=23221676; DOI=10.1093/gbe/evs117; RA Dagan T., Roettger M., Stucken K., Landan G., Koch R., Major P., RA Gould S.B., Goremykin V.V., Rippka R., Tandeau de Marsac N., RA Gugger M., Lockhart P.J., Allen J.F., Brune I., Maus I., Puhler A., RA Martin W.F.; RT "Genomes of Stigonematalean cyanobacteria (subsection V) and the RT evolution of oxygenic photosynthesis from prokaryotes to plastids."; RL Genome Biol. Evol. 5:31-44(2013). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KYC40306.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ANNX02000030; KYC40306.1; -; Genomic_DNA. DR EnsemblBacteria; KYC40306; KYC40306; WA1_27640. DR Proteomes; UP000076925; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000076925}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000076925}. FT DOMAIN 388 558 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 347 381 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 560 AA; 61771 MW; F1DB506364B7D527 CRC64; MAAISSEMNQ PVCTYLNRRG QVIRVGVGTP RQTQIPPLEL PRYGAERLSG IRCIATHLKS EPPNEVALTS MALQRLDALV MLNVTGTGFQ RRGGGATGYV KEAYLAHLAP QDARAFITSP AMRTAAPYLS SSEGGDEEPK GQEGNLTPAN WSASWSISPP LSLDMLTKQD FIELVEGLES EFRREYVAQD VDTDHDRVLI VGVMTDELTT QQFHDTLEEL GRLVDTAGGE VLQNMRQKRS RIHPQTVVGE GKVHEIALTA QTLGANLIVF DRDLSPAQIR NLESQIGVRV VDRTEVILDI FAQRAQSRAG KLQVELAQLE YMLPRLTGRG QAMSRQGGGI GTRGPGETKL ETERRAIQRR IARLQQEVNQ LQAHRERLRQ RRQHQEVPSI AIVGYTNAGK STLLNALTNA EVYTADQLFA TLDPTTRRLV VPHGMSGDTQ EILVTDTVGF IHELPASLMD AFRATLEEVT EADALLHLVD LSHPAWLSHI RSVRDILAQM PVTPGPALVV FNKIDQADSE TLALAREEFP LAVFISASNR LGLETLRQRL GQLVQYATSC // ID A0A140L0W6_9CLOT Unreviewed; 464 AA. AC A0A140L0W6; DT 08-JUN-2016, integrated into UniProtKB/TrEMBL. DT 08-JUN-2016, sequence version 1. DT 07-JUN-2017, entry version 8. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:KXG74191.1}; GN ORFNames=AN619_25090 {ECO:0000313|EMBL:KXG74191.1}; OS Thermotalea metallivorans. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Thermotalea. OX NCBI_TaxID=520762 {ECO:0000313|EMBL:KXG74191.1, ECO:0000313|Proteomes:UP000070456}; RN [1] {ECO:0000313|EMBL:KXG74191.1, ECO:0000313|Proteomes:UP000070456} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=B2-1 {ECO:0000313|EMBL:KXG74191.1, RC ECO:0000313|Proteomes:UP000070456}; RA Patel B.K.; RT "Draft genome sequence of the thermoanaerobe Thermotalea RT metallivorans, an isolate from the runoff channel of the Great RT Artesian Basin, Australia."; RL Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KXG74191.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LOEE01000061; KXG74191.1; -; Genomic_DNA. DR EnsemblBacteria; KXG74191; KXG74191; AN619_25090. DR PATRIC; fig|520762.4.peg.2788; -. DR Proteomes; UP000070456; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000070456}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000070456}. FT DOMAIN 233 404 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 464 AA; 52518 MW; 9AF02E5A5A5E754B CRC64; MDKIDVFLEF SSIIYGIERD KVGEGMQFNE NNEIINVIEQ RAILVGLSTG TRDEITTIEN SMEELKELAK AAGAVVLDMV VQNRPRVDAA YYIGKGKAEE IKIFCRALDA NLVIFNDELS GAQIRNLEEL MEVTVIDRTT LILDIFAQRA QSKEGKLQVE LAQLRYRLPR LIGLGNSLSR TGAGIGTRGP GEKKLELDRR HILDRISDIR HQLEEIRKNR ETQRTKRRKS EIPVVALVGY TNAGKSTLMN KLMSISGVQQ EEKEVYVEDM LFATLDTAHR KMVLPSKEEF ILIDTVGFVS KLPHSLVEAF KATLEEVQEA NLLLHVVDAT NEDFEMQIKV TEKVLNELGV KDKPTILIFN KIDKQEDQSA LIPRGENIVH LSALKDIGID ILMQMIKDKL FSNMKKVSLL LPYSKGDIVS YLCDKTKVVK TEYREDGVLV ETTVGPADYN KYRQYQVNKA EMAE // ID A0A140L3S2_9THEO Unreviewed; 415 AA. AC A0A140L3S2; DT 08-JUN-2016, integrated into UniProtKB/TrEMBL. DT 08-JUN-2016, sequence version 1. DT 07-JUN-2017, entry version 10. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:KXG75197.1}; GN ORFNames=AN618_20150 {ECO:0000313|EMBL:KXG75197.1}; OS Fervidicola ferrireducens. OC Bacteria; Firmicutes; Clostridia; Thermoanaerobacterales; OC Thermoanaerobacteraceae; Fervidicola. OX NCBI_TaxID=520764 {ECO:0000313|EMBL:KXG75197.1, ECO:0000313|Proteomes:UP000070427}; RN [1] {ECO:0000313|EMBL:KXG75197.1, ECO:0000313|Proteomes:UP000070427} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Y170 {ECO:0000313|EMBL:KXG75197.1, RC ECO:0000313|Proteomes:UP000070427}; RA Patel B.K.; RT "Draft genome sequnece of Fervidicola ferrireducens strain Y170."; RL Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KXG75197.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LOED01000031; KXG75197.1; -; Genomic_DNA. DR RefSeq; WP_066354559.1; NZ_LOED01000031.1. DR EnsemblBacteria; KXG75197; KXG75197; AN618_20150. DR PATRIC; fig|520764.3.peg.2161; -. DR Proteomes; UP000070427; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000070427}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000070427}. FT DOMAIN 195 357 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 164 191 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 415 AA; 46210 MW; 868622BE057B4A69 CRC64; MPLETRKPAT RAILAGLISG VSEQQTLEEL ALLAETAGAE VLAKVTQKRP SKDPAYYLGL GKVREIAQMA EFLGANAVIF DDDLTPVQIR NLEDIIGTQI IDRTTLVLDI FAQRARSLEG KIQVELAQLQ HLLPRLTGKG VELSREGGGI GTRGPGETKL ETDRRHIRRR ISYLKRELER IRKNRELLRS SRKYPVVSLV GYTNAGKSTL MNALTGAGVS ANDRLFDTLD TTTRALVLPD GRKVLLSDTV GFIRKLSHEI VEAFKATLEE VKESDLLILV ADASNPAVDE EIATVRAVLK EIQASDIPSI LALNKIDKLD CSKPLINDKN AVEISALKGT NLDLLLKKMC VLLPQTREHA SLLIPYEYGF LLDDIYENGK VEREEYRPEG IEIEGMIDSI LLRKLRKYLF DRSCF // ID A0A142EJB2_9BACT Unreviewed; 419 AA. AC A0A142EJB2; DT 08-JUN-2016, integrated into UniProtKB/TrEMBL. DT 08-JUN-2016, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=AO498_02330 {ECO:0000313|EMBL:AMQ55217.1}; OS Algoriphagus sp. M8-2. OC Bacteria; Bacteroidetes; Cytophagia; Cytophagales; Cyclobacteriaceae; OC Algoriphagus. OX NCBI_TaxID=1727163 {ECO:0000313|EMBL:AMQ55217.1, ECO:0000313|Proteomes:UP000073816}; RN [1] {ECO:0000313|Proteomes:UP000073816} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=M8-2 {ECO:0000313|Proteomes:UP000073816}; RA Shintani M.; RT "Complete sequence of Algoriphagus sp. M8-2."; RL Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP012836; AMQ55217.1; -; Genomic_DNA. DR RefSeq; WP_067543250.1; NZ_CP012836.1. DR EnsemblBacteria; AMQ55217; AMQ55217; AO498_02330. DR KEGG; alm:AO498_02330; -. DR PATRIC; fig|1727163.4.peg.489; -. DR KO; K03665; -. DR Proteomes; UP000073816; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000073816}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000073816}. FT DOMAIN 210 399 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 171 198 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 419 AA; 48172 MW; D17DDECAB93397FC CRC64; MSKFSRKIQK LHDTAPKIET AVLVTLIRQH QPEHEVEEHL EELAFLAETL GVKSVYRFTQ KMDKPDIRTF VGKGKLEEIQ AYIEHFAVDM VIFDDDLSPS QMRNLENELK VKIYDRSLLI LDIFLQRAQT AQAKTQVELA RFQYLLPRLT GMWTHLERQR GGTGTRGGAG EKEIETDKRD IRNKIALLRD KLKEIEKQGV TQRKGRKGIV RVALVGYTNV GKSTLMNLIT KTDILAENKL FATVDATVRK VVLDHIPFLL SDTVGFIRKL PTHLIESFKS TLDEIREADL LIHVVDISHP AFEDHIAVVN QTLREIKAGE KPVLLVFNKI DLVDQMPTEE ESMHISEHEL QESRYVDFKA LSEAYEKKNG IKPVFMAAAS AENVEEFRSA LVAEVKKQHR KIYPHYLEDQ VVDWGDKWE // ID A0A142HLM8_9BACT Unreviewed; 415 AA. AC A0A142HLM8; DT 08-JUN-2016, integrated into UniProtKB/TrEMBL. DT 08-JUN-2016, sequence version 1. DT 05-JUL-2017, entry version 12. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=A0257_14495 {ECO:0000313|EMBL:AMR29786.1}; OS Hymenobacter sp. PAMC 26554. OC Bacteria; Bacteroidetes; Cytophagia; Cytophagales; Hymenobacteraceae; OC Hymenobacter. OX NCBI_TaxID=1484116 {ECO:0000313|EMBL:AMR29786.1, ECO:0000313|Proteomes:UP000075086}; RN [1] {ECO:0000313|EMBL:AMR29786.1, ECO:0000313|Proteomes:UP000075086} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=PAMC 26554 {ECO:0000313|EMBL:AMR29786.1, RC ECO:0000313|Proteomes:UP000075086}; RA Park H.; RT "Hymenobacter sp. genome sequencing."; RL Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP014771; AMR29786.1; -; Genomic_DNA. DR EnsemblBacteria; AMR29786; AMR29786; A0257_14495. DR KEGG; hyp:A0257_14495; -. DR KO; K03665; -. DR Proteomes; UP000075086; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 2. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000075086}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000075086}. FT DOMAIN 204 402 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 172 199 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 415 AA; 46777 MW; 1D3612842454D32B CRC64; MLKTKTHETA KEVETAVLVS VPPRRQTDAQ TTEYLDELAF LIETAGAQAT KRFVQKLDKP DLRSYVGEGK LAEIKAWVKH EKTSMVVFDD ELLPSQLRNL EAELGVKIVD RSLLILDIFA LRAKSATSRT QVELAQYQYL LPRLTGLWTH LDKQRGGVGM KGPGETEIET DRRIVRDRIA FLKEKLEDLD KQAHTQRKTR TNSIRVALVG YTNVGKSTIM NLLGKAEVFA ENKLFATVDA TTRKVVLDNH VPFLLSDTVG FIRKLPTKLI ESFKSTLDEI READLLVHVV DISHPAFEEQ IEVVNETLRE IGAADKPMLL VFNKIDQYKS EESPAPVFEA DDDAEAEWPT DQAAPAPRPP LEQLQETYMA RLHDPVVFIS AQNKENIEAL RELLARRVGE LAAKRFPHFQ AGYGG // ID A0A142HPU9_9SPHI Unreviewed; 394 AA. AC A0A142HPU9; DT 08-JUN-2016, integrated into UniProtKB/TrEMBL. DT 08-JUN-2016, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=A0256_05445 {ECO:0000313|EMBL:AMR30907.1}; OS Mucilaginibacter sp. PAMC 26640. OC Bacteria; Bacteroidetes; Sphingobacteriia; Sphingobacteriales; OC Sphingobacteriaceae; Mucilaginibacter. OX NCBI_TaxID=1300914 {ECO:0000313|EMBL:AMR30907.1, ECO:0000313|Proteomes:UP000073092}; RN [1] {ECO:0000313|EMBL:AMR30907.1, ECO:0000313|Proteomes:UP000073092} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=PAMC 26640 {ECO:0000313|EMBL:AMR30907.1, RC ECO:0000313|Proteomes:UP000073092}; RA Park H.; RT "Mucilaginibacter sp. genome sequencing."; RL Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP014773; AMR30907.1; -; Genomic_DNA. DR RefSeq; WP_067188668.1; NZ_CP014773.1. DR EnsemblBacteria; AMR30907; AMR30907; A0256_05445. DR KEGG; mup:A0256_05445; -. DR KO; K03665; -. DR Proteomes; UP000073092; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000073092}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000073092}. FT DOMAIN 203 383 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 394 AA; 45355 MW; E50ACA28D3CFBF7B CRC64; MKQKFYDTAV KQEKVVLVGV ITPNETEARE KEYLEELEFL VATAGGLTVH TFTQKLQRPE RATFVGTGKL EEIKEYVTAE EIDIVVFDDE LTPSQLRNIE RELQVKVLDR SNLILDIFAG RAQTAQAKTQ VELAQLQYLL PRLTRLWTHL ERQKGGIGMR GPGESQIETD RRLILNKISL LKERLKLIDR QNETQRKNRQ QLIRVALVGY TNVGKSTIMN MLAKSDVFAE NKLFATLDTT VRKVVIENVP FLLSDTVGFI RKLPHHLVEC FKSTLDEVRE ADILIHVVDV SHPTFEDQIR TVNETLKELK VVDKKTITVF NKIDAFNPAD HNIDIKETPL TMDDFNHSWM AKNNAPAIFI SATEKENVEE FKTMLYDAVK TIHTERYPYD NLLY // ID A0A142L6N6_9BACT Unreviewed; 392 AA. AC A0A142L6N6; DT 08-JUN-2016, integrated into UniProtKB/TrEMBL. DT 08-JUN-2016, sequence version 1. DT 07-JUN-2017, entry version 10. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=AEM51_13495 {ECO:0000313|EMBL:AMS27882.1}; OS Bacteroidetes bacterium UKL13-3. OC Bacteria; Bacteroidetes. OX NCBI_TaxID=1690483 {ECO:0000313|EMBL:AMS27882.1, ECO:0000313|Proteomes:UP000075224}; RN [1] {ECO:0000313|EMBL:AMS27882.1, ECO:0000313|Proteomes:UP000075224} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=UKL13-3 {ECO:0000313|EMBL:AMS27882.1}; RA Noorani M.; RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP012155; AMS27882.1; -; Genomic_DNA. DR EnsemblBacteria; AMS27882; AMS27882; AEM51_13495. DR KEGG; bbau:AEM51_13495; -. DR PATRIC; fig|1690483.4.peg.2878; -. DR KO; K03665; -. DR Proteomes; UP000075224; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000075224}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000075224}. FT DOMAIN 204 388 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 392 AA; 44953 MW; 2E7FF795829EE0E2 CRC64; MAQQLGFDTK KKQEKAILVG VITQNQKQEK AEEYLEELAF LTLTAGARVV KRFLQRLTHP DRKTYIGSGK LEEVGEFVRA QEIDIVIFDD ELSPSQLRNL EMALKCKILD RSNLILDIFA TRARTAQAKY QVELAQSQYL LPRLTRMWTH LSKQKGGIGM KGPGETEIET DRRILRDNIS KLKQRLTDID KQSVTRRKNR DDKARVALVG YTNVGKSTLL NLLSKSEVLA EDKLFATLDS TVRKVVIGDV PFLLTDTVGF IRKLPHQLIE CFKSTLDEIR EADILLHIVD VSHPNFEEQI DVVNRTLLEL KVNDKPIILV FNKIDQLQEP LVQHIDDDDI QEEIPYIQRL KNTWIAKENA PVIFISASNK TNIDELKQML LEKIKPLMKA AY // ID A0A142LAM5_9RHOB Unreviewed; 458 AA. AC A0A142LAM5; DT 08-JUN-2016, integrated into UniProtKB/TrEMBL. DT 08-JUN-2016, sequence version 1. DT 07-JUN-2017, entry version 10. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=AEM38_07075 {ECO:0000313|EMBL:AMS29271.1}; OS Hyphomonadaceae bacterium UKL13-1. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Hyphomonadaceae. OX NCBI_TaxID=1690484 {ECO:0000313|EMBL:AMS29271.1, ECO:0000313|Proteomes:UP000075235}; RN [1] {ECO:0000313|EMBL:AMS29271.1, ECO:0000313|Proteomes:UP000075235} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=UKL13-1 {ECO:0000313|EMBL:AMS29271.1}; RA Noorani M.; RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP012156; AMS29271.1; -; Genomic_DNA. DR EnsemblBacteria; AMS29271; AMS29271; AEM38_07075. DR KEGG; hbc:AEM38_07075; -. DR PATRIC; fig|1690484.4.peg.1493; -. DR KO; K03665; -. DR Proteomes; UP000075235; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000075235}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000075235}. FT DOMAIN 205 381 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 458 AA; 50849 MW; 5007C11B3A734D2A CRC64; MHLIDRQAPV QRALVIHPLR SDASASRDPD LRLIEACGLA EALDLEVADA RLAPLRQVRP GAYFGTGKIE ELKAYCEELK VDVLILDHQM SPVQQRNLEK ELQVKVVDRT GLILEIFARR ARTREGRLQV ELARLSYEKS RLVKTWTHLE RQRGGTGKTG GPGERQIELD RRMIADKILK LKKELEEVKR TRALQRASRK RVPYPVIALV GYTNAGKSTL FNRAASADVF AKDMPFATLD TTLRAVRTPT GRDVILSDTV GFITDLPTEL VAAFRATLEE VAQADLLVHV RDIAHAESDN QRRDVELVLD RVLTDHESRP PLIEAWNKID CLDEAGAAYV RARAAASGLD GTAQGICVSA LTGEGVKELF ALIDSELALD ARPVDLVIGP DQGAARAWLF RKGAVRQEET DEQGFTHLKV RLTADDAARF VAQWPQILSE VPFVALGEVP EPVHFLEA // ID A0A142LJM9_9PROT Unreviewed; 470 AA. AC A0A142LJM9; DT 08-JUN-2016, integrated into UniProtKB/TrEMBL. DT 08-JUN-2016, sequence version 1. DT 07-JUN-2017, entry version 10. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=AEM42_08590 {ECO:0000313|EMBL:AMS32425.1}; OS Betaproteobacteria bacterium UKL13-2. OC Bacteria; Proteobacteria; Betaproteobacteria. OX NCBI_TaxID=1690485 {ECO:0000313|EMBL:AMS32425.1, ECO:0000313|Proteomes:UP000075227}; RN [1] {ECO:0000313|EMBL:AMS32425.1, ECO:0000313|Proteomes:UP000075227} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=UKL13-2 {ECO:0000313|EMBL:AMS32425.1}; RA Noorani M.; RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP012157; AMS32425.1; -; Genomic_DNA. DR EnsemblBacteria; AMS32425; AMS32425; AEM42_08590. DR KEGG; beb:AEM42_08590; -. DR PATRIC; fig|1690485.4.peg.1958; -. DR KO; K03665; -. DR Proteomes; UP000075227; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000075227}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000075227}. FT DOMAIN 240 415 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 199 235 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 470 AA; 51409 MW; DCAE87467F26C214 CRC64; MPKDTKTQNI RALVAAVHLQ NVSDTEFDSS LNELRELAKT LGYDVVHAFV QKRASFDRAA YFGVGKRREI RQYVEGDTGA KAIVDDLDDP APIEPALAPA DPETRAADIL LIDHDISPSQ ARNLEIAVGC EVMDRTMVIL EIFHRHASSR AARAQVEIAR LGYMAPRLRE AAKLAGPQGR QRSGTGGRGA GESQSALDKQ KIRNRISELQ VEIVAMEAER KIQRARRQAN QNTADGSGIA RVALVGYTNA GKSTLMRALT GSDVLVANKL FATLDTTVRT LYPETVPKVL VSDTVGFIKN LPHDLVASFK STLEEAAEAS LLLHIIDASD PGFQRQLEVT NEVLAEIGAD VVPRIHVFNK IDMVGAGTTN PAAAQAATAS HLRNQYPDCV VMSAKNPADV ARMHATIRRF FQKNLTEDEL FLPWSLQQLR GKIFANCEVL NERADNDGAF LRVRGEASMI KSLQDDLSAK // ID A0A142M8M0_AMIAI Unreviewed; 462 AA. AC A0A142M8M0; DT 08-JUN-2016, integrated into UniProtKB/TrEMBL. DT 08-JUN-2016, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=AA2016_3770 {ECO:0000313|EMBL:AMS42690.1}; OS Aminobacter aminovorans (Chelatobacter heintzii). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Phyllobacteriaceae; Aminobacter. OX NCBI_TaxID=83263 {ECO:0000313|EMBL:AMS42690.1, ECO:0000313|Proteomes:UP000075755}; RN [1] {ECO:0000313|EMBL:AMS42690.1, ECO:0000313|Proteomes:UP000075755} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=KCTC 2477 {ECO:0000313|EMBL:AMS42690.1, RC ECO:0000313|Proteomes:UP000075755}; RA Kim K.M.; RT "Complete genome of Aminobacter aminovorans KCTC 2477."; RL Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP015005; AMS42690.1; -; Genomic_DNA. DR RefSeq; WP_067962308.1; NZ_CP015005.1. DR EnsemblBacteria; AMS42690; AMS42690; AA2016_3770. DR KEGG; aak:AA2016_3770; -. DR PATRIC; fig|83263.3.peg.3887; -. DR KO; K03665; -. DR Proteomes; UP000075755; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000075755}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}. FT DOMAIN 231 404 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 190 217 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 462 AA; 50654 MW; 7E4CC42160054CB7 CRC64; MARDRTAGAK AGDSNGPESV GGDKAPTRAV VIVPVLTRQP KNDDDSARPR LQRSAEARHD EAVGLTRAID LEPVHTAIVT LNDPRPATLL GSGKVEEFAA IVKERGAELV IVDHPLTPVQ QRNLEKEMHA KVLDRTGLIL EIFGRRARTK EGTLQVELAH LNYQKGRLVR SWTHLERQRG GAGFLGGPGE TQIESDRRAL QEKIIKLKRE LETVVRTRDL HRSKRRKVPF PVVAIVGYTN AGKSTLFNRL TGASVLAENM LFATLDPTLR RVRLPHGTPI ILSDTVGFIS DLPTHLIAAF RATLEEVVEA DLVIHLRDIS DPDTAAQADD VERILSDLGV DAADTDRVVE VWNKIDQLDE GNRERLLADS SDGRKTPPIA ISAATGEGLS ALTGLIEQRV SGELESIDVT LEPSQLGQID WLYRNGDVVK RKDNDDGSVS MTLKATASAR DEIAAKILRN KR // ID A0A142X2R7_9PLAN Unreviewed; 499 AA. AC A0A142X2R7; DT 08-JUN-2016, integrated into UniProtKB/TrEMBL. DT 08-JUN-2016, sequence version 1. DT 07-JUN-2017, entry version 10. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:AMV21343.1}; GN ORFNames=VT03_25805 {ECO:0000313|EMBL:AMV21343.1}; OS Planctomyces sp. SH-PL14. OC Bacteria; Planctomycetes; Planctomycetia; Planctomycetales; OC Planctomycetaceae; Planctomyces. OX NCBI_TaxID=1632864 {ECO:0000313|EMBL:AMV21343.1, ECO:0000313|Proteomes:UP000076318}; RN [1] {ECO:0000313|EMBL:AMV21343.1, ECO:0000313|Proteomes:UP000076318} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SH-PL14 {ECO:0000313|EMBL:AMV21343.1, RC ECO:0000313|Proteomes:UP000076318}; RA van der Voort M., Raaijmakers J.M.; RT "Genome minning of novel planctomycete species."; RL Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP011270; AMV21343.1; -; Genomic_DNA. DR EnsemblBacteria; AMV21343; AMV21343; VT03_25805. DR KEGG; pls:VT03_25805; -. DR PATRIC; fig|1632864.3.peg.5921; -. DR KO; K03665; -. DR Proteomes; UP000076318; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000076318}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000076318}. FT DOMAIN 263 429 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 499 AA; 55369 MW; CFB37FD5A4C81F15 CRC64; MNPWEFRVSG EGQDFPGFRA GVGNGPARCV EFGGSRPAAG KPIQRDRVPR TQSSGDEKHL GEPTRDKLKV HAQRAILVAV VDPREQRGKD KALEEMQGLV ETAGAEVVGS VVQMRDKPDI GTYIGSGKID ELRELIHATD ANLIAFDNSL SPSQAKAVEE LTKTQVVDRS EVILDIFATH ARTHESRLQV ELAQLLYMRS RLTRMWTHLE RIAGGIVGGR GPGEKQLETD RRLIDKRITD LKRKLAEVEK RREREVAGRK EKMTVSLVGY TNAGKSTLMR ALTGADVYIA NQLFATLDTR TRSWTIPHWG DVLLSDTVGF IRNLPHHLVA SFRSTLEEAR HADLLLHVVD ASHPEAQLQI TTVQEVLGEL GVEDHHPLLV LNKTDAVEDR SFLDVLQSRY PEAISVSAVE GTGIAELGRA VADRLSDGFM KARVEGSAGN GRLLRYLQQH SELLKTEYDE NQVAYECRLP RRFTWAVEQE GGVVIPLDGT VLNGKANEE // ID A0A142Y8J6_9PLAN Unreviewed; 463 AA. AC A0A142Y8J6; DT 08-JUN-2016, integrated into UniProtKB/TrEMBL. DT 08-JUN-2016, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:AMV35538.1}; GN ORFNames=VN12_25830 {ECO:0000313|EMBL:AMV35538.1}; OS Pirellula sp. SH-Sr6A. OC Bacteria; Planctomycetes; Planctomycetia; Planctomycetales; OC Planctomycetaceae; Pirellula. OX NCBI_TaxID=1632865 {ECO:0000313|EMBL:AMV35538.1, ECO:0000313|Proteomes:UP000076398}; RN [1] {ECO:0000313|EMBL:AMV35538.1, ECO:0000313|Proteomes:UP000076398} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SH-Sr6A {ECO:0000313|EMBL:AMV35538.1, RC ECO:0000313|Proteomes:UP000076398}; RA van der Voort M., Raaijmakers J.M.; RT "Genome minning of novel planctomycete species."; RL Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP011272; AMV35538.1; -; Genomic_DNA. DR EnsemblBacteria; AMV35538; AMV35538; VN12_25830. DR KEGG; pir:VN12_25830; -. DR PATRIC; fig|1632865.3.peg.5681; -. DR KO; K03665; -. DR Proteomes; UP000076398; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000076398}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000076398}. FT DOMAIN 201 367 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 162 196 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 463 AA; 51150 MW; 9F4EEC878D82634B CRC64; MQTHDRSESL ASERSVLARL ILPNDFESED PFDELRGLAT TAGTTVVGTV LQRKDHPDQT TYLGKGKVQE LKAMLEMHDA DVVLFDNDLN PAQTRNLEKA LNVKVLDRSE LILDIFASNA RTHEARLAVE LAQLEYSLPR LKRMWTHLSR QTMGVGMRGP GEKQLEVDRR LAEKRVHDLK LELAKVERRK EREVASRRGM YSVSLAGYTN AGKSTLMNAL TDAGVEAVDK LFATLDTRTR RWMLPGWGPV LLSDTVGFIR DLPHRLIASF RATLEETRQA DLLLHVADAS NPNVLHQISS VYKVLQEIGI DEKDTLLVLN KIDCEGASER AELVKSRYPN AILISAKSGI GLSQFSIAVS DALTKHFAEL EVKLPLDDGK TMAWLAQHAE IISKQYNDDF AIIHCRLPVG AGGKLASQGV DLRVIAGQLP VASESKGPDR ATYVPVPLEE TPTSGSQNVG EVA // ID A0A142YLE6_9PLAN Unreviewed; 435 AA. AC A0A142YLE6; DT 08-JUN-2016, integrated into UniProtKB/TrEMBL. DT 08-JUN-2016, sequence version 1. DT 07-JUN-2017, entry version 10. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:AMV39996.1}; GN ORFNames=VT85_21360 {ECO:0000313|EMBL:AMV39996.1}; OS Planctomyces sp. SH-PL62. OC Bacteria; Planctomycetes; Planctomycetia; Planctomycetales; OC Planctomycetaceae; Planctomyces. OX NCBI_TaxID=1636152 {ECO:0000313|EMBL:AMV39996.1, ECO:0000313|Proteomes:UP000076365}; RN [1] {ECO:0000313|EMBL:AMV39996.1, ECO:0000313|Proteomes:UP000076365} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SH-PL62 {ECO:0000313|EMBL:AMV39996.1, RC ECO:0000313|Proteomes:UP000076365}; RA van der Voort M., Raaijmakers J.M.; RT "Genome minning of novel planctomycete species."; RL Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP011273; AMV39996.1; -; Genomic_DNA. DR RefSeq; WP_068419760.1; NZ_CP011273.1. DR KEGG; plh:VT85_21360; -. DR PATRIC; fig|1636152.3.peg.4826; -. DR KO; K03665; -. DR Proteomes; UP000076365; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000076365}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000076365}. FT DOMAIN 203 369 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 435 AA; 48310 MW; 587E2914FD24721C CRC64; MIDTSRNERS GNRERAVLVG VILPGGEYNT DDPLDEIRGL AKTAGLDVVG TMLQKRQQVD VATYIGSGKV DELKEQVRAF EADVVIFDSD LGPGQTRNLE KALECKVVDR TEVILDIFAI HAQTHEAHLQ VELAQLEYAM PRLKRMWTHL SRYKGGIGVR GPGEKQLEED KRLVVHRIQE LKAKLGKIQA RKEREVAGRG DFPTVSLVGY TNAGKSTLMN ALTDAGVLVE NKLFATLDTR TRKWRFRGGG AALLSDTVGF IRDLPHALVA SFKATLEEAR QADLLLHVVD ASSPDAEMQV RAVVEVLEEL GLKDHPTLLV LNKADRVPDR SFLDVLRAQH RDSIAISAAK GEGLEALEHA VRQALLESAL DAEVEISVAD GRVLSYLAQH AQIHGRTYDE ANDRVVVDCR LPRRCLDFLY EHGAEVREKE IRIYA // ID A0A143B906_9DELT Unreviewed; 551 AA. AC A0A143B906; DT 08-JUN-2016, integrated into UniProtKB/TrEMBL. DT 08-JUN-2016, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=DBW_2589 {ECO:0000313|EMBL:AMV72917.1}; OS Desulfuromonas sp. DDH964. OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfuromonadales; OC Desulfuromonadaceae; Desulfuromonas. OX NCBI_TaxID=1823759 {ECO:0000313|EMBL:AMV72917.1, ECO:0000313|Proteomes:UP000075994}; RN [1] {ECO:0000313|EMBL:AMV72917.1, ECO:0000313|Proteomes:UP000075994} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DDH964 {ECO:0000313|EMBL:AMV72917.1, RC ECO:0000313|Proteomes:UP000075994}; RA Badalamenti J.P., Bond D.R.; RT "A little goes a long way: Capturing complete genomes from a deep RT subsurface metagenome with long reads."; RL Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP015080; AMV72917.1; -; Genomic_DNA. DR RefSeq; WP_066727858.1; NZ_CP015080.1. DR EnsemblBacteria; AMV72917; AMV72917; DBW_2589. DR KEGG; deu:DBW_2589; -. DR PATRIC; fig|1823759.3.peg.2625; -. DR KO; K03665; -. DR Proteomes; UP000075994; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000075994}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000075994}. FT DOMAIN 381 545 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 340 367 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 551 AA; 61515 MW; 66903FF9400E2A42 CRC64; MAQTTLYGNL AGLKPSQLQA LERIYRRRIP PEQLISPELG RYLTERSHEL RRQLGLIIDR AGTIHHVIVG DDREIVIPDL SAFSFGRSGL RGLRCVHTHL KGEPLSQDDL TDLALLRLDL IAAIAVGSDG LPGRVDYAHL LPPRPGQPAT QILAAPHLHD FELDLTAFLP ALDAELERKM AETVDLSDTR EKALLISVSQ APRQAIEDSL DELSELARTA DVVVLERVVQ RPRQLNPNTL MGEGKLKEVI ISALQQGATL LIFDQELSPV QARSLAAITA LKILDRTQLI LDIFARRAHT LDGKVQVELA QLKYILPRLR GKGSAMSRLM GGIGGRGPGE TKLEIDLRRI RERISRLEKQ LDTLARGRKQ RRQKRIRAQV PIVSIVGYTN AGKSTLLNAL TQSSVFTENL LFATLDTATR RLRFPLEREV IITDTVGFIR QLPKNLIGAF KATLEELEDA DLLLHVVDIA NPRFEEQIMA VERILADLEL DRIPRQLVFN KIDLIDAGEA KALARRFSAL PVTALDRSSF LPLLAELQRR FWPGEAELLD T // ID A0A143BKC1_9BACT Unreviewed; 449 AA. AC A0A143BKC1; DT 08-JUN-2016, integrated into UniProtKB/TrEMBL. DT 08-JUN-2016, sequence version 1. DT 07-JUN-2017, entry version 8. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=GEMMAAP_09910 {ECO:0000313|EMBL:AMW05053.1}; OS Gemmatimonas phototrophica. OC Bacteria; Gemmatimonadetes; Gemmatimonadales; Gemmatimonadaceae; OC Gemmatimonas. OX NCBI_TaxID=1379270 {ECO:0000313|EMBL:AMW05053.1, ECO:0000313|Proteomes:UP000076404}; RN [1] {ECO:0000313|EMBL:AMW05053.1, ECO:0000313|Proteomes:UP000076404} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=AP64 {ECO:0000313|EMBL:AMW05053.1, RC ECO:0000313|Proteomes:UP000076404}; RX PubMed=24821787; DOI=10.1073/pnas.1400295111; RA Zeng Y., Feng F., Medova H., Dean J., Koblizek M.; RT "Functional type 2 photosynthetic reaction centers found in the rare RT bacterial phylum Gemmatimonadetes."; RL Proc. Natl. Acad. Sci. U.S.A. 111:7795-7800(2014). RN [2] {ECO:0000313|EMBL:AMW05053.1, ECO:0000313|Proteomes:UP000076404} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=AP64 {ECO:0000313|EMBL:AMW05053.1, RC ECO:0000313|Proteomes:UP000076404}; RX PubMed=26636755; DOI=10.1111/1758-2229.12363; RA Zeng Y., Baumbach J., Barbosa E.G., Azevedo V., Zhang C., Koblizek M.; RT "Metagenomic evidence for the presence of phototrophic RT Gemmatimonadetes bacteria in diverse environments."; RL Environ. Microbiol. Rep. 8:139-149(2016). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP011454; AMW05053.1; -; Genomic_DNA. DR EnsemblBacteria; AMW05053; AMW05053; GEMMAAP_09910. DR KEGG; gph:GEMMAAP_09910; -. DR KO; K03665; -. DR Proteomes; UP000076404; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000076404}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000076404}. FT DOMAIN 204 374 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 449 AA; 50150 MW; AFA2696ED020F490 CRC64; MSREPINLTL PVERAILVSA PFKRSSAKHF VDEHLQELAR LADTAGAQVV GTLTQQLDRP HPGTYLGSGK VEELKERIKE LGATLVIFDD ELSPAQGKNV ELIVNTRVMD RAELILDIFA TRARSNEARM QVELAQLEYL LPRLTRMWTH LEKMRGGIGM RGPGETQLET DRRLIQHRIR ILKERLADVE RAREVQRQGR HTHFRVALVG YTNAGKSSIL RSMANDSDVF VEDRLFATLD PLTREVEVGD GYTVLLTDTV GFIRKLPHHL VASFRATLSE AREADLLLHV IDSSHPAWEE QRDVVDGVLN DLGLSERPLT YVMNKMDAIS AEDASSVRER VANLMPNSLF VSALEPGGLD GLKATLLHSM RNQRPILEVH IPAANGRLIA EVHRDGEVLD QRADDDVIVL RARLDERTIG RLRQSGVRVI VTQGVTRSTS PNVAAVPLP // ID A0A143DES9_9PROT Unreviewed; 429 AA. AC A0A143DES9; DT 08-JUN-2016, integrated into UniProtKB/TrEMBL. DT 08-JUN-2016, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=AY555_08310 {ECO:0000313|EMBL:AMW35176.1}; OS Haematospirillum jordaniae. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales; OC Rhodospirillaceae; Haematospirillum. OX NCBI_TaxID=1549855 {ECO:0000313|EMBL:AMW35176.1, ECO:0000313|Proteomes:UP000076066}; RN [1] {ECO:0000313|EMBL:AMW35176.1, ECO:0000313|Proteomes:UP000076066} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=H5569 {ECO:0000313|EMBL:AMW35176.1, RC ECO:0000313|Proteomes:UP000076066}; RA Nicholson A.C., Humrighouse B.W., Loparov V., McQuiston J.R.; RT "Complete Genome of H5569, the type strain of the newly described RT species Haematospirillium jordaniae."; RL Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP014525; AMW35176.1; -; Genomic_DNA. DR RefSeq; WP_066135525.1; NZ_CP014525.1. DR EnsemblBacteria; AMW35176; AMW35176; AY555_08310. DR KEGG; hjo:AY555_08310; -. DR KO; K03665; -. DR Proteomes; UP000076066; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000076066}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000076066}. FT DOMAIN 207 372 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 429 AA; 46914 MW; 4060311714CE0165 CRC64; MDSDRSAVSG RSKSAVLCPF LKKTASGARA PEARLAEAVG LARAIDLDIV LSEVALVSAI RPATYVGGGL VERLAPVLDD LDVDIVVVDA RLSPVQQRNL EKAWGTKVID RTGLILEIFG ARARTREGQL QVELAHLEYQ KSRLVRSWTH LERQRGGFGF MGGPGESQIE IDRRLIGDRI VRLKKDLESV KRTRTLHRKA RKRTPFPIVA LVGYTNAGKS TLFNQMTRAA VMAEDQLFAT LDPTMRALQL PSGRTVILSD TVGFVSDLPH ELVAAFHATL EEVLEADLII HVRDCAHPDS ESQKRDVEKV LRDELGLDPA VEGRVVEVLN KADLLLESSV DPDTGALLLS ALSGDGVGNV LHRIDDCLAL ARVAVELVVP PSDGKMLAWI YRKGEVLSRE DHEEGVRLIV RLDPADAGRL ATRTTSLPD // ID A0A143HFE9_9BACL Unreviewed; 421 AA. AC A0A143HFE9; DT 08-JUN-2016, integrated into UniProtKB/TrEMBL. DT 08-JUN-2016, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=ATY39_12870 {ECO:0000313|EMBL:AMX00221.1}; OS Rummeliibacillus stabekisii. OC Bacteria; Firmicutes; Bacilli; Bacillales; Planococcaceae; OC Rummeliibacillus. OX NCBI_TaxID=241244 {ECO:0000313|EMBL:AMX00221.1, ECO:0000313|Proteomes:UP000076021}; RN [1] {ECO:0000313|Proteomes:UP000076021} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=PP9 {ECO:0000313|Proteomes:UP000076021}; RA Ploux O.; RL Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP014806; AMX00221.1; -; Genomic_DNA. DR RefSeq; WP_066790374.1; NZ_CP014806.1. DR KEGG; rst:ATY39_12870; -. DR KO; K03665; -. DR Proteomes; UP000076021; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000076021}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000076021}. FT DOMAIN 200 368 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 159 193 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 421 AA; 47975 MW; 9740304B2AF63F38 CRC64; MEELQEKAVL VGVNLHNDLH FDYSIEELGN LAEALNVEVV GVVTQNLERV NPSHYVGTGK IEEIKRYYEA VDANLVIFDD ELSPSQIRNL ERDLECKVID RTMLILDIFA RRAKSKEAQM QVELAQLQYM LPRLVGLRDS LSRQGGGTGG GFKNRGAGET KLELDRRKIE DQIAKLHKEL VSVKEQRETQ RKQRRKSEIP IVSIVGYTNA GKSTIMNQLL QNSSQEEHKQ VFEKNMLFAT LETSVRQISL PDNKSFLLTD TVGFVSKLPH HLVKAFRSTL EEARDADLLL HVVDASNPEN QYMMEVTNDT LEAVGVVDVP TINVFNKADL ANLAYPYTNH NQIWMSAKER KGIDELLQLI RSHIFKDYVT CTLCIPYEKG EIVSYLNEYA HILETSYEES GTVVKAEVKE AIMQKYKQYL I // ID A0A143HJC4_9GAMM Unreviewed; 438 AA. AC A0A143HJC4; DT 08-JUN-2016, integrated into UniProtKB/TrEMBL. DT 08-JUN-2016, sequence version 1. DT 30-AUG-2017, entry version 14. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=A3224_01160 {ECO:0000313|EMBL:AMX01372.1}, GN SAMN05660479_01557 {ECO:0000313|EMBL:SFC34681.1}; OS Microbulbifer thermotolerans. OC Bacteria; Proteobacteria; Gammaproteobacteria; Cellvibrionales; OC Microbulbiferaceae; Microbulbifer. OX NCBI_TaxID=252514 {ECO:0000313|EMBL:AMX01372.1, ECO:0000313|Proteomes:UP000076077}; RN [1] {ECO:0000313|EMBL:AMX01372.1, ECO:0000313|Proteomes:UP000076077} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DAU221 {ECO:0000313|EMBL:AMX01372.1, RC ECO:0000313|Proteomes:UP000076077}; RA Ploux O.; RL Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:SFC34681.1, ECO:0000313|Proteomes:UP000181967} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 19189 {ECO:0000313|EMBL:SFC34681.1, RC ECO:0000313|Proteomes:UP000181967}; RA de Groot N.N.; RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP014864; AMX01372.1; -; Genomic_DNA. DR EMBL; FOKT01000004; SFC34681.1; -; Genomic_DNA. DR RefSeq; WP_067150378.1; NZ_CP014864.1. DR EnsemblBacteria; AMX01372; AMX01372; A3224_01160. DR KEGG; mthd:A3224_01160; -. DR KO; K03665; -. DR Proteomes; UP000076077; Chromosome. DR Proteomes; UP000181967; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000076077}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000076077}. FT DOMAIN 199 366 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 158 192 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 438 AA; 48955 MW; 55D206E10F55EDD9 CRC64; MFFERPESGE LAVLVHLELS AIDSPDDPRE FEELALSAGA DPVAFIFGQR AAPDPKTFVG RGKLEDIRQA VVDHGAELVI FDHALSPSQE RNIERELKCR VLDRTGLILD IFAQRARTHE GKLQVELAQL RHMATRLVRG WTHLERQKGG IGLRGPGETQ LETDRRLLRA RIDSIEKKLE KVRRQREQGR RARSRAEVAT VSLVGYTNAG KSTLFNRLTD AGVYVRDQLF ATLDPTMRRV ELPSVGAMIL ADTVGFVSHL PHKLVEAFRA TLEEAGNATL LLHVVDAAAE DRLHLMEEVQ NVLEEIGAAE LPQLFVFNKI DLLADSEPRI ERDDQGQPRA VWLSAASGAG CDMLVDAIAE RLGEQMVSGL LLIPPQHSRL RAQLYAINAV QSERYRDNGD CELQLLLPRG ELQRLLAPYR DGDQAPQWQP REAVGDHC // ID A0A143PS01_9BACT Unreviewed; 432 AA. AC A0A143PS01; DT 08-JUN-2016, integrated into UniProtKB/TrEMBL. DT 08-JUN-2016, sequence version 1. DT 30-AUG-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:AMY10609.1}; GN ORFNames=LuPra_03847 {ECO:0000313|EMBL:AMY10609.1}; OS Luteitalea pratensis. OC Bacteria; Acidobacteria; Acidobacteria subdivision 6; Luteitalea. OX NCBI_TaxID=1855912 {ECO:0000313|EMBL:AMY10609.1, ECO:0000313|Proteomes:UP000076079}; RN [1] {ECO:0000313|Proteomes:UP000076079} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 100886 HEG_-6_39 {ECO:0000313|Proteomes:UP000076079}; RA Huang S., Vieira S., Bunk B., Riedel T., Sproeer C., Overmann J.; RT "First Complete Genome Sequence of a Subdivision 6 Acidobacterium."; RL Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP015136; AMY10609.1; -; Genomic_DNA. DR EnsemblBacteria; AMY10609; AMY10609; LuPra_03847. DR KEGG; abac:LuPra_03847; -. DR PATRIC; fig|1813736.3.peg.4053; -. DR KO; K03665; -. DR Proteomes; UP000076079; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000076079}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000076079}. FT DOMAIN 210 375 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 432 AA; 47889 MW; BC4474F8293F25E1 CRC64; MPSVTDVEGN GRGPEGRERA ALVGLITGDT RRTHVEDALE ELAGLADAAD IEPVLRFTQD RNRPDPATLI GSGKLEMLKA ACQESDLSLA IFDNELTPAQ LRNIEKILEL RVIDRTQLIL DIFARRARTR EGKLQVELAQ LRYLLPRLVG ASAALSRLGG GIGTRGPGET KLETDRRRIR LRIGTLTDDL AEVRRRRGQL RDRRRRSEMP AVALVGYTNA GKTTLFNRLT HDTAVASDAL FVTLDPLTRE LKLPNRQHAA LSDTVGFIDR LPHTLVAAFR ATLEEVADAD LLLHVVDASI DDYERHMQAV DRVLGEVDAG DVPMLLVFNK ADRLDEGARE HLRQAYEGSL QISALTGDGV AGLLTEIARA LALDTRRVTL SFDQARPEDR EAIERLYRVA RVLSHDADGD RVSIEAEVPR RLMQRLQEGL SL // ID A0A143Q8S9_9NOCA Unreviewed; 485 AA. AC A0A143Q8S9; DT 08-JUN-2016, integrated into UniProtKB/TrEMBL. DT 08-JUN-2016, sequence version 1. DT 07-JUN-2017, entry version 10. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:AMY18862.1}; GN ORFNames=A3Q40_01472 {ECO:0000313|EMBL:AMY18862.1}; OS Rhodococcus sp. PBTS 1. OC Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae; OC Rhodococcus. OX NCBI_TaxID=1653478 {ECO:0000313|EMBL:AMY18862.1, ECO:0000313|Proteomes:UP000076180}; RN [1] {ECO:0000313|Proteomes:UP000076180} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=PBTS 1 {ECO:0000313|Proteomes:UP000076180}; RA Stamer R., Vereecke D., Zhang Y., Schilkey F., Devitt N., Randall J.; RT "Complete Genome and Plasmid Sequences for Rhodococcus fascians D188 RT and Draft Sequences for Rhodococcus spp. Isolates PBTS 1 and PBTS 2."; RL Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP015219; AMY18862.1; -; Genomic_DNA. DR RefSeq; WP_068100809.1; NZ_CP015219.1. DR EnsemblBacteria; AMY18862; AMY18862; A3Q40_01472. DR PATRIC; fig|1653478.3.peg.1478; -. DR Proteomes; UP000076180; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000076180}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000076180}. FT DOMAIN 261 430 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 220 254 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 485 AA; 52407 MW; B543598DC5B8D965 CRC64; MTTTNAQPTR SETPRADADE AHENTWSTGE MQLEDRSALR RVAGLSTELT DITEVEYRQL RLERVVLVGV WTSGSAEEAE SSMTELAALA ETAGSEVLEG LVQRRDRPDA STYIGSGKAK ELREVVIATG ADTVICDGEL TPAQLTALEK IVKVKVIDRT ALILDIFAQH ASSREGKAQV ALAQMEYMLP RLRGWGESMS RQAGGRAGSN GGVGLRGPGE TKIETDRRRI RERMAKLRRE IRGMKQARDT KRERRLQGNV PSVAIVGYTN AGKSSLLNAL TGSGVLVQNA LFATLDPTTR KATLDDGREC VLTDTVGFVR HLPTQLVEAF RSTLEEVVDG DLLMHVVDGS DALPIGQIEA VREVIVEVIR EQNAAAPEEL IVVNKIDAAD PVTLTQLRGL LPGAVFVSAK TGEGIDELRT RLGELVRPPE VSVSVLVPYD RGDLVSRIHA DGRIASTSHE SGGTRIDATV PTALASQLAR YAHSA // ID A0A143YUS7_9LACT Unreviewed; 419 AA. AC A0A143YUS7; DT 08-JUN-2016, integrated into UniProtKB/TrEMBL. DT 08-JUN-2016, sequence version 1. DT 07-JUN-2017, entry version 10. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=TR210_1489 {ECO:0000313|EMBL:CZQ97640.1}; OS Trichococcus ilyis. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Carnobacteriaceae; OC Trichococcus. OX NCBI_TaxID=640938 {ECO:0000313|EMBL:CZQ97640.1, ECO:0000313|Proteomes:UP000076878}; RN [1] {ECO:0000313|EMBL:CZQ97640.1, ECO:0000313|Proteomes:UP000076878} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Trichococcus_R210 {ECO:0000313|EMBL:CZQ97640.1}; RA Wen L., He K., Yang H.; RL Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; FJNB01000010; CZQ97640.1; -; Genomic_DNA. DR RefSeq; WP_068622897.1; NZ_FJNB01000010.1. DR EnsemblBacteria; CZQ97640; CZQ97640; TR210_1489. DR Proteomes; UP000076878; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000076878}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000076878}. FT DOMAIN 197 358 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 419 AA; 47662 MW; D0F18003E8404966 CRC64; MENTREKVIL VNVQTDQTDE AFEYELRELA ELTETALGEV VGVLTQKRER KDSRTVIGKG KLEELVNLCA ELDADTVIFQ QELSSKQVRN IQESVDCKVI DRVQLILDIF AMRARSKEGK LQVALAQLSY LLPRLMGQGV NLSRLGGGIG TRGPGETKLE SDRRHIHSQM QEIKKTLEET ELHRQRAREK RHASEVFQIG LIGYTNAGKS TIINRLTDAG TLEEDKLFAT LDPLTRKMTF PNQFQATITD TVGFIQDLPT QLIHAFHSTL EESRNMDVFL HVVDASTSFI DQHEKTVLEL LKDLDMDKTP LLTIYNKRDL AGPDFQPRLF PNIVISALDD ADINRLKDFL WDEIAKMLVP YTKDIDASGP EARTMNKMQQ ETFVESIEYI EETNAYRLRG YAKSNSKWLG DKKTDASDE // ID A0A145WXS1_9GAMM Unreviewed; 443 AA. AC A0A145WXS1; DT 08-JUN-2016, integrated into UniProtKB/TrEMBL. DT 08-JUN-2016, sequence version 1. DT 07-JUN-2017, entry version 10. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=AMD27_03035 {ECO:0000313|EMBL:AMW77968.1}; OS Acinetobacter sp. TGL-Y2. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Moraxellaceae; Acinetobacter. OX NCBI_TaxID=1407071 {ECO:0000313|EMBL:AMW77968.1, ECO:0000313|Proteomes:UP000076238}; RN [1] {ECO:0000313|EMBL:AMW77968.1, ECO:0000313|Proteomes:UP000076238} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=TGL-Y2 {ECO:0000313|EMBL:AMW77968.1, RC ECO:0000313|Proteomes:UP000076238}; RA Evans L.H., Alamgir A., Owens N., Weber N.D., Virtaneva K., RA Barbian K., Babar A., Rosenke K.; RL Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP015110; AMW77968.1; -; Genomic_DNA. DR RefSeq; WP_067656192.1; NZ_CP015110.1. DR EnsemblBacteria; AMW77968; AMW77968; AMD27_03035. DR KEGG; acv:AMD27_03035; -. DR KO; K03665; -. DR Proteomes; UP000076238; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000076238}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000076238}. FT DOMAIN 199 364 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 158 185 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 443 AA; 49742 MW; 158069D15F041152 CRC64; MEDFEQHQGS ERAVLVSVSV QILQDLDQEE FRLLAKSAGA DILEHVQAQR VKPDPKYFIG SGKAEEIAEL VKAIEADIVI FDHSLSPSQE RNLERVIQCR VIDRTRLILD IFAQRARTHE GKLQVELAQL DHLSSRLVGG RMGLDSQKGG IGLRGPGETQ LETDRRLLRL RISQLKEKLE KVRLTRIQGR AARQKASIPT VSLVGYTNAG KSTLFNILAE SDVYAADQLF ATLDPTLRRL NWDGIGALVL ADTVGFVRNL AHALVDSFKA TLEETLEATL LLHVIDSSSP DMLEQIEAVE KVLKEIGTDV PILRVYNKID QSGEDAKIIY AKPHQPDRVY VSAHSSQGLD LLKQAVQECL MGQIQSFDVV LKPEYGKLRT QLYALNVIQA ERHDDLGHLI LRVNMAPQKL EQLIRQAHLP LDEILGMKAE QFKRPLEEFE IED // ID A0A146G9M1_9BACT Unreviewed; 434 AA. AC A0A146G9M1; DT 08-JUN-2016, integrated into UniProtKB/TrEMBL. DT 08-JUN-2016, sequence version 1. DT 07-JUN-2017, entry version 10. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=TSACC_21944 {ECO:0000313|EMBL:GAT33527.1}; OS Terrimicrobium sacchariphilum. OC Bacteria; Verrucomicrobia; Spartobacteria; Terrimicrobium. OX NCBI_TaxID=690879 {ECO:0000313|EMBL:GAT33527.1, ECO:0000313|Proteomes:UP000076023}; RN [1] {ECO:0000313|EMBL:GAT33527.1, ECO:0000313|Proteomes:UP000076023} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NM-5 {ECO:0000313|EMBL:GAT33527.1, RC ECO:0000313|Proteomes:UP000076023}; RA Qiu Y., Matsuura N., Ohashi A., Tourlousse M.D., Sekiguchi Y.; RT "Draft genome sequence of Terrimicrobium sacchariphilum strain NM-5."; RL Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:GAT33527.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BDCO01000002; GAT33527.1; -; Genomic_DNA. DR RefSeq; WP_075079253.1; NZ_BDCO01000002.1. DR EnsemblBacteria; GAT33527; GAT33527; TSACC_21944. DR Proteomes; UP000076023; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000076023}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000076023}. FT DOMAIN 204 370 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 163 197 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 434 AA; 49130 MW; D28F4E80C06EF5A9 CRC64; MFEIKAREKM VERALLVGAF TGNDLEDEAQ DLLSELEELV RTLGVPVREK MLVYHREPQS RYLIGSGKAE EIADRIKELD CDVLIFDNEL TPAQQRNWED LTKVLVIDRQ EIILDIFGAR AQTREAKIQV DLARMAYSLP RLTKAWSHLG QQGGGIGAKG EGESQLEQDR RKIRGQIDRL RRELQSVRKA RATQRKDRKR TPVPNAAIVG YTNAGKSSLL RRLTGAEVLV EDKLFATLDT TTRKIALPNK QPLLLTDTVG FVRKLPHQLV EAFHATLEEA TMSDFLIHVL DASNPRVMEY YNTTMKVLEE LGADTKKTLV VFNKMDKVSD PSTRAVLRRH FPEAVFVSVH SGDGIDALVN RIGDFVSDQV QETMLHIPTH RGDLLARLHR EAQIHEMAYE PEYAMVRASV PARLLEILTE FIVTPAKEST SLPR // ID A0A146GCH5_9BACT Unreviewed; 427 AA. AC A0A146GCH5; DT 08-JUN-2016, integrated into UniProtKB/TrEMBL. DT 08-JUN-2016, sequence version 1. DT 07-JUN-2017, entry version 10. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=TSACC_22919 {ECO:0000313|EMBL:GAT34494.1}; OS Terrimicrobium sacchariphilum. OC Bacteria; Verrucomicrobia; Spartobacteria; Terrimicrobium. OX NCBI_TaxID=690879 {ECO:0000313|EMBL:GAT34494.1, ECO:0000313|Proteomes:UP000076023}; RN [1] {ECO:0000313|EMBL:GAT34494.1, ECO:0000313|Proteomes:UP000076023} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NM-5 {ECO:0000313|EMBL:GAT34494.1, RC ECO:0000313|Proteomes:UP000076023}; RA Qiu Y., Matsuura N., Ohashi A., Tourlousse M.D., Sekiguchi Y.; RT "Draft genome sequence of Terrimicrobium sacchariphilum strain NM-5."; RL Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:GAT34494.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BDCO01000002; GAT34494.1; -; Genomic_DNA. DR RefSeq; WP_075080120.1; NZ_BDCO01000002.1. DR EnsemblBacteria; GAT34494; GAT34494; TSACC_22919. DR Proteomes; UP000076023; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000076023}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000076023}. FT DOMAIN 202 368 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 161 188 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 427 AA; 48382 MW; 8985AAD611D91A6A CRC64; MTDSRRSPHE KTILVGLERE GVTRWDVEDS LTELRQLAAT AGAQVVDTVV QKLDRPTAPY YIGKGKAEEV ARKCGEAQVT ALIFDDELSP AQGRNLEMLT SRKVLDRTQL ILDIFARRAR TREGRLQIEL AQLQYLLPRL TRMWTHLSRQ SGGIGTRGPG ETQLEVDRRR VQERIARLER DLKEVRRHRT VQREGRLRRN WPVAALVGYT NAGKSSLLNR LTNAGVLSED KLFATLDPTT RQMMLPNRQR ILLTDTVGFI RKLPHTVIES FKATLEEVQL ADLLIHVVDL SHPQCREQMA AVDATIAELG AHGKQTLVVF NKIDAIGDRE VIEGYLRFYP GSVAISARTG EGMDEFFQEL ELRLSSWRMR ARFRIPNTES AVLAELHRVG HVLSMEYEGD EALVTAHVPP ELKFRLAPYD IETSPSV // ID A0A147ED54_9SPHN Unreviewed; 444 AA. AC A0A147ED54; DT 08-JUN-2016, integrated into UniProtKB/TrEMBL. DT 08-JUN-2016, sequence version 1. DT 07-JUN-2017, entry version 9. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=NS277_13705 {ECO:0000313|EMBL:KTR82343.1}; OS Novosphingobium barchaimii. OC Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales; OC Sphingomonadaceae; Novosphingobium. OX NCBI_TaxID=1420591 {ECO:0000313|EMBL:KTR82343.1, ECO:0000313|Proteomes:UP000071549}; RN [1] {ECO:0000313|EMBL:KTR82343.1, ECO:0000313|Proteomes:UP000071549} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NS277 {ECO:0000313|EMBL:KTR82343.1, RC ECO:0000313|Proteomes:UP000071549}; RX PubMed=26793183; RA Midha S., Bansal K., Sharma S., Kumar N., Patil P.P., Chaudhry V., RA Patil P.B.; RT "Genomic Resource of Rice Seed Associated Bacteria."; RL Front. Microbiol. 6:1551-1551(2016). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KTR82343.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LDRW01000024; KTR82343.1; -; Genomic_DNA. DR RefSeq; WP_058737654.1; NZ_LDRW01000024.1. DR EnsemblBacteria; KTR82343; KTR82343; NS277_13705. DR PATRIC; fig|1420591.5.peg.1707; -. DR Proteomes; UP000071549; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000071549}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000071549}. FT DOMAIN 206 389 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 444 AA; 48897 MW; 79C0159E0F757D29 CRC64; MNDELQGEVT RGARAVVVYP QMRTNRDQDA DARLEEGKGL ALAIGLEIAD AFTIPIREPR AATLFGEGQI QNIAIACEQS EAELVVVDGS LSAIQQRNLE EKLKRKVIDR TGLILEIFGE RAATAEGRLQ VELAHLDYQA GRLVRSWTHL ERQRGGFGFL GGPGETQIEA DRRLIRDRMA RIRRELEQVR RTRGLHRDRR EKAPWPVVAL VGYTNAGKST LFNRLTGADV MAEDLLFATL DPTMRAIRLP GVEKAILSDT VGFISDLPTQ LVAAFRATLE EVTAADIILH VRDIANSETE AQKRQVLEIL TDLGVIPEDG GEPEKGGESG IPILEIWNKW DLLDPDHAEE LSGLISDKSD RDVVPISALT GEGCETLLAT VGEKLMAGAK LYSFAVPAED GERLAFLHAR GHVVSETIDE GDQTPVVRLQ VRLSDRELGR FSAL // ID A0A147EQM3_9MICO Unreviewed; 490 AA. AC A0A147EQM3; DT 08-JUN-2016, integrated into UniProtKB/TrEMBL. DT 08-JUN-2016, sequence version 1. DT 07-JUN-2017, entry version 9. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=NS354_03340 {ECO:0000313|EMBL:KTR86799.1}; OS Leucobacter chromiiresistens. OC Bacteria; Actinobacteria; Micrococcales; Microbacteriaceae; OC Leucobacter. OX NCBI_TaxID=1079994 {ECO:0000313|EMBL:KTR86799.1, ECO:0000313|Proteomes:UP000070810}; RN [1] {ECO:0000313|EMBL:KTR86799.1, ECO:0000313|Proteomes:UP000070810} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NS354 {ECO:0000313|EMBL:KTR86799.1, RC ECO:0000313|Proteomes:UP000070810}; RX PubMed=26793183; RA Midha S., Bansal K., Sharma S., Kumar N., Patil P.P., Chaudhry V., RA Patil P.B.; RT "Genomic Resource of Rice Seed Associated Bacteria."; RL Front. Microbiol. 6:1551-1551(2016). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KTR86799.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LDRK01000015; KTR86799.1; -; Genomic_DNA. DR RefSeq; WP_058593210.1; NZ_LDRK01000015.1. DR EnsemblBacteria; KTR86799; KTR86799; NS354_03340. DR PATRIC; fig|1079994.3.peg.656; -. DR Proteomes; UP000070810; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000070810}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000070810}. FT DOMAIN 272 437 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 490 AA; 53602 MW; 01FE5A25BB47C191 CRC64; MLARAAGAGS ATVIRDLTSG AQALGDADHD RLEGDLDAIR MEREDRASLK RVVGLSTELE DVTEVEYRQL RLENVVLIGV YSQRSAEDAE NSLRELSALA ETAGARVLDG LLQRRAHPDP ATYLGKGKAQ ELAELVAAVG ADTVIADTEL APSQRRALED VVKVKVIDRT AVILDIFSQH AKSREGKAQV ELAQLQYLLP RLRGWGESMS RQAGGQVGSG GAGMGSRGPG ETKMELDRRK IHIRMSKLRK QIAGFAPARE AKRANRKRGE VPSVAIAGYT NAGKSSLLNR LTGTQELVQN QLFATLDTAI RHGETEDGRR FTYADTVGFV RNLPHQLVEA FRSTFEEVGD ASVILHVVDG SHPDPEAQLR TVRDVIAEVE AQDITELVAF NKADLLDDSQ RLVLHGLVPD AVFVSARTGE GIEELKRRID AALPVPDREI TVVVPYDRGE LVAELHERNR VLETEYVETG TRVRAYVTAE TASKLEQYLS // ID A0A147H1P0_9BURK Unreviewed; 394 AA. AC A0A147H1P0; DT 08-JUN-2016, integrated into UniProtKB/TrEMBL. DT 08-JUN-2016, sequence version 1. DT 07-JUN-2017, entry version 9. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=NS331_06990 {ECO:0000313|EMBL:KTT23745.1}; OS Pseudacidovorax intermedius. OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Comamonadaceae; Pseudacidovorax. OX NCBI_TaxID=433924 {ECO:0000313|EMBL:KTT23745.1, ECO:0000313|Proteomes:UP000072741}; RN [1] {ECO:0000313|EMBL:KTT23745.1, ECO:0000313|Proteomes:UP000072741} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NS331 {ECO:0000313|EMBL:KTT23745.1, RC ECO:0000313|Proteomes:UP000072741}; RX PubMed=26793183; RA Midha S., Bansal K., Sharma S., Kumar N., Patil P.P., Chaudhry V., RA Patil P.B.; RT "Genomic Resource of Rice Seed Associated Bacteria."; RL Front. Microbiol. 6:1551-1551(2016). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KTT23745.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LDSL01000047; KTT23745.1; -; Genomic_DNA. DR RefSeq; WP_058641278.1; NZ_LDSL01000047.1. DR EnsemblBacteria; KTT23745; KTT23745; NS331_06990. DR PATRIC; fig|433924.3.peg.3345; -. DR Proteomes; UP000072741; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000072741}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000072741}. FT DOMAIN 207 380 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 394 AA; 43775 MW; BC57F135A9735019 CRC64; MNQAPPHLSE AIPRQEGAVV LIGVDFGLPH FDAELEELGL LAQTAGLEPV ARLVCKRKAP DAALFVGSGK AQEIRELAEL YRASEVIFDQ ALSPAQQRNL ERELGVAVYD RTFLILEIFA QRARSHEGKL QVELARLQYL STRLVRRWSH LERQTGGAGV RGGPGEKQIE LDRRMIDSSI KRTRERLARV QKQRGTQRRQ RERRDTFNIS LVGYTNAGKS SLFNALVKAR AYAADQLFAT LDTTTRHLYL GDVGRRVSIS DTVGFIRELP HGLVDAFRAT LQEAVDADLL LHVVDAANPH HPEQIAEVQQ VLADIGADDV PQLMVFNKLD ALPEERRPLK LADAMEIDGL AVPRLFLSAR GGEGLPALRE ELARRAAEAA ITPWPQSELQ SADH // ID A0A147JSS6_9EURY Unreviewed; 355 AA. AC A0A147JSS6; DT 08-JUN-2016, integrated into UniProtKB/TrEMBL. DT 08-JUN-2016, sequence version 1. DT 12-APR-2017, entry version 8. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=AVW05_04400 {ECO:0000313|EMBL:KUO39491.1}; OS Hadesarchaea archaeon DG-33. OC Archaea; Euryarchaeota; Hadesarchaea. OX NCBI_TaxID=1775754 {ECO:0000313|EMBL:KUO39491.1, ECO:0000313|Proteomes:UP000071776}; RN [1] {ECO:0000313|EMBL:KUO39491.1, ECO:0000313|Proteomes:UP000071776} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DG-33 {ECO:0000313|EMBL:KUO39491.1}; RA Baker B.J., Saw J.H., Lind A.E., Lazar C.S., Hinrichs K.-U., RA Teske A.P., Ettema T.J.; RT "Genomic inference of the metabolism of Hadesarchaea, cosmopolitan RT subsurface Archaea."; RL Nat. Microbiol. 0:0-0(2016). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KUO39491.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LQHI01000055; KUO39491.1; -; Genomic_DNA. DR Proteomes; UP000071776; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000071776}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000071776}. FT DOMAIN 186 352 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 355 AA; 40003 MW; 59D899B9803FEE61 CRC64; MRVVLAERRS PGERSSLEEL AALARTLNHE VVGVLEQVRK PDPAYLIGKG KAQELADLTR SKGANRVVFN NQLTPSQAYK LSRLVGVEVI DRFQLILEIF AMRAGSPEAK LQVEYARLSY EMPRIREQVR ALMSVEQPGL MGGGEYEVDV RYDMVKRKLV NLRRKLKSIA SVREQRRKRR HRRGFKLVAL AGYTNAGKST LLNALTAAKA EVDDMLFTTL MPRTRAMRAS RMILLTDTVG FIDGLPPWLV EAFKATLEEI YLADLVVLVF DVAEPLPEIL RKFRASREVL AEYPVKVVAA LNKADLIPRE ELERKLKTLN DVTMFAIPIS ALKHTNLSSL IEIIRTNVSG SREPA // ID A0A147JTT8_9EURY Unreviewed; 351 AA. AC A0A147JTT8; DT 08-JUN-2016, integrated into UniProtKB/TrEMBL. DT 08-JUN-2016, sequence version 1. DT 10-MAY-2017, entry version 9. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=AVW06_03255 {ECO:0000313|EMBL:KUO39864.1}; OS Hadesarchaea archaeon DG-33-1. OC Archaea; Euryarchaeota; Hadesarchaea. OX NCBI_TaxID=1775755 {ECO:0000313|EMBL:KUO39864.1, ECO:0000313|Proteomes:UP000075113}; RN [1] {ECO:0000313|EMBL:KUO39864.1, ECO:0000313|Proteomes:UP000075113} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DG-33-1 {ECO:0000313|EMBL:KUO39864.1}; RA Baker B.J., Saw J.H., Lind A.E., Lazar C.S., Hinrichs K.-U., RA Teske A.P., Ettema T.J.; RT "Genomic inference of the metabolism of Hadesarchaea, cosmopolitan RT subsurface Archaea."; RL Nat. Microbiol. 0:0-0(2016). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KUO39864.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LQHJ01000038; KUO39864.1; -; Genomic_DNA. DR Proteomes; UP000075113; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000075113}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000075113}. FT DOMAIN 186 351 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 351 AA; 39331 MW; 06E0DE1A7998D01F CRC64; MRVILVERRM PNDPSRLEEL ATLARTLGHE VVAKLEQVRR PDPAYHIGSG KAKELGELVK SISAERVIFE NQLTPSQAFK LSKLIGVEVI DKFQLILEIF AMRAGSPEAK LQVEYAKLSY ELPRVRERIR TLMSVEQPGL RGGGEYEVDV HYDMIKRRMV SLRRKLASVA KSREQRRKLR RRRGFNLVAI AGYTNAGKST LLNALTASNV EVDDMLFTTL TPRTRVVKSG QKILLTDTVG FIDGLPPWLI EAFKATLEEI YLADLVVLMV DISEPLHETL RKLKAARDIL AEYPVKVIAA FNKIDIVSQP ELERRLEVLS GIAPAAVPIS AINGTNLDLL LDAVRESIFG S // ID A0A147JWK7_9EURY Unreviewed; 348 AA. AC A0A147JWK7; DT 08-JUN-2016, integrated into UniProtKB/TrEMBL. DT 08-JUN-2016, sequence version 1. DT 10-MAY-2017, entry version 9. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=APZ16_02160 {ECO:0000313|EMBL:KUO40821.1}; OS Hadesarchaea archaeon YNP_45. OC Archaea; Euryarchaeota; Hadesarchaea. OX NCBI_TaxID=1776334 {ECO:0000313|EMBL:KUO40821.1, ECO:0000313|Proteomes:UP000074294}; RN [1] {ECO:0000313|EMBL:KUO40821.1, ECO:0000313|Proteomes:UP000074294} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=YNP_45 {ECO:0000313|EMBL:KUO40821.1}; RA Baker B.J., Saw J.H., Lind A.E., Lazar C.S., Hinrichs K.-U., RA Teske A.P., Ettema T.J.; RT "Genomic inference of the metabolism of cosmopolitan subsurface RT Archaea, Hadesarchaea."; RL Nat. Microbiol. 0:0-0(2016). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KUO40821.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LQMQ01000034; KUO40821.1; -; Genomic_DNA. DR Proteomes; UP000074294; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000074294}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000074294}. FT DOMAIN 186 348 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 152 182 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 348 AA; 39545 MW; CCCC8AD35A4FD284 CRC64; MRVVLVERLT PGEQSRLNEL EALVRTLGYE VVGALQQVRQ PDPAYQIGRG KAKELAELVK STGADRVVFR NQLTPSQAYK LSRLVGVEVV DRFQIVLEIF AMRAGSPEAK LQIEYARLKY ELPKIREQVK ALLSVEQPGF RGGGEYEVKV RYDMIKRKLA NLRRKLRSIE KTREERRKFR RKRGFKLVAL AGYTNSGKST LLNALTDAKA EVDDMYFTTL MPRTRALKAS RMILLTDTVG FIDDLPPWLF EAFKATLEEI YLADLVVLLV DASDSVPEMI RKLRTSQKVL EEYSVKTITA LNKIDLVSKE DLERKMEVLH SMTNTVVPIS AAHGINLDAL LEVIRAHT // ID A0A147K2P0_9EURY Unreviewed; 349 AA. AC A0A147K2P0; DT 08-JUN-2016, integrated into UniProtKB/TrEMBL. DT 08-JUN-2016, sequence version 1. DT 12-APR-2017, entry version 8. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=APU95_05100 {ECO:0000313|EMBL:KUO43109.1}; OS Hadesarchaea archaeon YNP_N21. OC Archaea; Euryarchaeota; Hadesarchaea. OX NCBI_TaxID=1776333 {ECO:0000313|EMBL:KUO43109.1, ECO:0000313|Proteomes:UP000074447}; RN [1] {ECO:0000313|EMBL:KUO43109.1, ECO:0000313|Proteomes:UP000074447} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=YNP_N21 {ECO:0000313|EMBL:KUO43109.1}; RA Baker B.J., Saw J.H., Lind A.E., Lazar C.S., Hinrichs K.-U., RA Teske A.P., Ettema T.J.; RT "Genomic inference of the metabolism of cosmopolitan subsurface RT Archaea, Hadesarchaea."; RL Nat. Microbiol. 0:0-0(2016). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KUO43109.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LQMP01000008; KUO43109.1; -; Genomic_DNA. DR Proteomes; UP000074447; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000074447}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000074447}. FT DOMAIN 177 349 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 349 AA; 39406 MW; DC3A208C2E11B6F8 CRC64; MQHESSRMAE LVELARTLNH QVLATVEQVR EPDPAFNIGR GKARELADLV KRLGAERVIF GNQLTPSQAF KLQQLIGVEV IDRFQLILEI FAMRAGSPEA KLQVEYARLS YELPRVRERI RALLSNEQPG LLGGGEYEVN VHYDAIKKRM VSLRKKLASI AKSREQRRKH RRRKGFKLVA LAGYTNAGKS TLMNALTRAN VEIDDLLFTT LTPKTRALKT GRKILLTDTV GFIDGLPPWL VEAFKATLEE IYLADLVVLV LDISEPIHEI LRKLRTSREV LSEYKVKVIT ALNKIDMLPP EELEYKLQVL GDAVQSPTPI SALKGLNIDH MINSICSNIM WEGEKPLAE // ID A0A147K917_9BACI Unreviewed; 416 AA. AC A0A147K917; DT 08-JUN-2016, integrated into UniProtKB/TrEMBL. DT 08-JUN-2016, sequence version 1. DT 07-JUN-2017, entry version 9. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=Q75_06935 {ECO:0000313|EMBL:KUP06814.1}; OS Bacillus coahuilensis p1.1.43. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus. OX NCBI_TaxID=1150625 {ECO:0000313|EMBL:KUP06814.1, ECO:0000313|Proteomes:UP000074108}; RN [1] {ECO:0000313|EMBL:KUP06814.1, ECO:0000313|Proteomes:UP000074108} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=p1.1.43 {ECO:0000313|Proteomes:UP000074108}; RX PubMed=26903955; DOI=10.3389/fmicb.2016.00058; RA Gomez-Lunar Z., Hernandez-Gonzalez I., Rodriguez-Torres M.D., RA Souza V., Olmedo-Alvarez G.; RT "Microevolution Analysis of Bacillus coahuilensis Unveils Differences RT in Phosphorus Acquisition Strategies and Their Regulation."; RL Front. Microbiol. 7:58-58(2016). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KUP06814.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LDYG01000026; KUP06814.1; -; Genomic_DNA. DR RefSeq; WP_059350867.1; NZ_LDYG01000026.1. DR EnsemblBacteria; KUP06814; KUP06814; Q75_06935. DR PATRIC; fig|1150625.3.peg.1455; -. DR Proteomes; UP000074108; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000074108}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000074108}. FT DOMAIN 198 360 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 416 AA; 46718 MW; A15483FAA329C1A5 CRC64; MSSVLNEKVI IVGVNIGLDE ERFLYSLSEL SSLTNTANGT VVATVTQNRH RVDTATYIGK GKVEELVILE EELEPDLIIF NDELTPSQVR NISTFVKAKV IDRTQLILDI FAQRARSKEG KLQVELAQLQ YLLPRLGGQG LVLSRLGGGI GTRGPGETKL ESDRRHIRRR IDDIKAQLSS VVKHRERYRA RRKKIMSFRS PIVGYTNAGK STWFNILSSA ESFEENLLFA TLDPMSRNMS LPLGYQCILT DTVGFIQDLP TTLIASFRST LEEVKGADLL VHIVDSSNTE FAHLERTVLD LLEELEMNTI PLLTVYNKSD QTAEGFIPIA SNDHIHVSAK SDQDPIIFKE AIQTQVLKQM DRYTALIPSK DGDILAYLKA ETIIKAMEYQ EESNSYQLIG YCLKDHPVNG VIKKYS // ID A0A148NB97_9GAMM Unreviewed; 420 AA. AC A0A148NB97; DT 08-JUN-2016, integrated into UniProtKB/TrEMBL. DT 08-JUN-2016, sequence version 1. DT 30-AUG-2017, entry version 9. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=AXA67_04040 {ECO:0000313|EMBL:KXJ41772.1}; OS Methylothermaceae bacteria B42. OC Bacteria; Proteobacteria; Gammaproteobacteria; Methylococcales; OC Methylothermaceae. OX NCBI_TaxID=1798802 {ECO:0000313|EMBL:KXJ41772.1, ECO:0000313|Proteomes:UP000074680}; RN [1] {ECO:0000313|EMBL:KXJ41772.1, ECO:0000313|Proteomes:UP000074680} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=B42 {ECO:0000313|EMBL:KXJ41772.1}; RX PubMed=26779119; DOI=10.3389/fmicb.2015.01425; RA Skennerton C.T., Ward L.M., Michel A., Metcalfe K., Valiente C., RA Mullin S., Chan K.Y., Gradinaru V., Orphan V.J.; RT "Genomic Reconstruction of an Uncultured Hydrothermal Vent RT Gammaproteobacterial Methanotroph (Family Methylothermaceae) Indicates RT Multiple Adaptations to Oxygen Limitation."; RL Front. Microbiol. 6:1425-1425(2015). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KXJ41772.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LSNW01000006; KXJ41772.1; -; Genomic_DNA. DR Proteomes; UP000074680; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000074680}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000074680}. FT DOMAIN 198 364 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 420 AA; 47166 MW; 90D35579ABC62B21 CRC64; MQFFERPGAG ERAVLVHLAT TFDAEDLNEL EALAQSAGAE PVAVIQGSRR QPDPRNFIGK GKLEELKRAV SEYDAQLVLF NHALTPSQER NLEKELAVRV VDRTGLILDI FAQRARSYEG KLQVELAQLR HLATRLVRGW THLERQKGGI GLRGPGETQL ETDRRLIGQR IRQIQQRLRK VAKQREQGRN ARKKAELPTV ALVGYTNAGK STLFNRMTQS RVYAADQLFA TLDSTLRRIE LGGGNAAILA DTVGFIRHLP HELVAAFRST LQETCEAEVV LHVIDASAER RQENIDAVNG VLKELGIDQN RVIEVFNKID QMQRPSRIDY DETGRPSRVW LSAKTGEGIE LLLQALTEVV AADKIRAKLH LVPAQGRLRA QLFRFGNVLR DEVGDDGGWD MEVELPRKHQ LLLDSIECQP // ID A0A149VWP2_9PROT Unreviewed; 409 AA. AC A0A149VWP2; DT 08-JUN-2016, integrated into UniProtKB/TrEMBL. DT 08-JUN-2016, sequence version 1. DT 07-JUN-2017, entry version 8. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX_2 {ECO:0000313|EMBL:KXW57629.1}; GN Synonyms=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=FEMY_18540 {ECO:0000313|EMBL:KXW57629.1}; OS Ferrovum sp. Z-31. OC Bacteria; Proteobacteria; Betaproteobacteria; Ferrovales; Ferrovaceae; OC Ferrovum. OX NCBI_TaxID=1789004 {ECO:0000313|EMBL:KXW57629.1, ECO:0000313|Proteomes:UP000075653}; RN [1] {ECO:0000313|EMBL:KXW57629.1, ECO:0000313|Proteomes:UP000075653} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Z-31 {ECO:0000313|EMBL:KXW57629.1, RC ECO:0000313|Proteomes:UP000075653}; RA Poehlein A., Ullrich S.R., Schloemann M., Muehling M., Daniel R.; RT "Genome sequence of the acidophilic iron oxidising Ferrovum strain Z- RT 31."; RL Submitted (JAN-2016) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KXW57629.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LRRD01000046; KXW57629.1; -; Genomic_DNA. DR EnsemblBacteria; KXW57629; KXW57629; FEMY_18540. DR PATRIC; fig|1789004.3.peg.1895; -. DR Proteomes; UP000075653; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000075653}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000075653}. FT DOMAIN 225 392 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 409 AA; 45042 MW; BA80230F4F9157BA CRC64; MTDLGPLLGR GRASARTKAG QGGLERVSEE VSANAQRVLL VRLVLGRGPV EFSLDELQRL AQSAGLTVVG WMEGRRERPD PSTFLGSGKV EEVAARVQAE AIGLVIVDDE LSPVQERNLE QRLGCRVIDR TSLILDIFAQ RARSHTGQLQ VELAQLKRLS TRLVRGWTHL ERQKGGIGLR GPGETQLETD RRLLAVRVKT LQSRLVKVRR TVQLQRRARQ RAGVLNVSLV GYTNAGKSTL FNRLTQGDSY VADQLFATLD TLTRRVYLAP GLQVTLSDTV GFVRRLPHTL VDAFRATLEE TREADLLVLV VDHADPEREA QIEAVNLVLA EIGADQVPQL RVYNKVDLLA QEGGRIERDA CGTISAVWAS ALTGMGLNEI RQAFLERCQS PGRPGELPVL QETQDSHGT // ID A0A149VXR6_9PROT Unreviewed; 435 AA. AC A0A149VXR6; DT 08-JUN-2016, integrated into UniProtKB/TrEMBL. DT 08-JUN-2016, sequence version 1. DT 07-JUN-2017, entry version 9. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX_1 {ECO:0000313|EMBL:KXW58020.1}; GN Synonyms=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=FEMY_14700 {ECO:0000313|EMBL:KXW58020.1}; OS Ferrovum sp. Z-31. OC Bacteria; Proteobacteria; Betaproteobacteria; Ferrovales; Ferrovaceae; OC Ferrovum. OX NCBI_TaxID=1789004 {ECO:0000313|EMBL:KXW58020.1, ECO:0000313|Proteomes:UP000075653}; RN [1] {ECO:0000313|EMBL:KXW58020.1, ECO:0000313|Proteomes:UP000075653} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Z-31 {ECO:0000313|EMBL:KXW58020.1, RC ECO:0000313|Proteomes:UP000075653}; RA Poehlein A., Ullrich S.R., Schloemann M., Muehling M., Daniel R.; RT "Genome sequence of the acidophilic iron oxidising Ferrovum strain Z- RT 31."; RL Submitted (JAN-2016) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KXW58020.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LRRD01000028; KXW58020.1; -; Genomic_DNA. DR RefSeq; WP_062188139.1; NZ_LRRD01000028.1. DR EnsemblBacteria; KXW58020; KXW58020; FEMY_14700. DR PATRIC; fig|1789004.3.peg.1497; -. DR Proteomes; UP000075653; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000075653}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000075653}. FT DOMAIN 214 384 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 172 206 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 435 AA; 48270 MW; EC3FD6B5C5EB45A2 CRC64; MQTEVKGKAA FAVVAAVQLP GVSDIEFEAS LAELRDLSKT LGYKVVRTFT QKRTAFDTSA YLGLGKRVEI RDFINGSEVP DSSIGTIDRV FVDHEISPSQ ARNLENDVGC DVMDRTMVIF SIFHRNARSR AAKAQVEIAR LGYMAPRLRE MAKLAGPQGR QRSGTGGRGA GESHTELDKR RIRDRIAELQ QEIAAMDVER KTQRSRRQER QGLASVALVG YTNAGKSTLM RALTGSEVLV ENKLFATLDT TVRTLYPESV PHVLVSDTVG FIKNLPHGLV ASFKSTLEEA LDASLLLHVI DASDPGFERQ LEVTDKVLAE ISAETVPRIR VFNKVDQVGD AVIQTEFEIM LRAQYPDCIV MSARRIDDVA TLHKAIVAFF RKDLIEAELF LPWSAQKLRG EIFSSCEVLE ERADIEGAFL RVRGTRGVLE KYTGL // ID A0A150AAF4_9BACT Unreviewed; 121 AA. AC A0A150AAF4; DT 08-JUN-2016, integrated into UniProtKB/TrEMBL. DT 08-JUN-2016, sequence version 1. DT 07-JUN-2017, entry version 5. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:KXX66879.1}; GN ORFNames=AVL50_30585 {ECO:0000313|EMBL:KXX66879.1}; OS Flammeovirga sp. SJP92. OC Bacteria; Bacteroidetes; Cytophagia; Cytophagales; Flammeovirgaceae; OC Flammeovirga. OX NCBI_TaxID=1775430 {ECO:0000313|EMBL:KXX66879.1, ECO:0000313|Proteomes:UP000075267}; RN [1] {ECO:0000313|EMBL:KXX66879.1, ECO:0000313|Proteomes:UP000075267} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SJP92 {ECO:0000313|EMBL:KXX66879.1, RC ECO:0000313|Proteomes:UP000075267}; RA Shamseldin A., Moawad H., Abd El-Rahim W.M., Sadowsky M.J.; RL Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KXX66879.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LQAQ01000116; KXX66879.1; -; Genomic_DNA. DR RefSeq; WP_062621730.1; NZ_LQAQ01000116.1. DR EnsemblBacteria; KXX66879; KXX66879; AVL50_30585. DR Proteomes; UP000075267; Unassembled WGS sequence. DR InterPro; IPR025121; GTPase_HflX_N. DR Pfam; PF13167; GTP-bdg_N; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000075267}; KW Reference proteome {ECO:0000313|Proteomes:UP000075267}. FT DOMAIN 66 113 GTP-bdg_N. {ECO:0000259|Pfam:PF13167}. SQ SEQUENCE 121 AA; 13692 MW; F6E24845982AE73B CRC64; MKSLTGYKII ISGLVSYKID LEEYLPSIKK RITELGGEIV GQHIQRRGVS RSRKLGGSKD LNKPLSTETY ISSGKVDELK EMVKQFDCDI VVFINDLTKS QINNLEKLTN TKVEIFQGQQ E // ID A0A150ANZ6_9BACT Unreviewed; 419 AA. AC A0A150ANZ6; DT 08-JUN-2016, integrated into UniProtKB/TrEMBL. DT 08-JUN-2016, sequence version 1. DT 07-JUN-2017, entry version 9. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=AVL50_04935 {ECO:0000313|EMBL:KXX71620.1}; OS Flammeovirga sp. SJP92. OC Bacteria; Bacteroidetes; Cytophagia; Cytophagales; Flammeovirgaceae; OC Flammeovirga. OX NCBI_TaxID=1775430 {ECO:0000313|EMBL:KXX71620.1, ECO:0000313|Proteomes:UP000075267}; RN [1] {ECO:0000313|EMBL:KXX71620.1, ECO:0000313|Proteomes:UP000075267} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SJP92 {ECO:0000313|EMBL:KXX71620.1, RC ECO:0000313|Proteomes:UP000075267}; RA Shamseldin A., Moawad H., Abd El-Rahim W.M., Sadowsky M.J.; RL Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KXX71620.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LQAQ01000019; KXX71620.1; -; Genomic_DNA. DR RefSeq; WP_062615544.1; NZ_LQAQ01000019.1. DR EnsemblBacteria; KXX71620; KXX71620; AVL50_04935. DR Proteomes; UP000075267; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000075267}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000075267}. FT DOMAIN 205 384 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 419 AA; 48213 MW; 22BF0E99C822E034 CRC64; MKKEFHHIRD NKAPQAVLVG LALKDQKVEK AQEYLDELAF LASTLGIETR KMFIQRLEHP DKKYFVGKGK LEEIMTYVKA EGIDTIIFDD DLSSAHSRNL DREVEDVMII DRSLLILQIF AMRAKSSQAK TQVELAQYQY MLPRLTNLWT HHSRQRGGVG MKGPGETELE TDKRIIRDKI SLLRKKLKKI AVQSDLRRKG RDKEVRVALV GYTNVGKSTI MRLLSKADVF AENKLFATVD STVRKITMNN VPFLMTDTVG FIRKLPTTLI ESFKSTLDEI VEADILIHVV DVSHESFEEH VTVVNNTLKE IKATDKPTLL VFNKVDSFEE KEYPPFEDHP PATIEEWKES YLAKENNSVF VSALKSEGVE ELKRKIFELV SDKFYKIYPN HHSFAYNQLW LKHGENWAEA LDNGEGLDE // ID A0A150KLT7_9BACI Unreviewed; 418 AA. AC A0A150KLT7; DT 08-JUN-2016, integrated into UniProtKB/TrEMBL. DT 08-JUN-2016, sequence version 1. DT 07-JUN-2017, entry version 10. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=B4102_3685 {ECO:0000313|EMBL:KYC94334.1}; OS Bacillus sporothermodurans. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus. OX NCBI_TaxID=46224 {ECO:0000313|EMBL:KYC94334.1, ECO:0000313|Proteomes:UP000075666}; RN [1] {ECO:0000313|EMBL:KYC94334.1, ECO:0000313|Proteomes:UP000075666} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=B4102 {ECO:0000313|EMBL:KYC94334.1, RC ECO:0000313|Proteomes:UP000075666}; RA Berendsen E.M., Wells-Bennik M.H., Krawcyk A.O., De Jong A., RA Holsappel S., Eijlander R.T., Kuipers O.P.; RT "Genome Sequences of Twelve Sporeforming Bacillus Species Isolated RT from Foods."; RL Submitted (JAN-2016) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KYC94334.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LQYN01000102; KYC94334.1; -; Genomic_DNA. DR RefSeq; WP_066235013.1; NZ_LQYN01000102.1. DR EnsemblBacteria; KYC94334; KYC94334; B4102_3685. DR PATRIC; fig|46224.3.peg.369; -. DR Proteomes; UP000075666; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000075666}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000075666}. FT DOMAIN 197 365 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 156 183 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 418 AA; 47707 MW; 26C688E7D689DBAD CRC64; MELREKAILV GVNLNHQDNF DYSMEELRNL TEACDIEVVG EITQNLQRIN KSHYVGTGKI DEIRALGEMV EANVIIFNDE LSPSQIRNLE ADIDCKVIDR TILILDIFAE RARTKEAQLQ VEVAQLQYML PRLVGLRASL GRQGGGSVLA NRGAGETKLE LDRRKIEAKI VALNKELEHL VAHRKTQRKQ RKKNDVPVVS LVGYTNAGKS TIMNALVEKF NPLENKQVFE KDMLFATLET SVRSISLADQ KSFLLTDTVG FVSKLPHHLV KAFRSTLEEV AESDLLIHVV DYSNPNYERL MDITNETLKD IGIENIPTIY AYNKSDLMDV QIPMIRGEDV FLSAKQRIGI DELIELIRKE IFTDYVQCEM LVPYDQGRII SYFKDHANVM GMSYEETGTK LVLECKESDY ERYKEFVI // ID A0A150M7D3_9BACI Unreviewed; 502 AA. AC A0A150M7D3; DT 08-JUN-2016, integrated into UniProtKB/TrEMBL. DT 08-JUN-2016, sequence version 1. DT 07-JUN-2017, entry version 8. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=B4135_1851 {ECO:0000313|EMBL:KYD20550.1}; OS Caldibacillus debilis. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Caldibacillus. OX NCBI_TaxID=301148 {ECO:0000313|EMBL:KYD20550.1, ECO:0000313|Proteomes:UP000075683}; RN [1] {ECO:0000313|EMBL:KYD20550.1, ECO:0000313|Proteomes:UP000075683} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=B4135 {ECO:0000313|EMBL:KYD20550.1, RC ECO:0000313|Proteomes:UP000075683}; RA Berendsen E.M., Wells-Bennik M.H., Krawcyk A.O., De Jong A., RA Holsappel S., Eijlander R.T., Kuipers O.P.; RT "Draft Genome Sequences of Seven Thermophilic Sporeformers Isolated RT from Foods."; RL Submitted (JAN-2016) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KYD20550.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LQYT01000034; KYD20550.1; -; Genomic_DNA. DR EnsemblBacteria; KYD20550; KYD20550; B4135_1851. DR PATRIC; fig|301148.3.peg.2882; -. DR Proteomes; UP000075683; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000075683}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000075683}. FT DOMAIN 280 442 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 502 AA; 56873 MW; 9B85DA12F1284B89 CRC64; MVRSGKSPAF LCSRRTRRTL CDSKRSIIAG IPMFPEETRV FLLSAARIPL QKDPICFFGR GQVIMGIDLR SGRHSFCKFH AENGGTMEKA ILVGCQLPNT DDSRFSYSME ELRSLADTAQ FRTAAVLSQK REKIEGNTYL GKGKLEELKA LIGELGADLV IFNDELSPVQ VRNLSELLDA EILDRTQLIL QIFAKRARSR EGKLQVELAR LEYMLPRLTG RGNELSRLGG GIGTRGPGET KLEADRRHIQ KRIYETKRQL DAVIKHRERY RERRKKNGMF RVALVGYTNA GKSTIFNRLT DADALAEDRL FATLDPLTRK MALPSGYRVL LSDTVGFIEK LPTALIAAFR STLEEALEAD LLLHVVDGSN PDHEQQEKTV QKILAELGAG HIPQLMVYNK ADRIDGPFFP SVSGDYLLIS AFEPEDIRRL RKKVEEMAVR EMERYQILLP FPEGKLYSRL KEETVLEHFS VMKDGECYQA SGYILPGHPL KKEIERFSKI RA // ID A0A150N5S9_9BACI Unreviewed; 416 AA. AC A0A150N5S9; DT 08-JUN-2016, integrated into UniProtKB/TrEMBL. DT 08-JUN-2016, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=B4110_1362 {ECO:0000313|EMBL:KYD32053.1}; OS Parageobacillus toebii. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; OC Parageobacillus. OX NCBI_TaxID=153151 {ECO:0000313|EMBL:KYD32053.1, ECO:0000313|Proteomes:UP000075324}; RN [1] {ECO:0000313|EMBL:KYD32053.1, ECO:0000313|Proteomes:UP000075324} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=B4110 {ECO:0000313|EMBL:KYD32053.1, RC ECO:0000313|Proteomes:UP000075324}; RA Berendsen E.M., Wells-Bennik M.H., Krawcyk A.O., De Jong A., RA Holsappel S., Eijlander R.T., Kuipers O.P.; RT "Draft Genome Sequences of Seven Thermophilic Sporeformers Isolated RT from Foods."; RL Submitted (JAN-2016) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KYD32053.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LQYW01000024; KYD32053.1; -; Genomic_DNA. DR RefSeq; WP_062677505.1; NZ_LQYW01000024.1. DR EnsemblBacteria; KYD32053; KYD32053; B4110_1362. DR PATRIC; fig|153151.4.peg.1139; -. DR Proteomes; UP000075324; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000075324}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}. FT DOMAIN 197 359 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 416 AA; 47968 MW; 0E1894939B666A0E CRC64; MNEREKVILV GCQLPHIDDE RFFYSMEELA SLVHTANGEV IMTVTQKREA IHPATYIGKG KVEELARLVE QLEPDVVIFN DELSPSQTRN LSRQLSVRII DRTQLILDIF AQRARSKEGK LQVELAQLQY LLPRLSGQGT ELSRLGGGIG TRGPGETKLE TDRRHIYRRI NEIKTQLKMV AEHRERYRER RKKNRVFQIS LVGYTNAGKS TLFNRLTDAD SFEENLLFAT LDPLTRKITL PSGYTALLTD TVGFIQDLPT TLVAAFRSTL EEVKEADLIL HVVDSSNPDY YNHEQTVYKL LDELGVSNVP IITVYNKRDI AHRNFVPSTK TDAIIISAFN AHDLHKLRQF IEETMIKQMV YYHIWIPSNE GKLLAQLKAE TILRELRYNV ESSMYECKGY MMPKHPLYGQ LRQYQK // ID A0A150WH60_BDEBC Unreviewed; 472 AA. AC A0A150WH60; DT 08-JUN-2016, integrated into UniProtKB/TrEMBL. DT 08-JUN-2016, sequence version 1. DT 07-JUN-2017, entry version 9. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=AZI86_16415 {ECO:0000313|EMBL:KYG62415.1}; OS Bdellovibrio bacteriovorus. OC Bacteria; Proteobacteria; Deltaproteobacteria; Bdellovibrionales; OC Bdellovibrionaceae; Bdellovibrio. OX NCBI_TaxID=959 {ECO:0000313|EMBL:KYG62415.1, ECO:0000313|Proteomes:UP000075320}; RN [1] {ECO:0000313|EMBL:KYG62415.1, ECO:0000313|Proteomes:UP000075320} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=R0 {ECO:0000313|EMBL:KYG62415.1, RC ECO:0000313|Proteomes:UP000075320}; RA Ploux O.; RL Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KYG62415.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LUKE01000005; KYG62415.1; -; Genomic_DNA. DR RefSeq; WP_061836376.1; NZ_LUKE01000005.1. DR EnsemblBacteria; KYG62415; KYG62415; AZI86_16415. DR Proteomes; UP000075320; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 2. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000075320}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000075320}. FT DOMAIN 253 418 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 221 248 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 472 AA; 52679 MW; 2FFE2D71901A5E58 CRC64; MDEFLDPQPL KALLIGVQLP KVSDQETQYS LAELSRLVTT LGYEVVGQTS QKRSSTRSAT VLGEGKLKDI AKWTGGPGFL GPMFKKKKHK AALRFEKEEE EDSFEGEEFF EESDEPEILE ESSGETAPQE KAQVAIFDCE LSPSQLRNME HVLGVPVLDR TGVIIEIFNR HARTREAKLQ VEIARLRYVA PRLRETGGGE DRGGGGIGAK GAGESVIELD RRHIRDRIKE LKDELASISQ EHETRRARRS QELVVALVGY TNAGKSSLMR ALTGSEIYVA DKLFATLDTT VRILQPETKP KILVSDTVGF IKKLPHDLVA SFKSTLDEAS NASLLLYVVD CSDPTFRSQL EVTKTTLREV GAGEIDNVLI LNKVDRLTAE ERASLAAEFP QGYFLSAHNP DDITQLHTYL VKHFENSMVD EDLFIPYDVQ KAIGEIRGKF AILGEEYDER GVTLKVRASP EDIRRLKTRH GI // ID A0A150WKL0_BDEBC Unreviewed; 425 AA. AC A0A150WKL0; DT 08-JUN-2016, integrated into UniProtKB/TrEMBL. DT 08-JUN-2016, sequence version 1. DT 07-JUN-2017, entry version 9. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=AZI86_14810 {ECO:0000313|EMBL:KYG64071.1}; OS Bdellovibrio bacteriovorus. OC Bacteria; Proteobacteria; Deltaproteobacteria; Bdellovibrionales; OC Bdellovibrionaceae; Bdellovibrio. OX NCBI_TaxID=959 {ECO:0000313|EMBL:KYG64071.1, ECO:0000313|Proteomes:UP000075320}; RN [1] {ECO:0000313|EMBL:KYG64071.1, ECO:0000313|Proteomes:UP000075320} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=R0 {ECO:0000313|EMBL:KYG64071.1, RC ECO:0000313|Proteomes:UP000075320}; RA Ploux O.; RL Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KYG64071.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LUKE01000003; KYG64071.1; -; Genomic_DNA. DR RefSeq; WP_061836037.1; NZ_LUKE01000003.1. DR EnsemblBacteria; KYG64071; KYG64071; AZI86_14810. DR Proteomes; UP000075320; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000075320}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000075320}. FT DOMAIN 208 371 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 425 AA; 47578 MW; 9C491FEDD587C093 CRC64; MTNQAFLNSK VTAQDRAIVI GVGLKSEPLT EIKENLLELE ELVAAAGGEV VGSLIQVLPS WNPATLIGTG KVEDVAEMVR DSGANIVIMD HQLSGVQQRN LAQTVKVRVI DRNQLILDIF AQRAQTFEGK LQVELAQLLD QMPRMIGAWM ESLSRQGGGI GTRGPGETAL ENDRRRIRER VAIIKDKLEG VRKNRAQHRQ SRRRHEIPSF ALIGYTNSGK SSLLNRLTGS EVLAKNQVFA TLDPTTRKIF LPDGPPSVVT DTVGFIRKLP TQLIEAFKAT LEESSEADVL IHVVDLSSPN MERQVEVVEG LIKEFNWSDK KIIHVFNKCD VAPLEKQFRV KAYPRVFVSA LTGQGIEQLK KLMAQMVSEM QTDVQLYFPR SEEYKIFDLG REAQIVRKET ATEGTVCYTQ LTPALMSRWK DYVVK // ID A0A150XBU8_9BACT Unreviewed; 399 AA. AC A0A150XBU8; DT 08-JUN-2016, integrated into UniProtKB/TrEMBL. DT 08-JUN-2016, sequence version 1. DT 07-JUN-2017, entry version 9. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=MB14_02800 {ECO:0000313|EMBL:KYG76193.1}; OS Roseivirga ehrenbergii. OC Bacteria; Bacteroidetes; Cytophagia; Cytophagales; Flammeovirgaceae; OC Roseivirga. OX NCBI_TaxID=279360 {ECO:0000313|EMBL:KYG76193.1, ECO:0000313|Proteomes:UP000075583}; RN [1] {ECO:0000313|EMBL:KYG76193.1, ECO:0000313|Proteomes:UP000075583} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=KMM 6017 {ECO:0000313|EMBL:KYG76193.1, RC ECO:0000313|Proteomes:UP000075583}; RA Selvaratnam C., Thevarajoo S., Goh K.M., Ee R., Chan K.-G., RA Chong C.S.; RT "Genome sequencing of Roseivirga ehrenbergii KMM 6017."; RL Submitted (JAN-2016) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KYG76193.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LQZQ01000023; KYG76193.1; -; Genomic_DNA. DR RefSeq; WP_062591272.1; NZ_LQZQ01000023.1. DR EnsemblBacteria; KYG76193; KYG76193; MB14_02800. DR Proteomes; UP000075583; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000075583}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000075583}. FT DOMAIN 203 386 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 164 191 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 399 AA; 46043 MW; 3B73F4463E2BF75B CRC64; MGGYLTTDTE KETAVLVALI NREQPEEKVI EYLDELAFLA DTMGLEVKKS FTQRLDKPEI RTFVGKGKFE EIYTYIKAEG IQVIIFDDDL SPSQLRNIER ELQIKIYDRS LLILDIFLKR AQTAQAKTQV ELARSKYLLP RLTRLWTHLE RQRGGTATRG GAGEKEIETD RRQIRNQITV LKKKLEKIEL QNEVQRKSRT NIVRVALVGY TNVGKSTLMR LMTKADVLAE NKLFATVDST VRKVAIDDIP FLLSDTVGFI RKLPTHLIES FKSTLDEVRE ADILLHIVDV SHPYYQDQME TVSQTLVDLG AADKPTIIIF NKIDKLLESL DPEIEEEMEH PPMTLERLKK TYLNAEGESV VFISAEKKEN IAEMREVIFE KVKKQHMTIF PNYLKDTYY // ID A0A150XHP1_9BACT Unreviewed; 398 AA. AC A0A150XHP1; DT 08-JUN-2016, integrated into UniProtKB/TrEMBL. DT 08-JUN-2016, sequence version 1. DT 07-JUN-2017, entry version 10. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=AWW68_05600 {ECO:0000313|EMBL:KYG78241.1}; OS Roseivirga spongicola. OC Bacteria; Bacteroidetes; Cytophagia; Cytophagales; Flammeovirgaceae; OC Roseivirga. OX NCBI_TaxID=333140 {ECO:0000313|EMBL:KYG78241.1, ECO:0000313|Proteomes:UP000075606}; RN [1] {ECO:0000313|EMBL:KYG78241.1, ECO:0000313|Proteomes:UP000075606} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=UST030701-084 {ECO:0000313|EMBL:KYG78241.1, RC ECO:0000313|Proteomes:UP000075606}; RA Selvaratnam C., Thevarajoo S., Goh K.M., Ee R., Chan K.-G., RA Chong C.S.; RT "Genome sequencing of Roseivirga spongicola UST030701-084."; RL Submitted (JAN-2016) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KYG78241.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LRPC01000001; KYG78241.1; -; Genomic_DNA. DR RefSeq; WP_068217584.1; NZ_LRPC01000001.1. DR EnsemblBacteria; KYG78241; KYG78241; AWW68_05600. DR Proteomes; UP000075606; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000075606}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000075606}. FT DOMAIN 203 385 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 398 AA; 45241 MW; 206D3A499840CBAE CRC64; MGGFETTPKE DDRAVLVALV NREQPEDTVV EYLDELAFLA ETMGLNVVKS FTQKMDKPDV RSFVGKGKLE EIQTYIKAEE IEVIIFDDDL SPSQLRNLEK ELKVKIYDRS LLILDIFLKR AQTAQAKTQV ELARSAYLLP RLTRMWTHLE RQRGGTGTRG GAGEKEIETD RRAIRNQITV LKGKLEKIEK QNAVQRKSRG TIVRVALVGY TNVGKSTLMR LLTKADVLAE DKLFATVDST VRKVVLDQIP FLLSDTVGFI RKLPTHLIES FKSTLAEVLE SDILLHVVDV SHPNFEDQMA TVNQTLIDIG ATDKPTILVF NKIDQLKIVD EEVREEMNNP PPTLDELKNT YIGKGEDSSV FISATNKTNM EEFKEVLMEK VKKRHFTIFP NYLNDSHY // ID A0A150Y9H4_9FIRM Unreviewed; 412 AA. AC A0A150Y9H4; DT 08-JUN-2016, integrated into UniProtKB/TrEMBL. DT 08-JUN-2016, sequence version 1. DT 07-JUN-2017, entry version 9. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=AXF09_05945 {ECO:0000313|EMBL:KYG87624.1}; OS Ruminococcus sp. DSM 100440. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Ruminococcaceae; OC Ruminococcus. OX NCBI_TaxID=1671366 {ECO:0000313|EMBL:KYG87624.1, ECO:0000313|Proteomes:UP000075299}; RN [1] {ECO:0000313|EMBL:KYG87624.1, ECO:0000313|Proteomes:UP000075299} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 100440 {ECO:0000313|EMBL:KYG87624.1, RC ECO:0000313|Proteomes:UP000075299}; RX PubMed=26946362; RA Hynonen U., Rasinkangas P., Satokari R., Paulin L., de Vos W.M., RA Pietila T.E., Kant R., Palva A.; RT "Isolation and whole genome sequencing of a Ruminococcus-like RT bacterium, associated with irritable bowel syndrome."; RL Anaerobe 39:60-67(2016). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KYG87624.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LFIL01000006; KYG87624.1; -; Genomic_DNA. DR RefSeq; WP_053769700.1; NZ_LFIL01000006.1. DR EnsemblBacteria; KYG87624; KYG87624; AXF09_05945. DR Proteomes; UP000075299; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000075299}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000075299}. FT DOMAIN 199 363 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 7 41 {ECO:0000256|SAM:Coils}. FT COILED 158 192 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 412 AA; 46435 MW; EF5C25386BE6E872 CRC64; MIETGKKQEK VILVAAATEE IEKAERSLDE LGELVKTAGA EVCGRMIQAR DMIHTGTYIG SGKLDELKWL VWEKEADGIV CDDELSPVQL KNLEEALDCK IMDRTLVILD IFAARASTKE GKIQVELAQL KYRQSRLTGL GKSLSRLGGG IGTRGPGEKK LEMDRRLIKN RIAQLNRELA DVRRHREITR EKRSQNHIPV CALVGYTNAG KSTLLNTLTG ASVLEEDQLF ATLDPTTRML ILPGNQKILL TDTVGFISKL PHNLIEAFRS TLEEAKYADM ILHVADLSNP QMEEQMHVTY ETLRELGVLN KTVITVFNKC DKASEEILIR DFQADAKVIV SAKTGEGLDR LQALLEDWVR EQRMEIKRLY PYTEAGKIQL IRAYGEVCKE EYQEEGIYIE GFVPSELYTK VN // ID A0A150YFQ0_9BACI Unreviewed; 425 AA. AC A0A150YFQ0; DT 08-JUN-2016, integrated into UniProtKB/TrEMBL. DT 08-JUN-2016, sequence version 1. DT 07-JUN-2017, entry version 10. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=A0U40_10305 {ECO:0000313|EMBL:KYG89795.1}; OS [Bacillus] sp. KCTC 13219. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; OC Lysinibacillus. OX NCBI_TaxID=1811976 {ECO:0000313|EMBL:KYG89795.1, ECO:0000313|Proteomes:UP000075350}; RN [1] {ECO:0000313|EMBL:KYG89795.1, ECO:0000313|Proteomes:UP000075350} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=KCTC 13219 {ECO:0000313|EMBL:KYG89795.1, RC ECO:0000313|Proteomes:UP000075350}; RA Jeong H., Park S.-H., Choi S.-K.; RT "Genome sequence of Bacillus sp. KCTC 13219."; RL Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KYG89795.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LUFJ01000033; KYG89795.1; -; Genomic_DNA. DR RefSeq; WP_066169447.1; NZ_LUFJ01000033.1. DR EnsemblBacteria; KYG89795; KYG89795; A0U40_10305. DR Proteomes; UP000075350; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000075350}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000075350}. FT DOMAIN 203 371 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 162 196 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 425 AA; 48144 MW; A0B7D3F2CD42DABE CRC64; MREIESIEER GILVGVNLKN DEHFAYSMEE LANLAEALDV EVVGSVTQNL ERVTPSHYVG TGKIEEIRAF YEEADANIII FNDELSPSQI RNLERDLECK VIDRTMLILD IFSRRAKTKE AQMQVELAQL QYMLPRLVGL HASLSRQGGG TGGGFKNRGA GETKLELDRR KIEDQIAKLR RDLEHVKAQR ETQRKQRRKN AVPVVSIVGY TNAGKSTIMN QLLAKVGQQE DKQVFEKDML FATLDTSVRN IELEDHKSFL LTDTVGFVSK LPHHLVKAFR STLEEAREAD LLLHVVDVSN EEYRFMMDVT NTTLKEVGVE EIPTIYVYNK SDLAGVEYPL MSGDNLWIAA KEGAGLEELL TMIRAHIFGD YIACKMLIPY DEGAVVSYLN EHATIFNTAY EEQGTLLSLE LKEADYQKYA SYVVE // ID A0A151ARW2_9CLOT Unreviewed; 596 AA. AC A0A151ARW2; DT 08-JUN-2016, integrated into UniProtKB/TrEMBL. DT 08-JUN-2016, sequence version 1. DT 07-JUN-2017, entry version 9. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:KYH30127.1}; GN ORFNames=CLCOL_00650 {ECO:0000313|EMBL:KYH30127.1}; OS Clostridium colicanis DSM 13634. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=1121305 {ECO:0000313|EMBL:KYH30127.1, ECO:0000313|Proteomes:UP000075374}; RN [1] {ECO:0000313|EMBL:KYH30127.1, ECO:0000313|Proteomes:UP000075374} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 13634 {ECO:0000313|EMBL:KYH30127.1, RC ECO:0000313|Proteomes:UP000075374}; RA Poehlein A., Daniel R.; RT "Genome sequence of Clostridium colicanis DSM 13634."; RL Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KYH30127.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LTBB01000001; KYH30127.1; -; Genomic_DNA. DR RefSeq; WP_061857022.1; NZ_LTBB01000001.1. DR EnsemblBacteria; KYH30127; KYH30127; CLCOL_00650. DR PATRIC; fig|1121305.3.peg.67; -. DR Proteomes; UP000075374; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000075374}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000075374}. FT DOMAIN 364 541 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 330 357 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 596 AA; 66915 MW; 02D43A217473899E CRC64; MIYGNIEGIK KTILRKLDSL YDFKVDKDMI SNLEIIEVIS SITEDINKEI SVAIDRKGNV EYVAIGDSST VEMPIVDLKN KKLSGVRILH THPNGYSTLS GLDISALVKL KLDCMAAIGV ENGKAKEITL GFCGIKDDKL IAEVTKPLKI EEALKVNILN VIENIEKNII ENEIHEDKGE RAILVGIEDE ESLEELEELA KACNVTTVGK ILQKRNKIDT AFYIGEGKVD EVAMERQARN ANVVIFDDEL SAAQIRNLED AIGSKVIDRT TLILEIFARR ARSKEAKIQV ELAQLKYRLP RLTGMGTVLS RTGGGIGTRG PGEKKLETDK RHIKERIYDL NRELAKIKKN REIQRDKRSR ENIPRVSLVG YTNAGKSTLR NKLCQIACPK DLVQKDEVFE ADMLFATLDV TTRALVLPDN RLITLTDTVG FIRKLPHDLI EAFKSTLEEV VSSDLLIHVV DSSSHKAKEQ IDAVNEVLKE LHADNKPTIL VLNKIDMASE EDIKALEDEY NNINIVKISA KEGFNLDELL NSVSKVLPNP LRKVEYIIPY TDSAAVALLH RSAKVLKEEY EEMGTHITAM VDEEIYNKCK QYIKSY // ID A0A151B5L6_9CLOT Unreviewed; 598 AA. AC A0A151B5L6; DT 08-JUN-2016, integrated into UniProtKB/TrEMBL. DT 08-JUN-2016, sequence version 1. DT 07-JUN-2017, entry version 10. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:KYH35090.1}; GN ORFNames=CLTEP_09100 {ECO:0000313|EMBL:KYH35090.1}; OS Clostridium tepidiprofundi DSM 19306. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=1121338 {ECO:0000313|EMBL:KYH35090.1, ECO:0000313|Proteomes:UP000075531}; RN [1] {ECO:0000313|EMBL:KYH35090.1, ECO:0000313|Proteomes:UP000075531} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 19306 {ECO:0000313|EMBL:KYH35090.1, RC ECO:0000313|Proteomes:UP000075531}; RA Poehlein A., Daniel R.; RT "Genome sequence of Clostridium tepidiprofundi DSM 19306."; RL Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KYH35090.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LTBA01000006; KYH35090.1; -; Genomic_DNA. DR RefSeq; WP_066823198.1; NZ_LTBA01000006.1. DR EnsemblBacteria; KYH35090; KYH35090; CLTEP_09100. DR PATRIC; fig|1121338.3.peg.936; -. DR Proteomes; UP000075531; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000075531}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000075531}. FT DOMAIN 365 545 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 324 358 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 598 AA; 67657 MW; 936BFF2C48026F00 CRC64; MIYGNTDGIR KTILNELENI YEYKIPRESI LTDELASIIV DISESINREI SIAVDRKGNI VSVSIGDSNT VEISGIFYSE NKLSGVRIIH THLNGNPKLS NMDISALIKL KLDCIASIAV DYNDGGHIID LGFCNIEDNT IKSVEIGPLS IEETLEFDFL GKINVVEDCL KNVCIEEKYS ERAILVGIES EESIDELEEL AKACNVQTLK KVLQVRSHID SAYFVGKGKM IEIQMLVQTL NANVVIFDDE LSASQVRNLE ENIGVKVIDR TTLILEIFAR RAKSSEAKLQ VELAQLRYRL PRLIGLGAVL SRTGAGIGTR GPGEKKLEVD KRHIRERIND IKKELHKHKK NRNIQREKRI KRNIPQVSLV GYTNAGKSTL RNKLCDIATY KEASIKEKVF EADMLFATLD TTTRAIVLPD NRIITISDTV GFIRKLPHDL VEAFKSTLEE VINSDVLLHV IDVSSDSFFE ELNVVNKVLE QLGADDKKII LVLNKIDKIE EDKLSEIRHE LQNITENECI EISAAKNVNL DLLLYKISKS IPEKLCKKEF IIPYSHQEYV AYIYRNGKVL AEEYKNTGTY IEALVDEETY NKCKKFKM // ID A0A151BAC2_9ARCH Unreviewed; 374 AA. AC A0A151BAC2; DT 08-JUN-2016, integrated into UniProtKB/TrEMBL. DT 08-JUN-2016, sequence version 1. DT 07-JUN-2017, entry version 6. DE SubName: Full=Small GTP-binding protein {ECO:0000313|EMBL:KYH36720.1}; GN ORFNames=AYL29_011880 {ECO:0000313|EMBL:KYH36720.1}; OS Candidatus Bathyarchaeota archaeon B24. OC Archaea; Candidatus Bathyarchaeota. OX NCBI_TaxID=1779368 {ECO:0000313|EMBL:KYH36720.1, ECO:0000313|Proteomes:UP000075406}; RN [1] {ECO:0000313|EMBL:KYH36720.1, ECO:0000313|Proteomes:UP000075406} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=B24 {ECO:0000313|EMBL:KYH36720.1}; RA He Y., Li M., Perumal V., Feng X., Fang J., Xie J., Sievert S., RA Wang F.; RT "Evidence for homoacetogenesis among multiple lineages of the archaeal RT phylum Bathyarchaeota widespread in marine sediments."; RL Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KYH36720.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LUCB01000017; KYH36720.1; -; Genomic_DNA. DR PATRIC; fig|1779368.3.peg.1430; -. DR Proteomes; UP000075406; Unassembled WGS sequence. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000075406}; KW Reference proteome {ECO:0000313|Proteomes:UP000075406}. FT DOMAIN 188 363 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 374 AA; 42600 MW; 9700DD165ECD7337 CRC64; MVKTNPHDHS LYLLKLREFR ALAEAAGYKV CGLVVQVRLK ESVNYAFGRG KVEEIKELVR ANDVDVFAVY NILTSKQKYN LEKALGVRVL DRYELTLEIF EKASSDELSK LQIELARLMK LYPYEKLRAA MRYRIGREHP WLRSSGEYIY HSVVNSLRRR MAKVRDKLER RKRFRIEQIV KRRKLGSPIV CIAGYYSSGK TTLFNALTGL DKPVSPKPFT TLSSKYYLIN GFKGLGKDLF IVDTIGFVHD LDPKMLEAFE LTLNDIRFSD LVLLVVDCSD PEPIMMLRLS TCLEVLESLG VEDERVVVAL NKIDLVNGDE LAERLKLVAN RVNPAPVIPI SARRGLNLDL LMGSIFSKLQ STLSSQLTLK TSLP // ID A0A151BDN4_9ARCH Unreviewed; 427 AA. AC A0A151BDN4; DT 08-JUN-2016, integrated into UniProtKB/TrEMBL. DT 08-JUN-2016, sequence version 1. DT 07-JUN-2017, entry version 9. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=AYL30_006180 {ECO:0000313|EMBL:KYH37832.1}; OS Candidatus Bathyarchaeota archaeon B25. OC Archaea; Candidatus Bathyarchaeota. OX NCBI_TaxID=1779369 {ECO:0000313|EMBL:KYH37832.1, ECO:0000313|Proteomes:UP000075493}; RN [1] {ECO:0000313|EMBL:KYH37832.1, ECO:0000313|Proteomes:UP000075493} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=B25 {ECO:0000313|EMBL:KYH37832.1}; RA He Y., Li M., Perumal V., Feng X., Fang J., Xie J., Sievert S., RA Wang F.; RT "Evidence for homoacetogenesis among multiple lineages of the archaeal RT phylum Bathyarchaeota widespread in marine sediments."; RL Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KYH37832.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LUCC01000038; KYH37832.1; -; Genomic_DNA. DR PATRIC; fig|1779369.3.peg.766; -. DR Proteomes; UP000075493; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000075493}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000075493}. FT DOMAIN 191 361 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 427 AA; 47573 MW; 4255F102E2344FD7 CRC64; MNRLGGRVVL VERRLHGEKS LLHELESLAQ TIGYTVAGKI EQVRRADPKF QIGAGKAEEL ARLVKEVGAE KVIFENDLKP VQAYNLAKET GVEVLDKFQL ILEVFSQHAS TKEAKLQIEL ARLRYELARA KEKVRLAKLG EQPGFHGLGK YEADVYYEAI RRRVSKIQEE LEKVRRSRRL KRLRRRSIGI PTVSLSGYTA AGKSTLFSAL SGVEAKVTGS LFTTLSTKIA LADFSGRRSL LVDTVGFIDG LPLTLIEAFK STLEETVFSD LVILVVDCSE TLSEVRRKLS YSLSTLHEIG IVSTPIITAL NKADLIGEDK AEKVAEKVSD IAPNPVPISA LYRINLETLR KTVADNLKDY VKASFELPLT SEALSLISSI RRFSTVRSQT FHEKAVLLEV ESTDYFMDKL KGRVEKLGGR MLEAVKI // ID A0A151BIH3_9ARCH Unreviewed; 354 AA. AC A0A151BIH3; DT 08-JUN-2016, integrated into UniProtKB/TrEMBL. DT 08-JUN-2016, sequence version 1. DT 07-JUN-2017, entry version 9. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=AYL32_015380 {ECO:0000313|EMBL:KYH39654.1}; OS Candidatus Bathyarchaeota archaeon B26-2. OC Archaea; Candidatus Bathyarchaeota. OX NCBI_TaxID=1779371 {ECO:0000313|EMBL:KYH39654.1, ECO:0000313|Proteomes:UP000075437}; RN [1] {ECO:0000313|EMBL:KYH39654.1, ECO:0000313|Proteomes:UP000075437} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=B26-2 {ECO:0000313|EMBL:KYH39654.1}; RA He Y., Li M., Perumal V., Feng X., Fang J., Xie J., Sievert S., RA Wang F.; RT "Evidence for homoacetogenesis among multiple lineages of the archaeal RT phylum Bathyarchaeota widespread in marine sediments."; RL Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KYH39654.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LUCE01000061; KYH39654.1; -; Genomic_DNA. DR PATRIC; fig|1779371.3.peg.1359; -. DR Proteomes; UP000075437; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000075437}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000075437}. FT DOMAIN 170 340 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 354 AA; 39856 MW; E430CAA550271B8E CRC64; MEELKSLAEA AGYTVVGSVE QVRRPDSRYQ IGRGKAEEIA DLVSKLGAEK IIFGNELKPV QAYNLAKLSG VEVIDRFQLI LEIFAKRAST REAKLQIALA RLKYELAQAK ERVRLAKMGE QPGFLGLGKY QVDVYYEMVK RRIKSIQRKL RKIRTTRELH RRHRRSLGFP LVSLAGYTNS GKSTLFNSLT AESVPTDSSV FTTLSTTVRM SDLEGIKILV TDTVGFIDRL PITLIEAFHS TLEEMVYSDL ILLVVDVSEP IEEIQRKVEC CLETIRQIGA SGLPMVTALN KIDLVPEHEL EEKIIRLGDV TPNPVPISAL HRINLRALKL EMLRHLESLL ETLTVHPFAK KIAN // ID A0A151BIJ8_9ARCH Unreviewed; 350 AA. AC A0A151BIJ8; DT 08-JUN-2016, integrated into UniProtKB/TrEMBL. DT 08-JUN-2016, sequence version 1. DT 07-JUN-2017, entry version 9. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=AYL31_009030 {ECO:0000313|EMBL:KYH39673.1}; OS Candidatus Bathyarchaeota archaeon B26-1. OC Archaea; Candidatus Bathyarchaeota. OX NCBI_TaxID=1779370 {ECO:0000313|EMBL:KYH39673.1, ECO:0000313|Proteomes:UP000075365}; RN [1] {ECO:0000313|EMBL:KYH39673.1, ECO:0000313|Proteomes:UP000075365} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=B26-1 {ECO:0000313|EMBL:KYH39673.1}; RA He Y., Li M., Perumal V., Feng X., Fang J., Xie J., Sievert S., RA Wang F.; RT "Evidence for homoacetogenesis among multiple lineages of the archaeal RT phylum Bathyarchaeota widespread in marine sediments."; RL Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KYH39673.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LUCD01000078; KYH39673.1; -; Genomic_DNA. DR PATRIC; fig|1779370.3.peg.1174; -. DR Proteomes; UP000075365; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000075365}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000075365}. FT DOMAIN 170 340 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 350 AA; 39406 MW; C2F0C7C854293D4E CRC64; MEELKGLAEA AGYTVVGSIE QVRRPDPRYQ VGPGKAREIA DLVRKLGAEK IIFGNELKPV QAYNLAKLSG VEVIDRFQLI LEIFVKRAST KEAKLQIALA RLNYELAQAK ERVRLAKMGE QPGFLGLGKY QVDIYYEMIR RRIKHIQKEL RRVRRTRELH RRHRRRLGFP LVSLAGYTNS GKSTLFNSLT RESVPTSSSV FTTLSTTVRM SSLQGVKVLV TDTVGFIDRL PITLIEAFHS TLEEMVYSDL ILLVVDVSEP LEEIRRKAEC CLETIRQIGA SKLPMVTALN KIDLTSEGEL DEKIASLKDV TPNPVPISAL YGINIETLKG EMLRQLEGSL ETVWMSPLAK // ID A0A151BJK8_9ARCH Unreviewed; 437 AA. AC A0A151BJK8; DT 08-JUN-2016, integrated into UniProtKB/TrEMBL. DT 08-JUN-2016, sequence version 1. DT 07-JUN-2017, entry version 9. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=AYL33_006750 {ECO:0000313|EMBL:KYH40040.1}; OS Candidatus Bathyarchaeota archaeon B63. OC Archaea; Candidatus Bathyarchaeota. OX NCBI_TaxID=1779372 {ECO:0000313|EMBL:KYH40040.1, ECO:0000313|Proteomes:UP000075614}; RN [1] {ECO:0000313|EMBL:KYH40040.1, ECO:0000313|Proteomes:UP000075614} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=B63 {ECO:0000313|EMBL:KYH40040.1}; RA He Y., Li M., Perumal V., Feng X., Fang J., Xie J., Sievert S., RA Wang F.; RT "Evidence for homoacetogenesis among multiple lineages of the archaeal RT phylum Bathyarchaeota widespread in marine sediments."; RL Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KYH40040.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LUCF01000074; KYH40040.1; -; Genomic_DNA. DR PATRIC; fig|1779372.3.peg.961; -. DR Proteomes; UP000075614; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000075614}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000075614}. FT DOMAIN 194 363 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 437 AA; 49391 MW; C44843CB4D974B8D CRC64; MRGGGNCRTK AIIVNVRERS EKSRIEELRS LAEAAGYEVV GSIEQVTTPH SQYYIGKGKA RELARLASEL GAERIIFGDE LKVTQAYNLA KLTGLEVIDR FQLILEIFDR RASTREAKLQ IELARWRYEL AHAREKVRLA RMGEQPGFLG LGKYEVDIYH EAVRRQVFSI QEKLRRIRRT RELHRRRRRE LGFPSVSLAG YTNSGKSTLF HALTGESVPI DRGVFTTLST TTRLLDLFGE PVLLTDTVGF IDKLPITLIE AFRSTLEETI FADLILLVID VSEPLEEIRR KMGCCLNTLR EIGASGMPML VALNKIDLIS EGELERKIRS LSEYSGLIPI SALHGANLDA LKLRMAEHLI KRVKFSFRVP INEEALSFLS WIYNHANVLE VAYLDSHLRV SLLAKPDVTE KIRHGIEGLG GTFKYEGAES LYPQIGS // ID A0A151BZU1_9MICO Unreviewed; 489 AA. AC A0A151BZU1; DT 08-JUN-2016, integrated into UniProtKB/TrEMBL. DT 08-JUN-2016, sequence version 1. DT 07-JUN-2017, entry version 8. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=AZH51_00565 {ECO:0000313|EMBL:KYH45445.1}; OS Branchiibius sp. NY16-3462-2. OC Bacteria; Actinobacteria; Micrococcales; Dermacoccaceae; Branchiibius. OX NCBI_TaxID=1807500 {ECO:0000313|EMBL:KYH45445.1, ECO:0000313|Proteomes:UP000075667}; RN [1] {ECO:0000313|EMBL:KYH45445.1, ECO:0000313|Proteomes:UP000075667} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NY16-3462-2 {ECO:0000313|EMBL:KYH45445.1}; RA Lapierre P., Halse T.A., Shea J., Musser K.A., Escuyer V.E.; RT "Draft genome assembly of Branchiibius sp. 15-3462-2 from a clinical RT sputum sample."; RL Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KYH45445.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LVCF01000007; KYH45445.1; -; Genomic_DNA. DR EnsemblBacteria; KYH45445; KYH45445; AZH51_00565. DR Proteomes; UP000075667; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 2. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000075667}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000075667}. FT DOMAIN 271 436 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 489 AA; 53258 MW; C18C8EF01613A3D0 CRC64; MTAEHTILNR RAEALAETGE DERYDEYGFL VEDEGTDGDQ FDREARSALR RVGGLSTELE DVTEVEYRQL RLERVVLVGV WTEGTVEDAE ANLRELAALA ETAGSEVLAG VLQRRTKPDP GTWLGSGKAK ELRDVVIAEG ADTVIADGEL APSQRRALED VVKVKVIDRT ALILDIFAQH AKSKEGKAQV ELAQLQYLLP RLRGWGESMS RQAGGQAAGG QGMGSRGPGE TKIELDRRRI NSRISKLKRE LSGMKTVRDT KRHSRKVNHV PSVAIAGYTN AGKSSILNRL TGAGVLVENQ LFATLDPTVR RSQTPDGRPY TLTDTVGFVR ELPHELVEAF RSTLEEVGDS DLLLHVVDGS HPDPESQITA VRAVLSDVGA TDVKEVIVIN KADVAEPEVI DRLTRAEKHS VVVSARTGAG FDELLALIAD ELPRPDIRVD VLLPYDRGDL VSRVHSEGEV LASEHTADGT RVQAKVTPTL EGELAAYAV // ID A0A151DV65_9EURY Unreviewed; 422 AA. AC A0A151DV65; DT 08-JUN-2016, integrated into UniProtKB/TrEMBL. DT 08-JUN-2016, sequence version 1. DT 12-APR-2017, entry version 7. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=AYK21_01700 {ECO:0000313|EMBL:KYK20160.1}; OS Thermoplasmatales archaeon SG8-52-2. OC Archaea; Euryarchaeota; Thermoplasmata; Thermoplasmatales. OX NCBI_TaxID=1803817 {ECO:0000313|EMBL:KYK20160.1, ECO:0000313|Proteomes:UP000075468}; RN [1] {ECO:0000313|EMBL:KYK20160.1, ECO:0000313|Proteomes:UP000075468} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SG8-52-2 {ECO:0000313|EMBL:KYK20160.1}; RA Wen L., He K., Yang H.; RL Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KYK20160.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LSSE01000068; KYK20160.1; -; Genomic_DNA. DR Proteomes; UP000075468; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000075468}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000075468}. FT DOMAIN 187 360 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 153 176 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 422 AA; 48749 MW; FC7FAD46C6F5995A CRC64; MEQKNAIIIA LNEDVSEIVD LADSLDYKVI KKFIQHRQTP DVNSYLGSGK IKEIEEYSET SKKNIDLVIV DGELKPSQWF NLEKKIGIDV FDRLRLILAI FEERADKKEA KLQVKLAQLQ YERPFVRELI HRARAGEHPG FMAGGEYQVD DYYEMIKKQM KKIKEQLNKI RNQRKVRRRH RHVVGFYLVS LAGYTNAGKS SLLNLLSDEK VKVEGRLFST LSTTTRRISQ KNIPILLTDT VGFIRNLPAY VIDAFHSTLE EIEVADVVLL VIDISEDKKI IEKKLKVSLD ELIELGVTSP IIIVFNKSDN LSNNEIESRI EYIKNQGFLD NKKFLTISVK NKDNIDNLLK TIYESLPKLV RFKIKLPINK ETQSLISWIY EKANVIDISY KQYAIITIDS NFSLKPKIIK KSKELNGSQV FK // ID A0A151EAA2_9EURY Unreviewed; 426 AA. AC A0A151EAA2; DT 08-JUN-2016, integrated into UniProtKB/TrEMBL. DT 08-JUN-2016, sequence version 1. DT 12-APR-2017, entry version 7. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=AYK25_05145 {ECO:0000313|EMBL:KYK25573.1}; OS Thermoplasmatales archaeon SM1-50. OC Archaea; Euryarchaeota; Thermoplasmata; Thermoplasmatales. OX NCBI_TaxID=1803815 {ECO:0000313|EMBL:KYK25573.1, ECO:0000313|Proteomes:UP000075446}; RN [1] {ECO:0000313|EMBL:KYK25573.1, ECO:0000313|Proteomes:UP000075446} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SM1-50 {ECO:0000313|EMBL:KYK25573.1}; RA Wen L., He K., Yang H.; RL Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KYK25573.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LSSI01000003; KYK25573.1; -; Genomic_DNA. DR Proteomes; UP000075446; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000075446}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000075446}. FT DOMAIN 189 366 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 426 AA; 48809 MW; 291D6F9248D03534 CRC64; MRTNQKKAIL ISLNDTNEEI KQLAKTLGYT IRKEFIQNRT KPDVNYYIGS GKVDEIKEFY GQMDTPIDLV IVNGELKPSQ WFTLEKKLKT NVYDRIRLIL AIFEEHAERR EALLQVKLAQ LQYERPYVRE LIHRTKAGEH PGLMAGGEYQ VNDYYEMIKR QTKKIREDLQ KIRENRELHR QTRSKSGFYS VSLAGYTNAG KSSLMNLLSA EKVKVEEQLF STLSTTTRSI ATKNKEKNIP ILLTDTVGFI ENLPAYIIDA FHSTLEEIEL ADVVVLVVDG SEAKEIVEKK LHVSINELRN IGVEAPIIIA INKIDLIDTT TFKTLQKSLA NTGIIKTHKI VPLSVKEQKN IEKLLQIIYN TLPHLVKLTF QLPLQEKSQT FISELYKKTK VLHITYSVTI TIKVECNEKI KEKLIASCHA IDGIVV // ID A0A151ENV3_9EURY Unreviewed; 422 AA. AC A0A151ENV3; DT 08-JUN-2016, integrated into UniProtKB/TrEMBL. DT 08-JUN-2016, sequence version 1. DT 12-APR-2017, entry version 7. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=AYK22_04140 {ECO:0000313|EMBL:KYK30300.1}; OS Thermoplasmatales archaeon SG8-52-3. OC Archaea; Euryarchaeota; Thermoplasmata; Thermoplasmatales. OX NCBI_TaxID=1803818 {ECO:0000313|EMBL:KYK30300.1, ECO:0000313|Proteomes:UP000075570}; RN [1] {ECO:0000313|EMBL:KYK30300.1, ECO:0000313|Proteomes:UP000075570} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SG8-52-3 {ECO:0000313|EMBL:KYK30300.1}; RA Wen L., He K., Yang H.; RL Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KYK30300.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LSSG01000084; KYK30300.1; -; Genomic_DNA. DR Proteomes; UP000075570; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000075570}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000075570}. FT DOMAIN 187 360 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 422 AA; 48745 MW; D44B887ACA461073 CRC64; MTKKNAIIIS LNEDVSEIID LAGSLDYKII KTYIQNRQIP DVNSFIGSGK VEEIKEYLDT SEQKIDLIII DGELKPSQWF NLEKKIGLDV FDRIRLILAI FEERADKKEA KLQVKLAQLQ YERPFVREII HRARSGEHPG FMAGGEYQVD DYYEMIKKQM KKIKEQLTNI RNQREVRRRH RHVGGFYLVS LAGYTNAGKS SLLNLLSDEK VKVEGRLFST LSTTTRRISK KRLPILITDT VGFIQNLPAY IIDAFHSTLE EIEESDVVLL IIDISEKKEI IANKLKVSLD ELIELGVKSP VIITLNKIDM ITEKEINSRI DYLKNQGFFE NKKIISISVK NEKNIDILLK LTYESLPQLV RFKIKLPLNE KSQSFISWIY ENANVLEISY GNYVILKIEC NSVIQSRIIT KCKNLDGFQL IE // ID A0A151NYI4_ALLMI Unreviewed; 417 AA. AC A0A151NYI4; DT 08-JUN-2016, integrated into UniProtKB/TrEMBL. DT 08-JUN-2016, sequence version 1. DT 07-JUN-2017, entry version 9. DE SubName: Full=Putative GTP-binding protein 6 {ECO:0000313|EMBL:KYO41495.1}; GN Name=GTPBP6 {ECO:0000313|EMBL:KYO41495.1}; GN ORFNames=Y1Q_0006288 {ECO:0000313|EMBL:KYO41495.1}; OS Alligator mississippiensis (American alligator). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Archelosauria; Archosauria; Crocodylia; Alligatoridae; Alligatorinae; OC Alligator. OX NCBI_TaxID=8496 {ECO:0000313|EMBL:KYO41495.1}; RN [1] {ECO:0000313|EMBL:KYO41495.1, ECO:0000313|Proteomes:UP000050525} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=KSC_2009_1 {ECO:0000313|EMBL:KYO41495.1}; RX PubMed=22293439; DOI=10.1186/gb-2012-13-1-415; RA St John J.A., Braun E.L., Isberg S.R., Miles L.G., Chong A.Y., RA Gongora J., Dalzell P., Moran C., Bed'hom B., Abzhanov A., RA Burgess S.C., Cooksey A.M., Castoe T.A., Crawford N.G., Densmore L.D., RA Drew J.C., Edwards S.V., Faircloth B.C., Fujita M.K., Greenwold M.J., RA Hoffmann F.G., Howard J.M., Iguchi T., Janes D.E., Khan S.Y., RA Kohno S., de Koning A.J., Lance S.L., McCarthy F.M., McCormack J.E., RA Merchant M.E., Peterson D.G., Pollock D.D., Pourmand N., Raney B.J., RA Roessler K.A., Sanford J.R., Sawyer R.H., Schmidt C.J., Triplett E.W., RA Tuberville T.D., Venegas-Anaya M., Howard J.T., Jarvis E.D., RA Guillette L.J.Jr., Glenn T.C., Green R.E., Ray D.A.; RT "Sequencing three crocodilian genomes to illuminate the evolution of RT archosaurs and amniotes."; RL Genome Biol. 13:415-415(2012). CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KYO41495.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AKHW03001628; KYO41495.1; -; Genomic_DNA. DR RefSeq; XP_006277511.1; XM_006277449.3. DR GeneID; 102563307; -. DR KEGG; amj:102563307; -. DR CTD; 8225; -. DR PhylomeDB; A0A151NYI4; -. DR Proteomes; UP000050525; Unassembled WGS sequence. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR CDD; cd01878; HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000050525}; KW Reference proteome {ECO:0000313|Proteomes:UP000050525}. FT DOMAIN 196 360 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 417 AA; 46822 MW; 668B363B61FE70A6 CRC64; MFVVQPRAGG LKRRRAAELQ VAEAVALVNT LHNWTVLDKI ILPTKNLDQK LIFGKGNFQI LTEKIKRLPQ ATAVFLNLER ISTLTKKELE DAWGVKVFDR YTVVLHIFRC NARTKEAKLQ IALAEIPLLR SNLKTEVSHL DQQRGGSRYI MGSGETFLET QTRLLREREL KIRNALENLR RKRSILRTQR QKREFPVISV MGYTNCGKTT LIKALTGDAG LQPQDQLFAT LDITAHAGYL PSHLAVIYVD TIGFLSDLPH DLIGSFSATL EEVAHSDLIV HVRDVSHPET VQQKASVLSV LKNLNLPSHL LDSIVEVHNK VDLVERYEPI EPNAVAISAL HGYGLQDLKE EIERTVLIAT GKKILTIKVN LTGPQLSWLY KEATVQEVDV MPDDGTASVK VIISESVLGK FRKTFPQ // ID A0A151RM75_CAJCA Unreviewed; 527 AA. AC A0A151RM75; DT 08-JUN-2016, integrated into UniProtKB/TrEMBL. DT 08-JUN-2016, sequence version 1. DT 07-JUN-2017, entry version 6. DE SubName: Full=GTP-binding protein hflX {ECO:0000313|EMBL:KYP43680.1}; GN ORFNames=KK1_034858 {ECO:0000313|EMBL:KYP43680.1}; OS Cajanus cajan (Pigeon pea) (Cajanus indicus). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae; OC Pentapetalae; rosids; fabids; Fabales; Fabaceae; Papilionoideae; OC Phaseoleae; Cajanus. OX NCBI_TaxID=3821 {ECO:0000313|EMBL:KYP43680.1, ECO:0000313|Proteomes:UP000075243}; RN [1] {ECO:0000313|EMBL:KYP43680.1, ECO:0000313|Proteomes:UP000075243} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Asha {ECO:0000313|Proteomes:UP000075243}; RX PubMed=22057054; DOI=10.1038/nbt.2022; RA Varshney R.K., Chen W., Li Y., Bharti A.K., Saxena R.K., RA Schlueter J.A., Donoghue M.T., Azam S., Fan G., Whaley A.M., RA Farmer A.D., Sheridan J., Iwata A., Tuteja R., Penmetsa R.V., Wu W., RA Upadhyaya H.D., Yang S.P., Shah T., Saxena K.B., Michael T., RA McCombie W.R., Yang B., Zhang G., Yang H., Wang J., Spillane C., RA Cook D.R., May G.D., Xu X., Jackson S.A.; RT "Draft genome sequence of pigeonpea (Cajanus cajan), an orphan legume RT crop of resource-poor farmers."; RL Nat. Biotechnol. 30:83-89(2012). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; KQ483657; KYP43680.1; -; Genomic_DNA. DR Proteomes; UP000075243; Unassembled WGS sequence. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 2. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000075243}; KW Reference proteome {ECO:0000313|Proteomes:UP000075243}. FT DOMAIN 302 468 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 527 AA; 58634 MW; 093195580BDF401D CRC64; MSAAFLYGSV IHPSPAIQQR FHYPSPPIPI RPFRLSPLTT TLVSSTVTTT TSVLHRDSAP ELASSSADSD DAVSSPNGAV RLDTEPRVEE AVPPLPAEDK GPRLRKKKED DVVSDNRYKL RNGREVFEEK AYLVGVERKN EVQDFGIEES LSELAQLADT AGLLVVGSTY QKLTSPNPRT YIGSGKVSEI KSAIHALDVE TVIFDDELSA GQLRNLEKIF GGDVRVCDVS LAQMEYQLPR LTKMWTHLER QAGGKVKGMG EKQIEVDKRI LRNQIGILKK ELESVRKHRK QYRNRRFSVP VPVVSLVGYT NAGKSTLLNQ LTGADVLAED KLFATLDPTT RRVQMKNGKE FLLTDTVGFI QKLPTTLVAA FRATLEEIAE SSLLVHVVDI SHPLAEQQIN AVDKVLSELD VSSIPRLMVW NKVDNVSDPL KLRLEAEKRE DVVCISALSG DGLQEFCNAV QDRLKDSMVW VEALVPFENG DLLSTIHQVG MVEKTEYTEQ GTYIKAHVPL RFARMLTPMR QLCVSRP // ID A0A151U203_CAJCA Unreviewed; 527 AA. AC A0A151U203; DT 08-JUN-2016, integrated into UniProtKB/TrEMBL. DT 08-JUN-2016, sequence version 1. DT 07-JUN-2017, entry version 8. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:KYP73301.1}; GN ORFNames=KK1_005921 {ECO:0000313|EMBL:KYP73301.1}; OS Cajanus cajan (Pigeon pea) (Cajanus indicus). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae; OC Pentapetalae; rosids; fabids; Fabales; Fabaceae; Papilionoideae; OC Phaseoleae; Cajanus. OX NCBI_TaxID=3821 {ECO:0000313|EMBL:KYP73301.1, ECO:0000313|Proteomes:UP000075243}; RN [1] {ECO:0000313|EMBL:KYP73301.1, ECO:0000313|Proteomes:UP000075243} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Asha {ECO:0000313|Proteomes:UP000075243}; RX PubMed=22057054; DOI=10.1038/nbt.2022; RA Varshney R.K., Chen W., Li Y., Bharti A.K., Saxena R.K., RA Schlueter J.A., Donoghue M.T., Azam S., Fan G., Whaley A.M., RA Farmer A.D., Sheridan J., Iwata A., Tuteja R., Penmetsa R.V., Wu W., RA Upadhyaya H.D., Yang S.P., Shah T., Saxena K.B., Michael T., RA McCombie W.R., Yang B., Zhang G., Yang H., Wang J., Spillane C., RA Cook D.R., May G.D., Xu X., Jackson S.A.; RT "Draft genome sequence of pigeonpea (Cajanus cajan), an orphan legume RT crop of resource-poor farmers."; RL Nat. Biotechnol. 30:83-89(2012). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CM003604; KYP73301.1; -; Genomic_DNA. DR Proteomes; UP000075243; Chromosome 2. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR CDD; cd01878; HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 2. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000075243}; KW Reference proteome {ECO:0000313|Proteomes:UP000075243}. FT DOMAIN 263 497 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 527 AA; 58464 MW; 1C030267D0DF6439 CRC64; MRAEATEQTN TTEIKSITSS LLWKRLYSSS LPKLLVVQPR VRSQKLLQAK LNEALCLANS LEDQRDGYFH TDFFDKPLPP HLLVQCRTPR ADTYFGQGTV DNVKCHIAAA ESKGDVDAVF VNAILSGIQQ RNLERAWGKP VLDRVGLIIE IFNAHAFTKE AKLQAELAAL SYKKTRLVRV RGPGGRYTFG ASGEAEVVSA RGRGSGGQGF MSGAGETELQ LQRRRILERR NYLLSQIEEV RRTRALQRAG RKRRGGSSGQ GLATVAIVGY TNAGKSTLVS RLSDSDLYSD CRLFATVDPR VRSAVLPSGK KVLLSDTVGF ISDLPIQLVE AFHATLEEVV EADLLVHVVD STAPNLNEHR STVLQVLKQI GVSEEKLQNM IEVWNKIDME EECMDNDEYL EDEDGDDAGS ISGLENEGIK EIDNHNDSGV MQEKEDYSDG WLYMDDTVDE EAFKKDNDVE KDGMIGQSGP HLKASAITGV GLQELMKLID EKLSVQNKKG AQVVERSSFD RKWRPSHNQE SGIVVEQ // ID A0A151WYB7_9HYME Unreviewed; 479 AA. AC A0A151WYB7; DT 08-JUN-2016, integrated into UniProtKB/TrEMBL. DT 08-JUN-2016, sequence version 1. DT 07-JUN-2017, entry version 8. DE SubName: Full=Putative GTP-binding protein 6 {ECO:0000313|EMBL:KYQ52691.1}; GN ORFNames=ALC60_08185 {ECO:0000313|EMBL:KYQ52691.1}; OS Trachymyrmex zeteki. OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; OC Pterygota; Neoptera; Holometabola; Hymenoptera; Apocrita; Aculeata; OC Vespoidea; Formicidae; Myrmicinae; Trachymyrmex. OX NCBI_TaxID=64791 {ECO:0000313|EMBL:KYQ52691.1, ECO:0000313|Proteomes:UP000075809}; RN [1] {ECO:0000313|EMBL:KYQ52691.1, ECO:0000313|Proteomes:UP000075809} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Tzet28-1 {ECO:0000313|EMBL:KYQ52691.1}; RC TISSUE=Whole body {ECO:0000313|EMBL:KYQ52691.1}; RA Nygaard S., Hu H., Boomsma J., Zhang G.; RT "Trachymyrmex zeteki WGS genome."; RL Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; KQ982658; KYQ52691.1; -; Genomic_DNA. DR RefSeq; XP_018307228.1; XM_018451726.1. DR RefSeq; XP_018307229.1; XM_018451727.1. DR RefSeq; XP_018307230.1; XM_018451728.1. DR GeneID; 108724982; -. DR Proteomes; UP000075809; Unassembled WGS sequence. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR CDD; cd01878; HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 4: Predicted; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000075809}; KW Reference proteome {ECO:0000313|Proteomes:UP000075809}. FT DOMAIN 262 421 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 228 258 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 479 AA; 54565 MW; 1C56D70BE68963DB CRC64; MHCIRKIINI TQWNLQVFNK VNRAHKRSGI LLQNIICRLN HDSEEYLSEE DEKKQNEYVK IASRYLGIAV GGHRTFILQP YIKWGKDKKR NTSPELQMAE AVALINTLPN WCVVGTKYAP LLTLQRKHLL GTGGIENLKK DLRQCPNPTA IFVSTNLLKF VQIRELEKIF GVPVYDRYSI VIHIFREHAK TAEARLQVAL AEIPYIRKKI FETCVSRSGA INVTEETKRL LDSKEKKLRN ELKKLQQHRR MIRNQRKKHG FPTVAVVGYT NAGKTSLIKA LTDDNSLQPR NKLFATLDTT AHQGILPNRL KILYMDTIGF IQDVPETLIE PFIVTLEDAI IADVIVHIYD VSHPDMKAQY EHVQETIKPM LDARPIIDVA NKCDLVQSEC IPKDAIAVSA KDLTGIDLLR LKIQEVLLAT TGLLTIRVRV KAGSSAASWL YKMTTVTNAE SDPNDVQYLI MKVIATAVDI QKFKKFLKE // ID A0A154BT94_9FIRM Unreviewed; 624 AA. AC A0A154BT94; DT 08-JUN-2016, integrated into UniProtKB/TrEMBL. DT 08-JUN-2016, sequence version 1. DT 07-JUN-2017, entry version 10. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=AXX12_03180 {ECO:0000313|EMBL:KYZ77149.1}; OS Anaerosporomusa subterranea. OC Bacteria; Firmicutes; Negativicutes; Selenomonadales; Sporomusaceae; OC Anaerosporomusa. OX NCBI_TaxID=1794912 {ECO:0000313|EMBL:KYZ77149.1, ECO:0000313|Proteomes:UP000076268}; RN [1] {ECO:0000313|EMBL:KYZ77149.1, ECO:0000313|Proteomes:UP000076268} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=RU4 {ECO:0000313|EMBL:KYZ77149.1, RC ECO:0000313|Proteomes:UP000076268}; RA Choi J.K., Shah M., Yee N.; RT "Anaerosporomusa subterraneum gen. nov., sp. nov., a spore-forming RT obligate anaerobe isolated from saprolite."; RL Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KYZ77149.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LSGP01000013; KYZ77149.1; -; Genomic_DNA. DR RefSeq; WP_066238947.1; NZ_LSGP01000013.1. DR EnsemblBacteria; KYZ77149; KYZ77149; AXX12_03180. DR Proteomes; UP000076268; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000076268}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000076268}. FT DOMAIN 376 541 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 335 362 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 624 AA; 69559 MW; 5298AE82FC4A64E5 CRC64; MEIYGDLEGL RTSLLNELKR LYEYSVAPAE MISLELAEHM AILTDELNRE IVVYINRRGQ VLRVAIGNAR TAPLPEAEGR RSLSRLSGIR CIHTHPNGDS RLSSIDVSSL REMRFDLMAA IGVADRKVQN ISFAVLAGWD GTIAKVQEFT DLTIQQFISI HLPQLIGQVE DQLAIRVDAT EVRQTEKAFL VGIEGGSRWD AEDSLRELAQ LAETAGAVVE GWTSQKRDKP DSTFFVGRGK VDELALIRQE KSIDLIIFDD ELTPAQQRNL EEALGTKIID RTGLILDIFA QRARSHEGKL QVELAQLRYL LPRLGGQGLV LSRLGGGIGT RGPGETKLEA DKRRLRSRIS DIQQEIVQVE KHRELQRRGR KKTAYPSIAL VGYTNAGKST LMNRLTSAGV LAEDKLFATL DPTTRCIRLP KGQDVFLSDT VGFIQKLPHQ LIAAFKATLE EVLQADLLLH VLDSSHPRVQ EQNTAVYQVL RELKADTKET VTVYNKMDQL DNPSLIERIL RQENTVTISA LTGDGIDTLL TMIEQVLSKR KTDISLLIPY EQSGILSSLY ECATVHSVDY QEQGIRVEAS IPVESTRRFI ELEIVEENDD AIYDEIGENP PRGVNGNSPS IGDD // ID A0A154NWQ6_9HYME Unreviewed; 487 AA. AC A0A154NWQ6; DT 08-JUN-2016, integrated into UniProtKB/TrEMBL. DT 08-JUN-2016, sequence version 1. DT 07-JUN-2017, entry version 7. DE SubName: Full=Putative GTP-binding protein 6 {ECO:0000313|EMBL:KZC04125.1}; GN ORFNames=WN55_02011 {ECO:0000313|EMBL:KZC04125.1}; OS Dufourea novaeangliae. OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; OC Pterygota; Neoptera; Holometabola; Hymenoptera; Apocrita; Aculeata; OC Apoidea; Halictidae; Rophitinae; Dufourea. OX NCBI_TaxID=178035 {ECO:0000313|EMBL:KZC04125.1, ECO:0000313|Proteomes:UP000076502}; RN [1] {ECO:0000313|EMBL:KZC04125.1, ECO:0000313|Proteomes:UP000076502} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=0120121106 {ECO:0000313|EMBL:KZC04125.1}; RC TISSUE=Whole body {ECO:0000313|EMBL:KZC04125.1}; RA Pan H., Kapheim K.; RT "The genome of Dufourea novaeangliae."; RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; KQ434777; KZC04125.1; -; Genomic_DNA. DR RefSeq; XP_015430539.1; XM_015575053.1. DR GeneID; 107187055; -. DR Proteomes; UP000076502; Unassembled WGS sequence. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR CDD; cd01878; HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 4: Predicted; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000076502}; KW Reference proteome {ECO:0000313|Proteomes:UP000076502}. FT DOMAIN 264 358 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 230 260 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 487 AA; 55835 MW; 9DDD316B7757241B CRC64; MQCLKKLFQV VENKAQYYNR INLIHRKGER TVLNLIHRFK HDFIQEFEGY EESEEEKHTY KEISEDYLGK ILDGHRVFII QPYIKWGFRK KRNTTPDLQL AEAVALVNTL PNWSVVGKKI VPLLTLQRNQ LVGSGALETL KGEIRGCPGV TAVFVSTNLL KFVQIAILQK AFGLPIYDRY TVVIHIFHKH AKTAEAKLQV AIAEIPYIKK KMIDLAESNI GRTRIDDKTK ELLETREKKL KNALQNLKEH RKLMKRQRQS YGFPTIAVVG YTNAGKTSLI KALTGDSSME PKDKLFATLD TTVHQGYLPN KLKVLYIDTI GFIQDVPETL IEPFKVTLED AIDANIIVHV YDMSHPDVNA QIQHIQKMLE PMIDKNKIII NVANKCDIVD KNSLEKETLP EDTYPISALK SIGTDLLRFK IEEEILKAAN LITKRFKVPV GGHVATWLYK ETTVTDAEPD SEDPQYLIMN VIMTTSAFYR LKRFCKQ // ID A0A154W8P1_9PROT Unreviewed; 428 AA. AC A0A154W8P1; DT 08-JUN-2016, integrated into UniProtKB/TrEMBL. DT 08-JUN-2016, sequence version 1. DT 05-JUL-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=AUP43_01035 {ECO:0000313|EMBL:KZD09882.1}; OS Oceanibaculum pacificum. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales; OC Rhodospirillaceae; Oceanibaculum. OX NCBI_TaxID=580166 {ECO:0000313|EMBL:KZD09882.1, ECO:0000313|Proteomes:UP000076400}; RN [1] {ECO:0000313|EMBL:KZD09882.1, ECO:0000313|Proteomes:UP000076400} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MCCC 1A02656 {ECO:0000313|EMBL:KZD09882.1, RC ECO:0000313|Proteomes:UP000076400}; RA Lu L., Lai Q., Shao Z., Qian P.; RT "Genome sequence of Oceanibaculum pacificum MCCC 1A02656."; RL Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KZD09882.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LPXN01000094; KZD09882.1; -; Genomic_DNA. DR EnsemblBacteria; KZD09882; KZD09882; AUP43_01035. DR Proteomes; UP000076400; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000076400}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000076400}. FT DOMAIN 200 372 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 166 196 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 428 AA; 47297 MW; 5494C121F4256272 CRC64; MLHPDIVGGP QSQQDSGDDA VRAPEARLAE AAGLALAIEL EIVHQEVVRV TKPTPATLLG SGQAERYGEL IDAMEVEVAV VDAALSPVQQ RNLERVWRCK VIDRTGLILE IFGARARTHE GRLQVDLAAL TYQRSRLVRS WTHLERQRGG AGFMGGPGES QIELDRRIID DKIVKLKRQL EEVKRTRELH RSARRKVPYP IVALVGYTNA GKSTLFNRLT RSDVFAKDLL FATLDPTMRR LKLPSGRQII LSDTVGFISD LPTQLVAAFR ATLEEVLEAD IILHVRDVAH PDSDAQRADV EEVLSDLGVG PEQGSEHIVE VLNKIDLLPA EERTRVGNIA ARDDSVIAVS ALDGSGSAEL LALLDRRLNA LRLTLRVDVD LADGATLAWL YQHGEVLERE DDERQAHLLV GLDPAEASRF ERRQAETA // ID A0A157Q5E5_9BORD Unreviewed; 368 AA. AC A0A157Q5E5; DT 08-JUN-2016, integrated into UniProtKB/TrEMBL. DT 08-JUN-2016, sequence version 1. DT 07-JUN-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:SAI74093.1}; GN ORFNames=SAMEA3906487_04023 {ECO:0000313|EMBL:SAI74093.1}; OS Bordetella trematum. OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Alcaligenaceae; Bordetella. OX NCBI_TaxID=123899 {ECO:0000313|EMBL:SAI74093.1, ECO:0000313|Proteomes:UP000076825}; RN [1] {ECO:0000313|EMBL:SAI74093.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=H044680328 {ECO:0000313|EMBL:SAI74093.1}; RG Pathogen Informatics; RL Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LT546645; SAI74093.1; -; Genomic_DNA. DR RefSeq; WP_025512554.1; NZ_LT546645.1. DR EnsemblBacteria; SAI74093; SAI74093; SAMEA3906487_04023. DR KEGG; btrm:SAMEA390648704023; -. DR PATRIC; fig|123899.6.peg.4019; -. DR KO; K03665; -. DR Proteomes; UP000076825; Chromosome 1. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000076825}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000076825}. FT DOMAIN 190 354 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 368 AA; 40407 MW; D544C38591577F39 CRC64; MRALIISVDL GDLDHPAHAQ EFVMLAEGAG AEIVGTLTAR RDRPDAKFFI GSGKVEEGVA LAKAVLADIV LFDQPLSPAQ QRNLEREFNL RVVDRVALIL DIFALRAKSH EGKLQVELAQ LQHLSTRLTR LWSHLERQRG GIGMRGPGES QLEMDRRMIG SKVRMLRERL DRVERQRITQ RRARARGGAL SVSLVGYTNA GKSTLFNALT RAGAYAADQL FATLDTTTRR IWIEAAGSVV ISDTVGFIRD LPPNLIAAFR ATLEETVHAD LLLHVVDAAS PQRDEQIFEV NKVLAEIGAA EIPTLLVYNK IDRVGLEPRI ERDAHGTIAR VFVSATERAG LDALRGAIAE IGQIAGNNAA NQENLQSE // ID A0A157SNI2_9BORD Unreviewed; 368 AA. AC A0A157SNI2; DT 08-JUN-2016, integrated into UniProtKB/TrEMBL. DT 08-JUN-2016, sequence version 1. DT 07-JUN-2017, entry version 10. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:SAI72048.1}; GN ORFNames=SAMEA3906486_03907 {ECO:0000313|EMBL:SAI72048.1}; OS Bordetella ansorpii. OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Alcaligenaceae; Bordetella. OX NCBI_TaxID=288768 {ECO:0000313|EMBL:SAI72048.1, ECO:0000313|Proteomes:UP000076848}; RN [1] {ECO:0000313|EMBL:SAI72048.1, ECO:0000313|Proteomes:UP000076848} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=H050680373 {ECO:0000313|EMBL:SAI72048.1, RC ECO:0000313|Proteomes:UP000076848}; RG Pathogen Informatics; RL Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; FKIF01000007; SAI72048.1; -; Genomic_DNA. DR RefSeq; WP_066130618.1; NZ_FKIF01000007.1. DR EnsemblBacteria; SAI72048; SAI72048; SAMEA3906486_03907. DR Proteomes; UP000076848; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000076848}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000076848}. FT DOMAIN 190 354 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 368 AA; 40400 MW; 90DCCDF471FB208E CRC64; MRALIISVDL GSPEHAAHAD EFAMLARGAG AEITGILTAR RDTPDAKFFI GSGKVEEAVM MAKAQLVDII LFDQPLSPAQ QRNLEREFNL RVVDRVALIL DIFALRAKSH EGKLQVELAQ LQHLATRLTR LWSHLERQRG GIGMRGPGEA QLEMDRRIIG DKVKVLRERL DRVERQRVTQ RRARARGGAL SVSLVGYTNA GKSTLFNAMT RAGAYAADQL FATLDTTTRR IWIEGAGNVV LSDTVGFIRD LPTKLIAAFR ATLEETVHAD LLLHVVDASS AQRDEQIFEV NKVLAEIGAA QIPTILVYNK IDRAGLEPRI DRDAHGTIAR IFVSATERAG LDALRGAIAE TGQIVGNNAS NHQTLQSE // ID A0A158M982_9BORD Unreviewed; 368 AA. AC A0A158M982; DT 08-JUN-2016, integrated into UniProtKB/TrEMBL. DT 08-JUN-2016, sequence version 1. DT 07-JUN-2017, entry version 9. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:KAK97627.1}; GN ORFNames=L497_2362 {ECO:0000313|EMBL:KAK97627.1}; OS Bordetella holmesii CDC-H585-BH. OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Alcaligenaceae; Bordetella. OX NCBI_TaxID=1331206 {ECO:0000313|EMBL:KAK97627.1, ECO:0000313|Proteomes:UP000026682}; RN [1] {ECO:0000313|EMBL:KAK97627.1, ECO:0000313|Proteomes:UP000026682} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CDC-H585-BH {ECO:0000313|EMBL:KAK97627.1, RC ECO:0000313|Proteomes:UP000026682}; RA Harvill E., Goodfield L.L., Ivanov Y., Meyer J.A., Newth C., RA Cassiday P., Tondella M.L., Liao P., Zimmerman J., Meert K., RA Wessel D., Berger J., Dean J.M., Holubkov R., Burr J., Liu T., RA Brinkac L.M., Sanka R., Kim M., Losada L.; RT "Genome sequence of Bordetella holmseii."; RL Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KAK97627.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JFZZ01000024; KAK97627.1; -; Genomic_DNA. DR RefSeq; WP_005015862.1; NZ_JFZZ01000024.1. DR EnsemblBacteria; KAK97627; KAK97627; L497_2362. DR GeneID; 23431046; -. DR PATRIC; fig|1331206.3.peg.646; -. DR Proteomes; UP000026682; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000026682}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}. FT DOMAIN 190 356 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 156 183 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 368 AA; 40286 MW; 199E651207542653 CRC64; MRALIISVDL GDPDHQAHAD EFLMLAEGAG AEIVGTLNAR RDRPDAKYFI GSGKVEEGVA LAGAALADIV LFDQPLSPAQ QRNLEREFNL RVVDRVALIL DIFALRAKSH EGKLQVELAQ LQHLSTRLTR MWSHLERQRG GIGMRGPGES QLEMDRRMIG AKVKMLRERL DRVERQRVTQ RRARARGGAL SVSLVGYTNA GKSTLFNSLT RAGAYAADQL FATLDTTTRR IWIEGAGSVV LSDTVGFIRD LPPNLIAAFR ATLEETVHAD LLLHVVDAAS PQRDEQVFEV NKVLAEIGAA EVPTILVYNK IDRAGLEPRV ERDAHGTIAR VFVSATERAG LDALRGAIAE ISQIAGNNAS NHQTLQSE // ID A0A158NIZ7_ATTCE Unreviewed; 476 AA. AC A0A158NIZ7; DT 08-JUN-2016, integrated into UniProtKB/TrEMBL. DT 08-JUN-2016, sequence version 1. DT 07-JUN-2017, entry version 7. DE SubName: Full=Uncharacterized protein {ECO:0000313|EnsemblMetazoa:XP_012057505.1}; OS Atta cephalotes (Leafcutter ant). OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; OC Pterygota; Neoptera; Holometabola; Hymenoptera; Apocrita; Aculeata; OC Vespoidea; Formicidae; Myrmicinae; Atta. OX NCBI_TaxID=12957 {ECO:0000313|EnsemblMetazoa:XP_012057505.1}; RN [1] {ECO:0000313|EnsemblMetazoa:XP_012057505.1, ECO:0000313|Proteomes:UP000005205} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=21347285; DOI=10.1371/journal.pgen.1002007; RA Suen G., Teiling C., Li L., Holt C., Abouheif E., Bornberg-Bauer E., RA Bouffard P., Caldera E.J., Cash E., Cavanaugh A., Denas O., Elhaik E., RA Fave M.J., Gadau J., Gibson J.D., Graur D., Grubbs K.J., Hagen D.E., RA Harkins T.T., Helmkampf M., Hu H., Johnson B.R., Kim J., Marsh S.E., RA Moeller J.A., Munoz-Torres M.C., Murphy M.C., Naughton M.C., Nigam S., RA Overson R., Rajakumar R., Reese J.T., Scott J.J., Smith C.R., Tao S., RA Tsutsui N.D., Viljakainen L., Wissler L., Yandell M.D., Zimmer F., RA Taylor J., Slater S.C., Clifton S.W., Warren W.C., Elsik C.G., RA Smith C.D., Weinstock G.M., Gerardo N.M., Currie C.R.; RT "The genome sequence of the leaf-cutter ant Atta cephalotes reveals RT insights into its obligate symbiotic lifestyle."; RL PLoS Genet. 7:e1002007-e1002007(2011). RN [2] {ECO:0000313|EnsemblMetazoa:XP_012057505.1} RP IDENTIFICATION. RG EnsemblMetazoa; RL Submitted (APR-2016) to UniProtKB. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR RefSeq; XP_012057505.1; XM_012202115.1. DR EnsemblMetazoa; XM_012202115.1; XP_012057505.1; LOC105620625. DR GeneID; 105620625; -. DR OMA; MDTVGFM; -. DR Proteomes; UP000005205; Unassembled WGS sequence. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR CDD; cd01878; HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 4: Predicted; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000005205}; KW Reference proteome {ECO:0000313|Proteomes:UP000005205}. FT DOMAIN 259 418 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 225 255 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 476 AA; 54122 MW; 1F7C67E0CBD3AE70 CRC64; MHCIHKIINI TQRNLQVFNK VHKRSGILLQ NIICRLNHDS EEYLSEEDEK KQNAYVKIIS HYLGIAVGGH RTFILQPYIK WGRDKKRNTS PELQMAEAVA LINTLPNWCV VGTKYSPLLT LQRKHLLGTG AIENLKKDLR QCSNPTAIFI STNQLKFVQI SELEKIFGLP VYDRYSIVIH IFREHAKTAE ARLQVAIAEI PYIRKKIFET CITRSGAINV TEETKLLLDS KEKKLKNELK KLQQHRRIIR SHRKKHSFST VAVVGYTNAG KTSLIKALTD DNSLQPRDKL FATLDTTAHQ GILPNRLKIL YMDTIGFIQD VPETLIEPFI VTLEDAMIAD VIVHIYDVSH PDMKAQYQHV QQTIKPMLDA RPIIDVANKC DLVQSDCIPK DAIAVSAKDL TGIDLLRLKI QEILLASTGL LSIRVRVKAG SSAASWLYKM TTVTNTESDP NDVQYLIMEV IATAVDIQKF KKFLKE // ID A0A158PFE3_ANGCS Unreviewed; 405 AA. AC A0A158PFE3; DT 08-JUN-2016, integrated into UniProtKB/TrEMBL. DT 08-JUN-2016, sequence version 1. DT 12-APR-2017, entry version 4. DE SubName: Full=Uncharacterized protein {ECO:0000313|WBParaSite:ACOC_0000330501-mRNA-1}; OS Angiostrongylus costaricensis (Nematode worm). OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida; OC Strongylida; Metastrongyloidea; Angiostrongylidae; Angiostrongylus. OX NCBI_TaxID=334426 {ECO:0000313|WBParaSite:ACOC_0000330501-mRNA-1}; RN [1] {ECO:0000313|Proteomes:UP000050601, ECO:0000313|WBParaSite:ACOC_0000330501-mRNA-1} RP NUCLEOTIDE SEQUENCE. RG Helminth Genomes Consortium; RL Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|WBParaSite:ACOC_0000330501-mRNA-1} RP IDENTIFICATION. RG WormBaseParasite; RL Submitted (APR-2016) to UniProtKB. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR WBParaSite; ACOC_0000330501-mRNA-1; ACOC_0000330501-mRNA-1; ACOC_0000330501. DR Proteomes; UP000050601; Genome assembly. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000050601}; KW Reference proteome {ECO:0000313|Proteomes:UP000050601}. FT DOMAIN 214 339 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 405 AA; 45971 MW; 7D4DF1D84F2A702F CRC64; MYEYSDLFTE AFSAAERIPE RWKCVKSVIA HDFLVVHPKV RWGASSASVL KDPQRQLNEA VALVNTLPGF RVVQTPSDVS LSLFRSAVLG VEYNTKRKTV WGSGQIEALM TIKQQSRVTA LMVNVDMLSP LQQHELFDIF RVPVYDRYNI VLSIFKHYAY TLEAHLQIQL AEIPYIRVDE FEVLRLREQS LRKKLRHLVE KNVERAREET QGAAMVAVVG YTNAGKTSLV KCLTGAVGLL PEDRLFATLD TTRHAARLPS GRKVVFADTI GFLSELPMHL LAAFHATLSH VKLADVIIHI RDLSNPDWPA QSEDVYKTLE AIGLPHDRIN DIIVADNKVS AKVCISTITD NAVKYSLSSL SIKAILVFFS FLGRRVWDPD YFKFRCYKDI MPDLRRCGKT YTTDR // ID A0A158PZG9_BRUMA Unreviewed; 481 AA. AC A0A158PZG9; DT 08-JUN-2016, integrated into UniProtKB/TrEMBL. DT 08-JUN-2016, sequence version 1. DT 30-AUG-2017, entry version 10. DE SubName: Full=Bm4133, isoform a {ECO:0000313|WBParaSite:Bm4133}; OS Brugia malayi (Filarial nematode worm). OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Spirurida; OC Filarioidea; Onchocercidae; Brugia. OX NCBI_TaxID=6279 {ECO:0000313|Proteomes:UP000006672, ECO:0000313|WBParaSite:Bm4133}; RN [1] {ECO:0000313|Proteomes:UP000006672, ECO:0000313|WBParaSite:Bm4133} RP NUCLEOTIDE SEQUENCE. RC STRAIN=FR3 {ECO:0000313|Proteomes:UP000006672, RC ECO:0000313|WBParaSite:Bm4133}; RX PubMed=17885136; DOI=10.1126/science.1145406; RA Ghedin E., Wang S., Spiro D., Caler E., Zhao Q., Crabtree J., RA Allen J.E., Delcher A.L., Guiliano D.B., Miranda-Saavedra D., RA Angiuoli S.V., Creasy T., Amedeo P., Haas B., El-Sayed N.M., RA Wortman J.R., Feldblyum T., Tallon L., Schatz M., Shumway M., Koo H., RA Salzberg S.L., Schobel S., Pertea M., Pop M., White O., Barton G.J., RA Carlow C.K., Crawford M.J., Daub J., Dimmic M.W., Estes C.F., RA Foster J.M., Ganatra M., Gregory W.F., Johnson N.M., Jin J., RA Komuniecki R., Korf I., Kumar S., Laney S., Li B.W., Li W., RA Lindblom T.H., Lustigman S., Ma D., Maina C.V., Martin D.M., RA McCarter J.P., McReynolds L., Mitreva M., Nutman T.B., Parkinson J., RA Peregrin-Alvarez J.M., Poole C., Ren Q., Saunders L., Sluder A.E., RA Smith K., Stanke M., Unnasch T.R., Ware J., Wei A.D., Weil G., RA Williams D.J., Zhang Y., Williams S.A., Fraser-Liggett C., Slatko B., RA Blaxter M.L., Scott A.L.; RT "Draft genome of the filarial nematode parasite Brugia malayi."; RL Science 317:1756-1760(2007). RN [2] {ECO:0000313|WBParaSite:Bm4133} RP IDENTIFICATION. RG WormBaseParasite; RL Submitted (APR-2016) to UniProtKB. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR WBParaSite; Bm4133; Bm4133; WBGene00224394. DR Proteomes; UP000006672; Unassembled WGS sequence. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR CDD; cd01878; HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000006672}; KW Reference proteome {ECO:0000313|Proteomes:UP000006672}. FT DOMAIN 257 420 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 481 AA; 54809 MW; 1F0037D4E7B265A7 CRC64; MKLLQNMTFS RNFAKIFVPL YSGRRFCTMI PEGAMQMTDE FNIISKSYGI QSIAPGVQRI LLIHPRLRRG RFFDLNPERA KLQLEEAVAL VNTLPNFKVM ETTAVSTDRS TKKKRLWGSG RIQRIIALKE KISATALMID VDILSPKQQA ELTSIFRTPV YDRYNIVLLI FKIFAKTKEA KLQIQLAEIP YIRQRLLSMY ELHVDPSLLH LDTSEKSKAE RLEVLRYREQ HLRKCLKAAV EEKVNLRIGE AQKNIRTVVA VAGYTNAGKS SLIKRLTGRN LYVEDRLFAT LDTSLHVFRL PSGLPILFAD TIGFISNLPT QLLASFQATL NHVANADLLL HVEDVSNPDY LTQRNVVMKT LSALKIRNEL LKSVIRVGNK IDKLCRLPPH ESNTYFVSCA DGRGFVELLA AIDKRVLAIS GVTIRRLKLR PHSEAFSYLC KYSFLVGQPI PSDDNNYLLC NVIMDDNEFS KFRANFSFSK I // ID A0A158Q8I1_9BILA Unreviewed; 607 AA. AC A0A158Q8I1; DT 08-JUN-2016, integrated into UniProtKB/TrEMBL. DT 08-JUN-2016, sequence version 1. DT 10-MAY-2017, entry version 7. DE SubName: Full=Uncharacterized protein {ECO:0000313|WBParaSite:EEL_0000766001-mRNA-1}; OS Elaeophora elaphi. OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Spirurida; OC Filarioidea; Onchocercidae; Elaeophora. OX NCBI_TaxID=1147741 {ECO:0000313|WBParaSite:EEL_0000766001-mRNA-1}; RN [1] {ECO:0000313|Proteomes:UP000050640, ECO:0000313|WBParaSite:EEL_0000766001-mRNA-1} RP NUCLEOTIDE SEQUENCE. RG Helminth Genomes Consortium; RL Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|WBParaSite:EEL_0000766001-mRNA-1} RP IDENTIFICATION. RG WormBaseParasite; RL Submitted (APR-2016) to UniProtKB. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR WBParaSite; EEL_0000766001-mRNA-1; EEL_0000766001-mRNA-1; EEL_0000766001. DR Proteomes; UP000050640; Genome Assembly. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR CDD; cd01878; HflX; 1. DR InterPro; IPR008584; DUF866_euk. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR Pfam; PF05907; DUF866; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000050640}; KW Reference proteome {ECO:0000313|Proteomes:UP000050640}. FT DOMAIN 221 384 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 607 AA; 69786 MW; 0BE29009A438F514 CRC64; MNDEFNIISK SYGIHSIAPG VHRILLIYPR LRRGRFFDLN PTKVRLQLEE AVALVNTLPN FKVIETTAVS TDRSTEKKRL WGKGRIERMI TLKEKISATA LMINVDILSP KQQAELTAIF RVPVYDRYNI VLLIFKMFAK TKEAKLQIQL AEIPYIRERL LSVYDLRVNS SVFHVDISEK SKAERLEVLR YREHHLRKCL KAAVEEKVNL RAGEAQKNIR TVVAVVGYTN AGKSSLIKRL TRRNLYVEDR LFATLDTSLH VFRLPSGLPI LFADTIGFIS NLPTQLLASF QATLNHVANA DLLLHVEDVS SPDYLAQRDV VMKTLSVLKI KEELLKSVIR VGNKIDKLSQ IPPNEPNTYF VSCADGRGFV ELMAAVDKRV LTISGVTIRR LKLRPHSEAF AYLCKYSFLV GQPIPSEDND YLLCSVIMDD NEFRESFCEL RKLSMPIIAL QLKANMVNVT SLEPMKDWTK FRWYLKLKCT NCGEEPEHWQ YVIEEEKFSV PGSRGTTNML GKCKLCNRTN SLEIVKDSFR PYKNSDDYCE LIRFDCRGLE PTDFDPRSGW RAVGTESKTV FENIDLTEKE WVDYDEKAAQ PTEINEIHCR FVLCRKQ // ID A0A160F5D2_9BACI Unreviewed; 413 AA. AC A0A160F5D2; DT 06-JUL-2016, integrated into UniProtKB/TrEMBL. DT 06-JUL-2016, sequence version 1. DT 07-JUN-2017, entry version 9. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:ANB61232.1}; GN ORFNames=GFC30_1616 {ECO:0000313|EMBL:ANB61232.1}; OS Anoxybacillus amylolyticus. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Anoxybacillus. OX NCBI_TaxID=294699 {ECO:0000313|EMBL:ANB61232.1, ECO:0000313|Proteomes:UP000076865}; RN [1] {ECO:0000313|EMBL:ANB61232.1, ECO:0000313|Proteomes:UP000076865} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 15939 {ECO:0000313|EMBL:ANB61232.1, RC ECO:0000313|Proteomes:UP000076865}; RX PubMed=16682297; DOI=10.1016/j.syapm.2005.10.003; RA Poli A., Esposito E., Lama L., Orlando P., Nicolaus G., RA de Appolonia F., Gambacorta A., Nicolaus B.; RT "Anoxybacillus amylolyticus sp. nov., a thermophilic amylase producing RT bacterium isolated from Mount Rittmann (Antarctica)."; RL Syst. Appl. Microbiol. 29:300-307(2006). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP015438; ANB61232.1; -; Genomic_DNA. DR EnsemblBacteria; ANB61232; ANB61232; GFC30_1616. DR KEGG; aamy:GFC30_1616; -. DR PATRIC; fig|294699.3.peg.1642; -. DR KO; K03665; -. DR Proteomes; UP000076865; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000076865}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000076865}. FT DOMAIN 194 356 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 413 AA; 47245 MW; 5B0A2E0DBF034CB4 CRC64; MEKVITVGCQ LPHVDDERFS YSMEELASLV HTANGEVVII LTQKRETIHP ATYIGKGKVE ELVRLVEQFE PDVVVFNDEL SPSQNRNLTK LLNVRVIDRT QLILDIFAQR AWSKEGKLQV ELAQLQYILP RLSGQGVELS RLGGGIGTRG PGETKLETDR RHIRRRIDEI KAQLKVIVEH RERYRERRKK NAVFQIALVG YTNAGKSTLF NRLTNADSFE ENLLFATLDP LTRKLVLPSG YTVLLTDTVG FIQDLPTTLV AAFRSTLEEV KEADLILHIV DSSNPDYIQH EQTVYRLLEE LEATTIPIAT VYNKRDIVLP SFVPSPKTDY MLVSALNEQD IQALRRFMET RITEAMERYD VAIRASEGKL LDQLKAETIV QHMHYNEQSG MYECSGYILP DHPLLLQLRT YKK // ID A0A160FE11_9BACI Unreviewed; 421 AA. AC A0A160FE11; DT 06-JUL-2016, integrated into UniProtKB/TrEMBL. DT 06-JUL-2016, sequence version 1. DT 07-JUN-2017, entry version 7. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:ANB65131.1}; GN ORFNames=GFC29_516 {ECO:0000313|EMBL:ANB65131.1}; OS Anoxybacillus sp. B7M1. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Anoxybacillus. OX NCBI_TaxID=1490057 {ECO:0000313|EMBL:ANB65131.1, ECO:0000313|Proteomes:UP000076753}; RN [1] {ECO:0000313|EMBL:ANB65131.1, ECO:0000313|Proteomes:UP000076753} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=b7m1 {ECO:0000313|Proteomes:UP000076753}; RA Evans L.H., Alamgir A., Owens N., Weber N.D., Virtaneva K., RA Barbian K., Babar A., Rosenke K.; RL Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP015436; ANB65131.1; -; Genomic_DNA. DR EnsemblBacteria; ANB65131; ANB65131; GFC29_516. DR KEGG; anl:GFC29_516; -. DR PATRIC; fig|1490057.3.peg.574; -. DR KO; K03665; -. DR Proteomes; UP000076753; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000076753}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000076753}. FT DOMAIN 202 364 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 421 AA; 48078 MW; 6EF2E1C43192860B CRC64; MQEIQKSDRE RVIIVGCQLA DEDDDRFSYS MEELASLVHT AHGEVILQLS QKREAVHPAT YIGKGKVEEL ARLVEQLEPD VIIFNDELSP SQARNLSKLL EARVIDRTQL ILDIFAQRAR SKEGKLQVEL AQLQYLLPRL SGQGVQLSRL GGGIGTRGPG ETKLETDRRH IRRRVDEIKN QLKWVVEHRV RYRERRKKNR TFQIALVGYT NAGKSTLFNR LTNADSFEEN LLFATLDPLT RKFILPSGYT ALLTDTVGFI QDLPTTLVAA FRSTLEEVKE ADLILHVVDS SNLDYVQHEQ TVYDLLQDLE VSAIPIVTIY NKRDLADKNF IPSSRTDSIF ISALNETDLQ QLRQFIETAM IEAMEPYDVS VSACDGKLLA QLKTETILQT LHYHEEKEMY ECQGFILPEH PLYPQLKTAQ L // ID A0A160FPF7_9BURK Unreviewed; 395 AA. AC A0A160FPF7; DT 06-JUL-2016, integrated into UniProtKB/TrEMBL. DT 06-JUL-2016, sequence version 1. DT 07-JUN-2017, entry version 8. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=AYM40_13140 {ECO:0000313|EMBL:ANB74699.1}; OS Burkholderia sp. OLGA172. OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Burkholderia. OX NCBI_TaxID=1804984 {ECO:0000313|EMBL:ANB74699.1, ECO:0000313|Proteomes:UP000076852}; RN [1] {ECO:0000313|EMBL:ANB74699.1, ECO:0000313|Proteomes:UP000076852} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=OLGA172 {ECO:0000313|EMBL:ANB74699.1, RC ECO:0000313|Proteomes:UP000076852}; RX PubMed=27063562; DOI=10.1016/j.gene.2016.04.018; RA Ricker N., Shen S.Y., Goordial J., Jin S., Fulthorpe R.R.; RT "PacBio SMRT assembly of a complex multi-replicon genome reveals RT chlorocatechol degradative operon in a region of genome plasticity."; RL Gene 586:239-247(2016). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP014578; ANB74699.1; -; Genomic_DNA. DR RefSeq; WP_063497996.1; NZ_CP014578.1. DR EnsemblBacteria; ANB74699; ANB74699; AYM40_13140. DR Proteomes; UP000076852; Chromosome 1. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000076852}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000076852}. FT DOMAIN 196 367 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 162 189 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 395 AA; 43434 MW; 72EA938BFA004816 CRC64; MIPSNLINAA LVGIDFGKID FEASLEELSL LAQSAGANPL VTLTGRRSSP DAKMFVGSGK AEELRLACEA NDIELVIFNH ALAPAQQRNL EQALNRRVID RTSLILDIFA QRARSHEGKL QVELAQLQYL STRLIRAWTH LERQKGGIGL RGPGETQLET DRRLIGERIK ALKTRLEKLR RQHGTQRRAR SRNQTMSVSL VGYTNAGKST LFNALTKAQA YAADQLFATL DTTSRRVYLG DEAGQVVVSD TVGFIRELPH QLVAAFRATL EETIHADLLL HVVDASSAVR LDQIDQVNEV LHAIGADTIR QVLVFNKIDA VPELAARGDA VERDEYGNIS RVFLSARTGQ GLDTLRAAIA EIATAEPLSD TLVDLSEEDR SAAPREDRKV SELGH // ID A0A160ILI3_9BACI Unreviewed; 418 AA. AC A0A160ILI3; DT 06-JUL-2016, integrated into UniProtKB/TrEMBL. DT 06-JUL-2016, sequence version 1. DT 07-JUN-2017, entry version 10. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=ABE65_009105 {ECO:0000313|EMBL:ANC76951.1}; OS Fictibacillus phosphorivorans. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Fictibacillus. OX NCBI_TaxID=1221500 {ECO:0000313|EMBL:ANC76951.1, ECO:0000313|Proteomes:UP000076623}; RN [1] {ECO:0000313|EMBL:ANC76951.1, ECO:0000313|Proteomes:UP000076623} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=G25-29 {ECO:0000313|EMBL:ANC76951.1, RC ECO:0000313|Proteomes:UP000076623}; RA Zheng Z.; RT "Complete genome sequence of Fictibacillus phosphorivorans G25-29, a RT strain toxic to nematodes."; RL Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP015378; ANC76951.1; -; Genomic_DNA. DR RefSeq; WP_066393865.1; NZ_CP015378.1. DR EnsemblBacteria; ANC76951; ANC76951; ABE65_009105. DR KEGG; fpn:ABE65_009105; -. DR KO; K03665; -. DR Proteomes; UP000076623; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000076623}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000076623}. FT DOMAIN 202 362 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 418 AA; 47079 MW; 71BE143C276DE1CA CRC64; MNKNNDSVHE KAILVGCQLP RQNDERFFYS MEELKSLTKT AQGTVCAVVT QKRDRYDSAT FIGKGKVEEI ITLEEELEAD IIIFNSELSP SQVRNLSSHF NARVIDRTQL ILDIFAQRAK TREGKLQVEL AQLEYLLPRL SGIGASLSRL GGGIGTRGPG ETKLEKDRRH IRFRIHELKT QINSVVSHRE RYRERRKHQG AFQAALVGYT NAGKSTIFNK LTEADSYEED QLFATLDPLT RKVKLKSGFQ MLLTDTVGFI QDLPTSLIAA FRSTLEEAGE ANLLIHVIDG SSEDRNQHEQ TVKRILSDLK ASHIPMLTVY NKKDQFGEDF IPESPSISIS ALESIDISSL LETIEKEVMK QMTFYEVKVP SHDGKLLSQL RGETILIAQE FNKVELVYEC KGYALPSSSI PSISNKGE // ID A0A160KS45_9MICO Unreviewed; 517 AA. AC A0A160KS45; DT 06-JUL-2016, integrated into UniProtKB/TrEMBL. DT 06-JUL-2016, sequence version 1. DT 07-JUN-2017, entry version 10. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=A6122_1005 {ECO:0000313|EMBL:AND16154.1}; OS Rathayibacter tritici. OC Bacteria; Actinobacteria; Micrococcales; Microbacteriaceae; OC Rathayibacter. OX NCBI_TaxID=33888 {ECO:0000313|EMBL:AND16154.1, ECO:0000313|Proteomes:UP000077071}; RN [1] {ECO:0000313|EMBL:AND16154.1, ECO:0000313|Proteomes:UP000077071} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NCPPB 1953 {ECO:0000313|EMBL:AND16154.1, RC ECO:0000313|Proteomes:UP000077071}; RA Park J., Lee H.-H., Lee S.-W., Seo Y.-S.; RT "Complete genome sequence of Rathayibacter tritici NCPPB 1953."; RL Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP015515; AND16154.1; -; Genomic_DNA. DR RefSeq; WP_068252389.1; NZ_CP015515.1. DR EnsemblBacteria; AND16154; AND16154; A6122_1005. DR KEGG; rtn:A6122_1005; -. DR PATRIC; fig|33888.3.peg.1109; -. DR KO; K03665; -. DR Proteomes; UP000077071; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 2. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000077071}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000077071}. FT DOMAIN 292 457 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 517 AA; 55371 MW; 8D13B057224FFFE2 CRC64; MTEDLNETDT TEAVDVVSRV LANAQSRSTG YSRFVAGGAQ ALQSAGHAGE NSHGENSDGE QFDRDDRQAL RRVAGLSTEL EDVTEVEYRQ VRLENVVLIG VYSQNSLDDA ENSLHELAAL AETAGATVLD GLLQRRPHPD PSTYLGKGKA QELAGLVAAV GADTVVADTE LAPSQRRALE DVVKVKVIDR TAVILDIFSQ HATSREGKAQ VELAQLEYLL PRLRGWGESM SRQAGGQVGA GAGMGSRGPG ETKIELDRRR IHTRMARLRK QITAMKPARE AKRANRKRNA VPSVAIAGYT NAGKSSLLNR MTHAGVLVEN ALFATLDATV RKAQTSDGRV YTLADTVGFV RALPHQLVEA FRSTLEEVAD SDVIVHVVDA SHPDPAGQIA TVRDVIGEVG ARGIPEIIAF NKADLVDEGT RLVLRGLAPD AVFVSARSGE GIDELEARIA EILPEPDVQI DLLVPYDRGD VISHLHRSGR ILSTQYVEGG TRVIALVHAD LAGSLAEFQV PGAAVQA // ID A0A160MWX8_9GAMM Unreviewed; 437 AA. AC A0A160MWX8; DT 06-JUL-2016, integrated into UniProtKB/TrEMBL. DT 06-JUL-2016, sequence version 1. DT 07-JUN-2017, entry version 10. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=ATSB10_02470 {ECO:0000313|EMBL:AND67701.1}; OS Dyella thiooxydans. OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales; OC Rhodanobacteraceae; Dyella. OX NCBI_TaxID=445710 {ECO:0000313|EMBL:AND67701.1, ECO:0000313|Proteomes:UP000077255}; RN [1] {ECO:0000313|EMBL:AND67701.1, ECO:0000313|Proteomes:UP000077255} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATSB10 {ECO:0000313|EMBL:AND67701.1, RC ECO:0000313|Proteomes:UP000077255}; RA Lee Y., Hwangbo K., Chung H., Yoo J., Kim K.Y., Sa T.M., Um Y., RA Madhaiyan M.; RT "Complete genome sequencing and analysis of ATSB10, Dyella thiooxydans RT isolated from rhizosphere soil of sunflower (Helianthus annuus L.)."; RL Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP014841; AND67701.1; -; Genomic_DNA. DR RefSeq; WP_063670049.1; NZ_CP014841.1. DR EnsemblBacteria; AND67701; AND67701; ATSB10_02470. DR KEGG; dtx:ATSB10_02470; -. DR PATRIC; fig|445710.3.peg.245; -. DR KO; K03665; -. DR Proteomes; UP000077255; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000077255}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000077255}. FT DOMAIN 200 366 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 437 AA; 47418 MW; 9727A9A4B0F93327 CRC64; MFDRQKRGDR ALLVQPHSRG EGDAARRAEE FAELAKSAGA EILGTVPARV DVPNPRFYIG TGKADEVAEM ARALEADLVL VDHLLSPVQE RNLEKHLGVR VVDRAGLILD IFAQRARSHE GKLEVELAQL KHIATRLVRG WTHLDAQRGG AIGNRGPGET QLETDRRLLA ERVKMLTKRL EKVQVQRGQQ RRARLRNTVP RVALVGYTNA GKSTLFNAIT AGGVYAADQL FATLDPTVRR IEDLSCGPAV IADTVGFVRD LPHDLVAAFR GTLAEARDAD LLLHVSDAAD EERDRLHRVV DGVLEEIGAG DLPQLHVMNK IDLAGAEPRI VRDGEGRPVQ VWLSAGTGQG LELLREALGE LLGGDRVRSE LSLPLSAGRL HARLKAAGAI AGERVDEDGW HLDIDAPRSV IAPLSGGPGG DAVLLRDLLE RTAPPLE // ID A0A161GWL7_9RHOB Unreviewed; 413 AA. AC A0A161GWL7; DT 06-JUL-2016, integrated into UniProtKB/TrEMBL. DT 06-JUL-2016, sequence version 1. DT 07-JUN-2017, entry version 9. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=AKL17_2083 {ECO:0000313|EMBL:AMY69329.1}; OS Defluviimonas alba. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae; Defluviimonas. OX NCBI_TaxID=1335048 {ECO:0000313|EMBL:AMY69329.1, ECO:0000313|Proteomes:UP000076128}; RN [1] {ECO:0000313|EMBL:AMY69329.1, ECO:0000313|Proteomes:UP000076128} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cai42 {ECO:0000313|Proteomes:UP000076128}; RA Geng S., Pan X., Wu X.; RT "Complete genome sequence of Defluviimonas alba cai42t isolated from RT an oilfield in Xinjiang."; RL Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP012661; AMY69329.1; -; Genomic_DNA. DR EnsemblBacteria; AMY69329; AMY69329; AKL17_2083. DR KEGG; daa:AKL17_2083; -. DR PATRIC; fig|1335048.3.peg.2172; -. DR KO; K03665; -. DR Proteomes; UP000076128; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000076128}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000076128}. FT DOMAIN 191 360 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 413 AA; 45343 MW; 4965030259868F3E CRC64; MKSGPGHVRS RREPDLALAE AVALAIALPD LEVVGSEVVR LPRAQPGLLF GTGKVDELKA RMAEAEVDLV LVDGPVSPVQ QRNLEKAWKV KLLDRTGLIL EIFADRARTR EGVLQVELAA LNYQRTRLVR AWTHLERQRG GLGFVGGPGE TQIEADRRAI DEEVVKIRRQ LGKVVRTREL HRAARRKVPF PVVALVGYTN AGKSTLFNKM TGAEVMAKDM LFATLDPTMR GLVLPSGKKV ILSDTVGFIS DLPTQLVAAF RATLEEVLEA DLILHVRDIA HPETEEQAAD VGEILESLGV DEDVPMFEVW NKIDMLGPDT RAALLATDAR TPGVHAVSAL TGDGLETLLA AIGSVLDEER TEAVLHLGFE EGRARAYLHR ENVVLEEAEL ETGHRIHVRW TARQRAAYEA IPG // ID A0A161JH12_9PROT Unreviewed; 438 AA. AC A0A161JH12; DT 06-JUL-2016, integrated into UniProtKB/TrEMBL. DT 06-JUL-2016, sequence version 1. DT 05-JUL-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=A6A40_05190 {ECO:0000313|EMBL:ANC91347.1}; OS Azospirillum humicireducens. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales; OC Rhodospirillaceae; Azospirillum. OX NCBI_TaxID=1226968 {ECO:0000313|EMBL:ANC91347.1, ECO:0000313|Proteomes:UP000077405}; RN [1] {ECO:0000313|EMBL:ANC91347.1, ECO:0000313|Proteomes:UP000077405} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SgZ-5 {ECO:0000313|EMBL:ANC91347.1, RC ECO:0000313|Proteomes:UP000077405}; RX PubMed=23264502; DOI=10.1099/ijs.0.046813-0; RA Zhou S., Han L., Wang Y., Yang G., Zhuang L., Hu P.; RT "Azospirillum humicireducens sp. nov., a nitrogen-fixing bacterium RT isolated from a microbial fuel cell."; RL Int. J. Syst. Evol. Microbiol. 63:2618-2624(2013). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP015285; ANC91347.1; -; Genomic_DNA. DR EnsemblBacteria; ANC91347; ANC91347; A6A40_05190. DR KEGG; ahu:A6A40_05190; -. DR KO; K03665; -. DR Proteomes; UP000077405; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000077405}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000077405}. FT DOMAIN 209 380 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 438 AA; 48153 MW; AEB4CED127F7FCCB CRC64; MTNGNGAAPE GAARAIVVHP VLRNEADGDM RPPESRLEEA VGLAQAIQLD VIHAECAKVN RPQPSTLLGS GTVEQLAQVV EETEATLVIL DHALSPVQQR NLERSLKAKV IDRTGLILEI FGARARTREG MLQVELASLT YQKSRLVRSW THLERQRGGF GFLGGPGESQ LELDRRLIGD RIIKIKKELE EVRRTRGLHR KARAKVPYPV VALVGYTNAG KSTLFNRLAN ADVFAQNLLF ATLDPTMRQV TLPSGRKVIL SDTVGFISDL PHGLVAAFRA TLEEVDAADI ILHVRDIAHI DSDAQKADVH EVLSDMGIDP ETDDRVIEVL NKIDALDDES RAAILAQTGR NPRAVAVSAL SGEGIDDLDR LLDQRMNVNR QVVDLSVELG DGAALAWLYA KGEVLERRDD EERAHLHVSL DPADLARFEK RFQPQSQA // ID A0A161LUM4_9MICO Unreviewed; 503 AA. AC A0A161LUM4; DT 06-JUL-2016, integrated into UniProtKB/TrEMBL. DT 06-JUL-2016, sequence version 1. DT 07-JUN-2017, entry version 10. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=MHM582_1363 {ECO:0000313|EMBL:GAT72886.1}; OS Microbacterium sp. HM58-2. OC Bacteria; Actinobacteria; Micrococcales; Microbacteriaceae; OC Microbacterium. OX NCBI_TaxID=1778770 {ECO:0000313|EMBL:GAT72886.1, ECO:0000313|Proteomes:UP000077073}; RN [1] {ECO:0000313|Proteomes:UP000077073} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=HM58-2 {ECO:0000313|Proteomes:UP000077073}; RG Microbacterium sp. strain HM58-2 genome sequencing; RA Akiyama T., Ishige T., Kanesaki Y., Ito S., Oinumam K., Takaya N., RA Sasaki Y., Yajima S.; RL Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Proteomes:UP000077073} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=HM58-2 {ECO:0000313|Proteomes:UP000077073}; RA Akiyama T., Ishige T., Kanesaki Y., Ito S., Oinumam K., Takaya N., RA Sasaki Y., Yajima S.; RT "Draft genome sequence of Microbacterium sp. strain HM58-2 that RT catabolites acylhydrazides."; RL Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:GAT72886.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BDCY01000002; GAT72886.1; -; Genomic_DNA. DR RefSeq; WP_067351220.1; NZ_BDCY01000002.1. DR EnsemblBacteria; GAT72886; GAT72886; MHM582_1363. DR Proteomes; UP000077073; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 2. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000077073}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000077073}. FT DOMAIN 283 448 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 503 AA; 54537 MW; 7790DCAFB6DB58F1 CRC64; MTETPTHSTD DEAVERVLAN AEKRTEARVF GAAQALQDEA TAAHTATDGA QWDLEDRHAL RRVAGLSTEL EDVTEVEYRQ LRLENVVLVG VYPQGAQEDA ENSLRELAAL AETAGAVVLD GVLQRRPHPD AATYIGRGKA QELKDIVAAT GADTVIADTE LAPSQRRALE DVVKVKVIDR TTVILDIFSQ HAKSREGKAQ VELAQLEYLL PRLRGWGESM SRQAGGQVGA GGAGMGSRGP GETKIELDRR RIRTKMALLR RQIRDFAPAR EAKRAERKRN TIPSVAIAGY TNAGKSSLLN ALTSAGVLVE NALFATLDAT VRRSETSDGR VYTLTDTVGF VRNLPHQLVE AFRSTLEEVG DADVVLHVVD GSHPDPAGQL QTVRDVMGDV GVRDMPEIVV FNKADLLDED ERLVLRGLEP NAHFVSSRSG EGIPELRAAI EEALPKPAVE IRAVVPYDRG DLVAAIHETG MLLSVEHREE GTAVHARVSE RLAADLAPFA IES // ID A0A161QED4_9BACT Unreviewed; 446 AA. AC A0A161QED4; DT 06-JUL-2016, integrated into UniProtKB/TrEMBL. DT 06-JUL-2016, sequence version 1. DT 07-JUN-2017, entry version 7. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=AO396_00565 {ECO:0000313|EMBL:KZD17035.1}; OS candidate division Hyd24-12 bacterium Vib_1. OC Bacteria; candidate division Hyd24-12. OX NCBI_TaxID=1729715 {ECO:0000313|EMBL:KZD17035.1, ECO:0000313|Proteomes:UP000076781}; RN [1] {ECO:0000313|EMBL:KZD17035.1, ECO:0000313|Proteomes:UP000076781} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Vib_1 {ECO:0000313|EMBL:KZD17035.1}; RX PubMed=27058503; RA Kirkegaard R.H., Dueholm M.S., McIlroy S.J., Nierychlo M., Karst S.M., RA Albertsen M., Nielsen P.H.; RT "Genomic insights into members of the candidate phylum Hyd24-12 common RT in mesophilic anaerobic digesters."; RL ISME J. 0:0-0(2016). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KZD17035.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LKHD01000159; KZD17035.1; -; Genomic_DNA. DR EnsemblBacteria; KZD17035; KZD17035; AO396_00565. DR Proteomes; UP000076781; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR Gene3D; 3.40.50.10190; -; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR001357; BRCT_dom. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000076781}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000076781}. FT DOMAIN 207 365 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 168 202 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 446 AA; 48007 MW; BD3CAED1EF0EC0C3 CRC64; MGSRPAFGGG TERPGSEEEL FVAVSVTLSG ETPSPGAADE LASLVRTAGG RVVATVSQNR AFPDSSTFVG KGKLEELKAS VEACGVTSVV FDHNLAPAQV SRLEEAVGCK VLDRTELIMS IFARQARTSE SKLQVELAQL RYALPRLSGM WHHLSRLGGG IGTRGPGETQ LEVDKRKARA RIRVLEKELE RIAGRRDRLS RRRSDVFNVA LTGYTNTGKS TLLNSICGSE AYSADKLFAT LDSTTRRLDS PGGGTVFSDT VGFIDRLPEE LIASFYSTLS VVREADLLLL VGDASHPCRD LQTESVRATL ERIGAGGVPR LQVWNKMDIV SPDSAPVGGI LVSALTGAGL PDLLAAVECE RRSRLDWFRL TLSGSDGRLE NWLHENCVME SFERAGEGTR TLAGALMGIG SVRERLADED PSSWTLEPVP WADVSCSSES GRCRNG // ID A0A161RAX1_9MICO Unreviewed; 505 AA. AC A0A161RAX1; DT 06-JUL-2016, integrated into UniProtKB/TrEMBL. DT 06-JUL-2016, sequence version 1. DT 30-AUG-2017, entry version 10. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=AVW09_13640 {ECO:0000313|EMBL:KZE40635.1}; OS Microbacterium sp. T32. OC Bacteria; Actinobacteria; Micrococcales; Microbacteriaceae; OC Microbacterium. OX NCBI_TaxID=1776083 {ECO:0000313|EMBL:KZE40635.1, ECO:0000313|Proteomes:UP000076494}; RN [1] {ECO:0000313|Proteomes:UP000076494} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=T32 {ECO:0000313|Proteomes:UP000076494}; RA Hong K.W.; RT "Whole genome sequencing of Bhargavaea cecembensis T14."; RL Submitted (JAN-2016) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KZE40635.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LQQP01000016; KZE40635.1; -; Genomic_DNA. DR RefSeq; WP_063257951.1; NZ_LQQP01000016.1. DR EnsemblBacteria; KZE40635; KZE40635; AVW09_13640. DR Proteomes; UP000076494; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000076494}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}. FT DOMAIN 287 452 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 505 AA; 54250 MW; 95C315BCA6B980D5 CRC64; MTEQTTPPST DGSPVDPVDR VLALADAHRG VRVFGAAQAL QDASTAYGGS SDGDQWDREE RAALRRVPGL STELEDVTEV EYRQLRLENV VLVGVHPQGE QTDAENSLRE LAALAETAGA VVLDGVLQRR PHPDPATYVG RGKAEELRDI VAAVGADTVI ADTELAPSQR RALEDVVKVK VIDRTTVILD IFSQHAKSRE GKAQVELAQL EYLLPRLRGW GDSMSRQAGG QVGAGGAGMG SRGPGETKIE LDRRRIRTRM AQLRKQLRDF APAREAKRAE RKRHTIPSVA IAGYTNAGKS SLLNRLTSAG VLVENALFAT LDATVRRSET TDGRVYTLTD TVGFVRNLPH QLVEAFRSTL EEVGGADVIL HVVDGSHPDP AAQLSTVRDV MGDVDADFGH EIVVFNKADL LSPDDRLVLR GLAPAALFVS SRTGEGIAEL RAAIEAALPL PAVEVQAVVP YDRGDLVSAV HETGLIVAQE HREQGTFLHA HVGARLAAEL APFTG // ID A0A161RBF0_9FIRM Unreviewed; 406 AA. AC A0A161RBF0; DT 06-JUL-2016, integrated into UniProtKB/TrEMBL. DT 06-JUL-2016, sequence version 1. DT 07-JUN-2017, entry version 7. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:KYO68689.1}; GN ORFNames=ATZ99_01980 {ECO:0000313|EMBL:KYO68689.1}; OS Thermovenabulum gondwanense. OC Bacteria; Firmicutes; Clostridia; Thermoanaerobacterales; OC Thermoanaerobacterales Family III. Incertae Sedis; Thermovenabulum. OX NCBI_TaxID=520767 {ECO:0000313|EMBL:KYO68689.1, ECO:0000313|Proteomes:UP000075737}; RN [1] {ECO:0000313|EMBL:KYO68689.1, ECO:0000313|Proteomes:UP000075737} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=R270 {ECO:0000313|EMBL:KYO68689.1, RC ECO:0000313|Proteomes:UP000075737}; RA Patel B.K.; RT "Draft genome of Thermovenabulum gondwanense isolated from a red RT thermophilic microbial mat colonisisng an outflow channel of a bore RT well."; RL Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KYO68689.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LOHZ01000015; KYO68689.1; -; Genomic_DNA. DR EnsemblBacteria; KYO68689; KYO68689; ATZ99_01980. DR PATRIC; fig|520767.4.peg.207; -. DR Proteomes; UP000075737; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000075737}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000075737}. FT DOMAIN 190 353 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 406 AA; 45489 MW; 8ECA8303612C6749 CRC64; MASNTKAIVA GIVKNIQDEE SIEELELLAK TAGAEVVAKV VQRKTSYDSA FYIGKGKAQE IAEVAKALEA NAVIFDDDLT PVQIRNLENL IELQIIDRTT LILDIFAQRA KSKEGKIQVE LAQLQHLLPR LTGKGIELSR FGGGIGTRGP GETKLETDKR HIKRRISYLK KELQKIKDSR HLLRSARKFP VISLVGYTNA GKSTLMNALT NAKVSSNDRL FDTLDTTTRL LILPDGRKAL LSDTVGFIRK LPHEIVEAFK ATLEEIKEAD LLLLVADGSS RNFEEEINTV FKVLKDIQAD NKPIVIAINK VDKINSSFIL PLNSKNTVEI SALYKKNLDE LLKRICENLS KTRKFAEFLI PYDKLSIVDI IYQNGLIFSK ESLPEGVKIQ GEIEEFVINK YKNFLI // ID A0A161SGG7_9NEIS Unreviewed; 378 AA. AC A0A161SGG7; DT 06-JUL-2016, integrated into UniProtKB/TrEMBL. DT 06-JUL-2016, sequence version 1. DT 07-JUN-2017, entry version 9. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=AVW16_09530 {ECO:0000313|EMBL:KZE32630.1}; OS Crenobacter luteus. OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Crenobacter. OX NCBI_TaxID=1452487 {ECO:0000313|EMBL:KZE32630.1, ECO:0000313|Proteomes:UP000076625}; RN [1] {ECO:0000313|Proteomes:UP000076625} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CN10 {ECO:0000313|Proteomes:UP000076625}; RA Hong K.W.; RT "Draft genome of Chromobacterium sp. F49."; RL Submitted (JAN-2016) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KZE32630.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LQQU01000017; KZE32630.1; -; Genomic_DNA. DR RefSeq; WP_066611416.1; NZ_LQQU01000017.1. DR EnsemblBacteria; KZE32630; KZE32630; AVW16_09530. DR Proteomes; UP000076625; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000076625}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000076625}. FT DOMAIN 198 364 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 378 AA; 41725 MW; F3D1384C5E1D18B0 CRC64; MFDRPDIGDK AVLVCLDFGE PDYADGVAEC VDLVKSSGVE VLDVVEARRS RPDAALFAGK GKVEEIAALV KMYSANVVIF NHSLSPAQER NLERAIQCRV VDRVSLILDI FAQRARSHEG KLQVELAQLN HLATRLVRGW THLERQKGGI GLRGPGETQL ETDRRLLGKR VKLLKDRLEA VGRQRKTQRR GRERNGVYSV SIVGYTNAGK STLFNSLTKA RAYAADQLFA TLDTTSRRLY LNENVSLVVS DTVGFIRDLP HTLVAAFRAT LEETIEADLL LHVVDSANEA RDKQIEEVDK VLAEIGADDI PQLIVWNKTD LKGLPPGMER DELGRLVAVR VSALTGEGLD LLRAALIERV TGESPESGND EQENDVTA // ID A0A161SRQ5_9MICO Unreviewed; 508 AA. AC A0A161SRQ5; DT 06-JUL-2016, integrated into UniProtKB/TrEMBL. DT 06-JUL-2016, sequence version 1. DT 07-JUN-2017, entry version 9. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:KZE90186.1}; GN ORFNames=AVP41_01596 {ECO:0000313|EMBL:KZE90186.1}; OS Microbacterium sp. TNHR37B. OC Bacteria; Actinobacteria; Micrococcales; Microbacteriaceae; OC Microbacterium. OX NCBI_TaxID=1775956 {ECO:0000313|EMBL:KZE90186.1, ECO:0000313|Proteomes:UP000076535}; RN [1] {ECO:0000313|EMBL:KZE90186.1, ECO:0000313|Proteomes:UP000076535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=TNHR37B {ECO:0000313|EMBL:KZE90186.1, RC ECO:0000313|Proteomes:UP000076535}; RA Adelskov J., Patel B.K.; RT "Draft Genome Sequence of Microbacterium sp. TNHR37B isolated from the RT Great Artesian Basin of Australia."; RL Submitted (JAN-2016) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KZE90186.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LQGV01000002; KZE90186.1; -; Genomic_DNA. DR RefSeq; WP_067163048.1; NZ_LQGV01000002.1. DR EnsemblBacteria; KZE90186; KZE90186; AVP41_01596. DR PATRIC; fig|1775956.3.peg.1589; -. DR Proteomes; UP000076535; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 2. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000076535}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000076535}. FT DOMAIN 287 452 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 508 AA; 54972 MW; 4823401A520D324A CRC64; MTDTSTSHDA DETSVDPVDR VLAHAEGRSG VRVFGAAQAL QHESTVAYGD TDGEQWDREE RAALRRVAGL STELEDVTEV EYRQLRLENV VLVGVYPQGS QEDAENSLRE LAALAETAGA VVLDGVLQRR PHPDPATYIG RGKAAELRDL VAAVGADTVI ADTELAASQR RALEDVVKVK VIDRTTVILD IFSQHAKSRE GKAQVELAQL EYLLPRLRGW GESMSRQAGG QVGAGGAGMG SRGPGETKIE LDRRRIRTRM AQLRRQIRDF APARDAKRAE RKRHTIPSVA IAGYTNAGKS SLLNRLTSAG VLVENALFAT LDATVRRAQA SDGRVYTLTD TVGFVRNLPH QLVEAFRSTL EEVGDADVIV HVVDGSHPDP AAQVTTVREV MADVGARSTR EIIVFNKADL VDDDTRLVLR GLEPQAVFVS SRTGEGIDEL RAAIEEALPL PAVEVRALVP YDRGDLVNAV HESGHLLSTE HHEDGTVLHA HVNERLAAEL APYAVAAG // ID A0A161YRX0_9CLOT Unreviewed; 593 AA. AC A0A161YRX0; DT 06-JUL-2016, integrated into UniProtKB/TrEMBL. DT 06-JUL-2016, sequence version 1. DT 07-JUN-2017, entry version 10. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX_1 {ECO:0000313|EMBL:KZL93752.1}; GN Synonyms=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=CLMAG_08030 {ECO:0000313|EMBL:KZL93752.1}; OS Clostridium magnum DSM 2767. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=1121326 {ECO:0000313|EMBL:KZL93752.1, ECO:0000313|Proteomes:UP000076603}; RN [1] {ECO:0000313|EMBL:KZL93752.1, ECO:0000313|Proteomes:UP000076603} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 2767 {ECO:0000313|EMBL:KZL93752.1, RC ECO:0000313|Proteomes:UP000076603}; RA Poehlein A., Uhlig R., Fischer R., Bahl H., Daniel R.; RT "Genome sequence of Clostridium magnum DSM 2767."; RL Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KZL93752.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LWAE01000001; KZL93752.1; -; Genomic_DNA. DR RefSeq; WP_066618167.1; NZ_LWAE01000001.1. DR EnsemblBacteria; KZL93752; KZL93752; CLMAG_08030. DR PATRIC; fig|1121326.3.peg.761; -. DR Proteomes; UP000076603; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000076603}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000076603}. SQ SEQUENCE 593 AA; 66449 MW; 87F895DA931EE29A CRC64; MVYGNIEGVK NFILEKLNGV YDIRVPRDSI CTEELISIIS EATIYLNREV SVAVNRKGTV VAVAVGDSST VEMPEIDVKE KKLCGVRIIH THPNGNSRLS AIDMSALLKL KLDCIAAIGV CDKGCTDITL GFCSIENDIL VGEMTRPLSI DQTIQYNILD KVKYIENLLK NEDIIDDDSE RAVLVGVDDE ESIDELAELA KACNVKVVEK VLQKRSSIDT AFYVGKGKVE EIGLLRQACG ANVVIFDDEL SASQVRNLEE NIGAKVIDRT TLILEIFARR ARSRESKIQV ELAQLKYRLP RLSGLGTVLS RTGGGIGTRG PGEKKLEVDK RHIREKIYDL MRELKKIKLV RETQRERRNN IPKVSLVGYT NAGKSTLRNK LCEIAMPKET AQKEKVFEAD MLFATLDITT RAIELPDSRT ITVTDTVGFI KKLPHDLVEA FKSTLEEVTY ADLLLHVVDA SSSTAEEQID AVNNVLMQLG VKDKPTMLVL NKIDRASEEH IKSIQEKYSN INTISISAKQ EINIDLLLDE VSKLLPYTMK KAEYIVPYNE QSIVAFLHRN AKVESEEYKD EGTYISAIVD DEVYNKCERY MIK // ID A0A161ZW98_9BACI Unreviewed; 401 AA. AC A0A161ZW98; DT 06-JUL-2016, integrated into UniProtKB/TrEMBL. DT 06-JUL-2016, sequence version 1. DT 05-JUL-2017, entry version 9. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=AZI98_02625 {ECO:0000313|EMBL:KZN97687.1}; OS Aeribacillus pallidus. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Aeribacillus. OX NCBI_TaxID=33936 {ECO:0000313|EMBL:KZN97687.1, ECO:0000313|Proteomes:UP000076476}; RN [1] {ECO:0000313|EMBL:KZN97687.1, ECO:0000313|Proteomes:UP000076476} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=8m3 {ECO:0000313|EMBL:KZN97687.1, RC ECO:0000313|Proteomes:UP000076476}; RA Poltaraus A.B., Nazina T.N., Tourova T.P., Malakho S.M., RA Korshunova A.V., Sokolova D.S.; RT "Draft genome sequence of Aeribacillus pallidus 8m3 from petroleum RT reservoir."; RL Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KZN97687.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LWBR01000007; KZN97687.1; -; Genomic_DNA. DR EnsemblBacteria; KZN97687; KZN97687; AZI98_02625. DR Proteomes; UP000076476; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000076476}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000076476}. FT DOMAIN 183 345 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 401 AA; 45634 MW; 5D70384F84DD834A CRC64; METDEEQFFY LMEELKSLTA AAGGQVAAVC TQNRLRAEPS TYIGKGKVDE IKQLIETTEA NTVIFNNELS PSQLRNLARL LEVKVIDRTQ LILDIFSKRA KSREGKLQVE LAQLEYLLPR LSGHGLNLSR QGGGIGTRGP GETKLETDQR HIRNRIHDIK QQLSHIVSHR ERYRSQRKRN HQTQIALVGY TNAGKSTLFN KLTAADSFQE DMVFATLDPM TRKMFLPSGM KVLMTDTVGF IQQLPTSLIA AFRSTLEEIK EADLLLHIVD SSHPDYIQHE NTVNELLKEL GTDGLPVLTV YNKKDQQLEH FFPSLKEDYI VISAFCDEDI ERLKTAIEEK LKKKMHPYVV SVPTGDGKRL SLLKANTLVS TLQFDEQNQH YIVSGLVFRD HPVYDQIMKN K // ID A0A162AJL1_DAUCA Unreviewed; 560 AA. AC A0A162AJL1; DT 06-JUL-2016, integrated into UniProtKB/TrEMBL. DT 06-JUL-2016, sequence version 1. DT 07-JUN-2017, entry version 7. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:KZN02043.1}; GN ORFNames=DCAR_010797 {ECO:0000313|EMBL:KZN02043.1}; OS Daucus carota subsp. sativus. OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae; OC Pentapetalae; asterids; campanulids; Apiales; Apiaceae; Apioideae; OC Scandiceae; Daucinae; Daucus; Daucus sect. Daucus. OX NCBI_TaxID=79200 {ECO:0000313|EMBL:KZN02043.1, ECO:0000313|Proteomes:UP000077755}; RN [1] {ECO:0000313|EMBL:KZN02043.1, ECO:0000313|Proteomes:UP000077755} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. DH1 {ECO:0000313|Proteomes:UP000077755}; RC TISSUE=Leaf {ECO:0000313|EMBL:KZN02043.1}; RX PubMed=27158781; DOI=10.1038/ng.3565; RA Iorizzo M., Ellison S., Senalik D., Zeng P., Satapoomin P., Huang J., RA Bowman M., Iovene M., Sanseverino W., Cavagnaro P., Yildiz M., RA Macko-Podgorni A., Moranska E., Grzebelus E., Grzebelus D., RA Ashrafi H., Zheng Z., Cheng S., Spooner D., Van Deynze A., Simon P.; RT "A high-quality carrot genome assembly provides new insights into RT carotenoid accumulation and asterid genome evolution."; RL Nat. Genet. 48:657-666(2016). CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KZN02043.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LNRQ01000003; KZN02043.1; -; Genomic_DNA. DR RefSeq; XP_017242153.1; XM_017386664.1. DR GeneID; 108214583; -. DR Proteomes; UP000077755; Chromosome 3. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR CDD; cd01878; HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000077755}; KW Reference proteome {ECO:0000313|Proteomes:UP000077755}. FT DOMAIN 286 535 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 560 AA; 61871 MW; 0A5DE4F1F75F57CE CRC64; MLRAISHIRN SISQTLTNPT QLPSCYLLTS HSQARLRHRE SKSDESNTDP NTPPRLFVVQ PKIRPDSVLK LKLEEALNLA NSLEEQRDGF YATEFSDKDL PSHLVVQNPA ARTTRADTYF GLGTVNNVKC HLNAADSGDG FDAVFVNAIL SGVQQRNLEQ AWGKPVLDRV SLIIEIFHAH AQTKEAKLQA ELAALMYKRS RLVRVRGPGG RYTFGGEVEV VSARGRGSGG RGFISGAGET ELQLQRRRII ERRNQLLSEI KEVRRTRALQ RASRKRQGRS DGQDMATIAV VGYTNAGKST LVSALSDTYL YSDDRLFATV DPKLRSVVLP SGRKVLLSDT VGFISELPVQ LVEAFHATLE EVVEADLLVH VLDSSAPNLD EHRQTVMQVL EQLGVSKEKL QNMIEVWNKI DIGEKQIDGD ETGAGEDVEF EHLSDDQEDN SNADVEELSL GNDEGDYSDG WLASENGQVT LSDNDGSSLG CKNTNDLQEN PCMIIDNGSQ CQPENVGPHV KTSALTGVGL QELLELIDER LEVQKVVHRS MFNSKWRPLN ADEAVVAAEQ // ID A0A162NXL9_9BACT Unreviewed; 409 AA. AC A0A162NXL9; DT 06-JUL-2016, integrated into UniProtKB/TrEMBL. DT 06-JUL-2016, sequence version 1. DT 12-APR-2017, entry version 6. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=A1D16_20720 {ECO:0000313|EMBL:KYP13887.1}; OS Flavihumibacter sp. CACIAM 22H1. OC Bacteria; Bacteroidetes; Chitinophagia; Chitinophagales; OC Chitinophagaceae; Flavihumibacter. OX NCBI_TaxID=1812911 {ECO:0000313|EMBL:KYP13887.1, ECO:0000313|Proteomes:UP000075747}; RN [1] {ECO:0000313|EMBL:KYP13887.1, ECO:0000313|Proteomes:UP000075747} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CACIAM 22H1 {ECO:0000313|EMBL:KYP13887.1}; RA Moraes P.G., Lima A.R.; RT "Draft Genome of Flavihumibacter sp. CACIAM 22H1."; RL Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KYP13887.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LUKG01000064; KYP13887.1; -; Genomic_DNA. DR Proteomes; UP000075747; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000075747}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000075747}. FT DOMAIN 205 387 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 409 AA; 47270 MW; 0C668ED9FDF94E80 CRC64; MEENLIEKKQ IAENERTVLV GVVQKDQTDQ QVREYLDELA FLAETAGAEA VKRFTQKLAH PDSKTFVGKG KLEEIKEYIS GRNINLVIFD DELTGSQITN IEKALGVKTI DRSDLILDIF ARRAKTAQAK TQVELAQYQY LLPRLKGMWK HLERQGGGIG TRGPGETEIE TDRRIVKEKI ALLRKRLSEI DKQSFTQRKD RGEFIRVALV GYTNVGKSTI MNLLSKSEVF AENKLFATLD TTTRKVVFDT TPFLLSDTVG FIRKLPHHLV ESFKSTLDEV READILLHVV DLSHPQYEDQ FNVVNKTLQE LKVTEKPMIT IFNKLDQYEK NTFDDWLEPE VKTQILEELR ERWENSTLGN CVFISAVERR NLEGLRATIL SKVRKLYRER YPYKTEFFGS FEQQDEGQE // ID A0A162Q1E1_9BACL Unreviewed; 432 AA. AC A0A162Q1E1; DT 06-JUL-2016, integrated into UniProtKB/TrEMBL. DT 06-JUL-2016, sequence version 1. DT 07-JUN-2017, entry version 10. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=PBAT_22290 {ECO:0000313|EMBL:OAB41280.1}; OS Paenibacillus antarcticus. OC Bacteria; Firmicutes; Bacilli; Bacillales; Paenibacillaceae; OC Paenibacillus. OX NCBI_TaxID=253703 {ECO:0000313|EMBL:OAB41280.1, ECO:0000313|Proteomes:UP000077355}; RN [1] {ECO:0000313|EMBL:OAB41280.1, ECO:0000313|Proteomes:UP000077355} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CECT 5836 {ECO:0000313|EMBL:OAB41280.1, RC ECO:0000313|Proteomes:UP000077355}; RA Shin S.-K., Yi H.; RT "Draft genome sequence of Paenibacillus antarcticus CECT 5836."; RL Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:OAB41280.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LVJI01000048; OAB41280.1; -; Genomic_DNA. DR RefSeq; WP_068652870.1; NZ_LVJI01000048.1. DR EnsemblBacteria; OAB41280; OAB41280; PBAT_22290. DR Proteomes; UP000077355; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000077355}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000077355}. FT DOMAIN 209 373 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 168 202 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 432 AA; 48224 MW; BC391DCCF85E7D27 CRC64; MANNITFDTE TDIPDRAVLV SLVTDAVKKK GINPEYSLHE LMQLAETAGV EVMDTISQNL AKPDPKFFIG KGKVEELRMA MEAVDATTAI FDHELSGAQV RHLEESLDVK IIDRTQLILD IFAQRANTRE GIIQVELAQL TYLLPRLSGH STNLSRLGGG IGTRGPGESK LEMDRRHIRN RVNDLKDQLE EITKHRTLYR ERRQKAGVFQ VALVGYTNAG KSTLLKELTD ADVYIQDQLF ATLDPTTRVL ELPTGKEVVI TDTVGFIQNL PHDLIAAFRA TLEEANEANL ILHVVDASSE MREDQMAVVQ SILVDLGASD KPQIVLYNKK DRCTPEQLEM LNTGEGHLTI SAFDEADLLA IRDAIQTILT GDTIIFRIPA DRGDLASLLY RVGEIVNQEF DGSDSLYEVI LHKDDYVKNG YLLQDYIEVS HT // ID A0A162SXK9_9CLOT Unreviewed; 414 AA. AC A0A162SXK9; DT 06-JUL-2016, integrated into UniProtKB/TrEMBL. DT 06-JUL-2016, sequence version 1. DT 07-JUN-2017, entry version 10. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX_2 {ECO:0000313|EMBL:KZL91999.1}; GN Synonyms=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=CLMAG_18050 {ECO:0000313|EMBL:KZL91999.1}; OS Clostridium magnum DSM 2767. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=1121326 {ECO:0000313|EMBL:KZL91999.1, ECO:0000313|Proteomes:UP000076603}; RN [1] {ECO:0000313|EMBL:KZL91999.1, ECO:0000313|Proteomes:UP000076603} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 2767 {ECO:0000313|EMBL:KZL91999.1, RC ECO:0000313|Proteomes:UP000076603}; RA Poehlein A., Uhlig R., Fischer R., Bahl H., Daniel R.; RT "Genome sequence of Clostridium magnum DSM 2767."; RL Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KZL91999.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LWAE01000002; KZL91999.1; -; Genomic_DNA. DR RefSeq; WP_066621075.1; NZ_LWAE01000002.1. DR EnsemblBacteria; KZL91999; KZL91999; CLMAG_18050. DR PATRIC; fig|1121326.3.peg.1789; -. DR Proteomes; UP000076603; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000076603}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000076603}. SQ SEQUENCE 414 AA; 47082 MW; 8EAD5FB971D7E260 CRC64; MKQKQRAVIV GCNLKDDKEF LNMMEELCSL ANACDIELVG EITQKLERVY PSHYLGRGKI QELFTLIHEK DVNMVIFNDE LSPSQIRNLY TALKCKVIDR TVLILDILAK RSKSKEAQLQ VEIAKLQYIL PRVTGLGETL GHQAFGTGFI NKGSGETKLE LDHKKIKDRT SGLHAELETL VVQRQNQRKQ RKKSGIPVVV LVGYTNAGKS SIMNSMIDLY SSSIDKKVFE KDMLFATLET YVRNIKLPDN KSFLLSDTVG FISKLPRQLV NAFRSTLEEI TEADLLVHVV DCSNPNYKQY IEVTKKTLKE LGAGNIPIIY AYNKTDLVEG EITKDKKDCI YISAKNKAGI GELVNEICKK TFLQYVYCEL LIPYEKGNLL SYFKNNANIK SIKYNSNGVL ISMECKESDY RRYK // ID A0A162Z6P9_9FLAO Unreviewed; 402 AA. AC A0A162Z6P9; DT 06-JUL-2016, integrated into UniProtKB/TrEMBL. DT 06-JUL-2016, sequence version 1. DT 07-JUN-2017, entry version 9. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=AWE51_08020 {ECO:0000313|EMBL:KZS39589.1}; OS Aquimarina sp. RZW4-3-2. OC Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales; OC Flavobacteriaceae; Aquimarina. OX NCBI_TaxID=1642818 {ECO:0000313|EMBL:KZS39589.1, ECO:0000313|Proteomes:UP000076715}; RN [1] {ECO:0000313|EMBL:KZS39589.1, ECO:0000313|Proteomes:UP000076715} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=RZW4-3-2 {ECO:0000313|EMBL:KZS39589.1, RC ECO:0000313|Proteomes:UP000076715}; RA Wang Y.; RT "The draft genome sequence of Aquimarina sp. RZW4-3-2."; RL Submitted (JAN-2016) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KZS39589.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LQRT01000024; KZS39589.1; -; Genomic_DNA. DR RefSeq; WP_066315195.1; NZ_LQRT01000024.1. DR EnsemblBacteria; KZS39589; KZS39589; AWE51_08020. DR Proteomes; UP000076715; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000076715}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000076715}. FT DOMAIN 200 385 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 402 AA; 46622 MW; BCA749845D0BEE6E CRC64; MLEHKEIAYE RTVLIGIITK NQDEEKLDEF LDELEFLTYT AGGEVVKRFT QKMDMPNSKT FIGSGKMEDV RVYVEQHDIG TVVFDDELTP AQMRNIERIL KAKIIDRTNL ILDIFAQRAQ TSYARTQVEL AQYQYLLPRL TGLWTHLERQ RGGIGMRGPG ETEIETDRRI VRDRISLLKK KLLTIDKQMA TQRGNRGKLV RVALVGYTNV GKSTLMNVIA KSKVFAENKL FATLDTTVRK VVIGNLPFLL SDTVGFIRKL PTQLVESFKS TLDEVREADL LLHVVDISHP QFEDHIESVN KILGEIDCRD KATIMVFNKI DTYEHETIDA DDLTTERTKA HYTLEEWKQT WMSRIGDNAL FISAIQKENI EDFRKRVYKE VRDIHVTRFP YNNFLYPEIV EE // ID A0A163UUP6_9RHOB Unreviewed; 468 AA. AC A0A163UUP6; DT 06-JUL-2016, integrated into UniProtKB/TrEMBL. DT 06-JUL-2016, sequence version 1. DT 07-JUN-2017, entry version 8. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=OA90_16905 {ECO:0000313|EMBL:KZM49131.1}; OS Labrenzia sp. OB1. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae; Labrenzia. OX NCBI_TaxID=1561204 {ECO:0000313|EMBL:KZM49131.1, ECO:0000313|Proteomes:UP000076616}; RN [1] {ECO:0000313|EMBL:KZM49131.1, ECO:0000313|Proteomes:UP000076616} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=OB1 {ECO:0000313|EMBL:KZM49131.1, RC ECO:0000313|Proteomes:UP000076616}; RA Paerl R.W., Allen E., Palenik B., Azam F.; RT "Marine bacterioplankton release vitamin B1 sources."; RL Submitted (OCT-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KZM49131.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JSEP01000012; KZM49131.1; -; Genomic_DNA. DR EnsemblBacteria; KZM49131; KZM49131; OA90_16905. DR PATRIC; fig|1561204.3.peg.1007; -. DR Proteomes; UP000076616; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000076616}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000076616}. FT DOMAIN 240 410 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 468 AA; 51538 MW; 828073F4B735213E CRC64; MKPKSRADDF SKSNGSEEPG QASLRLKETG VDRLPQAFRA MILEPVLQLR GDGGQHDLRS NRSPEARLEE AIGLSAAINL NIVHSGIVRI SNPKPATLFG EGKVAEFAGI VASEDLDLVV IDHPLSPVQQ RNLERRLKTK VIDRTGLILE IFGDRARTKE GRLQVDLAHL SWQKSRLVRS WTHLERQRGG AGFMGGPGET QIEADRRQIQ DRIIALQKQL QGVRRTRDLH RKKRKKIPQP VVALVGYTNA GKSTLFNRLT EADVFAKDLL FATLDPTLRK VSLPHGREVI VSDTVGFISD LPTHLVAAFR ATLEEVLEAD LILHVRDISH ADTDAQAEDV RKTLSDLGVD AISGAPVVEV WNKIDCLDPA YRQKLLEDAG EEGPIALSAL TGEGVGGLLA RMDAFMAQHD DILALKIPVA EGALLAKLYQ LAEVLERTDA EDFVTAEVRV SDKQRGPFRD TFGAHIVD // ID A0A163ZW18_9BRAD Unreviewed; 460 AA. AC A0A163ZW18; DT 06-JUL-2016, integrated into UniProtKB/TrEMBL. DT 06-JUL-2016, sequence version 1. DT 07-JUN-2017, entry version 9. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=A4A58_25420 {ECO:0000313|EMBL:KZD23936.1}; OS Tardiphaga robiniae. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Bradyrhizobiaceae; Tardiphaga. OX NCBI_TaxID=943830 {ECO:0000313|EMBL:KZD23936.1, ECO:0000313|Proteomes:UP000076574}; RN [1] {ECO:0000313|EMBL:KZD23936.1, ECO:0000313|Proteomes:UP000076574} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Vaf07 {ECO:0000313|EMBL:KZD23936.1, RC ECO:0000313|Proteomes:UP000076574}; RA Kopat V., Chirak E., Kimeklis A., Andronov E.; RT "Microsymbionts genomes from the relict species Vavilovia formosa RT (Stev.) Fed."; RL Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KZD23936.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LVYV01000007; KZD23936.1; -; Genomic_DNA. DR RefSeq; WP_068731832.1; NZ_LVYV01000007.1. DR EnsemblBacteria; KZD23936; KZD23936; A4A58_25420. DR Proteomes; UP000076574; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000076574}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000076574}. FT DOMAIN 225 399 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 460 AA; 50945 MW; 4204711403307B50 CRC64; MEFRSFEGNA ADRPSASSES TGRVLVVGPY MRERRGDADA QAYSHVRDTE ARLEEAVGLA RAIDLTVVEA VAAPLSQIRP ATYLGKGKVE EIAGLIAANE IGIVVMDCAL SPIQQRNLEK ELKAKVLDRT GLILEIFGRR AKTKEGTLQV ELAHLNYQRS RLVRSWTHLE RQRGGFGFMG GPGETQIEAD RRMIGDRIAR LEADLRKVQA TRRLHRAGRQ RVPYRVVALV GYTNAGKSTL FNRLTRADVQ AEDMLFATLD PTLRALTLPH GGKAMLSDTV GFISNLPTQL VAAFRATLEE VLEADIILHV RDISHEDADA QQSDVDKVLR QLGIDTDASA RILEVWNKID RFSPDERENL ANIAARRPPE KPCFMVSAET GEGIDALLNA IEERLAAARV TLDLQIDAAD GAGVSWLHRN AEILVKELHD GHFDMVVRVD ETKRDVVISK YGAVLHPVEY // ID A0A164BJ93_9SYNE Unreviewed; 570 AA. AC A0A164BJ93; DT 06-JUL-2016, integrated into UniProtKB/TrEMBL. DT 06-JUL-2016, sequence version 1. DT 07-JUN-2017, entry version 10. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:KZR88793.1}; GN ORFNames=MITS9508_01972 {ECO:0000313|EMBL:KZR88793.1}; OS Synechococcus sp. MIT S9508. OC Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; OC Synechococcus. OX NCBI_TaxID=1801629 {ECO:0000313|EMBL:KZR88793.1, ECO:0000313|Proteomes:UP000076799}; RN [1] {ECO:0000313|EMBL:KZR88793.1, ECO:0000313|Proteomes:UP000076799} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MIT S9508 {ECO:0000313|EMBL:KZR88793.1, RC ECO:0000313|Proteomes:UP000076799}; RA Cubillos-Ruiz A., Berta-Thompson J.W., Becker J.W., Chisholm S.W.; RT "Evolutionary Radiation of Lanthipeptides in Marine RT Picocyanobacteria."; RL Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KZR88793.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LVHU01000009; KZR88793.1; -; Genomic_DNA. DR RefSeq; WP_067096679.1; NZ_LVHU01000009.1. DR EnsemblBacteria; KZR88793; KZR88793; MITS9508_01972. DR PATRIC; fig|1801629.3.peg.2096; -. DR Proteomes; UP000076799; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000076799}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000076799}. FT DOMAIN 380 552 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 570 AA; 62969 MW; 7E51CE3381F5E32F CRC64; MKQAHLAGRT RGLRPSQLKQ LDRLSHRRHP DDSGADVFTL ERLAELAVKL EETLHLLIDD RGVCRLLWVG PLGESDRLDR HLQGGSRRRP RQWRLISTLH ERRSPDLVPD GRDAVIALDV QPESWLRYQA VISPSGIRSG ALWVPNPQAE SGWSCGETGD LTILCHCDTP AGQGDPHSEP FQSAQEHTAT VDQVLLLTLT GTDPARNERE LAELEGLARS AGANTVAVCR QRQGQINPHT LWGRGKLQEA ALDIRKHGAT LVITDRELTP VQARNLERLL DSPVMDRSEL ILDIFAQRAS SAAGRLQVEL AQLRYRLPRL AGRGLSLSRQ GGGIGTRGPG ETQLEKDKRA ISRRIEHLGR EFRQLGAHRA RLRERRQDIP SVALVGYTNA GKSSLLNALC DRAQGGPVQA ENILFATLDP TTRRLCLPRA GAAPRELLIT DTVGFIRELP APLMQAFMAT LEETRNADQL LLVVDLGDPD WQGQLKAVHS ILDSLGCEQP RQVLANQIDR CDAEALQQIR ELEPEALYLS ATQGTGLRGL RTWLEQTFWE STPETVSPPV TEPTGAPPNG // ID A0A164LQI1_9NOCA Unreviewed; 479 AA. AC A0A164LQI1; DT 06-JUL-2016, integrated into UniProtKB/TrEMBL. DT 06-JUL-2016, sequence version 1. DT 05-JUL-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=A2J03_05650 {ECO:0000313|EMBL:KZF05507.1}; OS Rhodococcus sp. EPR-157. OC Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae; OC Rhodococcus. OX NCBI_TaxID=1813677 {ECO:0000313|EMBL:KZF05507.1, ECO:0000313|Proteomes:UP000077673}; RN [1] {ECO:0000313|EMBL:KZF05507.1, ECO:0000313|Proteomes:UP000077673} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=EPR-157 {ECO:0000313|EMBL:KZF05507.1, RC ECO:0000313|Proteomes:UP000077673}; RA Ploux O.; RL Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KZF05507.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LVCV01000345; KZF05507.1; -; Genomic_DNA. DR EnsemblBacteria; KZF05507; KZF05507; A2J03_05650. DR Proteomes; UP000077673; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 2. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000077673}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000077673}. FT DOMAIN 252 421 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 211 245 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 479 AA; 51797 MW; 15FD862F38300E9B CRC64; MARSPIAASN TDEDSNPSSG DMQLEERTAL RRVAGLSTEL ADVTEVEYRQ LRLERVVLVG VWTTGTAAQV ESSMAELAAL AETAGSEVLD ALVQRRDKPD SATYIGSGKA HELRDVVLAT GADTVVCDGE LTPAQLNALE KVVKVKVIDR TALILDIFAQ HATSREGKAQ VAFAQMEYML PRLRGWGESM SRQAGGRAGS NGGVGLRGPG ETKIETDRRR IRERMAKLRR EIKGMKQARD TKRERRLEST VPSIAIVGYT NAGKSSLLNA LTGSGVLVQN ALFATLDPTS RKSTLEDGRA VVLTDTVGFV RHLPTQLVEA FRSTLEEVTD ADLLLHVVDG SDPLPTDQIK AVREVIADVV KERDSAMPPE LIVVNKIDAA DPVQLTQLRG LLPGARFVSA RTGEGIDELR DHLGKILAWP ESEVDVLVPY TRGDLVARIH TEGKISKSSH EADGTRVEAR VPTALASVLT DFAYEIATA // ID A0A164NZS7_9NOCA Unreviewed; 500 AA. AC A0A164NZS7; DT 06-JUL-2016, integrated into UniProtKB/TrEMBL. DT 06-JUL-2016, sequence version 1. DT 07-JUN-2017, entry version 9. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=AWN90_23225 {ECO:0000313|EMBL:KZM74927.1}; OS Nocardia terpenica. OC Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae; Nocardia. OX NCBI_TaxID=455432 {ECO:0000313|EMBL:KZM74927.1, ECO:0000313|Proteomes:UP000076512}; RN [1] {ECO:0000313|EMBL:KZM74927.1, ECO:0000313|Proteomes:UP000076512} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=IFM 0406 {ECO:0000313|EMBL:KZM74927.1, RC ECO:0000313|Proteomes:UP000076512}; RA Evans L.H., Alamgir A., Owens N., Weber N.D., Virtaneva K., RA Barbian K., Babar A., Rosenke K.; RL Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KZM74927.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LWGR01000004; KZM74927.1; -; Genomic_DNA. DR RefSeq; WP_067586837.1; NZ_KV411304.1. DR EnsemblBacteria; KZM74927; KZM74927; AWN90_23225. DR Proteomes; UP000076512; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 2. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000076512}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000076512}. FT DOMAIN 265 434 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 231 258 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 500 AA; 53975 MW; 14EB1408E1FFD2BB CRC64; MRKSETYEFT PIEELDENGD GRNGWAPEPT VGELQLDERS SLRRVAGLST ELADITEVEY RQLRLERVVL VGVWTEGSAA QAEASMAELA ALAETAGSEV LDALIQRRDK PDPATYIGSG KADELRAVVL ETGADTVICD GELTPAQLTA LEKVVKVKVV DRTALILDIF AQHATSREGK AQVSLAQMEY MLPRLRGWGQ SMSRQAGGRA GGSGGGVGLR GPGETKIETD RRRIRERMSR LRRDIKEMKT ARDTKRARRT GSGIPSVAIV GYTNAGKSSL MNALTGAGIL VQDALFATLD PTTRRAALDD GREVVFTDTV GFVRHLPTQL VEAFRSTLEE VTGADLLLHV VDGSDPMPDQ QIKAVREVIT DVLRESKTPA PPELLVVNKI DALDPTDLTH LRAQLPGAVY VSARTGRGLN TLRDKLAEFM GGLDVEVGVL LPYTRGDLLA RIHADGRIID SSHEEGGTRL RARVPHALAA VLSQYAHAGT DVAEAADLSG // ID A0A164YBT3_DAUCA Unreviewed; 555 AA. AC A0A164YBT3; DT 06-JUL-2016, integrated into UniProtKB/TrEMBL. DT 06-JUL-2016, sequence version 1. DT 12-APR-2017, entry version 5. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:KZM94273.1}; GN ORFNames=DCAR_017516 {ECO:0000313|EMBL:KZM94273.1}; OS Daucus carota subsp. sativus. OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae; OC Pentapetalae; asterids; campanulids; Apiales; Apiaceae; Apioideae; OC Scandiceae; Daucinae; Daucus; Daucus sect. Daucus. OX NCBI_TaxID=79200 {ECO:0000313|EMBL:KZM94273.1, ECO:0000313|Proteomes:UP000077755}; RN [1] {ECO:0000313|EMBL:KZM94273.1, ECO:0000313|Proteomes:UP000077755} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. DH1 {ECO:0000313|Proteomes:UP000077755}; RC TISSUE=Leaf {ECO:0000313|EMBL:KZM94273.1}; RX PubMed=27158781; DOI=10.1038/ng.3565; RA Iorizzo M., Ellison S., Senalik D., Zeng P., Satapoomin P., Huang J., RA Bowman M., Iovene M., Sanseverino W., Cavagnaro P., Yildiz M., RA Macko-Podgorni A., Moranska E., Grzebelus E., Grzebelus D., RA Ashrafi H., Zheng Z., Cheng S., Spooner D., Van Deynze A., Simon P.; RT "A high-quality carrot genome assembly provides new insights into RT carotenoid accumulation and asterid genome evolution."; RL Nat. Genet. 48:657-666(2016). CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KZM94273.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LNRQ01000005; KZM94273.1; -; Genomic_DNA. DR Proteomes; UP000077755; Chromosome 5. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000077755}; KW Reference proteome {ECO:0000313|Proteomes:UP000077755}. FT DOMAIN 332 498 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 555 AA; 61747 MW; 4770DB927C0179A6 CRC64; MTSCFFNSSI LIPSSSSSSL CNSDNYTNPN ISFPFRKHAA HRCVIRAVQD GAAAGILSPE VVVDDTLVTQ VEQVAEEEKV QSTPRKRVSK KKDDDDDDTR FKLRNGREVF EEKAYLVGVT QKGDKDDAFG IEESLKELAQ LADTAGLLVV DSTYQKLSTP NSRTYIGSGK VAEIKTAIQA LDVETVIFDD ELSPGQLRNL EKAFGGYVRV CDRTALILDI FDQRAATREA ALQAILSDLK ISSLTFGMAL LKILSSLQVS LAQMEYQLPR LTKMWTHLER QAGGQVKGMG EKQIEVDKRI LRTQIGTLKK ELESVRKHRK QYRNRRVSVP VPVVSLVGYT NAGKSTLLNQ LTGANVLAED RLFATLDPTT RRVQMKNGKE FLLTDTVGFI QKLPTTLVAA FRATLEEIAE SSLMVHVVDI SHPLAEQQID AVDKVLSELD TASIPKLIVW NKVDKASDPQ RIKLEAKKKE DTICISALTG EGMDEFCNAV HDKLKDSMVW VEALIPFDKG ELLNTIHQVG MVEKAEYTER GTLVRAHVPL RFARLLTPLR QMCVQ // ID A0A165NP29_9SPHN Unreviewed; 431 AA. AC A0A165NP29; DT 06-JUL-2016, integrated into UniProtKB/TrEMBL. DT 06-JUL-2016, sequence version 1. DT 07-JUN-2017, entry version 10. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=A3711_10665 {ECO:0000313|EMBL:KZX50411.1}; OS Erythrobacter sp. HI00D59. OC Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales; OC Erythrobacteraceae; Erythrobacter. OX NCBI_TaxID=1822215 {ECO:0000313|EMBL:KZX50411.1, ECO:0000313|Proteomes:UP000077319}; RN [1] {ECO:0000313|EMBL:KZX50411.1, ECO:0000313|Proteomes:UP000077319} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=HI00D59 {ECO:0000313|EMBL:KZX50411.1, RC ECO:0000313|Proteomes:UP000077319}; RA Sosa O.A.; RT "Microbial cycling of marine high molecular weight dissolved organic RT matter."; RL Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KZX50411.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LWEG01000113; KZX50411.1; -; Genomic_DNA. DR RefSeq; WP_067676396.1; NZ_LWEG01000113.1. DR EnsemblBacteria; KZX50411; KZX50411; A3711_10665. DR Proteomes; UP000077319; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000077319}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000077319}. FT DOMAIN 202 376 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 431 AA; 47289 MW; E5FB5687D280008A CRC64; MGEVTRGARA LVVCPDIRGM AYDLDAQSRL SEAEGLALAI GVVIADSFVL PVRDVRPNLL FGAGQVDNIR IACEQHEAEL VVVDGALTPI QQRNLEDKLA RKVIDRTGLI LEIFGERAAT AEGRLQVELA HLDYQQSRLV RSWTHLERQR GGFGFLGGPG ETQIEADRRM IRQRMGRLRK ELEQVRKTRG LHRERRERAP WPVVALVGYT NAGKSTLFNR LTGAGVMAED LLFATLDPTM RAIALPGVEK AILSDTVGFI SDLPTQLVAA FRATLEEVTA ADVICHVRDI SNPSSAAQKA QVLHVLRDLG VIDGEGEASI PILEIWNKWD QLDHEDADDL AAQVEANDDI VATSAVTGEG VDVLLHRLGE MLTRNAALRT FEVAAIDGRR IAWLHAHGEV IEDIEAEEGG STRLITVRLN PKELGQYEAL A // ID A0A165R191_9SPHN Unreviewed; 449 AA. AC A0A165R191; DT 06-JUL-2016, integrated into UniProtKB/TrEMBL. DT 06-JUL-2016, sequence version 1. DT 07-JUN-2017, entry version 10. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=A3736_06065 {ECO:0000313|EMBL:KZY57285.1}; OS Erythrobacter sp. HI0063. OC Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales; OC Erythrobacteraceae; Erythrobacter. OX NCBI_TaxID=1822240 {ECO:0000313|EMBL:KZY57285.1, ECO:0000313|Proteomes:UP000077326}; RN [1] {ECO:0000313|EMBL:KZY57285.1, ECO:0000313|Proteomes:UP000077326} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=HI0063 {ECO:0000313|EMBL:KZY57285.1, RC ECO:0000313|Proteomes:UP000077326}; RA Sosa O.A.; RT "Microbial cycling of marine high molecular weight dissolved organic RT matter."; RL Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KZY57285.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LWFF01000098; KZY57285.1; -; Genomic_DNA. DR RefSeq; WP_067679640.1; NZ_LWFF01000098.1. DR EnsemblBacteria; KZY57285; KZY57285; A3736_06065. DR Proteomes; UP000077326; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000077326}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000077326}. FT DOMAIN 202 376 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 168 195 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 449 AA; 49256 MW; 31243FCE1AF90F8B CRC64; MGEVSRGARA LVVVPDIRNQ SRDLDAEARL EEAKGLALAI GIVVAEGIVL PVRDVKPNTL FGSGQVENIA TKCEQDEIEL LVVDGALSPI QQRNLEETLK RKVIDRTGLI LEIFGERAAT AEGRLQVELA HLDYQQSRLV RSWTHLERQR GGFGFLGGPG ETQIEADRRM IRTRMARLRK ELEQVRKTRA LHRERRGRAP WPIMALVGYT NAGKSTLFNR MTGAQVMAED LLFATLDPTM RAVALPGIEK AILSDTVGFI SDLPTQLVAA FRATLEEVTA ADVIVHVRDM ANPDAAAQKR EVLDILSDLG VMDEDGISSI PIIEAWNKWD ALSDERRAEI EPLATEDEDV IAISAVTGMG VDILTDRLGR LLTSGARRYA ITLSAADGSR IAWLHAHGQV FDDIPADADG VQDGEGPFRT LDVRLTDKEL GRFETLGDGA TAEPLIRRA // ID A0A165S795_9GAMM Unreviewed; 430 AA. AC A0A165S795; DT 06-JUL-2016, integrated into UniProtKB/TrEMBL. DT 06-JUL-2016, sequence version 1. DT 30-AUG-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=A3737_11645 {ECO:0000313|EMBL:KZY71005.1}, GN A3737_21085 {ECO:0000313|EMBL:KZY61908.1}; OS Oleiphilus sp. HI0065. OC Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales; OC Oleiphilaceae; Oleiphilus. OX NCBI_TaxID=1822241 {ECO:0000313|EMBL:KZY61908.1, ECO:0000313|Proteomes:UP000077382}; RN [1] {ECO:0000313|EMBL:KZY61908.1, ECO:0000313|Proteomes:UP000077382} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=HI0065 {ECO:0000313|EMBL:KZY61908.1, RC ECO:0000313|Proteomes:UP000077382}; RA Sosa O.A.; RT "Microbial cycling of marine high molecular weight dissolved organic RT matter."; RL Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KZY61908.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LWFG01002199; KZY61908.1; -; Genomic_DNA. DR EMBL; LWFG01000668; KZY71005.1; -; Genomic_DNA. DR RefSeq; WP_068457073.1; NZ_LWFG01002199.1. DR EnsemblBacteria; KZY61908; KZY61908; A3737_21085. DR EnsemblBacteria; KZY71005; KZY71005; A3737_11645. DR Proteomes; UP000077382; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000077382}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000077382}. FT DOMAIN 198 365 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 430 AA; 48423 MW; B85ADD9F1FDABB4B CRC64; MFDRPDAGER AILVHIDFPN ENDREDVNEF KELVRSAGVE PVAIVSGSRT QPSARYFVGS GKLEELQAEL EASEADVVLF NHALSPSQQR NLEGVLECRV IDRTGVILDI FAQRARTHEG KLQVELAQLE YMSTRLIRGW THLERQKGGI GLRGPGETQL ETDRRLLRAR IKALQGRLGK VRKQRDQGRR ARTRAEIPTI SLVGYTNAGK STLFNRVTQS EVYSADQLFA TLDPTLRKID FPDVGRAILV DTVGFIRHLP HKLVDAFRAT LEETIAATLL LHVIDCADDR RLENVEAVET VLDEIGADEV PTLKVYNKLD LLDDASPRID RDEEGRPVRV WVSANTGAGI DLLHEAVAEL LTEEVVHAVI ALRHEQSRLR ALFYEEKAVL NEHYNDEGQC VVEVRLQASD FERMLKRCGV SHAELLIKRI // ID A0A165TZF6_9GAMM Unreviewed; 423 AA. AC A0A165TZF6; DT 06-JUL-2016, integrated into UniProtKB/TrEMBL. DT 06-JUL-2016, sequence version 1. DT 30-AUG-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=A3709_18460 {ECO:0000313|EMBL:KZX58599.1}; OS Halioglobus sp. HI00S01. OC Bacteria; Proteobacteria; Gammaproteobacteria; Cellvibrionales; OC Halieaceae; Halioglobus. OX NCBI_TaxID=1822214 {ECO:0000313|EMBL:KZX58599.1, ECO:0000313|Proteomes:UP000077184}; RN [1] {ECO:0000313|EMBL:KZX58599.1, ECO:0000313|Proteomes:UP000077184} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=HI00S01 {ECO:0000313|EMBL:KZX58599.1, RC ECO:0000313|Proteomes:UP000077184}; RA Sosa O.A.; RT "Microbial cycling of marine high molecular weight dissolved organic RT matter."; RL Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KZX58599.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LWEE01000044; KZX58599.1; -; Genomic_DNA. DR RefSeq; WP_066052838.1; NZ_LWEE01000044.1. DR EnsemblBacteria; KZX58599; KZX58599; A3709_18460. DR Proteomes; UP000077184; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000077184}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000077184}. FT DOMAIN 199 365 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 423 AA; 47599 MW; 6234B7CEE7B6E094 CRC64; MFFDRPESGE RAVLVHLNLD SESEREDPRE FEELVLSAGG DPAAYIMGSR SAPHPGTFVG AGKLEEIRDE VALHEAEVVM FNHSLSPSQE RNLEQELKCR VLDRTGLILD IFAQRARTHE GKLQVELAQL QHMSTRLVRG WTHLERQKGG IGLRGPGETQ LETDRRLLRV RIKSITARLE KVRKQRDQGR RSRKRQEIPT VSLVGYTNAG KSTLFNYITQ SGVYAADQLF ATLDPTLRRL ELENVGPVVF ADTVGFIAHL PHKLVEAFKA TLEETLNADL LLHVIDAASD EREDNIYQVQ DVLHEIGADE IPRLEVFNKL DLLEQQPRID RNAEGKPERV WLSAATGDGV ELLLQAVSEL VGQDMVNEEL ELAPDQGQLR AAFYALGAVE SENYADDGTA HLQVRLPRAD WNRLMKKGPE PMF // ID A0A166IM96_9MICO Unreviewed; 269 AA. AC A0A166IM96; DT 06-JUL-2016, integrated into UniProtKB/TrEMBL. DT 06-JUL-2016, sequence version 1. DT 07-JUN-2017, entry version 4. DE SubName: Full=GTPase HflX {ECO:0000313|EMBL:KZX22611.1}; GN Name=hflX_2 {ECO:0000313|EMBL:KZX22611.1}; GN ORFNames=ACH61_00241 {ECO:0000313|EMBL:KZX22611.1}; OS Rathayibacter tanaceti. OC Bacteria; Actinobacteria; Micrococcales; Microbacteriaceae; OC Rathayibacter. OX NCBI_TaxID=1671680 {ECO:0000313|EMBL:KZX22611.1, ECO:0000313|Proteomes:UP000076717}; RN [1] {ECO:0000313|EMBL:KZX22611.1, ECO:0000313|Proteomes:UP000076717} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=VKM Ac-2596 {ECO:0000313|EMBL:KZX22611.1, RC ECO:0000313|Proteomes:UP000076717}; RA Vasilenko O.V., Starodumova I.P., Tarlachkov S.V., Dorofeeva L.V., RA Evtushenko L.I.; RT "Draft Genome Sequence of Rathayibacter sp. Strain VKM Ac-2596 RT Isolated from Leaf Gall Induced by Plant-Parasitic Nematodes."; RL Submitted (AUG-2015) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KZX22611.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LIIN01000004; KZX22611.1; -; Genomic_DNA. DR EnsemblBacteria; KZX22611; KZX22611; ACH61_00241. DR PATRIC; fig|1671680.3.peg.256; -. DR Proteomes; UP000076717; Unassembled WGS sequence. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000076717}; KW Reference proteome {ECO:0000313|Proteomes:UP000076717}. FT DOMAIN 106 193 GTP-bdg_N. {ECO:0000259|Pfam:PF13167}. FT DOMAIN 196 232 GTP-bdg_M. {ECO:0000259|Pfam:PF16360}. SQ SEQUENCE 269 AA; 28906 MW; FB378ED3E9927429 CRC64; MTEDLNETGT TEGVDVVSRV LANAQSRSAG YSRFVAGGAQ ALQSTGQEGE NSDGEQFDRD DRQALRRVAG LSTELEDVTE VEYRQLRLEN VVLIGVYSQN SLEDAENSLH ELAALAETAG ATVLDGLLQR RPHPDPSTYL GKGKAQELAA LVAALGADTV VADTELAPSQ RRALEDVVKV KVIDRTAVIL DIFSQHAKSR EGKAQVELAQ LEYLLPRLRG WGESMSRQAG GQVAPAQAWA RAVPVRPRSS STAAGSTRAW RGCASRSPR // ID A0A166KJX4_9GAMM Unreviewed; 430 AA. AC A0A166KJX4; DT 06-JUL-2016, integrated into UniProtKB/TrEMBL. DT 06-JUL-2016, sequence version 1. DT 30-AUG-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=A3715_14375 {ECO:0000313|EMBL:KZX75573.1}; OS Oleiphilus sp. HI0009. OC Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales; OC Oleiphilaceae; Oleiphilus. OX NCBI_TaxID=1822219 {ECO:0000313|EMBL:KZX75573.1, ECO:0000313|Proteomes:UP000077127}; RN [1] {ECO:0000313|EMBL:KZX75573.1, ECO:0000313|Proteomes:UP000077127} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=HI0009 {ECO:0000313|EMBL:KZX75573.1, RC ECO:0000313|Proteomes:UP000077127}; RA Sosa O.A.; RT "Microbial cycling of marine high molecular weight dissolved organic RT matter."; RL Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KZX75573.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LWEK01002163; KZX75573.1; -; Genomic_DNA. DR RefSeq; WP_068481638.1; NZ_LWEK01002163.1. DR EnsemblBacteria; KZX75573; KZX75573; A3715_14375. DR Proteomes; UP000077127; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000077127}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000077127}. FT DOMAIN 198 365 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 430 AA; 48356 MW; 613248D6EEA60748 CRC64; MFDRPDAGER AVLVHLDFPN ENDREDAQEF RELVRSAGVE PVGIVTGSRS QPSARFFVGS GKLEEIITEK AVTDADVVLF NHALSPSQQR NLEGSLECRV IDRTGVILDI FAQRARTHEG KLQVELAQLE YISTRLIRGW THLERQKGGI GLRGPGETQL ETDRRLLRGR IKALTGRLEK VRKQRDQGRR SRTRAEIPTI SLVGYTNAGK STLFNRLTDS GVYAADQLFA TLDPTLRRID FPDIGRAILV DTVGFIRHLP HKLVDAFRAT LEETISATLL LHVIDGADSR RLDNIEAVEQ VLDEIGAGDV KVLRVYNKID LLDDGVSRID RDEDGAPVRV WLSANSGEGT DLLSDAVAEL LSDEVMHCIL RLRPEQGRLR AMLFESNHVI QEEYDDKGMA RVEVRLQTSD FERMLKRCNV PRADLLIDRL // ID A0A166MG94_9GAMM Unreviewed; 291 AA. AC A0A166MG94; DT 06-JUL-2016, integrated into UniProtKB/TrEMBL. DT 06-JUL-2016, sequence version 1. DT 07-JUN-2017, entry version 8. DE SubName: Full=GTPase HflX {ECO:0000313|EMBL:KZX85642.1}; DE Flags: Fragment; GN ORFNames=A3715_27900 {ECO:0000313|EMBL:KZX85642.1}; OS Oleiphilus sp. HI0009. OC Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales; OC Oleiphilaceae; Oleiphilus. OX NCBI_TaxID=1822219 {ECO:0000313|EMBL:KZX85642.1, ECO:0000313|Proteomes:UP000077127}; RN [1] {ECO:0000313|EMBL:KZX85642.1, ECO:0000313|Proteomes:UP000077127} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=HI0009 {ECO:0000313|EMBL:KZX85642.1, RC ECO:0000313|Proteomes:UP000077127}; RA Sosa O.A.; RT "Microbial cycling of marine high molecular weight dissolved organic RT matter."; RL Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KZX85642.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LWEK01000178; KZX85642.1; -; Genomic_DNA. DR RefSeq; WP_068473821.1; NZ_LWEK01000178.1. DR EnsemblBacteria; KZX85642; KZX85642; A3715_27900. DR Proteomes; UP000077127; Unassembled WGS sequence. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000077127}; KW Reference proteome {ECO:0000313|Proteomes:UP000077127}. FT DOMAIN 198 291 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT NON_TER 291 291 {ECO:0000313|EMBL:KZX85642.1}. SQ SEQUENCE 291 AA; 32597 MW; C3E8A8A9244BEB85 CRC64; MFDRPDAGER AVLVHLDFPN ENDREDAQEF RELVRSAGVE PVGIVTGSRS QPSARFFVGS GKLEEIITEK AVTDADVVLF NHALSPSQQR NLEGSLECRV IDRTGVILDI FAQRARTHEG KLQVELAQLE YISTRLIRGW THLERQKGGI GLRGPGETQL ETDRRLLRGR IKALTGRLEK VRKQRDQGRR SRTRAEIPTI SLVGYTNAGK STLFNRLTDS GVYAADQLFA TLDPTLRRID FPDIGRAILV DTVGFIRHLP HKLVDAFRAT LEETISATLL LHVIDGADSR R // ID A0A166Q6G1_9ACTN Unreviewed; 508 AA. AC A0A166Q6G1; DT 06-JUL-2016, integrated into UniProtKB/TrEMBL. DT 06-JUL-2016, sequence version 1. DT 07-JUN-2017, entry version 10. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=UG55_102874 {ECO:0000313|EMBL:OAA24742.1}; OS Frankia sp. EI5c. OC Bacteria; Actinobacteria; Frankiales; Frankiaceae; Frankia. OX NCBI_TaxID=683316 {ECO:0000313|EMBL:OAA24742.1, ECO:0000313|Proteomes:UP000077018}; RN [1] {ECO:0000313|EMBL:OAA24742.1, ECO:0000313|Proteomes:UP000077018} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=EI5c {ECO:0000313|EMBL:OAA24742.1, RC ECO:0000313|Proteomes:UP000077018}; RA Wen L., He K., Yang H.; RL Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:OAA24742.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LRTK01000028; OAA24742.1; -; Genomic_DNA. DR RefSeq; WP_066068703.1; NZ_LRTK01000028.1. DR EnsemblBacteria; OAA24742; OAA24742; UG55_102874. DR PATRIC; fig|683316.3.peg.3311; -. DR Proteomes; UP000077018; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000077018}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000077018}. FT DOMAIN 276 441 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 508 AA; 54400 MW; 8EFAA412135F6390 CRC64; MSLRTDAVTA STRYPTSNPD SDSDDEGVVR LDAAESFAFF DEQGDGFDLE ERSALRRIPG LTTELEDVTE VEYRQLRLER VVLIGVWTSG TPAEAEASMT ELAALATTAG SMVLEAVVQR RDRPDAATFV GSGKARELAE IVQATGADTV ICDGELTPGQ LRQLEEVVKV KVIDRTALIL DIFAQHATSK EGKAQVELAQ LQYMLPRLRG WGESMSRAAA SSGGRAPIGT RGPGETKIET DRRRLRTRMA RLRRDLAGMA TVRATKRSAR RRGDIPAVAI AGYTNAGKSS LXNRLTGAGV LVEDALFATL DPTVRRATLP DGRVFTLADT VGFVRHLPHQ IVEAFRSTLE EVADADLVLH VVDGSAPDPM GQIAAVREVL AEIDAAGVPE LVVVNKVDAV DPTTLAVLRK AIPDAVLVSA RSGAGLPELV DALSARIPHP EVEMSLLVPY TRGDLVSRIH REGEVLSLEH TGAGTEVAAR LPAGLAAELE PYRVAQQPST AQQPSTVP // ID A0A166RQW8_9RHOB Unreviewed; 432 AA. AC A0A166RQW8; DT 06-JUL-2016, integrated into UniProtKB/TrEMBL. DT 06-JUL-2016, sequence version 1. DT 05-JUL-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=A3721_00440 {ECO:0000313|EMBL:KZX98960.1}; OS Sulfitobacter sp. HI0023. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae; Sulfitobacter. OX NCBI_TaxID=1822225 {ECO:0000313|EMBL:KZX98960.1, ECO:0000313|Proteomes:UP000077323}; RN [1] {ECO:0000313|EMBL:KZX98960.1, ECO:0000313|Proteomes:UP000077323} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=HI0023 {ECO:0000313|EMBL:KZX98960.1, RC ECO:0000313|Proteomes:UP000077323}; RA Sosa O.A.; RT "Microbial cycling of marine high molecular weight dissolved organic RT matter."; RL Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KZX98960.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LWEQ01000334; KZX98960.1; -; Genomic_DNA. DR RefSeq; WP_067920209.1; NZ_LWEQ01000334.1. DR EnsemblBacteria; KZX98960; KZX98960; A3721_00440. DR Proteomes; UP000077323; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000077323}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000077323}. FT DOMAIN 212 381 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 432 AA; 47947 MW; A89A7AA2634C37E0 CRC64; MSRPPFQIDE TEGPRVTRAW VLHPDIRSDP DRRAPEPALA EAVALAEALP QLEVQGAEVV PLRSVSAGML FGSGKIEELR QRLEESEIEL VLVDGHVSPV QQRNLEKAWK VKLLDRTGLI LEIFSDRAAT REGVLQVEMA ALNYQRTRLV RAWTHLERQR GGLGFVGGPG ETQIEADRRA IDEQLVRLRR QLDKVVRTRA LHRAARAKVP YPIVALVGYT NAGKSTLFNR LTGAEVMAKD MLFATLDPTM RSLVLPDGPE VILSDTVGFI SDLPTELVAA FRATLEEVLA ADIICHVRDV SHSETEEQAQ DVRDILASLG VDKQTRTFEV WNKIDLMPPE AADALRAAAA RDPDVLAISA ISGEGLDALQ STIAEALQGH LREADLSLSF EEGRKRAWLF EQDVVIEERQ TDSGFDLAVR WSAQQEAQFQ KL // ID A0A166RXD8_9EURY Unreviewed; 431 AA. AC A0A166RXD8; DT 06-JUL-2016, integrated into UniProtKB/TrEMBL. DT 06-JUL-2016, sequence version 1. DT 07-JUN-2017, entry version 9. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=A4G99_11280 {ECO:0000313|EMBL:KZN23493.1}; OS Haladaptatus sp. R4. OC Archaea; Euryarchaeota; Halobacteria; Halobacteriales; OC Halobacteriaceae; Haladaptatus. OX NCBI_TaxID=1679489 {ECO:0000313|EMBL:KZN23493.1, ECO:0000313|Proteomes:UP000076599}; RN [1] {ECO:0000313|EMBL:KZN23493.1, ECO:0000313|Proteomes:UP000076599} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=R4 {ECO:0000313|EMBL:KZN23493.1, RC ECO:0000313|Proteomes:UP000076599}; RA Mukhopadhyay S.K.; RT "Genome sequence of halophilic archaea."; RL Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KZN23493.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LWHG01000028; KZN23493.1; -; Genomic_DNA. DR RefSeq; WP_066145377.1; NZ_LWHG01000028.1. DR EnsemblBacteria; KZN23493; KZN23493; A4G99_11280. DR Proteomes; UP000076599; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000076599}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000076599}. FT DOMAIN 186 369 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 102 129 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 431 AA; 48236 MW; FDA0EF23F64A6F1D CRC64; MKAILAKRVD DGTASIDELS ELARAAGYDV AAEVTQSREE DAAYQFGEGK VAELSAAVTE RDAGIVIFDN QLGPYQTYNL GQRLPDGTEV IDRFRLILEI FGQRAQTRKA QLQVELAELR FELPRVEAKT SLAKRDERPG FMGLGEYDES HEQAIKDQIS RIKDELDAIA DKEADRRQKR RESGFDLVAL AGYTNAGKST LLQRLAEDLE IGENDDLHPD LDPTAEAEDR LFTTLGTTTR KADIDRRDVL LTDTVGFISD LPHWLVESFK STLDAVYYAD LVLLVVDVSE PVDDIREKLV TCHDTLYERN QAPIVTVLNK IDAVSDEELD EKRKALSALA PNPVAISGKD DLNVAELKRR IDIELPDWEF ERLVMPMTDE TMSVVSWVHD HGRVEDVTYT DDEVVVEFEA RPSIVQQSRS KASDLTAVPS A // ID A0A166T4U1_9CYAN Unreviewed; 467 AA. AC A0A166T4U1; DT 06-JUL-2016, integrated into UniProtKB/TrEMBL. DT 06-JUL-2016, sequence version 1. DT 05-JUL-2017, entry version 10. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=AY599_17370 {ECO:0000313|EMBL:OAB60301.1}; OS Leptolyngbya valderiana BDU 20041. OC Bacteria; Cyanobacteria; Synechococcales; Leptolyngbyaceae; OC Leptolyngbya. OX NCBI_TaxID=322866 {ECO:0000313|EMBL:OAB60301.1, ECO:0000313|Proteomes:UP000077404}; RN [1] {ECO:0000313|EMBL:OAB60301.1, ECO:0000313|Proteomes:UP000077404} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BDU 20041 {ECO:0000313|EMBL:OAB60301.1, RC ECO:0000313|Proteomes:UP000077404}; RA Wen L., He K., Yang H.; RL Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:OAB60301.1, ECO:0000313|Proteomes:UP000077404} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BDU 20041 {ECO:0000313|EMBL:OAB60301.1, RC ECO:0000313|Proteomes:UP000077404}; RA Peter A.P., Garlapati D., Kaliaperumal E.M., Lakshmanan K., RA Tyagaraj B.; RT "De novo Whole Genome Sequencing of Leptolyngbya valderiana BDU RT 20041."; RL Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:OAB60301.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LSYZ01000236; OAB60301.1; -; Genomic_DNA. DR EnsemblBacteria; OAB60301; OAB60301; AY599_17370. DR Proteomes; UP000077404; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000077404}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000077404}. FT DOMAIN 215 350 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 175 209 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 467 AA; 51948 MW; C39B2C764A6BD019 CRC64; MPPGYSKTNK ERTSIEVRSE RAVLAAARLP DSTYDPADPF GELRALAEQA GAVVVGELEQ RLQRPVAGTY MGKGKVDELK GLCEALGATT IIFDHDLSPA QISAIERVTE RKVLDRSELI LDIFASRATS YEAKLQVELA QLEYTYPRLR AMWDHLERIV GSGGIGGVGT RGPGEQQLEI DRRLVQRRRL ELERELERVQ GRKRRAVRQR NAERFTVGLV GYTNAGKSTL FNTLTEGGAY ADDRVFATLM TRTRAWDLGG GLEVMLSDTV GFVRDLPHRL IASFRATLEE ATHADVLLVV LDVSDPACEL QYQTVMKTLD DLDAETAKME DAGAWSPPTR VIVLNKIDRL RDNRELLVWQ QRLPDAIALC SLPPVGDQSR PGQDKLARRI RRLAEGDVGD VTLRVPMSNP KAINLIETQA TVRDRQYEDG VMVVTADMSD RLLRQLRSLG VQTPGRGEAQ RAGWKGL // ID A0A166T8G5_9GAMM Unreviewed; 442 AA. AC A0A166T8G5; DT 06-JUL-2016, integrated into UniProtKB/TrEMBL. DT 06-JUL-2016, sequence version 1. DT 30-AUG-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=A3759_02015 {ECO:0000313|EMBL:KZZ41662.1}; OS Thalassolituus sp. HI0120. OC Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales; OC Thalassolituus. OX NCBI_TaxID=1822263 {ECO:0000313|EMBL:KZZ41662.1, ECO:0000313|Proteomes:UP000077137}; RN [1] {ECO:0000313|EMBL:KZZ41662.1, ECO:0000313|Proteomes:UP000077137} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=HI0120 {ECO:0000313|EMBL:KZZ41662.1, RC ECO:0000313|Proteomes:UP000077137}; RA Sosa O.A.; RT "Microbial cycling of marine high molecular weight dissolved organic RT matter."; RL Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KZZ41662.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LWGC01001850; KZZ41662.1; -; Genomic_DNA. DR RefSeq; WP_068659985.1; NZ_LWGC01001850.1. DR EnsemblBacteria; KZZ41662; KZZ41662; A3759_02015. DR Proteomes; UP000077137; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000077137}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000077137}. FT DOMAIN 206 373 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 442 AA; 50125 MW; D8CB5B1B74AB1C88 CRC64; MFFERPTNNS GQKQGGETAI LVHIDFPEGL NREDLNEFRE LVISAGADPL ELVTAKRSTP DPKTFIGLGK VEEIRDMLNL HDCQLVMFNH ALSPSQERNL EKALECRVVD RTGLILDIFA QRARTHEGKL QVELAQLQYQ STRLVRGWTH LERQQGGIGS RGAGESQLET DRRLVRNRVS QIHKRLEKVR AQRNQGRRAR QRSSIPTVAI VGYTNAGKST LFNALTTSEV YAADQLFATL DPTLRRHSVD DIGEVVLADT VGFIRHLPHK LVEAFRATLQ EAAEADLLMH VIDCAADERD SNIEQVEMVL GEIEADEVPQ LRVYNKIDLL EHGEARIDRD DQGLPVAVWL SAREHEGFDL LNKAIAELLG DDLFAEEIRL RPAESKLRAI LYDMGAIREE AYTDDGDILL QIRMQRQDFR RAIAKAGITE HRFLPQQKEP WQ // ID A0A167AQR9_9BACL Unreviewed; 419 AA. AC A0A167AQR9; DT 06-JUL-2016, integrated into UniProtKB/TrEMBL. DT 06-JUL-2016, sequence version 1. DT 07-JUN-2017, entry version 10. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=PNBC_20275 {ECO:0000313|EMBL:OAB71325.1}; OS Paenibacillus sp. LPB0068. OC Bacteria; Firmicutes; Bacilli; Bacillales; Paenibacillaceae; OC Paenibacillus. OX NCBI_TaxID=1763538 {ECO:0000313|EMBL:OAB71325.1, ECO:0000313|Proteomes:UP000077134}; RN [1] {ECO:0000313|EMBL:OAB71325.1, ECO:0000313|Proteomes:UP000077134} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=LPB0068 {ECO:0000313|EMBL:OAB71325.1, RC ECO:0000313|Proteomes:UP000077134}; RA Shin S.-K., Yi H.; RT "Paenibacillus sp. LPB0068, isolated from Crassostrea gigas."; RL Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:OAB71325.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LSFN01000041; OAB71325.1; -; Genomic_DNA. DR RefSeq; WP_068661238.1; NZ_LSFN01000041.1. DR EnsemblBacteria; OAB71325; OAB71325; PNBC_20275. DR Proteomes; UP000077134; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000077134}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000077134}. FT DOMAIN 198 366 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 157 184 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 419 AA; 47600 MW; 28C71E2B47FE6A39 CRC64; MEELQQKAII VGVNVNHQED FEYSMEELGN LAVACHVEVV GQITQNLEKV NKSHYIGKGK VQDVLAIYEE LEANVVIFND ELSPSQIRNL EADLQCKVID RTILILDIFE KRAKTREAQL QVEVAQLQYM LPRLIGLRES LGRQGGGVGT KNKGVGETKL ELDRRRIEDK ISALNKELET LVSHRQTQRK QRQRNELPVV SLVGYTNAGK STIMNALVEL FNSSGNKMVF EKDMLFATLE TSVRNIQLED KKSFLLTDTV GFVSKLPHHL IKAFRSTLEE VAEADLLIHV VDYSNANYEK LKRITETTLQ EIGITNIDTI YAYNKCDMVD CEIPVIKDDS IYLAAKPRIG IEELIALIRA HVFKDYINCV MSIPFEQGQV VSYLNKCAHV ISTEYDEVGT RLTLECRAMD AEKYQEFII // ID A0A167DRX4_9BACL Unreviewed; 429 AA. AC A0A167DRX4; DT 06-JUL-2016, integrated into UniProtKB/TrEMBL. DT 06-JUL-2016, sequence version 1. DT 07-JUN-2017, entry version 10. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=PNBC_11775 {ECO:0000313|EMBL:OAB74710.1}; OS Paenibacillus sp. LPB0068. OC Bacteria; Firmicutes; Bacilli; Bacillales; Paenibacillaceae; OC Paenibacillus. OX NCBI_TaxID=1763538 {ECO:0000313|EMBL:OAB74710.1, ECO:0000313|Proteomes:UP000077134}; RN [1] {ECO:0000313|EMBL:OAB74710.1, ECO:0000313|Proteomes:UP000077134} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=LPB0068 {ECO:0000313|EMBL:OAB74710.1, RC ECO:0000313|Proteomes:UP000077134}; RA Shin S.-K., Yi H.; RT "Paenibacillus sp. LPB0068, isolated from Crassostrea gigas."; RL Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:OAB74710.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LSFN01000014; OAB74710.1; -; Genomic_DNA. DR RefSeq; WP_068658283.1; NZ_LSFN01000014.1. DR EnsemblBacteria; OAB74710; OAB74710; PNBC_11775. DR Proteomes; UP000077134; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000077134}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000077134}. FT DOMAIN 209 373 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 429 AA; 48083 MW; 2C4537221B8D676F CRC64; MAYSITFDTD TEIQDRAVLV SLVTDEVKKK GIDPEHSLHE LIQLAETAGV EVLDSLSQNL QKPDPKYFIG KGKVDELRML MEAVEANTAI FDHELSGAQV RHLEERLDAK IIDRTQLILD IFAQRANTRE GIIQVELAQL TYLLPRLSGH GSNLSRLGGG IGTRGPGESK LEMDRRHIRG RVDDLKHQLA EISRHRKLYR ERRKKSDAVQ VALVGYTNAG KSTLLKQLTD ADVYIQNQLF ATLDPTSRVL ELPSGKEVVL TDTVGFIQNL PHDLIAAFRA TLEEVNEANL ILHVVDASSE MREDQMAVVQ KILVELGSSD KPQIVLYNKK DACTPEQLEM LNSGDDHLTI SAFDDADLLA IREAIQNTLK GDTINFRIPA NRGDLVSLLY RVGEITNQEF EGSDSIYTVL LHKADYEKNG YMLQDYIEL // ID A0A167GX38_9GAMM Unreviewed; 421 AA. AC A0A167GX38; DT 06-JUL-2016, integrated into UniProtKB/TrEMBL. DT 06-JUL-2016, sequence version 1. DT 07-JUN-2017, entry version 9. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=I596_1974 {ECO:0000313|EMBL:ANB17996.1}; OS Dokdonella koreensis DS-123. OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales; OC Rhodanobacteraceae; Dokdonella. OX NCBI_TaxID=1300342 {ECO:0000313|EMBL:ANB17996.1, ECO:0000313|Proteomes:UP000076830}; RN [1] {ECO:0000313|EMBL:ANB17996.1, ECO:0000313|Proteomes:UP000076830} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DS-123 {ECO:0000313|EMBL:ANB17996.1, RC ECO:0000313|Proteomes:UP000076830}; RA Kim J.F., Lee H., Kwak M.-J.; RT "Complete genome sequence of Dokdonella koreensis DS-123T."; RL Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP015249; ANB17996.1; -; Genomic_DNA. DR EnsemblBacteria; ANB17996; ANB17996; I596_1974. DR KEGG; dko:I596_1974; -. DR PATRIC; fig|1300342.3.peg.1929; -. DR KO; K03665; -. DR Proteomes; UP000076830; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000076830}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000076830}. FT DOMAIN 175 342 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 141 168 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 421 AA; 45940 MW; 6964C4587F3661E5 CRC64; MLLDEFAELA RSAGASVVGS LSARVERPNP RYFVGTGKAD ELKAQRDALG ADLILVNHAL SPVQERNLEK LTACRVVDRT GLILDIFAQR ARSHEGKLQV ELAQLKHMST RLVRGWTHLE RQRGGAIGLR GPGETQLELD RRLLGERMKQ LQKRLDKVAT QRAQARRARL RNALPVVALV GYTNAGKSTL FNALTGAGVY AADQLFATLD PTLRRLSGLQ SGPAVLADTV GFIRDLPHDL VAAFRSTLAE AREADLLLHV IDVADPERDQ RVVDVEAVLA EIGAGDVPQV LVYNKIDQLE GVEARLDTGD PESPPRVWVS ARDGRGLEPL REAIARRLAA ERVQAVLHVP AAAGRLRARL HAQGLVAAEA AEDTGWRIEI DAPRALVEPL FGLSDGDGHW LRERLLAPAE VETYNPQATA H // ID A0A167IWM9_9FLAO Unreviewed; 402 AA. AC A0A167IWM9; DT 06-JUL-2016, integrated into UniProtKB/TrEMBL. DT 06-JUL-2016, sequence version 1. DT 07-JUN-2017, entry version 10. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=ULVI_04935 {ECO:0000313|EMBL:OAB80088.1}; OS Ulvibacter sp. LPB0005. OC Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales; OC Flavobacteriaceae; Ulvibacter. OX NCBI_TaxID=1763537 {ECO:0000313|EMBL:OAB80088.1, ECO:0000313|Proteomes:UP000077013}; RN [1] {ECO:0000313|EMBL:OAB80088.1, ECO:0000313|Proteomes:UP000077013} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=LPB0005 {ECO:0000313|EMBL:OAB80088.1, RC ECO:0000313|Proteomes:UP000077013}; RA Shin S.-K., Yi H.; RT "Ulvibacter sp. LPB0005, isolated from Thais luteostoma."; RL Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:OAB80088.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LRXL01000026; OAB80088.1; -; Genomic_DNA. DR RefSeq; WP_068590332.1; NZ_LRXL01000026.1. DR EnsemblBacteria; OAB80088; OAB80088; ULVI_04935. DR Proteomes; UP000077013; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000077013}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000077013}. FT DOMAIN 200 385 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 402 AA; 46157 MW; A270FC9C59B56D8D CRC64; MIEEVTIEYE KTILIGLITQ QQDEEKSNEY LDELEFLAYT AGGEVLKRFV QKMEKPNPKT FIGTGKMEDV RAFVEANDVG VAIFDDELSP AQQKNIEKIL QCKIIDRTNL ILDIFAQRAQ TSYARTQVEL AQYEYLLPRL AGMWTHLERQ RGGIGMRGPG ETEIETDRRI VRDRISLLKK KIAKIDKQME VQRGNRGALV RVALVGYTNV GKSTLMNVIS KSEVFAENKL FATLDTTVRK VVIGNLPFLL TDTVGFIRKL PTQLVESFKG TLDEVREADL LLHVVDISHD SFEDHIASVN KILDEIGSAD KPTLMVFNKI DAYEPEIIEE DDLVTLKTKA HYTLKEWKKT WMNSTNGDAI FISALNKDNF EEFRKTVYDK VRDIHVTRFP YNNFLYPEEY VE // ID A0A168AGQ8_9FLAO Unreviewed; 416 AA. AC A0A168AGQ8; DT 06-JUL-2016, integrated into UniProtKB/TrEMBL. DT 06-JUL-2016, sequence version 1. DT 07-JUN-2017, entry version 10. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=FBFR_01090 {ECO:0000313|EMBL:OAB31455.1}; OS Flavobacterium fryxellicola. OC Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales; OC Flavobacteriaceae; Flavobacterium. OX NCBI_TaxID=249352 {ECO:0000313|EMBL:OAB31455.1, ECO:0000313|Proteomes:UP000077164}; RN [1] {ECO:0000313|EMBL:OAB31455.1, ECO:0000313|Proteomes:UP000077164} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 16209 {ECO:0000313|EMBL:OAB31455.1, RC ECO:0000313|Proteomes:UP000077164}; RA Shin S.-K., Yi H.; RT "Draft genome sequence of Flavobacterium fryxellicola DSM 16209."; RL Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:OAB31455.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LVJE01000001; OAB31455.1; -; Genomic_DNA. DR RefSeq; WP_066075703.1; NZ_LVJE01000001.1. DR EnsemblBacteria; OAB31455; OAB31455; FBFR_01090. DR Proteomes; UP000077164; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000077164}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000077164}. FT DOMAIN 201 387 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 416 AA; 47865 MW; 32D7060C35CDE2F5 CRC64; MLEKEVINFE KTAIVGIVTQ NQSEAKLNEY LDELEFLTFT AGGQVVKRFS QKMERPNPKT FVGTGKIEEI HLFVKENDIS TLVFDDELSP SQQKNISKII TECKILDRTH LILDIFAQRA ETSYARTQVE LAQCQYLLPR LSGMWTHLER QKGGIGMRGP GETEIETDRR IVRDRIALLK EKIKTIDRQM GVQRGNRGAM VRVALVGYTN VGKSTLMNAV GKSDVFVENK LFATLDTTVR KVVIKNLPFL LSDTVGFIRK LPTQLVDSFK STLDEVREAD LLLHVVDISH PEFEDHIASV NQTLLDIKAN DKPVIMVFNK IDAYKPLTID EDDLMTEKTP RHFTLAEWKS TWMSRVGEQN ALFISATNKE NFEEFRERVY EAVRHIHITR FPYNKFLYPD YKDAVEKEVD EDTEEE // ID A0A168EWK7_9MICO Unreviewed; 515 AA. AC A0A168EWK7; DT 06-JUL-2016, integrated into UniProtKB/TrEMBL. DT 06-JUL-2016, sequence version 1. DT 07-JUN-2017, entry version 10. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:ANC30568.1}; GN ORFNames=I598_0999 {ECO:0000313|EMBL:ANC30568.1}; OS Isoptericola dokdonensis DS-3. OC Bacteria; Actinobacteria; Micrococcales; Promicromonosporaceae; OC Isoptericola. OX NCBI_TaxID=1300344 {ECO:0000313|EMBL:ANC30568.1, ECO:0000313|Proteomes:UP000076794}; RN [1] {ECO:0000313|EMBL:ANC30568.1, ECO:0000313|Proteomes:UP000076794} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DS-3 {ECO:0000313|EMBL:ANC30568.1, RC ECO:0000313|Proteomes:UP000076794}; RA Kwon S.-K., Kim J.F.; RT "Complete genome sequence of a soil Actinobacterium, Isoptericola RT dokdonensis DS-3."; RL Submitted (JAN-2016) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP014209; ANC30568.1; -; Genomic_DNA. DR RefSeq; WP_068201809.1; NZ_CP014209.1. DR EnsemblBacteria; ANC30568; ANC30568; I598_0999. DR KEGG; ido:I598_0999; -. DR PATRIC; fig|1300344.3.peg.1002; -. DR KO; K03665; -. DR Proteomes; UP000076794; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 2. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000076794}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000076794}. FT DOMAIN 296 462 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 515 AA; 55177 MW; A49F481BB40418F3 CRC64; MTHIPTGPEQ PATQSDEPTE QTVAPSRDAQ AIADDVVARV LARAGTARSE GGTVHSAHDG DQLDLAERAA LRRVANLSTE LEDVTEVEYR QLRLEKVVLV GTYPGGEAAA REAEVSLREL AALAETAGSQ VLDGILQKRA KPDPGTFLGS GKAADLADVV AATGADTVVV DTELAPSQRR GLEDIVKVKV VDRTALILDI FAQHAKSREG KAQVELAQLE YLLPRLRGWG ESMSRQAGGQ VGGAGAGMGS RGPGETKIEL DRRRIRNRMA KLRREIAAMA PARETKRLDR KRNAIPNVAI AGYTNAGKSS LLNALTDAGV LVENALFATL DPTVRRTRTD DGRVYTLADT VGFVRHLPHQ LVEAFRSTLE EVGDAALLLH VVDASHPDPE GQIAAVREVL ADIPGVEDVP EVIVLNKADV ADPAVIGRVQ RRERRTVVVS AHSGEGVAEL RALIADELPR PAVEIDLVVP YSRGDLVHRV HENGELTDEE HLAEGTRLRG RVDAALAAEL EQVAV // ID A0A168QPT6_9BACL Unreviewed; 418 AA. AC A0A168QPT6; DT 06-JUL-2016, integrated into UniProtKB/TrEMBL. DT 06-JUL-2016, sequence version 1. DT 07-JUN-2017, entry version 10. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=PBAT_04025 {ECO:0000313|EMBL:OAB48046.1}; OS Paenibacillus antarcticus. OC Bacteria; Firmicutes; Bacilli; Bacillales; Paenibacillaceae; OC Paenibacillus. OX NCBI_TaxID=253703 {ECO:0000313|EMBL:OAB48046.1, ECO:0000313|Proteomes:UP000077355}; RN [1] {ECO:0000313|EMBL:OAB48046.1, ECO:0000313|Proteomes:UP000077355} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CECT 5836 {ECO:0000313|EMBL:OAB48046.1, RC ECO:0000313|Proteomes:UP000077355}; RA Shin S.-K., Yi H.; RT "Draft genome sequence of Paenibacillus antarcticus CECT 5836."; RL Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:OAB48046.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LVJI01000002; OAB48046.1; -; Genomic_DNA. DR RefSeq; WP_068646804.1; NZ_LVJI01000002.1. DR EnsemblBacteria; OAB48046; OAB48046; PBAT_04025. DR Proteomes; UP000077355; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000077355}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000077355}. FT DOMAIN 197 291 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 156 190 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 418 AA; 47709 MW; 935BC7B3581B9F52 CRC64; MEEQQKAIIV GVNVKHQEDF EYSMEELRNL SSACHVEVVG QLVQNLERVN NSHYIGKGKV QEVKALYDMQ EANMVIFNDE LSPSQIRNLE AELQCKVIDR TILILDIFEK RAKTREAQLQ VEVAQLQYML PRLIGLRESL GRQGGGVGTK NKGAGETKLE LDRRRIEDKI SALNKELEIL VSQRQTQRKK RQRNELPVVS LVGYTNAGKS TIMNAMVESF GPSSEKLVFE KDMLFATLET SVRKIRLKDN KSFLLTDTVG FVSKLPHHLV KAFRSTLEEV AEADLLIHVI DYSNSEHENL MDITDNTLKE IGITDIDTVL AYNKCDMVNC TIPLVEDQSI YLAAKQRVGL TELVDIISSH VFKDYIHCEM FIPYEQGQVV SYLNEHAHVI STTYDPDGTR LNIECRPMVI EKYREYVV // ID A0A170XA36_9ACTN Unreviewed; 515 AA. AC A0A170XA36; DT 06-JUL-2016, integrated into UniProtKB/TrEMBL. DT 06-JUL-2016, sequence version 1. DT 07-JUN-2017, entry version 8. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=STXM2123_2326 {ECO:0000313|EMBL:GAT81625.1}; OS Streptomyces sp. F-3. OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae; OC Streptomyces. OX NCBI_TaxID=1840095 {ECO:0000313|EMBL:GAT81625.1, ECO:0000313|Proteomes:UP000078145}; RN [1] {ECO:0000313|EMBL:GAT81625.1, ECO:0000313|Proteomes:UP000078145} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Wang L.S., Gao P.J., Liu L., Zhang H.Q., Cheng Z., Sun X.M.; RT "Streptomyces sp. F-3 geneom sequencing."; RL Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:GAT81625.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BDDR01000012; GAT81625.1; -; Genomic_DNA. DR EnsemblBacteria; GAT81625; GAT81625; STXM2123_2326. DR Proteomes; UP000078145; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000313|EMBL:GAT81625.1}; KW Complete proteome {ECO:0000313|Proteomes:UP000078145}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900, KW ECO:0000313|EMBL:GAT81625.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000078145}. FT DOMAIN 293 458 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 515 AA; 56184 MW; 7A4C33D51CA6E781 CRC64; MTGDDNVPRR KDPMTSSSSS SQTFRASRSG RRLANTRPEG LRADALMEED VAWSPEIDGE RDGDQLDRFD RAALRRVAGL STELEDVTEV EYRQLRLERV VLVGVWTSGT VQDAENSLAE LAALAETAGA VVLDGVIQRR DKPDPATYIG SGKADELRDI VVETGADTVI CDGELSPGQL IQLEDVVKVK VIDRTALILD IFAQHAKSRE GKAQVALAQM EYMLPRLRGW GQSLSRQMGG GSGGIATRGP GETKIETDRR RIREKMAKMR REIASMKTGR EVKRQERRRN RVPSVAIAGY TNAGKSSLLN RLTGAGVLVE NALFATLDPT VRRAETPSGR TYTLADTVGF VRHLPHHLVE AFRSTMEEVG DADLILHVVD GAHPDPEEQL AAVREVIRDI GAAGIPEIVV INKADAADPL VLQRLLRIEK RSIAVSARTG EGIPELLDLI DRELPRPAVE IEALVPYTCG NLIARAHSEG EVLSQEHTAE GTLLKAWVHE ELAAELAPYT PAPAA // ID A0A171C689_9ACTN Unreviewed; 117 AA. AC A0A171C689; DT 06-JUL-2016, integrated into UniProtKB/TrEMBL. DT 06-JUL-2016, sequence version 1. DT 07-JUN-2017, entry version 6. DE SubName: Full=GTPase {ECO:0000313|EMBL:GAT66180.1}; GN ORFNames=PS9374_01824 {ECO:0000313|EMBL:GAT66180.1}; OS Planomonospora sphaerica. OC Bacteria; Actinobacteria; Streptosporangiales; Streptosporangiaceae; OC Planomonospora. OX NCBI_TaxID=161355 {ECO:0000313|EMBL:GAT66180.1, ECO:0000313|Proteomes:UP000077701}; RN [1] {ECO:0000313|Proteomes:UP000077701} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=JCM 9374 {ECO:0000313|Proteomes:UP000077701}; RA Suzuki T., Dohra H., Kodani S.; RT "Planomonospora sphaerica JCM9374 whole genome shotgun sequence."; RL Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:GAT66180.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BDCX01000004; GAT66180.1; -; Genomic_DNA. DR EnsemblBacteria; GAT66180; GAT66180; PS9374_01824. DR Proteomes; UP000077701; Unassembled WGS sequence. DR InterPro; IPR025121; GTPase_HflX_N. DR Pfam; PF13167; GTP-bdg_N; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000077701}; KW Reference proteome {ECO:0000313|Proteomes:UP000077701}. FT DOMAIN 25 111 GTP-bdg_N. {ECO:0000259|Pfam:PF13167}. SQ SEQUENCE 117 AA; 12578 MW; DAC7229054151624 CRC64; MVLAGKDALL VGYFSAKQKR YTVLMDELAA AVETLGARVV GRFVQRRGVS DGGVRTMDRP YSSRTLVSGG KVREITSACE RTGAEAVVFL NPLTDHQREV LSETFGCSVI SAVDLPA // ID A0A171CJJ9_9ACTN Unreviewed; 489 AA. AC A0A171CJJ9; DT 06-JUL-2016, integrated into UniProtKB/TrEMBL. DT 06-JUL-2016, sequence version 1. DT 07-JUN-2017, entry version 10. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=PS9374_02452 {ECO:0000313|EMBL:GAT66800.1}; OS Planomonospora sphaerica. OC Bacteria; Actinobacteria; Streptosporangiales; Streptosporangiaceae; OC Planomonospora. OX NCBI_TaxID=161355 {ECO:0000313|EMBL:GAT66800.1, ECO:0000313|Proteomes:UP000077701}; RN [1] {ECO:0000313|Proteomes:UP000077701} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=JCM 9374 {ECO:0000313|Proteomes:UP000077701}; RA Suzuki T., Dohra H., Kodani S.; RT "Planomonospora sphaerica JCM9374 whole genome shotgun sequence."; RL Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:GAT66800.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BDCX01000005; GAT66800.1; -; Genomic_DNA. DR RefSeq; WP_068896899.1; NZ_BDCX01000005.1. DR EnsemblBacteria; GAT66800; GAT66800; PS9374_02452. DR Proteomes; UP000077701; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 2. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000313|EMBL:GAT66800.1}; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000077701}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900, KW ECO:0000313|EMBL:GAT66800.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000077701}. FT DOMAIN 265 431 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 224 251 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 489 AA; 53839 MW; F30EB28655CD92A5 CRC64; MTHTETEHPN RSNDIDTRES LDFDQFDDLP ETGEMDLAER QALRRVAGLS TELEDVTEVE YRQLRLERVV LVGVWTSGTV TDAENSLLEL KLLAETAGSE VLEGLIQRRQ KPDTATYIGS GKAQELADIV AATGADTVVC DGELSPGQLR QLEEVVKVKV IDRTMLILDI FAQHAKSREG KAQVELAQLN YLLPRLRGWG GNLSRQVGGR AAGGVGIGGR GPGETKIELD RRRIRERMAK LRRQIGEMTT ARETKRARRT QREVPAVAIA GYTNAGKSSL LNRLTGAGVL VENALFATLD PTVRRAYTPE GRLFTLADTV GFVRHLPHQL VEAFRSTLEE VGDADLILHV VDGSHPDPES QLAAVREVFS EIEGAGDIPE IVVVNKADAA DPVVLAQLTA REKHTVVVSA RTGAGIDELR AVIERELPRF DREVRMLVPY QRGDLVSRVH EEGEVLDVEH TEEGTILHAR VLPGLFAELE RTARPVETV // ID A0A171KU81_9BURK Unreviewed; 368 AA. AC A0A171KU81; DT 06-JUL-2016, integrated into UniProtKB/TrEMBL. DT 06-JUL-2016, sequence version 1. DT 07-JUN-2017, entry version 10. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=AAV32_05140 {ECO:0000313|EMBL:KKO72448.1}; OS Kerstersia gyiorum. OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Alcaligenaceae; Kerstersia. OX NCBI_TaxID=206506 {ECO:0000313|EMBL:KKO72448.1, ECO:0000313|Proteomes:UP000078084}; RN [1] {ECO:0000313|EMBL:KKO72448.1, ECO:0000313|Proteomes:UP000078084} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CG1 {ECO:0000313|EMBL:KKO72448.1, RC ECO:0000313|Proteomes:UP000078084}; RA Greninger A.L., Kozyreva V., Chaturvedi V.; RT "Genome sequence of Kerstersia gyiorum CG1."; RL Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KKO72448.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LBNE01000002; KKO72448.1; -; Genomic_DNA. DR RefSeq; WP_068368434.1; NZ_LBNE01000002.1. DR EnsemblBacteria; KKO72448; KKO72448; AAV32_05140. DR PATRIC; fig|206506.3.peg.1103; -. DR Proteomes; UP000078084; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000078084}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000078084}. FT DOMAIN 190 356 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 368 AA; 40534 MW; 8027D601F13D7BEB CRC64; MRALIISVDL GSPDHIAHAE EFKMLAEGAG AEIVDVITVK RQRPDAAYFI GTGKLEEAVA LSKAHEAEVI LFDQPLSPAQ QRNLERQIGL RVVDRVALIL DIFALRAQSH EGKLQVELAQ LQHLSTRLTR LWTHLERQRG GIGMRGPGES QLEMDRRMIG DKVKGLRERL AKVERQRRTQ RRSRNRGVHM SVSLVGYTNA GKSTLFNALT RAGAYAADQL FATLDTTTRR IWIEGAGQVT ISDTVGFIRD LPPTLIAAFR ATLEETVHAD LLLHVVDASS PQRDEQILEV EKVLQDIGAG DIPRIQVYNK IDLAGLAPRV DYDVHGTIAR VFVSAAERIG LDALRGAIAQ AAINAGNNVS TFQTVQSE // ID A0A172Q803_9STRE Unreviewed; 413 AA. AC A0A172Q803; DT 07-SEP-2016, integrated into UniProtKB/TrEMBL. DT 07-SEP-2016, sequence version 1. DT 07-JUN-2017, entry version 9. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=A0O21_05930 {ECO:0000313|EMBL:AND79594.1}; OS Streptococcus pantholopis. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=1811193 {ECO:0000313|EMBL:AND79594.1, ECO:0000313|Proteomes:UP000077317}; RN [1] {ECO:0000313|EMBL:AND79594.1, ECO:0000313|Proteomes:UP000077317} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=TA 26 {ECO:0000313|EMBL:AND79594.1, RC ECO:0000313|Proteomes:UP000077317}; RA Bai X.; RT "Streptococcus antelopensis sp. nov., isolated from the feces of the RT Tibetan antelope (Pantholops hodgsonii) in Hoh Xil National Nature RT Reserve, Qinghai, China."; RL Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP014699; AND79594.1; -; Genomic_DNA. DR RefSeq; WP_067062773.1; NZ_CP014699.1. DR EnsemblBacteria; AND79594; AND79594; A0O21_05930. DR Proteomes; UP000077317; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000077317}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000077317}. FT DOMAIN 199 359 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 413 AA; 46659 MW; 5E4B193FE5BCBBAC CRC64; MLATAPKQER VLLFGVELPE SRHFAASMNE LARLAQTAGA HVAARSSQKR SQYDSRFLLG SGKLADLQSI IKAKHIDTLI VNNRLSPRQH NNLESALNLK VLDRMQLILD IFALHARSYE GKLQVQLAQL DYLLPRLTGK GAFLSRQAGG IGSRGPGESQ LELNRRLIRS QMTTIKRELR KISQNRQLLR EERLGADTFK IGLVGYTNAG KSTIMNLLTR GDEYVADSLF ATLDSSTKQL YLQGQFQATL TDTVGFIQDL PTELIAAFKS TLEESRHVNM LLHVIDASDP QHERQESLVL KLLEELDMMS IPRLTVYNKI DLAEHFSPTL FPYIQLSARE QKSKKKLQQQ LIAEIKKQFT VFDLNLSADR HGKLYELGKY ALLNYGSADS SGSQTVRAYI APENKWRLED FYD // ID A0A172RY99_9ACTN Unreviewed; 434 AA. AC A0A172RY99; DT 07-SEP-2016, integrated into UniProtKB/TrEMBL. DT 07-SEP-2016, sequence version 1. DT 07-JUN-2017, entry version 10. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=AAY81_05730 {ECO:0000313|EMBL:ANE22700.1}, GN SAMN02910314_01462 {ECO:0000313|EMBL:SEO87535.1}; OS Denitrobacterium detoxificans. OC Bacteria; Actinobacteria; Coriobacteriia; Eggerthellales; OC Eggerthellaceae; Denitrobacterium. OX NCBI_TaxID=79604 {ECO:0000313|EMBL:ANE22700.1, ECO:0000313|Proteomes:UP000077372}; RN [1] {ECO:0000313|EMBL:ANE22700.1, ECO:0000313|Proteomes:UP000077372} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NPOH1 {ECO:0000313|EMBL:ANE22700.1, RC ECO:0000313|Proteomes:UP000077372}; RA Anderson R.A.; RT "Genome of Denitrobactrium detoxificans, a ruminal bacterium that RT respires on nitrocompounds."; RL Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:SEO87535.1, ECO:0000313|Proteomes:UP000182975} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 21843 {ECO:0000313|EMBL:SEO87535.1, RC ECO:0000313|Proteomes:UP000182975}; RA de Groot N.N.; RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP011402; ANE22700.1; -; Genomic_DNA. DR EMBL; FOEC01000009; SEO87535.1; -; Genomic_DNA. DR RefSeq; WP_066662487.1; NZ_FOEC01000009.1. DR EnsemblBacteria; ANE22700; ANE22700; AAY81_05730. DR KEGG; ddt:AAY81_05730; -. DR PATRIC; fig|79604.3.peg.1156; -. DR KO; K03665; -. DR Proteomes; UP000077372; Chromosome. DR Proteomes; UP000182975; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000077372}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000077372}. FT DOMAIN 214 379 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 434 AA; 48157 MW; BA00634292FE17A7 CRC64; MSVNKNRFPL RETAEVAERA ILVGIDRPGA AWPLSETMAE LERLTATAGA EVVAQTTQRL DAPNPRTFVG SGKAVEIAEL CTAYSADIVI FDDELTPSQQ GNLEKIMGRD VKVIDRTALI LDIFALHATT REGRLQVKLA QNQYLYPRLR GMWAHLASNR MGGGVGSRFG EGESQLEVDR RIVRNRITSI RRELAELDKN RSVQRQGRQE SGMLRVALAG YTNAGKSSLL NALTNASVLS YDKLFATLDS TTRKYTLPEG REITLTDTVG FIQKLPTTLV ESFKSTLDEV REANIILHVV DASSDYFEGQ MRAVDDVLNQ IGAQDIPSIL VLNKIDLLDD EGREALAYHF PNAMQISSVT REGLDALIAR IVKLAAAQDE ILHVLVPYTR GDIVALAHER CYIVEEHYDE QGTWMTIRVS PSLASRFEPF SVRA // ID A0A172TBI5_9DEIO Unreviewed; 583 AA. AC A0A172TBI5; DT 07-SEP-2016, integrated into UniProtKB/TrEMBL. DT 07-SEP-2016, sequence version 1. DT 07-JUN-2017, entry version 8. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=SU48_12150 {ECO:0000313|EMBL:ANE44388.1}; OS Deinococcus puniceus. OC Bacteria; Deinococcus-Thermus; Deinococci; Deinococcales; OC Deinococcaceae; Deinococcus. OX NCBI_TaxID=1182568 {ECO:0000313|EMBL:ANE44388.1, ECO:0000313|Proteomes:UP000077363}; RN [1] {ECO:0000313|EMBL:ANE44388.1, ECO:0000313|Proteomes:UP000077363} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DY1 {ECO:0000313|EMBL:ANE44388.1, RC ECO:0000313|Proteomes:UP000077363}; RA Kim M.K., Srinivasan S., Lee J.-J.; RT "Deinococcus puniceus/DY1/ whole genome sequencing."; RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP011387; ANE44388.1; -; Genomic_DNA. DR RefSeq; WP_064015467.1; NZ_CP011387.1. DR EnsemblBacteria; ANE44388; ANE44388; SU48_12150. DR KEGG; dpu:SU48_12150; -. DR PATRIC; fig|1182568.3.peg.2512; -. DR KO; K03665; -. DR Proteomes; UP000077363; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000077363}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000077363}. FT DOMAIN 388 565 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 347 381 {ECO:0000256|SAM:Coils}. FT COILED 547 577 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 583 AA; 64025 MW; AD3DC53864DD0914 CRC64; MDKVLGNTSG LRPAQLKSLS NLYRRRIEPG RVGSPELARN LAELAFDIRR EVSVLIDRRG RVISVSVADA KAAELPELRM GENRLAGFHL LHAHPKGGGL SKGDLSTLFL KRLDAMSAIE VRAANGEGQP GLVHTAHLTP PGTVGEEEDW RILPPVPSFQ IDEFDLGAQV SALEEEIARA ARTRQATKDR ERAILVQIDQ GEFDADERLT ELAELARTAG ADVVHKELVF RRNLKPGTLV GAGKLEELTS RAYHLDAELL IFGQELGPAQ AREIEAATGL KIVDRTQLIL DIFALHAQGV ESRLQVELAQ LRYMKPRLLG AGAQLSRIGG GGGSAAGGAI GTRGPGETKL ELDRRRINDR LSFLEKQLEN VAMRREERRK QRSRNEVPVV SIVGYTNAGK STLLNAFTHA TDEPRRVLAE NKLFATLRPT SRQGFIEGIG PVVLTDTVGF IRDLPKDLTR AFRSTLEEIG DADVLLHVLD AASPGADTRF DAVNRILEDL GFRDMPTVVA LNKADATDED TLRREQGRIL DTVGEETPSI PTSALNNRGL TELREALADA INRVQREELA AREEVRERAA EWQ // ID A0A172TIU9_9BACL Unreviewed; 423 AA. AC A0A172TIU9; DT 07-SEP-2016, integrated into UniProtKB/TrEMBL. DT 07-SEP-2016, sequence version 1. DT 07-JUN-2017, entry version 9. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=SY83_12035 {ECO:0000313|EMBL:ANE46886.1}; OS Paenibacillus swuensis. OC Bacteria; Firmicutes; Bacilli; Bacillales; Paenibacillaceae; OC Paenibacillus. OX NCBI_TaxID=1178515 {ECO:0000313|EMBL:ANE46886.1, ECO:0000313|Proteomes:UP000076927}; RN [1] {ECO:0000313|EMBL:ANE46886.1, ECO:0000313|Proteomes:UP000076927} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DY6 {ECO:0000313|EMBL:ANE46886.1, RC ECO:0000313|Proteomes:UP000076927}; RA Kim M.K., Srinivasan S., Lee J.-J.; RT "Paenibacillus swuensis/DY6/whole genome sequencing."; RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP011388; ANE46886.1; -; Genomic_DNA. DR RefSeq; WP_068606795.1; NZ_CP011388.1. DR EnsemblBacteria; ANE46886; ANE46886; SY83_12035. DR PATRIC; fig|1178515.4.peg.2403; -. DR Proteomes; UP000076927; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000076927}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000076927}. FT DOMAIN 198 366 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 164 191 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 423 AA; 48134 MW; C1CBFD0532B91C9F CRC64; MEQLKEKAII MGVHLANRPD FAYAMEELSN LAEACHIELA GELTQKVTRI VPSTYIGKGK IQELSELIEE KGASLVISND ELTPSQIRNL ESSLDCKVID RTVLILEIFA ERAQTRESQL QVEIAQLQYM LPRLVGLRTS LGRQGGGSGM INRGSGETKR ELDRRRIEER ITALQAELEM LVTRRQTQRK QRRKNEVPVV CLVGYTNAGK SSLMNAILQQ YNRGTTKQVL AKDMLFATLE TSVRNINLPD RKSFLLTDTV GFVSQLPHHL VKAFRSTLEE VAEADLLIHV VDLSSPEYTK QMEVTKHTLK ELGASEIPVI IAYNKADLTE YPYPQIEGDS VYLSAREHRG IDEMAQVIRD QVFQQYVHCE MIIPYDQSRL VAYFNEHAHV TETSYEEDGT RLKMECRASD LEQYRELLHQ ANL // ID A0A172TLD9_9BACL Unreviewed; 428 AA. AC A0A172TLD9; DT 07-SEP-2016, integrated into UniProtKB/TrEMBL. DT 07-SEP-2016, sequence version 1. DT 07-JUN-2017, entry version 9. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=SY83_18025 {ECO:0000313|EMBL:ANE47875.1}; OS Paenibacillus swuensis. OC Bacteria; Firmicutes; Bacilli; Bacillales; Paenibacillaceae; OC Paenibacillus. OX NCBI_TaxID=1178515 {ECO:0000313|EMBL:ANE47875.1, ECO:0000313|Proteomes:UP000076927}; RN [1] {ECO:0000313|EMBL:ANE47875.1, ECO:0000313|Proteomes:UP000076927} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DY6 {ECO:0000313|EMBL:ANE47875.1, RC ECO:0000313|Proteomes:UP000076927}; RA Kim M.K., Srinivasan S., Lee J.-J.; RT "Paenibacillus swuensis/DY6/whole genome sequencing."; RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP011388; ANE47875.1; -; Genomic_DNA. DR RefSeq; WP_068609040.1; NZ_CP011388.1. DR EnsemblBacteria; ANE47875; ANE47875; SY83_18025. DR PATRIC; fig|1178515.4.peg.3633; -. DR Proteomes; UP000076927; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000076927}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000076927}. FT DOMAIN 208 372 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 428 AA; 47997 MW; C4BC7557A6844A80 CRC64; MRNQTHDTNA TLADRAVLVS LYTNDLKLKE VNLEYSLAEL VGLAETAGVE VLDTITQNKD TKDPKWFIGK GKVEELKLRI DELGATTAIF DQELSGAQVR NLEAALDVKI IDRTQLILDI FAGRAKTREG IVQVELAQLS YLLPRLSGQG KNLSRLGGGI GTRGPGETKL ETDRRHIRDR INELKGHLHE MVRHRTLHRE RRKKTGIFQV ALVGYTNAGK STLLKQLTQA DVLVENQLFA TLDPTSRNLM LPAGKEIVLT DTVGFIQNLP HDLVAAFRAT LEEANEADLI LHIVDSSSDN RSDQMKVVQK VLEELGASGK EQMTVFNKID LCSPEEREML TTEGEYIKIN AYSPSDLDKL KEAVQERMTG DTLTFRIPSD RGDLAAHVYR IGEVLEQSFD ESDILYNVRI NRLDYEKLGY VLEPYTEA // ID A0A172TWG2_9BACT Unreviewed; 396 AA. AC A0A172TWG2; DT 07-SEP-2016, integrated into UniProtKB/TrEMBL. DT 07-SEP-2016, sequence version 1. DT 07-JUN-2017, entry version 9. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=SY85_13470 {ECO:0000313|EMBL:ANE51370.1}; OS Flavisolibacter sp. LCS9. OC Bacteria; Bacteroidetes; Chitinophagia; Chitinophagales; OC Chitinophagaceae; Flavisolibacter. OX NCBI_TaxID=1492898 {ECO:0000313|EMBL:ANE51370.1, ECO:0000313|Proteomes:UP000077177}; RN [1] {ECO:0000313|EMBL:ANE51370.1, ECO:0000313|Proteomes:UP000077177} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=LCS9 {ECO:0000313|EMBL:ANE51370.1, RC ECO:0000313|Proteomes:UP000077177}; RA Kim M.K., Srinivasan S., Lee J.-J.; RT "Flavisolibacter sp./LCS9/ whole genome sequencing."; RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP011390; ANE51370.1; -; Genomic_DNA. DR RefSeq; WP_066405333.1; NZ_CP011390.1. DR EnsemblBacteria; ANE51370; ANE51370; SY85_13470. DR KEGG; fla:SY85_13470; -. DR PATRIC; fig|1492898.3.peg.2906; -. DR KO; K03665; -. DR Proteomes; UP000077177; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000077177}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000077177}. FT DOMAIN 202 384 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 396 AA; 45715 MW; D500807D2173C3A6 CRC64; MIEKKNIVKH EERAVLVGVI QKDQTEHQVK EYLDELAFLA ETAGAVTIKK FMQKLAHPDS RTFVGKGKLQ EIAEYAKLHD VSMLIFDDEL SGAQISNIEK ETNTKTIDRS DLILDIFARR AKTAQAKAQV ELAQYQYILP RLRGMWKHLE RLGGGIGTRG PGETEIETDR RIVRDKISLL RKRLAEIDKQ AFTQRKDRGE FIRVALVGYT NVGKSTIMNL LSKSDVLAEN KLFATLDTTT RKIVYENTPF LLSDTVGFIR KLPHHLVESF KSTLDEVREA DILLHVVDIA HANYEDQIGV VNKTLQELKA FDKPVLTIFN KMDLYIKHTF DEWLEESTKE EILKDLKERW QDATQGNAIF ISALERTHID DLRTAILEKV REMYKIRYPY KTAFFY // ID A0A172UAF9_9GAMM Unreviewed; 421 AA. AC A0A172UAF9; DT 07-SEP-2016, integrated into UniProtKB/TrEMBL. DT 07-SEP-2016, sequence version 1. DT 07-JUN-2017, entry version 8. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=AYM39_13275 {ECO:0000313|EMBL:ANE56053.1}; OS Methylomonas sp. DH-1. OC Bacteria; Proteobacteria; Gammaproteobacteria; Methylococcales; OC Methylococcaceae; Methylomonas. OX NCBI_TaxID=1727196 {ECO:0000313|EMBL:ANE56053.1, ECO:0000313|Proteomes:UP000077385}; RN [1] {ECO:0000313|EMBL:ANE56053.1, ECO:0000313|Proteomes:UP000077385} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DH-1 {ECO:0000313|EMBL:ANE56053.1, RC ECO:0000313|Proteomes:UP000077385}; RA Hur D.H., Na J.-G., Jeong H., Yoon S.H., Lee E.Y.; RT "Complete genome sequence of the methanotrophic bacterium Methylomonas RT sp. DH-1."; RL Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP014360; ANE56053.1; -; Genomic_DNA. DR RefSeq; WP_064022035.1; NZ_CP014360.1. DR EnsemblBacteria; ANE56053; ANE56053; AYM39_13275. DR KEGG; mdh:AYM39_13275; -. DR KO; K03665; -. DR Proteomes; UP000077385; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000077385}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000077385}. FT DOMAIN 196 363 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 162 189 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 421 AA; 46581 MW; 9C51B7139D958E7C CRC64; MFERPDAGER AILVHLNLQV GQEDLDELKE LTKSAGAQPI HVVTGSRHRP DPKYFVGIGK LDEIKAAVVE HQADIIIVNH PLSPSQERNL ERALEVRVVD RNGLILDIFA QRAQTFEGKL QVELAQLKHL STRLIRGWTH LERQKGGIGL RGPGETQLET DRRLLAVRIK QIQQRLEKVE KQRHQSRSKR KKAEIPTVSL VGYTNAGKST LFNTLTGAGI YAADQLFATL DPTLRQLPLP DGGEIILADT VGFIRHLPHE LVAAFRSTLQ EAAEADLLLH VIDSAAEDRD DTIIQVNQVL EDIGAGKIAQ LKVFNKIDLL GDLEPHIDYD AEGRPVCVWI SAQSGAGCDL LQQALGELFA SSKVIRKCYL PAGQAGLKAK LFAFVRIISD VTDDHGDCEL TIEIDKKHLG LLKHIRVEAV A // ID A0A172UQ59_9MYCO Unreviewed; 470 AA. AC A0A172UQ59; DT 07-SEP-2016, integrated into UniProtKB/TrEMBL. DT 07-SEP-2016, sequence version 1. DT 07-JUN-2017, entry version 9. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=A7U43_18780 {ECO:0000313|EMBL:ANE81058.1}; OS Mycobacterium sp. YC-RL4. OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae; OC Mycobacterium. OX NCBI_TaxID=1682113 {ECO:0000313|EMBL:ANE81058.1, ECO:0000313|Proteomes:UP000077143}; RN [1] {ECO:0000313|EMBL:ANE81058.1, ECO:0000313|Proteomes:UP000077143} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=YC-RL4 {ECO:0000313|EMBL:ANE81058.1, RC ECO:0000313|Proteomes:UP000077143}; RA Ren L., Fan S., Ruth N., Jia Y., Wang J., Qiao C.; RT "Complete genome sequence of a phthalic acid esters degrading RT Mycobacterium sp. YC-RL4."; RL Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP015596; ANE81058.1; -; Genomic_DNA. DR RefSeq; WP_067998324.1; NZ_CP015596.1. DR EnsemblBacteria; ANE81058; ANE81058; A7U43_18780. DR Proteomes; UP000077143; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000077143}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}. FT DOMAIN 247 416 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 470 AA; 50779 MW; C97087A5F03096BC CRC64; MTESELTRNP VPSTGELALE DRAALRRVAG LSTELTDISE VEYRQLRLER VVLVGVWTEG TAADVDASMA ELAALAETAG SEVLEGLVQR RDKPDASTYI GSGKAIELRD IVTATGADTV ICDGELSPAQ LNSLEKVVKV KVIDRTALIL DIFAQHATSA EGKAQVSLAQ MEYMLPRLRG WGESMSRQGG GAGGSSGGVG TRGPGETKIE TDRRRIRERM TKLRREIKDM KKIRDTQRGK RRAADLPAVA IVGYTNAGKS SLLNALTGAG VLVENALFAT LEPTTRRGEL DDGRPFVLTD TVGFVRHLPT QLVEAFRSTL EEVVDADLLV HVVDGSDATP LAQINAVREV VRDVYADHDG SPAPELLVVN KIDAADELAL AQLRRALPDA VFVSAHTGEG LDRLRARLVE LVEPTDAFVD VTVPYDRGDL VARVHTEGRI DTTEHTDTGT KITARVPVPL AASLREFSNW // ID A0A172X3J4_9MICO Unreviewed; 511 AA. AC A0A172X3J4; DT 07-SEP-2016, integrated into UniProtKB/TrEMBL. DT 07-SEP-2016, sequence version 1. DT 07-JUN-2017, entry version 8. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=A0130_04795 {ECO:0000313|EMBL:ANF31089.1}; OS Leifsonia xyli. OC Bacteria; Actinobacteria; Micrococcales; Microbacteriaceae; Leifsonia. OX NCBI_TaxID=1575 {ECO:0000313|EMBL:ANF31089.1, ECO:0000313|Proteomes:UP000077845}; RN [1] {ECO:0000313|EMBL:ANF31089.1, ECO:0000313|Proteomes:UP000077845} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SE134 {ECO:0000313|EMBL:ANF31089.1, RC ECO:0000313|Proteomes:UP000077845}; RA Ploux O.; RL Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP014761; ANF31089.1; -; Genomic_DNA. DR RefSeq; WP_064109382.1; NZ_CP014761.1. DR EnsemblBacteria; ANF31089; ANF31089; A0130_04795. DR Proteomes; UP000077845; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 2. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000077845}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000077845}. FT DOMAIN 289 454 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 511 AA; 55357 MW; 5C49DD9F514D3F84 CRC64; MTDKTNIREH TEDDVVARVL ATENNRASVT LFGAGSADRA QALQAERADG GLHDGEQFER EERAALRRVS GLSTELQDVT EVEYRQLRLE NVVLIGVYSQ GSLQDAENSM RELAALAETA GAAVLDGLLQ RRPHPDPSTY LGRGKAEELA GIVAALGADT VIADTELAPS QRRALEDVVK VKVIDRTAVI LDIFSQHAKS REGKAQVELA QLEYLLPRLR GWGESMSRQA GGQVGGAGAG MGSRGPGETK IELDRRRIHT RMARLRKQIA GFKPAREAKR ANRNRNSVPS VAIAGYTNAG KSSLLNRVTK AGVLVENALF ATLDATVRRS VTADGRLYTL ADTVGFVRNL PHQLVEAFRS TLEEVADSDV ILHVVDGSHP DPASQLATVR DVIGEVGARD IPEIVVFNKA DLIPEDERLV LRGLEPGAIF ASARTGEGVD EVLAAIARLL PDPSLEVELV VPYDRGDLIS ALHERGRVIS TEYVEEGTRV TARIMPEYHA AFEPFEVTAT A // ID A0A172YDS8_9GAMM Unreviewed; 435 AA. AC A0A172YDS8; DT 07-SEP-2016, integrated into UniProtKB/TrEMBL. DT 07-SEP-2016, sequence version 1. DT 30-AUG-2017, entry version 9. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=A5892_07970 {ECO:0000313|EMBL:ANF57409.1}; OS Halotalea alkalilenta. OC Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales; OC Halomonadaceae; Halotalea. OX NCBI_TaxID=376489 {ECO:0000313|EMBL:ANF57409.1, ECO:0000313|Proteomes:UP000077875}; RN [1] {ECO:0000313|EMBL:ANF57409.1, ECO:0000313|Proteomes:UP000077875} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=IHB B 13600 {ECO:0000313|EMBL:ANF57409.1, RC ECO:0000313|Proteomes:UP000077875}; RA Swarnkar M.K., Sharma A., Kaushal K., Soni R., Rana S., Singh A.K., RA Gulati A.; RT "Complete Genome Sequence of Halotalea alkalilenta IHB B 13600."; RL Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP015243; ANF57409.1; -; Genomic_DNA. DR RefSeq; WP_064122360.1; NZ_CP015243.1. DR EnsemblBacteria; ANF57409; ANF57409; A5892_07970. DR KEGG; haa:A5892_07970; -. DR KO; K03665; -. DR Proteomes; UP000077875; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000077875}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000077875}. FT DOMAIN 199 365 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 435 AA; 49203 MW; 1EA8DCF4F3B77780 CRC64; MFFERPDSGE TAILVHIEFQ DGREPEDPME LLELARSAGA IPAALIEGSR RYPEARMFIG EGKLEEVREA LRAHEAELVI FNHALKPSQE RNLEKELKCR VLDRTGLILD IFAQRARTHE GKLQVELAQL EYMSTRLVRG WTHLERQKGG IGLRGPGETQ LETDRRLLRA RIRQINKRLE KVRSQRSQNR RARDRAEIPS TSLVGYTNAG KSTLFNALTS SDVYAADQLF ATLDPTLRRL EVADVGPVVL ADTVGFIRHL PHKLVQAFKA TLEEAAEADL LIHVIDAADP DREANIAQVD AVLEEIGAQD VPRLLVMNKI DLLGSQPRLE RDAQGRPHTV WLSARDAQGF ELFHQALSEL LAVDLVELSL RLAPHKGWLR AQLHELGAVR EEHYDEQGYA CLDIRLPQRD FLQLLSRGEE NPRDYLPAEA FASDY // ID A0A172ZIK9_9BACL Unreviewed; 428 AA. AC A0A172ZIK9; DT 07-SEP-2016, integrated into UniProtKB/TrEMBL. DT 07-SEP-2016, sequence version 1. DT 07-JUN-2017, entry version 8. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=AR543_15310 {ECO:0000313|EMBL:ANF97232.1}; OS Paenibacillus bovis. OC Bacteria; Firmicutes; Bacilli; Bacillales; Paenibacillaceae; OC Paenibacillus. OX NCBI_TaxID=1616788 {ECO:0000313|EMBL:ANF97232.1, ECO:0000313|Proteomes:UP000078148}; RN [1] {ECO:0000313|EMBL:ANF97232.1, ECO:0000313|Proteomes:UP000078148} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BD3526 {ECO:0000313|EMBL:ANF97232.1, RC ECO:0000313|Proteomes:UP000078148}; RA Wu Z., Gao C., Liu Z., Zheng H.; RT "Genome of Paenibacillus bovis sp. nov."; RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP013023; ANF97232.1; -; Genomic_DNA. DR RefSeq; WP_060535346.1; NZ_CP013023.1. DR EnsemblBacteria; ANF97232; ANF97232; AR543_15310. DR KEGG; pbv:AR543_15310; -. DR KO; K03665; -. DR Proteomes; UP000078148; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000078148}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000078148}. FT DOMAIN 208 372 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 428 AA; 48650 MW; 8A51213F577248FC CRC64; MKNETHDTQT EQQARAILVS LYTQLDKRNG VNAEGSMEEL VSLAETAGVE VLEQLTQNKE KPDFRWFIGK GKVEELRILV DSLEANTVIF DQELSGAQVR NLEEQLDAKI IDRTQLILDI FAQRAKTREG ILQVELAQYN YLLPRLSGQG KNLSRLGGGI GTRGPGESKL EIDRRHIRTR VTELKRQLEE IMRHRTLYRE RRKKTGIVQV ALVGYTNAGK STLLKQLTDA DVYIQNQLFA TLDPTSRNLE LPGGKEIVLT DTVGFIQNLP HDLIAAFRAT LEEVNEADLI LHVVDASSER RDEQMQVVDE ILQELGSGNK PQVILYNKID LCTPQQLEML PVDQTHLRIS AYHEPDLEAV KNIIQDQLAG GIKTYRIPAE RGDLISQLYT FSSIISQDYE DNDALFTVEI NQTDYDKFGY KLQEYEIK // ID A0A176FWB7_9RHOB Unreviewed; 376 AA. AC A0A176FWB7; DT 07-SEP-2016, integrated into UniProtKB/TrEMBL. DT 07-SEP-2016, sequence version 1. DT 07-JUN-2017, entry version 6. DE SubName: Full=GTPase HflX {ECO:0000313|EMBL:KZY48803.1}; DE Flags: Fragment; GN ORFNames=A3731_27215 {ECO:0000313|EMBL:KZY48803.1}; OS Roseovarius sp. HI0049. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae; Roseovarius. OX NCBI_TaxID=1822235 {ECO:0000313|EMBL:KZY48803.1, ECO:0000313|Proteomes:UP000077043}; RN [1] {ECO:0000313|EMBL:KZY48803.1, ECO:0000313|Proteomes:UP000077043} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=HI0049 {ECO:0000313|EMBL:KZY48803.1, RC ECO:0000313|Proteomes:UP000077043}; RA Sosa O.A.; RT "Microbial cycling of marine high molecular weight dissolved organic RT matter."; RL Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KZY48803.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LWFA01000032; KZY48803.1; -; Genomic_DNA. DR EnsemblBacteria; KZY48803; KZY48803; A3731_27215. DR Proteomes; UP000077043; Unassembled WGS sequence. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000077043}. FT DOMAIN 155 325 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT NON_TER 1 1 {ECO:0000313|EMBL:KZY48803.1}. SQ SEQUENCE 376 AA; 42056 MW; 531B6F90FEBA22EF CRC64; NVMRLRQPHP GTLFSKGKLE ELRNLIEAEE VQLLLVDGPV TPVQQRNLEN DLKVKLLDRT GLILEIFSDR AATREGVLQV EMAALSYQRT RLVRAWTHLE RQRGGLGFVG GPGETQIEAD RRAIDEQLVR LKRQLEKVVR TRSLHRAARA KVPFPIVALV GYTNAGKSTL FNRMTGADVM AKDMLFATLD PTMRKIELPG NGPEVILSDT VGFISNLPTE LVAAFRATLE EVTAADLIVH VRDISHPESE EQAADVAAIL ESLGVQKEVP QIELWNKIDR VDSEARPLLE NRAARSENVY LLSAVTGEGI ADVVEAIKEE IAGVTTVEDL HLGFDDGRRR AWLFERGLVE EERQDEDGYH LTVRWNARQA AQFEAL // ID A0A176H234_9GAMM Unreviewed; 431 AA. AC A0A176H234; DT 07-SEP-2016, integrated into UniProtKB/TrEMBL. DT 07-SEP-2016, sequence version 1. DT 30-AUG-2017, entry version 10. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=A3741_09985 {ECO:0000313|EMBL:KZY77361.1}; OS Oleiphilus sp. HI0069. OC Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales; OC Oleiphilaceae; Oleiphilus. OX NCBI_TaxID=1822245 {ECO:0000313|EMBL:KZY77361.1, ECO:0000313|Proteomes:UP000077151}; RN [1] {ECO:0000313|EMBL:KZY77361.1, ECO:0000313|Proteomes:UP000077151} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=HI0069 {ECO:0000313|EMBL:KZY77361.1, RC ECO:0000313|Proteomes:UP000077151}; RA Sosa O.A.; RT "Microbial cycling of marine high molecular weight dissolved organic RT matter."; RL Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KZY77361.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LWFK01001951; KZY77361.1; -; Genomic_DNA. DR RefSeq; WP_068514973.1; NZ_LWFK01001951.1. DR EnsemblBacteria; KZY77361; KZY77361; A3741_09985. DR Proteomes; UP000077151; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000077151}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000077151}. FT DOMAIN 198 365 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 431 AA; 48642 MW; 01DAEAB79F9EDDB5 CRC64; MFDRPDSGEL AILVHIDFNS EKEREDPDEF KELVSSAGVE TLAVITGSRD KPDARHFVGK GKLEEIQFEL EHGEADVVLF NHALSPSQQR NLEAALECRI IDRTGIILDI FAQRARTHEG KLQVELAQLE YMSTRLIRGW THLERQKGGI GLRGPGETQL ESDRRLLRGR IKTITSRLEK VRKQRDQGRR ARTRAEIPTV SLVGYTNAGK STLFNRVTEA DVYAADQLFA TLDPTLRKLN LPDIGNAILV DTVGFIRHLP HKLVDAFRAT LEETCNATLL LHVIDCHDEG RMDNIEQVEH VLKEIGADKV PTLKVYNKLD LLDGREPRID RDEDGVPQRV WVSAYTGAGV DLLNQAIIEI LGDEIVHQKI KLDPSKGGKL RALFYAASVV QDESYDEEGG LVLEIRLQRL DYERLLRQAE VNESDLDITN L // ID A0A176I6D8_9GAMM Unreviewed; 436 AA. AC A0A176I6D8; DT 07-SEP-2016, integrated into UniProtKB/TrEMBL. DT 07-SEP-2016, sequence version 1. DT 05-JUL-2017, entry version 10. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=A3746_03340 {ECO:0000313|EMBL:KZZ06619.1}; OS Oleibacter sp. HI0075. OC Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales; OC Oleibacter. OX NCBI_TaxID=1822250 {ECO:0000313|EMBL:KZZ06619.1, ECO:0000313|Proteomes:UP000077099}; RN [1] {ECO:0000313|EMBL:KZZ06619.1, ECO:0000313|Proteomes:UP000077099} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=HI0075 {ECO:0000313|EMBL:KZZ06619.1, RC ECO:0000313|Proteomes:UP000077099}; RA Sosa O.A.; RT "Microbial cycling of marine high molecular weight dissolved organic RT matter."; RL Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KZZ06619.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LWFP01000890; KZZ06619.1; -; Genomic_DNA. DR RefSeq; WP_068437344.1; NZ_LWFP01000890.1. DR EnsemblBacteria; KZZ06619; KZZ06619; A3746_03340. DR Proteomes; UP000077099; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000077099}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000077099}. FT DOMAIN 200 367 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 436 AA; 49103 MW; 9B0C3A6A99B3306F CRC64; MFFERPDSGG EEAILVHVDF PEGANREDLS EFRELVISAG ADPVDLVTTK RDVPHVKTFV GKGKVEEIAE AVRMHDVSLV IFNHALTPSQ ERNVEREIKC RVLDRTGLIL DIFAQRARTH EGKLQVELAQ LQHQSTRLVR GWTHLERQKG GIGMRGPGET QLETDRRLLR ERVKSIHARL EKVRAQRNQS RRARKRSDVP TVAIVGYTNA GKSTLFNALT QAEVYAADQL FATLDPTLRR LEIDDVGEIV LADTVGFIRH LPHKLVEAFR ATLQEAAEAD LLMHVIDCAS DEREGNIEQV ELVLGEIQAD ELPELRVYNK IDLLESGEPR IDRNEDGVPV AVWVSAQERL GFDLLCQAMS ELLGEEIFED RLTLAPADAR LRAILYESGG VQGEDFADNG DIHLQIRMQL QDFKRALSKA EVPESRFIAQ PADPWL // ID A0A176J1F3_9BACI Unreviewed; 424 AA. AC A0A176J1F3; DT 07-SEP-2016, integrated into UniProtKB/TrEMBL. DT 07-SEP-2016, sequence version 1. DT 05-JUL-2017, entry version 10. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=AS29_018275 {ECO:0000313|EMBL:KZZ82754.1}; OS Bacillus sp. SJS. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus. OX NCBI_TaxID=1423321 {ECO:0000313|EMBL:KZZ82754.1, ECO:0000313|Proteomes:UP000028527}; RN [1] {ECO:0000313|EMBL:KZZ82754.1, ECO:0000313|Proteomes:UP000028527} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SJS {ECO:0000313|EMBL:KZZ82754.1, RC ECO:0000313|Proteomes:UP000028527}; RA Newman J.D., Stropko S.J., Pipes S.E.; RT "Bacillus sp. SJS genome."; RL Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KZZ82754.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JAQV02000031; KZZ82754.1; -; Genomic_DNA. DR EnsemblBacteria; KZZ82754; KZZ82754; AS29_018275. DR Proteomes; UP000028527; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000028527}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000028527}. FT DOMAIN 202 364 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 424 AA; 48060 MW; 56BDB59970A3D284 CRC64; MSDLSKTQPE QAIVVGCQLP FVSDEQFYYS LEELKSLIKT AQGSVLADIS QKRDRLHPAT CIGKGKLEEL KSLTEELEPD VVIFNGELSP SQIRNLQKEL EIKVIDRTQL ILDIFAQRAQ TREGKLQVEL AQLDYLLPRL SGQGIHLSRQ GGGIGARGPG ETQLETDRRH INKRMVEIKQ QLKTVISHRA RYRERRKRNQ AFQIALVGYT NAGKSTLFNR LTESDSFEEN LLFATLDPMT RKMGLPSGYQ ALLTDTVGFI QDLPTTLVAA FRSTLEEAKE ADLILHVVDT SSEDSINHEK TVFKLLEELE ASSIPRLTIY NKKDKILPEF TPNTADPYIV ISALNKQDLD DLKMKIEEQV KNEMVPYSME LPPDEGRLIS QLKRDTIVQS FSFNEEKEAY EISGYAQEGD SKLPSKELAD EDEW // ID A0A176K0H6_9BACT Unreviewed; 370 AA. AC A0A176K0H6; DT 07-SEP-2016, integrated into UniProtKB/TrEMBL. DT 07-SEP-2016, sequence version 1. DT 07-JUN-2017, entry version 7. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=AT15_00890 {ECO:0000313|EMBL:OAA30102.1}; OS Kosmotoga arenicorallina S304. OC Bacteria; Thermotogae; Kosmotogales; Kosmotogaceae; Kosmotoga. OX NCBI_TaxID=1453497 {ECO:0000313|EMBL:OAA30102.1, ECO:0000313|Proteomes:UP000077339}; RN [1] {ECO:0000313|EMBL:OAA30102.1, ECO:0000313|Proteomes:UP000077339} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=S304 {ECO:0000313|EMBL:OAA30102.1, RC ECO:0000313|Proteomes:UP000077339}; RA Pollo S.M., Charchuk R., Nesbo C.L.; RT "Kosmotoga genome sequencing."; RL Submitted (FEB-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:OAA30102.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JFHK01000015; OAA30102.1; -; Genomic_DNA. DR EnsemblBacteria; OAA30102; OAA30102; AT15_00890. DR PATRIC; fig|1453497.3.peg.188; -. DR Proteomes; UP000077339; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000077339}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}. FT DOMAIN 148 313 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 107 141 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 370 AA; 42641 MW; 584971A033A3D649 CRC64; MPNPKHYLGT GKLKELKRLI QVYEPDVVFI RHNLTPSQRK NLIRELGIEI IDRTQLILEI FEKHAFTLEG KLEVELARLR YELPFFKGKG GELSNPGGGI GTRGPGEKRL ELDRRKALQR MAFLKKELKK LQLDRQIMRK KRQKVGMPLI ALVGYTNAGK SSLMNRICES GVLVEDKLFS TLDTRIRKSK LPSGREVLII DTVGFIRELP HQLVESFRST LEEISYADFL LVVVDASTPN EDGRLRVINE TLVEIKAADV PKMLVFNKID KCTNERIQFL EGKFPESVFV SALKDINIDE LKHRLDKAIN EMRERYVLRM KIGDYEEVLK IRGKLEILSE KFNGDSVEIE YITDNVTNKR LLNRLKEAGR // ID A0A176KVT1_9ACTN Unreviewed; 497 AA. AC A0A176KVT1; DT 07-SEP-2016, integrated into UniProtKB/TrEMBL. DT 07-SEP-2016, sequence version 1. DT 30-AUG-2017, entry version 10. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=A6P39_35345 {ECO:0000313|EMBL:OAA96210.1}; OS Streptomyces sp. FXJ1.172. OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae; OC Streptomyces. OX NCBI_TaxID=710705 {ECO:0000313|EMBL:OAA96210.1, ECO:0000313|Proteomes:UP000077074}; RN [1] {ECO:0000313|EMBL:OAA96210.1, ECO:0000313|Proteomes:UP000077074} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=FXJ1.172 {ECO:0000313|EMBL:OAA96210.1, RC ECO:0000313|Proteomes:UP000077074}; RA Liu M., Liu N., Shang F., Huang Y.; RT "Activation and identification of NC-1, a novel cryptic RT cyclodepsipeptide from red soil-derived Streptomyces sp. FXJ1.172."; RL Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:OAA96210.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LWRP01000175; OAA96210.1; -; Genomic_DNA. DR RefSeq; WP_067054839.1; NZ_LWRP01000175.1. DR EnsemblBacteria; OAA96210; OAA96210; A6P39_35345. DR Proteomes; UP000077074; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 2. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000077074}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}. FT DOMAIN 275 440 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 497 AA; 54248 MW; 2E33FC1C19EFAF7A CRC64; MTSSSSPSQD TKRLAHDYPE GLRADALMEE DVAWSHEIDG ERDGDQFDRS ERAALRRVAG LSTELEDVTE VEYRQLRLER VVLVGVWTTG TAQDADNSLA ELAALAETAG ALVLDGVIQR RDKPDAATYI GSGKAQELRD IVIETGADTV ICDGELSPGQ LIQLEDVVKV KVIDRTALIL DIFAQHAKSR EGKAQVALAQ MQYMLPRLRG WGQSLSRQMG GGKGGGLATR GPGETKIETD RRRIREKMAK MRREIADMKT GREIKRQERR RNKVPSVAIA GYTNAGKSSL LNRLTGAGVL VENALFATLD PTVRRAETPS GRLYTLADTV GFVRHLPHHL VEAFRSTMEE VGDADLILHV VDGSHPVPEE QLAAVREVIR DVGATDVPEI VVINKADAAD PLVLQRLLRT EKRSLAVSAR TGQGMQELLA LIDNDLPRPS VEIEALVPYT HGKLVARAHS EGEVISEEHT AEGTLLKVRV HEELAADLAP YVPAPAA // ID A0A176QE39_9MICO Unreviewed; 489 AA. AC A0A176QE39; DT 07-SEP-2016, integrated into UniProtKB/TrEMBL. DT 07-SEP-2016, sequence version 1. DT 07-JUN-2017, entry version 9. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=AWH69_08470 {ECO:0000313|EMBL:OAB88028.1}; OS Janibacter melonis. OC Bacteria; Actinobacteria; Micrococcales; Intrasporangiaceae; OC Janibacter. OX NCBI_TaxID=262209 {ECO:0000313|EMBL:OAB88028.1, ECO:0000313|Proteomes:UP000076976}; RN [1] {ECO:0000313|EMBL:OAB88028.1, ECO:0000313|Proteomes:UP000076976} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CD11-4 {ECO:0000313|EMBL:OAB88028.1, RC ECO:0000313|Proteomes:UP000076976}; RA Nair G.R., Kaur G., Chander A.M., Mayilraj S.; RT "Janibacter melonis strain CD11_4 genome sequencing and assembly."; RL Submitted (JAN-2016) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:OAB88028.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LQZG01000002; OAB88028.1; -; Genomic_DNA. DR RefSeq; WP_068273974.1; NZ_LQZG01000002.1. DR EnsemblBacteria; OAB88028; OAB88028; AWH69_08470. DR Proteomes; UP000076976; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 2. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000076976}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000076976}. FT DOMAIN 268 433 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 489 AA; 53269 MW; EDDFE17293E45D7A CRC64; MTEPRSTATD DILARRASAL ADDDGFFDDA DRFDGDQLDR EERTALRRVS GLSTELEDIT EVEYRQLRLE RVVLAAVWSE GTAQDAENSM RELAALAETA GSEVLAGVLQ RRQRPDPGTY LGSGKAVELR DIVIAEGADT VVCDTELAPS QRRALEDVVK VKVIDRTALI LDIFAQHAKS KEGKAQVELA QLQYLLPRLR GWGESMSRQA GGQAAGGQGM GSRGPGETKI ELDRRRINSR IAKLRRELSS MKTHRDTRRG ARDAHGVPAV VIAGYTNAGK STLLNRLTHA GVLVDNQLFA TLDTTVRRAE TPEGRDFTLA DTVGFVRALP HQLVEAFRST LEEVADADLL LHVVDGSHPD PEGQISAVRA VLADVDATDV KEVVVINKAD LADPEVVDRL LRHERHSIAV SARTGLGVDA LRDLISVELP QPDIEVDVVL PYDRGDLVSR IYEEADILGE DHLAEGTRVR AKVMGDLAAE LAPFAAKTA // ID A0A176TDL3_9FLAO Unreviewed; 403 AA. AC A0A176TDL3; DT 07-SEP-2016, integrated into UniProtKB/TrEMBL. DT 07-SEP-2016, sequence version 1. DT 07-JUN-2017, entry version 9. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=LPB303_05390 {ECO:0000313|EMBL:OAD45721.1}; OS Polaribacter atrinae. OC Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales; OC Flavobacteriaceae; Polaribacter. OX NCBI_TaxID=1333662 {ECO:0000313|EMBL:OAD45721.1, ECO:0000313|Proteomes:UP000076923}; RN [1] {ECO:0000313|EMBL:OAD45721.1, ECO:0000313|Proteomes:UP000076923} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=KACC 17473 {ECO:0000313|EMBL:OAD45721.1, RC ECO:0000313|Proteomes:UP000076923}; RA Shin S.-K., Yi H.; RT "Draft genome sequence of Polaribacter atrinae KACC17473."; RL Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:OAD45721.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LVWE01000010; OAD45721.1; -; Genomic_DNA. DR RefSeq; WP_068448681.1; NZ_LVWE01000010.1. DR EnsemblBacteria; OAD45721; OAD45721; LPB303_05390. DR Proteomes; UP000076923; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000076923}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000076923}. FT DOMAIN 200 385 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 403 AA; 46403 MW; 02F290BCAC732E8B CRC64; MIDEREVISE KAVLIGIISQ QQNEIQSTEY LDELEFLTLT AGGVAVKRFV QKMEKPNPKT FLGVGKLEEV RDYIVSNNIG TAIFDDELSP AQIRNIEKVL DCKILDRTNL ILDIFAQRAQ TSSAKTQVEL AQCQYLLPRL TRLWTHLDKQ KGGIGMRGPG ETEIETDRRI IRDKISVLQK KLLTIDRQMA VQRKNRGKMV RVALVGYTNV GKSTLMNVIS KSDVFAENKL FATLDTTVRK VVIKNIPFLL TDTVGFIRKL PTQLVESFKS TLDEVREADL LLHVVDISHP NFEDHIASVN SVLADIKCAD KPSVMVFNKI DAYSHETIDE DDIVTERGKE HYTLQDWKKT WMNDYDVDSI FISALNKDNL EDFKEKTYEE VKKIHIQRFP YNDFLYYEYK EEE // ID A0A176U546_9FIRM Unreviewed; 415 AA. AC A0A176U546; DT 07-SEP-2016, integrated into UniProtKB/TrEMBL. DT 07-SEP-2016, sequence version 1. DT 07-JUN-2017, entry version 9. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=HMPREF2738_02082 {ECO:0000313|EMBL:OAD87929.1}; OS Clostridiales bacterium KLE1615. OC Bacteria; Firmicutes; Clostridia; Clostridiales. OX NCBI_TaxID=1715004 {ECO:0000313|EMBL:OAD87929.1, ECO:0000313|Proteomes:UP000077212}; RN [1] {ECO:0000313|EMBL:OAD87929.1, ECO:0000313|Proteomes:UP000077212} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=KLE1615 {ECO:0000313|EMBL:OAD87929.1, RC ECO:0000313|Proteomes:UP000077212}; RA Wen L., He K., Yang H.; RL Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:OAD87929.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LXPQ01000157; OAD87929.1; -; Genomic_DNA. DR RefSeq; WP_066561484.1; NZ_KV441354.1. DR EnsemblBacteria; OAD87929; OAD87929; HMPREF2738_02082. DR PATRIC; fig|1715004.3.peg.2074; -. DR Proteomes; UP000077212; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000077212}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000077212}. FT DOMAIN 199 366 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 415 AA; 46706 MW; 6CEF2EFA8CEA37EA CRC64; MIETAQKKER LLLVAVNTAE ESRVRASLEE LALLVDTAGG EAVGSIYQNL DHPISATYVG KGKIEEIRQM AAQLDADGIV CDDELTPAQM KNLEQELGFN VLDRTMVILD IFASRARSSE GKIQVELAQL RYRANRLTGM GQSMSRLGGG IGTRGPGESK LETDRRLIHQ RIGQLKSELE QVKRTREVTR KRRNDTHIPV AAIVGYTNAG KSSLLNKLTG SEVLAEDKLF ATLDPTTRLL SLGNDEPLLM TDTVGFIDKL PHHLIDAFRS TLEEAKHADL IIHVVDCSNP EHETQMQVVY QTLKELGVEG KPIFTLMNKQ DLLSEEEKNL FERDMQADRT IEISVKDGTG LDELREVLLS FLRNRKKYVE RLYGYDEMGK IQLLRKYGQI VTEEYRDDGV AVTGYVPNEY YNQIQ // ID A0A176V8A2_9PSED Unreviewed; 433 AA. AC A0A176V8A2; DT 07-SEP-2016, integrated into UniProtKB/TrEMBL. DT 07-SEP-2016, sequence version 1. DT 30-AUG-2017, entry version 8. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=A2T76_09220 {ECO:0000313|EMBL:OAE16837.1}; OS Pseudomonas brenneri. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=129817 {ECO:0000313|EMBL:OAE16837.1, ECO:0000313|Proteomes:UP000077403}; RN [1] {ECO:0000313|EMBL:OAE16837.1, ECO:0000313|Proteomes:UP000077403} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=RGCB 108 {ECO:0000313|EMBL:OAE16837.1, RC ECO:0000313|Proteomes:UP000077403}; RA Dharmaprakash A., Reghunathan D., Krishnankutty S.C., RA Prasannakumar M., Thomas S.; RT "Draft genome sequence of Pseudomonas sp. strain isolated from Arctic RT region producing acyl homoserine lactone molecule."; RL Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:OAE16837.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LVWZ01000007; OAE16837.1; -; Genomic_DNA. DR EnsemblBacteria; OAE16837; OAE16837; A2T76_09220. DR Proteomes; UP000077403; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000077403}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000077403}. FT DOMAIN 199 366 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 433 AA; 48980 MW; 68F43E8BEA86040A CRC64; MFFERHGGGE RVILVHLDGQ DPEAREDPQE FQELANSAGA ETVAFFNVPR HRPTAKFLIG SGKVEELRDL VHAEEADLVI FNHILTPSQE RNLERVFECR VIDRTGLILD IFAQRARTHE GKLQVELAQL DHMSTRLVRG WTHLERQGGG IGMRGPGETQ LETDRRLLRV RLRQIKGRLE KVRSQREQSR RGRTRADIPT VSLVGYTNAG KSTLFNNVTK SDVYAADQLF ATLDPTLRRL ELDDLGPIVL ADTVGFIRHL PHKLVEAFRS TLEESSNSDL LLHVIDAAEP DRMLQIEQVM VVLGEIGAQD LPILEVYNKL DLLEGVEPQI QRDENGRPQR VWLSARDGSG LELLEQAIAE LLGGDLFVGT LRLPQRFARL RAQFFELGAV QKEEHDEEGV SLLAVRLPRS ELNRLVSREG VVPTEFLEQH TLQ // ID A0A176VB33_MARPO Unreviewed; 541 AA. AC A0A176VB33; DT 07-SEP-2016, integrated into UniProtKB/TrEMBL. DT 07-SEP-2016, sequence version 1. DT 07-JUN-2017, entry version 6. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:OAE18099.1}; GN ORFNames=AXG93_2899s1280 {ECO:0000313|EMBL:OAE18099.1}; OS Marchantia polymorpha subsp. polymorpha. OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Marchantiophyta; OC Marchantiopsida; Marchantiidae; Marchantiales; Marchantiaceae; OC Marchantia. OX NCBI_TaxID=1480153 {ECO:0000313|EMBL:OAE18099.1, ECO:0000313|Proteomes:UP000077202}; RN [1] {ECO:0000313|EMBL:OAE18099.1, ECO:0000313|Proteomes:UP000077202} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC TISSUE=Whole gametophyte {ECO:0000313|EMBL:OAE18099.1}; RA Honkanen S., Jones V.A., Morieri G., Champion C., Hetherington A.J., RA Kelly S., Saint-Marcoux D., Proust H., Prescott H., Dolan L.; RT "Mechanisms controlling the formation of the plant cell surface in RT tip-growing cells are functionally conserved among land plants."; RL Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:OAE18099.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LVLJ01004132; OAE18099.1; -; Genomic_DNA. DR Proteomes; UP000077202; Unassembled WGS sequence. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR CDD; cd01878; HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 2. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 2. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000077202}; KW Reference proteome {ECO:0000313|Proteomes:UP000077202}. FT DOMAIN 292 518 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 541 AA; 59048 MW; FDDC6666851A0DA9 CRC64; MRMGFKSCRV SRTCLRLFVD RGSELLAGAG GPGAFQEASS IFRENGTTFP RAGVTELAAP IPWRSAGAGR CVRGFRSSAP GAFWNNDDDE PPRLLVVQPR LHPLPVLKAK LLEALRLADS LEDPRNVDKG KKQRREPSPY VLGRLDAIFV NAPLSGVQQR NLENAWGKPV LDRVGLIIEI FGAHAQSKAA KLQVELASLN YYRSRLVRAR GKAGARLGFG AGGESEVVSA RGRATGAIGG AGETEIQLQR RRILTRKTRL KALLAEVDRT QTLHRAARTR EGITPGQGKS LPVVAVVGYT NAGKSSLVAA LSRSDMYVDD KLFATLDTRS RRVVLPSGKK VLLSDTVGFI SDLPIQLVEA FQATLNEVVE ADYLLHVIDS SAANASEQRE TVLEVLQQIG VSRHKMENCM IEVWNKSDLS GKEFEITQSE DLPEGAVKNT LSEVLSTEAD GLDMAEDSHV THPLKMEHTD IETLSDGAEL LDLEWAREGV SCVSTSVRTK TGLAELLRLL DTKIQSDWAE EGLILSEENL TTDSVEKEIV R // ID A0A176WRM1_MARPO Unreviewed; 669 AA. AC A0A176WRM1; DT 07-SEP-2016, integrated into UniProtKB/TrEMBL. DT 07-SEP-2016, sequence version 1. DT 12-APR-2017, entry version 5. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:OAE35760.1}; GN ORFNames=AXG93_500s1000 {ECO:0000313|EMBL:OAE35760.1}; OS Marchantia polymorpha subsp. polymorpha. OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Marchantiophyta; OC Marchantiopsida; Marchantiidae; Marchantiales; Marchantiaceae; OC Marchantia. OX NCBI_TaxID=1480153 {ECO:0000313|EMBL:OAE35760.1, ECO:0000313|Proteomes:UP000077202}; RN [1] {ECO:0000313|EMBL:OAE35760.1, ECO:0000313|Proteomes:UP000077202} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC TISSUE=Whole gametophyte {ECO:0000313|EMBL:OAE35760.1}; RA Honkanen S., Jones V.A., Morieri G., Champion C., Hetherington A.J., RA Kelly S., Saint-Marcoux D., Proust H., Prescott H., Dolan L.; RT "Mechanisms controlling the formation of the plant cell surface in RT tip-growing cells are functionally conserved among land plants."; RL Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:OAE35760.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LVLJ01000085; OAE35760.1; -; Genomic_DNA. DR Proteomes; UP000077202; Unassembled WGS sequence. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000077202}; KW Reference proteome {ECO:0000313|Proteomes:UP000077202}. FT DOMAIN 447 613 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 669 AA; 74031 MW; C557E79871E4AF5C CRC64; MAEIRSVAGA GAGAGTCSAA KIVAGRFDRR VPRFSAGVSF SRGLSKIARS RAELSPRSLD CRASFSCGGV SRSSLKHAGT GLWSVSSASK STSTAIGLGD YESSSRVRVE LLRVSCVLSD ETSSSAVGNR RRERGPKIVN KSDGILELDK DRRVNRLDTL DVDEIETEYS DEIEGWTDSD DGEISEFEGD EEEWWDKEVL EEEEEDGLQT PSTAIVGTTE AVEEDVARFK LRNGREVYGE RTYLVGIDRK GAGQRSAFGI KDSLAELAQL ADTAGLSVVG STYQKLDITN PRTYIGMGKV AEIQAAVRAF KVETIIFDDE LSPGYTFEST AFFGIFAVST EKQGHQTHLP SQDSLVEVRQ LRNLEKAFEG DVRVELAQCE YQLPRLTRMW THLERQAGGM VKGMGEKQIE VDKRILRSKI SGLKRQLDSV RDHRQQYRDR RAAVPIPVVS LVGYTNAGKS TFLNRLSGAD VLAEDRLFAT LDPTTRRVQL PSGKECLFTD TVGFIQKLPT QLVAAFRATL EEITDSTILV HMVDISHPMA ELQMEAVDNV LDELDVNHIP FLTVWNKIDR AKNASELRAE AAERDDIICL SALTGEGVDS FYDAVERNIK DLLVWVEAVV PYDQGDLISL IHRLGIVDTE EYTEQGTLIR AHVPLALSRK MLHLRQAMT // ID A0A177H4H7_9RHOB Unreviewed; 424 AA. AC A0A177H4H7; DT 07-SEP-2016, integrated into UniProtKB/TrEMBL. DT 07-SEP-2016, sequence version 1. DT 07-JUN-2017, entry version 7. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:OAH05843.1}; GN ORFNames=pfor_36c3250 {ECO:0000313|EMBL:OAH05843.1}; OS Rhodobacteraceae bacterium SB2. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae. OX NCBI_TaxID=1689867 {ECO:0000313|EMBL:OAH05843.1, ECO:0000313|Proteomes:UP000077333}; RN [1] {ECO:0000313|EMBL:OAH05843.1, ECO:0000313|Proteomes:UP000077333} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SB2 {ECO:0000313|EMBL:OAH05843.1, RC ECO:0000313|Proteomes:UP000077333}; RA Poehlein A., Billerbeck S., Voget S., Wemheuer B., Giebel H.-A., RA Brinkhoff T., Daniel R., Simon M.; RT "A new prominent pelagic Roseobacter clade subcluster - CHAB-I-5: RT biogeography and genomic comparison to other roseobacters."; RL Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:OAH05843.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LGRT01000037; OAH05843.1; -; Genomic_DNA. DR EnsemblBacteria; OAH05843; OAH05843; pfor_36c3250. DR PATRIC; fig|1689867.3.peg.3273; -. DR Proteomes; UP000077333; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000077333}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000077333}. FT DOMAIN 204 373 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 424 AA; 47186 MW; E445CC6E106CE1C1 CRC64; MIEHEGRVTR AWVLHPELKT VSGRRDPVAA LAEATSLARA LPELDVVGAT VIGLKKLLPG TLFGSGKLTE LKEIFEEHNV ELVLLDGHVT PVQQRNLEKK WGVKLLDRTA LILEIFSDRA STREGVLQVE MAALGYQRTR LVRAWTHLER QRGGLGFVGG PGETQIEADR RAIDDQLLRL RRQLDKVVKT RALHRAARAK VPFPIVALIG YTNAGKSTLF NRLTGAQVMA KDMLFATLDP TMRNLTLATG HRVILSDTVG FISDLPTELV AAFRATLEEV LSADIIIHVR DIAHASSEEQ ATDVERTLEK LGVSSQVPLL EVWNKIDELE EEARASVLLR AERQENVIAI SALTGAGLEG LQTRISTQLN VSRYVMDVKL SHAEGRRRAW LYQEGVILKE ETTETGSIFE VEWDDAQRQQ FDAL // ID A0A177HVJ3_9ACTN Unreviewed; 507 AA. AC A0A177HVJ3; DT 07-SEP-2016, integrated into UniProtKB/TrEMBL. DT 07-SEP-2016, sequence version 1. DT 07-JUN-2017, entry version 9. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:OAH14690.1}; GN ORFNames=STSP_19510 {ECO:0000313|EMBL:OAH14690.1}; OS Streptomyces jeddahensis. OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae; OC Streptomyces. OX NCBI_TaxID=1716141 {ECO:0000313|EMBL:OAH14690.1, ECO:0000313|Proteomes:UP000077381}; RN [1] {ECO:0000313|EMBL:OAH14690.1, ECO:0000313|Proteomes:UP000077381} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=G25(2015) {ECO:0000313|Proteomes:UP000077381}; RA Poehlein A., Roettig A., Hiessl S., Hauschild P., Schauer J., RA Madkour M.H., Al-Ansari A.M., Almakishah N.H., Steinbuechel A., RA Daniel R.; RT "Genome sequence of Streptomyces sp. G25."; RL Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:OAH14690.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LOHS01000058; OAH14690.1; -; Genomic_DNA. DR RefSeq; WP_067274742.1; NZ_LOHS01000058.1. DR EnsemblBacteria; OAH14690; OAH14690; STSP_19510. DR PATRIC; fig|1716141.3.peg.2047; -. DR Proteomes; UP000077381; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000077381}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000077381}. FT DOMAIN 279 444 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 507 AA; 55231 MW; C76553CBEACC318D CRC64; MTSSSSPSQD EQRFAQNYPE GLRADALMEE DVAWSYEIDG DRDGDQFDRH DRAALRRVAG LSTELEDVTE VEYRQLRLER VVLVGVWTSG TVTDAENSLA ELAALAETAG AMVLDGVIQR RDKPDPATYI GSGKAQELRD IVLETGADTV VCDGELTPGQ LIHLEDVVKV KVVDRTALIL DIFAQHAKSR EGKAQVSLAQ MQYMLPRLRG WGQSLSRQMG GGGSGSSGGG MATRGPGETK IETDRRRIRE KMAKMRREIA DMKTGREIKR QERRRNKVPS VAIAGYTNAG KSSLLNRLTG AGVLVENALF ATLDPTVRRA ETPSGRLYTL ADTVGFVRHL PHHLVEAFRS TMEEVGDADL ILHVVDGAHP APEEQLAAVR EVIRDVGATD VPEIVVINKA DAADPLVLQR LLRIEKRSIA VSARTGQGID ELLALIDNDL PRPEVELEAL VPYSLGRLVS RAHAEGEVIS EEHTAEGTLL KARVHEELAA ELAPYVPALP GARSAGH // ID A0A177L8A4_9BACL Unreviewed; 417 AA. AC A0A177L8A4; DT 07-SEP-2016, integrated into UniProtKB/TrEMBL. DT 07-SEP-2016, sequence version 1. DT 07-JUN-2017, entry version 8. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=AWH49_11835 {ECO:0000313|EMBL:OAH61704.1}; OS [Bacillus] aminovorans. OC Bacteria; Firmicutes; Bacilli; Bacillales; Planococcaceae. OX NCBI_TaxID=29332 {ECO:0000313|EMBL:OAH61704.1, ECO:0000313|Proteomes:UP000076935}; RN [1] {ECO:0000313|EMBL:OAH61704.1, ECO:0000313|Proteomes:UP000076935} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 1314 {ECO:0000313|EMBL:OAH61704.1, RC ECO:0000313|Proteomes:UP000076935}; RA Verma A., Pal Y., Krishnamurthi S.; RT "Investigation of taxonomic status of Bacillus aminovorans."; RL Submitted (JAN-2016) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:OAH61704.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LQWY01000016; OAH61704.1; -; Genomic_DNA. DR RefSeq; WP_026221740.1; NZ_LQWY01000016.1. DR EnsemblBacteria; OAH61704; OAH61704; AWH49_11835. DR Proteomes; UP000076935; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000076935}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000076935}. FT DOMAIN 196 363 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 417 AA; 46695 MW; 32B96F796D3E619F CRC64; MDQLKGIVAG VNLDNGDDFA YSMEELKNLA EACGIDVRGE LTQNLPRIHS ALYMGTGKVE ELKSLAEYEE ADVVIFDGEL SPSQIRNLEK ELDCEVIDRT MLILDIFGRR AKTKEAQLQV EMARLQYMLP RLVGTYIALG RQGGGSGFKN RGAGETKLEL DRRKIETKIA YLRKELAKIS EQRTVQRKQR KKNNMPVAAL VGYTNAGKST VMNAMLQTYE GGGSEVFEKD MLFATLDTSV RSITLPDKKE FLLADTVGFV NKLPHHLVKA FRSTLEEAAA ADLLIHVIDV SSPQYQTMID ITEKTLVDIG AKDMPVIYAY NKADLAGIDY PGAAGNSVYL SAKERAGILE LTEVMKSHLF KDYVRCELLI PYDEGEVVSY FNEQATIFET AYEEEGTKLT IECHRSDYEK YKSFVVK // ID A0A177PFC1_9GAMM Unreviewed; 421 AA. AC A0A177PFC1; DT 07-SEP-2016, integrated into UniProtKB/TrEMBL. DT 07-SEP-2016, sequence version 1. DT 05-JUL-2017, entry version 11. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=A1356_05355 {ECO:0000313|EMBL:OAI28956.1}; OS Methylomonas koyamae. OC Bacteria; Proteobacteria; Gammaproteobacteria; Methylococcales; OC Methylococcaceae; Methylomonas. OX NCBI_TaxID=702114 {ECO:0000313|EMBL:OAI28956.1, ECO:0000313|Proteomes:UP000077734}; RN [1] {ECO:0000313|EMBL:OAI28956.1, ECO:0000313|Proteomes:UP000077734} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=R-49807 {ECO:0000313|EMBL:OAI28956.1, RC ECO:0000313|Proteomes:UP000077734}; RA Ploux O.; RL Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:OAI28956.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LUUL01000052; OAI28956.1; -; Genomic_DNA. DR RefSeq; WP_064022035.1; NZ_LUUL01000052.1. DR EnsemblBacteria; OAI28956; OAI28956; A1356_05355. DR Proteomes; UP000077734; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000077734}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}. FT DOMAIN 196 363 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 162 189 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 421 AA; 46581 MW; 9C51B7139D958E7C CRC64; MFERPDAGER AILVHLNLQV GQEDLDELKE LTKSAGAQPI HVVTGSRHRP DPKYFVGIGK LDEIKAAVVE HQADIIIVNH PLSPSQERNL ERALEVRVVD RNGLILDIFA QRAQTFEGKL QVELAQLKHL STRLIRGWTH LERQKGGIGL RGPGETQLET DRRLLAVRIK QIQQRLEKVE KQRHQSRSKR KKAEIPTVSL VGYTNAGKST LFNTLTGAGI YAADQLFATL DPTLRQLPLP DGGEIILADT VGFIRHLPHE LVAAFRSTLQ EAAEADLLLH VIDSAAEDRD DTIIQVNQVL EDIGAGKIAQ LKVFNKIDLL GDLEPHIDYD AEGRPVCVWI SAQSGAGCDL LQQALGELFA SSKVIRKCYL PAGQAGLKAK LFAFVRIISD VTDDHGDCEL TIEIDKKHLG LLKHIRVEAV A // ID A0A177PNR6_9RHIZ Unreviewed; 449 AA. AC A0A177PNR6; DT 07-SEP-2016, integrated into UniProtKB/TrEMBL. DT 07-SEP-2016, sequence version 1. DT 05-JUL-2017, entry version 9. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=A1351_05120 {ECO:0000313|EMBL:OAI31414.1}; OS Methylosinus sp. R-45379. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Methylocystaceae; Methylosinus. OX NCBI_TaxID=980563 {ECO:0000313|EMBL:OAI31414.1, ECO:0000313|Proteomes:UP000078138}; RN [1] {ECO:0000313|EMBL:OAI31414.1, ECO:0000313|Proteomes:UP000078138} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=R-45379 {ECO:0000313|EMBL:OAI31414.1, RC ECO:0000313|Proteomes:UP000078138}; RA Ploux O.; RL Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:OAI31414.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LUUM01000035; OAI31414.1; -; Genomic_DNA. DR EnsemblBacteria; OAI31414; OAI31414; A1351_05120. DR Proteomes; UP000078138; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000078138}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000078138}. FT DOMAIN 206 380 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 449 AA; 49427 MW; C7507ED90A093F46 CRC64; MSTKALVVGP YPTRARPSES SAGQGAERDP VSRLAEAVGL AEAIELDIVG EIAVSLHDVR PATYLGKGKV EEIAETVKAT EAELVTMDCQ LSPVQQRNLE KAWGAKVIDR TGLILEIFGR RARTKEGSLQ VELAHLAYQK SRLVRSWTHL ERQRGGFGFL GGPGETQIET DRRLIEERMA RIERDLDQVK RTRGLHRKKR REVPYPVVAL VGYTNAGKST LFNRLTKAGV LAEDMLFATL DPTLRQIRLP HGAKVLLSDT VGFISDLPTM LISAFRATLE EVTLADVILH VRDVSHPDWE AQAADVESIL GELGLSGEAG TRILEVWNKI DALDDDIVAA MKIAARGKKI VDRPSLVSAL TGEGLDALLG RIETRLAEGR IQLEVELDPA DGAGIAWLHA HTEVLDRQTL ADGRARLIVR VAPERFDGVT RRYPQAEVRA RASSKRRAR // ID A0A177YBG2_9NOCA Unreviewed; 509 AA. AC A0A177YBG2; DT 07-SEP-2016, integrated into UniProtKB/TrEMBL. DT 07-SEP-2016, sequence version 1. DT 07-JUN-2017, entry version 8. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=A3K89_08780 {ECO:0000313|EMBL:OAK52847.1}; OS Rhodococcus kyotonensis. OC Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae; OC Rhodococcus. OX NCBI_TaxID=398843 {ECO:0000313|EMBL:OAK52847.1, ECO:0000313|Proteomes:UP000077519}; RN [1] {ECO:0000313|EMBL:OAK52847.1, ECO:0000313|Proteomes:UP000077519} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=KB10 {ECO:0000313|EMBL:OAK52847.1, RC ECO:0000313|Proteomes:UP000077519}; RA Jeong H., Hong C.E., Jo S.H., Park J.M.; RT "Genome sequence of Rhodococcus kyotonensis KB10."; RL Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:OAK52847.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LVHI01000023; OAK52847.1; -; Genomic_DNA. DR EnsemblBacteria; OAK52847; OAK52847; A3K89_08780. DR Proteomes; UP000077519; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000077519}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000077519}. FT DOMAIN 282 451 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 241 275 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 509 AA; 55338 MW; 281838AF25C18C88 CRC64; MTETHHPENH VGPQADTDSA ERWTPQESEA WSRRIARSPL PLDEDTPSSG DMQLEERTAL RRVAGLSTEL ADVTEVEYRQ LRLERVVLVG VWTSGTAAQA ENSMAELAAL AETAGSEVLD ALMQRRDKPD PATYIGSGKA HELRDVVLST GADTVICDGE LTPAQLNALE KVVKVKVIDR TALILDIFAQ HATSREGKAQ VAFAQMEYML PRLRGWGESM SRQAGGRAGS NGGVGLRGPG ETKIETDRRR IRERMAKLRR EIKGMKQARD TKRERRVGST TPNIAIVGYT NAGKSSLLNK LTGSGVLVQN ALFATLDPTS RKSTLDDGRA IVLTDTVGFV RHLPTQLVEA FRSTLEEVTD ADLLLHVVDG SDPLPTDQIK AVREVIMDVV KEHDAPMPPE LIVVNKIDAA DPVQLTQLRG LLPGARFVSA RTGEGVAELR DHLGEILAWP EAEVDVLIPY TRGDLVARIH SEGRISESTH EAGGTHVAAR VPHALASVLS DFAYDAVTA // ID A0A180EL84_9BACT Unreviewed; 403 AA. AC A0A180EL84; DT 02-NOV-2016, integrated into UniProtKB/TrEMBL. DT 02-NOV-2016, sequence version 1. DT 07-JUN-2017, entry version 8. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=A3850_005495 {ECO:0000313|EMBL:OAV43980.1}; OS Lewinella sp. 4G2. OC Bacteria; Bacteroidetes; Saprospiria; Saprospirales; Lewinellaceae; OC Lewinella. OX NCBI_TaxID=1803372 {ECO:0000313|EMBL:OAV43980.1, ECO:0000313|Proteomes:UP000076582}; RN [1] {ECO:0000313|EMBL:OAV43980.1, ECO:0000313|Proteomes:UP000076582} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=4G2 {ECO:0000313|EMBL:OAV43980.1, RC ECO:0000313|Proteomes:UP000076582}; RA Wong S.-K., Yoshizawa S., Ogura Y., Tetsuya H., Nakajima Y., RA Hamasaki K.; RT "Lewinella sp. 4G2 Genome sequencing."; RL Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:OAV43980.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LVWJ02000014; OAV43980.1; -; Genomic_DNA. DR RefSeq; WP_068215238.1; NZ_LVWJ02000014.1. DR EnsemblBacteria; OAV43980; OAV43980; A3850_005495. DR Proteomes; UP000076582; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000076582}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000076582}. FT DOMAIN 210 392 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 403 AA; 46231 MW; BC6A7DC1ED52EFDD CRC64; MAQEWNVGQK KTGLKKKTEY AVIVGLITRR QTEEQVQEYL DELEFLALTA GAVTKARYTQ KLDSPDNKTF IGKGKVEEIK EYIDKHEEIT MVIFDDDLSG KQTGVLEERL KVKIIDRSSL ILDIFASRAQ TAQAKTQVEL AQMQYMLPRL RGLWTHLERQ RGGIGMRGPG ETEIETDRRI IRDKISKLKK DLEKIDRQAE TRRKGRDAMV RVALVGYTNV GKSTLMNLLT KSDVFAEDKL FATLDTTVRK VAYEGVPFLL TDTVGFIRKL PHNLVESFKS TLDEVRESDI LLHVVDVAHP AHGDQIRTVQ TLLDELGVKE KPTLLVFNKI DLFRERNFDM YLDDEGKEEV ENDLRKGLEA EFGNEAMLVS AHTRENVDAL RQRITEMVKG EYQATYPYIA KHW // ID A0A183DZN7_9BILA Unreviewed; 226 AA. AC A0A183DZN7; DT 07-SEP-2016, integrated into UniProtKB/TrEMBL. DT 07-SEP-2016, sequence version 1. DT 12-APR-2017, entry version 4. DE SubName: Full=Uncharacterized protein {ECO:0000313|WBParaSite:GPUH_0001419401-mRNA-1}; OS Gongylonema pulchrum. OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Spirurida; OC Spiruroidea; Gongylonematidae; Gongylonema. OX NCBI_TaxID=637853 {ECO:0000313|Proteomes:UP000050760, ECO:0000313|WBParaSite:GPUH_0001419401-mRNA-1}; RN [1] {ECO:0000313|Proteomes:UP000050760, ECO:0000313|WBParaSite:GPUH_0001419401-mRNA-1} RP NUCLEOTIDE SEQUENCE. RG Helminth Genomes Consortium; RL Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|WBParaSite:GPUH_0001419401-mRNA-1} RP IDENTIFICATION. RG WormBaseParasite; RL Submitted (JUN-2016) to UniProtKB. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR WBParaSite; GPUH_0001419401-mRNA-1; GPUH_0001419401-mRNA-1; GPUH_0001419401. DR Proteomes; UP000050760; Genome assembly. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR Pfam; PF13167; GTP-bdg_N; 1. DR SUPFAM; SSF52540; SSF52540; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000050760}; KW Reference proteome {ECO:0000313|Proteomes:UP000050760}. FT DOMAIN 22 111 GTP-bdg_N. {ECO:0000259|Pfam:PF13167}. SQ SEQUENCE 226 AA; 25826 MW; 6189018E36D182F9 CRC64; LLIYPRIRRG RFFDVNPAKA KQRLEEAVAL VNTLPKFTVI QTTAVSTDTS TAKKRLWGIG RIERVIALKE KIGATALMID VDILSPKQQA ELFALFRVPI YDRYNIVLLI FKLFAKTKEA RLQIQLAEIP YIRQQRLLSM YELHASPTAF HVDAPTKSKA VKLEVLRFRE QHLRKCIKAA VDEKAATRFG EAQKNIRTVV AVVGYTNAGK SSLIKRLHLG LHFQRY // ID A0A183FIE3_HELBK Unreviewed; 391 AA. AC A0A183FIE3; DT 07-SEP-2016, integrated into UniProtKB/TrEMBL. DT 07-SEP-2016, sequence version 1. DT 07-JUN-2017, entry version 7. DE SubName: Full=Uncharacterized protein {ECO:0000313|WBParaSite:HPBE_0000665601-mRNA-1}; OS Heligmosomoides polygyrus bakeri (Parasitic nematode) (Heligmosomoides OS bakeri). OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida; OC Strongylida; Trichostrongyloidea; Heligmosomatidae; Heligmosomoides. OX NCBI_TaxID=375939 {ECO:0000313|Proteomes:UP000050761, ECO:0000313|WBParaSite:HPBE_0000665601-mRNA-1}; RN [1] {ECO:0000313|Proteomes:UP000050761, ECO:0000313|WBParaSite:HPBE_0000665601-mRNA-1} RP NUCLEOTIDE SEQUENCE. RG Helminth Genomes Consortium; RL Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|WBParaSite:HPBE_0000665601-mRNA-1} RP IDENTIFICATION. RG WormBaseParasite; RL Submitted (JUN-2016) to UniProtKB. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR WBParaSite; HPBE_0000665601-mRNA-1; HPBE_0000665601-mRNA-1; HPBE_0000665601. DR Proteomes; UP000050761; Genome Assembly. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 2. DR SUPFAM; SSF52540; SSF52540; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000050761}; KW Reference proteome {ECO:0000313|Proteomes:UP000050761}. FT DOMAIN 191 348 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 391 AA; 44158 MW; AEBE075A143C77BD CRC64; MCLFVCTGVR WSVLGKIRWG SSSASSLKDP QRQLDEAVTL VNTLPGFRVA ESAVIGVDYN TKRRSVWGPG QIEKLVRMKQ QSRVTALMVN VDMLTPLQQH ELFSIFQVPI YDRYNIVLSI FKHYAKTPEA HLQIQLAEIP YIRNRLHYLN KYRSDPSALH TRLEIQRVWE ECYQLGALNT MLHVMTCCLS YTNAGKTSLV KCLTGASSLE PKDRLFATLD TTRHLARLPS GRKVVFTDTI GFLSDLPMHL LAAFQATLSH VKLADVIIHI RDISNPDWRA QSEDVEKTLE AIGLPTDRLK DVVVADNKID VDGAPPSSTP NAIRISCKSS EGVEGLIEEV DKVCLCFKYS YFVTAALQDP DRRGTEKLVL WMIMILIFAP TVNRSRTYTR C // ID A0A183H3N6_9BILA Unreviewed; 521 AA. AC A0A183H3N6; DT 07-SEP-2016, integrated into UniProtKB/TrEMBL. DT 07-SEP-2016, sequence version 1. DT 10-MAY-2017, entry version 5. DE SubName: Full=Uncharacterized protein {ECO:0000313|WBParaSite:OFLC_0000209501-mRNA-1}; OS Onchocerca flexuosa. OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Spirurida; OC Filarioidea; Onchocercidae; Onchocerca. OX NCBI_TaxID=387005 {ECO:0000313|Proteomes:UP000050787, ECO:0000313|WBParaSite:OFLC_0000209501-mRNA-1}; RN [1] {ECO:0000313|Proteomes:UP000050787, ECO:0000313|WBParaSite:OFLC_0000209501-mRNA-1} RP NUCLEOTIDE SEQUENCE. RG Helminth Genomes Consortium; RL Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|WBParaSite:OFLC_0000209501-mRNA-1} RP IDENTIFICATION. RG WormBaseParasite; RL Submitted (JUN-2016) to UniProtKB. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR WBParaSite; OFLC_0000209501-mRNA-1; OFLC_0000209501-mRNA-1; OFLC_0000209501. DR Proteomes; UP000050787; Genome assembly. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR CDD; cd01878; HflX; 1. DR InterPro; IPR008584; DUF866_euk. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF05907; DUF866; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000050787}; KW Reference proteome {ECO:0000313|Proteomes:UP000050787}. FT DOMAIN 161 324 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 521 AA; 59829 MW; B5094E126653B899 CRC64; LYRFRTTAIS TDCSTKKKRL WGKGRLERII ALYEKINATA LMIDVDILSP KQQTELTSMF RIPVYDRYNI VLLIFKMFAK TKEAKLQIEL AEIPYIRQRL LSMYELRANP STFHLDTSDK SKAERLEVLR YREQHLRKCL KAAVEEKVNL RIGEAQKNIR IVVAVVGYTN AGKSSLIKRL TGRDLYVEDR LFATLDTSLH VFRLPSGLSI LFADTIGFIS NLPTQLLASF QATLNHVANA DLLLHVEDVS NPDYLTQRDV VMKTLSLLKI RSELLNSIIR VGNKIDKLNQ LPPDEPNTYF VSCANGRGLV ELMAAVDKKV LTISGKTIRR LKLRPHSEAF SYLCKYSFLV GQPVPSEDNN YLLCNVIMDD NEFSKFRAHF SPIIALQFKA NMVNLKCTNC GEEPEHWQYE KFNMPGSRGT ANILEKCKLC SRVNSLEIVK DSFRSYKNND DYDELIRFDC RGLEPTDFDP KSGWRAIGTE SATVFENIDL TEKEWVDYDE EAAQPTEINE IQCRFVLCRK Q // ID A0A199NR99_9MICC Unreviewed; 527 AA. AC A0A199NR99; DT 05-OCT-2016, integrated into UniProtKB/TrEMBL. DT 05-OCT-2016, sequence version 1. DT 07-JUN-2017, entry version 8. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=AN277_0210055 {ECO:0000313|EMBL:OAX51221.1}; OS Kocuria kristinae. OC Bacteria; Actinobacteria; Micrococcales; Micrococcaceae; Kocuria. OX NCBI_TaxID=37923 {ECO:0000313|EMBL:OAX51221.1, ECO:0000313|Proteomes:UP000053171}; RN [1] {ECO:0000313|EMBL:OAX51221.1, ECO:0000313|Proteomes:UP000053171} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=RuSp02-3 {ECO:0000313|Proteomes:UP000053171}; RA Evans L.H., Alamgir A., Owens N., Weber N.D., Virtaneva K., RA Barbian K., Babar A., Rosenke K.; RL Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:OAX51221.1, ECO:0000313|Proteomes:UP000053171} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=RuSp02-3 {ECO:0000313|Proteomes:UP000053171}; RA Waterworth S.C., Walmsley T.A., Matongo T., Davies-Coleman M.T., RA Dorrington R.A.; RT "Identification of putative biosynthetic pathways for the production RT of bioactive secondary metabolites by the marine actinomycete Kocuria RT kristinae RUTW2-3."; RL Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:OAX51221.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; LJBJ02000030; OAX51221.1; -; Genomic_DNA. DR RefSeq; WP_061225230.1; NZ_LJBJ02000030.1. DR EnsemblBacteria; OAX51221; OAX51221; AN277_0210055. DR Proteomes; UP000053171; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 2. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000053171}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000053171}. FT DOMAIN 305 470 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 527 AA; 58371 MW; 9C72BB2C2914BA9B CRC64; MPQHHPRTAD DAAPEHTDER TEQPRQPSDA QLRATVDRVL GRFSPEEEHQ ASILDRRAPE LAETTQHTEH DGEQQDLEER RALRRVAGLS TELEDVTEVE YRQLRLERVV LAGIWSEGTL EDAENSLREL AALAETAGSD VLDGLVQRRL KPDPGTFLGS GKAQELKEIV AETGADTVVI DSELAPSQRR GLEDIVKVKV IDRTALILDI FAQHAKSREG KAQVELAQLE YLLPRLRGWG ESMSRQAGGR AAGGEGIGSR GPGETKIELD RRRIRQRMAK LRREIAAMKP ARETKRANRR RNHIPSVAIA GYTNAGKSSL LNRLTDAGVL VENALFATLD PTVRRAETPD GIGYTLSDTV GFVRNLPTQL VEAFRSTLEE VADADVILHV VDASHPDPEG QIRAVREVLA EVDAQDVPEI IVLNKADAAD PFVLDRIRLR EPHHAIVSAK TGEGIPELKE LISRTIPRPS VRMEILVPYT HGEVVSRLHE WDAEILSTAF EEDGTRMSVL VREETAPELQ PYAVTAP // ID A0A1A6C2M7_9GAMM Unreviewed; 428 AA. AC A0A1A6C2M7; DT 02-NOV-2016, integrated into UniProtKB/TrEMBL. DT 02-NOV-2016, sequence version 1. DT 07-JUN-2017, entry version 7. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=Thpro_023054 {ECO:0000313|EMBL:OBS08804.1}; OS Acidihalobacter prosperus. OC Bacteria; Proteobacteria; Gammaproteobacteria; Chromatiales; OC Ectothiorhodospiraceae; Acidihalobacter. OX NCBI_TaxID=160660 {ECO:0000313|EMBL:OBS08804.1, ECO:0000313|Proteomes:UP000029273}; RN [1] {ECO:0000313|EMBL:OBS08804.1, ECO:0000313|Proteomes:UP000029273} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 5130 {ECO:0000313|EMBL:OBS08804.1, RC ECO:0000313|Proteomes:UP000029273}; RX PubMed=25342676; RA Ossandon F.J., Cardenas J.P., Corbett M., Quatrini R., Holmes D.S., RA Watkin E.; RT "Draft Genome Sequence of the Iron-Oxidizing, Acidophilic, and RT Halotolerant 'Thiobacillus prosperus' Type Strain DSM 5130."; RL Genome Announc. 2:0-0(2014). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:OBS08804.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JQSG02000006; OBS08804.1; -; Genomic_DNA. DR EnsemblBacteria; OBS08804; OBS08804; Thpro_023054. DR Proteomes; UP000029273; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000029273}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000029273}. FT DOMAIN 198 364 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 428 AA; 47598 MW; 18488C303B24F8F9 CRC64; MFERPRSGET AILVQVDIAG LAEPGERDEF IELARSAGAT IARVIDVRRH SPDPKYFIGT GKADEIAEAV IAEGAELVIF SRVLSPSQER NLEAKFKARV LDRTGLILDI FAQRARSHEG KLQVELAQLN HLSTRLVRGW THLERQKGGI GLRGPGETQL ETDRRLLGDR IKQILRRLDK VRRQRQQGRQ ARMKAELPSV ALVGYTNAGK STLFNRLSQA GVYAADQLFA TLDPTLRRLE LDAANAVVLA DTVGFVRELP HELVAAFHAT LQETREADLL LHVIDASNPE HDRTETDVDQ VLAEVGASEV PMLRIFNKID CIEAAPRIDR DAEGRPVRAW VSAQTGAGID ELLTALKEYF MPDVVHGWVH LPASAGRLRA RLFGLGAVLD ERVDDCGGSE LEVRLPRRRY DAWLSETADP EALRLRPL // ID A0A1B1KK82_SERPL Unreviewed; 426 AA. AC A0A1B1KK82; DT 02-NOV-2016, integrated into UniProtKB/TrEMBL. DT 02-NOV-2016, sequence version 1. DT 30-AUG-2017, entry version 8. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:ANS40842.1}; GN ORFNames=Q5A_001715 {ECO:0000313|EMBL:ANS40842.1}; OS Serratia plymuthica PRI-2C. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; OC Yersiniaceae; Serratia. OX NCBI_TaxID=1154756 {ECO:0000313|EMBL:ANS40842.1, ECO:0000313|Proteomes:UP000013567}; RN [1] {ECO:0000313|EMBL:ANS40842.1, ECO:0000313|Proteomes:UP000013567} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Serratia sp. PRI-2C {ECO:0000313|Proteomes:UP000013567}; RX PubMed=22815440; DOI=10.1128/JB.00679-12; RA Garbeva P., van Elsas J.D., de Boer W.; RT "Draft genome sequence of the antagonistic rhizosphere bacterium RT Serratia plymuthica strain PRI-2C."; RL J. Bacteriol. 194:4119-4120(2012). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP015613; ANS40842.1; -; Genomic_DNA. DR RefSeq; WP_006317445.1; NZ_CP015613.1. DR EnsemblBacteria; ANS40842; ANS40842; Q5A_001715. DR KEGG; sply:Q5A_001715; -. DR KO; K03665; -. DR Proteomes; UP000013567; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000013567}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}. FT DOMAIN 198 365 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 426 AA; 48051 MW; 5C9BEF35DCA523E5 CRC64; MFDRYEAGEQ AVLVHIYFSQ DKDTEDLSEF ESLVSSAGVE ALQVVTGSRK APHPKYFVGE GKAEEIADAV KASGASVVLF DHSLSPAQER NLERLCECRV IDRTGLILDI FAQRARTHEG KLQVELAQLR HIATRLVRGW THLERQKGGI GLRGPGETQL ETDRRLLRDR ISLILRRLER VAKQREQGRR ARTRAEVPTV SLVGYTNAGK STLFNRITSA DVYAADQLFA TLDPTLRRID VADVGDTVLA DTVGFIRHLP HDLVAAFKAT LQETRQASLL LHVIDAADTR VDENIEAVNT VLAEIESDEI PTLLVMNKID MLDDFVPRID RNDENLPIRV WLSAASGEGI PLLYQALTER LSGEIAQYEL RLPPQAGRLR SRFYQLQAIE KEWNEEDGSI GMVIRMPIVE WRRLCKQEQD LINFIV // ID A0A1B6PT12_SORBI Unreviewed; 620 AA. AC A0A1B6PT12; DT 02-NOV-2016, integrated into UniProtKB/TrEMBL. DT 02-NOV-2016, sequence version 1. DT 30-AUG-2017, entry version 5. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:KXG28812.1}; GN ORFNames=SORBI_005G169800 {ECO:0000313|EMBL:KXG28812.1}; OS Sorghum bicolor (Sorghum) (Sorghum vulgare). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACMAD clade; Panicoideae; Andropogonodae; Andropogoneae; Sorghinae; OC Sorghum. OX NCBI_TaxID=4558 {ECO:0000313|EMBL:KXG28812.1, ECO:0000313|Proteomes:UP000000768}; RN [1] {ECO:0000313|EMBL:KXG28812.1, ECO:0000313|Proteomes:UP000000768} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. BTx623 {ECO:0000313|Proteomes:UP000000768}; RX PubMed=19189423; DOI=10.1038/nature07723; RA Paterson A.H., Bowers J.E., Bruggmann R., Dubchak I., Grimwood J., RA Gundlach H., Haberer G., Hellsten U., Mitros T., Poliakov A., RA Schmutz J., Spannagl M., Tang H., Wang X., Wicker T., Bharti A.K., RA Chapman J., Feltus F.A., Gowik U., Grigoriev I.V., Lyons E., RA Maher C.A., Martis M., Narechania A., Otillar R.P., Penning B.W., RA Salamov A.A., Wang Y., Zhang L., Carpita N.C., Freeling M., RA Gingle A.R., Hash C.T., Keller B., Klein P., Kresovich S., RA McCann M.C., Ming R., Peterson D.G., Mehboob-ur-Rahman, Ware D., RA Westhoff P., Mayer K.F., Messing J., Rokhsar D.S.; RT "The Sorghum bicolor genome and the diversification of grasses."; RL Nature 457:551-556(2009). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CM000764; KXG28812.1; -; Genomic_DNA. DR EnsemblPlants; KXG28812; KXG28812; SORBI_005G169800. DR Gramene; KXG28812; KXG28812; SORBI_005G169800. DR Proteomes; UP000000768; Chromosome 5. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000000768}; KW Reference proteome {ECO:0000313|Proteomes:UP000000768}. FT DOMAIN 396 561 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 620 AA; 68342 MW; B30D58A45028DCB5 CRC64; MHGKMFMPRH AAPSGLRLRV KYTGPTASTE GTSPRHHRLP RLSTRPLALT TQKPPLHSLS ARRAMSAAAC LFAAATASLS LPSTSAPTSS GRRSVRSPTA LLRCSLTRRR GQPVRVRALD ERLLEAAPAE TEEAQTGVDV GDGGGVAEGD GVGAEEELEL EQQRPSPRAF MESRRQRQEE EEAAAGQDRF RLINGKEIFQ EKAYLVGVEC KRTGGNLFGI VESLKELEQL ADTAGLVVVG STYQKLSTPN PRTYIGSGKV SEIRSAIQAL DVETVIFDDE LSPGQLRNLE KSFGGSVRVC DRTALILDIF NQRAATHEAA LQVTLAQMEY QLPRLTKMWS HLERQAGGQV KGMGEKQIEV DKRILRTQIG ALRKELESVR KHRKLYRNRR QSVPIPVVSL VGYTNAGKST LLNRLTGADV LAEDKLFATL DPTTRRVLMK NGTEFLLTDT VGFIQKLPTM LVAAFRATLE EISESSVIVH LVDISHPLAQ QQIDAVERVL KELDVESIPK LIVWNKIDNT DEPLRVKEEA QKQGIICISA MNGDGLEEFC NAVQAKLKDS MVPIEAIVPY DKGDLLNDIH KVGMVEKMEY KENGTFVKAH VPLPLARLLT PLRQQVVATV // ID A0A1B6PT39_SORBI Unreviewed; 500 AA. AC A0A1B6PT39; DT 02-NOV-2016, integrated into UniProtKB/TrEMBL. DT 02-NOV-2016, sequence version 1. DT 30-AUG-2017, entry version 6. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:KXG28811.1}; GN ORFNames=SORBI_005G169800 {ECO:0000313|EMBL:KXG28811.1}; OS Sorghum bicolor (Sorghum) (Sorghum vulgare). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACMAD clade; Panicoideae; Andropogonodae; Andropogoneae; Sorghinae; OC Sorghum. OX NCBI_TaxID=4558 {ECO:0000313|EMBL:KXG28811.1, ECO:0000313|Proteomes:UP000000768}; RN [1] {ECO:0000313|EMBL:KXG28811.1, ECO:0000313|Proteomes:UP000000768} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. BTx623 {ECO:0000313|Proteomes:UP000000768}; RX PubMed=19189423; DOI=10.1038/nature07723; RA Paterson A.H., Bowers J.E., Bruggmann R., Dubchak I., Grimwood J., RA Gundlach H., Haberer G., Hellsten U., Mitros T., Poliakov A., RA Schmutz J., Spannagl M., Tang H., Wang X., Wicker T., Bharti A.K., RA Chapman J., Feltus F.A., Gowik U., Grigoriev I.V., Lyons E., RA Maher C.A., Martis M., Narechania A., Otillar R.P., Penning B.W., RA Salamov A.A., Wang Y., Zhang L., Carpita N.C., Freeling M., RA Gingle A.R., Hash C.T., Keller B., Klein P., Kresovich S., RA McCann M.C., Ming R., Peterson D.G., Mehboob-ur-Rahman, Ware D., RA Westhoff P., Mayer K.F., Messing J., Rokhsar D.S.; RT "The Sorghum bicolor genome and the diversification of grasses."; RL Nature 457:551-556(2009). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CM000764; KXG28811.1; -; Genomic_DNA. DR EnsemblPlants; KXG28811; KXG28811; SORBI_005G169800. DR Gramene; KXG28811; KXG28811; SORBI_005G169800. DR Proteomes; UP000000768; Chromosome 5. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR CDD; cd01878; HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000768}; KW Reference proteome {ECO:0000313|Proteomes:UP000000768}. FT DOMAIN 396 459 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 500 AA; 55250 MW; 8F649E719F252A71 CRC64; MHGKMFMPRH AAPSGLRLRV KYTGPTASTE GTSPRHHRLP RLSTRPLALT TQKPPLHSLS ARRAMSAAAC LFAAATASLS LPSTSAPTSS GRRSVRSPTA LLRCSLTRRR GQPVRVRALD ERLLEAAPAE TEEAQTGVDV GDGGGVAEGD GVGAEEELEL EQQRPSPRAF MESRRQRQEE EEAAAGQDRF RLINGKEIFQ EKAYLVGVEC KRTGGNLFGI VESLKELEQL ADTAGLVVVG STYQKLSTPN PRTYIGSGKV SEIRSAIQAL DVETVIFDDE LSPGQLRNLE KSFGGSVRVC DRTALILDIF NQRAATHEAA LQVTLAQMEY QLPRLTKMWS HLERQAGGQV KGMGEKQIEV DKRILRTQIG ALRKELESVR KHRKLYRNRR QSVPIPVVSL VGYTNAGKST LLNRLTGADV LAEDKLFATL DPTTRRVLMK NGTEFLLTDT VGFIQKLPTM LVHIHKAYSS CLHVMLLDNK TSNIESFSYL YDVNFAYIVY // ID A0A1B6QIB0_SORBI Unreviewed; 600 AA. AC A0A1B6QIB0; DT 02-NOV-2016, integrated into UniProtKB/TrEMBL. DT 02-NOV-2016, sequence version 1. DT 30-AUG-2017, entry version 6. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:KXG37655.1}; GN ORFNames=SORBI_001G105700 {ECO:0000313|EMBL:KXG37655.1}; OS Sorghum bicolor (Sorghum) (Sorghum vulgare). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACMAD clade; Panicoideae; Andropogonodae; Andropogoneae; Sorghinae; OC Sorghum. OX NCBI_TaxID=4558 {ECO:0000313|EMBL:KXG37655.1, ECO:0000313|Proteomes:UP000000768}; RN [1] {ECO:0000313|EMBL:KXG37655.1, ECO:0000313|Proteomes:UP000000768} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. BTx623 {ECO:0000313|Proteomes:UP000000768}; RX PubMed=19189423; DOI=10.1038/nature07723; RA Paterson A.H., Bowers J.E., Bruggmann R., Dubchak I., Grimwood J., RA Gundlach H., Haberer G., Hellsten U., Mitros T., Poliakov A., RA Schmutz J., Spannagl M., Tang H., Wang X., Wicker T., Bharti A.K., RA Chapman J., Feltus F.A., Gowik U., Grigoriev I.V., Lyons E., RA Maher C.A., Martis M., Narechania A., Otillar R.P., Penning B.W., RA Salamov A.A., Wang Y., Zhang L., Carpita N.C., Freeling M., RA Gingle A.R., Hash C.T., Keller B., Klein P., Kresovich S., RA McCann M.C., Ming R., Peterson D.G., Mehboob-ur-Rahman, Ware D., RA Westhoff P., Mayer K.F., Messing J., Rokhsar D.S.; RT "The Sorghum bicolor genome and the diversification of grasses."; RL Nature 457:551-556(2009). RN [2] {ECO:0000313|EMBL:KXG37655.1} RP NUCLEOTIDE SEQUENCE. RA Paterson A.H., Bowers J.E., Bruggmann R., Dubchak I., Grimwood J., RA Gundlach H., Haberer G., Hellsten U., Mitros T., Poliakov A., RA Schmutz J., Spannagl M., Tang H., Wang X., Wicker T., Bharti A.K., RA Chapman J., Feltus F.A., Gowik U., Grigoriev I.V., Lyons E., RA Maher C.A., Martis M., Narechania A., Otillar R.P., Penning B.W., RA Salamov A.A., Wang Y., Zhang L., Carpita N.C., Freeling M., RA Gingle A.R., Hash C.T., Keller B., Klein P., Kresovich S., RA Mccann M.C., Ming R., Peterson D.G., Rahman M., Ware D., Westhoff P., RA Mayer K.F., Messing J., Sims D., Jenkins J., Shu S., Rokhsar D.S.; RT "WGS assembly of Sorghum bicolor."; RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CM000760; KXG37655.1; -; Genomic_DNA. DR EMBL; CM000760; KXG37656.1; -; Genomic_DNA. DR EnsemblPlants; KXG37655; KXG37655; SORBI_001G105700. DR EnsemblPlants; KXG37656; KXG37656; SORBI_001G105700. DR Gramene; KXG37655; KXG37655; SORBI_001G105700. DR Gramene; KXG37656; KXG37656; SORBI_001G105700. DR Proteomes; UP000000768; Chromosome 1. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR CDD; cd01878; HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000768}; KW Reference proteome {ECO:0000313|Proteomes:UP000000768}. FT DOMAIN 301 573 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 600 AA; 65803 MW; 060BAF44D658D0ED CRC64; MLRGAISRLG ARLRLHADPS PVSPYLRALS TRRGKRSSPT VSPADSDDEG PLRGLFVLSR DPECPPRLLV VQPRLRPGSL LDSKLAEALN LANSLEEPRD GFYHSEFGAK GAPPHLVVQN PASRGRSHAD TYFGPGTVDN VKCYLRASES EEDVDAVFVN AILSGIQQRN LEVAWGKPVL DRVGLIIEIF NAHAETKEAK LQSELAALMY MKTRLVRVRG PGGRLTFGPS GEAEVVSARG RGSGGRGFMS GAGETELQLQ RRRIQERRVS LLAQIEDVRR TRAIQRSSRK RHGGSFGHEL VTVAVVGYTN AGKSTLVSAL SEADLYSDDR LFATVDPRLR SVILPSGRKA LLSDTVGFIS DLPVQLVEAF HATLEEVVEA DMLVHVLDSS ASDLEEHRST VLQVLQQIGV SQEKINNMIE VWNKIDLVDE NVTSDGIEDE IFLTEGEEED DIFSEDDIPS EQSSFDSVDD GADSEYLSEE NSEDSNDEVP CKESFAEPTE MEAMKVLSSK ECFGAMEAVK ASKECFGELR VPYTNGRTLP QPTSNCHVKT SAVTGTGLQE LLALIDRKLT EQQTVVQRSD GPFDRKWRPS SMDGENAAEQ // ID A0BMK2_PARTE Unreviewed; 608 AA. AC A0BMK2; DT 28-NOV-2006, integrated into UniProtKB/TrEMBL. DT 28-NOV-2006, sequence version 1. DT 07-JUN-2017, entry version 51. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:CAK59769.1}; GN ORFNames=GSPATT00030405001 {ECO:0000313|EMBL:CAK59769.1}; OS Paramecium tetraurelia. OC Eukaryota; Alveolata; Ciliophora; Intramacronucleata; OC Oligohymenophorea; Peniculida; Parameciidae; Paramecium. OX NCBI_TaxID=5888 {ECO:0000313|EMBL:CAK59769.1, ECO:0000313|Proteomes:UP000000600}; RN [1] {ECO:0000313|EMBL:CAK59769.1, ECO:0000313|Proteomes:UP000000600} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Stock d4-2 {ECO:0000313|EMBL:CAK59769.1, RC ECO:0000313|Proteomes:UP000000600}; RX PubMed=17086204; DOI=10.1038/nature05230; RG Genoscope; RA Aury J.-M., Jaillon O., Duret L., Noel B., Jubin C., Porcel B.M., RA Segurens B., Daubin V., Anthouard V., Aiach N., Arnaiz O., Billaut A., RA Beisson J., Blanc I., Bouhouche K., Camara F., Duharcourt S., RA Guigo R., Gogendeau D., Katinka M., Keller A.-M., Kissmehl R., RA Klotz C., Koll F., Le Mouel A., Lepere G., Malinsky S., Nowacki M., RA Nowak J.K., Plattner H., Poulain J., Ruiz F., Serrano V., Zagulski M., RA Dessen P., Betermier M., Weissenbach J., Scarpelli C., Schaechter V., RA Sperling L., Meyer E., Cohen J., Wincker P.; RT "Global trends of whole-genome duplications revealed by the ciliate RT Paramecium tetraurelia."; RL Nature 444:171-178(2006). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CT868004; CAK59769.1; -; Genomic_DNA. DR RefSeq; XP_001427167.1; XM_001427130.1. DR ProteinModelPortal; A0BMK2; -. DR STRING; 412030.XP_001427167.1; -. DR EnsemblProtists; CAK59769; CAK59769; GSPATT00030405001. DR GeneID; 5012951; -. DR KEGG; ptm:GSPATT00030405001; -. DR eggNOG; KOG0410; Eukaryota. DR eggNOG; COG2262; LUCA. DR InParanoid; A0BMK2; -. DR OMA; IIVLHPI; -. DR Proteomes; UP000000600; Partially assembled WGS sequence. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR CDD; cd01878; HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000600}; KW Reference proteome {ECO:0000313|Proteomes:UP000000600}. FT DOMAIN 354 525 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 608 AA; 70371 MW; 77BD8BAA042C64F1 CRC64; MLIKKLSNII AKYRFSKETL DFAKSTPPKQ QLASQPVNCM VLHPVFYPNK GPELELYMAE EAIGLSKSLN WTLEQGPLWK QEYTQDIRRS QGKIDEDEEN QGDQSKEQNK VQDFQMNEDD LGHEWRNKII RNSIAKSSLV KIPRIHSTTF FTKGKLAMLG QHIQSKKINA VFINHELTPL QTRNLEKLWT QYSRGEITSA IKEDINENNE STENIPDEID SDSEFEGLSV KVFDRFTMIL QIFAKRSTQG VSRLQIELSF LRFAKTKLVR SGSAFVSLSS IFKGDLMMAK EVYVEVVSAK QRRALGKMSG SGESELQLQR RLIDDRIAKV KKLIEEECQQ RSKIKRKKLI HTVPRIALIG YTNAGKSQLL NCILQKDVVQ SKDLLFQTLD TTSKSIRLAS GQKAIMLDTI GFITDLPHDL VESFKCTLEE VEDADIVLHI RDISHPCTEQ QKQVVLDVLK ELGFNQDFYN KKMIEVWNKI DLMSYPIDYE FIESQDYPIV PVSALMNINI KKLLQVMEEK SNQILNKKLY RIRYNIEQHF ERLRWLYDNG NISGVKNEMQ IPPIKKGDPT IMEYDVILDE VTYNRYIATF QPEMRVKKNK GMPPSNWK // ID A0BWU6_PARTE Unreviewed; 604 AA. AC A0BWU6; DT 28-NOV-2006, integrated into UniProtKB/TrEMBL. DT 28-NOV-2006, sequence version 1. DT 07-JUN-2017, entry version 49. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:CAK63013.1}; GN ORFNames=GSPATT00032865001 {ECO:0000313|EMBL:CAK63013.1}; OS Paramecium tetraurelia. OC Eukaryota; Alveolata; Ciliophora; Intramacronucleata; OC Oligohymenophorea; Peniculida; Parameciidae; Paramecium. OX NCBI_TaxID=5888 {ECO:0000313|EMBL:CAK63013.1, ECO:0000313|Proteomes:UP000000600}; RN [1] {ECO:0000313|EMBL:CAK63013.1, ECO:0000313|Proteomes:UP000000600} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Stock d4-2 {ECO:0000313|EMBL:CAK63013.1, RC ECO:0000313|Proteomes:UP000000600}; RX PubMed=17086204; DOI=10.1038/nature05230; RG Genoscope; RA Aury J.-M., Jaillon O., Duret L., Noel B., Jubin C., Porcel B.M., RA Segurens B., Daubin V., Anthouard V., Aiach N., Arnaiz O., Billaut A., RA Beisson J., Blanc I., Bouhouche K., Camara F., Duharcourt S., RA Guigo R., Gogendeau D., Katinka M., Keller A.-M., Kissmehl R., RA Klotz C., Koll F., Le Mouel A., Lepere G., Malinsky S., Nowacki M., RA Nowak J.K., Plattner H., Poulain J., Ruiz F., Serrano V., Zagulski M., RA Dessen P., Betermier M., Weissenbach J., Scarpelli C., Schaechter V., RA Sperling L., Meyer E., Cohen J., Wincker P.; RT "Global trends of whole-genome duplications revealed by the ciliate RT Paramecium tetraurelia."; RL Nature 444:171-178(2006). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CT868023; CAK63013.1; -; Genomic_DNA. DR RefSeq; XP_001430411.1; XM_001430374.1. DR ProteinModelPortal; A0BWU6; -. DR STRING; 412030.XP_001430411.1; -. DR EnsemblProtists; CAK63013; CAK63013; GSPATT00032865001. DR GeneID; 5016177; -. DR KEGG; ptm:GSPATT00032865001; -. DR eggNOG; KOG0410; Eukaryota. DR eggNOG; COG2262; LUCA. DR InParanoid; A0BWU6; -. DR OMA; WANDEYA; -. DR Proteomes; UP000000600; Partially assembled WGS sequence. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR SUPFAM; SSF52540; SSF52540; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000600}; KW Reference proteome {ECO:0000313|Proteomes:UP000000600}. FT DOMAIN 131 239 GTP-bdg_N. {ECO:0000259|Pfam:PF13167}. FT DOMAIN 351 472 G (guanine nucleotide-binding). FT {ECO:0000259|Pfam:PF01926}. SQ SEQUENCE 604 AA; 69916 MW; 2492B9D770ED11BB CRC64; MLIKRLSNAI AKYRFCKEIL DFAKPNPIKQ QLTQHPLNYM VVHPIGSQNK GPELEFYMAE EAIGFSKQLN WTLVKGSFEW NNQTKIKDMN TSQEKIHQDQ QDNQSQKQRE QQEFQEDDLG QEWGNYITGN SIVKSSLVKL PSIHSTTFFT KAKLSMLGQH IQSKGVNAVF INHELTSLQT RNLKKVWTQY SRGEIASAFT EDVIDNDENN KNAEEQAKSD SEGLSVQVYD RFTMLLLLFA KRSTQGISKL QVELTFLKFA KAKLETGDSS LQTLASIFKE QLMVAKEIDF EILSAKQKKN QGKNNEYREN ELLLQRRIID DKIEKVKQLI EEDNQSRLKI KRKIHAHTIP KIALIGFTNA GKAQLLNCIL QKDETESKDQ ISQILSTNQK SVRLASGQKA IILNTIGFIT DLPQDFIEVF KSTLGEVEDA DIVLHIRDIS HPHSEKQKQV VYGVLKDLGF NQDFFNQKMI EVWNKIDLMK HSLDYDQIES YDYPIVPTSA LMNINIQKLL QVMEEKSNYI MNKKLYRLKY NIDQHFERLR WLYDVGNISG VKNEVQKLPI KRGDPTIIEY DVIIDEVTYN RYIATFQPEI RIKKDQGISP KGWK // ID A0C1Z4_PARTE Unreviewed; 634 AA. AC A0C1Z4; DT 28-NOV-2006, integrated into UniProtKB/TrEMBL. DT 28-NOV-2006, sequence version 1. DT 07-JUN-2017, entry version 43. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:CAK64811.1}; GN ORFNames=GSPATT00034288001 {ECO:0000313|EMBL:CAK64811.1}; OS Paramecium tetraurelia. OC Eukaryota; Alveolata; Ciliophora; Intramacronucleata; OC Oligohymenophorea; Peniculida; Parameciidae; Paramecium. OX NCBI_TaxID=5888 {ECO:0000313|EMBL:CAK64811.1, ECO:0000313|Proteomes:UP000000600}; RN [1] {ECO:0000313|EMBL:CAK64811.1, ECO:0000313|Proteomes:UP000000600} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Stock d4-2 {ECO:0000313|EMBL:CAK64811.1, RC ECO:0000313|Proteomes:UP000000600}; RX PubMed=17086204; DOI=10.1038/nature05230; RG Genoscope; RA Aury J.-M., Jaillon O., Duret L., Noel B., Jubin C., Porcel B.M., RA Segurens B., Daubin V., Anthouard V., Aiach N., Arnaiz O., Billaut A., RA Beisson J., Blanc I., Bouhouche K., Camara F., Duharcourt S., RA Guigo R., Gogendeau D., Katinka M., Keller A.-M., Kissmehl R., RA Klotz C., Koll F., Le Mouel A., Lepere G., Malinsky S., Nowacki M., RA Nowak J.K., Plattner H., Poulain J., Ruiz F., Serrano V., Zagulski M., RA Dessen P., Betermier M., Weissenbach J., Scarpelli C., Schaechter V., RA Sperling L., Meyer E., Cohen J., Wincker P.; RT "Global trends of whole-genome duplications revealed by the ciliate RT Paramecium tetraurelia."; RL Nature 444:171-178(2006). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CT868034; CAK64811.1; -; Genomic_DNA. DR RefSeq; XP_001432208.1; XM_001432171.1. DR ProteinModelPortal; A0C1Z4; -. DR STRING; 412030.XP_001432208.1; -. DR EnsemblProtists; CAK64811; CAK64811; GSPATT00034288001. DR GeneID; 5017993; -. DR KEGG; ptm:GSPATT00034288001; -. DR eggNOG; KOG0410; Eukaryota. DR eggNOG; COG2262; LUCA. DR InParanoid; A0C1Z4; -. DR OMA; NKMIEVW; -. DR Proteomes; UP000000600; Partially assembled WGS sequence. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR CDD; cd01878; HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000600}; KW Reference proteome {ECO:0000313|Proteomes:UP000000600}. FT DOMAIN 381 552 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 634 AA; 73203 MW; 4C6F5FAD54DA089B CRC64; MLIRRLSNAL LKYRFSKEAA EPQQVQRVKA PFGFTQVNCL VIHPIFYPNK GPELELYLAE EAVGLSKSLN WTLEKGPFWK EEYSQKIRIS QGRNPLQVKV ENNEDELKEE GWELSSKAHL RNGEYIYLPF LNGTYDDGQM LVDLSSESDD DLGHEWKNKI IRNSIAKSSL VKVKRIHSST FFTKGKVAML GEHIYDKKIN AVFINHELTP LQTRNLEKVW TQYAKGEIAT FRRSENPDDS DMATDAETDI EYEDAYVKVF DRFTMILQIF AKRSTQGVAR QQIELSFLKF AKTKLVRSGS AFASLSSIFL GDLMMAKEVY LEVVSAKQRR ALGKMSGSGE SEIQIQRRQI DERIAKVRRQ IEEEGLQRGK LKQKKLIHTV PRIALIGYTN AGKSQLLNCI LQKEVVESKD LLFQTLSTTS KQIRLASGQK AIMLDTIGFI TDLPHDLVES FKCTLEEVAD ADIVLHIRDI SHPCSEQQKQ VVLEVLQQLG FNEEFYSKKM IEVWNKIDLM RTPIDFKQIQ QETYPIVPIS ALFNTNVKQL LQIMEDKSNL IMNKRPYKLR YNIDEHQQRL KWLFDNGNIS GIKNEIHITP VKKGNPTEIE YEVILDEITY NRYIATFTPE LRIKKNKGMP PPNW // ID A0JUZ0_ARTS2 Unreviewed; 522 AA. AC A0JUZ0; DT 12-DEC-2006, integrated into UniProtKB/TrEMBL. DT 12-DEC-2006, sequence version 1. DT 07-JUN-2017, entry version 81. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Arth_1466 {ECO:0000313|EMBL:ABK02860.1}; OS Arthrobacter sp. (strain FB24). OC Bacteria; Actinobacteria; Micrococcales; Micrococcaceae; Arthrobacter. OX NCBI_TaxID=290399 {ECO:0000313|EMBL:ABK02860.1, ECO:0000313|Proteomes:UP000000754}; RN [1] {ECO:0000313|EMBL:ABK02860.1, ECO:0000313|Proteomes:UP000000754} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=FB24 {ECO:0000313|EMBL:ABK02860.1, RC ECO:0000313|Proteomes:UP000000754}; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., RA Pitluck S., Chertkov O., Thompson S., Brettin T., Bruce D., Han C., RA Tapia R., Gilna P., Schmutz J., Larimer F., Land M., Hauser L., RA Kyrpides N., Mikhailova N., Beasley F., Chen W., Jerke K., RA Nakatsu C.H., Richardson P.; RT "Complete sequence of chromosome 1 of Arthrobacter sp. FB24."; RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000454; ABK02860.1; -; Genomic_DNA. DR RefSeq; WP_011691327.1; NC_008541.1. DR ProteinModelPortal; A0JUZ0; -. DR STRING; 290399.Arth_1466; -. DR EnsemblBacteria; ABK02860; ABK02860; Arth_1466. DR KEGG; art:Arth_1466; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000000754; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 2. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000000754}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000000754}. FT DOMAIN 301 466 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 522 AA; 56721 MW; D4127B50E1CB6149 CRC64; MTNQPNTGSD SASQDMSPEE IQAVIDRILS KDVPARAAGS APENPRGVLG SAQAISRQDS EHSIFDGDQQ DLEERRALRR TAGLSTELED VTEVEYRQLR LERVVLAGLW TEGTLADAEN SLRELAALAE TAGSEVLDGI VQRRAKPDPG TFLGSGKAQE LKDIVMSTGA DTVVVDAELA PSQRRGLEDI VKVKVIDRTA LILDIFAQHA KSREGKAQVE LAQLEYLLPR LRGWGESMSR QAGGQVGGAG AGMGSRGPGE TKIELDRRRI RTRMAKLRRE IAAMKPARET KRANRRRNSV PSVAIAGYTN AGKSSLLNRL TDAGVLVENA LFATLDPTVR KAETADGLGY TLADTVGFVR SLPTQLVEAF RSTLEEVADS DLILHVVDVS HPDPEGQIAA VRAVFSEVDA RKVPEIIVLN KADAADPFVV ERLKQREPRH VVVSARTGQG IAELLKAISE SIPRPSVKME LLIPYNRGDL ISKLHETDAE ILRLDHEEEG TRALVMVREG LAAELESFIS NV // ID A0KGS2_AERHH Unreviewed; 428 AA. AC A0KGS2; DT 12-DEC-2006, integrated into UniProtKB/TrEMBL. DT 12-DEC-2006, sequence version 1. DT 30-AUG-2017, entry version 74. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=AHA_0925 {ECO:0000313|EMBL:ABK37175.1}; OS Aeromonas hydrophila subsp. hydrophila (strain ATCC 7966 / DSM 30187 / OS JCM 1027 / KCTC 2358 / NCIMB 9240). OC Bacteria; Proteobacteria; Gammaproteobacteria; Aeromonadales; OC Aeromonadaceae; Aeromonas. OX NCBI_TaxID=380703 {ECO:0000313|EMBL:ABK37175.1, ECO:0000313|Proteomes:UP000000756}; RN [1] {ECO:0000313|EMBL:ABK37175.1, ECO:0000313|Proteomes:UP000000756} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 7966 / DSM 30187 / JCM 1027 / KCTC 2358 / NCIMB 9240 RC {ECO:0000313|Proteomes:UP000000756}; RX PubMed=16980456; DOI=10.1128/JB.00621-06; RA Seshadri R., Joseph S.W., Chopra A.K., Sha J., Shaw J., Graf J., RA Haft D., Wu M., Ren Q., Rosovitz M.J., Madupu R., Tallon L., Kim M., RA Jin S., Vuong H., Stine O.C., Ali A., Horneman A.J., Heidelberg J.F.; RT "Genome sequence of Aeromonas hydrophila ATCC 7966T: jack of all RT trades."; RL J. Bacteriol. 188:8272-8282(2006). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000462; ABK37175.1; -; Genomic_DNA. DR RefSeq; WP_011704865.1; NC_008570.1. DR RefSeq; YP_855468.1; NC_008570.1. DR ProteinModelPortal; A0KGS2; -. DR STRING; 380703.AHA_0925; -. DR EnsemblBacteria; ABK37175; ABK37175; AHA_0925. DR GeneID; 4488411; -. DR KEGG; aha:AHA_0925; -. DR PATRIC; fig|380703.7.peg.925; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR Proteomes; UP000000756; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000000756}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000000756}. FT DOMAIN 198 365 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 428 AA; 48060 MW; 4DF40C357F2C6433 CRC64; MFDRYEAGEQ AVLVHVNFSD EGEREDLEEL KMLVSSAGVN ALGVITTSRS APSAKFFVGS GKAEEIASQV QMLDADVVIF NHALTPAQER NLERLFQCRV VDRTGLILDI FAQRARTHEG KLQVELAQLR HLSTRLVRGW THLERQKGGI GLRGPGETQL ETDRRLLRER IKAILRRLDK VAKQREQGRR ARNRNEVPTV SLVGYTNAGK STLFNQLTAA SVYAADQLFA TLDPTLRKLV IQDVGDVILA DTVGFIRHLP HDLVAAFKAT LQETREADLL LHVVDCADEQ MQENIESVQQ VLAEIEADDR PQLMICNKID KLGEHPVGLE RDEEGRPVRV WLSAQTGEGC ADLFTALTEL LAGSMVHHTL QLPPSAARLR SALYRLKGIE QEGFSEEGDF VLEVRLQLAD WNRLMKQEGE SLQRFIRH // ID A0LN54_SYNFM Unreviewed; 532 AA. AC A0LN54; DT 12-DEC-2006, integrated into UniProtKB/TrEMBL. DT 12-DEC-2006, sequence version 1. DT 07-JUN-2017, entry version 77. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Sfum_3183 {ECO:0000313|EMBL:ABK18856.1}; OS Syntrophobacter fumaroxidans (strain DSM 10017 / MPOB). OC Bacteria; Proteobacteria; Deltaproteobacteria; Syntrophobacterales; OC Syntrophobacteraceae; Syntrophobacter. OX NCBI_TaxID=335543 {ECO:0000313|EMBL:ABK18856.1, ECO:0000313|Proteomes:UP000001784}; RN [1] {ECO:0000313|EMBL:ABK18856.1, ECO:0000313|Proteomes:UP000001784} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 10017 / MPOB {ECO:0000313|Proteomes:UP000001784}; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Hammon N., Israni S., Pitluck S., Goltsman E.G., RA Martinez M., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., RA Kim E., Boone D.R., Brockman F., Culley D., Ferry J., Gunsalus R., RA McInerney M.J., Morrison M., Plugge C., Rohlin L., Scholten J., RA Sieber J., Stams A.J.M., Worm P., Henstra A.M., Richardson P.; RT "Complete sequence of Syntrophobacter fumaroxidans MPOB."; RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000478; ABK18856.1; -; Genomic_DNA. DR ProteinModelPortal; A0LN54; -. DR STRING; 335543.Sfum_3183; -. DR EnsemblBacteria; ABK18856; ABK18856; Sfum_3183. DR KEGG; sfu:Sfum_3183; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; EREVIIT; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000001784; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000001784}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000001784}. FT DOMAIN 342 506 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 532 AA; 59775 MW; 3165A3B7442871A7 CRC64; MARDLARLSF ECGRRLGLLI GRDGTVEMVL VGGPRSLFIP DLPKSRGGRW RLRGLRLVHT HLQAEGLSQD DLMDLVFLRL DCVAGIRVDP NGGATLLDVA HILPGAGHDR GWEVLPPLWC YDPDLDFQEL VKSLEDELDR NRLAIPATTR QDRAILVSVT EKDRETARRS MEELVELART SGIVVADTIV QRLRSVNPKY LIGKGKLSEI VLRALQCGVD LLIFDRELNP SQVRSLTDTT ELRVIDRTQL ILDIFAQRAQ SREGKIQVET AQLKYLLPRL GVKDDALSRL TGGIGARGPG ETTLEINRRR IKDRIAHLDD QLRGVRRNRD QRRARRLRKD IPTVSIVGYT NAGKSTLLNT LTHSGVFVED KLFATLDPTS RRLRFPRDFE VIVTDTVGFI RDLPQDLLDA FAATLEELDD ADLLLHVVDI SNPHFEEQME AVDRILGKLE LQAKPTVLVF NKIDRVDPEW ARRKVRRHGG VAISALSTGT VDPLIAAMQD QVEALMEEGF YAAARQPEPE IAEEPDESAW EL // ID A0LUZ4_ACIC1 Unreviewed; 524 AA. AC A0LUZ4; DT 12-DEC-2006, integrated into UniProtKB/TrEMBL. DT 12-DEC-2006, sequence version 1. DT 07-JUN-2017, entry version 80. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Acel_1482 {ECO:0000313|EMBL:ABK53254.1}; OS Acidothermus cellulolyticus (strain ATCC 43068 / 11B). OC Bacteria; Actinobacteria; Acidothermales; Acidothermaceae; OC Acidothermus. OX NCBI_TaxID=351607 {ECO:0000313|EMBL:ABK53254.1, ECO:0000313|Proteomes:UP000008221}; RN [1] {ECO:0000313|EMBL:ABK53254.1, ECO:0000313|Proteomes:UP000008221} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43068 / 11B {ECO:0000313|Proteomes:UP000008221}; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., RA Pitluck S., Zharchuk I., Schmutz J., Larimer F., Land M., Hauser L., RA Kyrpides N., Mikhailova N., Berry A.M., Adney W.S., Normand P., RA Leu D., Pujic P., Richardson P.; RT "Complete sequence of Acidothermus cellulolyticus 11B."; RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Proteomes:UP000008221} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43068 / 11B {ECO:0000313|Proteomes:UP000008221}; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., RA Pitluck S., Zharchuk I., Schmutz J., Larimer F., Land M., Hauser L., RA Kyrpides N., Mikhailova N., Berry A.M., Adney W.S., Normand P., RA Leu D., Pujic P., Richardson P.; RT "Complete sequence of Acidothermus cellulolyticus 11B."; RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000481; ABK53254.1; -; Genomic_DNA. DR RefSeq; WP_011720317.1; NC_008578.1. DR ProteinModelPortal; A0LUZ4; -. DR STRING; 351607.Acel_1482; -. DR EnsemblBacteria; ABK53254; ABK53254; Acel_1482. DR KEGG; ace:Acel_1482; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000008221; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000008221}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Hydrolase {ECO:0000313|EMBL:ABK53254.1}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000008221}. FT DOMAIN 299 468 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 265 292 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 524 AA; 56766 MW; 55576BCB1425CE01 CRC64; MKKSAFDSDV TESVQIAGAA DMTDTPAPDL SARDPQPSAR GVRDMRPSTL SARDAQPSGL SAADDENLDV ADRHALRRVP GLSTELRDVT EVEYRRLRLE RVVLVGVWTH GTMRDAENSL VELKLLAETA GSQVLAGLLQ RRDKPDPATY IGAGKARELR DIVVTSGADT VICDGELSPS QLRNLEQLVK VKVVDRTALI LDIFAQHARS REGKAQVELA QMTYLLPRLR GWGESLSRQA GGRAGAGGVG IGGRGPGETK IELDRRRIRA RMTKLRRELA ELATTRDVKR RKRRVNDIPA VAIAGYTNAG KSSLLNRLTG AGVLVEDALF ATLDPTVRRA TTSDGRIYTL TDTVGFVRHL PHQLVEAFRS TLEEVTDADL VLHVVDGAHA DPFGQIDAVR AVFDEIGASH IPELVAVNKT DIADPAVVAT VLRAEERKGN RAVAVSVRTG AGLDDLRRAI EEMLPRPAVH VDVLVPYDEG RWVARIYELG DVDAVEHTPA GTRVRARVPA ALAAELAHLG SPSR // ID A0M622_GRAFK Unreviewed; 407 AA. AC A0M622; DT 12-DEC-2006, integrated into UniProtKB/TrEMBL. DT 12-DEC-2006, sequence version 1. DT 07-JUN-2017, entry version 79. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=GFO_3123 {ECO:0000313|EMBL:CAL68067.1}; OS Gramella forsetii (strain KT0803). OC Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales; OC Flavobacteriaceae; Gramella. OX NCBI_TaxID=411154 {ECO:0000313|EMBL:CAL68067.1, ECO:0000313|Proteomes:UP000000755}; RN [1] {ECO:0000313|EMBL:CAL68067.1, ECO:0000313|Proteomes:UP000000755} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=KT0803 {ECO:0000313|EMBL:CAL68067.1, RC ECO:0000313|Proteomes:UP000000755}; RX PubMed=17107561; DOI=10.1111/j.1462-2920.2006.01152.x; RA Bauer M., Kube M., Teeling H., Richter M., Lombardot T., Allers E., RA Wuerdemann C.A., Quast C., Kuhl H., Knaust F., Woebken D., Bischof K., RA Mussmann M., Choudhuri J.V., Meyer F., Reinhardt R., Amann R.I., RA Gloeckner F.O.; RT "Whole genome analysis of the marine Bacteroidetes'Gramella forsetii' RT reveals adaptations to degradation of polymeric organic matter."; RL Environ. Microbiol. 8:2201-2213(2006). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CU207366; CAL68067.1; -; Genomic_DNA. DR RefSeq; WP_011710968.1; NC_008571.1. DR ProteinModelPortal; A0M622; -. DR STRING; 411154.GFO_3123; -. DR EnsemblBacteria; CAL68067; CAL68067; GFO_3123. DR KEGG; gfo:GFO_3123; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000000755; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000000755}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000000755}. FT DOMAIN 200 385 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 407 AA; 47195 MW; F2FC03C0A183473B CRC64; MIEKTDLSYE RTVLIGIVTR EQDEEKLEEY LDELEFLTYT AGGEVIKRFS QRLDKPDPKT FIGSGKMNDV KEFAAENDIG AVIFDDELSP AQQKNIEKLL KCKILDRTGL ILDIFAQRAK TSYARTQVEL AQYEYLLPRL AGMWTHLERQ RGGIGMRGPG ETEIETDRRI VRDKISLLKN KLKVIDKQME VQRGNRGQLV RVALVGYTNV GKSTLMNVIS KSDVFAENKL FATLDTTVRK VVIRNLPFLL SDTVGFIRKL PTQLVESFKS TLDEVREADL LLHVVDISHP NFEDHIDSVN KILTEIETLD KPTIMVFNKI DSYEAEKIDE DDLITERTSA HYSLKDWKKT WMNRMGDNVL FISALNKENM EEFRKKVYEA VREIHITRFP YNNFLYPEYD KYGEEKE // ID A0P765_9PROT Unreviewed; 373 AA. AC A0P765; DT 03-OCT-2012, integrated into UniProtKB/TrEMBL. DT 03-OCT-2012, sequence version 1. DT 30-AUG-2017, entry version 33. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=MB2181_04840 {ECO:0000313|EMBL:EAV47375.1}; OS Methylophilales bacterium HTCC2181. OC Bacteria; Proteobacteria; Betaproteobacteria; Nitrosomonadales; OC OM43 clade. OX NCBI_TaxID=383631 {ECO:0000313|EMBL:EAV47375.1, ECO:0000313|Proteomes:UP000054262}; RN [1] {ECO:0000313|EMBL:EAV47375.1, ECO:0000313|Proteomes:UP000054262} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=HTCC2181 {ECO:0000313|EMBL:EAV47375.1, RC ECO:0000313|Proteomes:UP000054262}; RA Giovannoni S., Vergin K., Ferriera S., Johnson J., Kravitz S., RA Beeson K., Sutton G., Rogers Y.-H., Friedman R., Frazier M., RA Venter J.C.; RL Submitted (NOV-2006) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EAV47375.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AAUX01000001; EAV47375.1; -; Genomic_DNA. DR RefSeq; WP_008107449.1; NZ_AAUX01000001.1. DR STRING; 383631.MB2181_04840; -. DR EnsemblBacteria; EAV47375; EAV47375; MB2181_04840. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000054262; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000054262}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000054262}. FT DOMAIN 199 365 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 165 192 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 373 AA; 42140 MW; FED649FC1C9393CB CRC64; MFDRPEVGEK AILVNINFNN INHEEDTTEL TQLVLSAGFE VADIIESNKS QPDAKYFIGS GKAQELVTLK EVTEASTIVF NHELTPSQER NIEKLTGLRV YDRTALILYI FSQRAKSYEG KLQVELAHLA HLASRLTKGW SHLERQKGGI GVRGGPGEKQ IELDRRMIGI RIKQLKEKLK KLDKQRGMQR RARRRSNVLT VSIVGYTNAG KSTLFNTLTH EKILAEDKLF ATLDTTSRKL FLEPNHKLVI SDTVGFIKNL PTTLVEAFKS TLEEATDSDL LIHVVDVSNN NKSEQIVEVD KILKEIKAND LPQILVLNQI DKIPLKAMFD RDEYGTISRI QLSAKTGNGI EFLKQALVEY DVNLTNERKG QYA // ID A0PZT4_CLONN Unreviewed; 594 AA. AC A0PZT4; DT 09-JAN-2007, integrated into UniProtKB/TrEMBL. DT 09-JAN-2007, sequence version 1. DT 05-JUL-2017, entry version 81. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=NT01CX_1813 {ECO:0000313|EMBL:ABK61903.1}; OS Clostridium novyi (strain NT). OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=386415 {ECO:0000313|EMBL:ABK61903.1, ECO:0000313|Proteomes:UP000008220}; RN [1] {ECO:0000313|EMBL:ABK61903.1, ECO:0000313|Proteomes:UP000008220} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NT {ECO:0000313|EMBL:ABK61903.1, RC ECO:0000313|Proteomes:UP000008220}; RX PubMed=17115055; DOI=10.1038/nbt1256; RA Bettegowda C., Huang X., Lin J., Cheong I., Kohli M., Szabo S.A., RA Zhang X., Diaz L.A. Jr., Velculescu V.E., Parmigiani G., Kinzler K.W., RA Vogelstein B., Zhou S.; RT "The genome and transcriptomes of the anti-tumor agent Clostridium RT novyi-NT."; RL Nat. Biotechnol. 24:1573-1580(2006). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000382; ABK61903.1; -; Genomic_DNA. DR ProteinModelPortal; A0PZT4; -. DR STRING; 386415.NT01CX_1813; -. DR EnsemblBacteria; ABK61903; ABK61903; NT01CX_1813. DR KEGG; cno:NT01CX_1813; -. DR PATRIC; fig|386415.7.peg.916; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000008220; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000008220}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000008220}. FT DOMAIN 364 541 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 330 357 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 594 AA; 66156 MW; F1DFFB9D43E95FC9 CRC64; MIVGNLEGIR KTILKKLESI YDFKVDRQSI ANEQIIQIIS EITGDINKEI SVAIDRKGNI LSVAVGDSST VEMPIIDIKS KKLSGVRIIH THPNGNSRLS SLDVSALIAL KLDCMVAVAV EDGKCKDVTV GFCGIDNNTL IAEVAPNLPL DKALNINILN VVKNIEINLS SNEVEEDKGE RAVLVGIENE ESLDELCELA KACNVVTVDR VMQRRVKIDT AYFIGEGKVE ELSMVRQASN ANLIIFDDEL SASQIRNLES ATGTKVIDRT TLILEIFARR AKSKEAKIQV ELAQLKYRLP RLIGMGAVLS RTGAGIGTRG PGEKKLEIDK RHIRERIYDL NKELAKIKKN RQVQREKRSK DNVPKISLVG YTNAGKSTLR NKLCEIASPK DVVDKETVFE ADMLFATLDV TTRALVLPDN RLVTLTDTVG FIRKLPHDLV EAFKSTLEEV VNSDLLLHVV DSSSKDAYKQ IEAVNFVLEE LESINKPMIL LLNKIDKADK EQLEGLKEKF NNLKVLEISA KDNLNLDTLL NDICTALPNP LKKVEFLIPY SDSASVAMLH RNGKVLEEEY KDNGTRIIAM VDDKIYNKCE KYVI // ID A0QVY1_MYCS2 Unreviewed; 470 AA. AC A0QVY1; DT 09-JAN-2007, integrated into UniProtKB/TrEMBL. DT 09-JAN-2007, sequence version 1. DT 07-JUN-2017, entry version 89. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=MSMEG_2736 {ECO:0000313|EMBL:ABK75983.1}; OS Mycobacterium smegmatis (strain ATCC 700084 / mc(2)155). OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae; OC Mycobacterium. OX NCBI_TaxID=246196 {ECO:0000313|EMBL:ABK75983.1, ECO:0000313|Proteomes:UP000000757}; RN [1] {ECO:0000313|EMBL:ABK75983.1, ECO:0000313|Proteomes:UP000000757} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700084 / mc(2)155 {ECO:0000313|Proteomes:UP000000757}; RA Fleischmann R.D., Dodson R.J., Haft D.H., Merkel J.S., Nelson W.C., RA Fraser C.M.; RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000480; ABK75983.1; -; Genomic_DNA. DR RefSeq; WP_003894120.1; NZ_CP009494.1. DR RefSeq; YP_887069.1; NC_008596.1. DR STRING; 246196.MSMEG_2736; -. DR EnsemblBacteria; ABK75983; ABK75983; MSMEG_2736. DR EnsemblBacteria; AFP39137; AFP39137; MSMEI_2669. DR GeneID; 4531279; -. DR KEGG; msb:LJ00_13605; -. DR KEGG; msg:MSMEI_2669; -. DR KEGG; msm:MSMEG_2736; -. DR PATRIC; fig|246196.19.peg.2704; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000000757; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000000757}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000000757}. SQ SEQUENCE 470 AA; 50572 MW; 527DBCA7B9ADED0E CRC64; MTYPENSVAP STGELALEDR ASLRRVAGLS TELADVSEVE YRQLRLERVV LVGVWTEGSA ADAEASLAEL AALAETAGSE VLEGLIQRRD KPDPSTYIGS GKAAELREVV LATGADTVIC DGELSPAQLN ALEKAVKVKV IDRTALILDI FAQHATSREG KAQVSLAQME YMLPRLRGWG ESMSRQAGGR AGGAGGGVGT RGPGETKIET DRRRIRERMA KLRREIRDMK KIRDTQRGSR RRSEIPSVAI VGYTNAGKSS LLNALTGAGV LVENALFATL EPTTRRGEFE DGRPFVLTDT VGFVRHLPTQ LVEAFRSTLE EVVDADLLIH VVDGSDVNPL AQINAVRTVI NEVVAEYDIA PPPELLVVNK IDAATGVGLA QLRRALPDAV FVSARTGDGL DKLRSRMGEL VESTDATVDV TIPYDRGDLV ARVHTDGHVD ATEHTDAGTR IKARVPAPLA ATLREYATFA // ID A0RYD2_CENSY Unreviewed; 360 AA. AC A0RYD2; DT 09-JAN-2007, integrated into UniProtKB/TrEMBL. DT 09-JAN-2007, sequence version 1. DT 07-JUN-2017, entry version 66. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=CENSYa_1738 {ECO:0000313|EMBL:ABK78349.1}; OS Cenarchaeum symbiosum (strain A). OC Archaea; Thaumarchaeota; Cenarchaeales; Cenarchaeaceae; Cenarchaeum. OX NCBI_TaxID=414004 {ECO:0000313|EMBL:ABK78349.1, ECO:0000313|Proteomes:UP000000758}; RN [1] {ECO:0000313|EMBL:ABK78349.1, ECO:0000313|Proteomes:UP000000758} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=A {ECO:0000313|Proteomes:UP000000758}; RX PubMed=17114289; DOI=10.1073/pnas.0608549103; RA Hallam S.J., Konstantinidis K.T., Putnam N., Schleper C., Watanabe Y., RA Sugahara J., Preston C., de la Torre J., Richardson P.M., DeLong E.F.; RT "Genomic analysis of the uncultivated marine crenarchaeote Cenarchaeum RT symbiosum."; RL Proc. Natl. Acad. Sci. U.S.A. 103:18296-18301(2006). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; DP000238; ABK78349.1; -; Genomic_DNA. DR ProteinModelPortal; A0RYD2; -. DR EnsemblBacteria; ABK78349; ABK78349; CENSYa_1738. DR KEGG; csy:CENSYa_1738; -. DR PATRIC; fig|414004.10.peg.1585; -. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; FNNHAHV; -. DR Proteomes; UP000000758; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000000758}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000000758}. FT DOMAIN 184 355 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 360 AA; 39868 MW; 53D6592D867B0EA3 CRC64; MKKAILISYD REDAVAEAVD LCGAAGYNPE LIIRQKYLNR PKYGISGGAV ESLEEDAKRI DPDVIVFDEM LRPSQNYNLA SRLHRNVLDR EALILEIFEL RATGHESRLQ VKLAQMRYEM SRAREKVRLA KMGEQPGFMG IGKFEVDVYY NDIKHRMTSV RSKLAKAGRQ RELHRQARRR VGFGTISLAG YTSAGKTTLF NRLTGEAREE DVRPFTTLST MTRRVGDGPG ALLISDTVGF ISKLPAYMIE AFKSTLEEML HTDVILLVVD ISDTPEDLEK KFRSCTRTLS ELGVPPDKVI TALNKSDLVD AAEIRKKTEL LGLDGGGNWA VVSATTGQNL EGLMGLARGF ISSRGGPGAA // ID A0Y803_9GAMM Unreviewed; 433 AA. AC A0Y803; DT 23-JAN-2007, integrated into UniProtKB/TrEMBL. DT 23-JAN-2007, sequence version 1. DT 07-JUN-2017, entry version 54. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=GP2143_13416 {ECO:0000313|EMBL:EAW32257.1}; OS marine gamma proteobacterium HTCC2143. OC Bacteria; Proteobacteria; Gammaproteobacteria; Cellvibrionales; OC Spongiibacteraceae; BD1-7 clade. OX NCBI_TaxID=247633 {ECO:0000313|EMBL:EAW32257.1, ECO:0000313|Proteomes:UP000004931}; RN [1] {ECO:0000313|EMBL:EAW32257.1, ECO:0000313|Proteomes:UP000004931} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=HTCC2143 {ECO:0000313|EMBL:EAW32257.1, RC ECO:0000313|Proteomes:UP000004931}; RX PubMed=20601481; DOI=10.1128/JB.00683-10; RA Oh H.M., Kang I., Ferriera S., Giovannoni S.J., Cho J.C.; RT "Genome sequence of the oligotrophic marine Gammaproteobacterium RT HTCC2143, isolated from the Oregon Coast."; RL J. Bacteriol. 192:4530-4531(2010). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EAW32257.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AAVT01000001; EAW32257.1; -; Genomic_DNA. DR RefSeq; WP_007223631.1; NZ_AAVT01000001.1. DR ProteinModelPortal; A0Y803; -. DR STRING; 247633.GP2143_13416; -. DR EnsemblBacteria; EAW32257; EAW32257; GP2143_13416. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000004931; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000004931}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000004931}. FT DOMAIN 199 365 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 433 AA; 48766 MW; 0AF97BBAF9BC324E CRC64; MLFERPDSGE RAVLVHMDFH HEIEREDPRE FEELVLSAGG DPVAFIGGQR SSPSPRFFVG SGKVEEIRTQ VEQQKAEVVL FNHALSPSQE RNLESELKCR VLDRTGLILD IFAQRARTHE GKLQVELAQL QHMSTRLVRG WTHLERQKGG IGLRGPGETQ LESDRRLLRA RIKAISKRLD KVRKQRDQGR RARSRADIPT VSLVGYTNAG KSTLFNTLTQ ANVYVADQLF ATLDPTLRRV SIPDFGPIVL ADTVGFIRHL PHKLVEAFRA TLEEAAQSDL LIHVIDCADE EREDNIAQVE VVLNEIGADA IPRLEIYNKI DLVDSKPRID RDKDGIARRV WVSAQNGSGL DLIEQCLAEW LGEDIIHGRL TLDVGQGRLR AAFYQQNVVV SERYTEQGLS DIEIRLPKQD FCRLLSAEEL DPQTVLAEMG AVS // ID A0YGX6_9GAMM Unreviewed; 443 AA. AC A0YGX6; DT 23-JAN-2007, integrated into UniProtKB/TrEMBL. DT 23-JAN-2007, sequence version 1. DT 07-JUN-2017, entry version 54. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=GP2143_06864 {ECO:0000313|EMBL:EAW29994.1}; OS marine gamma proteobacterium HTCC2143. OC Bacteria; Proteobacteria; Gammaproteobacteria; Cellvibrionales; OC Spongiibacteraceae; BD1-7 clade. OX NCBI_TaxID=247633 {ECO:0000313|EMBL:EAW29994.1, ECO:0000313|Proteomes:UP000004931}; RN [1] {ECO:0000313|EMBL:EAW29994.1, ECO:0000313|Proteomes:UP000004931} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=HTCC2143 {ECO:0000313|EMBL:EAW29994.1, RC ECO:0000313|Proteomes:UP000004931}; RX PubMed=20601481; DOI=10.1128/JB.00683-10; RA Oh H.M., Kang I., Ferriera S., Giovannoni S.J., Cho J.C.; RT "Genome sequence of the oligotrophic marine Gammaproteobacterium RT HTCC2143, isolated from the Oregon Coast."; RL J. Bacteriol. 192:4530-4531(2010). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EAW29994.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AAVT01000012; EAW29994.1; -; Genomic_DNA. DR RefSeq; WP_007226753.1; NZ_AAVT01000012.1. DR ProteinModelPortal; A0YGX6; -. DR STRING; 247633.GP2143_06864; -. DR EnsemblBacteria; EAW29994; EAW29994; GP2143_06864. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000004931; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000004931}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000004931}. FT DOMAIN 217 387 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 182 209 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 443 AA; 48546 MW; FE0BEF26ECF5DA39 CRC64; MLNPENPGVQ RALIVAVQLD NVSDVEFESS LAELGDLAKT LGLEVVGQFT QKRSSFDSTA YMGVGKREEI RQFINGEQSG FGRLEDVSQV ELILVDHEIS PSQALNLENE LDCEVMDRTV VILEIFHRNA RSHAAQVQVE IARLSYMAPR LREAAKRAGP SGRQRSGSGG RGTGQSRSQM DSRKVRDRIA ELQKEIDTME AGRDTQRSRR QGQSGLGQVA LVGYTNAGKS TLMRALTGSE VLVANQLFAT LDTKVRTLHP ESVPRVLVTD TVGFIKNLPH GLVASFKSTL DEALSASLLL HVVDAGDPGF EMQLEVTDKV LAEIGADSVP RIRIFNKIDY LDGAVAQAER KAILQAKYPD CIVLSARNSD DIALLHQAIV EVFQRELVDA EIFLPWSAQG LRGEIFAAGE VLEERADTAG AFFRFRAPAD VVARLRDLAD KVI // ID A0YJQ8_LYNSP Unreviewed; 557 AA. AC A0YJQ8; DT 23-JAN-2007, integrated into UniProtKB/TrEMBL. DT 23-JAN-2007, sequence version 1. DT 07-JUN-2017, entry version 54. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=L8106_15030 {ECO:0000313|EMBL:EAW38739.1}; OS Lyngbya sp. (strain PCC 8106) (Lyngbya aestuarii (strain CCY9616)). OC Bacteria; Cyanobacteria; Oscillatoriophycideae; Oscillatoriales; OC Oscillatoriaceae; Lyngbya. OX NCBI_TaxID=313612 {ECO:0000313|EMBL:EAW38739.1, ECO:0000313|Proteomes:UP000000737}; RN [1] {ECO:0000313|EMBL:EAW38739.1, ECO:0000313|Proteomes:UP000000737} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=PCC8106 {ECO:0000313|Proteomes:UP000000737}; RA Stal L., Ferriera S., Johnson J., Kravitz S., Halpern A., RA Remington K., Beeson K., Tran B., Rogers Y.-H., Friedman R., RA Venter J.C.; RL Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EAW38739.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AAVU01000003; EAW38739.1; -; Genomic_DNA. DR ProteinModelPortal; A0YJQ8; -. DR STRING; 313612.L8106_15030; -. DR EnsemblBacteria; EAW38739; EAW38739; L8106_15030. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR OMA; EREVIIT; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000000737; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000000737}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000000737}. FT DOMAIN 384 557 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 343 377 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 557 AA; 61122 MW; BC37AB3E0C00D52D CRC64; MQRLYHQRIP GDSITTPEFA QRLAASSTEI GQPVCAYLNR RGQVIRVGVG TPRQTQIPPL ELPRYGEGRL SGIRCIATQV KPEPPNESAL TAMAIQRLDA LVILTLTGSG FQRRGGGGTG YIKETYLAHL VPPTAEENNG NLTTPLAPIP YYLSPPQSLD MLSAQDFLDL VDNLEAELQR EFIAQTVESD GDQVLLVGMK TEGISPQRFE DGLAELVRLV DTAGGRVLET VRQKRSRPHP QTVVGDGKVQ EIALTAQTVG ATLIVFDRDL SPAQVRNLET RIGIRVVDRT EVILDIFAQR AQSRAGKLQV ELAQLEYNLP RLTGRGQAMS RLGGGIGTRG PGETKLETER RAIQRRIARL QTEVNQLQAH RSRLRQRRQQ QEVPTIAIVG YTNAGKSTLL NVLTSSEIYA ADQLFATLDP TSRRLTIPDA ITNEPQTAVL TDTVGFIHEL PPALIDAFRA TLEEVSDADA LVHVVDLSHP AWQGQIESVM KILMSMPITP GPALLAFNKI DQVEGETLRF AQEEYPQAAF ISASNALGLE TLRQRIGQLV HYVSTLS // ID A0Z0Q7_9GAMM Unreviewed; 405 AA. AC A0Z0Q7; DT 23-JAN-2007, integrated into UniProtKB/TrEMBL. DT 23-JAN-2007, sequence version 1. DT 30-AUG-2017, entry version 52. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=MGP2080_05792 {ECO:0000313|EMBL:EAW42229.1}; OS marine gamma proteobacterium HTCC2080. OC Bacteria; Proteobacteria; Gammaproteobacteria; Cellvibrionales; OC Halieaceae. OX NCBI_TaxID=247639 {ECO:0000313|EMBL:EAW42229.1, ECO:0000313|Proteomes:UP000004719}; RN [1] {ECO:0000313|EMBL:EAW42229.1, ECO:0000313|Proteomes:UP000004719} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=HTCC2080 {ECO:0000313|EMBL:EAW42229.1, RC ECO:0000313|Proteomes:UP000004719}; RX PubMed=20472793; DOI=10.1128/JB.00511-10; RA Thrash J.C., Cho J.C., Ferriera S., Johnson J., Vergin K.L., RA Giovannoni S.J.; RT "Genome sequences of strains HTCC2148 and HTCC2080, belonging to the RT OM60/NOR5 clade of the Gammaproteobacteria."; RL J. Bacteriol. 192:3842-3843(2010). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EAW42229.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AAVV01000001; EAW42229.1; -; Genomic_DNA. DR RefSeq; WP_007233404.1; NZ_AAVV01000001.1. DR ProteinModelPortal; A0Z0Q7; -. DR STRING; 247639.MGP2080_05792; -. DR EnsemblBacteria; EAW42229; EAW42229; MGP2080_05792. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000004719; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000004719}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000004719}. FT DOMAIN 186 352 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 405 AA; 44970 MW; 49D786E65818C2DD CRC64; MVQLAIDDGA QALDAQEFEE LVVSAGGKPV ALVTGHRRSP TAKFFVGTGK LEEIRIIKEA ENADLVVFNH PLSPSQERNL EAALECRVIA RTGLILDIFA QRARTHEGKL QVELAQLQHM STRLVRGWTH LERQKGGIGL RGPGETQLET DRRLLRVRIS AIETRLGKVK AQRAQSRRAR KRAELPLVSI VGYTNAGKST LFNRYASADV YAADQLFATL DPTLRRVEIP HLGDVVLADT VGFISDLPHT LIDAFKATLE ETLNADLLIH VIDVSADQRE YWMSEVDLVL SEIGAGDVPM LCVFNKLDLL EQQPRIVRNE EGLPTAVYLS ARTGEGLPLL EEALRERLQD EVFEGEVELT PSQGKLRAAL FDLGAVLDES FTASGNTLLG VRLPQKIWNR LQHQY // ID A0ZI19_NODSP Unreviewed; 521 AA. AC A0ZI19; DT 23-JAN-2007, integrated into UniProtKB/TrEMBL. DT 23-JAN-2007, sequence version 1. DT 07-JUN-2017, entry version 53. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=NSP_14370 {ECO:0000313|EMBL:AHJ27772.1}; OS Nodularia spumigena CCY9414. OC Bacteria; Cyanobacteria; Nostocales; Aphanizomenonaceae; Nodularia. OX NCBI_TaxID=313624 {ECO:0000313|EMBL:AHJ27772.1, ECO:0000313|Proteomes:UP000019325}; RN [1] {ECO:0000313|EMBL:AHJ27772.1, ECO:0000313|Proteomes:UP000019325} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CCY9414 {ECO:0000313|EMBL:AHJ27772.1}; RX PubMed=23555932; RA Voss B., Bolhuis H., Fewer D.P., Kopf M., Moke F., Haas F., RA El-Shehawy R., Hayes P., Bergman B., Sivonen K., Dittmann E., RA Scanlan D.J., Hagemann M., Stal L.J., Hess W.R.; RT "Insights into the physiology and ecology of the brackish-water- RT adapted Cyanobacterium Nodularia spumigena CCY9414 based on a genome- RT transcriptome analysis."; RL PLoS ONE 8:E60224-E60224(2013). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP007203; AHJ27772.1; -; Genomic_DNA. DR RefSeq; WP_006197389.1; NZ_CP007203.1. DR ProteinModelPortal; A0ZI19; -. DR STRING; 313624.N9414_17822; -. DR EnsemblBacteria; AHJ27772; AHJ27772; NSP_14370. DR PATRIC; fig|313624.11.peg.1444; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR Proteomes; UP000019325; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000019325}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000019325}. FT DOMAIN 348 518 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 307 341 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 521 AA; 57235 MW; 2727F02BF7BB273A CRC64; MRVGVGTPRQ TQIPPLELPR YGAERLSGIR CIATHLKPEP PNESALTAMA LQRLDALAVI NITGTGFTKR GGGSTGYVKE TYLAHLVSST KHLVSTPQLV ISDEKSLAQD TALYSSVSPP MSLDMLSEHD FIELVEGLEA EFQRDFVAQE VDADHDRVLL VGLITDKTTP QRFQDTILEL ARLVDTAGGE VLQTVQQKRS RIHPQTVVGE GKVEEIALTA QTLGANLVVF DRDLSPAQVR NLERKIGVRV VDRTEVILDI FAQRAQSRAG KLQVELAQLG YMMPRLSGRG LAMSRLGGGI GTRGPGETKL ETERRAIQKR ISRLQQEVNQ LQAHRSRLRL RRQNQEVPSV ALVGYTNAGK STLLNALTNA EVYTADQLFA TLDPTTRRLV IADGDTGGTQ EILLTDTVGF IHELPASLMD AFRATLEEVT EADALLHLVD LSHPAWLSHI RSVREILAQM PVTPGPALVI FNKIDQVDSA TLAIAQEEFP LAVFISASQR LGLETLRQRL TKLIQYVVDA R // ID A1A2G6_BIFAA Unreviewed; 498 AA. AC A1A2G6; DT 23-JAN-2007, integrated into UniProtKB/TrEMBL. DT 23-JAN-2007, sequence version 1. DT 07-JUN-2017, entry version 69. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:BAF39899.1}; GN OrderedLocusNames=BAD_1118 {ECO:0000313|EMBL:BAF39899.1}; OS Bifidobacterium adolescentis (strain ATCC 15703 / DSM 20083 / NCTC OS 11814 / E194a). OC Bacteria; Actinobacteria; Bifidobacteriales; Bifidobacteriaceae; OC Bifidobacterium. OX NCBI_TaxID=367928 {ECO:0000313|EMBL:BAF39899.1, ECO:0000313|Proteomes:UP000008702}; RN [1] {ECO:0000313|EMBL:BAF39899.1, ECO:0000313|Proteomes:UP000008702} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 15703 / DSM 20083 / NCTC 11814 / E194a RC {ECO:0000313|Proteomes:UP000008702}; RA Suzuki T., Tsuda Y., Kanou N., Inoue T., Kumazaki K., Nagano S., RA Hirai S., Tanaka K., Watanabe K.; RT "Bifidobacterium adolescentis complete genome sequence."; RL Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AP009256; BAF39899.1; -; Genomic_DNA. DR ProteinModelPortal; A1A2G6; -. DR STRING; 367928.BAD_1118; -. DR EnsemblBacteria; BAF39899; BAF39899; BAD_1118. DR KEGG; bad:BAD_1118; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000008702; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000008702}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000008702}. FT DOMAIN 278 444 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 498 AA; 54285 MW; BBD90A5DCBC0F281 CRC64; MPLSQDNDIE QSMTAGDVTG VLADQSDVLL DTNGGEHLRE THDEQWQERE SRNALKHVAG LGEIQDVTEV EYRKVRLERV VLVGVWSSRE TTQAAAEESL RELAALAETA GAVVCDGLLQ HRIKPDAATY VGSGKARELA GIVAQDEADT IVVDDDLPPS QRRALEDATK VKVVDRTAVI LDIFAQHATS REGKAQVELA QLEYMLPRLR GWGGSLSRQA GGRAAGDAGI GSRGPGETKI EMDRRVIRSR IAKLRRQIAQ MAPARDVKRG ARRRFGLPTV AVVGYTNAGK SSLTNRLTGS AELVENALFA TLDTAVRRAK AKDGRLYAYV DTVGFVRRLP TQLIEAFKST LEEVADADLI VHVVDGSHPD PFSQIDAVND VLSDIDGVET IPTIVAFNKA DRMDEAARER VEALMPDAYI VSAFSGEGVE ALREKVESML PTPNVHVEAL LPYAAGSLMS RVREYGRVVN VEYRDDGMML EAEVDDQLAA QIVEQAID // ID A1AT22_PELPD Unreviewed; 580 AA. AC A1AT22; DT 23-JAN-2007, integrated into UniProtKB/TrEMBL. DT 23-JAN-2007, sequence version 1. DT 07-JUN-2017, entry version 78. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Ppro_2895 {ECO:0000313|EMBL:ABL00493.1}; OS Pelobacter propionicus (strain DSM 2379 / NBRC 103807 / OttBd1). OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfuromonadales; OC Desulfuromonadaceae; Pelobacter. OX NCBI_TaxID=338966 {ECO:0000313|EMBL:ABL00493.1, ECO:0000313|Proteomes:UP000006732}; RN [1] {ECO:0000313|EMBL:ABL00493.1, ECO:0000313|Proteomes:UP000006732} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 2379 / NBRC 103807 / OttBd1 RC {ECO:0000313|Proteomes:UP000006732}; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., RA Pitluck S., Saunders E., Brettin T., Bruce D., Han C., Tapia R., RA Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E., RA Lovley D., Richardson P.; RT "Complete sequence of chromosome of Pelobacter propionicus DSM 2379."; RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000482; ABL00493.1; -; Genomic_DNA. DR ProteinModelPortal; A1AT22; -. DR STRING; 338966.Ppro_2895; -. DR EnsemblBacteria; ABL00493; ABL00493; Ppro_2895. DR KEGG; ppd:Ppro_2895; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; EREVIIT; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000006732; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000006732}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000006732}. FT DOMAIN 402 575 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 361 395 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 580 AA; 65747 MW; 564B59B0E20DCCA2 CRC64; MPSARGRSIL KSIFRSWQQR SHPIKEVFGN LTGLKTSQIQ ALERLYRRRI PQAEFCTQEL AGRLVELSLD IRRQIGILVN RSGMVEYVIV GDERGLVIPE LRDYPLGKRP LRGLRLIHTH LKNEQVSEDD LTDLSLLRLD LLAALLFSPE KRRISVQMAW ISPTSSGPST ITGAITTFER VDLECARFLE ELEADLSRST RAKSSGVEAL ERAILVSVTV EGTRQEAEDS IMELRELART AQIEVLDEFI QRPRSINPRF VMGEGKMRDV VIRALQHGAT MLIFDQELTP AQIRSISAMT ELKAIDRSQL ILDIFARRAQ TLDGKVQVEL AQLKYLLPRL TGRGVQMSRL MGGIGGRGPG ETKLETDRRR IRDRIASLER ELKELSRGRD QRRRKRVKAS VPIVSIVGYT NAGKSTLLNT LTKSRVFTED LLFATLDTST RRLRFPLERE VIITDTVGFI RSLPASLLGA FKATLEELRD ADLLLHVVDA SNPRFETHIQ QVNRILDELE LGDKPRLLIF NKSDLLAKLK KSDTIAFLRV RQFARTCGGI MIAATDRTSM SPLLEELQRR FWPDESSLID // ID A1AVN8_RUTMC Unreviewed; 441 AA. AC A1AVN8; DT 23-JAN-2007, integrated into UniProtKB/TrEMBL. DT 23-JAN-2007, sequence version 1. DT 07-JUN-2017, entry version 82. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Rmag_0207 {ECO:0000313|EMBL:ABL01995.1}; OS Ruthia magnifica subsp. Calyptogena magnifica. OC Bacteria; Proteobacteria; Gammaproteobacteria; OC sulfur-oxidizing symbionts; Candidatus Ruthia. OX NCBI_TaxID=413404 {ECO:0000313|EMBL:ABL01995.1, ECO:0000313|Proteomes:UP000002587}; RN [1] {ECO:0000313|EMBL:ABL01995.1, ECO:0000313|Proteomes:UP000002587} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Cm {ECO:0000313|EMBL:ABL01995.1}; RX PubMed=17303757; DOI=10.1126/science.1138438; RA Newton I.L.G., Woyke T., Auchtung T.A., Dilly G.F., Dutton R.J., RA Fisher M.C., Fontanez K.M., Lau E., Stewart F.J., Richardson P.M., RA Barry K.W., Saunders E., Detter J.C., Wu D., Eisen J.A., RA Cavanaugh C.M.; RT "The Calyptogena magnifica chemoautotrophic symbiont genome."; RL Science 315:998-1000(2007). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000488; ABL01995.1; -; Genomic_DNA. DR RefSeq; WP_011737620.1; NC_008610.1. DR ProteinModelPortal; A1AVN8; -. DR STRING; 413404.Rmag_0207; -. DR EnsemblBacteria; ABL01995; ABL01995; Rmag_0207. DR KEGG; rma:Rmag_0207; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000002587; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000002587}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Hydrolase {ECO:0000313|EMBL:ABL01995.1}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000002587}. FT DOMAIN 205 372 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 441 AA; 49479 MW; A01A9CE02D4896FB CRC64; MVLFEQQKDA IGKGERTLLV YVELTSNKQS HNAQVEFKEL AESSGLNIVK TIKVNCNSVL IRFFIGTGKV EEIAKIVEDS ALDLVIFSPE LSPSQERNLK KSLKCQVMDR TGLILDIFAL RASSFEGKLQ VELAQLKHLS TRLIRGWTHL ERQKGGIGLR GPGETQLETD KRLIAIRIKN ITKRLYKVHK QRDLGRKSRT KNELPMIALA GYTNAGKSTL FNVLTNAEVF ANDQLFATLN STIRRVILPA SGEAAIVDTV GFIQDLPHDL VDAFKSTLEE TKCANVLLHI VDAADEYNIE KIAQVEDIIF EIGASNIPSI LVMNKIDCLD NFVPRMDRDE NGHIHRVWLS AQTGKGIDFL HQALAEQLSG MMTRAKVHLD VGSAYIRSNI HDIGHIHHEK VDDFGAWVLE IFVTKHYLSK LLNFKGVTLL WEQSSPTNKL I // ID A1B9J3_PARDP Unreviewed; 435 AA. AC A1B9J3; DT 23-JAN-2007, integrated into UniProtKB/TrEMBL. DT 23-JAN-2007, sequence version 1. DT 07-JUN-2017, entry version 79. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Pden_4123 {ECO:0000313|EMBL:ABL72187.1}; OS Paracoccus denitrificans (strain Pd 1222). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae; Paracoccus. OX NCBI_TaxID=318586 {ECO:0000313|EMBL:ABL72187.1, ECO:0000313|Proteomes:UP000000361}; RN [1] {ECO:0000313|Proteomes:UP000000361} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Pd 1222 {ECO:0000313|Proteomes:UP000000361}; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., RA Pitluck S., Munk A.C., Brettin T., Bruce D., Han C., Tapia R., RA Gilna P., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., RA Lykidis A., Spiro S., Richardson D.J., Moir J.W.B., Ferguson S.J., RA van Spanning R.J.M., Richardson P.; RT "Complete sequence of chromosome 2 of Paracoccus denitrificans RT PD1222."; RL Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000490; ABL72187.1; -; Genomic_DNA. DR RefSeq; WP_011750354.1; NC_008687.1. DR ProteinModelPortal; A1B9J3; -. DR STRING; 318586.Pden_4123; -. DR EnsemblBacteria; ABL72187; ABL72187; Pden_4123. DR KEGG; pde:Pden_4123; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000000361; Chromosome 2. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000000361}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Hydrolase {ECO:0000313|EMBL:ABL72187.1}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000000361}. FT DOMAIN 211 380 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 435 AA; 48097 MW; CA9C2A9503659372 CRC64; MAEPTETRER PTRAYVIHPD LGNSRTRRSP DLALEEAVAL AHALPAIEVT GAEVARLRNP DPGMLFSKGK REEIGQHLEA AAAGEGAELV LIDGPVTPVQ QRNLEKEWGV KILDRTGLIL EIFADRAQTR EGVLQVELAA LAYQRTRLVR AWTHLERQRG GLGFVGGPGE TQIEADRRAI DEQVVRLRRQ LERVVKTREL HRKARAKVPY PIVALVGYTN AGKSTLFNRL TGAEVLAQDQ LFATLDPTMR QLTLPGGRRV ILSDTVGFIS DLPHELVAAF RATLEEVLAA DLILHVRDIS HPETEEQAGD VGEILDSLGV EEDVPLIEVW NKIDALSPET RAALQRTDAR TQGVQAISAL SGEGLDTLLA AIEARLAEVL DEPRREAELV LPHSDGRRRA WLHEQGVITA EEVAEDGVRL RLRWTDRQKA AFQAL // ID A1BH77_CHLPD Unreviewed; 434 AA. AC A1BH77; DT 23-JAN-2007, integrated into UniProtKB/TrEMBL. DT 23-JAN-2007, sequence version 1. DT 07-JUN-2017, entry version 73. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Cpha266_1737 {ECO:0000313|EMBL:ABL65754.1}; OS Chlorobium phaeobacteroides (strain DSM 266). OC Bacteria; Chlorobi; Chlorobia; Chlorobiales; Chlorobiaceae; OC Chlorobium/Pelodictyon group; Chlorobium. OX NCBI_TaxID=290317 {ECO:0000313|EMBL:ABL65754.1, ECO:0000313|Proteomes:UP000008701}; RN [1] {ECO:0000313|EMBL:ABL65754.1, ECO:0000313|Proteomes:UP000008701} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 266 {ECO:0000313|EMBL:ABL65754.1, RC ECO:0000313|Proteomes:UP000008701}; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Hammon N., Israni S., Pitluck S., Goltsman E., RA Schmutz J., Larimer F., Land M., Hauser L., Mikhailova N., Li T., RA Overmann J., Bryant D.A., Richardson P.; RT "Complete sequence of Chlorobium phaeobacteroides DSM 266."; RL Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000492; ABL65754.1; -; Genomic_DNA. DR RefSeq; WP_011745563.1; NC_008639.1. DR ProteinModelPortal; A1BH77; -. DR STRING; 290317.Cpha266_1737; -. DR EnsemblBacteria; ABL65754; ABL65754; Cpha266_1737. DR KEGG; cph:Cpha266_1737; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000008701; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000008701}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Hydrolase {ECO:0000313|EMBL:ABL65754.1}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000008701}. FT DOMAIN 202 369 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 434 AA; 49089 MW; 70871F3C2063DDC7 CRC64; MNITTCEKNR EKAVLIGLCS PPELPRTLVE EYLQELAFLA DTAGADVLMS IIQEKKQRDP ASFLGKGKVD ELAVFVKENA VDIVICDDDL TPVQARNLER ALECKVIDRT GLILQIFAIR AQSSQAKIQV ELAQLEYMLP RLSGQWTHLS KQKGGIGSKG PGETQIETDR RLVRNRISLL KRKLREVLLQ HDTQTRGRLI IPRVALVGYT NAGKSTLMNI LCPEAEAFAE NRLFATLDTK TRRLELKINK LVLLSDTVGF IRKLPHHLVE SFKSTLDEVL QADFLLHVID VSHPAFEEQM VVVRDTLREL GVEHDNIIDV FNKIDALEDP GALGALRMKY PEAVFVSAAR GLNIAVLKEI ISDHVALDYR ERKIRTHVSN YKLIGYLYEH TEVVSKRYLD EDVELTFRVH KNSLKHIDAL IKPLLIHDYA VADL // ID A1HMU1_9FIRM Unreviewed; 597 AA. AC A1HMU1; DT 06-FEB-2007, integrated into UniProtKB/TrEMBL. DT 06-FEB-2007, sequence version 1. DT 07-JUN-2017, entry version 60. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=TcarDRAFT_2047 {ECO:0000313|EMBL:EAX48575.1}; OS Thermosinus carboxydivorans Nor1. OC Bacteria; Firmicutes; Negativicutes; Selenomonadales; Sporomusaceae; OC Thermosinus. OX NCBI_TaxID=401526 {ECO:0000313|EMBL:EAX48575.1, ECO:0000313|Proteomes:UP000005139}; RN [1] {ECO:0000313|EMBL:EAX48575.1, ECO:0000313|Proteomes:UP000005139} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Nor1 {ECO:0000313|EMBL:EAX48575.1, RC ECO:0000313|Proteomes:UP000005139}; RG US DOE Joint Genome Institute (JGI-ORNL); RA Larimer F., Land M., Hauser L.; RT "Annotation of the draft genome assembly of Thermosinus RT carboxydivorans Nor1."; RL Submitted (JAN-2007) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:EAX48575.1, ECO:0000313|Proteomes:UP000005139} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Nor1 {ECO:0000313|EMBL:EAX48575.1, RC ECO:0000313|Proteomes:UP000005139}; RG US DOE Joint Genome Institute (JGI-PGF); RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., RA Dalin E., Tice H., Bruce D., Pitluck S., Richardson P.; RT "Sequencing of the draft genome and assembly of Thermosinus RT carboxydivorans Nor1."; RL Submitted (JAN-2007) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EAX48575.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AAWL01000002; EAX48575.1; -; Genomic_DNA. DR RefSeq; WP_007288346.1; NZ_AAWL01000002.1. DR ProteinModelPortal; A1HMU1; -. DR STRING; 401526.TcarDRAFT_2047; -. DR EnsemblBacteria; EAX48575; EAX48575; TcarDRAFT_2047. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000005139; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000005139}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000005139}. FT DOMAIN 377 542 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 336 370 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 597 AA; 66656 MW; EEAFCF719A371977 CRC64; MAEIHGDIAG LRKSTISRLE KLYDFVVPSG QVATEEIIQL LAELSGELNR EIALYLNRRG QVIRVAIGNA TTVDLPQANG RHALNRLSGL RCLHTHPSGD SRLSDVDLAS LREMRFDLMA ALGVEGGAVK QVSFGYISGC RNDELLVQTV GPVRLEDFIL LDFSFLLKQI ENQLVNRKQA SEAIKPERAL LVGIEKDTGW NISDSLKELA QLAETAGAQV VDIISQRRER PDAAFFIGRG KVHEINLLRQ SKDINLIIFD DELSPAQQRN LEQALGVKVL DRTALILDIF AQRARTREGK LQVELAQLRY NLPRLGGQGL VLSRLGGGIG TRGPGETKLE VDKRRIRERI ADIEAEIEQI KKHRSLHRER RQRAHVPTLA LVGYTNAGKS TLLNTLTNAS VLAEDKLFAT LDPTTRRLKL PNGQEALLTD TVGFIQKLPH QLIAAFRATL EEVVYADLLL HIVDASHPRY EEQMDSVFEV LRELQADTKD IITVFNKIDK IENPNIIARL VRESGSVAIS ALTGLGIDSL LEQVQNKLRI ITTDVCLVIP YSETGLVSQL YDLGSVISID YKTENIVVHA QLPLQYRKRF EPYMKQE // ID A1K3Z5_AZOSB Unreviewed; 379 AA. AC A1K3Z5; DT 06-FEB-2007, integrated into UniProtKB/TrEMBL. DT 06-FEB-2007, sequence version 1. DT 30-AUG-2017, entry version 74. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Synonyms=hflX1 {ECO:0000313|EMBL:CAL93550.1}; GN OrderedLocusNames=azo0933 {ECO:0000313|EMBL:CAL93550.1}; OS Azoarcus sp. (strain BH72). OC Bacteria; Proteobacteria; Betaproteobacteria; Rhodocyclales; OC Zoogloeaceae; Azoarcus. OX NCBI_TaxID=62928 {ECO:0000313|EMBL:CAL93550.1, ECO:0000313|Proteomes:UP000002588}; RN [1] {ECO:0000313|EMBL:CAL93550.1, ECO:0000313|Proteomes:UP000002588} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BH72 {ECO:0000313|EMBL:CAL93550.1, RC ECO:0000313|Proteomes:UP000002588}; RX PubMed=17057704; DOI=10.1038/nbt1243; RA Krause A., Ramakumar A., Bartels D., Battistoni F., Bekel T., Boch J., RA Boehm M., Friedrich F., Hurek T., Krause L., Linke B., McHardy A.C., RA Sarkar A., Schneiker S., Syed A.A., Thauer R., Vorhoelter F.-J., RA Weidner S., Puehler A., Reinhold-Hurek B., Kaiser O., Goesmann A.; RT "Complete genome of the mutualistic, N2-fixing grass endophyte RT Azoarcus sp. strain BH72."; RL Nat. Biotechnol. 24:1385-1391(2006). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AM406670; CAL93550.1; -; Genomic_DNA. DR RefSeq; WP_011764667.1; NC_008702.1. DR ProteinModelPortal; A1K3Z5; -. DR STRING; 62928.azo0933; -. DR EnsemblBacteria; CAL93550; CAL93550; azo0933. DR KEGG; azo:azo0933; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000002588; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000002588}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Hydrolase {ECO:0000313|EMBL:CAL93550.1}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Protease {ECO:0000313|EMBL:CAL93550.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000002588}. FT DOMAIN 198 363 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 379 AA; 41116 MW; 5DB045DB37434E2F CRC64; MFDRPATGER AVLVQMDLGQ GAIEERLSEL ELLATSAGAT VEAVVRGRRS APDSALFAGS GKVQEIAEAL QAHGGDLVIF NHALSPAQQR NLERSLSCRV IDRTALILDI FALRARSHEG KLQVELAQLQ HLSTRLVRGW THLERQKGGI GLRGPGEKQL ETDRRLLGGR VKLLKSRLAQ IEKQRRVRRR ARERNDALTV SLVGYTNAGK STLFNALTKA GAYAADQLFA TLDTTSRRLF VGGGNVVLSD TVGFIRDLPH ALVAAFEATL EETAHADVLL HVVDAASEDR DAQIEAVNRV LEEIGAAEVP QILVWNKIDL THAAPAVERG DCDRIRRVFL SARTGEGLEL LREALAELAC RDALPGSGAA DPVGNQPIQ // ID A1K539_AZOSB Unreviewed; 464 AA. AC A1K539; DT 06-FEB-2007, integrated into UniProtKB/TrEMBL. DT 06-FEB-2007, sequence version 1. DT 30-AUG-2017, entry version 70. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Synonyms=hflX2 {ECO:0000313|EMBL:CAL93944.1}; GN OrderedLocusNames=azo1327 {ECO:0000313|EMBL:CAL93944.1}; OS Azoarcus sp. (strain BH72). OC Bacteria; Proteobacteria; Betaproteobacteria; Rhodocyclales; OC Zoogloeaceae; Azoarcus. OX NCBI_TaxID=62928 {ECO:0000313|EMBL:CAL93944.1, ECO:0000313|Proteomes:UP000002588}; RN [1] {ECO:0000313|EMBL:CAL93944.1, ECO:0000313|Proteomes:UP000002588} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BH72 {ECO:0000313|EMBL:CAL93944.1, RC ECO:0000313|Proteomes:UP000002588}; RX PubMed=17057704; DOI=10.1038/nbt1243; RA Krause A., Ramakumar A., Bartels D., Battistoni F., Bekel T., Boch J., RA Boehm M., Friedrich F., Hurek T., Krause L., Linke B., McHardy A.C., RA Sarkar A., Schneiker S., Syed A.A., Thauer R., Vorhoelter F.-J., RA Weidner S., Puehler A., Reinhold-Hurek B., Kaiser O., Goesmann A.; RT "Complete genome of the mutualistic, N2-fixing grass endophyte RT Azoarcus sp. strain BH72."; RL Nat. Biotechnol. 24:1385-1391(2006). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AM406670; CAL93944.1; -; Genomic_DNA. DR ProteinModelPortal; A1K539; -. DR STRING; 62928.azo1327; -. DR EnsemblBacteria; CAL93944; CAL93944; azo1327. DR KEGG; azo:azo1327; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; VILEIFH; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000002588; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000002588}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Hydrolase {ECO:0000313|EMBL:CAL93944.1}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000002588}. FT DOMAIN 238 408 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 203 230 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 464 AA; 51564 MW; 364774FA7301DD6A CRC64; MASSGSISTY CRPTRARMQK DLADKPRYAI AASVQLPNVS DAEFEASLAE LRELAKTLGY QVVHTFVQKR GGFDTTGYLG VGKRQEIRDF VSAQAGFDAA PNATVPRTGE IEALLVDHEI SPSQARNLEL ETGCEVMDRT MVILEIFHRN ARSRAAKAQV EIARLGYMAP RLREAAKLAG PQGRQRSGVG GRGAGESHTE LDRRKIRDRI AELQLEIVAM EAERKTQRAR RQGRQSLANV ALVGYTNAGK STLMRALTGS EVLVANKLFA TLDTTVRTLY PESVPRVLVS DTVGFIKNLP HGLVASFKST LDEALDAALL LHVIDASDPG FERQLEVTDK VLEEIDAQDI PRIRVFNKID HVGDAEAQAE CEAALRAKYP DCIVMSARRP DEVAKLRQTI VAFFQRDLVE AELLLPWSAQ QLRKEIYANC QVLEERAEDE GAVFRLRGER DVVERLRERF LLVD // ID A1R554_PAEAT Unreviewed; 629 AA. AC A1R554; DT 06-FEB-2007, integrated into UniProtKB/TrEMBL. DT 06-FEB-2007, sequence version 1. DT 07-JUN-2017, entry version 88. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=AAur_1600 {ECO:0000313|EMBL:ABM06879.1}; OS Paenarthrobacter aurescens (strain TC1). OC Bacteria; Actinobacteria; Micrococcales; Micrococcaceae; OC Paenarthrobacter. OX NCBI_TaxID=290340 {ECO:0000313|EMBL:ABM06879.1, ECO:0000313|Proteomes:UP000000637}; RN [1] {ECO:0000313|EMBL:ABM06879.1, ECO:0000313|Proteomes:UP000000637} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=TC1 {ECO:0000313|EMBL:ABM06879.1, RC ECO:0000313|Proteomes:UP000000637}; RX PubMed=17194220; DOI=10.1371/journal.pgen.0020214; RA Mongodin E.F., Shapir N., Daugherty S.C., DeBoy R.T., Emerson J.B., RA Shvartzbeyn A., Radune D., Vamathevan J., Riggs F., Grinberg V., RA Khouri H., Wackett L.P., Nelson K.E., Sadowsky M.J.; RT "Secrets of soil survival revealed by the genome sequence of RT Arthrobacter aurescens TC1."; RL PLoS Genet. 2:2094-2106(2006). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000474; ABM06879.1; -; Genomic_DNA. DR ProteinModelPortal; A1R554; -. DR STRING; 290340.AAur_1600; -. DR EnsemblBacteria; ABM06879; ABM06879; AAur_1600. DR KEGG; aau:AAur_1600; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000000637; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000000637}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000000637}. FT DOMAIN 408 570 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 629 AA; 68170 MW; E93A25BF20A7EA51 CRC64; MAQFGRNGSV RWFHAEPDTL KIPSRLSIRC GPLTFCGRSA GTGSASSPWP RTLPAESTTP HHNSPAPTRP GLPSTQEALL ADARQPSANS APPSSKQHYS GIAEQSKETM TTQKHSGSDS DAQDMSPEQI QAVIDRILSK DVPAQASDDN DANGVFGKAQ AISTLDQEHS IFDGDQEDLA ERRALRRTAG LSTELEDVTE VEYRQLRLER VVLAGLWTEG TLADAENSLR ELAALAETAG SEVLDGLVQR RQKPDPGTFL GSGKAQELKD IVAATGADTV VVDTELAPSQ RRGLEDIVKV KVVDRTTLIL DIFAQHAKSR EGKAQVELAQ LEYLLPRLRG WGDSMSRQAG GQVGGAGAGM GSRGPGETKI ELDRRRIRTR MAKLRREIAA MKPARETKRA NRRRNAVPSV AIAGYTNAGK SSLLNRLTDA GVLVENALFA TLDPTVRKAQ TPDGIGYTLA DTVGFVRSLP TQLIEAFRST LEEVADADLI LHVVDASHPD PEGQIAAVRA VFTEVDARKV PEIIVLNKVD VADPFVVERL KQKEPRHAVV STRTGQGIAE LLEDISRSIP RPGVRLELLI PYDRGEMINK LHNSDSEILS LEHEENGTRV VVMVREGLAA ELESFVSNG // ID A1S3K3_SHEAM Unreviewed; 443 AA. AC A1S3K3; DT 06-FEB-2007, integrated into UniProtKB/TrEMBL. DT 06-FEB-2007, sequence version 1. DT 07-JUN-2017, entry version 69. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Sama_0751 {ECO:0000313|EMBL:ABL98959.1}; OS Shewanella amazonensis (strain ATCC BAA-1098 / SB2B). OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales; OC Shewanellaceae; Shewanella. OX NCBI_TaxID=326297 {ECO:0000313|EMBL:ABL98959.1, ECO:0000313|Proteomes:UP000009175}; RN [1] {ECO:0000313|EMBL:ABL98959.1, ECO:0000313|Proteomes:UP000009175} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-1098 / SB2B {ECO:0000313|Proteomes:UP000009175}; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., RA Pitluck S., Munk A.C., Brettin T., Bruce D., Han C., Tapia R., RA Gilna P., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., RA Mikhailova N., Fredrickson J., Richardson P.; RT "Complete sequence of Shewanella amazonensis SB2B."; RL Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000507; ABL98959.1; -; Genomic_DNA. DR RefSeq; WP_011758869.1; NC_008700.1. DR ProteinModelPortal; A1S3K3; -. DR STRING; 326297.Sama_0751; -. DR EnsemblBacteria; ABL98959; ABL98959; Sama_0751. DR KEGG; saz:Sama_0751; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; VILEIFH; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000009175; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000009175}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000009175}. FT DOMAIN 222 387 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 186 217 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 443 AA; 48734 MW; 6F1AABDE940AEE7F CRC64; MPPIQEQVVT RALLISIHTP NIGAKEVERS LAELARLVST LGFAVYATET QRQQSTKRLS VLGTGKLEQL ARMTGALDEA EDSLVNIDEA GLESFLAGNQ RQHANVVVFD CDLSPMQLRN LEDALGVEVF DRSGIIIEIF SRHASSKTAR LQVELARLNY LTPRVRREHA GDRQRTGGRS VGESAIELER RAIRDKQAEL RRELKKVQEV MQEQKSSRMD TPSAALVGYT NAGKSSLMRA LTGSEVLVEN KLFATLDTTV RALSPQTQPR ILISDTVGFI NKLPHDLVPA FHSTLEEAKD ASLLLYVVDA SDADFRAQLE VVRNVLGQSK LAGKDKLLLL NKVDCLSDEA RSALAQEFPD ALQISALSQE DVARVHQAIV DAIANQLLSA CFNIPYAASA LMGEVHGRMQ IIDEAYHESG LRITVRGRSA DLDRLNKRLQ TGG // ID A1SA20_SHEAM Unreviewed; 435 AA. AC A1SA20; DT 06-FEB-2007, integrated into UniProtKB/TrEMBL. DT 06-FEB-2007, sequence version 1. DT 30-AUG-2017, entry version 78. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Sama_3024 {ECO:0000313|EMBL:ABM01227.1}; OS Shewanella amazonensis (strain ATCC BAA-1098 / SB2B). OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales; OC Shewanellaceae; Shewanella. OX NCBI_TaxID=326297 {ECO:0000313|EMBL:ABM01227.1, ECO:0000313|Proteomes:UP000009175}; RN [1] {ECO:0000313|EMBL:ABM01227.1, ECO:0000313|Proteomes:UP000009175} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-1098 / SB2B {ECO:0000313|Proteomes:UP000009175}; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., RA Pitluck S., Munk A.C., Brettin T., Bruce D., Han C., Tapia R., RA Gilna P., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., RA Mikhailova N., Fredrickson J., Richardson P.; RT "Complete sequence of Shewanella amazonensis SB2B."; RL Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000507; ABM01227.1; -; Genomic_DNA. DR RefSeq; WP_011761131.1; NC_008700.1. DR ProteinModelPortal; A1SA20; -. DR STRING; 326297.Sama_3024; -. DR EnsemblBacteria; ABM01227; ABM01227; Sama_3024. DR KEGG; saz:Sama_3024; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000009175; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000009175}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000009175}. FT DOMAIN 198 364 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 164 191 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 435 AA; 48701 MW; 0C37C0D36217F10F CRC64; MFDRYEAGET AVLVHIDFTD EGSREDLAEL QLLVESAGAR SVGVITGSRR APDRKFFVGT GKAEELAAMV AATDANVVIF NHALSPAQER NLEHLCRCRV LDRTTLILDI FAQRARTHEG KLQVELAQLR HMSTRLVRGW THLERQKGGI GLRGPGETQL ETDRRLLRGR IKNINRRLEK VDKQREQSRR ARQRSDMAAV SLVGYTNAGK STLFNTLTSA EVYAADQLFA TLDPTLRKLE LPDGAAILAD TVGFIRHLPH DLVAAFKATL QETREADLLL HVIDCADEKM RDNIEQVQAV LKEIDADEIP QLIVCNKIDL VEGIKPAIDR DDTGKPFRVW LSAQQNQGLD LLRQAVQELV GNVIAELTLK IPATAGHYLG QFYRLDAIQQ KEYDDLGNCI LSVRLPDADW RRLAKQSQGE LETFIVDTAT DRVVC // ID A1SNF0_NOCSJ Unreviewed; 493 AA. AC A1SNF0; DT 06-FEB-2007, integrated into UniProtKB/TrEMBL. DT 06-FEB-2007, sequence version 1. DT 07-JUN-2017, entry version 73. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Noca_3837 {ECO:0000313|EMBL:ABL83335.1}; OS Nocardioides sp. (strain ATCC BAA-499 / JS614). OC Bacteria; Actinobacteria; Propionibacteriales; Nocardioidaceae; OC Nocardioides. OX NCBI_TaxID=196162 {ECO:0000313|EMBL:ABL83335.1, ECO:0000313|Proteomes:UP000000640}; RN [1] {ECO:0000313|Proteomes:UP000000640} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-499 / JS614 {ECO:0000313|Proteomes:UP000000640}; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., RA Pitluck S., Thompson L.S., Brettin T., Bruce D., Han C., Tapia R., RA Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E., RA Mattes T., Gossett J., Richardson P.; RT "Complete sequence of chromosome 1 of Nocardioides sp. JS614."; RL Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000509; ABL83335.1; -; Genomic_DNA. DR RefSeq; WP_011757266.1; NC_008699.1. DR ProteinModelPortal; A1SNF0; -. DR STRING; 196162.Noca_3837; -. DR EnsemblBacteria; ABL83335; ABL83335; Noca_3837. DR KEGG; nca:Noca_3837; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000000640; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 2. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000000640}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Hydrolase {ECO:0000313|EMBL:ABL83335.1}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000000640}. FT DOMAIN 275 440 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 241 268 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 493 AA; 54196 MW; 134938AA7AC07E21 CRC64; MTNAPDLNSF SLDDELAATE DWEDDDFRSG YVDEPDPEEP TTGDLDLAER HELRRVAGLR TELEDITEVE YRQLRLERVV LVGVWTEGSV EDAENSMAEL ALLAETAGSE VLDAIYQRRQ KPDPATYIGR GKVDGLREIV QATGADTVIC DGELAPSQLR NLEDRLKVKV VDRTALILDI FAQHAKSKEG QAQVELAQLN YLKQRLRGWG GNLSRQVGGR AAGGVGIGGR GPGETKIETD RRRINTKIAK LRRELKEMKG TRDTKRQERR RHHIPSVSIA GYTNAGKSSL LNRLTDAGVL VEDALFATLD PTTRRTTTAD GRVYTMSDTV GFVRHLPHQL VEAFRSTLEE VADADLILHV VDGSHPDPEG QLTAVREVFA EIGASQVPEL VVINKADAAD PMVIARLRQR EPHSVVVSAK TGEGVAEALR VIEGELPRPG VEFKALLPYE RGDLINRLHQ HGEIDSMEHT GEGTIVVGRA NEDLAGELAA YAV // ID A1SXB1_PSYIN Unreviewed; 443 AA. AC A1SXB1; DT 06-FEB-2007, integrated into UniProtKB/TrEMBL. DT 06-FEB-2007, sequence version 1. DT 07-JUN-2017, entry version 74. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Ping_2390 {ECO:0000313|EMBL:ABM04126.1}; OS Psychromonas ingrahamii (strain 37). OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales; OC Psychromonadaceae; Psychromonas. OX NCBI_TaxID=357804 {ECO:0000313|EMBL:ABM04126.1, ECO:0000313|Proteomes:UP000000639}; RN [1] {ECO:0000313|EMBL:ABM04126.1, ECO:0000313|Proteomes:UP000000639} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=37 {ECO:0000313|EMBL:ABM04126.1, RC ECO:0000313|Proteomes:UP000000639}; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., RA Pitluck S., Thompson L.S., Brettin T., Bruce D., Han C., Tapia R., RA Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Ivanova N., RA Staley J., Richardson P.; RT "Complete sequence of Psychromonas ingrahamii 37."; RL Submitted (JAN-2007) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000510; ABM04126.1; -; Genomic_DNA. DR RefSeq; WP_011770686.1; NC_008709.1. DR ProteinModelPortal; A1SXB1; -. DR STRING; 357804.Ping_2390; -. DR EnsemblBacteria; ABM04126; ABM04126; Ping_2390. DR KEGG; pin:Ping_2390; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; VILEIFH; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000000639; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000000639}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Hydrolase {ECO:0000313|EMBL:ABM04126.1}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000000639}. FT DOMAIN 222 387 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 190 217 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 443 AA; 49653 MW; 7DD95B3DA1B6C3C6 CRC64; MTIPTTEKSV TRALLISIRT PDVSLQEVEE SLAELSRLVS TLGFSVVATK TQRQRSTKQL SVLGSGKLEE LAELTSESED QSQLDFNPDE LSALIAAGDI QEQANVAVFD CELSPNQIRH VEAALGVEVY DRTRVIIEIF SKHARTRTAK LQVEIARLNY LTPRLRDENS GDRERQKGSW IGESAFEINS RRIRDKIADL KREIKKLQEE MQGRRSSRVE QLCVALVGYT NAGKSSLMRA LTDSEVLVED KLFATLDTTV RTLQPPTQPR ILISDTVGFI KKLPHDLVAS FHSTLEEAKD ADLLLYVVDA SDENFTAQLA VVDHVLAELN VDASNRLLLL NKVDCISEER QLALLEQYPD ALQISARNKG DVALVHQEIQ DFLEKKMCPA CFHIPYTASG VMGEIHSKMQ VTDEQYHEDG MRITLKATPV ALERLHKMLQ SSF // ID A1SZK9_PSYIN Unreviewed; 430 AA. AC A1SZK9; DT 06-FEB-2007, integrated into UniProtKB/TrEMBL. DT 06-FEB-2007, sequence version 1. DT 30-AUG-2017, entry version 74. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Ping_3237 {ECO:0000313|EMBL:ABM04924.1}; OS Psychromonas ingrahamii (strain 37). OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales; OC Psychromonadaceae; Psychromonas. OX NCBI_TaxID=357804 {ECO:0000313|EMBL:ABM04924.1, ECO:0000313|Proteomes:UP000000639}; RN [1] {ECO:0000313|EMBL:ABM04924.1, ECO:0000313|Proteomes:UP000000639} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=37 {ECO:0000313|EMBL:ABM04924.1, RC ECO:0000313|Proteomes:UP000000639}; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., RA Pitluck S., Thompson L.S., Brettin T., Bruce D., Han C., Tapia R., RA Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Ivanova N., RA Staley J., Richardson P.; RT "Complete sequence of Psychromonas ingrahamii 37."; RL Submitted (JAN-2007) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000510; ABM04924.1; -; Genomic_DNA. DR RefSeq; WP_011771476.1; NC_008709.1. DR ProteinModelPortal; A1SZK9; -. DR STRING; 357804.Ping_3237; -. DR EnsemblBacteria; ABM04924; ABM04924; Ping_3237. DR KEGG; pin:Ping_3237; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000000639; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000000639}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Hydrolase {ECO:0000313|EMBL:ABM04924.1}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000000639}. FT DOMAIN 198 365 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 430 AA; 47856 MW; BB64D243FF132C59 CRC64; MFDRYEAGEL AVLVHITFSD ENKKEDLDEL KHLVSSAGVN TLDTVTGSRQ APHARYFVGT GKAQEIADAV KTLGANVVVF NHALTPAQQR NLEALCECLV LDRTALILDI FAQRARTYEG RLQVELAQLR YLSTRLIRGW THLERQKGGI GLRGPGETQL ETDRRLLRAR ISTIKSRLAK VEKQREQGRR ARKRNEVPTV ALVGYTNAGK STLFNHLTDA GVYAADQLFA TLDPTLRKVD VVDVGTCILA DTVGFIRHLP HDLVAAFKAT LQETRDATLL LHIVDCADPS HHDNIVAVQT VLDEIDAGDV PQLMIMNKID DVDGIEPYVD FDELGKPVKV WLSAQTGIGV ELLFESLTTL LSGQIRSLQL AIPSEEGKLR ALFYQLDCIE HESYSDNGDC ILDIRLNAIE WQRLIKQQGA SIEEYVVNAK // ID A1T7U9_MYCVP Unreviewed; 482 AA. AC A1T7U9; DT 06-FEB-2007, integrated into UniProtKB/TrEMBL. DT 06-FEB-2007, sequence version 1. DT 07-JUN-2017, entry version 74. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Mvan_2436 {ECO:0000313|EMBL:ABM13249.1}; OS Mycobacterium vanbaalenii (strain DSM 7251 / PYR-1). OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae; OC Mycobacterium. OX NCBI_TaxID=350058 {ECO:0000313|EMBL:ABM13249.1, ECO:0000313|Proteomes:UP000009159}; RN [1] {ECO:0000313|EMBL:ABM13249.1, ECO:0000313|Proteomes:UP000009159} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 7251 / PYR-1 {ECO:0000313|Proteomes:UP000009159}; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., RA Pitluck S., Singan V., Schmutz J., Larimer F., Land M., Hauser L., RA Kyrpides N., Anderson I.J., Miller C., Richardson P.; RT "Complete sequence of Mycobacterium vanbaalenii PYR-1."; RL Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000511; ABM13249.1; -; Genomic_DNA. DR RefSeq; WP_011779661.1; NC_008726.1. DR ProteinModelPortal; A1T7U9; -. DR STRING; 350058.Mvan_2436; -. DR EnsemblBacteria; ABM13249; ABM13249; Mvan_2436. DR KEGG; mva:Mvan_2436; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000009159; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000009159}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Hydrolase {ECO:0000313|EMBL:ABM13249.1}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000009159}. FT DOMAIN 259 428 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 218 245 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 482 AA; 52071 MW; 2642047D58146D48 CRC64; MLSDIRANLD SPMTYPEFSN DNPSVGELAL EDRTALRRVA GLSTELTDVS EVEYRQLRLE RVVLVGVWTE GSAADADASL AELAALAETA GSEVLDGLIQ RRDKPDPSTY IGSGKALELR EIVVATGADT VICDGELSPA QLNALEKVVK VKVIDRTALI LDIFAQHATS REGKAQVSLA QMEYMLPRLR GWGESMSRQA GGRAGGAGGG VGTRGPGETK IETDRRRIRE RMAKLRREIK DMKKIRDTQR SGRRRTEIPS IAIVGYTNAG KSSLLNALTG AGVLVENALF ATLEPTTRRG QFDDGRPFVL TDTVGFVRHL PTQLVEAFRS TLEEVVDAEL LVHVVDGSDV NPLAQINAVR QVINEVAAEY DIAPPPELLV VNKTDAADGV TLAQLRRALP GAVFVSAHTG DGLDRLRARM AELVVPTDTV VDVTIPYSRG DLVARLHADG RIDATEHTER GTRIKARVPV SLAAGLADYA TY // ID A1TM33_ACIAC Unreviewed; 390 AA. AC A1TM33; DT 06-FEB-2007, integrated into UniProtKB/TrEMBL. DT 06-FEB-2007, sequence version 1. DT 07-JUN-2017, entry version 77. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Aave_1430 {ECO:0000313|EMBL:ABM32021.1}; OS Acidovorax citrulli (strain AAC00-1) (Acidovorax avenae subsp. OS citrulli). OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Comamonadaceae; Acidovorax. OX NCBI_TaxID=397945 {ECO:0000313|EMBL:ABM32021.1, ECO:0000313|Proteomes:UP000002596}; RN [1] {ECO:0000313|EMBL:ABM32021.1, ECO:0000313|Proteomes:UP000002596} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=AAC00-1 {ECO:0000313|EMBL:ABM32021.1, RC ECO:0000313|Proteomes:UP000002596}; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Dalin E., Tice H., Pitluck S., Kiss H., RA Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J., RA Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Stahl D., RA Richardson P.; RT "Complete sequence of Acidovorax avenae subsp. citrulli AAC00-1."; RL Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Proteomes:UP000002596} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=AAC00-1 {ECO:0000313|Proteomes:UP000002596}; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Dalin E., Tice H., Pitluck S., Kiss H., RA Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J., RA Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Stahl D., RA Richardson P.; RT "Complete sequence of Acidovorax avenae subsp. citrulli AAC00-1."; RL Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000512; ABM32021.1; -; Genomic_DNA. DR RefSeq; WP_011794571.1; NC_008752.1. DR ProteinModelPortal; A1TM33; -. DR STRING; 397945.Aave_1430; -. DR EnsemblBacteria; ABM32021; ABM32021; Aave_1430. DR KEGG; aav:Aave_1430; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; FNNHAHV; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000002596; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000002596}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Hydrolase {ECO:0000313|EMBL:ABM32021.1}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000002596}. FT DOMAIN 202 375 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 168 195 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 390 AA; 42919 MW; CB0D8C1A64FA1123 CRC64; MSSSSSPEPQ STPVILVGVD FGLPHFDAEL EELGLLAQTA GLAPVARLTC KRKAPDAALF VGSGKADEIR MLAQMHGAVE VLFDQALSPA QQRNLERHLE LPVTDRTLLI LEIFAQRARS HEGKLQVELA RLQYLSTRLV RRWSHLERQR GGIGARGGPG ETQIELDRRM IDDAIKRTRE RLQKVKRQRA TQRRQRARRD TFNISLVGYT NAGKSTLFNA LVKARAYAAD QLFATLDTTT RQLYLAELGG TVSLSDTVGF IRDLPHGLID AFQATLQEAV DADLLLHVVD ASNPDFPEQI AEVEKVLGEI GAGEIPQVLI FNKLDAVPAE QQPLAMQDTY EWDGRQLPKL FVSARTGQGL PELRSQLTAA ALAARENPMT PGADAEFPAP // ID A1U4C4_MARHV Unreviewed; 432 AA. AC A1U4C4; DT 06-FEB-2007, integrated into UniProtKB/TrEMBL. DT 06-FEB-2007, sequence version 1. DT 30-AUG-2017, entry version 76. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Maqu_2768 {ECO:0000313|EMBL:ABM19843.1}; OS Marinobacter hydrocarbonoclasticus (strain ATCC 700491 / DSM 11845 / OS VT8). OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales; OC Alteromonadaceae; Marinobacter. OX NCBI_TaxID=351348 {ECO:0000313|EMBL:ABM19843.1, ECO:0000313|Proteomes:UP000000998}; RN [1] {ECO:0000313|Proteomes:UP000000998} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700491 / DSM 11845 / VT8 RC {ECO:0000313|Proteomes:UP000000998}; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., RA Pitluck S., Kiss H., Brettin T., Bruce D., Han C., Tapia R., Gilna P., RA Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E., RA Edwards K., Richardson P.; RT "Complete sequence of chromosome 1 of Marinobacter aquaeolei VT8."; RL Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000514; ABM19843.1; -; Genomic_DNA. DR RefSeq; WP_011786213.1; NC_008740.1. DR ProteinModelPortal; A1U4C4; -. DR STRING; 351348.Maqu_2768; -. DR EnsemblBacteria; ABM19843; ABM19843; Maqu_2768. DR KEGG; maq:Maqu_2768; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000000998; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000000998}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}. FT DOMAIN 198 365 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 432 AA; 48733 MW; 8B56ABC6D3D9DA27 CRC64; MFERPDVGER AVLVHIDFTA HDDTEDPGEF RELVTSAGVE PVATVTGTRK QPSPRFFVGE GKLEEIRDAV AASEADVVLF NHALSPSQER NIERELKCRV LDRTGVILDI FAQRARTHEG KLQVELAQLE HMSTRLVRGW THLERQKGGI GLRGPGETQL ETDRRLLRER IKSIHRRLEK VRKQRDQGRR ARKRADIPTL SLVGYTNAGK STLFNRITTS SVYAADQLFA TLDPTLRRLE LPDIGPVVMA DTVGFIRHLP HKLVEAFRAT LEETTQATLL LHVIDCHDSR RDENIEQVES VLAEIGADEI PMLQVFNKID LLDGFEPRID RNEEGLPVRA WVSAVSGEGL PLLFDAIVER LAEDVVHHFV RLGPADGKLR ALLHEAGSVL SEEHCDNGDQ VLEVRLQNRD WLQLLSRAGV REDVIRLESR PV // ID A1UF00_MYCSK Unreviewed; 483 AA. AC A1UF00; DT 06-FEB-2007, integrated into UniProtKB/TrEMBL. DT 06-FEB-2007, sequence version 1. DT 30-AUG-2017, entry version 75. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Mkms_2210 {ECO:0000313|EMBL:ABL91408.1}; OS Mycobacterium sp. (strain KMS). OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae; OC Mycobacterium. OX NCBI_TaxID=189918 {ECO:0000313|EMBL:ABL91408.1, ECO:0000313|Proteomes:UP000000638}; RN [1] {ECO:0000313|EMBL:ABL91408.1, ECO:0000313|Proteomes:UP000000638} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=KMS {ECO:0000313|EMBL:ABL91408.1, RC ECO:0000313|Proteomes:UP000000638}; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., RA Pitluck S., Kiss H., Brettin T., Bruce D., Han C., Tapia R., Gilna P., RA Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., RA Mikhailova N., Miller C.D., Richardson P.; RT "Complete sequence of chromosome of Mycobacterium sp. KMS."; RL Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000518; ABL91408.1; -; Genomic_DNA. DR RefSeq; WP_011559562.1; NC_008705.1. DR ProteinModelPortal; A1UF00; -. DR EnsemblBacteria; ABL91408; ABL91408; Mkms_2210. DR KEGG; mkm:Mkms_2210; -. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000000638; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000000638}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000000638}. FT DOMAIN 260 429 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 219 246 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 483 AA; 52057 MW; E1B55036FFE58877 CRC64; MKSDLRANLD SLMTFPEFPA HQTPSAGELA LEDRSALRRV AGLSTELADI SEVEYRQLRL ERVVLVGVWT DGSAADAEAS LAELAALAET AGSEVLEGVV QRRDKPDAST YIGSGKAAEL REIVLATGAD TVICDGELSP AQLTALEKIV KVKVIDRTAL ILDIFAQHAT SREGKAQVSL AQMEYMLPRL RGWGESMSRQ AGGRAGGAGG GVGTRGPGET KIETDRRRIR ERMSKLRREI KDMKKIRDTQ RSGRRRTEVP SVAIVGYTNA GKSSLLNALT GAGVLVENAL FATLEPTTRR GEFDDGRPFV LTDTVGFVRH LPTQLIEAFR STLEEVADAD LLVHVVDGSD ANPLAQISAV REVINEVIAE QNAKPAPELL VVNKIDAADG LSLAHLRRAL PEAVFVSART GQGLDRLSAR MSELVESTDV TVDVTIPYDR GDLVARVHSE GRIDATEHTT DGTRVKARVP VALAAGLRDF ATF // ID A1USH7_BARBK Unreviewed; 457 AA. AC A1USH7; DT 06-FEB-2007, integrated into UniProtKB/TrEMBL. DT 06-FEB-2007, sequence version 1. DT 07-JUN-2017, entry version 72. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:ABM45150.1}; GN OrderedLocusNames=BARBAKC583_0625 {ECO:0000313|EMBL:ABM45150.1}; OS Bartonella bacilliformis (strain ATCC 35685 / KC583). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Bartonellaceae; Bartonella. OX NCBI_TaxID=360095 {ECO:0000313|EMBL:ABM45150.1, ECO:0000313|Proteomes:UP000000643}; RN [1] {ECO:0000313|EMBL:ABM45150.1, ECO:0000313|Proteomes:UP000000643} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 35685 / KC583 {ECO:0000313|Proteomes:UP000000643}; RA Hendrix L., Mohamoud Y., Radune D., Shvartsbeyn A., Daugherty S., RA Dodson R., Durkin A.S., Harkins D., Huot H., Kothari S.P., Madupu R., RA Li J., Nelson W.C., Shrivastava S., Giglio M.G., Haft D., Selengut J., RA Fraser-Ligget C., Seshadri R.; RL Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000524; ABM45150.1; -; Genomic_DNA. DR ProteinModelPortal; A1USH7; -. DR STRING; 360095.BARBAKC583_0625; -. DR EnsemblBacteria; ABM45150; ABM45150; BARBAKC583_0625. DR KEGG; bbk:BARBAKC583_0625; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000000643; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000000643}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000000643}. FT DOMAIN 220 392 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 457 AA; 51561 MW; 2AD0781DEE43CCCB CRC64; MDVNEGCGRF ISQVLKRGRT VIFVPVYHGN KNEKIANERS VSSRVKEALG LARAIGLDVV HHEIVNITTP HPSTLFGSGK VEEFKQVLSH FNEPRIAVLI VDYSLTPVQQ CNLEKLWNCK VIDRTALILE IFGDRAQTKE GVLQVELAYL SYQKGRLVRS WTHLERQRGG HGFLGGPGET QIEADRRILQ DKIVRVRREL KTVIKTRALH RANRKKTCHP VIALVGYTNA GKSTLFNRLS GANILTKDML FATLDPTLRK ITLPYGKTVL LSDTVGFISN LPTHLIAAFR ATLEEVIEAD LIIHVRDISD PDHQFHAQDV LEILSSLGID INDKGRIIEV WNKIDILDQH VLNALQMNTK TLLNPALMVS ALTGEGLKQL LITIEKLISG EMQNIEFVLR PESMSLIDWF YKNSGKIEQE SHDDGSITIK AVLTCEAKKR FDRIKRNYTS KSHLKSY // ID A1VNG0_POLNA Unreviewed; 383 AA. AC A1VNG0; DT 06-FEB-2007, integrated into UniProtKB/TrEMBL. DT 06-FEB-2007, sequence version 1. DT 07-JUN-2017, entry version 73. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Pnap_1878 {ECO:0000313|EMBL:ABM37188.1}; OS Polaromonas naphthalenivorans (strain CJ2). OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Comamonadaceae; Polaromonas. OX NCBI_TaxID=365044 {ECO:0000313|EMBL:ABM37188.1, ECO:0000313|Proteomes:UP000000644}; RN [1] {ECO:0000313|Proteomes:UP000000644} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CJ2 {ECO:0000313|Proteomes:UP000000644}; RX PubMed=19453698; DOI=10.1111/j.1462-2920.2009.01947.x; RA Yagi J.M., Sims D., Brettin T., Bruce D., Madsen E.L.; RT "The genome of Polaromonas naphthalenivorans strain CJ2, isolated from RT coal tar-contaminated sediment, reveals physiological and metabolic RT versatility and evolution through extensive horizontal gene RT transfer."; RL Environ. Microbiol. 11:2253-2270(2009). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000529; ABM37188.1; -; Genomic_DNA. DR RefSeq; WP_011801269.1; NC_008781.1. DR ProteinModelPortal; A1VNG0; -. DR STRING; 365044.Pnap_1878; -. DR EnsemblBacteria; ABM37188; ABM37188; Pnap_1878. DR KEGG; pna:Pnap_1878; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; FNNHAHV; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000000644; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000000644}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Hydrolase {ECO:0000313|EMBL:ABM37188.1}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000000644}. FT DOMAIN 195 371 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 383 AA; 42092 MW; 3371CB35CE736AE5 CRC64; MKTQALALLV GVDLGLPNFD TNLQELGLLA QTAGLEPVAR ITCKRKAPDA ALFIGSGKAD EIKMLALDTG ATEVLFDQSL SPAQQRNLER HLEMPVNDRT LLILEIFAQR ARSHEGKLQV ELARLQYVST RLVRRWSHLE RQTGGAGVRG GPGEKQIELD KRMIGDAIKR TKERLTKVKK QRQTQRKQRE RRNALSISLV GYTNAGKSTL FNALVKASAY TADQLFATLD TTTRQLYLGE AGRSASLSDT VGFIRDLPHG LIDAFAATLK EAVDADLLLH VVDGSNPDYL EQIEQVQRVL SEIGAADVPQ ILVFNKLDAI ENGSLPLHLK DRFELRDAFE GSSRSVERVF VSAKTGEGLN LLRELLAAQA VSVQASDIPQ APQ // ID A1W583_ACISJ Unreviewed; 392 AA. AC A1W583; DT 06-FEB-2007, integrated into UniProtKB/TrEMBL. DT 06-FEB-2007, sequence version 1. DT 07-JUN-2017, entry version 81. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Ajs_1176 {ECO:0000313|EMBL:ABM41408.1}; OS Acidovorax sp. (strain JS42). OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Comamonadaceae; Acidovorax. OX NCBI_TaxID=232721 {ECO:0000313|EMBL:ABM41408.1, ECO:0000313|Proteomes:UP000000645}; RN [1] {ECO:0000313|Proteomes:UP000000645} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=JS42 {ECO:0000313|Proteomes:UP000000645}; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Dalin E., Tice H., Pitluck S., Chertkov O., RA Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J., RA Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Stahl D., RA Richardson P.; RT "Complete sequence of chromosome 1 of Acidovorax sp. JS42."; RL Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000539; ABM41408.1; -; Genomic_DNA. DR RefSeq; WP_011804608.1; NC_008782.1. DR ProteinModelPortal; A1W583; -. DR STRING; 232721.Ajs_1176; -. DR EnsemblBacteria; ABM41408; ABM41408; Ajs_1176. DR KEGG; ajs:Ajs_1176; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; FNNHAHV; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000000645; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000000645}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Hydrolase {ECO:0000313|EMBL:ABM41408.1}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000000645}. FT DOMAIN 202 375 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 392 AA; 43229 MW; 6F17FA3238EAC613 CRC64; MSSHSSPDTK STPVLLVGVD FGLPHFDAEL EELGLLAQTA GLNPVARLTC KRKTPDAALF VGSGKADEIR TLAQMHGAKE VLFDQALSPA QQRNLERSLE LPVNDRTLLI LEIFAQRARS HEGKLQVELA RLQYLSTRLV RRWSHLERQR GGIGTRGGPG ETQIELDRRM ISEAIKRTRE RLVKVKRQRA TQRRQRQRRD TFNISLVGYT NAGKSTLFNA LVKARAYAAD QLFATLDTTT RHLYLGEAAG SVSLSDTVGF IRDLPHGLVD AFQATLQEAV DADLLLHVVD AANPAFPEQI AQVQLVLGEI GAADIPQLLV FNKLDALTPE VRPNVRQDTY ELDGRPVPRI FVSAGLGEGV ADLRQLLADM VQKSLSSGMP PETVAELKGE WD // ID A1WE10_VEREI Unreviewed; 387 AA. AC A1WE10; DT 06-FEB-2007, integrated into UniProtKB/TrEMBL. DT 06-FEB-2007, sequence version 1. DT 07-JUN-2017, entry version 70. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Veis_0074 {ECO:0000313|EMBL:ABM55867.1}; OS Verminephrobacter eiseniae (strain EF01-2). OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Comamonadaceae; Verminephrobacter. OX NCBI_TaxID=391735 {ECO:0000313|EMBL:ABM55867.1, ECO:0000313|Proteomes:UP000000374}; RN [1] {ECO:0000313|Proteomes:UP000000374} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=EF01-2 {ECO:0000313|Proteomes:UP000000374}; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Dalin E., Tice H., Pitluck S., Chertkov O., RA Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J., RA Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Stahl D., RA Richardson P.; RT "Complete sequence of chromosome 1 of Verminephrobacter eiseniae EF01- RT 2."; RL Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000542; ABM55867.1; -; Genomic_DNA. DR RefSeq; WP_011807886.1; NC_008786.1. DR ProteinModelPortal; A1WE10; -. DR STRING; 391735.Veis_0074; -. DR EnsemblBacteria; ABM55867; ABM55867; Veis_0074. DR KEGG; vei:Veis_0074; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000000374; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000000374}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000000374}. FT DOMAIN 198 371 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 387 AA; 42571 MW; 2416712CB427D679 CRC64; MSSQAGSAAV VLVGVDLGLP HFDGELEELG LLAQAAGMQP VARMACKRKA PDAALFVGSG KADEIRSLAQ LHGAEEVLFD QSLSPAQQRN LEQHIELPVN DRTLLILEIF ARRARSHEGK LQVELARLQY LSTRLVRRWS HLERQSGGIG GRGGPGEKQI ELDRRMIGAA IKRTRERLVK VKRQRSTQRR QRERRDTFNI SLVGYTNAGK STLFNALVKA GAYAADQLFA TLDTTTRQLY LANAGRSVSL SDTVGFIRDL PHGLIDAFEA TLQEAVDADL LLHVVDASNP DFPEQMAQVE RVLHEIGAAD IAQMLVFNKL DALPAQRRPL RLQDQYERAG QGLERWFVSA RSGEGLDLLR QALAAKVLAT PADIAPADSV QLPYARP // ID A1WUT5_HALHL Unreviewed; 445 AA. AC A1WUT5; DT 06-FEB-2007, integrated into UniProtKB/TrEMBL. DT 06-FEB-2007, sequence version 1. DT 30-AUG-2017, entry version 73. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Hhal_0665 {ECO:0000313|EMBL:ABM61447.1}; OS Halorhodospira halophila (strain DSM 244 / SL1) (Ectothiorhodospira OS halophila (strain DSM 244 / SL1)). OC Bacteria; Proteobacteria; Gammaproteobacteria; Chromatiales; OC Ectothiorhodospiraceae; Halorhodospira. OX NCBI_TaxID=349124 {ECO:0000313|EMBL:ABM61447.1, ECO:0000313|Proteomes:UP000000647}; RN [1] {ECO:0000313|Proteomes:UP000000647} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 244 / SL1 {ECO:0000313|Proteomes:UP000000647}; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., RA Pitluck S., Saunders E., Brettin T., Bruce D., Han C., Tapia R., RA Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., RA Mikhailova N., Hoff W., Richardson P.; RT "Complete sequence of Halorhodospira halophila SL1."; RL Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000544; ABM61447.1; -; Genomic_DNA. DR ProteinModelPortal; A1WUT5; -. DR STRING; 349124.Hhal_0665; -. DR EnsemblBacteria; ABM61447; ABM61447; Hhal_0665. DR KEGG; hha:Hhal_0665; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR BioCyc; HHAL349124:GI3I-684-MONOMER; -. DR Proteomes; UP000000647; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000000647}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Hydrolase {ECO:0000313|EMBL:ABM61447.1}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000000647}. FT DOMAIN 216 382 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 445 AA; 49320 MW; 37144A3A3A14CA5E CRC64; MSARRRAITE QRIGSGPADL FARPSGGERA VVLHVRLPGD ALDAAEEFEA LGDSAGAEVV GRFRHRRDTP DPRTFIGRGK VAELADWVRE LEAALVLVDQ PLSAAQERNL ETDLGCRVLD RTGLILDIFA QRARTFEGRL QVELAQLKHV ASRLVRGWSH LERQKGGIGL RGPGEKQLEM DRRLIGGRIQ QIERRLAKVR RTREQGRKAR RKRELPVVSL VGYTNAGKST LFNHVTGSQR RAEDRLFATL DPSWRRVDLA RGSAAVVSDT VGFISRLPHD LVAAFRSTLE EVTDADLLLH VIDAGAEERE HQIEQVEAVL AELGADAVPT LRVYNKVDTC ALAPGRIEDD EGLVTGVRIS AATGEGVETL LEAVAERLGP ERIRRRVHLR PDQGRLRAQL FRLGCVIEEH CAEDGQLALE VELPVHELER LHVREGLPRG EVVPA // ID A1ZKR7_9BACT Unreviewed; 381 AA. AC A1ZKR7; DT 20-FEB-2007, integrated into UniProtKB/TrEMBL. DT 20-FEB-2007, sequence version 1. DT 07-JUN-2017, entry version 62. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=M23134_00036 {ECO:0000313|EMBL:EAY28883.1}; OS Microscilla marina ATCC 23134. OC Bacteria; Bacteroidetes; Cytophagia; Cytophagales; Microscillaceae; OC Microscilla. OX NCBI_TaxID=313606 {ECO:0000313|EMBL:EAY28883.1, ECO:0000313|Proteomes:UP000004095}; RN [1] {ECO:0000313|EMBL:EAY28883.1, ECO:0000313|Proteomes:UP000004095} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 23134 {ECO:0000313|EMBL:EAY28883.1, RC ECO:0000313|Proteomes:UP000004095}; RA Haygood M., Podell S., Anderson C., Hopkinson B., Roe K., Barbeau K., RA Gaasterland T., Ferriera S., Johnson J., Kravitz S., Beeson K., RA Sutton G., Rogers Y.-H., Friedman R., Frazier M., Venter J.C.; RL Submitted (JAN-2007) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EAY28883.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AAWS01000013; EAY28883.1; -; Genomic_DNA. DR RefSeq; WP_002696997.1; NZ_AAWS01000013.1. DR ProteinModelPortal; A1ZKR7; -. DR STRING; 313606.M23134_00036; -. DR EnsemblBacteria; EAY28883; EAY28883; M23134_00036. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000004095; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000004095}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000004095}. FT DOMAIN 202 368 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 381 AA; 43283 MW; E5F008109460E5BD CRC64; MKGPYSTTKS QETAVLVAVI RTNQTEEATQ AYLDELEFLA KTLGVKTLAN FTQRLETPDK KTFVRKGKLE EIHAVVEAEK ADMVIFDDDL NPSQVRNLER DLECKILDRS LLILDIFALR AKTAQAKTQV ELAQYQYVLP RLTNMWTHLS KQKGGIGMRG PGETELETDR RIIKDKITLL RKKLDKIDLQ NATRRKTRGQ QVRVALVGYT NVGKSTIMQL FSKADIYAKN ELFATVDSTV RKVVFNNIPF LLTDTVGFIR KLPTTLIESF KSTLDEVREA DILIHVADVS TSFCEEQIET VNKTLLEIDA IDKPTILVLN KIDLVDEMPA WVSSLEYDNT EVVVVSAQEK QGIDELKAKV LALVEEKFYK IFPNYTKDSQ F // ID A2SHA9_METPP Unreviewed; 414 AA. AC A2SHA9; DT 06-MAR-2007, integrated into UniProtKB/TrEMBL. DT 06-MAR-2007, sequence version 1. DT 07-JUN-2017, entry version 84. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Mpe_A1990 {ECO:0000313|EMBL:ABM94948.1}; OS Methylibium petroleiphilum (strain ATCC BAA-1232 / LMG 22953 / PM1). OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Methylibium. OX NCBI_TaxID=420662 {ECO:0000313|EMBL:ABM94948.1, ECO:0000313|Proteomes:UP000000366}; RN [1] {ECO:0000313|EMBL:ABM94948.1, ECO:0000313|Proteomes:UP000000366} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-1232 / LMG 22953 / PM1 RC {ECO:0000313|Proteomes:UP000000366}; RX PubMed=17158667; DOI=10.1128/JB.01259-06; RA Kane S.R., Chakicherla A.Y., Chain P.S.G., Schmidt R., Shin M.W., RA Legler T.C., Scow K.M., Larimer F.W., Lucas S.M., Richardson P.M., RA Hristova K.R.; RT "Whole-genome analysis of the methyl tert-butyl ether-degrading beta- RT proteobacterium Methylibium petroleiphilum PM1."; RL J. Bacteriol. 189:1931-1945(2007). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000555; ABM94948.1; -; Genomic_DNA. DR RefSeq; WP_011829585.1; NC_008825.1. DR ProteinModelPortal; A2SHA9; -. DR STRING; 420662.Mpe_A1990; -. DR EnsemblBacteria; ABM94948; ABM94948; Mpe_A1990. DR KEGG; mpt:Mpe_A1990; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000000366; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000000366}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000000366}. FT DOMAIN 201 375 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 414 AA; 44759 MW; 99B5C1A272EFD8A5 CRC64; MSASTAVNEA RAVLVGVDLG AGASFDATLD ELALLAESAG DTPVARLIAR RKAPDAALFL GSGKADELKA LVAESGGQCV IFDQALSPTQ QRNLERHLGV EVLDRTGLIL EIFAARAQSH EGKLQVELAQ LQYLSNRLVR RWTHLERQRG GVGHRGGPGE RQIELDRRMI GERIKALKAR LDKVKRQRGT QRRSRERAGT FRVSLIGYTN AGKSTLFNAL VKARSYAADQ LFATLDTTTR QLYLEDAQRS VSLSDTVGFI RDLPHTLVKA FAATLQEAAD ADLLLHVVDA SSPVLAEQRV EVERVLAEID AAGIPQILVY NKLDQLDEEQ RPRVLVDRLE LDGGRRIPRV FVSALRGVGL AELRALVSEA LLADGGEAGA PGASVSDAPV RDVADAAPSD HDPIPASVLL QRHA // ID A2TYV5_9FLAO Unreviewed; 414 AA. AC A2TYV5; DT 20-MAR-2007, integrated into UniProtKB/TrEMBL. DT 29-MAY-2013, sequence version 2. DT 07-JUN-2017, entry version 65. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:EAQ42613.2}; GN ORFNames=MED152_07825 {ECO:0000313|EMBL:EAQ42613.2}; OS Polaribacter sp. MED152. OC Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales; OC Flavobacteriaceae; Polaribacter. OX NCBI_TaxID=313598 {ECO:0000313|EMBL:EAQ42613.2, ECO:0000313|Proteomes:UP000006470}; RN [1] {ECO:0000313|EMBL:EAQ42613.2, ECO:0000313|Proteomes:UP000006470} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MED152 {ECO:0000313|EMBL:EAQ42613.2}; RX PubMed=17215843; DOI=10.1038/nature05381; RA Gomez-Consarnau L., Gonzalez J.M., Coll-Llado M., Gourdon P., RA Pascher T., Neutze R., Pedros-Alio C., Pinhassi J.; RT "Light stimulates growth of proteorhodopsin-containing marine RT Flavobacteria."; RL Nature 445:210-213(2007). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP004349; EAQ42613.2; -; Genomic_DNA. DR STRING; 313598.MED152_07825; -. DR EnsemblBacteria; EAQ42613; EAQ42613; MED152_07825. DR KEGG; pom:MED152_07825; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR KO; K03665; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000006470; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000006470}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000006470}. FT DOMAIN 211 396 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 414 AA; 47777 MW; 7B8013B33F9AB645 CRC64; MVSTFFLPLF SMIDQKEAIS EKAVLIGVIT QQQDETKSTE YLDELEFLTQ TAGGVVVKRF VQKMERPNPK TFLGAGKLED VKAYIQSNMI GTAIFDDELS PAQLRNIEKI LDCKILDRTN LILDIFAQRA QTSSAKTQVE LAQSEYLLPR LTRLWTHLDK QKGGIGMRGP GETEIETDRR IIRDKITLLK KRLKTIDKQM AVQRKNRGKM VRVALVGYTN VGKSTLMNVV SKSDVFAENK LFATLDTTVR KVVIKNIPFL MTDTVGFIRK LPTQLVESFK STLDEVREAD LLLHVVDISH PNFEDHIASV NSILTDIKCA DKPTLMVFNK IDAYQHETIE EDDLETEKGK EHYTLQDWKK TWMNDNEVES IFISALNKEN LEDFKEKTYE EVKKIHIQRF PYNDFLYYEY KEEE // ID A3CNS1_STRSV Unreviewed; 412 AA. AC A3CNS1; DT 20-MAR-2007, integrated into UniProtKB/TrEMBL. DT 20-MAR-2007, sequence version 1. DT 07-JUN-2017, entry version 81. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:ABN44826.1}; GN OrderedLocusNames=SSA_1432 {ECO:0000313|EMBL:ABN44826.1}; OS Streptococcus sanguinis (strain SK36). OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=388919 {ECO:0000313|EMBL:ABN44826.1, ECO:0000313|Proteomes:UP000002148}; RN [1] {ECO:0000313|EMBL:ABN44826.1, ECO:0000313|Proteomes:UP000002148} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SK36 {ECO:0000313|EMBL:ABN44826.1, RC ECO:0000313|Proteomes:UP000002148}; RX PubMed=17277061; DOI=10.1128/JB.01808-06; RA Xu P., Alves J.M., Kitten T., Brown A., Chen Z., Ozaki L.S., RA Manque P., Ge X., Serrano M.G., Puiu D., Hendricks S., Wang Y., RA Chaplin M.D., Akan D., Paik S., Peterson D.L., Macrina F.L., RA Buck G.A.; RT "Genome of the opportunistic pathogen Streptococcus sanguinis."; RL J. Bacteriol. 189:3166-3175(2007). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000387; ABN44826.1; -; Genomic_DNA. DR RefSeq; WP_011837131.1; NC_009009.1. DR RefSeq; YP_001035376.1; NC_009009.1. DR ProteinModelPortal; A3CNS1; -. DR STRING; 388919.SSA_1432; -. DR EnsemblBacteria; ABN44826; ABN44826; SSA_1432. DR GeneID; 4807722; -. DR KEGG; ssa:SSA_1432; -. DR PATRIC; fig|388919.9.peg.1358; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR Proteomes; UP000002148; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000002148}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000002148}. FT DOMAIN 199 359 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 158 192 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 412 AA; 46632 MW; B83675FBFFED10B5 CRC64; MIETEKKTER VFLVGVELAD TENFDLSMEE LQSLAKTAGA EVVGFYSQKR EKYDSKTFVG SGKLEEIRQM VDAEEISTVI VNNRLTPRQN VNLEESLGVK VIDRMQLILD IFAMRARSHE GKLQVHLAQL KYLLPRLVGQ GIMLSRQAGG IGSRGPGESQ LELNRRSVRN QIHDIERQLK AVEKNRATVR EKRLESSIFK IGLIGYTNAG KSTIMNCLTS KSQYEADELF ATLDATTKNI NLSGQLNVTL TDTVGFIQDL PTELVSSFKS TLEESKNVDL LVHVIDASDP HHEEHEKTVL DIMKELDMLD IPRLTLYNKA DKAEDFTPTL TPYSLISAKA DNSRALLQQV LLERMKELFL PFTIKVAPAK AYKIHDLEKV AIMGNREYID DVEVVSGWIA EKNKWKLEEF YD // ID A3DH59_CLOTH Unreviewed; 582 AA. AC A3DH59; DT 20-MAR-2007, integrated into UniProtKB/TrEMBL. DT 20-MAR-2007, sequence version 1. DT 07-JUN-2017, entry version 78. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Cthe_2081 {ECO:0000313|EMBL:ABN53288.1}; OS Clostridium thermocellum (strain ATCC 27405 / DSM 1237 / NBRC 103400 / OS NCIMB 10682 / NRRL B-4536 / VPI 7372) (Ruminiclostridium OS thermocellum). OC Bacteria; Firmicutes; Clostridia; Clostridiales; Ruminococcaceae; OC Ruminiclostridium. OX NCBI_TaxID=203119 {ECO:0000313|EMBL:ABN53288.1, ECO:0000313|Proteomes:UP000002145}; RN [1] {ECO:0000313|Proteomes:UP000002145} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 27405 / DSM 1237 / NBRC 103400 / NCIMB 10682 / NRRL B-4536 RC / VPI 7372 {ECO:0000313|Proteomes:UP000002145}; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., RA Pitluck S., Chertkov O., Brettin T., Bruce D., Han C., Tapia R., RA Gilna P., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., RA Mikhailova N., Wu J.H.D., Newcomb M., Richardson P.; RT "Complete sequence of Clostridium thermocellum ATCC 27405."; RL Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000568; ABN53288.1; -; Genomic_DNA. DR RefSeq; WP_020457705.1; NC_009012.1. DR ProteinModelPortal; A3DH59; -. DR STRING; 203119.Cthe_2081; -. DR EnsemblBacteria; ABN53288; ABN53288; Cthe_2081. DR KEGG; cth:Cthe_2081; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; EREVIIT; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000002145; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000002145}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000002145}. FT DOMAIN 359 524 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 318 352 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 582 AA; 64507 MW; D2A3D36114D0B973 CRC64; MQGAKDEFLP AGLAVKMAEL TGKINREIAV YINRKGNIID VSVGDSSTVS LPEVEGRKDL ARLVGVRCIH THPNGEGMVS LVDLNSLVKM RLDAMVAVGV KDGRITEIYA ALPVRDENGN LGKTTVYGPF GKDDKRMNRL WDIILETDKL KSTVVHLNES DEERAVLVGL ETSSKVIVGG KSEGERSLDE LEELARTAGA VVLEKIIQRR PAKDPAFFIG RGKVEELSLI CQALDANLII FDDELSGVQM RNIEEMTGVK VVDRTTLILD IFAKRARSRE GKLQVELAQL KYRVSRLVGL GTQLSRLGGG IGTRGPGEKK LEVDRRHIKR RISFLEAQLK DVEKRRNSFR ESRTRNAIPT IALVGYTNAG KSTLMNRLCE SNVLAEDKLF ATLDPTTRSF RLSDGREALL IDTVGFIRKL PHELVEAFKS TLEEAVYADM LIHVVDASNE EAEEQVKVVN DILESLGAAN KPVIMALNKM DMVKGGLRLA ISNPNGRIFE ISAVTGQGID AMLEGIREML PEDEKEVRLF IPYSDGWVIS YIYQNGRILE QVHGESGTEV KALIKKHRLK PVRAYICGKY PV // ID A3DN05_STAMF Unreviewed; 368 AA. AC A3DN05; DT 20-MAR-2007, integrated into UniProtKB/TrEMBL. DT 20-MAR-2007, sequence version 1. DT 07-JUN-2017, entry version 78. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Smar_0916 {ECO:0000313|EMBL:ABN70015.1}; OS Staphylothermus marinus (strain ATCC 43588 / DSM 3639 / JCM 9404 / OS F1). OC Archaea; Crenarchaeota; Thermoprotei; Desulfurococcales; OC Desulfurococcaceae; Staphylothermus. OX NCBI_TaxID=399550 {ECO:0000313|EMBL:ABN70015.1, ECO:0000313|Proteomes:UP000000254}; RN [1] {ECO:0000313|Proteomes:UP000000254} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43588 / DSM 3639 / JCM 9404 / F1 RC {ECO:0000313|Proteomes:UP000000254}; RX PubMed=19341479; DOI=10.1186/1471-2164-10-145; RA Anderson I.J., Dharmarajan L., Rodriguez J., Hooper S., Porat I., RA Ulrich L.E., Elkins J.G., Mavromatis K., Sun H., Land M., Lapidus A., RA Lucas S., Barry K., Huber H., Zhulin I.B., Whitman W.B., RA Mukhopadhyay B., Woese C., Bristow J., Kyrpides N.; RT "The complete genome sequence of Staphylothermus marinus reveals RT differences in sulfur metabolism among heterotrophic Crenarchaeota."; RL BMC Genomics 10:145-145(2009). RN [2] {ECO:0000313|Proteomes:UP000000254} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43588 / DSM 3639 / JCM 9404 / F1 RC {ECO:0000313|Proteomes:UP000000254}; RX PubMed=21304655; DOI=10.4056/sigs.30527; RA Anderson I.J., Sun H., Lapidus A., Copeland A., Glavina Del Rio T., RA Tice H., Dalin E., Lucas S., Barry K., Land M., Richardson P., RA Huber H., Kyrpides N.C.; RT "Complete genome sequence of Staphylothermus marinus Stetter and Fiala RT 1986 type strain F1."; RL Stand. Genomic Sci. 1:183-188(2009). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000575; ABN70015.1; -; Genomic_DNA. DR RefSeq; WP_011839206.1; NC_009033.1. DR ProteinModelPortal; A3DN05; -. DR STRING; 399550.Smar_0916; -. DR EnsemblBacteria; ABN70015; ABN70015; Smar_0916. DR GeneID; 4906592; -. DR KEGG; smr:Smar_0916; -. DR eggNOG; arCOG00353; Archaea. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG093Z07D6; -. DR Proteomes; UP000000254; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000000254}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000000254}. FT DOMAIN 179 353 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 368 AA; 42807 MW; 471DD103236DA882 CRC64; MSVDVVIPYK YRKFLDEELS LIKTVYPEIN EVVMIRKPNS KYYLTLNKID IVKNSSSQKI ILMDRAKPSQ IINLMRETRK EIIDRILLIL EIFAQHAGSK EAKLQIELAK LKHQLPLIKE TIRYAKLGEL HGFLGAGRYG YEKYYRMMRE REARIRRELE KLRSIRSRRR EHRRQMGYPH ISIVGYTCAG KTTLFNRLTH NLKPAGPEPF TTLSPKSSAI IIDGLKMILT DTVGFIRDLP HEIIEAFYAT LEEIIDSNII IHVIDASKSS EAIIKEMVET RRIFERIGVH GIPIIIALNK IDLLNSEEEI MDKIRLVEKY IDGNNVIVPI SAINGKNIRY LLNVLKEIIR GYSIENLRSK IWSQTRQR // ID A3HU64_9BACT Unreviewed; 422 AA. AC A3HU64; DT 03-APR-2007, integrated into UniProtKB/TrEMBL. DT 03-APR-2007, sequence version 1. DT 07-JUN-2017, entry version 62. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=ALPR1_00555 {ECO:0000313|EMBL:EAZ81686.1}; OS Algoriphagus machipongonensis. OC Bacteria; Bacteroidetes; Cytophagia; Cytophagales; Cyclobacteriaceae; OC Algoriphagus. OX NCBI_TaxID=388413 {ECO:0000313|EMBL:EAZ81686.1, ECO:0000313|Proteomes:UP000003919}; RN [1] {ECO:0000313|EMBL:EAZ81686.1, ECO:0000313|Proteomes:UP000003919} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=PR1 {ECO:0000313|EMBL:EAZ81686.1}; RX PubMed=21183675; DOI=10.1128/JB.01421-10; RA Alegado R.A., Ferriera S., Nusbaum C., Young S.K., Zeng Q., RA Imamovic A., Fairclough S.R., King N.; RT "Complete genome sequence of Algoriphagus sp. PR1, bacterial prey of a RT colony-forming choanoflagellate."; RL J. Bacteriol. 193:1485-1486(2011). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EAZ81686.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AAXU02000001; EAZ81686.1; -; Genomic_DNA. DR RefSeq; WP_008197662.1; NZ_CM001023.1. DR ProteinModelPortal; A3HU64; -. DR STRING; 388413.ALPR1_00555; -. DR EnsemblBacteria; EAZ81686; EAZ81686; ALPR1_00555. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000003919; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 2. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000003919}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000003919}. FT DOMAIN 210 399 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 171 198 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 422 AA; 48626 MW; 1876ECA276E1C764 CRC64; MGKFSRKLQK LYDTAPKIDT AVLVSIVRQG QTEMEIDEHL DELAFLTETL GAKTVYRFTQ KMEKPDIRTF IGSGKLDEIK AYIEHFEVDM VIFDDDLSPS QMRNLENEMK VKIYDRSLLI LDIFLNRAQT AQAKTQVELA RFQYLLPRLT RMWTHLERQR GGTSTRGGAG EKEIETDKRD IRNKITLLKQ KLREIEKQGV TQRKGRKGIV RVALVGYTNV GKSTLMNLVT KTDILAENKL FATVDSTVRK VVLERVPFLL SDTVGFIRKL PTHLIEAFKS TLDEIREADL LVHVVDISHP NFEDHISVVN QTLREINAGD KPILLVFNKI DLVEQMPSEE AIMNMTELEL EESNYLDFAS LSDAYEKKTE IKPVFMAANS GLHVDEFRES LITEVKKAHR KIYPHYLEDE TVDWESKAYE ED // ID A3J318_9FLAO Unreviewed; 407 AA. AC A3J318; DT 03-APR-2007, integrated into UniProtKB/TrEMBL. DT 03-APR-2007, sequence version 1. DT 07-JUN-2017, entry version 47. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=FBBAL38_05020 {ECO:0000313|EMBL:EAZ96757.1}; OS Flavobacteria bacterium BAL38. OC Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales. OX NCBI_TaxID=391598 {ECO:0000313|EMBL:EAZ96757.1, ECO:0000313|Proteomes:UP000003784}; RN [1] {ECO:0000313|EMBL:EAZ96757.1, ECO:0000313|Proteomes:UP000003784} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BAL38 {ECO:0000313|EMBL:EAZ96757.1, RC ECO:0000313|Proteomes:UP000003784}; RA Hagstrom A., Ferriera S., Johnson J., Kravitz S., Beeson K., RA Sutton G., Rogers Y.-H., Friedman R., Frazier M., Venter J.C.; RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EAZ96757.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AAXX01000001; EAZ96757.1; -; Genomic_DNA. DR RefSeq; WP_008255275.1; NZ_AAXX01000001.1. DR ProteinModelPortal; A3J318; -. DR STRING; 391598.FBBAL38_05020; -. DR EnsemblBacteria; EAZ96757; EAZ96757; FBBAL38_05020. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000003784; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000003784}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000003784}. FT DOMAIN 200 386 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 407 AA; 47006 MW; 4B6069EDB53EDF58 CRC64; MLEKEVIDFE KSIIVGIVTQ NQSEEKLNEY LDELEFLTFT AGGTVVKRFS QKMDKPNPKT FVGTGKLEEI KYYIKDNDIK TVIFDDELTP SQSKNITKEL DCKVLDRTNL ILDIFAQRAE TSYARTQVEL AQCQYLLPRL TGMWTHLERQ KGGIGMRGPG ETEIETDRRI VRDRISLLKE KIKVIDKQMA TQRSNRGAMV RVALVGYTNV GKSTLMNAVG KSDVFVENKL FATLDTTVRK TVIKNLPFLL SDTVGFIRKL PTQLVESFKS TLDEVREADL LLHVVDISHP EFEEHIASVN KILLDIKSAD KPTIMVFNKI DAYHPVYFDE NDLSIEKTTK HYTLEEWQNT WMSKLGENNT LFISATEKAN FEEFREKVYE AVREIHITRF PYNKFLYPDY KDAIENE // ID A3JTN8_9RHOB Unreviewed; 390 AA. AC A3JTN8; DT 03-APR-2007, integrated into UniProtKB/TrEMBL. DT 03-APR-2007, sequence version 1. DT 07-JUN-2017, entry version 51. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=RB2150_02949 {ECO:0000313|EMBL:EBA02888.1}; OS Rhodobacteraceae bacterium HTCC2150. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae. OX NCBI_TaxID=388401 {ECO:0000313|EMBL:EBA02888.1, ECO:0000313|Proteomes:UP000004731}; RN [1] {ECO:0000313|EMBL:EBA02888.1, ECO:0000313|Proteomes:UP000004731} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=HTCC2150 {ECO:0000313|EMBL:EBA02888.1, RC ECO:0000313|Proteomes:UP000004731}; RX PubMed=20889754; DOI=10.1128/JB.01088-10; RA Kang I., Oh H.M., Vergin K.L., Giovannoni S.J., Cho J.C.; RT "Genome sequence of the marine alphaproteobacterium HTCC2150, assigned RT to the Roseobacter clade."; RL J. Bacteriol. 192:6315-6316(2010). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EBA02888.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AAXZ01000005; EBA02888.1; -; Genomic_DNA. DR ProteinModelPortal; A3JTN8; -. DR STRING; 388401.RB2150_02949; -. DR EnsemblBacteria; EBA02888; EBA02888; RB2150_02949. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000004731; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000004731}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000004731}. FT DOMAIN 170 343 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 390 AA; 43308 MW; 8149C83EA862B403 CRC64; MSLARALPQL DVLGNTHVRL PKAQPGTLFG KGKIEELKGM FKAAEVELVV IDGPVSPVQQ RNLEKEWNVK ILDRTGLILE IFSDRARTRE GVLQVEMAAL SYQKTRLVRA WTHLERQRGG LGFVGGPGET QIESDRRALD EAIIRIRRQL EKTVKTRELH RAARKKVPYP VVALVGYTNA GKSTFFNHLT GAKVFAKDML FATLDPTMRA VNLPNGLDVI LSDTVGFISD LPTELVAAFR ATLEDALSAD LILHVRDIAH PETESQAGNV RTILSSLGIG HETPQIEIWN KTDLLNEEDA GRVAALAERK EDVFGVSSIT GDGMEVLLAA IKAKLDDERS TDILSLPFSA GQKRAWLFQE DVVQVEDQDE NGFKLTVSWT QRQKERFDAL // ID A3K6E5_9RHOB Unreviewed; 396 AA. AC A3K6E5; DT 03-APR-2007, integrated into UniProtKB/TrEMBL. DT 03-APR-2007, sequence version 1. DT 07-JUN-2017, entry version 49. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=SSE37_06649 {ECO:0000313|EMBL:EBA07295.1}; OS Sagittula stellata E-37. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae; Sagittula. OX NCBI_TaxID=388399 {ECO:0000313|EMBL:EBA07295.1, ECO:0000313|Proteomes:UP000005713}; RN [1] {ECO:0000313|EMBL:EBA07295.1, ECO:0000313|Proteomes:UP000005713} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=E-37 {ECO:0000313|EMBL:EBA07295.1, RC ECO:0000313|Proteomes:UP000005713}; RA Moran M.A., Ferriera S., Johnson J., Kravitz S., Beeson K., Sutton G., RA Rogers Y.-H., Friedman R., Frazier M., Venter J.C.; RL Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EBA07295.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AAYA01000010; EBA07295.1; -; Genomic_DNA. DR ProteinModelPortal; A3K6E5; -. DR STRING; 388399.SSE37_06649; -. DR EnsemblBacteria; EBA07295; EBA07295; SSE37_06649. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000005713; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000005713}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000005713}. FT DOMAIN 176 345 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 396 AA; 43807 MW; 46418BF4F9A80A39 CRC64; MALEEAVSLA RALPDLEVVG ETVVPLRDPH PGMLFGSGKI SELKELILEN EVELVLVDGP VTPVQQRNLE REWKVKLLDR TGLILEIFSD RAATREGVLQ VEMAALSYQR TRLVRAWTHL ERQRGGLGFV GGPGETQIEA DRRAIDEQLV RLRRQLEKVV KTRELHRKAR AKVPYPIVAL VGYTNAGKST LFNRLTGAEV MAKDMLFATL DPTMRAVRLP TGADVILSDT VGFISDLPTE LVAAFRATLE EVLAADVIVH VRDISHPETD AQAEDVRTIL DGLGVDEGTP QIELWNKIDR LSGDVKVATE ARADRDAGIF AVSAVTGEGL DGFLDAVTEA LGEERRTEAL TLAFDEGRKR AWLFEKGLVE DERQTEDGYA LTVTWSARDR ARFGQL // ID A3N3Q0_ACTP2 Unreviewed; 407 AA. AC A3N3Q0; DT 03-APR-2007, integrated into UniProtKB/TrEMBL. DT 03-APR-2007, sequence version 1. DT 30-AUG-2017, entry version 73. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:ABN75036.1}; GN OrderedLocusNames=APL_1962 {ECO:0000313|EMBL:ABN75036.1}; OS Actinobacillus pleuropneumoniae serotype 5b (strain L20). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Actinobacillus. OX NCBI_TaxID=416269 {ECO:0000313|EMBL:ABN75036.1, ECO:0000313|Proteomes:UP000001432}; RN [1] {ECO:0000313|EMBL:ABN75036.1, ECO:0000313|Proteomes:UP000001432} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=L20 {ECO:0000313|EMBL:ABN75036.1, RC ECO:0000313|Proteomes:UP000001432}; RX PubMed=18065534; DOI=10.1128/JB.01845-07; RA Foote S.J., Bosse J.T., Bouevitch A.B., Langford P.R., Young N.M., RA Nash J.H.; RT "The complete genome sequence of Actinobacillus pleuropneumoniae L20 RT (serotype 5b)."; RL J. Bacteriol. 190:1495-1496(2008). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000569; ABN75036.1; -; Genomic_DNA. DR ProteinModelPortal; A3N3Q0; -. DR STRING; 416269.APL_1962; -. DR EnsemblBacteria; ABN75036; ABN75036; APL_1962. DR KEGG; apl:APL_1962; -. DR PATRIC; fig|416269.6.peg.2044; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR Proteomes; UP000001432; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000001432}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000001432}. FT DOMAIN 172 339 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 138 165 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 407 AA; 45639 MW; C279D665F037A835 CRC64; MEFQTLAESA GVEILATLTT SRSAPHIKYF VGQGKADEIA QAVKDLEATV VLVNHELSPS QTRNLQALCE CRVVDRTGLI LDIFAQRARS HEGKLQVELA QLKHLATRLV RRLGNQDQQK GGAVGLRGPG ETQLETDRRL IKVRIQQLQN RLEKVNKQRS QNRKTRQKAD IPTVSLVGYT NAGKSTLFNA ITNAGVYAAD QLFATLDPTL RRMQIQDVGT TILADTVGFI RFLPHDLVSA FKSTLQETTE ASLLLHVIDA ADDRKNENID AVNQVLDEIG ALDIPTLLVY NKVDKLEGIV PHIERNDDGK PVAVYLSAQA NQGIDLLYEA IRECLRNELV CEKVLLPATA GQIYTQLHLQ HCIKNESFNQ FGDRLVEVEV DLVQWNKWLK QFPELTEYIE FASWEEN // ID A3QAE1_SHELP Unreviewed; 432 AA. AC A3QAE1; DT 17-APR-2007, integrated into UniProtKB/TrEMBL. DT 17-APR-2007, sequence version 1. DT 30-AUG-2017, entry version 69. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Shew_0567 {ECO:0000313|EMBL:ABO22439.1}; OS Shewanella loihica (strain ATCC BAA-1088 / PV-4). OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales; OC Shewanellaceae; Shewanella. OX NCBI_TaxID=323850 {ECO:0000313|EMBL:ABO22439.1, ECO:0000313|Proteomes:UP000001558}; RN [1] {ECO:0000313|EMBL:ABO22439.1, ECO:0000313|Proteomes:UP000001558} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-1088 / PV-4 {ECO:0000313|Proteomes:UP000001558}; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., RA Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., RA Romine M.F., Serres G., Fredrickson J., Tiedje J., Richardson P.; RT "Complete sequence of Shewanella loihica PV-4."; RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000606; ABO22439.1; -; Genomic_DNA. DR RefSeq; WP_011864373.1; NC_009092.1. DR ProteinModelPortal; A3QAE1; -. DR STRING; 323850.Shew_0567; -. DR EnsemblBacteria; ABO22439; ABO22439; Shew_0567. DR KEGG; slo:Shew_0567; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000001558; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000001558}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000001558}. FT DOMAIN 198 364 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 432 AA; 48363 MW; 93119810685087A5 CRC64; MFERYEAGEA AVLVHIDFSD EDSREDITEL RLLVESAGAE TVGVITGSRR SPDRKYFVGT GKAEELAAMV AATDANVVIF NHALSPAQER NLELICQCRV LDRTTLILDI FAQRARTYEG KLQVELAQLR HMSTRLIRGW THLERQKGGI GLRGPGETQL ETDRRLLRGR IKTINKRLEK VDKQREQSRR ARQRSELATV SLVGYTNAGK STLFNALTVS EVYAADQLFA TLDPTLRKLD LQDGSVILAD TVGFIRHLPH DLVAAFKATL QETREADLLL HVVDSADENM GDNFEQVQLV LKEIGAEEIP QLIVCNKIDL LEDVGPKIDY DGDGVPIRVW VSAQQSLGLD LLEKAINQLV GRAILELTLR IPATAGHYLG QFYRLDVIQQ KEYDDLGNCI LSVRLLEADW HRLAKQSQGE LETFIVETAA IE // ID A3SPW4_ROSNI Unreviewed; 425 AA. AC A3SPW4; DT 03-APR-2007, integrated into UniProtKB/TrEMBL. DT 03-APR-2007, sequence version 1. DT 07-JUN-2017, entry version 46. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=ISM_16600 {ECO:0000313|EMBL:EAP76504.1}; OS Roseovarius nubinhibens (strain ATCC BAA-591 / DSM 15170 / ISM). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae; Roseovarius. OX NCBI_TaxID=89187 {ECO:0000313|EMBL:EAP76504.1, ECO:0000313|Proteomes:UP000005954}; RN [1] {ECO:0000313|EMBL:EAP76504.1, ECO:0000313|Proteomes:UP000005954} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-591 / DSM 15170 / ISM RC {ECO:0000313|Proteomes:UP000005954}; RA Moran M.A., Ferriera S., Johnson J., Kravitz S., Halpern A., RA Remington K., Beeson K., Tran B., Rogers Y.-H., Friedman R., RA Venter J.C.; RL Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EAP76504.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AALY01000002; EAP76504.1; -; Genomic_DNA. DR RefSeq; WP_009815329.1; NZ_CH724156.1. DR ProteinModelPortal; A3SPW4; -. DR STRING; 89187.ISM_16600; -. DR EnsemblBacteria; EAP76504; EAP76504; ISM_16600. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000005954; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000005954}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000005954}. FT DOMAIN 204 374 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 425 AA; 46958 MW; C5055A90325BC176 CRC64; MTSHDPAVTR AWVLHPDIYG QNDDRDPKRA LEEAVALGVA LPGLDVVGSE IVRLPKPHPG ALFGSGKIEE LKARLEANEV DLVLIDGPVT PVQQRNLEKA WGLKLLDRTG LILEIFSDRA ATREGVLQVE MAALSYQRTR LVRAWTHLER QRGGLGFVGG PGETQIEADR RAIDDQLVRL RRQLEKVVKT RTLHRAARAK VPFPIVALVG YTNAGKSTLF NRLTGSDVMA KDMLFATLDP TMRKVSLPHG GPDVILSDTV GFISDLPTEL VAAFRATLEE VVSADLVVHV RDISHPETEE QARDVEAILE SLDVAEGTPR IELWNKADLL DPEARETFAN QAARREEVIL VSAVSGEGME AFVDQATEAL SGVQHEATIT LGFGEGRRRA WLFDQGVVEA ERQTDEGWEF DLRWTARQAG QFQDL // ID A3TXM2_PSEBH Unreviewed; 424 AA. AC A3TXM2; DT 03-APR-2007, integrated into UniProtKB/TrEMBL. DT 03-APR-2007, sequence version 1. DT 07-JUN-2017, entry version 60. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=OB2597_03142 {ECO:0000313|EMBL:EAQ03582.1}; OS Pseudooceanicola batsensis (strain ATCC BAA-863 / DSM 15984 / KCTC OS 12145 / HTCC2597) (Oceanicola batsensis). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae; Pseudooceanicola. OX NCBI_TaxID=252305 {ECO:0000313|EMBL:EAQ03582.1, ECO:0000313|Proteomes:UP000004318}; RN [1] {ECO:0000313|EMBL:EAQ03582.1, ECO:0000313|Proteomes:UP000004318} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-863 / DSM 15984 / KCTC 12145 / HTCC2597 RC {ECO:0000313|Proteomes:UP000004318}; RX PubMed=20418400; DOI=10.1128/JB.00412-10; RA Thrash J.C., Cho J.C., Vergin K.L., Giovannoni S.J.; RT "Genome sequences of Oceanicola granulosus HTCC2516(T) and Oceanicola RT batsensis HTCC2597(TDelta)."; RL J. Bacteriol. 192:3549-3550(2010). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EAQ03582.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AAMO01000004; EAQ03582.1; -; Genomic_DNA. DR RefSeq; WP_009804881.1; NZ_CH724131.1. DR ProteinModelPortal; A3TXM2; -. DR STRING; 252305.OB2597_03142; -. DR EnsemblBacteria; EAQ03582; EAQ03582; OB2597_03142. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000004318; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000004318}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000004318}. FT DOMAIN 204 373 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 424 AA; 47101 MW; 319F1F89FE1151FE CRC64; MIPRDRPDTR AWVLHPDLLG EDRRHAAEFA LEEAVSLARA LPGLEVVGSS IVRLANPTPA TLFGSGKVAE LSAFFADNKV ELVLVDGPVT PVQQRNLEKA WGGKLLDRTG LILEIFSDRA RTREGVLQVE MAALAYQRTR LVRAWTHLER QRGGLGFVGG PGETQIEADR RAIDEQLTRL RRQLEKVVRT RELHRAARAR VPFPIVALVG YTNAGKSTLF NRLTGAEVLA KDMLFATLDP TMRRVRLPNN GPEVILSDTV GFISDLPTQL VAAFRATLEE VLEADLILHI RDISHPEAEE QKADVEDILS DLGLPEEVPV LEVWNKVDRL PPEDAGALAR RAERDGTFVI SAVTGAGLDP LLDAVERTLD QGSVTEELTL GFDEGRRRAW LYEQGLVVEE TQGEEGHRIT VRWSPRQSAR FRSL // ID A3U6X5_CROAH Unreviewed; 407 AA. AC A3U6X5; DT 03-APR-2007, integrated into UniProtKB/TrEMBL. DT 03-APR-2007, sequence version 1. DT 07-JUN-2017, entry version 66. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=CA2559_04515 {ECO:0000313|EMBL:EAP87992.1}; OS Croceibacter atlanticus (strain ATCC BAA-628 / HTCC2559 / KCTC 12090). OC Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales; OC Flavobacteriaceae; Croceibacter. OX NCBI_TaxID=216432 {ECO:0000313|EMBL:EAP87992.1, ECO:0000313|Proteomes:UP000002297}; RN [1] {ECO:0000313|EMBL:EAP87992.1, ECO:0000313|Proteomes:UP000002297} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-628 / HTCC2559 / KCTC 12090 RC {ECO:0000313|Proteomes:UP000002297}; RX PubMed=20639333; DOI=10.1128/JB.00733-10; RA Oh H.M., Kang I., Ferriera S., Giovannoni S.J., Cho J.C.; RT "The complete genome sequence of Croceibacter atlanticus HTCC2559T."; RL J. Bacteriol. 192:4796-4797(2010). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002046; EAP87992.1; -; Genomic_DNA. DR RefSeq; WP_013186668.1; NC_014230.1. DR ProteinModelPortal; A3U6X5; -. DR STRING; 216432.CA2559_04515; -. DR EnsemblBacteria; EAP87992; EAP87992; CA2559_04515. DR KEGG; cat:CA2559_04515; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000002297; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000002297}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000002297}. FT DOMAIN 200 385 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 407 AA; 47196 MW; C2E996334A0CFCD0 CRC64; MLEKNTTEYE SAVLIGVITQ LQDEEQSKEY LDELEFLTYT AGGEVLKRFT QKLEHPNPKT FINSGKLETV RQFIEEHEVG SAIFDDELSP AQQKNLERIL KCKVVDRTYL ILDIFAQRAT TSYARTQVEL AQYEYLLPRL VGLWTHLERQ RGGIGMRGPG ETEIETDRRI VRDKISLLKN KIKKIDKQME VQRGNRGQLV RVALVGYTNV GKSTLMNAIS KSEVFAENKL FATLDTTVRK VVIRNLPFLL TDTVGFIRKL PTQLVESFKS TLDEVREADL LLHVVDISHH NFEEHIASVN QILDEIDSAD KPSIMVFNKI DAYEPETIDE DDLDTEKTTK HNTLEDWKKT WMNRTEYGSL FISALNKDNF DELRKTVYNA VREIHVTRFP YNSFLYPEYD DDFNEQQ // ID A3UCL6_9RHOB Unreviewed; 443 AA. AC A3UCL6; DT 03-APR-2007, integrated into UniProtKB/TrEMBL. DT 03-APR-2007, sequence version 1. DT 07-JUN-2017, entry version 50. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=OA2633_02446 {ECO:0000313|EMBL:EAP90997.1}; OS Oceanicaulis sp. HTCC2633. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Hyphomonadaceae; Oceanicaulis. OX NCBI_TaxID=314254 {ECO:0000313|EMBL:EAP90997.1, ECO:0000313|Proteomes:UP000006011}; RN [1] {ECO:0000313|EMBL:EAP90997.1, ECO:0000313|Proteomes:UP000006011} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=HTCC2633 {ECO:0000313|EMBL:EAP90997.1, RC ECO:0000313|Proteomes:UP000006011}; RX PubMed=21036991; DOI=10.1128/JB.01267-10; RA Oh H.M., Kang I., Vergin K.L., Lee K., Giovannoni S.J., Cho J.C.; RT "Genome sequence of Oceanicaulis sp. strain HTCC2633, isolated from RT the Western Sargasso Sea."; RL J. Bacteriol. 193:317-318(2011). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EAP90997.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AAMQ01000001; EAP90997.1; -; Genomic_DNA. DR RefSeq; WP_009800893.1; NZ_CH672428.1. DR ProteinModelPortal; A3UCL6; -. DR STRING; 314254.OA2633_02446; -. DR EnsemblBacteria; EAP90997; EAP90997; OA2633_02446. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000006011; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000006011}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000006011}. FT DOMAIN 202 378 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 168 195 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 443 AA; 48648 MW; 8A83F950DD904B76 CRC64; MIDRKPAPQT ALVLSPQYPG TDANRAQARL EEAIGLAQAL DLVTAEARIE PLRRVEASGF FGTGKIAQIA ERVKDAEITV VIIDAALSPI QQRNLEKKLN AKVIDRTGLI LEIFGLRAQT REGRLQVELA RLAYERSRLV RTWTHLERQR GGRGFLAGPG ETQIETDRRI LADKMAKLRR ELDEVKRTRS LHRKKRQTAP WPTVALVGYT NAGKSTLFNL LSDAQVLAKD MPFATLDPTV RGVKLPSGRR VLMSDTVGFI TDLPTELIAA FRATLEEVIE ADVLIHVRDM ADPDHEGRKA DVESVLAALG AGAEADQHVI EAWNKADQLS AEDHEELVWR AKLPKRDNGP VSIVTSAVTG AGVDALLEQV ELALSVDDVA LRLEFGPSDA EALAFVHRHG AILSETTDRD TGVVSVHVRL SEADAGRFNQ RYGVFEEADS LAD // ID A3V661_9RHOB Unreviewed; 424 AA. AC A3V661; DT 03-APR-2007, integrated into UniProtKB/TrEMBL. DT 03-APR-2007, sequence version 1. DT 07-JUN-2017, entry version 48. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=SKA53_04838 {ECO:0000313|EMBL:EAQ06385.1}; OS Loktanella vestfoldensis SKA53. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae; Loktanella. OX NCBI_TaxID=314232 {ECO:0000313|EMBL:EAQ06385.1, ECO:0000313|Proteomes:UP000004507}; RN [1] {ECO:0000313|EMBL:EAQ06385.1, ECO:0000313|Proteomes:UP000004507} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SKA53 {ECO:0000313|EMBL:EAQ06385.1, RC ECO:0000313|Proteomes:UP000004507}; RA Hagstrom A., Ferriera S., Johnson J., Kravitz S., Halpern A., RA Remington K., Beeson K., Tran B., Rogers Y.-H., Friedman R., RA Venter J.C.; RL Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EAQ06385.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AAMS01000005; EAQ06385.1; -; Genomic_DNA. DR ProteinModelPortal; A3V661; -. DR STRING; 314232.SKA53_04838; -. DR EnsemblBacteria; EAQ06385; EAQ06385; SKA53_04838. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000004507; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000004507}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000004507}. FT DOMAIN 204 373 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 424 AA; 46797 MW; 57BAE6B16296D77F CRC64; MLEHDKPVTR AWVLHPELKS DHSRRAPVPA LAEAVALAAA LPDLDVLGAD IVRLPKLHAG KLFGKGKIEE LRIIFAEAEV ELVLVDGSVT PVQQRNLEKA WGVKLLDRTG LILEIFSDRA RTSEGVLQVE MAALSYQRTR LVRAWTHLER QRGGLGFVGG PGETQIEADR RAIDDQLVRL RRQLEKVGKT RALHRASRAK VPFPIVALVG YTNAGKSTLF NMLTGADVLA KDMLFATLDP TMRKITLPTG DEVIMSDTVG FISDLPTELV AAFRATLEEV LDADLILHIR DISHDQTEEQ ACDVMAILHK LGVAENAPLI EVWNKVDLLQ GEAFEGRVNQ AARTEDLFAV SALTGEGMAA LLAAIPEKLK DPRSEALLTL SFAEGRKRAW LFEAGIVTDD QQTDEGYCMT VVWTALQQER FSRL // ID A3VDV8_9RHOB Unreviewed; 427 AA. AC A3VDV8; DT 03-APR-2007, integrated into UniProtKB/TrEMBL. DT 03-APR-2007, sequence version 1. DT 07-JUN-2017, entry version 58. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=RB2654_03249 {ECO:0000313|EMBL:EAQ13697.1}; OS Maritimibacter alkaliphilus HTCC2654. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae; Maritimibacter. OX NCBI_TaxID=314271 {ECO:0000313|EMBL:EAQ13697.1, ECO:0000313|Proteomes:UP000002931}; RN [1] {ECO:0000313|EMBL:EAQ13697.1, ECO:0000313|Proteomes:UP000002931} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=HTCC2654 {ECO:0000313|EMBL:EAQ13697.1, RC ECO:0000313|Proteomes:UP000002931}; RX PubMed=20729358; DOI=10.1128/JB.00873-10; RA Thrash J.C., Cho J.C., Ferriera S., Johnson J., Vergin K.L., RA Giovannoni S.J.; RT "Genome sequences of Pelagibaca bermudensis HTCC2601T and RT Maritimibacter alkaliphilus HTCC2654T, the type strains of two marine RT Roseobacter genera."; RL J. Bacteriol. 192:5552-5553(2010). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EAQ13697.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AAMT01000004; EAQ13697.1; -; Genomic_DNA. DR RefSeq; WP_008328668.1; NZ_CH902578.1. DR ProteinModelPortal; A3VDV8; -. DR STRING; 314271.RB2654_03249; -. DR EnsemblBacteria; EAQ13697; EAQ13697; RB2654_03249. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000002931; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000002931}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000002931}. FT DOMAIN 205 374 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 427 AA; 47139 MW; BA066363D286FDE4 CRC64; MEPTGEPGAT RAWVIHPELT SDQERRDAGP ALEEAVSLAL ALPGLEVVGS QIVRLPKPHP GHLFGTGKTD ELAALLKANE IELVLIDGPV SPVQQRNLER EWKVKILDRT GLILEIFSDR AATREGVLQV EMAALSYQRT RLVRAWTHLE RQRGGLGFVG GPGETQIEAD RRAIDEQLTR LRKQLAKVVK TRELRRAARA KVPFPVVALV GYTNAGKSTL FNRMTGAEVM AKDMLFATLD PTMRGVDLPG GRTVILSDTV GFISDLPTQL VAAFRATLEE VLGADLILHV RDIAHDETQE QAEDVLAILE DLGVDEDVPL IEVWNKIDKL DDQTRAAYLT QADRTDEVVA MSAWTGEGVD ALYPAIDAAL SVETREEDLL IPFSEGRKRA SLHETGVVLD EVQTEDGWEI TVRWTDKQAN QFHKSHA // ID A3WC60_9SPHN Unreviewed; 432 AA. AC A3WC60; DT 03-APR-2007, integrated into UniProtKB/TrEMBL. DT 03-APR-2007, sequence version 1. DT 07-JUN-2017, entry version 47. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=NAP1_05520 {ECO:0000313|EMBL:EAQ30210.1}; OS Erythrobacter sp. NAP1. OC Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales; OC Erythrobacteraceae; Erythrobacter. OX NCBI_TaxID=237727 {ECO:0000313|EMBL:EAQ30210.1, ECO:0000313|Proteomes:UP000002995}; RN [1] {ECO:0000313|EMBL:EAQ30210.1, ECO:0000313|Proteomes:UP000002995} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NAP1 {ECO:0000313|EMBL:EAQ30210.1, RC ECO:0000313|Proteomes:UP000002995}; RX PubMed=21952547; DOI=10.1128/JB.05845-11; RA Koblizek M., Janouskovec J., Obornik M., Johnson J.H., Ferriera S., RA Falkowski P.G.; RT "Genome Sequence of the Marine Photoheterotrophic Bacterium RT Erythrobacter sp. Strain NAP1."; RL J. Bacteriol. 193:5881-5882(2011). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EAQ30210.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AAMW01000001; EAQ30210.1; -; Genomic_DNA. DR RefSeq; WP_007164240.1; NZ_CH672390.1. DR ProteinModelPortal; A3WC60; -. DR STRING; 237727.NAP1_05520; -. DR EnsemblBacteria; EAQ30210; EAQ30210; NAP1_05520. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000002995; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000002995}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000002995}. FT DOMAIN 202 376 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 432 AA; 47502 MW; 4E0C080E7A0AD477 CRC64; MDEVTRGARA LVLCPDIRSF SYDLDAAERL AEAEGLALAI GVAIEHSEIL PVRQMQPNTL FGSGQVENIK ILCEQHECEL VIVDGALTPI QQRNLEDKLK RKVIDRTGLI LEIFGERAAT AEGRLQVELA HLDYQQSRLV RSWTHLERQR GGFGFLGGPG ETQIEADRRM IRQRMGRLRR ELEQVRKTRT LHRERRGRAP WPVIALVGYT NAGKSTLFNR LTGAEVMAED LLFATLDPTM RAISLPGVEK AILSDTVGFI SDLPTQLVAA FRATLEEVTG ADIICHVRDM ANPAHSAQKK QVMEVLSDLG VVDAESGESE IPILEVWNKA DLLSEDTLTE LREAAAGQDA VLLSASSGEG VEAFADKIAD MLTASAKEVT ITLPASDGRR LAWLHAHGDV LEDCDAGEGE HGPERRLTVR LNPKELGQYA SL // ID A3WJ81_9GAMM Unreviewed; 412 AA. AC A3WJ81; DT 03-APR-2007, integrated into UniProtKB/TrEMBL. DT 03-APR-2007, sequence version 1. DT 30-AUG-2017, entry version 51. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=OS145_01970 {ECO:0000313|EMBL:EAQ33096.1}; OS Idiomarina baltica OS145. OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales; OC Idiomarinaceae; Idiomarina. OX NCBI_TaxID=314276 {ECO:0000313|EMBL:EAQ33096.1, ECO:0000313|Proteomes:UP000016543}; RN [1] {ECO:0000313|EMBL:EAQ33096.1, ECO:0000313|Proteomes:UP000016543} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=OS145 {ECO:0000313|EMBL:EAQ33096.1, RC ECO:0000313|Proteomes:UP000016543}; RA Brettar I., Hofle M., Ferriera S., Johnson J., Kravitz S., Halpern A., RA Remington K., Beeson K., Tran B., Rogers Y.-H., Friedman R., RA Venter J.C.; RL Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EAQ33096.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AAMX01000001; EAQ33096.1; -; Genomic_DNA. DR ProteinModelPortal; A3WJ81; -. DR STRING; 314276.OS145_01970; -. DR EnsemblBacteria; EAQ33096; EAQ33096; OS145_01970. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000016543; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000016543}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000016543}. FT DOMAIN 183 350 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 412 AA; 46263 MW; F4B59FCB0213A5BA CRC64; MDLPAEVDRE DLSELHLLAS SAGVEPLGVV TASRSAPSPK YFVGSGKAEE IAEQVQALDA NIVIFNHALS PTQERNLEKI CKCRVLDRTG LILDIFAQRA RTHEGKLQVE LAQLRHISTR LVRGWTHLER QKGGIGLRGP GETQLETDRR LIRGRIKNIL RRLEKVQKQR EQGRRARQRA EIPTVSLVGY TNAGKSTLFN TMTESGVYAA DQLFATLDPT LRKLEVEDVG RIILADTVGF IRHLPHDLVA AFKATLQETQ EADILLHVVD VADEHQQSNI EQVSEVLDEI GAGEVPQLMI CNKIDKLEDS APRIDRDDEG KPVRVWVSAQ DNIGTELIFE ALKERLGPQM VNLSLKLPPS MGKLRGTLYQ LNSVSAERID EQGELELDIK MSIVDWNKLQ KEYDNRLDNY IQ // ID A3XAT0_9RHOB Unreviewed; 423 AA. AC A3XAT0; DT 03-APR-2007, integrated into UniProtKB/TrEMBL. DT 03-APR-2007, sequence version 1. DT 07-JUN-2017, entry version 48. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=MED193_04576 {ECO:0000313|EMBL:EAQ45075.1}; OS Roseobacter sp. MED193. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae; Roseobacter. OX NCBI_TaxID=314262 {ECO:0000313|EMBL:EAQ45075.1, ECO:0000313|Proteomes:UP000005943}; RN [1] {ECO:0000313|EMBL:EAQ45075.1, ECO:0000313|Proteomes:UP000005943} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MED193 {ECO:0000313|EMBL:EAQ45075.1, RC ECO:0000313|Proteomes:UP000005943}; RA Pinhassi J., Pedros-Alio C., Ferriera S., Johnson J., Kravitz S., RA Halpern A., Remington K., Beeson K., Tran B., Rogers Y.-H., RA Friedman R., Venter J.C.; RL Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EAQ45075.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AANB01000006; EAQ45075.1; -; Genomic_DNA. DR RefSeq; WP_009808442.1; NZ_CH902583.1. DR ProteinModelPortal; A3XAT0; -. DR STRING; 314262.MED193_04576; -. DR EnsemblBacteria; EAQ45075; EAQ45075; MED193_04576. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000005943; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000005943}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}. FT DOMAIN 203 372 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 423 AA; 47002 MW; 952E0560B5D2151A CRC64; MEHDRIRTRA WVLHPDIKSD QGRRPAEPAL AEGVALAEAL PDLDVVGSTV VRLPKAHAGM LFGSGKIEEL KDLLHSNEVD LVLIDGPVSP VQQRNLEKAW KVKILDRTGL ILEIFSDRAR TREGVLQVEM AALSYQRTRL VRAWTHLERQ RGGLGFVGGP GETQIEADRR AIDDQLVNLR RQLAKVVKTR SLHRAARAKI PFPIVALVGY TNAGKSTLFN RLTGAEVMAK DMLFATLDPT MRRVEMPDGP EIILSDTVGF ISDLPTELVA AFRATLEEVL AADVILHVRD ISHEDSQNQA NDVAAILSTL GVDETRAQIE VWNKLDQLPE DVAEARRQRA AREEGIHAIS ALTGEGIEAL LDDVALKLEG VRHVEEFTLS FAQGKERAWL FQQDVVTNEE QGEEGFALTV RWTDKQKAQF KAL // ID A3XHI6_LEEBM Unreviewed; 406 AA. AC A3XHI6; DT 03-APR-2007, integrated into UniProtKB/TrEMBL. DT 03-APR-2007, sequence version 1. DT 07-JUN-2017, entry version 60. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=MED217_16990 {ECO:0000313|EMBL:EAQ51259.1}; OS Leeuwenhoekiella blandensis (strain CECT 7118 / CCUG 51940 / MED217) OS (Flavobacterium sp. (strain MED217)). OC Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales; OC Flavobacteriaceae; Leeuwenhoekiella. OX NCBI_TaxID=398720 {ECO:0000313|EMBL:EAQ51259.1, ECO:0000313|Proteomes:UP000001601}; RN [1] {ECO:0000313|EMBL:EAQ51259.1, ECO:0000313|Proteomes:UP000001601} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MED217 {ECO:0000313|EMBL:EAQ51259.1, RC ECO:0000313|Proteomes:UP000001601}; RX PubMed=17215843; DOI=10.1038/nature05381; RA Gomez-Consarnau L., Gonzalez J.M., Coll-Llado M., Gourdon P., RA Pascher T., Neutze R., Pedros-Alio C., Pinhassi J.; RT "Light stimulates growth of proteorhodopsin-containing marine RT Flavobacteria."; RL Nature 445:210-213(2007). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EAQ51259.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AANC01000001; EAQ51259.1; -; Genomic_DNA. DR RefSeq; WP_009781738.1; NZ_CH672395.1. DR ProteinModelPortal; A3XHI6; -. DR STRING; 398720.MED217_16990; -. DR EnsemblBacteria; EAQ51259; EAQ51259; MED217_16990. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000001601; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000001601}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000001601}. FT DOMAIN 200 385 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 406 AA; 47064 MW; AA3C90307034C25B CRC64; MIEETKIEYE KTVLIGLITQ FQDEDKATEY LDELEFLAYT AGGEVLKRFT QKMDTPNPKT FIGSGKMEEV RAYVDQYEIG TAIFDDELSP AQQKNIEKIL KCKVIDRTNL ILDIFAQRAQ TSYARTQVEL AQYEYLLPRL AGMWTHLERQ RGGIGMRGPG ETEIETDRRI VRDRISLLKK KLEKIDKQQA IQRGNRGALV RVALVGYTNV GKSTLMNTIS KSEVFAENKL FATLDTTVRK VVIRNLPFLL SDTVGFIRKL PTQLVESFKS TLDEVREADL LLHVVDISHP QFEDHIASVN QIMDEIGGSD KPMLMVFNKI DQYTHKTIDE DDLVTERTEE HFTLEEWERT WMSRVDGDAI FISALNKDNM EAFRKKVYDR VREIHITRFP YNNFLYPEYD AYGEEE // ID A3YW12_9SYNE Unreviewed; 548 AA. AC A3YW12; DT 03-APR-2007, integrated into UniProtKB/TrEMBL. DT 03-APR-2007, sequence version 1. DT 07-JUN-2017, entry version 47. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=WH5701_15996 {ECO:0000313|EMBL:EAQ76324.1}; OS Synechococcus sp. WH 5701. OC Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; OC Synechococcus. OX NCBI_TaxID=69042 {ECO:0000313|EMBL:EAQ76324.1, ECO:0000313|Proteomes:UP000002935}; RN [1] {ECO:0000313|EMBL:EAQ76324.1, ECO:0000313|Proteomes:UP000002935} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=WH5701 {ECO:0000313|Proteomes:UP000002935}; RA Scanlan D., Ferriera S., Johnson J., Kravitz S., Halpern A., RA Remington K., Beeson K., Tran B., Rogers Y.-H., Friedman R., RA Venter J.C.; RL Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EAQ76324.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AANO01000002; EAQ76324.1; -; Genomic_DNA. DR RefSeq; WP_006172155.1; NZ_CH724159.1. DR ProteinModelPortal; A3YW12; -. DR STRING; 69042.WH5701_15996; -. DR EnsemblBacteria; EAQ76324; EAQ76324; WH5701_15996. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000002935; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000002935}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000002935}. FT DOMAIN 377 548 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 338 372 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 548 AA; 60057 MW; ED9E123BDCDD6C29 CRC64; MKQSVLAGRV TGLRPAQKRR LERLAQRRHP EQGGADLLGL QRLAAEAREL ELPLSLVVDG RGLCRLLWVG PLEQSGRLIE RLPGSERRQG QDLRLLSCIG RGQSLEPVGS DALVGMDLQP LFWLRFSDRA RSGGRWPAAV YGLSRDEAQP WTCRLEGELA DLCDPGINPA EASELEAAGA INQTRQGPEQ VMLLALVSGE ESESQRDIAE LEGLVRSAGG LPVGVVRQKR QQAAPHTLWG EGKLREAALE ARRLGATLVV TDRELTPVQA RNLERLLDLP VSDRSELILD IFAQRAASSA GRLQVELAQL RYRLPRLSGR GLSLSRQGGG IGTRGPGETQ LEKDRRAIAR RIERLQRDVE RLGEHRARLR QGRGGLKRLA LVGYTNAGKS SLLNALTQPV AGEEVLAENK LFATLDPTTR RLDLPDGSGA VRRLLLTDTV GFIRELPPPL VEAFRSTLEE TLEADGLLIV VDLADPAWPV QLRTVHTILD SLGSHAPRRL VANQIDRCPA TALEQARSFD ADVVFISATA GLGLQHLRDM LQDWPQST // ID A3Z9N7_9SYNE Unreviewed; 573 AA. AC A3Z9N7; DT 03-APR-2007, integrated into UniProtKB/TrEMBL. DT 03-APR-2007, sequence version 1. DT 07-JUN-2017, entry version 45. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=RS9917_07565 {ECO:0000313|EMBL:EAQ68287.1}; OS Synechococcus sp. RS9917. OC Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; OC Synechococcus. OX NCBI_TaxID=221360 {ECO:0000313|EMBL:EAQ68287.1, ECO:0000313|Proteomes:UP000005593}; RN [1] {ECO:0000313|EMBL:EAQ68287.1, ECO:0000313|Proteomes:UP000005593} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=RS9917 {ECO:0000313|EMBL:EAQ68287.1, RC ECO:0000313|Proteomes:UP000005593}; RA Scanlan D., Ferriera S., Johnson J., Kravitz S., Halpern A., RA Remington K., Beeson K., Tran B., Rogers Y.-H., Friedman R., RA Venter J.C.; RL Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EAQ68287.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AANP01000006; EAQ68287.1; -; Genomic_DNA. DR RefSeq; WP_007101485.1; NZ_CH724158.1. DR ProteinModelPortal; A3Z9N7; -. DR STRING; 221360.RS9917_07565; -. DR EnsemblBacteria; EAQ68287; EAQ68287; RS9917_07565. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000005593; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000005593}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000005593}. FT DOMAIN 383 555 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 573 AA; 63177 MW; 17BA534542900B84 CRC64; MKQAHLAGRT RGLRPSQLRQ AERLSHRRHP SDNGADPLTL ERLADLCLDL KQPLHLLIDA RGLCRLLWVG PLTESGQLLS HLPGGERRRT GDRRRWRLVS CLAASGRGLL SPEPREAVVA LDLEPELWLR YLAKPEPGGR RPARGWQPAR HSSLGWATLE GDDLDAFCRL SPAGSGTAST STGPPLDRRS AGGPERVLLL TLTGRDEQRN ERDLAELEGL VRSAGAEPVN NCPQALSSAH PQTLWGTGKL QEAALEVRRH QASLVITDRE LTPVQVRNLE RWLDCPVMDR TELILDIFAQ RAASAAGRLQ VELAQLRYRL PRLIGRGRSL SRQGGGIGTR GPGETQLEKD RRAISRRIEA LRRGLTQLRQ HRGRLRDRRG DLHRLALVGY TNAGKSSLLN ALCGQRGRST VLAENKLFAT LDPTTRRLAF PRDAAAADVL LITDTVGFIR ELPEALMEAF KATLEETVDA DLLLLVVDLG DPDWSGQLQA VHSLLDALGC DQPRQVVANQ IDRCDADAID TIRRLEPEVL YVSATSGLGL QGLKQRLDER FWGSGTRTDT LAPATDSTVP WPS // ID A4A1M2_9PLAN Unreviewed; 442 AA. AC A4A1M2; DT 03-APR-2007, integrated into UniProtKB/TrEMBL. DT 03-APR-2007, sequence version 1. DT 07-JUN-2017, entry version 48. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=DSM3645_04740 {ECO:0000313|EMBL:EAQ77327.1}; OS Blastopirellula marina DSM 3645. OC Bacteria; Planctomycetes; Planctomycetia; Planctomycetales; OC Planctomycetaceae; Blastopirellula. OX NCBI_TaxID=314230 {ECO:0000313|EMBL:EAQ77327.1, ECO:0000313|Proteomes:UP000004358}; RN [1] {ECO:0000313|EMBL:EAQ77327.1, ECO:0000313|Proteomes:UP000004358} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 3645 {ECO:0000313|EMBL:EAQ77327.1, RC ECO:0000313|Proteomes:UP000004358}; RA Amann R., Ferriera S., Johnson J., Kravitz S., Halpern A., RA Remington K., Beeson K., Tran B., Rogers Y.-H., Friedman R., RA Venter J.C.; RL Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EAQ77327.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AANZ01000036; EAQ77327.1; -; Genomic_DNA. DR RefSeq; WP_002654542.1; NZ_CH672377.1. DR ProteinModelPortal; A4A1M2; -. DR STRING; 314230.DSM3645_04740; -. DR EnsemblBacteria; EAQ77327; EAQ77327; DSM3645_04740. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000004358; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000004358}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000004358}. FT DOMAIN 201 367 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 162 189 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 442 AA; 49501 MW; D713E4991D1FBC7C CRC64; MTQRERKQSV AEEKSVLVKV ILPETIVGDD PFDELAGLAT TAGTDVVGKM TQRRDKPETA TYLGSGKVEE LKLCAEASEA NVIIFDNELS PAQTRNLEQG TGLKVIDRTE LILDIFATHA QTYESRLAVE LAQLQYALPR LKRMWSHLDR IKMGVGMRGP GEKQLEVDRR LVEKRIRDLK DDLAKVQGRR EREVASRRNV MTISIVGYTN AGKSTLMNYL TEAQVLAEDK LFATLDTRTR RWQLPHWGPV LLSDTVGFIR NLPHRLIASF KATLEEARQA DLLLHVADAS NADVVNQISA VYEVLEEIGI EEKDALLVLN KIDAVTDQHT LEVLLQRYPD ALLVSAKTGE GREKFALAVS DALSRSFRDV DVETGIDNGR LMAYLASHGE VVSKTYSETR MRIHCRLPAH FLGRIDDPDT VIRDHVPTET TAEDQDPIEE VA // ID A4A6K4_9GAMM Unreviewed; 420 AA. AC A4A6K4; DT 03-APR-2007, integrated into UniProtKB/TrEMBL. DT 03-APR-2007, sequence version 1. DT 30-AUG-2017, entry version 53. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=KT71_01700 {ECO:0000313|EMBL:EAQ98651.1}; OS Congregibacter litoralis KT71. OC Bacteria; Proteobacteria; Gammaproteobacteria; Cellvibrionales; OC Halieaceae; Congregibacter. OX NCBI_TaxID=314285 {ECO:0000313|EMBL:EAQ98651.1, ECO:0000313|Proteomes:UP000019205}; RN [1] {ECO:0000313|EMBL:EAQ98651.1, ECO:0000313|Proteomes:UP000019205} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=KT71 {ECO:0000313|EMBL:EAQ98651.1}; RX PubMed=17299055; DOI=10.1073/pnas.0608046104; RA Fuchs B.M., Spring S., Teeling H., Quast C., Wulf J., RA Schattenhofer M., Yan S., Ferriera S., Johnson J., Glockner F.O., RA Amann R.; RT "Characterization of a marine gammaproteobacterium capable of aerobic RT anoxygenic photosynthesis."; RL Proc. Natl. Acad. Sci. U.S.A. 104:2891-2896(2007). RN [2] {ECO:0000313|EMBL:EAQ98651.1, ECO:0000313|Proteomes:UP000019205} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=KT71 {ECO:0000313|EMBL:EAQ98651.1}; RX PubMed=19287491; DOI=10.1371/journal.pone.0004866; RA Spring S., Lunsdorf H., Fuchs B.M., Tindall B.J.; RT "The photosynthetic apparatus and its regulation in the aerobic RT gammaproteobacterium Congregibacter litoralis gen. nov., sp. nov."; RL PLoS ONE 4:E4866-E4866(2009). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EAQ98651.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AAOA02000002; EAQ98651.1; -; Genomic_DNA. DR RefSeq; WP_008292734.1; NZ_CM002299.1. DR ProteinModelPortal; A4A6K4; -. DR STRING; 314285.KT71_01700; -. DR EnsemblBacteria; EAQ98651; EAQ98651; KT71_01700. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000019205; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000019205}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Hydrolase {ECO:0000313|EMBL:EAQ98651.1}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000019205}. FT DOMAIN 199 365 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 420 AA; 46844 MW; BC5B9F79F5746FBB CRC64; MFFDRPDSGE RAVLVNISLD NDGGGIDPRE FEALVISAGG DPIALVTGHR STPKARSFVG SGKLEEIEEI LRAEDASLVI FNHSLSPSQE RNLEASLKAR VLDRTGLILD IFAQRARTHE GKLQVELAQL RHMSTRLVRG WTHLERQKGG IGMRGPGETQ LETDRRLLRA RIKSISARLD RVRRQRGQGR RARQRAELAT VALVGYTNAG KSTLFNTLTD AKVYAADQLF ATLDPTLRRL EVDNLGPLVI ADTVGFIARL PHGLVEAFKA TLEETREADL LLHVVDAASE DRDDNRHEVQ AVLEEIGAEE RPVLEIYNKI DLLEMQPRID RDDEGRPYRV WISAEKKLGL DLVMQALAER LGADVMAQDV ELRPDQAKLR AALYALGAVE NEEFGDDGSA HLQVRLPRSD WERLISREGA // ID A4AHJ9_9ACTN Unreviewed; 516 AA. AC A4AHJ9; DT 03-APR-2007, integrated into UniProtKB/TrEMBL. DT 03-APR-2007, sequence version 1. DT 07-JUN-2017, entry version 57. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=A20C1_01416 {ECO:0000313|EMBL:EAR25205.1}; OS marine actinobacterium PHSC20C1. OC Bacteria; Actinobacteria. OX NCBI_TaxID=312284 {ECO:0000313|EMBL:EAR25205.1, ECO:0000313|Proteomes:UP000003868}; RN [1] {ECO:0000313|EMBL:EAR25205.1, ECO:0000313|Proteomes:UP000003868} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=PHSC20C1 {ECO:0000313|EMBL:EAR25205.1, RC ECO:0000313|Proteomes:UP000003868}; RA Murray A., Ferriera S., Johnson J., Kravitz S., Halpern A., RA Remington K., Beeson K., Tran B., Rogers Y.-H., Friedman R., RA Venter J.C.; RL Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EAR25205.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AAOB01000004; EAR25205.1; -; Genomic_DNA. DR RefSeq; WP_009771932.1; NZ_CH672415.1. DR ProteinModelPortal; A4AHJ9; -. DR STRING; 312284.A20C1_01416; -. DR EnsemblBacteria; EAR25205; EAR25205; A20C1_01416. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000003868; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 2. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000003868}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000003868}. FT DOMAIN 295 460 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 516 AA; 56138 MW; D74270447CB8A887 CRC64; MTRNTTESSI EADNGDDAER SVDRVLATET TDHAAVTRFG SGPSGAQALQ ADAHYESDRD GDQFDREDRH ALKRVRGLST ELEDVTEVEY RQLRIENVVL IGIYGQGALR EAENSLRELS ALAETAGAVV LDGLLQRRSN PDPSTYFGKG KAIELRDVVA ATGADTVIAD TELAPSQRRA LEDVVGVKVI DRTAVILDIF SQHATSREGK AQVELAQMEY LLPRLRGWGE SMSRQAGGQV GGAGAGMGSR GPGETKIELD RRRIHTRMAR LRKQIKGFAP AREAKRANRD RFEVPSVAIA GYTNAGKSSL LNRLTRAGVL VENALFATLD ATVRRSETAD GRLFTLSDTV GFVRNLPHQL VEAFRSTLEE IGQADVIVHV VDASHPDPGA QLSTVRDVIG ELGARDIPEI VVFNKSDLAD DDQRLVIRGL EPTGIFVSAR SGEGIDELNS RIAELLPAPE IKVTLLVPYD RGEIISRLHV QGRVLSTDYR EDGTLVTALV HPARVDELTE FVVTSA // ID A4ANU4_MARSH Unreviewed; 403 AA. AC A4ANU4; DT 03-APR-2007, integrated into UniProtKB/TrEMBL. DT 03-APR-2007, sequence version 1. DT 07-JUN-2017, entry version 68. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=FB2170_05245 {ECO:0000313|EMBL:EAR02666.1}; OS Maribacter sp. (strain HTCC2170 / KCCM 42371). OC Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales; OC Flavobacteriaceae; Maribacter. OX NCBI_TaxID=313603 {ECO:0000313|EMBL:EAR02666.1, ECO:0000313|Proteomes:UP000001602}; RN [1] {ECO:0000313|EMBL:EAR02666.1, ECO:0000313|Proteomes:UP000001602} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=HTCC2170 / KCCM 42371 {ECO:0000313|Proteomes:UP000001602}; RX PubMed=21037013; DOI=10.1128/JB.01207-10; RA Oh H.M., Kang I., Yang S.J., Jang Y., Vergin K.L., Giovannoni S.J., RA Cho J.C.; RT "Complete genome sequence of strain HTCC2170, a novel member of the RT genus Maribacter in the family Flavobacteriaceae."; RL J. Bacteriol. 193:303-304(2011). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002157; EAR02666.1; -; Genomic_DNA. DR RefSeq; WP_013305731.1; NC_014472.1. DR ProteinModelPortal; A4ANU4; -. DR STRING; 313603.FB2170_05245; -. DR EnsemblBacteria; EAR02666; EAR02666; FB2170_05245. DR KEGG; fbc:FB2170_05245; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000001602; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000001602}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000001602}. FT DOMAIN 200 385 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 403 AA; 46903 MW; A29CC66C679EC2C9 CRC64; MLEKKSIEYE KAVLIGVINR EQNEEKVNEY LDELEFLTYT AGGEVSKRFV QRVEVPNPKT LIGSGKMQEV EHYVEENKIG SVIFDDELSP GQQRNIEKQL RCKILDRTSL ILDIFAQRAR TSYSRTQVEL AQYEYLLPRL TGLWTHLERQ KGGIGMRGPG ETEIETDRRI VRDRISLLKK KLLKIDKQME TQRGNRGAMV RVALVGYTNV GKSTLMNVIS KSDVFAENKL FATLDTTVRK VVIGNLPFLL SDTVGFIRKL PTQLVESFKS TLDEVREADL LLHVVDISHP NFEEHIESVN NILAEIKSAD KKTIMVFNKI DQYKHETIDD DDLITERTSK HFTIEEWKRT WMQRMGENAL FISALNKENL DEFRKRVYNV VRDIHVTRFP YNNFLYPEHL DQY // ID A4BEB5_9GAMM Unreviewed; 436 AA. AC A4BEB5; DT 03-APR-2007, integrated into UniProtKB/TrEMBL. DT 03-APR-2007, sequence version 1. DT 07-JUN-2017, entry version 51. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=MED297_12717 {ECO:0000313|EMBL:EAR09593.1}; OS Reinekea blandensis MED297. OC Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales; OC Saccharospirillaceae; Reinekea. OX NCBI_TaxID=314283 {ECO:0000313|EMBL:EAR09593.1, ECO:0000313|Proteomes:UP000005953}; RN [1] {ECO:0000313|EMBL:EAR09593.1, ECO:0000313|Proteomes:UP000005953} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MED297 {ECO:0000313|EMBL:EAR09593.1, RC ECO:0000313|Proteomes:UP000005953}; RA Pinhassi J., Pedros-Alio C., Ferriera S., Johnson J., Kravitz S., RA Halpern A., Remington K., Beeson K., Tran B., Rogers Y.-H., RA Friedman R., Venter J.C.; RL Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EAR09593.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AAOE01000009; EAR09593.1; -; Genomic_DNA. DR RefSeq; WP_008042329.1; NZ_CH724149.1. DR ProteinModelPortal; A4BEB5; -. DR STRING; 314283.MED297_12717; -. DR EnsemblBacteria; EAR09593; EAR09593; MED297_12717. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000005953; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000005953}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000005953}. FT DOMAIN 199 370 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 436 AA; 49063 MW; 82241D06B1E8BED1 CRC64; MFFERVEGGN RAILIHVDFP ESDHREDPAE FEELVVSAGA DPATFIKASR TTPHPKYFVG TGKMEEIRQA VKTYEADVVL FNHALSPSQE RNIEAGIECR VLDRTGLILD IFAQRARTHE GKLQVELAQL QYQSTRLVRG WTHLERQKGG IGLRGPGETQ LETDRRLLRA RISTIHKKLN KVEKQRNQSR RARDRSDTPT VSLVGYTNAG KSTLFNYLTD SGVYAADQLF ATLDPTLRRL AIPDMGDIVL ADTVGFIRHL PHKLVEAFKA TLQETAEADL LLHVVDCADE DRLGNIEQVE NVLDEIGSSD IPRLEVFNKI DLLDDFEPAI ERNDEGIPVR VWVSAKTGQG AALILAALTE LLGDEVISKS ISLSPAESGL RAALYEQNAV LSENYDEHGH VELEIRMQKK DFKQLLKRFN LPQERFGVAR TKEFFE // ID A4BLP5_9GAMM Unreviewed; 435 AA. AC A4BLP5; DT 03-APR-2007, integrated into UniProtKB/TrEMBL. DT 03-APR-2007, sequence version 1. DT 07-JUN-2017, entry version 58. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=NB231_15473 {ECO:0000313|EMBL:EAR23233.1}; OS Nitrococcus mobilis Nb-231. OC Bacteria; Proteobacteria; Gammaproteobacteria; Chromatiales; OC Ectothiorhodospiraceae; Nitrococcus. OX NCBI_TaxID=314278 {ECO:0000313|EMBL:EAR23233.1, ECO:0000313|Proteomes:UP000003374}; RN [1] {ECO:0000313|EMBL:EAR23233.1, ECO:0000313|Proteomes:UP000003374} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Nb-231 {ECO:0000313|EMBL:EAR23233.1, RC ECO:0000313|Proteomes:UP000003374}; RA Waterbury J., Ferriera S., Johnson J., Kravitz S., Halpern A., RA Remington K., Beeson K., Tran B., Rogers Y.-H., Friedman R., RA Venter J.C.; RL Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EAR23233.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AAOF01000001; EAR23233.1; -; Genomic_DNA. DR RefSeq; WP_005004291.1; NZ_CH672427.1. DR ProteinModelPortal; A4BLP5; -. DR STRING; 314278.NB231_15473; -. DR EnsemblBacteria; EAR23233; EAR23233; NB231_15473. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000003374; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000003374}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000003374}. FT DOMAIN 205 371 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 164 198 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 435 AA; 48516 MW; 7D399A6E3DDE4F1A CRC64; MDAAPARLFA RPDGGERAIL VQLDSGIVDL DEAFVELAAL AETAGAVVVD KLVNRRAAPD PRYFIGKGKV GELAARIRET DANLVLINHG LSAVQERNLE QAFGARVLDR TGLILDIFAL RARSHEGKLQ VELAQLRHIA SRLVRGWSHL ERQKGGIGLR GPGETQLELD RRLLGQRIKQ LEKRLTKVRR QREQGRQARR KREFVTVSFV GYTNAGKSAL FNRLTESHVY IADLLFATLD TTLRRIELPG SEQAIIADTV GFIRELPHQL IAAFRSTLEE VAQADLLLHV IDIADPLREQ RRWEVERVLS DIGAGDIPAL LIFNKLDLSG GPARLERDGT GQPVAVWVSA QTGEGMELLR AAIAERIGLT RVHGRVRLSP TEGRLRARLY ALGQVRCERI SEQGVCELEV DLPQREWARL RRQDGASIEL WPADH // ID A4BWN5_9FLAO Unreviewed; 402 AA. AC A4BWN5; DT 03-APR-2007, integrated into UniProtKB/TrEMBL. DT 03-APR-2007, sequence version 1. DT 07-JUN-2017, entry version 57. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=PI23P_02742 {ECO:0000313|EMBL:EAR13376.1}; OS Polaribacter irgensii 23-P. OC Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales; OC Flavobacteriaceae; Polaribacter. OX NCBI_TaxID=313594 {ECO:0000313|EMBL:EAR13376.1, ECO:0000313|Proteomes:UP000003053}; RN [1] {ECO:0000313|EMBL:EAR13376.1, ECO:0000313|Proteomes:UP000003053} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=23-P {ECO:0000313|EMBL:EAR13376.1, RC ECO:0000313|Proteomes:UP000003053}; RA Murray A., Staley J., Ferriera S., Johnson J., Kravitz S., Halpern A., RA Remington K., Beeson K., Tran B., Rogers Y.-H., Friedman R., RA Venter J.C.; RL Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EAR13376.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AAOG01000001; EAR13376.1; -; Genomic_DNA. DR RefSeq; WP_004569173.1; NZ_CH724148.1. DR ProteinModelPortal; A4BWN5; -. DR STRING; 313594.PI23P_02742; -. DR EnsemblBacteria; EAR13376; EAR13376; PI23P_02742. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000003053; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000003053}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000003053}. FT DOMAIN 200 385 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 402 AA; 46006 MW; C6584C053D768176 CRC64; MIDPKEAISE KAVLIGVITQ QQDETQSDEY LDELEFLTST AGGVAVKRFV QKMEKPNPKT FLGVGKLDEV RGYIESNGIG TAIFDDELSP AQIRNIEKVL DCKILDRTNL ILDIFAQRAQ SSSARTQVEL AQCQYLLPRL TRLWTHLDKQ KGGIGMRGPG ETEIETDRRI IRDKIDVLKK KLLTIDKQMA VQRKNRGKMV RIALVGYTNV GKSTLMNVIS KSDVFAENKL FATLDTTVRK VVIKNIPFLM TDTVGFIRKL PTQLVESFKS TLDEVREADL LLHVIDISHP NFEDHIASVN SVLQDIKCAD KPTLMVFNKI DAFVHETIKE DDLVTEKTKE HYTLQDWKKT WMNDKEQTSI FISALNKENL EDFKEVVYEA VKTIHIQRFP YNDFLYNEYE GE // ID A4C505_9GAMM Unreviewed; 453 AA. AC A4C505; DT 03-APR-2007, integrated into UniProtKB/TrEMBL. DT 03-APR-2007, sequence version 1. DT 07-JUN-2017, entry version 49. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=PTD2_03671 {ECO:0000313|EMBL:EAR30637.1}; OS Pseudoalteromonas tunicata D2. OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales; OC Pseudoalteromonadaceae; Pseudoalteromonas. OX NCBI_TaxID=87626 {ECO:0000313|EMBL:EAR30637.1, ECO:0000313|Proteomes:UP000006201}; RN [1] {ECO:0000313|EMBL:EAR30637.1, ECO:0000313|Proteomes:UP000006201} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=D2 {ECO:0000313|EMBL:EAR30637.1, RC ECO:0000313|Proteomes:UP000006201}; RA Moran M.A., Kjelleberg S., Egan S., Saunders N., Thomas T., RA Ferriera S., Johnson J., Kravitz S., Halpern A., Remington K., RA Beeson K., Tran B., Rogers Y.-H., Friedman R., Venter J.C.; RL Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EAR30637.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AAOH01000001; EAR30637.1; -; Genomic_DNA. DR RefSeq; WP_009836935.1; NZ_AAOH01000001.1. DR ProteinModelPortal; A4C505; -. DR STRING; 87626.PTD2_03671; -. DR EnsemblBacteria; EAR30637; EAR30637; PTD2_03671. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000006201; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000006201}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000006201}. FT DOMAIN 231 396 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 192 219 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 453 AA; 50497 MW; 2A9DA99444566109 CRC64; MPFSQNALQH RALLISIRTP QQKEHEAEES LAELARLVTT LGFDVVGSQT QRQASTKRIT VLGSGKLSEL AKLTASQAAE FDEEEPTSDT FSTDVDDETL EELAHSALPV KTADVVVFDC DLSPSQLRNV ETQLGVEVFD RTGIIIEIFS RHARTRTARL QVEIARLKYL TPRLRESHIG TKERQMGKGA GESALELDRR RVRDQLAELR RELISVQGQM QGRREKRSEH FCVALVGYTN AGKSSMMRAL TGSEVLVENK LFATLDTTVR ALQPETQPRI LISDTVGFIK KLPHDLVASF HSTLEEAHDA SLLLYVVDAS DPSFRSQLAV VNEVMQEVGV DETPKILILN KSDNLTLQQQ GELLEQYPDS IMMSTHNPLH ISALHQKIVT ISEKDMQDEQ ILVPYTANGI VGEIRSNMKV LAEEYGADGI AITVRASTIA LERLHKLMQQ KTK // ID A4C8N0_9GAMM Unreviewed; 429 AA. AC A4C8N0; DT 03-APR-2007, integrated into UniProtKB/TrEMBL. DT 03-APR-2007, sequence version 1. DT 30-AUG-2017, entry version 63. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=PTD2_07874 {ECO:0000313|EMBL:EAR28945.1}; OS Pseudoalteromonas tunicata D2. OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales; OC Pseudoalteromonadaceae; Pseudoalteromonas. OX NCBI_TaxID=87626 {ECO:0000313|EMBL:EAR28945.1, ECO:0000313|Proteomes:UP000006201}; RN [1] {ECO:0000313|EMBL:EAR28945.1, ECO:0000313|Proteomes:UP000006201} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=D2 {ECO:0000313|EMBL:EAR28945.1, RC ECO:0000313|Proteomes:UP000006201}; RA Moran M.A., Kjelleberg S., Egan S., Saunders N., Thomas T., RA Ferriera S., Johnson J., Kravitz S., Halpern A., Remington K., RA Beeson K., Tran B., Rogers Y.-H., Friedman R., Venter J.C.; RL Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EAR28945.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AAOH01000003; EAR28945.1; -; Genomic_DNA. DR RefSeq; WP_009838206.1; NZ_AAOH01000003.1. DR ProteinModelPortal; A4C8N0; -. DR STRING; 87626.PTD2_07874; -. DR EnsemblBacteria; EAR28945; EAR28945; PTD2_07874. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000006201; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000006201}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Hydrolase {ECO:0000313|EMBL:EAR28945.1}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Protease {ECO:0000313|EMBL:EAR28945.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000006201}. FT DOMAIN 198 365 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 429 AA; 48637 MW; 59AA119E0DA9D775 CRC64; MFDRYKAGEQ AVLVHIEFPK EGDREDLQEL EMLVSSAGAN CLAIVQGSRQ SPHPKFFVGT GKAEEIAEVV QLHQADVVIF NHELSPSQER NLERICQCRV LDRTTLILDI FAQRARTHEG KLQVELAQLR HISTRLIRGW THLERQKGGI GLRGPGETQL ETDRRLIRDK IKTILKRLDK VAKQREQGRR ARTRNEIPTV SLVGYTNAGK STLFNRATAS DVYAADQLFA TLDPTLRKID VADIGSVIMA DTVGFIRHLP HDLVAAFKAT LVETREADLQ LHVIDVADER RQENIDQVND VLHEIEADDV PQLLIYNKID LVEELVPRID RDDEGKPIRI WLSAQTGVGC ELLLQAISEC LAEKMLKCRL RVPARFGSLR GALYKLNCIH AEQYDDLGNC LLNIRLPMAD WNRLKKDNGT EIEKFIITD // ID A4CHL1_ROBBH Unreviewed; 405 AA. AC A4CHL1; DT 03-APR-2007, integrated into UniProtKB/TrEMBL. DT 03-APR-2007, sequence version 1. DT 07-JUN-2017, entry version 62. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=RB2501_05955 {ECO:0000313|EMBL:EAR16419.1}; OS Robiginitalea biformata (strain ATCC BAA-864 / HTCC2501 / KCTC 12146). OC Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales; OC Flavobacteriaceae; Robiginitalea. OX NCBI_TaxID=313596 {ECO:0000313|EMBL:EAR16419.1, ECO:0000313|Proteomes:UP000009049}; RN [1] {ECO:0000313|EMBL:EAR16419.1, ECO:0000313|Proteomes:UP000009049} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-864 / HTCC2501 / KCTC 12146 RC {ECO:0000313|Proteomes:UP000009049}; RX PubMed=19767438; DOI=10.1128/JB.01191-09; RA Oh H.M., Giovannoni S.J., Lee K., Ferriera S., Johnson J., Cho J.C.; RT "Complete genome sequence of Robiginitalea biformata HTCC2501."; RL J. Bacteriol. 191:7144-7145(2009). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001712; EAR16419.1; -; Genomic_DNA. DR RefSeq; WP_015753176.1; NC_013222.1. DR ProteinModelPortal; A4CHL1; -. DR STRING; 313596.RB2501_05955; -. DR EnsemblBacteria; EAR16419; EAR16419; RB2501_05955. DR KEGG; rbi:RB2501_05955; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000009049; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000009049}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000009049}. FT DOMAIN 200 385 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 405 AA; 46802 MW; 74F81E2D4CAE4B7C CRC64; MLERKTTEYE KAVLIGIITR EQPEEKVNEY LDELEFLTYT AGGEVVGRFV QRIDVPNPKT FIGSGKLEEV QAFVKKEEVG SVIFDDELSP VQQRNIEKQL RCKIIDRTGL ILDIFAQRAT TSYARTQVEL AQYEYLLPRL TGLWTHLERQ RGGIGMRGPG ETEIETDRRI VRDRISLLKK KLAKIDKQME TQRGNRGSLV RVALVGYTNV GKSTLMNVVS KSEVFAENKL FATLDTTVRK VVLGNLPFLL SDTVGFIRKL PTQLVESFKS TLDEVREADL LLHVVDISHP NFEEHIDSVN QILAEIDCAE KETLMVFNKI DLYEAEPLEE DDLITERTSR HYSIDEWRAT WMQRMSGDAI FISALNKENL DEFRKRVYQR VRDIHVTRFP YNNFLYPENL DAYSQ // ID A4CQL0_SYNPV Unreviewed; 568 AA. AC A4CQL0; DT 03-APR-2007, integrated into UniProtKB/TrEMBL. DT 03-APR-2007, sequence version 1. DT 07-JUN-2017, entry version 48. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=WH7805_11543 {ECO:0000313|EMBL:EAR19547.1}; OS Synechococcus sp. (strain WH7805). OC Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; OC Synechococcus. OX NCBI_TaxID=59931 {ECO:0000313|EMBL:EAR19547.1, ECO:0000313|Proteomes:UP000001224}; RN [1] {ECO:0000313|EMBL:EAR19547.1, ECO:0000313|Proteomes:UP000001224} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=WH7805 {ECO:0000313|Proteomes:UP000001224}; RA Scanlan D., Ostrowski M., Mazard S., Wilkinson N., Partensky F., RA Dufresne A., Garczarek L., Hess W., Gierga G., Voss B., Axmann I., RA Post A., Ferriera S., Johnson J., Kravitz S., Halpern A., RA Remington K., Beeson K., Tran B., Rogers Y.-H., Friedman R., RA Venter J.C.; RL Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EAR19547.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AAOK01000001; EAR19547.1; -; Genomic_DNA. DR RefSeq; WP_006043104.1; NZ_CH724168.1. DR ProteinModelPortal; A4CQL0; -. DR STRING; 59931.WH7805_11543; -. DR EnsemblBacteria; EAR19547; EAR19547; WH7805_11543. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR OrthoDB; POG091H0464; -. DR PhylomeDB; A4CQL0; -. DR Proteomes; UP000001224; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000001224}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000001224}. FT DOMAIN 378 550 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 568 AA; 62810 MW; 9743910DA1E84359 CRC64; MKQTHLSGRT RGLRPSQLHQ LESLSHRRHP PEDGADLFTL ERLAELSLEL KQSLHLLVDA RGVCRLLWVG PFGESERIEG HWPKESRRRQ RWRLISALAG TQGEGLKPEG REAVIALDVH TSHWLRLQAT VSASGTRPAA IWRADSAATL GWRCDTTGRL QDLCEAGQTE RRSDQAAVAE VLDNPGSRQE RVLLLTLTGA DPAINERDLA ELEGLTRSAG ACPVAVCRQR LGQINPQTLW GTGKLQEAAL DVRRHGASLV ITDRELTPVQ ARNLERLLDC PVMDRSELIL DIFAQRASSA AGRLQVELAQ LRYRLPRLKG RGLSLSRQGG GIGTRGPGET QLEKDRRAIS RRIEHLGREL RQLGAHRARL RQQRSMLPKV ALVGYTNAGK SSLLNALCDR GQGRSVEARN SLFATLDPTT RRLCLPRSGS APRELLITDT VGFIRELPEP LIEAFMATLE ETREADRLLL VVDLGDPDWL GQLTAVHSIL NGLNCHQPRQ VLANQIDRCD ASTLELIRNL ESEVLYVSAT QGTGLKGLRA WLEQTFWGAS PSPVNPDLAY QNSADADA // ID A4EM87_9RHOB Unreviewed; 412 AA. AC A4EM87; DT 17-APR-2007, integrated into UniProtKB/TrEMBL. DT 17-APR-2007, sequence version 1. DT 07-JUN-2017, entry version 48. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=RCCS2_00794 {ECO:0000313|EMBL:EBA10974.1}; OS Roseobacter sp. CCS2. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae; Roseobacter. OX NCBI_TaxID=391593 {ECO:0000313|EMBL:EBA10974.1, ECO:0000313|Proteomes:UP000003535}; RN [1] {ECO:0000313|EMBL:EBA10974.1, ECO:0000313|Proteomes:UP000003535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CCS2 {ECO:0000313|EMBL:EBA10974.1, RC ECO:0000313|Proteomes:UP000003535}; RA Mary Ann M.A., Ferriera S., Johnson J., Kravitz S., Beeson K., RA Sutton G., Rogers Y.-H., Friedman R., Frazier M., Venter J.C.; RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EBA10974.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AAYB01000006; EBA10974.1; -; Genomic_DNA. DR ProteinModelPortal; A4EM87; -. DR STRING; 391593.RCCS2_00794; -. DR EnsemblBacteria; EBA10974; EBA10974; RCCS2_00794. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000003535; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000003535}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}. FT DOMAIN 192 361 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 151 178 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 412 AA; 45683 MW; E6781613C61E26F5 CRC64; MLHPDLKTDH TRRAAEPALE EGVSLAAALP DLDVVGADIV RLPRIHPGKL FGKGKIAELK QVFHDAEVEL VLIDGPVTPV QQRNLEKEWG VKLLDRTGLI LEIFSDRART SEGVLQVEMA ALSYQRTRLV RAWTHLERQR GGLGFVGGPG ETQIEADRRA IDEQLNRLRK QLAKVVKTRE LHRASRAKVP FPIVALVGYT NAGKSTLFNR LTGAQVFAKD MLFATLDPTM RKIVLPTGDE VIMSDTVGFI SDLPTELVAA FRATLEEVLD ADLIVHVRDI SHPQTEEQAE DVHAILQSLG VAEEAPIIEV WNKTDLLEGD ARDAVLTQAA RTDDLFAVSA ITGEGMDPLL AAIPDKLKDP RSEEHLSLPF ADGKKRAWLF EAGVVTDEVQ TETGYDLTVF WTQLQKERFV RL // ID A4ER82_9RHOB Unreviewed; 423 AA. AC A4ER82; DT 17-APR-2007, integrated into UniProtKB/TrEMBL. DT 17-APR-2007, sequence version 1. DT 07-JUN-2017, entry version 50. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=RSK20926_18657 {ECO:0000313|EMBL:EBA17788.1}; OS Roseobacter sp. SK209-2-6. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae; Roseobacter. OX NCBI_TaxID=388739 {ECO:0000313|EMBL:EBA17788.1, ECO:0000313|Proteomes:UP000005964}; RN [1] {ECO:0000313|EMBL:EBA17788.1, ECO:0000313|Proteomes:UP000005964} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SK209-2-6 {ECO:0000313|EMBL:EBA17788.1, RC ECO:0000313|Proteomes:UP000005964}; RA Ward B., Ferriera S., Johnson J., Kravitz S., Beeson K., Sutton G., RA Rogers Y.-H., Friedman R., Frazier M., Venter J.C.; RL Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EBA17788.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AAYC01000002; EBA17788.1; -; Genomic_DNA. DR RefSeq; WP_008204625.1; NZ_AAYC01000002.1. DR ProteinModelPortal; A4ER82; -. DR STRING; 388739.RSK20926_18657; -. DR EnsemblBacteria; EBA17788; EBA17788; RSK20926_18657. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000005964; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000005964}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000005964}. FT DOMAIN 203 372 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 423 AA; 47332 MW; 2D82869B4C507957 CRC64; MEHDRIRTRA WVLHPEIKSD FDRRNAEAAL AEGVALAEAL PDLDVIGSNV VRLPKAHAGM LFGSGKIEEL STKLKAEEIE LVLIDGPVSP VQQRNLEKAW KVKILDRTGL ILEIFSDRAR TREGVLQVEM AALSYQRTRL VRAWTHLERQ RGGLGFVGGP GETQIEADRR AIDEQLVRLR RQLEKVAKTR TLHRAARAKV PYPIVALVGY TNAGKSTLFN RLTGAEVMAK DMLFATLDPT MRRVELPDGP EIILSDTVGF ISDLPTELVA AFRATLEEVL AADVILHVRD ISHDETAKQA EDVASILESL GVDDSRAQIE IWNKLDQLSE EEAIARRERA EREEDVHAIS ALTGEGLPGL LQDIATKLQG VLFEEQFTLP YSDGRKRAWL FAQDVVTEEE QGEEGFVLTV RWTEKQKAQF QSV // ID A4FAJ7_SACEN Unreviewed; 502 AA. AC A4FAJ7; DT 17-APR-2007, integrated into UniProtKB/TrEMBL. DT 17-APR-2007, sequence version 1. DT 07-JUN-2017, entry version 66. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:CAM01072.1}; GN OrderedLocusNames=SACE_1754 {ECO:0000313|EMBL:CAM01072.1}; OS Saccharopolyspora erythraea (strain ATCC 11635 / DSM 40517 / JCM 4748 OS / NBRC 13426 / NCIMB 8594 / NRRL 2338). OC Bacteria; Actinobacteria; Pseudonocardiales; Pseudonocardiaceae; OC Saccharopolyspora. OX NCBI_TaxID=405948 {ECO:0000313|EMBL:CAM01072.1, ECO:0000313|Proteomes:UP000006728}; RN [1] {ECO:0000313|EMBL:CAM01072.1, ECO:0000313|Proteomes:UP000006728} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 11635 / DSM 40517 / JCM 4748 / NBRC 13426 / NCIMB 8594 / RC NRRL 2338 {ECO:0000313|Proteomes:UP000006728}; RX PubMed=17369815; DOI=10.1038/nbt1297; RA Oliynyk M., Samborskyy M., Lester J.B., Mironenko T., Scott N., RA Dickens S., Haydock S.F., Leadlay P.F.; RT "Complete genome sequence of the erythromycin-producing bacterium RT Saccharopolyspora erythraea NRRL23338."; RL Nat. Biotechnol. 25:447-453(2007). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AM420293; CAM01072.1; -; Genomic_DNA. DR RefSeq; WP_009943779.1; NZ_ABFV01000010.1. DR ProteinModelPortal; A4FAJ7; -. DR STRING; 405948.SeryN2_010100006977; -. DR EnsemblBacteria; CAM01072; CAM01072; SACE_1754. DR KEGG; sen:SACE_1754; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000006728; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000006728}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000006728}. FT DOMAIN 278 447 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 502 AA; 54107 MW; 2E8B727AE9FDB2A2 CRC64; MKKSAIRSAD FHPAESNGAV PHDSAFGQAE ADVYEAILAE EPSTGEMELA DRNSLRRVSG LSTELADITE VEYRRLRLER VVLVGVWTEG DAQHAEDSLA ELGRLAETAG SEVLEGLVQR RDRPDPSTYV GSGKVRELRE VVVATGADTV ICDGELSPGQ LRQLEDKLKV KVIDRTALIL DIFAQHASSK EGKAQVELAQ LQYLLPRLRG WGEAMSRQAG GRAGGASGGV GTRGPGETKL ETDRRRIHKR ISKLRKEIAA MRTVRGTKRG RREANAVPGV AIAGYTNAGK SSLLNALTGA GVLVEDALFA TLDPTTRRAD TPDGRPHTLT DTVGFVRHLP HQLVEAFRST LEEVTGADLL VHVVDGAEQA PHEQVAAVRE VLTEIAEDHG APVPPELLVV NKIDSVAPTR MAELRRLLPG AVFVSAHSGE GVEALREIIA DRLPRPEVFV DALVPYTRGE LVARVHSEGE LVDEEHTAEG TRLRAKVRSD LASALKPFVG AG // ID A4G4K8_HERAR Unreviewed; 372 AA. AC A4G4K8; DT 17-APR-2007, integrated into UniProtKB/TrEMBL. DT 02-SEP-2008, sequence version 2. DT 07-JUN-2017, entry version 70. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:CAL61445.2}; GN OrderedLocusNames=HEAR1271 {ECO:0000313|EMBL:CAL61445.2}; OS Herminiimonas arsenicoxydans. OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Oxalobacteraceae; Herminiimonas. OX NCBI_TaxID=204773 {ECO:0000313|EMBL:CAL61445.2, ECO:0000313|Proteomes:UP000006697}; RN [1] {ECO:0000313|EMBL:CAL61445.2, ECO:0000313|Proteomes:UP000006697} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ULPAs1 {ECO:0000313|Proteomes:UP000006697}; RX PubMed=17432936; DOI=10.1371/journal.pgen.0030053; RA Muller D., Medigue C., Koechler S., Barbe V., Barakat M., Talla E., RA Bonnefoy V., Krin E., Arsene-Ploetze F., Carapito C., Chandler M., RA Cournoyer B., Cruveiller S., Dossat C., Duval S., Heymann M., RA Leize E., Lieutaud A., Lievremont D., Makita Y., Mangenot S., RA Nitschke W., Ortet P., Perdrial N., Schoepp B., Siguier N., RA Simeonova D.D., Rouy Z., Segurens B., Turlin E., Vallenet D., RA Van Dorsselaer A., Weiss S., Weissenbach J., Lett M.C., Danchin A., RA Bertin P.N.; RT "A tale of two oxidation states: bacterial colonization of arsenic- RT rich environments."; RL PLoS Genet. 3:518-530(2007). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CU207211; CAL61445.2; -; Genomic_DNA. DR RefSeq; WP_041322243.1; NC_009138.1. DR ProteinModelPortal; A4G4K8; -. DR STRING; 204773.HEAR1271; -. DR EnsemblBacteria; CAL61445; CAL61445; HEAR1271. DR KEGG; har:HEAR1271; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000006697; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000006697}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000006697}. FT DOMAIN 190 356 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 372 AA; 40696 MW; 35395E6A1C77E757 CRC64; MRAVLVGVDF GKGDFAASLE ELSLLSRSAG AEPIMTITGK RASPDAALFV GSGKANEVAD AIVDHEIDIV IFNHALSPAQ QRNLERHLKI RVVDRTSLIL DIFAQRAQSH VGKVQVELAQ LQHLSTRLIR GWTHLERQKG GIGLRGPGET QLETDRRLLG VRVKALRAKL EKLHKQHITQ RRARGRNNAF SVSLVGYTNA GKSTLFNALA KTKMLAADQL FATLDTTSRR IYLGEAGNVV ISDTVGFIRE LPHQLVAAFR ATLEETIHAD LLLHVVDGAS PARMEQIEEV NAVLREIGAD QIPQILVWNK IDAAGLEPAL ERDEYDKIRR VFISAQTGSG LDLLREAIAE CAKERAAGLE DVSLVASDDA KV // ID A4J3Z0_DESRM Unreviewed; 421 AA. AC A4J3Z0; DT 01-MAY-2007, integrated into UniProtKB/TrEMBL. DT 01-MAY-2007, sequence version 1. DT 07-JUN-2017, entry version 69. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Dred_1259 {ECO:0000313|EMBL:ABO49793.1}; OS Desulfotomaculum reducens (strain MI-1). OC Bacteria; Firmicutes; Clostridia; Clostridiales; Peptococcaceae; OC Desulfotomaculum. OX NCBI_TaxID=349161 {ECO:0000313|EMBL:ABO49793.1, ECO:0000313|Proteomes:UP000001556}; RN [1] {ECO:0000313|EMBL:ABO49793.1, ECO:0000313|Proteomes:UP000001556} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MI-1 {ECO:0000313|EMBL:ABO49793.1, RC ECO:0000313|Proteomes:UP000001556}; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., RA Pitluck S., Sims D., Brettin T., Bruce D., Han C., Tapia R., RA Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E., RA Tebo B.M., Richardson P.; RT "Complete sequence of Desulfotomaculum reducens MI-1."; RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000612; ABO49793.1; -; Genomic_DNA. DR RefSeq; WP_011877619.1; NC_009253.1. DR ProteinModelPortal; A4J3Z0; -. DR STRING; 349161.Dred_1259; -. DR EnsemblBacteria; ABO49793; ABO49793; Dred_1259. DR KEGG; drm:Dred_1259; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000001556; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000001556}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000001556}. FT DOMAIN 202 365 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 161 195 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 421 AA; 47205 MW; DE046777BFAB75DA CRC64; MHDIKTTIEE RAVLVGVKLP GFHEHQICQS LDELANLAST AGADVMGTFM QSRQYPDSAT FIGKGKAQEL AEYCREIHAN MVVIDRELSP AQARNLEDRL GVKVIDRTQL ILDIFARRAQ TREGKLQVEL AQLKYLLPRL TGLGTQLSRL GGGIGTRGPG ETKLEVDRRR IRKRISDLEQ ELKEVQRHRS LLRKSRKSEP LPIVSLVGYT NAGKSTLLKS LTGADILVED KLFATLDPTT RRISLPNNDN VLLTDTVGFI QNLPHHLVAA FRATLEEVQE SDLLLHIVDA SHPNYEGQIR AVETVLESLH VLDKPSIMVF NKIDMVKDVQ EIPFTENPRV YISATSGEGS DQLLDMIAGV LKERYSILKL TVPYDKTNLI SILHQKGKVL NEKYTPEGIE IKAEISNIWA ARIRKIFSKN T // ID A4RYQ9_OSTLU Unreviewed; 519 AA. AC A4RYQ9; DT 15-MAY-2007, integrated into UniProtKB/TrEMBL. DT 15-MAY-2007, sequence version 1. DT 07-JUN-2017, entry version 68. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:ABO96729.1}; GN ORFNames=OSTLU_32115 {ECO:0000313|EMBL:ABO96729.1}; OS Ostreococcus lucimarinus (strain CCE9901). OC Eukaryota; Viridiplantae; Chlorophyta; prasinophytes; Mamiellophyceae; OC Mamiellales; Bathycoccaceae; Ostreococcus. OX NCBI_TaxID=436017 {ECO:0000313|EMBL:ABO96729.1, ECO:0000313|Proteomes:UP000001568}; RN [1] {ECO:0000313|EMBL:ABO96729.1, ECO:0000313|Proteomes:UP000001568} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CCE9901 {ECO:0000313|EMBL:ABO96729.1, RC ECO:0000313|Proteomes:UP000001568}; RX PubMed=17460045; DOI=10.1073/pnas.0611046104; RA Palenik B., Grimwood J., Aerts A., Rouze P., Salamov A., Putnam N., RA Dupont C., Jorgensen R., Derelle E., Rombauts S., Zhou K., Otillar R., RA Merchant S.S., Podell S., Gaasterland T., Napoli C., Gendler K., RA Manuell A., Tai V., Vallon O., Piganeau G., Jancek S., Heijde M., RA Jabbari K., Bowler C., Lohr M., Robbens S., Werner G., Dubchak I., RA Pazour G.J., Ren Q., Paulsen I., Delwiche C., Schmutz J., Rokhsar D., RA Van de Peer Y., Moreau H., Grigoriev I.V.; RT "The tiny eukaryote Ostreococcus provides genomic insights into the RT paradox of plankton speciation."; RL Proc. Natl. Acad. Sci. U.S.A. 104:7705-7710(2007). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000586; ABO96729.1; -; Genomic_DNA. DR RefSeq; XP_001418436.1; XM_001418399.1. DR ProteinModelPortal; A4RYQ9; -. DR STRING; 436017.A4RYQ9; -. DR EnsemblPlants; ABO96729; ABO96729; OSTLU_32115. DR GeneID; 5002228; -. DR Gramene; ABO96729; ABO96729; OSTLU_32115. DR KEGG; olu:OSTLU_32115; -. DR eggNOG; KOG0410; Eukaryota. DR eggNOG; COG2262; LUCA. DR KO; K03665; -. DR OMA; VILEIFH; -. DR Proteomes; UP000001568; Chromosome 6. DR GO; GO:0009507; C:chloroplast; IEA:EnsemblPlants. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 2. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000001568}; KW Reference proteome {ECO:0000313|Proteomes:UP000001568}. FT DOMAIN 295 463 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 519 AA; 58233 MW; FAC0FF72FB5D958C CRC64; MSWEEIIERR HGARGTTLAI DASSATDATV GAGREREDLW GWDARPERVV VVGVAGKNRS YESAGEFDLE DSLDELERLV NTAGCEVVGR MTQRLARGPA PATYLGSGKI GELREMCGLP RAMEADEEDD DEREDDEDDE IFWEDDEDED EDEERSRDRR NGFRVDAAAV DIVIFDDELS PKQARNLERK LGSKVRICDR TALILDIFSQ RAQTAEGQLQ VEMAQLEYEM PRLTKMWSHL ERQSGSGAVK GMGEKQIEID KRLLRERKSL LNAKIESMRT HREQYRQKRK AERVPIVSLA GYTNAGKSSL LNKLTNAEVL AEDKLFATLD PTTRRLELAN GMTVLMTDTV GFIQKLPTQL VAAFRATLEE VLESSLILHV VDISSDLSEA HMSTVDSVLD ELDAGEIPQL LVWNKIDNVL DEEERLEIEI AAEDAGAVVV STLTGEGLDA LQDKIVEIIK KRTLSRCEML IPYERGALIG EIRRTGFVES EEFLENGTRV VAHLPVGMAR RKDVVVYLT // ID A4SYD5_POLAQ Unreviewed; 387 AA. AC A4SYD5; DT 15-MAY-2007, integrated into UniProtKB/TrEMBL. DT 15-MAY-2007, sequence version 1. DT 05-JUL-2017, entry version 68. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Pnuc_1285 {ECO:0000313|EMBL:ABP34499.1}; OS Polynucleobacter asymbioticus (strain DSM 18221 / CIP 109841 / OS QLW-P1DMWA-1) (Polynucleobacter necessarius subsp. asymbioticus). OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Polynucleobacter. OX NCBI_TaxID=312153 {ECO:0000313|EMBL:ABP34499.1, ECO:0000313|Proteomes:UP000000231}; RN [1] {ECO:0000313|EMBL:ABP34499.1, ECO:0000313|Proteomes:UP000000231} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 18221 / CIP 109841 / QLW-P1DMWA-1 RC {ECO:0000313|Proteomes:UP000000231}; RX PubMed=22675600; DOI=10.4056/sigs.2395367; RA Meincke L., Copeland A., Lapidus A., Lucas S., Berry K.W., RA Del Rio T.G., Hammon N., Dalin E., Tice H., Pitluck S., Richardson P., RA Bruce D., Goodwin L., Han C., Tapia R., Detter J.C., Schmutz J., RA Brettin T., Larimer F., Land M., Hauser L., Kyrpides N.C., Ivanova N., RA Goker M., Woyke T., Wu Q.L., Pockl M., Hahn M.W., Klenk H.P.; RT "Complete genome sequence of Polynucleobacter necessarius subsp. RT asymbioticus type strain (QLW-P1DMWA-1(T))."; RL Stand. Genomic Sci. 6:74-83(2012). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000655; ABP34499.1; -; Genomic_DNA. DR ProteinModelPortal; A4SYD5; -. DR STRING; 312153.Pnuc_1285; -. DR EnsemblBacteria; ABP34499; ABP34499; Pnuc_1285. DR KEGG; pnu:Pnuc_1285; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000000231; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000000231}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Hydrolase {ECO:0000313|EMBL:ABP34499.1}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000000231}. FT DOMAIN 173 342 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 139 169 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 387 AA; 43161 MW; 3E2E53FA1DAEFDAC CRC64; MAELSLLADS AGSIPTASVI ARKGRTDPAL FIGSGKANEL KKVMEEQEAE LAIFNHPLSP TQQRNLERHI GRHVMDRTGL ILDIFSQRAQ SHIGKTQVEL AQVRYRMSRL VRAWSHLERQ RGGIGVRGGP GETQMELDRR MLATKAKRLE NELEKLQRQQ RTQRRARNRK DVFSVSLVGY TNAGKSTLFN ALTKAGTYAA DQLFATLDTT SRRVHLEGVG SIVVSDTVGF IRDLPHQLVE AFRATLDETI HADLILHVID ACSPVAREQK AEVEAVLEEI GADDIPRIEV MNKIDLMPQT FTRGAVLERD GQGFPSQVFL SAQTGLGLDL LRSALAECSQ MTDRIRVEHN RAKKQMAPDE FLAPLPERPE TAEFNPIPNR SYLSNDT // ID A4VQN9_PSEU5 Unreviewed; 419 AA. AC A4VQN9; DT 29-MAY-2007, integrated into UniProtKB/TrEMBL. DT 29-MAY-2007, sequence version 1. DT 30-AUG-2017, entry version 72. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:ABP81290.1}; GN OrderedLocusNames=PST_3667 {ECO:0000313|EMBL:ABP81290.1}; OS Pseudomonas stutzeri (strain A1501). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=379731 {ECO:0000313|EMBL:ABP81290.1, ECO:0000313|Proteomes:UP000000233}; RN [1] {ECO:0000313|Proteomes:UP000000233} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=A1501 {ECO:0000313|Proteomes:UP000000233}; RA Yan Y., Yang J., Dou Y., Ping S., Chen M., Yao Z., Li H., Lu W., RA Zhang W., Peng J., Liu W., He S., Geng L., Zhang X., Yang F., Li D., RA Lin Z., Wang Y., Elmerich C., Lin M., Jin Q.; RT "Complete genome sequence of the metabolically versatile and root- RT associated nitrogen-fixing bacterium Pseudomonas stutzeri A1501."; RL Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000304; ABP81290.1; -; Genomic_DNA. DR ProteinModelPortal; A4VQN9; -. DR STRING; 379731.PST_3667; -. DR EnsemblBacteria; ABP81290; ABP81290; PST_3667. DR KEGG; psa:PST_3667; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000000233; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000000233}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000000233}. FT DOMAIN 185 352 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 151 178 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 419 AA; 47329 MW; 2CEA0F07FD4F2B80 CRC64; MHLDGQDPAA REDPQEFQEL ARSAGAETVG FVNVSRHQPS AKFLIGSGKV EELHDLVKEG EAELVIFNHT LTPSQERNLE RALECRVLDR TGLILDIFAQ RARTHEGKLQ VELAQLEHMS TRLVRGWTHL ERQKGGIGLR GPGETQLETD RRLLRVRIRQ IKQRLEKVRG QREQARRGRR RADIPSVSLV GYTNAGKSTL FNALTESEVY AANQLFATLD PTLRRLELED VGPVILADTV GFIRHLPHKL VESFRATLEE SSNADLLLHV IDAHEPERDQ QIEQVLAVLG EIGANELPML EVYNKLDLLE GIEPQIQRDA DGKPQRVWVS ARDGLGLDLL RQAVAELLGD DLFVGTLCLP QRLGRLRAQF FELGAVQRET HDEEGGSLLE VRLPRVELNR LISREGLRVD EFIEQHTLQ // ID A4VVZ2_STRSY Unreviewed; 416 AA. AC A4VVZ2; DT 29-MAY-2007, integrated into UniProtKB/TrEMBL. DT 29-MAY-2007, sequence version 1. DT 07-JUN-2017, entry version 73. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=SSU05_1315 {ECO:0000313|EMBL:ABP90281.1}; OS Streptococcus suis (strain 05ZYH33). OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=391295 {ECO:0000313|EMBL:ABP90281.1, ECO:0000313|Proteomes:UP000000243}; RN [1] {ECO:0000313|EMBL:ABP90281.1, ECO:0000313|Proteomes:UP000000243} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=05ZYH33 {ECO:0000313|EMBL:ABP90281.1, RC ECO:0000313|Proteomes:UP000000243}; RX PubMed=17375201; DOI=10.1371/journal.pone.0000315; RG BGI; RA Chen C., Tang J., Dong W., Wang C., Feng Y., Wang J., Zheng F., RA Pan X., Liu D., Li M., Song Y., Zhu X., Sun H., Feng T., Guo Z., RA Ju A., Ge J., Dong Y., Sun W., Jiang Y., Wang J., Yan J., Yang H., RA Wang X., Gao G.F., Yang R., Wang J., Yu J.; RT "A glimpse of streptococcal toxic shock syndrome from comparative RT genomics of S. suis 2 Chinese isolates."; RL PLoS ONE 2:E315-E315(2007). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000407; ABP90281.1; -; Genomic_DNA. DR ProteinModelPortal; A4VVZ2; -. DR STRING; 391295.SSU05_1315; -. DR EnsemblBacteria; ABP90281; ABP90281; SSU05_1315. DR KEGG; ssu:SSU05_1315; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000000243; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000000243}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000000243}. FT DOMAIN 199 360 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 158 192 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 416 AA; 47095 MW; 2B62408D5AFD8DE6 CRC64; MIETQKEQER ALLVGVELQQ TDNFDVSMEE LASLAKTAGA LVKGVYTQKR EKYDSKTFVG SGKLDEIAQM VEADEIDTVI VNNRLTPRQN VNLEEILGVK VIDRMQLILD IFAMRARSHE GKLQVHLAQL KYMLPRLVGQ GIMLSRQAGG IGSRGPGESQ LELNRRSIRN QIHDIERQLK TVEKNRATVR ERRLQSGVFK IGLIGYTNAG KSTIMNAMTD KRQYEADELF ATLDATTKQI NLADKFNVTL TDTVGFIQDL PTELISAFKS TLEESMNVDL LLHIIDASDP NHSEQEQVVL DILKDLDMLD IPRLALYNKL DKTDDSFTPS QFPHVMLSTK DENAKGHIQM MVLAKIKTMF ERFEVRVPLA ESYKLHDLAT LALIENRTYE EDVEVVSGYI ASSNKWKLEE FYDGLS // ID A4W5R4_ENT38 Unreviewed; 426 AA. AC A4W5R4; DT 29-MAY-2007, integrated into UniProtKB/TrEMBL. DT 29-MAY-2007, sequence version 1. DT 30-AUG-2017, entry version 74. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Ent638_0356 {ECO:0000313|EMBL:ABP59044.1}; OS Enterobacter sp. (strain 638). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; OC Enterobacteriaceae; Enterobacter. OX NCBI_TaxID=399742 {ECO:0000313|EMBL:ABP59044.1, ECO:0000313|Proteomes:UP000000230}; RN [1] {ECO:0000313|Proteomes:UP000000230} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=638 {ECO:0000313|Proteomes:UP000000230}; RX PubMed=20485560; DOI=10.1371/journal.pgen.1000943; RA Taghavi S., van der Lelie D., Hoffman A., Zhang Y.B., Walla M.D., RA Vangronsveld J., Newman L., Monchy S.; RT "Genome sequence of the plant growth promoting endophytic bacterium RT Enterobacter sp. 638."; RL PLoS Genet. 6:E1000943-E1000943(2010). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000653; ABP59044.1; -; Genomic_DNA. DR RefSeq; WP_011915617.1; NC_009436.1. DR ProteinModelPortal; A4W5R4; -. DR STRING; 399742.Ent638_0356; -. DR EnsemblBacteria; ABP59044; ABP59044; Ent638_0356. DR GeneID; 32442475; -. DR KEGG; ent:Ent638_0356; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR Proteomes; UP000000230; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000000230}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Hydrolase {ECO:0000313|EMBL:ABP59044.1}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000000230}. FT DOMAIN 198 365 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 426 AA; 48097 MW; 73BB3520A38719C0 CRC64; MFDRYDAGEH AVLVHIYFTQ DKDKEDLEEF EALVSSAGVE AMQVITGSRK APHPKFFVGE GKAIEIAEAV KATGASVVLF DHALSPAQER NLESLCECRV IDRTGLILDI FAQRARTHEG KLQVELAQLR HLATRLVRGW THLERQKGGI GLRGPGETQL ETDRRLLRGR ITQILSRLAR VEKRREQGRR SRTKADIPTV SLVGYTNAGK STLFNQITNA EVYAADQLFA TLDPTLRRID VADVGETVLA DTVGFIRHLP HDLVAAFKAT LQETRQATLL LHIIDAADFR LQENIDAVNT VLEEIEADDI PTLLVMNKID MLEDFEPRID RDDENKPIRV WLSAQTGVGV PLLFQALTER LSGEVAQHTL RLPPQEGKLR SRFYQLQAIE KEWMEDDGSV GMQVRMPIVD WRRLCKQEPT LIDYVV // ID A4X4W5_SALTO Unreviewed; 494 AA. AC A4X4W5; DT 29-MAY-2007, integrated into UniProtKB/TrEMBL. DT 29-MAY-2007, sequence version 1. DT 07-JUN-2017, entry version 71. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Strop_1449 {ECO:0000313|EMBL:ABP53915.1}; OS Salinispora tropica (strain ATCC BAA-916 / DSM 44818 / CNB-440). OC Bacteria; Actinobacteria; Micromonosporales; Micromonosporaceae; OC Salinispora. OX NCBI_TaxID=369723 {ECO:0000313|EMBL:ABP53915.1, ECO:0000313|Proteomes:UP000000235}; RN [1] {ECO:0000313|Proteomes:UP000000235} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-916 / DSM 44818 / CNB-440 RC {ECO:0000313|Proteomes:UP000000235}; RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., RA Dalin E., Tice H., Pitluck S., Sun H., Schmutz J., Larimer F., RA Land M., Hauser L., Kyrpides N., Kim E., Jensen P.R., Moore B.S., RA Udwary D.W., Richardson P.; RT "Complete sequence of Salinispora tropica CNB-440."; RL Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000667; ABP53915.1; -; Genomic_DNA. DR RefSeq; WP_011905347.1; NC_009380.1. DR ProteinModelPortal; A4X4W5; -. DR STRING; 369723.Strop_1449; -. DR EnsemblBacteria; ABP53915; ABP53915; Strop_1449. DR GeneID; 5057902; -. DR KEGG; stp:Strop_1449; -. DR PATRIC; fig|369723.5.peg.1478; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000000235; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000000235}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000000235}. FT DOMAIN 255 420 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 494 AA; 53729 MW; 53F26A7068668BDA CRC64; MREQETFLPD EGDEFDATTG EFELSERQAL RRVPGLSTEL TDITEVEYRQ LRLERVVLVG VWTEGSQQDA ENSLVELAAL AETAGSQVLE GLIQRRQRPD PATYVGRGKV DDLGAAVLAS GADTVICDGE LSPSQLRNLE QRTKVKVVDR TALILDIFAQ HAKSREGKAQ VELAQLEYLL PRLRGWGETL SRQSGGSGRG GGAGGGVGLR GPGETKLETD RRRIRHRIAR LRREIKGMRT VRQTKRARRY RNEVPAVAIA GYTNAGKSSL LNQLTGAGVL VENALFATLD PTIRKATTSD GRNFTFSDTV GFVRHLPHQI VEAFRSTLEE VAEADLVVHV VDGTHPDPEE QVRAVRAVLA EVGADRLPEL LVVNKTDAAG EETLLRLKRL WPEAIFVSAH SGYGVDDLRR SVEARLPRPA VEVRAVLPYD RGDLVARVYQ QGEVLSTAHL PEGTLLHVRV GAALAAELAP FQSIEATDPG PMPAPAAAGS GARS // ID A4XI38_CALS8 Unreviewed; 509 AA. AC A4XI38; DT 29-MAY-2007, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 2. DT 07-JUN-2017, entry version 71. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Csac_0959 {ECO:0000313|EMBL:ABP66573.2}; OS Caldicellulosiruptor saccharolyticus (strain ATCC 43494 / DSM 8903 / OS Tp8T 6331). OC Bacteria; Firmicutes; Clostridia; Thermoanaerobacterales; OC Thermoanaerobacterales Family III. Incertae Sedis; OC Caldicellulosiruptor. OX NCBI_TaxID=351627 {ECO:0000313|EMBL:ABP66573.2, ECO:0000313|Proteomes:UP000000256}; RN [1] {ECO:0000313|Proteomes:UP000000256} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43494 / DSM 8903 / Tp8T 6331 RC {ECO:0000313|Proteomes:UP000000256}; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., RA Pitluck S., Kiss H., Brettin T., Bruce D., Han C., Schmutz J., RA Larimer F., Land M., Hauser L., Kyrpides N., Lykidis A., RA van de Werken H.J.G., Verhaart M.R.A., VanFossen A.L., Lewis D.L., RA Nichols J.D., Goorissen H.P., van Niel E.W.J., Stams F.J.M., RA Willquist K.U., Ward D.E., van der Oost J., Kelly R.M., Kengen S.M.W., RA Richardson P.; RT "Genome sequence of the thermophilic hydrogen-producing bacterium RT Caldicellulosiruptor saccharolyticus DSM 8903."; RL Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000679; ABP66573.2; -; Genomic_DNA. DR RefSeq; WP_011916519.1; NC_009437.1. DR STRING; 351627.Csac_0959; -. DR EnsemblBacteria; ABP66573; ABP66573; Csac_0959. DR KEGG; csc:Csac_0959; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000000256; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000000256}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000000256}. FT DOMAIN 351 509 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 310 344 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 509 AA; 58625 MW; E93CDC568C61433E CRC64; MIQKLKFHQT EEYMIDEFVY NTLKEFSLNL NKEIAIALNR KGRIEEVLIE KKEFAELENQ DSFPKKAALI FTRLSSASHP SILDLSILIM KKYDYVMTIS LKTEEASIAF WGSQLKEVEI IGPHKIEYFY NLDISSKISE VDEKQKEREK IHEILVEKEE KALLVDVWTK SSSELDRHLL EELESLCKTA GVKVVDKVVQ VRRNIDPAYF IGKGKAEEIF SICQQKDIDV VIFNRELSPA QIKNLEELLL RKVIDRTDVI LDIFARRART REGKLQVELA QLLTLLPRLR GTGVLLSRLG GGIGTRGPGE TKLEIDRRHI QRRIEEIKKE LEKVKKSREV QRKSRIENQV PVVSIIGYTN AGKSTLMNRI SKADVLVEDK LFATLDTTTR RVYHKGKEFL LTDTVGFIRN LPHHLVEAFS STLEEVKYSN LILNVVDISD PYYYDHIKVS ENLLKHLGAE NIPLIRVYNK IDKVDLSTVD VFDNVPHVFI CAQDGRGIDN LLDMIVERI // ID A4XPY8_PSEMY Unreviewed; 433 AA. AC A4XPY8; DT 29-MAY-2007, integrated into UniProtKB/TrEMBL. DT 29-MAY-2007, sequence version 1. DT 30-AUG-2017, entry version 73. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Pmen_0636 {ECO:0000313|EMBL:ABP83404.1}; OS Pseudomonas mendocina (strain ymp). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=399739 {ECO:0000313|EMBL:ABP83404.1, ECO:0000313|Proteomes:UP000000229}; RN [1] {ECO:0000313|EMBL:ABP83404.1, ECO:0000313|Proteomes:UP000000229} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ymp {ECO:0000313|Proteomes:UP000000229}; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., RA Dalin E., Tice H., Pitluck S., Kiss H., Brettin T., Detter J.C., RA Bruce D., Han C., Schmutz J., Larimer F., Land M., Hauser L., RA Kyrpides N., Mikhailova N., Hersman L., Dubois J., Maurice P., RA Richardson P.; RT "Complete sequence of Pseudomonas mendocina ymp."; RL Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000680; ABP83404.1; -; Genomic_DNA. DR RefSeq; WP_003246509.1; NC_009439.1. DR ProteinModelPortal; A4XPY8; -. DR STRING; 399739.Pmen_0636; -. DR EnsemblBacteria; ABP83404; ABP83404; Pmen_0636. DR GeneID; 5109598; -. DR KEGG; pmy:Pmen_0636; -. DR PATRIC; fig|399739.8.peg.643; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000000229; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000000229}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Hydrolase {ECO:0000313|EMBL:ABP83404.1}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000000229}. FT DOMAIN 199 366 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 165 192 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 433 AA; 48969 MW; 056791C4B84F4C7F CRC64; MFFERHEGGE RAILVHLEGQ DSEASEDPQE FQELAMSAGA DMVAFFSVPS SRLTAKYLIG SGKVEELRDQ VRAIEAELVI FNHTLTPSQE RNLERAFECR VLDRTGLILD IFAQRARTHE GKLQVELAQL DHMSTRLVRG WTHLERQKGG IGLRGPGETQ LETDRRLLRV RIRQIKQKLE KVRSQREQAR RGRKRADIPS VSLVGYTNAG KSTLFNALTA SEVYAADQLF ATLDPTLRRL ELDDLGPIVL ADTVGFIRHL PHKLVEAFRA TLEESSNSDL LLHVIDAHEP ERMAQIEQVQ AVLKEIGAHE LPMLEVYNKL DLLEGVEPQI QRDADGKPQR VWLSAREGRG LELLRQAVAE LLGEDLFVGV LQLPQRLGRL RAQFFELGAV QSEGHDEQGQ SLLSVRLPRI ELNRLVSREG LEPQAFIEQH TLQ // ID A4YJ13_METS5 Unreviewed; 350 AA. AC A4YJ13; DT 29-MAY-2007, integrated into UniProtKB/TrEMBL. DT 29-MAY-2007, sequence version 1. DT 07-JUN-2017, entry version 68. DE SubName: Full=GTP-binding protein HflX {ECO:0000313|EMBL:ABP96415.1}; DE EC=3.1.5.- {ECO:0000313|EMBL:ABP96415.1}; GN OrderedLocusNames=Msed_2277 {ECO:0000313|EMBL:ABP96415.1}; OS Metallosphaera sedula (strain ATCC 51363 / DSM 5348 / JCM 9185 / NBRC OS 15509 / TH2). OC Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae; OC Metallosphaera. OX NCBI_TaxID=399549 {ECO:0000313|EMBL:ABP96415.1, ECO:0000313|Proteomes:UP000000242}; RN [1] {ECO:0000313|EMBL:ABP96415.1, ECO:0000313|Proteomes:UP000000242} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51363 / DSM 5348 / JCM 9185 / NBRC 15509 / TH2 RC {ECO:0000313|Proteomes:UP000000242}; RX PubMed=18083856; DOI=10.1128/AEM.02019-07; RA Auernik K.S., Maezato Y., Blum P.H., Kelly R.M.; RT "The genome sequence of the metal-mobilizing, extremely RT thermoacidophilic archaeon Metallosphaera sedula provides insights RT into bioleaching-associated metabolism."; RL Appl. Environ. Microbiol. 74:682-692(2008). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000682; ABP96415.1; -; Genomic_DNA. DR RefSeq; WP_012022202.1; NC_009440.1. DR ProteinModelPortal; A4YJ13; -. DR STRING; 399549.Msed_2277; -. DR EnsemblBacteria; ABP96415; ABP96415; Msed_2277. DR GeneID; 5104229; -. DR KEGG; mse:Msed_2277; -. DR eggNOG; arCOG00353; Archaea. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG093Z07D6; -. DR BioCyc; MSED399549:GH1O-2282-MONOMER; -. DR Proteomes; UP000000242; Chromosome. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW. DR CDD; cd01878; HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000242}; KW Hydrolase {ECO:0000313|EMBL:ABP96415.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000242}. FT DOMAIN 177 350 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 350 AA; 39339 MW; B7E28A9151C44744 CRC64; MKATLFVSQD FADEAVSLLE TAGYEVEKTY PLPSKPNRLY YIPQDKLKLL QDQETDAVVV FDLLSPRHFI NLNRSLNGKK VLDKLLILLE IFALHAGSKE AKLQIELARL KYELPIIKDI YSKTKISEQQ GPLGAGTYGV ESALRLYNRK ISKITKELEG LKKFREMQMQ NRREEFPYVA ITGYTNAGKT SIFNALTGLN KPTDQSMFTT TAPKRYAIPI GSKKVTLVDT VGFIRGIPPQ IIDAFFVTLS EIRYANALLL VVDISLEDSL LLEMTRSSFE ILRELGISGK PMIIVGNKAD LVDGRSKEKM DMVYSLSDNL YSPVVDAILV SAKKGWNLDS LRDKIFSLVN // ID A4YUP2_BRASO Unreviewed; 459 AA. AC A4YUP2; DT 29-MAY-2007, integrated into UniProtKB/TrEMBL. DT 29-MAY-2007, sequence version 1. DT 07-JUN-2017, entry version 71. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=BRADO3854 {ECO:0000313|EMBL:CAL77618.1}; OS Bradyrhizobium sp. (strain ORS 278). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Bradyrhizobiaceae; Bradyrhizobium. OX NCBI_TaxID=114615 {ECO:0000313|EMBL:CAL77618.1, ECO:0000313|Proteomes:UP000001994}; RN [1] {ECO:0000313|EMBL:CAL77618.1, ECO:0000313|Proteomes:UP000001994} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ORS 278 {ECO:0000313|Proteomes:UP000001994}; RX PubMed=17540897; DOI=10.1126/science.1139548; RA Giraud E., Moulin L., Vallenet D., Barbe V., Cytryn E., Avarre J.C., RA Jaubert M., Simon D., Cartieaux F., Prin Y., Bena G., Hannibal L., RA Fardoux J., Kojadinovic M., Vuillet L., Lajus A., Cruveiller S., RA Rouy Z., Mangenot S., Segurens B., Dossat C., Franck W.L., Chang W.S., RA Saunders E., Bruce D., Richardson P., Normand P., Dreyfus B., RA Pignol D., Stacey G., Emerich D., Vermeglio A., Medigue C., RA Sadowsky M.; RT "Legumes symbioses: absence of nod genes in photosynthetic RT bradyrhizobia."; RL Science 316:1307-1312(2007). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CU234118; CAL77618.1; -; Genomic_DNA. DR RefSeq; WP_011926756.1; NC_009445.1. DR ProteinModelPortal; A4YUP2; -. DR STRING; 114615.BRADO3854; -. DR EnsemblBacteria; CAL77618; CAL77618; BRADO3854. DR KEGG; bra:BRADO3854; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000001994; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000001994}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000001994}. FT DOMAIN 226 400 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 459 AA; 50700 MW; DC647C1A3DC9156F CRC64; MEPRDRDGTI GLARPDDVKT TGRVIVVGPY LRTRRGDDGA PASHSEMRDV EARIDEAAGL ARAINLTVAE SILALIGQIR PATYLGKGKV DEIAGVIASQ EAELVVMDCA LSPIQQRNLE KAWNTKVLDR TGLILEIFGR RAKTKEGALQ VELAHLNYQR SRLVRSWTHL ERQRGGFGFM GGPGETQIEA DRRLIGDRIT RLENELKKVQ ATRRLHRAGR QRVPYRVVAL VGYTNAGKST LFNRLTRADV QAADMLFATL DPTLRAISLP HGGKAMLSDT VGFISNLPTQ LVAAFRATLE EVLEADVILH VRDMSHEDAE AQQHDVELVL SQLGIDPEAT DTIIEVWNKI DRLDDAAREN LANIAARRPP ERPCFMVSAE TGEGVDALLQ AIEDRLAAAR TTLDLTIDAA DGAGISWLHR NAEVLSKELH EGHYDMTVRV DATKRDIVVE RYHGIPRVA // ID A5D0F0_PELTS Unreviewed; 434 AA. AC A5D0F0; DT 12-JUN-2007, integrated into UniProtKB/TrEMBL. DT 12-JUN-2007, sequence version 1. DT 07-JUN-2017, entry version 74. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=HflX {ECO:0000313|EMBL:BAF60301.1}; GN Synonyms=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=PTH_2120 {ECO:0000313|EMBL:BAF60301.1}; OS Pelotomaculum thermopropionicum (strain DSM 13744 / JCM 10971 / SI). OC Bacteria; Firmicutes; Clostridia; Clostridiales; Peptococcaceae; OC Pelotomaculum. OX NCBI_TaxID=370438 {ECO:0000313|EMBL:BAF60301.1, ECO:0000313|Proteomes:UP000006556}; RN [1] {ECO:0000313|Proteomes:UP000006556} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 13744 / JCM 10971 / SI {ECO:0000313|Proteomes:UP000006556}; RX PubMed=18218977; DOI=10.1101/gr.7136508; RA Kosaka T., Kato S., Shimoyama T., Ishii S., Abe T., Watanabe K.; RT "The genome of Pelotomaculum thermopropionicum reveals niche- RT associated evolution in anaerobic microbiota."; RL Genome Res. 18:442-448(2008). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AP009389; BAF60301.1; -; Genomic_DNA. DR ProteinModelPortal; A5D0F0; -. DR STRING; 370438.PTH_2120; -. DR EnsemblBacteria; BAF60301; BAF60301; PTH_2120. DR KEGG; pth:PTH_2120; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000006556; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000006556}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000006556}. FT DOMAIN 214 378 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 173 207 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 434 AA; 47923 MW; EAE463C581541355 CRC64; MRPEFLAKGE SLLEHRPENG REKAVLVGVE LPGDETWQSA YSMQELARLA DTAGADAVHQ FIQKRDRPDP ATLLGRGKAS EIAALCRNSG AGLVIFDREL TPAQARNLEE ITGAKVIDRT QLILDIFARR ARTREGRLQV ELAQLSYLLP RLTGLGGQLS RLGGGIGTRG PGETKLEMDR RRVRRRIAAL KKEIKEVRER RDLLRRNRKE VPFPLVAIVG YTNAGKSTLL KKLTGADVLV EDKLFATLDP VTRRVVLPDN ETILLTDTVG FIQNLPHHLV AAFRATLEEV MEADLLLHVV DASHPYMEEQ IGAVNEVLAS LGAAGKPLVM VYNKADLLPD AKFFREKSSP PAVAVSALKG WGMEDLLAAI ARALPGRRIK ASFFIPYRKS GLLPVLHEKG RVLREEHGNG GITVEAEIDA VWARRVEAKL KGQE // ID A5EVD7_DICNV Unreviewed; 428 AA. AC A5EVD7; DT 12-JUN-2007, integrated into UniProtKB/TrEMBL. DT 12-JUN-2007, sequence version 1. DT 07-JUN-2017, entry version 68. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:ABQ13600.1}; GN OrderedLocusNames=DNO_0596 {ECO:0000313|EMBL:ABQ13600.1}; OS Dichelobacter nodosus (strain VCS1703A). OC Bacteria; Proteobacteria; Gammaproteobacteria; Cardiobacteriales; OC Cardiobacteriaceae; Dichelobacter. OX NCBI_TaxID=246195 {ECO:0000313|EMBL:ABQ13600.1, ECO:0000313|Proteomes:UP000000248}; RN [1] {ECO:0000313|EMBL:ABQ13600.1, ECO:0000313|Proteomes:UP000000248} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=VCS1703A {ECO:0000313|EMBL:ABQ13600.1, RC ECO:0000313|Proteomes:UP000000248}; RX PubMed=17468768; DOI=10.1038/nbt1302; RA Myers G.S., Parker D., Al-Hasani K., Kennan R.M., Seemann T., Ren Q., RA Badger J.H., Selengut J.D., Deboy R.T., Tettelin H., Boyce J.D., RA McCarl V.P., Han X., Nelson W.C., Madupu R., Mohamoud Y., Holley T., RA Fedorova N., Khouri H., Bottomley S.P., Whittington R.J., Adler B., RA Songer J.G., Rood J.I., Paulsen I.T.; RT "Genome sequence and identification of candidate vaccine antigens from RT the animal pathogen Dichelobacter nodosus."; RL Nat. Biotechnol. 25:569-575(2007). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000513; ABQ13600.1; -; Genomic_DNA. DR RefSeq; WP_012030930.1; NC_009446.1. DR ProteinModelPortal; A5EVD7; -. DR STRING; 246195.DNO_0596; -. DR EnsemblBacteria; ABQ13600; ABQ13600; DNO_0596. DR KEGG; dno:DNO_0596; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000000248; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000000248}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000000248}. FT DOMAIN 200 366 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 166 193 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 428 AA; 48427 MW; BFB47B98F1BF6E6B CRC64; MFDVEHSQKG ERAALIQVDI GRAFDAAVEE EFHLLAASAG AQIVWTKSIV RGEAEARYLI GKGQVEEIAR AVCEHQIELV IFNAQLTPSQ ERNLEKILQA RVLDRNGLVL DIFAQRARSH EGKLQVELAQ LNHLSTRLVR GWTHLERQKG GIGLRGPGET QLETDRRLLA IRIRQLEKKL EKVARQRDET RKNRARKDRP TVALAGYTNS GKSTLFNLLT DANVLTQDLL FATLDPTWRK LNHASNMMIL LADTVGFVSD LPHELVAAFQ STLEETIYAD LILQVIDISY KEYIARTEIV DDVLAEIGAE AVPRIRVYNK IDLVGKEPQV IVDEHGLART VFVSALTGAG RDLIADAIVQ FFQQYQKEGW ITLQPHEGAL RAELFNEKAV LEERIAADGA MNLRIVIDEK RLQQLQSRYN RRFELKSY // ID A5FKR3_FLAJ1 Unreviewed; 409 AA. AC A5FKR3; DT 12-JUN-2007, integrated into UniProtKB/TrEMBL. DT 12-JUN-2007, sequence version 1. DT 07-JUN-2017, entry version 72. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Fjoh_1171 {ECO:0000313|EMBL:ABQ04204.1}; OS Flavobacterium johnsoniae (strain ATCC 17061 / DSM 2064 / UW101) OS (Cytophaga johnsonae). OC Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales; OC Flavobacteriaceae; Flavobacterium. OX NCBI_TaxID=376686 {ECO:0000313|EMBL:ABQ04204.1, ECO:0000313|Proteomes:UP000006694}; RN [1] {ECO:0000313|EMBL:ABQ04204.1, ECO:0000313|Proteomes:UP000006694} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 17061 / DSM 2064 / UW101 RC {ECO:0000313|Proteomes:UP000006694}; RX PubMed=19717629; DOI=10.1128/AEM.01495-09; RA McBride M.J., Xie G., Martens E.C., Lapidus A., Henrissat B., RA Rhodes R.G., Goltsman E., Wang W., Xu J., Hunnicutt D.W., RA Staroscik A.M., Hoover T.R., Cheng Y.Q., Stein J.L.; RT "Novel features of the polysaccharide-digesting gliding bacterium RT Flavobacterium johnsoniae as revealed by genome sequence analysis."; RL Appl. Environ. Microbiol. 75:6864-6875(2009). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000685; ABQ04204.1; -; Genomic_DNA. DR RefSeq; WP_012023255.1; NC_009441.1. DR ProteinModelPortal; A5FKR3; -. DR STRING; 376686.Fjoh_1171; -. DR EnsemblBacteria; ABQ04204; ABQ04204; Fjoh_1171. DR GeneID; 31764048; -. DR KEGG; fjo:Fjoh_1171; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000006694; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000006694}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000006694}. FT DOMAIN 200 386 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 409 AA; 47427 MW; 4E469A518D667754 CRC64; MLEKEVINFE KTAIVGIVTQ NQSEEKLNEY LDELEFLTFT AGGEVIKRFS QKMERPNPKT FVGTGKIDEI NLFVKENKIS TVIFDDELTP SQQKNISRII DCKILDRTNL ILDIFAQRAE TSYARTQVEL AQCIYLLPRL SGLWTHLERQ KGGIGMRGPG ETEIETDRRI VRDRISLLKE KIKTIDKQMS IQRSNRGAMV RVALVGYTNV GKSTLMNAIG KSEVFVENKL FATLDTTVRK VVIKNLPFLL SDTVGFIRKL PTQLVDSFKS TLDEVREADL LLHVVDISHP DFEDHIESVN QILQEIKSND KPTIMVFNKI DAYKHLTIDD DDLITERTRK HWTLDEWKQT WMSNVGHDKA LFISATQKEN FEEFREMVYE AVRQIHITRF PYNNFLYPDY KDAIEKEEE // ID A5FZD2_ACICJ Unreviewed; 435 AA. AC A5FZD2; DT 12-JUN-2007, integrated into UniProtKB/TrEMBL. DT 12-JUN-2007, sequence version 1. DT 07-JUN-2017, entry version 69. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Acry_1761 {ECO:0000313|EMBL:ABQ30964.1}; OS Acidiphilium cryptum (strain JF-5). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales; OC Acetobacteraceae; Acidiphilium. OX NCBI_TaxID=349163 {ECO:0000313|EMBL:ABQ30964.1, ECO:0000313|Proteomes:UP000000245}; RN [1] {ECO:0000313|EMBL:ABQ30964.1, ECO:0000313|Proteomes:UP000000245} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=JF-5 {ECO:0000313|EMBL:ABQ30964.1, RC ECO:0000313|Proteomes:UP000000245}; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., RA Pitluck S., Sims D., Brettin T., Bruce D., Han C., Schmutz J., RA Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Magnuson T., RA Richardson P.; RT "Complete sequence of chromosome of Acidiphilium cryptum JF-5."; RL Submitted (MAY-2007) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000697; ABQ30964.1; -; Genomic_DNA. DR RefSeq; WP_007423554.1; NC_009484.1. DR ProteinModelPortal; A5FZD2; -. DR STRING; 349163.Acry_1761; -. DR EnsemblBacteria; ABQ30964; ABQ30964; Acry_1761. DR KEGG; acr:Acry_1761; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000000245; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000000245}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Hydrolase {ECO:0000313|EMBL:ABQ30964.1}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000000245}. FT DOMAIN 205 374 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 171 198 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 435 AA; 47293 MW; 64243B71085610E4 CRC64; MSIPTQAAPT RAAVLLPWEH GGRNGPREAE ARLAEAIGLT ASIGLVIAHD EIVQIRAHRP ATLFGEGQVR RIGESIAEAE IGVAVVDSTL SPVQQRNLER AWKCKVIDRT GLILDIFGER ARTAEGVLQV ELAHLAYQRS RLVRSWTHLE RQRGGFGFLG GPGETQIEAD RRLITDRIAR LRRELDEVRR TRALHRAARN RVPYPVVALV GYTNAGKSTL FNALTGATVH AQDQLFATLD PTMRLIVLPS GRQAILSDTV GFISDLPTEL VAAFRATLEE VAAADIILHV RDCAHPDSAA QRADVVSVLD GMARSGMIDE GWSSRCIEVM NKIDLLDPAA RDLPGASAIA VSALSGENLD TLRATIDARL AGAMQVATYW LAPADGAGLA WLYRHGEVIS RADGEDAIAI EVRLRPEDRA RFERDHEAAL HAPVP // ID A5GBD4_GEOUR Unreviewed; 546 AA. AC A5GBD4; DT 12-JUN-2007, integrated into UniProtKB/TrEMBL. DT 12-JUN-2007, sequence version 1. DT 07-JUN-2017, entry version 75. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Gura_0905 {ECO:0000313|EMBL:ABQ25111.1}; OS Geobacter uraniireducens (strain Rf4) (Geobacter uraniumreducens). OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfuromonadales; OC Geobacteraceae; Geobacter. OX NCBI_TaxID=351605 {ECO:0000313|EMBL:ABQ25111.1, ECO:0000313|Proteomes:UP000006695}; RN [1] {ECO:0000313|EMBL:ABQ25111.1, ECO:0000313|Proteomes:UP000006695} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Rf4 {ECO:0000313|EMBL:ABQ25111.1, RC ECO:0000313|Proteomes:UP000006695}; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., RA Pitluck S., Chertkov O., Brettin T., Bruce D., Han C., Schmutz J., RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., RA Shelobolina E., Aklujkar M., Lovley D., Richardson P.; RT "Complete sequence of Geobacter uraniireducens Rf4."; RL Submitted (MAY-2007) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000698; ABQ25111.1; -; Genomic_DNA. DR RefSeq; WP_011937835.1; NC_009483.1. DR ProteinModelPortal; A5GBD4; -. DR STRING; 351605.Gura_0905; -. DR EnsemblBacteria; ABQ25111; ABQ25111; Gura_0905. DR KEGG; gur:Gura_0905; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; EREVIIT; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000006695; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000006695}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000006695}. FT DOMAIN 369 542 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 328 355 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 546 AA; 61864 MW; 05DCFDFEA0CE4C4D CRC64; MKPSQLKGLE RLYRRRIPPD ELITPDLSRE MVELSREIRR QLGILVNRSG DVEYVLVGDE RGLYIPELAD YPLGKKLLRG LRLIHTHLKG EALSDDDLTD LALLRLDLVA ALQMSPNDGQ FFVQTACLAP PTLGKTPYKI EPPRPFDRFS MDFATFVDTL EKSLEKAVKG TKEVKGGEER GILISVTKLS HEEAQDSIEE LKELARTAGV EVLDAVIQRP RQFNPRFLMG EGKMRDVVIR ALQLGATLLV FDQELTPTQI RSISAMTELK VIDRSQLILD IFARRAKSLD GKVQVELAQL KYLLPRLTGR GVQMSRLMGG IGGRGPGETK LEVDRRRIRD RIAKLERELK ELSHGRYQRR QKRVKAGLPI ISIVGYTNAG KSTLLNTLTQ SAVFTENLLF ATLDTSTRRL RFPRDREVII TDTVGFIRSL PKSLMGAFKA TLEELQDADL LLHLVDCSNP RFEEQIGQVE TILAELDLGE KARLLVFNKS DLLSQLKKSD PLTFMKVRQV FRRLQAISIS AADRKSMEPL IEELQRRFWP DEAPVQ // ID A5GNT7_SYNPW Unreviewed; 568 AA. AC A5GNT7; DT 12-JUN-2007, integrated into UniProtKB/TrEMBL. DT 12-JUN-2007, sequence version 1. DT 07-JUN-2017, entry version 65. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:CAK24602.1}; GN OrderedLocusNames=SynWH7803_2176 {ECO:0000313|EMBL:CAK24602.1}; OS Synechococcus sp. (strain WH7803). OC Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; OC Synechococcus. OX NCBI_TaxID=32051 {ECO:0000313|EMBL:CAK24602.1, ECO:0000313|Proteomes:UP000001566}; RN [1] {ECO:0000313|Proteomes:UP000001566} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=WH7803 {ECO:0000313|Proteomes:UP000001566}; RG Genoscope; RL Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CT971583; CAK24602.1; -; Genomic_DNA. DR RefSeq; WP_011934064.1; NC_009481.1. DR ProteinModelPortal; A5GNT7; -. DR STRING; 32051.SynWH7803_2176; -. DR EnsemblBacteria; CAK24602; CAK24602; SynWH7803_2176. DR KEGG; syx:SynWH7803_2176; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; NPQTLWG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000001566; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000001566}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000001566}. FT DOMAIN 378 550 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 339 373 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 568 AA; 62253 MW; 1FC0BFB1BA188953 CRC64; MKQAHLAGRT RGLRPSQLRQ LERLSHRRHP QNAGSDLLTL ERLAELTSEL KQSLHLLIDA RGVCRLLWVG PLGESSRLDD QLPGGLRRRQ RWRLVSSLPG TQGVDLKPEG REAVIALDVA PSTWLRLQAA ATRSGTRPAA LWRADAAAAI GWRCDAIDAL SALCADETTP SAAEPAGVKD PGDHPGSQEE RVLLLTLIGA DPAINERELA ELEGLTRSAG ACPVAVCRQR LGQINPQTLW GTGKLQEAAV DVRRHGASLV ITDRELTPVQ ARNLERLLDC PVMDRSELIL DIFAQRATSA AGRLQVELAQ LRYRLPRLTG RGLSLSRQGG GIGTRGPGET QLEKDRRAIS RRIEHLSREL RQLGAHRARL RQQRSTLPRV ALVGYTNAGK SSLLNALCDR GQGRAVEAKN RLFATLDPTT RRLCLPQSGA APKELLITDT VGFIRELPEP LMQAFMATLE ETREADQLLL VVDLADPDWQ GQLTAVHSIL NGLHCQQPRQ VIANQIDRCD ASALEVIRTV EPEALYLSAT QGTGLKGLRS WLEQTFWETS PEQNCPSSSD QTSARAHG // ID A5I6G1_CLOBH Unreviewed; 594 AA. AC A5I6G1; A7G7P4; DT 26-JUN-2007, integrated into UniProtKB/TrEMBL. DT 26-JUN-2007, sequence version 1. DT 07-JUN-2017, entry version 84. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:CAL84643.1}; GN OrderedLocusNames=CBO3080 {ECO:0000313|EMBL:CAL84643.1}; OS Clostridium botulinum (strain Hall / ATCC 3502 / NCTC 13319 / Type A). OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=441771 {ECO:0000313|Proteomes:UP000001986}; RN [1] {ECO:0000313|EMBL:CAL84643.1, ECO:0000313|Proteomes:UP000001986} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Hall / ATCC 3502 / NCTC 13319 / Type A [Sanger] RC {ECO:0000313|Proteomes:UP000001986}; RX PubMed=17519437; DOI=10.1101/gr.6282807; RA Sebaihia M., Peck M.W., Minton N.P., Thomson N.R., Holden M.T.G., RA Mitchell W.J., Carter A.T., Bentley S.D., Mason D.R., Crossman L., RA Paul C.J., Ivens A., Wells-Bennik M.H.J., Davis I.J., RA Cerdeno-Tarraga A.M., Churcher C., Quail M.A., Chillingworth T., RA Feltwell T., Fraser A., Goodhead I., Hance Z., Jagels K., Larke N., RA Maddison M., Moule S., Mungall K., Norbertczak H., Rabbinowitsch E., RA Sanders M., Simmonds M., White B., Whithead S., Parkhill J.; RT "Genome sequence of a proteolytic (Group I) Clostridium botulinum RT strain Hall A and comparative analysis of the clostridial genomes."; RL Genome Res. 17:1082-1092(2007). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AM412317; CAL84643.1; -; Genomic_DNA. DR RefSeq; WP_012048095.1; NC_009698.1. DR RefSeq; YP_001255572.1; NC_009495.1. DR RefSeq; YP_001388809.1; NC_009698.1. DR ProteinModelPortal; A5I6G1; -. DR GeneID; 5187339; -. DR GeneID; 5398421; -. DR KEGG; cbh:CLC_2982; -. DR KEGG; cbo:CBO3080; -. DR PATRIC; fig|413999.7.peg.3058; -. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR Proteomes; UP000001986; Chromosome. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0043022; F:ribosome binding; IBA:GO_Central. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000001986}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000001986}. FT DOMAIN 362 538 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 159 182 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 594 AA; 67651 MW; C72D45878DCD57F0 CRC64; MIYGNIDGIR KTVLEELEKI YEMKIEKNEI INEELMNVLC KLTEQLNREI SVGISRKGGI IAVSVGDSTT VEMPEVEIKT NKLSSIRIVH THPNGNPKLS SVDLSALLKL KLDCMVAIGV EYEKITGFGV AFCTMEDSKL SIEEKYFKDI NSLLDFNLLN EINHIEQNLK NEELEYQEEE KVILVSIDDE ESIDELEELA KACNLKVVEK VLQNKNKIDS AYYIGTGKVG EIALIRQTLN ADVVIFDDEL SASQIRNLEE SIGTKVIDRN TLILDIFARR AKSKESKIQV ELAQLKYRLA RLTGLGLVLS RTGGGIGTKG PGEKKLETDK RHIKERIYDL KKELYKIKKV RETQRSKRND IPKVSLVGYT NAGKSTLRNK LCDTGIASAQ NKEKVFEADM LFATLDITTR AISLPNNEII TLTDTVGFVR KLPHELVEAF KSTLEEVIYS DLLLHVIDIS SDTAEKQIDA VNNVLEELGT ENKQIILVFN KIDKVSMERL NYFRDKFKDE KVIEISARLG INLEDLLKLI EETLPYKLAE VEYIIPYDKQ KTVAFLHRNS KIIEEEYREK GTYIKTKVDT EVYNKCQEFL VNKE // ID A5K4F0_PLAVS Unreviewed; 713 AA. AC A5K4F0; DT 10-JUL-2007, integrated into UniProtKB/TrEMBL. DT 10-JUL-2007, sequence version 1. DT 05-JUL-2017, entry version 53. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EDL45528.1}; GN ORFNames=PVX_091320 {ECO:0000313|EMBL:EDL45528.1}; OS Plasmodium vivax (strain Salvador I). OC Eukaryota; Alveolata; Apicomplexa; Aconoidasida; Haemosporida; OC Plasmodiidae; Plasmodium; Plasmodium (Plasmodium). OX NCBI_TaxID=126793 {ECO:0000313|Proteomes:UP000008333}; RN [1] {ECO:0000313|EMBL:EDL45528.1, ECO:0000313|Proteomes:UP000008333} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Salvador I {ECO:0000313|EMBL:EDL45528.1, RC ECO:0000313|Proteomes:UP000008333}; RX PubMed=18843361; DOI=10.1038/nature07327; RA Carlton J.M., Adams J.H., Silva J.C., Bidwell S.L., Lorenzi H., RA Caler E., Crabtree J., Angiuoli S.V., Merino E.F., Amedeo P., RA Cheng Q., Coulson R.M., Crabb B.S., Del Portillo H.A., Essien K., RA Feldblyum T.V., Fernandez-Becerra C., Gilson P.R., Gueye A.H., Guo X., RA Kang'a S., Kooij T.W., Korsinczky M., Meyer E.V., Nene V., Paulsen I., RA White O., Ralph S.A., Ren Q., Sargeant T.J., Salzberg S.L., RA Stoeckert C.J., Sullivan S.A., Yamamoto M.M., Hoffman S.L., RA Wortman J.R., Gardner M.J., Galinski M.R., Barnwell J.W., RA Fraser-Liggett C.M.; RT "Comparative genomics of the neglected human malaria parasite RT Plasmodium vivax."; RL Nature 455:757-763(2008). CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EDL45528.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AAKM01000005; EDL45528.1; -; Genomic_DNA. DR RefSeq; XP_001615255.1; XM_001615205.1. DR ProteinModelPortal; A5K4F0; -. DR STRING; 5855.PVX_091320; -. DR EnsemblProtists; EDL45528; EDL45528; PVX_091320. DR GeneID; 5474551; -. DR KEGG; pvx:PVX_091320; -. DR EuPathDB; PlasmoDB:PVX_091320; -. DR HOGENOM; HOG000282270; -. DR InParanoid; A5K4F0; -. DR OMA; IIVLHPI; -. DR Proteomes; UP000008333; Chromosome 9. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 4: Predicted; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000008333}; KW Reference proteome {ECO:0000313|Proteomes:UP000008333}. FT DOMAIN 465 635 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 248 273 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 713 AA; 81182 MW; D3346239EE54AC59 CRC64; MLRWSTTLRT FPRTQKRSFT NGSKKEIIVL HPILKKTKSG SKSFDEIIYD AQEALGLARS AGFKVANGIS MPLGGWTFFK RPSGSKGEGE GEGEGEGGDL ANSFREEDTF RGSRQSNVGA NAGAPSEVPP QGEDLEKKIA ESIIIKTNRI DNKFYFGKGK LNELSTYFLK HPTPYVFINA LLSPEQFRNL DMLFNGLLRS HHDELKLRRQ KQRGEDCLSV RVSEFSAEDD DGEEDARGEE LPYVEMYNEW MERQAEREER EEEHADLEEE EEHDDLEEEE EHADLGEQEE HAASGEEEEH AALGELNQWD VLHRHTADNC DVPLHVELFD RYSIILQILK SRAKNNLSKL QLELARANFI FNTYAEDNKS RMKYVKYIEN NVLGKSNFDY EEECSGQSAF HADRQMGGKN SYNHPGYTSS YIKSSETYKE YEKRIIHNLY AKLKKELGKC KNNNALQSSA RKHKGLIAVV GYTNVGKTKL INYLTKSNLK ARNLLFQTLD NAFKSANISD GHSTIFIDSI GFIQNIPFSL YESFKLTLEA IKSADVLIHV IDVCHPYREK HKKCVVDTLH KIGIPSDFLK CNMIEVWNKV DQLADEELLN LYKTKPKNVL PISAKVGTNC DVLIKIIQTM INRIKDVQVM TLQFSTMEAQ ERIPYLVKNF KVVPNSISYS SDGNTTFIKL VENPRNLRKY YERFDRGERG PSGGGARKGA ASS // ID A5N214_CLOK5 Unreviewed; 592 AA. AC A5N214; DT 10-JUL-2007, integrated into UniProtKB/TrEMBL. DT 10-JUL-2007, sequence version 1. DT 07-JUN-2017, entry version 73. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=CKL_3152 {ECO:0000313|EMBL:EDK35160.1}; OS Clostridium kluyveri (strain ATCC 8527 / DSM 555 / NCIMB 10680). OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=431943 {ECO:0000313|EMBL:EDK35160.1, ECO:0000313|Proteomes:UP000002411}; RN [1] {ECO:0000313|EMBL:EDK35160.1, ECO:0000313|Proteomes:UP000002411} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 8527 / DSM 555 / NCIMB 10680 RC {ECO:0000313|Proteomes:UP000002411}; RX PubMed=18218779; DOI=10.1073/pnas.0711093105; RA Seedorf H., Fricke W.F., Veith B., Brueggemann H., Liesegang H., RA Strittmatter A., Miethke M., Buckel W., Hinderberger J., Li F., RA Hagemeier C., Thauer R.K., Gottschalk G.; RT "The genome of Clostridium kluyveri, a strict anaerobe with unique RT metabolic features."; RL Proc. Natl. Acad. Sci. U.S.A. 105:2128-2133(2008). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000673; EDK35160.1; -; Genomic_DNA. DR RefSeq; WP_012103495.1; NC_009706.1. DR ProteinModelPortal; A5N214; -. DR STRING; 431943.CKL_3152; -. DR EnsemblBacteria; EDK35160; EDK35160; CKL_3152. DR KEGG; ckl:CKL_3152; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000002411; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000002411}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000002411}. FT DOMAIN 361 538 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 592 AA; 66991 MW; D71E7B03DC334067 CRC64; MIYGNTEGIR KSILDELEEI YDIKIPKDSV CSMEIVEILC KNTIHLNREI SVLINRKGKV LNISVGDSNS VNIEVYTWSN KLSGIRMIHT HPNGNSQLSK IDISALMKLK LDCISAIGVN DQGPTGMSLG FLSIKGDSVE SEVLSNLTLE EAANYNVLRK INEIEELVKN IYTLEEYEER AILVGTDSKE SLDELEELAR ACNVKVLEKV FQKRTTVDTA FYVGKGKVGE IGLIAQVHNA NVVIFDDEIS GSQARNLEEN LKIKIIDRTT LILHIFATRA KSKESKMQVE LAQLKYRLAR LSGLGIVLSR TGGGIGTRGP GEKKLETDKR HIRERIYEIN RELKKIKGVR KVQREKRNEI YNVSLVGYTN SGKSTLRNKL CEIAVPKESV VKDKVFEADM LFATLDTTTR AVELKDGRTI TITDTVGFIN KLPHDLVEAF KSTLEEVYYS DLLLHVVDIS SEDAYQHIES VDKVLNQLGI NDKPVLLVFN KIDKGKTEKI EDIKDKYNGV ESIYISAKQG INLEELLERI SHMLPQSIKK VEYLIPYTEQ AAVAFIHRNC KIEKEDYREQ GTYISALVDE EVYNKFRKFI IE // ID A5P7L4_9SPHN Unreviewed; 407 AA. AC A5P7L4; DT 10-JUL-2007, integrated into UniProtKB/TrEMBL. DT 10-JUL-2007, sequence version 1. DT 07-JUN-2017, entry version 57. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=ED21_27628 {ECO:0000313|EMBL:EDL50315.1}; OS Erythrobacter sp. SD-21. OC Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales; OC Erythrobacteraceae; Erythrobacter. OX NCBI_TaxID=161528 {ECO:0000313|EMBL:EDL50315.1, ECO:0000313|Proteomes:UP000005498}; RN [1] {ECO:0000313|EMBL:EDL50315.1, ECO:0000313|Proteomes:UP000005498} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SD-21 {ECO:0000313|EMBL:EDL50315.1, RC ECO:0000313|Proteomes:UP000005498}; RA Tebo B., Ferriera S., Johnson J., Kravitz S., Beeson K., Sutton G., RA Rogers Y.-H., Friedman R., Frazier M., Venter J.C.; RL Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EDL50315.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABCG01000001; EDL50315.1; -; Genomic_DNA. DR ProteinModelPortal; A5P7L4; -. DR STRING; 161528.ED21_27628; -. DR EnsemblBacteria; EDL50315; EDL50315; ED21_27628. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000005498; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000005498}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000005498}. FT DOMAIN 176 351 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 407 AA; 45044 MW; E92FAFB2D543B2E4 CRC64; MNRLREAEGL ALAIGIEIED SFVLPVREVR PNLLFGAGQV ENIRIACEQN EAELVVVDGA LSPIQQRNLE EKLGRKVIDR TGLILEIFGE RAATAEGRLQ VELAHLDYQQ SRLVRSWTHL ERQRGGFGFL GGPGETQIEA DRRMIRQRMG RLRKELEQVR KTRGLHRERR ERAPWPVVAL VGYTNAGKST LFNRLTGAEV MAEDLLFATL DPTMRAISLP GVEKAILSDT VGFISDLPTQ LVAAFRATLE EVTAADVICH VRDISNSSAE AQKTQVLRVL KGLDVIDGDD GTSSIPILEV WNKWDLLDDE KADELGQLAD NSDDIIRISA VTGEGVQELL VQLGEMLTAK ASVREFEVPA SDGKRIAWLH AHGEVLVEED AGEGASGPLR RFVVRLNPKE LGQFESL // ID A5UVR0_ROSS1 Unreviewed; 454 AA. AC A5UVR0; DT 10-JUL-2007, integrated into UniProtKB/TrEMBL. DT 10-JUL-2007, sequence version 1. DT 07-JUN-2017, entry version 72. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=RoseRS_2334 {ECO:0000313|EMBL:ABQ90713.1}; OS Roseiflexus sp. (strain RS-1). OC Bacteria; Chloroflexi; Chloroflexia; Chloroflexales; Roseiflexineae; OC Roseiflexaceae; Roseiflexus. OX NCBI_TaxID=357808 {ECO:0000313|EMBL:ABQ90713.1, ECO:0000313|Proteomes:UP000006554}; RN [1] {ECO:0000313|Proteomes:UP000006554} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=RS-1 {ECO:0000313|Proteomes:UP000006554}; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., RA Pitluck S., Chertkov O., Brettin T., Bruce D., Han C., Schmutz J., RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., RA Bryant D.A., Richardson P.; RT "Complete sequence of Roseiflexus sp. RS-1."; RL Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000686; ABQ90713.1; -; Genomic_DNA. DR RefSeq; WP_011957059.1; NC_009523.1. DR ProteinModelPortal; A5UVR0; -. DR STRING; 357808.RoseRS_2334; -. DR EnsemblBacteria; ABQ90713; ABQ90713; RoseRS_2334. DR KEGG; rrs:RoseRS_2334; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000006554; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000006554}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000006554}. FT DOMAIN 225 396 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 454 AA; 51112 MW; 6AA4C97D8E4D089E CRC64; MAIRDDQTTP NGGRRLHETR PPRERAFLVG VELTGGRSAW KAEDSLQELA LLADTAGLDV VGSTYQRLKH PFPRYFIGPG KIEEIAALRD TLQYDLVVFD DELTPGQARN VEDALQTRVL DRTGLILDIF ARHAQTHEGR VQVELAQYRY LLPRLRRQWT HLERQAGGGG SSAGGVVGLR GPGETQLEVD RRLIARRIQW LEQQIEEVHR HREVYRERRR QSGIPVIAIV GYTNAGKSTL LNALSGANVR AEDRLFATLD PTTRQVTLPG GQQALLTDTV GFIQKLPTQL VAAFRATLEE IREADVLLHV LDITHPNAAQ QTQTVLDTLR DLHVEDRPII TVLNKVDLMA GMNEVETERV AEALGMPDDY VAVSARKGWG LDTLLSRIEQ TLSERMMPLT AFIPYRRNDL VSLWHMRGVI DEERYEAEGT LIAGRLPVEL LRWFEPFSKP VFAA // ID A5V2V7_SPHWW Unreviewed; 442 AA. AC A5V2V7; DT 10-JUL-2007, integrated into UniProtKB/TrEMBL. DT 10-JUL-2007, sequence version 1. DT 07-JUN-2017, entry version 68. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Swit_0252 {ECO:0000313|EMBL:ABQ66623.1}; OS Sphingomonas wittichii (strain RW1 / DSM 6014 / JCM 10273). OC Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales; OC Sphingomonadaceae; Sphingomonas. OX NCBI_TaxID=392499 {ECO:0000313|EMBL:ABQ66623.1, ECO:0000313|Proteomes:UP000001989}; RN [1] {ECO:0000313|Proteomes:UP000001989} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=RW1 / DSM 6014 / JCM 10273 {ECO:0000313|Proteomes:UP000001989}; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., RA Dalin E., Tice H., Pitluck S., Saunders E., Brettin T., Bruce D., RA Detter J.C., Han C., Tapia R., Gilna P., Schmutz J., Larimer F., RA Land M., Hauser L., Kyrpides N., Kim E., Halden R.U., Miller T.R., RA Salzberg S.L., Eisen J.A., Richardson P.; RT "Complete sequence of chromosome of Sphingomonas wittichii RW1."; RL Submitted (MAY-2007) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000699; ABQ66623.1; -; Genomic_DNA. DR RefSeq; WP_011951103.1; NC_009511.1. DR ProteinModelPortal; A5V2V7; -. DR STRING; 392499.Swit_0252; -. DR EnsemblBacteria; ABQ66623; ABQ66623; Swit_0252. DR KEGG; swi:Swit_0252; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000001989; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 2. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000001989}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000001989}. FT DOMAIN 209 391 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 175 202 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 442 AA; 47767 MW; EA2F5E9F45662FBF CRC64; MSVFNRDEDD GLSRGARALV ALPERSGDNP RSAEARLDEA AGLAAAIGVD VVDKLAFRLR DPKPATLFGS GQVDQIALAA RQGEAELIIV DAALTPIQQR NLEKATEAKV IDRTGLILEI FGERAATAEG RLQVELAHLD YQAGRLVRSW THLERQRGGF GFLGGPGETQ IEADRRLIRD RMAKLRRELE QVRRTRGLHR ARRQRAPWPV IALVGYTNAG KSTLFNRMTG AKVMAEDLLF ATLDPTMRQI SLPGLDKAIL SDTVGFVSDL PTQLVAAFRA TLEEVTGADI ILHVRDISHP DSDAQAGDVL AVLGEIGVGP RAPEGHGSGE AGEGAPILEV WNKIDMLDPE ARAATEAEAA RRDDVAPLSA LTGEGVEELR RLVSDRLSTG NRVRTLSVPI ADGAALAWLH ANGEVIGQEV EGDAMIVEVR LSDKDLARFE AR // ID A5VLZ4_LACRD Unreviewed; 425 AA. AC A5VLZ4; DT 10-JUL-2007, integrated into UniProtKB/TrEMBL. DT 10-JUL-2007, sequence version 1. DT 07-JUN-2017, entry version 78. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Lreu_1628 {ECO:0000313|EMBL:ABQ83868.1}; OS Lactobacillus reuteri (strain DSM 20016). OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; OC Lactobacillus. OX NCBI_TaxID=557436 {ECO:0000313|EMBL:ABQ83868.1, ECO:0000313|Proteomes:UP000001991}; RN [1] {ECO:0000313|Proteomes:UP000001991} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 20016 {ECO:0000313|Proteomes:UP000001991}; RX PubMed=21379339; DOI=10.1371/journal.pgen.1001314; RA Frese S.A., Benson A.K., Tannock G.W., Loach D.M., Kim J., Zhang M., RA Oh P.L., Heng N.C., Patil P.B., Juge N., Mackenzie D.A., Pearson B.M., RA Lapidus A., Dalin E., Tice H., Goltsman E., Land M., Hauser L., RA Ivanova N., Kyrpides N.C., Walter J.; RT "The evolution of host specialization in the vertebrate gut symbiont RT Lactobacillus reuteri."; RL PLoS Genet. 7:E1001314-E1001314(2011). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000705; ABQ83868.1; -; Genomic_DNA. DR RefSeq; WP_003669021.1; NZ_AZDD01000011.1. DR ProteinModelPortal; A5VLZ4; -. DR EnsemblBacteria; ABQ83868; ABQ83868; Lreu_1628. DR GeneID; 5188309; -. DR KEGG; lre:Lreu_1628; -. DR PATRIC; fig|557436.17.peg.254; -. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; FNNHAHV; -. DR Proteomes; UP000001991; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000001991}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000001991}. FT DOMAIN 202 371 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 425 AA; 47759 MW; 1F1947A30FA260F7 CRC64; METNIQTLEP VIITGLNTGQ EDFDYSMVEL AELAQANHME VIDRIDQVID RPNPATYFGK GKVEEIRDVA DANHVPTIIT NDELSPSQLR NLEEGTGCRI LDRTALILEI FATRAQSKEA KLQVQIAELQ YRLPRLQTSA SERLDQQTGG GSGFTNRGAG ETKLEMDRRT IQHQISHLRQ ELAAIDKSEQ TKRKQRAKSA IPTAALVGYT NAGKSTIMNG LVRRYGAAEE KTVFEKNMLF ATLDTSVRQL TLPDQKRFLL SDTVGFVSKL PTHLVESFKS TLAEAANADL LIQVIDYSDP HYKEMMETTN ETLKQIGIND IPMINVFNKA DKTEIEFPIL EGDDQVVISA KQDASLDLLV DVIKKRLFKD YVTTTLLIPF TDGHVVSYLN EHTNILDTTY ESDGTLLTVE MSVQDYHRFG KYEKN // ID A5WGL7_PSYWF Unreviewed; 481 AA. AC A5WGL7; DT 10-JUL-2007, integrated into UniProtKB/TrEMBL. DT 10-JUL-2007, sequence version 1. DT 30-AUG-2017, entry version 72. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=PsycPRwf_1868 {ECO:0000313|EMBL:ABQ94808.1}; OS Psychrobacter sp. (strain PRwf-1). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Moraxellaceae; Psychrobacter. OX NCBI_TaxID=349106 {ECO:0000313|EMBL:ABQ94808.1, ECO:0000313|Proteomes:UP000001993}; RN [1] {ECO:0000313|EMBL:ABQ94808.1, ECO:0000313|Proteomes:UP000001993} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=PRwf-1 {ECO:0000313|EMBL:ABQ94808.1, RC ECO:0000313|Proteomes:UP000001993}; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., RA Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., RA Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Tiedje J., RA Richardson P.; RT "Complete sequence of chromosome of Psychrobacter sp. PRwf-1."; RL Submitted (MAY-2007) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000713; ABQ94808.1; -; Genomic_DNA. DR RefSeq; WP_011961085.1; NC_009524.1. DR ProteinModelPortal; A5WGL7; -. DR STRING; 349106.PsycPRwf_1868; -. DR EnsemblBacteria; ABQ94808; ABQ94808; PsycPRwf_1868. DR KEGG; prw:PsycPRwf_1868; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; FNNHAHV; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000001993; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000001993}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000001993}. FT DOMAIN 200 365 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 166 193 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 481 AA; 53914 MW; DF78139C7794848C CRC64; MDYFGRHEGG ERAILVHLEV RQIADPDDLE EFKLLVDSAG AQQLAVITGS RQKPDAKYFI GSGKAQEIAE QVQALEADIV IFNHSLTPSQ ERNLETLLQC RVLDRTGLIL DIFAQRARTY EGKLQVELAQ LNHLATRLVR GWTHLERQKG GIGLRGPGET QLETDRRLLQ IRVSQLKARL DKVKQTRAQG RAKRQKSDVL TISLVGYTNA GKSSLFNRLV DEDIYAADQL FATLDPTLRR MDWQGVGRVV LVDTVGFVRH LPHELVESFH ATLEETLEAD LLLHVIDSSS PDMHEQIKAV KEVLSEIDNH VPVLNVYNKI DITGEPAQIN YSGPGVPSRV YVSAKADLGM SMLHTAVQQL LTGKLNTFEI TLPFNAGNLK NELYRLDVVE QESYDEQGHE VLTLRLPSDK LQQLLGQANI DPLSVLPKDQ AELLIPTLEP FEKQLKADQE AKAALLDLEA DFEAPDFEPV ADWPEDDDIL R // ID A5Z9L7_9FIRM Unreviewed; 410 AA. AC A5Z9L7; DT 24-JUL-2007, integrated into UniProtKB/TrEMBL. DT 24-JUL-2007, sequence version 1. DT 07-JUN-2017, entry version 57. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:EDM50461.1}; GN ORFNames=EUBVEN_02413 {ECO:0000313|EMBL:EDM50461.1}; OS Eubacterium ventriosum ATCC 27560. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Eubacteriaceae; OC Eubacterium. OX NCBI_TaxID=411463 {ECO:0000313|EMBL:EDM50461.1, ECO:0000313|Proteomes:UP000006000}; RN [1] {ECO:0000313|EMBL:EDM50461.1, ECO:0000313|Proteomes:UP000006000} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 27560 {ECO:0000313|EMBL:EDM50461.1, RC ECO:0000313|Proteomes:UP000006000}; RA Fulton L., Clifton S., Fulton B., Xu J., Minx P., Pepin K.H., RA Johnson M., Thiruvilangam P., Bhonagiri V., Nash W.E., Mardis E.R., RA Wilson R.K.; RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:EDM50461.1, ECO:0000313|Proteomes:UP000006000} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 27560 {ECO:0000313|EMBL:EDM50461.1, RC ECO:0000313|Proteomes:UP000006000}; RA Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., RA Liep D., Gordon J.; RT "Draft genome sequence of Eubacterium ventriosum (ATCC 27560)."; RL Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EDM50461.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AAVL02000037; EDM50461.1; -; Genomic_DNA. DR RefSeq; WP_005363881.1; NZ_DS264286.1. DR ProteinModelPortal; A5Z9L7; -. DR STRING; 411463.EUBVEN_02413; -. DR EnsemblBacteria; EDM50461; EDM50461; EUBVEN_02413. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000006000; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000006000}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000006000}. FT DOMAIN 198 361 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 164 191 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 410 AA; 46453 MW; CC16ED4C34708B9D CRC64; MYETEQEIEK VILVAVCSNP NQDPEESLDE LEELVKTAGA TVVGRMIQNL EHASSATYIG SGKVEELKDL IWETEATAVV CDDELTPAQY KNLEDELDVK VMDRTLIILD IFAGRAKTAE GKIQVELAQL RYRSTRLIGM RNLSRQGGGI GTRGPGEKKL EVDRRLIRDR ISQLKSQVED LESHRQVTRA RRQENPVPVI AIVGYTNAGK STLLNTLTDA RVLEEDKLFA TLDPTTRNYK LPDGQEVLLT DTVGFIRKLP HHLIDAFRST LEEAKYSDII IHVVDSSNPV MDKNVQAVYD TLKNLEVKDK IIITVFNKID KLEEKPIMKD FNADYTVETA IKKGIGLDEL NEIIEKALKS MRIHIEKLFP YTDAGKPGLI RKYGQLIKEE YREDGIWVEA YVPSELMDRL // ID A6CEA6_9PLAN Unreviewed; 450 AA. AC A6CEA6; DT 24-JUL-2007, integrated into UniProtKB/TrEMBL. DT 24-JUL-2007, sequence version 1. DT 07-JUN-2017, entry version 48. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=PM8797T_13570 {ECO:0000313|EMBL:EDL56951.1}; OS Gimesia maris DSM 8797. OC Bacteria; Planctomycetes; Planctomycetia; Planctomycetales; OC Planctomycetaceae; Gimesia. OX NCBI_TaxID=344747 {ECO:0000313|EMBL:EDL56951.1, ECO:0000313|Proteomes:UP000003087}; RN [1] {ECO:0000313|EMBL:EDL56951.1, ECO:0000313|Proteomes:UP000003087} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 8797T {ECO:0000313|Proteomes:UP000003087}; RA Amann R., Ferriera S., Johnson J., Kravitz S., Beeson K., Sutton G., RA Rogers Y.-H., Friedman R., Frazier M., Venter J.C.; RL Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EDL56951.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABCE01000045; EDL56951.1; -; Genomic_DNA. DR RefSeq; WP_002648888.1; NZ_ABCE01000045.1. DR ProteinModelPortal; A6CEA6; -. DR STRING; 344747.PM8797T_13570; -. DR EnsemblBacteria; EDL56951; EDL56951; PM8797T_13570. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000003087; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000003087}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000003087}. FT DOMAIN 204 370 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 165 199 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 450 AA; 50667 MW; 1EA3342A591F765B CRC64; MADPKREELQ VKAKRAILVS VVSPSNHIDK NQALDELKGL VDTAGVKVVG TLVQNRENPH PATCLGKGKL EELKQMVKHV DAELIIFDNN LSPSQGRNIE EETGTVIVDR SELILDIFAT HAKTYEAKLQ VELAQLLYFR PRLKRLWTHL ERIEGGVGAG RGPGEKQLET DRRLLDKRVA ELKRKLSEVE RRRERTVSNR FQQLTVSLVG YTNAGKSTLM NALTGADVYI ADQLFATLDT RTRRWELPHW GEILLSDTVG FVRDLPHHLV ASFKSTLEEA RQADLLLHVV DCSNPEVEHH IKTVNKVLDE IEIEHKNAIL VFNKTDKVED RSKLDVLRLK YDNAISVSAV SGEGLDRLSQ AVIDRLASGY VIVELETPVG NGKLLSQLED HSLILSREYS HDDTRVTFQA RIARRFLPML KTGPDTSLKI HDDESAVPGD MIPEESVNEY // ID A6CNQ3_9BACI Unreviewed; 359 AA. AC A6CNQ3; DT 24-JUL-2007, integrated into UniProtKB/TrEMBL. DT 24-JUL-2007, sequence version 1. DT 07-JUN-2017, entry version 34. DE SubName: Full=GTP-binding protein (HflX) {ECO:0000313|EMBL:EDL64554.1}; DE Flags: Fragment; GN ORFNames=BSG1_08446 {ECO:0000313|EMBL:EDL64554.1}; OS Bacillus sp. SG-1. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus. OX NCBI_TaxID=161544 {ECO:0000313|EMBL:EDL64554.1, ECO:0000313|Proteomes:UP000004417}; RN [1] {ECO:0000313|EMBL:EDL64554.1, ECO:0000313|Proteomes:UP000004417} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SG-1 {ECO:0000313|EMBL:EDL64554.1, RC ECO:0000313|Proteomes:UP000004417}; RA Tebo B., Ferriera S., Johnson J., Kravitz S., Beeson K., Sutton G., RA Rogers Y.-H., Friedman R., Frazier M., Venter J.C.; RL Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EDL64554.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABCF01000018; EDL64554.1; -; Genomic_DNA. DR RefSeq; WP_006836968.1; NZ_ABCF01000018.1. DR ProteinModelPortal; A6CNQ3; -. DR EnsemblBacteria; EDL64554; EDL64554; BSG1_08446. DR Proteomes; UP000004417; Unassembled WGS sequence. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000004417}; KW Reference proteome {ECO:0000313|Proteomes:UP000004417}. FT DOMAIN 140 302 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT NON_TER 1 1 {ECO:0000313|EMBL:EDL64554.1}. SQ SEQUENCE 359 AA; 41087 MW; F07EA3CC709D11BA CRC64; GKGKVEELVA LEEQFEPDLV IFNDELSPSQ IRNLSEQLEA RVIDRTQLIL DIFAQRARSR EGKLQVELAQ LQYLLPRLIG QGASLSRLGG GIGTRGPGET KLESDRRHIR RRIDDIKKSL QVVVDHRERY RERRKKNKTF QLALMGYTNA GKSTLFNRIS IAESYEENQL FATLDPLTRK LILPSGYSAL VTDTVGFIQD LPTALVAAFR STLEEVKEAD LLLHVVDSSN PDYNNHEKTV QSLLEELKMD HIPQLTIYNK RDEMHPDFVP DSSNEKIIIS ALNEEDRTVL KDKIEELVIE QMEAYHVHLP SNEGKLLSQL KNETILRKLE FNEETHTYEA KGYSLTDHPV TGSIKKYQK // ID A6D8D2_9VIBR Unreviewed; 429 AA. AC A6D8D2; DT 24-JUL-2007, integrated into UniProtKB/TrEMBL. DT 24-JUL-2007, sequence version 1. DT 30-AUG-2017, entry version 50. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=VSAK1_09958 {ECO:0000313|EMBL:EDL51145.1}; OS Vibrio shilonii AK1. OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; OC Vibrionaceae; Vibrio. OX NCBI_TaxID=391591 {ECO:0000313|EMBL:EDL51145.1, ECO:0000313|Proteomes:UP000003769}; RN [1] {ECO:0000313|EMBL:EDL51145.1, ECO:0000313|Proteomes:UP000003769} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=AK1 {ECO:0000313|EMBL:EDL51145.1, RC ECO:0000313|Proteomes:UP000003769}; RA Rosenberg E., Ferriera S., Johnson J., Kravitz S., Beeson K., RA Sutton G., Rogers Y.-H., Friedman R., Frazier M., Venter J.C.; RL Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EDL51145.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABCH01000072; EDL51145.1; -; Genomic_DNA. DR RefSeq; WP_006075247.1; NZ_ABCH01000072.1. DR ProteinModelPortal; A6D8D2; -. DR STRING; 391591.VSAK1_09958; -. DR EnsemblBacteria; EDL51145; EDL51145; VSAK1_09958. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR Proteomes; UP000003769; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000003769}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000003769}. FT DOMAIN 198 365 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 429 AA; 48749 MW; 882B4AE9A87DB6CC CRC64; MFDRYESGEQ AVLVHINFTQ EGEWEDLSEF EMLVSSAGVN ALQVVTGSRQ SPHPKYYVGE GKAQEIAQTV QLTGADIVIF NHALSPAQER NLESLCKCRV LDRTGLILDI FAQRARTHEG KLQVELAQLR HISTRLIRGW THLERQKGGI GLRGPGETQL ETDRRLLRDR IKAILRRLEK VAKQREQGRR ARNRAEIPTI SLVGYTNAGK STLFNRITEA GVYAADQLFA TLDPTLRKIQ LADVGPAILA DTVGFIRHLP HDLVAAFKAT LQETQEADIL LHVVDASDDR FRENIQAVHD VLEEIDAHEV PSLVVMNKID NLDGQRPRIE RNDEGIPRAV WVSAMEGQGI ELLFEALTER LASQMVQYQL RIPPQFQGRF RSTFFQMNCI QREEYDEEGN LLIDIRMQQV DWSRLEKREG AVLSDFIVT // ID A6DH78_9BACT Unreviewed; 434 AA. AC A6DH78; DT 24-JUL-2007, integrated into UniProtKB/TrEMBL. DT 24-JUL-2007, sequence version 1. DT 07-JUN-2017, entry version 57. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=LNTAR_14132 {ECO:0000313|EMBL:EDM28961.1}; OS Lentisphaera araneosa HTCC2155. OC Bacteria; Lentisphaerae; Lentisphaeria; Lentisphaerales; OC Lentisphaeraceae; Lentisphaera. OX NCBI_TaxID=313628 {ECO:0000313|EMBL:EDM28961.1, ECO:0000313|Proteomes:UP000004947}; RN [1] {ECO:0000313|EMBL:EDM28961.1, ECO:0000313|Proteomes:UP000004947} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=HTCC2155 {ECO:0000313|EMBL:EDM28961.1, RC ECO:0000313|Proteomes:UP000004947}; RX PubMed=20363947; DOI=10.1128/JB.00208-10; RA Thrash J.C., Cho J.C., Vergin K.L., Morris R.M., Giovannoni S.J.; RT "Genome sequence of Lentisphaera araneosa HTCC2155T, the type species RT of the order Lentisphaerales in the phylum Lentisphaerae."; RL J. Bacteriol. 192:2938-2939(2010). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EDM28961.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABCK01000003; EDM28961.1; -; Genomic_DNA. DR ProteinModelPortal; A6DH78; -. DR STRING; 313628.LNTAR_14132; -. DR EnsemblBacteria; EDM28961; EDM28961; LNTAR_14132. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000004947; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000004947}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000004947}. FT DOMAIN 205 371 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 20 43 {ECO:0000256|SAM:Coils}. FT COILED 171 198 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 434 AA; 49669 MW; 2962A9BEBA833412 CRC64; MSISDEKKLD INNTAFLVGV YKKNDEKEEC DQLLEELEEL MQTMGVDVAG KKAIRNQKPS ARFLLTSGKA EELFHNVMEA EAGIIVFDAD ISPSQQRNME RESCLAVIDR REVILEIFSQ RATTREARLQ IDLARAEYDL PRLTRAWTHL SRQRGGTNMK GEGERQIELD RRMVRARISR LQKELVKVRS QRATQRKQRR KKPVPNAAIV GYTNAGKSSL LNRLTNAGIL ADDKLFATLD PTTRRILLNN NQELLLTDTV GFIRKLPHDL VEAFKATLEE TVVADFLIHV VDASDPDALQ QMDTTFKVLN ELDADTKKTI IAFNKIDQVE HSNRLASLRS AYPDCIFISV KSGQGIELLQ ERMCELIEHK LFDVELNIPF DRFDLMALIH RQCQVHSEKY DDNFIYVKCT APNDLKNEIE DYIVNATIPN THRC // ID A6EE08_9SPHI Unreviewed; 297 AA. AC A6EE08; DT 24-JUL-2007, integrated into UniProtKB/TrEMBL. DT 24-JUL-2007, sequence version 1. DT 07-JUN-2017, entry version 35. DE SubName: Full=GTP-binding protein HflX {ECO:0000313|EMBL:EDM36496.1}; DE Flags: Fragment; GN ORFNames=PBAL39_12347 {ECO:0000313|EMBL:EDM36496.1}; OS Pedobacter sp. BAL39. OC Bacteria; Bacteroidetes; Sphingobacteriia; Sphingobacteriales; OC Sphingobacteriaceae; Pedobacter. OX NCBI_TaxID=391596 {ECO:0000313|EMBL:EDM36496.1, ECO:0000313|Proteomes:UP000003664}; RN [1] {ECO:0000313|EMBL:EDM36496.1, ECO:0000313|Proteomes:UP000003664} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BAL39 {ECO:0000313|EMBL:EDM36496.1, RC ECO:0000313|Proteomes:UP000003664}; RA Hagstrom A., Ferriera S., Johnson J., Kravitz S., Beeson K., RA Sutton G., Rogers Y.-H., Friedman R., Frazier M., Venter J.C.; RL Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EDM36496.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABCM01000008; EDM36496.1; -; Genomic_DNA. DR RefSeq; WP_008242051.1; NZ_ABCM01000008.1. DR ProteinModelPortal; A6EE08; -. DR STRING; 391596.PBAL39_12347; -. DR EnsemblBacteria; EDM36496; EDM36496; PBAL39_12347. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000003664; Unassembled WGS sequence. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000003664}; KW Reference proteome {ECO:0000313|Proteomes:UP000003664}. FT DOMAIN 204 297 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT NON_TER 297 297 {ECO:0000313|EMBL:EDM36496.1}. SQ SEQUENCE 297 AA; 33908 MW; 7A4FA680092ED773 CRC64; MGRQKYYDTA PKQERAVLVG VIRPGETQEE TKEYLDELAF LVDTAGGAVE KVFTQKMLKP DRATFVGTGK LEEIQAYVKS EEIDMVVFDD ELSPSQLRNI ERELQVKILD RSNLILDIFA GRAQTAQAKT QVELAQLQYL LPRLTRLWTH LERQKGGIGM RGPGETQIES DRRMILEKIS LLKERLKLID KQNETQRKNR GQLIRVALVG YTNVGKSTIM NMLSKSEVFA ENKLFATLDT TVRKVVIENL PFLLSDTVGF IRKLPHHLVE CFKSTLDEVR EADILIHVVD VSHPNFE // ID A6ELQ3_9BACT Unreviewed; 403 AA. AC A6ELQ3; DT 24-JUL-2007, integrated into UniProtKB/TrEMBL. DT 24-JUL-2007, sequence version 1. DT 07-JUN-2017, entry version 56. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=SCB49_06837 {ECO:0000313|EMBL:EDM45503.1}; OS unidentified eubacterium SCB49. OC Bacteria; Bacteroidetes; environmental samples. OX NCBI_TaxID=50743 {ECO:0000313|EMBL:EDM45503.1, ECO:0000313|Proteomes:UP000003659}; RN [1] {ECO:0000313|EMBL:EDM45503.1, ECO:0000313|Proteomes:UP000003659} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SCB49 {ECO:0000313|EMBL:EDM45503.1, RC ECO:0000313|Proteomes:UP000003659}; RA Hagstrom A., Ferriera S., Johnson J., Kravitz S., Beeson K., RA Sutton G., Rogers Y.-H., Friedman R., Frazier M., Venter J.C.; RL Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EDM45503.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABCO01000001; EDM45503.1; -; Genomic_DNA. DR ProteinModelPortal; A6ELQ3; -. DR STRING; 50743.SCB49_06837; -. DR EnsemblBacteria; EDM45503; EDM45503; SCB49_06837. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR Proteomes; UP000003659; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000003659}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000003659}. FT DOMAIN 200 385 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 403 AA; 46505 MW; 2C58D3F17412A8FF CRC64; MLEKEKIEYE KTILIGVITQ DQNEEKSKEY LDELEFLAYT AGGEVKKRFT QKMASPNPKT FVGTGKMEEI QAYIEAHNIG TAIFDDELSP GQQRNIEKIL ECKIIDRTYL ILDIFAQRAQ TSYARTQVEL AQYEYLLPRL TGLWTHLERQ RGGIGMRGPG ETEIETDRRI VRDRISLLKK KMLAIDKQMA TQRGNRGSLI RVALVGYTNV GKSTLMNVIS KSDVFAENKL FATLDTTVRK VVIGNLPFLL TDTVGFIRKL PTQLVESFKS TLDEVREADL LLHVVDISHE SFEDHIDSVN VILNEIKSSD KPVLMVFNKI DAYEPETIDA DDLVTEKTKA HYTIEDWKRT WMNTENETAI FISATEKENI VDFRKTVYDK VRALHSKRFP YNNYLYPDYY EEE // ID A6FRT7_9RHOB Unreviewed; 425 AA. AC A6FRT7; DT 24-JUL-2007, integrated into UniProtKB/TrEMBL. DT 24-JUL-2007, sequence version 1. DT 07-JUN-2017, entry version 56. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=rpsB {ECO:0000313|EMBL:EDM70903.1}; GN Synonyms=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=RAZWK3B_15940 {ECO:0000313|EMBL:EDM70903.1}; OS Roseobacter sp. AzwK-3b. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae; Roseobacter. OX NCBI_TaxID=351016 {ECO:0000313|EMBL:EDM70903.1, ECO:0000313|Proteomes:UP000004119}; RN [1] {ECO:0000313|EMBL:EDM70903.1, ECO:0000313|Proteomes:UP000004119} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=AzwK-3b {ECO:0000313|EMBL:EDM70903.1, RC ECO:0000313|Proteomes:UP000004119}; RA Francis C., Ferriera S., Johnson J., Kravitz S., Beeson K., Sutton G., RA Rogers Y.-H., Friedman R., Frazier M., Venter J.C.; RL Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EDM70903.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABCR01000006; EDM70903.1; -; Genomic_DNA. DR RefSeq; WP_007815400.1; NZ_ABCR01000006.1. DR ProteinModelPortal; A6FRT7; -. DR STRING; 351016.RAZWK3B_15940; -. DR EnsemblBacteria; EDM70903; EDM70903; RAZWK3B_15940. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000004119; Unassembled WGS sequence. DR GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000004119}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000004119}; KW Ribonucleoprotein {ECO:0000313|EMBL:EDM70903.1}; KW Ribosomal protein {ECO:0000313|EMBL:EDM70903.1}. FT DOMAIN 204 374 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 425 AA; 47316 MW; 39775408A7931168 CRC64; MTLTERADTR AWVLHPDIPN AASGRDPQLA LEEAVSLGHA LPGLDVVGAQ VVRVRQPHPG TLFGKGKLEE LHALIDAQEI ELVLIDGPVT PVQQRNLEKA WGVKLLDRTG LILEIFSDRA ATREGVLQVE MAALSYQRTR LVRAWTHLER QRGGLGFVGG PGETQIEADR RAIDEQLVRL RRQLSKVVRT RELHRAARAK VPFPIVALVG YTNAGKSTLF NRMTGADVMA KDMLFATLDP TMRRIELPGG GPEVILSDTV GFISDLPTEL VAAFRATLEE VLAADLIVHV RDISHPESEA QARDVRTILE SLGVRDSIPQ IEVWNKIDKL DDETRQAVLT RAARHEHVQA LSAVTGEGMS ELVGVITSAM TDTTQEAHLH LRFDEGRKRA WLYERGLIED ERQTEDGFDL TVRWSLRQQA QFEQV // ID A6FWT5_9DELT Unreviewed; 465 AA. AC A6FWT5; DT 24-JUL-2007, integrated into UniProtKB/TrEMBL. DT 24-JUL-2007, sequence version 1. DT 07-JUN-2017, entry version 50. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=PPSIR1_04813 {ECO:0000313|EMBL:EDM81759.1}; OS Plesiocystis pacifica SIR-1. OC Bacteria; Proteobacteria; Deltaproteobacteria; Myxococcales; OC Nannocystineae; Nannocystaceae; Plesiocystis. OX NCBI_TaxID=391625 {ECO:0000313|EMBL:EDM81759.1, ECO:0000313|Proteomes:UP000005801}; RN [1] {ECO:0000313|EMBL:EDM81759.1, ECO:0000313|Proteomes:UP000005801} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SIR-1 {ECO:0000313|EMBL:EDM81759.1, RC ECO:0000313|Proteomes:UP000005801}; RA Shimkets L., Ferriera S., Johnson J., Kravitz S., Beeson K., RA Sutton G., Rogers Y.-H., Friedman R., Frazier M., Venter J.C.; RL Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EDM81759.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABCS01000001; EDM81759.1; -; Genomic_DNA. DR RefSeq; WP_006968934.1; NZ_ABCS01000001.1. DR ProteinModelPortal; A6FWT5; -. DR STRING; 391625.PPSIR1_04813; -. DR EnsemblBacteria; EDM81759; EDM81759; PPSIR1_04813. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000005801; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000005801}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000005801}. FT DOMAIN 239 408 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 207 234 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 465 AA; 50164 MW; D002C07C95ECA3FD CRC64; MKFHSDSIEE HNEAPLADDG ALDQLIARWT AKSGESGPAK PGLGEPNHAW VVAVGDWEAY EERSAEAQLA ELVALVGAQG DAIVGYELCR RAKPDPRTYL GSGTAAAIAE RARAAGADML VIDAELSPSQ TRNLEDVTGF SVCDREAVIL NVFLRHAKTR TARIQVEIAQ LEYLRPRIRG IGLDMDQQAG GLMTARGPGE TASELLARRI DGRLAELRRQ VARLERAGQR QREGRASCGR VALVGYTNAG KTSLMNALTQ AELSARDMPF ETLDTTTRSL TRHGGDVIIS DTVGFIRRLP QRLLASFETT LAEIREASVV CVVVDLSDPE WDMHLDTTHA LLERLGAGAL ARVYVFNKLD KLAPAERPRP AVLEACAQGH AHWALSAHDE DAVASVRAAL IDAARPHHRR ARVRLPYAAS EAISAVYAHC RLLSSEAIAE GLVVDIDGPA HHVAAIVAAG QVLEG // ID A6G4F3_9DELT Unreviewed; 583 AA. AC A6G4F3; DT 24-JUL-2007, integrated into UniProtKB/TrEMBL. DT 24-JUL-2007, sequence version 1. DT 07-JUN-2017, entry version 48. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=PPSIR1_03973 {ECO:0000313|EMBL:EDM79265.1}; OS Plesiocystis pacifica SIR-1. OC Bacteria; Proteobacteria; Deltaproteobacteria; Myxococcales; OC Nannocystineae; Nannocystaceae; Plesiocystis. OX NCBI_TaxID=391625 {ECO:0000313|EMBL:EDM79265.1, ECO:0000313|Proteomes:UP000005801}; RN [1] {ECO:0000313|EMBL:EDM79265.1, ECO:0000313|Proteomes:UP000005801} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SIR-1 {ECO:0000313|EMBL:EDM79265.1, RC ECO:0000313|Proteomes:UP000005801}; RA Shimkets L., Ferriera S., Johnson J., Kravitz S., Beeson K., RA Sutton G., Rogers Y.-H., Friedman R., Frazier M., Venter J.C.; RL Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EDM79265.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABCS01000021; EDM79265.1; -; Genomic_DNA. DR RefSeq; WP_006971602.1; NZ_ABCS01000021.1. DR ProteinModelPortal; A6G4F3; -. DR STRING; 391625.PPSIR1_03973; -. DR EnsemblBacteria; EDM79265; EDM79265; PPSIR1_03973. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000005801; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000005801}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000005801}. FT DOMAIN 399 564 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 358 392 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 583 AA; 64787 MW; D512388D8A0E661D CRC64; MSDVVFGETS NLKPSQARTL ARLGERRVSA DAVVSAPLAR DLLALSHELN RRIGLFLDRR GRVNRVILGD AHSLELPEFE RVRGADGRLR GIRLVLTHLV PDPLDREELA DLAKLRLDMV AALHDSPGGM HVDIACLEPA REKGKGFAIR RIDRAPVALL SPDAGGRNRE AHPRPDLPSD FTAFIRELEG LLVAATAQTK AAGTGTRAMV LQVHTDQMNR EGGIEARQAE LRELCRTAGV DLVELVCQRR RYPDPRTFLG SGKLREVLIS ALEQDVELLI CDPELSASQA RVIADSTDLG VIDRTMLILD IFAQHARSSD GKLQVELAQL RYRLPRMIGK GTMMSRLGGG IGGRGPGESK LEVDRRRAQK RINELEKRLQ KLQRQRDQRR ARRRRSDVPV VAIVGYTNAG KSTLLNTVTE SEVIAENKLF ATLDPTVRRV RFPDEREVVM LDTVGFIREL PPALMQAFSA TLEEVAEADL LLHVVDATDP DNTQQIRTVE KILGDLGAGG VERFMVYNKC DLLPPELILP PEEQKQGSFQ ISAQDRRSTR GLMLAIEERL WQRGKVDSPR PDYAVDGSEP VED // ID A6GNK3_9BURK Unreviewed; 373 AA. AC A6GNK3; DT 24-JUL-2007, integrated into UniProtKB/TrEMBL. DT 24-JUL-2007, sequence version 1. DT 07-JUN-2017, entry version 47. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=LMED105_01973 {ECO:0000313|EMBL:EDM84291.1}; OS Limnobacter sp. MED105. OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Limnobacter. OX NCBI_TaxID=391597 {ECO:0000313|EMBL:EDM84291.1, ECO:0000313|Proteomes:UP000010322}; RN [1] {ECO:0000313|EMBL:EDM84291.1, ECO:0000313|Proteomes:UP000010322} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MED105 {ECO:0000313|EMBL:EDM84291.1, RC ECO:0000313|Proteomes:UP000010322}; RA Pinhassi J., Pedros-Alio C., Ferriera S., Johnson J., Kravitz S., RA Beeson K., Sutton G., Rogers Y.-H., Friedman R., Frazier M., RA Venter J.C.; RL Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EDM84291.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABCT01000003; EDM84291.1; -; Genomic_DNA. DR RefSeq; WP_008248718.1; NZ_ABCT01000003.1. DR ProteinModelPortal; A6GNK3; -. DR STRING; 391597.LMED105_01973; -. DR EnsemblBacteria; EDM84291; EDM84291; LMED105_01973. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR Proteomes; UP000010322; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000010322}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000010322}. FT DOMAIN 191 357 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 157 184 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 373 AA; 41218 MW; D37677149C68F6C5 CRC64; MTRSSLVALD LGQHEFRESV DELALLATSA GAEVIGVFVS KRRSPDSATF IGSGKVQEIL AHCEAEEVEL VIFNHSLSPA QQRNLEHALG RRVIDRTGLI LDIFAIRARS FEGKLQVELA QLQYMASRLV RGNANLYGQQ GGIGMRGPGE TQLETDRRLI GVKVKQLKTR LEKLQKQRQT QRRQRERRGQ FTVAIVGYTN AGKSTLFNAI ASDKAYAADQ LFATLDTTTR RVWLAPKVDM ALSDTVGFIR DLSHSLVDAF KATLESAVHA DVLLHVVDVS SPVRHSQIDE VNKVLLEIEA GDVPQVIIWN KIDACERSVE VERNGDGKIL SVAVSARYGL GIPELRECLT ELAGNFYAQS RGADTQSDEL QWA // ID A6L1G7_BACV8 Unreviewed; 417 AA. AC A6L1G7; DT 24-JUL-2007, integrated into UniProtKB/TrEMBL. DT 24-JUL-2007, sequence version 1. DT 07-JUN-2017, entry version 76. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=BVU_1856 {ECO:0000313|EMBL:ABR39531.1}; OS Bacteroides vulgatus (strain ATCC 8482 / DSM 1447 / JCM 5826 / NBRC OS 14291 / NCTC 11154). OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae; OC Bacteroides. OX NCBI_TaxID=435590 {ECO:0000313|EMBL:ABR39531.1, ECO:0000313|Proteomes:UP000002861}; RN [1] {ECO:0000313|EMBL:ABR39531.1, ECO:0000313|Proteomes:UP000002861} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 8482 / DSM 1447 / JCM 5826 / NBRC 14291 / NCTC 11154 RC {ECO:0000313|Proteomes:UP000002861}; RX PubMed=17579514; DOI=10.1371/journal.pbio.0050156; RA Xu J., Mahowald M.A., Ley R.E., Lozupone C.A., Hamady M., RA Martens E.C., Henrissat B., Coutinho P.M., Minx P., Latreille P., RA Cordum H., Van Brunt A., Kim K., Fulton R.S., Fulton L.A., RA Clifton S.W., Wilson R.K., Knight R.D., Gordon J.I.; RT "Evolution of symbiotic bacteria in the distal human intestine."; RL PLoS Biol. 5:1574-1586(2007). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000139; ABR39531.1; -; Genomic_DNA. DR RefSeq; WP_005839821.1; NC_009614.1. DR ProteinModelPortal; A6L1G7; -. DR STRING; 435590.BVU_1856; -. DR EnsemblBacteria; ABR39531; ABR39531; BVU_1856. DR GeneID; 5302822; -. DR KEGG; bvu:BVU_1856; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR Proteomes; UP000002861; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000002861}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000002861}. FT DOMAIN 216 400 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 417 AA; 47627 MW; AE1E95B938ADAB60 CRC64; MKEFVISEAQ VETAILVGLI TQTQDERKTK EYLDELEFLA ETAGATVVKR FTQKLPAANS VTYVGKGKLE EIKEYIHQEE ENEREVGMVI FDDELSAKQI RNIEAELKVK ILDRTSLILD IFAMRAQTAN AKTQVELAQY KYMLPRLQRL WTHLERQGGG SGAGGGKGSV GLRGPGETQL EMDRRIILNR MSLLKERLAE IDKQKSTQRK NRGRMIRVAL VGYTNVGKST LMNLLSKSEV FAENKLFATL DTTVRKVIIE NLPFLLTDTV GFIRKLPTDL VDSFKSTLDE VREADLLIHV VDISHPDFEE QISVVDKTIA DLGAGGKPTM IVFNKIDAYT YIEKAEDDLT PKTRENITLE ELMKTWMAKL NDNCIFISAR EKINMDELKT IIYNKVRELH VQKYPYNDFL YQTYDEE // ID A6LH29_PARD8 Unreviewed; 403 AA. AC A6LH29; DT 24-JUL-2007, integrated into UniProtKB/TrEMBL. DT 24-JUL-2007, sequence version 1. DT 30-AUG-2017, entry version 79. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=BDI_3288 {ECO:0000313|EMBL:ABR44993.1}; OS Parabacteroides distasonis (strain ATCC 8503 / DSM 20701 / CIP 104284 OS / JCM 5825 / NCTC 11152). OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Tannerellaceae; OC Parabacteroides. OX NCBI_TaxID=435591 {ECO:0000313|EMBL:ABR44993.1, ECO:0000313|Proteomes:UP000000566}; RN [1] {ECO:0000313|EMBL:ABR44993.1, ECO:0000313|Proteomes:UP000000566} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 8503 / DSM 20701 / CIP 104284 / JCM 5825 / NCTC 11152 RC {ECO:0000313|Proteomes:UP000000566}; RX PubMed=17579514; DOI=10.1371/journal.pbio.0050156; RA Xu J., Mahowald M.A., Ley R.E., Lozupone C.A., Hamady M., RA Martens E.C., Henrissat B., Coutinho P.M., Minx P., Latreille P., RA Cordum H., Van Brunt A., Kim K., Fulton R.S., Fulton L.A., RA Clifton S.W., Wilson R.K., Knight R.D., Gordon J.I.; RT "Evolution of symbiotic bacteria in the distal human intestine."; RL PLoS Biol. 5:1574-1586(2007). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000140; ABR44993.1; -; Genomic_DNA. DR RefSeq; WP_005859898.1; NC_009615.1. DR ProteinModelPortal; A6LH29; -. DR STRING; 435591.BDI_3288; -. DR EnsemblBacteria; ABR44993; ABR44993; BDI_3288. DR GeneID; 5308437; -. DR KEGG; pdi:BDI_3288; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000000566; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000000566}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000000566}. FT DOMAIN 202 386 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 403 AA; 46607 MW; B6C6523FE13310AA CRC64; MKEFIISEAQ TEKAVLVGLV TPEQNEQKVK EYLDELAFLA DTAGVDAVKR FTQKMDYPNS VTFVGTGKLQ EIKEYVVENE IGLVIFDDEL SPKQLRNIEK ELQVKILDRT SLILDIFASR AQTAHAKTQV ELAQYKYMLP RLTRLWTHLE RQRGGVGMRG PGETQLETDK RIILDKIARL KKELVDIDKQ KSVQRKNRGK MVRVALVGYT NVGKSTLMNL LSKSEVFAEN KLFATLDTTV RKVIIENLPF LLSDTVGFIR KLPTELVESF KSTLDEVREA DLLVHIVDIS HPTFEEQIEV VNRTLAEIDK TEKPMIMVFN KVDAFTFVPK EEDDLTPRGR ENIDLDELKR TWMGKLQDNC IFISAKERTN IEALKEMLYE RVKQIHITRF PYNDFLFQQY DEE // ID A6LNU7_THEM4 Unreviewed; 361 AA. AC A6LNU7; DT 24-JUL-2007, integrated into UniProtKB/TrEMBL. DT 24-JUL-2007, sequence version 1. DT 07-JUN-2017, entry version 73. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Tmel_1759 {ECO:0000313|EMBL:ABR31598.1}; OS Thermosipho melanesiensis (strain DSM 12029 / CIP 104789 / BI429). OC Bacteria; Thermotogae; Thermotogales; Fervidobacteriaceae; OC Thermosipho. OX NCBI_TaxID=391009 {ECO:0000313|EMBL:ABR31598.1, ECO:0000313|Proteomes:UP000001110}; RN [1] {ECO:0000313|EMBL:ABR31598.1, ECO:0000313|Proteomes:UP000001110} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 12029 / CIP 104789 / BI429 RC {ECO:0000313|Proteomes:UP000001110}; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., RA Dalin E., Tice H., Pitluck S., Chertkov O., Brettin T., Bruce D., RA Detter J.C., Han C., Schmutz J., Larimer F., Land M., Hauser L., RA Kyrpides N., Mikhailova N., Nelson K., Gogarten J.P., Noll K., RA Richardson P.; RT "Complete sequence of Thermosipho melanesiensis BI429."; RL Submitted (MAY-2007) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000716; ABR31598.1; -; Genomic_DNA. DR RefSeq; WP_012057957.1; NC_009616.1. DR ProteinModelPortal; A6LNU7; -. DR STRING; 391009.Tmel_1759; -. DR EnsemblBacteria; ABR31598; ABR31598; Tmel_1759. DR KEGG; tme:Tmel_1759; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000001110; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000001110}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000001110}. FT DOMAIN 192 357 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 158 185 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 361 AA; 42067 MW; A87123DBE09D2527 CRC64; MKKNKQVLIA GIYKKFVDES FYELEQLCKT LGWNVFDKIF QKRRTPDARF YFGKGLLLKI KELIEKGEID YLVIDDDITN IQRRNIETIL YKKVYDRTEV ILEIFSKHAK TKEGRIQVEI ARLRYLMPYL VGKGKELSRL GGGIGTRGPG EKKLEYEKRY LKRRISTLQN KLKMIKRNRD IQRKKRLNSN LLKISIVGYT NAGKTTLLSK LSKQNLYSKD EMFTTLAPTS RKVMLPSGKF AVFSDTVGFI RKMHPLIIEA FLSTLEEIIY SDLALVVVDV SDVSFREKIK VIYETLEKIG VNLGRTKLVF NKIDLCNSNY LKNLENEFKD AIFISAKKKV NFDYLLNEID KVRLKEVSIK K // ID A6M157_CLOB8 Unreviewed; 596 AA. AC A6M157; DT 24-JUL-2007, integrated into UniProtKB/TrEMBL. DT 24-JUL-2007, sequence version 1. DT 07-JUN-2017, entry version 68. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Cbei_4227 {ECO:0000313|EMBL:ABR36337.1}; OS Clostridium beijerinckii (strain ATCC 51743 / NCIMB 8052) (Clostridium OS acetobutylicum). OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=290402 {ECO:0000313|EMBL:ABR36337.1, ECO:0000313|Proteomes:UP000000565}; RN [1] {ECO:0000313|EMBL:ABR36337.1, ECO:0000313|Proteomes:UP000000565} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51743 / NCIMB 8052 {ECO:0000313|Proteomes:UP000000565}; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., RA Pitluck S., Sims D., Brettin T., Bruce D., Tapia R., Brainard J., RA Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., RA Mikhailova N., Bennet G., Cann I., Chen J.-S., Contreras A.L., RA Jones D., Kashket E., Mitchell W., Stoddard S., Schwarz W., RA Qureshi N., Young M., Shi Z., Ezeji T., White B., Blaschek H., RA Richardson P.; RT "Complete sequence of Clostridium beijerinckii NCIMB 8052."; RL Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000721; ABR36337.1; -; Genomic_DNA. DR RefSeq; WP_012060384.1; NC_009617.1. DR ProteinModelPortal; A6M157; -. DR STRING; 290402.Cbei_4227; -. DR EnsemblBacteria; ABR36337; ABR36337; Cbei_4227. DR KEGG; cbe:Cbei_4227; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000000565; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000000565}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000000565}. FT DOMAIN 364 542 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 596 AA; 67225 MW; 782CC6D4D78106FF CRC64; MIYGNIEGIR KSLIEELENI YSIRNLKDEI CNEEILNIIS RVSSFIEREI SVAINRKGNV TSVAIGDSTS VEVPIIDIDE KRLSGVRVIH THPNGYCNLS ALDLTALLKL KLDAIISVAI TDGNIIDFSL GMLSLYNNKL ETEEKSNLSL NEIMSINILD RIRFIENLIK NNDVIEETEE KAILVGSDTK ESLEELAELT EACNIPVLKT VFQSRSKIDP AYFIGRGKVL EIASMRQVER ANVIIFDDEL SGSQVRNLEA ALGAKVIDRT TLILEIFATR AKTKESKIQV ELAQLKYRLG RLQGLGTILS RTGGGIGTRG PGEKKLETDR RHIMETIYDL KDELKKIKRT REVQREKRRK ENIPKVSLVG YTNAGKSTLR NTLCDLAAKN ENKTKEKVFE ANMLFATLDT TTRAVTLSKK GVITLTDTVG FVRKLPHDLV EAFKSTLEEV IFSDLLCHVI DVSSDSAIDQ YNAVNEVLSE LGAIDKETIL VLNKIDKATE EQKARIKEFA VGNFDVIEIS AKEKINLDKL LSLIEEKLPY NYRKVEYLIP YEKGDIQSFL HRNARILEEE YKDNGTYMVA EVDDEVFNKT QEYAKI // ID A6NVW7_9FIRM Unreviewed; 430 AA. AC A6NVW7; DT 21-AUG-2007, integrated into UniProtKB/TrEMBL. DT 21-AUG-2007, sequence version 1. DT 07-JUN-2017, entry version 50. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:EDM99860.1}; GN ORFNames=BACCAP_02360 {ECO:0000313|EMBL:EDM99860.1}; OS Pseudoflavonifractor capillosus ATCC 29799. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Pseudoflavonifractor. OX NCBI_TaxID=411467 {ECO:0000313|EMBL:EDM99860.1, ECO:0000313|Proteomes:UP000003639}; RN [1] {ECO:0000313|EMBL:EDM99860.1, ECO:0000313|Proteomes:UP000003639} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29799 {ECO:0000313|EMBL:EDM99860.1, RC ECO:0000313|Proteomes:UP000003639}; RA Fulton L., Clifton S., Fulton B., Xu J., Minx P., Pepin K.H., RA Johnson M., Thiruvilangam P., Bhonagiri V., Nash W.E., Mardis E.R., RA Wilson R.K.; RL Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:EDM99860.1, ECO:0000313|Proteomes:UP000003639} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29799 {ECO:0000313|EMBL:EDM99860.1, RC ECO:0000313|Proteomes:UP000003639}; RA Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., RA Liep D., Gordon J.; RT "Draft genome sequence of Pseudoflavonifractor capillosus ATCC RT 29799."; RL Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EDM99860.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AAXG02000014; EDM99860.1; -; Genomic_DNA. DR RefSeq; WP_006572891.1; NZ_AAXG02000014.1. DR ProteinModelPortal; A6NVW7; -. DR STRING; 411467.BACCAP_02360; -. DR EnsemblBacteria; EDM99860; EDM99860; BACCAP_02360. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000003639; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000003639}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000003639}. FT DOMAIN 205 366 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 164 198 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 430 AA; 47877 MW; 2F66F6204FBC36E7 CRC64; MTEHTTEEKR NRAVLVGLNA SCLSRTENAD EESMAELAAL LETAGGECVG EVLQNKDAPD PRTFIGEGKV REVKELVQSM EADMVVFDNA LSPSQQRALT DDLGVSVLDR SALILDIFAQ RARTKEGRLQ VELAQYKYLL PRLLGMWTHL ERQEGAIGTR GPGETQLETD RRHIRKKISK LEEDLEQVRR VRATQRERRI KNEVPVVAIV GYTNAGKSTL LNKLTGADIP ANNRLFDTLD TTTRTLEISD TCTVLISDTV GFISKLPHHL VEAFKATLEE LSFADLLLHV IDTSNPEWRE QAAVVEKLIV ELGAAQTPRI DVFNKSDLYV GDIVPHGEDI VSISAKTGAG LDELLKKIGD RLDTGAHRVV LRIPYDQGGV LDMLHREAKV ERVDYGEAIE VEAVCTPIQL GRLKDFIVSG WTPPKEFWED // ID A6TH88_KLEP7 Unreviewed; 426 AA. AC A6TH88; DT 21-AUG-2007, integrated into UniProtKB/TrEMBL. DT 21-AUG-2007, sequence version 1. DT 30-AUG-2017, entry version 65. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:ABR79922.1}; GN ORFNames=KPN_04571 {ECO:0000313|EMBL:ABR79922.1}; OS Klebsiella pneumoniae subsp. pneumoniae (strain ATCC 700721 / MGH OS 78578). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; OC Enterobacteriaceae; Klebsiella. OX NCBI_TaxID=272620 {ECO:0000313|EMBL:ABR79922.1, ECO:0000313|Proteomes:UP000000265}; RN [1] {ECO:0000313|EMBL:ABR79922.1, ECO:0000313|Proteomes:UP000000265} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700721 / MGH 78578 {ECO:0000313|Proteomes:UP000000265}; RG The Klebsiella pneumonia Genome Sequencing Project; RA McClelland M., Sanderson E.K., Spieth J., Clifton W.S., Latreille P., RA Sabo A., Pepin K., Bhonagiri V., Porwollik S., Ali J., Wilson R.K.; RL Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000647; ABR79922.1; -; Genomic_DNA. DR RefSeq; WP_004146725.1; NC_009648.1. DR ProteinModelPortal; A6TH88; -. DR STRING; 272620.KPN_04571; -. DR EnsemblBacteria; ABR79922; ABR79922; KPN_04571. DR KEGG; kpn:KPN_04571; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR Proteomes; UP000000265; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000000265}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Hydrolase {ECO:0000313|EMBL:ABR79922.1}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Protease {ECO:0000313|EMBL:ABR79922.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000265}. FT DOMAIN 198 365 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 426 AA; 48070 MW; 7E24BDE9CE348D9F CRC64; MFDRYDAGEQ AVLVHIYFSQ DKDMEDLQEF ETLASSAGVE AMQVITGSRK APHPKYFVGE GKAVEIAEAV KATGASVVLF DHALSPAQER NLERLCECRV IDRTGLILDI FAQRARTHEG KLQVELAQLR HMATRLVRGW THLERQKGGI GLRGPGETQL ETDRRLLRNR IMQILSRLEK VEKQREQGRR SRAKADIPTV SLVGYTNAGK STLFNQITAA EVYAANQLFA TLDPTLRRID VPDVGETVLA DTVGFIRHLP HDLVAAFKAT LQETRQATLL LHVIDAADVR VQENIDAVNT VLAEIEADEI PALLVMNKID MLDDFEPRID RDDENKPIRV WLSAQTGVGV PLLFQALTER LSGEVAQHTL RLPPKEGRLR SRFYQLQAIE KEWMEDDGSV SLQVRMPIVD WRRLCKQEPT LVDYVV // ID A6TQB5_ALKMQ Unreviewed; 429 AA. AC A6TQB5; DT 21-AUG-2007, integrated into UniProtKB/TrEMBL. DT 21-AUG-2007, sequence version 1. DT 07-JUN-2017, entry version 67. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Amet_2225 {ECO:0000313|EMBL:ABR48383.1}; OS Alkaliphilus metalliredigens (strain QYMF). OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Alkaliphilus. OX NCBI_TaxID=293826 {ECO:0000313|EMBL:ABR48383.1, ECO:0000313|Proteomes:UP000001572}; RN [1] {ECO:0000313|Proteomes:UP000001572} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=QYMF {ECO:0000313|Proteomes:UP000001572}; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., RA Pitluck S., Chertkov O., Brettin T., Bruce D., Han C., Schmutz J., RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Ye Q., RA Zhou J., Fields M., Richardson P.; RT "Complete sequence of Alkaliphilus metalliredigens QYMF."; RL Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Proteomes:UP000001572} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=QYMF {ECO:0000313|Proteomes:UP000001572}; RX PubMed=27811105; DOI=10.1128/genomeA.01226-16; RA Hwang C., Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina Del Rio T., Hammon N., Israni S., Dalin E., Tice H., RA Pitluck S., Chertkov O., Brettin T., Bruce D., Han C., Schmutz J., RA Larimer F., Land M.L., Hauser L., Kyrpides N., Mikhailova N., Ye Q., RA Zhou J., Richardson P., Fields M.W.; RT "Complete genome sequence of Alkaliphilus metalliredigens strain QYMF, RT an alkaliphilic and metal-reducing bacterium isolated from borax- RT contaminated leachate ponds."; RL Genome Announc. 4:0-0(2016). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000724; ABR48383.1; -; Genomic_DNA. DR RefSeq; WP_012063359.1; NC_009633.1. DR ProteinModelPortal; A6TQB5; -. DR STRING; 293826.Amet_2225; -. DR EnsemblBacteria; ABR48383; ABR48383; Amet_2225. DR KEGG; amt:Amet_2225; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000001572; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000001572}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000001572}. FT DOMAIN 206 376 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 172 199 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 429 AA; 48454 MW; B562E8EA0F4D4000 CRC64; METENLQSNK RPVAVLVGLN TTGKRKNDFD IEESMDELKE LAKAAGADVE AIVIQNRPAV DVTYYIGKGK VEEIKVFCDS VEADMVIFND VLSGSQIRNI EAAMDIDVID RTTLILDIFA QRAQAKEGKL QVELAQLKYR MPRLKGLGKQ MSKQGAGIGT RGPGEKKLET DRRHILSRIH DIEQELKEVK QNREVQRAQR KKSEIPIVAV VGYTNAGKST LMNRLLQMSE TYQEDREVFV KDMLFATLDV SLRKLVFNEK LTFILTDTVG FVSKLPHDLV NAFKATLEEV QYADLLLHVI DASNDNFEMQ RKTTLGVLHD LGVQSKKIID VYNKIDKVSD ASVLPKDDNT LHISALNKIN LDKLIESIRQ EIGVKVIECK LLIPFADGSV VSQIHQEGTV LSTEYVEEGV LIHIKIEDMY YQKYQSYEV // ID A6VN07_ACTSZ Unreviewed; 439 AA. AC A6VN07; DT 21-AUG-2007, integrated into UniProtKB/TrEMBL. DT 21-AUG-2007, sequence version 1. DT 30-AUG-2017, entry version 74. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Asuc_0986 {ECO:0000313|EMBL:ABR74354.1}; OS Actinobacillus succinogenes (strain ATCC 55618 / 130Z). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Actinobacillus. OX NCBI_TaxID=339671 {ECO:0000313|EMBL:ABR74354.1, ECO:0000313|Proteomes:UP000001114}; RN [1] {ECO:0000313|Proteomes:UP000001114} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 55618 / 130Z {ECO:0000313|Proteomes:UP000001114}; RX PubMed=21118570; DOI=10.1186/1471-2164-11-680; RA McKinlay J.B., Laivenieks M., Schindler B.D., McKinlay A.A., RA Siddaramappa S., Challacombe J.F., Lowry S.R., Clum A., Lapidus A.L., RA Burkhart K.B., Harkins V., Vieille C.; RT "A genomic perspective on the potential of Actinobacillus succinogenes RT for industrial succinate production."; RL BMC Genomics 11:680-680(2010). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000746; ABR74354.1; -; Genomic_DNA. DR ProteinModelPortal; A6VN07; -. DR STRING; 339671.Asuc_0986; -. DR EnsemblBacteria; ABR74354; ABR74354; Asuc_0986. DR KEGG; asu:Asuc_0986; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000001114; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000001114}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000001114}. FT DOMAIN 207 374 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 173 200 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 439 AA; 49246 MW; 2FEFA2A49336BC26 CRC64; MENTSTSTAL SLSENGHDKA IIVHVFFSQN KNSEDLAEFQ LLAQSAQADI LQTVTANRCA PQAKYFVGQG KAEEIAELAK QLNADVILVN HQLTPAQTRN LESLCGCRVV DRTGLILDIF AQRARSHEGK LQVELAQLKH LSTRLVRRKT GLDQQKGAVG LRGPGETQLE TDRRLIKVRI AQLQNRLEKV SRQRNQNRQT RQKADIPTVS LVGYTNAGKS TLFNRLTQAD VYAADQLFAT LDPTLRRLSV QDVGTAILAD TVGFIRDLPH DLVSAFKSTL QETTEASLLL HVIDAADMRK QENIAAVNAV LNEIQADNVP TLLVYNKIDR LNGVRPHIEF NDEQQPIAVY ISAQANVGID LLFDAIRQRL RNEILSLTVS LKPDQGKIRH AFYQLDCIRR ENTGEQGEYL LKLEIDKIEW LKLLKRFPEL APFNPIKNQ // ID A6VYL5_MARMS Unreviewed; 429 AA. AC A6VYL5; DT 21-AUG-2007, integrated into UniProtKB/TrEMBL. DT 21-AUG-2007, sequence version 1. DT 30-AUG-2017, entry version 67. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Mmwyl1_2631 {ECO:0000313|EMBL:ABR71544.1}; OS Marinomonas sp. (strain MWYL1). OC Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales; OC Marinomonas. OX NCBI_TaxID=400668 {ECO:0000313|EMBL:ABR71544.1, ECO:0000313|Proteomes:UP000001113}; RN [1] {ECO:0000313|EMBL:ABR71544.1, ECO:0000313|Proteomes:UP000001113} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MWYL1 {ECO:0000313|EMBL:ABR71544.1, RC ECO:0000313|Proteomes:UP000001113}; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., RA Dalin E., Tice H., Pitluck S., Kiss H., Brettin T., Bruce D., RA Detter J.C., Han C., Schmutz J., Larimer F., Land M., Hauser L., RA Kyrpides N., Kim E., Johnston A.W.B., Todd J.D., Rogers R., Wexler M., RA Bond P.L., Li Y., Richardson P.; RT "Complete sequence of Marinomonas sp. MWYL1."; RL Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000749; ABR71544.1; -; Genomic_DNA. DR RefSeq; WP_012070320.1; NC_009654.1. DR ProteinModelPortal; A6VYL5; -. DR STRING; 400668.Mmwyl1_2631; -. DR EnsemblBacteria; ABR71544; ABR71544; Mmwyl1_2631. DR KEGG; mmw:Mmwyl1_2631; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000001113; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000001113}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000001113}. FT DOMAIN 199 366 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 429 AA; 48145 MW; DAB98BBBC34CDE60 CRC64; MFFERPDSGE IAVLVHIDFH DQSESYGPEE FVELAISAGA DPVAVVSGTR QRPDARYFIG TGKLAEIKDI VDREEAQVVL FDHALSPSQE RNLESVLQCR VLDRTGLILD IFAQRARTHE GKLQVELAQL QHMSTRLIRG WTHLERQKGG IGMRGPGETQ LETDRRLLRE RIKAIQKRLA KVGSQRDQNR RSRDRSSVPT VSLVGYTNAG KSTLFNRATG ADVYAADQLF ATLDPTLRRL DIEQIGSIVL ADTVGFIRQL PHRLIKAFQA TLKESSEADL LLHIVDAADI SRDENMKHVD SVLEEIGANE VPTLTIFNKI DLLPTAEPRI DRDVNGNPFR VWLSARDGQG IDLLKQAIAE LLAEDVFNET LYLSSKYGRL RAMLFEHGAV KSERFDEAGR FVLDVKLPKK DYLQILARVG MSEDQIEAA // ID A6W852_KINRD Unreviewed; 530 AA. AC A6W852; DT 21-AUG-2007, integrated into UniProtKB/TrEMBL. DT 21-AUG-2007, sequence version 1. DT 07-JUN-2017, entry version 76. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Krad_1503 {ECO:0000313|EMBL:ABS02991.1}; OS Kineococcus radiotolerans (strain ATCC BAA-149 / DSM 14245 / OS SRS30216). OC Bacteria; Actinobacteria; Kineosporiales; Kineosporiaceae; OC Kineococcus. OX NCBI_TaxID=266940 {ECO:0000313|EMBL:ABS02991.1, ECO:0000313|Proteomes:UP000001116}; RN [1] {ECO:0000313|Proteomes:UP000001116} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-149 / DSM 14245 / SRS30216 RC {ECO:0000313|Proteomes:UP000001116}; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., RA Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Saunders E., RA Brettin T., Bruce D., Detter J.C., Han C., Schmutz J., Larimer F., RA Land M., Hauser L., Kyrpides N., Lykidis A., Bagwell C.E., RA Shimkets L., Berry C.J., Fliermans C., Richardson P.; RT "Complete sequence of chromosome of Kineococcus radiotolerans RT SRS30216."; RL Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000750; ABS02991.1; -; Genomic_DNA. DR RefSeq; WP_011981870.1; NC_009664.2. DR ProteinModelPortal; A6W852; -. DR STRING; 266940.Krad_1503; -. DR EnsemblBacteria; ABS02991; ABS02991; Krad_1503. DR KEGG; kra:Krad_1503; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000001116; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000001116}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000001116}. FT DOMAIN 308 474 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 530 AA; 56900 MW; 4726A107C6B2E7B7 CRC64; MNHRHASATP QSAEPEVSTT TASTRDEEFD RAVARILRGH GGEDGTRAVG SPEGAGGAPE DGDTGDGHTS YDGEQLDLAD RRALRRAAGL STELTDVTEV EYRQLRLERV VLAGVWSSAD SNRAEAEVSL QELSALAATA GSDVLAGVLQ RRTTPDVSTY LGSGKAAALA DLVAAEGADT VICDGELSAS QRRGLEDIVK VKVVDRTAVI LDIFAQHAKS REGKAQVELA QLEYLLPRLR GWGESMSRQA GGRVAAGAGI GSRGPGETKI ELDRRRIRSR MAKLRREIKG MGTARVEKRS LRHARAVPAV SIAGYTNAGK SSLLNRLTGA GVLVENALFA TLDPTVRRAQ TPEGRPYTLA DTVGFVRSLP HQLVEAFRST LEEVAESDVV LHVVDGSHPD PEGQLAAVRG VLADVDAQDV PELVAINKAD VADPEVVDRL LRREKNAVAV SARTGEGIEE LLERIARMLP VPDVEMEVCV PYDHGELVNR VHTTGQVLSE EHTGEGTRMR VRVRPRLAAE LERYRPAPTA // ID A6X119_OCHA4 Unreviewed; 472 AA. AC A6X119; DT 21-AUG-2007, integrated into UniProtKB/TrEMBL. DT 21-AUG-2007, sequence version 1. DT 07-JUN-2017, entry version 64. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Oant_2207 {ECO:0000313|EMBL:ABS14923.1}; OS Ochrobactrum anthropi (strain ATCC 49188 / DSM 6882 / JCM 21032 / NBRC OS 15819 / NCTC 12168). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Brucellaceae; Ochrobactrum. OX NCBI_TaxID=439375 {ECO:0000313|EMBL:ABS14923.1, ECO:0000313|Proteomes:UP000002301}; RN [1] {ECO:0000313|EMBL:ABS14923.1, ECO:0000313|Proteomes:UP000002301} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 49188 / DSM 6882 / JCM 21032 / NBRC 15819 / NCTC 12168 RC {ECO:0000313|Proteomes:UP000002301}; RX PubMed=21685287; DOI=10.1128/JB.05335-11; RA Chain P.S., Lang D.M., Comerci D.J., Malfatti S.A., Vergez L.M., RA Shin M., Ugalde R.A., Garcia E., Tolmasky M.E.; RT "Genome of Ochrobactrum anthropi ATCC 49188 T, a versatile RT opportunistic pathogen and symbiont of several eukaryotic hosts."; RL J. Bacteriol. 193:4274-4275(2011). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000758; ABS14923.1; -; Genomic_DNA. DR RefSeq; WP_012092092.1; NC_009667.1. DR ProteinModelPortal; A6X119; -. DR STRING; 439375.Oant_2207; -. DR EnsemblBacteria; ABS14923; ABS14923; Oant_2207. DR GeneID; 5380721; -. DR KEGG; oan:Oant_2207; -. DR PATRIC; fig|439375.7.peg.2320; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000002301; Chromosome 1. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000002301}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000002301}. FT DOMAIN 233 407 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 472 AA; 52339 MW; 041A3901361307B4 CRC64; MSKFKDKKPT SADADKAFEL SEPEPTRAAV IVPVLPERYN TGTSAEDGAR PEFQRSNEAR LEEAVGLARA INLDIEHAEI AIVANPRPAT LLGAGKVESI AETVKEKAIG LVIVDHALTP VQQRNLEKEW NVKVIDRTGL ILEIFGERAR TKEGALQVEL AHLNYQKGRL VRSWTHLERQ RGGGGFLGGP GETQIEADRR LLQDKILKIK RELETVVRTR TLHRQKRRKV PHPIVALVGY TNAGKSTLFN RMTGAEVLAE DMLFATLDPT LRRIRLPHGE TVILSDTVGF ISNLPHHLVA AFRATLEEVV EADLILHVRD ISDPDNAAQA EDVESILSGL GIEPQDRKRV VEIWNKIDNL DESGREAALR LAAAGSEEGR PIPLSAITGE GVDRLLSLIE TRIAGSLGPV DVVLSPFELH LLDWIYQHGS SVERENLEDG SVRIKARLTE VARKTLDEKR GIRPEKPESD WE // ID A7GNP5_BACCN Unreviewed; 419 AA. AC A7GNP5; DT 11-SEP-2007, integrated into UniProtKB/TrEMBL. DT 11-SEP-2007, sequence version 1. DT 07-JUN-2017, entry version 74. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Bcer98_1434 {ECO:0000313|EMBL:ABS21753.1}; OS Bacillus cytotoxicus (strain DSM 22905 / CIP 110041 / 391-98 / NVH OS 391-98). OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=315749 {ECO:0000313|EMBL:ABS21753.1, ECO:0000313|Proteomes:UP000002300}; RN [1] {ECO:0000313|EMBL:ABS21753.1, ECO:0000313|Proteomes:UP000002300} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 22905 / CIP 110041 / 391-98 / NVH 391-98 RC {ECO:0000313|Proteomes:UP000002300}; RX PubMed=17434157; DOI=10.1016/j.cbi.2007.03.003; RA Lapidus A., Goltsman E., Auger S., Galleron N., Segurens B., RA Dossat C., Land M.L., Broussolle V., Brillard J., Guinebretiere M.-H., RA Sanchis V., Nguen-the C., Lereclus D., Richardson P., Wincker P., RA Weissenbach J., Ehrlich S.D., Sorokin A.; RT "Extending the Bacillus cereus group genomics to putative food-borne RT pathogens of different toxicity."; RL Chem. Biol. Interact. 171:236-249(2008). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000764; ABS21753.1; -; Genomic_DNA. DR RefSeq; WP_012093927.1; NC_009674.1. DR ProteinModelPortal; A7GNP5; -. DR STRING; 315749.Bcer98_1434; -. DR EnsemblBacteria; ABS21753; ABS21753; Bcer98_1434. DR KEGG; bcy:Bcer98_1434; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; FNNHAHV; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000002300; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000002300}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}. FT DOMAIN 198 366 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 157 184 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 419 AA; 47803 MW; F1A58A047E018B89 CRC64; MEEFVQRAIL VGVNLGHESD FQYSMEELAN LAEACDVEVV GQVTQNLQRV NPSHYIGTGK IGEVAAYVKE VDANIVIFND ELSPSQIRNL EKDLDCKVID RTILILDIFA QRAKTKEAQL QVEVAHLQYM MPRLVGLRES LGRQSGGVGT KNKGVGEKKL ELDRRKIEEQ ISVLNKELEA LVVQRKTQRK QRKKNEIPVV ALVGYTNAGK STTMNAMLEI FNGTIEKQVF EKDMLFATLE TSVRNIELPD NKSFLLTDTV GFVSKLPHHL VKAFRSTLEE VAEADLLIHV VDYSNPNYEQ LIEITNQTLK QIGVENIPTI YAYNKSDMMD VEIPKTKKDR VYLSAKKQIG MEELVEMIRS HIYKEYTKCE MLIPYDQGQI VSYFNEYAHV ICTSYENEGT KLSLECKISD FEKYKRFAI // ID A7GR64_BACCN Unreviewed; 420 AA. AC A7GR64; DT 11-SEP-2007, integrated into UniProtKB/TrEMBL. DT 11-SEP-2007, sequence version 1. DT 07-JUN-2017, entry version 76. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Bcer98_2384 {ECO:0000313|EMBL:ABS22622.1}; OS Bacillus cytotoxicus (strain DSM 22905 / CIP 110041 / 391-98 / NVH OS 391-98). OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=315749 {ECO:0000313|EMBL:ABS22622.1, ECO:0000313|Proteomes:UP000002300}; RN [1] {ECO:0000313|EMBL:ABS22622.1, ECO:0000313|Proteomes:UP000002300} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 22905 / CIP 110041 / 391-98 / NVH 391-98 RC {ECO:0000313|Proteomes:UP000002300}; RX PubMed=17434157; DOI=10.1016/j.cbi.2007.03.003; RA Lapidus A., Goltsman E., Auger S., Galleron N., Segurens B., RA Dossat C., Land M.L., Broussolle V., Brillard J., Guinebretiere M.-H., RA Sanchis V., Nguen-the C., Lereclus D., Richardson P., Wincker P., RA Weissenbach J., Ehrlich S.D., Sorokin A.; RT "Extending the Bacillus cereus group genomics to putative food-borne RT pathogens of different toxicity."; RL Chem. Biol. Interact. 171:236-249(2008). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000764; ABS22622.1; -; Genomic_DNA. DR RefSeq; WP_012094819.1; NC_009674.1. DR ProteinModelPortal; A7GR64; -. DR STRING; 315749.Bcer98_2384; -. DR EnsemblBacteria; ABS22622; ABS22622; Bcer98_2384. DR KEGG; bcy:Bcer98_2384; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000002300; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000002300}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}. FT DOMAIN 197 359 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 420 AA; 47640 MW; 60BBF77061175FA2 CRC64; MEEKEKVILV GCQLPQDDDE RFMYSMTELA SLAKTARAEV LLSTTQKRPK FHPATYIGKG KLDELVTLSE ELEPDVIIFN NELTPSQIRN ISSVLDARVI DRTQLILDIF AQRAKSREGK LQVELAQLQY MMPRLMGQGL VLSRLGGGIG TRGPGETKLE TDRRHIRSRI DEIKKQLAVV VEHRKRYRER RKNNQTFQVA LIGYTNAGKS TLFNRLTEAD TFEENLLFAT LDPTTRKMQL PCGYTVLLTD TVGFIQDLPT SLVAAFRSTL EEAGEADVIL HVVDAADPNY AGHEQTVKQL LTELGIDHIP VITVYNKKDK LHQNFIPFPK SDFLMTSAFQ ENDLFNLKQA VEKKMIEEME PYKVKIPPSE GRLLALLKTD TVLTSMVFKE TELLYECTGY IFTHSALNES LQRFLVGKGE // ID A7H6U0_ANADF Unreviewed; 599 AA. AC A7H6U0; DT 11-SEP-2007, integrated into UniProtKB/TrEMBL. DT 11-SEP-2007, sequence version 1. DT 07-JUN-2017, entry version 63. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Anae109_0218 {ECO:0000313|EMBL:ABS24436.1}; OS Anaeromyxobacter sp. (strain Fw109-5). OC Bacteria; Proteobacteria; Deltaproteobacteria; Myxococcales; OC Cystobacterineae; Anaeromyxobacteraceae; Anaeromyxobacter. OX NCBI_TaxID=404589 {ECO:0000313|EMBL:ABS24436.1, ECO:0000313|Proteomes:UP000006382}; RN [1] {ECO:0000313|Proteomes:UP000006382} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Fw109-5 {ECO:0000313|Proteomes:UP000006382}; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., RA Dalin E., Tice H., Pitluck S., Sims D., Brettin T., Bruce D., RA Detter J.C., Han C., Schmutz J., Larimer F., Land M., Hauser L., RA Kyrpides N., Lykidis A., Fields M., Richardson P.; RT "Complete sequence of Anaeromyxobacter sp. Fw109-5."; RL Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000769; ABS24436.1; -; Genomic_DNA. DR RefSeq; WP_011984542.1; NC_009675.1. DR ProteinModelPortal; A7H6U0; -. DR STRING; 404589.Anae109_0218; -. DR EnsemblBacteria; ABS24436; ABS24436; Anae109_0218. DR KEGG; afw:Anae109_0218; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; EREVIIT; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000006382; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000006382}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000006382}. FT DOMAIN 379 543 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 599 AA; 65422 MW; 2CD26B6031CE4EF9 CRC64; MQDVLGNTLG LKPSQLHALR RTYRRRVDAA SIVSPELARH LSEVSRETNR QIGVLLDRKG DVHSVIVGDA RKLELPDVGR GRAGESRLRG LRLVHTHLNG EPLTRDDHTD LALLRLDLVA AIEVREDGLP GKVHFAHLVP ENAQGAMWKD EAAASVHDLA YDALSGALAL EEEFARARAV RRTGGRERAI LVGFGGKGRS RADAESSLEE LKELARTAGV EVIDATVQLR RDPDPRYLIG KGKLEDVVLR SMQLMATVIV FDAELSPSQA RHIAEATSLK ILDRTQLILD IFAQRAQSAD GKLQVELAQL KYLYPRLVGR DDSLSRLAGG IGGRGPGETK LEIDRRRVRD RITALERRIE ALGSSRQLRR KQRNGRGLPV LSIVGYTNAG KSTLLNALTD SAVLAEDKLF ATLDPTSRRL RFPRDREVII TDTVGFIRDL PPDLVNAFRA TLEELSDADL LLHVVDASDP RHPEQIEAVE TILASLGLEQ KQRLLVFNKA DRLPPGEGAA LAHRAEGIAV SALSRDGLAE LLHLCDRLLW EDRRVAFADV AASAPPPPAT PEPGEEGAAR AAATDRAAPE PTPPSPAARL LPSRIARVS // ID A7HJA6_FERNB Unreviewed; 421 AA. AC A7HJA6; DT 11-SEP-2007, integrated into UniProtKB/TrEMBL. DT 11-SEP-2007, sequence version 1. DT 07-JUN-2017, entry version 64. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Fnod_0122 {ECO:0000313|EMBL:ABS59989.1}; OS Fervidobacterium nodosum (strain ATCC 35602 / DSM 5306 / Rt17-B1). OC Bacteria; Thermotogae; Thermotogales; Fervidobacteriaceae; OC Fervidobacterium. OX NCBI_TaxID=381764 {ECO:0000313|EMBL:ABS59989.1, ECO:0000313|Proteomes:UP000002415}; RN [1] {ECO:0000313|EMBL:ABS59989.1, ECO:0000313|Proteomes:UP000002415} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 35602 / DSM 5306 / Rt17-B1 RC {ECO:0000313|Proteomes:UP000002415}; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., RA Dalin E., Tice H., Pitluck S., Saunders E., Brettin T., Bruce D., RA Detter J.C., Han C., Schmutz J., Larimer F., Land M., Hauser L., RA Kyrpides N., Mikhailova N., Nelson K., Gogarten J.P., Noll K., RA Richardson P.; RT "Complete sequence of Fervidobacterium nodosum Rt17-B1."; RL Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000771; ABS59989.1; -; Genomic_DNA. DR ProteinModelPortal; A7HJA6; -. DR STRING; 381764.Fnod_0122; -. DR PRIDE; A7HJA6; -. DR EnsemblBacteria; ABS59989; ABS59989; Fnod_0122. DR KEGG; fno:Fnod_0122; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000002415; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000002415}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000002415}. FT DOMAIN 196 324 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 162 189 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 421 AA; 48435 MW; 330D4F0A60B7A91F CRC64; MEKFGKKAIL LGVESTYNKD SFDSLDELET LCKTLEIEVV DKVIQRRVKP DSVTYVGSGK LHKIKDYCLA NSIDLIVIDD EITPIQLRNI EEITGLKVVD RTQIILEIFS KHASTHEGKL QVEMAKLIYD LPRLRGKGLE LSNPGGGIGT RGPGETILEL DRRRIKDRIS QLKKELEKIR KNRHTVRKSR LESGYYIFSV VGYTNAGKST LLSALSKEED IIISDKMFST LNPTVRRIKL PDGRFVLLSD TVGFIRKLPH TLVEAFHSTL EEILYSDVII ILVDVSDTNY KKKLSASFSV LEEIKANDKP YFIVFNKIDL VPEDYLDMIR YEYPNSVFIS AKSKLGFEVL YKKIREYIDI FDIRKRIHIK AEQLSVILKY ADFIEWNVVE YLNDGYILDI KGPENIVEKI SKQLKDDKQM F // ID A7HXU7_PARL1 Unreviewed; 474 AA. AC A7HXU7; DT 11-SEP-2007, integrated into UniProtKB/TrEMBL. DT 11-SEP-2007, sequence version 1. DT 07-JUN-2017, entry version 62. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Plav_3123 {ECO:0000313|EMBL:ABS64730.1}; OS Parvibaculum lavamentivorans (strain DS-1 / DSM 13023 / NCIMB 13966). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Rhodobiaceae; Parvibaculum. OX NCBI_TaxID=402881 {ECO:0000313|EMBL:ABS64730.1, ECO:0000313|Proteomes:UP000006377}; RN [1] {ECO:0000313|EMBL:ABS64730.1, ECO:0000313|Proteomes:UP000006377} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DS-1 / DSM 13023 / NCIMB 13966 RC {ECO:0000313|Proteomes:UP000006377}; RX PubMed=22675581; DOI=10.4056/sigs.2215005; RA Schleheck D., Weiss M., Pitluck S., Bruce D., Land M.L., Han S., RA Saunders E., Tapia R., Detter C., Brettin T., Han J., Woyke T., RA Goodwin L., Pennacchio L., Nolan M., Cook A.M., Kjelleberg S., RA Thomas T.; RT "Complete genome sequence of Parvibaculum lavamentivorans type strain RT (DS-1(T))."; RL Stand. Genomic Sci. 5:298-310(2011). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000774; ABS64730.1; -; Genomic_DNA. DR ProteinModelPortal; A7HXU7; -. DR STRING; 402881.Plav_3123; -. DR EnsemblBacteria; ABS64730; ABS64730; Plav_3123. DR KEGG; pla:Plav_3123; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000006377; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000006377}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000006377}. FT DOMAIN 227 402 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 193 220 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 474 AA; 51710 MW; F34AAD6E907D5548 CRC64; MTEEPKEEGA EKRGERGFRV KPAELTRAFV VVPWLKSVAK QAKRGGGGRS PESRLDEAVG LAAAISLNVV GSVVVPLASP RPATLFGEGK VDEIKGQIAE LRVDLVIVDG ALGPGQQRNL EKAWNVKVLD RTGLILEIFG ERARTREGSL QVELAHLNYQ KSRLVRSWTH LERQRGGFGF LGGPGETQIE ADRRLIQERI AKIEHQLETV KRTRELHRKK RREAPYPIVA LVGYTNAGKS TLFNRLTEAG VFAENLLFAT LDPTMRALVL PSGRKIILSD TVGFISDLPT HLVAAFRATL EEVLEAEVIL HVRDAAHEET AIQKTDVEKV LTSLGVTRES TAANGQHVVD VLNKIDLLEG EFRDAAVNLA MREPMTVAVS ALTGDGTENL LNLIDSLIVD DERPVHFDVP ANEGEAIAWL HANAHIRNRV DGDEGIVHLD LGLTPIVAGR FEKRFPALAR QLGEAAAAAA AAAE // ID A7INL9_XANP2 Unreviewed; 457 AA. AC A7INL9; DT 11-SEP-2007, integrated into UniProtKB/TrEMBL. DT 11-SEP-2007, sequence version 1. DT 07-JUN-2017, entry version 74. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Xaut_4392 {ECO:0000313|EMBL:ABS69613.1}; OS Xanthobacter autotrophicus (strain ATCC BAA-1158 / Py2). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Xanthobacteraceae; Xanthobacter. OX NCBI_TaxID=78245 {ECO:0000313|EMBL:ABS69613.1, ECO:0000313|Proteomes:UP000002417}; RN [1] {ECO:0000313|EMBL:ABS69613.1, ECO:0000313|Proteomes:UP000002417} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-1158 / Py2 {ECO:0000313|Proteomes:UP000002417}; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., RA Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Sims D., RA Brettin T., Bruce D., Detter J.C., Han C., Tapia R., Brainard J., RA Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E., RA Ensigns S.A., Richardson P.; RT "Complete sequence of chromosome of Xanthobacter autotrophicus Py2."; RL Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000781; ABS69613.1; -; Genomic_DNA. DR RefSeq; WP_012116362.1; NC_009720.1. DR ProteinModelPortal; A7INL9; -. DR STRING; 78245.Xaut_4392; -. DR EnsemblBacteria; ABS69613; ABS69613; Xaut_4392. DR KEGG; xau:Xaut_4392; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000002417; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000002417}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000002417}. FT DOMAIN 223 396 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 457 AA; 50077 MW; 57CA0B257F73F893 CRC64; MDVSVSAPAR EEGRGGIDRR APPTRCAVIT PALTKRATRG APERRSPQSR LEEAVGLAAA IDLDVVYSAT IPLSEIRPAT FLGSGKVEEL EGVVRAEAVD LVFFDAALSP VQQRNLEKAW SAKVVDRTAL ILEIFGMRAR TKEGALQVEL AHLNYQRSRL VRSWTHLERQ RGGFGFLGGP GETQIEADRR LIGERIVRIE KELEQVKRTR GLHRASRKRV PYPIVALVGY TNAGKSTLFN RLTRAEVMAK DLLFATLDPT LRAVDLPHGT RIILSDTVGF ISELPTQLVA AFRATLEEVL EADLILHVRD ISHPDTDAQA ADVSDVLEDL GVDPQPGGRV IEVWNKIDRL APDEREQVEN RAARGGAEAP VPVSALTGEG TDDLLGLIER RITAGRVTVS VTLAAEDGEG LGWLYRHGEV LERTTDEDGA IHVALRIPPD RAGLITRRFG ARRVHPT // ID A7MM90_CROS8 Unreviewed; 426 AA. AC A7MM90; DT 02-OCT-2007, integrated into UniProtKB/TrEMBL. DT 02-OCT-2007, sequence version 1. DT 30-AUG-2017, entry version 65. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=ESA_00183 {ECO:0000313|EMBL:ABU75484.1}; OS Cronobacter sakazakii (strain ATCC BAA-894) (Enterobacter sakazakii). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; OC Enterobacteriaceae; Cronobacter. OX NCBI_TaxID=290339 {ECO:0000313|EMBL:ABU75484.1, ECO:0000313|Proteomes:UP000000260}; RN [1] {ECO:0000313|EMBL:ABU75484.1, ECO:0000313|Proteomes:UP000000260} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-894 {ECO:0000313|EMBL:ABU75484.1, RC ECO:0000313|Proteomes:UP000000260}; RX PubMed=20221447; DOI=10.1371/journal.pone.0009556; RA Kucerova E., Clifton S.W., Xia X.Q., Long F., Porwollik S., Fulton L., RA Fronick C., Minx P., Kyung K., Warren W., Fulton R., Feng D., RA Wollam A., Shah N., Bhonagiri V., Nash W.E., Hallsworth-Pepin K., RA Wilson R.K., McClelland M., Forsythe S.J.; RT "Genome sequence of Cronobacter sakazakii BAA-894 and comparative RT genomic hybridization analysis with other Cronobacter species."; RL PLoS ONE 5:E9556-E9556(2010). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000783; ABU75484.1; -; Genomic_DNA. DR RefSeq; WP_004385294.1; NC_009778.1. DR ProteinModelPortal; A7MM90; -. DR STRING; 290339.ESA_00183; -. DR EnsemblBacteria; ABU75484; ABU75484; ESA_00183. DR GeneID; 29458691; -. DR KEGG; esa:ESA_00183; -. DR PATRIC; fig|290339.8.peg.161; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR Proteomes; UP000000260; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000000260}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000000260}. FT DOMAIN 198 365 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 426 AA; 48066 MW; D1C1E3CDC324A2F1 CRC64; MFDRYDAGEQ AVLVHIYFTQ DKDMEDLQEF ESLVSSAGVE ALQVITGSRK APHPKYFVGE GKAVEIADAV KATGASVVLF DHALTPAQER NLERLCECRV IDRTGLILDI FAQRARTHEG KLQVELAQLR HLATRLVRGW THLERQKGGI GLRGPGETQL ETDRRLLRNR ITQILSRLER VEKQREQGRR SRTKADIPTV SLVGYTNAGK STLFNQITTA EVYAADQLFA TLDPTLRRID VADVGETVLA DTVGFIRHLP HDLVAAFKAT LQETRQATLL LHVIDAADVR MAENIEAVNT VLEEIDAHEI PTLLVMNKVD MLEDFEPRID RNDENVPIRV WLSAQTGAGV PLLFQALTER LSGEIVQRAL RLPPEAGRLR SRFYQLQAIE KEWMEEDGCV GLQVRMPIVD WRRLCKQEPA LVDYVV // ID A7RKY6_NEMVE Unreviewed; 517 AA. AC A7RKY6; DT 02-OCT-2007, integrated into UniProtKB/TrEMBL. DT 02-OCT-2007, sequence version 1. DT 07-JUN-2017, entry version 55. DE SubName: Full=Predicted protein {ECO:0000313|EMBL:EDO47840.1}; GN ORFNames=v1g198618 {ECO:0000313|EMBL:EDO47840.1}; OS Nematostella vectensis (Starlet sea anemone). OC Eukaryota; Metazoa; Cnidaria; Anthozoa; Hexacorallia; Actiniaria; OC Edwardsiidae; Nematostella. OX NCBI_TaxID=45351 {ECO:0000313|Proteomes:UP000001593}; RN [1] {ECO:0000313|EMBL:EDO47840.1, ECO:0000313|Proteomes:UP000001593} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CH2 X CH6 {ECO:0000313|Proteomes:UP000001593}; RX PubMed=17615350; DOI=10.1126/science.1139158; RA Putnam N.H., Srivastava M., Hellsten U., Dirks B., Chapman J., RA Salamov A., Terry A., Shapiro H., Lindquist E., Kapitonov V.V., RA Jurka J., Genikhovich G., Grigoriev I.V., Lucas S.M., Steele R.E., RA Finnerty J.R., Technau U., Martindale M.Q., Rokhsar D.S.; RT "Sea anemone genome reveals ancestral eumetazoan gene repertoire and RT genomic organization."; RL Science 317:86-94(2007). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; DS469517; EDO47840.1; -; Genomic_DNA. DR RefSeq; XP_001639903.1; XM_001639853.1. DR ProteinModelPortal; A7RKY6; -. DR STRING; 45351.NEMVEDRAFT_v1g198618-PA; -. DR EnsemblMetazoa; EDO47840; EDO47840; NEMVEDRAFT_v1g198618. DR GeneID; 5519970; -. DR KEGG; nve:NEMVE_v1g198618; -. DR eggNOG; KOG0410; Eukaryota. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR InParanoid; A7RKY6; -. DR OMA; MDTVGFM; -. DR OrthoDB; EOG091G0852; -. DR Proteomes; UP000001593; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR GO; GO:0043022; F:ribosome binding; IBA:GO_Central. DR CDD; cd01878; HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000001593}; KW Reference proteome {ECO:0000313|Proteomes:UP000001593}. FT DOMAIN 288 458 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 517 AA; 58881 MW; 16FCF09C5FC1BB2D CRC64; MHSPLTRLLT SKLKHRSFLC KGHKEALGIL SAYRHLSKSN NKTPSWQEGL EEDDHPDTLE VLKSLRAKHH YHGKAVDDPK KHGVMVIEPD YKWGRHRFKK ATAEHRLEEA CGLVQAISNW TVNTSAIEPI RKVDTKSFFG KGKIEELQER ISQAKQIEEN TLDAVYLDVG QLTPRQHKEL EVFWDVKVFD RFGIVLQIFK ERAQTAEAKI QVELAEIPYI RSRLVGDDSV EFDQQRGGTH FISGSGETQL ERERRVLTER ELKLKKKLEA LRKHREHVRH ERQKRHIPVV SVVGYTNAGK TTLIKSLTGD NKMQPDNKLF ATLDVTAHPG KLPSGMQVLF VDTVGFVSDL PPELVESFSA TLEDMVDSDL VVHVRDVCHP EQEAQNEDVL SVLQQLKLRP ALMKTIINVY NKIDKCSAEH LQDTVSHMHT CEVQISALHG MGLDLLRKHI EEGIMKSTGR MIKRVVIPPD GPQLSWLYHE ATVHETVADE DGFITATVII DEATNNKFEK KFGKLLH // ID A7T861_NEMVE Unreviewed; 296 AA. AC A7T861; DT 02-OCT-2007, integrated into UniProtKB/TrEMBL. DT 02-OCT-2007, sequence version 1. DT 07-JUN-2017, entry version 44. DE SubName: Full=Predicted protein {ECO:0000313|EMBL:EDO27833.1}; DE Flags: Fragment; GN ORFNames=v1g223664 {ECO:0000313|EMBL:EDO27833.1}; OS Nematostella vectensis (Starlet sea anemone). OC Eukaryota; Metazoa; Cnidaria; Anthozoa; Hexacorallia; Actiniaria; OC Edwardsiidae; Nematostella. OX NCBI_TaxID=45351 {ECO:0000313|Proteomes:UP000001593}; RN [1] {ECO:0000313|EMBL:EDO27833.1, ECO:0000313|Proteomes:UP000001593} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CH2 X CH6 {ECO:0000313|Proteomes:UP000001593}; RX PubMed=17615350; DOI=10.1126/science.1139158; RA Putnam N.H., Srivastava M., Hellsten U., Dirks B., Chapman J., RA Salamov A., Terry A., Shapiro H., Lindquist E., Kapitonov V.V., RA Jurka J., Genikhovich G., Grigoriev I.V., Lucas S.M., Steele R.E., RA Finnerty J.R., Technau U., Martindale M.Q., Rokhsar D.S.; RT "Sea anemone genome reveals ancestral eumetazoan gene repertoire and RT genomic organization."; RL Science 317:86-94(2007). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; DS472516; EDO27833.1; -; Genomic_DNA. DR RefSeq; XP_001619933.1; XM_001619883.1. DR ProteinModelPortal; A7T861; -. DR STRING; 45351.NEMVEDRAFT_v1g223664-PA; -. DR EnsemblMetazoa; EDO27833; EDO27833; NEMVEDRAFT_v1g223664. DR GeneID; 5498179; -. DR KEGG; nve:NEMVE_v1g223664; -. DR eggNOG; KOG0410; Eukaryota. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR InParanoid; A7T861; -. DR OrthoDB; EOG091G0852; -. DR Proteomes; UP000001593; Unassembled WGS sequence. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR InterPro; IPR000644; CBS_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF00571; CBS; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51371; CBS; 2. PE 4: Predicted; KW CBS domain {ECO:0000256|PROSITE-ProRule:PRU00703}; KW Complete proteome {ECO:0000313|Proteomes:UP000001593}; KW Reference proteome {ECO:0000313|Proteomes:UP000001593}. FT DOMAIN 7 66 CBS. {ECO:0000259|PROSITE:PS51371}. FT DOMAIN 73 130 CBS. {ECO:0000259|PROSITE:PS51371}. FT NON_TER 296 296 {ECO:0000313|EMBL:EDO27833.1}. SQ SEQUENCE 296 AA; 33881 MW; CC266986B9DC8007 CRC64; MQLNKQIERN FVKLYPEMSL GTLLKEAVAK SSRNIFPVVD NQQQFLGVVM LDDIRPMMFD QTMYDKVYVS DVMKLAPEII TETDTAEQVM QKFKESVMIE AKEVTSEKAV LIGVITQHQD ENQLEEYLDE LEFLTLTAGG KAVKRFTQKL EKPHPKTFIG AGKLEDVRSY IETHDIGTAI FDDELSPAQL RNIEKALDCK ILDRTNLILD IFAQRAQTSS AKTQVELAQC QYFLPRLTKL WTHLDKQKGG IGMRGPGETE IETDRRIIRD KIALLKKKLA TIDKQMAVQR KNRGKM // ID A8A964_IGNH4 Unreviewed; 372 AA. AC A8A964; DT 23-OCT-2007, integrated into UniProtKB/TrEMBL. DT 23-OCT-2007, sequence version 1. DT 07-JUN-2017, entry version 64. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Igni_0283 {ECO:0000313|EMBL:ABU81466.1}; OS Ignicoccus hospitalis (strain KIN4/I / DSM 18386 / JCM 14125). OC Archaea; Crenarchaeota; Thermoprotei; Desulfurococcales; OC Desulfurococcaceae; Ignicoccus. OX NCBI_TaxID=453591 {ECO:0000313|EMBL:ABU81466.1, ECO:0000313|Proteomes:UP000000262}; RN [1] {ECO:0000313|EMBL:ABU81466.1, ECO:0000313|Proteomes:UP000000262} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=KIN4/I / DSM 18386 / JCM 14125 RC {ECO:0000313|Proteomes:UP000000262}; RX PubMed=19000309; DOI=10.1186/gb-2008-9-11-r158; RA Podar M., Anderson I., Makarova K.S., Elkins J.G., Ivanova N., RA Wall M.A., Lykidis A., Mavromatis K., Sun H., Hudson M.E., Chen W., RA Deciu C., Hutchison D., Eads J.R., Anderson A., Fernandes F., RA Szeto E., Lapidus A., Kyrpides N.C., Saier M.H.Jr., Richardson P.M., RA Rachel R., Huber H., Eisen J.A., Koonin E.V., Keller M., Stetter K.O.; RT "A genomic analysis of the archaeal system Ignicoccus hospitalis- RT Nanoarchaeum equitans."; RL Genome Biol. 9:R158.1-R158.18(2008). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000816; ABU81466.1; -; Genomic_DNA. DR RefSeq; WP_011998318.1; NC_009776.1. DR ProteinModelPortal; A8A964; -. DR STRING; 453591.Igni_0283; -. DR EnsemblBacteria; ABU81466; ABU81466; Igni_0283. DR GeneID; 5561888; -. DR KEGG; iho:Igni_0283; -. DR eggNOG; arCOG00353; Archaea. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; FNNHAHV; -. DR OrthoDB; POG093Z07D6; -. DR Proteomes; UP000000262; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000000262}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000000262}. FT DOMAIN 179 362 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 144 171 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 372 AA; 41518 MW; F73B1BC9F8B7AA33 CRC64; MACKKRADFQ EALALCETAG YEVVATVNFC KKPHPATYIT PGKLEELKAT IKEGGAEAVI VYGNPKPSQF YRLKKELGVE VVDRTSLILK IFELHAGSKE AKLQTELARL KYELTLAREY VRRVKMGEQV DFLGPGEYAA KYVIKAIKRR IKKIEEELEK IRTMREQQKL RRVKRLRVPE VAVTGYTCAG KTALVNALGK LNLKEGPEMF TTLAPKHVRV SVYENGLYEA IFIDTVGFIE GIPPQILEVF HATLAEITYS DAAVLVLDGS EELSRALDKL ESSLATLAEI GFIGKPLVIA FNKIDLVDDY EEKVLEVDDW ARSLYPWTWG TVPISAKKGT NLRRLVIESV LAARGARNIK EPETNVCGKG AC // ID A8AMM8_CITK8 Unreviewed; 426 AA. AC A8AMM8; DT 23-OCT-2007, integrated into UniProtKB/TrEMBL. DT 23-OCT-2007, sequence version 1. DT 30-AUG-2017, entry version 66. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=CKO_03662 {ECO:0000313|EMBL:ABV14741.1}; OS Citrobacter koseri (strain ATCC BAA-895 / CDC 4225-83 / SGSC4696). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; OC Enterobacteriaceae; Citrobacter. OX NCBI_TaxID=290338 {ECO:0000313|EMBL:ABV14741.1, ECO:0000313|Proteomes:UP000008148}; RN [1] {ECO:0000313|EMBL:ABV14741.1, ECO:0000313|Proteomes:UP000008148} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-895 / CDC 4225-83 / SGSC4696 RC {ECO:0000313|Proteomes:UP000008148}; RG The Citrobacter koseri Genome Sequencing Project; RA McClelland M., Sanderson E.K., Porwollik S., Spieth J., Clifton W.S., RA Latreille P., Courtney L., Wang C., Pepin K., Bhonagiri V., Nash W., RA Johnson M., Thiruvilangam P., Wilson R.; RL Submitted (AUG-2007) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000822; ABV14741.1; -; Genomic_DNA. DR RefSeq; WP_012134438.1; NC_009792.1. DR ProteinModelPortal; A8AMM8; -. DR STRING; 290338.CKO_03662; -. DR EnsemblBacteria; ABV14741; ABV14741; CKO_03662. DR KEGG; cko:CKO_03662; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000008148; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000008148}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000008148}. FT DOMAIN 198 365 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 164 191 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 426 AA; 48306 MW; D27F1A68BACA84FE CRC64; MFDRYDAGEQ AVLVHIYFSQ DKDMEDLQEF ESLVSSAGVE AMQVITGSRK APHPKYFVGE GKAVEIAEAV KASNAAVVLF DHALSPAQER NLERLCECRV IDRTGLILDI FAQRARTHEG KLQVELAQLR HLATRLVRGW THLERQKGGI GLRGPGETQL ETDRRLLRNR IVQIQSRLEK VEKQREQGRQ SRIKADVPTV SLVGYTNAGK STLFNQITEA RVYAADQLFA TLDPTLRRID VADVGETVLA DTVGFIRHLP HDLVAAFKAT LQETRQATLL LHVVDAADVR VQENIDAVDT VLEEIDAHEI PTLMVMNKID MLDDFEPRID RDEENKPIRV WLSAQTGIGI PQLFQALTER LSGEVAQHTL RLPPQEGRLR SRFYQLQAIE KEWMEEDGSV SLQVRMPIVD WRRLCKQEPA LIDYVI // ID A8F5B5_PSELT Unreviewed; 416 AA. AC A8F5B5; DT 13-NOV-2007, integrated into UniProtKB/TrEMBL. DT 13-NOV-2007, sequence version 1. DT 07-JUN-2017, entry version 64. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Tlet_0783 {ECO:0000313|EMBL:ABV33349.1}; OS Pseudothermotoga lettingae (strain ATCC BAA-301 / DSM 14385 / NBRC OS 107922 / TMO) (Thermotoga lettingae). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; OC Pseudothermotoga. OX NCBI_TaxID=416591 {ECO:0000313|EMBL:ABV33349.1, ECO:0000313|Proteomes:UP000002016}; RN [1] {ECO:0000313|EMBL:ABV33349.1, ECO:0000313|Proteomes:UP000002016} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-301 / DSM 14385 / NBRC 107922 / TMO RC {ECO:0000313|Proteomes:UP000002016}; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., RA Dalin E., Tice H., Pitluck S., Foster B., Bruce D., Schmutz J., RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Nelson K., RA Gogarten J.P., Noll K., Richardson P.; RT "Complete sequence of Thermotoga lettingae TMO."; RL Submitted (AUG-2007) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000812; ABV33349.1; -; Genomic_DNA. DR RefSeq; WP_012002830.1; NC_009828.1. DR ProteinModelPortal; A8F5B5; -. DR STRING; 416591.Tlet_0783; -. DR EnsemblBacteria; ABV33349; ABV33349; Tlet_0783. DR KEGG; tle:Tlet_0783; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000002016; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000002016}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000002016}. FT DOMAIN 195 360 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 154 181 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 416 AA; 47377 MW; 9D88A6931AC64A4A CRC64; MQQIKRNELM RAIVITIKGD YSSVEEIQQL LRTLNIDTVE VLYQKRERPD SRYYVGEGKI GKLLELIDFS GAHMVVVDDE LTPVQAKNLE KKLSVVIKDR TQVILDIFAQ HATTEEGKLQ VEFAKLKYEL PRLIGQGKWL SRLGGGTGTR GPGEQKIEEK RRKIRERIVA IKRQLSELAK DRTQQRKMRL NSELPMVSVV GYTNAGKSSL IKIISGSDIL IANQLFSTLS PVVRRVKLPS GRVALFKDTV GFIKNVPHTI IEAFKSTLEE ILFSDLILLV VDLSDENFQE KLDTSLSVVY ELGADEIPRL LVFNKVDLIP YSQRIKILQS YPGAILISAV KADGIRELLS CIDKELEKSE KEALLTFKLQ DMSWVLKERE KIVVKEQIFR DNQVIVRIKA RSSVLERLRQ HSTQEG // ID A8FDJ9_BACP2 Unreviewed; 420 AA. AC A8FDJ9; DT 13-NOV-2007, integrated into UniProtKB/TrEMBL. DT 13-NOV-2007, sequence version 1. DT 07-JUN-2017, entry version 77. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=BPUM_1634 {ECO:0000313|EMBL:ABV62316.1}; OS Bacillus pumilus (strain SAFR-032). OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus. OX NCBI_TaxID=315750 {ECO:0000313|EMBL:ABV62316.1, ECO:0000313|Proteomes:UP000001355}; RN [1] {ECO:0000313|EMBL:ABV62316.1, ECO:0000313|Proteomes:UP000001355} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SAFR-032 {ECO:0000313|EMBL:ABV62316.1, RC ECO:0000313|Proteomes:UP000001355}; RX PubMed=17895969; DOI=10.1371/journal.pone.0000928; RA Gioia J., Yerrapragada S., Qin X., Jiang H., Igboeli O.C., Muzny D., RA Dugan-Rocha S., Ding Y., Hawes A., Liu W., Perez L., Kovar C., RA Dinh H., Lee S., Nazareth L., Blyth P., Holder M., Buhay C., RA Tirumalai M.R., Liu Y., Dasgupta I., Bokhetache L., Fujita M., RA Karouia F., Eswara Moorthy P., Siefert J., Uzman A., Buzumbo P., RA Verma A., Zwiya H., McWilliams B.D., Olowu A., Clinkenbeard K.D., RA Newcombe D., Golebiewski L., Petrosino J.F., Nicholson W.L., Fox G.E., RA Venkateswaran K., Highlander S.K., Weinstock G.M.; RT "Paradoxical DNA repair and peroxide resistance gene conservation in RT Bacillus pumilus SAFR-032."; RL PLoS ONE 2:E928-E928(2007). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000813; ABV62316.1; -; Genomic_DNA. DR RefSeq; WP_012010048.1; NC_009848.4. DR ProteinModelPortal; A8FDJ9; -. DR STRING; 315750.BPUM_1634; -. DR EnsemblBacteria; ABV62316; ABV62316; BPUM_1634. DR KEGG; bpu:BPUM_1634; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000001355; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000001355}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000001355}. FT DOMAIN 200 362 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 420 AA; 47743 MW; 96F0E9E1C5F1F481 CRC64; MNEHEMTEKA ILVGCQLPHV TDERFQYSME ELASLTKTAG GEAVSVMTQK RNRQDSATYI GKGKVEELEV LCEEFECDVI IFNDELSPSQ LKSLATALDV KIIDRTQLIL DIFAKRARTR EGKLQIELAQ LQYALPRLSG QGISLSRQGG GIGARGPGET KLETDRRHIR NRIHEINGQL STVKEHRTRY RERRKKNGVF QIAIVGYTNA GKSTLFNQLT DADSHEEDLL FATLDPMTRK MTLASGYSVL ISDTVGFIQD LPTTLIAAFR STLEEVKEAD YLLHVIDSSN EDYEGHERTV HELLEELEAD RIPMLTVYNK EDQIRPDFIP SSKHRHLLIS ARREEDVKRL KADIMAELKQ NFLKPYHVKI PAYEGKLISA LKSETLVESL EFQKEAELYD ITGFSGEEQT ILGQIKKYML // ID A8G8V0_SERP5 Unreviewed; 426 AA. AC A8G8V0; DT 13-NOV-2007, integrated into UniProtKB/TrEMBL. DT 13-NOV-2007, sequence version 1. DT 30-AUG-2017, entry version 64. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Spro_0432 {ECO:0000313|EMBL:ABV39540.1}; OS Serratia proteamaculans (strain 568). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; OC Yersiniaceae; Serratia. OX NCBI_TaxID=399741 {ECO:0000313|EMBL:ABV39540.1, ECO:0000313|Proteomes:UP000007074}; RN [1] {ECO:0000313|EMBL:ABV39540.1, ECO:0000313|Proteomes:UP000007074} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=568 {ECO:0000313|EMBL:ABV39540.1, RC ECO:0000313|Proteomes:UP000007074}; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., RA Dalin E., Tice H., Pitluck S., Chain P., Malfatti S., Shin M., RA Vergez L., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., RA Kim E., Taghavi S., Newman L., Vangronsveld J., van der Lelie D., RA Richardson P.; RT "Complete sequence of chromosome of Serratia proteamaculans 568."; RL Submitted (SEP-2007) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000826; ABV39540.1; -; Genomic_DNA. DR RefSeq; WP_012004895.1; NC_009832.1. DR ProteinModelPortal; A8G8V0; -. DR STRING; 399741.Spro_0432; -. DR EnsemblBacteria; ABV39540; ABV39540; Spro_0432. DR KEGG; spe:Spro_0432; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000007074; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000007074}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000007074}. FT DOMAIN 198 365 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 426 AA; 47974 MW; CE6BAF7904B4ED87 CRC64; MFDRYEAGEQ AVLVHIYFSQ DKDTEDLSEF ESLVSSAGVE ALQVVTGSRK APHPKYFVGE GKAEEIADAV KASGASVVLF DHSLSAAQER NLERLCECRV IDRTGLILDI FAQRARTHEG KLQVELAQLR HIATRLVRGW THLERQKGGI GLRGPGETQL ETDRRLLRDR ISLILRRLER VAKQREQGRR ARTRAEVPTV SLVGYTNAGK STLFNRITSA DVYAADQLFA TLDPTLRRID VADVGDTVLA DTVGFIRHLP HDLVAAFKAT LQETRQASLL LHVIDAADTR VDENIEAVNT VLAEIESDEI PTLLVMNKID MLDDFVPRID RNDENLPIRV WLSAASGEGI PLLYQALTER LSGEIAHYEL RLPPEAGRLR SRFYQLQAIE KEWNEEDGSI GVVVRMPIVE WRRLCKQELD LINFIV // ID A8H8G5_SHEPA Unreviewed; 431 AA. AC A8H8G5; DT 13-NOV-2007, integrated into UniProtKB/TrEMBL. DT 13-NOV-2007, sequence version 1. DT 30-AUG-2017, entry version 72. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Spea_3539 {ECO:0000313|EMBL:ABV88852.1}; OS Shewanella pealeana (strain ATCC 700345 / ANG-SQ1). OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales; OC Shewanellaceae; Shewanella. OX NCBI_TaxID=398579 {ECO:0000313|EMBL:ABV88852.1, ECO:0000313|Proteomes:UP000002608}; RN [1] {ECO:0000313|EMBL:ABV88852.1, ECO:0000313|Proteomes:UP000002608} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700345 / ANG-SQ1 {ECO:0000313|Proteomes:UP000002608}; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., RA Dalin E., Tice H., Pitluck S., Chertkov O., Brettin T., Bruce D., RA Detter J.C., Han C., Schmutz J., Larimer F., Land M., Hauser L., RA Kyrpides N., Kim E., Zhao J.-S.Z., Manno D., Hawari J., Richardson P.; RT "Complete sequence of Shewanella pealeana ATCC 700345."; RL Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000851; ABV88852.1; -; Genomic_DNA. DR RefSeq; WP_012156737.1; NC_009901.1. DR ProteinModelPortal; A8H8G5; -. DR STRING; 398579.Spea_3539; -. DR EnsemblBacteria; ABV88852; ABV88852; Spea_3539. DR KEGG; spl:Spea_3539; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000002608; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000002608}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000002608}. FT DOMAIN 198 364 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 431 AA; 48600 MW; 085E93EA2C3107A1 CRC64; MFDRYEAGEK AVLVHIDFTD ENNREDLDEL KLLVDSAGAQ SIGVISGSRR SPDRKYFVGS GKAEELAAMV AATDANVVIF NHKLSPAQER NLEKICECRV LDRTTLILDI FAQRARTFEG KLQVELAQLR HMSTRLIRGW THLERQKGGI GLRGPGETQL ETDRRLLRGR IRTINRRLEK VDKQRDQSRR ARQRSDMSTV SLVGYTNAGK STLFNGLTTS DVYAADQLFA TLDPTLRKLE LPDGDVILAD TVGFIRHLPH DLVAAFKATL QETRQADLLL HVVDSADEKM ADNFEQVQKV LKEIDAIDIP QLIVCNKIDL LDEVKPRIDY DDEGTPIRVW VSAQQQKGLE LVEDAINQLV GKAIQELTLQ IPASAGHYLG QFYKLDVIQQ KEYDDLGNCM ISVRLLDADW RRLVKQSQGE LETFVVDPVV A // ID A8IBJ4_AZOC5 Unreviewed; 459 AA. AC A8IBJ4; DT 04-DEC-2007, integrated into UniProtKB/TrEMBL. DT 04-DEC-2007, sequence version 1. DT 07-JUN-2017, entry version 65. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=AZC_3079 {ECO:0000313|EMBL:BAF89077.1}; OS Azorhizobium caulinodans (strain ATCC 43989 / DSM 5975 / JCM 20966 / OS NBRC 14845 / NCIMB 13405 / ORS 571). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Xanthobacteraceae; Azorhizobium. OX NCBI_TaxID=438753 {ECO:0000313|EMBL:BAF89077.1, ECO:0000313|Proteomes:UP000000270}; RN [1] {ECO:0000313|Proteomes:UP000000270} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43989 / DSM 5975 / JCM 20966 / NBRC 14845 / NCIMB 13405 / RC ORS 571 {ECO:0000313|Proteomes:UP000000270}; RA Lee K.B., Backer P.D., Aono T., Liu C.T., Suzuki S., Suzuki T., RA Kaneko T., Yamada M., Tabata S., Kupfer D.M., Najar F.Z., Wiley G.B., RA Roe B., Binnewies T., Ussery D., Vereecke D., Gevers D., Holsters M., RA Oyaizu H.; RT "Complete genome sequence of the nitrogen-fixing bacterium RT Azorhizobium caulinodans ORS571."; RL Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AP009384; BAF89077.1; -; Genomic_DNA. DR ProteinModelPortal; A8IBJ4; -. DR STRING; 438753.AZC_3079; -. DR EnsemblBacteria; BAF89077; BAF89077; AZC_3079. DR KEGG; azc:AZC_3079; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000000270; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000000270}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000000270}. FT DOMAIN 223 397 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 459 AA; 49955 MW; B401CFD98A234629 CRC64; MELKGPRGAA GGGLKGVDRH APPTRCAVIT PQVTKRGARA GADRRSPEAR LEEAVGLAAA IDLDVVYKGL VLISEVKPAT YIGSGKVEEI AGIVAAEEVG LVFVDAALSP VQQRNLEKAW SAKVVDRTAL ILEIFGSRAR TKEGTLQVEL AHLNYQRSRL VRSWTHLERQ RGGFGFLGGP GETQIEADRR QIGERIIRIE RELEQVKRTR ALHRTSRKRV PYPVVALVGY TNAGKSTLFN RLTQAEVMAQ DLLFATLDPT LRAVDLPHGT RVILSDTVGF ISELPTQLVA AFRATLEEVI EADVILHVRD ISHPDTDAQA ADVKDVLTEL GIDVEAGGRL VEVWNKIDIL PEAEREQLLN TAARAEPEAR PELVSALTGE GAPALLDRIE AHVTAGRTLL SVTLAAEDGE GLGWLYRHGE VLERESGADG HVVVSLRILP ERVDLVKRRF GAAQVRGED // ID A8JF79_CHLRE Unreviewed; 403 AA. AC A8JF79; DT 04-DEC-2007, integrated into UniProtKB/TrEMBL. DT 04-DEC-2007, sequence version 1. DT 07-JUN-2017, entry version 55. DE SubName: Full=Predicted protein {ECO:0000313|EMBL:EDO97467.1}; DE Flags: Fragment; GN ORFNames=CHLREDRAFT_107789 {ECO:0000313|EMBL:EDO97467.1}; OS Chlamydomonas reinhardtii (Chlamydomonas smithii). OC Eukaryota; Viridiplantae; Chlorophyta; Chlorophyceae; OC Chlamydomonadales; Chlamydomonadaceae; Chlamydomonas. OX NCBI_TaxID=3055 {ECO:0000313|Proteomes:UP000006906}; RN [1] {ECO:0000313|EMBL:EDO97467.1, ECO:0000313|Proteomes:UP000006906} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CC-503 {ECO:0000313|Proteomes:UP000006906}; RX PubMed=17932292; DOI=10.1126/science.1143609; RA Merchant S.S., Prochnik S.E., Vallon O., Harris E.H., Karpowicz S.J., RA Witman G.B., Terry A., Salamov A., Fritz-Laylin L.K., RA Marechal-Drouard L., Marshall W.F., Qu L.H., Nelson D.R., RA Sanderfoot A.A., Spalding M.H., Kapitonov V.V., Ren Q., Ferris P., RA Lindquist E., Shapiro H., Lucas S.M., Grimwood J., Schmutz J., RA Cardol P., Cerutti H., Chanfreau G., Chen C.L., Cognat V., Croft M.T., RA Dent R., Dutcher S., Fernandez E., Fukuzawa H., Gonzalez-Ballester D., RA Gonzalez-Halphen D., Hallmann A., Hanikenne M., Hippler M., Inwood W., RA Jabbari K., Kalanon M., Kuras R., Lefebvre P.A., Lemaire S.D., RA Lobanov A.V., Lohr M., Manuell A., Meier I., Mets L., Mittag M., RA Mittelmeier T., Moroney J.V., Moseley J., Napoli C., Nedelcu A.M., RA Niyogi K., Novoselov S.V., Paulsen I.T., Pazour G.J., Purton S., RA Ral J.P., Riano-Pachon D.M., Riekhof W., Rymarquis L., Schroda M., RA Stern D., Umen J., Willows R., Wilson N., Zimmer S.L., Allmer J., RA Balk J., Bisova K., Chen C.J., Elias M., Gendler K., Hauser C., RA Lamb M.R., Ledford H., Long J.C., Minagawa J., Page M.D., Pan J., RA Pootakham W., Roje S., Rose A., Stahlberg E., Terauchi A.M., Yang P., RA Ball S., Bowler C., Dieckmann C.L., Gladyshev V.N., Green P., RA Jorgensen R., Mayfield S., Mueller-Roeber B., Rajamani S., Sayre R.T., RA Brokstein P., Dubchak I., Goodstein D., Hornick L., Huang Y.W., RA Jhaveri J., Luo Y., Martinez D., Ngau W.C., Otillar B., Poliakov A., RA Porter A., Szajkowski L., Werner G., Zhou K., Grigoriev I.V., RA Rokhsar D.S., Grossman A.R.; RT "The Chlamydomonas genome reveals the evolution of key animal and RT plant functions."; RL Science 318:245-250(2007). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; DS496174; EDO97467.1; -; Genomic_DNA. DR RefSeq; XP_001701470.1; XM_001701418.1. DR ProteinModelPortal; A8JF79; -. DR STRING; 3055.EDO97467; -. DR PaxDb; A8JF79; -. DR EnsemblPlants; EDO97467; EDO97467; CHLREDRAFT_107789. DR GeneID; 5726984; -. DR Gramene; EDO97467; EDO97467; CHLREDRAFT_107789. DR KEGG; cre:CHLREDRAFT_107789; -. DR eggNOG; KOG0410; Eukaryota. DR eggNOG; COG2262; LUCA. DR InParanoid; A8JF79; -. DR KO; K03665; -. DR Proteomes; UP000006906; Unassembled WGS sequence. DR GO; GO:0009507; C:chloroplast; IEA:EnsemblPlants. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR GO; GO:0043022; F:ribosome binding; IBA:GO_Central. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000006906}; KW Reference proteome {ECO:0000313|Proteomes:UP000006906}. FT DOMAIN 206 372 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 165 199 {ECO:0000256|SAM:Coils}. FT NON_TER 1 1 {ECO:0000313|EMBL:EDO97467.1}. FT NON_TER 403 403 {ECO:0000313|EMBL:EDO97467.1}. SQ SEQUENCE 403 AA; 44214 MW; 7A608628865380E6 CRC64; ERVFLVGAAI KGEQKKYTYD VHESVEELGR LAETAGLKVM GSTFQMLEAP NMSTYIGSGK VAEVARAVAA LDVETVIFDD ELSPGQLRNL ERALGGTGPD GLPVDVRVCD RTALILDIFS QRAQTREGQL QVELAQTEYQ LPRLTKMWSH LDRVGGGGQV KGTGEKQIEI DKRLLRDKAA QLRRELEAVR THRRQYREKR SSTPIPVVGI CGYTNAGKST LLNTITGAGV LAEDQLFATL DPTTRRVRLK GNKEILLSDT VGFIQKLPTE LVAAFRATLE EIQDASIILH VVDISHPNAA AQNEAVMQVL TELGVDHIPI VTAWNKIDAC SNPDEVRRIA AKRTRTVCIS GMTGEGLEQL MEVLGGELEK AMVEVHALLP YSAGDLLNDL HTGGRVKNQE YKE // ID A8L6K3_FRASN Unreviewed; 503 AA. AC A8L6K3; DT 04-DEC-2007, integrated into UniProtKB/TrEMBL. DT 04-DEC-2007, sequence version 1. DT 07-JUN-2017, entry version 70. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Franean1_1231 {ECO:0000313|EMBL:ABW10685.1}; OS Frankia sp. (strain EAN1pec). OC Bacteria; Actinobacteria; Frankiales; Frankiaceae; Frankia. OX NCBI_TaxID=298653 {ECO:0000313|EMBL:ABW10685.1, ECO:0000313|Proteomes:UP000001313}; RN [1] {ECO:0000313|Proteomes:UP000001313} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=EAN1pec {ECO:0000313|Proteomes:UP000001313}; RX PubMed=17151343; DOI=10.1101/gr.5798407; RA Normand P., Lapierre P., Tisa L.S., Gogarten J.P., Alloisio N., RA Bagnarol E., Bassi C.A., Berry A.M., Bickhart D.M., Choisne N., RA Couloux A., Cournoyer B., Cruveiller S., Daubin V., Demange N., RA Francino M.P., Goltsman E., Huang Y., Kopp O.R., Labarre L., RA Lapidus A., Lavire C., Marechal J., Martinez M., Mastronunzio J.E., RA Mullin B.C., Niemann J., Pujic P., Rawnsley T., Rouy Z., RA Schenowitz C., Sellstedt A., Tavares F., Tomkins J.P., Vallenet D., RA Valverde C., Wall L.G., Wang Y., Medigue C., Benson D.R.; RT "Genome characteristics of facultatively symbiotic Frankia sp. strains RT reflect host range and host plant biogeography."; RL Genome Res. 17:7-15(2007). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000820; ABW10685.1; -; Genomic_DNA. DR RefSeq; WP_020458860.1; NC_009921.1. DR ProteinModelPortal; A8L6K3; -. DR STRING; 298653.Franean1_1231; -. DR EnsemblBacteria; ABW10685; ABW10685; Franean1_1231. DR KEGG; fre:Franean1_1231; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000001313; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000001313}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000001313}. FT DOMAIN 285 450 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 503 AA; 53811 MW; F026AB7BCE7B4468 CRC64; MSLRADAAVA STRHLKLHSG ENDGHDGHDG RDGRAGTALA LAEADGFSFF DEEGDGLDLE DRGALRRVPG LTTELEDVTE VEYRQLRLEQ VVLIGVWTSG SQVEAEASMA ELAALATTAG SVVLDALVQR RDRPDAATFV GSGKAKELAE IVLATGADTV ICDGELTPGQ LRQLEEVVKV KVIDRTALIL DIFAQHATSR EGKAQVELAQ LQYMLPRLRG WGESMSRQAA SGGRAPIGTR GPGETKIETD RRRLRARITK LRRELTGMAT VRATKRSSRR RGAVPAVAIA GYTNAGKSSL LNRLTGAGVL VEDALFATLD PTVRRATLPD GRIFTLADTV GFVRHLPHQI VEAFRSTLEE VVDADLVLHV VDGSAPDPMG QISAVREVLA EIDAAGVPEL IVVNKVDAVD PTTLAVLRQA VPDAIFVSAR SGAGLQELVE ALSARIPHPE VEMSLLVPYT RGDLVSRIHQ IGEVLRVEHT GKGTEVAARV PVGLAAELEP FRA // ID A8LKU4_DINSH Unreviewed; 415 AA. AC A8LKU4; DT 04-DEC-2007, integrated into UniProtKB/TrEMBL. DT 04-DEC-2007, sequence version 1. DT 07-JUN-2017, entry version 64. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:ABV93308.1}; GN OrderedLocusNames=Dshi_1566 {ECO:0000313|EMBL:ABV93308.1}; OS Dinoroseobacter shibae (strain DSM 16493 / NCIMB 14021 / DFL 12). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae; Dinoroseobacter. OX NCBI_TaxID=398580 {ECO:0000313|EMBL:ABV93308.1, ECO:0000313|Proteomes:UP000006833}; RN [1] {ECO:0000313|Proteomes:UP000006833} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 16493 / NCIMB 14021 / DFL 12 RC {ECO:0000313|Proteomes:UP000006833}; RX PubMed=19741735; DOI=10.1038/ismej.2009.94; RA Wagner-Dobler I., Ballhausen B., Berger M., Brinkhoff T., Buchholz I., RA Bunk B., Cypionka H., Daniel R., Drepper T., Gerdts G., Hahnke S., RA Han C., Jahn D., Kalhoefer D., Kiss H., Klenk H.P., Kyrpides N., RA Liebl W., Liesegang H., Meincke L., Pati A., Petersen J., RA Piekarski T., Pommerenke C., Pradella S., Pukall R., Rabus R., RA Stackebrandt E., Thole S., Thompson L., Tielen P., Tomasch J., RA von Jan M., Wanphrut N., Wichels A., Zech H., Simon M.; RT "The complete genome sequence of the algal symbiont Dinoroseobacter RT shibae: a hitchhiker's guide to life in the sea."; RL ISME J. 4:61-77(2010). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000830; ABV93308.1; -; Genomic_DNA. DR ProteinModelPortal; A8LKU4; -. DR STRING; 398580.Dshi_1566; -. DR EnsemblBacteria; ABV93308; ABV93308; Dshi_1566. DR KEGG; dsh:Dshi_1566; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000006833; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000006833}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000006833}. FT DOMAIN 192 361 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 415 AA; 45482 MW; 51107F507AB4E620 CRC64; MLHPELTADR GRRLAGPALE EAVALAAALP RLDVAGADIV RLSKVQPGLL FGSGKIEELR ARIEADEIGL VLIDGPVSPV QQRNLERAWK TKILDSTGLI LEIFADRART REGVLQVELA ALAYQRTRLV RSWTHLERQR GGLGFVGGPG ETQIEADRRA IDEAVTRIKR QLAKVVKTRE LHRAARKKVP YPIVALVGYT NAGKSTLFNH LTGAEVLAKD MLFATLDPTM RALKLPDGLE VILSDTVGFI SSLPTELVAA FRATLEEVLD ADLILHVRDI AHPDSAAQAE DVHKILEALG VKDERPMIEV WNKLDLLPEA EAEALRTSAA RQDDVLAISA LSGEGFDTLQ AAISARLTPA LLDEVVVVPF AQGRVRAWLF EQGVVLDESQ DEDGYHLSLR WSPVQKARFE ALLHA // ID A8MA57_CALMQ Unreviewed; 409 AA. AC A8MA57; DT 04-DEC-2007, integrated into UniProtKB/TrEMBL. DT 04-DEC-2007, sequence version 1. DT 07-JUN-2017, entry version 64. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Cmaq_0139 {ECO:0000313|EMBL:ABW00989.1}; OS Caldivirga maquilingensis (strain ATCC 700844 / DSM 13496 / JCM 10307 OS / IC-167). OC Archaea; Crenarchaeota; Thermoprotei; Thermoproteales; OC Thermoproteaceae; Caldivirga. OX NCBI_TaxID=397948 {ECO:0000313|EMBL:ABW00989.1, ECO:0000313|Proteomes:UP000001137}; RN [1] {ECO:0000313|EMBL:ABW00989.1, ECO:0000313|Proteomes:UP000001137} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700844 / DSM 13496 / JCM 10307 / IC-167 RC {ECO:0000313|Proteomes:UP000001137}; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., RA Dalin E., Tice H., Pitluck S., Saunders E., Brettin T., Bruce D., RA Detter J.C., Han C., Schmutz J., Larimer F., Land M., Hauser L., RA Kyrpides N., Ivanova N., Biddle J.F., Zhang Z., Fitz-Gibbon S.T., RA Lowe T.M., Saltikov C., House C.H., Richardson P.; RT "Complete sequence of Caldivirga maquilingensis IC-167."; RL Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000852; ABW00989.1; -; Genomic_DNA. DR RefSeq; WP_012185209.1; NC_009954.1. DR ProteinModelPortal; A8MA57; -. DR STRING; 397948.Cmaq_0139; -. DR EnsemblBacteria; ABW00989; ABW00989; Cmaq_0139. DR GeneID; 5709996; -. DR KEGG; cma:Cmaq_0139; -. DR eggNOG; arCOG00353; Archaea. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG093Z07D6; -. DR Proteomes; UP000001137; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000001137}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000001137}. FT DOMAIN 187 356 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 409 AA; 46123 MW; 8143C5FBE0F7966D CRC64; MGKEALLVYV DPNPMESKVN EFRMLAEVAG YEVKGLVVQR RIPDSRYYVG IGKLMDVKRL IEDGVNYLIT YHQLKPNQSF NLSRELRVNV MDRVKLILEI FDKRAGDAEA KLQIKLAELK YSLPLIREYI RLSKKGEQIG FHGLGEYGAE TYYKHALRQI ASVKRRLNAI KSMRDTHIIK RKDKGIPEVA LTGYTMAGKT TLFNRLTGEG KYIDGKAFAT LSTYSRLVNF NGKYAVITDT VGFIDDLPPV LVESFYSTIR EIAYADLILL IIDSSDSAEE VRRKVSSSIS ILNDIAVPMS KVIPVFNKID EVKDTDSLLN VALEFKLSNP LFISAKAGIG LESLKSRIAS ELRDYTTVRL AVGDLDTVNQ LLRHRASIMF INNDSALVNV RREDLALLDE KGISYRIEG // ID A8MG05_ALKOO Unreviewed; 416 AA. AC A8MG05; DT 04-DEC-2007, integrated into UniProtKB/TrEMBL. DT 04-DEC-2007, sequence version 1. DT 07-JUN-2017, entry version 62. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Clos_0996 {ECO:0000313|EMBL:ABW18543.1}; OS Alkaliphilus oremlandii (strain OhILAs) (Clostridium oremlandii OS (strain OhILAs)). OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Alkaliphilus. OX NCBI_TaxID=350688 {ECO:0000313|EMBL:ABW18543.1, ECO:0000313|Proteomes:UP000000269}; RN [1] {ECO:0000313|Proteomes:UP000000269} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=OhILAs {ECO:0000313|Proteomes:UP000000269}; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., RA Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., RA Stolz J.F., Dawson A., Fisher E., Crable B., Perera E., Lisak J., RA Ranganathan M., Basu P., Richardson P.; RT "Complete genome of Alkaliphilus oremlandii OhILAs."; RL Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000853; ABW18543.1; -; Genomic_DNA. DR ProteinModelPortal; A8MG05; -. DR STRING; 350688.Clos_0996; -. DR EnsemblBacteria; ABW18543; ABW18543; Clos_0996. DR KEGG; aoe:Clos_0996; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; FNNHAHV; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000000269; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000000269}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000000269}. FT DOMAIN 195 361 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 154 188 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 416 AA; 47253 MW; 6A9C63155B1016E4 CRC64; MNQKGIVVGL NLNNRNNFEE SMVELENLSL ACDIHIVGRI TQNARKVNSA YYIGNGKIEE LIELISEKNA EIVIFNHELS GSQLRNIEEK VQCRVADRTA LILDIFAQRA KTREAKLQVE VAWLQYELPR LVGSNENLGR QSGGVGTKNR GAGEKKIELD RRKIEERIAA LNKELEILKG QRTTQRKERK ESNIPNVALV GYTNAGKSSI MNAMMDQSQH KDNKKVFEKD MLFATLETSV RHIKVSGNKS FLLSDTVGFV SDLPHNLVKA FRSTLEEVCE ADLLIHVVDI SNPHYEAQID VTKETLKQIG ADHIPVIYAY NKIDLVDETL EHKEGIYISA KKNRGIEKLI NLICDEVFTD RIQCTMLIPY DDVKAVPYFN QNANVLDTAY VNEGTVLNME CTQMDFYKYK KYVITQ // ID A8MHP4_ALKOO Unreviewed; 429 AA. AC A8MHP4; DT 04-DEC-2007, integrated into UniProtKB/TrEMBL. DT 04-DEC-2007, sequence version 1. DT 07-JUN-2017, entry version 63. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Clos_1786 {ECO:0000313|EMBL:ABW19326.1}; OS Alkaliphilus oremlandii (strain OhILAs) (Clostridium oremlandii OS (strain OhILAs)). OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Alkaliphilus. OX NCBI_TaxID=350688 {ECO:0000313|EMBL:ABW19326.1, ECO:0000313|Proteomes:UP000000269}; RN [1] {ECO:0000313|Proteomes:UP000000269} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=OhILAs {ECO:0000313|Proteomes:UP000000269}; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., RA Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., RA Stolz J.F., Dawson A., Fisher E., Crable B., Perera E., Lisak J., RA Ranganathan M., Basu P., Richardson P.; RT "Complete genome of Alkaliphilus oremlandii OhILAs."; RL Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000853; ABW19326.1; -; Genomic_DNA. DR RefSeq; WP_012159638.1; NC_009922.1. DR ProteinModelPortal; A8MHP4; -. DR STRING; 350688.Clos_1786; -. DR EnsemblBacteria; ABW19326; ABW19326; Clos_1786. DR KEGG; aoe:Clos_1786; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000000269; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000000269}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000000269}. FT DOMAIN 205 375 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 164 198 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 429 AA; 48263 MW; 32AEA07E9BBAD0CD CRC64; MEIENIEDKE ITKAILVGLN NTGKREKIDI EVSMEELEEL AKAAGAQVLA TAIQSRPAVD VTYFIGKGKV EEIKELCENL EANMVIFNDE LSGSQIRNLE EEIGVDVIDR TALILDIFAQ RASTKEGKLQ VELAQLKYRM PRLIGLGRQL SQQGAGIGTR GPGEKKLETD RRHILKRIDD IESELKEVRK NREVQRGKRS KSEIPIVALV GYTNAGKSTL MNTLLKLSDH HDDTKEVYVE DMLFATLDVS LRRLSFPDKL DFILTDTVGF VSKLPHALVN AFKATLEEVK YADLLIHVID ASNEEYNLQK DTTLGVLNDL GVENKNIITV YNKIDKISDE ALLPKEENCI HISAVTHKNI DVLIEKIRAE IGPDIIEVDL LIPYDKGNLL SSLHKEGIVL STEYVEGGTQ VNARLENMYY HKYEPYKLN // ID A8PN68_9COXI Unreviewed; 366 AA. AC A8PN68; DT 15-JAN-2008, integrated into UniProtKB/TrEMBL. DT 15-JAN-2008, sequence version 1. DT 07-JUN-2017, entry version 55. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:EDP46280.1}; GN ORFNames=RICGR_0917 {ECO:0000313|EMBL:EDP46280.1}; OS Rickettsiella grylli. OC Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales; OC Coxiellaceae; Rickettsiella. OX NCBI_TaxID=59196 {ECO:0000313|EMBL:EDP46280.1, ECO:0000313|Proteomes:UP000054075}; RN [1] {ECO:0000313|EMBL:EDP46280.1, ECO:0000313|Proteomes:UP000054075} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Seshadri R., Federici B.A.; RL Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:EDP46280.1, ECO:0000313|Proteomes:UP000054075} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Myers G.S.; RL Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EDP46280.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AAQJ02000001; EDP46280.1; -; Genomic_DNA. DR RefSeq; WP_006035263.1; NZ_AAQJ02000001.1. DR ProteinModelPortal; A8PN68; -. DR STRING; 59196.RICGR_0917; -. DR EnsemblBacteria; EDP46280; EDP46280; RICGR_0917. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000054075; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000054075}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000054075}. FT DOMAIN 198 364 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 164 191 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 366 AA; 41567 MW; C061B88DA16BCD19 CRC64; MFERPQRGEL ALLVHIYFKK YENEEIIKEF RELALAAGAH PTALITGRQY QPQAKYFIGV GKLEEIRTAG LAHQSQLILF NHDLSPAQER NLEQKLHCRV LGRTGLILDI FAQRARTFEG QLQVKLAQLE HLSTRLIRGW THLERQRGGI GLRGPGETQL ETDKRLIRQQ IKTIKKRLEK VRRQRAQSQR ARKKSKAPYI SLVGYTNTGK STLFNRLTQS NVLIANQPFA TLDPSIRRMS LNGKIAILAD TVGFIRHLPH HLIAAFRATL EETQHADLLL HVVDAANTEK KECTHAVDHV LKRIHTVPIT QLIVVNKIDR LNDSSPRLER SATGLPTKVW ISAQFALGID LLKSAVIECL AYQTNQ // ID A8T8N7_9VIBR Unreviewed; 429 AA. AC A8T8N7; DT 15-JAN-2008, integrated into UniProtKB/TrEMBL. DT 15-JAN-2008, sequence version 1. DT 30-AUG-2017, entry version 56. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=AND4_12664 {ECO:0000313|EMBL:EDP58275.1}; OS Vibrio sp. AND4. OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; OC Vibrionaceae; Vibrio. OX NCBI_TaxID=314289 {ECO:0000313|EMBL:EDP58275.1, ECO:0000313|Proteomes:UP000005159}; RN [1] {ECO:0000313|EMBL:EDP58275.1, ECO:0000313|Proteomes:UP000005159} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=AND4 {ECO:0000313|EMBL:EDP58275.1, RC ECO:0000313|Proteomes:UP000005159}; RX PubMed=20436956; DOI=10.1371/journal.pbio.1000358; RA Gomez-Consarnau L., Akram N., Lindell K., Pedersen A., Neutze R., RA Milton D.L., Gonzalez J.M., Pinhassi J.; RT "Proteorhodopsin phototrophy promotes survival of marine bacteria RT during starvation."; RL PLoS Biol. 8:E1000358-E1000358(2010). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EDP58275.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABGR01000012; EDP58275.1; -; Genomic_DNA. DR RefSeq; WP_009843400.1; NZ_ABGR01000012.1. DR ProteinModelPortal; A8T8N7; -. DR EnsemblBacteria; EDP58275; EDP58275; AND4_12664. DR Proteomes; UP000005159; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000005159}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000005159}. FT DOMAIN 198 365 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 429 AA; 48810 MW; 1BBD81C44CD55F3A CRC64; MFDRYETGER AVLVHINFTQ EGEWEDLAEF EMLVSSAGVE ALQVVTGSRQ SPHPKYYVGE GKAQEIATAV QLTGAEIVIF NHSLSPAQER NLEALCKCRV LDRTGLILDI FAQRARTHEG KLQVELAQLR HISTRLIRGW THLERQKGGI GLRGPGETQL ETDRRLLRER IKTILRRLEK VAKQREQGRR ARNRAEIPTV SLVGYTNAGK STLFNRITQA GVYAADQLFA TLDPTLRKIE LADVGPAILA DTVGFIRHLP HDLVAAFKAT LKETQEADIL LHVVDASDER FRENIQAVHE VLEEIDADEV PTLVVMNKID NLEEQKPRIE RDEEGVPRAV WVSAMDGLGI ELLFDALTER LASQMVEYQL RIPPQYQGRL RSTFFDMKCI QREEYDQEGD LLIDIRMQQV DWSRLEKREG AVLVDFIVT // ID A8TUN8_9PROT Unreviewed; 437 AA. AC A8TUN8; DT 15-JAN-2008, integrated into UniProtKB/TrEMBL. DT 15-JAN-2008, sequence version 1. DT 07-JUN-2017, entry version 51. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=BAL199_25827 {ECO:0000313|EMBL:EDP63616.1}; OS alpha proteobacterium BAL199. OC Bacteria; Proteobacteria; Alphaproteobacteria. OX NCBI_TaxID=331869 {ECO:0000313|EMBL:EDP63616.1, ECO:0000313|Proteomes:UP000003417}; RN [1] {ECO:0000313|EMBL:EDP63616.1, ECO:0000313|Proteomes:UP000003417} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BAL199 {ECO:0000313|EMBL:EDP63616.1, RC ECO:0000313|Proteomes:UP000003417}; RA Hagstrom A., Ferriera S., Johnson J., Kravitz S., Beeson K., RA Sutton G., Rogers Y.-H., Friedman R., Frazier M., Venter J.C.; RL Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EDP63616.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABHC01000012; EDP63616.1; -; Genomic_DNA. DR RefSeq; WP_007675127.1; NZ_ABHC01000012.1. DR ProteinModelPortal; A8TUN8; -. DR STRING; 331869.BAL199_25827; -. DR EnsemblBacteria; EDP63616; EDP63616; BAL199_25827. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000003417; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000003417}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000003417}. FT DOMAIN 202 377 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 437 AA; 47827 MW; 40A0E004AC4BB38B CRC64; MGTRALVVHP RLKTKEDASA DSVRDPEARL EEAVGLTSAI DLLSVHAEVV TVNKPRPGSL LGGGQIERIA QLVEALEIEV VVVDRPLTPV QQRNLEKELD AKVIDRTQLI LEIFGARART HEGRLHVDLA SLTFQRSRLV RSWTHLERQR GGGGFMGGPG ERQLEIDRRL IDDKIIRIRR ELEEVKRTRE LHRGARRRVP YPIVALVGYT NAGKSTLFNR LSGASVVAED LLFATLDPTM RRIEVPGGRT IILSDTVGFI SDLPTHLVAA FRATLEEVTE ADVVVHVRDI AHPDSNAQKS DVEGVLASLG IDETTRSGRM LEVLNKIDRL PDDQRIAVKQ RAASGNEPVA AVSAITGEGI DELRSVIAQL LGVNDQVCAF TLDLSDGAAI AWLYAHGEVV ERTDAPEGTT AVSVRLASAD ADRFEKRFGS AIRRPAS // ID A8USN5_9AQUI Unreviewed; 379 AA. AC A8USN5; DT 15-JAN-2008, integrated into UniProtKB/TrEMBL. DT 15-JAN-2008, sequence version 1. DT 07-JUN-2017, entry version 53. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=HG1285_18374 {ECO:0000313|EMBL:EDP76163.1}; OS Hydrogenivirga sp. 128-5-R1-1. OC Bacteria; Aquificae; Aquificales; Aquificaceae; Hydrogenivirga. OX NCBI_TaxID=392423 {ECO:0000313|EMBL:EDP76163.1, ECO:0000313|Proteomes:UP000005981}; RN [1] {ECO:0000313|EMBL:EDP76163.1, ECO:0000313|Proteomes:UP000005981} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=128-5-R1-1 {ECO:0000313|EMBL:EDP76163.1, RC ECO:0000313|Proteomes:UP000005981}; RA Reysenbach A.-L., Ferriera S., Johnson J., Kravitz S., Beeson K., RA Sutton G., Rogers Y.-H., Friedman R., Frazier M., Venter J.C.; RL Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EDP76163.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABHJ01000002; EDP76163.1; -; Genomic_DNA. DR RefSeq; WP_008286373.1; NZ_ABHJ01000002.1. DR ProteinModelPortal; A8USN5; -. DR EnsemblBacteria; EDP76163; EDP76163; HG1285_18374. DR PATRIC; fig|392423.7.peg.3281; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000005981; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000005981}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000005981}. FT DOMAIN 197 367 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 11 35 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 379 AA; 42843 MW; D3C6CF6A1A42CA0C CRC64; MRAVLVGIWN RDTTKEEAKE SLKELKRLVE AVGGKSIGYV LQNRNRPDVR YFIGEGKARE LREVLKGTGA DTVVFDDSLT PSQVRNLEKL TGRKVLDRTD LVIEIFSRRA KSKEAKLQVE LARLTHELPR LQGRGKSMSR LGGGVGTRGP GEQETEIRRR LIKKRIYQVR EELEEVKKMR RHQRKRRERS DSGESILKVA LVGYTNAGKS TLLRVLTGRE SFSADMLFAT LDTKTSSRFL SSDLKVLFTD TVGFIKKLPT ELIESFKATL EEVTEADLIL HVVDVSDDRW LDYIHTVRDI LKELSADGKP VIYVLNKADR IVDSEEEMRH LPHGAFVEGA SVVVSAERRW GIDELINKIR LFGERMLAVG SGAEGSTQT // ID A8XVG8_CAEBR Unreviewed; 1390 AA. AC A8XVG8; DT 15-JAN-2008, integrated into UniProtKB/TrEMBL. DT 16-DEC-2008, sequence version 2. DT 07-JUN-2017, entry version 59. DE SubName: Full=Protein CBG19372 {ECO:0000313|EMBL:CAP36636.2}; GN ORFNames=CBG19372 {ECO:0000313|EMBL:CAP36636.2, GN ECO:0000313|WormBase:CBG19372}, GN CBG_19372 {ECO:0000313|EMBL:CAP36636.2}; OS Caenorhabditis briggsae. OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida; OC Rhabditoidea; Rhabditidae; Peloderinae; Caenorhabditis. OX NCBI_TaxID=6238 {ECO:0000313|EMBL:CAP36636.2, ECO:0000313|Proteomes:UP000008549}; RN [1] {ECO:0000313|EMBL:CAP36636.2, ECO:0000313|Proteomes:UP000008549} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=AF16 {ECO:0000313|EMBL:CAP36636.2, RC ECO:0000313|Proteomes:UP000008549}; RX PubMed=14624247; DOI=10.1371/journal.pbio.0000045; RA Stein L.D., Bao Z., Blasiar D., Blumenthal T., Brent M.R., Chen N., RA Chinwalla A., Clarke L., Clee C., Coghlan A., Coulson A., RA D'Eustachio P., Fitch D.H., Fulton L.A., Fulton R.E., RA Griffiths-Jones S., Harris T.W., Hillier L.W., Kamath R., RA Kuwabara P.E., Mardis E.R., Marra M.A., Miner T.L., Minx P., RA Mullikin J.C., Plumb R.W., Rogers J., Schein J.E., Sohrmann M., RA Spieth J., Stajich J.E., Wei C., Willey D., Wilson R.K., Durbin R., RA Waterston R.H.; RT "The genome sequence of Caenorhabditis briggsae: a platform for RT comparative genomics."; RL PLoS Biol. 1:166-192(2003). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; HE601047; CAP36636.2; -; Genomic_DNA. DR ProteinModelPortal; A8XVG8; -. DR STRING; 6238.CBG19372; -. DR EnsemblMetazoa; CBG19372; CBG19372; WBGene00038607. DR WormBase; CBG19372; CBP36066; WBGene00038607; -. DR eggNOG; KOG0410; Eukaryota. DR eggNOG; COG2262; LUCA. DR InParanoid; A8XVG8; -. DR OrthoDB; EOG091G0852; -. DR Proteomes; UP000008549; Chromosome V. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR CDD; cd01878; HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR006594; LisH. DR InterPro; IPR027417; P-loop_NTPase. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF08513; LisH; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SMART; SM00667; LisH; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR PROSITE; PS51705; G_HFLX; 1. DR PROSITE; PS50896; LISH; 1. PE 4: Predicted; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000008549}; KW Reference proteome {ECO:0000313|Proteomes:UP000008549}. FT DOMAIN 39 71 LisH. {ECO:0000259|PROSITE:PS50896}. FT DOMAIN 1162 1329 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 535 572 {ECO:0000256|SAM:Coils}. FT COILED 1114 1149 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 1390 AA; 157858 MW; F250E04B4DC84C7A CRC64; MQTDEQSGTT GGRRGNRHAA AQARSQQQQN QQVEENQVFG ERLHSLIYGY LLRNGFNSAA AALQQDSEHL QNSVTRPDTD RPQQVIVLND RMHDRNLEEI VQMFNRDGSF GLHDRLMDFG GDLNRLNNRF QTLVNYFGST NTSRLHQQLY GRQSYSRLQQ PQNYSLGPAP QAVSQMRLQQ VNQIAEERYR QEQQMRERSV SIASNSQSQL QKMPTPVQEQ GQLQDQNMLQ GAPEHTEPME HSQEADGEVH RSRRKLNHPQ NYNVRLGNSV NAIADYINDP NYQLDDFVNL NYGFLNAMDY NPPPFALTRM EQDDQQMLEE IFNEELIDND MFMESGVVRE EIVETEEIPI ENRAAQYATP PEELLSPVPR ASYMVSHQSV SSQPSTSEAS VARSSRKDDY YIPSKGVNLS TSKSEVKIHK ERDRSQTSDT GYHRERSETS TIINTSELVP DREKNREEVH RHKVRDHMKV DGIESVKKRK RKIRVEKQER DRHRDERSDL HDRPSSSFSS SHHRDHRSKV QDERESTPGS RTTERDDDKD KKRKERKERE KAEEREKEKQ RTKDKKEKED RDRSKHLGQS SSSYASAEQH PQHVLNTMRT SHAAGVMKQS EHLDSSAAGG GAKRKADQTI TSETKPLPFK IPKKNTTSSS SDLRQAGGGS RDSSRTSSPK GDRLKVVTCG IFWTECGKLQ KSPPTTNNKI SDGGEDRPVA THFIAPIGHL ARCKFSRISS ILINCDRSYH MYQLDHPSKE NKVRSTSQSP ANSTHSSGPI TPSSVTLVPH PKGKMYAPIK GDRTETRKES DKNSTSSSTT VESSDDDTSR ASSSSSNNSR QKKPVDGLLA EKLLARVHKQ KYYTILRCSY RFPSLCACNH FLFLLVAFVI DLINYSGVVE ISQISPKMFT VFKFLSCYSY PNLCFSGQTV NEILRLFRMI FRRITRLISF RSFSIGRPDV ATTSSKFAND RWSVLVVHPK VRWGSGSASV LKQADRQLEE AVALVNNLPN MIAVDSLIMP VDYNTKRKSI WAAGNLEKLV TRREAARATA LMINVDVLSP SQQEELFRIF EVPIFDRYNI VLSTFKEFAQ TDEAQLQIAL AEIPYIKNRI HALSSKRLHS RPEILHIEQQ YAEVEGDLNE ILRKREQDLR RDLKELTRKS SESIKSKNSS DAVVAVVGYT NAGKTSLVKR LTGASSLTPK NQLFATLDTT RHVAKLPSGR SAVFTDTIGF LSDLPMHLIS AFEATLAHVK SADVIIHLRD VSNPDWKAQE EDVVATLKSI GVAENVLTER MITVDNKIDK EGVENIADAT TKSIRISCKT GDGMQDLIDR INQKVTIATK CKTIRFRLDV RSPVIEWLYH NEFVVVEPVA DGNNLIFDVV MSESEIGRFR KKFDHLRKKV // ID A8YX92_LACH4 Unreviewed; 421 AA. AC A8YX92; DT 15-JAN-2008, integrated into UniProtKB/TrEMBL. DT 15-JAN-2008, sequence version 1. DT 07-JUN-2017, entry version 66. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=lhv_1808 {ECO:0000313|EMBL:ABX27672.1}; OS Lactobacillus helveticus (strain DPC 4571). OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; OC Lactobacillus. OX NCBI_TaxID=405566 {ECO:0000313|EMBL:ABX27672.1, ECO:0000313|Proteomes:UP000000790}; RN [1] {ECO:0000313|EMBL:ABX27672.1, ECO:0000313|Proteomes:UP000000790} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DPC 4571 {ECO:0000313|EMBL:ABX27672.1, RC ECO:0000313|Proteomes:UP000000790}; RX PubMed=17993529; DOI=10.1128/JB.01295-07; RA Callanan M., Kaleta P., O'Callaghan J., O'Sullivan O., Jordan K., RA McAuliffe O., Sangrador-Vegas A., Slattery L., Fitzgerald G.F., RA Beresford T., Ross R.P.; RT "Genome sequence of Lactobacillus helveticus: an organism RT distinguished by selective gene loss and IS element expansion."; RL J. Bacteriol. 190:727-735(2008). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000517; ABX27672.1; -; Genomic_DNA. DR RefSeq; WP_012212251.1; NC_010080.1. DR ProteinModelPortal; A8YX92; -. DR STRING; 405566.lhv_1808; -. DR EnsemblBacteria; ABX27672; ABX27672; lhv_1808. DR KEGG; lhe:lhv_1808; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR Proteomes; UP000000790; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000000790}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000000790}. FT DOMAIN 199 368 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 421 AA; 47192 MW; 78CF1469DAD87FD0 CRC64; MIDNQPKKIK AYIAGVNLND PNFDYYMTEL ANLTEANNME VVGQSYQNAE SIVAGTYFGL GKINEIKAMA HGLKAKVLVL NDELTPVQIR NLEKLTKLRV IDRTELILEI FASRARTKQA KLQVQLARLQ YELPRLHPSE NNLDQQRGGG YSNRGAGESK LELNRRTIGK QISAIKKELK AVASQEEIKS ARRNQSRIPK VALVGYTNAG KSTTMNGLLK EFSAEGTNKE VFVKNMLFAT LDTSVRRIDL KDNFSFILSD TVGFISKLPH NLVESFKATL QETKDADLLI NVVDASDPNM VQMIRTTQNV LDEIGVKGIP MITAYNKADK TDRNYPQIEG DDILYSAIDP KSIKMLADLI TKRVFSNYEE FSLLLPLSAG KELAYLHENA QVLSEDYEDD GVHLKANIAP DDQGRFKQYL V // ID A8ZRP8_DESOH Unreviewed; 565 AA. AC A8ZRP8; DT 15-JAN-2008, integrated into UniProtKB/TrEMBL. DT 15-JAN-2008, sequence version 1. DT 07-JUN-2017, entry version 59. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Dole_0005 {ECO:0000313|EMBL:ABW65815.1}; OS Desulfococcus oleovorans (strain DSM 6200 / Hxd3). OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfobacterales; OC Desulfobacteraceae; Desulfococcus. OX NCBI_TaxID=96561 {ECO:0000313|EMBL:ABW65815.1, ECO:0000313|Proteomes:UP000008561}; RN [1] {ECO:0000313|EMBL:ABW65815.1, ECO:0000313|Proteomes:UP000008561} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 6200 / Hxd3 {ECO:0000313|Proteomes:UP000008561}; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., RA Dalin E., Tice H., Pitluck S., Kiss H., Brettin T., Bruce D., RA Detter J.C., Han C., Schmutz J., Larimer F., Land M., Hauser L., RA Kyrpides N., Kim E., Wawrik B., Richardson P.; RT "Complete sequence of Desulfococcus oleovorans Hxd3."; RL Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000859; ABW65815.1; -; Genomic_DNA. DR RefSeq; WP_012173434.1; NC_009943.1. DR ProteinModelPortal; A8ZRP8; -. DR STRING; 96561.Dole_0005; -. DR EnsemblBacteria; ABW65815; ABW65815; Dole_0005. DR KEGG; dol:Dole_0005; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; EREVIIT; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000008561; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000008561}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000008561}. FT DOMAIN 386 550 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 345 379 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 565 AA; 61446 MW; 9D5A7EEB3B52813B CRC64; MKKRPHGNTG GLKADHLRRL DNLYRRRVPS SFLVTPELAR ELCLLSREIR RQIGLLIDRQ GVVAHVIVGT DSAIVIPDIS EYRTAAGRLR GLKCVHTHLG PDPLTADDIT DLSLLRLDIM AAVADTGGPE ENPRYRVYGA HLLPGNGEGG PSGPSCKVLD PLGHADLDIG CDGLIASLED ELAQAGALRE AGQKSDRAIL VSVTGAPRAA AGASLTELSA LAASADIAVV DTVLQFRKKT DARFLLGRGK LGELAVLALQ TGANLLVFDQ ELNPSQIRSI TDQVDIKVID RTQLILDIFA QRAQSMEGKL QVAHAQLKYL LPRLVTKNTA MSRLTGGIGG RGPGETKLEI NRRRVRDQLA RLEKQLESIK KQRRQQKARR DKRALPVISI LGYTNAGKST LLNTLSKSGV ATADRLFMTL DPASRRIRFP REMDVILTDT VGFIQNLPKE LMVAFRATLE ELERADLFIH VVDAANPAAE AQIRSVERIV TELGLSLTPM VYAVNKADRA TPEQVEALVR ATGGVPVSAN NAATLGPLID RLADRVGQIV KHNRRLSENP VISDY // ID A9B3J2_HERA2 Unreviewed; 444 AA. AC A9B3J2; DT 15-JAN-2008, integrated into UniProtKB/TrEMBL. DT 15-JAN-2008, sequence version 1. DT 07-JUN-2017, entry version 70. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Haur_2926 {ECO:0000313|EMBL:ABX05564.1}; OS Herpetosiphon aurantiacus (strain ATCC 23779 / DSM 785). OC Bacteria; Chloroflexi; Chloroflexia; Herpetosiphonales; OC Herpetosiphonaceae; Herpetosiphon. OX NCBI_TaxID=316274 {ECO:0000313|EMBL:ABX05564.1, ECO:0000313|Proteomes:UP000000787}; RN [1] {ECO:0000313|Proteomes:UP000000787} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 23779 / DSM 785 {ECO:0000313|Proteomes:UP000000787}; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., RA Dalin E., Tice H., Pitluck S., Kiss H., Brettin T., Bruce D., RA Detter J.C., Han C., Schmutz J., Larimer F., Land M., Hauser L., RA Kyrpides N., Kim E., Bryant D.A., Richardson P.; RT "Complete sequence of chromosome of Herpetosiphon aurantiacus ATCC RT 23779."; RL Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000875; ABX05564.1; -; Genomic_DNA. DR ProteinModelPortal; A9B3J2; -. DR STRING; 316274.Haur_2926; -. DR EnsemblBacteria; ABX05564; ABX05564; Haur_2926. DR KEGG; hau:Haur_2926; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR BioCyc; HAUR316274:GHYA-2957-MONOMER; -. DR Proteomes; UP000000787; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000000787}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000000787}. FT DOMAIN 218 390 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 444 AA; 49599 MW; AB414D8924C1CBC4 CRC64; MSNSVRERMH VTAKPKERAL LVGGDIYNNR EAWHIDDSLD ELALLADTAG LEVVGTVSQK LDHPNPKTYI GPGKVREVAD LRSETPYDVV IFDEELSPSQ ARNLEEAIKV KVIDRTTLIL DIFAQHARTR EGSLQVELAQ YDYLLPRLRR AWTHLERQSG GGGGGSGVGV GLRGPGETQL ESDQRIIGKR IALLKEQLAD VHRHRELYRQ NRQESGLPII SVVGYTNAGK STLLNRLAQA DVLAADMLFA TLDPTTRKVA LPGGRAVLMT DTVGFIQRLP TALVAAFRAT LEEIAEADVL LHVLDLTHAN VEEQFKTVID TLSELKVQDK PILTVFNKID KIDSPSDAEI VRMITELGLP IDRWVAISAQ QNIGIDRLQT AIEQMLMERM VKFEVMIPYR ANELVALWHE RGMIESEEFG AEGTTLRGAV PRQFAHRFEP YRVK // ID A9BMU7_DELAS Unreviewed; 404 AA. AC A9BMU7; DT 15-JAN-2008, integrated into UniProtKB/TrEMBL. DT 15-JAN-2008, sequence version 1. DT 07-JUN-2017, entry version 70. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Daci_5013 {ECO:0000313|EMBL:ABX37642.1}; OS Delftia acidovorans (strain DSM 14801 / SPH-1). OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Comamonadaceae; Delftia. OX NCBI_TaxID=398578 {ECO:0000313|EMBL:ABX37642.1, ECO:0000313|Proteomes:UP000000784}; RN [1] {ECO:0000313|Proteomes:UP000000784} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 14801 / SPH-1 {ECO:0000313|Proteomes:UP000000784}; RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., RA Dalin E., Tice H., Pitluck S., Lowry S., Clum A., Schmutz J., RA Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Schleheck D., RA Richardson P.; RT "Complete sequence of Delftia acidovorans DSM 14801 / SPH-1."; RL Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000884; ABX37642.1; -; Genomic_DNA. DR RefSeq; WP_012206812.1; NC_010002.1. DR ProteinModelPortal; A9BMU7; -. DR STRING; 398578.Daci_5013; -. DR EnsemblBacteria; ABX37642; ABX37642; Daci_5013. DR GeneID; 24115011; -. DR KEGG; dac:Daci_5013; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR Proteomes; UP000000784; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000000784}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000000784}. FT DOMAIN 202 375 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 168 195 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 404 AA; 45065 MW; 6B03D35FD5ADE330 CRC64; MSSESFDRST PTPVLLVGVD FGFPHFDGEL EELGLLAGTA GLRPVARLTC KRKVPDAALF VGSGKADEIR MLAQMHGAQE VLFDQALSPA QQRNLERHLQ MPVNDRTLLI LEIFAQRARS HEGKLQVELA RLQYVATRLV RRWTHLERQM GGIGGRGGPG EKQIELDRRM IDESIKRTKE RLQKVKKQRA TQRRRRERHG IFNISLVGYT NAGKSTLFNA LVKARAYAAD QLFATLDTTT RQLYLNEAQQ SVSLSDTVGF IRDLPHGLVD AFQATLQEAI DADLLLHVVD ASNPNFPEQI QQVQKVLKEI GAQEVPLVLV FNKLDAVDPE RLPAQLQDQY ELDGLPVSRV FVSARSGEGL PQLRQLLAEH ALRAEAEHAE AHGGDERDQE EVDGAMPPGQ DAEY // ID A9D8V8_HOEPD Unreviewed; 479 AA. AC A9D8V8; DT 05-FEB-2008, integrated into UniProtKB/TrEMBL. DT 26-NOV-2014, sequence version 2. DT 07-JUN-2017, entry version 45. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=HPDFL43_07624 {ECO:0000313|EMBL:EDQ32800.2}; OS Hoeflea phototrophica (strain DSM 17068 / NCIMB 14078 / DFL-43). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Phyllobacteriaceae; Hoeflea. OX NCBI_TaxID=411684 {ECO:0000313|EMBL:EDQ32800.2, ECO:0000313|Proteomes:UP000004291}; RN [1] {ECO:0000313|EMBL:EDQ32800.2, ECO:0000313|Proteomes:UP000004291} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DFL-43 {ECO:0000313|EMBL:EDQ32800.2, RC ECO:0000313|Proteomes:UP000004291}; RA Wagner-Dobler I., Ferriera S., Johnson J., Kravitz S., Beeson K., RA Sutton G., Rogers Y.-H., Friedman R., Frazier M., Venter J.C.; RL Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:EDQ32800.2, ECO:0000313|Proteomes:UP000004291} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DFL-43 {ECO:0000313|EMBL:EDQ32800.2, RC ECO:0000313|Proteomes:UP000004291}; RA Fiebig A.; RL Submitted (JUN-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EDQ32800.2}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABIA03000002; EDQ32800.2; -; Genomic_DNA. DR STRING; 411684.HPDFL43_07624; -. DR EnsemblBacteria; EDQ32800; EDQ32800; HPDFL43_07624. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000004291; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000004291}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000004291}. FT DOMAIN 239 410 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 198 232 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 479 AA; 52663 MW; A60719D066EF6135 CRC64; MKTQAATPDW TTHIETVGNS GNFADADSKS DVTSAIVLVP ALRTRNAAPG SGPDGSNITK RPDALRMEEA VGLAGAIDLQ VAEALIVPIS APRPSTLFGK GKMLEVKGVI ETTGSGLVIV DHPLTPVQQR NMETEWKVKV IDRTGLILEI FGRRASTREG VLQVELAHLN YQKGRLVRSW THLERQRGGG GFMGGPGETQ IEADRRLLQD RIVKLERELE QVRRTRQLHR AKRKKVPHPI VALVGYTNAG KSTLFNRVTG AEVLAEDMLF ATLDPTLRRM KLPHGNTVIL SDTVGFISSL PTHLVAAFRA TLEEVVEADL ILHVRDMADP DRASQAGDVE EILKSLGLNE GDGRKLVEVW NKIDLLSEEA AEDLKTRAEK SENAIAVSSV TGEGIDELLM RIETIISGKL VSRNVTLGPD QMKLVPWIYE RGRVSEREDM EDGSVMIEVE FTTADSEELD RRMGNGPKPS DSWEDDLDD // ID A9DNJ9_9FLAO Unreviewed; 413 AA. AC A9DNJ9; DT 05-FEB-2008, integrated into UniProtKB/TrEMBL. DT 05-FEB-2008, sequence version 1. DT 07-JUN-2017, entry version 53. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=KAOT1_18647 {ECO:0000313|EMBL:EDP97210.1}; OS Kordia algicida OT-1. OC Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales; OC Flavobacteriaceae; Kordia. OX NCBI_TaxID=391587 {ECO:0000313|EMBL:EDP97210.1, ECO:0000313|Proteomes:UP000002945}; RN [1] {ECO:0000313|EMBL:EDP97210.1, ECO:0000313|Proteomes:UP000002945} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=OT-1 {ECO:0000313|EMBL:EDP97210.1, RC ECO:0000313|Proteomes:UP000002945}; RX PubMed=21622754; DOI=10.1128/JB.05241-11; RA Lee H.S., Kang S.G., Kwon K.K., Lee J.H., Kim S.J.; RT "Genome sequence of the algicidal bacterium Kordia algicida OT-1."; RL J. Bacteriol. 193:4031-4032(2011). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EDP97210.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABIB01000002; EDP97210.1; -; Genomic_DNA. DR ProteinModelPortal; A9DNJ9; -. DR STRING; 391587.KAOT1_18647; -. DR EnsemblBacteria; EDP97210; EDP97210; KAOT1_18647. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000002945; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000002945}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000002945}. FT DOMAIN 210 395 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 413 AA; 47337 MW; B6CDCF7D81D4EDC4 CRC64; MCNFVFLILF MLEKKTIAYE RAVLIGVITK DQDEAKSKEY LDELEFLTYT AGGEVVKRFT QKIDVPNPKT FIGTGKMDEV EQFVKSNDIG SVIFDDELSP SQQKNIERLL KCKIIDRTGL ILDIFAQRAK TSYARTQVEL AQYQYLLPRL TGLWTHLERQ RGGIGMRGPG ETEIETDRRI VRDKIALLRK KMVTIDKQMA VQRGNRGALI RVALVGYTNV GKSTLMNVIS KSEVFAENKL FATLDTTVRK VVIGNLPFLL SDTVGFIRKL PTQLVDSFKS TLDEVREADL LLHVVDISHP NFEDHIASVN QILSEIKSGD KPTVMVFNKI DAYTHETIDS DDLVTEKTKA HYTLDDWKKT WMNSSAEDVL FISALNKENL DEFKRKVYTV VREIHVTRFP YNNFLYPDYE DLQ // ID A9E430_9RHOB Unreviewed; 432 AA. AC A9E430; DT 05-FEB-2008, integrated into UniProtKB/TrEMBL. DT 05-FEB-2008, sequence version 1. DT 07-JUN-2017, entry version 46. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=OIHEL45_12580 {ECO:0000313|EMBL:EDQ04535.1}; OS Oceanibulbus indolifex HEL-45. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae; Oceanibulbus. OX NCBI_TaxID=391624 {ECO:0000313|EMBL:EDQ04535.1, ECO:0000313|Proteomes:UP000003257}; RN [1] {ECO:0000313|EMBL:EDQ04535.1, ECO:0000313|Proteomes:UP000003257} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=HEL-45 {ECO:0000313|EMBL:EDQ04535.1, RC ECO:0000313|Proteomes:UP000003257}; RA Wagner-Dobler I., Ferriera S., Johnson J., Kravitz S., Beeson K., RA Sutton G., Rogers Y.-H., Friedman R., Frazier M., Venter J.C.; RL Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EDQ04535.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABID01000003; EDQ04535.1; -; Genomic_DNA. DR RefSeq; WP_007119531.1; NZ_ABID01000003.1. DR ProteinModelPortal; A9E430; -. DR STRING; 391624.OIHEL45_12580; -. DR EnsemblBacteria; EDQ04535; EDQ04535; OIHEL45_12580. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000003257; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000003257}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000003257}. FT DOMAIN 212 381 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 432 AA; 47826 MW; A261623DAD4829B5 CRC64; MSRPTFQIDN SDGPRVTRAW VLHPDIKTDN DRRAPEPALA EAVALAEALP ELEVVGAEVV PLRTVHAGML FGKGKIEELE QRMKAAEVEL VLVDGPVTPV QQRNLEKAWG VKLLDRTGLI LEIFSDRAAT REGVLQVEMA ALNYQRTRLV RAWTHLERQR GGLGFVGGPG ETQIEADRRA IDDQLVRLRR QLEKVVKTRA LHRAARAKVP FPIVALVGYT NAGKSTLFNR LTGAEVMAKD MLFATLDPTM RSLVLPDGPE IILSDTVGFI SDLPTELVAS FRATLEEVLA ADIICHVRDV SHAETEEQAQ NVRDILASLG VPKETRSFEV WNKLDLLPED RADAMRARAA RNDDLLAISA ITGEGLEALQ ETIAEALQGA VREAVLTLGF SDGKKRAWLF AQDVVEGERQ TEDGFEITVR WSARQEAEFQ QN // ID A9FVS2_SORC5 Unreviewed; 446 AA. AC A9FVS2; DT 05-FEB-2008, integrated into UniProtKB/TrEMBL. DT 05-FEB-2008, sequence version 1. DT 07-JUN-2017, entry version 67. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Synonyms=hflX2 {ECO:0000313|EMBL:CAN92306.1}; GN OrderedLocusNames=sce2147 {ECO:0000313|EMBL:CAN92306.1}; OS Sorangium cellulosum (strain So ce56) (Polyangium cellulosum (strain OS So ce56)). OC Bacteria; Proteobacteria; Deltaproteobacteria; Myxococcales; OC Sorangiineae; Polyangiaceae; Sorangium. OX NCBI_TaxID=448385 {ECO:0000313|EMBL:CAN92306.1, ECO:0000313|Proteomes:UP000002139}; RN [1] {ECO:0000313|EMBL:CAN92306.1, ECO:0000313|Proteomes:UP000002139} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=So ce56 {ECO:0000313|Proteomes:UP000002139}; RX PubMed=17965706; DOI=10.1038/nbt1354; RA Schneiker S., Perlova O., Kaiser O., Gerth K., Alici A., RA Altmeyer M.O., Bartels D., Bekel T., Beyer S., Bode E., Bode H.B., RA Bolten C.J., Choudhuri J.V., Doss S., Elnakady Y.A., Frank B., RA Gaigalat L., Goesmann A., Groeger C., Gross F., Jelsbak L., RA Jelsbak L., Kalinowski J., Kegler C., Knauber T., Konietzny S., RA Kopp M., Krause L., Krug D., Linke B., Mahmud T., Martinez-Arias R., RA McHardy A.C., Merai M., Meyer F., Mormann S., Munoz-Dorado J., RA Perez J., Pradella S., Rachid S., Raddatz G., Rosenau F., Rueckert C., RA Sasse F., Scharfe M., Schuster S.C., Suen G., Treuner-Lange A., RA Velicer G.J., Vorholter F.-J., Weissman K.J., Welch R.D., Wenzel S.C., RA Whitworth D.E., Wilhelm S., Wittmann C., Bloecker H., Puehler A., RA Mueller R.; RT "Complete genome sequence of the myxobacterium Sorangium cellulosum."; RL Nat. Biotechnol. 25:1281-1289(2007). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AM746676; CAN92306.1; -; Genomic_DNA. DR RefSeq; WP_012234781.1; NC_010162.1. DR ProteinModelPortal; A9FVS2; -. DR STRING; 448385.sce2147; -. DR EnsemblBacteria; CAN92306; CAN92306; sce2147. DR KEGG; scl:sce2147; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; FNNHAHV; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000002139; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000002139}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000002139}. FT DOMAIN 226 391 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 194 221 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 446 AA; 48796 MW; E247E51E48BE81A1 CRC64; MPASKRSTRA CRNSPVHKAI VIAVQLPEAA EADVHRSLAE LKQLLLGLDI TAVAEVVQKR SVRSSPTYLG EGKLRELAAL TGGTGEVPRG PEARRADRAA SEPAERLVVV ADDELSPGQL RNLQAALGVD VLDRTAVILR VFESRARTRE ARLEIELARI EYELPRIRDD HTLGDREGGG GRASRGHTNV ELAKQRARDR MAAVRRELEQ LKESAEQRRL ARADSFRVAL VGYTNAGKSS FMRQLTGSDV LVEDRPFATL GTTVRQLSPP ATPAVLVADT VGFIHRLPHA LVASFHSTLS EAREAWLLLH VVDAADPAFR SQIRVTEQVL ADIGAAETPA LLLLNKADRL DREERDALAR EHPGALLMSA LDHRDGDALR ARIEAFFAQH LVEQTVSIPY DRHGVLAELR DRLQVVREEY GDEVSVTVRG TPETLGKLAA RLSGGG // ID A9GIX2_SORC5 Unreviewed; 476 AA. AC A9GIX2; DT 05-FEB-2008, integrated into UniProtKB/TrEMBL. DT 05-FEB-2008, sequence version 1. DT 07-JUN-2017, entry version 64. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=sce3166 {ECO:0000313|EMBL:CAN93325.1}; OS Sorangium cellulosum (strain So ce56) (Polyangium cellulosum (strain OS So ce56)). OC Bacteria; Proteobacteria; Deltaproteobacteria; Myxococcales; OC Sorangiineae; Polyangiaceae; Sorangium. OX NCBI_TaxID=448385 {ECO:0000313|EMBL:CAN93325.1, ECO:0000313|Proteomes:UP000002139}; RN [1] {ECO:0000313|EMBL:CAN93325.1, ECO:0000313|Proteomes:UP000002139} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=So ce56 {ECO:0000313|Proteomes:UP000002139}; RX PubMed=17965706; DOI=10.1038/nbt1354; RA Schneiker S., Perlova O., Kaiser O., Gerth K., Alici A., RA Altmeyer M.O., Bartels D., Bekel T., Beyer S., Bode E., Bode H.B., RA Bolten C.J., Choudhuri J.V., Doss S., Elnakady Y.A., Frank B., RA Gaigalat L., Goesmann A., Groeger C., Gross F., Jelsbak L., RA Jelsbak L., Kalinowski J., Kegler C., Knauber T., Konietzny S., RA Kopp M., Krause L., Krug D., Linke B., Mahmud T., Martinez-Arias R., RA McHardy A.C., Merai M., Meyer F., Mormann S., Munoz-Dorado J., RA Perez J., Pradella S., Rachid S., Raddatz G., Rosenau F., Rueckert C., RA Sasse F., Scharfe M., Schuster S.C., Suen G., Treuner-Lange A., RA Velicer G.J., Vorholter F.-J., Weissman K.J., Welch R.D., Wenzel S.C., RA Whitworth D.E., Wilhelm S., Wittmann C., Bloecker H., Puehler A., RA Mueller R.; RT "Complete genome sequence of the myxobacterium Sorangium cellulosum."; RL Nat. Biotechnol. 25:1281-1289(2007). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AM746676; CAN93325.1; -; Genomic_DNA. DR RefSeq; WP_012235797.1; NC_010162.1. DR ProteinModelPortal; A9GIX2; -. DR STRING; 448385.sce3166; -. DR EnsemblBacteria; CAN93325; CAN93325; sce3166. DR KEGG; scl:sce3166; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; VILEIFH; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000002139; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 2. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000002139}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000002139}. FT DOMAIN 257 422 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 218 245 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 476 AA; 51042 MW; D1A47A152F16AF5C CRC64; MTTTNQERPL AVLVGVQLPG VDDVEHAADL AELGRLVHTL GFDVIATVSQ RRSALAAAAV LGEGKLRELA ELTGGSGVVP SGAPERKNKA RARRAAESGE GDEDDVELGG DDGDGAGDDG GAEPRAGGAG QAARLATVVA VDHDISPSQA RNLERATGAQ VLDRAGVIIE IFHRHARSRE AKLEVEIARL NYVAPRLRET GGGGDRQRGG IGGKGAGESA LELDRRKIRD RIAELKEELA AVQREQSTRR ALRQGQRRVA LVGYTNAGKS SLMRALTGSE VLVADKLFAT LDTTVRALHP EVRPRILVSD TVGFIKKLPH DLVASFRSTL DEALEASLLL YVADASDPTF RDQLAVTRGV LSEIGASEVP SRLLLNKVDR LSEEERDALR LEFPEATQLS AKIPDDVAAL REAIIAFFEQ SMVEAELLLP YAKQGLIGEI YENARVLSEE YDDVGGRLSV RAHAAALDRL RSLLAR // ID A9GR64_SORC5 Unreviewed; 622 AA. AC A9GR64; DT 05-FEB-2008, integrated into UniProtKB/TrEMBL. DT 05-FEB-2008, sequence version 1. DT 07-JUN-2017, entry version 73. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Synonyms=hflX1 {ECO:0000313|EMBL:CAN90547.1}; GN OrderedLocusNames=sce0390 {ECO:0000313|EMBL:CAN90547.1}; OS Sorangium cellulosum (strain So ce56) (Polyangium cellulosum (strain OS So ce56)). OC Bacteria; Proteobacteria; Deltaproteobacteria; Myxococcales; OC Sorangiineae; Polyangiaceae; Sorangium. OX NCBI_TaxID=448385 {ECO:0000313|EMBL:CAN90547.1, ECO:0000313|Proteomes:UP000002139}; RN [1] {ECO:0000313|EMBL:CAN90547.1, ECO:0000313|Proteomes:UP000002139} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=So ce56 {ECO:0000313|Proteomes:UP000002139}; RX PubMed=17965706; DOI=10.1038/nbt1354; RA Schneiker S., Perlova O., Kaiser O., Gerth K., Alici A., RA Altmeyer M.O., Bartels D., Bekel T., Beyer S., Bode E., Bode H.B., RA Bolten C.J., Choudhuri J.V., Doss S., Elnakady Y.A., Frank B., RA Gaigalat L., Goesmann A., Groeger C., Gross F., Jelsbak L., RA Jelsbak L., Kalinowski J., Kegler C., Knauber T., Konietzny S., RA Kopp M., Krause L., Krug D., Linke B., Mahmud T., Martinez-Arias R., RA McHardy A.C., Merai M., Meyer F., Mormann S., Munoz-Dorado J., RA Perez J., Pradella S., Rachid S., Raddatz G., Rosenau F., Rueckert C., RA Sasse F., Scharfe M., Schuster S.C., Suen G., Treuner-Lange A., RA Velicer G.J., Vorholter F.-J., Weissman K.J., Welch R.D., Wenzel S.C., RA Whitworth D.E., Wilhelm S., Wittmann C., Bloecker H., Puehler A., RA Mueller R.; RT "Complete genome sequence of the myxobacterium Sorangium cellulosum."; RL Nat. Biotechnol. 25:1281-1289(2007). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AM746676; CAN90547.1; -; Genomic_DNA. DR RefSeq; WP_012233025.1; NC_010162.1. DR ProteinModelPortal; A9GR64; -. DR STRING; 448385.sce0390; -. DR EnsemblBacteria; CAN90547; CAN90547; sce0390. DR KEGG; scl:sce0390; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; EREVIIT; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000002139; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000002139}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000002139}. FT DOMAIN 402 567 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 368 395 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 622 AA; 67986 MW; 46A412DFA12D858E CRC64; MPTLYGNTTG LSPQATKTLE RIYRRKVPLA SIATPELIKA LAEASHETGR QVGALVHRSG EIDYVIVGDA TRLMLPDIGR LRAAQGRFRA LRLVHTHLFN EPLTRDDLVD LVRLRLDLVA AVQLTPQGEP RTLQYAYNVP VHGKEAVTVT VDEAEGRGGS RGEAALPYRT VGPVAIGRAD VDFGALIQAL EDEFTKRSRT RSVAAKDGRA ILVHVAEKSK AGALARAEES LRELTELAGT AGVDVADTVL QLRDRLDPRL VLGKGKLDEV VLRASELDAE TLVFDRDLTP SQASAIAKHT DLKVLDRTQL ILDIFAQRAE SSDGKLQVEL AQLKYTLPRL GQKDDSLSRL TGGIGGRGPG ETKLEIGRRR AKERVSFLEA QLKRLSRQRE QRRRRRARLG VPVVSIVGYT NAGKSTLLNT LTGADVLAEN KLFATLDTRS RRLRFPEERE VVITDTVGFI RELPKDLFAA FRATFEEAAD ADLLLHVVDA SDPARDQHIE TTEALLTELD LIGIPRIVVF NKADLIAPAE GRRLLLGHPD AVVLSATDRE TTRELLAKLA ERLKSRWEEA AMVPAYEAEA AEDELGDGGL FEGEAESMTV LGPPSSSGAG EISARLRGTF EA // ID A9HLR8_GLUDA Unreviewed; 428 AA. AC A9HLR8; DT 05-FEB-2008, integrated into UniProtKB/TrEMBL. DT 05-FEB-2008, sequence version 1. DT 05-JUL-2017, entry version 69. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:CAP56204.1}; GN OrderedLocusNames=GDI2261 {ECO:0000313|EMBL:CAP56204.1}; OS Gluconacetobacter diazotrophicus (strain ATCC 49037 / DSM 5601 / OS PAl5). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales; OC Acetobacteraceae; Gluconacetobacter. OX NCBI_TaxID=272568 {ECO:0000313|EMBL:CAP56204.1, ECO:0000313|Proteomes:UP000001176}; RN [1] {ECO:0000313|EMBL:CAP56204.1, ECO:0000313|Proteomes:UP000001176} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 49037 / DSM 5601 / PAl5 RC {ECO:0000313|Proteomes:UP000001176}; RX PubMed=19775431; DOI=10.1186/1471-2164-10-450; RA Bertalan M., Albano R., Padua V., Rouws L., Rojas C., Hemerly A., RA Teixeira K., Schwab S., Araujo J., Oliveira A., Franca L., RA Magalhaes V., Alqueres S., Cardoso A., Almeida W., Loureiro M.M., RA Nogueira E., Cidade D., Oliveira D., Simao T., Macedo J., Valadao A., RA Dreschsel M., Freitas F., Vidal M., Guedes H., Rodrigues E., RA Meneses C., Brioso P., Pozzer L., Figueiredo D., Montano H., RA Junior J., Filho G., Flores V., Ferreira B., Branco A., Gonzalez P., RA Guillobel H., Lemos M., Seibel L., Macedo J., Alves-Ferreira M., RA Sachetto-Martins G., Coelho A., Santos E., Amaral G., Neves A., RA Pacheco A.B., Carvalho D., Lery L., Bisch P., Rossle S.C., Urmenyi T., RA Kruger W.V., Martins O., Baldani J.I., Ferreira P.C.; RT "Complete genome sequence of the sugarcane nitrogen-fixing endophyte RT Gluconacetobacter diazotrophicus Pal5."; RL BMC Genomics 10:450-450(2009). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AM889285; CAP56204.1; -; Genomic_DNA. DR ProteinModelPortal; A9HLR8; -. DR EnsemblBacteria; CAP56204; CAP56204; GDI2261. DR KEGG; gdi:GDI2261; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR KO; K03665; -. DR OMA; HPATYIG; -. DR Proteomes; UP000001176; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000001176}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000001176}. FT DOMAIN 202 371 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 428 AA; 47138 MW; 729D4DF01F18C30A CRC64; MSQSATRAAV ILPWERPDRQ EEVRAAEARL EEAVGLAASI GLVIVRQAVL VLRARRPSTL LGNGQVESLR AAVQQDRVAV VIVDSRLSPV QQRNLERALG CKVIDRTALI LDIFGERAAT KEGTLQVELA HLEYQRSRLV RTWTHLERQR GGFGFLGGPG ETQIEADRRM IGDRIVRLKR ELEQVRRTRG LHRAARRRVP FPVVALVGYT NAGKSTLFNA LTGATVFAQD QLFATLDPTM RGIRLPSGRR IILSDTVGFI SDLPTELIAA FRATLEEVAE ADVILHVRDI SHPDSAAQRA DVEDVLEGMA GSGTLEDDWR RRVIEVQNKA DLIGGRDAVP PRKGSVVISA ITGEGLPDLL AAIDSRLTEA METVRYTIPV KDGAMLAWLY AHGEVTSRED GEQAIVVTVR LLPADRARFE MQIAGQDQ // ID A9IK71_BORPD Unreviewed; 368 AA. AC A9IK71; DT 05-FEB-2008, integrated into UniProtKB/TrEMBL. DT 05-FEB-2008, sequence version 1. DT 07-JUN-2017, entry version 66. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:CAP42366.1}; GN OrderedLocusNames=Bpet2026 {ECO:0000313|EMBL:CAP42366.1}; OS Bordetella petrii (strain ATCC BAA-461 / DSM 12804 / CCUG 43448). OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Alcaligenaceae; Bordetella. OX NCBI_TaxID=340100 {ECO:0000313|Proteomes:UP000001225}; RN [1] {ECO:0000313|EMBL:CAP42366.1, ECO:0000313|Proteomes:UP000001225} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-461 / DSM 12804 / CCUG 43448 RC {ECO:0000313|Proteomes:UP000001225}; RX PubMed=18826580; DOI=10.1186/1471-2164-9-449; RA Gross R., Guzman C.A., Sebaihia M., Martins Dos Santos V.A., RA Pieper D.H., Koebnik R., Lechner M., Bartels D., Buhrmester J., RA Choudhuri J.V., Ebensen T., Gaigalat L., Herrmann S., Khachane A.N., RA Larisch C., Link S., Linke B., Meyer F., Mormann S., Nakunst D., RA Rueckert C., Schneiker-Bekel S., Schulze K., Vorhoelter F.J., RA Yevsa T., Engle J.T., Goldman W.E., Puehler A., Goebel U.B., RA Goesmann A., Bloecker H., Kaiser O., Martinez-Arias R.; RT "The missing link: Bordetella petrii is endowed with both the RT metabolic versatility of environmental bacteria and virulence traits RT of pathogenic Bordetellae."; RL BMC Genomics 9:449-449(2008). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AM902716; CAP42366.1; -; Genomic_DNA. DR ProteinModelPortal; A9IK71; -. DR STRING; 340100.Bpet2026; -. DR EnsemblBacteria; CAP42366; CAP42366; Bpet2026. DR KEGG; bpt:Bpet2026; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000001225; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000001225}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000001225}. FT DOMAIN 190 354 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 368 AA; 40137 MW; 8641F26A93E14D68 CRC64; MRALIISVDL GSPDFLAHAE EFAMLARGAG AEIVGTVTVR RDRPDAKFFI GSGKVQEAVA MAGALLADLV LFDQPLSPAQ QRNLEREFNL RVVDRVALIL DIFALRAKSH EGKLQVELAQ LQHLVTRLTR LWTHLERQRG GIGMRGPGES QLEMDRRMIG AKVKVLRERL DRVERQRVTQ RRARARGGAL SVSLVGYTNA GKSTLFNALT RAGAYAADQL FATLDTTTRR IWIEGTGSVV LSDTVGFIRD LPPNLIAAFR ATLEETIHAD LLLHVVDAAS PQRDEQIAEV NKVLAEIGAG SIPTILVHNK IDRAGLAPRI ERNAHGTIAR VFVSATERAG LDALRGAIAE IGQIVGNNAS NHQTLQSE // ID A9KI87_LACP7 Unreviewed; 420 AA. AC A9KI87; DT 05-FEB-2008, integrated into UniProtKB/TrEMBL. DT 05-FEB-2008, sequence version 1. DT 07-JUN-2017, entry version 75. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Cphy_0534 {ECO:0000313|EMBL:ABX40921.1}; OS Lachnoclostridium phytofermentans (strain ATCC 700394 / DSM 18823 / OS ISDg) (Clostridium phytofermentans). OC Bacteria; Firmicutes; Clostridia; Clostridiales; Lachnospiraceae. OX NCBI_TaxID=357809 {ECO:0000313|EMBL:ABX40921.1, ECO:0000313|Proteomes:UP000000370}; RN [1] {ECO:0000313|Proteomes:UP000000370} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700394 / DSM 18823 / ISDg RC {ECO:0000313|Proteomes:UP000000370}; RA Leschine S.B., Warnick T.A., Blanchard J.L., Schnell D.J., Petit E.L., RA LaTouf W.G., Copeland A., Lucas S., Lapidus A., Barry K., RA Glavina del Rio T., Dalin E., Tice H., Pitluck S., Kiss H., RA Brettin T., Bruce D., Detter J.C., Han C., Kuske C., Schmutz J., RA Larimer F., Land M., Hauser L., Kyrpides N., Kim E.A., Richardson P.; RT "Complete genome sequence of Clostridium phytofermentans ISDg."; RL Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000885; ABX40921.1; -; Genomic_DNA. DR RefSeq; WP_012198565.1; NC_010001.1. DR ProteinModelPortal; A9KI87; -. DR STRING; 357809.Cphy_0534; -. DR EnsemblBacteria; ABX40921; ABX40921; Cphy_0534. DR KEGG; cpy:Cphy_0534; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000000370; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000000370}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000000370}. FT DOMAIN 202 366 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 161 195 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 420 AA; 47339 MW; D134E68C8AD67269 CRC64; MSELYEIKEE QEKVILVAVS ENDNDDTEES LDELMELVDT AGAVTVGRIT QNREKIHPGT YVGKGKIEEI RLLIEQLGAT GIICDDELSP AQLRNLEDAL QAKVMDRTMI ILDIFAQHAS TREGKIQVEL AQLKYRATRL IGMRNSLSRL GGGIGTRGPG EKKLEIDRRL IKDRIAQLNR ELDDIKRNRE VARSLRMKNP IPVVAIVGYT NAGKSTLLNR LTEADVLEAN MLFATLDPTT RNLSLESGQQ VLLTDTVGFI RKLPHHLIDA FRSTLEEAKY ADIIIHVVDA SNPQAYKQMH IVYETLKKLQ VTDKTVITVF NKQDLVQEEE PMKDLKADKT VKISAKQGVG VVELLDIIEE VLREAKVLIE HIFSYQEAGS IQLIRKYGQL LEEEYQEGGI FVKAYVPKDI ANQIVWSKQS // ID A9KMM6_LACP7 Unreviewed; 438 AA. AC A9KMM6; DT 05-FEB-2008, integrated into UniProtKB/TrEMBL. DT 05-FEB-2008, sequence version 1. DT 07-JUN-2017, entry version 64. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Cphy_1093 {ECO:0000313|EMBL:ABX41471.1}; OS Lachnoclostridium phytofermentans (strain ATCC 700394 / DSM 18823 / OS ISDg) (Clostridium phytofermentans). OC Bacteria; Firmicutes; Clostridia; Clostridiales; Lachnospiraceae. OX NCBI_TaxID=357809 {ECO:0000313|EMBL:ABX41471.1, ECO:0000313|Proteomes:UP000000370}; RN [1] {ECO:0000313|Proteomes:UP000000370} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700394 / DSM 18823 / ISDg RC {ECO:0000313|Proteomes:UP000000370}; RA Leschine S.B., Warnick T.A., Blanchard J.L., Schnell D.J., Petit E.L., RA LaTouf W.G., Copeland A., Lucas S., Lapidus A., Barry K., RA Glavina del Rio T., Dalin E., Tice H., Pitluck S., Kiss H., RA Brettin T., Bruce D., Detter J.C., Han C., Kuske C., Schmutz J., RA Larimer F., Land M., Hauser L., Kyrpides N., Kim E.A., Richardson P.; RT "Complete genome sequence of Clostridium phytofermentans ISDg."; RL Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000885; ABX41471.1; -; Genomic_DNA. DR ProteinModelPortal; A9KMM6; -. DR STRING; 357809.Cphy_1093; -. DR EnsemblBacteria; ABX41471; ABX41471; Cphy_1093. DR KEGG; cpy:Cphy_1093; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; FNNHAHV; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000000370; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000000370}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000000370}. FT DOMAIN 201 384 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 160 194 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 438 AA; 48875 MW; 82551F6BE2E647FA CRC64; MKQIGIIVGV NVKNEEHFHE GMQELIALSD ACDIEIVDSI VQNADSINRA TYLGKGKLAE LGELARVRGA EVVIFNGELT ASQIRNIQTV VDTVVLDRTN LILTIFASRA KTREAKLQVE VVRLQYELPR LIGANENLSR QAGGIGGGTG AGGRNKGAGE TKLELDKRRV EEKINVMQRE LEELITQRLT QRNQRKKNEI NTVALVGYTN AGKSTVMNYM VQQFIGKEEK EVLAKDMLFA TLETSVRKIN LKNRKEFLLS DTVGFVSNLP HKLVKAFRST LEEVCEADLL VHVVDRSNED YQSQIEVTNA TLSQIGAGHI PVIYAYNKAD LIKTDLIKEE ALQGDMEEKQ MLETKEDTVL ISAKKGDGMN ELIELICKRL YPNEVRTKVL IPYHLGALIA KINASTNILS SNSEEAGMVY EIECNEQIYQ QVEAFVLK // ID A9MFN9_SALAR Unreviewed; 426 AA. AC A9MFN9; DT 05-FEB-2008, integrated into UniProtKB/TrEMBL. DT 05-FEB-2008, sequence version 1. DT 30-AUG-2017, entry version 64. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=SARI_03269 {ECO:0000313|EMBL:ABX23105.1}; OS Salmonella arizonae (strain ATCC BAA-731 / CDC346-86 / RSK2980). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; OC Enterobacteriaceae; Salmonella. OX NCBI_TaxID=41514 {ECO:0000313|EMBL:ABX23105.1, ECO:0000313|Proteomes:UP000002084}; RN [1] {ECO:0000313|EMBL:ABX23105.1, ECO:0000313|Proteomes:UP000002084} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-731 / CDC346-86 / RSK2980 RC {ECO:0000313|Proteomes:UP000002084}; RG The Salmonella enterica serovar Arizonae Genome Sequencing Project; RA McClelland M., Sanderson E.K., Porwollik S., Spieth J., Clifton W.S., RA Fulton R., Chunyan W., Wollam A., Shah N., Pepin K., Bhonagiri V., RA Nash W., Johnson M., Thiruvilangam P., Wilson R.; RL Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000880; ABX23105.1; -; Genomic_DNA. DR RefSeq; WP_000460335.1; NC_010067.1. DR ProteinModelPortal; A9MFN9; -. DR STRING; 882884.SARI_03269; -. DR EnsemblBacteria; ABX23105; ABX23105; SARI_03269. DR KEGG; ses:SARI_03269; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000002084; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000002084}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000002084}. FT DOMAIN 198 365 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 164 191 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 426 AA; 48279 MW; 3FF3BEC49E2723B3 CRC64; MFDRYDAGEQ AVLVHIYFSQ DKDMEDLLEF ESLVSSAGVE AMQVITGSRK APHPKYFVGE GKAVEIAEAV KATGAAVVLF DHALSPAQER NLERLCECRV IDRTGLILDI FAQRARTHEG KLQVELAQLR HLATRLVRGW THLERQKGGI GLRGPGETQL ETDRRLLRNR IVQIQSRLEK VEKQREQGRQ SRIKADVPTV SLVGYTNAGK STLFNQITEA RVYAADQLFA TLDPTLRRID VADVGETVLA DTVGFIRHLP HDLVAAFKAT LQETRQATLL LHVVDAADVR VQENIEAVNT VLEEIDAHEI PTLMVMNKID MLDNFEPRID RDEENKPIRV WLSAQTGVGI PQLFQALTER LSGEVAQRTL RLPPQEGRLR SRFYQLQAIE KEWMEEDGSV SLQVRMPIVD WRRLCKQEPA LIEYVI // ID A9NE02_ACHLI Unreviewed; 416 AA. AC A9NE02; DT 05-FEB-2008, integrated into UniProtKB/TrEMBL. DT 05-FEB-2008, sequence version 1. DT 07-JUN-2017, entry version 68. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=ACL_1370 {ECO:0000313|EMBL:ABX81962.1}; OS Acholeplasma laidlawii (strain PG-8A). OC Bacteria; Tenericutes; Mollicutes; Acholeplasmatales; OC Acholeplasmataceae; Acholeplasma. OX NCBI_TaxID=441768 {ECO:0000313|EMBL:ABX81962.1, ECO:0000313|Proteomes:UP000008558}; RN [1] {ECO:0000313|EMBL:ABX81962.1, ECO:0000313|Proteomes:UP000008558} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=PG-8A {ECO:0000313|EMBL:ABX81962.1, RC ECO:0000313|Proteomes:UP000008558}; RX PubMed=21784942; DOI=10.1128/JB.05059-11; RA Lazarev V.N., Levitskii S.A., Basovskii Y.I., Chukin M.M., RA Akopian T.A., Vereshchagin V.V., Kostrjukova E.S., Kovaleva G.Y., RA Kazanov M.D., Malko D.B., Vitreschak A.G., Sernova N.V., Gelfand M.S., RA Demina I.A., Serebryakova M.V., Galyamina M.A., Vtyurin N.N., RA Rogov S.I., Alexeev D.G., Ladygina V.G., Govorun V.M.; RT "Complete genome and proteome of Acholeplasma laidlawii."; RL J. Bacteriol. 193:4943-4953(2011). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000896; ABX81962.1; -; Genomic_DNA. DR RefSeq; WP_012243293.1; NC_010163.1. DR ProteinModelPortal; A9NE02; -. DR STRING; 441768.ACL_1370; -. DR EnsemblBacteria; ABX81962; ABX81962; ACL_1370. DR KEGG; acl:ACL_1370; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000008558; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000008558}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000008558}. FT DOMAIN 197 362 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 416 AA; 47167 MW; 2ED6940A6A0FA1A6 CRC64; MQKLDRAILV ALNYQGNYES CKLSLDELEE LAKAVQIKTV DKVIQSNDKI EPKFFIGSGK VLEIKQMIDI LNVDMVIFDD TLSPAQIRNL EEALDVQIFD RAFLILQIFA LRAQTKQAML EVALAQKLYM LPRLAGMGKS LSRQGGGSFN AKGPGETKLE TDRRRLNMEI TRLRVSLEGI KKERGESRKR RFKNSIPVVA LVGYTNAGKS SLMNHLSNLY GTNKTEVFEK DMLFATLDTK SKRIQKDNQP PFILIDTVGF ISKLPPELIK SFESTLADIA SADLILHIVD GKNYSPLQIN FTKQVIKDLG LEETPRLLVV TKKDLLVHQP NILEDYLLIS NKTGEGMNDL YQAISAHIYK DSRIFKLLLP FDKGSIYERL KSDTTIIETN YTADGMFVKV VLTPYLYNLY KPYIMN // ID A9T136_PHYPA Unreviewed; 425 AA. AC A9T136; DT 05-FEB-2008, integrated into UniProtKB/TrEMBL. DT 05-FEB-2008, sequence version 1. DT 07-JUN-2017, entry version 62. DE SubName: Full=Predicted protein {ECO:0000313|EMBL:EDQ62844.1}; GN ORFNames=PHYPADRAFT_138684 {ECO:0000313|EMBL:EDQ62844.1}; OS Physcomitrella patens subsp. patens (Moss). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Bryophyta; OC Bryophytina; Bryopsida; Funariidae; Funariales; Funariaceae; OC Physcomitrella. OX NCBI_TaxID=3218 {ECO:0000313|Proteomes:UP000006727}; RN [1] {ECO:0000313|EMBL:EDQ62844.1, ECO:0000313|Proteomes:UP000006727} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Gransden 2004 {ECO:0000313|Proteomes:UP000006727}; RX PubMed=18079367; DOI=10.1126/science.1150646; RA Rensing S.A., Lang D., Zimmer A.D., Terry A., Salamov A., Shapiro H., RA Nishiyama T., Perroud P.-F., Lindquist E.A., Kamisugi Y., RA Tanahashi T., Sakakibara K., Fujita T., Oishi K., Shin-I T., RA Kuroki Y., Toyoda A., Suzuki Y., Hashimoto S.-I., Yamaguchi K., RA Sugano A., Kohara Y., Fujiyama A., Anterola A., Aoki S., Ashton N., RA Barbazuk W.B., Barker E., Bennetzen J.L., Blankenship R., Cho S.H., RA Dutcher S.K., Estelle M., Fawcett J.A., Gundlach H., Hanada K., RA Heyl A., Hicks K.A., Hughes J., Lohr M., Mayer K., Melkozernov A., RA Murata T., Nelson D.R., Pils B., Prigge M., Reiss B., Renner T., RA Rombauts S., Rushton P.J., Sanderfoot A., Schween G., Shiu S.-H., RA Stueber K., Theodoulou F.L., Tu H., Van de Peer Y., Verrier P.J., RA Waters E., Wood A., Yang L., Cove D., Cuming A.C., Hasebe M., RA Lucas S., Mishler B.D., Reski R., Grigoriev I.V., Quatrano R.S., RA Boore J.L.; RT "The Physcomitrella genome reveals evolutionary insights into the RT conquest of land by plants."; RL Science 319:64-69(2008). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; DS545038; EDQ62844.1; -; Genomic_DNA. DR RefSeq; XP_001772373.1; XM_001772321.1. DR UniGene; Ppa.7121; -. DR ProteinModelPortal; A9T136; -. DR STRING; 3218.PP1S149_31V6.1; -. DR GeneID; 5935614; -. DR KEGG; ppp:PHYPADRAFT_138684; -. DR eggNOG; KOG0410; Eukaryota. DR eggNOG; COG2262; LUCA. DR InParanoid; A9T136; -. DR KO; K03665; -. DR Proteomes; UP000006727; Partially assembled WGS sequence. DR GO; GO:0009507; C:chloroplast; IEA:EnsemblPlants. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR GO; GO:0043022; F:ribosome binding; IBA:GO_Central. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000006727}; KW Reference proteome {ECO:0000313|Proteomes:UP000006727}. FT DOMAIN 202 368 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 161 195 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 425 AA; 47193 MW; 20FFB92B53E2E6D0 CRC64; MQVFEERAYL VGIERKNTGA RSAFGISESL EELAQLADTA GLTVVGTTYQ KYVNPSPRTY VGSGKVSQVA TAVKALKVES VIFDDELSPG QLRNLEKAFG GDVRVCDRTA LILDIFSQRA ATREATLQVD LAQLEYQLPR LTRMWTHLER QAGGLVKGMG EKQIEVDKRI LRSQIAQLKK QLDTVRGHRQ QYRDRRASVP IPVISLVGYT NAGKSTLLNR LSGAGVLAED RLFATLDPTT RRVELPNGKE CLFTDTVGFI QKLPTQLVAA FRATLEEISD SSLLLHVMDI SHPMADQQRE AVDNVLADLD VGHIPYLCVW NKFDKAKDPK LLKLEAAKRG DVVCISALTG EGMEEFYEAV ESRLKDLMVR VEAVVPYGQG ELVNLIHRLG IVELEEYTDR GTLVKAHVPL ALSMQLMPLR QQPIA // ID A9UQC0_MONBE Unreviewed; 616 AA. AC A9UQC0; DT 05-FEB-2008, integrated into UniProtKB/TrEMBL. DT 05-FEB-2008, sequence version 1. DT 07-JUN-2017, entry version 37. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EDQ92569.1}; GN ORFNames=22354 {ECO:0000313|EMBL:EDQ92569.1}; OS Monosiga brevicollis (Choanoflagellate). OC Eukaryota; Choanoflagellida; Craspedida; Salpingoecidae; Monosiga. OX NCBI_TaxID=81824 {ECO:0000313|Proteomes:UP000001357}; RN [1] {ECO:0000313|EMBL:EDQ92569.1, ECO:0000313|Proteomes:UP000001357} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MX1 / ATCC 50154 {ECO:0000313|Proteomes:UP000001357}; RX PubMed=18273011; DOI=10.1038/nature06617; RG JGI Sequencing; RA King N., Westbrook M.J., Young S.L., Kuo A., Abedin M., Chapman J., RA Fairclough S., Hellsten U., Isogai Y., Letunic I., Marr M., Pincus D., RA Putnam N., Rokas A., Wright K.J., Zuzow R., Dirks W., Good M., RA Goodstein D., Lemons D., Li W., Lyons J.B., Morris A., Nichols S., RA Richter D.J., Salamov A., Bork P., Lim W.A., Manning G., Miller W.T., RA McGinnis W., Shapiro H., Tjian R., Grigoriev I.V., Rokhsar D.; RT "The genome of the choanoflagellate Monosiga brevicollis and the RT origin of metazoans."; RL Nature 451:783-788(2008). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CH991543; EDQ92569.1; -; Genomic_DNA. DR RefSeq; XP_001742331.1; XM_001742279.1. DR ProteinModelPortal; A9UQC0; -. DR STRING; 431895.XP_001742331.1; -. DR EnsemblProtists; EDQ92569; EDQ92569; MONBRDRAFT_22354. DR GeneID; 5887425; -. DR KEGG; mbr:MONBRDRAFT_22354; -. DR eggNOG; KOG0410; Eukaryota. DR eggNOG; COG2262; LUCA. DR InParanoid; A9UQC0; -. DR Proteomes; UP000001357; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR GO; GO:0043022; F:ribosome binding; IBA:GO_Central. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000001357}; KW Reference proteome {ECO:0000313|Proteomes:UP000001357}. FT DOMAIN 362 551 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 616 AA; 68496 MW; BD7AB636EFA17882 CRC64; MEPDLEWHDQ DLESEDDFTH HPDAVPQAAP PGLCAQTRRC GLASSIMRRP KVKKRGVYQF PKLTTSSCCA HKTLSLSLSL SLSLSLLLSR ALSLSLSLAL VLAVADQQRR GLRLSPGQAT ETLHMVADGE SDADADMPLP QLNLRKKIHR HAELGFNSED ATKVLVLQPD FKDARLQGVR PPQLQLEESL SLIDAVQGLT AVEGEVVRMR ELRERTFFGK GKLVEVSARV HELKQRGCDV VMINTSRLTP RQQEFLQKSW GLPVYDRFTV ILAIFESRAV SRQAQLQVEL ARIEYERARL VLGLEAGYDR QGGHSGTLGG AGETELEHNR RRLQRRELRI RELLRAADAS RPSIRKGTKD MPVVAVVGYT NAGKTALVKC LTHDAGLEPE NKLFATLDTT TRAGKLTDGT QCLFVDTVGF VADLPPTLVE AFRSTLVDLA AADVLVHVTD ATDPDRLDQH ACVIDVLEGL GLSTALLESR ICVHNKIDLR EFDDTAAHQD LDVHVAGSSR AKRERAAKLW RDHPALPISV HRGDNLEELL ERITQAVQRQ RGRVHRAVRF RIDQGDVLQY LHRHGAVQDH QVDADGLHQT VEVIMSADRL SQLVHTKKVQ VGRFAD // ID A9WDT2_CHLAA Unreviewed; 445 AA. AC A9WDT2; DT 05-FEB-2008, integrated into UniProtKB/TrEMBL. DT 05-FEB-2008, sequence version 1. DT 07-JUN-2017, entry version 75. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Caur_0438 {ECO:0000313|EMBL:ABY33688.1}; OS Chloroflexus aurantiacus (strain ATCC 29366 / DSM 635 / J-10-fl). OC Bacteria; Chloroflexi; Chloroflexia; Chloroflexales; Chloroflexineae; OC Chloroflexaceae; Chloroflexus. OX NCBI_TaxID=324602 {ECO:0000313|EMBL:ABY33688.1, ECO:0000313|Proteomes:UP000002008}; RN [1] {ECO:0000313|Proteomes:UP000002008} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29366 / DSM 635 / J-10-fl RC {ECO:0000313|Proteomes:UP000002008}; RX PubMed=21714912; DOI=10.1186/1471-2164-12-334; RA Tang K.H., Barry K., Chertkov O., Dalin E., Han C.S., Hauser L.J., RA Honchak B.M., Karbach L.E., Land M.L., Lapidus A., Larimer F.W., RA Mikhailova N., Pitluck S., Pierson B.K., Blankenship R.E.; RT "Complete genome sequence of the filamentous anoxygenic phototrophic RT bacterium Chloroflexus aurantiacus."; RL BMC Genomics 12:334-334(2011). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000909; ABY33688.1; -; Genomic_DNA. DR RefSeq; WP_012256344.1; NC_010175.1. DR RefSeq; YP_001634077.1; NC_010175.1. DR ProteinModelPortal; A9WDT2; -. DR STRING; 324602.Caur_0438; -. DR EnsemblBacteria; ABY33688; ABY33688; Caur_0438. DR GeneID; 5827711; -. DR KEGG; cau:Caur_0438; -. DR PATRIC; fig|324602.8.peg.497; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR InParanoid; A9WDT2; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000002008; Chromosome. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0043022; F:ribosome binding; IBA:GO_Central. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000002008}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000002008}. FT DOMAIN 218 389 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 445 AA; 49711 MW; 12E5B5F5114264FE CRC64; MRTHDGKRLY PTAVPRRRAL LVGAEIASMR SPWPVEDSLD ELALLAQTAE LEVVGRIFQR LPEPQPKFFI GPGKVKEVAA LREQTQADLI VFDDELSPAQ TRNLEEELQT QVIDRTGLIL DIFARHARTH EGRLQVELAQ YQYLLPRLRR QWTHLERQAG TGGTAAGGVV GLRGPGETQL EIDRRLIERR IAWLKDQLAD VHRHRELYRQ RRRQTGIPVI ALVGYTNAGK STLLNAMTGA DVLAEDKLFA TLDPTTRQVL LPGNIVALMT DTVGFIQKLP PQLVAAFRAT LEEIEEADLL LHVVDVTHRN AQEHAQTVEQ TLRELGVDHK PVLTVLNKID LLEGATAEDV GQIAAEMGLP TDIVAVSAQR GWGLQTLGER IVAMLAQRMV RVDAYIPYQR NDLVALWRQR GVIEVEEFEG DGAHIVGRLP PALAPQFARF ARSSL // ID A9WQ52_RENSM Unreviewed; 526 AA. AC A9WQ52; DT 05-FEB-2008, integrated into UniProtKB/TrEMBL. DT 05-FEB-2008, sequence version 1. DT 07-JUN-2017, entry version 74. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=RSal33209_0731 {ECO:0000313|EMBL:ABY22478.1}; OS Renibacterium salmoninarum (strain ATCC 33209 / DSM 20767 / JCM 11484 OS / NBRC 15589 / NCIMB 2235). OC Bacteria; Actinobacteria; Micrococcales; Micrococcaceae; OC Renibacterium. OX NCBI_TaxID=288705 {ECO:0000313|EMBL:ABY22478.1, ECO:0000313|Proteomes:UP000002007}; RN [1] {ECO:0000313|Proteomes:UP000002007} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33209 / DSM 20767 / JCM 11484 / NBRC 15589 / NCIMB 2235 RC {ECO:0000313|Proteomes:UP000002007}; RX PubMed=18723615; DOI=10.1128/JB.00721-08; RA Wiens G.D., Rockey D.D., Wu Z., Chang J., Levy R., Crane S., RA Chen D.S., Capri G.R., Burnett J.R., Sudheesh P.S., Schipma M.J., RA Burd H., Bhattacharyya A., Rhodes L.D., Kaul R., Strom M.S.; RT "Genome sequence of the fish pathogen Renibacterium salmoninarum RT suggests reductive evolution away from an environmental Arthrobacter RT ancestor."; RL J. Bacteriol. 190:6970-6982(2008). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000910; ABY22478.1; -; Genomic_DNA. DR RefSeq; WP_012244177.1; NC_010168.1. DR ProteinModelPortal; A9WQ52; -. DR STRING; 288705.RSal33209_0731; -. DR EnsemblBacteria; ABY22478; ABY22478; RSal33209_0731. DR KEGG; rsa:RSal33209_0731; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000002007; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 2. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000002007}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000002007}. FT DOMAIN 305 470 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 526 AA; 56815 MW; A4C09C2289E635AC CRC64; MTTQEESNQG IEKSDAAGQD MSPAEIQAVI DRILAKDTAK GGSPQDAHDG VLDGRAQALS SLSQEHSEYD GEQEDLQERR ALGRVAGLST ELDDVTEVEY RQLRLERVVL AGLWSEGTLA DAENSLRELA ALAETAGSEV LDGLVQRRSK PDPGTFLGSG KALALKDVVS ATGADTVVVD AELAPSQRRS LEDIVKVKVI DRTALILDIF AQHAKSREGK AQVELAQLEY LLPRLRGWGE SMSRQAGGQV GGAGAGMGSR GPGETKIELD RRRIRTRMAK LRREIAAMKP AREAKRANRR RSEVPSAAIA GYTNAGKSSI LNRLTHAGVL VQNALFATLD PTVRKAATPD GIGFTLADTV GFVRSLPTQL VEAFRSTLEE VADADLILHV VDVSHPDPEG QIAAVREVLS EVDARKIPEI IVLNKADAAD PLVIQRLTQR ETRSVLVSAR TGQGIDELLE LISQAIPRPG VELELMIPYD RGDLVSKLHQ TDAEILSQEH GEAGTWLKVK VREGLAAELK EFAHRG // ID B0C134_ACAM1 Unreviewed; 571 AA. AC B0C134; DT 26-FEB-2008, integrated into UniProtKB/TrEMBL. DT 26-FEB-2008, sequence version 1. DT 07-JUN-2017, entry version 64. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:ABW28432.1}; GN OrderedLocusNames=AM1_3438 {ECO:0000313|EMBL:ABW28432.1}; OS Acaryochloris marina (strain MBIC 11017). OC Bacteria; Cyanobacteria; Synechococcales; Acaryochloridaceae; OC Acaryochloris. OX NCBI_TaxID=329726 {ECO:0000313|EMBL:ABW28432.1, ECO:0000313|Proteomes:UP000000268}; RN [1] {ECO:0000313|EMBL:ABW28432.1, ECO:0000313|Proteomes:UP000000268} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MBIC 11017 {ECO:0000313|Proteomes:UP000000268}; RX PubMed=18252824; DOI=10.1073/pnas.0709772105; RA Swingley W.D., Chen M., Cheung P.C., Conrad A.L., Dejesa L.C., Hao J., RA Honchak B.M., Karbach L.E., Kurdoglu A., Lahiri S., Mastrian S.D., RA Miyashita H., Page L., Ramakrishna P., Satoh S., Sattley W.M., RA Shimada Y., Taylor H.L., Tomo T., Tsuchiya T., Wang Z.T., Raymond J., RA Mimuro M., Blankenship R.E., Touchman J.W.; RT "Niche adaptation and genome expansion in the chlorophyll d-producing RT cyanobacterium Acaryochloris marina."; RL Proc. Natl. Acad. Sci. U.S.A. 105:2005-2010(2008). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000828; ABW28432.1; -; Genomic_DNA. DR RefSeq; WP_012163831.1; NC_009925.1. DR ProteinModelPortal; B0C134; -. DR STRING; 329726.AM1_3438; -. DR EnsemblBacteria; ABW28432; ABW28432; AM1_3438. DR KEGG; amr:AM1_3438; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; EREVIIT; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000000268; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000000268}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000000268}. FT DOMAIN 397 571 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 356 390 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 571 AA; 62913 MW; BFF3EB71C3F2565F CRC64; MARQGRLIET IYGNLKGLKS NQIKQLRRLY HQRLPSDRIT TSDFAQRLAA ISTDIHQPIS TYLNRRGQVI RVGVGSPRQT QIPPLELPRY GADRLSGIRC VATTLKQEVP KESALTAMAL QRLDALAVLT MTGSGFERRG GGATGYVRST YLAHLVPDPT TPWTISSPLS LEQLAQQNLM DLVEALESEF GRSLNPRLSE TAETEQVLMV GVIPQAVSKA EMKANLAEVA LLVESAGGVV VETIHQKRSH PHPQTVVGAG KVKEIALRAQ TLGVTLIVFN LDLSPSQVRN LETQIGIRIV DRTEVILDIF AQRAQSQAGK LQVELAQLEY MLPRLAGRGQ AMSRLGGGIG TRGPGETKLE TERRAIQRRI NTLQQAVNQL QAHRSRLRQR RQHQRVPSVA VVGYTNAGKS TLLNVLTNAE AYTADQLFAT LDPTTRRLSI PDPETHQMRT LVLTDTVGFI HNLPPPLMDA FRATLEEVTD ADVLLHVVDL SHPDWENHLR SVMDLLGTMP ITPGPGLIAF NKMDQVSSEA LAIAQDQFPQ AVFISAQERL GLNTLRQKLL ELIDYAAMPT V // ID B0JHG9_MICAN Unreviewed; 547 AA. AC B0JHG9; DT 18-MAR-2008, integrated into UniProtKB/TrEMBL. DT 18-MAR-2008, sequence version 1. DT 05-JUL-2017, entry version 62. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=MAE_24990 {ECO:0000313|EMBL:BAG02321.1}; OS Microcystis aeruginosa (strain NIES-843). OC Bacteria; Cyanobacteria; Oscillatoriophycideae; Chroococcales; OC Microcystaceae; Microcystis. OX NCBI_TaxID=449447 {ECO:0000313|EMBL:BAG02321.1, ECO:0000313|Proteomes:UP000001510}; RN [1] {ECO:0000313|EMBL:BAG02321.1, ECO:0000313|Proteomes:UP000001510} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NIES-843 {ECO:0000313|EMBL:BAG02321.1, RC ECO:0000313|Proteomes:UP000001510}; RX PubMed=18192279; DOI=10.1093/dnares/dsm026; RA Kaneko T., Nakajima N., Okamoto S., Suzuki I., Tanabe Y., Tamaoki M., RA Nakamura Y., Kasai F., Watanabe A., Kawashima K., Kishida Y., Ono A., RA Shimizu Y., Takahashi C., Minami C., Fujishiro T., Kohara M., RA Katoh M., Nakazaki N., Nakayama S., Yamada M., Tabata S., RA Watanabe M.M.; RT "Complete genomic structure of the bloom-forming toxic cyanobacterium RT Microcystis aeruginosa NIES-843."; RL DNA Res. 14:247-256(2007). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AP009552; BAG02321.1; -; Genomic_DNA. DR ProteinModelPortal; B0JHG9; -. DR STRING; 449447.MAE_24990; -. DR PaxDb; B0JHG9; -. DR PRIDE; B0JHG9; -. DR EnsemblBacteria; BAG02321; BAG02321; MAE_24990. DR KEGG; mar:MAE_24990; -. DR PATRIC; fig|449447.4.peg.2285; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; EREVIIT; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000001510; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000001510}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000001510}. FT DOMAIN 380 547 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 339 376 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 547 AA; 60809 MW; 8D8B679AC99B1BD0 CRC64; MKQLQRLYHE RLPIDTLTTP EFAQRLAAIS TDIHQPLCTY INRRGQVIRV GVGTPRQTQF SLLELPRYGS ERLCGIRCIA TEIKQEPPKE SSLTAMALQR LDALVILTLT GTGMIRRGGG ATGYVEQVYL AHLIPQSQTN VNSNIYWSVS PPLNLEDLSK QDFLELVEGL EAEFQREFTA ITVDTAEDRV LLVGLITDGM SDRQFEDGLS ELERLVDTAG GKVLQVTRQK RDHPHPQTVI GSGKVAEIAL QVQTSGANLV VFNRDLSPAQ IRNLENQIGV RVVDRTEVIL DIFAQRAQSQ AGKLQVELAQ LEYTLPRLTG RGLAMSRLGG GIGTRGPGET KLETERRTIQ RRLSRLQDEV DQLQAHRSRL RKQRQKQDVA SVAIVGYTNA GKSTLINALT AAEVYTADQL FATLDPTTRR LTITDPLSQV SHTLLLTDTV GFIHELPPSL VDAFRATLEE VTEAEALLHL VDLSHPAWES QIASVLKILS EMPIQTGPML MVFNKLDQVK SEDLEIAKEK YPQAVFISAI RRLGLETLKQ KLIDLTA // ID B0K943_THEP3 Unreviewed; 413 AA. AC B0K943; DT 18-MAR-2008, integrated into UniProtKB/TrEMBL. DT 18-MAR-2008, sequence version 1. DT 07-JUN-2017, entry version 69. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Teth39_1001 {ECO:0000313|EMBL:ABY94656.1}; OS Thermoanaerobacter pseudethanolicus (strain ATCC 33223 / 39E) OS (Clostridium thermohydrosulfuricum). OC Bacteria; Firmicutes; Clostridia; Thermoanaerobacterales; OC Thermoanaerobacteraceae; Thermoanaerobacter. OX NCBI_TaxID=340099 {ECO:0000313|EMBL:ABY94656.1, ECO:0000313|Proteomes:UP000002156}; RN [1] {ECO:0000313|Proteomes:UP000002156} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33223 / 39E {ECO:0000313|Proteomes:UP000002156}; RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., RA Dalin E., Tice H., Pitluck S., Bruce D., Goodwin L., Saunders E., RA Brettin T., Detter J.C., Han C., Schmutz J., Larimer F., Land M., RA Hauser L., Kyrpides N., Lykidis A., Hemme C., Fields M.W., He Z., RA Zhou J., Richardson P.; RT "Complete sequence of Thermoanaerobacter pseudethanolicus 39E."; RL Submitted (JAN-2008) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000924; ABY94656.1; -; Genomic_DNA. DR RefSeq; WP_012269271.1; NC_010321.1. DR ProteinModelPortal; B0K943; -. DR STRING; 340099.Teth39_1001; -. DR EnsemblBacteria; ABY94656; ABY94656; Teth39_1001. DR KEGG; tpd:Teth39_1001; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR Proteomes; UP000002156; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000002156}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000002156}. FT DOMAIN 199 359 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 158 192 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 413 AA; 47224 MW; 4EAAC9C3F8B72C71 CRC64; MEELNREGYK ERAILVGIVS TPEYEESMEE LKELALTAGA EVVGIMTQKR NTIDKAHYIG KGKLEELKFF VENQEVDLVI VNDELTGTQI KNIEDFLNVK VIDRTNLILD IFAKRAKSRE GMLQVELAQL KYRLPRLVGL GGQLSRLGGG IGTRGPGETK LETDRRHIKN RIKAIEKKLE EIERHRSLQR ERRKKNRIPV IAIVGYTNAG KSTLLNALTN AEVYVEDKLF ATLDPTARRL VLPSGREVIL IDTVGFIRKL PHDLVEAFKS TLEEAKYADL LLHVIDVTSP DMEEKIKVVE KVLSDLDVIN TPRINVFNKI DLLDVVPKGN EKEIYISAKN KIGLDKLLQA IEKEIFKDVE IVNFLLPYDK TKEYNYLKEK TKVIEESYDE KGIIIKAEVQ KETKERFKDF IIV // ID B0PD12_9FIRM Unreviewed; 438 AA. AC B0PD12; DT 08-APR-2008, integrated into UniProtKB/TrEMBL. DT 08-APR-2008, sequence version 1. DT 07-JUN-2017, entry version 45. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:EDS10698.1}; GN ORFNames=ANACOL_02675 {ECO:0000313|EMBL:EDS10698.1}; OS Anaerotruncus colihominis DSM 17241. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Ruminococcaceae; OC Anaerotruncus. OX NCBI_TaxID=445972 {ECO:0000313|EMBL:EDS10698.1, ECO:0000313|Proteomes:UP000003803}; RN [1] {ECO:0000313|EMBL:EDS10698.1, ECO:0000313|Proteomes:UP000003803} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 17241 {ECO:0000313|EMBL:EDS10698.1, RC ECO:0000313|Proteomes:UP000003803}; RA Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., RA Liep D., Gordon J.; RT "Draft genome sequence of Anaerotruncus colihominis(DSM 17241)."; RL Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:EDS10698.1, ECO:0000313|Proteomes:UP000003803} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 17241 {ECO:0000313|EMBL:EDS10698.1, RC ECO:0000313|Proteomes:UP000003803}; RA Fulton L., Clifton S., Fulton B., Xu J., Minx P., Pepin K.H., RA Johnson M., Thiruvilangam P., Bhonagiri V., Nash W.E., Mardis E.R., RA Wilson R.K.; RL Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EDS10698.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABGD02000022; EDS10698.1; -; Genomic_DNA. DR ProteinModelPortal; B0PD12; -. DR STRING; 445972.ANACOL_02675; -. DR EnsemblBacteria; EDS10698; EDS10698; ANACOL_02675. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000003803; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000003803}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000003803}. FT DOMAIN 224 385 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 183 217 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 438 AA; 47768 MW; 9C334808F58CB026 CRC64; MSVSHLREKC NAKNLVKARP GKGEAMFDNQ KQTIQRAVLA AVDTGEYDIQ ASLDELEALA QTAGAQTAAK LVQKRPSCDP ATVIGSGRLE ELAQLCENDG ADLVIFDCEL SPAQLRNIEN ACGVAVIDRT ALILDIFAQR AVTAEGKLQV ELAQLRYRLP RLGGMGKALS RLGGGIGTRG PGETQLETDR RHIRRRIAAL QEQLAELKKR RGLLRARRKK EGVTTVAIVG YTNVGKSTLL NALTGAGVLS EDKLFATLDP TSRALTLPDG RSVMLIDTVG LVRRLPHQLV EAFQSTLEEA AGADLLWCVC DAASDEMAEQ VDVTRQLMRE LGAQDIPMLV ILNKCDLVAD VPRALNQQTA LISARTGFGF DMLLQKTSEL LAPTHRRVTL MLPYDKTGLI SEIMASGKVY AQTYEPEGTR VDALVDLRLL HKVSQWRV // ID B0RHB2_CLAMS Unreviewed; 521 AA. AC B0RHB2; DT 08-APR-2008, integrated into UniProtKB/TrEMBL. DT 08-APR-2008, sequence version 1. DT 07-JUN-2017, entry version 63. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=CMS1214 {ECO:0000313|EMBL:CAQ01329.1}; OS Clavibacter michiganensis subsp. sepedonicus (strain ATCC 33113 / DSM OS 20744 / JCM 9667 / LMG 2889 / C-1) (Corynebacterium sepedonicum). OC Bacteria; Actinobacteria; Micrococcales; Microbacteriaceae; OC Clavibacter. OX NCBI_TaxID=31964 {ECO:0000313|EMBL:CAQ01329.1, ECO:0000313|Proteomes:UP000001318}; RN [1] {ECO:0000313|EMBL:CAQ01329.1, ECO:0000313|Proteomes:UP000001318} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33113 / DSM 20744 / JCM 9667 / LMG 2889 / C-1 RC {ECO:0000313|Proteomes:UP000001318}; RX PubMed=18192393; DOI=10.1128/JB.01598-07; RA Bentley S.D., Corton C., Brown S.E., Barron A., Clark L., Doggett J., RA Harris B., Ormond D., Quail M.A., May G., Francis D., Knudson D., RA Parkhill J., Ishimaru C.A.; RT "Genome of the actinomycete plant pathogen Clavibacter michiganensis RT subsp. sepedonicus suggests recent niche adaptation."; RL J. Bacteriol. 190:2150-2160(2008). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AM849034; CAQ01329.1; -; Genomic_DNA. DR RefSeq; WP_012298607.1; NC_010407.1. DR ProteinModelPortal; B0RHB2; -. DR STRING; 31964.CMS_1214; -. DR EnsemblBacteria; CAQ01329; CAQ01329; CMS1214. DR GeneID; 29470161; -. DR KEGG; cms:CMS1214; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000001318; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 2. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000001318}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000001318}. FT DOMAIN 299 464 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 521 AA; 56140 MW; 49B75D2E9FF68BDB CRC64; MTTHDGHDHE PADTTTTSTE NIDRDDVVAR VLGRAENRSA GYALFRGSGA QALSAAPDTE QGSDGDQSER ADRQALRRVP GLSTELEDVT EVEYRQLRLE NVVLIGVYSQ GSVDDAENSM RELAALAETA GAVVLDGLLQ RRPTPDPSTY FGRGKAEELR ALVAAVGADT VIADTELAPS QRRALEDVVK VKVIDRTAVI LDIFSQHAKS REGKAQVELA QLQYLLPRLR GWGDSMSRQA GGQVGGAGAG MGSRGPGETK IELDRRRINT RMARLRKQIA AMKPARDTKR ANRDRHSVPS VAIVGYTNAG KSSLLNRVTK AGVLVENALF ATLDATVRKT ETDQGQLYTL ADTVGFVRNL PHQLVEAFRS TLEELADSDV LVHVVDASHP DPGAQLATVH EVIAEVNASA IPEIVVFNKS DLASADDRVV LRGLAPQGVF VSARTGEGVE ELRRRIAELL PQPTIEVDLL VPFEHGEVVA MLHDGAKVLE TSYVEEGTRV RALVTAEQQA QVQAYAVAPA A // ID B0S1S4_FINM2 Unreviewed; 415 AA. AC B0S1S4; DT 08-APR-2008, integrated into UniProtKB/TrEMBL. DT 08-APR-2008, sequence version 1. DT 07-JUN-2017, entry version 63. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=FMG_0896 {ECO:0000313|EMBL:BAG08314.1}; OS Finegoldia magna (strain ATCC 29328) (Peptostreptococcus magnus). OC Bacteria; Firmicutes; Tissierellia; Tissierellales; Peptoniphilaceae; OC Finegoldia. OX NCBI_TaxID=334413 {ECO:0000313|EMBL:BAG08314.1, ECO:0000313|Proteomes:UP000001319}; RN [1] {ECO:0000313|EMBL:BAG08314.1, ECO:0000313|Proteomes:UP000001319} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29328 {ECO:0000313|EMBL:BAG08314.1, RC ECO:0000313|Proteomes:UP000001319}; RX PubMed=18263572; DOI=10.1093/dnares/dsm030; RA Goto T., Yamashita A., Hirakawa H., Matsutani M., Todo K., Ohshima K., RA Toh H., Miyamoto K., Kuhara S., Hattori M., Shimizu T., Akimoto S.; RT "Complete genome sequence of Finegoldia magna, an anaerobic RT opportunistic pathogen."; RL DNA Res. 15:39-47(2008). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AP008971; BAG08314.1; -; Genomic_DNA. DR RefSeq; WP_012290696.1; NC_010376.1. DR ProteinModelPortal; B0S1S4; -. DR STRING; 334413.FMG_0896; -. DR EnsemblBacteria; BAG08314; BAG08314; FMG_0896. DR KEGG; fma:FMG_0896; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000001319; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000001319}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000001319}. FT DOMAIN 193 362 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 152 186 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 415 AA; 47621 MW; 9A913007AC4CC2DB CRC64; MKEKTILVYF EFKNKKINDE DIGEMESLIE SSGGEVCAIS EVRKNSIDSK YFIGKGKCLE IKDAAEKLDV TTLIFNVELS GSNIKNLEDI TGLKIVDKTN LILDIFASRA KTKQSVLQVE LAEYKYRLPR LIGFRDHLSR TGGGIGTRGP GETKLEVDRR TIQKKIDNIK RELKSIDKSQ ENMRKQRLKS DIKMVSMVGY TNAGKSTLSN KLVNFYKDKY TEEFETEDLL FKTLDTTLRK CTLPNKKQCL VIDTVGFIKD IPTDLIEAFK STLLDLKHSD LILFVLDSSS SDLDNQITTT MDILKELKVL DKPMVTVFNK SDKNPNVIFP YNLDNKIKIS AFNDKDIEKL LYKIQEELYG NYKCVNMKFD YNHQDVLNAV LQNFKCENVS YNNDDVSLEV EISESEIEKY KEFII // ID B0SJP6_LEPBP Unreviewed; 518 AA. AC B0SJP6; DT 08-APR-2008, integrated into UniProtKB/TrEMBL. DT 08-APR-2008, sequence version 1. DT 07-JUN-2017, entry version 70. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=LEPBI_I0062 {ECO:0000313|EMBL:ABZ96209.1}; OS Leptospira biflexa serovar Patoc (strain Patoc 1 / ATCC 23582 / OS Paris). OC Bacteria; Spirochaetes; Leptospirales; Leptospiraceae; Leptospira. OX NCBI_TaxID=456481 {ECO:0000313|EMBL:ABZ96209.1, ECO:0000313|Proteomes:UP000001847}; RN [1] {ECO:0000313|EMBL:ABZ96209.1, ECO:0000313|Proteomes:UP000001847} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Patoc 1 / ATCC 23582 / Paris RC {ECO:0000313|Proteomes:UP000001847}; RX PubMed=18270594; DOI=10.1371/journal.pone.0001607; RA Picardeau M., Bulach D.M., Bouchier C., Zuerner R.L., Zidane N., RA Wilson P.J., Creno S., Kuczek E.S., Bommezzadri S., Davis J.C., RA McGrath A., Johnson M.J., Boursaux-Eude C., Seemann T., Rouy Z., RA Coppel R.L., Rood J.I., Lajus A., Davies J.K., Medigue C., Adler B.; RT "Genome sequence of the saprophyte Leptospira biflexa provides RT insights into the evolution of Leptospira and the pathogenesis of RT leptospirosis."; RL PLoS ONE 3:E1607-E1607(2008). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000786; ABZ96209.1; -; Genomic_DNA. DR RefSeq; WP_012387099.1; NC_010602.1. DR ProteinModelPortal; B0SJP6; -. DR STRING; 456481.LEPBI_I0062; -. DR PRIDE; B0SJP6; -. DR EnsemblBacteria; ABZ96209; ABZ96209; LEPBI_I0062. DR KEGG; lbi:LEPBI_I0062; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; EREVIIT; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000001847; Chromosome I. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000001847}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000001847}. FT DOMAIN 345 508 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 304 338 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 518 AA; 58896 MW; 1EA449211063DE75 CRC64; MELARLVGEI SVEMGRQVGL LIERTGYVTH LIVGNDHSIE IPHLDRYRVA HSRLRGLRLF HTHLKEQPLN QEDLMDLVLN RFDSITAACV DKEGIPKFFF SAFINPDPDA KEPWILSPKQ YPGQIKYGYS EQVDALESEF TKKTSNLKES QKENRAFLVG VYDVRKMKRS PEHSMDELKE LCRTAGIHVV DTYVQKRDPD PRTVVGKGKL QEIILTSVHK DIEHLIFDLE LTPSQAKKIS DASDLKIIDR TQLILDIFSK NAKSRDGKLQ VELAQLKYLK NRLSELDDNM SRLTGGIGGR GPGETKLEIG NRRVEEKINR LENELKDLKR RRELNRKSRS RNEIPIVGIV GYTNAGKSTL LNALTNSTVI AEDKLFATLD PTTRRIRFPE EREIIISDTV GFIHDLPPDL SQAFKATLEE LGDADLLLHV VDVTNPNYTE QMDAVDTILN SLHLNEIPRM VVFNKADGLD EETHDILQKN GALLVSAVTR EGLSKLLDLI EYEIWKKKEQ KLLEVTSS // ID B0SXF3_CAUSK Unreviewed; 446 AA. AC B0SXF3; DT 08-APR-2008, integrated into UniProtKB/TrEMBL. DT 08-APR-2008, sequence version 1. DT 07-JUN-2017, entry version 61. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Caul_2611 {ECO:0000313|EMBL:ABZ71738.1}; OS Caulobacter sp. (strain K31). OC Bacteria; Proteobacteria; Alphaproteobacteria; Caulobacterales; OC Caulobacteraceae; Caulobacter. OX NCBI_TaxID=366602 {ECO:0000313|EMBL:ABZ71738.1, ECO:0000313|Proteomes:UP000001316}; RN [1] {ECO:0000313|EMBL:ABZ71738.1, ECO:0000313|Proteomes:UP000001316} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K31 {ECO:0000313|EMBL:ABZ71738.1, RC ECO:0000313|Proteomes:UP000001316}; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., RA Dalin E., Tice H., Pitluck S., Bruce D., Goodwin L., Thompson L.S., RA Brettin T., Detter J.C., Han C., Schmutz J., Larimer F., Land M., RA Hauser L., Kyrpides N., Kim E., Stephens C., Richardson P.; RT "Complete sequence of chromosome of Caulobacter sp. K31."; RL Submitted (JAN-2008) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000927; ABZ71738.1; -; Genomic_DNA. DR RefSeq; WP_012286641.1; NC_010338.1. DR ProteinModelPortal; B0SXF3; -. DR STRING; 366602.Caul_2611; -. DR EnsemblBacteria; ABZ71738; ABZ71738; Caul_2611. DR KEGG; cak:Caul_2611; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000001316; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000001316}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000001316}. FT DOMAIN 214 384 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 446 AA; 49425 MW; 131D2487F170F280 CRC64; MTKSTSKSID HAVPVLRALV IHPVRPTRGQ SALEARDPRV RLEEAVGLAI ALDLDVVETM VAPLRLVTPA TLFGKGKIEE FAAICEVEKI DVAVFDDQLT PVQQRNLEKA LNVKVVDRTG LILEIFARRA RTREGKLQVE LARLDYERSR LVRTWTHLER QRGGTGNTGG PGETQIELDR RLIRDNILKL KRELDEVRRT RTLHRSQRKK APYPTVALVG YTNAGKSTLF NRLTHATVVA QDMLFATLDP TLRNVKLPDG RPAILSDTVG FISDLPHELV EAFRATLEEV QEADVVLHVR DVANPDTDAQ ARDVQVVLAE LKVTAEDGKT IIEVWNKIDL VDGEAREILD GQARRLGASA VSAVTGEGCA ELLKRVGTLI DDTPPVAVRL AAKDGEALAW IYRNGRVESR DEEAEGGVRL IARLDAQALG RFERQFPDVW VMATGD // ID B0TAZ9_HELMI Unreviewed; 550 AA. AC B0TAZ9; DT 08-APR-2008, integrated into UniProtKB/TrEMBL. DT 08-APR-2008, sequence version 1. DT 07-JUN-2017, entry version 62. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=HM1_2573 {ECO:0000313|EMBL:ABZ85110.1}; OS Heliobacterium modesticaldum (strain ATCC 51547 / Ice1). OC Bacteria; Firmicutes; Clostridia; Clostridiales; Heliobacteriaceae; OC Heliobacterium. OX NCBI_TaxID=498761 {ECO:0000313|EMBL:ABZ85110.1, ECO:0000313|Proteomes:UP000008550}; RN [1] {ECO:0000313|EMBL:ABZ85110.1, ECO:0000313|Proteomes:UP000008550} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51547 / Ice1 {ECO:0000313|Proteomes:UP000008550}; RX PubMed=18441057; DOI=10.1128/JB.00299-08; RA Sattley W.M., Madigan M.T., Swingley W.D., Cheung P.C., Clocksin K.M., RA Conrad A.L., Dejesa L.C., Honchak B.M., Jung D.O., Karbach L.E., RA Kurdoglu A., Lahiri S., Mastrian S.D., Page L.E., Taylor H.L., RA Wang Z.T., Raymond J., Chen M., Blankenship R.E., Touchman J.W.; RT "The genome of Heliobacterium modesticaldum, a phototrophic RT representative of the Firmicutes containing the simplest RT photosynthetic apparatus."; RL J. Bacteriol. 190:4687-4696(2008). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000930; ABZ85110.1; -; Genomic_DNA. DR ProteinModelPortal; B0TAZ9; -. DR STRING; 498761.HM1_2573; -. DR EnsemblBacteria; ABZ85110; ABZ85110; HM1_2573. DR KEGG; hmo:HM1_2573; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; EREVIIT; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000008550; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000008550}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000008550}. FT DOMAIN 319 491 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 278 305 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 550 AA; 60856 MW; C22F8E8BDAE11267 CRC64; MFADRRGRVV DLVVGDAHTV AMMDHDIRRG TRRLAGVRCI HTHPGDSPYL SDVDLSALRQ LHLDCMAVIA AADPHCGSAA YLSPGSDHAI ESIGPLSYEK LCAFPWQEMV RRYEKRISSV DTTATGAEQE RAFLIGLEDS VAGEERPLEE LAQLAEAAGA VVVGQMTQRL ERPDRATYLG SGKIRELTLA LQVTRADLLI VDEELLPAQQ RRLENLTGIR VVDRTALILD IFAGRARTRE GKLQVELAQL HYLLPRLTGQ GQALSRLGGG IGTRGPGETK LETDRRHLRR RMRDLEGELN HVRHHRERLR HSRQRLDLPL ISMVGYTNAG KSTLSNLLVS RFAPFGGTSP AGEDKLFATL DPTTRRIRLL AERDVLLSDT VGFIRKLPHS LVRAFRATLE EIVAADLLLH IVDASHPAAV EQMRTVEAVL AEIGAGEKPI LTVLNKIDRL QPGGIDALLR PPDPWVALSA YTGEGVDGLL EKIARLLPDD RVTIDVLIPY DEGKQIHHLY QIGVVRELTH EVEGVRVRAD VPKAYVASLP GRQMTVPEKY // ID B0UIY4_METS4 Unreviewed; 474 AA. AC B0UIY4; DT 08-APR-2008, integrated into UniProtKB/TrEMBL. DT 08-APR-2008, sequence version 1. DT 07-JUN-2017, entry version 62. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=M446_5943 {ECO:0000313|EMBL:ACA20223.1}; OS Methylobacterium sp. (strain 4-46). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Methylobacteriaceae; Methylobacterium. OX NCBI_TaxID=426117 {ECO:0000313|EMBL:ACA20223.1, ECO:0000313|Proteomes:UP000001185}; RN [1] {ECO:0000313|EMBL:ACA20223.1, ECO:0000313|Proteomes:UP000001185} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=4-46 {ECO:0000313|EMBL:ACA20223.1, RC ECO:0000313|Proteomes:UP000001185}; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., RA Tice H., Bruce D., Goodwin L., Pitluck S., Chertkov O., Brettin T., RA Detter J.C., Han C., Kuske C.R., Schmutz J., Larimer F., Land M., RA Hauser L., Kyrpides N., Ivanova N., Marx C.J., Richardson P.; RT "Complete sequence of chromosome of Methylobacterium sp. 4-46."; RL Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000943; ACA20223.1; -; Genomic_DNA. DR RefSeq; WP_012335601.1; NC_010511.1. DR ProteinModelPortal; B0UIY4; -. DR STRING; 426117.M446_5943; -. DR EnsemblBacteria; ACA20223; ACA20223; M446_5943. DR KEGG; met:M446_5943; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000001185; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000001185}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000001185}. FT DOMAIN 235 406 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 474 AA; 52301 MW; 7896F544A4052127 CRC64; MEPRIPGDTR LSDEARPGEA RLQRMAEPEG TIAAATRTLV LGPYLTRRGD AARAPTRPPE ARLDEAVGLA AAIDLAVVDR LMLPVQAIRP STYLGKGRVE EIAGRIAAES VRLVVMDCAL SPVQQRNLEK AWGVKVIDRT GMILEIFGRR ASTREGALQV EHAHLAYQRS RLVRSWTHLE RQRGGFGFLG GPGETQIEAD RRLIQERMTR IERELGTVTR TRGLHRQSRR RVPYPIVALV GYTNAGKSTL FNRLTEAEVR AEDMLFATLD PTARAIKLPH GETAILSDTV GFISDLPTML IAAFRATLED VIEADILLHV RDMAHEDTQA QGEDVQAVLA ELGIAPQADR IIEVWNKADL LGPEERERLL NLSRQTGTRP VLISALTGEG TDALLARIEG RIAESRASFA LVLDPAEGAG LHWLYENAEV LDRREDAGGR LHLVVRVAPE KEPRLLNRFG TARRLRAAGE AARP // ID B0UTF6_HISS2 Unreviewed; 458 AA. AC B0UTF6; DT 08-APR-2008, integrated into UniProtKB/TrEMBL. DT 08-APR-2008, sequence version 1. DT 30-AUG-2017, entry version 62. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=HSM_1075 {ECO:0000313|EMBL:ACA30790.1}; OS Histophilus somni (strain 2336) (Haemophilus somnus). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Histophilus. OX NCBI_TaxID=228400 {ECO:0000313|EMBL:ACA30790.1, ECO:0000313|Proteomes:UP000008543}; RN [1] {ECO:0000313|EMBL:ACA30790.1, ECO:0000313|Proteomes:UP000008543} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=2336 {ECO:0000313|EMBL:ACA30790.1, RC ECO:0000313|Proteomes:UP000008543}; RG US DOE Joint Genome Institute; RA Siddaramappa S., Duncan A.J., Challacombe J.F., Rainey D., RA Gillaspy A.F., Carson M., Gipson J., Gipson M., Bruce D., Detter J.C., RA Han C.S., Land M., Tapia R., Thompson L.S., Orvis J., Zaitshik J., RA Barnes G., Brettin T.S., Dyer D.W., Inzana T.J.; RT "Complete sequence of Haemophilus somnus 2336."; RL Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000947; ACA30790.1; -; Genomic_DNA. DR RefSeq; WP_012340262.1; NC_010519.1. DR ProteinModelPortal; B0UTF6; -. DR EnsemblBacteria; ACA30790; ACA30790; HSM_1075. DR GeneID; 31487375; -. DR KEGG; hsm:HSM_1075; -. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000008543; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000008543}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000008543}. FT DOMAIN 223 390 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 189 219 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 458 AA; 51927 MW; 33CA02B6ED76B322 CRC64; MNTNKQFKVY TASAVDFAQD PTALSSNINV PQFDKAIVVH VFFSQNKNLE DLQEFQLLVK SANVDILSII TTSRSTPQAK YFVGQGKAEE IAQAVEQLNA DIVLVNHSLT PAQTRNLESI CQCRVVDRTG LILDIFAQRA RSHEGKLQVE LAQLRHLATR LVRRKTGLDQ QKGAVGLRGP GETQLETDRR LIKVRITQLQ NRLEKVAKQR NQNRQTRRKA DIPTISLVGY TNAGKSTLFN VLTQANVYVA DQLFATLDPT LKRLPIQDVG NCVLADTVGF IRELPHDLVS AFKSTLQETT EASLLLHVID VADSRKLENM LTVNEVLSEI KANQVTTLLV YNKIDQVENI QPHIEFDEEN QPIAVYLSAQ LNQGLDLLVE AIRQKLSHEI LHLEINLAAQ YGKIRHCFYQ LNCVRQEKIN EQGEFLLDIQ IDKIEWLKLS KQFPLLKRFY ETTEISDK // ID B0VIH3_CLOAI Unreviewed; 447 AA. AC B0VIH3; DT 08-APR-2008, integrated into UniProtKB/TrEMBL. DT 08-APR-2008, sequence version 1. DT 07-JUN-2017, entry version 63. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:CAO79962.1}; GN OrderedLocusNames=CLOAM0044 {ECO:0000313|EMBL:CAO79962.1}; OS Cloacimonas acidaminovorans (strain Evry). OC Bacteria; Candidatus Cloacimonetes; Candidatus Cloacimonas. OX NCBI_TaxID=459349 {ECO:0000313|EMBL:CAO79962.1, ECO:0000313|Proteomes:UP000002019}; RN [1] {ECO:0000313|EMBL:CAO79962.1, ECO:0000313|Proteomes:UP000002019} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Evry {ECO:0000313|Proteomes:UP000002019}; RX PubMed=18245282; DOI=10.1128/JB.01248-07; RA Pelletier E., Kreimeyer A., Bocs S., Rouy Z., Gyapay G., Chouari R., RA Riviere D., Ganesan A., Daegelen P., Sghir A., Cohen G.N., Medigue C., RA Weissenbach J., Le Paslier D.; RT "'Candidatus Cloacamonas acidaminovorans': genome sequence RT reconstruction provides a first glimpse of a new bacterial division."; RL J. Bacteriol. 190:2572-2579(2008). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CU466930; CAO79962.1; -; Genomic_DNA. DR RefSeq; WP_015423823.1; NC_020449.1. DR ProteinModelPortal; B0VIH3; -. DR HOGENOM; HOG000260368; -. DR OMA; HPATYIG; -. DR Proteomes; UP000002019; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000002019}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000002019}. FT DOMAIN 223 388 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 34 57 {ECO:0000256|SAM:Coils}. FT COILED 198 225 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 447 AA; 51324 MW; 49E9DF337F690838 CRC64; MNNEEYKALD EFELEPENWE QAERTEKTAF LAALANSRET DKDIKESLNE LERLAETAGI QVLGTYHQRR NAPERGTYFG KGFLTELSRK MMQAQADILI VNDELGPSQA YNIERDYQIK VMDRTEVILD IFHKHAKTRE SKLQVHLAEL EYQLPRLKRM WEHFDKERGG VRNTGGTATR GMGEKQIEID RRLIKDKIRK INKAIETIQH QKETQRKQRE KAKKICLVGY TNAGKSTLFN QLTNAGVLVE DKLFATLDST SRQLKLSTGN PVVLSDTVGF ISKLPHHLIA SFKATLMEVQ DANLLLHIVD VSDERFEYYI QQVNSVLQQI GAETIPQILV FNKIDNVDSI LVSLLESRFP EGVFISAIQG INIDKLLAKM EEILLGNRIL QLKIPYDKTA LVSKMHDIAE IISEDYKEDG IYLKVEISRD DRFLVEDYVL ENEEGKN // ID B0VV36_ACIBS Unreviewed; 444 AA. AC B0VV36; DT 08-APR-2008, integrated into UniProtKB/TrEMBL. DT 08-APR-2008, sequence version 1. DT 07-JUN-2017, entry version 64. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:CAP02149.1}; GN OrderedLocusNames=ABSDF2856 {ECO:0000313|EMBL:CAP02149.1}; OS Acinetobacter baumannii (strain SDF). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Moraxellaceae; Acinetobacter; OC Acinetobacter calcoaceticus/baumannii complex. OX NCBI_TaxID=509170 {ECO:0000313|EMBL:CAP02149.1, ECO:0000313|Proteomes:UP000001741}; RN [1] {ECO:0000313|EMBL:CAP02149.1, ECO:0000313|Proteomes:UP000001741} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SDF {ECO:0000313|EMBL:CAP02149.1, RC ECO:0000313|Proteomes:UP000001741}; RX PubMed=18350144; DOI=10.1371/journal.pone.0001805; RA Vallenet D., Nordmann P., Barbe V., Poirel L., Mangenot S., RA Bataille E., Dossat C., Gas S., Kreimeyer A., Lenoble P., Oztas S., RA Poulain J., Segurens B., Robert C., Abergel C., Claverie J.-M., RA Raoult D., Medigue C., Weissenbach J., Cruveiller S.; RT "Comparative analysis of Acinetobacters: three genomes for three RT lifestyles."; RL PLoS ONE 3:E1805-E1805(2008). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CU468230; CAP02149.1; -; Genomic_DNA. DR ProteinModelPortal; B0VV36; -. DR EnsemblBacteria; CAP02149; CAP02149; ABSDF2856. DR KEGG; abm:ABSDF2856; -. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR Proteomes; UP000001741; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000001741}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000001741}. FT DOMAIN 200 365 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 444 AA; 49992 MW; 7524C5FBB3C39ECD CRC64; MEYVDRHQGG ERTILVSVSV QLLDDLDAEE FALLAQSAGA DILEHIKVQR NKPDPKFFIG SGKVDEIAEQ VQDLKASLVI FDHELTPAQE RNLEKILKCR VIDRTGLILD IFAQRARTHE GKLQVELAQL KHLSTRLIRG WSADFEQQKG GIGLRGPGES QLETDRRLIR VRITQLKDKL EKVHQTRMQG RAARQKASIP TVSLVGYTNA GKSTLFNILA KSDVYAADQL FATLDPTLRR LEWDGIGTVV LADTVGFVRN LQHDLVESFK ATLEETLEAT LLLHVIDSSS HDMLDQIKAV EGVLKEIGAD APVLRVYNKI DLSGEEAKII YSEPRVPDRV YVSAHSGLGL DLLRQAVQEC LMGQLQHFSL VLKPAYGKLR TQLYALNVIQ SEHYDDEGLL HIDIRIAPHK LEQLIRQAKL PIDEILGERA SQFKRPLEEF EIKH // ID B0WJA8_CULQU Unreviewed; 515 AA. AC B0WJA8; DT 08-APR-2008, integrated into UniProtKB/TrEMBL. DT 08-APR-2008, sequence version 1. DT 30-AUG-2017, entry version 56. DE SubName: Full=GTP-binding protein hflx {ECO:0000313|EMBL:EDS29044.1, ECO:0000313|VectorBase:CPIJ007256-PA}; GN Name=6039132 {ECO:0000313|VectorBase:CPIJ007256-PA}; GN ORFNames=CpipJ_CPIJ007256 {ECO:0000313|EMBL:EDS29044.1}; OS Culex quinquefasciatus (Southern house mosquito) (Culex pungens). OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; OC Pterygota; Neoptera; Holometabola; Diptera; Nematocera; Culicoidea; OC Culicidae; Culicinae; Culicini; Culex; Culex. OX NCBI_TaxID=7176 {ECO:0000313|Proteomes:UP000002320}; RN [1] {ECO:0000313|EMBL:EDS29044.1, ECO:0000313|VectorBase:CPIJ007256-PA} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=JHB {ECO:0000313|EMBL:EDS29044.1, RC ECO:0000313|VectorBase:CPIJ007256-PA}; RG The Broad Institute Genome Sequencing Platform; RA Atkinson P.W., Hemingway J., Christensen B.M., Higgs S., Kodira C., RA Hannick L., Megy K., O'Leary S., Pearson M., Haas B.J., Mauceli E., RA Wortman J.R., Lee N.H., Guigo R., Stanke M., Alvarado L., Amedeo P., RA Antoine C.H., Arensburger P., Bidwell S.L., Crawford M., Camaro F., RA Devon K., Engels R., Hammond M., Howarth C., Koehrsen M., Lawson D., RA Montgomery P., Nene V., Nusbaum C., Puiu D., Romero-Severson J., RA Severson D.W., Shumway M., Sisk P., Stolte C., Zeng Q., Eisenstadt E., RA Fraser-Liggett C., Strausberg R., Galagan J., Birren B., Collins F.H.; RT "Annotation of Culex pipiens quinquefasciatus."; RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Proteomes:UP000002320} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=JHB {ECO:0000313|Proteomes:UP000002320}; RG The Broad Institute Genome Sequencing Platform; RA Atkinson P.W., Hemingway J., Christensen B.M., Higgs S., Kodira C.D., RA Hannick L.I., Megy K., O'Leary S.B., Pearson M., Haas B.J., RA Mauceli E., Wortman J.R., Lee N.H., Guigo R., Stanke M., Alvarado L., RA Amedeo P., Antoine C.H., Arensburger P., Bidwell S.L., Crawford M., RA Camaro F., Devon K., Engels R., Hammond M., Howarth C., Koehrsen M., RA Lawson D., Montgomery P., Nene V., Nusbaum C., Puiu D., RA Romero-Severson J., Severson D.W., Shumway M., Sisk P., Stolte C., RA Zeng Q., Eisenstadt E., Fraser-Liggett C.M., Strausberg R., RA Galagan J., Birren B., Collins F.H.; RT "Annotation of Culex pipiens quinquefasciatus."; RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases. RN [3] {ECO:0000313|VectorBase:CPIJ007256-PA} RP IDENTIFICATION. RC STRAIN=JHB {ECO:0000313|VectorBase:CPIJ007256-PA}; RG VectorBase; RL Submitted (FEB-2017) to UniProtKB. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; DS231958; EDS29044.1; -; Genomic_DNA. DR RefSeq; XP_001848793.1; XM_001848741.1. DR UniGene; Cpi.3783; -. DR ProteinModelPortal; B0WJA8; -. DR STRING; 7176.CPIJ007256-PA; -. DR EnsemblMetazoa; CPIJ007256-RA; CPIJ007256-PA; CPIJ007256. DR GeneID; 6039132; -. DR KEGG; cqu:CpipJ_CPIJ007256; -. DR VectorBase; CPIJ007256-RA; CPIJ007256-PA; CPIJ007256. DR eggNOG; KOG0410; Eukaryota. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000045792; -. DR InParanoid; B0WJA8; -. DR OMA; MDTVGFM; -. DR OrthoDB; EOG091G0852; -. DR PhylomeDB; B0WJA8; -. DR Proteomes; UP000002320; Partially assembled WGS sequence. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR CDD; cd01878; HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000002320}; KW Reference proteome {ECO:0000313|Proteomes:UP000002320}. FT DOMAIN 287 454 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 515 AA; 57509 MW; B4D13FFFB6D6D61D CRC64; MASSLTRLRC WRPMVQRALT VCRRPPSPVL GTVVSLRCKY TESSKYKGFK GKFQAKAAEG SEEDGEGSSQ EVDLDDAEYD AVANSAMHVQ KRLQNEQHVF IIQPYVKWGP KKVASDPEHQ LQEAEALVRS LPRWTIEHSL KVPLESLEKR QLFGTGKLGE LKSTLRNLQS AGKSVTCVFI SKGTLTFSQK QLLEQHFKLP VMDRYSVVIQ ILRLHAISTE AKLQVAMAEI PYIWSQLKDQ DGKGRVFLSE SQKQMLRLRE RKLKTQLTAI RSHRELLRNK RKQKAYPIVA VVGYTNAGKT SLIKALTEEE SLQPKNQLFA TLDVTAHAGL LPSKLEVLFM DTVGFMADIP TGLIECFVAT LEDAMFADLI IHVQDISHPN HAEQKNHVES TLAALLKSTG TNNENPPNII NVGNKVDLLP NSTPPSNLHL VSSKTLAGVN DLLAKIEQNI LESTGRQRII IRVPMGGAEV AWLYKNAAVT ETGADPDDSQ RMLVSAVITD AKLAQFRHQF VNRKR // ID B1BCH4_CLOBO Unreviewed; 598 AA. AC B1BCH4; DT 29-APR-2008, integrated into UniProtKB/TrEMBL. DT 29-APR-2008, sequence version 1. DT 30-AUG-2017, entry version 55. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=CBC_A0080 {ECO:0000313|EMBL:EDS76851.1}; OS Clostridium botulinum C str. Eklund. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=445337 {ECO:0000313|EMBL:EDS76851.1, ECO:0000313|Proteomes:UP000003482}; RN [1] {ECO:0000313|EMBL:EDS76851.1, ECO:0000313|Proteomes:UP000003482} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Eklund {ECO:0000313|EMBL:EDS76851.1, RC ECO:0000313|Proteomes:UP000003482}; RX PubMed=23516187; RA Hassan K.A., Tetu S.G., Elbourne L.D., Johnson E.A., Paulsen I.T.; RT "Genome Sequence of the Group III Clostridium botulinum Strain Eklund- RT C."; RL Genome Announc. 1:E0004413-E0004413(2013). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EDS76851.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABDQ01000012; EDS76851.1; -; Genomic_DNA. DR ProteinModelPortal; B1BCH4; -. DR STRING; 445337.CBC_A0080; -. DR EnsemblBacteria; EDS76851; EDS76851; CBC_A0080. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000003482; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000003482}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}. FT DOMAIN 364 541 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 598 AA; 66869 MW; DD5DEAD08D65C686 CRC64; MILGNLEGIR KTILKKIETI YDFRVDRQSI ANEEIIEIIS EVTADINKEI SVAIDRKGNV LSVAVGDSST VEMPIIDIKS KKLSGVRIIH THPNGNSRLS SLDVSALISL KLDCMVAVAV EEGKCKDLTI GFCGVHNNNL IAEIAPNLPL SKALNINILN VVKNIEINLS YNEVEEDKGE RAVLVGIENE ESLDELCELA KACNVSTVDR VLQKRVKIDT AYFIGEGKVE ELSMVRQASN ANLIIFDDEL SASQIRNLES MTGTKVIDRT TLILEIFARR AKSKEAKIQV ELAQLKYRLP RLIGMGAVLS RTGAGIGTRG PGEKKLEIDK RHIRERVYDL NKELSKIKKN RQIQREKRSR DNVPKISLVG YTNAGKSTLR NKLCDIASPR DVVDKETVFE ADMLFATLDV TTRALVLPDN RLVTLTDTVG FIRKLPHDLV EAFKSTLEEV VNSDLLLHVV DSSSKDAYKQ IEAVNLVLEE LESIDKPMIL ILNKIDKADK EQLEGLEEKF NNLKVLEISA RDNLNLDTLL NEVCRALPNP LKKVEFLIPY SDSATVAMLH RSGKVLEEEY KDNGTRIVAM VDEKIYNKCK EYTVIDTI // ID B1BZR2_9FIRM Unreviewed; 408 AA. AC B1BZR2; DT 29-APR-2008, integrated into UniProtKB/TrEMBL. DT 29-APR-2008, sequence version 1. DT 07-JUN-2017, entry version 47. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:EDS75909.1}; GN ORFNames=CLOSPI_00439 {ECO:0000313|EMBL:EDS75909.1}; OS [Clostridium] spiroforme DSM 1552. OC Bacteria; Firmicutes; Erysipelotrichia; Erysipelotrichales; OC Erysipelotrichaceae; Erysipelatoclostridium. OX NCBI_TaxID=428126 {ECO:0000313|EMBL:EDS75909.1, ECO:0000313|Proteomes:UP000004910}; RN [1] {ECO:0000313|EMBL:EDS75909.1, ECO:0000313|Proteomes:UP000004910} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 1552 {ECO:0000313|EMBL:EDS75909.1, RC ECO:0000313|Proteomes:UP000004910}; RA Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., RA Liep D., Gordon J.; RT "Draft genome sequence of Clostridium spiroforme (DSM 1552)."; RL Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:EDS75909.1, ECO:0000313|Proteomes:UP000004910} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 1552 {ECO:0000313|EMBL:EDS75909.1, RC ECO:0000313|Proteomes:UP000004910}; RA Fulton L., Clifton S., Fulton B., Xu J., Minx P., Pepin K.H., RA Johnson M., Thiruvilangam P., Bhonagiri V., Nash W.E., Mardis E.R., RA Wilson R.K.; RL Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EDS75909.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABIK02000004; EDS75909.1; -; Genomic_DNA. DR RefSeq; WP_004609599.1; NZ_DS562848.1. DR ProteinModelPortal; B1BZR2; -. DR STRING; 428126.CLOSPI_00439; -. DR EnsemblBacteria; EDS75909; EDS75909; CLOSPI_00439. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000004910; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000004910}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000004910}. FT DOMAIN 190 353 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 408 AA; 47198 MW; E88C3AFB7AB0BCBE CRC64; MDALIVGVKY KEMDYDLDSS LVELEELCKA CNIKVIKKCV QNLDKINPSL YIGTGKVQEI KMQLDDIDIV IFDEELSPLQ IKNLTDGLDI EVTDRTDLIL RIFEQRAKSK EAKLQVEIAK GQYLLPRLAG MKEHLYSQQG GSGFRGSGEK QIELDRRMIA NQIYQAKNQL AKIVKQRQTQ RKKRKNNEMK VIALVGYTNS GKSTLMNAFC IDKNKQVLQK NMLFATLQTA TRNIKINHHP CLLTDTVGFI NRLPHHLVQA FRSTLEEVVE ADLLIHVVDT TNENYEMCIE TTNQVLKELG IKDTPMIYAY NKIDLNKYAF IIPKDPYVFI SAKEQIGFEQ LEKMISSILF KDYAIYNLNI PYRDGEIFSY LHQHCLVLEF EYLEDSIYLK VEMHPSMISR YSKYILKN // ID B1I3R4_DESAP Unreviewed; 422 AA. AC B1I3R4; DT 29-APR-2008, integrated into UniProtKB/TrEMBL. DT 29-APR-2008, sequence version 1. DT 07-JUN-2017, entry version 59. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Daud_1110 {ECO:0000313|EMBL:ACA59621.1}; OS Desulforudis audaxviator (strain MP104C). OC Bacteria; Firmicutes; Clostridia; Clostridiales; Peptococcaceae; OC Candidatus Desulforudis. OX NCBI_TaxID=477974 {ECO:0000313|EMBL:ACA59621.1, ECO:0000313|Proteomes:UP000008544}; RN [1] {ECO:0000313|Proteomes:UP000008544} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MP104C {ECO:0000313|Proteomes:UP000008544}; RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., RA Dalin E., Tice H., Bruce D., Pitluck S., Lowry S.R., Larimer F., RA Land M.L., Hauser L., Kyrpides N., Ivanova N.N., Richardson P.; RT "Complete sequence of chromosome of Desulforudis audaxviator MP104C."; RL Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000860; ACA59621.1; -; Genomic_DNA. DR RefSeq; WP_012302207.1; NC_010424.1. DR ProteinModelPortal; B1I3R4; -. DR STRING; 477974.Daud_1110; -. DR EnsemblBacteria; ACA59621; ACA59621; Daud_1110. DR KEGG; dau:Daud_1110; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000008544; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000008544}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000008544}. FT DOMAIN 202 364 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 161 195 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 422 AA; 45931 MW; AD71600F562A47AC CRC64; MTAVPDGSAE KAVLVGVELG SLTGAEVRES LNELNRLART AGAEVAGTVL QKRPRPDPAH FVGRGKAEEL AALCSAAGAG LLIFDQDLSP AQARNLENVT GVRVLDRTQI ILDIFARRAR TREGKLQVEL AQLNYVLPRL TGRGTELSRL GGGIGTRGPG ETKLETDRRR IRQRIADLQR EIAEVRRHRQ LLRRARKVAP VPLVALVGYT NAGKSSLLNA LTGAVVSVED RLFATLDPTS RQLRLPTNEV VVLTDTVGFI RHLPHHLVAA FRATLEEVVE ADLLLHVVDL SHPAHQAHIT AVDGVLEELG AGGKPRLMVF NKTDLVEPGE LDLLGRNDVA VSALTGAGLD TLRAAVADAL STWRTRERFL IPYSRTQLVA LAYEHGRVLA EHHREDGVEI EVELPVAWAR RIAARLEEQA DS // ID B1KHU7_SHEWM Unreviewed; 432 AA. AC B1KHU7; DT 29-APR-2008, integrated into UniProtKB/TrEMBL. DT 29-APR-2008, sequence version 1. DT 30-AUG-2017, entry version 72. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Swoo_4169 {ECO:0000313|EMBL:ACA88425.1}; OS Shewanella woodyi (strain ATCC 51908 / MS32). OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales; OC Shewanellaceae; Shewanella. OX NCBI_TaxID=392500 {ECO:0000313|EMBL:ACA88425.1, ECO:0000313|Proteomes:UP000002168}; RN [1] {ECO:0000313|EMBL:ACA88425.1, ECO:0000313|Proteomes:UP000002168} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51908 / MS32 {ECO:0000313|Proteomes:UP000002168}; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., RA Tice H., Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T., RA Detter J.C., Han C., Kuske C.R., Schmutz J., Larimer F., Land M., RA Hauser L., Kyrpides N., Lykidis A., Zhao J.-S., Richardson P.; RT "Complete sequence of Shewanella woodyi ATCC 51908."; RL Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000961; ACA88425.1; -; Genomic_DNA. DR RefSeq; WP_012326754.1; NC_010506.1. DR ProteinModelPortal; B1KHU7; -. DR STRING; 392500.Swoo_4169; -. DR EnsemblBacteria; ACA88425; ACA88425; Swoo_4169. DR KEGG; swd:Swoo_4169; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000002168; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000002168}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000002168}. FT DOMAIN 198 364 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 432 AA; 48454 MW; 5885EA2655F98B85 CRC64; MFDRYEAGEN AVLVHIDFSD EDSREDLVEL QLLVESAGAQ SVGVITGSRR SPDRKFFVGS GKADELAAMV AATEANVVIF NHALSPAQER NLEMVCQCRV LDRTTLILDI FAQRARTYEG KLQVELAQLR HMSTRLIRGW THLERQKGGI GMRGPGETQL ETDRRLLRGR ISNINKRLAK VDKQREQSRR ARRRSDLATV SLVGYTNAGK STLFNSLTTS DVYAADQLFA TLDPTLRKLD LDDGSIILAD TVGFIRHLPH DLVAAFKATL QETREADLLL HIVDCHDENM GDNFEQVQLV LKEIGAEDIP QLIVCNKIDL LDEVNPKIDY DDEGVPIRVW VSAQKQQGLV LLKEAINSIV GKTTLSLNLE IPATAGHYLG QLYRLDVIQQ KEYDDLGNCI LSVRILEADW RRLVKQSEGE LETFVVEHSA VE // ID B1L6F4_KORCO Unreviewed; 364 AA. AC B1L6F4; DT 29-APR-2008, integrated into UniProtKB/TrEMBL. DT 29-APR-2008, sequence version 1. DT 07-JUN-2017, entry version 61. DE SubName: Full=Small GTP-binding protein {ECO:0000313|EMBL:ACB08033.1}; GN OrderedLocusNames=Kcr_1287 {ECO:0000313|EMBL:ACB08033.1}; OS Korarchaeum cryptofilum (strain OPF8). OC Archaea; Candidatus Korarchaeota; Candidatus Korarchaeum. OX NCBI_TaxID=374847 {ECO:0000313|EMBL:ACB08033.1, ECO:0000313|Proteomes:UP000001686}; RN [1] {ECO:0000313|EMBL:ACB08033.1, ECO:0000313|Proteomes:UP000001686} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=OPF8 {ECO:0000313|Proteomes:UP000001686}; RX PubMed=18535141; DOI=10.1073/pnas.0801980105; RA Elkins J.G., Podar M., Graham D.E., Makarova K.S., Wolf Y., Randau L., RA Hedlund B.P., Brochier-Armanet C., Kunin V., Anderson I., Lapidus A., RA Goltsman E., Barry K., Koonin E.V., Hugenholtz P., Kyrpides N., RA Wanner G., Richardson P., Keller M., Stetter K.O.; RT "A korarchaeal genome reveals new insights into the evolution of the RT Archaea."; RL Proc. Natl. Acad. Sci. U.S.A. 105:8102-8107(2008). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000968; ACB08033.1; -; Genomic_DNA. DR RefSeq; WP_012309930.1; NC_010482.1. DR ProteinModelPortal; B1L6F4; -. DR STRING; 374847.Kcr_1287; -. DR EnsemblBacteria; ACB08033; ACB08033; Kcr_1287. DR GeneID; 6094564; -. DR KEGG; kcr:Kcr_1287; -. DR eggNOG; arCOG00353; Archaea. DR eggNOG; COG2262; LUCA. DR InParanoid; B1L6F4; -. DR KO; K03665; -. DR OMA; FNNHAHV; -. DR OrthoDB; POG093Z07D6; -. DR Proteomes; UP000001686; Chromosome. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR GO; GO:0043022; F:ribosome binding; IBA:GO_Central. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 4: Predicted; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000001686}; KW Reference proteome {ECO:0000313|Proteomes:UP000001686}. FT DOMAIN 193 361 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 159 186 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 364 AA; 41690 MW; CF6CC62820032803 CRC64; MLKAITGMVK TDVHDHYLYK IKMGELESLL DALGYRIVER IIQVREKESV DFVFGKGKID EIKDRVRKLD PDVFVLYNNI TSKQKWNLER ALGVEVIDRY DVTLMIFREA ASDILSKLQI ELASLEKHFP YVKLSASIKY KRMKAGFKGG GEYAYHKQIR AMQKRIKILN DKIEKLSRQK ELEILKRIDD GAKIAVLTGY YNAGKTSIFN ALTGFNKPVS DKPFTTLSSK YAGIEGEKVY LVDTIGFVID LDPRLIASFK LNLLDIKYSN KQILVIDISD RDELLKIKLK EDLRILKELG KREESMIIAA NKADLVGDSD MRRKEELIVD IAGKDVPLIP VSTVDGRGLR ELVRTMMEEL ELIR // ID B1M598_METRJ Unreviewed; 470 AA. AC B1M598; DT 29-APR-2008, integrated into UniProtKB/TrEMBL. DT 29-APR-2008, sequence version 1. DT 07-JUN-2017, entry version 60. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Mrad2831_1494 {ECO:0000313|EMBL:ACB23489.1}; OS Methylobacterium radiotolerans (strain ATCC 27329 / DSM 1819 / JCM OS 2831). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Methylobacteriaceae; Methylobacterium. OX NCBI_TaxID=426355 {ECO:0000313|EMBL:ACB23489.1, ECO:0000313|Proteomes:UP000006589}; RN [1] {ECO:0000313|EMBL:ACB23489.1, ECO:0000313|Proteomes:UP000006589} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 27329 / DSM 1819 / JCM 2831 RC {ECO:0000313|Proteomes:UP000006589}; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., RA Tice H., Bruce D., Goodwin L., Pitluck S., Kiss H., Brettin T., RA Detter J.C., Han C., Kuske C.R., Schmutz J., Larimer F., Land M., RA Hauser L., Kyrpides N., Mikhailova N., Marx C.J., Richardson P.; RT "Complete sequence of chromosome of Methylobacterium radiotolerans JCM RT 2831."; RL Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001001; ACB23489.1; -; Genomic_DNA. DR RefSeq; WP_012318477.1; NC_010505.1. DR ProteinModelPortal; B1M598; -. DR STRING; 426355.Mrad2831_1494; -. DR EnsemblBacteria; ACB23489; ACB23489; Mrad2831_1494. DR GeneID; 6137516; -. DR KEGG; mrd:Mrad2831_1494; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000006589; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000006589}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000006589}. FT DOMAIN 229 406 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 470 AA; 50896 MW; B7ED287C752DB119 CRC64; MTETLTSGEA RLQAQAAPEG EIAAATHTLV IGPYLARGAA GAGPGPAAPS RSVEARLDEA TGLAAAIELD VVESLAISLP RIRPSTYLGK GRVEEIAGLI RAREIGLVVM DCALSPVQQR NLEKAWGAKV IDRTGLILEI FGRRASTREG TLQVEHAHLA YQKSRLVRSW THLERQRGGF GFLGGPGETQ IEADRRMIQE RMTRIERDLD AVVRTRGLHR QSRARVPYPI VALVGYTNAG KSSLFNALTR AEVTAKDMLF ATLDPTARAT KLPHGETVIL SDTVGFISDL PTPLIAAFRA TLEDAIEADV LLHVRDVSHV DSEAQAEDVG AVLRELGIET SADRIIEVWN KADLLDDDER TRLLNLSGQA RARNDRDSAA PVLVSALTGE GLAALTSRIE ARVGRNRASF AVALPPEDGA ALNWLYENAE ILDRRSEADG TLHLAIRIAP EKEPRFLNRF AAARRLGRGG // ID B1MCZ9_MYCA9 Unreviewed; 464 AA. AC B1MCZ9; DT 29-APR-2008, integrated into UniProtKB/TrEMBL. DT 29-APR-2008, sequence version 1. DT 07-JUN-2017, entry version 64. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=MAB_3042c {ECO:0000313|EMBL:CAM63120.1}; OS Mycobacterium abscessus (strain ATCC 19977 / DSM 44196 / CIP 104536 / OS JCM 13569 / NCTC 13031 / TMC 1543). OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae; OC Mycobacterium; Mycobacterium abscessus. OX NCBI_TaxID=561007 {ECO:0000313|EMBL:CAM63120.1, ECO:0000313|Proteomes:UP000007137}; RN [1] {ECO:0000313|EMBL:CAM63120.1, ECO:0000313|Proteomes:UP000007137} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 19977 / DSM 44196 / CIP 104536 / JCM 13569 / NCTC 13031 / RC TMC 1543 {ECO:0000313|Proteomes:UP000007137}; RX PubMed=19543527; DOI=10.1371/journal.pone.0005660; RA Ripoll F., Pasek S., Schenowitz C., Dossat C., Barbe V., Rottman M., RA Macheras E., Heym B., Herrmann J.L., Daffe M., Brosch R., Risler J.L., RA Gaillard J.L.; RT "Non mycobacterial virulence genes in the genome of the emerging RT pathogen Mycobacterium abscessus."; RL PLoS ONE 4:E5660-E5660(2009). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CU458896; CAM63120.1; -; Genomic_DNA. DR ProteinModelPortal; B1MCZ9; -. DR STRING; 561007.MAB_3042c; -. DR EnsemblBacteria; CAM63120; CAM63120; MAB_3042c. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR OMA; HPATYIG; -. DR Proteomes; UP000007137; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000007137}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000007137}. FT DOMAIN 244 413 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 203 237 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 464 AA; 49837 MW; D9E1829FAB4DC4D0 CRC64; MRTTYETPTD GELALEDRAA LKRVAGLSTE LADVTEVEYR QLRLERVVLV GVWTEGTSQE AEASMAELAA LAETAGSEVL EGLIQRRQKP DPATYIGSGK AIELREIVLA TGADTVICDG ELSPAQLVAL EKAVKVKVID RTALILDIFA QHATSREGKA QVSLAQMEYM LPRLRGWGES MSRQAGGRAG GAGGGVGTRG PGETKIETDR RRIRERMSKL RREIRDMKKV RDTKRSRRLE SDVPSVAIVG YTNAGKSSLL NAITGAGVLV QDALFATLEP TTRRGTFDDG REFVITDTVG FVRHLPTQLV EAFRSTLEEV ADADLLVHVV DGSDMAPLAQ IEAVRTVIGE VVADHDASAA PELLVINKVD AAGDLALAQL RRALPKALFV SAHTGEGIAT LREAIAEAVP RGDVPVDVVI PYERGDLVAR IHTEGQVQST EHLADGTRVV GRVPRALAAV LTAL // ID B1MVY0_LEUCK Unreviewed; 432 AA. AC B1MVY0; DT 29-APR-2008, integrated into UniProtKB/TrEMBL. DT 29-APR-2008, sequence version 1. DT 07-JUN-2017, entry version 61. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=LCK_01561 {ECO:0000313|EMBL:ACA83384.1}; OS Leuconostoc citreum (strain KM20). OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Leuconostocaceae; OC Leuconostoc. OX NCBI_TaxID=349519 {ECO:0000313|EMBL:ACA83384.1, ECO:0000313|Proteomes:UP000002166}; RN [1] {ECO:0000313|EMBL:ACA83384.1, ECO:0000313|Proteomes:UP000002166} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=KM20 {ECO:0000313|EMBL:ACA83384.1, RC ECO:0000313|Proteomes:UP000002166}; RX PubMed=18281406; DOI=10.1128/JB.01862-07; RA Kim J.F., Jeong H., Lee J.-S., Choi S.-H., Ha M., Hur C.-G., RA Kim J.-S., Lee S., Park H.-S., Park Y.-H., Oh T.K.; RT "Complete genome sequence of Leuconostoc citreum KM20."; RL J. Bacteriol. 190:3093-3094(2008). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; DQ489736; ACA83384.1; -; Genomic_DNA. DR RefSeq; WP_004904430.1; NC_010471.1. DR ProteinModelPortal; B1MVY0; -. DR STRING; 349519.LCK_01561; -. DR EnsemblBacteria; ACA83384; ACA83384; LCK_01561. DR KEGG; lci:LCK_01561; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; FNNHAHV; -. DR Proteomes; UP000002166; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000002166}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000002166}. FT DOMAIN 206 379 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 432 AA; 47823 MW; 552D1E5694AA1251 CRC64; MTEQHVTNQG QRRVFLIGLS TNASNIDYEL EELANLAKAN QLIPEIIFSQ KLERPNPATY FGKGKVDELA EAVKTYDVDM IVANDELSPS QIRNLEKVTQ ATVLDRTGLI LDIFAQRAQT KAAKLQVQLA RLQYQLPRLR TSMSVSLDQQ TGAGGGGFTS RGSGETKLEE SRRRITSQMV HIRQELADLS KGEDTRSARR TANNLPNVAL VGYTNAGKST LMNRLLARFG IGAESDDTKQ VFEKDMLFAT LNTTVRQLTL PDKTQFLLSD TVGFVSKLPH NLVAAFKSTL QEAAQADLLL QVVDISDPHY KDMMTTTENT LREVGVTNIP MVTVYNKADK TTLNYPDVSG ENAITLSALE AASQDALITL IQKHVFKDNE TVTLHIPFDQ GAVQAKLAAN HTFIAENYDD SGTLLTVELS QLELEQFKKY II // ID B1VDE3_CORU7 Unreviewed; 506 AA. AC B1VDE3; DT 20-MAY-2008, integrated into UniProtKB/TrEMBL. DT 20-MAY-2008, sequence version 1. DT 07-JUN-2017, entry version 71. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=cu0881 {ECO:0000313|EMBL:CAQ04841.1}; OS Corynebacterium urealyticum (strain ATCC 43042 / DSM 7109). OC Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae; OC Corynebacterium. OX NCBI_TaxID=504474 {ECO:0000313|EMBL:CAQ04841.1, ECO:0000313|Proteomes:UP000001727}; RN [1] {ECO:0000313|EMBL:CAQ04841.1, ECO:0000313|Proteomes:UP000001727} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43042 / DSM 7109 {ECO:0000313|Proteomes:UP000001727}; RX PubMed=18367281; DOI=10.1016/j.jbiotec.2008.02.009; RA Tauch A., Trost E., Tilker A., Ludewig U., Schneiker S., Goesmann A., RA Arnold W., Bekel T., Brinkrolf K., Brune I., Goetker S., RA Kalinowski J., Kamp P.-B., Lobo F.P., Viehoever P., Weisshaar B., RA Soriano F., Droege M., Puehler A.; RT "The lifestyle of Corynebacterium urealyticum derived from its RT complete genome sequence established by pyrosequencing."; RL J. Biotechnol. 136:11-21(2008). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AM942444; CAQ04841.1; -; Genomic_DNA. DR RefSeq; WP_012360130.1; NC_010545.1. DR ProteinModelPortal; B1VDE3; -. DR STRING; 504474.cur_0881; -. DR EnsemblBacteria; CAQ04841; CAQ04841; cu0881. DR KEGG; cur:cu0881; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000001727; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000001727}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000001727}. FT DOMAIN 268 437 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 227 261 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 506 AA; 55076 MW; F33157F3F3867722 CRC64; MASNSDNVVD LFSDSSEGED FDLESQQSPT IGELDLEARS SLRRLTRGVS SYTDDQSEIT EVEYRQLRLE KVILVGVWTE GTIAQIEASL EELVALAETA GSEVLETVYQ KRDKPDPGTY IGRGKVSELA EIIQSTGADT VICDGELSPG QMIALENALN AKVIDRTMLI LDIFAQHAKS REGKAQVSLA QMEYLINRVR GWGTSLSRQT GGRAGSNGGV GLRGPGETKI EADRRRLRAE MARLRKEIAA MKTSRDTKRQ RRDASAVPQV AIAGYTNAGK SSLINALTGA GVLVEDALFA TLDPTTRRAE LADGRSVIFS DTVGFVRHLP TQLVEAFRST LEEVMAADVV LHVVDGSDPF PLEQIRSVNT VISEIVAESG QDAPPEIMVV NKIDKADPLV LAELRHKLND VVFVSAHTGE GIDELETRLE LFLNSLDETG VFAVPFDRGD VVSRIHDLGT VTQEEYDATG TVLTARVPKK LARELDAFRV TDREHDDLDV DGAATS // ID B1VXT7_STRGG Unreviewed; 506 AA. AC B1VXT7; DT 20-MAY-2008, integrated into UniProtKB/TrEMBL. DT 20-MAY-2008, sequence version 1. DT 07-JUN-2017, entry version 67. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=SGR_1724 {ECO:0000313|EMBL:BAG18553.1}; OS Streptomyces griseus subsp. griseus (strain JCM 4626 / NBRC 13350). OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae; OC Streptomyces. OX NCBI_TaxID=455632 {ECO:0000313|EMBL:BAG18553.1, ECO:0000313|Proteomes:UP000001685}; RN [1] {ECO:0000313|EMBL:BAG18553.1, ECO:0000313|Proteomes:UP000001685} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=JCM 4626 / NBRC 13350 {ECO:0000313|Proteomes:UP000001685}; RX PubMed=18375553; DOI=10.1128/JB.00204-08; RA Ohnishi Y., Ishikawa J., Hara H., Suzuki H., Ikenoya M., Ikeda H., RA Yamashita A., Hattori M., Horinouchi S.; RT "Genome sequence of the streptomycin-producing microorganism RT Streptomyces griseus IFO 13350."; RL J. Bacteriol. 190:4050-4060(2008). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AP009493; BAG18553.1; -; Genomic_DNA. DR RefSeq; WP_012378736.1; NC_010572.1. DR ProteinModelPortal; B1VXT7; -. DR STRING; 455632.SGR_1724; -. DR EnsemblBacteria; BAG18553; BAG18553; SGR_1724. DR GeneID; 6213273; -. DR KEGG; sgr:SGR_1724; -. DR PATRIC; fig|455632.4.peg.1750; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR Proteomes; UP000001685; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 2. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000001685}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000001685}. FT DOMAIN 285 450 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 506 AA; 54965 MW; 0F6FA928E210D179 CRC64; MTSSSSLPQD AQDARSATEN TTESLTESLR ADALMEEDVA WSHEIDGARD GDQLDRSERA ALRRVAGLST ELEDVTEVEY RQLRLERVVL VGVWTSGTVR DAEISLAELA ALAETAGAQV LDAVYQRRDK PDPATYIGSG KALELRDIVL ESGADTVVCD GELSPGQLIH LEDVVKVKVV DRTALILDIF AQHAKSREGK AQVSLAQMQY MLPRLRGWGQ SLSRQMGGGG SSGGGGMATR GPGETKIETD RRRIREKMAK MRREIAEMKT GREIKRQERK RNKVPSVAIA GYTNAGKSSL LNRLTGAGVL VENALFATLD PTVRRAETPS GRVYTLADTV GFVRHLPHHL VEAFRSTMEE VGESDLILHV VDGSHPVPEE QLAAVREVIR DVGAVDVREI VVINKADAAD PLVLQRLLRN EKHAIAVSAR TGAGIDELLA LIDTELPRPS VEIEVLVPYI QGALVSRVHA EGEVLSEEHT AEGTLLKAQV HEELAAELGT FVPAAH // ID B1WVU1_CYAA5 Unreviewed; 530 AA. AC B1WVU1; DT 20-MAY-2008, integrated into UniProtKB/TrEMBL. DT 20-MAY-2008, sequence version 1. DT 07-JUN-2017, entry version 60. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:ACB50678.1}; GN OrderedLocusNames=cce_1328 {ECO:0000313|EMBL:ACB50678.1}; OS Cyanothece sp. (strain ATCC 51142). OC Bacteria; Cyanobacteria; Oscillatoriophycideae; Oscillatoriales; OC Cyanothecaceae; Cyanothece. OX NCBI_TaxID=43989 {ECO:0000313|EMBL:ACB50678.1, ECO:0000313|Proteomes:UP000001203}; RN [1] {ECO:0000313|EMBL:ACB50678.1, ECO:0000313|Proteomes:UP000001203} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51142 {ECO:0000313|EMBL:ACB50678.1, RC ECO:0000313|Proteomes:UP000001203}; RX PubMed=18812508; DOI=10.1073/pnas.0805418105; RA Welsh E.A., Liberton M., Stoeckel J., Loh T., Elvitigala T., Wang C., RA Wollam A., Fulton R.S., Clifton S.W., Jacobs J.M., Aurora R., RA Ghosh B.K., Sherman L.A., Smith R.D., Wilson R.K., Pakrasi H.B.; RT "The genome of Cyanothece 51142, a unicellular diazotrophic RT cyanobacterium important in the marine nitrogen cycle."; RL Proc. Natl. Acad. Sci. U.S.A. 105:15094-15099(2008). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000806; ACB50678.1; -; Genomic_DNA. DR ProteinModelPortal; B1WVU1; -. DR STRING; 43989.cce_1328; -. DR EnsemblBacteria; ACB50678; ACB50678; cce_1328. DR KEGG; cyt:cce_1328; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; EREVIIT; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000001203; Chromosome circular. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000001203}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000001203}. FT DOMAIN 355 525 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 314 351 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 530 AA; 58747 MW; E0DB26F95138E300 CRC64; MAAVSSDIGQ GVCAYVNRRG QVIRVGVGTP RQTQIPALEL PRYGAERLSG IRCIATQLKN DPPKESSLTA MVLQRLDTLV VLSVTSEGKM RRGGGATGYV KDAYIAHLLP ASEFNPNHTY YWTVSPPMTL ETLSEQDFLG LVEGLEAEFR REYVAQQVEG DHERVVIVGL QTGKMSDRTF AEELAEVERL VETAGGETVE TIQQKRSHPH PQTVVGKGKV EEIALRVQTL GANLVVFSID LSPAQVRNLE TQLGVKVIDR TEVILDIFAQ RAQSRAGKLQ VELAQLEYML PRLVGRGQAM SRLGGGIGTR GPGETKLETE RRSIQRRISR LQQEVNKLQS HRSRLRQQRQ KQEVPTIAIV GYTNAGKSTL INALTNAEVY TADQLFATLD PTTRRLSGVD SDTQQPYTFL LTDTVGFIHE LPPSLVDAFR ATLEEVTEAD ALLHLVDLSH PAWQHHIQSV MTILQEMPLV PGPILLVFNK IDTVDGETLR IAQEEYPLAV FISASQRLGL ETLRYKLSQL VQYALNNSSF // ID B1XJ06_SYNP2 Unreviewed; 534 AA. AC B1XJ06; DT 20-MAY-2008, integrated into UniProtKB/TrEMBL. DT 20-MAY-2008, sequence version 1. DT 07-JUN-2017, entry version 58. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=SYNPCC7002_A0944 {ECO:0000313|EMBL:ACA98948.1}; OS Synechococcus sp. (strain ATCC 27264 / PCC 7002 / PR-6) (Agmenellum OS quadruplicatum). OC Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; OC Synechococcus. OX NCBI_TaxID=32049 {ECO:0000313|EMBL:ACA98948.1, ECO:0000313|Proteomes:UP000001688}; RN [1] {ECO:0000313|Proteomes:UP000001688} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 27264 / PCC 7002 / PR-6 RC {ECO:0000313|Proteomes:UP000001688}; RA Li T., Zhao J., Zhao C., Liu Z., Zhao F., Marquardt J., Nomura C.T., RA Persson S., Detter J.C., Richardson P.M., Lanz C., Schuster S.C., RA Wang J., Li S., Huang X., Cai T., Yu Z., Luo J., Zhao J., Bryant D.A.; RT "Complete sequence of Synechococcus sp. PCC 7002."; RL Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000951; ACA98948.1; -; Genomic_DNA. DR ProteinModelPortal; B1XJ06; -. DR STRING; 32049.SYNPCC7002_A0944; -. DR EnsemblBacteria; ACA98948; ACA98948; SYNPCC7002_A0944. DR KEGG; syp:SYNPCC7002_A0944; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; EREVIIT; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000001688; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000001688}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000001688}. FT DOMAIN 366 534 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 325 362 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 534 AA; 59183 MW; E13F0222D7F08D87 CRC64; MPGDRLTTPE LAQRIAALST ELNQAVCVYL NRRGKVIRVG VGSPQQTQIP PLELPRYGAE RLSGIRCLTA SPKDEPPKES SLTSMVLQRL DALVSFTLTG TGTTKRGRGA AGYVKNVYVA HLLPQTHPSH AYWLVSESQA LEEVSQQDFL DLVEGLEAEF RREFTAQQVD QSHDRVILVG LQTSDIGDRP FQDRLTELAR LVDTAGGEVL LTLEQKRSTP HPQTVVGTGK VEEIALQVQT LGANLVVFDR DLSPAQGRNL ERQLGVKVCD RTEVILDIFA QRAQSRAGKL QVELAQLEYL LPRLVGRGQA MSRLGGGIGT RGPGETKLET ERRTIQSRLS RLQKEVDQLQ AHRSRMRSQR QRQDVPTFAI VGYTNAGKST LINALTNAEV YAADQLFATL DPTTRRLTLT DEAFQTQTIL LTDTVGFIHE LPPALVDAFR ATLEEVTEAD ALIHVVDLSH PAWQHQLESV EKILGEMPIM PAQALLVFNK LDQVSSEALQ EAKLRHPNAV YISASDRLGF ETLRQRLAQM LKQL // ID B1XXK7_LEPCP Unreviewed; 412 AA. AC B1XXK7; DT 20-MAY-2008, integrated into UniProtKB/TrEMBL. DT 20-MAY-2008, sequence version 1. DT 05-JUL-2017, entry version 62. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Lcho_2862 {ECO:0000313|EMBL:ACB35127.1}; OS Leptothrix cholodnii (strain ATCC 51168 / LMG 8142 / SP-6) (Leptothrix OS discophora (strain SP-6)). OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Leptothrix. OX NCBI_TaxID=395495 {ECO:0000313|EMBL:ACB35127.1, ECO:0000313|Proteomes:UP000001693}; RN [1] {ECO:0000313|EMBL:ACB35127.1, ECO:0000313|Proteomes:UP000001693} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51168 / LMG 8142 / SP-6 RC {ECO:0000313|Proteomes:UP000001693}; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., RA Tice H., Bruce D., Goodwin L., Pitluck S., Chertkov O., Brettin T., RA Detter J.C., Han C., Kuske C.R., Schmutz J., Larimer F., Land M., RA Hauser L., Kyrpides N., Lykidis A., Emerson D., Richardson P.; RT "Complete sequence of Leptothrix cholodnii SP-6."; RL Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001013; ACB35127.1; -; Genomic_DNA. DR ProteinModelPortal; B1XXK7; -. DR STRING; 395495.Lcho_2862; -. DR EnsemblBacteria; ACB35127; ACB35127; Lcho_2862. DR KEGG; lch:Lcho_2862; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000001693; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000001693}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000001693}. FT DOMAIN 201 375 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 412 AA; 45516 MW; F058552291124BDA CRC64; MTASDVTPRP RALLVGVDLG VGSSFDPTLD ELALLAESAG DEAVARLIAR RKAPDPALFV GSGKADEIKE LIALHQADCV IFDQAIGPAQ QRNLERHLGV EVLDRTGLIL EIFAARARSH EGKLQVELAR LQYLSTRLVR RWSHLERQRG GVGLRGGPGE TQIELDRRMI DVRIKSVKER LEKVKRQRGT QRKSRERHGT FRVSLVGYTN AGKSTLFNVL VKAQAYAADQ LFATLDTTTR QMYLEDARRS VSLSDTVGFI RDLPHSLVEA FQATLQESAD SDLLLHVVDA ASPTWLEQLH EVQRVLREIG AESVPQFLVF NKIDLLEDDA LPRVMCDQYE IEPGRVVSRF FISAAANEGL GALRRAIAQA SLDADARRGQ PLADVRFDPV PPDAEPMAPE ASNDVPAHPH EA // ID B1YMH3_EXIS2 Unreviewed; 413 AA. AC B1YMH3; DT 20-MAY-2008, integrated into UniProtKB/TrEMBL. DT 20-MAY-2008, sequence version 1. DT 07-JUN-2017, entry version 68. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Exig_1080 {ECO:0000313|EMBL:ACB60560.1}; OS Exiguobacterium sibiricum (strain DSM 17290 / JCM 13490 / 255-15). OC Bacteria; Firmicutes; Bacilli; Bacillales; OC Bacillales Family XII. Incertae Sedis; Exiguobacterium. OX NCBI_TaxID=262543 {ECO:0000313|EMBL:ACB60560.1, ECO:0000313|Proteomes:UP000001681}; RN [1] {ECO:0000313|Proteomes:UP000001681} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 17290 / JCM 13490 / 255-15 RC {ECO:0000313|Proteomes:UP000001681}; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., RA Tice H., Bruce D., Goodwin L., Pitluck S., Kiss H., Chertkov O., RA Monk C., Brettin T., Detter J.C., Han C., Kuske C.R., Schmutz J., RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., RA Vishnivetskaya T., Rodrigues D.F., Gilichinsky D., Tiedje J., RA Richardson P.; RT "Complete sequence of chromosome of Exiguobacterium sibiricum 255- RT 15."; RL Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001022; ACB60560.1; -; Genomic_DNA. DR RefSeq; WP_012369983.1; NC_010556.1. DR ProteinModelPortal; B1YMH3; -. DR STRING; 262543.Exig_1080; -. DR EnsemblBacteria; ACB60560; ACB60560; Exig_1080. DR GeneID; 31769234; -. DR KEGG; esi:Exig_1080; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000001681; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000001681}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000001681}. FT DOMAIN 199 357 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 413 AA; 46501 MW; 5F78CF4621386787 CRC64; MSERVIVVGC QLPGVPDHIY EESVAELEAL VTTAHAVVVG RLDQKRQSID RRTFIGKGKV EELVALAQEL EPDLIIFNAE VTPGQMKNIR IALEDPESIK LIDRTQLILD IFAGRAQSRE GKLQVELAQM SYLLPRLSGQ GTQLSRLGGG IGTRGPGESK LETDRRHIRR RVDEIKKQLE TSVAHRARYR ERRKENQTFQ IALVGYTNAG KSTIFNRLTN ADTYEKNELF ATLDPLTRQL DLPEGGQILL TDTVGFIQDL PTKLIAAFRS TLEEVLEADL ILHVIDASSE HYLNQMQTTN DVLDELGAGD IPQLEVFNKK DQLTHLFSGG KLLISALDPA DIDRLTVEIE KAISDILEYL EIRIPVHAFA HYNPAKEVMM NLTEQYEEDG SVTLKGYLRK DTRLYSTLKQ YEV // ID B2A049_OPITP Unreviewed; 425 AA. AC B2A049; DT 20-MAY-2008, integrated into UniProtKB/TrEMBL. DT 20-MAY-2008, sequence version 1. DT 07-JUN-2017, entry version 60. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Oter_4111 {ECO:0000313|EMBL:ACB77385.1}; OS Opitutus terrae (strain DSM 11246 / JCM 15787 / PB90-1). OC Bacteria; Verrucomicrobia; Opitutae; Opitutales; Opitutaceae; OC Opitutus. OX NCBI_TaxID=452637 {ECO:0000313|EMBL:ACB77385.1, ECO:0000313|Proteomes:UP000007013}; RN [1] {ECO:0000313|EMBL:ACB77385.1, ECO:0000313|Proteomes:UP000007013} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 11246 / JCM 15787 / PB90-1 RC {ECO:0000313|Proteomes:UP000007013}; RX PubMed=21398538; DOI=10.1128/JB.00228-11; RA van Passel M.W., Kant R., Palva A., Copeland A., Lucas S., Lapidus A., RA Glavina del Rio T., Pitluck S., Goltsman E., Clum A., Sun H., RA Schmutz J., Larimer F.W., Land M.L., Hauser L., Kyrpides N., RA Mikhailova N., Richardson P.P., Janssen P.H., de Vos W.M., Smidt H.; RT "Genome sequence of the verrucomicrobium Opitutus terrae PB90-1, an RT abundant inhabitant of rice paddy soil ecosystems."; RL J. Bacteriol. 193:2367-2368(2011). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001032; ACB77385.1; -; Genomic_DNA. DR RefSeq; WP_012376913.1; NC_010571.1. DR ProteinModelPortal; B2A049; -. DR STRING; 452637.Oter_4111; -. DR EnsemblBacteria; ACB77385; ACB77385; Oter_4111. DR KEGG; ote:Oter_4111; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000007013; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000007013}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000007013}. FT DOMAIN 205 370 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 164 191 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 425 AA; 46786 MW; 80A2F586C5FBADA4 CRC64; MAVFPTEKPS KLERAFLIGV QTSDMPAGEG TELLAELKEL VENLRLTVVS STLVKLRSPT PALLLGSGKA QELAALAKAD GADVIVFDEQ LSPAQQRNWE ELTGLAVIDR EEVILEVFAD RAHTREAVLQ VGLARMEYSL PRLTRAWTHL SRQRGKGALG GEGETQLEQD RRIVRDRIAH LKAELAEVVQ QRGVQRRRRL RVPVPTASIV GYTNAGKSSL LNALTGATVL AEDKLFATLD PTTRQLQLRG NQKLLVTDTV GFIRRLPHRL VEAFKATLEE VVVADFLIHV LDVANPDFEK HHATTLGVLQ ELGAADKTIL TVFNKVDIAA PEMLARARHL VPDGLFVSAR TRAGFDVLET RCVELIADSF GSTELLVPHD RFDVVARLHE LGDIQEQEHV DGAVRIKGRF PAAQSAYFAP FVVAK // ID B2A830_NATTJ Unreviewed; 435 AA. AC B2A830; DT 20-MAY-2008, integrated into UniProtKB/TrEMBL. DT 20-MAY-2008, sequence version 1. DT 07-JUN-2017, entry version 71. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Nther_2262 {ECO:0000313|EMBL:ACB85828.1}; OS Natranaerobius thermophilus (strain ATCC BAA-1301 / DSM 18059 / OS JW/NM-WN-LF). OC Bacteria; Firmicutes; Clostridia; Natranaerobiales; Natranaerobiaceae; OC Natranaerobius. OX NCBI_TaxID=457570 {ECO:0000313|EMBL:ACB85828.1, ECO:0000313|Proteomes:UP000001683}; RN [1] {ECO:0000313|EMBL:ACB85828.1, ECO:0000313|Proteomes:UP000001683} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-1301 / DSM 18059 / JW/NM-WN-LF RC {ECO:0000313|Proteomes:UP000001683}; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., RA Tice H., Bruce D., Goodwin L., Pitluck S., Chertkov O., Brettin T., RA Detter J.C., Han C., Kuske C.R., Schmutz J., Larimer F., Land M., RA Hauser L., Kyrpides N., Lykidis A., Mesbah N.M., Wiegel J.; RT "Complete sequence of chromosome of Natranaerobius thermophilus JW/NM- RT WN-LF."; RL Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001034; ACB85828.1; -; Genomic_DNA. DR ProteinModelPortal; B2A830; -. DR STRING; 457570.Nther_2262; -. DR EnsemblBacteria; ACB85828; ACB85828; Nther_2262. DR KEGG; nth:Nther_2262; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; FNNHAHV; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000001683; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000001683}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000001683}. FT DOMAIN 208 372 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 167 204 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 435 AA; 49866 MW; 261E9A360E3B9919 CRC64; MSNSFDGFDN RMEPKRAILV ALEQTDRNER FSTEESLEEL QRLADTAEIE CVTEIVQKRP KPHPGFFIGK GKAREIGLLL EELDCNMVIF DDELSPGQIR NLEDTLDTDV WDRTALILDI FYRRANSKEA KLQVELARLE YLLPRLVGRG SEMSRLAGGI GTRGRGEQKL EIDRRHLREQ IQEIRRKLAE VRKRREENRQ YRKKHNLPVV SLVGYTNAGK STLLSTLTGS KVTAKDELFN TLDPKLADMS MSSGSKALLS DTVGFINKLP HHLVAAFRAT LEEVEEADLI LHVIDASSPR MYEEIEAVEE VLSSLDLEGT PIIKVYNKTD LLQESEPLME SGFPKEVAIS ALKKDGLHRL RKAIQRYLES SWVRKEYIIP YHREDLKARL YEVGEVLDIE YKETVMEVYA RVPPHEDQRL EKDLAEIKGG NSRHE // ID B2FL27_STRMK Unreviewed; 436 AA. AC B2FL27; DT 10-JUN-2008, integrated into UniProtKB/TrEMBL. DT 10-JUN-2008, sequence version 1. DT 30-AUG-2017, entry version 70. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:CAQ45260.1}; GN OrderedLocusNames=Smlt1737 {ECO:0000313|EMBL:CAQ45260.1}; OS Stenotrophomonas maltophilia (strain K279a). OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales; OC Xanthomonadaceae; Stenotrophomonas; OC Stenotrophomonas maltophilia group. OX NCBI_TaxID=522373 {ECO:0000313|EMBL:CAQ45260.1, ECO:0000313|Proteomes:UP000008840}; RN [1] {ECO:0000313|EMBL:CAQ45260.1, ECO:0000313|Proteomes:UP000008840} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K279a {ECO:0000313|EMBL:CAQ45260.1, RC ECO:0000313|Proteomes:UP000008840}; RX PubMed=18419807; DOI=10.1186/gb-2008-9-4-r74; RA Crossman L.C., Gould V.C., Dow J.M., Vernikos G.S., Okazaki A., RA Sebaihia M., Saunders D., Arrowsmith C., Carver T., Peters N., RA Adlem E., Kerhornou A., Lord A., Murphy L., Seeger K., Squares R., RA Rutter S., Quail M.A., Rajandream M.A., Harris D., Churcher C., RA Bentley S.D., Parkhill J., Thomson N.R., Avison M.B.; RT "The complete genome, comparative and functional analysis of RT Stenotrophomonas maltophilia reveals an organism heavily shielded by RT drug resistance determinants."; RL Genome Biol. 9:R74.1-R74.13(2008). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AM743169; CAQ45260.1; -; Genomic_DNA. DR RefSeq; WP_005412934.1; NC_010943.1. DR ProteinModelPortal; B2FL27; -. DR STRING; 522373.Smlt1737; -. DR EnsemblBacteria; CAQ45260; CAQ45260; Smlt1737. DR GeneID; 6392613; -. DR KEGG; sml:Smlt1737; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR Proteomes; UP000008840; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000008840}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}. FT DOMAIN 198 368 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 157 191 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 436 AA; 48182 MW; 467F8C27FBC5A7EA CRC64; MFDRSKKGEH ALLIQPHFGK LEDDVLEEFG DLARSAGASI AATITARLDR PNPSTLIGSG KLDEIKAAAD ASGADLILVN HALSPGQERN LERFLERRVI DRTGLILDIF AQRAHSHEGK LQVELAQLRH LATRLVRGWT HLERQRGGSI GLRGPGETQL ETDRRLLQKR VEQLQKRLEK VEVQRTQMRR ARVRSELPRV ALVGYTNAGK STLFNAMTGA EAYAADQLFA TLDPTVRRIA VPGGNVVLAD TVGFVRDLPH DLVAAFRSTL SEAREADFLL HVVDAADPHR EERIAQVDEV LTAVGAGDLP QLLVFNKIDR IDGADVRHDG QDGIPDESRR ERVWISARDG QGLELLQAVL GKRLGLQHVT GELRLPPDAG RLRARLHQLE VIRSEQADED GWLLQVDLPI AEAEKLAASA DGAPIRALLP EKLPEW // ID B2GKG6_KOCRD Unreviewed; 552 AA. AC B2GKG6; DT 10-JUN-2008, integrated into UniProtKB/TrEMBL. DT 10-JUN-2008, sequence version 1. DT 07-JUN-2017, entry version 69. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:BAG29925.1}; GN OrderedLocusNames=KRH_15780 {ECO:0000313|EMBL:BAG29925.1}; OS Kocuria rhizophila (strain ATCC 9341 / DSM 348 / NBRC 103217 / OS DC2201). OC Bacteria; Actinobacteria; Micrococcales; Micrococcaceae; Kocuria. OX NCBI_TaxID=378753 {ECO:0000313|EMBL:BAG29925.1, ECO:0000313|Proteomes:UP000008838}; RN [1] {ECO:0000313|EMBL:BAG29925.1, ECO:0000313|Proteomes:UP000008838} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 9341 / DSM 348 / NBRC 103217 / DC2201 RC {ECO:0000313|Proteomes:UP000008838}; RX PubMed=18408034; DOI=10.1128/JB.01853-07; RA Takarada H., Sekine M., Kosugi H., Matsuo Y., Fujisawa T., Omata S., RA Kishi E., Shimizu A., Tsukatani N., Tanikawa S., Fujita N., RA Harayama S.; RT "Complete genome sequence of the soil actinomycete Kocuria RT rhizophila."; RL J. Bacteriol. 190:4139-4146(2008). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AP009152; BAG29925.1; -; Genomic_DNA. DR ProteinModelPortal; B2GKG6; -. DR STRING; 378753.KRH_15780; -. DR EnsemblBacteria; BAG29925; BAG29925; KRH_15780. DR KEGG; krh:KRH_15780; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000008838; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000008838}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000008838}. FT DOMAIN 317 482 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 552 AA; 60008 MW; 487EA4508FB91719 CRC64; MTDTSSHRNH ASDEPGRSGD LTGSELEDVV SRVLARARSR TEPVVTADGH VPEDDAAAPR AGHERLGRAR ELADEDDVHV PSDGDQQDLA ERHALRRVAG LSTELEDVTE VEYRQLRLER VVLAGLYSSG TLAEAENSLR ELAALAETAG SEVMDGMLQR RVNPDPGTYL GSGKALELKD VVAATGADTV IVDAELAPSQ RRALEDVVKV KVIDRTGLIL DIFAQHAKSK EGKAQVELAQ LEYMLPRLRG WGESLSRQAG GRAASGEGIG SRGPGETKIE LDRRRIRQRM AKLRREIAAM KPARETKRLN RRRNAVPSVA IAGYTNAGKS SLLNRLTDAG VLVENALFAT LDPTVRKAQT PDGIGYTLAD TVGFVRSLPT QLVEAFRSTL EEVADADVIV HVVDASHPDP EGQLKAVRDV LTDVGANDIP EIVALNKSDI ADPVVLARLR NHESPSVAVS ARTGEGIEEL RRMISAAIPR PNHDLDLLVP YVHGEVVSRL HAQDAEILST EHTPDGTRLH VRVREDLVED LQQYRSDRPQ PHDVGEQDTQ GA // ID B2HL17_MYCMM Unreviewed; 504 AA. AC B2HL17; DT 10-JUN-2008, integrated into UniProtKB/TrEMBL. DT 10-JUN-2008, sequence version 1. DT 07-JUN-2017, entry version 62. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:ACC40438.1}; GN OrderedLocusNames=MMAR_1988 {ECO:0000313|EMBL:ACC40438.1}; OS Mycobacterium marinum (strain ATCC BAA-535 / M). OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae; OC Mycobacterium. OX NCBI_TaxID=216594 {ECO:0000313|EMBL:ACC40438.1, ECO:0000313|Proteomes:UP000001190}; RN [1] {ECO:0000313|EMBL:ACC40438.1, ECO:0000313|Proteomes:UP000001190} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-535 / M {ECO:0000313|Proteomes:UP000001190}; RX PubMed=18403782; DOI=10.1101/gr.075069.107; RA Stinear T.P., Seemann T., Harrison P.F., Jenkin G.A., Davies J.K., RA Johnson P.D., Abdellah Z., Arrowsmith C., Chillingworth T., RA Churcher C., Clarke K., Cronin A., Davis P., Goodhead I., Holroyd N., RA Jagels K., Lord A., Moule S., Mungall K., Norbertczak H., Quail M.A., RA Rabbinowitsch E., Walker D., White B., Whitehead S., Small P.L., RA Brosch R., Ramakrishnan L., Fischbach M.A., Parkhill J., Cole S.T.; RT "Insights from the complete genome sequence of Mycobacterium marinum RT on the evolution of Mycobacterium tuberculosis."; RL Genome Res. 18:729-741(2008). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000854; ACC40438.1; -; Genomic_DNA. DR RefSeq; WP_012393773.1; NC_010612.1. DR ProteinModelPortal; B2HL17; -. DR STRING; 216594.MMAR_1988; -. DR EnsemblBacteria; ACC40438; ACC40438; MMAR_1988. DR KEGG; mmi:MMAR_1988; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000001190; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000001190}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000001190}. FT DOMAIN 256 444 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 215 249 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 504 AA; 53636 MW; 88C1573826492B72 CRC64; MTYSEFPDSV RRASQPAAEP SIGELALEDR SALRRVAGLS TELADVSEVE YRQLRLERVV LVGVWTEGTA ADNQASLAEL AALAETAGSQ VLEGLIQRRD RPDPSTYIGS GKAAELREVV VATGADTVIC DGELSPAQLT ALEKAVKVKV IDRTALILDI FAQHATSREG KAQVALAQME YMLPRLRGWG ESMSRQAGGR AGGSGGGVGL RGPGETKIET DRRRIRERMA KLRREIKAMK QARDTQRSRR LHSDVPSIAI VGYTNAGKSS LLNALTGAGV LVQDALFATL DPTTRRAEFD PDSNGARPFL FTDTVGFVRH LPTQLVEAFR STLEEVIDAD LLLHVVDGSD PNPLAQINAV RQVISEVIAD EATGGGEASD GRAGSAGAEA PQELLVVNKV DAAGDLALAE LRHALPGALF VSAHTGDGID VLWRKLAELA APTDTAVDVV IPYDRGDLVA RMHADGRVQQ AEHQPEGTRI RARVPGALAA TLREFAASPA GPGE // ID B2IB75_BEII9 Unreviewed; 466 AA. AC B2IB75; DT 10-JUN-2008, integrated into UniProtKB/TrEMBL. DT 10-JUN-2008, sequence version 1. DT 05-JUL-2017, entry version 61. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Bind_1526 {ECO:0000313|EMBL:ACB95159.1}; OS Beijerinckia indica subsp. indica (strain ATCC 9039 / DSM 1715 / NCIB OS 8712). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Beijerinckiaceae; Beijerinckia. OX NCBI_TaxID=395963 {ECO:0000313|EMBL:ACB95159.1, ECO:0000313|Proteomes:UP000001695}; RN [1] {ECO:0000313|Proteomes:UP000001695} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 9039 / DSM 1715 / NCIB 8712 RC {ECO:0000313|Proteomes:UP000001695}; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., RA Tice H., Bruce D., Goodwin L., Pitluck S., LaButti K., Schmutz J., RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., RA Dunfield P.F., Dedysh S.N., Liesack W., Saw J.H., Alam M., Chen Y., RA Murrell J.C., Richardson P.; RT "Complete sequence of chromosome of Beijerinckia indica subsp. indica RT ATCC 9039."; RL Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001016; ACB95159.1; -; Genomic_DNA. DR ProteinModelPortal; B2IB75; -. DR STRING; 395963.Bind_1526; -. DR EnsemblBacteria; ACB95159; ACB95159; Bind_1526. DR KEGG; bid:Bind_1526; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000001695; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000001695}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000001695}. FT DOMAIN 226 401 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 185 212 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 466 AA; 51389 MW; EAD94EB89D142EFA CRC64; MPGESNKGSP ALTRAAKTRA MVVGPYLNQR ATQPHGRSAV ALPEKAFRSP QARFDEVLGL AEALDLDIVD QRLLTLAEIK PSTFLGTGKV AELGEAIKAA EAELVIMDCA LSPVQQRNLE KALGAKVIDR TGLILEIFGR RARTREGSLQ VELAHLAYQK SRLVRSWTHL ERQRGGFGFL GGPGETQIEA DRRLLQERMT RLEQDLAGVK RTRGLHRKTR RDVPYPIIAL VGYTNAGKST LFNRLTEADV LAQNMLFATL DPTLRSLTLP HGAKVILSDT VGFISDLPTM LVSAFRATLE EVLEADLILH VRDIAHQDAE AQCQDVESVL AELGIDMADE QRILEVWNKA DLLDEEAQAA ALNNARRWKN AENQPILVSA LTGQGVATLE AEIEARLARG RLLFDITLDP ANGEGLHWLH EHTEVMHKSI DEDGTIHVSV RVAPERAEPI KRRFGAMLVE REGLTA // ID B2IZ42_NOSP7 Unreviewed; 530 AA. AC B2IZ42; DT 10-JUN-2008, integrated into UniProtKB/TrEMBL. DT 10-JUN-2008, sequence version 1. DT 07-JUN-2017, entry version 58. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Npun_F4800 {ECO:0000313|EMBL:ACC83149.1}; OS Nostoc punctiforme (strain ATCC 29133 / PCC 73102). OC Bacteria; Cyanobacteria; Nostocales; Nostocaceae; Nostoc. OX NCBI_TaxID=63737 {ECO:0000313|EMBL:ACC83149.1, ECO:0000313|Proteomes:UP000001191}; RN [1] {ECO:0000313|Proteomes:UP000001191} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29133 / PCC 73102 {ECO:0000313|Proteomes:UP000001191}; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., RA Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., RA Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E., RA Meeks J.C., Elhai J., Campbell E.L., Thiel T., Longmire J., Potts M., RA Atlas R.; RT "Complete sequence of chromosome of Nostoc punctiforme ATCC 29133."; RL Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001037; ACC83149.1; -; Genomic_DNA. DR ProteinModelPortal; B2IZ42; -. DR STRING; 63737.Npun_F4800; -. DR EnsemblBacteria; ACC83149; ACC83149; Npun_F4800. DR KEGG; npu:Npun_F4800; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; EREVIIT; -. DR OrthoDB; POG091H0464; -. DR PhylomeDB; B2IZ42; -. DR Proteomes; UP000001191; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000001191}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000001191}. FT DOMAIN 357 527 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 530 AA; 58859 MW; 244D0E81151780CD CRC64; MCAYINRRGQ VIRVGVGTPR QTQIPPMELP RYGAERLSGI RCIATHLKPE PPNEAALTAM ALQRLDALVV LNITGTGFTR RGGGATGYVK EAYLAHLIPQ ESRTLITSPA AFKVEESKIQ TPSWNISPPM DLDDLADQDL VDLVENLEAE FQREFIAQEV DADHDRVLIV GLMTSETTPL QFQDTLAELA RLVDTAGGDV LQTIQQKRSR VHPQTVVGEG KVQEIALTAQ TLGVNLVVFD RDLSPSQVRN LELQIGIRVV DRTEVILDIF AQRAQSRAGK LQVELAQLEY MQPRLAGRGR TMSRLGGGIG TRGPGETKLE TERRAIGQRI SRLQKEVTQL QAHRSRLRQR RQHREVPSVA LVGYTNAGKS TLLNALTNAE VYTADQLFAT LDPTTRRLVI PYGETNEHQE ILITDTVGFI HELPASLMDA FRATLEEVTE ADALLHLVDL SHPAWLRHIR SVREILAQMP ITPGPALVIF NKIDQANSET LALAREEFPL AVFISASQRL GLETLRHRLA QLIEYAVDSR // ID B2J4P0_NOSP7 Unreviewed; 562 AA. AC B2J4P0; DT 10-JUN-2008, integrated into UniProtKB/TrEMBL. DT 10-JUN-2008, sequence version 1. DT 07-JUN-2017, entry version 56. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Npun_F0224 {ECO:0000313|EMBL:ACC79012.1}; OS Nostoc punctiforme (strain ATCC 29133 / PCC 73102). OC Bacteria; Cyanobacteria; Nostocales; Nostocaceae; Nostoc. OX NCBI_TaxID=63737 {ECO:0000313|EMBL:ACC79012.1, ECO:0000313|Proteomes:UP000001191}; RN [1] {ECO:0000313|Proteomes:UP000001191} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29133 / PCC 73102 {ECO:0000313|Proteomes:UP000001191}; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., RA Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., RA Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E., RA Meeks J.C., Elhai J., Campbell E.L., Thiel T., Longmire J., Potts M., RA Atlas R.; RT "Complete sequence of chromosome of Nostoc punctiforme ATCC 29133."; RL Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001037; ACC79012.1; -; Genomic_DNA. DR RefSeq; WP_012407039.1; NC_010628.1. DR ProteinModelPortal; B2J4P0; -. DR STRING; 63737.Npun_F0224; -. DR EnsemblBacteria; ACC79012; ACC79012; Npun_F0224. DR KEGG; npu:Npun_F0224; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR OMA; WESHITS; -. DR OrthoDB; POG091H0464; -. DR PhylomeDB; B2J4P0; -. DR Proteomes; UP000001191; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000001191}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000001191}. FT DOMAIN 382 562 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 341 378 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 562 AA; 63518 MW; 7D4F943A6CD1FD7A CRC64; MQKIYGNVQG IKASQIKRLQ QLYEQNQPAD RFITPEFAQA LATISQQIHH PICCYLNRRG QVIRIAVGTP IQTQIPPEEL PRRSAERLSG IRCIATQVKS EPPDEAALIA MMRQRLDALV MLTAIDGKVK EAFLSYLFPD SESPWVISPP LSLDDLTEQE FDELVHEWER EIVDAGDGIF LSQEIVSDQD RVLLVGVQTE DISVQRFEDG LAELVRLVES AGGIVLDTMR QKRDRPHPQT VVGKGKIEEI TLLAQKQRAN LIVFDRDISA SQARNLEQEI GIRVVDRTEV ILDIFAQRAR TQEGKLQVEL AQLEYMLPRL RGRGQEMSRL GAGIGTRGPG ETKLETERRT IQRRINQLQQ EVNDLQAHRA RIRQQRQQQE IPVLALVGYT NAGKSTLLNV LTNAEVFTAD QLFATLDPTT RKVVITEPET QERRSILLTD TVGFIHELPP PLMDAFRATL EEVVEADAMI HVVDLSHPAW ESHITSVLEI LEEMPEIPEK SLIAFNKVDK VDSETLDRVQ QDYPEAVFIS ATQRLGLETL KMRSLQLIDE PVKAIAVPQN SY // ID B2JIU5_PARP8 Unreviewed; 414 AA. AC B2JIU5; DT 10-JUN-2008, integrated into UniProtKB/TrEMBL. DT 10-JUN-2008, sequence version 1. DT 30-AUG-2017, entry version 73. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Bphy_1414 {ECO:0000313|EMBL:ACC70596.1}; OS Paraburkholderia phymatum (strain DSM 17167 / CIP 108236 / LMG 21445 / OS STM815) (Burkholderia phymatum). OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Paraburkholderia. OX NCBI_TaxID=391038 {ECO:0000313|EMBL:ACC70596.1, ECO:0000313|Proteomes:UP000001192}; RN [1] {ECO:0000313|Proteomes:UP000001192} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 17167 / CIP 108236 / LMG 21445 / STM815 RC {ECO:0000313|Proteomes:UP000001192}; RX PubMed=25197461; DOI=10.4056/sigs.4861021; RA Moulin L., Klonowska A., Caroline B., Booth K., Vriezen J.A., RA Melkonian R., James E.K., Young J.P., Bena G., Hauser L., Land M., RA Kyrpides N., Bruce D., Chain P., Copeland A., Pitluck S., Woyke T., RA Lizotte-Waniewski M., Bristow J., Riley M.; RT "Complete genome sequence of Burkholderia phymatum STM815(T), a broad RT host range and efficient nitrogen-fixing symbiont of Mimosa species."; RL Stand. Genomic Sci. 9:763-774(2014). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001043; ACC70596.1; -; Genomic_DNA. DR RefSeq; WP_012400810.1; NC_010622.1. DR ProteinModelPortal; B2JIU5; -. DR STRING; 391038.Bphy_1414; -. DR EnsemblBacteria; ACC70596; ACC70596; Bphy_1414. DR GeneID; 27741103; -. DR KEGG; bph:Bphy_1414; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000001192; Chromosome 1. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000001192}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000001192}. FT DOMAIN 196 367 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 414 AA; 45458 MW; 7ADDBA8D9270A689 CRC64; MTSTNLINAA LVGIDFGKID FEASLEELSL LAQSAGAHPA VTLTGRRSSP DAAMFVGSGK AEELRLACEA NDVDIVIFNH ALAPAQQRNL ERTLNRRVVD RTSLILDIFA QRARSHEGKL QVELAQLQYL ATRLVRAWTH LERQKGGIGL RGPGETQLET DRRLIGERIK MLKGRLEKLG RQHGTQRRAR ARNRTMSVSL VGYTNAGKST LFNALTKAQA YAADQLFATL DTTSRRVYLG EEVGQIVVSD TVGFIRELPH QLVAAFRATL EETIHADLLL HVVDASSAVR LDQIDQVNDV LREIGADAIR QVLVFNKIDA VPELAARGDA VERDEYGNIS RVFLSARTGQ GLDTLRAAIA EIATAEQLPE PDGLLSEGDP RAAVIHQAQR DDAGEDYRDD RKIPDTGADP FQLH // ID B2KDR8_ELUMP Unreviewed; 415 AA. AC B2KDR8; DT 10-JUN-2008, integrated into UniProtKB/TrEMBL. DT 10-JUN-2008, sequence version 1. DT 07-JUN-2017, entry version 74. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Emin_1112 {ECO:0000313|EMBL:ACC98664.1}; OS Elusimicrobium minutum (strain Pei191). OC Bacteria; Elusimicrobia; Elusimicrobia; Elusimicrobiales; OC Elusimicrobiaceae; Elusimicrobium. OX NCBI_TaxID=445932 {ECO:0000313|EMBL:ACC98664.1, ECO:0000313|Proteomes:UP000001029}; RN [1] {ECO:0000313|EMBL:ACC98664.1, ECO:0000313|Proteomes:UP000001029} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Pei191 {ECO:0000313|EMBL:ACC98664.1, RC ECO:0000313|Proteomes:UP000001029}; RX PubMed=19270133; DOI=10.1128/AEM.02698-08; RA Herlemann D.P.R., Geissinger O., Ikeda-Ohtsubo W., Kunin V., Sun H., RA Lapidus A., Hugenholtz P., Brune A.; RT "Genomic analysis of 'Elusimicrobium minutum,' the first cultivated RT representative of the phylum 'Elusimicrobia' (formerly termite group RT 1)."; RL Appl. Environ. Microbiol. 75:2841-2849(2009). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001055; ACC98664.1; -; Genomic_DNA. DR RefSeq; WP_012415279.1; NC_010644.1. DR ProteinModelPortal; B2KDR8; -. DR STRING; 445932.Emin_1112; -. DR EnsemblBacteria; ACC98664; ACC98664; Emin_1112. DR KEGG; emi:Emin_1112; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000001029; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000001029}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000001029}. FT DOMAIN 196 362 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 155 189 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 415 AA; 46209 MW; D6F089933A38BADA CRC64; MEKVILVAAS LKGEKYSKES VAELERLAHT AGGSVYKTYE VLLNAYNPAT LIGKGKCEEI ALEVKANDIS AVIFNEEITP AQQKNLANII PAKIIDRTWL ILDIFASRAR TKEGELQVEL AQLKFLLPRL SGKGGALMQQ TGGRRGGMGT RGPGERKLEY DRRRLRVRIA KLEEEIEKVK KERGIRRARR AVVPLPQVAI VGYTNAGKST LLNTLTQETA VYADDKLFAT LDPTTRRVKM PGGGQILFTD TVGFIQKLPH NLVSAFRATL EEVSEADVIL HVKDASSKDI SEQSRTVFKI IKDLGAQNIP MAEVFNKCDL LPHYPLAALK NANPGAVFIS AKENKGIKEL LKKIEETLLF KWHLKTIRIP VSKAYLTGFV YENAMVKKRV ENKDGSLTLK IMITKGNYDK IKKEL // ID B2TML9_CLOBB Unreviewed; 605 AA. AC B2TML9; U4PIC1; DT 01-JUL-2008, integrated into UniProtKB/TrEMBL. DT 01-JUL-2008, sequence version 1. DT 30-AUG-2017, entry version 69. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=CLL_A1004 {ECO:0000313|EMBL:ACD23272.1}; OS Clostridium botulinum (strain Eklund 17B / Type B). OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=935198 {ECO:0000313|EMBL:ACD23272.1, ECO:0000313|Proteomes:UP000001195}; RN [1] {ECO:0000313|Proteomes:UP000001195} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Eklund 17B / Type B {ECO:0000313|Proteomes:UP000001195}; RA Brinkac L.M., Brown J.L., Bruce D., Detter C., Munk C., Smith L.A., RA Smith T.J., Sutton G., Brettin T.S.; RT "Complete sequence of Clostridium botulinum strain Eklund."; RL Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001056; ACD23272.1; -; Genomic_DNA. DR RefSeq; WP_012424096.1; NC_018648.1. DR ProteinModelPortal; B2TML9; -. DR EnsemblBacteria; ACD23272; ACD23272; CLL_A1004. DR GeneID; 19965568; -. DR KEGG; cbk:CLL_A1004; -. DR PATRIC; fig|935198.13.peg.953; -. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR Proteomes; UP000001195; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000001195}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000001195}. FT DOMAIN 365 548 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 605 AA; 68265 MW; EBFD587F567C2B4E CRC64; MIEGNIDGIR NSILSELEKI HSIRTSKDEV CNIEILNIIA KVSANIEREV SVAINRKGNV TSVAIGDSTS VEVPLIDISE KRLSGVRVIH THPNGYCNLS ALDVTALLKL KLDAIVSVAI TEEGEIRDFS LGLLRLYNNK LEYDENMNLS LEEITSINIL DKIKFIENLI KVNDVIEEIG EKAILVGSDT KESLEELEEL TKACNIPVLQ TVFQSRNKID PSFFIGRGKV LEIASIRQIE RANVIIFDDE LTGSQVRNLE AALGAKVIDR TTLILEIFAT RAKSKEAKIQ VELAQLKYRL SRLQGLGTIL SRTGGGIGTR GPGEKKLETD RRHIMETIYD LRKELKRIKK TREVQREKRN KESIPKVSLA GYTNAGKSTL RNVLCDLSAR KDTVGKEKVF EADMLFATLD TTTRALTLKN KGLITLTDTV GFVRKLPHDL VEAFKSTLEE VIFSDILCHV VDVSSETAIE QYKAVNEVLT ELEAIDKETI LVLNKIDKAT EEQINNFIEF IENDETNKEQ VIIKISAKEG INLEEFLSLI EEKLPYNYKK AEYLIPYDKS NMQSFLHRNG RVLEEDYRED GTFMIVEVDD EVYNKTKEYV LNVLS // ID B2U9V5_RALPJ Unreviewed; 417 AA. AC B2U9V5; DT 01-JUL-2008, integrated into UniProtKB/TrEMBL. DT 01-JUL-2008, sequence version 1. DT 07-JUN-2017, entry version 61. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Rpic_1065 {ECO:0000313|EMBL:ACD26213.1}; OS Ralstonia pickettii (strain 12J). OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Ralstonia. OX NCBI_TaxID=402626 {ECO:0000313|EMBL:ACD26213.1, ECO:0000313|Proteomes:UP000002566}; RN [1] {ECO:0000313|Proteomes:UP000002566} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=12J {ECO:0000313|Proteomes:UP000002566}; RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., RA Tice H., Bruce D., Goodwin L., Pitluck S., Meincke L., Brettin T., RA Detter J.C., Han C., Kuske C.R., Schmutz J., Larimer F., Land M., RA Hauser L., Kyrpides N., Mikhailova N., Marsh T., Richardson P.; RT "Complete sequence of chromosome 1 of Ralstonia pickettii 12J."; RL Submitted (MAY-2008) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001068; ACD26213.1; -; Genomic_DNA. DR RefSeq; WP_012435321.1; NC_010682.1. DR ProteinModelPortal; B2U9V5; -. DR STRING; 402626.Rpic_1065; -. DR EnsemblBacteria; ACD26213; ACD26213; Rpic_1065. DR GeneID; 6288145; -. DR KEGG; rpi:Rpic_1065; -. DR PATRIC; fig|402626.5.peg.2269; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR Proteomes; UP000002566; Chromosome 1. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000002566}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000002566}. FT DOMAIN 202 372 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 161 195 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 417 AA; 45871 MW; D5B15DA31F473C20 CRC64; MASHPTSSSE PTRAILVAVD FGKHDFQESL SELALLASTA GSEPLRAVTG KRTRPDAALF IGAGKAEEVK IAADEEDAEI VIFNHALSPA QQRNLERFFG RHVVDRTGLI LDIFSQRAQS HVGKVQVELA RVRYQAARLV RAWSHLERQK GGVGLRGGPG ERQLELDRRM LDERAKRLSS ELDKLQRQHD TQRRSRSRND AFSVSLVGYT NAGKSTLFNA LTKARAYAAN QLFATLDTTS RRLYLEGLGN VVLSDTVGFI RDLPTQLVAA FRATLEETVH ADVLLHVVDA ASTVKHEQME QVDRVLDEIN ASGIPQILVM NKIDAAEELR AAGPRIERDE TGAVRRVFVS AIEGTGLDLL REALVETAIR LREHPASHGG DFDPRFDTRR DSPPAHRDEL SQSLPSSGSS AKGDEEG // ID B2VAE6_SULSY Unreviewed; 372 AA. AC B2VAE6; DT 01-JUL-2008, integrated into UniProtKB/TrEMBL. DT 01-JUL-2008, sequence version 1. DT 07-JUN-2017, entry version 71. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=SYO3AOP1_1309 {ECO:0000313|EMBL:ACD66919.1}; OS Sulfurihydrogenibium sp. (strain YO3AOP1). OC Bacteria; Aquificae; Aquificales; Hydrogenothermaceae; OC Sulfurihydrogenibium. OX NCBI_TaxID=436114 {ECO:0000313|EMBL:ACD66919.1, ECO:0000313|Proteomes:UP000001201}; RN [1] {ECO:0000313|Proteomes:UP000001201} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=YO3AOP1 {ECO:0000313|Proteomes:UP000001201}; RX PubMed=19136599; DOI=10.1128/JB.01645-08; RA Reysenbach A.-L., Hamamura N., Podar M., Griffiths E., Ferreira S., RA Hochstein R., Heidelberg J., Johnson J., Mead D., Pohorille A., RA Sarmiento M., Schweighofer K., Seshadri R., Voytek M.A.; RT "Complete and draft genome sequences of six members of the RT Aquificales."; RL J. Bacteriol. 191:1992-1993(2009). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001080; ACD66919.1; -; Genomic_DNA. DR RefSeq; WP_012459978.1; NC_010730.1. DR ProteinModelPortal; B2VAE6; -. DR STRING; 436114.SYO3AOP1_1309; -. DR EnsemblBacteria; ACD66919; ACD66919; SYO3AOP1_1309. DR KEGG; sul:SYO3AOP1_1309; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000001201; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000001201}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000001201}. FT DOMAIN 194 360 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 159 189 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 372 AA; 42043 MW; EA28B4028B13A97E CRC64; MKAVIVAVNL NDKEEDFEYK IQELEGLVEA AGGTVAGKVY QKRESPDPAY FIGRGKVKEI AQLVEGIGAD TVVFNVNLSP VQISTLSKEL NVEVLDRTDL ILKIFLNNAR TKQAKLQVEL AYLQHQLPRV YGGKGKELSR IGGGMKTKGA GEKLGEIKTR TIKDRINKIK KQLKEIEKQR EEQRKSREDN PNILKVSLVG YTNAGKSSLL KRLTKRDVFI SDQLFATLDT KTSLIYFPDI KKKVLITDTV GFVEDMPSEI MDAFMTTLKE IEDADVILHV IDISDKNCMK KKTTVENVLK QLKLQDKPII TVFNKIDKVV PSKDLIEEDV MENTITISAE KGWNIDKLFD ILKKYAKQKE ENHGLCFLQN SQ // ID B3DXP8_METI4 Unreviewed; 432 AA. AC B3DXP8; DT 22-JUL-2008, integrated into UniProtKB/TrEMBL. DT 22-JUL-2008, sequence version 1. DT 07-JUN-2017, entry version 69. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:ACD82282.1}; GN OrderedLocusNames=Minf_0222 {ECO:0000313|EMBL:ACD82282.1}; OS Methylacidiphilum infernorum (isolate V4) (Methylokorus infernorum OS (strain V4)). OC Bacteria; Verrucomicrobia; Methylacidiphilae; Methylacidiphilales; OC Methylacidiphilaceae; Methylacidiphilum. OX NCBI_TaxID=481448 {ECO:0000313|EMBL:ACD82282.1, ECO:0000313|Proteomes:UP000009149}; RN [1] {ECO:0000313|EMBL:ACD82282.1, ECO:0000313|Proteomes:UP000009149} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Isolate V4 {ECO:0000313|Proteomes:UP000009149}; RX PubMed=18593465; DOI=10.1186/1745-6150-3-26; RA Hou S., Makarova K.S., Saw J.H., Senin P., Ly B.V., Zhou Z., Ren Y., RA Wang J., Galperin M.Y., Omelchenko M.V., Wolf Y.I., Yutin N., RA Koonin E.V., Stott M.B., Mountain B.W., Crowe M.A., Smirnova A.V., RA Dunfield P.F., Feng L., Wang L., Alam M.; RT "Complete genome sequence of the extremely acidophilic methanotroph RT isolate V4, Methylacidiphilum infernorum, a representative of the RT bacterial phylum Verrucomicrobia."; RL Biol. Direct 3:26-26(2008). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000975; ACD82282.1; -; Genomic_DNA. DR RefSeq; WP_012462564.1; NC_010794.1. DR ProteinModelPortal; B3DXP8; -. DR STRING; 481448.Minf_0222; -. DR EnsemblBacteria; ACD82282; ACD82282; Minf_0222. DR KEGG; min:Minf_0222; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000009149; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000009149}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Hydrolase {ECO:0000313|EMBL:ACD82282.1}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Protease {ECO:0000313|EMBL:ACD82282.1}. FT DOMAIN 200 366 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 159 186 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 432 AA; 48960 MW; B244ADC6A6679D79 CRC64; MIATVEEARL ERGILVGLDR GERDFEESFK ELAQLASSAG AVIVERLVQK MSSPTAPYYI GKGKAKEIAE ICRQKKVSFV LFNEELSPIQ CRNLSSLFGC KVLDRTQLIL DIFAQRAKTR EGKLQIELAQ LLYLLPRLTR LWTHLSRQTG GIGTRGPGET QLEVDRRRIL EKIHRLKKEL EEVKKTRFIQ RSSRQKFPWP TACLVGYTNA GKSTLFNRLT NAHVLVEDKL FATLDPTIRL FEFSGGYKIF LSDTVGFIQK LPHHLIESFK ATLEEVTEAD LLIHLVDVSH PWAETQINEV NKVLEQIGAI HKPTILVWNK IDLVNTSGLI KRRIEEYPGS VPISAATGFG CENLLVKIEE WLKSQRRFLS LKLPLERTDI VAKLHRIGSG IVTDYQPDGI WVYGWIPLSL SSFLEQFDGA AGVYRNGISE SH // ID B3E8E4_GEOLS Unreviewed; 560 AA. AC B3E8E4; DT 22-JUL-2008, integrated into UniProtKB/TrEMBL. DT 22-JUL-2008, sequence version 1. DT 07-JUN-2017, entry version 69. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Glov_2913 {ECO:0000313|EMBL:ACD96620.1}; OS Geobacter lovleyi (strain ATCC BAA-1151 / DSM 17278 / SZ). OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfuromonadales; OC Geobacteraceae; Geobacter. OX NCBI_TaxID=398767 {ECO:0000313|EMBL:ACD96620.1, ECO:0000313|Proteomes:UP000002420}; RN [1] {ECO:0000313|EMBL:ACD96620.1, ECO:0000313|Proteomes:UP000002420} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-1151 / DSM 17278 / SZ RC {ECO:0000313|Proteomes:UP000002420}; RG US DOE Joint Genome Institute; RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., RA Tice H., Bruce D., Goodwin L., Pitluck S., Chertkov O., Meincke L., RA Brettin T., Detter J.C., Han C., Tapia R., Kuske C.R., Schmutz J., RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Sung Y., RA Fletcher K.E., Ritalahti K.M., Loeffler F.E., Richardson P.; RT "Complete sequence of chromosome of Geobacter lovleyi SZ."; RL Submitted (MAY-2008) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001089; ACD96620.1; -; Genomic_DNA. DR ProteinModelPortal; B3E8E4; -. DR STRING; 398767.Glov_2913; -. DR EnsemblBacteria; ACD96620; ACD96620; Glov_2913. DR KEGG; glo:Glov_2913; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; EREVIIT; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000002420; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000002420}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000002420}. FT DOMAIN 376 549 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 335 369 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 560 AA; 62756 MW; 8672ACF6B8329EBE CRC64; MHELHGNLAG LKQSQIQAAE RLYRRRIPAD ELCSAELAGR LLELSLELRR QIGLLVNRQG AIELILIGTE KGLLIPDLKE YPLGRKRLRG LRLIHTHLKS EPLTEDDLTD LKLLRLDLIA ALCPLDGRRS IVHLAHLSTE PGGISVLPPQ LLEKAVDYGN DFISTLERSL DRAIQTEAPA QDGQERAILI SVRAGGERRE VDDSLAELQE LARTAGVQVL DSFIQLPRKL NPRTLMGEGK LQEVVIRALQ RGATLLIFDQ ELTPAQVRAI STMTELKVID RSQLILDIFA GRAKSRDGKV QVELAQLKYL LPRLTGRGVQ MSRLMGGIGG RGPGETKLEI DRRRIRDRIT ALERELQELS RDREQRRSRR VRSGVPIISI VGYTNAGKST LLNALTQSEI FTENLLFATL DTSSRRLRLP REREVIITDT VGFIRSLPAS LMGAFKATLE ELQDADLLLH LVDASNPRFE AQIAQVRTIL AELGLAEKPE LVVFNKTDQL EGLKRKDTIA FLRIAQAKRR HNAISISAVD RKSLAPLLDE LKRRFWPDAD DSFQTPTDIL // ID B3EDK4_CHLL2 Unreviewed; 434 AA. AC B3EDK4; DT 22-JUL-2008, integrated into UniProtKB/TrEMBL. DT 22-JUL-2008, sequence version 1. DT 07-JUN-2017, entry version 61. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Clim_1584 {ECO:0000313|EMBL:ACD90629.1}; OS Chlorobium limicola (strain DSM 245 / NBRC 103803 / 6330). OC Bacteria; Chlorobi; Chlorobia; Chlorobiales; Chlorobiaceae; OC Chlorobium/Pelodictyon group; Chlorobium. OX NCBI_TaxID=290315 {ECO:0000313|EMBL:ACD90629.1, ECO:0000313|Proteomes:UP000008841}; RN [1] {ECO:0000313|EMBL:ACD90629.1, ECO:0000313|Proteomes:UP000008841} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 245 / NBRC 103803 / 6330 RC {ECO:0000313|Proteomes:UP000008841}; RG US DOE Joint Genome Institute; RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., RA Tice H., Bruce D., Goodwin L., Pitluck S., Schmutz J., Larimer F., RA Land M., Hauser L., Kyrpides N., Ovchinnikova G., Zhao F., Li T., RA Liu Z., Overmann J., Bryant D.A., Richardson P.; RT "Complete sequence of Chlorobium limicola DSM 245."; RL Submitted (MAY-2008) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001097; ACD90629.1; -; Genomic_DNA. DR RefSeq; WP_012466503.1; NC_010803.1. DR ProteinModelPortal; B3EDK4; -. DR STRING; 290315.Clim_1584; -. DR EnsemblBacteria; ACD90629; ACD90629; Clim_1584. DR KEGG; cli:Clim_1584; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000008841; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000008841}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000008841}. FT DOMAIN 202 369 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 434 AA; 48801 MW; EDADCF97F117EE16 CRC64; MNTFIFNRPR ERAVLIGLCS PPEVTRAQIE EYLEELAFLA DTAGADVFAT VIQERKLPDH ASYIGSGKVD ELSQLVRDEV IDIVIVDDDL SPVQARNLEK AFECKVIDRT GLILQIFAIR AKSARAKMQV ELAQLEYMLP RLSGQWTHLS KQKGGIGTKG PGETQIETDR RLVRNRIASL KRKLRAVSLQ HDTQTRGRRS IPGVALVGYT NAGKSTLMNA LCPEAEAFAE NRLFATLDTK TRRLELKINK LVLLSDTVGF IRKLPHDLVE SFKSTLDEVL QADFLLHVID ASHPGFAEQM QVVRQTLKEI GVGHDNIIDV FNKIDALPDS GSLRELRVNY PDAVFVSAAR EINLSALKDA IGDHLAQEFR ERSIRTHVSN YKLIGYLYDH AEVIEKHYLD EEILLTFRVH KNSLKHMEAL IRASQNTAYA TADL // ID B3EPY2_CHLPB Unreviewed; 433 AA. AC B3EPY2; DT 22-JUL-2008, integrated into UniProtKB/TrEMBL. DT 22-JUL-2008, sequence version 1. DT 07-JUN-2017, entry version 60. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Cphamn1_0970 {ECO:0000313|EMBL:ACE03914.1}; OS Chlorobium phaeobacteroides (strain BS1). OC Bacteria; Chlorobi; Chlorobia; Chlorobiales; Chlorobiaceae; OC Chlorobium/Pelodictyon group; Chlorobium. OX NCBI_TaxID=331678 {ECO:0000313|EMBL:ACE03914.1, ECO:0000313|Proteomes:UP000001228}; RN [1] {ECO:0000313|EMBL:ACE03914.1, ECO:0000313|Proteomes:UP000001228} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BS1 {ECO:0000313|EMBL:ACE03914.1, RC ECO:0000313|Proteomes:UP000001228}; RG US DOE Joint Genome Institute; RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., RA Tice H., Bruce D., Goodwin L., Pitluck S., Schmutz J., Larimer F., RA Land M., Hauser L., Kyrpides N., Ovchinnikova G., Li T., Liu Z., RA Zhao F., Overmann J., Bryant D.A., Richardson P.; RT "Complete sequence of Chlorobium phaeobacteroides BS1."; RL Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001101; ACE03914.1; -; Genomic_DNA. DR RefSeq; WP_012474402.1; NC_010831.1. DR ProteinModelPortal; B3EPY2; -. DR STRING; 331678.Cphamn1_0970; -. DR EnsemblBacteria; ACE03914; ACE03914; Cphamn1_0970. DR KEGG; cpb:Cphamn1_0970; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000001228; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000001228}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000001228}. FT DOMAIN 203 370 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 433 AA; 49392 MW; 4D825ACF8B501F18 CRC64; MDTYTSSEVT KERALLVGVS SSPELTRSLV EEYLEELAFL ADTAGAEVVS SIIQDRKFKD PAWFLGKGKV EEIEHIVKGG LIDVVIFDEE LSPVQTRNLE RAFDCKVVDR TELILQIFAI RAQSSQAKMQ VELAQLEYLL PRLTRLWTHL SKQKGGIGTK GPGETQIETD RRLVRRRISF LKGKLKDVAL QHATQTKDRG RITRVALVGY TNAGKSTLMN RLCPEAEAYV EDRLFATLDT KTRRLELKIN KVVLLSDTVG FIRKLPHRLV ESFRSTLDEV LQADFLLHVI DTSHEGFEEQ MRVVLETLQE IGVQHGNIIN VFNKIDAVED KETLRSLRRK YPEALFVSAV RGINLNSLKE AVSAYIERDY KESTIRTHIS NYKLIGYLYD HAEVIEKKHE DEDVVLKYRA HYKDLKQIEA RIAASEKTNS HVA // ID B3ETK5_AMOA5 Unreviewed; 395 AA. AC B3ETK5; DT 22-JUL-2008, integrated into UniProtKB/TrEMBL. DT 22-JUL-2008, sequence version 1. DT 07-JUN-2017, entry version 72. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Aasi_1232 {ECO:0000313|EMBL:ACE06557.1}; OS Amoebophilus asiaticus (strain 5a2). OC Bacteria; Bacteroidetes; Cytophagia; Cytophagales; Amoebophilaceae; OC Candidatus Amoebophilus. OX NCBI_TaxID=452471 {ECO:0000313|EMBL:ACE06557.1, ECO:0000313|Proteomes:UP000001227}; RN [1] {ECO:0000313|EMBL:ACE06557.1, ECO:0000313|Proteomes:UP000001227} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=5a2 {ECO:0000313|EMBL:ACE06557.1, RC ECO:0000313|Proteomes:UP000001227}; RX PubMed=20023027; DOI=10.1128/JB.01379-09; RA Schmitz-Esser S., Tischler P., Arnold R., Montanaro J., Wagner M., RA Rattei T., Horn M.; RT "The genome of the amoeba symbiont 'Candidatus Amoebophilus asiaticus' RT reveals common mechanisms for host cell interaction among amoeba- RT associated bacteria."; RL J. Bacteriol. 192:1045-1057(2010). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001102; ACE06557.1; -; Genomic_DNA. DR RefSeq; WP_012473312.1; NC_010830.1. DR ProteinModelPortal; B3ETK5; -. DR STRING; 452471.Aasi_1232; -. DR EnsemblBacteria; ACE06557; ACE06557; Aasi_1232. DR KEGG; aas:Aasi_1232; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000001227; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000001227}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000001227}. FT DOMAIN 203 382 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 395 AA; 45236 MW; 2116E32CEB913AEA CRC64; MTAYIETATK QETAVLVSLA TPKQPLQKAK EYLAELSLLC YTLNIKPVST FIQNLDRPQT GTLIGKGKLE EIKTFIQTEE VDKVIFDEEL TPSQTRNLER ILERPILDRN SIILAIFAMR AKTRQAKIQV ELAQYQYLLP RLTKMWSHLS RQKGGFSGMR GPGEKELETD RRIVQDKISL LRKKLESINK QSITQRKTRQ DLVRVALVGY TNVGKSTLMH LLSKSDAYVE DKLFATITST VRRVVINHIP FLLTDTVGFI RKLPHTLIES FKSTLDEIRE ADILLHVVDA SHPACEEHIQ VVQQTLHEIG AEHIPAILVF NKMDQLEEEN SANGQQHTIT MEAISNKYAE QYGHQAIFIS AKQQKNIDIL KDMLYQQVLN KHLLIYPNYL KSDHQ // ID B3L4T6_PLAKH Unreviewed; 689 AA. AC B3L4T6; DT 02-SEP-2008, integrated into UniProtKB/TrEMBL. DT 02-SEP-2008, sequence version 1. DT 05-JUL-2017, entry version 49. DE SubName: Full=GTP-binding protein, putative {ECO:0000313|EMBL:CAQ39907.1}; GN ORFNames=PKH_091070 {ECO:0000313|EMBL:CAQ39907.1}; OS Plasmodium knowlesi (strain H). OC Eukaryota; Alveolata; Apicomplexa; Aconoidasida; Haemosporida; OC Plasmodiidae; Plasmodium; Plasmodium (Plasmodium). OX NCBI_TaxID=5851 {ECO:0000313|EMBL:CAQ39907.1, ECO:0000313|Proteomes:UP000031513}; RN [1] {ECO:0000313|EMBL:CAQ39907.1, ECO:0000313|Proteomes:UP000031513} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=H {ECO:0000313|EMBL:CAQ39907.1, RC ECO:0000313|Proteomes:UP000031513}; RA Pain A., Boehme U., Berry A.E., Mungall K., Finn R., Jackson A.P., RA Mourier T., Mistry J., Pasini E.M., Aslett M., Balasubrammaniam S., RA Borgwardt K., Brooks K., Carret C., Carver T.J., Cherevach I., RA Chillingworth T., Clarke T.G., Galinski M.R., Hall N., Harper D., RA Harris D., Hauser H., Ivens A., Janssen C.S., Keane T., Larke N., RA Lapp S., Marti M., Moule S., Meyer I.M., Ormond D., Peters N., RA Sanders M., Sanders S., Sergeant T.J., Simmonds M., Smith F., RA Squares R., Thurston S., Tivey A.R., Walker D., White B., RA Zuiderwijk E., Churcher C., Quail M.A., Cowman A.F., Turner C.M.R., RA Rajandream M.A., Kocken C.H.M., Thomas A.W., Newbold C.I., RA Barrell B.G., Berriman M.; RT "The genome of Plasmodium knowlesi strain H, a zoonotic malaria RT parasite with host range from monkey to man."; RL Nature 455:799-803(2008). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AM910991; CAQ39907.1; -; Genomic_DNA. DR RefSeq; XP_002259134.1; XM_002259098.1. DR STRING; 5850.PKH_091070; -. DR EnsemblProtists; CAQ39907; CAQ39907; PKH_091070. DR GeneID; 7320696; -. DR KEGG; pkn:PKH_091070; -. DR EuPathDB; PlasmoDB:PKNH_0911100; -. DR HOGENOM; HOG000282270; -. DR InParanoid; B3L4T6; -. DR Proteomes; UP000031513; Chromosome 9. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 4: Predicted; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000031513}; KW Reference proteome {ECO:0000313|Proteomes:UP000031513}. FT COILED 415 442 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 689 AA; 79089 MW; DF896EE0172F6683 CRC64; MLRWSTTLRI FPRTQKRSFT SGRKKEIIVL HPILKRTKNG SKSFDEIIYD AQEALGLARS AGFKVANGIS MPLGGWKFFK HSSGSKGEGD DLANNYREEN IFRDLRQLNE GIPCEGDANK VETCPTNEDT GTDALVDTPV DDVTSEEMSP QGDDLEKKIA ESIIIKTNRI DNKFYFGKGK LNELSIYFLK HPTPYVFINT VLSPEQFRNL DMLFNSLLRS YHDELKLRRE AQRGEDCLSV RASEINAEDD GSAEDRNGEE LTYIEMYNKW MERQAEREDQ EDGNFSDGEE EGVFLHDDVE DGDVPLYVEL FDRYSIILQI LKSRAKNNLS KLQLELARAN FIFNTYAEDN KSRMKYIKYI ENNVLGKSNF DYEEKYSRQN TFDVDKQIGK KKNYDNLGYT SSYIKSSETY KEYEKRIIQS LYAKLKKELE KCKNNNALQS SARKHKALIA VVGYTNVGKT KLINYLTNSN LKARNLLFQT LDNAYKSVKI SDGHSSIFID SIGFIQNIPF SLYESFKVTL EAIKNADVFI HVVDVCHPYR EQHKNCVIDT LQKIGIPSDF LKYNMIEVWN KVDKLPDDEI LNLYKTKPKN VLPISAKVGT NCDVLIKIIQ TMINRIKDVQ VLTLQFSALE AKERIPYLVK NFKVVPNSIS YSSDGSTTFI KLVENPRNLR KYYERFDKGE EGTSGGGTT // ID B3LZ12_DROAN Unreviewed; 523 AA. AC B3LZ12; DT 02-SEP-2008, integrated into UniProtKB/TrEMBL. DT 02-SEP-2008, sequence version 1. DT 30-AUG-2017, entry version 49. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EDV41886.1}; GN Name=Dana\GF17695 {ECO:0000313|EMBL:EDV41886.1}; GN ORFNames=Dana_GF17695 {ECO:0000313|EMBL:EDV41886.1}, GN GF17695 {ECO:0000313|FlyBase:FBgn0094713}; OS Drosophila ananassae (Fruit fly). OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; OC Pterygota; Neoptera; Holometabola; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila; Sophophora. OX NCBI_TaxID=7217 {ECO:0000313|EMBL:EDV41886.1, ECO:0000313|Proteomes:UP000007801}; RN [1] {ECO:0000313|EMBL:EDV41886.1, ECO:0000313|Proteomes:UP000007801} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Tucson 14024-0371.13 {ECO:0000313|Proteomes:UP000007801}; RX PubMed=17994087; DOI=10.1038/nature06341; RG Drosophila 12 Genomes Consortium; RA Clark A.G., Eisen M.B., Smith D.R., Bergman C.M., Oliver B., RA Markow T.A., Kaufman T.C., Kellis M., Gelbart W., Iyer V.N., RA Pollard D.A., Sackton T.B., Larracuente A.M., Singh N.D., Abad J.P., RA Abt D.N., Adryan B., Aguade M., Akashi H., Anderson W.W., RA Aquadro C.F., Ardell D.H., Arguello R., Artieri C.G., Barbash D.A., RA Barker D., Barsanti P., Batterham P., Batzoglou S., Begun D., RA Bhutkar A., Blanco E., Bosak S.A., Bradley R.K., Brand A.D., RA Brent M.R., Brooks A.N., Brown R.H., Butlin R.K., Caggese C., RA Calvi B.R., Bernardo de Carvalho A., Caspi A., Castrezana S., RA Celniker S.E., Chang J.L., Chapple C., Chatterji S., Chinwalla A., RA Civetta A., Clifton S.W., Comeron J.M., Costello J.C., Coyne J.A., RA Daub J., David R.G., Delcher A.L., Delehaunty K., Do C.B., Ebling H., RA Edwards K., Eickbush T., Evans J.D., Filipski A., Findeiss S., RA Freyhult E., Fulton L., Fulton R., Garcia A.C., Gardiner A., RA Garfield D.A., Garvin B.E., Gibson G., Gilbert D., Gnerre S., RA Godfrey J., Good R., Gotea V., Gravely B., Greenberg A.J., RA Griffiths-Jones S., Gross S., Guigo R., Gustafson E.A., Haerty W., RA Hahn M.W., Halligan D.L., Halpern A.L., Halter G.M., Han M.V., RA Heger A., Hillier L., Hinrichs A.S., Holmes I., Hoskins R.A., RA Hubisz M.J., Hultmark D., Huntley M.A., Jaffe D.B., Jagadeeshan S., RA Jeck W.R., Johnson J., Jones C.D., Jordan W.C., Karpen G.H., RA Kataoka E., Keightley P.D., Kheradpour P., Kirkness E.F., RA Koerich L.B., Kristiansen K., Kudrna D., Kulathinal R.J., Kumar S., RA Kwok R., Lander E., Langley C.H., Lapoint R., Lazzaro B.P., Lee S.J., RA Levesque L., Li R., Lin C.F., Lin M.F., Lindblad-Toh K., Llopart A., RA Long M., Low L., Lozovsky E., Lu J., Luo M., Machado C.A., RA Makalowski W., Marzo M., Matsuda M., Matzkin L., McAllister B., RA McBride C.S., McKernan B., McKernan K., Mendez-Lago M., Minx P., RA Mollenhauer M.U., Montooth K., Mount S.M., Mu X., Myers E., Negre B., RA Newfeld S., Nielsen R., Noor M.A., O'Grady P., Pachter L., RA Papaceit M., Parisi M.J., Parisi M., Parts L., Pedersen J.S., RA Pesole G., Phillippy A.M., Ponting C.P., Pop M., Porcelli D., RA Powell J.R., Prohaska S., Pruitt K., Puig M., Quesneville H., RA Ram K.R., Rand D., Rasmussen M.D., Reed L.K., Reenan R., Reily A., RA Remington K.A., Rieger T.T., Ritchie M.G., Robin C., Rogers Y.H., RA Rohde C., Rozas J., Rubenfield M.J., Ruiz A., Russo S., Salzberg S.L., RA Sanchez-Gracia A., Saranga D.J., Sato H., Schaeffer S.W., Schatz M.C., RA Schlenke T., Schwartz R., Segarra C., Singh R.S., Sirot L., Sirota M., RA Sisneros N.B., Smith C.D., Smith T.F., Spieth J., Stage D.E., RA Stark A., Stephan W., Strausberg R.L., Strempel S., Sturgill D., RA Sutton G., Sutton G.G., Tao W., Teichmann S., Tobari Y.N., RA Tomimura Y., Tsolas J.M., Valente V.L., Venter E., Venter J.C., RA Vicario S., Vieira F.G., Vilella A.J., Villasante A., Walenz B., RA Wang J., Wasserman M., Watts T., Wilson D., Wilson R.K., Wing R.A., RA Wolfner M.F., Wong A., Wong G.K., Wu C.I., Wu G., Yamamoto D., RA Yang H.P., Yang S.P., Yorke J.A., Yoshida K., Zdobnov E., Zhang P., RA Zhang Y., Zimin A.V., Baldwin J., Abdouelleil A., Abdulkadir J., RA Abebe A., Abera B., Abreu J., Acer S.C., Aftuck L., Alexander A., RA An P., Anderson E., Anderson S., Arachi H., Azer M., Bachantsang P., RA Barry A., Bayul T., Berlin A., Bessette D., Bloom T., Blye J., RA Boguslavskiy L., Bonnet C., Boukhgalter B., Bourzgui I., Brown A., RA Cahill P., Channer S., Cheshatsang Y., Chuda L., Citroen M., RA Collymore A., Cooke P., Costello M., D'Aco K., Daza R., De Haan G., RA DeGray S., DeMaso C., Dhargay N., Dooley K., Dooley E., Doricent M., RA Dorje P., Dorjee K., Dupes A., Elong R., Falk J., Farina A., Faro S., RA Ferguson D., Fisher S., Foley C.D., Franke A., Friedrich D., RA Gadbois L., Gearin G., Gearin C.R., Giannoukos G., Goode T., RA Graham J., Grandbois E., Grewal S., Gyaltsen K., Hafez N., Hagos B., RA Hall J., Henson C., Hollinger A., Honan T., Huard M.D., Hughes L., RA Hurhula B., Husby M.E., Kamat A., Kanga B., Kashin S., Khazanovich D., RA Kisner P., Lance K., Lara M., Lee W., Lennon N., Letendre F., RA LeVine R., Lipovsky A., Liu X., Liu J., Liu S., Lokyitsang T., RA Lokyitsang Y., Lubonja R., Lui A., MacDonald P., Magnisalis V., RA Maru K., Matthews C., McCusker W., McDonough S., Mehta T., Meldrim J., RA Meneus L., Mihai O., Mihalev A., Mihova T., Mittelman R., Mlenga V., RA Montmayeur A., Mulrain L., Navidi A., Naylor J., Negash T., Nguyen T., RA Nguyen N., Nicol R., Norbu C., Norbu N., Novod N., O'Neill B., RA Osman S., Markiewicz E., Oyono O.L., Patti C., Phunkhang P., RA Pierre F., Priest M., Raghuraman S., Rege F., Reyes R., Rise C., RA Rogov P., Ross K., Ryan E., Settipalli S., Shea T., Sherpa N., Shi L., RA Shih D., Sparrow T., Spaulding J., Stalker J., Stange-Thomann N., RA Stavropoulos S., Stone C., Strader C., Tesfaye S., Thomson T., RA Thoulutsang Y., Thoulutsang D., Topham K., Topping I., Tsamla T., RA Vassiliev H., Vo A., Wangchuk T., Wangdi T., Weiand M., Wilkinson J., RA Wilson A., Yadav S., Young G., Yu Q., Zembek L., Zhong D., Zimmer A., RA Zwirko Z., Jaffe D.B., Alvarez P., Brockman W., Butler J., Chin C., RA Gnerre S., Grabherr M., Kleber M., Mauceli E., MacCallum I.; RT "Evolution of genes and genomes on the Drosophila phylogeny."; RL Nature 450:203-218(2007). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CH902617; EDV41886.1; -; Genomic_DNA. DR RefSeq; XP_001953303.1; XM_001953268.2. DR ProteinModelPortal; B3LZ12; -. DR STRING; 7217.FBpp0120887; -. DR EnsemblMetazoa; FBtr0122395; FBpp0120887; FBgn0094713. DR GeneID; 6500478; -. DR KEGG; dan:Dana_GF17695; -. DR FlyBase; FBgn0094713; Dana\GF17695. DR eggNOG; KOG0410; Eukaryota. DR eggNOG; COG2262; LUCA. DR InParanoid; B3LZ12; -. DR OMA; MDTVGFM; -. DR OrthoDB; EOG091G0852; -. DR PhylomeDB; B3LZ12; -. DR Proteomes; UP000007801; Unassembled WGS sequence. DR Bgee; FBgn0094713; -. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR CDD; cd01878; HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 4: Predicted; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000007801}; KW Reference proteome {ECO:0000313|Proteomes:UP000007801}. FT DOMAIN 294 386 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 255 287 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 523 AA; 59090 MW; C3A8A1A5A0DC3A19 CRC64; MSGIRVLVRL ARVSSLRPVV VMPCRFKYTQ HQGVKGIRNR KSFFEAQMQA GQRADDHDEE ETLLSGDLTD VRFLDDRAYD EVAGGAMRIT RDIATSQQVL ILQPYVKWAA KRQPTLTDVR PDDQLAEASA LVHSLPNWQV AKALKVPLES LEKKTLFGSG KLAELKALVT DLRQERHLTC LFVSKGTLSF AQKRFLEAEF RLPVMDRYSV VIQILRLHAT SAEARLQVAM AELPYIWAQA KDASVTQTRR QGYALTDLQK EILRTRERKL RAELDRVRRQ RQLLRQKRKQ QNYPIVAVVG CTNAGKTSLI KALTVEDALQ PRNQLFATLD VTAHAGCLPC NLEVIYMDTV GFMSDLPTGL FECFVATLED AMLADVIIHV QDLSHPCHVA QRNHVEATLR SLAFNMSGGD STASQLPPII NVYNKCDLIP MKGQKTSKTD HHISARTQMG LDTLLVDVEQ QILVATGRKK LKMRVPNGGQ EMAWLYKNAA VVETMADEKN PEWLMMQVVI TQRTLDQFKR QFC // ID B3PDC0_CELJU Unreviewed; 445 AA. AC B3PDC0; DT 02-SEP-2008, integrated into UniProtKB/TrEMBL. DT 02-SEP-2008, sequence version 1. DT 30-AUG-2017, entry version 64. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=CJA_3078 {ECO:0000313|EMBL:ACE85084.1}; OS Cellvibrio japonicus (strain Ueda107) (Pseudomonas fluorescens subsp. OS cellulosa). OC Bacteria; Proteobacteria; Gammaproteobacteria; Cellvibrionales; OC Cellvibrionaceae; Cellvibrio. OX NCBI_TaxID=498211 {ECO:0000313|EMBL:ACE85084.1, ECO:0000313|Proteomes:UP000001036}; RN [1] {ECO:0000313|EMBL:ACE85084.1, ECO:0000313|Proteomes:UP000001036} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Ueda107 {ECO:0000313|EMBL:ACE85084.1, RC ECO:0000313|Proteomes:UP000001036}; RX PubMed=18556790; DOI=10.1128/JB.01701-07; RA Deboy R.T., Mongodin E.F., Fouts D.E., Tailford L.E., Khouri H., RA Emerson J.B., Mohamoud Y., Watkins K., Henrissat B., Gilbert H.J., RA Nelson K.E.; RT "Insights into plant cell wall degradation from the genome sequence of RT the soil bacterium Cellvibrio japonicus."; RL J. Bacteriol. 190:5455-5463(2008). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000934; ACE85084.1; -; Genomic_DNA. DR RefSeq; WP_012488656.1; NC_010995.1. DR ProteinModelPortal; B3PDC0; -. DR STRING; 498211.CJA_3078; -. DR EnsemblBacteria; ACE85084; ACE85084; CJA_3078. DR KEGG; cja:CJA_3078; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000001036; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000001036}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000001036}. FT DOMAIN 199 366 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 445 AA; 49546 MW; 8CFEF9C660E2B690 CRC64; MFFDRPESGE LAVLVHLNLS HGQEAEDPRE FEELVLSAGG DPVAFLTGSR VTPTAKYLIS TGKLEELRQL VQEHKAELAI FNHTLTPSQE RNLEKELQCR VLDRTGLILD IFAQRARTFE GKLQVELAQL RHTATRLIRG WTHLERQKGG IGLRGPGETQ LETDRRLLRN RITQIESRLE KVRSQREQGR RSRQRAAIPT VSLVGYTNAG KSTLFNLITG AEVYAENQLF ATLDPTMRRI ELADIGAVVL ADTVGFISHL PHRLVEAFRA TLEEASNSSL LLHVIDSAAE ERLRNIEQVD LVLEEIGAAD LPQLRVYNKL DLLEGASPQI DRDDSGKPIA VWLSAQTGVG LDLLAQAISE LLGKGIVAGS LVLEPQQGRL RAMLYSQQAV IDEHYRDDGN LEIYIRLPKD DLLRILSACG TQYDSLLWLD PGDDGELQNP DASPT // ID B3QTG4_CHLT3 Unreviewed; 432 AA. AC B3QTG4; DT 02-SEP-2008, integrated into UniProtKB/TrEMBL. DT 02-SEP-2008, sequence version 1. DT 07-JUN-2017, entry version 59. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Ctha_0239 {ECO:0000313|EMBL:ACF12710.1}; OS Chloroherpeton thalassium (strain ATCC 35110 / GB-78). OC Bacteria; Chlorobi; Chlorobia; Chlorobiales; Chlorobiaceae; OC Chloroherpeton. OX NCBI_TaxID=517418 {ECO:0000313|EMBL:ACF12710.1, ECO:0000313|Proteomes:UP000001208}; RN [1] {ECO:0000313|EMBL:ACF12710.1, ECO:0000313|Proteomes:UP000001208} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 35110 / GB-78 {ECO:0000313|Proteomes:UP000001208}; RG US DOE Joint Genome Institute; RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., RA Tice H., Bruce D., Goodwin L., Pitluck S., Schmutz J., Larimer F., RA Land M., Hauser L., Kyrpides N., Mikhailova N., Liu Z., Li T., RA Zhao F., Overmann J., Bryant D.A., Richardson P.; RT "Complete sequence of Chloroherpeton thalassium ATCC 35110."; RL Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001100; ACF12710.1; -; Genomic_DNA. DR RefSeq; WP_012498794.1; NC_011026.1. DR ProteinModelPortal; B3QTG4; -. DR STRING; 517418.Ctha_0239; -. DR EnsemblBacteria; ACF12710; ACF12710; Ctha_0239. DR KEGG; cts:Ctha_0239; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000001208; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000001208}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000001208}. FT DOMAIN 207 374 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 432 AA; 49389 MW; 9C0465BB8042D86B CRC64; MENQAVGFVS LENSPEKAVL IGISHPPEVL KWQAEEHLEE LEELADTAGA KVLFKFIQDR KQIDPVYAIG SGKVQELKPI IEENTIDLVI FDDELTPGQK RNLERELDCK ILDRTGLILQ IFAVRAKSAQ AKHQVELAQL EYLLPRLTRQ WTHLSKQKGG IGTKGPGETQ IETDRRLIWR RISTLKQKLK EHSRQRETRT SWRDSITKIA LVGYTNAGKS TLMNALCPKA NAYSEDRLFA TLDTTTRRLH LKQNKQAILS DTVGFIRKLP HNLVESFKST LEEVREADIL LHVVDVSHPS FEEHIRIVDE TLDEIGAKNK QTILVLNKID RLEQNDTFLG LAQKFEGSVL ISAARGINLS GLMERLSDLI QADFDERFIR VHVSDYKLIS YLHEKTEIIS KRYDDEDVEI QFRVPKKIAN QIDGVLRQHQ VS // ID B3RKJ7_TRIAD Unreviewed; 436 AA. AC B3RKJ7; DT 02-SEP-2008, integrated into UniProtKB/TrEMBL. DT 02-SEP-2008, sequence version 1. DT 30-AUG-2017, entry version 48. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EDV29414.1}; GN ORFNames=TRIADDRAFT_18641 {ECO:0000313|EMBL:EDV29414.1}; OS Trichoplax adhaerens (Trichoplax reptans). OC Eukaryota; Metazoa; Placozoa; Trichoplax. OX NCBI_TaxID=10228 {ECO:0000313|Proteomes:UP000009022}; RN [1] {ECO:0000313|EMBL:EDV29414.1, ECO:0000313|Proteomes:UP000009022} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Grell-BS-1999 {ECO:0000313|EMBL:EDV29414.1, RC ECO:0000313|Proteomes:UP000009022}; RX PubMed=18719581; DOI=10.1038/nature07191; RA Srivastava M., Begovic E., Chapman J., Putnam N.H., Hellsten U., RA Kawashima T., Kuo A., Mitros T., Salamov A., Carpenter M.L., RA Signorovitch A.Y., Moreno M.A., Kamm K., Grimwood J., Schmutz J., RA Shapiro H., Grigoriev I.V., Buss L.W., Schierwater B., RA Dellaporta S.L., Rokhsar D.S.; RT "The Trichoplax genome and the nature of placozoans."; RL Nature 454:955-960(2008). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; DS985241; EDV29414.1; -; Genomic_DNA. DR RefSeq; XP_002108616.1; XM_002108580.1. DR ProteinModelPortal; B3RKJ7; -. DR STRING; 10228.TriadP18641; -. DR EnsemblMetazoa; TriadT18641; TriadP18641; TriadG18641. DR GeneID; 6749030; -. DR KEGG; tad:TRIADDRAFT_18641; -. DR eggNOG; KOG0410; Eukaryota. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR InParanoid; B3RKJ7; -. DR OMA; MDTVGFM; -. DR OrthoDB; EOG091G0852; -. DR Proteomes; UP000009022; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR GO; GO:0043022; F:ribosome binding; IBA:GO_Central. DR CDD; cd01878; HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 4: Predicted; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000009022}; KW Reference proteome {ECO:0000313|Proteomes:UP000009022}. FT DOMAIN 211 379 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 177 204 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 436 AA; 49560 MW; 00584D4CF3796120 CRC64; MYEKLNLDNQ LTQVVIVHPN IKWGRNRDTL STPQLRVAEA VALMDTLKGK VVATTVESLK IEDKKTFFGK GKTGELCNLM NKLKQKHQVT AVFLNTTQLQ ANQRQTLQKL WSLPVYDRYG IVLQIFKRHA RTQEAKIQVE LASLKYLRSQ LSFTVEAYDL DRGHLGRAGE SGQEIGRRAL EYKYRQLSRK LKDIRQKRAT VRLKRQRNEI PTVAVLGYTN AGKTTLIKAL TGEKSMIPKD KLFATLDTTV YSGQLISGFQ ILYIDTIGFI SDLPHDLLES FSATLEDVIN ADLLLHIRDI SHPETEKQKA SVLNVLRDLY LPRTALENMI EVHNKIDLIE DYQSNLSTDD HNAVAVSATK KENFELLSQN IENGLMKTTG KQFYKLQIPN GGQQLSWLYR EANVSDLVPS KNGKSLIVKC IMSNGVYRKF CSKFGQ // ID B4CUC9_9BACT Unreviewed; 96 AA. AC B4CUC9; DT 23-SEP-2008, integrated into UniProtKB/TrEMBL. DT 23-SEP-2008, sequence version 1. DT 07-JUN-2017, entry version 22. DE SubName: Full=GTPase-like protein {ECO:0000313|EMBL:EDY22167.1}; GN ORFNames=CfE428DRAFT_0292 {ECO:0000313|EMBL:EDY22167.1}; OS Chthoniobacter flavus Ellin428. OC Bacteria; Verrucomicrobia; Spartobacteria; Chthoniobacterales; OC Chthoniobacteraceae; Chthoniobacter. OX NCBI_TaxID=497964 {ECO:0000313|EMBL:EDY22167.1, ECO:0000313|Proteomes:UP000005824}; RN [1] {ECO:0000313|EMBL:EDY22167.1, ECO:0000313|Proteomes:UP000005824} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Ellin428 {ECO:0000313|EMBL:EDY22167.1, RC ECO:0000313|Proteomes:UP000005824}; RX PubMed=21460085; DOI=10.1128/JB.00295-11; RA Kant R., van Passel M.W., Palva A., Lucas S., Lapidus A., RA Glavina Del Rio T., Dalin E., Tice H., Bruce D., Goodwin L., RA Pitluck S., Larimer F.W., Land M.L., Hauser L., Sangwan P., RA de Vos W.M., Janssen P.H., Smidt H.; RT "Genome sequence of Chthoniobacter flavus Ellin428, an aerobic RT heterotrophic soil bacterium."; RL J. Bacteriol. 193:2902-2903(2011). CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EDY22167.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABVL01000001; EDY22167.1; -; Genomic_DNA. DR ProteinModelPortal; B4CUC9; -. DR STRING; 497964.CfE428DRAFT_0292; -. DR EnsemblBacteria; EDY22167; EDY22167; CfE428DRAFT_0292. DR eggNOG; ENOG41078NE; Bacteria. DR eggNOG; COG2262; LUCA. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000005824; Unassembled WGS sequence. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000005824}; KW Reference proteome {ECO:0000313|Proteomes:UP000005824}. FT DOMAIN 17 48 GTP-bdg_N. {ECO:0000259|Pfam:PF13167}. FT DOMAIN 50 94 GTP-bdg_M. {ECO:0000259|Pfam:PF16360}. SQ SEQUENCE 96 AA; 10972 MW; ED66E375F82FC6C0 CRC64; MNRQTREGSG PRRHHLRHEL TPSQQRNWEN LAGITVIDRQ EVILDIFARR AQTREARLQV ELAQLEYSLP RLTRAWGHLV RQGGGIGARG EGETPA // ID B4CUD0_9BACT Unreviewed; 75 AA. AC B4CUD0; DT 23-SEP-2008, integrated into UniProtKB/TrEMBL. DT 23-SEP-2008, sequence version 1. DT 05-JUL-2017, entry version 21. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EDY22168.1}; GN ORFNames=CfE428DRAFT_0293 {ECO:0000313|EMBL:EDY22168.1}; OS Chthoniobacter flavus Ellin428. OC Bacteria; Verrucomicrobia; Spartobacteria; Chthoniobacterales; OC Chthoniobacteraceae; Chthoniobacter. OX NCBI_TaxID=497964 {ECO:0000313|EMBL:EDY22168.1, ECO:0000313|Proteomes:UP000005824}; RN [1] {ECO:0000313|EMBL:EDY22168.1, ECO:0000313|Proteomes:UP000005824} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Ellin428 {ECO:0000313|EMBL:EDY22168.1, RC ECO:0000313|Proteomes:UP000005824}; RX PubMed=21460085; DOI=10.1128/JB.00295-11; RA Kant R., van Passel M.W., Palva A., Lucas S., Lapidus A., RA Glavina Del Rio T., Dalin E., Tice H., Bruce D., Goodwin L., RA Pitluck S., Larimer F.W., Land M.L., Hauser L., Sangwan P., RA de Vos W.M., Janssen P.H., Smidt H.; RT "Genome sequence of Chthoniobacter flavus Ellin428, an aerobic RT heterotrophic soil bacterium."; RL J. Bacteriol. 193:2902-2903(2011). CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EDY22168.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABVL01000001; EDY22168.1; -; Genomic_DNA. DR STRING; 497964.CfE428DRAFT_0293; -. DR EnsemblBacteria; EDY22168; EDY22168; CfE428DRAFT_0293. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000005824; Unassembled WGS sequence. DR InterPro; IPR025121; GTPase_HflX_N. DR Pfam; PF13167; GTP-bdg_N; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000005824}; KW Reference proteome {ECO:0000313|Proteomes:UP000005824}. FT DOMAIN 33 73 GTP-bdg_N. {ECO:0000259|Pfam:PF13167}. SQ SEQUENCE 75 AA; 8422 MW; 3E6214C39E0EED19 CRC64; MIDIKEKEKM VERALLVGAY TDTNGRPEAT SLLEELEELV KTLGIPIMDR LLVYHREQHA RLLIGTGKAD ESSNA // ID B4EAW3_BURCJ Unreviewed; 395 AA. AC B4EAW3; DT 23-SEP-2008, integrated into UniProtKB/TrEMBL. DT 23-SEP-2008, sequence version 1. DT 07-JUN-2017, entry version 67. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:CAR52178.1}; GN ORFNames=BCAL1878 {ECO:0000313|EMBL:CAR52178.1}; OS Burkholderia cenocepacia (strain ATCC BAA-245 / DSM 16553 / LMG 16656 OS / NCTC 13227 / J2315 / CF5610) (Burkholderia cepacia (strain J2315)). OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Burkholderia; Burkholderia cepacia complex. OX NCBI_TaxID=216591 {ECO:0000313|EMBL:CAR52178.1, ECO:0000313|Proteomes:UP000001035}; RN [1] {ECO:0000313|EMBL:CAR52178.1, ECO:0000313|Proteomes:UP000001035} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-245 / DSM 16553 / LMG 16656 / NCTC 13227 / J2315 / RC CF5610 {ECO:0000313|Proteomes:UP000001035}; RX PubMed=18931103; DOI=10.1128/JB.01230-08; RA Holden M.T., Seth-Smith H.M., Crossman L.C., Sebaihia M., RA Bentley S.D., Cerdeno-Tarraga A.M., Thomson N.R., Bason N., RA Quail M.A., Sharp S., Cherevach I., Churcher C., Goodhead I., RA Hauser H., Holroyd N., Mungall K., Scott P., Walker D., White B., RA Rose H., Iversen P., Mil-Homens D., Rocha E.P., Fialho A.M., RA Baldwin A., Dowson C., Barrell B.G., Govan J.R., Vandamme P., RA Hart C.A., Mahenthiralingam E., Parkhill J.; RT "The genome of Burkholderia cenocepacia J2315, an epidemic pathogen of RT cystic fibrosis patients."; RL J. Bacteriol. 191:261-277(2009). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AM747720; CAR52178.1; -; Genomic_DNA. DR RefSeq; WP_011694299.1; NC_011000.1. DR ProteinModelPortal; B4EAW3; -. DR STRING; 216591.BCAL1878; -. DR EnsemblBacteria; CAR52178; CAR52178; BCAL1878. DR KEGG; bcj:BCAL1878; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000001035; Chromosome 1. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000001035}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000001035}. FT DOMAIN 196 367 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 162 189 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 395 AA; 43309 MW; 73CBBCA7CBB84622 CRC64; MTPDNLINAA LVGIDFGKTD FEASLEELSL LASSAGARPA VTLTGRRASP DAKMFIGSGK AEELRLACDA HNVEIVIFNH ALAPAQQRNL EQALNRRVVD RTSLILDIFA QRARSHEGKL QVELAQLQYL STRLIRAWTH LERQKGGIGL RGPGETQLET DRRLIGERIK MLKSRLDRLR RQHSTQRRQR ARSGTMSVSL VGYTNAGKST LFNALTKAQA YAADQLFATL DTTSRRVYLG DEVGQIVVSD TVGFIRELPH QLVAAFRATL EETIHADLLL HVVDASSAVR LEQIEQVNGV LHEIGADTIR QVLVFNKIDA VPELAARGDA VERDEYGNIS RVFLSARTGQ GLDTLRAAIA EIASAEHLSS ATLPDALDGT SAEPHEDHTI SEHGR // ID B4F267_PROMH Unreviewed; 427 AA. AC B4F267; DT 23-SEP-2008, integrated into UniProtKB/TrEMBL. DT 23-SEP-2008, sequence version 1. DT 30-AUG-2017, entry version 59. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:CAR46603.1}; GN OrderedLocusNames=PMI3366 {ECO:0000313|EMBL:CAR46603.1}; OS Proteus mirabilis (strain HI4320). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; OC Morganellaceae; Proteus. OX NCBI_TaxID=529507 {ECO:0000313|Proteomes:UP000008319}; RN [1] {ECO:0000313|EMBL:CAR46603.1, ECO:0000313|Proteomes:UP000008319} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=HI4320 {ECO:0000313|EMBL:CAR46603.1, RC ECO:0000313|Proteomes:UP000008319}; RX PubMed=18375554; DOI=10.1128/JB.01981-07; RA Pearson M.M., Sebaihia M., Churcher C., Quail M.A., Seshasayee A.S., RA Luscombe N.M., Abdellah Z., Arrosmith C., Atkin B., Chillingworth T., RA Hauser H., Jagels K., Moule S., Mungall K., Norbertczak H., RA Rabbinowitsch E., Walker D., Whithead S., Thomson N.R., Rather P.N., RA Parkhill J., Mobley H.L.; RT "Complete genome sequence of uropathogenic Proteus mirabilis, a master RT of both adherence and motility."; RL J. Bacteriol. 190:4027-4037(2008). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AM942759; CAR46603.1; -; Genomic_DNA. DR RefSeq; WP_004246290.1; NC_010554.1. DR ProteinModelPortal; B4F267; -. DR STRING; 529507.PMI3366; -. DR EnsemblBacteria; CAR46603; CAR46603; PMI3366. DR GeneID; 6802249; -. DR KEGG; pmr:PMI3366; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000008319; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000008319}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000008319}. FT DOMAIN 198 365 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 427 AA; 48317 MW; 880E3F774221D311 CRC64; MFDRYEGGEL AVLVHVFFSQ EKDIDDLQEF ESLVTSAGVK PVQIITGSRR APHSKYYVGE GKAEEIAEAV KASGADVVLF NHALSPAQER NLERLCECRV VDRTGVILDI FAQRARTHEG KLQVELAQLR HLSTRLVRGW THLERQKGGI GLRGPGETQL ETDRRLLRGK ISQILMRLGK VERQREQGRQ ARSKADIPTL SLVGYTNAGK SSLFNRITCA DVYAADQLFA TLDPTLRRIQ VDDVGTVVLA DTVGFIRHLP HDLVAAFKAT LQETREATLL LHVIDAADSR FEENIHAVEN VLEEIDAHEI PTLYVMNKID LLEDFTPRID RNEDNLPVRV WVSAQTGEGI PLLYQALTER LSGEIAHVEL RLPPEEAGRL RSRFYQLQAI EREWIEKDGK VGLITRMPMV DWHRLCKQEP TLLDYVV // ID B4GF52_DROPE Unreviewed; 525 AA. AC B4GF52; DT 23-SEP-2008, integrated into UniProtKB/TrEMBL. DT 23-SEP-2008, sequence version 1. DT 07-JUN-2017, entry version 43. DE SubName: Full=GL22142 {ECO:0000313|EMBL:EDW34237.1}; GN Name=Dper\GL22142 {ECO:0000313|EMBL:EDW34237.1}; GN ORFNames=Dper_GL22142 {ECO:0000313|EMBL:EDW34237.1}, GN GL22142 {ECO:0000313|FlyBase:FBgn0159734}; OS Drosophila persimilis (Fruit fly). OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; OC Pterygota; Neoptera; Holometabola; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila; Sophophora. OX NCBI_TaxID=7234 {ECO:0000313|Proteomes:UP000008744}; RN [1] {ECO:0000313|EMBL:EDW34237.1, ECO:0000313|Proteomes:UP000008744} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MSH-3 / Tucson 14011-0111.49 RC {ECO:0000313|Proteomes:UP000008744}; RX PubMed=17994087; DOI=10.1038/nature06341; RG Drosophila 12 Genomes Consortium; RA Clark A.G., Eisen M.B., Smith D.R., Bergman C.M., Oliver B., RA Markow T.A., Kaufman T.C., Kellis M., Gelbart W., Iyer V.N., RA Pollard D.A., Sackton T.B., Larracuente A.M., Singh N.D., Abad J.P., RA Abt D.N., Adryan B., Aguade M., Akashi H., Anderson W.W., RA Aquadro C.F., Ardell D.H., Arguello R., Artieri C.G., Barbash D.A., RA Barker D., Barsanti P., Batterham P., Batzoglou S., Begun D., RA Bhutkar A., Blanco E., Bosak S.A., Bradley R.K., Brand A.D., RA Brent M.R., Brooks A.N., Brown R.H., Butlin R.K., Caggese C., RA Calvi B.R., Bernardo de Carvalho A., Caspi A., Castrezana S., RA Celniker S.E., Chang J.L., Chapple C., Chatterji S., Chinwalla A., RA Civetta A., Clifton S.W., Comeron J.M., Costello J.C., Coyne J.A., RA Daub J., David R.G., Delcher A.L., Delehaunty K., Do C.B., Ebling H., RA Edwards K., Eickbush T., Evans J.D., Filipski A., Findeiss S., RA Freyhult E., Fulton L., Fulton R., Garcia A.C., Gardiner A., RA Garfield D.A., Garvin B.E., Gibson G., Gilbert D., Gnerre S., RA Godfrey J., Good R., Gotea V., Gravely B., Greenberg A.J., RA Griffiths-Jones S., Gross S., Guigo R., Gustafson E.A., Haerty W., RA Hahn M.W., Halligan D.L., Halpern A.L., Halter G.M., Han M.V., RA Heger A., Hillier L., Hinrichs A.S., Holmes I., Hoskins R.A., RA Hubisz M.J., Hultmark D., Huntley M.A., Jaffe D.B., Jagadeeshan S., RA Jeck W.R., Johnson J., Jones C.D., Jordan W.C., Karpen G.H., RA Kataoka E., Keightley P.D., Kheradpour P., Kirkness E.F., RA Koerich L.B., Kristiansen K., Kudrna D., Kulathinal R.J., Kumar S., RA Kwok R., Lander E., Langley C.H., Lapoint R., Lazzaro B.P., Lee S.J., RA Levesque L., Li R., Lin C.F., Lin M.F., Lindblad-Toh K., Llopart A., RA Long M., Low L., Lozovsky E., Lu J., Luo M., Machado C.A., RA Makalowski W., Marzo M., Matsuda M., Matzkin L., McAllister B., RA McBride C.S., McKernan B., McKernan K., Mendez-Lago M., Minx P., RA Mollenhauer M.U., Montooth K., Mount S.M., Mu X., Myers E., Negre B., RA Newfeld S., Nielsen R., Noor M.A., O'Grady P., Pachter L., RA Papaceit M., Parisi M.J., Parisi M., Parts L., Pedersen J.S., RA Pesole G., Phillippy A.M., Ponting C.P., Pop M., Porcelli D., RA Powell J.R., Prohaska S., Pruitt K., Puig M., Quesneville H., RA Ram K.R., Rand D., Rasmussen M.D., Reed L.K., Reenan R., Reily A., RA Remington K.A., Rieger T.T., Ritchie M.G., Robin C., Rogers Y.H., RA Rohde C., Rozas J., Rubenfield M.J., Ruiz A., Russo S., Salzberg S.L., RA Sanchez-Gracia A., Saranga D.J., Sato H., Schaeffer S.W., Schatz M.C., RA Schlenke T., Schwartz R., Segarra C., Singh R.S., Sirot L., Sirota M., RA Sisneros N.B., Smith C.D., Smith T.F., Spieth J., Stage D.E., RA Stark A., Stephan W., Strausberg R.L., Strempel S., Sturgill D., RA Sutton G., Sutton G.G., Tao W., Teichmann S., Tobari Y.N., RA Tomimura Y., Tsolas J.M., Valente V.L., Venter E., Venter J.C., RA Vicario S., Vieira F.G., Vilella A.J., Villasante A., Walenz B., RA Wang J., Wasserman M., Watts T., Wilson D., Wilson R.K., Wing R.A., RA Wolfner M.F., Wong A., Wong G.K., Wu C.I., Wu G., Yamamoto D., RA Yang H.P., Yang S.P., Yorke J.A., Yoshida K., Zdobnov E., Zhang P., RA Zhang Y., Zimin A.V., Baldwin J., Abdouelleil A., Abdulkadir J., RA Abebe A., Abera B., Abreu J., Acer S.C., Aftuck L., Alexander A., RA An P., Anderson E., Anderson S., Arachi H., Azer M., Bachantsang P., RA Barry A., Bayul T., Berlin A., Bessette D., Bloom T., Blye J., RA Boguslavskiy L., Bonnet C., Boukhgalter B., Bourzgui I., Brown A., RA Cahill P., Channer S., Cheshatsang Y., Chuda L., Citroen M., RA Collymore A., Cooke P., Costello M., D'Aco K., Daza R., De Haan G., RA DeGray S., DeMaso C., Dhargay N., Dooley K., Dooley E., Doricent M., RA Dorje P., Dorjee K., Dupes A., Elong R., Falk J., Farina A., Faro S., RA Ferguson D., Fisher S., Foley C.D., Franke A., Friedrich D., RA Gadbois L., Gearin G., Gearin C.R., Giannoukos G., Goode T., RA Graham J., Grandbois E., Grewal S., Gyaltsen K., Hafez N., Hagos B., RA Hall J., Henson C., Hollinger A., Honan T., Huard M.D., Hughes L., RA Hurhula B., Husby M.E., Kamat A., Kanga B., Kashin S., Khazanovich D., RA Kisner P., Lance K., Lara M., Lee W., Lennon N., Letendre F., RA LeVine R., Lipovsky A., Liu X., Liu J., Liu S., Lokyitsang T., RA Lokyitsang Y., Lubonja R., Lui A., MacDonald P., Magnisalis V., RA Maru K., Matthews C., McCusker W., McDonough S., Mehta T., Meldrim J., RA Meneus L., Mihai O., Mihalev A., Mihova T., Mittelman R., Mlenga V., RA Montmayeur A., Mulrain L., Navidi A., Naylor J., Negash T., Nguyen T., RA Nguyen N., Nicol R., Norbu C., Norbu N., Novod N., O'Neill B., RA Osman S., Markiewicz E., Oyono O.L., Patti C., Phunkhang P., RA Pierre F., Priest M., Raghuraman S., Rege F., Reyes R., Rise C., RA Rogov P., Ross K., Ryan E., Settipalli S., Shea T., Sherpa N., Shi L., RA Shih D., Sparrow T., Spaulding J., Stalker J., Stange-Thomann N., RA Stavropoulos S., Stone C., Strader C., Tesfaye S., Thomson T., RA Thoulutsang Y., Thoulutsang D., Topham K., Topping I., Tsamla T., RA Vassiliev H., Vo A., Wangchuk T., Wangdi T., Weiand M., Wilkinson J., RA Wilson A., Yadav S., Young G., Yu Q., Zembek L., Zhong D., Zimmer A., RA Zwirko Z., Jaffe D.B., Alvarez P., Brockman W., Butler J., Chin C., RA Gnerre S., Grabherr M., Kleber M., Mauceli E., MacCallum I.; RT "Evolution of genes and genomes on the Drosophila phylogeny."; RL Nature 450:203-218(2007). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CH479182; EDW34237.1; -; Genomic_DNA. DR RefSeq; XP_002017137.1; XM_002017101.1. DR ProteinModelPortal; B4GF52; -. DR EnsemblMetazoa; FBtr0187757; FBpp0186249; FBgn0159734. DR GeneID; 6591776; -. DR KEGG; dpe:Dper_GL22142; -. DR FlyBase; FBgn0159734; Dper\GL22142. DR OMA; MDTVGFM; -. DR OrthoDB; EOG091G0852; -. DR PhylomeDB; B4GF52; -. DR Proteomes; UP000008744; Unassembled WGS sequence. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR CDD; cd01878; HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 4: Predicted; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000008744}; KW Reference proteome {ECO:0000313|Proteomes:UP000008744}. FT DOMAIN 298 468 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 259 291 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 525 AA; 59037 MW; F2D7D0340B3D19D2 CRC64; MTSLRPLMRL TRALPLRPAM VGVLHSRFKY TQHQGVKGIR NRKSFFEAQM QAGQHGDEDH EEAERGDSNG NLADMRFLDD RAYDEVAGGA MRISRDIAST QQVLILQPYV KWSAKRQKIP SDVRPVDQLA EASALIHSLP NWQVAKALKV PLESLERKTL FGSGKMVELK ALIADLRQEK HLTCLFVSKG TLSFAQKRFL EAEFRLPVMD RYSVVIQILR LHATTAEARL QVAMAELPYI WSQAKDASVT QTRRQGYSLT DLQKEILRTR ERKLRAELDR VRRQRQLLRQ KRKQQNYPIV AVVGYTNAGK TSLIKALTVE DALQPRNQLF ATLDVTAHAG QLPCNLQVIY MDTVGFMSDL PTGLFECFVA TLEDAMLADV IVHVQDLSHP CHAAQRSHVE STLRSLAFNV SGGDSATSQL PPIINVYNKC DLVSQPSSDA AVHHISARAQ TGLEPLLADI EEQILAATGR RKLQMRVPSG GPEMAWLYKN AAVVDTVADE AYPNRLMMHV VISQRTLDQF KREFL // ID B4ICA1_DROSE Unreviewed; 526 AA. AC B4ICA1; DT 23-SEP-2008, integrated into UniProtKB/TrEMBL. DT 23-SEP-2008, sequence version 1. DT 07-JUN-2017, entry version 44. DE SubName: Full=GM10247 {ECO:0000313|EMBL:EDW44997.1}; GN Name=Dsec\GM10247 {ECO:0000313|EMBL:EDW44997.1}; GN ORFNames=Dsec_GM10247 {ECO:0000313|EMBL:EDW44997.1}, GN GM10247 {ECO:0000313|FlyBase:FBgn0165198}; OS Drosophila sechellia (Fruit fly). OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; OC Pterygota; Neoptera; Holometabola; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila; Sophophora. OX NCBI_TaxID=7238 {ECO:0000313|Proteomes:UP000001292}; RN [1] {ECO:0000313|EMBL:EDW44997.1, ECO:0000313|Proteomes:UP000001292} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Rob3c / Tucson 14021-0248.25 RC {ECO:0000313|Proteomes:UP000001292}; RX PubMed=17994087; DOI=10.1038/nature06341; RG Drosophila 12 Genomes Consortium; RA Clark A.G., Eisen M.B., Smith D.R., Bergman C.M., Oliver B., RA Markow T.A., Kaufman T.C., Kellis M., Gelbart W., Iyer V.N., RA Pollard D.A., Sackton T.B., Larracuente A.M., Singh N.D., Abad J.P., RA Abt D.N., Adryan B., Aguade M., Akashi H., Anderson W.W., RA Aquadro C.F., Ardell D.H., Arguello R., Artieri C.G., Barbash D.A., RA Barker D., Barsanti P., Batterham P., Batzoglou S., Begun D., RA Bhutkar A., Blanco E., Bosak S.A., Bradley R.K., Brand A.D., RA Brent M.R., Brooks A.N., Brown R.H., Butlin R.K., Caggese C., RA Calvi B.R., Bernardo de Carvalho A., Caspi A., Castrezana S., RA Celniker S.E., Chang J.L., Chapple C., Chatterji S., Chinwalla A., RA Civetta A., Clifton S.W., Comeron J.M., Costello J.C., Coyne J.A., RA Daub J., David R.G., Delcher A.L., Delehaunty K., Do C.B., Ebling H., RA Edwards K., Eickbush T., Evans J.D., Filipski A., Findeiss S., RA Freyhult E., Fulton L., Fulton R., Garcia A.C., Gardiner A., RA Garfield D.A., Garvin B.E., Gibson G., Gilbert D., Gnerre S., RA Godfrey J., Good R., Gotea V., Gravely B., Greenberg A.J., RA Griffiths-Jones S., Gross S., Guigo R., Gustafson E.A., Haerty W., RA Hahn M.W., Halligan D.L., Halpern A.L., Halter G.M., Han M.V., RA Heger A., Hillier L., Hinrichs A.S., Holmes I., Hoskins R.A., RA Hubisz M.J., Hultmark D., Huntley M.A., Jaffe D.B., Jagadeeshan S., RA Jeck W.R., Johnson J., Jones C.D., Jordan W.C., Karpen G.H., RA Kataoka E., Keightley P.D., Kheradpour P., Kirkness E.F., RA Koerich L.B., Kristiansen K., Kudrna D., Kulathinal R.J., Kumar S., RA Kwok R., Lander E., Langley C.H., Lapoint R., Lazzaro B.P., Lee S.J., RA Levesque L., Li R., Lin C.F., Lin M.F., Lindblad-Toh K., Llopart A., RA Long M., Low L., Lozovsky E., Lu J., Luo M., Machado C.A., RA Makalowski W., Marzo M., Matsuda M., Matzkin L., McAllister B., RA McBride C.S., McKernan B., McKernan K., Mendez-Lago M., Minx P., RA Mollenhauer M.U., Montooth K., Mount S.M., Mu X., Myers E., Negre B., RA Newfeld S., Nielsen R., Noor M.A., O'Grady P., Pachter L., RA Papaceit M., Parisi M.J., Parisi M., Parts L., Pedersen J.S., RA Pesole G., Phillippy A.M., Ponting C.P., Pop M., Porcelli D., RA Powell J.R., Prohaska S., Pruitt K., Puig M., Quesneville H., RA Ram K.R., Rand D., Rasmussen M.D., Reed L.K., Reenan R., Reily A., RA Remington K.A., Rieger T.T., Ritchie M.G., Robin C., Rogers Y.H., RA Rohde C., Rozas J., Rubenfield M.J., Ruiz A., Russo S., Salzberg S.L., RA Sanchez-Gracia A., Saranga D.J., Sato H., Schaeffer S.W., Schatz M.C., RA Schlenke T., Schwartz R., Segarra C., Singh R.S., Sirot L., Sirota M., RA Sisneros N.B., Smith C.D., Smith T.F., Spieth J., Stage D.E., RA Stark A., Stephan W., Strausberg R.L., Strempel S., Sturgill D., RA Sutton G., Sutton G.G., Tao W., Teichmann S., Tobari Y.N., RA Tomimura Y., Tsolas J.M., Valente V.L., Venter E., Venter J.C., RA Vicario S., Vieira F.G., Vilella A.J., Villasante A., Walenz B., RA Wang J., Wasserman M., Watts T., Wilson D., Wilson R.K., Wing R.A., RA Wolfner M.F., Wong A., Wong G.K., Wu C.I., Wu G., Yamamoto D., RA Yang H.P., Yang S.P., Yorke J.A., Yoshida K., Zdobnov E., Zhang P., RA Zhang Y., Zimin A.V., Baldwin J., Abdouelleil A., Abdulkadir J., RA Abebe A., Abera B., Abreu J., Acer S.C., Aftuck L., Alexander A., RA An P., Anderson E., Anderson S., Arachi H., Azer M., Bachantsang P., RA Barry A., Bayul T., Berlin A., Bessette D., Bloom T., Blye J., RA Boguslavskiy L., Bonnet C., Boukhgalter B., Bourzgui I., Brown A., RA Cahill P., Channer S., Cheshatsang Y., Chuda L., Citroen M., RA Collymore A., Cooke P., Costello M., D'Aco K., Daza R., De Haan G., RA DeGray S., DeMaso C., Dhargay N., Dooley K., Dooley E., Doricent M., RA Dorje P., Dorjee K., Dupes A., Elong R., Falk J., Farina A., Faro S., RA Ferguson D., Fisher S., Foley C.D., Franke A., Friedrich D., RA Gadbois L., Gearin G., Gearin C.R., Giannoukos G., Goode T., RA Graham J., Grandbois E., Grewal S., Gyaltsen K., Hafez N., Hagos B., RA Hall J., Henson C., Hollinger A., Honan T., Huard M.D., Hughes L., RA Hurhula B., Husby M.E., Kamat A., Kanga B., Kashin S., Khazanovich D., RA Kisner P., Lance K., Lara M., Lee W., Lennon N., Letendre F., RA LeVine R., Lipovsky A., Liu X., Liu J., Liu S., Lokyitsang T., RA Lokyitsang Y., Lubonja R., Lui A., MacDonald P., Magnisalis V., RA Maru K., Matthews C., McCusker W., McDonough S., Mehta T., Meldrim J., RA Meneus L., Mihai O., Mihalev A., Mihova T., Mittelman R., Mlenga V., RA Montmayeur A., Mulrain L., Navidi A., Naylor J., Negash T., Nguyen T., RA Nguyen N., Nicol R., Norbu C., Norbu N., Novod N., O'Neill B., RA Osman S., Markiewicz E., Oyono O.L., Patti C., Phunkhang P., RA Pierre F., Priest M., Raghuraman S., Rege F., Reyes R., Rise C., RA Rogov P., Ross K., Ryan E., Settipalli S., Shea T., Sherpa N., Shi L., RA Shih D., Sparrow T., Spaulding J., Stalker J., Stange-Thomann N., RA Stavropoulos S., Stone C., Strader C., Tesfaye S., Thomson T., RA Thoulutsang Y., Thoulutsang D., Topham K., Topping I., Tsamla T., RA Vassiliev H., Vo A., Wangchuk T., Wangdi T., Weiand M., Wilkinson J., RA Wilson A., Yadav S., Young G., Yu Q., Zembek L., Zhong D., Zimmer A., RA Zwirko Z., Jaffe D.B., Alvarez P., Brockman W., Butler J., Chin C., RA Gnerre S., Grabherr M., Kleber M., Mauceli E., MacCallum I.; RT "Evolution of genes and genomes on the Drosophila phylogeny."; RL Nature 450:203-218(2007). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CH480828; EDW44997.1; -; Genomic_DNA. DR RefSeq; XP_002041259.1; XM_002041223.1. DR ProteinModelPortal; B4ICA1; -. DR EnsemblMetazoa; FBtr0193232; FBpp0191724; FBgn0165198. DR GeneID; 6616928; -. DR KEGG; dse:Dsec_GM10247; -. DR FlyBase; FBgn0165198; Dsec\GM10247. DR OMA; MDTVGFM; -. DR OrthoDB; EOG091G0852; -. DR PhylomeDB; B4ICA1; -. DR Proteomes; UP000001292; Unassembled WGS sequence. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR CDD; cd01878; HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 4: Predicted; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000001292}; KW Reference proteome {ECO:0000313|Proteomes:UP000001292}. FT DOMAIN 296 468 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 262 289 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 526 AA; 59267 MW; 16808B27801C3432 CRC64; MSALRIFARL VRSRTLRLCP ILEIPARCKY TQHQGVKGIR NRKSFYEAQI QAGQQGEEDE DLERTASSDL ADMRFLDDRA YDEVAGGAMR ITRDIASSQQ VLILQPYVKW AAKRQSGPLD VRPEDQLAEA SALIHSLPNW QVARALKVPL ESLEKKTLFG SGKLVELKEL VAELRQERHL TCLFVSKGTL SFAQKRFLEA EFRLPVMDRY SVVIQILRLH ATSAEAKLQV AMAELPYIWA QAKDASVTQT RRQGYALTDL QKEILRTRER KLRTELDRVR RQRQLLRQKR KQQNYPIVAV VGYTNAGKTS LIKALTVEDA LQPRNQLFAT LDVTAHAGCL PCNLEVIYMD TVGFMSDLPT GLFECFVATL EDAMLADVIV HVQDLSHPCH AAQRSHVEAT LRSLAFNVAG GDSTASQLPP IINVYNKCDL VSQEAQSSSD PVHHISARAQ TGLEPLLDDI EQQILTATGR RKLQMRVPSG GPEMAWLYKN AAVVETTADA ENPERLMMHV VISQRTLDQF KRQFCR // ID B4JHK5_DROGR Unreviewed; 519 AA. AC B4JHK5; DT 23-SEP-2008, integrated into UniProtKB/TrEMBL. DT 23-SEP-2008, sequence version 1. DT 07-JUN-2017, entry version 50. DE SubName: Full=GH18978 {ECO:0000313|EMBL:EDV92832.1}; GN Name=Dgri\GH18978 {ECO:0000313|EMBL:EDV92832.1}; GN ORFNames=Dgri_GH18978 {ECO:0000313|EMBL:EDV92832.1}, GN GH18978 {ECO:0000313|FlyBase:FBgn0126445}; OS Drosophila grimshawi (Fruit fly) (Idiomyia grimshawi). OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; OC Pterygota; Neoptera; Holometabola; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila; Hawaiian Drosophila. OX NCBI_TaxID=7222 {ECO:0000313|Proteomes:UP000001070}; RN [1] {ECO:0000313|EMBL:EDV92832.1, ECO:0000313|Proteomes:UP000001070} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Tucson 15287-2541.00 {ECO:0000313|Proteomes:UP000001070}; RX PubMed=17994087; DOI=10.1038/nature06341; RG Drosophila 12 Genomes Consortium; RA Clark A.G., Eisen M.B., Smith D.R., Bergman C.M., Oliver B., RA Markow T.A., Kaufman T.C., Kellis M., Gelbart W., Iyer V.N., RA Pollard D.A., Sackton T.B., Larracuente A.M., Singh N.D., Abad J.P., RA Abt D.N., Adryan B., Aguade M., Akashi H., Anderson W.W., RA Aquadro C.F., Ardell D.H., Arguello R., Artieri C.G., Barbash D.A., RA Barker D., Barsanti P., Batterham P., Batzoglou S., Begun D., RA Bhutkar A., Blanco E., Bosak S.A., Bradley R.K., Brand A.D., RA Brent M.R., Brooks A.N., Brown R.H., Butlin R.K., Caggese C., RA Calvi B.R., Bernardo de Carvalho A., Caspi A., Castrezana S., RA Celniker S.E., Chang J.L., Chapple C., Chatterji S., Chinwalla A., RA Civetta A., Clifton S.W., Comeron J.M., Costello J.C., Coyne J.A., RA Daub J., David R.G., Delcher A.L., Delehaunty K., Do C.B., Ebling H., RA Edwards K., Eickbush T., Evans J.D., Filipski A., Findeiss S., RA Freyhult E., Fulton L., Fulton R., Garcia A.C., Gardiner A., RA Garfield D.A., Garvin B.E., Gibson G., Gilbert D., Gnerre S., RA Godfrey J., Good R., Gotea V., Gravely B., Greenberg A.J., RA Griffiths-Jones S., Gross S., Guigo R., Gustafson E.A., Haerty W., RA Hahn M.W., Halligan D.L., Halpern A.L., Halter G.M., Han M.V., RA Heger A., Hillier L., Hinrichs A.S., Holmes I., Hoskins R.A., RA Hubisz M.J., Hultmark D., Huntley M.A., Jaffe D.B., Jagadeeshan S., RA Jeck W.R., Johnson J., Jones C.D., Jordan W.C., Karpen G.H., RA Kataoka E., Keightley P.D., Kheradpour P., Kirkness E.F., RA Koerich L.B., Kristiansen K., Kudrna D., Kulathinal R.J., Kumar S., RA Kwok R., Lander E., Langley C.H., Lapoint R., Lazzaro B.P., Lee S.J., RA Levesque L., Li R., Lin C.F., Lin M.F., Lindblad-Toh K., Llopart A., RA Long M., Low L., Lozovsky E., Lu J., Luo M., Machado C.A., RA Makalowski W., Marzo M., Matsuda M., Matzkin L., McAllister B., RA McBride C.S., McKernan B., McKernan K., Mendez-Lago M., Minx P., RA Mollenhauer M.U., Montooth K., Mount S.M., Mu X., Myers E., Negre B., RA Newfeld S., Nielsen R., Noor M.A., O'Grady P., Pachter L., RA Papaceit M., Parisi M.J., Parisi M., Parts L., Pedersen J.S., RA Pesole G., Phillippy A.M., Ponting C.P., Pop M., Porcelli D., RA Powell J.R., Prohaska S., Pruitt K., Puig M., Quesneville H., RA Ram K.R., Rand D., Rasmussen M.D., Reed L.K., Reenan R., Reily A., RA Remington K.A., Rieger T.T., Ritchie M.G., Robin C., Rogers Y.H., RA Rohde C., Rozas J., Rubenfield M.J., Ruiz A., Russo S., Salzberg S.L., RA Sanchez-Gracia A., Saranga D.J., Sato H., Schaeffer S.W., Schatz M.C., RA Schlenke T., Schwartz R., Segarra C., Singh R.S., Sirot L., Sirota M., RA Sisneros N.B., Smith C.D., Smith T.F., Spieth J., Stage D.E., RA Stark A., Stephan W., Strausberg R.L., Strempel S., Sturgill D., RA Sutton G., Sutton G.G., Tao W., Teichmann S., Tobari Y.N., RA Tomimura Y., Tsolas J.M., Valente V.L., Venter E., Venter J.C., RA Vicario S., Vieira F.G., Vilella A.J., Villasante A., Walenz B., RA Wang J., Wasserman M., Watts T., Wilson D., Wilson R.K., Wing R.A., RA Wolfner M.F., Wong A., Wong G.K., Wu C.I., Wu G., Yamamoto D., RA Yang H.P., Yang S.P., Yorke J.A., Yoshida K., Zdobnov E., Zhang P., RA Zhang Y., Zimin A.V., Baldwin J., Abdouelleil A., Abdulkadir J., RA Abebe A., Abera B., Abreu J., Acer S.C., Aftuck L., Alexander A., RA An P., Anderson E., Anderson S., Arachi H., Azer M., Bachantsang P., RA Barry A., Bayul T., Berlin A., Bessette D., Bloom T., Blye J., RA Boguslavskiy L., Bonnet C., Boukhgalter B., Bourzgui I., Brown A., RA Cahill P., Channer S., Cheshatsang Y., Chuda L., Citroen M., RA Collymore A., Cooke P., Costello M., D'Aco K., Daza R., De Haan G., RA DeGray S., DeMaso C., Dhargay N., Dooley K., Dooley E., Doricent M., RA Dorje P., Dorjee K., Dupes A., Elong R., Falk J., Farina A., Faro S., RA Ferguson D., Fisher S., Foley C.D., Franke A., Friedrich D., RA Gadbois L., Gearin G., Gearin C.R., Giannoukos G., Goode T., RA Graham J., Grandbois E., Grewal S., Gyaltsen K., Hafez N., Hagos B., RA Hall J., Henson C., Hollinger A., Honan T., Huard M.D., Hughes L., RA Hurhula B., Husby M.E., Kamat A., Kanga B., Kashin S., Khazanovich D., RA Kisner P., Lance K., Lara M., Lee W., Lennon N., Letendre F., RA LeVine R., Lipovsky A., Liu X., Liu J., Liu S., Lokyitsang T., RA Lokyitsang Y., Lubonja R., Lui A., MacDonald P., Magnisalis V., RA Maru K., Matthews C., McCusker W., McDonough S., Mehta T., Meldrim J., RA Meneus L., Mihai O., Mihalev A., Mihova T., Mittelman R., Mlenga V., RA Montmayeur A., Mulrain L., Navidi A., Naylor J., Negash T., Nguyen T., RA Nguyen N., Nicol R., Norbu C., Norbu N., Novod N., O'Neill B., RA Osman S., Markiewicz E., Oyono O.L., Patti C., Phunkhang P., RA Pierre F., Priest M., Raghuraman S., Rege F., Reyes R., Rise C., RA Rogov P., Ross K., Ryan E., Settipalli S., Shea T., Sherpa N., Shi L., RA Shih D., Sparrow T., Spaulding J., Stalker J., Stange-Thomann N., RA Stavropoulos S., Stone C., Strader C., Tesfaye S., Thomson T., RA Thoulutsang Y., Thoulutsang D., Topham K., Topping I., Tsamla T., RA Vassiliev H., Vo A., Wangchuk T., Wangdi T., Weiand M., Wilkinson J., RA Wilson A., Yadav S., Young G., Yu Q., Zembek L., Zhong D., Zimmer A., RA Zwirko Z., Jaffe D.B., Alvarez P., Brockman W., Butler J., Chin C., RA Gnerre S., Grabherr M., Kleber M., Mauceli E., MacCallum I.; RT "Evolution of genes and genomes on the Drosophila phylogeny."; RL Nature 450:203-218(2007). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CH916369; EDV92832.1; -; Genomic_DNA. DR RefSeq; XP_001989770.1; XM_001989734.1. DR ProteinModelPortal; B4JHK5; -. DR STRING; 7222.FBpp0152884; -. DR EnsemblMetazoa; FBtr0154392; FBpp0152884; FBgn0126445. DR GeneID; 6563233; -. DR KEGG; dgr:Dgri_GH18978; -. DR FlyBase; FBgn0126445; Dgri\GH18978. DR eggNOG; KOG0410; Eukaryota. DR eggNOG; COG2262; LUCA. DR InParanoid; B4JHK5; -. DR OMA; MDTVGFM; -. DR OrthoDB; EOG091G0852; -. DR PhylomeDB; B4JHK5; -. DR Proteomes; UP000001070; Unassembled WGS sequence. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR CDD; cd01878; HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 2. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 4: Predicted; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000001070}; KW Reference proteome {ECO:0000313|Proteomes:UP000001070}. FT DOMAIN 291 462 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 252 284 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 519 AA; 58215 MW; 517F383459FC3BA3 CRC64; MKCLRAALHV AWLPQLRPAT TQILARLKYT QHQGVKGIRS RKSFYEAQMQ AGQQEDSEER SMAMSSGDMR FLDDRAYDEV AGGAMRISRD VATAQHVFIL QPYVKWSAKR TTPNDVRPDD QLIEATALIH SLPNWQVARA LKVPLESLER KTLFGSGKLT ELKQLIAQLR EERHISCVFV SKGTLSFAQK QFLESEFQLP VLDRYSVVIQ ILRLHATTAE ARLQVAMAEL PYIWAQAKDA SATQTRRQGY SLSDLQKEIL RTRERKLRAE LDAVRRQRQL LRQKRKQQNY PIAAVVGYTN AGKTSLIKAL TVEDSLQPRN QLFATLDVTA HAGSLPCNLQ LIYMDTVGFM SDLPTGLFEC FVATLEDAML ADIIIHVQDL SHPCHAAQRA HVESTLRSLA FSVAGGDSSA SQLPPIINVY NKCDLVTPQA QTAAGGHLIS ARAQSGLEPL LMDIEEQILN VTGRRKLQVR VPSGGPEMAW LYKNAAVVNT KADEQNSEKI LMRVVISQRT LDQFKRQFC // ID B4K4X4_DROMO Unreviewed; 522 AA. AC B4K4X4; DT 23-SEP-2008, integrated into UniProtKB/TrEMBL. DT 23-SEP-2008, sequence version 1. DT 30-AUG-2017, entry version 47. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EDW16127.1}; GN Name=Dmoj\GI22404 {ECO:0000313|EMBL:EDW16127.1}; GN ORFNames=Dmoj_GI22404 {ECO:0000313|EMBL:EDW16127.1}, GN GI22404 {ECO:0000313|FlyBase:FBgn0145132}; OS Drosophila mojavensis (Fruit fly). OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; OC Pterygota; Neoptera; Holometabola; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7230 {ECO:0000313|EMBL:EDW16127.1, ECO:0000313|Proteomes:UP000009192}; RN [1] {ECO:0000313|EMBL:EDW16127.1, ECO:0000313|Proteomes:UP000009192} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Tucson 15081-1352.22 {ECO:0000313|Proteomes:UP000009192}; RX PubMed=17994087; DOI=10.1038/nature06341; RG Drosophila 12 Genomes Consortium; RA Clark A.G., Eisen M.B., Smith D.R., Bergman C.M., Oliver B., RA Markow T.A., Kaufman T.C., Kellis M., Gelbart W., Iyer V.N., RA Pollard D.A., Sackton T.B., Larracuente A.M., Singh N.D., Abad J.P., RA Abt D.N., Adryan B., Aguade M., Akashi H., Anderson W.W., RA Aquadro C.F., Ardell D.H., Arguello R., Artieri C.G., Barbash D.A., RA Barker D., Barsanti P., Batterham P., Batzoglou S., Begun D., RA Bhutkar A., Blanco E., Bosak S.A., Bradley R.K., Brand A.D., RA Brent M.R., Brooks A.N., Brown R.H., Butlin R.K., Caggese C., RA Calvi B.R., Bernardo de Carvalho A., Caspi A., Castrezana S., RA Celniker S.E., Chang J.L., Chapple C., Chatterji S., Chinwalla A., RA Civetta A., Clifton S.W., Comeron J.M., Costello J.C., Coyne J.A., RA Daub J., David R.G., Delcher A.L., Delehaunty K., Do C.B., Ebling H., RA Edwards K., Eickbush T., Evans J.D., Filipski A., Findeiss S., RA Freyhult E., Fulton L., Fulton R., Garcia A.C., Gardiner A., RA Garfield D.A., Garvin B.E., Gibson G., Gilbert D., Gnerre S., RA Godfrey J., Good R., Gotea V., Gravely B., Greenberg A.J., RA Griffiths-Jones S., Gross S., Guigo R., Gustafson E.A., Haerty W., RA Hahn M.W., Halligan D.L., Halpern A.L., Halter G.M., Han M.V., RA Heger A., Hillier L., Hinrichs A.S., Holmes I., Hoskins R.A., RA Hubisz M.J., Hultmark D., Huntley M.A., Jaffe D.B., Jagadeeshan S., RA Jeck W.R., Johnson J., Jones C.D., Jordan W.C., Karpen G.H., RA Kataoka E., Keightley P.D., Kheradpour P., Kirkness E.F., RA Koerich L.B., Kristiansen K., Kudrna D., Kulathinal R.J., Kumar S., RA Kwok R., Lander E., Langley C.H., Lapoint R., Lazzaro B.P., Lee S.J., RA Levesque L., Li R., Lin C.F., Lin M.F., Lindblad-Toh K., Llopart A., RA Long M., Low L., Lozovsky E., Lu J., Luo M., Machado C.A., RA Makalowski W., Marzo M., Matsuda M., Matzkin L., McAllister B., RA McBride C.S., McKernan B., McKernan K., Mendez-Lago M., Minx P., RA Mollenhauer M.U., Montooth K., Mount S.M., Mu X., Myers E., Negre B., RA Newfeld S., Nielsen R., Noor M.A., O'Grady P., Pachter L., RA Papaceit M., Parisi M.J., Parisi M., Parts L., Pedersen J.S., RA Pesole G., Phillippy A.M., Ponting C.P., Pop M., Porcelli D., RA Powell J.R., Prohaska S., Pruitt K., Puig M., Quesneville H., RA Ram K.R., Rand D., Rasmussen M.D., Reed L.K., Reenan R., Reily A., RA Remington K.A., Rieger T.T., Ritchie M.G., Robin C., Rogers Y.H., RA Rohde C., Rozas J., Rubenfield M.J., Ruiz A., Russo S., Salzberg S.L., RA Sanchez-Gracia A., Saranga D.J., Sato H., Schaeffer S.W., Schatz M.C., RA Schlenke T., Schwartz R., Segarra C., Singh R.S., Sirot L., Sirota M., RA Sisneros N.B., Smith C.D., Smith T.F., Spieth J., Stage D.E., RA Stark A., Stephan W., Strausberg R.L., Strempel S., Sturgill D., RA Sutton G., Sutton G.G., Tao W., Teichmann S., Tobari Y.N., RA Tomimura Y., Tsolas J.M., Valente V.L., Venter E., Venter J.C., RA Vicario S., Vieira F.G., Vilella A.J., Villasante A., Walenz B., RA Wang J., Wasserman M., Watts T., Wilson D., Wilson R.K., Wing R.A., RA Wolfner M.F., Wong A., Wong G.K., Wu C.I., Wu G., Yamamoto D., RA Yang H.P., Yang S.P., Yorke J.A., Yoshida K., Zdobnov E., Zhang P., RA Zhang Y., Zimin A.V., Baldwin J., Abdouelleil A., Abdulkadir J., RA Abebe A., Abera B., Abreu J., Acer S.C., Aftuck L., Alexander A., RA An P., Anderson E., Anderson S., Arachi H., Azer M., Bachantsang P., RA Barry A., Bayul T., Berlin A., Bessette D., Bloom T., Blye J., RA Boguslavskiy L., Bonnet C., Boukhgalter B., Bourzgui I., Brown A., RA Cahill P., Channer S., Cheshatsang Y., Chuda L., Citroen M., RA Collymore A., Cooke P., Costello M., D'Aco K., Daza R., De Haan G., RA DeGray S., DeMaso C., Dhargay N., Dooley K., Dooley E., Doricent M., RA Dorje P., Dorjee K., Dupes A., Elong R., Falk J., Farina A., Faro S., RA Ferguson D., Fisher S., Foley C.D., Franke A., Friedrich D., RA Gadbois L., Gearin G., Gearin C.R., Giannoukos G., Goode T., RA Graham J., Grandbois E., Grewal S., Gyaltsen K., Hafez N., Hagos B., RA Hall J., Henson C., Hollinger A., Honan T., Huard M.D., Hughes L., RA Hurhula B., Husby M.E., Kamat A., Kanga B., Kashin S., Khazanovich D., RA Kisner P., Lance K., Lara M., Lee W., Lennon N., Letendre F., RA LeVine R., Lipovsky A., Liu X., Liu J., Liu S., Lokyitsang T., RA Lokyitsang Y., Lubonja R., Lui A., MacDonald P., Magnisalis V., RA Maru K., Matthews C., McCusker W., McDonough S., Mehta T., Meldrim J., RA Meneus L., Mihai O., Mihalev A., Mihova T., Mittelman R., Mlenga V., RA Montmayeur A., Mulrain L., Navidi A., Naylor J., Negash T., Nguyen T., RA Nguyen N., Nicol R., Norbu C., Norbu N., Novod N., O'Neill B., RA Osman S., Markiewicz E., Oyono O.L., Patti C., Phunkhang P., RA Pierre F., Priest M., Raghuraman S., Rege F., Reyes R., Rise C., RA Rogov P., Ross K., Ryan E., Settipalli S., Shea T., Sherpa N., Shi L., RA Shih D., Sparrow T., Spaulding J., Stalker J., Stange-Thomann N., RA Stavropoulos S., Stone C., Strader C., Tesfaye S., Thomson T., RA Thoulutsang Y., Thoulutsang D., Topham K., Topping I., Tsamla T., RA Vassiliev H., Vo A., Wangchuk T., Wangdi T., Weiand M., Wilkinson J., RA Wilson A., Yadav S., Young G., Yu Q., Zembek L., Zhong D., Zimmer A., RA Zwirko Z., Jaffe D.B., Alvarez P., Brockman W., Butler J., Chin C., RA Gnerre S., Grabherr M., Kleber M., Mauceli E., MacCallum I.; RT "Evolution of genes and genomes on the Drosophila phylogeny."; RL Nature 450:203-218(2007). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CH933806; EDW16127.1; -; Genomic_DNA. DR RefSeq; XP_002000666.1; XM_002000630.2. DR ProteinModelPortal; B4K4X4; -. DR EnsemblMetazoa; FBtr0173129; FBpp0171621; FBgn0145132. DR GeneID; 6574632; -. DR KEGG; dmo:Dmoj_GI22404; -. DR FlyBase; FBgn0145132; Dmoj\GI22404. DR InParanoid; B4K4X4; -. DR OMA; MDTVGFM; -. DR OrthoDB; EOG091G0852; -. DR PhylomeDB; B4K4X4; -. DR Proteomes; UP000009192; Unassembled WGS sequence. DR Bgee; FBgn0145132; -. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR CDD; cd01878; HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 4: Predicted; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000009192}; KW Reference proteome {ECO:0000313|Proteomes:UP000009192}. FT DOMAIN 286 378 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 252 279 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 522 AA; 58835 MW; 8F88980D227A2B4D CRC64; MNCLQVLLRG TQLRPAITRI STRFRYTQHQ GVKGIRNRKS FYEAPVQPGL HEQNELATVN AGDMRFLDDR AYEEVAGGAM RINRDVATAQ HVFILQPYVK WSAKRTTPVD VTPDDQLAEA TALIHSLPNW KVARSLKVPL ESLERKTLFG SGKIAEIKEL LAQLRNERQV NSVFVSKGTL SFAQRQFLED EFKLPVLDRY SVVIQILRLH ATSAEARLQV AMAELPYIWS QAKDASVTQT RRQGYSLTDQ QKEILRTRER KLRAELDDVR RQRRLLRKKR KQLNCPTAAV VGYTNAGKTS LIKALTMEDT MQPRNQLFAT LDVTAHAGYL PCNLQIIYMD TVGFMSDLPT GLFECFVATL EDAMLADIII HVQDLSHPCH AAQRAHVEAT LRSLAFSVSQ GNSNVGELPP IINVFNKCDL LKPKAQVSVL AEQTDTGMCH LTSARTHAGL QTLLKDVEQQ ILDVTGRRKL QVRVPSGGPE MAWLYKNAAV VDTKADEQNA EKILMRVVIS QCTLDQFMRE FC // ID B4M4L7_DROVI Unreviewed; 525 AA. AC B4M4L7; DT 23-SEP-2008, integrated into UniProtKB/TrEMBL. DT 23-SEP-2008, sequence version 1. DT 30-AUG-2017, entry version 53. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EDW59578.1}; GN Name=Dvir\GJ10964 {ECO:0000313|EMBL:EDW59578.1}; GN ORFNames=Dvir_GJ10964 {ECO:0000313|EMBL:EDW59578.1}, GN GJ10964 {ECO:0000313|FlyBase:FBgn0198232}; OS Drosophila virilis (Fruit fly). OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; OC Pterygota; Neoptera; Holometabola; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7244 {ECO:0000313|EMBL:EDW59578.1, ECO:0000313|Proteomes:UP000008792}; RN [1] {ECO:0000313|EMBL:EDW59578.1, ECO:0000313|Proteomes:UP000008792} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Tucson 15010-1051.87 {ECO:0000313|Proteomes:UP000008792}; RX PubMed=17994087; DOI=10.1038/nature06341; RG Drosophila 12 Genomes Consortium; RA Clark A.G., Eisen M.B., Smith D.R., Bergman C.M., Oliver B., RA Markow T.A., Kaufman T.C., Kellis M., Gelbart W., Iyer V.N., RA Pollard D.A., Sackton T.B., Larracuente A.M., Singh N.D., Abad J.P., RA Abt D.N., Adryan B., Aguade M., Akashi H., Anderson W.W., RA Aquadro C.F., Ardell D.H., Arguello R., Artieri C.G., Barbash D.A., RA Barker D., Barsanti P., Batterham P., Batzoglou S., Begun D., RA Bhutkar A., Blanco E., Bosak S.A., Bradley R.K., Brand A.D., RA Brent M.R., Brooks A.N., Brown R.H., Butlin R.K., Caggese C., RA Calvi B.R., Bernardo de Carvalho A., Caspi A., Castrezana S., RA Celniker S.E., Chang J.L., Chapple C., Chatterji S., Chinwalla A., RA Civetta A., Clifton S.W., Comeron J.M., Costello J.C., Coyne J.A., RA Daub J., David R.G., Delcher A.L., Delehaunty K., Do C.B., Ebling H., RA Edwards K., Eickbush T., Evans J.D., Filipski A., Findeiss S., RA Freyhult E., Fulton L., Fulton R., Garcia A.C., Gardiner A., RA Garfield D.A., Garvin B.E., Gibson G., Gilbert D., Gnerre S., RA Godfrey J., Good R., Gotea V., Gravely B., Greenberg A.J., RA Griffiths-Jones S., Gross S., Guigo R., Gustafson E.A., Haerty W., RA Hahn M.W., Halligan D.L., Halpern A.L., Halter G.M., Han M.V., RA Heger A., Hillier L., Hinrichs A.S., Holmes I., Hoskins R.A., RA Hubisz M.J., Hultmark D., Huntley M.A., Jaffe D.B., Jagadeeshan S., RA Jeck W.R., Johnson J., Jones C.D., Jordan W.C., Karpen G.H., RA Kataoka E., Keightley P.D., Kheradpour P., Kirkness E.F., RA Koerich L.B., Kristiansen K., Kudrna D., Kulathinal R.J., Kumar S., RA Kwok R., Lander E., Langley C.H., Lapoint R., Lazzaro B.P., Lee S.J., RA Levesque L., Li R., Lin C.F., Lin M.F., Lindblad-Toh K., Llopart A., RA Long M., Low L., Lozovsky E., Lu J., Luo M., Machado C.A., RA Makalowski W., Marzo M., Matsuda M., Matzkin L., McAllister B., RA McBride C.S., McKernan B., McKernan K., Mendez-Lago M., Minx P., RA Mollenhauer M.U., Montooth K., Mount S.M., Mu X., Myers E., Negre B., RA Newfeld S., Nielsen R., Noor M.A., O'Grady P., Pachter L., RA Papaceit M., Parisi M.J., Parisi M., Parts L., Pedersen J.S., RA Pesole G., Phillippy A.M., Ponting C.P., Pop M., Porcelli D., RA Powell J.R., Prohaska S., Pruitt K., Puig M., Quesneville H., RA Ram K.R., Rand D., Rasmussen M.D., Reed L.K., Reenan R., Reily A., RA Remington K.A., Rieger T.T., Ritchie M.G., Robin C., Rogers Y.H., RA Rohde C., Rozas J., Rubenfield M.J., Ruiz A., Russo S., Salzberg S.L., RA Sanchez-Gracia A., Saranga D.J., Sato H., Schaeffer S.W., Schatz M.C., RA Schlenke T., Schwartz R., Segarra C., Singh R.S., Sirot L., Sirota M., RA Sisneros N.B., Smith C.D., Smith T.F., Spieth J., Stage D.E., RA Stark A., Stephan W., Strausberg R.L., Strempel S., Sturgill D., RA Sutton G., Sutton G.G., Tao W., Teichmann S., Tobari Y.N., RA Tomimura Y., Tsolas J.M., Valente V.L., Venter E., Venter J.C., RA Vicario S., Vieira F.G., Vilella A.J., Villasante A., Walenz B., RA Wang J., Wasserman M., Watts T., Wilson D., Wilson R.K., Wing R.A., RA Wolfner M.F., Wong A., Wong G.K., Wu C.I., Wu G., Yamamoto D., RA Yang H.P., Yang S.P., Yorke J.A., Yoshida K., Zdobnov E., Zhang P., RA Zhang Y., Zimin A.V., Baldwin J., Abdouelleil A., Abdulkadir J., RA Abebe A., Abera B., Abreu J., Acer S.C., Aftuck L., Alexander A., RA An P., Anderson E., Anderson S., Arachi H., Azer M., Bachantsang P., RA Barry A., Bayul T., Berlin A., Bessette D., Bloom T., Blye J., RA Boguslavskiy L., Bonnet C., Boukhgalter B., Bourzgui I., Brown A., RA Cahill P., Channer S., Cheshatsang Y., Chuda L., Citroen M., RA Collymore A., Cooke P., Costello M., D'Aco K., Daza R., De Haan G., RA DeGray S., DeMaso C., Dhargay N., Dooley K., Dooley E., Doricent M., RA Dorje P., Dorjee K., Dupes A., Elong R., Falk J., Farina A., Faro S., RA Ferguson D., Fisher S., Foley C.D., Franke A., Friedrich D., RA Gadbois L., Gearin G., Gearin C.R., Giannoukos G., Goode T., RA Graham J., Grandbois E., Grewal S., Gyaltsen K., Hafez N., Hagos B., RA Hall J., Henson C., Hollinger A., Honan T., Huard M.D., Hughes L., RA Hurhula B., Husby M.E., Kamat A., Kanga B., Kashin S., Khazanovich D., RA Kisner P., Lance K., Lara M., Lee W., Lennon N., Letendre F., RA LeVine R., Lipovsky A., Liu X., Liu J., Liu S., Lokyitsang T., RA Lokyitsang Y., Lubonja R., Lui A., MacDonald P., Magnisalis V., RA Maru K., Matthews C., McCusker W., McDonough S., Mehta T., Meldrim J., RA Meneus L., Mihai O., Mihalev A., Mihova T., Mittelman R., Mlenga V., RA Montmayeur A., Mulrain L., Navidi A., Naylor J., Negash T., Nguyen T., RA Nguyen N., Nicol R., Norbu C., Norbu N., Novod N., O'Neill B., RA Osman S., Markiewicz E., Oyono O.L., Patti C., Phunkhang P., RA Pierre F., Priest M., Raghuraman S., Rege F., Reyes R., Rise C., RA Rogov P., Ross K., Ryan E., Settipalli S., Shea T., Sherpa N., Shi L., RA Shih D., Sparrow T., Spaulding J., Stalker J., Stange-Thomann N., RA Stavropoulos S., Stone C., Strader C., Tesfaye S., Thomson T., RA Thoulutsang Y., Thoulutsang D., Topham K., Topping I., Tsamla T., RA Vassiliev H., Vo A., Wangchuk T., Wangdi T., Weiand M., Wilkinson J., RA Wilson A., Yadav S., Young G., Yu Q., Zembek L., Zhong D., Zimmer A., RA Zwirko Z., Jaffe D.B., Alvarez P., Brockman W., Butler J., Chin C., RA Gnerre S., Grabherr M., Kleber M., Mauceli E., MacCallum I.; RT "Evolution of genes and genomes on the Drosophila phylogeny."; RL Nature 450:203-218(2007). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CH940652; EDW59578.1; -; Genomic_DNA. DR RefSeq; XP_002056466.1; XM_002056430.2. DR ProteinModelPortal; B4M4L7; -. DR STRING; 7244.FBpp0225381; -. DR EnsemblMetazoa; FBtr0226889; FBpp0225381; FBgn0198232. DR GeneID; 6632660; -. DR KEGG; dvi:Dvir_GJ10964; -. DR FlyBase; FBgn0198232; Dvir\GJ10964. DR eggNOG; KOG0410; Eukaryota. DR eggNOG; COG2262; LUCA. DR InParanoid; B4M4L7; -. DR OMA; MDTVGFM; -. DR OrthoDB; EOG091G0852; -. DR PhylomeDB; B4M4L7; -. DR Proteomes; UP000008792; Unassembled WGS sequence. DR Bgee; FBgn0198232; -. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR CDD; cd01878; HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 4: Predicted; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000008792}; KW Reference proteome {ECO:0000313|Proteomes:UP000008792}. FT DOMAIN 289 468 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 250 282 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 525 AA; 58898 MW; 7547DCD3741BE89A CRC64; MKCLRSVLRV AWPAQLRPFI TQIPARFKYT QHQGVKGIRN RKSFYEAQMQ AGLQEQSDPT AVSSGDMRFL DDRAYDEVAG GAMRISRDVA TAQHVFILQP YVKWSAKRTT PDNVTPDDQL AEATALIHSL PNWQVARSLK VPLESLERKT LFGSGKLTEL KQLMTDLRQE RQVTCLFVSK GTLSFAQKQF LETEFQLPVL DRYSVVIQIL RLHATSAEAR LQVAMAELPY IWALAKDASV TQTRRQGYSL SDLQKEILRT RERKLRAELD GVRRQRQLLR QKRKQQNYPV AAVVGYTNAG KTSLIKALTV QDKLQPRNQL FATLDVTAHA GNLPCNQQLI YMDTVGFMSD LPTGLFECFV ATLEDAMLAD IIIHVQDLSH PCHSAQRAHV ESTLRSLAFS IAGGDPSAGQ LPPIINVYNK CDLLTPKAQL AAVAQLQNTA VGHLISARAQ TGLEPLLKDV EKQILAATGR RKLQVRVPSG GPEMAWLYKN AAVVDTRADE QNAEKILMRV VISQRTLEQF KREFC // ID B4NKS7_DROWI Unreviewed; 523 AA. AC B4NKS7; DT 23-SEP-2008, integrated into UniProtKB/TrEMBL. DT 23-SEP-2008, sequence version 1. DT 07-JUN-2017, entry version 53. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EDW84138.1}; GN Name=Dwil\GK13306 {ECO:0000313|EMBL:EDW84138.1}; GN ORFNames=Dwil_GK13306 {ECO:0000313|EMBL:EDW84138.1}, GN GK13306 {ECO:0000313|FlyBase:FBgn0215315}; OS Drosophila willistoni (Fruit fly). OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; OC Pterygota; Neoptera; Holometabola; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila; Sophophora. OX NCBI_TaxID=7260 {ECO:0000313|EMBL:EDW84138.1, ECO:0000313|Proteomes:UP000007798}; RN [1] {ECO:0000313|EMBL:EDW84138.1, ECO:0000313|Proteomes:UP000007798} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Tucson 14030-0811.24 {ECO:0000313|Proteomes:UP000007798}; RX PubMed=17994087; DOI=10.1038/nature06341; RG Drosophila 12 Genomes Consortium; RA Clark A.G., Eisen M.B., Smith D.R., Bergman C.M., Oliver B., RA Markow T.A., Kaufman T.C., Kellis M., Gelbart W., Iyer V.N., RA Pollard D.A., Sackton T.B., Larracuente A.M., Singh N.D., Abad J.P., RA Abt D.N., Adryan B., Aguade M., Akashi H., Anderson W.W., RA Aquadro C.F., Ardell D.H., Arguello R., Artieri C.G., Barbash D.A., RA Barker D., Barsanti P., Batterham P., Batzoglou S., Begun D., RA Bhutkar A., Blanco E., Bosak S.A., Bradley R.K., Brand A.D., RA Brent M.R., Brooks A.N., Brown R.H., Butlin R.K., Caggese C., RA Calvi B.R., Bernardo de Carvalho A., Caspi A., Castrezana S., RA Celniker S.E., Chang J.L., Chapple C., Chatterji S., Chinwalla A., RA Civetta A., Clifton S.W., Comeron J.M., Costello J.C., Coyne J.A., RA Daub J., David R.G., Delcher A.L., Delehaunty K., Do C.B., Ebling H., RA Edwards K., Eickbush T., Evans J.D., Filipski A., Findeiss S., RA Freyhult E., Fulton L., Fulton R., Garcia A.C., Gardiner A., RA Garfield D.A., Garvin B.E., Gibson G., Gilbert D., Gnerre S., RA Godfrey J., Good R., Gotea V., Gravely B., Greenberg A.J., RA Griffiths-Jones S., Gross S., Guigo R., Gustafson E.A., Haerty W., RA Hahn M.W., Halligan D.L., Halpern A.L., Halter G.M., Han M.V., RA Heger A., Hillier L., Hinrichs A.S., Holmes I., Hoskins R.A., RA Hubisz M.J., Hultmark D., Huntley M.A., Jaffe D.B., Jagadeeshan S., RA Jeck W.R., Johnson J., Jones C.D., Jordan W.C., Karpen G.H., RA Kataoka E., Keightley P.D., Kheradpour P., Kirkness E.F., RA Koerich L.B., Kristiansen K., Kudrna D., Kulathinal R.J., Kumar S., RA Kwok R., Lander E., Langley C.H., Lapoint R., Lazzaro B.P., Lee S.J., RA Levesque L., Li R., Lin C.F., Lin M.F., Lindblad-Toh K., Llopart A., RA Long M., Low L., Lozovsky E., Lu J., Luo M., Machado C.A., RA Makalowski W., Marzo M., Matsuda M., Matzkin L., McAllister B., RA McBride C.S., McKernan B., McKernan K., Mendez-Lago M., Minx P., RA Mollenhauer M.U., Montooth K., Mount S.M., Mu X., Myers E., Negre B., RA Newfeld S., Nielsen R., Noor M.A., O'Grady P., Pachter L., RA Papaceit M., Parisi M.J., Parisi M., Parts L., Pedersen J.S., RA Pesole G., Phillippy A.M., Ponting C.P., Pop M., Porcelli D., RA Powell J.R., Prohaska S., Pruitt K., Puig M., Quesneville H., RA Ram K.R., Rand D., Rasmussen M.D., Reed L.K., Reenan R., Reily A., RA Remington K.A., Rieger T.T., Ritchie M.G., Robin C., Rogers Y.H., RA Rohde C., Rozas J., Rubenfield M.J., Ruiz A., Russo S., Salzberg S.L., RA Sanchez-Gracia A., Saranga D.J., Sato H., Schaeffer S.W., Schatz M.C., RA Schlenke T., Schwartz R., Segarra C., Singh R.S., Sirot L., Sirota M., RA Sisneros N.B., Smith C.D., Smith T.F., Spieth J., Stage D.E., RA Stark A., Stephan W., Strausberg R.L., Strempel S., Sturgill D., RA Sutton G., Sutton G.G., Tao W., Teichmann S., Tobari Y.N., RA Tomimura Y., Tsolas J.M., Valente V.L., Venter E., Venter J.C., RA Vicario S., Vieira F.G., Vilella A.J., Villasante A., Walenz B., RA Wang J., Wasserman M., Watts T., Wilson D., Wilson R.K., Wing R.A., RA Wolfner M.F., Wong A., Wong G.K., Wu C.I., Wu G., Yamamoto D., RA Yang H.P., Yang S.P., Yorke J.A., Yoshida K., Zdobnov E., Zhang P., RA Zhang Y., Zimin A.V., Baldwin J., Abdouelleil A., Abdulkadir J., RA Abebe A., Abera B., Abreu J., Acer S.C., Aftuck L., Alexander A., RA An P., Anderson E., Anderson S., Arachi H., Azer M., Bachantsang P., RA Barry A., Bayul T., Berlin A., Bessette D., Bloom T., Blye J., RA Boguslavskiy L., Bonnet C., Boukhgalter B., Bourzgui I., Brown A., RA Cahill P., Channer S., Cheshatsang Y., Chuda L., Citroen M., RA Collymore A., Cooke P., Costello M., D'Aco K., Daza R., De Haan G., RA DeGray S., DeMaso C., Dhargay N., Dooley K., Dooley E., Doricent M., RA Dorje P., Dorjee K., Dupes A., Elong R., Falk J., Farina A., Faro S., RA Ferguson D., Fisher S., Foley C.D., Franke A., Friedrich D., RA Gadbois L., Gearin G., Gearin C.R., Giannoukos G., Goode T., RA Graham J., Grandbois E., Grewal S., Gyaltsen K., Hafez N., Hagos B., RA Hall J., Henson C., Hollinger A., Honan T., Huard M.D., Hughes L., RA Hurhula B., Husby M.E., Kamat A., Kanga B., Kashin S., Khazanovich D., RA Kisner P., Lance K., Lara M., Lee W., Lennon N., Letendre F., RA LeVine R., Lipovsky A., Liu X., Liu J., Liu S., Lokyitsang T., RA Lokyitsang Y., Lubonja R., Lui A., MacDonald P., Magnisalis V., RA Maru K., Matthews C., McCusker W., McDonough S., Mehta T., Meldrim J., RA Meneus L., Mihai O., Mihalev A., Mihova T., Mittelman R., Mlenga V., RA Montmayeur A., Mulrain L., Navidi A., Naylor J., Negash T., Nguyen T., RA Nguyen N., Nicol R., Norbu C., Norbu N., Novod N., O'Neill B., RA Osman S., Markiewicz E., Oyono O.L., Patti C., Phunkhang P., RA Pierre F., Priest M., Raghuraman S., Rege F., Reyes R., Rise C., RA Rogov P., Ross K., Ryan E., Settipalli S., Shea T., Sherpa N., Shi L., RA Shih D., Sparrow T., Spaulding J., Stalker J., Stange-Thomann N., RA Stavropoulos S., Stone C., Strader C., Tesfaye S., Thomson T., RA Thoulutsang Y., Thoulutsang D., Topham K., Topping I., Tsamla T., RA Vassiliev H., Vo A., Wangchuk T., Wangdi T., Weiand M., Wilkinson J., RA Wilson A., Yadav S., Young G., Yu Q., Zembek L., Zhong D., Zimmer A., RA Zwirko Z., Jaffe D.B., Alvarez P., Brockman W., Butler J., Chin C., RA Gnerre S., Grabherr M., Kleber M., Mauceli E., MacCallum I.; RT "Evolution of genes and genomes on the Drosophila phylogeny."; RL Nature 450:203-218(2007). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CH964272; EDW84138.1; -; Genomic_DNA. DR RefSeq; XP_002073152.1; XM_002073116.1. DR ProteinModelPortal; B4NKS7; -. DR STRING; 7260.FBpp0242449; -. DR EnsemblMetazoa; FBtr0243957; FBpp0242449; FBgn0215315. DR GeneID; 6650389; -. DR KEGG; dwi:Dwil_GK13306; -. DR FlyBase; FBgn0215315; Dwil\GK13306. DR eggNOG; KOG0410; Eukaryota. DR eggNOG; COG2262; LUCA. DR InParanoid; B4NKS7; -. DR OMA; MDTVGFM; -. DR OrthoDB; EOG091G0852; -. DR PhylomeDB; B4NKS7; -. DR Proteomes; UP000007798; Unassembled WGS sequence. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR CDD; cd01878; HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 4: Predicted; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000007798}; KW Reference proteome {ECO:0000313|Proteomes:UP000007798}. FT DOMAIN 296 466 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 257 292 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 523 AA; 59363 MW; 4826ABACEDC0D045 CRC64; MAGLRNFIKL AKWRPTLSLA LASQQRSKYT QHQGVKGIRN RKSYFEAQMQ QGKRDDDNDE QNGDSRSSGE LFDMRFLDDR AYDEVAGGAM RITRNVATSQ QVLILQPYVK WSAKRNLPQD VKPEDQLAEA TALIRSLPNW QVAKALKVPL ENLKRRTLFG SGKIDELKTL IADLRQEMSL TCLFVSKGTL SFAQKRYLEE EFHLPVMDRY SVVIQILRLH ATSAEARLQV AMAELPYIWS QAKDASASQI RRQGYALSDL QKEILKTRER KLRAELEQVR RHRQLLRQKR KQQNYPIISV VGYTNAGKTS LIKALTAESD ALQPRNQLFA TLDVTAHAGQ LPCNLQVIYM DTVGFMSDLP TGLFECFVAT LEDAMLADII IHVQDISHPC HNAQRNHVES TLRSLAFNVG GEHQPPIINV FNKCDLVPNA DDHAEESTAH HRISARSQIG LDPLLLDIEA QILSVTGRRK IQMRVPSGGP EMAWLYKNAA VIDTQADLEN PQRLLMQVVI SQRTLEQFKR EFC // ID B4QUW9_DROSI Unreviewed; 526 AA. AC B4QUW9; DT 23-SEP-2008, integrated into UniProtKB/TrEMBL. DT 23-SEP-2008, sequence version 1. DT 30-AUG-2017, entry version 45. DE SubName: Full=GD21220 {ECO:0000313|EMBL:EDX14435.1}; GN Name=Dsim\GD21220 {ECO:0000313|EMBL:EDX14435.1}; GN ORFNames=Dsim_GD21220 {ECO:0000313|EMBL:EDX14435.1}, GN GD21220 {ECO:0000313|FlyBase:FBgn0192671}; OS Drosophila simulans (Fruit fly). OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; OC Pterygota; Neoptera; Holometabola; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila; Sophophora. OX NCBI_TaxID=7240 {ECO:0000313|EMBL:EDX14435.1, ECO:0000313|Proteomes:UP000000304}; RN [1] {ECO:0000313|EMBL:EDX14435.1, ECO:0000313|Proteomes:UP000000304} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Mixed {ECO:0000313|EMBL:EDX14435.1}; RX PubMed=17994087; DOI=10.1038/nature06341; RG Drosophila 12 Genomes Consortium; RA Clark A.G., Eisen M.B., Smith D.R., Bergman C.M., Oliver B., RA Markow T.A., Kaufman T.C., Kellis M., Gelbart W., Iyer V.N., RA Pollard D.A., Sackton T.B., Larracuente A.M., Singh N.D., Abad J.P., RA Abt D.N., Adryan B., Aguade M., Akashi H., Anderson W.W., RA Aquadro C.F., Ardell D.H., Arguello R., Artieri C.G., Barbash D.A., RA Barker D., Barsanti P., Batterham P., Batzoglou S., Begun D., RA Bhutkar A., Blanco E., Bosak S.A., Bradley R.K., Brand A.D., RA Brent M.R., Brooks A.N., Brown R.H., Butlin R.K., Caggese C., RA Calvi B.R., Bernardo de Carvalho A., Caspi A., Castrezana S., RA Celniker S.E., Chang J.L., Chapple C., Chatterji S., Chinwalla A., RA Civetta A., Clifton S.W., Comeron J.M., Costello J.C., Coyne J.A., RA Daub J., David R.G., Delcher A.L., Delehaunty K., Do C.B., Ebling H., RA Edwards K., Eickbush T., Evans J.D., Filipski A., Findeiss S., RA Freyhult E., Fulton L., Fulton R., Garcia A.C., Gardiner A., RA Garfield D.A., Garvin B.E., Gibson G., Gilbert D., Gnerre S., RA Godfrey J., Good R., Gotea V., Gravely B., Greenberg A.J., RA Griffiths-Jones S., Gross S., Guigo R., Gustafson E.A., Haerty W., RA Hahn M.W., Halligan D.L., Halpern A.L., Halter G.M., Han M.V., RA Heger A., Hillier L., Hinrichs A.S., Holmes I., Hoskins R.A., RA Hubisz M.J., Hultmark D., Huntley M.A., Jaffe D.B., Jagadeeshan S., RA Jeck W.R., Johnson J., Jones C.D., Jordan W.C., Karpen G.H., RA Kataoka E., Keightley P.D., Kheradpour P., Kirkness E.F., RA Koerich L.B., Kristiansen K., Kudrna D., Kulathinal R.J., Kumar S., RA Kwok R., Lander E., Langley C.H., Lapoint R., Lazzaro B.P., Lee S.J., RA Levesque L., Li R., Lin C.F., Lin M.F., Lindblad-Toh K., Llopart A., RA Long M., Low L., Lozovsky E., Lu J., Luo M., Machado C.A., RA Makalowski W., Marzo M., Matsuda M., Matzkin L., McAllister B., RA McBride C.S., McKernan B., McKernan K., Mendez-Lago M., Minx P., RA Mollenhauer M.U., Montooth K., Mount S.M., Mu X., Myers E., Negre B., RA Newfeld S., Nielsen R., Noor M.A., O'Grady P., Pachter L., RA Papaceit M., Parisi M.J., Parisi M., Parts L., Pedersen J.S., RA Pesole G., Phillippy A.M., Ponting C.P., Pop M., Porcelli D., RA Powell J.R., Prohaska S., Pruitt K., Puig M., Quesneville H., RA Ram K.R., Rand D., Rasmussen M.D., Reed L.K., Reenan R., Reily A., RA Remington K.A., Rieger T.T., Ritchie M.G., Robin C., Rogers Y.H., RA Rohde C., Rozas J., Rubenfield M.J., Ruiz A., Russo S., Salzberg S.L., RA Sanchez-Gracia A., Saranga D.J., Sato H., Schaeffer S.W., Schatz M.C., RA Schlenke T., Schwartz R., Segarra C., Singh R.S., Sirot L., Sirota M., RA Sisneros N.B., Smith C.D., Smith T.F., Spieth J., Stage D.E., RA Stark A., Stephan W., Strausberg R.L., Strempel S., Sturgill D., RA Sutton G., Sutton G.G., Tao W., Teichmann S., Tobari Y.N., RA Tomimura Y., Tsolas J.M., Valente V.L., Venter E., Venter J.C., RA Vicario S., Vieira F.G., Vilella A.J., Villasante A., Walenz B., RA Wang J., Wasserman M., Watts T., Wilson D., Wilson R.K., Wing R.A., RA Wolfner M.F., Wong A., Wong G.K., Wu C.I., Wu G., Yamamoto D., RA Yang H.P., Yang S.P., Yorke J.A., Yoshida K., Zdobnov E., Zhang P., RA Zhang Y., Zimin A.V., Baldwin J., Abdouelleil A., Abdulkadir J., RA Abebe A., Abera B., Abreu J., Acer S.C., Aftuck L., Alexander A., RA An P., Anderson E., Anderson S., Arachi H., Azer M., Bachantsang P., RA Barry A., Bayul T., Berlin A., Bessette D., Bloom T., Blye J., RA Boguslavskiy L., Bonnet C., Boukhgalter B., Bourzgui I., Brown A., RA Cahill P., Channer S., Cheshatsang Y., Chuda L., Citroen M., RA Collymore A., Cooke P., Costello M., D'Aco K., Daza R., De Haan G., RA DeGray S., DeMaso C., Dhargay N., Dooley K., Dooley E., Doricent M., RA Dorje P., Dorjee K., Dupes A., Elong R., Falk J., Farina A., Faro S., RA Ferguson D., Fisher S., Foley C.D., Franke A., Friedrich D., RA Gadbois L., Gearin G., Gearin C.R., Giannoukos G., Goode T., RA Graham J., Grandbois E., Grewal S., Gyaltsen K., Hafez N., Hagos B., RA Hall J., Henson C., Hollinger A., Honan T., Huard M.D., Hughes L., RA Hurhula B., Husby M.E., Kamat A., Kanga B., Kashin S., Khazanovich D., RA Kisner P., Lance K., Lara M., Lee W., Lennon N., Letendre F., RA LeVine R., Lipovsky A., Liu X., Liu J., Liu S., Lokyitsang T., RA Lokyitsang Y., Lubonja R., Lui A., MacDonald P., Magnisalis V., RA Maru K., Matthews C., McCusker W., McDonough S., Mehta T., Meldrim J., RA Meneus L., Mihai O., Mihalev A., Mihova T., Mittelman R., Mlenga V., RA Montmayeur A., Mulrain L., Navidi A., Naylor J., Negash T., Nguyen T., RA Nguyen N., Nicol R., Norbu C., Norbu N., Novod N., O'Neill B., RA Osman S., Markiewicz E., Oyono O.L., Patti C., Phunkhang P., RA Pierre F., Priest M., Raghuraman S., Rege F., Reyes R., Rise C., RA Rogov P., Ross K., Ryan E., Settipalli S., Shea T., Sherpa N., Shi L., RA Shih D., Sparrow T., Spaulding J., Stalker J., Stange-Thomann N., RA Stavropoulos S., Stone C., Strader C., Tesfaye S., Thomson T., RA Thoulutsang Y., Thoulutsang D., Topham K., Topping I., Tsamla T., RA Vassiliev H., Vo A., Wangchuk T., Wangdi T., Weiand M., Wilkinson J., RA Wilson A., Yadav S., Young G., Yu Q., Zembek L., Zhong D., Zimmer A., RA Zwirko Z., Jaffe D.B., Alvarez P., Brockman W., Butler J., Chin C., RA Gnerre S., Grabherr M., Kleber M., Mauceli E., MacCallum I.; RT "Evolution of genes and genomes on the Drosophila phylogeny."; RL Nature 450:203-218(2007). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CM000364; EDX14435.1; -; Genomic_DNA. DR RefSeq; XP_016036259.1; XM_016177525.1. DR ProteinModelPortal; B4QUW9; -. DR EnsemblMetazoa; FBtr0221130; FBpp0219622; FBgn0192671. DR GeneID; 6729624; -. DR KEGG; dsi:Dsimw501_GD21220; -. DR FlyBase; FBgn0192671; Dsim\GD21220. DR OMA; MDTVGFM; -. DR OrthoDB; EOG091G0852; -. DR PhylomeDB; B4QUW9; -. DR Proteomes; UP000000304; Chromosome 3R. DR Bgee; FBgn0192671; -. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR CDD; cd01878; HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 4: Predicted; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000000304}; KW Reference proteome {ECO:0000313|Proteomes:UP000000304}. FT DOMAIN 296 468 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 257 289 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 526 AA; 59246 MW; BD68EC4E0479803F CRC64; MSALRIFARL VSTRTLRIRP ILEIPARCKY TQHQGVKGIR NRKSFYEAQI QAGQQGEEDE DLERTASSDL ADMRFLDDRA YDEVAGGAMR ITRDIASSQQ VLILQPYVKW AAKRHSGPVD VRPEDQLAEA SALIHSLPNW QVARALKVPL ESLEKKTLFG SGKLVELKEL VAELRQERHL TCLFVSKGTL SFAQKRFLEA EFRLPVMDRY SVVIQILRLH ATSAEAKLQV AMAELPYIWA QAKDSSVTQT RRQGYALTDL QKEILRTRER KLRAELDRVR RQRQLLRQKR KQQNYPIVAV VGYTNAGKTS LIKALTVEDA LQPRNQLFAT LDVTAHAGCL PCNLEVIYMD TVGFMSDLPT GLFECFVATL EDAMLADVIV HVQDLSHPCH AAQRSHVEAT LRSLAFNVAG GDSTASQLPP IINVYNKCDL VSQEAQSSSD PVHHISARAQ TGLEPLLDDI EKQILTATGR RKLQMRVPSG GPEMAWLYKN AAVVETTADA ENPERLMMHV VISQRTLDQF KRQFCR // ID B4RBT9_PHEZH Unreviewed; 424 AA. AC B4RBT9; DT 23-SEP-2008, integrated into UniProtKB/TrEMBL. DT 23-SEP-2008, sequence version 1. DT 07-JUN-2017, entry version 62. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=PHZ_c1725 {ECO:0000313|EMBL:ACG78136.1}; OS Phenylobacterium zucineum (strain HLK1). OC Bacteria; Proteobacteria; Alphaproteobacteria; Caulobacterales; OC Caulobacteraceae; Phenylobacterium. OX NCBI_TaxID=450851 {ECO:0000313|EMBL:ACG78136.1, ECO:0000313|Proteomes:UP000001868}; RN [1] {ECO:0000313|EMBL:ACG78136.1, ECO:0000313|Proteomes:UP000001868} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=HLK1 {ECO:0000313|EMBL:ACG78136.1, RC ECO:0000313|Proteomes:UP000001868}; RX PubMed=18700039; DOI=10.1186/1471-2164-9-386; RA Luo Y., Xu X., Ding Z., Liu Z., Zhang B., Yan Z., Sun J., Hu S., RA Hu X.; RT "Complete genome of Phenylobacterium zucineum - a novel facultative RT intracellular bacterium isolated from human erythroleukemia cell line RT K562."; RL BMC Genomics 9:386-386(2008). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000747; ACG78136.1; -; Genomic_DNA. DR RefSeq; WP_012522278.1; NC_011144.1. DR ProteinModelPortal; B4RBT9; -. DR STRING; 450851.PHZ_c1725; -. DR EnsemblBacteria; ACG78136; ACG78136; PHZ_c1725. DR KEGG; pzu:PHZ_c1725; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000001868; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000001868}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000001868}. FT DOMAIN 192 363 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 424 AA; 46962 MW; 32743C92F6574C38 CRC64; MIHPDREGRT SAVRDPQARL EEAVGLAQAL DLEVRETLVA PLRRLTPATL FGKGKVEEVA AVVDSVEADV VVVDDALTPV QQRNLEKAWK AKVIDRTGLI LEIFARRART REGRLQVELA RLTYERSRLV RTWTHLERQR GGFGVMGGPG ETQIETDRRL LAEKIGKLKR ELVEVRRTRT LQRSARRRVP YPTVALVGYT NAGKSTLFNR LTQAEVLAQD MLFATLDPTL RMLKLPDGRP AILSDTVGFI SDLPHELVEA FRATLEEVRE ADVVLHVRDI ASEETEAQAQ DVRTVLQRLG VDMDERRILE VWNKVDLLPA DERQDAAGDA RRAHPPAILV SAVTGEGCDD LLRAVGALVD EAPPVDVYAP AGEGAAIAWL YRHGRVVERV EGKDGSVRLA VSLSPQALGQ FEQLFPHAEV RGAG // ID B4S8Y9_PROA2 Unreviewed; 433 AA. AC B4S8Y9; DT 23-SEP-2008, integrated into UniProtKB/TrEMBL. DT 23-SEP-2008, sequence version 1. DT 07-JUN-2017, entry version 62. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Paes_1506 {ECO:0000313|EMBL:ACF46526.1}; OS Prosthecochloris aestuarii (strain DSM 271 / SK 413). OC Bacteria; Chlorobi; Chlorobia; Chlorobiales; Chlorobiaceae; OC Prosthecochloris. OX NCBI_TaxID=290512 {ECO:0000313|EMBL:ACF46526.1, ECO:0000313|Proteomes:UP000002725}; RN [1] {ECO:0000313|EMBL:ACF46526.1, ECO:0000313|Proteomes:UP000002725} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 271 / SK 413 {ECO:0000313|Proteomes:UP000002725}; RG US DOE Joint Genome Institute; RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., RA Tice H., Bruce D., Goodwin L., Pitluck S., Schmutz J., Larimer F., RA Land M., Hauser L., Kyrpides N., Anderson I., Liu Z., Li T., Zhao F., RA Overmann J., Bryant D.A., Richardson P.; RT "Complete sequence of chromosome of Prosthecochloris aestuarii DSM RT 271."; RL Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001108; ACF46526.1; -; Genomic_DNA. DR RefSeq; WP_012506059.1; NC_011059.1. DR ProteinModelPortal; B4S8Y9; -. DR STRING; 290512.Paes_1506; -. DR EnsemblBacteria; ACF46526; ACF46526; Paes_1506. DR KEGG; paa:Paes_1506; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000002725; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000002725}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000002725}. FT DOMAIN 203 370 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 433 AA; 49229 MW; E53274499E908B8E CRC64; MDTYFSSEIT RETALLVGVS ATPELPRALV EDYLDELAFL ADTAGADVVA RIVQERKVKD PAWFIGKGKV DEMSHIVEGG QIDLVIFDDD LTPVQARNLE KAFDCKVLDR TELILQIFAI RAKSSQAKMQ VELAQLEYLL PRLTRLWTHL SKQKGGIGTK GPGETQIETD RRLVRNRISL LKKKLKDLSL QHATQTKDRA DIARVALVGY TNAGKSTLMN RLCPSAGAYA EDRLFATLDT KTRRLELRIN KVVLLSDTVG FIRKLPHHLV ECFRSTLDEV LQADFLLHII DVSHPGFEEQ MIVVRKTLEE IGVRHDNIID VFNKVDALDD AEKLRGLREH YPEALFVSAT RGLNLNALKE AISDYVGRQY HERHIRTHVS NYKLIGYIYQ HAEVLDKGYE DEDVILTYRA HTRNLKHIDA RIRAFENSES HVA // ID B4SB20_PELPB Unreviewed; 434 AA. AC B4SB20; DT 23-SEP-2008, integrated into UniProtKB/TrEMBL. DT 23-SEP-2008, sequence version 1. DT 07-JUN-2017, entry version 56. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Ppha_1731 {ECO:0000313|EMBL:ACF43966.1}; OS Pelodictyon phaeoclathratiforme (strain DSM 5477 / BU-1). OC Bacteria; Chlorobi; Chlorobia; Chlorobiales; Chlorobiaceae; OC Chlorobium/Pelodictyon group; Pelodictyon. OX NCBI_TaxID=324925 {ECO:0000313|EMBL:ACF43966.1, ECO:0000313|Proteomes:UP000002724}; RN [1] {ECO:0000313|EMBL:ACF43966.1, ECO:0000313|Proteomes:UP000002724} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 5477 / BU-1 {ECO:0000313|Proteomes:UP000002724}; RG US DOE Joint Genome Institute; RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., RA Tice H., Bruce D., Goodwin L., Pitluck S., Schmutz J., Larimer F., RA Land M., Hauser L., Kyrpides N., Mikhailova N., Liu Z., Li T., RA Zhao F., Overmann J., Bryant D.A., Richardson P.; RT "Complete sequence of Pelodictyon phaeoclathratiforme BU-1."; RL Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001110; ACF43966.1; -; Genomic_DNA. DR RefSeq; WP_012508453.1; NC_011060.1. DR ProteinModelPortal; B4SB20; -. DR STRING; 324925.Ppha_1731; -. DR EnsemblBacteria; ACF43966; ACF43966; Ppha_1731. DR KEGG; pph:Ppha_1731; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000002724; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000002724}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000002724}. FT DOMAIN 202 369 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 434 AA; 49181 MW; 9D1C3A224E96E903 CRC64; MNTVTSENRR EKAVLVGLCS PPEIPRSLVE EYLDELAFLA DTAGADTVES FIQDKKLRDP AYCIGKGKVE ELVLFVKEKE IDLVIFDDDL SPAQARNLEK SLECKVIDRT GLILQIFAIR AQSAQAKMQV ELAQLEYMLP RLSGQWTHLS KQKGGIGNKG PGETQIETDR RLVRNRIALL KKKLREVSLQ HDTQTRGRQT VPRVSLVGYT NAGKSTLMNA LCPEAEAFAE NRLFATLDTK TRRLELNINK LVLLSDTVGF IRKLPHTLVE SFKSTLDEVL QADFLLHVID ISHPGFEDQM QIVRDTLKEI GVGHDNIIDV FNKIDALEDP SILRTMSEKY PDAVFISARR GLNLSLLKEM IGQQVARDYS ERKISVHVSN YKLITWLYEH TEVIDKRHVD EEVELTFRVR KNELKHIDAL INSSQTLIDD AANP // ID B4U9V5_HYDS0 Unreviewed; 370 AA. AC B4U9V5; DT 23-SEP-2008, integrated into UniProtKB/TrEMBL. DT 23-SEP-2008, sequence version 1. DT 07-JUN-2017, entry version 70. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=HY04AAS1_1231 {ECO:0000313|EMBL:ACG57916.1}; OS Hydrogenobaculum sp. (strain Y04AAS1). OC Bacteria; Aquificae; Aquificales; Aquificaceae; Hydrogenobaculum. OX NCBI_TaxID=380749 {ECO:0000313|EMBL:ACG57916.1, ECO:0000313|Proteomes:UP000001872}; RN [1] {ECO:0000313|Proteomes:UP000001872} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Y04AAS1 {ECO:0000313|Proteomes:UP000001872}; RX PubMed=19136599; DOI=10.1128/JB.01645-08; RA Reysenbach A.-L., Hamamura N., Podar M., Griffiths E., Ferreira S., RA Hochstein R., Heidelberg J., Johnson J., Mead D., Pohorille A., RA Sarmiento M., Schweighofer K., Seshadri R., Voytek M.A.; RT "Complete and draft genome sequences of six members of the RT Aquificales."; RL J. Bacteriol. 191:1992-1993(2009). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001130; ACG57916.1; -; Genomic_DNA. DR RefSeq; WP_012514272.1; NC_011126.1. DR ProteinModelPortal; B4U9V5; -. DR STRING; 380749.HY04AAS1_1231; -. DR EnsemblBacteria; ACG57916; ACG57916; HY04AAS1_1231. DR KEGG; hya:HY04AAS1_1231; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000001872; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000001872}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000001872}. FT DOMAIN 194 363 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 370 AA; 42219 MW; D592978971B9A80F CRC64; MIKAISVALQ LRHQTRSQVL ESLEELEGLV EAIGGKSVGY LVKKRDFPDA STLVGSSYLN LIKELVEGTG SNTVVFDEFL SPSQVRNIES FLGVSVLDRA NVVFEIFMAR AKTQQAKLQI ELAKLTYELP RLYGVGTKLS RQSGKMGTRG PGEQLIEIKR RAIQKRIYKI KEEIEQIKKH HKEQRKNRLK TNYLKVALVG YTNAGKSSLM KALTKKNVFI SDMLFATLDT KVGTSFIDGE KIFITDTVGF IDRLPPELVE SFKTTLEEVT LADLLVFVVD ISDHRWLKKI DVVNKILEDI GVKDKPILYV FNKIDRLVSS KEYIVGFEKE FFFEKPYVLV SSEKDWNIDV LLERIKSYYK AHFDLGYIYA // ID B4VD87_9ACTN Unreviewed; 510 AA. AC B4VD87; DT 23-SEP-2008, integrated into UniProtKB/TrEMBL. DT 23-SEP-2008, sequence version 1. DT 07-JUN-2017, entry version 55. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=M444_25580 {ECO:0000313|EMBL:AKL68235.1}, GN SSAG_05715 {ECO:0000313|EMBL:EDX25924.1}; OS Streptomyces sp. Mg1. OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae; OC Streptomyces. OX NCBI_TaxID=465541 {ECO:0000313|EMBL:EDX25924.1, ECO:0000313|Proteomes:UP000005764}; RN [1] {ECO:0000313|EMBL:EDX25924.1, ECO:0000313|Proteomes:UP000005764} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Mg1 {ECO:0000313|EMBL:EDX25924.1, RC ECO:0000313|Proteomes:UP000005764}; RG The Broad Institute Genome Sequencing Platform; RA Fischbach M., Ward D., Young S., Jaffe D., Gnerre S., Berlin A., RA Heiman D., Hepburn T., Sykes S., Mehta T., Alvarado L., Kodira C.D., RA Straight P., Clardy J., Hung D., Kolter R., Mekalanos J., Walker S., RA Walsh C.T., Lander E., Galagan J., Nusbaum C., Birren B.; RT "Annotation of Streptomyces sp. Mg1."; RL Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:AKL68235.1, ECO:0000313|Proteomes:UP000035653} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Mg1 {ECO:0000313|EMBL:AKL68235.1, RC ECO:0000313|Proteomes:UP000035653}; RX PubMed=23908282; RA Hoefler B.C., Konganti K., Straight P.D.; RT "De Novo Assembly of the Streptomyces sp. Strain Mg1 Genome Using RT PacBio Single-Molecule Sequencing."; RL Genome Announc. 1:e00535-13(2013). RN [3] {ECO:0000313|EMBL:AKL68235.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=Mg1 {ECO:0000313|EMBL:AKL68235.1}; RA Hoefler B.C., Straight P.D.; RL Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP011664; AKL68235.1; -; Genomic_DNA. DR EMBL; DS570436; EDX25924.1; -; Genomic_DNA. DR RefSeq; WP_008742941.1; NZ_DS570436.1. DR STRING; 465541.SSAG_05715; -. DR EnsemblBacteria; AKL68235; AKL68235; M444_25580. DR EnsemblBacteria; EDX25924; EDX25924; SSAG_05715. DR KEGG; strm:M444_25580; -. DR PATRIC; fig|465541.12.peg.5402; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR KO; K03665; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000005764; Unassembled WGS sequence. DR Proteomes; UP000035653; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000313|EMBL:AKL68235.1}; KW Complete proteome {ECO:0000313|Proteomes:UP000035653}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900, KW ECO:0000313|EMBL:AKL68235.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000035653}. FT DOMAIN 289 454 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 510 AA; 55615 MW; ACFD018E7D718706 CRC64; MTSSSSPSQD ARDARDARDA RDARDASDPQ SFTESLRADA LMEEDVAWSH AIDGDRDGDQ FERSERAALR RVVGLSTELE DVTEVEYRQL RLERVVLVGV WTSGTVNDAE NSLAELAALA ETAGALVLDG VIQRRDKPDP ATFIGSGKAR ELRDIVLESG ADTVVCDGEL SPGQLIALED VVKVKVVDRT ALILDIFAQH AKSREGKAQV ALAQMQYMLP RLRGWGASLS RQMGGGGGGG MATRGPGETK IETDRRRIRE KMAKMRREIA EMKTGREIKR QERRRNKVPS VAIAGYTNAG KSSLLNRLTG AGVLVENALF ATLDPTVRRA ETPSGRIYTL ADTVGFVRHL PHHLVEAFRS TMEEVGDSDL ILHIVDGSHP APEEQLAAVR EVIREVGAVN VPEIVVINKA DAADPLVLQR LLRIERHSIA VSARTGMGIA KLLELIDTEL PRPEVEVEAL VPYTRGSLIA RAHAEGEVIS EEHTPEGTLL KARVHQELAA DLAPYVPAKH // ID B4VUP7_9CYAN Unreviewed; 532 AA. AC B4VUP7; DT 23-SEP-2008, integrated into UniProtKB/TrEMBL. DT 23-SEP-2008, sequence version 1. DT 07-JUN-2017, entry version 46. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=MC7420_3998 {ECO:0000313|EMBL:EDX74474.1}; OS Coleofasciculus chthonoplastes PCC 7420. OC Bacteria; Cyanobacteria; Oscillatoriophycideae; Oscillatoriales; OC Coleofasciculaceae; Coleofasciculus. OX NCBI_TaxID=118168 {ECO:0000313|EMBL:EDX74474.1, ECO:0000313|Proteomes:UP000003835}; RN [1] {ECO:0000313|EMBL:EDX74474.1, ECO:0000313|Proteomes:UP000003835} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=PCC 7420 {ECO:0000313|EMBL:EDX74474.1, RC ECO:0000313|Proteomes:UP000003835}; RA Tandeau de Marsac N., Ferriera S., Johnson J., Kravitz S., Beeson K., RA Sutton G., Rogers Y.-H., Friedman R., Frazier M., Venter J.C.; RL Submitted (JUL-2008) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; DS989853; EDX74474.1; -; Genomic_DNA. DR ProteinModelPortal; B4VUP7; -. DR STRING; 118168.MC7420_3998; -. DR EnsemblBacteria; EDX74474; EDX74474; MC7420_3998. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000003835; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000003835}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000003835}. FT DOMAIN 358 528 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 317 351 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 532 AA; 58717 MW; 004612C1621684DA CRC64; MAAISADIKQ PLCTYLNRRG QVIRVGVGTP TQTKIPPLDL PRYGAERLCG IRCIATQLKS HTPRNADLTA MAIQRLDALV LLTVSESGFE RRGGGATGYV NETYLAHLIP VTQSSKQDND GQPSWHLSPA LSLDLLTKQD FFDLVEGLEA EFRREFIAQH VDVDQDRVLI VGLMTGNMNK GQFEDGLAEI ARLVQTAGGE VLQTLRQRRS QPHPQTVVGA GKVQEIALTV QTLGTNLVVF DRDLSPAQVR NLEAQTGVRV VDRTEVILDI FAQRAQSRAG KLQVELAQLE YMLPRLTGRG QAMSRLGGGI GTRGPGETKL ETERRAIQRR IARLQQEVNQ LQAHRSRMRQ RRQKQDVPTI SVVGYTNAGK STLLNTLTNA EVYTADQLFA TLDPTTRRLP ITYAETGESI TVLLTDTVGF IHELPPPLVD SFRATLEEVT EADALIHLVD LSHPAWQNHI RSVMSILADM PVTPGPILVV FNKIDDVDSD TLVLAQEEFP QGVFVSASKR LGLETLRQKI AQLVDYAIAP QM // ID B4WMK9_SYNS7 Unreviewed; 588 AA. AC B4WMK9; DT 23-SEP-2008, integrated into UniProtKB/TrEMBL. DT 23-SEP-2008, sequence version 1. DT 07-JUN-2017, entry version 52. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=S7335_4544 {ECO:0000313|EMBL:EDX86837.1}; OS Synechococcus sp. (strain ATCC 29403 / PCC 7335). OC Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; OC Synechococcus. OX NCBI_TaxID=91464 {ECO:0000313|EMBL:EDX86837.1, ECO:0000313|Proteomes:UP000005766}; RN [1] {ECO:0000313|EMBL:EDX86837.1, ECO:0000313|Proteomes:UP000005766} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29403 / PCC 7335 {ECO:0000313|Proteomes:UP000005766}; RA Tandeau de Marsac N., Ferriera S., Johnson J., Kravitz S., Beeson K., RA Sutton G., Rogers Y.-H., Friedman R., Frazier M., Venter J.C.; RL Submitted (JUL-2008) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; DS989904; EDX86837.1; -; Genomic_DNA. DR ProteinModelPortal; B4WMK9; -. DR STRING; 91464.S7335_4544; -. DR EnsemblBacteria; EDX86837; EDX86837; S7335_4544. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR OMA; EREVIIT; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000005766; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000005766}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000005766}. FT DOMAIN 416 586 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 375 409 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 588 AA; 65527 MW; 7DF700A2A32D325E CRC64; MVGDRPFIPS RFLKIESTYT KVLQEHPIEK IYGELKGLKS SQLKELQRIY HQRLPIDRVT TPEFAQRLAA VSTDINQAIC AYVDRRGHVI RVGVGSPRKT QIPVLELPRY GAERLCGIRC IATQLKLEPP SHSVLTAMAI QRLDAMALLT LTGTGFKRKG GGATGYIRDA YLAHLVPNPK EQWAVSDPLS LEALDQQDFL NLAESLEEEF RREFIAQQVD SDHDRVLVVG LLTEKMAEES FRNGLAEIER LVETAGGDVL QVTKQKRSRP HPQTVIGAGK VDEIALSVQT LGANLIVFNR DLSPGQIRNL EKHVGVRVVD RTELILDIFA QRAKSGEGKL QVELAQLEYQ LPRLTGRGQA MSRLGGGIGT RGPGETKLET ERRAIQKRIT RLQAEVNQLQ AHRTRLRQRR QANSVPSVAI IGYTNAGKST LLNHLTESEV YAADQLFATL DPTTRRVVIN DEETHELQSL VLTDTVGFIQ DLPPALMDAF RATLEEVTEA DALIHVVDAS HHAWKDHIHS VMKLLGQMPI APGPILLVFN KLDQTDTDAL EVAKDEYPQA VFVSVAKNLG MDTLRQKILQ LVHYAITH // ID B5CRC1_9FIRM Unreviewed; 413 AA. AC B5CRC1; DT 14-OCT-2008, integrated into UniProtKB/TrEMBL. DT 14-OCT-2008, sequence version 1. DT 05-JUL-2017, entry version 41. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:EDY32143.1}; GN ORFNames=RUMLAC_02022 {ECO:0000313|EMBL:EDY32143.1}; OS Ruminococcus lactaris ATCC 29176. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Ruminococcaceae; OC Ruminococcus. OX NCBI_TaxID=471875 {ECO:0000313|EMBL:EDY32143.1, ECO:0000313|Proteomes:UP000003254}; RN [1] {ECO:0000313|EMBL:EDY32143.1, ECO:0000313|Proteomes:UP000003254} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29176 {ECO:0000313|EMBL:EDY32143.1, RC ECO:0000313|Proteomes:UP000003254}; RA Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., RA Liep D., Gordon J.; RT "Draft genome sequence of Ruminococcus lactaris ATCC 29176."; RL Submitted (AUG-2008) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:EDY32143.1, ECO:0000313|Proteomes:UP000003254} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29176 {ECO:0000313|EMBL:EDY32143.1, RC ECO:0000313|Proteomes:UP000003254}; RA Fulton L., Clifton S., Fulton B., Xu J., Minx P., Pepin K.H., RA Johnson M., Bhonagiri V., Nash W.E., Mardis E.R., Wilson R.K.; RL Submitted (AUG-2008) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EDY32143.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABOU02000047; EDY32143.1; -; Genomic_DNA. DR ProteinModelPortal; B5CRC1; -. DR STRING; 471875.RUMLAC_02022; -. DR EnsemblBacteria; EDY32143; EDY32143; RUMLAC_02022. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000003254; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000003254}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000003254}. FT DOMAIN 201 365 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 160 197 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 413 AA; 46187 MW; 23EEB306902539CF CRC64; MQMYNMDDIR ERVILVGVDT EGGETAERSL DELAELAATA GAEVTGRLIQ TRECVHPATY IGRGKLIELK ELLWETEATG IICDDELSST QLGNLEEELD CKVLDRTLLI LDIFAARAVS GEGKIQVELA QLRYRASRLS GLGRSLSRLG GGIGTRGPGE KKLEMDRRLI RERISRLKKE LADVERHREL LRSQRNQSGM KVAALVGYTS AGKSSIENAL TNAGILEDAM LFSTLDTTTR ALQLDGTQEI LLTDTVGFIR KLPHHLIEAF KSTLEEAKYA DIIIHVVDVS NPRMDEQMYV VYDTLRQMGA EGKPVITLFN KQDRLEKEES HKDFQADYSI ATSAKTGQGL DKLKAALLEI IRRDQIYVER LYPFADAGKI QMIRSKGQLL SEEYLPEGIQ IKAYVPQDVY GKL // ID B5EIB7_GEOBB Unreviewed; 557 AA. AC B5EIB7; DT 14-OCT-2008, integrated into UniProtKB/TrEMBL. DT 14-OCT-2008, sequence version 1. DT 07-JUN-2017, entry version 60. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Gbem_2815 {ECO:0000313|EMBL:ACH39819.1}; OS Geobacter bemidjiensis (strain Bem / ATCC BAA-1014 / DSM 16622). OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfuromonadales; OC Geobacteraceae; Geobacter. OX NCBI_TaxID=404380 {ECO:0000313|EMBL:ACH39819.1, ECO:0000313|Proteomes:UP000008825}; RN [1] {ECO:0000313|EMBL:ACH39819.1, ECO:0000313|Proteomes:UP000008825} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Bem / ATCC BAA-1014 / DSM 16622 RC {ECO:0000313|Proteomes:UP000008825}; RG US DOE Joint Genome Institute; RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., RA Tice H., Bruce D., Goodwin L., Pitluck S., Kiss H., Brettin T., RA Detter J.C., Han C., Kuske C.R., Schmutz J., Larimer F., Land M., RA Hauser L., Kyrpides N., Lykidis A., Lovley D., Richardson P.; RT "Complete sequence of Geobacter bemidjiensis BEM."; RL Submitted (JUL-2008) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001124; ACH39819.1; -; Genomic_DNA. DR RefSeq; WP_012531246.1; NC_011146.1. DR ProteinModelPortal; B5EIB7; -. DR STRING; 404380.Gbem_2815; -. DR EnsemblBacteria; ACH39819; ACH39819; Gbem_2815. DR KEGG; gbm:Gbem_2815; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; EREVIIT; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000008825; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000008825}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000008825}. FT DOMAIN 369 542 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 328 355 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 557 AA; 63272 MW; 7D00B0A419B76D15 CRC64; MKSSQVKRLE RLYRRRVKPG EVISLELARE MADISLEIRR QLGILVSRIG EIAYVVVGDE RALMIPALED YPLGRRLLRG IRLVHTHLKG EPLSDDDLTD LSLLRLDMVA ALQLTQNPDR FSIQTAELVP PEGHNLPYQV EPSVPFAKFD LDFRSFVETL EQTLERGLKE GTLVATGQER GILISVTQRP MEEAVDSMEE LKELARTAGV GVLDTVIQRP KEFNPRYLLG EGKIREVLIK ALQFGATMLV FDQELSPAQV RSISELTELK VIDRSQLILD IFARRATSQD GKVQVELAQL KYLLPRLIGR GVQMSRLMGG IGGRGPGETK LEVDRRRIRD RIAHLERELK ELSNGRYQRR QKRVKAGIPI ISIVGYTNAG KSTLLNTLTR SEVFTEDLLF ATLDTSSRRL RFPMDREVII TDTVGFIRSL PKSLLGAFKA TLEELKDADL LIHLVDCSNP RFEEQIIQVD AILGELELSQ KPKLLVFNKA DLLPELKKGD PLAFMKVRQL TRRYGAVTIS AADRKTLEPL LKELQHRFWH DVEDYRAPGQ NHDEFEE // ID B5G784_STRSH Unreviewed; 496 AA. AC B5G784; DT 14-OCT-2008, integrated into UniProtKB/TrEMBL. DT 14-OCT-2008, sequence version 1. DT 07-JUN-2017, entry version 52. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=SSBG_00356 {ECO:0000313|EMBL:EDY42180.2}; OS Streptomyces sp. (strain SPB074). OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae; OC Streptomyces. OX NCBI_TaxID=465543 {ECO:0000313|EMBL:EDY42180.2, ECO:0000313|Proteomes:UP000002779}; RN [1] {ECO:0000313|Proteomes:UP000002779} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SPB074 {ECO:0000313|Proteomes:UP000002779}; RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R., RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., RA Venter J.C.; RL Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:EDY42180.2, ECO:0000313|Proteomes:UP000002779} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SPB074 {ECO:0000313|Proteomes:UP000002779}; RG The Broad Institute Genome Sequencing Platform; RG Broad Institute Microbial Sequencing Center; RA Fischbach M., Godfrey P., Ward D., Young S., Zeng Q., Koehrsen M., RA Alvarado L., Berlin A.M., Bochicchio J., Borenstein D., Chapman S.B., RA Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A., RA Gujja S., Heilman E.R., Heiman D.I., Hepburn T.A., Howarth C., Jen D., RA Larson L., Lewis B., Mehta T., Park D., Pearson M., Richards J., RA Roberts A., Saif S., Shea T.D., Shenoy N., Sisk P., Stolte C., RA Sykes S.N., Thomson T., Walk T., White J., Yandava C., Straight P., RA Clardy J., Hung D., Kolter R., Mekalanos J., Walker S., Walsh C.T., RA Wieland-Brown L.C., Haas B., Nusbaum C., Birren B.; RT "The genome sequence of Streptomyces sp. strain SPB74."; RL Submitted (OCT-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GG770539; EDY42180.2; -; Genomic_DNA. DR ProteinModelPortal; B5G784; -. DR EnsemblBacteria; EDY42180; EDY42180; SSBG_00356. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000002779; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 2. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000002779}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000002779}. FT DOMAIN 274 439 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 496 AA; 54147 MW; D75D056237BB1737 CRC64; MNETHPRGQQ PSPSQGLRAG ALMEEDAAWS QQADGARDGE QYDREERAAL RRVAGLSTEL EDVTEVEYRQ LRLERVILVG VWTSGTVHDA ENSLAELAAL AETAGALVLD GVIQRRDKPD PATYIGSGKA IELRDLVLES GADTVVCDGE LSPGQLIHLE DVVKVKVVDR TALILDIFAQ HAKSREGKAQ VALAQMQYML PRLRGWGQSL SRQMGGGGSG SSGGGMATRG PGETKIETDR RRIREKMAKM RREIAEMKTG RDLKRQERRR NKVPSVAIAG YTNAGKSSLL NRLTGAGVLV ENALFATLDP TVRRAETPSG RLYTLADTVG FVRHLPHHLV EAFRSTMEEV GDSDLILHVV DGSHPAPEEQ LAAVREVIRE VGATDVPEIV VINKADAADP VVLQRLLRVE KHSIAVSARS GQGIEELLAL IDEELPRPAV EVDVLVPYTE GRYIARTHVE GEVLSEEHTP EGTRLKALVH EELAAELHRF SPVGSR // ID B5HF71_STRPR Unreviewed; 496 AA. AC B5HF71; DT 14-OCT-2008, integrated into UniProtKB/TrEMBL. DT 14-OCT-2008, sequence version 1. DT 07-JUN-2017, entry version 52. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=SSDG_03911 {ECO:0000313|EMBL:EDY65482.1}; OS Streptomyces pristinaespiralis ATCC 25486. OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae; OC Streptomyces. OX NCBI_TaxID=457429 {ECO:0000313|EMBL:EDY65482.1, ECO:0000313|Proteomes:UP000002805}; RN [1] {ECO:0000313|Proteomes:UP000002805} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 25486 {ECO:0000313|Proteomes:UP000002805}; RG The Broad Institute Genome Sequencing Platform; RA Fischbach M., Ward D., Young S., Jaffe D., Gnerre S., Berlin A., RA Heiman D., Hepburn T., Sykes S., Alvarado L., Kodira C.D., RA Straight P., Clardy J., Hung D., Kolter R., Mekalanos J., Walker S., RA Walsh C.T., Lander E., Galagan J., Nusbaum C., Birren B.; RL Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:EDY65482.1, ECO:0000313|Proteomes:UP000002805} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 25486 {ECO:0000313|EMBL:EDY65482.1, RC ECO:0000313|Proteomes:UP000002805}; RG The Broad Institute Genome Sequencing Platform; RG Broad Institute Microbial Sequencing Center; RA Fischbach M., Godfrey P., Ward D., Young S., Zeng Q., Koehrsen M., RA Alvarado L., Berlin A.M., Bochicchio J., Borenstein D., Chapman S.B., RA Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A., RA Gujja S., Heilman E.R., Heiman D.I., Hepburn T.A., Howarth C., Jen D., RA Larson L., Lewis B., Mehta T., Park D., Pearson M., Richards J., RA Roberts A., Saif S., Shea T.D., Shenoy N., Sisk P., Stolte C., RA Sykes S.N., Thomson T., Walk T., White J., Yandava C., Straight P., RA Clardy J., Hung D., Kolter R., Mekalanos J., Walker S., Walsh C.T., RA Wieland-Brown L.C., Haas B., Nusbaum C., Birren B.; RT "The genome sequence of Streptomyces pristinaespiralis strain ATCC RT 25486."; RL Submitted (OCT-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CM000950; EDY65482.1; -; Genomic_DNA. DR RefSeq; WP_005311086.1; NZ_CM000950.1. DR ProteinModelPortal; B5HF71; -. DR STRING; 457429.SSDG_03911; -. DR EnsemblBacteria; EDY65482; EDY65482; SSDG_03911. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000002805; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 2. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000002805}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000002805}. FT DOMAIN 275 440 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 496 AA; 54107 MW; 1FDE7C7507654E37 CRC64; MTSSSSTSQE QQSLAETRTE SLRADALMEE DVAWSYEIDT ERDGDQLDRS ERAALRRVAG LSTELEDVTE VEYRQLRLER VVLVGVWTTG TMQDAENSLA ELAALAETAG ALVLDGVIQR RDKPDPATYI GSGKAQELRD IVLESGADTV VCDGELSPGQ LIQLEDVVKV KVVDRTALIL DIFAQHAKSR EGKAQVALAQ MQYMLPRLRG WGQSLSRQMG GGGGGGMATR GPGETKIETD RRRIREKMAK MRREIAEMKT GREIKRQERR RNRVPSVAIA GYTNAGKSSL LNRLTGAGVL VENALFATLD PTVRRAETPS GRGYTLADTV GFVRHLPHHL VEAFRSTMEE VGDSDLILHV VDGSHPAPEE QLAAVREVIR DVGAVDVPEI VVINKADAAD PLVLQRLLRI ERHAIAVSAR TGAGMAELVQ LIDDELPRPQ IEIEALVPYT EGGLVSRVHA DGEVLSEEHT TEGTLLKARV HEELAAALSP FVPAAH // ID B5I9D0_9ACTN Unreviewed; 498 AA. AC B5I9D0; DT 14-OCT-2008, integrated into UniProtKB/TrEMBL. DT 10-AUG-2010, sequence version 2. DT 07-JUN-2017, entry version 53. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=SSEG_08265 {ECO:0000313|EMBL:EDY61685.2}; OS Streptomyces sviceus ATCC 29083. OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae; OC Streptomyces. OX NCBI_TaxID=463191 {ECO:0000313|EMBL:EDY61685.2, ECO:0000313|Proteomes:UP000002785}; RN [1] {ECO:0000313|Proteomes:UP000002785} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29083 {ECO:0000313|Proteomes:UP000002785}; RG The Broad Institute Genome Sequencing Platform; RA Fischbach M., Ward D., Young S., Jaffe D., Gnerre S., Berlin A., RA Heiman D., Hepburn T., Sykes S., Alvarado L., Kodira C.D., RA Straight P., Clardy J., Hung D., Kolter R., Mekalanos J., Walker S., RA Walsh C.T., Lander E., Galagan J., Nusbaum C., Birren B.; RL Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:EDY61685.2, ECO:0000313|Proteomes:UP000002785} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29083 {ECO:0000313|EMBL:EDY61685.2, RC ECO:0000313|Proteomes:UP000002785}; RG The Broad Institute Genome Sequencing Platform; RG Broad Institute Microbial Sequencing Center; RA Fischbach M., Godfrey P., Ward D., Young S., Zeng Q., Koehrsen M., RA Alvarado L., Berlin A.M., Bochicchio J., Borenstein D., Chapman S.B., RA Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A., RA Gujja S., Heilman E.R., Heiman D.I., Hepburn T.A., Howarth C., Jen D., RA Larson L., Lewis B., Mehta T., Park D., Pearson M., Richards J., RA Roberts A., Saif S., Shea T.D., Shenoy N., Sisk P., Stolte C., RA Sykes S.N., Thomson T., Walk T., White J., Yandava C., Straight P., RA Clardy J., Hung D., Kolter R., Mekalanos J., Walker S., Walsh C.T., RA Wieland-Brown L.C., Haas B., Nusbaum C., Birren B.; RT "The genome sequence of Streptomyces sviceus strain ATCC 29083."; RL Submitted (OCT-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CM000951; EDY61685.2; -; Genomic_DNA. DR RefSeq; WP_007385155.1; NZ_CM000951.1. DR ProteinModelPortal; B5I9D0; -. DR STRING; 463191.SSEG_08265; -. DR EnsemblBacteria; EDY61685; EDY61685; SSEG_08265. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000002785; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 2. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000002785}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000002785}. FT DOMAIN 275 440 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 498 AA; 54254 MW; 1679C720AAE5299B CRC64; MTSSSSPSQD TQRLAHTYAE GLRADALMEE DVAWSHEIDG ERDGDQFDRS ERAALRRVAG LSTELEDVTE VEYRQLRLER VVLVGVWTTG TVQDADNSLA ELAALAETAG ALVLDGVIQR RDKPDAATFI GSGKALELRD IVVESGADTV ICDGELSPGQ LIALEDVVKV KVIDRTALIL DIFAQHAKSR EGKAQVALAQ MQYMLPRLRG WGQSLSRQMG GGKGGGLATR GPGETKIETD RRRIREKMAK MRREIADMKT GREIKRQERK RHKVPSVAIA GYTNAGKSSL LNRLTGAGVL VENALFATLD PTVRRAETPS GRLYTLADTV GFVRHLPHHL VEAFRSTMEE VGESDLILHV VDGSHPNPEE QLAAVREVVR DVGATGVPEI VVINKADAAD PLTLQRLMRI EKRSIAVSAR TGQGIPELLA LIDNELPRPS VEIEALVPYT HGKLVARAHD EGEVISEEHT AEGTLLKVRV HEELAAELAP YVPAPVVA // ID B5IL72_9CYAN Unreviewed; 790 AA. AC B5IL72; DT 14-OCT-2008, integrated into UniProtKB/TrEMBL. DT 14-OCT-2008, sequence version 1. DT 07-JUN-2017, entry version 55. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=CPCC7001_2491 {ECO:0000313|EMBL:EDY39610.1}; OS Cyanobium sp. PCC 7001. OC Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Cyanobium. OX NCBI_TaxID=180281 {ECO:0000313|EMBL:EDY39610.1, ECO:0000313|Proteomes:UP000003950}; RN [1] {ECO:0000313|EMBL:EDY39610.1, ECO:0000313|Proteomes:UP000003950} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=PCC 7001 {ECO:0000313|EMBL:EDY39610.1, RC ECO:0000313|Proteomes:UP000003950}; RA Lily E., Ferriera S., Johnson J., Kravitz S., Beeson K., Sutton G., RA Rogers Y.-H., Friedman R., Frazier M., Venter J.C.; RL Submitted (JUL-2008) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; DS990556; EDY39610.1; -; Genomic_DNA. DR ProteinModelPortal; B5IL72; -. DR STRING; 180281.CPCC7001_2491; -. DR EnsemblBacteria; EDY39610; EDY39610; CPCC7001_2491. DR eggNOG; ENOG4105D3R; Bacteria. DR eggNOG; COG0450; LUCA. DR eggNOG; COG2262; LUCA. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000003950; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0051920; F:peroxiredoxin activity; IEA:InterPro. DR GO; GO:0045454; P:cell redox homeostasis; IEA:InterPro. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR000866; AhpC/TSA. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR019479; Peroxiredoxin_C. DR InterPro; IPR012336; Thioredoxin-like_fold. DR InterPro; IPR013766; Thioredoxin_domain. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF10417; 1-cysPrx_C; 1. DR Pfam; PF00578; AhpC-TSA; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF52833; SSF52833; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. DR PROSITE; PS51352; THIOREDOXIN_2; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000003950}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000003950}. FT DOMAIN 380 556 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT DOMAIN 582 738 Thioredoxin. FT {ECO:0000259|PROSITE:PS51352}. FT COILED 341 375 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 790 AA; 85992 MW; 88923F44255E8549 CRC64; MRQGSVAGRT SGLRPAQRRR LERLCHRRHP EDGIAEPLGL QRLAAESREL ELPITLVVDG RGLCRLLWVG PLEQSGRLLE KLPGAPRRQG RGLRLLTCCG RSKQLAPSTQ EGVVGLDLQP SLWLRFGDQP AAGGHWAAAI YRPGGSATTP WELALEGDLA SLGPLDPGLG GVAGPATARE EVPRPMAGQA GERVLLLALT PGDRSAAQRL IAELEGLVRS AGGVPVGVVE QRRSQLAPQT VWGEGKLAEA ALEARRLGAT LVVTDRELTP VQARNLERLL DLPISDRSEL ILDIFAQRAS SAAGRLQVEL AQLRYRLPRL SGRGRSLSRQ GGGIGTRGPG ETQLEKDRRA IARRIDRLQR DVRQLEAHRE RLRRGRRGQR RLALVGYTNA GKSSLLNALT GAQGQAAVLA ENKLFATLDP TTRRLQLRWP GSGSGIRPMP LLLTDTVGFI RDLPPPLVEA FRSTLEETLD ADGLLLVVDL SDPAWPEQRQ TVHAILDALG ATMPRRLVAN QIDRCPAGEI ARARALEPDA LFVSATGALG LQHLREALLS WPPPLAGSPV AASAITGPGA PSVPATPIPM ALQLGDTVPD FTQDSQLGPI HFYDYAGDSW VVLFSHPADY TPVCTTELGE VSRLRPEWEK RNVKTIALSV DSAESHKGWI CDINETQNTA VDYPILADED KKVSDLYGMI HPNALNNLTV RSVFIIDPNK KLRLQITYPA STGRNFDEIL RVIDSLQLTD YHQVATPVNW KDGDDCVVVP SIPTDEARTK FPKGVTEVKP YLRMTPQPNK // ID B5JFZ7_9BACT Unreviewed; 435 AA. AC B5JFZ7; DT 14-OCT-2008, integrated into UniProtKB/TrEMBL. DT 14-OCT-2008, sequence version 1. DT 07-JUN-2017, entry version 51. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=VDG1235_1065 {ECO:0000313|EMBL:EDY81447.1}; OS Verrucomicrobiae bacterium DG1235. OC Bacteria; Verrucomicrobia; Verrucomicrobiae; Verrucomicrobiales. OX NCBI_TaxID=382464 {ECO:0000313|EMBL:EDY81447.1, ECO:0000313|Proteomes:UP000003839}; RN [1] {ECO:0000313|EMBL:EDY81447.1, ECO:0000313|Proteomes:UP000003839} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DG1235 {ECO:0000313|EMBL:EDY81447.1, RC ECO:0000313|Proteomes:UP000003839}; RA Hart M., Ferriera S., Johnson J., Kravitz S., Beeson K., Sutton G., RA Rogers Y.-H., Friedman R., Frazier M., Venter J.C.; RL Submitted (JUL-2008) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; DS990592; EDY81447.1; -; Genomic_DNA. DR RefSeq; WP_008098583.1; NZ_DS990592.1. DR ProteinModelPortal; B5JFZ7; -. DR STRING; 382464.VDG1235_1065; -. DR EnsemblBacteria; EDY81447; EDY81447; VDG1235_1065. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000003839; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000003839}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000003839}. FT DOMAIN 205 371 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 19 42 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 435 AA; 49099 MW; 627E77EF766A540A CRC64; MFDLEDNRKK VQRALLVGIQ DSKMSSEDAE RLLDELQELT ANLDIPTVDR VVVKLRKANP AFLLGTGKVQ ELIAHAKEIE ADVIIFDDEL TPAQQRNWEA EAKIAVIDRQ EIIIDIFSER AHTKEASLQV ALARMEYSLP RLRRAWTHLS RQRGGGTGAR GQGETQLEAD SRMIRDRIAI TKKELKEVIQ HRHVQRAKRL RKPVPTVAIV GYTNAGKSSL LNTMTDSDVL AADKLFATLD PTTRRLELDN SQHVLVTDTV GFVRRLPHRL VEAFKATLEE AVVADLLIHV VDVTNPDAEK HFQTTMEVLK EIEADKNPML VVFNKIDALE DPSDRERFMF THKDALYISA NTGEGIAELK ETIAHHLNAK FKSKELLIPH ERYDVISKLH SSGGIRVQET QDDGVYIEGI FPPALDGLIE PFIQKRQTVP DDTKS // ID B5JRL7_9GAMM Unreviewed; 448 AA. AC B5JRL7; DT 14-OCT-2008, integrated into UniProtKB/TrEMBL. DT 14-OCT-2008, sequence version 1. DT 07-JUN-2017, entry version 43. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:EDY87373.1}; GN ORFNames=GP5015_854 {ECO:0000313|EMBL:EDY87373.1}; OS gamma proteobacterium HTCC5015. OC Bacteria; Proteobacteria; Gammaproteobacteria. OX NCBI_TaxID=391615 {ECO:0000313|EMBL:EDY87373.1, ECO:0000313|Proteomes:UP000004692}; RN [1] {ECO:0000313|Proteomes:UP000004692} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=HTCC5015 {ECO:0000313|Proteomes:UP000004692}; RX PubMed=20472792; DOI=10.1128/JB.00510-10; RA Thrash J.C., Stingl U., Cho J.C., Ferriera S., Johnson J., RA Vergin K.L., Giovannoni S.J.; RT "Genome sequence of the novel marine member of the Gammaproteobacteria RT strain HTCC5015."; RL J. Bacteriol. 192:3838-3839(2010). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; DS990598; EDY87373.1; -; Genomic_DNA. DR RefSeq; WP_008283276.1; NZ_DS990598.1. DR ProteinModelPortal; B5JRL7; -. DR STRING; 391615.GP5015_854; -. DR EnsemblBacteria; EDY87373; EDY87373; GP5015_854. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000004692; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000004692}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000004692}. FT DOMAIN 210 376 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 448 AA; 50328 MW; F2139F6DD757A10E CRC64; MFERPSSGER ALLVHVEITQ NLVAAGGRKR LSVSREAEEQ EFHELATSAG SEPILAVRTS RYRPDPKLFI GSGKAEEVAD LVRHHEIELV LVDHTISPSQ ERNLERLFKC RVLDRTGLIL DIFAQRARSF EGKLQVELAQ LKHIATRLVR GWTHLERQKG GIGLRGPGET QLETDRRLIG QRIKMLEKKL KKVSRQREQS RSSRQKAEVP TVSLVGYTNA GKSTLFNHIT NAEVFAQDQL FATLDPTLRR LVLPDKREMV LADTVGFIRD LPHDLVAAFR STLQETEEAS LLLHVIDVAD DERELRMQEV EDVLALIGAD SVPQIRVYNK IDQTERSPEL RYGENGEVSE VYLSAHTGEG LEELMTALMD ALATSQYVAE LWLEPSEGKL RAALYAQGVV DDEQVDERGR CLLQVRLTDE MVGRLGIDES RVNRLEGTDY LATAGAGQ // ID B5WSS5_9BURK Unreviewed; 395 AA. AC B5WSS5; DT 25-NOV-2008, integrated into UniProtKB/TrEMBL. DT 25-NOV-2008, sequence version 1. DT 07-JUN-2017, entry version 51. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=BH160DRAFT_6128 {ECO:0000313|EMBL:EDZ98558.1}; OS Burkholderia sp. H160. OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Burkholderia. OX NCBI_TaxID=516466 {ECO:0000313|EMBL:EDZ98558.1, ECO:0000313|Proteomes:UP000004534}; RN [1] {ECO:0000313|EMBL:EDZ98558.1, ECO:0000313|Proteomes:UP000004534} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=H160 {ECO:0000313|EMBL:EDZ98558.1, RC ECO:0000313|Proteomes:UP000004534}; RX PubMed=23209196; DOI=10.1128/JB.01756-12; RA Ormeno-Orrillo E., Rogel M.A., Chueire L.M., Tiedje J.M., RA Martinez-Romero E., Hungria M.; RT "Genome Sequences of Burkholderia sp. Strains CCGE1002 and H160, RT Isolated from Legume Nodules in Mexico and Brazil."; RL J. Bacteriol. 194:6927-6927(2012). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EDZ98558.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABYL01000142; EDZ98558.1; -; Genomic_DNA. DR ProteinModelPortal; B5WSS5; -. DR EnsemblBacteria; EDZ98558; EDZ98558; BH160DRAFT_6128. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000004534; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000004534}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000004534}. FT DOMAIN 196 367 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 162 189 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 395 AA; 43513 MW; B6C44CF6B7070114 CRC64; MIPSNLINAA LVGIDFGKID FEASLEELSL LAQSAGANPV VTLTGRRSSP DAKMFVGSGK AEELRLACEA NDIELVIFNH ALAPAQQRNL ERALNRRVVD RTSLILDIFA QRARSHEGKL QVELAQLQYL STRLIRAWTH LERQKGGIGL RGPGETQLET DRRLIGERIK ALKIRLDKLR RQHGTQRRAR NRNQTMSVSL VGYTNAGKST LFNALTKAQA YAADQLFATL DTTSRRVYLG DEAGQVVVSD TVGFIRELPH QLVAAFRATL EETIHADLLL HVVDASSAVR LDQIDQVNEV LHAIGADTIR QVLVFNKIDA VPELAARGHA VERDEYGNIS RVFLSARTGQ GLDALRAAIA EIATAEPLSE MSLDASEHDR TAQLRDDHKV PELGH // ID B5Y9F9_COPPD Unreviewed; 350 AA. AC B5Y9F9; DT 25-NOV-2008, integrated into UniProtKB/TrEMBL. DT 25-NOV-2008, sequence version 1. DT 07-JUN-2017, entry version 58. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:ACI18198.1}; GN OrderedLocusNames=COPRO5265_1095 {ECO:0000313|EMBL:ACI18198.1}; OS Coprothermobacter proteolyticus (strain ATCC 35245 / DSM 5265 / BT). OC Bacteria; Firmicutes; Clostridia; Thermoanaerobacterales; OC Thermodesulfobiaceae; Coprothermobacter. OX NCBI_TaxID=309798 {ECO:0000313|EMBL:ACI18198.1, ECO:0000313|Proteomes:UP000001732}; RN [1] {ECO:0000313|Proteomes:UP000001732} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 35245 / DSM 5265 / BT {ECO:0000313|Proteomes:UP000001732}; RA Dodson R.J., Durkin A.S., Wu M., Eisen J., Sutton G.; RT "The complete genome sequence of Coprothermobacter proteolyticus RT strain ATCC 5245 / DSM 5265 / BT."; RL Submitted (AUG-2008) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001145; ACI18198.1; -; Genomic_DNA. DR ProteinModelPortal; B5Y9F9; -. DR STRING; 309798.COPRO5265_1095; -. DR EnsemblBacteria; ACI18198; ACI18198; COPRO5265_1095. DR KEGG; cpo:COPRO5265_1095; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000001732; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000001732}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000001732}. FT DOMAIN 185 345 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 152 179 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 350 AA; 39287 MW; BF57577402244DEB CRC64; MLHNHIDSAL LDYDIQEIKE LAKVIGFEVE SVVIQKREPD VKYFMGEGKV KELSAMVKDL GVDAVIFNEE LSPRQVRALE AMLEPAQVWD RTQVILEIFR RRAVTKESKL QVELAGLNYL YPRIYGLGGV MSRLGGGIGT RGPGETKLEI LKRVIRGRIR KLEKELKEAE ARRVTTSKQR VRNTMQVSIV GYTNAGKSTL LNAFSKTSKP SYADDKVFAT LDTRHRRFLN LEGKPVILVD TVGFVNFMPE KVLDAFKSTL EVIRYSDLIL HVIDLSSPIM DEQERTVMRI LEELGAGDRP VIKVYNKLDL YKGPVLQDGI SVSALKGTNL DELKNAVVSA LLTVDNDAVT // ID B5YFQ8_THEYD Unreviewed; 509 AA. AC B5YFQ8; DT 25-NOV-2008, integrated into UniProtKB/TrEMBL. DT 25-NOV-2008, sequence version 1. DT 07-JUN-2017, entry version 65. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=THEYE_A1292 {ECO:0000313|EMBL:ACI20892.1}; OS Thermodesulfovibrio yellowstonii (strain ATCC 51303 / DSM 11347 / OS YP87). OC Bacteria; Nitrospirae; Nitrospirales; Nitrospiraceae; OC Thermodesulfovibrio. OX NCBI_TaxID=289376 {ECO:0000313|EMBL:ACI20892.1, ECO:0000313|Proteomes:UP000000718}; RN [1] {ECO:0000313|Proteomes:UP000000718} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51303 / DSM 11347 / YP87 RC {ECO:0000313|Proteomes:UP000000718}; RA Dodson R.J., Durkin A.S., Wu M., Eisen J., Sutton G.; RT "The complete genome sequence of Thermodesulfovibrio yellowstonii RT strain ATCC 51303 / DSM 11347 / YP87."; RL Submitted (AUG-2008) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001147; ACI20892.1; -; Genomic_DNA. DR RefSeq; WP_012545622.1; NC_011296.1. DR RefSeq; YP_002249106.1; NC_011296.1. DR ProteinModelPortal; B5YFQ8; -. DR STRING; 289376.THEYE_A1292; -. DR EnsemblBacteria; ACI20892; ACI20892; THEYE_A1292. DR GeneID; 6941488; -. DR KEGG; tye:THEYE_A1292; -. DR PATRIC; fig|289376.4.peg.1262; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR InParanoid; B5YFQ8; -. DR KO; K03665; -. DR OMA; EREVIIT; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000000718; Chromosome. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0043022; F:ribosome binding; IBA:GO_Central. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000000718}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000000718}. FT DOMAIN 338 502 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 297 324 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 509 AA; 57914 MW; 8FC2E6DECD7CED18 CRC64; MAKSLCSISY ELNRQIGVLI DRSGNITHVI IGTAHSIFIP PLEDFPIGKK QLRGLRYIHT HLNKEMPDRE DITDLRLLRF DLVAVLTHEK GIPETVHIVH LLPYGKQNQF EIISSNLYSL KHNFKEFIDN LEAEMDRARV IDMQDPREKA ILISVSTAPK YILEEHMEEL KDLAESADLI VIDKIIQRVK QINPKYLLGE GKLRELIIKA MDMGATLLVF DQNLTPSQIR AITDMTELKV IDRSQLILDI FAKRAHTMDG KVQVELAQLR YMLPRLTGKG TAMSRLAGGI GGRGPGETKL ELDRRRINKR IHHLENELEK LTLARIERKK RRKELSIPIV SIIGYTNAGK STLLNALTKS SVFVEDKMFA TLDTSSRRLK FPEEKELIIT DTVGFIRDLP DDLVAAFKAT LEELQDASLL IHLVDISNPQ FENHIESVNR ILSQLGLDIK PVILVFNKID KLSSLETKQI CNRYNAIGIS AIDKKTLIPL IDEIKNRLWE EKVTCNAPL // ID B6AX22_9RHOB Unreviewed; 423 AA. AC B6AX22; DT 25-NOV-2008, integrated into UniProtKB/TrEMBL. DT 25-NOV-2008, sequence version 1. DT 07-JUN-2017, entry version 46. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:EDZ41013.1}; GN ORFNames=RB2083_527 {ECO:0000313|EMBL:EDZ41013.1}; OS Rhodobacteraceae bacterium HTCC2083. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae. OX NCBI_TaxID=314270 {ECO:0000313|EMBL:EDZ41013.1, ECO:0000313|Proteomes:UP000005746}; RN [1] {ECO:0000313|Proteomes:UP000005746} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=HTCC2083 {ECO:0000313|Proteomes:UP000005746}; RX PubMed=21036993; DOI=10.1128/JB.01268-10; RA Kang I., Vergin K.L., Oh H.M., Choi A., Giovannoni S.J., Cho J.C.; RT "Genome sequence of strain HTCC2083, a novel member of the marine RT clade Roseobacter."; RL J. Bacteriol. 193:319-320(2011). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; DS995276; EDZ41013.1; -; Genomic_DNA. DR RefSeq; WP_009827887.1; NZ_DS995276.1. DR ProteinModelPortal; B6AX22; -. DR STRING; 314270.RB2083_527; -. DR EnsemblBacteria; EDZ41013; EDZ41013; RB2083_527. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000005746; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000005746}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000005746}. FT DOMAIN 203 372 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 423 AA; 46925 MW; 4DD86E4278B3E777 CRC64; MGHDPAITRT WVLHPDIKSN NDRRLPEPAL AEAVALAEAL PGLEVFGDII VRLPKAHSGM LFGKGKIEEL HQLFDAEEVD LVLIDGPVTP VQQRNLEKAW GVKLLDRTGL ILEIFSDRAR TSEGVLQVEM AALSYQRTRL VRAWTHLERQ RGGLGFVGGP GETQIESDRR AIDDQLVRLR RKLSKVVKTR ALHREARAKV PFPIVALVGY TNAGKSTLFN RLTGAEVFAK DMLFATLDPT MRAVELPDGP QVILSDTVGF ISDLPTELVA SFRATLEEVL AADLIVHVRD ISHEGTEEQA TDVRAILTSL GVGEGAKQIE VWNKIDLLEP DDKDAVLARA ARHDDVIAVS SISGYGMQDF VVAVEEALEG EIITETLVLP YSEGRKRAWL FERSLVEAER QGENGFELDL RWKAKDRAQF QTI // ID B6BTN6_9PROT Unreviewed; 378 AA. AC B6BTN6; DT 25-NOV-2008, integrated into UniProtKB/TrEMBL. DT 25-NOV-2008, sequence version 1. DT 30-AUG-2017, entry version 56. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:EDZ64129.1}; GN ORFNames=KB13_261 {ECO:0000313|EMBL:EDZ64129.1}; OS beta proteobacterium KB13. OC Bacteria; Proteobacteria; Betaproteobacteria; Nitrosomonadales; OC OM43 clade. OX NCBI_TaxID=314607 {ECO:0000313|EMBL:EDZ64129.1, ECO:0000313|Proteomes:UP000004188}; RN [1] {ECO:0000313|Proteomes:UP000004188} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=KB13 {ECO:0000313|Proteomes:UP000004188}; RX PubMed=22675594; DOI=10.4056/sigs.2305090; RA Huggett M.J., Hayakawa D.H., Rappe M.S.; RT "Genome sequence of strain HIMB624, a cultured representative from the RT OM43 clade of marine Betaproteobacteria."; RL Stand. Genomic Sci. 6:11-20(2012). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; DS995299; EDZ64129.1; -; Genomic_DNA. DR ProteinModelPortal; B6BTN6; -. DR STRING; 314607.KB13_261; -. DR EnsemblBacteria; EDZ64129; EDZ64129; KB13_261. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000004188; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000004188}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000004188}. FT DOMAIN 201 367 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 160 194 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 378 AA; 43175 MW; B5B25829EB0FEAB5 CRC64; MTSNNTIIPK DKCLIINTHD GYGRKEYDHH EIKELVKTAG FDIVESLDIK IVTPNPSFYI GKGKVDEIKQ LKNVFSFEFL IINEDITPAQ EKKLSDALKV TIIDRTNLIL NIFSQRAKSH EGKLQVELAQ LEYLSTRLVR GWTHLERQKG GIGVRGGPGE KQIELDRRML RVRVKQLKER LKKLTKQRDM QRQRRRKSGV FTVAIVGYTN AGKSTLFNEL TKQKIYAADQ LFATLDTTSR KLFIPPSTSL VISDTVGFIK NLPTNLIESF KSTLEESTSA DLLLHVVDST NEEKKEHIDQ VNRILKEIHA DQVDQILILN QIDKNNSLPQ KDIDEYGRIK RIELSAKTGQ GIEFLKEALV GRASAFNNQE IINYDENF // ID B6FW66_9FIRM Unreviewed; 93 AA. AC B6FW66; DT 16-DEC-2008, integrated into UniProtKB/TrEMBL. DT 16-DEC-2008, sequence version 1. DT 18-JAN-2017, entry version 27. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EEA86236.1}; DE Flags: Fragment; GN ORFNames=CLOHIR_00115 {ECO:0000313|EMBL:EEA86236.1}; OS [Clostridium] hiranonis DSM 13275. OC Bacteria; Firmicutes; Clostridia; Clostridiales; OC Peptostreptococcaceae. OX NCBI_TaxID=500633 {ECO:0000313|EMBL:EEA86236.1, ECO:0000313|Proteomes:UP000003178}; RN [1] {ECO:0000313|EMBL:EEA86236.1, ECO:0000313|Proteomes:UP000003178} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 13275 {ECO:0000313|EMBL:EEA86236.1, RC ECO:0000313|Proteomes:UP000003178}; RA Fulton L., Clifton S., Fulton B., Xu J., Minx P., Pepin K.H., RA Johnson M., Thiruvilangam P., Bhonagiri V., Nash W.E., Mardis E.R., RA Wilson R.K.; RL Submitted (SEP-2008) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:EEA86236.1, ECO:0000313|Proteomes:UP000003178} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 13275 {ECO:0000313|EMBL:EEA86236.1, RC ECO:0000313|Proteomes:UP000003178}; RA Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., RA Liep D., Gordon J.; RT "Draft genome sequence of Clostridium hiranonis (DSM 13275)."; RL Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EEA86236.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABWP01000005; EEA86236.1; -; Genomic_DNA. DR ProteinModelPortal; B6FW66; -. DR STRING; 500633.CLOHIR_00115; -. DR EnsemblBacteria; EEA86236; EEA86236; CLOHIR_00115. DR eggNOG; COG2262; LUCA. DR OrthoDB; POG091H51FC; -. DR Proteomes; UP000003178; Unassembled WGS sequence. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF13167; GTP-bdg_N; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000003178}; KW Reference proteome {ECO:0000313|Proteomes:UP000003178}. FT DOMAIN 21 92 GTP-bdg_N. {ECO:0000259|Pfam:PF13167}. FT NON_TER 93 93 {ECO:0000313|EMBL:EEA86236.1}. SQ SEQUENCE 93 AA; 10656 MW; E6C23EC7F0774315 CRC64; MKMRKRVIIV GININNKNNF EESIIELKNL CIACDMEVVG KVEQNLKKIN PTFYMGSGKI EELQDLIEKT NAEIIVFNNE LSASQIKNIE EEV // ID B6G154_9FIRM Unreviewed; 436 AA. AC B6G154; DT 16-DEC-2008, integrated into UniProtKB/TrEMBL. DT 16-DEC-2008, sequence version 1. DT 07-JUN-2017, entry version 44. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:EEA84460.1}; GN ORFNames=CLOHIR_01860 {ECO:0000313|EMBL:EEA84460.1}; OS [Clostridium] hiranonis DSM 13275. OC Bacteria; Firmicutes; Clostridia; Clostridiales; OC Peptostreptococcaceae. OX NCBI_TaxID=500633 {ECO:0000313|EMBL:EEA84460.1, ECO:0000313|Proteomes:UP000003178}; RN [1] {ECO:0000313|EMBL:EEA84460.1, ECO:0000313|Proteomes:UP000003178} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 13275 {ECO:0000313|EMBL:EEA84460.1, RC ECO:0000313|Proteomes:UP000003178}; RA Fulton L., Clifton S., Fulton B., Xu J., Minx P., Pepin K.H., RA Johnson M., Thiruvilangam P., Bhonagiri V., Nash W.E., Mardis E.R., RA Wilson R.K.; RL Submitted (SEP-2008) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:EEA84460.1, ECO:0000313|Proteomes:UP000003178} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 13275 {ECO:0000313|EMBL:EEA84460.1, RC ECO:0000313|Proteomes:UP000003178}; RA Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., RA Liep D., Gordon J.; RT "Draft genome sequence of Clostridium hiranonis (DSM 13275)."; RL Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EEA84460.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABWP01000071; EEA84460.1; -; Genomic_DNA. DR RefSeq; WP_006440722.1; NZ_DS995358.1. DR ProteinModelPortal; B6G154; -. DR STRING; 500633.CLOHIR_01860; -. DR EnsemblBacteria; EEA84460; EEA84460; CLOHIR_01860. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000003178; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000003178}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000003178}. FT DOMAIN 211 381 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 436 AA; 49344 MW; 424C57C95475A468 CRC64; MTTELDINLH EQVVERALLV GMNITTVSKR IDDIDINDSM EELKELAKAA GAEIVGSVIQ NRPAVDAAYY IGKGKVEEIK GYCEGLDATL IIFNDELSGA QTRNIEDLTG IKTIDRTTLI LDIFAQRAKS KEGKLQVELA QLKYRLPRLY GMGGAMSRTG AGIGTRGPGE QKLEIDKRHI LNRAADIRAE LKLVKKNRET QRNQRKKSNI PIVALVGYTN AGKSTLLNEL IKTHKEYESE KEVFVKDMLF ATLDVTLRKA VLPNKRDFLV VDTVGFVSKL PHDLVDAFKS TLEEVNYADL ILHVIDATND SYEIQKKTTE KVLKELGADD KKTILVYNKV DKLELDIYPK NQDDVVYISA KQGINMDKLL NMIEKAVMEN TYDVELLIPY DRGDIFSKCK DKYNIDEFEY LGEGTKFRVA LDEEDFGKYK EYIVEK // ID B6G1T1_9FIRM Unreviewed; 369 AA. AC B6G1T1; DT 16-DEC-2008, integrated into UniProtKB/TrEMBL. DT 16-DEC-2008, sequence version 1. DT 05-JUL-2017, entry version 35. DE SubName: Full=GTP-binding protein HflX {ECO:0000313|EMBL:EEA84269.1}; DE Flags: Fragment; GN Name=hflX {ECO:0000313|EMBL:EEA84269.1}; GN ORFNames=CLOHIR_02089 {ECO:0000313|EMBL:EEA84269.1}; OS [Clostridium] hiranonis DSM 13275. OC Bacteria; Firmicutes; Clostridia; Clostridiales; OC Peptostreptococcaceae. OX NCBI_TaxID=500633 {ECO:0000313|EMBL:EEA84269.1, ECO:0000313|Proteomes:UP000003178}; RN [1] {ECO:0000313|EMBL:EEA84269.1, ECO:0000313|Proteomes:UP000003178} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 13275 {ECO:0000313|EMBL:EEA84269.1, RC ECO:0000313|Proteomes:UP000003178}; RA Fulton L., Clifton S., Fulton B., Xu J., Minx P., Pepin K.H., RA Johnson M., Thiruvilangam P., Bhonagiri V., Nash W.E., Mardis E.R., RA Wilson R.K.; RL Submitted (SEP-2008) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:EEA84269.1, ECO:0000313|Proteomes:UP000003178} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 13275 {ECO:0000313|EMBL:EEA84269.1, RC ECO:0000313|Proteomes:UP000003178}; RA Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., RA Liep D., Gordon J.; RT "Draft genome sequence of Clostridium hiranonis (DSM 13275)."; RL Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EEA84269.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABWP01000081; EEA84269.1; -; Genomic_DNA. DR ProteinModelPortal; B6G1T1; -. DR STRING; 500633.CLOHIR_02089; -. DR EnsemblBacteria; EEA84269; EEA84269; CLOHIR_02089. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000003178; Unassembled WGS sequence. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000003178}; KW Reference proteome {ECO:0000313|Proteomes:UP000003178}. FT DOMAIN 150 316 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 109 143 {ECO:0000256|SAM:Coils}. FT NON_TER 1 1 {ECO:0000313|EMBL:EEA84269.1}. SQ SEQUENCE 369 AA; 41865 MW; FA79EAA924FE92EB CRC64; KVNSTFYMGS GKIDELKNLV EENNADIVIF NNELSASQVK NIEEEINCNV IDRTALILDI FANRAKTRES KLQVEVAKLQ YELPRLVGSN EDLGRQSGGV GTKNRGAGET KLELDRRRIE DKIANLNKEL EVLKNQREVQ KSKRKKSNIP NVALVGYTNA GKSSVMNALV EKFINDEDKK VFEKNMLFAT LETYVRNIKL DNNKSFLLSD TVGFVGDLPH SLVKAFRSTL EEVCDADLLL HVIDISNPNY ENHINVTNET LNQIGADNIP VIYVYNKVDL MELDTFNIEG MLVSAKKYIG IEELLESICK NIFMDYIKCK VMVPYKDGKM TSYIIDSSTV LETEYTNEGT LFSIECSKED YVKYQSYII // ID B6GBU5_9ACTN Unreviewed; 429 AA. AC B6GBU5; DT 16-DEC-2008, integrated into UniProtKB/TrEMBL. DT 16-DEC-2008, sequence version 1. DT 07-JUN-2017, entry version 50. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:EEA90209.1}; GN ORFNames=COLSTE_01559 {ECO:0000313|EMBL:EEA90209.1}; OS Collinsella stercoris DSM 13279. OC Bacteria; Actinobacteria; Coriobacteriia; Coriobacteriales; OC Coriobacteriaceae; Collinsella. OX NCBI_TaxID=445975 {ECO:0000313|EMBL:EEA90209.1, ECO:0000313|Proteomes:UP000003560}; RN [1] {ECO:0000313|EMBL:EEA90209.1, ECO:0000313|Proteomes:UP000003560} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 13279 {ECO:0000313|EMBL:EEA90209.1, RC ECO:0000313|Proteomes:UP000003560}; RA Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., RA Liep D., Gordon J.; RT "Draft genome sequence of Collinsella stercoris (DSM 13279)."; RL Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:EEA90209.1, ECO:0000313|Proteomes:UP000003560} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 13279 {ECO:0000313|EMBL:EEA90209.1, RC ECO:0000313|Proteomes:UP000003560}; RA Fulton L., Clifton S., Fulton B., Xu J., Minx P., Pepin K.H., RA Johnson M., Thiruvilangam P., Bhonagiri V., Nash W.E., Mardis E.R., RA Wilson R.K.; RL Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EEA90209.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABXJ01000083; EEA90209.1; -; Genomic_DNA. DR RefSeq; WP_006721198.1; NZ_DS995476.1. DR ProteinModelPortal; B6GBU5; -. DR STRING; 445975.COLSTE_01559; -. DR EnsemblBacteria; EEA90209; EEA90209; COLSTE_01559. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000003560; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000003560}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000003560}. FT DOMAIN 210 375 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 429 AA; 47937 MW; E7F3E2B37255C979 CRC64; MSRFQPISTE RVAERAVLMG VDTRDGLWPT ERSLDELERL ADTAGAVVVA RLTQRLDRPS PKTYIGSGKV EELRGFVQRL DADVVIFDDD LSPSQQSNLE RALGEPIKII DRTALILDIF GLHARTREGR LQVQLAQLQY LLPRLRGMWT HLAKEQTRGG IGSRFGQGES QLEVDRRMIR NRIASLRKEL AVVERRRAVQ SKSRTGSLAF RIALAGYTNA GKSSLLNRLT GSDVLAQDKL FATLDPTTRS YELPGGRAIT ITDTVGFIQK LPHGLVEAFK STLSEVRDAD LILKVVDVSD EDRDRQIESV DRVLCDVHAE SQRALTVYNK IDLLDPSEVE RLKRRHPDAL FFSARTGAGI EELRQRIARE AALTDELMSC EIPYGEGALM AAIRQQGSIL SESFESDHVC MVCRVPAHIA ALVRPFQTE // ID B6IQ49_RHOCS Unreviewed; 430 AA. AC B6IQ49; DT 16-DEC-2008, integrated into UniProtKB/TrEMBL. DT 16-DEC-2008, sequence version 1. DT 07-JUN-2017, entry version 68. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:ACI97585.1}; GN OrderedLocusNames=RC1_0136 {ECO:0000313|EMBL:ACI97585.1}; OS Rhodospirillum centenum (strain ATCC 51521 / SW). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales; OC Rhodospirillaceae; Rhodospirillum. OX NCBI_TaxID=414684 {ECO:0000313|EMBL:ACI97585.1, ECO:0000313|Proteomes:UP000001591}; RN [1] {ECO:0000313|Proteomes:UP000001591} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51521 / SW {ECO:0000313|Proteomes:UP000001591}; RA Touchman J.W., Bauer C., Blankenship R.E.; RT "Genome sequence of Rhodospirillum centenum."; RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000613; ACI97585.1; -; Genomic_DNA. DR ProteinModelPortal; B6IQ49; -. DR STRING; 414684.RC1_0136; -. DR EnsemblBacteria; ACI97585; ACI97585; RC1_0136. DR KEGG; rce:RC1_0136; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000001591; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000001591}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000001591}. FT DOMAIN 182 353 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 148 175 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 430 AA; 47090 MW; FB2B433A85E324B9 CRC64; MASRSPEAQL EEAVGLARAI ELEVVGARSI RVMRPRPAAL LGQGAVEELA AAIEAETATL VVVDHALTPV QQRNLEKAWK AKVIDRTGLI LEIFGARART REGQLQVELA ALTYQRSRLV RSWTHLERQR GGFGFLGGPG ESQLEIDRRL IGERIARLKA ELEEVRRTRG LHRRAREKVP YPVVALVGYT NAGKSTLFNR MAGADVFAKD LLFATLDPTM RAITLPSNRK IILSDTVGFI SDLPHGLVEA FRATLEEVQA ADIVLHVRDV SHPDTEAQKA DVETVLRELG IEVDSDARVV EVLNKIDLVP EGERDALLRQ ARRTGDTVAI SALTGEGLGG LFDLIDRRMV ADRDVVSVAV DLADGAALAW LYQRGEVLER QDDDARALVR VGLETADVGR FRERFGYLPV PAAPVGTAAP DAGPWEARRA // ID B6SXP6_MAIZE Unreviewed; 552 AA. AC B6SXP6; DT 16-DEC-2008, integrated into UniProtKB/TrEMBL. DT 16-DEC-2008, sequence version 1. DT 30-AUG-2017, entry version 74. DE SubName: Full=GTP-binding protein hflX {ECO:0000313|EMBL:ACG29629.1, ECO:0000313|EnsemblPlants:Zm00001d048944_P007}; GN Name=100281675 {ECO:0000313|EnsemblPlants:Zm00001d048944_P007}; GN ORFNames=ZEAMMB73_Zm00001d048944 {ECO:0000313|EMBL:AQK49226.1}; OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACMAD clade; Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; OC Zea. OX NCBI_TaxID=4577 {ECO:0000313|EMBL:ACG29629.1}; RN [1] {ECO:0000313|EMBL:ACG29629.1} RP NUCLEOTIDE SEQUENCE. RX PubMed=18937034; DOI=10.1007/s11103-008-9415-4; RA Alexandrov N.N., Brover V.V., Freidin S., Troukhan M.E., RA Tatarinova T.V., Zhang H., Swaller T.J., Lu Y.P., Bouck J., RA Flavell R.B., Feldmann K.A.; RT "Insights into corn genes derived from large-scale cDNA sequencing."; RL Plant Mol. Biol. 69:179-194(2009). RN [2] {ECO:0000313|Proteomes:UP000007305} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. B73 {ECO:0000313|Proteomes:UP000007305}; RX PubMed=19965430; DOI=10.1126/science.1178534; RA Schnable P.S., Ware D., Fulton R.S., Stein J.C., Wei F., Pasternak S., RA Liang C., Zhang J., Fulton L., Graves T.A., Minx P., Reily A.D., RA Courtney L., Kruchowski S.S., Tomlinson C., Strong C., Delehaunty K., RA Fronick C., Courtney B., Rock S.M., Belter E., Du F., Kim K., RA Abbott R.M., Cotton M., Levy A., Marchetto P., Ochoa K., Jackson S.M., RA Gillam B., Chen W., Yan L., Higginbotham J., Cardenas M., RA Waligorski J., Applebaum E., Phelps L., Falcone J., Kanchi K., RA Thane T., Scimone A., Thane N., Henke J., Wang T., Ruppert J., RA Shah N., Rotter K., Hodges J., Ingenthron E., Cordes M., Kohlberg S., RA Sgro J., Delgado B., Mead K., Chinwalla A., Leonard S., Crouse K., RA Collura K., Kudrna D., Currie J., He R., Angelova A., Rajasekar S., RA Mueller T., Lomeli R., Scara G., Ko A., Delaney K., Wissotski M., RA Lopez G., Campos D., Braidotti M., Ashley E., Golser W., Kim H., RA Lee S., Lin J., Dujmic Z., Kim W., Talag J., Zuccolo A., Fan C., RA Sebastian A., Kramer M., Spiegel L., Nascimento L., Zutavern T., RA Miller B., Ambroise C., Muller S., Spooner W., Narechania A., Ren L., RA Wei S., Kumari S., Faga B., Levy M.J., McMahan L., Van Buren P., RA Vaughn M.W., Ying K., Yeh C.-T., Emrich S.J., Jia Y., Kalyanaraman A., RA Hsia A.-P., Barbazuk W.B., Baucom R.S., Brutnell T.P., Carpita N.C., RA Chaparro C., Chia J.-M., Deragon J.-M., Estill J.C., Fu Y., RA Jeddeloh J.A., Han Y., Lee H., Li P., Lisch D.R., Liu S., Liu Z., RA Nagel D.H., McCann M.C., SanMiguel P., Myers A.M., Nettleton D., RA Nguyen J., Penning B.W., Ponnala L., Schneider K.L., Schwartz D.C., RA Sharma A., Soderlund C., Springer N.M., Sun Q., Wang H., Waterman M., RA Westerman R., Wolfgruber T.K., Yang L., Yu Y., Zhang L., Zhou S., RA Zhu Q., Bennetzen J.L., Dawe R.K., Jiang J., Jiang N., Presting G.G., RA Wessler S.R., Aluru S., Martienssen R.A., Clifton S.W., McCombie W.R., RA Wing R.A., Wilson R.K.; RT "The B73 maize genome: complexity, diversity, and dynamics."; RL Science 326:1112-1115(2009). RN [3] {ECO:0000313|EMBL:AQK49226.1} RP NUCLEOTIDE SEQUENCE. RC TISSUE=Seedling {ECO:0000313|EMBL:AQK49226.1}; RG Maize Genome Sequencing Project; RA Ware D.; RT "Update maize B73 reference genome by single molecule sequencing RT technologies."; RL Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases. RN [4] {ECO:0000313|EnsemblPlants:Zm00001d048944_P007} RP IDENTIFICATION. RC STRAIN=cv. B73 {ECO:0000313|EnsemblPlants:Zm00001d048944_P007}; RG EnsemblPlants; RL Submitted (MAY-2017) to UniProtKB. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; EU957511; ACG29629.1; -; mRNA. DR EMBL; EU975611; ACG47729.1; -; mRNA. DR EMBL; CM000780; AQK49226.1; -; Genomic_DNA. DR RefSeq; NP_001148067.1; NM_001154595.2. DR UniGene; Zm.140192; -. DR UniGene; Zm.5437; -. DR STRING; 4577.GRMZM2G027021_P01; -. DR EnsemblPlants; Zm00001d048944_T007; Zm00001d048944_P007; Zm00001d048944. DR GeneID; 100281675; -. DR Gramene; Zm00001d048944_T007; Zm00001d048944_P007; Zm00001d048944. DR KEGG; zma:100281675; -. DR eggNOG; KOG0410; Eukaryota. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; VILEIFH; -. DR OrthoDB; EOG093609UJ; -. DR Proteomes; UP000007305; Chromosome 4. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 2: Evidence at transcript level; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000007305}; KW Reference proteome {ECO:0000313|Proteomes:UP000007305}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1 21 {ECO:0000256|SAM:SignalP}. FT CHAIN 22 552 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5010825372. FT DOMAIN 328 493 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 294 321 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 552 AA; 61146 MW; 995B1A780C645BC1 CRC64; MSAAACLFAA AVSLSFPSTS APSSARRRRL RSPTTLLRCS PTRRRGPVRR TLDERLLEAA PAETEDVQTA VDVEDGGGIA EGDEVGTEEM EELEQRPPTR AFVKSRRQRQ EEEEAAAGQD RFKLINGKEI FQEKAYLVGV ECKRTGGNLF GIEESLKELE QLADTAGLLV VGSTYQKLST PNPRTYIGSG KVSEIRTAIQ ALDVETVILD DELSPGQLRN LEKSFGGSVR VCDRTALILD IFNQRAATHE ASLQVTLAQM EYQLPRLTKM WSHLERQAGG QVKGMGEKQI EVDKRILRTQ ISALRKELES VRKHRKLYRN RRQSVPIPVV SLVGYTNAGK STLLNRLTGA DVLAEDKLFA TLDPTTRRVL MKNGTEFLLT DTVGFIQKLP TMLVAAFRAT LEEISESSVI VHLVDISHPL AQQQIDAVER VLKELDVESI PKLVVWNKID NTDEPLSVKE EAQKQGIICI SAMNGDGLED LCNAVQAKLK DSMVPIEAFV PYDKGDLLND IHKVGMVEKM EYKESGTFVK AHVPLPLARL LTPLRQQVAA TV // ID B6WWI2_9DELT Unreviewed; 544 AA. AC B6WWI2; DT 20-JAN-2009, integrated into UniProtKB/TrEMBL. DT 20-JAN-2009, sequence version 1. DT 07-JUN-2017, entry version 51. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:EEB32599.1}; GN ORFNames=DESPIG_02450 {ECO:0000313|EMBL:EEB32599.1}; OS Desulfovibrio piger ATCC 29098. OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfovibrionales; OC Desulfovibrionaceae; Desulfovibrio. OX NCBI_TaxID=411464 {ECO:0000313|EMBL:EEB32599.1, ECO:0000313|Proteomes:UP000003676}; RN [1] {ECO:0000313|EMBL:EEB32599.1, ECO:0000313|Proteomes:UP000003676} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29098 {ECO:0000313|EMBL:EEB32599.1, RC ECO:0000313|Proteomes:UP000003676}; RA Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., RA Liep D., Gordon J.; RT "Draft genome sequence of Desulvovibrio piger (ATCC 29098)."; RL Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:EEB32599.1, ECO:0000313|Proteomes:UP000003676} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29098 {ECO:0000313|EMBL:EEB32599.1, RC ECO:0000313|Proteomes:UP000003676}; RA Fulton L., Clifton S., Fulton B., Xu J., Minx P., Pepin K.H., RA Johnson M., Bhonagiri V., Nash W.E., Mardis E.R., Wilson R.K.; RL Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EEB32599.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABXU01000074; EEB32599.1; -; Genomic_DNA. DR ProteinModelPortal; B6WWI2; -. DR STRING; 411464.DESPIG_02450; -. DR EnsemblBacteria; EEB32599; EEB32599; DESPIG_02450. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000003676; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000003676}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000003676}. FT DOMAIN 363 528 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 322 356 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 544 AA; 60862 MW; B81CB4BBF66DC875 CRC64; MKALNRLTTR RFPATDVYTI DQARELSLLS RALGRQLGML IDRKGRVDMV LVGEAGGILI PELPRARSGA DRLRGLRLLH THLTPDGLSQ EDLMDLLFLR LDAIIVLTVN PDGDPVQWQE AHLLPTPVAG QPYRVEQLRP WDQTSAHFTA TAEALEEELA RRSDDTREAS DAPRALLVSV AAQPRIIQER NLDELAELAR TAGLAVAGRM VQRVAQVNPK FILGKGKMAE LEVLALEGRA GTLVFDGELS PAQLHNLADI TERKVLDRTQ LILDIFAQHA VTRAGKLQVE LAQLRYTQPR LTGKNRAMDR LMGGIGGRGP GETKLETDRR RSRERMARLR KELDQLRRQR AFTRSRRARR GIPMAALVGY TNAGKSTLLN NLTRSEVLAE NKLFATLDPT TRRLRFPAER EIILADTVGF IRNLPKELMD AFRATLEELE SADLLVHVAD ASHPDLLQQI TSVETILEEL ELQHMPRILL LNKWDLLDVP ARAELADAFP HAIPISARTG DGLKRLLEVL ENMLLSTQQS QLLIPFEDDG LVLQ // ID B6YRR1_AZOPC Unreviewed; 408 AA. AC B6YRR1; DT 20-JAN-2009, integrated into UniProtKB/TrEMBL. DT 20-JAN-2009, sequence version 1. DT 07-JUN-2017, entry version 60. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=CFPG_620 {ECO:0000313|EMBL:BAG83883.1}; OS Azobacteroides pseudotrichonymphae genomovar. CFP2. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; OC Candidatus Azobacteroides. OX NCBI_TaxID=511995 {ECO:0000313|EMBL:BAG83883.1, ECO:0000313|Proteomes:UP000000723}; RN [1] {ECO:0000313|EMBL:BAG83883.1, ECO:0000313|Proteomes:UP000000723} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=19008447; DOI=10.1126/science.1165578; RA Hongoh Y., Sharma V.K., Prakash T., Noda S., Toh H., Taylor T.D., RA Kudo T., Sakaki Y., Toyoda A., Hattori M., Ohkuma M.; RT "Genome of an endosymbiont coupling N2 fixation to cellulolysis within RT RT protist cells in termite gut."; RL Science 322:1108-1109(2008). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AP010656; BAG83883.1; -; Genomic_DNA. DR RefSeq; WP_012573643.1; NC_011565.1. DR ProteinModelPortal; B6YRR1; -. DR STRING; 511995.CFPG_620; -. DR EnsemblBacteria; BAG83883; BAG83883; CFPG_620. DR KEGG; aps:CFPG_620; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000000723; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000000723}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000000723}. FT DOMAIN 195 379 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 408 AA; 47288 MW; 149091100AAFE0DC CRC64; MINNAILIGL ITPEQSETKL GEYLDELEFL AKTAGIQSVK RFTQRLDYSH PVSFVGSGKL LEIKDFTENK NNKIDIVIFD DELTTKQLRN LETILKVKIM DRTSLILDIF ASRAQTAHAK KQVELAQYNY MLPRLTHLWT HLERQSGGFR MRGPGETQLE TDRRIILNKI IHLKKELKKI DKQKVVQRSN RGRMVRVALV GYTNVGKSTL MSLLSKSDIF TENKLFATID TTVRKVTINN LVFLLTDTVG FIRKLPTELI ESFKSTLDEV READLLIHIV DISHPSFEEQ VKVVIQTLNE INKEKKPYIV VFNKIDALLH ITGDKNDLIS RDQANVPLDE LKKTWGGKLH ENCVFISARK KQNIEKLKKK LYDRVKEIHI QRFSYKEFIS PSFKPLRKNT KIYDREIK // ID B6YY01_THEON Unreviewed; 429 AA. AC B6YY01; DT 20-JAN-2009, integrated into UniProtKB/TrEMBL. DT 20-JAN-2009, sequence version 1. DT 07-JUN-2017, entry version 71. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=TON_1474 {ECO:0000313|EMBL:ACJ16964.1}; OS Thermococcus onnurineus (strain NA1). OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae; OC Thermococcus. OX NCBI_TaxID=523850 {ECO:0000313|EMBL:ACJ16964.1, ECO:0000313|Proteomes:UP000002727}; RN [1] {ECO:0000313|EMBL:ACJ16964.1, ECO:0000313|Proteomes:UP000002727} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NA1 {ECO:0000313|EMBL:ACJ16964.1, RC ECO:0000313|Proteomes:UP000002727}; RX PubMed=18790866; DOI=10.1128/JB.00746-08; RA Lee H.S., Kang S.G., Bae S.S., Lim J.K., Cho Y., Kim Y.J., Jeon J.H., RA Cha S.S., Kwon K.K., Kim H.T., Park C.J., Lee H.W., Kim S.I., Chun J., RA Colwell R.R., Kim S.J., Lee J.H.; RT "The complete genome sequence of Thermococcus onnurineus NA1 reveals a RT mixed heterotrophic and carboxydotrophic metabolism."; RL J. Bacteriol. 190:7491-7499(2008). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000855; ACJ16964.1; -; Genomic_DNA. DR ProteinModelPortal; B6YY01; -. DR STRING; 523850.TON_1474; -. DR EnsemblBacteria; ACJ16964; ACJ16964; TON_1474. DR KEGG; ton:TON_1474; -. DR PATRIC; fig|523850.10.peg.1486; -. DR eggNOG; arCOG00353; Archaea. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG093Z07D6; -. DR Proteomes; UP000002727; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000002727}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000002727}. FT DOMAIN 187 363 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 429 AA; 49477 MW; 5565DA869F85F44C CRC64; MMRAIGVIRK SRRERISREE FEELLRSAGY EVVAILEQNR EEHPKYNIGK GKLEELKELV RELQPDKVIF ANKLTPSQAY NLWKELRVEI IDKWQLVLEI FERRAHSKEA KLQVELASLQ YEVPLVKEAI RRIKLGDRAG FKGMGEYQTQ QYLKHIRYRM GKIRKELERV KADREVKRKR REEVGFILLA LAGYTNAGKS TLLNTLAGEE IEARDQMFTT LDTTTRRFKL GGKRVLVTDT VGFIDGLPPF IVEAFHSTLE EIVKADIVLL VLDVSEPWPE IRRKFLASLN VLRELKALDK PMVVVLNKRD LTSEEDVKDK AERIIEIVEE RGINVSRVVS ISAKFGQLEE LYGALEEVVL TLPKYGAFEI TVREPEKVPQ VMALINAIGE VLSVEYGEET KIEAYIQTGM IKELTRLGVE IKRLNQPHQ // ID B7AEC4_BACEV Unreviewed; 418 AA. AC B7AEC4; DT 10-FEB-2009, integrated into UniProtKB/TrEMBL. DT 10-FEB-2009, sequence version 1. DT 07-JUN-2017, entry version 41. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=BACEGG_00744 {ECO:0000313|EMBL:EEC54867.1}; OS Bacteroides eggerthii (strain ATCC 27754 / DSM 20697 / JCM 12986 / CIP OS 104285 / NCTC 11155 / VPI T5-42B-1). OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae; OC Bacteroides. OX NCBI_TaxID=483216 {ECO:0000313|EMBL:EEC54867.1, ECO:0000313|Proteomes:UP000004742}; RN [1] {ECO:0000313|EMBL:EEC54867.1, ECO:0000313|Proteomes:UP000004742} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 20697 {ECO:0000313|EMBL:EEC54867.1, RC ECO:0000313|Proteomes:UP000004742}; RA Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., RA Liep D., Gordon J.; RT "Draft genome sequence of Bacteroides eggerthii (DSM 20697)."; RL Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:EEC54867.1, ECO:0000313|Proteomes:UP000004742} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 20697 {ECO:0000313|EMBL:EEC54867.1, RC ECO:0000313|Proteomes:UP000004742}; RA Fulton L., Clifton S., Fulton B., Xu J., Minx P., Pepin K.H., RA Johnson M., Thiruvilangam P., Bhonagiri V., Nash W.E., Mardis E.R., RA Wilson R.K.; RL Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABVO01000013; EEC54867.1; -; Genomic_DNA. DR RefSeq; WP_004289025.1; NZ_DS995509.1. DR ProteinModelPortal; B7AEC4; -. DR STRING; 483216.BACEGG_00744; -. DR EnsemblBacteria; EEC54867; EEC54867; BACEGG_00744. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR Proteomes; UP000004742; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000004742}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}. FT DOMAIN 216 400 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 418 AA; 47784 MW; 0D925D7EFF71648C CRC64; MKEFVISEAQ VETAVLVGLV TKTQDERKTN EYLDELEFLA ETAGAEVVKR FTQKLDQANS VTYVGKGKLE EIKEYIRNEE EAEREIGMVI FDDELSAKQI RNIEAELKIK ILDRTSLILD IFAMRAQTAN AKTQVELAQY KYMLPRLQRL WTHLERQGGG SGAGGGKGSV GLRGPGETQL EMDRRIILNR MSLLKERLAE IDKQKATQRK NRGRLIRVAL VGYTNVGKST LMTLLSKSEV FAENKLFATL DTTVRKVIIE NLPFLLSDTV GFIRKLPTDL VDSFKSTLDE VREADLLLHI VDISHPDFEE QIEVVNKTLA DIGASGKPMI LVFNKIDAYT YIAKAEDDLT PRTKENLTLE ELMKTWMAKM EDNCLFISAR ERINVEELKS VVYQRVKELH VQKYPYNDFL YQTYEEEV // ID B7CCS2_9FIRM Unreviewed; 408 AA. AC B7CCS2; DT 10-FEB-2009, integrated into UniProtKB/TrEMBL. DT 10-FEB-2009, sequence version 1. DT 07-JUN-2017, entry version 42. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:EEC89444.1}; GN ORFNames=EUBIFOR_02000 {ECO:0000313|EMBL:EEC89444.1}; OS Holdemanella biformis DSM 3989. OC Bacteria; Firmicutes; Erysipelotrichia; Erysipelotrichales; OC Erysipelotrichaceae; Holdemanella. OX NCBI_TaxID=518637 {ECO:0000313|EMBL:EEC89444.1, ECO:0000313|Proteomes:UP000004315}; RN [1] {ECO:0000313|EMBL:EEC89444.1, ECO:0000313|Proteomes:UP000004315} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 3989 {ECO:0000313|EMBL:EEC89444.1, RC ECO:0000313|Proteomes:UP000004315}; RA Fulton L., Clifton S., Fulton B., Xu J., Minx P., Pepin K.H., RA Johnson M., Bhonagiri V., Nash W.E., Mardis E.R., Wilson R.K.; RL Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:EEC89444.1, ECO:0000313|Proteomes:UP000004315} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 3989 {ECO:0000313|EMBL:EEC89444.1, RC ECO:0000313|Proteomes:UP000004315}; RA Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., RA Liep D., Gordon J.; RT "Draft genome sequence of Eubacterium biforme (DSM 3989)."; RL Submitted (NOV-2008) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EEC89444.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABYT01000105; EEC89444.1; -; Genomic_DNA. DR RefSeq; WP_003865784.1; NZ_DS996846.1. DR ProteinModelPortal; B7CCS2; -. DR STRING; 518637.EUBIFOR_02000; -. DR EnsemblBacteria; EEC89444; EEC89444; EUBIFOR_02000. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000004315; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000004315}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000004315}. FT DOMAIN 192 355 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 408 AA; 47138 MW; 91A84AC749FAF1B7 CRC64; MEKAILIGVQ TYTSHSFEER MEEMKELALA CDIEICMSVS QNLEHPHKKY YMNPGKIEEI KRILEDQACS MVLVLETISP SVQRNLSDFF DCEVMDKSAL ILEIFASRAK TKESMLQVEC ARLKYLLPRL QGSYKHMDRQ RGGSKNKGTG EKKIELDARR IESKIHFVEK ELDKIHTQRS VQRNQRKKGM VKSVALTGYT NAGKSSIMNG FVNEDKSVFE KDMLFATLTT STRQIETENH NVFTLSDTVG FISDLPHSLV QAFHSTLEEA VVSDLILKVV DISDEHKDSK LQVCEETLKE IGCEKVPYLY VFNKCDQTNI EYPKRVENRI YICAKEKSSI AFLKQEIEKE LFHMETLHVV IPYEKVSVLD YIHTNGKVHK QEYKEDGIEV DFSIQQDLIH RVDRLLRI // ID B7GDG2_PHATC Unreviewed; 415 AA. AC B7GDG2; DT 10-FEB-2009, integrated into UniProtKB/TrEMBL. DT 10-FEB-2009, sequence version 1. DT 05-JUL-2017, entry version 47. DE SubName: Full=Predicted protein {ECO:0000313|EMBL:EEC43339.1}; DE Flags: Fragment; GN ORFNames=PHATRDRAFT_1719 {ECO:0000313|EMBL:EEC43339.1}; OS Phaeodactylum tricornutum (strain CCAP 1055/1). OC Eukaryota; Stramenopiles; Bacillariophyta; Bacillariophyceae; OC Bacillariophycidae; Naviculales; Phaeodactylaceae; Phaeodactylum. OX NCBI_TaxID=556484 {ECO:0000313|Proteomes:UP000000759}; RN [1] {ECO:0000313|EMBL:EEC43339.1, ECO:0000313|Proteomes:UP000000759} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CCAP 1055/1 {ECO:0000313|EMBL:EEC43339.1, RC ECO:0000313|Proteomes:UP000000759}; RX PubMed=18923393; DOI=10.1038/nature07410; RA Bowler C., Allen A.E., Badger J.H., Grimwood J., Jabbari K., Kuo A., RA Maheswari U., Martens C., Maumus F., Otillar R.P., Rayko E., RA Salamov A., Vandepoele K., Beszteri B., Gruber A., Heijde M., RA Katinka M., Mock T., Valentin K., Verret F., Berges J.A., Brownlee C., RA Cadoret J.P., Chiovitti A., Choi C.J., Coesel S., De Martino A., RA Detter J.C., Durkin C., Falciatore A., Fournet J., Haruta M., RA Huysman M.J., Jenkins B.D., Jiroutova K., Jorgensen R.E., Joubert Y., RA Kaplan A., Kroger N., Kroth P.G., La Roche J., Lindquist E., RA Lommer M., Martin-Jezequel V., Lopez P.J., Lucas S., Mangogna M., RA McGinnis K., Medlin L.K., Montsant A., Oudot-Le Secq M.P., Napoli C., RA Obornik M., Parker M.S., Petit J.L., Porcel B.M., Poulsen N., RA Robison M., Rychlewski L., Rynearson T.A., Schmutz J., Shapiro H., RA Siaut M., Stanley M., Sussman M.R., Taylor A.R., Vardi A., RA von Dassow P., Vyverman W., Willis A., Wyrwicz L.S., Rokhsar D.S., RA Weissenbach J., Armbrust E.V., Green B.R., Van de Peer Y., RA Grigoriev I.V.; RT "The Phaeodactylum genome reveals the evolutionary history of diatom RT genomes."; RL Nature 456:239-244(2008). RN [2] {ECO:0000313|EMBL:EEC43339.1, ECO:0000313|Proteomes:UP000000759} RP GENOME REANNOTATION. RC STRAIN=CCAP 1055/1 {ECO:0000313|EMBL:EEC43339.1, RC ECO:0000313|Proteomes:UP000000759}; RG Diatom Consortium; RA Grigoriev I., Grimwood J., Kuo A., Otillar R.P., Salamov A., RA Detter J.C., Lindquist E., Shapiro H., Lucas S., Glavina del Rio T., RA Pitluck S., Rokhsar D., Bowler C.; RL Submitted (AUG-2008) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CM000630; EEC43339.1; -; Genomic_DNA. DR RefSeq; XP_002185207.1; XM_002185171.1. DR UniGene; Ptc.2053; -. DR ProteinModelPortal; B7GDG2; -. DR STRING; 2850.Phatr1719; -. DR GeneID; 7199022; -. DR KEGG; pti:PHATRDRAFT_1719; -. DR HOGENOM; HOG000260368; -. DR InParanoid; B7GDG2; -. DR KO; K03665; -. DR Proteomes; UP000000759; Chromosome 28. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000000759}; KW Reference proteome {ECO:0000313|Proteomes:UP000000759}. FT DOMAIN 194 365 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT NON_TER 1 1 {ECO:0000313|EMBL:EEC43339.1}. FT NON_TER 415 415 {ECO:0000313|EMBL:EEC43339.1}. SQ SEQUENCE 415 AA; 46533 MW; BA30E65BE6EE8350 CRC64; FTLDESLIEM RELIKTAGLE LVGEVTQRLN DVNPRTYIGS GKVKEAEEKM KEYDCCTIVF DAELSPGQQK SLENAFNKES LQNDFLFQGG EIKVIDRTAL ILDIFAQHAK TREGKLQVDL ALHEYRKPRL TRMWTHLERQ SGAGGVGLRG PGESQLEIDK RLVRDRIITL KQKIDDVQKQ RAMHRRGRER TGLPILSLVG YTNAGKSSML NYLTKAGVMA ESMLFATLDP TTRKVKLPGY KTHPEVLLTD TVGFIQKLPT HLVAAFRATL EEVQEADVLI HVIDVSNPTW RKQEQSVRSV LADIEASDKP MVRVLNKIDL LDPVEADELR CQAALEDFTV AVSALEGDGM QDFVSVVEDA MSSLLVPIEV ELPYSKGEEL NIVHEQGNVE VVDYREKGTY VRALVPQAVA NRLEP // ID B7GI94_ANOFW Unreviewed; 415 AA. AC B7GI94; DT 10-FEB-2009, integrated into UniProtKB/TrEMBL. DT 10-FEB-2009, sequence version 1. DT 07-JUN-2017, entry version 68. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Aflv_1510 {ECO:0000313|EMBL:ACJ33876.1}; OS Anoxybacillus flavithermus (strain DSM 21510 / WK1). OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Anoxybacillus. OX NCBI_TaxID=491915 {ECO:0000313|EMBL:ACJ33876.1, ECO:0000313|Proteomes:UP000000742}; RN [1] {ECO:0000313|EMBL:ACJ33876.1, ECO:0000313|Proteomes:UP000000742} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 21510 / WK1 {ECO:0000313|Proteomes:UP000000742}; RX PubMed=19014707; DOI=10.1186/gb-2008-9-11-r161; RA Saw J.H., Mountain B.W., Feng L., Omelchenko M.V., Hou S., Saito J.A., RA Stott M.B., Li D., Zhao G., Wu J., Galperin M.Y., Koonin E.V., RA Makarova K.S., Wolf Y.I., Rigden D.J., Dunfield P.F., Wang L., RA Alam M.; RT "Encapsulated in silica: genome, proteome and physiology of the RT thermophilic bacterium Anoxybacillus flavithermus WK1."; RL Genome Biol. 9:R161.1-R161.16(2008). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000922; ACJ33876.1; -; Genomic_DNA. DR RefSeq; WP_012575106.1; NC_011567.1. DR ProteinModelPortal; B7GI94; -. DR STRING; 491915.Aflv_1510; -. DR EnsemblBacteria; ACJ33876; ACJ33876; Aflv_1510. DR KEGG; afl:Aflv_1510; -. DR PATRIC; fig|491915.6.peg.1553; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000000742; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000000742}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Hydrolase {ECO:0000313|EMBL:ACJ33876.1}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Protease {ECO:0000313|EMBL:ACJ33876.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000742}. FT DOMAIN 196 358 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 415 AA; 47235 MW; D5F21186792E247E CRC64; MQKERVIIVG CQLPHVDDER FSYSMEELSS LVHTANGEVV ISLTQRRDTI HPATYIGKGK VEELVRLIEQ FEPDVVIFND ELSPSQNRNL TKVLNVRVID RTQLILDIFA SRARSKEGKL QVELAQLQYI LPRLSGQGVE LSRLGGGIGT RGPGETKLET DRRHIRRRID EIKAQLKAVV EHRERYRERR KKNAVFQIAL VGYTNAGKST LFNRLTNADA LEENLLFATL DPLTRKLVLP SGYTALLTDT VGFIQDLPTT LVAAFRSTLE EVKEADLILH IVDSSNPDYI QHEQTVYRLL EELEATAIPI ATVYNKRDIV LPSFVPSPKT DYLLVSAFHE QDVQTLRHFI EQKMIEVMEH YNVAIPSFAG KLLAQLKAET IVQHMYFNEQ SGMYECSGYL LPEHPLLAQL TTYQK // ID B7JBY7_ACIF2 Unreviewed; 432 AA. AC B7JBY7; DT 10-FEB-2009, integrated into UniProtKB/TrEMBL. DT 10-FEB-2009, sequence version 1. DT 07-JUN-2017, entry version 59. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:ACK78687.1}; GN OrderedLocusNames=AFE_1885 {ECO:0000313|EMBL:ACK78687.1}; OS Acidithiobacillus ferrooxidans (strain ATCC 23270 / DSM 14882 / CIP OS 104768 / NCIMB 8455) (Ferrobacillus ferrooxidans (strain ATCC 23270)). OC Bacteria; Proteobacteria; Acidithiobacillia; Acidithiobacillales; OC Acidithiobacillaceae; Acidithiobacillus. OX NCBI_TaxID=243159 {ECO:0000313|EMBL:ACK78687.1, ECO:0000313|Proteomes:UP000001362}; RN [1] {ECO:0000313|EMBL:ACK78687.1, ECO:0000313|Proteomes:UP000001362} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 23270 / DSM 14882 / CIP 104768 / NCIMB 8455 RC {ECO:0000313|Proteomes:UP000001362}; RX PubMed=19077236; DOI=10.1186/1471-2164-9-597; RA Valdes J., Pedroso I., Quatrini R., Dodson R.J., Tettelin H., RA Blake R.II., Eisen J.A., Holmes D.S.; RT "Acidithiobacillus ferrooxidans metabolism: from genome sequence to RT industrial applications."; RL BMC Genomics 9:597-597(2008). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001219; ACK78687.1; -; Genomic_DNA. DR RefSeq; WP_012536820.1; NC_011761.1. DR ProteinModelPortal; B7JBY7; -. DR STRING; 243159.AFE_1885; -. DR PaxDb; B7JBY7; -. DR PRIDE; B7JBY7; -. DR EnsemblBacteria; ACK78687; ACK78687; AFE_1885. DR KEGG; afr:AFE_1885; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000001362; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000001362}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000001362}. FT DOMAIN 195 361 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 432 AA; 47470 MW; 7F879D59726C6B43 CRC64; MAAPRERILL VHVVLHGEAD PDAGAEFFHL ATDSGADVLE LLSVQRGRPD PATFLGRGKV AELAERVAAL SVDLVLFDRV LSPVQERNLE GALHCRVVDR VGLILDIFAR RARTHEGKLQ VELAQLTRLR TRLVRGWTHL ERQRGGIGLR GPGETQLETD RRLIGERILS LRGRLIKVAA HRATQRRARQ RAPLPTVALV GYTNAGKSSL FNTLTKSSSY AADRLFATLD PAIRRLQIEG HEAILLADTV GFLRDLPTDL IAAFRATLEE VNQAQLLLHV VDSSAPDRDA QIAAVDAVLR EIGAEDIPRL LVLNKVELTG DMPGNVYESS GKLAAVRVSA HSGIGIPELL QAVTQRVGRS MLRADLTLMP EEGALRARIH RLASVIAERF DEQGRTHLTF DIDGLNWRRL HTQMRDSGCQ AMDAPPTIPV DG // ID B7K355_CYAP8 Unreviewed; 564 AA. AC B7K355; DT 10-FEB-2009, integrated into UniProtKB/TrEMBL. DT 10-FEB-2009, sequence version 1. DT 07-JUN-2017, entry version 56. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=PCC8801_0275 {ECO:0000313|EMBL:ACK64375.1}; OS Cyanothece sp. (strain PCC 8801) (Synechococcus sp. (strain PCC 8801 / OS RF-1)). OC Bacteria; Cyanobacteria; Oscillatoriophycideae; Oscillatoriales; OC Cyanothecaceae; Cyanothece. OX NCBI_TaxID=41431 {ECO:0000313|EMBL:ACK64375.1, ECO:0000313|Proteomes:UP000008204}; RN [1] {ECO:0000313|Proteomes:UP000008204} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=PCC 8801 {ECO:0000313|Proteomes:UP000008204}; RX PubMed=21972240; DOI=10.1128/mBio.00214-11; RA Bandyopadhyay A., Elvitigala T., Welsh E., Stockel J., Liberton M., RA Min H., Sherman L.A., Pakrasi H.B.; RT "Novel metabolic attributes of the genus Cyanothece, comprising a RT group of unicellular nitrogen-fixing Cyanobacteria."; RL MBio 2:E214-E214(2011). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001287; ACK64375.1; -; Genomic_DNA. DR RefSeq; WP_012593652.1; NC_011726.1. DR ProteinModelPortal; B7K355; -. DR STRING; 41431.PCC8801_0275; -. DR EnsemblBacteria; ACK64375; ACK64375; PCC8801_0275. DR KEGG; cyp:PCC8801_0275; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; EREVIIT; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000008204; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000008204}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000008204}. FT DOMAIN 395 564 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 354 391 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 564 AA; 62540 MW; 552F1C2C71C2A1EA CRC64; METIYGNLQG LKTSQLKQLQ NLYHQRLRSD RLTTPEFAQR LAAISSEINQ PVSAYVNRRG QVIRVGVGTP QQTQIPLLEL PRYGAERLSG IRCLATQLKP EAPKESSLTA MVLQRLDALV VLPLSGEGKL RRGGGATGYV KEAYLAHLLP SSDLNPNQQY YWTVSPPMSL ETLAEQDFLS LVEGLETEFR REYVAQQVDS DHERVMVVGL QTDDLSDRQF EEGLAEVGRL VETAGGEILE TLRQKRATPH PQTVVGSGKV QEIALRVQTL GANLVVFDRD LSPAQVRNLE RQLGVRVVDR TEIILDIFAQ RAQSRAGKLQ VELAQLEYML PRLVGRGQAM SRLGGGIGTR GPGETKLETE RRAIGRRISR LQQEVNQLQA HRSRLRHQRQ QQEVPSVAIV GYTNAGKSTL INALTKADVY TADQLFATLD PTTRRLQVVE PTTGESTTLL LTDTVGFIHE LPPSLVDAFR ATLEEVTEAD ALLHVVDLSH PAWEHQIESV MTILEEISLT PGVILLAFNK IDQVDSDTLE RAKLNYPEAV FISAQQGFGL ETLRQQLVRV GVGG // ID B7RFN2_9RHOB Unreviewed; 412 AA. AC B7RFN2; DT 10-FEB-2009, integrated into UniProtKB/TrEMBL. DT 10-FEB-2009, sequence version 1. DT 07-JUN-2017, entry version 40. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:EEB84480.1}; GN ORFNames=RGAI101_1630 {ECO:0000313|EMBL:EEB84480.1}; OS Roseobacter sp. GAI101. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae; Roseobacter. OX NCBI_TaxID=391589 {ECO:0000313|EMBL:EEB84480.1, ECO:0000313|Proteomes:UP000002944}; RN [1] {ECO:0000313|EMBL:EEB84480.1, ECO:0000313|Proteomes:UP000002944} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=GAI101 {ECO:0000313|EMBL:EEB84480.1, RC ECO:0000313|Proteomes:UP000002944}; RA Edwards R., Ferriera S., Johnson J., Kravitz S., Beeson K., Sutton G., RA Rogers Y.-H., Friedman R., Frazier M., Venter J.C.; RL Submitted (JUL-2008) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; DS999213; EEB84480.1; -; Genomic_DNA. DR ProteinModelPortal; B7RFN2; -. DR STRING; 391589.RGAI101_1630; -. DR EnsemblBacteria; EEB84480; EEB84480; RGAI101_1630. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000002944; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000002944}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000002944}. FT DOMAIN 192 361 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 412 AA; 45536 MW; A6F14BB0A0673F03 CRC64; MLHPDIKSNN DRRIAEPALA EAVALAEALP QLEVTGADVV PLRTVSAGML FGSGKIEELK QKFEAAEVEL VLVDGAVTPV QQRNLEKAWG VKLLDRTGLI LEIFSDRAAT REGVLQVEMA ALNYQRTRLV RAWTHLERQR GGLGFVGGPG ETQIESDRRA IDEQLVRLRR QLDKVVKTRA LHRAARAKVP YPIVALVGYT NAGKSTLFNR LTGADVMAKD MLFATLDPTM RSLVLPDGPE IILSDTVGFI SDLPTELVAA FRATLEEVLA ADIICHVRDI SHAETEEQAQ NVRDILASLG VPKETRSFEV WNKLDLLAPD RADAVRARAE RDPNVLAISA ITGEGLEQMQ SVIAEALQGV VREADLVLGY DQGKKRAWLF EQEVVLNEEQ TEDGFVLTVR WSAQQEAQFQ RL // ID B7RW33_9GAMM Unreviewed; 436 AA. AC B7RW33; DT 10-FEB-2009, integrated into UniProtKB/TrEMBL. DT 10-FEB-2009, sequence version 1. DT 30-AUG-2017, entry version 44. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:EEB79496.1}; GN ORFNames=GPB2148_2427 {ECO:0000313|EMBL:EEB79496.1}; OS marine gamma proteobacterium HTCC2148. OC Bacteria; Proteobacteria; Gammaproteobacteria; Cellvibrionales; OC Halieaceae. OX NCBI_TaxID=247634 {ECO:0000313|EMBL:EEB79496.1, ECO:0000313|Proteomes:UP000002793}; RN [1] {ECO:0000313|Proteomes:UP000002793} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=HTCC2148 {ECO:0000313|Proteomes:UP000002793}; RX PubMed=20472793; DOI=10.1128/JB.00511-10; RA Thrash J.C., Cho J.C., Ferriera S., Johnson J., Vergin K.L., RA Giovannoni S.J.; RT "Genome sequences of strains HTCC2148 and HTCC2080, belonging to the RT OM60/NOR5 clade of the Gammaproteobacteria."; RL J. Bacteriol. 192:3842-3843(2010). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; DS999224; EEB79496.1; -; Genomic_DNA. DR ProteinModelPortal; B7RW33; -. DR STRING; 247634.GPB2148_2427; -. DR EnsemblBacteria; EEB79496; EEB79496; GPB2148_2427. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000002793; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000002793}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000002793}. FT DOMAIN 212 378 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 436 AA; 48960 MW; 4790AB1066F51866 CRC64; MSAVAPVSKT EVALFFDRPE SGERAVLVHL NLDSESERED PREFEELVLS AGGDPAAYIM GHRTAPHPRT FIGSGKLEEI RDEVNLQEAE VVMFNHILSP SQERNLEQEL ECRVLDRTGL ILDIFAQRAR THEGKLQVEL AQLQHVATRL VRGWTHLERQ KGGIGLRGPG ETQLETDRRL LRIRIKSITA RLEKVRKQRD QGRRSRKRQE IPTVSLVGYT NAGKSTLFNY ITDSGVYAAD QLFATLDPTL RRLELENVGP VVLADTVGFI AHLPHKLVEA FKATLEETLN ADLLLHVIDA ASDEREDNIY QVHEVLQEIG ADEIPRLEIY NKLDLLEQKP RIDRNADGIP ERVWLSAATG DGVSLLLQAV SEVVGQDMVD EQLEIAPDQG GLRAALYRLG AVESENYSDD GVAHLQVRLP RADWNRLMKK GPEPLF // ID B7VI56_VIBTL Unreviewed; 435 AA. AC B7VI56; DT 10-FEB-2009, integrated into UniProtKB/TrEMBL. DT 10-FEB-2009, sequence version 1. DT 30-AUG-2017, entry version 64. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=VS_0271 {ECO:0000313|EMBL:CAV17293.1}; OS Vibrio tasmaniensis (strain LGP32) (Vibrio splendidus (strain Mel32)). OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; OC Vibrionaceae; Vibrio. OX NCBI_TaxID=575788 {ECO:0000313|EMBL:CAV17293.1, ECO:0000313|Proteomes:UP000009100}; RN [1] {ECO:0000313|EMBL:CAV17293.1, ECO:0000313|Proteomes:UP000009100} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=LGP32 {ECO:0000313|EMBL:CAV17293.1, RC ECO:0000313|Proteomes:UP000009100}; RA Mazel D., Le Roux F.; RT "Vibrio splendidus str. LGP32 complete genome."; RL Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; FM954972; CAV17293.1; -; Genomic_DNA. DR RefSeq; WP_009847881.1; NC_011753.2. DR ProteinModelPortal; B7VI56; -. DR STRING; 575788.VS_0271; -. DR EnsemblBacteria; CAV17293; CAV17293; VS_0271. DR GeneID; 7159922; -. DR KEGG; vsp:VS_0271; -. DR PATRIC; fig|575788.5.peg.1650; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000009100; Chromosome 1. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000009100}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000009100}. FT DOMAIN 198 365 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 435 AA; 49215 MW; 37D126A59E75596F CRC64; MFDRYESGER AVLVHINFTQ EGEWEDLSEC EMLVSSAGVE TLQVITGSRQ SPLPKYYVGE GKALEIAQAV QLTGAEIVIF NHSLSPAQER NLEQLCKCRV IDRTGLILDI FAQRARTHEG KLQVELAQLR HISTRLIRGW THLERQKGGI GLRGPGETQL ETDRRLLRDR IKAILRRLAK VAKQREQGRR ARNRAEIPTI SLVGYTNAGK STLFNRITSA GVYAADQLFA TLDPTLRKID LADVGPAILA DTVGFIRHLP HDLVAAFKAT LQETQEADIL LHVVDASDDR FRENIQAVHE VLEEIDAHEV PTLVVMNKID CMEDQKPRIE RDEEGAPRAV WVSAMEGEGI ELLFEALTER LASQMVQFRL CIPHQHQGRI RSLFFEMKCI QQEEYDENGN LLIDIRMQQI DWSKLEKREG ALLGGFIVTK ETATV // ID B7VL62_VIBTL Unreviewed; 455 AA. AC B7VL62; DT 10-FEB-2009, integrated into UniProtKB/TrEMBL. DT 10-FEB-2009, sequence version 1. DT 07-JUN-2017, entry version 54. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=VS_0880 {ECO:0000313|EMBL:CAV17887.1}; OS Vibrio tasmaniensis (strain LGP32) (Vibrio splendidus (strain Mel32)). OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; OC Vibrionaceae; Vibrio. OX NCBI_TaxID=575788 {ECO:0000313|EMBL:CAV17887.1, ECO:0000313|Proteomes:UP000009100}; RN [1] {ECO:0000313|EMBL:CAV17887.1, ECO:0000313|Proteomes:UP000009100} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=LGP32 {ECO:0000313|EMBL:CAV17887.1, RC ECO:0000313|Proteomes:UP000009100}; RA Mazel D., Le Roux F.; RT "Vibrio splendidus str. LGP32 complete genome."; RL Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; FM954972; CAV17887.1; -; Genomic_DNA. DR RefSeq; WP_012603471.1; NC_011753.2. DR ProteinModelPortal; B7VL62; -. DR STRING; 575788.VS_0880; -. DR EnsemblBacteria; CAV17887; CAV17887; VS_0880. DR GeneID; 7160478; -. DR KEGG; vsp:VS_0880; -. DR PATRIC; fig|575788.5.peg.2207; -. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; VILEIFH; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000009100; Chromosome 1. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000009100}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000009100}. FT DOMAIN 235 370 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 196 230 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 455 AA; 50497 MW; 357353C4549019A5 CRC64; MKLTAKPAAN NALLISITTP DFKGDEAKES LAELARLVTT LGFKVVGTQS QHHSSSQRQN VLGAGKLAEI AHLTGYQGSI EEAEDEDFLD ESGLFDSEID ELDFDDLPTG NFQYGAADVV VFDCDLSPSQ MRTVEASLGV EVFDRTGIII EIFSRHARTR TARLQVDIAR LNYLVPRLRE TAEGDKERQM GQGAGETSLE LDRRNVRDQI AALKRELVSV QDEMKTRRTR RAELFTVALV GYTNAGKSSM MRAMTATEVV GEDKLFATLD TTVRALQPIT QPRILVSDTV GFIKKLPHDL VASFHSTLAE AHDASLLLYV VDASDVSFRA QLDVVHDVLA QVGVEGSEKL LVLNKCDRLT EEQQLELIEE FPDAMLTSTR DPLDITKLHK YIVGVAEEGM IEEEITIPYS GQGIIGEIRS NMSVVKEEYD YECIKLTVRS SEIDLARLKK RMQNS // ID B8AVN9_ORYSI Unreviewed; 552 AA. AC B8AVN9; DT 03-MAR-2009, integrated into UniProtKB/TrEMBL. DT 03-MAR-2009, sequence version 1. DT 30-AUG-2017, entry version 53. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EEC76814.1}; GN ORFNames=OsI_14944 {ECO:0000313|EMBL:EEC76814.1}; OS Oryza sativa subsp. indica (Rice). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; BOP clade; OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa. OX NCBI_TaxID=39946 {ECO:0000313|EMBL:EEC76814.1, ECO:0000313|Proteomes:UP000007015}; RN [1] {ECO:0000313|EMBL:EEC76814.1, ECO:0000313|Proteomes:UP000007015} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. 93-11 {ECO:0000313|Proteomes:UP000007015}; RX PubMed=15685292; DOI=10.1371/journal.pbio.0030038; RA Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S., RA Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., RA Cong L., Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., RA Wang J., Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., RA Wang J., Wang X., Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., RA Zhang Z., Bao J., Han Y., Dong L., Ji J., Chen P., Wu S., Liu J., RA Xiao Y., Bu D., Tan J., Yang L., Ye C., Zhang J., Xu J., Zhou Y., RA Yu Y., Zhang B., Zhuang S., Wei H., Liu B., Lei M., Yu H., Li Y., RA Xu H., Wei S., He X., Fang L., Zhang Z., Zhang Y., Huang X., Su Z., RA Tong W., Li J., Tong Z., Li S., Ye J., Wang L., Fang L., Lei T., RA Chen C., Chen H., Xu Z., Li H., Huang H., Zhang F., Xu H., Li N., RA Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q., Li W., RA Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J., Gao L., RA Zheng W., Hao B., Liu S., Wang W., Yuan L., Cao M., McDermott J., RA Samudrala R., Wang J., Wong G.K., Yang H.; RT "The genomes of Oryza sativa: a history of duplications."; RL PLoS Biol. 3:266-281(2005). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CM000129; EEC76814.1; -; Genomic_DNA. DR ProteinModelPortal; B8AVN9; -. DR STRING; 39946.BGIOSGA015550-PA; -. DR EnsemblPlants; BGIOSGA015550-TA; BGIOSGA015550-PA; BGIOSGA015550. DR Gramene; BGIOSGA015550-TA; BGIOSGA015550-PA; BGIOSGA015550. DR eggNOG; KOG0410; Eukaryota. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR OMA; VILEIFH; -. DR OrthoDB; EOG093609UJ; -. DR Proteomes; UP000007015; Chromosome 4. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000007015}; KW Reference proteome {ECO:0000313|Proteomes:UP000007015}. FT DOMAIN 328 493 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 294 321 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 552 AA; 60736 MW; 9BD066B73EB83E26 CRC64; MRAACFFTGA AATASLPLPS TSASASSCCQ RRPASLRCSR PRRSFGVARA LDERLVEAAP PAETEVEEPG VADGGGEGEG EVEDSAPSGE EEEEEEPARA PVRSRRRQEE EEEEAAPGHD RFKLINGKEI FQEKAYLVGV ECKRSGGSMF SIEESLEELE QLADTAGLMV VGSTYQKLST PNPRTYIGSG KVAEIKSAIH AHDVETVIFD DELSPGQLRN LEKSFGGGVR VCDRTALILD IFNQRAATHE AALQVTLAQM EYQLPRLTKM WSHLERQSGG QVKGMGEKQI EVDKRILRTQ ISALRKELES VRKHRKLYRN RRQSVPIPVV SLVGYTNAGK STLLNRLTGA DVLAEDKLFA TLDPTTRRVL MKNGTEFLLT DTVGFIQKLP TMLVAAFRAT LEEISESSVI VHLVDISHPL AQQQIDAVDK VLKELDIESI PKLVVWNKID NTDDTLRVKE EAEKQGIICI SAINGDGLEE FCNAIQAKLK DSLVPIEAFV PYDKGELLSD IHKVGMVEKT EYTENGTFVK AHVPLPLARL LTPLRQQVAA VS // ID B8CC20_THAPS Unreviewed; 453 AA. AC B8CC20; DT 03-MAR-2009, integrated into UniProtKB/TrEMBL. DT 03-MAR-2009, sequence version 1. DT 07-JUN-2017, entry version 51. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EED88881.1}; GN ORFNames=THAPSDRAFT_42307 {ECO:0000313|EMBL:EED88881.1}; OS Thalassiosira pseudonana (Marine diatom) (Cyclotella nana). OC Eukaryota; Stramenopiles; Bacillariophyta; Coscinodiscophyceae; OC Thalassiosirophycidae; Thalassiosirales; Thalassiosiraceae; OC Thalassiosira. OX NCBI_TaxID=35128 {ECO:0000313|Proteomes:UP000001449}; RN [1] {ECO:0000313|EMBL:EED88881.1, ECO:0000313|Proteomes:UP000001449} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CCMP1335 {ECO:0000313|EMBL:EED88881.1, RC ECO:0000313|Proteomes:UP000001449}; RX PubMed=15459382; DOI=10.1126/science.1101156; RA Armbrust E.V., Berges J.A., Bowler C., Green B.R., Martinez D., RA Putnam N.H., Zhou S., Allen A.E., Apt K.E., Bechner M., RA Brzezinski M.A., Chaal B.K., Chiovitti A., Davis A.K., Demarest M.S., RA Detter J.C., Glavina T., Goodstein D., Hadi M.Z., Hellsten U., RA Hildebrand M., Jenkins B.D., Jurka J., Kapitonov V.V., Kroger N., RA Lau W.W., Lane T.W., Larimer F.W., Lippmeier J.C., Lucas S., RA Medina M., Montsant A., Obornik M., Parker M.S., Palenik B., RA Pazour G.J., Richardson P.M., Rynearson T.A., Saito M.A., RA Schwartz D.C., Thamatrakoln K., Valentin K., Vardi A., Wilkerson F.P., RA Rokhsar D.S.; RT "The genome of the diatom Thalassiosira pseudonana: ecology, RT evolution, and metabolism."; RL Science 306:79-86(2004). RN [2] {ECO:0000313|EMBL:EED88881.1, ECO:0000313|Proteomes:UP000001449} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CCMP1335 {ECO:0000313|EMBL:EED88881.1, RC ECO:0000313|Proteomes:UP000001449}; RX PubMed=18923393; DOI=10.1038/nature07410; RA Bowler C., Allen A.E., Badger J.H., Grimwood J., Jabbari K., Kuo A., RA Maheswari U., Martens C., Maumus F., Otillar R.P., Rayko E., RA Salamov A., Vandepoele K., Beszteri B., Gruber A., Heijde M., RA Katinka M., Mock T., Valentin K., Verret F., Berges J.A., Brownlee C., RA Cadoret J.P., Chiovitti A., Choi C.J., Coesel S., De Martino A., RA Detter J.C., Durkin C., Falciatore A., Fournet J., Haruta M., RA Huysman M.J., Jenkins B.D., Jiroutova K., Jorgensen R.E., Joubert Y., RA Kaplan A., Kroger N., Kroth P.G., La Roche J., Lindquist E., RA Lommer M., Martin-Jezequel V., Lopez P.J., Lucas S., Mangogna M., RA McGinnis K., Medlin L.K., Montsant A., Oudot-Le Secq M.P., Napoli C., RA Obornik M., Parker M.S., Petit J.L., Porcel B.M., Poulsen N., RA Robison M., Rychlewski L., Rynearson T.A., Schmutz J., Shapiro H., RA Siaut M., Stanley M., Sussman M.R., Taylor A.R., Vardi A., RA von Dassow P., Vyverman W., Willis A., Wyrwicz L.S., Rokhsar D.S., RA Weissenbach J., Armbrust E.V., Green B.R., Van de Peer Y., RA Grigoriev I.V.; RT "The Phaeodactylum genome reveals the evolutionary history of diatom RT genomes."; RL Nature 456:239-244(2008). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CM000649; EED88881.1; -; Genomic_DNA. DR RefSeq; XP_002293872.1; XM_002293836.1. DR ProteinModelPortal; B8CC20; -. DR STRING; 35128.Thaps42307; -. DR EnsemblProtists; EED88881; EED88881; THAPSDRAFT_42307. DR GeneID; 7450829; -. DR KEGG; tps:THAPSDRAFT_42307; -. DR eggNOG; KOG0410; Eukaryota. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR InParanoid; B8CC20; -. DR KO; K03665; -. DR Proteomes; UP000001449; Chromosome 14. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR GO; GO:0043022; F:ribosome binding; IBA:GO_Central. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000001449}; KW Reference proteome {ECO:0000313|Proteomes:UP000001449}. FT DOMAIN 194 366 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 453 AA; 50253 MW; F642FE2C29C27811 CRC64; MGFSLEESMV EMRELIKTAG MTCQGEITQR LQEVNPRTYI GTGKVKESQE LLDEINDKLA KELGDGNNCC TVVFDAELTP GQQKALENAF NRKVVDRTAL ILDIFAQHAK TREGKLQVDL ALHEYRKPRL TRMWTHLERQ SGSGGVGLRG PGETQLEVDK RILRDRILVL KEKIDDVQKQ RDLHRRGRKK GGLPVLALVG YTNAGKSTLL NCLTKAGILA ENILFATLDP TTRRVKLPGY KTHPEVLLTD TVGFIQKLPT QLVAAFRATL EEVKEADVLV HIVDVSNPCW RKQEDSVTKV LSEIGAGDKP TVRVFNKLDL LDKEDAELIK YEAACSENFS VGISSLTGEG LSDFVAVVED ALSGLLVPIE LELPYSCGNE INLIHEVGSI EVIDYREMGT YVMGRVPRSL AMKLEQYSIA ASDVEAREAK ASDGDEIDWV ALGKGRHEKK EVS // ID B8CX48_HALOH Unreviewed; 395 AA. AC B8CX48; DT 03-MAR-2009, integrated into UniProtKB/TrEMBL. DT 03-MAR-2009, sequence version 1. DT 07-JUN-2017, entry version 62. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Hore_11140 {ECO:0000313|EMBL:ACL69867.1}; OS Halothermothrix orenii (strain H 168 / OCM 544 / DSM 9562). OC Bacteria; Firmicutes; Clostridia; Halanaerobiales; Halanaerobiaceae; OC Halothermothrix. OX NCBI_TaxID=373903 {ECO:0000313|EMBL:ACL69867.1, ECO:0000313|Proteomes:UP000000719}; RN [1] {ECO:0000313|EMBL:ACL69867.1, ECO:0000313|Proteomes:UP000000719} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=H 168 / OCM 544 / DSM 9562 {ECO:0000313|Proteomes:UP000000719}; RX PubMed=19145256; DOI=10.1371/journal.pone.0004192; RA Mavromatis K., Ivanova N., Anderson I., Lykidis A., Hooper S.D., RA Sun H., Kunin V., Lapidus A., Hugenholtz P., Patel B., Kyrpides N.C.; RT "Genome analysis of the anaerobic thermohalophilic bacterium RT Halothermothrix orenii."; RL PLoS ONE 4:E4192-E4192(2009). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001098; ACL69867.1; -; Genomic_DNA. DR RefSeq; WP_012636052.1; NC_011899.1. DR ProteinModelPortal; B8CX48; -. DR STRING; 373903.Hore_11140; -. DR EnsemblBacteria; ACL69867; ACL69867; Hore_11140. DR KEGG; hor:Hore_11140; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR BioCyc; HORE373903:GHB1-1162-MONOMER; -. DR Proteomes; UP000000719; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000000719}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000000719}. FT DOMAIN 177 342 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 395 AA; 44845 MW; 6DE6EC5DFB781C3F CRC64; MVGQDEISLE ELKRLADTAG VKVLKKLMQR RFVINPAFYI GKGKLKELKH LVFENGANLV IFDNELTPAQ FRNLENFLET RVVDRTQLIL DIFAQHAHTR ESKLQVELAQ LQYLLPRLTG KGEELSRLGG GIGTRGPGET KLEIDRRRIE KRIYKLKQEL KNVKKNRQIQ RKSRKDPVVA LVGYTNAGKS TLLNTLTNAN TEVADKLFAT LDSTLRRLTL PFGKQIIISD TVGFIKKLPH QLVASFQATL EEIKEADILL HVVDSSEPEL ENHIKVVNAV LKELGVFHKE KIMVLNKIDR LEKGQLLDLG IKYPRAVPVS ALSGKCIDNL MGKICEIMLN EMTTVHLKIP YHEAGWINTI HHQGLVLKEK YVNDSIIIKA TIPTELANRL KKYTY // ID B8D665_DESK1 Unreviewed; 351 AA. AC B8D665; DT 03-MAR-2009, integrated into UniProtKB/TrEMBL. DT 03-MAR-2009, sequence version 1. DT 30-AUG-2017, entry version 65. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=DKAM_1270 {ECO:0000313|EMBL:ACL11596.1}; OS Desulfurococcus kamchatkensis (strain DSM 18924 / JCM 16383 / VKM OS B-2413 / 1221n). OC Archaea; Crenarchaeota; Thermoprotei; Desulfurococcales; OC Desulfurococcaceae; Desulfurococcus. OX NCBI_TaxID=490899 {ECO:0000313|EMBL:ACL11596.1, ECO:0000313|Proteomes:UP000006903}; RN [1] {ECO:0000313|EMBL:ACL11596.1, ECO:0000313|Proteomes:UP000006903} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 18924 / JCM 16383 / VKM B-2413 / 1221n RC {ECO:0000313|Proteomes:UP000006903}; RX PubMed=19114480; DOI=10.1128/JB.01525-08; RA Ravin N.V., Mardanov A.V., Beletsky A.V., Kublanov I.V., RA Kolganova T.V., Lebedinsky A.V., Chernyh N.A., RA Bonch-Osmolovskaya E.A., Skryabin K.G.; RT "Complete genome sequence of the anaerobic, protein-degrading RT hyperthermophilic crenarchaeon Desulfurococcus kamchatkensis."; RL J. Bacteriol. 191:2371-2379(2009). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001140; ACL11596.1; -; Genomic_DNA. DR ProteinModelPortal; B8D665; -. DR STRING; 490899.DKAM_1270; -. DR EnsemblBacteria; ACL11596; ACL11596; DKAM_1270. DR KEGG; dka:DKAM_1270; -. DR eggNOG; arCOG00353; Archaea. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; FNNHAHV; -. DR OrthoDB; POG093Z07D6; -. DR Proteomes; UP000006903; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000006903}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000006903}. FT DOMAIN 179 350 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 351 AA; 40093 MW; 01759D81743C58E7 CRC64; MRVVVVVPRK YWVFLEEELG LVKTIYSDIV EVLKTKGSPS GTYLPREKIE FLRGSDFDKL IVMDRLKPIQ IVNLIKELRR DVIDRVMLIL EIFAEHAGSK EAKMQIELAR LKYYIPLVKE AIRYAKIGEL HGFLGAGRYG YEKYYLMLKK REARVRRELE ELRRIRGIRR MQRLKAGFPH VAIAGYTCAG KTTLFNAITG LSMLVGPEPF TTLSPKSRRI VYRDASFILT DTVGFIRDLP PEVIEAFYAT LEEITAADVI VNVVDASKPI ERIRIELETT REILSRIGVH SKPMVVALNK IDLVDDYASI ASEVKVLLAS NETLIPISSV KRINIDRLMD TVYMLVKGGY Q // ID B8DQ26_DESVM Unreviewed; 655 AA. AC B8DQ26; DT 03-MAR-2009, integrated into UniProtKB/TrEMBL. DT 03-MAR-2009, sequence version 1. DT 07-JUN-2017, entry version 63. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=DvMF_1947 {ECO:0000313|EMBL:ACL08890.1}; OS Desulfovibrio vulgaris (strain Miyazaki F / DSM 19637). OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfovibrionales; OC Desulfovibrionaceae; Desulfovibrio. OX NCBI_TaxID=883 {ECO:0000313|EMBL:ACL08890.1, ECO:0000313|Proteomes:UP000001361}; RN [1] {ECO:0000313|Proteomes:UP000001361} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Miyazaki F / DSM 19637 {ECO:0000313|Proteomes:UP000001361}; RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., RA Tice H., Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T., RA Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N., RA Mikhailova N., Hazen T.C., Richardson P.; RT "Complete sequence of Desulfovibrio vulgaris str. 'Miyazaki F'."; RL Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001197; ACL08890.1; -; Genomic_DNA. DR RefSeq; WP_012613065.1; NC_011769.1. DR ProteinModelPortal; B8DQ26; -. DR STRING; 883.DvMF_1947; -. DR EnsemblBacteria; ACL08890; ACL08890; DvMF_1947. DR KEGG; dvm:DvMF_1947; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; EREVIIT; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000001361; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000001361}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000001361}. FT DOMAIN 432 597 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 398 425 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 655 AA; 71701 MW; 44DC6CB5FAB9F415 CRC64; MTADDRAHHV SFRQRRSTPI AKVLGNTQGL KPSHVKALTR LYQRRFPSVG GYSHEQAREL AALSRSVGRQ VAVLIDRQGR VAMVLVGDTG AITIPELPRA RTGTGRLRGL RLLHTHLGPD LLSQEDLMDL LFLRLDGFGV LTVNEWGEPL TFQHAHLLPQ QEDGKPYRVQ PAQPWDRVDT DVVAQVEALE EEMARAASDA RAVAPARARG TAATAAGAVP QGRSHAEHIA HTAALAAEAE GPAAVLVSVS TAPRPLQELN LTELTELART AGVRCAGTLI QRVPSLNPKF ILGKGKLAEL EVLALQGNAT MIIFDGELSP AQLRNLADLT ERKVLDRTQL ILDIFAQHAT TRAGKLQVEM AQLKYTQPRL VGKNRAMDRL MGGIGGRGPG ETKLETDRRR IRDRIGRIKD ELESLRRQRA YARARRAKQR VPLASLVGYT NAGKSTLLNA LTNSAVLAEN KLFATLDPTT RRLRFPHERE LILADTVGFI RNLPKELLEA FRATLEELEA ADLLIHVADA GHPELDRQLG AVDTILTDME LHEVPRLLVL NKWDTLDEET REALRAVHPD AITLSAATRQ GLDELVASIA ARIDWERDLR PCGKRAGKGG GEGDGNECPA DDGNEGSYGA NPDEAGTDEA EAGYDWPEME SDRLN // ID B8DSV6_BIFA0 Unreviewed; 506 AA. AC B8DSV6; DT 03-MAR-2009, integrated into UniProtKB/TrEMBL. DT 03-MAR-2009, sequence version 1. DT 07-JUN-2017, entry version 61. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:ACL29085.1}; GN OrderedLocusNames=BLA_0793 {ECO:0000313|EMBL:ACL29085.1}; OS Bifidobacterium animalis subsp. lactis (strain AD011). OC Bacteria; Actinobacteria; Bifidobacteriales; Bifidobacteriaceae; OC Bifidobacterium. OX NCBI_TaxID=442563 {ECO:0000313|EMBL:ACL29085.1, ECO:0000313|Proteomes:UP000002456}; RN [1] {ECO:0000313|EMBL:ACL29085.1, ECO:0000313|Proteomes:UP000002456} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=AD011 {ECO:0000313|EMBL:ACL29085.1, RC ECO:0000313|Proteomes:UP000002456}; RX PubMed=19011029; DOI=10.1128/JB.01515-08; RA Kim J.F., Jeong H., Yu D.S., Choi S.-H., Hur C.-G., Park M.-S., RA Yoon S.H., Kim D.-W., Ji G.E., Park H.-S., Oh T.K.; RT "Genome sequence of the probiotic bacterium Bifidobacterium animalis RT subsp. lactis AD011."; RL J. Bacteriol. 191:678-679(2009). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001213; ACL29085.1; -; Genomic_DNA. DR RefSeq; WP_012619834.1; NC_011835.1. DR ProteinModelPortal; B8DSV6; -. DR EnsemblBacteria; ACL29085; ACL29085; BLA_0793. DR GeneID; 29695617; -. DR KEGG; bla:BLA_0793; -. DR PATRIC; fig|442563.4.peg.826; -. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR Proteomes; UP000002456; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000002456}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000002456}. FT DOMAIN 274 440 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 506 AA; 55591 MW; AC4367CA2D20EED4 CRC64; MGNPRYTEDS QTTDSQNVLD GQSQVLLDDD HAGWRGEDET WREREGRNEL KHVAGLGELE DVTEVEYRKV RLEKVVLVGV WSSRESTFAQ AEESLRELAA LAETAGAEVC DGVLQQRSRP DGTSYVGSGK AREIADIVAA NDADTIIVDA DLPPSQRRAL EDLTHVKVVD RTAVILDIFA QHATSREGKA QVELAQLQYM LPRLRGWGAA LSRQAGGRAA GADAGIGSRG PGETKIEMDR RVIRTRIARL RKQIKEMSGT REVKRGSRRR YGLPTIAVVG YTNAGKSSLT NRLTGSTELV ENALFATLDT AVRRTQTRDG RLYAYVDTVG FVRRLPTNLV EAFKSTLEEI ADADLIVHVV DASHPDPFSQ IDAVNEVLQT IDGVERLPVI TVFNKADLID DAKRERLHAL APDAHIVSSA TGEGVDALRA DVESMLVDPD VHVEALLPYT EGSLLAKVRE YGRLESLEYR DDGIMLQAFV DERLAARIMD VALHETDAPE HGEGGE // ID B8E283_DICTD Unreviewed; 405 AA. AC B8E283; DT 03-MAR-2009, integrated into UniProtKB/TrEMBL. DT 03-MAR-2009, sequence version 1. DT 07-JUN-2017, entry version 66. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Dtur_1081 {ECO:0000313|EMBL:ACK42360.1}; OS Dictyoglomus turgidum (strain Z-1310 / DSM 6724). OC Bacteria; Dictyoglomi; Dictyoglomales; Dictyoglomaceae; Dictyoglomus. OX NCBI_TaxID=515635 {ECO:0000313|EMBL:ACK42360.1, ECO:0000313|Proteomes:UP000007719}; RN [1] {ECO:0000313|EMBL:ACK42360.1, ECO:0000313|Proteomes:UP000007719} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Z-1310 / DSM 6724 {ECO:0000313|Proteomes:UP000007719}; RG US DOE Joint Genome Institute; RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., RA Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T., Detter J.C., RA Han C., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., RA Mead D.; RT "Complete sequence of Dictyoglomus turgidum DSM 6724."; RL Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001251; ACK42360.1; -; Genomic_DNA. DR RefSeq; WP_012583443.1; NC_011661.1. DR RefSeq; YP_002352974.1; NC_011661.1. DR ProteinModelPortal; B8E283; -. DR STRING; 515635.Dtur_1081; -. DR EnsemblBacteria; ACK42360; ACK42360; Dtur_1081. DR GeneID; 7083024; -. DR KEGG; dtu:Dtur_1081; -. DR PATRIC; fig|515635.4.peg.1117; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR InParanoid; B8E283; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000007719; Chromosome. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0043022; F:ribosome binding; IBA:GO_Central. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000007719}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000007719}. FT DOMAIN 186 353 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 154 181 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 405 AA; 46982 MW; F976F80587056D37 CRC64; MEIEKAILVA KISDLEELEE LKLLSKTAGV KVQNVLLFGG EPDPASFLRS GKLEELKYLV MEQRADLVIF NNDLSPVQLR NIEKEIPARI VDRTMLILDI FAQHARSKEG KIQVELAQLE YLLPRLTGRG ETLSRLGGGI GTRGPGETKL EIDRRKIRKR IHTLKKELEE IKREREVQRK QRLNLPQIAL VGYTNAGKST LFNLLTGANV RAEDLLFATL DPTVRKVNFK NNWEVLISDT VGFIRNLPEE LLTAFRATLE EIYYVDLILH VIDISDKDFR KQIEVVESIL EDMGIEDKTI IRVYNKIDLL SKEEVRYLKQ ELDYKPSVFI SAKEGIGIEK LKDLIVNELL KGVRRYKINI PYNKFNLFQK YRGKLYIEEE NYKENFVEIK ARVPKEYKKL LDELR // ID B8ELB9_METSB Unreviewed; 469 AA. AC B8ELB9; DT 03-MAR-2009, integrated into UniProtKB/TrEMBL. DT 03-MAR-2009, sequence version 1. DT 07-JUN-2017, entry version 55. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Msil_0536 {ECO:0000313|EMBL:ACK49508.1}; OS Methylocella silvestris (strain DSM 15510 / CIP 108128 / LMG 27833 / OS NCIMB 13906 / BL2). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Beijerinckiaceae; Methylocella. OX NCBI_TaxID=395965 {ECO:0000313|EMBL:ACK49508.1, ECO:0000313|Proteomes:UP000002257}; RN [1] {ECO:0000313|EMBL:ACK49508.1, ECO:0000313|Proteomes:UP000002257} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 15510 / CIP 108128 / LMG 27833 / NCIMB 13906 / BL2 RC {ECO:0000313|Proteomes:UP000002257}; RX PubMed=20472789; DOI=10.1128/JB.00506-10; RA Chen Y., Crombie A., Rahman M.T., Dedysh S.N., Liesack W., Stott M.B., RA Alam M., Theisen A.R., Murrell J.C., Dunfield P.F.; RT "Complete genome sequence of the aerobic facultative methanotroph RT Methylocella silvestris BL2."; RL J. Bacteriol. 192:3840-3841(2010). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001280; ACK49508.1; -; Genomic_DNA. DR RefSeq; WP_012589578.1; NC_011666.1. DR ProteinModelPortal; B8ELB9; -. DR STRING; 395965.Msil_0536; -. DR EnsemblBacteria; ACK49508; ACK49508; Msil_0536. DR KEGG; msl:Msil_0536; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000002257; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000002257}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000002257}. FT DOMAIN 224 400 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 469 AA; 51688 MW; 3303CD863B8D736C CRC64; MLDKRPGLED KSQGSDKMLT RALVVGPYLN EKSQSKKSSS AGFAARSTEA RMDEAAGLAA AIDLDIVGAM IVMLANVRPA TFIGKGKAQE IADLVQAENI DLVIMDCALS PIQQRNLEKA FSAKVIDRTG LILEIFGQRA RTSEGALQVE LAHLAYQKSR LVRSWTHLER QRGGFGFLGG PGETQIETDR RLIQERMTRI EQDLEKVKRT RGLHRKSRRD VPYPVVALVG YTNAGKSTLF NRMTHSDVFA ENMLFATLDP TLRAVSLGAG AKIILSDTVG FISDLPLMLV SAFRATLEEV LEADLILHVR DIAHEDADAQ RTDVETILRD LGVDPDDHRR ILEVWNKADL LDEAARDAAR NAAKRRAGRD GAEPVIVSAL TGQGLDELRA QIETRLAMDR LTFEIELQPE NGEGLHWLYE NAEVLRRSAG ADGTLHMKVR VGPERAESIR RRFIPMADGS AQVEAGSPS // ID B8F664_HAEPS Unreviewed; 408 AA. AC B8F664; DT 03-MAR-2009, integrated into UniProtKB/TrEMBL. DT 03-MAR-2009, sequence version 1. DT 05-JUL-2017, entry version 61. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:ACL32816.1}; GN OrderedLocusNames=HAPS_1213 {ECO:0000313|EMBL:ACL32816.1}; OS Haemophilus parasuis serovar 5 (strain SH0165). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=557723 {ECO:0000313|EMBL:ACL32816.1, ECO:0000313|Proteomes:UP000006743}; RN [1] {ECO:0000313|EMBL:ACL32816.1, ECO:0000313|Proteomes:UP000006743} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SH0165 {ECO:0000313|EMBL:ACL32816.1, RC ECO:0000313|Proteomes:UP000006743}; RX PubMed=19074396; DOI=10.1128/JB.01682-08; RA Yue M., Yang F., Yang J., Bei W., Cai X., Chen L., Dong J., Zhou R., RA Jin M., Jin Q., Chen H.; RT "Complete genome sequence of Haemophilus parasuis SH0165."; RL J. Bacteriol. 191:1359-1360(2009). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001321; ACL32816.1; -; Genomic_DNA. DR ProteinModelPortal; B8F664; -. DR STRING; 557723.HAPS_1213; -. DR EnsemblBacteria; ACL32816; ACL32816; HAPS_1213. DR KEGG; hap:HAPS_1213; -. DR PATRIC; fig|557723.8.peg.1204; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR Proteomes; UP000006743; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000006743}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000006743}. FT DOMAIN 172 339 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 408 AA; 46205 MW; FE061F1E276F4133 CRC64; MEFQTLAESA GVEVVATLTT TRSAPHIKYY VGQGKAQEIA DAIKDFDATV VLINHQLSPA QTRNLQSLCD CRVVDRTGLI LDIFAQRARS HEGKLQVELA QLRHLSTRLV RRLGNQDQQK GGAVGLRGPG ETQLETDRRL IKVRIQQLQN RLEKVSKQRD QNRKTRQKAD IPTISLVGYT NAGKSTLFNA ITDAGVYAAD QLFATLDPTL RRIQIQDVGT AILADTVGFI RFLPHDLVSA FKSTLQETTE ATLLLHVIDG ADDRKNENID AVNQVLDEIE ALEIPTLLVY NKVDRLDSIE PHIEYNDDGK PVAVYLSAQQ NQGIDLLFEA MRVRLKNELV CERVLLPTTS GQIYTKFYQQ QCIKSERFTE FGDRLVEIEV DKIQWQKWLK QYPELTEFVE FAQWEAES // ID B8FJV1_DESAA Unreviewed; 544 AA. AC B8FJV1; DT 03-MAR-2009, integrated into UniProtKB/TrEMBL. DT 03-MAR-2009, sequence version 1. DT 07-JUN-2017, entry version 61. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Dalk_0674 {ECO:0000313|EMBL:ACL02379.1}; OS Desulfatibacillum alkenivorans (strain AK-01). OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfobacterales; OC Desulfobacteraceae; Desulfatibacillum. OX NCBI_TaxID=439235 {ECO:0000313|EMBL:ACL02379.1, ECO:0000313|Proteomes:UP000000739}; RN [1] {ECO:0000313|EMBL:ACL02379.1, ECO:0000313|Proteomes:UP000000739} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=AK-01 {ECO:0000313|EMBL:ACL02379.1, RC ECO:0000313|Proteomes:UP000000739}; RG US DOE Joint Genome Institute; RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., RA Tice H., Bruce D., Goodwin L., Pitluck S., Chertkov O., Brettin T., RA Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N., RA Ovchinnikova G., Wawrik B., Richardson P.; RT "Complete sequence of Desulfatibacillum alkenivorans AK-01."; RL Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001322; ACL02379.1; -; Genomic_DNA. DR RefSeq; WP_012609818.1; NC_011768.1. DR ProteinModelPortal; B8FJV1; -. DR STRING; 439235.Dalk_0674; -. DR EnsemblBacteria; ACL02379; ACL02379; Dalk_0674. DR KEGG; dal:Dalk_0674; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; EREVIIT; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000000739; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000000739}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000000739}. FT DOMAIN 378 542 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 544 AA; 61035 MW; 07FD1B9A8AA20276 CRC64; MKKVYGYTKG LKTAQLKHLE KFYNRKVAPD LIVSQELALD MGRLSAEIRR QIGILVDRLG RIRFVMVGDG VQINIPSLHD YRAAMGRLNG LRLIHTHLKN EPLTDDDLTD LALLRLDLIT AVTLDETGAP HRFHAAHLIP SKPGETPYEV LPPMDPGSRD ISFRAFVREL EAELVRSSGV TKSQKQQASA FLVSVTNAPR REATDSMTEL KELCRTNDIF VAAEMIQYRT RMDARFLMGK GKIRELTIAA MQYGVDIVIF DQDLNPSQIQ AITNQVELPV IDRTQLILDI FAQRAMTSEG KLQVELAQLK YMLPRLLGRG TAMSRLMGGI GGRGPGETKL EVDRRRVRER ITRLEKSLKN VSKRRQTQKS ARERKGLPIV SIVGYTNAGK STLLNTLTQA EVLAESKLFA TLDPTSRRLR FPEDKEIIIT DTVGFIRDLP KDLVTAFAAT LEELKSADLL LHVIDASNPR MAEQVESVDK ILEDIGVSAI PTIRVLNKAD KVEPEEMERL CRSLEGMPIS ALDRPSLRPL TETIIERLFA ESSE // ID B8GNC8_THISH Unreviewed; 417 AA. AC B8GNC8; DT 03-MAR-2009, integrated into UniProtKB/TrEMBL. DT 03-MAR-2009, sequence version 1. DT 30-AUG-2017, entry version 58. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Tgr7_0898 {ECO:0000313|EMBL:ACL71989.1}; OS Thioalkalivibrio sulfidiphilus (strain HL-EbGR7). OC Bacteria; Proteobacteria; Gammaproteobacteria; Chromatiales; OC Ectothiorhodospiraceae; Thioalkalivibrio. OX NCBI_TaxID=396588 {ECO:0000313|EMBL:ACL71989.1, ECO:0000313|Proteomes:UP000002383}; RN [1] {ECO:0000313|EMBL:ACL71989.1, ECO:0000313|Proteomes:UP000002383} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=HL-EbGR7 {ECO:0000313|EMBL:ACL71989.1, RC ECO:0000313|Proteomes:UP000002383}; RX PubMed=21475584; RA Muyzer G., Sorokin D.Y., Mavromatis K., Lapidus A., Clum A., RA Ivanova N., Pati A., d'Haeseleer P., Woyke T., Kyrpides N.C.; RT "Complete genome sequence of 'Thioalkalivibrio sulfidophilus' HL- RT EbGr7."; RL Stand. Genomic Sci. 4:23-35(2011). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001339; ACL71989.1; -; Genomic_DNA. DR ProteinModelPortal; B8GNC8; -. DR STRING; 396588.Tgr7_0898; -. DR EnsemblBacteria; ACL71989; ACL71989; Tgr7_0898. DR KEGG; tgr:Tgr7_0898; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000002383; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000002383}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000002383}. FT DOMAIN 183 350 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 149 176 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 417 AA; 46686 MW; 8B88824B9F75D67F CRC64; MDLPDSPRDD DCSEFTELVN SAGAEPVALI TGPRQSPDPR LFVGSGKAEE IREQVEAQGA EVVIFDHELS PSQERNLERL FKCRVLDRTG LILDIFAQRA RSHEGKLQVE LAQLRHMSTR LVRGWTHLER QKGGIGLRGP GETQLETDRR LLAGRIKQIL RRLEKVEAQR EQGRQSRRRA EIPTVSLVGY TNAGKSTLFN RLTNAGVYAA DQLFATLDPT LRRVDLPDQQ AIILADTVGF VRQLPHDLVA AFKATLTETR EASLLLHVVD AADPRREDNI QQVNNVLEEI GAAEVPRILV YNKIDALPEV QPQLVEAAHG EPARVYLSAR TGEGVELLMD WLAKRFAESL VQGWISLPPS AGRERAGLYR MQAVLGEEVQ PDGGLRLHIR LPRRRFDELF RDSGFIPELQ ADARQVA // ID B8HG95_PSECP Unreviewed; 553 AA. AC B8HG95; DT 03-MAR-2009, integrated into UniProtKB/TrEMBL. DT 03-MAR-2009, sequence version 1. DT 30-AUG-2017, entry version 72. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Achl_1468 {ECO:0000313|EMBL:ACL39457.1}; OS Pseudarthrobacter chlorophenolicus (strain ATCC 700700 / DSM 12829 / OS CIP 107037 / JCM 12360 / KCTC 9906 / NCIMB 13794 / A6) (Arthrobacter OS chlorophenolicus). OC Bacteria; Actinobacteria; Micrococcales; Micrococcaceae; OC Pseudarthrobacter. OX NCBI_TaxID=452863 {ECO:0000313|EMBL:ACL39457.1, ECO:0000313|Proteomes:UP000002505}; RN [1] {ECO:0000313|EMBL:ACL39457.1, ECO:0000313|Proteomes:UP000002505} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700700 / DSM 12829 / CIP 107037 / JCM 12360 / KCTC 9906 / RC NCIMB 13794 / A6 {ECO:0000313|Proteomes:UP000002505}; RG US DOE Joint Genome Institute; RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., RA Bruce D., Goodwin L., Pitluck S., Goltsman E., Clum A., Larimer F., RA Land M., Hauser L., Kyrpides N., Mikhailova N., Jansson J., RA Richardson P.; RT "Complete sequence of chromosome of Arthrobacter chlorophenolicus RT A6."; RL Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001341; ACL39457.1; -; Genomic_DNA. DR ProteinModelPortal; B8HG95; -. DR STRING; 452863.Achl_1468; -. DR EnsemblBacteria; ACL39457; ACL39457; Achl_1468. DR KEGG; ach:Achl_1468; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000002505; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000002505}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000002505}. FT DOMAIN 332 497 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 553 AA; 59629 MW; 73A6341423AB4063 CRC64; MTAAPQPSAN TSPHSTERHY SGNAETSKET MTSQPNTGSD PAAQDMSPAE IQAVIDRILA KDVPAGSRTS EGAGDAKAVL GKAQAISHLD AEHSEYDGDQ QDLEERRALR RTAGLSTELE DVTEVEYRQL RLERVVLAGL WSEGTLADAE NSLRELAALA ETAGSEVLDG LVQRRAKPDP GTFLGSGKAQ ELKDIVMSTG ADTVVVDAEL APSQRRGLED IVKVKVIDRT GLILDIFAQH AKSREGKAQV ELAQLEYLLP RLRGWGESMS RQAGGQVGGA AAGMGSRGPG ETKIELDRRR IRTRMAKLRR EIAAMKPARE TKRANRRRNE VPSVAIAGYT NAGKSSLLNR LTDAGVLVEN ALFATLDPTI RKAETSDGLG YTLADTVGFV RSLPTQLVEA FRSTLEEVAD SDLILHVVDA SHPDPEGQIA AVRKVFGEVD ARKIPEIIVL NKADAADPFV VERLKQREPR HVVVSARTGE GIAELLKTIS DSIPRPGVQL ELLIPYNRGD LISKLHDSDA EIISMDHVEA GTRAVVKVRE GLAAELESFA VNA // ID B8HNY1_CYAP4 Unreviewed; 553 AA. AC B8HNY1; DT 03-MAR-2009, integrated into UniProtKB/TrEMBL. DT 03-MAR-2009, sequence version 1. DT 07-JUN-2017, entry version 56. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Cyan7425_3241 {ECO:0000313|EMBL:ACL45568.1}; OS Cyanothece sp. (strain PCC 7425 / ATCC 29141). OC Bacteria; Cyanobacteria; Oscillatoriophycideae; Oscillatoriales; OC Cyanothecaceae; Cyanothece. OX NCBI_TaxID=395961 {ECO:0000313|EMBL:ACL45568.1, ECO:0000313|Proteomes:UP000002511}; RN [1] {ECO:0000313|Proteomes:UP000002511} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=PCC 7425 / ATCC 29141 {ECO:0000313|Proteomes:UP000002511}; RX PubMed=21972240; DOI=10.1128/mBio.00214-11; RA Bandyopadhyay A., Elvitigala T., Welsh E., Stockel J., Liberton M., RA Min H., Sherman L.A., Pakrasi H.B.; RT "Novel metabolic attributes of the genus Cyanothece, comprising a RT group of unicellular nitrogen-fixing Cyanobacteria."; RL MBio 2:E214-E214(2011). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001344; ACL45568.1; -; Genomic_DNA. DR RefSeq; WP_012628631.1; NC_011884.1. DR ProteinModelPortal; B8HNY1; -. DR STRING; 395961.Cyan7425_3241; -. DR EnsemblBacteria; ACL45568; ACL45568; Cyan7425_3241. DR KEGG; cyn:Cyan7425_3241; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; WESHITS; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000002511; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000002511}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000002511}. FT DOMAIN 386 553 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 345 382 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 553 AA; 62189 MW; 24A614917C0E11ED CRC64; MAISYDNIQG LKSSQIRQLE QLREQQQPGH LITLDFAQQL VSLSQTIHQP ICCYINRRGQ VVRIGVGTPG QIQLADTDLP RRSGHRLSGI RCVVAQTHAI DPTALMAMLR QRLDALVVLI YPERKGHRDS LSTTSLQTWL AHIVPDREQP WLVEPFQLQD LAEQDADELI HAWERELQAS GWDLTQWQER GAGDRVLLVG LQTDELSDQG FADSLVELER LVESAAGQVV GQVQQKRSQP HPQTVVGQGK VEEIALAAQR EGANLIVFNQ DISAAQVRNL EEQTGLRVVD RTEVILDIFA QRARSQAGKL QVELAQLEYL LPRLRGRGQS MSRLGAGIGT RGPGETKLET ERRTLQRRVT QLQREVNQLQ AHRARLRHQR ERQDIPLVTL VGYTNAGKST LLNVLTQAEV YTADQLFATL DPTTRRLSLA DPDHQSRRDL LLTDTVGFIH HLPPALMDAF RATLEEVSEA DALLHVVDLS HPAWERHIHS VAEMLAELPT VPPRQLLVFN KLDQVDSETL QQAQQSYPDA VFISATARLG LETLRCRLLQ WLS // ID B8I4L2_CLOCE Unreviewed; 596 AA. AC B8I4L2; DT 03-MAR-2009, integrated into UniProtKB/TrEMBL. DT 03-MAR-2009, sequence version 1. DT 07-JUN-2017, entry version 66. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Ccel_0178 {ECO:0000313|EMBL:ACL74566.1}; OS Clostridium cellulolyticum (strain ATCC 35319 / DSM 5812 / JCM 6584 / OS H10). OC Bacteria; Firmicutes; Clostridia; Clostridiales; Ruminococcaceae; OC Ruminiclostridium. OX NCBI_TaxID=394503 {ECO:0000313|EMBL:ACL74566.1, ECO:0000313|Proteomes:UP000001349}; RN [1] {ECO:0000313|EMBL:ACL74566.1, ECO:0000313|Proteomes:UP000001349} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 35319 / DSM 5812 / JCM 6584 / H10 RC {ECO:0000313|Proteomes:UP000001349}; RG US DOE Joint Genome Institute; RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., RA Tice H., Bruce D., Goodwin L., Pitluck S., Chertkov O., Saunders E., RA Brettin T., Detter J.C., Han C., Larimer F., Land M., Hauser L., RA Kyrpides N., Ivanova N., Zhou J., Richardson P.; RT "Complete sequence of Clostridium cellulolyticum H10."; RL Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001348; ACL74566.1; -; Genomic_DNA. DR ProteinModelPortal; B8I4L2; -. DR STRING; 394503.Ccel_0178; -. DR EnsemblBacteria; ACL74566; ACL74566; Ccel_0178. DR KEGG; cce:Ccel_0178; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000001349; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000001349}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000001349}. FT DOMAIN 378 543 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 337 371 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 596 AA; 66661 MW; 478435394EC422CA CRC64; MKVNGNIQSI KDKVLQELED LYDKKYGSRD LVPEELALTI TRISAEINRE ISVLLNRRGV VVDISIGDSG TVTLPQVDGR RGTARLSAIR CIHTHPNGSG MLSQVDASTL QKLRLDAMIA VGITDGQPSD IYAGCLNHEE GVDIYGPFEI RDTRLNYIYR IIEELDASAK NEIYENEEEA ETAILVSLET SQSRLENITS RDAQESLEEL EELAKTAGAV VVDKVLQKKQ TEDSAYYIGK GKIEELSLMC QARDVQLLIF DDELSGAQIR NIEEMTKVRV IDRTTLILDI FAQRAVSKEG KLQVELAQLK YKLPRLVGMG TELSRLGGGI GTRGPGEKKL EVDRRHIRRR ITGLEQELKH LEKRRQFLRS NRTSNNTPVV AIVGYTNAGK STLLNRFCGS SVFVEDKLFA TLDPSARQLT LSDGREAVLI DTVGFIRKLP HDLIEAFKST LEEAVHADML LHVVDASNEN VSMQISVVEK LLEELGASTK RTILVLNKQD LVQEDRRISS VGYSAVCEIS AVTGYGIEQL LEKITEGFMH QLKEVQLLVP YNDGWVMPYI YKNGRIIDQE YEEGGIKVKA LVKVEKVSRL TDFMVV // ID B8IDE8_METNO Unreviewed; 471 AA. AC B8IDE8; DT 03-MAR-2009, integrated into UniProtKB/TrEMBL. DT 03-MAR-2009, sequence version 1. DT 07-JUN-2017, entry version 59. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Mnod_6545 {ECO:0000313|EMBL:ACL61314.1}; OS Methylobacterium nodulans (strain LMG 21967 / CNCM I-2342 / ORS 2060). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Methylobacteriaceae; Methylobacterium. OX NCBI_TaxID=460265 {ECO:0000313|EMBL:ACL61314.1, ECO:0000313|Proteomes:UP000008207}; RN [1] {ECO:0000313|EMBL:ACL61314.1, ECO:0000313|Proteomes:UP000008207} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=LMG 21967 / CNCM I-2342 / ORS 2060 RC {ECO:0000313|Proteomes:UP000008207}; RG US DOE Joint Genome Institute; RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., RA Tice H., Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T., RA Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N., RA Ivanova N., Marx C.J., Richardson P.; RT "Complete sequence of chromosome of Methylobacterium nodulans ORS RT 2060."; RL Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001349; ACL61314.1; -; Genomic_DNA. DR RefSeq; WP_015932886.1; NC_011894.1. DR ProteinModelPortal; B8IDE8; -. DR STRING; 460265.Mnod_6545; -. DR EnsemblBacteria; ACL61314; ACL61314; Mnod_6545. DR KEGG; mno:Mnod_6545; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000008207; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000008207}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000008207}. FT DOMAIN 232 403 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 471 AA; 52005 MW; 795B484A085DEDCC CRC64; MEPRIPGDAR LPGEARLQRM AEPEGTIAAE TRTLVVGPYP ARRGAEAARP GAGRPPEARL DEAVGLAAAI DLDVVDHLML PVQAIRPSTY LGKGRVEEIA GRIAAESVRL VVMDCALSPV QQRNLEKAWG VKVIDRTGLI LEIFGRRAST REGALQVEHA HLAYQRSRLV RSWTHLERQR GGFGFLGGPG ETQIEADRRL IQERMTRIER ELETVTRTRG LHRQSRRRVP YPVVALVGYT NAGKSTLFNR LTAAEVRAED LLFATLDPTA RAIKLPHGET AILSDTVGFI SDLPTMLIAA FRATLEDVIE ADFLLHVRDM AHEDTQAQGQ DVQAVLAELG IAPETDRIIE VWNKADLLDA PERERLLNLS RQAGAKPVLI SALTGEGTDR LLARIEARIA ESRASFALVL EPTEGAGLHW LYENAEVLDR REDAGGQLHL VVRIAPEKEP RLLNRFGTAR RLRTGGDAIR R // ID B8IZ59_DESDA Unreviewed; 561 AA. AC B8IZ59; DT 03-MAR-2009, integrated into UniProtKB/TrEMBL. DT 03-MAR-2009, sequence version 1. DT 05-JUL-2017, entry version 57. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Ddes_0879 {ECO:0000313|EMBL:ACL48786.1}; OS Desulfovibrio desulfuricans (strain ATCC 27774 / DSM 6949). OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfovibrionales; OC Desulfovibrionaceae; Desulfovibrio. OX NCBI_TaxID=525146 {ECO:0000313|EMBL:ACL48786.1, ECO:0000313|Proteomes:UP000002598}; RN [1] {ECO:0000313|EMBL:ACL48786.1, ECO:0000313|Proteomes:UP000002598} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 27774 / DSM 6949 {ECO:0000313|Proteomes:UP000002598}; RG US DOE Joint Genome Institute; RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., RA Bruce D., Goodwin L., Pitluck S., Sims D., Lu M., Kiss H., Meineke L., RA Brettin T., Detter J.C., Han C., Larimer F., Land M., Hauser L., RA Kyrpides N., Ovchinnikova G., Hazen T.C.; RT "Complete sequence of Desulfovibrio desulfuricans subsp. desulfuricans RT str. ATCC 27774."; RL Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001358; ACL48786.1; -; Genomic_DNA. DR ProteinModelPortal; B8IZ59; -. DR STRING; 525146.Ddes_0879; -. DR EnsemblBacteria; ACL48786; ACL48786; Ddes_0879. DR KEGG; dds:Ddes_0879; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; EREVIIT; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000002598; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000002598}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000002598}. FT DOMAIN 384 549 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 350 377 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 561 AA; 62731 MW; B8B66B9F71F34B0B CRC64; MRQEHDISKP EGNLQGLKPS QLAALNRLFN RRFPAEDVYT VEQARELALL SRALGRQIGL LIDRKGRVQT VIVGKAGSIL IPELPRGRSG GERLRGLRLL HTHLTPDGLS QEDLMDMLFL RLDAVIVLTV NPVGEPVQWQ AAHLLPTNVN GQGYHLELPR PWDRTAAQMV GTAEALEKDL SRRAESSHEA ENRPRALLIS VAALPRIMQE RNLDELAELA RTAGLAIAGR MVQRVPQVNP RLIMGRGKVA ELEVLTLQGR ADTLVFDGEL SPAQLHNLAD ITERKVIDRT QLILDIFAQH AVSRAGKLQV ELAQLRYTQP RLVGKNRAMD RLMGGIGGRG PGETKLETDR RKIRERMARI RKDLERLRRQ RAFTRDRRSR QGIPLAALVG YTNAGKSTLL NTLTRSEVLV ENKLFATLDP TTRRLRFPAE KELILADTVG FIRNLPKELM DAFRATLEEL EAAHLLLHVA DASHPDLLQQ ISAVETILAE MELDRMPRLL ILNKWDQLEA PARAELADAF PHALPVAAKT GEGCKPLLEQ LEMRLLHQAT NIVTEISPSL N // ID B8KW65_9GAMM Unreviewed; 416 AA. AC B8KW65; DT 03-MAR-2009, integrated into UniProtKB/TrEMBL. DT 03-MAR-2009, sequence version 1. DT 30-AUG-2017, entry version 45. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:EED36633.1}; GN ORFNames=NOR51B_2585 {ECO:0000313|EMBL:EED36633.1}; OS Luminiphilus syltensis NOR5-1B. OC Bacteria; Proteobacteria; Gammaproteobacteria; Cellvibrionales; OC Halieaceae; Luminiphilus. OX NCBI_TaxID=565045 {ECO:0000313|EMBL:EED36633.1, ECO:0000313|Proteomes:UP000004699}; RN [1] {ECO:0000313|Proteomes:UP000004699} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NOR51-B {ECO:0000313|Proteomes:UP000004699}; RX PubMed=23705883; RA Spring S., Riedel T., Sproer C., Yan S., Harder J., Fuchs B.M.; RT "Taxonomy and evolution of bacteriochlorophyll a-containing members of RT the OM60/NOR5 clade of marine gammaproteobacteria: description of RT Luminiphilus syltensis gen. nov., sp. nov., reclassification of Haliea RT rubra as Pseudohaliea rubra gen. nov., comb. nov., and emendation of RT Chromatocurvus halotolerans."; RL BMC Microbiol. 13:118-118(2013). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; DS999411; EED36633.1; -; Genomic_DNA. DR RefSeq; WP_009021376.1; NZ_DS999411.1. DR ProteinModelPortal; B8KW65; -. DR STRING; 565045.NOR51B_2585; -. DR EnsemblBacteria; EED36633; EED36633; NOR51B_2585. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000004699; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000004699}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000004699}. FT DOMAIN 199 365 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 165 192 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 416 AA; 46732 MW; 18E424D599FBBD15 CRC64; MFFERHESGE RAILVQLSLD DGAPAQDPRE FEELVVSAGG EPVAFISGHR RAPTSKTFVG SGKLDEIREA KEAFEAELVV FNHPLSPSQE RNLEQELCCR VIARTGLILD IFAQRARTHE GKLQVELAQL RHMSTRLIRG WTHLERQKGG IGLRGPGETQ LETDRRLLRA RIRTIEQRLE RVRSQRAQSR RSRQRAEIPL VSLVGYTNAG KSSLFNRVTE AAVYAADKLF ATLDPTLRGI EIDHLGKVVL ADTVGFIAHL PHTLVEAFKA TLEETLNATL LLHVIDIVAE DRDYLVDEVE SVLAEIGAGD IPQLRVYNKL DLAQQSPRIL RNEQGVIEAV YLSARTGAGI DLLELALSER LQDQVFQDEI TLAPSEGRLR AALYDVGAVE RESWDSNGDN RLRIRLPLKD WERLKN // ID B9CKH3_9ACTN Unreviewed; 429 AA. AC B9CKH3; DT 24-MAR-2009, integrated into UniProtKB/TrEMBL. DT 24-MAR-2009, sequence version 1. DT 07-JUN-2017, entry version 41. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:EEE18039.1}; GN ORFNames=ATORI0001_0521 {ECO:0000313|EMBL:EEE18039.1}; OS Atopobium rimae ATCC 49626. OC Bacteria; Actinobacteria; Coriobacteriia; Coriobacteriales; OC Atopobiaceae; Atopobium. OX NCBI_TaxID=553184 {ECO:0000313|EMBL:EEE18039.1, ECO:0000313|Proteomes:UP000004070}; RN [1] {ECO:0000313|EMBL:EEE18039.1, ECO:0000313|Proteomes:UP000004070} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 49626 {ECO:0000313|EMBL:EEE18039.1, RC ECO:0000313|Proteomes:UP000004070}; RA Madupu R., Sebastian Y., Durkin A.S., Torralba M., Methe B., RA Sutton G.G., Strausberg R.L., Nelson K.E.; RL Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EEE18039.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACFE01000001; EEE18039.1; -; Genomic_DNA. DR RefSeq; WP_003148624.1; NZ_ACFE01000001.1. DR ProteinModelPortal; B9CKH3; -. DR STRING; 553184.ATORI0001_0521; -. DR EnsemblBacteria; EEE18039; EEE18039; ATORI0001_0521. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000004070; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000004070}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000004070}. FT DOMAIN 210 375 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 176 203 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 429 AA; 48040 MW; 1C5F4C7225511CD7 CRC64; MSRFKPFDTE PVPERALLVG VEYGRREWSL EDSMAELARL AETDGAEVVA TLTQRLDTPV SKTFIGKGKA EELVSFVRNL NVDVVIFDDE LSPSQQSNLE KIVGSPTKII DRTALILDIF GTHAKTREGR LQVQLAQLQY VLPRLRGMWS HLVGEQTRGG IGSRFGQGES QLEIDRRLIR DKISMLQHEL RNLEKRREVQ SKLRWDSGIF SVSLAGYTNA GKSTLLNQLT NASVYAKDEL FATLDPTTRT ITLEEGRKIT LTDTVGFIQK LPTTLIESFK STLAEAQAAD LILLVVDASD KNFDKEIEVV TSILNDIKVS AHKKLLVFNK IDLLDTNNLA KMRTLYPDAV FISAQKAMGL RGLLYTIAHI AGEDDKTLHV CIPFDQGFLI HMVHERCQII RTCYQASGLQ MTVRADKQMQ ATLSPFTCS // ID B9DPA4_STACT Unreviewed; 420 AA. AC B9DPA4; DT 24-MAR-2009, integrated into UniProtKB/TrEMBL. DT 24-MAR-2009, sequence version 1. DT 07-JUN-2017, entry version 61. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Sca_0955 {ECO:0000313|EMBL:CAL27863.1}; OS Staphylococcus carnosus (strain TM300). OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae; OC Staphylococcus. OX NCBI_TaxID=396513 {ECO:0000313|EMBL:CAL27863.1, ECO:0000313|Proteomes:UP000000444}; RN [1] {ECO:0000313|EMBL:CAL27863.1, ECO:0000313|Proteomes:UP000000444} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=TM300 {ECO:0000313|EMBL:CAL27863.1, RC ECO:0000313|Proteomes:UP000000444}; RX PubMed=19060169; DOI=10.1128/AEM.01982-08; RA Rosenstein R., Nerz C., Biswas L., Resch A., Raddatz G., RA Schuster S.C., Goetz F.; RT "Genome analysis of the meat starter culture bacterium Staphylococcus RT carnosus TM300."; RL Appl. Environ. Microbiol. 75:811-822(2009). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AM295250; CAL27863.1; -; Genomic_DNA. DR RefSeq; WP_015900204.1; NC_012121.1. DR ProteinModelPortal; B9DPA4; -. DR STRING; 396513.Sca_0955; -. DR KEGG; sca:SCA_0955; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR Proteomes; UP000000444; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000000444}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000000444}. FT DOMAIN 206 367 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 420 AA; 48217 MW; 271936C21410D7F4 CRC64; MPQEKIYNTE ETVEKALLVG VDAYDEQDYD FASTMEELKA LSESCRLDVI GEITQSKDRI EEKTYVGKGK QYEIKEFVDM YDVDVVVVND ELTTSQSKSL NDTLGVKIID RTQLILEIFA MRASSKEGKL QVELAQLDYL MPRLQGHGKS LSRLGGGIGT RGPGETKLET DRRHIRRRMN EIKHQLKATV EHRERYRSKR RQNQVFQVAL VGYTNAGKST WFNILADEST YEKDLLFATL DPKTRQIQIN DGFNLIISDT VGFIQKLPTT LIAAFKSTLE EARDADLLLH VVDASNEDYR TQFDTVNRII GDLDMDKIPQ AVIFNKKDMH EGPAPASQLP NVFVSAKNEE DRERVRALLI EQVEKQMEPY TEKVPADDAD RLYFLKRHTI INQLDFNEED ESYTVEGYRQ KTNDEGKKQD // ID B9DUP7_STRU0 Unreviewed; 412 AA. AC B9DUP7; DT 24-MAR-2009, integrated into UniProtKB/TrEMBL. DT 24-MAR-2009, sequence version 1. DT 07-JUN-2017, entry version 65. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=SUB1133 {ECO:0000313|EMBL:CAR42505.1}; OS Streptococcus uberis (strain ATCC BAA-854 / 0140J). OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=218495 {ECO:0000313|EMBL:CAR42505.1, ECO:0000313|Proteomes:UP000000449}; RN [1] {ECO:0000313|Proteomes:UP000000449} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-854 / 0140J {ECO:0000313|Proteomes:UP000000449}; RX PubMed=19175920; DOI=10.1186/1471-2164-10-54; RA Ward P.N., Holden M.T.G., Leigh J.A., Lennard N., Bignell A., RA Barron A., Clark L., Quail M.A., Woodward J., Barrell B.G., Egan S.A., RA Field T.R., Maskell D., Kehoe M., Dowson C.G., Chanter N., RA Whatmore A.M., Bentley S.D., Parkhill J.; RT "Evidence for niche adaptation in the genome of the bovine pathogen RT Streptococcus uberis."; RL BMC Genomics 10:54-54(2009). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AM946015; CAR42505.1; -; Genomic_DNA. DR ProteinModelPortal; B9DUP7; -. DR STRING; 218495.SUB1133; -. DR EnsemblBacteria; CAR42505; CAR42505; SUB1133. DR KEGG; sub:SUB1133; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000000449; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000000449}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000000449}. FT DOMAIN 199 359 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 165 192 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 412 AA; 46900 MW; BAE2B0C7EDD6F249 CRC64; MTETNVKQER VILLGVALQK TENVDMSMEE LASLAKTAGA EVVGSYTQKR EKYDSKTFIG SGKLEELKAM VEAEEVDTVI VNNRLTPRQN SNLEAALEVK VIDRMQLILD IFAMRARSHE GKLQVHLAQL KYMLPRLVGQ GIMLSRQAGG IGSRGPGESQ LELNRRSIRH QISDIERQLA LVEKNRQTIR DKRIASDTFK IGLIGYTNAG KSTIMNVLTD DKQYEANELF ATLDATTKQI YLQNQFQATL TDTVGFIQDL PTELVAAFKS TLEESRHVDL LLHVIDASDP NHSEHEKVVL DILKDLEMLD IPRLAIYNKM DQTNHLTATA FPNVRLSAKE KGSRNLLRRI IVDQIRDILE PFSINVHQDK AYKLFDLNKV ALLEPYDFEE EYEMISGYIA PKNRWRLEEL YD // ID B9EBJ3_MACCJ Unreviewed; 425 AA. AC B9EBJ3; DT 24-MAR-2009, integrated into UniProtKB/TrEMBL. DT 24-MAR-2009, sequence version 1. DT 07-JUN-2017, entry version 58. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=MCCL_0897 {ECO:0000313|EMBL:BAH17604.1}; OS Macrococcus caseolyticus (strain JCSC5402). OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae; OC Macrococcus. OX NCBI_TaxID=458233 {ECO:0000313|EMBL:BAH17604.1, ECO:0000313|Proteomes:UP000001383}; RN [1] {ECO:0000313|EMBL:BAH17604.1, ECO:0000313|Proteomes:UP000001383} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=JCSC5402 {ECO:0000313|EMBL:BAH17604.1, RC ECO:0000313|Proteomes:UP000001383}; RX PubMed=19074389; DOI=10.1128/JB.01058-08; RA Baba T., Kuwahara-Arai K., Uchiyama I., Takeuchi F., Ito T., RA Hiramatsu K.; RT "Complete genome sequence of Macrococcus caseolyticus strain RT JCSCS5402, reflecting the ancestral genome of the human-pathogenic RT staphylococci."; RL J. Bacteriol. 191:1180-1190(2009). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AP009484; BAH17604.1; -; Genomic_DNA. DR RefSeq; WP_012656804.1; NC_011999.1. DR ProteinModelPortal; B9EBJ3; -. DR STRING; 458233.MCCL_0897; -. DR EnsemblBacteria; BAH17604; BAH17604; MCCL_0897. DR KEGG; mcl:MCCL_0897; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000001383; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000001383}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000001383}. FT DOMAIN 203 364 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 425 AA; 48843 MW; 42279663E16BDFC8 CRC64; MKDTQKATER ALIIAVHLKK NDDFNFGESL EEIKSLCHTA GIEVTEVVIQ NKDRVDNSYY IGKGKLEEIV ELKEREDIAF DMVVVNNELT TSQSKHLNEV LDCKIIDRTQ LILDIFAQRA KSREGKLQVE LAQLEYLLPR LSGHGLSLSR LGGGIGTRGP GETKLEMNRR HIRSRIHDIK LQLETIKQHR QRYRENRKKR NIFQVALVGY TNAGKSTWFN ALSDSDTYME DLLFATLDPK SKMMKLHEGY PVLLSDTVGF IQQLPTHLIE AFSSTLEEAK YADILIHVVD RSHPNYMNHI DTVIALLKEL DMDTIPVLTL LNKKDKLESF VTAAGKDELL VSVFDKQDKI HIQNKLIDMM QRNMSKYAIE VDKDAGQIIA FLKEHTLVSA INFNEDKDKY EIYGYEHRHE GILNKLLSNE QIKRL // ID B9GRJ2_POPTR Unreviewed; 539 AA. AC B9GRJ2; DT 24-MAR-2009, integrated into UniProtKB/TrEMBL. DT 11-DEC-2013, sequence version 2. DT 30-AUG-2017, entry version 49. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EEE80016.2}; GN ORFNames=POPTR_0002s03250g {ECO:0000313|EMBL:EEE80016.2}; OS Populus trichocarpa (Western balsam poplar) (Populus balsamifera OS subsp. trichocarpa). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae; OC Pentapetalae; rosids; fabids; Malpighiales; Salicaceae; Saliceae; OC Populus. OX NCBI_TaxID=3694 {ECO:0000313|EMBL:EEE80016.2, ECO:0000313|Proteomes:UP000006729}; RN [1] {ECO:0000313|EMBL:EEE80016.2, ECO:0000313|Proteomes:UP000006729} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Nisqually {ECO:0000313|Proteomes:UP000006729}; RX PubMed=16973872; DOI=10.1126/science.1128691; RA Tuskan G.A., Difazio S., Jansson S., Bohlmann J., Grigoriev I., RA Hellsten U., Putnam N., Ralph S., Rombauts S., Salamov A., Schein J., RA Sterck L., Aerts A., Bhalerao R.R., Bhalerao R.P., Blaudez D., RA Boerjan W., Brun A., Brunner A., Busov V., Campbell M., Carlson J., RA Chalot M., Chapman J., Chen G.-L., Cooper D., Coutinho P.M., RA Couturier J., Covert S., Cronk Q., Cunningham R., Davis J., RA Degroeve S., Dejardin A., dePamphilis C.W., Detter J., Dirks B., RA Dubchak I., Duplessis S., Ehlting J., Ellis B., Gendler K., RA Goodstein D., Gribskov M., Grimwood J., Groover A., Gunter L., RA Hamberger B., Heinze B., Helariutta Y., Henrissat B., Holligan D., RA Holt R., Huang W., Islam-Faridi N., Jones S., Jones-Rhoades M., RA Jorgensen R., Joshi C., Kangasjaervi J., Karlsson J., Kelleher C., RA Kirkpatrick R., Kirst M., Kohler A., Kalluri U., Larimer F., RA Leebens-Mack J., Leple J.-C., Locascio P., Lou Y., Lucas S., RA Martin F., Montanini B., Napoli C., Nelson D.R., Nelson C., RA Nieminen K., Nilsson O., Pereda V., Peter G., Philippe R., Pilate G., RA Poliakov A., Razumovskaya J., Richardson P., Rinaldi C., Ritland K., RA Rouze P., Ryaboy D., Schmutz J., Schrader J., Segerman B., Shin H., RA Siddiqui A., Sterky F., Terry A., Tsai C.-J., Uberbacher E., RA Unneberg P., Vahala J., Wall K., Wessler S., Yang G., Yin T., RA Douglas C., Marra M., Sandberg G., Van de Peer Y., Rokhsar D.S.; RT "The genome of black cottonwood, Populus trichocarpa (Torr. & Gray)."; RL Science 313:1596-1604(2006). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CM000338; EEE80016.2; -; Genomic_DNA. DR RefSeq; XP_002300743.2; XM_002300707.2. DR STRING; 3694.POPTR_0002s03250.1; -. DR EnsemblPlants; POPTR_0002s03250.1; POPTR_0002s03250.1; POPTR_0002s03250. DR GeneID; 7471934; -. DR Gramene; POPTR_0002s03250.1; POPTR_0002s03250.1; POPTR_0002s03250. DR KEGG; pop:POPTR_0002s03250g; -. DR eggNOG; KOG0410; Eukaryota. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR InParanoid; B9GRJ2; -. DR KO; K03665; -. DR OMA; VILEIFH; -. DR OrthoDB; EOG093609UJ; -. DR Proteomes; UP000006729; Linkage group LGII. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR GO; GO:0043022; F:ribosome binding; IBA:GO_Central. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 2. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000006729}; KW Reference proteome {ECO:0000313|Proteomes:UP000006729}. FT DOMAIN 316 482 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 539 AA; 60146 MW; 6F4BBD72036FC483 CRC64; MIVSHCSLTR PWHPSTHEPY FPNLKKPKFP LIFTSSITYS LKLTAHVLPQ GTEVVSPDNV LVQNPVIETI EAKEEEVHGV FNGVASTKSE DKTPVKKKKK EEEDSFENRF QLRNGREVYE EKAYLVGVER KGNTVDAFGI EESLEELGQL ADTAGVAVVG STCQKLASPN PRTYIGSGKV AEIKSAIHGL GAETVIFDDE LSPGQLRNLE KIFGGDVRVC DRTALILDIF NQRAATHEAS LQVALAQMEY QLPRLTRMWS HLERQAGGRV KGMGEKQIEV DKRILRTQIG VLKKELESVR KHRKQYRNRR TSVPVPVVSL VGYTNAGKST LLNQLTGADV LAEDRLFATL DPTTRRVQIK NGNEFLLTDT VGFIQKLPTT LVAAFRATLE EISESSLLVH VVDISHPLVE QQVHAVDEVL SELDVSSIPR LMVWNKVDRV SDPKKLKLEA ERKQDVVCVS ALNGDGLEEF CNAVQEKMKD SMVWVEALVP FDKGELLSTI HQVGMVERTE YTESGTLIKA HVPLRFARLL TPMRQLCAS // ID B9HFU2_POPTR Unreviewed; 511 AA. AC B9HFU2; DT 24-MAR-2009, integrated into UniProtKB/TrEMBL. DT 11-DEC-2013, sequence version 2. DT 07-JUN-2017, entry version 54. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EEE91329.2}; DE Flags: Fragment; GN ORFNames=POPTR_0007s14660g {ECO:0000313|EMBL:EEE91329.2}; OS Populus trichocarpa (Western balsam poplar) (Populus balsamifera OS subsp. trichocarpa). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae; OC Pentapetalae; rosids; fabids; Malpighiales; Salicaceae; Saliceae; OC Populus. OX NCBI_TaxID=3694 {ECO:0000313|EMBL:EEE91329.2, ECO:0000313|Proteomes:UP000006729}; RN [1] {ECO:0000313|EMBL:EEE91329.2, ECO:0000313|Proteomes:UP000006729} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Nisqually {ECO:0000313|Proteomes:UP000006729}; RX PubMed=16973872; DOI=10.1126/science.1128691; RA Tuskan G.A., Difazio S., Jansson S., Bohlmann J., Grigoriev I., RA Hellsten U., Putnam N., Ralph S., Rombauts S., Salamov A., Schein J., RA Sterck L., Aerts A., Bhalerao R.R., Bhalerao R.P., Blaudez D., RA Boerjan W., Brun A., Brunner A., Busov V., Campbell M., Carlson J., RA Chalot M., Chapman J., Chen G.-L., Cooper D., Coutinho P.M., RA Couturier J., Covert S., Cronk Q., Cunningham R., Davis J., RA Degroeve S., Dejardin A., dePamphilis C.W., Detter J., Dirks B., RA Dubchak I., Duplessis S., Ehlting J., Ellis B., Gendler K., RA Goodstein D., Gribskov M., Grimwood J., Groover A., Gunter L., RA Hamberger B., Heinze B., Helariutta Y., Henrissat B., Holligan D., RA Holt R., Huang W., Islam-Faridi N., Jones S., Jones-Rhoades M., RA Jorgensen R., Joshi C., Kangasjaervi J., Karlsson J., Kelleher C., RA Kirkpatrick R., Kirst M., Kohler A., Kalluri U., Larimer F., RA Leebens-Mack J., Leple J.-C., Locascio P., Lou Y., Lucas S., RA Martin F., Montanini B., Napoli C., Nelson D.R., Nelson C., RA Nieminen K., Nilsson O., Pereda V., Peter G., Philippe R., Pilate G., RA Poliakov A., Razumovskaya J., Richardson P., Rinaldi C., Ritland K., RA Rouze P., Ryaboy D., Schmutz J., Schrader J., Segerman B., Shin H., RA Siddiqui A., Sterky F., Terry A., Tsai C.-J., Uberbacher E., RA Unneberg P., Vahala J., Wall K., Wessler S., Yang G., Yin T., RA Douglas C., Marra M., Sandberg G., Van de Peer Y., Rokhsar D.S.; RT "The genome of black cottonwood, Populus trichocarpa (Torr. & Gray)."; RL Science 313:1596-1604(2006). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CM000343; EEE91329.2; -; Genomic_DNA. DR RefSeq; XP_002310879.2; XM_002310843.2. DR STRING; 3694.POPTR_0007s14660.1; -. DR EnsemblPlants; POPTR_0007s14660.1; POPTR_0007s14660.1; POPTR_0007s14660. DR GeneID; 7497729; -. DR Gramene; POPTR_0007s14660.1; POPTR_0007s14660.1; POPTR_0007s14660. DR KEGG; pop:POPTR_0007s14660g; -. DR eggNOG; KOG0410; Eukaryota. DR eggNOG; KOG4197; Eukaryota. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000083465; -. DR InParanoid; B9HFU2; -. DR OMA; CNEDEVP; -. DR OrthoDB; EOG09360975; -. DR Proteomes; UP000006729; Linkage group LGVII. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR GO; GO:0043022; F:ribosome binding; IBA:GO_Central. DR CDD; cd01878; HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 2. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000006729}; KW Reference proteome {ECO:0000313|Proteomes:UP000006729}. FT DOMAIN 219 478 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT NON_TER 1 1 {ECO:0000313|EMBL:EEE91329.2}. SQ SEQUENCE 511 AA; 57028 MW; 4AFB808C1001EFDF CRC64; DPTSPPRLFV VQPRLRPDTL LQAKLNEALC LANSLEEQRD GYFDSDFFDK PLPPHILVQN PIFRSSKARD DVDAVFVNAI LSGIQLRNLE RKWNKPVLDR VSLIIEIFNA HAHTKEAKLQ AELAALMYAK SRLVRVRSSD GRLTFGAFGD AEVVSARGRG SGGRGFTSGA GETELQLQRR RILERRETLR TQIKDVRRTR ALQRASRKRH CQLDSQYLAT VAVVGYTNAG KSTLVSALSG NDLYSDSRLF ATLDARLKSV VLPSGRKVLL GDTVGFISDL PVQLVQAFRA TLEEVVEADL LVHLMDSTAP NLEEHRATVL QALQQIGVSE EKLQNMIEVW NKIDYQEEMV ADEYLCDGED GEASSLSGDE GGDVASGADD EINGFSGRSE GDFEETIDNE QDDYSGDWLL SGDDQEMVGD HWLKTLDEQR DEALNDLGME NFLQCQAQHG PHLKISAMTG VGLQELLELI DDRLKTQDEK FKEQNVVERG FFNKKWRPPR TEDAGIAAAE Q // ID B9JF09_AGRRK Unreviewed; 443 AA. AC B9JF09; DT 24-MAR-2009, integrated into UniProtKB/TrEMBL. DT 24-MAR-2009, sequence version 1. DT 07-JUN-2017, entry version 60. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Arad_2272 {ECO:0000313|EMBL:ACM26500.1}; OS Agrobacterium radiobacter (strain K84 / ATCC BAA-868). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Rhizobiaceae; Rhizobium/Agrobacterium group; Agrobacterium; OC Agrobacterium tumefaciens complex. OX NCBI_TaxID=311403 {ECO:0000313|EMBL:ACM26500.1, ECO:0000313|Proteomes:UP000001600}; RN [1] {ECO:0000313|EMBL:ACM26500.1, ECO:0000313|Proteomes:UP000001600} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K84 / ATCC BAA-868 {ECO:0000313|Proteomes:UP000001600}; RX PubMed=19251847; DOI=10.1128/JB.01779-08; RA Slater S.C., Goldman B.S., Goodner B., Setubal J.C., Farrand S.K., RA Nester E.W., Burr T.J., Banta L., Dickerman A.W., Paulsen I., RA Otten L., Suen G., Welch R., Almeida N.F., Arnold F., Burton O.T., RA Du Z., Ewing A., Godsy E., Heisel S., Houmiel K.L., Jhaveri J., Lu J., RA Miller N.M., Norton S., Chen Q., Phoolcharoen W., Ohlin V., RA Ondrusek D., Pride N., Stricklin S.L., Sun J., Wheeler C., Wilson L., RA Zhu H., Wood D.W.; RT "Genome sequences of three Agrobacterium biovars help elucidate the RT evolution of multichromosome genomes in bacteria."; RL J. Bacteriol. 191:2501-2511(2009). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000628; ACM26500.1; -; Genomic_DNA. DR RefSeq; WP_007693483.1; NC_011985.1. DR ProteinModelPortal; B9JF09; -. DR STRING; 311403.Arad_2272; -. DR EnsemblBacteria; ACM26500; ACM26500; Arad_2272. DR KEGG; ara:Arad_2272; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000001600; Chromosome 1. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000001600}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000001600}. FT DOMAIN 206 378 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 165 199 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 443 AA; 49098 MW; AA8989D3C4461A16 CRC64; MRAVVIVPVL KQGRSRSAQA DGAATTSRTP ESRLEEGKGL AQAIDLDIVN GSIVPINDPR PATLLGTGKI EEILALLDEL NAGLVIVDHP LTPVQQRNLE KAWNAKVIDR TGLILEIFGR RASTKEGTLQ VELAHLNYQK GRLVRSWTHL ERQRGGAGFM GGPGETQIEA DRRQLQERII RLERELEQVV RTRQLHRAKR RKVPHPIVAL VGYTNAGKST LFNRITGAGV LAEDMLFATL DPTLRRMKLP HGRTVILSDT VGFISDLPTH LVAAFRATLE EVLEADLILH VRDLSDEDNQ AQSADVMRIL GDLGIGEAEG AERILEVWNK IDRLEPEAHD AIVQKASTAE NVIAVSAMSG EGVDRLMDEI SRRLSGVLTE TTITLPLDKL ALLSWVYNHA IVDSREDNED GTVKLEVRLT ETEATELERR LGRGPKPQRE DWE // ID B9JW98_AGRVS Unreviewed; 444 AA. AC B9JW98; DT 24-MAR-2009, integrated into UniProtKB/TrEMBL. DT 24-MAR-2009, sequence version 1. DT 07-JUN-2017, entry version 62. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflx {ECO:0000313|EMBL:ACM36526.1}; GN Synonyms=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Avi_2142 {ECO:0000313|EMBL:ACM36526.1}; OS Agrobacterium vitis (strain S4 / ATCC BAA-846) (Rhizobium vitis OS (strain S4)). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Rhizobiaceae; Rhizobium/Agrobacterium group; Agrobacterium. OX NCBI_TaxID=311402 {ECO:0000313|EMBL:ACM36526.1, ECO:0000313|Proteomes:UP000001596}; RN [1] {ECO:0000313|EMBL:ACM36526.1, ECO:0000313|Proteomes:UP000001596} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=S4 / ATCC BAA-846 {ECO:0000313|Proteomes:UP000001596}; RX PubMed=19251847; DOI=10.1128/JB.01779-08; RA Slater S.C., Goldman B.S., Goodner B., Setubal J.C., Farrand S.K., RA Nester E.W., Burr T.J., Banta L., Dickerman A.W., Paulsen I., RA Otten L., Suen G., Welch R., Almeida N.F., Arnold F., Burton O.T., RA Du Z., Ewing A., Godsy E., Heisel S., Houmiel K.L., Jhaveri J., Lu J., RA Miller N.M., Norton S., Chen Q., Phoolcharoen W., Ohlin V., RA Ondrusek D., Pride N., Stricklin S.L., Sun J., Wheeler C., Wilson L., RA Zhu H., Wood D.W.; RT "Genome sequences of three Agrobacterium biovars help elucidate the RT evolution of multichromosome genomes in bacteria."; RL J. Bacteriol. 191:2501-2511(2009). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000633; ACM36526.1; -; Genomic_DNA. DR RefSeq; WP_015915947.1; NC_011989.1. DR ProteinModelPortal; B9JW98; -. DR STRING; 311402.Avi_2142; -. DR EnsemblBacteria; ACM36526; ACM36526; Avi_2142. DR GeneID; 31495369; -. DR KEGG; avi:Avi_2142; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000001596; Chromosome 1. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000001596}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000001596}. FT DOMAIN 207 379 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 166 200 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 444 AA; 49250 MW; 933BF261744A4F2A CRC64; MRAVVLVPVL KQARSSEKAS AELGPTTTRS HESRLEEAMG LARAIDLTIV QGLIVAVNQP RPATLIGSGK IEEIKALLDN HDAGLVIVDH PLTPVQQRNL EKQWNAKVID RTGLILEIFG RRASTKEGTL QVDLAHLNYQ KGRLVRSWTH LERQRGGAGF MGGPGETQIE ADRRMLQDRI VRLERELEQV VRTRQLHRAK RRKVPHPIVA LVGYTNAGKS TLFNRITGAG VLAEDMLFAT LDPTLRRMKL PQGRTVILSD TVGFISDLPT HLVAAFRATL EEVLEADLIL HVRDMADPDN GAQAGDVMRI LSDLGIDEKE RDERIIEVWN KIDRLEPEAH QAIAEKATGR QNVMAVSAVT GEGVDALMAE IAQRLSGVVT ETTVILPPDK LSLISWVYEN TMVDSREDRD DGSVSLDLRL SEQQASALER KLGLIQPVRS EDWN // ID B9KZE3_THERP Unreviewed; 424 AA. AC B9KZE3; DT 24-MAR-2009, integrated into UniProtKB/TrEMBL. DT 24-MAR-2009, sequence version 1. DT 07-JUN-2017, entry version 55. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=trd_0861 {ECO:0000313|EMBL:ACM04550.1}; OS Thermomicrobium roseum (strain ATCC 27502 / DSM 5159 / P-2). OC Bacteria; Chloroflexi; Thermomicrobiales; Thermomicrobiaceae; OC Thermomicrobium. OX NCBI_TaxID=309801 {ECO:0000313|EMBL:ACM04550.1, ECO:0000313|Proteomes:UP000000447}; RN [1] {ECO:0000313|EMBL:ACM04550.1, ECO:0000313|Proteomes:UP000000447} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 27502 / DSM 5159 / P-2 RC {ECO:0000313|Proteomes:UP000000447}; RX PubMed=19148287; DOI=10.1371/journal.pone.0004207; RA Wu D., Raymond J., Wu M., Chatterji S., Ren Q., Graham J.E., RA Bryant D.A., Robb F., Colman A., Tallon L.J., Badger J.H., Madupu R., RA Ward N.L., Eisen J.A.; RT "Complete genome sequence of the aerobic CO-oxidizing thermophile RT Thermomicrobium roseum."; RL PLoS ONE 4:E4207-E4207(2009). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001275; ACM04550.1; -; Genomic_DNA. DR ProteinModelPortal; B9KZE3; -. DR STRING; 309801.trd_0861; -. DR EnsemblBacteria; ACM04550; ACM04550; trd_0861. DR KEGG; tro:trd_0861; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000000447; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000000447}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000000447}. FT DOMAIN 194 363 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 424 AA; 48045 MW; 9FDF9208925DB376 CRC64; MERALLVCVE WRRDGWEADA SLEELAQLAR TAGVEVVGTV TQRLPHPHPQ HYVGPGKLRE LLTMRDQLGY TLLLADDELS PAQLRHLEDA LQVKVLDRTA LILDIFARHA RTREGRLQVE LAQLEYRLPR LTRMWTHLSR QAVGGVGLRG PGETQLEIDR RRARERIAWI RRQLEEVREH RARYRQRRRQ NRLPVIALVG YTNAGKSTLL NALTGADVLA ADKLFATLDP TTRRLRLSDS QVALLTDTVG FIHKLPTTLV AAFRATLEEI LDAHLLLHVV DITHPKAAEQ AAAVRQVLRE LGADRYPTIT VLNKIDRLEP TIDPDRLARE LDIPTNAVFV SAATGYGLET LRDRIARTLR DIATPRAVQL LIPYREQRLI ATLEEHGIIS ERRYLAEGIL LRARLPNSLL PRLEPFLAPS VDDA // ID B9LNF7_HALLT Unreviewed; 449 AA. AC B9LNF7; DT 24-MAR-2009, integrated into UniProtKB/TrEMBL. DT 24-MAR-2009, sequence version 1. DT 07-JUN-2017, entry version 56. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Hlac_1303 {ECO:0000313|EMBL:ACM56895.1}; OS Halorubrum lacusprofundi (strain ATCC 49239 / DSM 5036 / JCM 8891 / OS ACAM 34). OC Archaea; Euryarchaeota; Halobacteria; Haloferacales; Halorubraceae; OC Halorubrum. OX NCBI_TaxID=416348 {ECO:0000313|EMBL:ACM56895.1, ECO:0000313|Proteomes:UP000000740}; RN [1] {ECO:0000313|EMBL:ACM56895.1, ECO:0000313|Proteomes:UP000000740} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 49239 / DSM 5036 / JCM 8891 / ACAM 34 RC {ECO:0000313|Proteomes:UP000000740}; RG US DOE Joint Genome Institute; RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., RA Tice H., Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T., RA Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N., RA Ivanova N., Anderson I., DasSarma S., Cavicchioli R., Richardson P.; RT "Complete sequence of chromosome1 of Halorubrum lacusprofundi ATCC RT 49239."; RL Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001365; ACM56895.1; -; Genomic_DNA. DR RefSeq; WP_015910037.1; NC_012029.1. DR ProteinModelPortal; B9LNF7; -. DR STRING; 416348.Hlac_1303; -. DR EnsemblBacteria; ACM56895; ACM56895; Hlac_1303. DR GeneID; 7399398; -. DR KEGG; hla:Hlac_1303; -. DR eggNOG; arCOG00353; Archaea. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG093Z07D6; -. DR BioCyc; HLAC416348:GIWW-1329-MONOMER; -. DR Proteomes; UP000000740; Chromosome 1. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000000740}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000000740}. FT DOMAIN 204 387 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 449 AA; 49387 MW; A6A21386F9BB3C11 CRC64; MTGSVEGRDT DTEPTAAERR AVVAKRVESG SADLTEITQL AAAAGYDVVG ELTQTRTEDA AFMFGEGKVA ELRDLVRRTD ANAVIIDNDV GPYQTFNIGG ELPEGVEVID RFALILEIFG QRANTRKAQL QVELAELRYE LPRAEAKASL AKRDERPGFM GLGEYDESVE RDIKRQISEI RDELASIAEK EEARREQRRD SGFDLVALAG YTNAGKSTLM RRLAAEIDVD ENAERHPDLD TTAESQDMLF TTLGTTTRRA EMEKRDVLLT DTVGFIADLP HWLVESFEST LDSVYRADLV LLVVDASEPV ETMREKLVTS HDTLYERNEA PVVTVFNKVD RLAPGELADK RAALSGVAPD PVAVSAKTSA GVAELRDRVE AELPDWERER LVLPLSDDAM SLVSWIHDHG HVEAETYADD QVTLDFEAKP SIVARARSKA AGLAPAGST // ID B9M6K6_GEODF Unreviewed; 552 AA. AC B9M6K6; DT 24-MAR-2009, integrated into UniProtKB/TrEMBL. DT 24-MAR-2009, sequence version 1. DT 07-JUN-2017, entry version 64. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Geob_1708 {ECO:0000313|EMBL:ACM20066.1}; OS Geobacter daltonii (strain DSM 22248 / JCM 15807 / FRC-32). OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfuromonadales; OC Geobacteraceae; Geobacter. OX NCBI_TaxID=316067 {ECO:0000313|EMBL:ACM20066.1, ECO:0000313|Proteomes:UP000007721}; RN [1] {ECO:0000313|EMBL:ACM20066.1, ECO:0000313|Proteomes:UP000007721} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 22248 / JCM 15807 / FRC-32 RC {ECO:0000313|Proteomes:UP000007721}; RG US DOE Joint Genome Institute; RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., RA Tice H., Bruce D., Goodwin L., Pitluck S., Saunders E., Brettin T., RA Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N., RA Ovchinnikova G., Kostka J., Richardson P.; RT "Complete sequence of Geobacter sp. FRC-32."; RL Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001390; ACM20066.1; -; Genomic_DNA. DR RefSeq; WP_012646795.1; NC_011979.1. DR ProteinModelPortal; B9M6K6; -. DR STRING; 316067.Geob_1708; -. DR EnsemblBacteria; ACM20066; ACM20066; Geob_1708. DR KEGG; geo:Geob_1708; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; EREVIIT; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000007721; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000007721}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000007721}. FT DOMAIN 369 542 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 184 211 {ECO:0000256|SAM:Coils}. FT COILED 328 355 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 552 AA; 62603 MW; 1E1EF62446CF71EE CRC64; MKPSQHKGLE RLYRRRVPPE EVITLDLARE LVELSREIRR QLGLLVNRSG DVEYVIVGDE RGLYIPELSD YPLGKKLLRE LRLIHTHLKG ESLTDDDLTD LALLRLDLIA ALQISPVEGQ FSIQTAYLAP HTPGKAPYRT ERPQPFSRFE LDFASFVETL ESSLHQAANG TRVIMKGEER GILISVTKAS LDEAEDSIEE LKELARTAGV EVLDTVIQRP RQFNPRFLMG EGKMRDVVIR ALQLGASLLV FDQELSPTQI RSISAMTELK VIDRSQLILD IFARRAQSLD GKVQVELAQL KYLLPRLTGR GVQMSRLMGG IGGRGPGETK LEMDRRRIRD RIARLEKELK ELSHGRYQRR QKRVKAGLPI ISIVGYTNAG KSTLLNTLTQ SDVFTENLLF ATLDTSTRRL RFPRDREVII TDTVGFIRSL PKSLMGAFKA TLEELQDADL LLHLVDCSNP RFEEHISQVE TILDELELET KPRLLVFNKT DLLTEMKKKD PLTAMKVRQA SRRLSAIAIS AADRKSLAPL MEELQRRFWP QETAIAGQVI PE // ID B9NQT5_9RHOB Unreviewed; 423 AA. AC B9NQT5; DT 24-MAR-2009, integrated into UniProtKB/TrEMBL. DT 24-MAR-2009, sequence version 1. DT 07-JUN-2017, entry version 40. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:EEE36442.1}; GN ORFNames=RKLH11_275 {ECO:0000313|EMBL:EEE36442.1}; OS Rhodobacteraceae bacterium KLH11. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae. OX NCBI_TaxID=467661 {ECO:0000313|EMBL:EEE36442.1, ECO:0000313|Proteomes:UP000005135}; RN [1] {ECO:0000313|Proteomes:UP000005135} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=KLH11 {ECO:0000313|Proteomes:UP000005135}; RX PubMed=21742885; DOI=10.1128/JB.05556-11; RA Zan J., Fricke W.F., Fuqua C., Ravel J., Hill R.T.; RT "Genome Sequence of Ruegeria sp. Strain KLH11, an N-Acylhomoserine RT Lactone-Producing Bacterium Isolated from the Marine Sponge Mycale RT laxissima."; RL J. Bacteriol. 193:5011-5012(2011). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; DS999531; EEE36442.1; -; Genomic_DNA. DR RefSeq; WP_008755623.1; NZ_DS999531.1. DR ProteinModelPortal; B9NQT5; -. DR STRING; 467661.RKLH11_275; -. DR EnsemblBacteria; EEE36442; EEE36442; RKLH11_275. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000005135; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000005135}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000005135}. FT DOMAIN 203 372 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 423 AA; 47096 MW; 5FA6AEF2D40B124C CRC64; MEHERARTRA WVLHPEIKSD EQRRVPGPAL EEAVALAAAL PDLDVVGSEI VRLQRAQAGL LFGSGKIEEL AERLHDHEIE LVLIDGPVTP VQQRNLEKAW KVKILDRTGL ILEIFSDRAR TREGVLQVEM AALSYQRTRL VRAWTHLERQ RGGLGFVGGP GETQIEADRR AIDEQLVRLR RQLQKVVKTR TLHRAARAKV PYPIVALVGY TNAGKSTLFN SLTGAEVMAK DMLFATLDPT MRRVELQDGP EVILSDTVGF ISNLPTELVA AFRATLEEVL GADLVVHVRD ISHEDSEAQA QDVETILASL GVDDDRPRLE VWNKIDLLGA EAREATLARA ERDPQVFAIS AVTGEGVAPL LTEIATKLQG TRHQHVLNLG FAEGDKRAWL YRQDVVRSEE QTEDGFEITV LWTEKQAAQF AAL // ID B9QRY0_LABAD Unreviewed; 431 AA. AC B9QRY0; DT 24-MAR-2009, integrated into UniProtKB/TrEMBL. DT 24-MAR-2009, sequence version 1. DT 07-JUN-2017, entry version 48. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:EEE46897.1}; GN ORFNames=SADFL11_4186 {ECO:0000313|EMBL:EEE46897.1}; OS Labrenzia alexandrii (strain DSM 17067 / NCIMB 14079 / DFL-11) OS (Stappia alexandrii). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae; Labrenzia. OX NCBI_TaxID=244592 {ECO:0000313|EMBL:EEE46897.1, ECO:0000313|Proteomes:UP000004703}; RN [1] {ECO:0000313|EMBL:EEE46897.1, ECO:0000313|Proteomes:UP000004703} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 17067 / NCIMB 14079 / DFL-11 RC {ECO:0000313|Proteomes:UP000004703}; RA Wagner-Dobler I., Ferriera S., Johnson J., Kravitz S., Beeson K., RA Sutton G., Rogers Y.-H., Friedman R., Frazier M., Venter J.C.; RL Submitted (JAN-2008) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; EQ973121; EEE46897.1; -; Genomic_DNA. DR ProteinModelPortal; B9QRY0; -. DR STRING; 244592.SADFL11_4186; -. DR EnsemblBacteria; EEE46897; EEE46897; SADFL11_4186. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000004703; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000004703}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000004703}. FT DOMAIN 200 370 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 159 193 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 431 AA; 47990 MW; 69B52F7EE2349FF7 CRC64; MILEPIIQLR SENSQADLRS NRSPEARLDE AIGLSAAINL DIVHSGVVRI NNPKPATLFG EGKVAELAGI VASEDLDLVV IDHPLSPVQQ RNLERRLKTK VIDRTGLILE IFGDRARTKE GKLQVDLAHL TWQKSRLVRS WTHLERQRGG AGFMGGPGET QIEADRRQIQ ERIIALQKQL ESVRRTRELH RKKRKKIPQP VVALVGYTNA GKSTLFNRLT ESEVFAKDLL FATLDPTLRK ITLPHGREII LSDTVGFISD LPTHLVAAFR ATLEEVLEAD LILHVRDISH ADTDAQAEDV QKTLEELGVD ALTGAPIIEV WNKIDLLDKD YRAKLLSEEQ GEGPVALSAV TGEGIEHLSA RVDSFMARHD DILSVRVPVA EGALIAKLYQ MAEVLERSDG EEYVIAEVRV SDKQRGPFRD LFGKFAIDPS E // ID B9R801_RICCO Unreviewed; 541 AA. AC B9R801; DT 24-MAR-2009, integrated into UniProtKB/TrEMBL. DT 24-MAR-2009, sequence version 1. DT 07-JUN-2017, entry version 39. DE SubName: Full=GTP-binding protein hflx, putative {ECO:0000313|EMBL:EEF52631.1}; GN ORFNames=RCOM_1595750 {ECO:0000313|EMBL:EEF52631.1}; OS Ricinus communis (Castor bean). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae; OC Pentapetalae; rosids; fabids; Malpighiales; Euphorbiaceae; OC Acalyphoideae; Acalypheae; Ricinus. OX NCBI_TaxID=3988 {ECO:0000313|Proteomes:UP000008311}; RN [1] {ECO:0000313|Proteomes:UP000008311} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Hale {ECO:0000313|Proteomes:UP000008311}; RX PubMed=20729833; DOI=10.1038/nbt.1674; RA Chan A.P., Crabtree J., Zhao Q., Lorenzi H., Orvis J., Puiu D., RA Melake-Berhan A., Jones K.M., Redman J., Chen G., Cahoon E.B., RA Gedil M., Stanke M., Haas B.J., Wortman J.R., Fraser-Liggett C.M., RA Ravel J., Rabinowicz P.D.; RT "Draft genome sequence of the oilseed species Ricinus communis."; RL Nat. Biotechnol. 28:951-956(2010). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; EQ973772; EEF52631.1; -; Genomic_DNA. DR RefSeq; XP_002510444.1; XM_002510398.2. DR ProteinModelPortal; B9R801; -. DR GeneID; 8275781; -. DR KEGG; rcu:8275781; -. DR InParanoid; B9R801; -. DR KO; K03665; -. DR Proteomes; UP000008311; Unassembled WGS sequence. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000008311}; KW Reference proteome {ECO:0000313|Proteomes:UP000008311}. FT DOMAIN 318 484 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 541 AA; 60394 MW; AF90FAFAB99B6D2D CRC64; MIACYCNSPV RPSPLHDHYF PWNSNPYNRP NYPLTLSTHK SRLTTRVLQQ GFEVASPINA PFPGQLIYNN EVEEVHGPVN GVAGPASEDK PAVSSTKFRK KKQDGDSLED RFKLRNGREV YEEKGYLVGV ERKGDTLDSF GIEESLKELA QLADTAGLTV VGSTYQKLTS PNPRTYIGSG KVAEIKSAIH ALDIETVIFD DELSPGQLRN LEKIFGGDVR VCDRTALILD IFNQRAATHE ASLQVALAQM EYQLPRLTRM WTHLERQAGG KVKGMGEKQI EVDKRILRTQ IGVLKKELES VRNHRKQYRN RRTSVPVPVV SLVGYTNAGK STLLNQLTGA NVLAEDRLFA TLDPTTRRVQ MKNGNEFLLT DTVGFIQKLP TTLVAAFRAT LEEISESSLL VHVVDISHPL AEQQIDAVDR VLSELDVASI SKLMVWNKVD RVSNPSEIKL EAEKRQDVVC ISALGGDGLQ EFCIAVQEKL KDSMVWVEAL VPFEKGDLLS TIHQVGMVER TEYTENGTLI KAHVPLRFAR LLTPMRQLCK A // ID B9SX85_RICCO Unreviewed; 625 AA. AC B9SX85; DT 24-MAR-2009, integrated into UniProtKB/TrEMBL. DT 24-MAR-2009, sequence version 1. DT 12-APR-2017, entry version 34. DE SubName: Full=GTP-binding protein hflx, putative {ECO:0000313|EMBL:EEF31784.1}; GN ORFNames=RCOM_0859540 {ECO:0000313|EMBL:EEF31784.1}; OS Ricinus communis (Castor bean). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae; OC Pentapetalae; rosids; fabids; Malpighiales; Euphorbiaceae; OC Acalyphoideae; Acalypheae; Ricinus. OX NCBI_TaxID=3988 {ECO:0000313|Proteomes:UP000008311}; RN [1] {ECO:0000313|Proteomes:UP000008311} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Hale {ECO:0000313|Proteomes:UP000008311}; RX PubMed=20729833; DOI=10.1038/nbt.1674; RA Chan A.P., Crabtree J., Zhao Q., Lorenzi H., Orvis J., Puiu D., RA Melake-Berhan A., Jones K.M., Redman J., Chen G., Cahoon E.B., RA Gedil M., Stanke M., Haas B.J., Wortman J.R., Fraser-Liggett C.M., RA Ravel J., Rabinowicz P.D.; RT "Draft genome sequence of the oilseed species Ricinus communis."; RL Nat. Biotechnol. 28:951-956(2010). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; EQ974218; EEF31784.1; -; Genomic_DNA. DR ProteinModelPortal; B9SX85; -. DR InParanoid; B9SX85; -. DR Proteomes; UP000008311; Unassembled WGS sequence. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR CDD; cd01878; HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 2. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008311}; KW Reference proteome {ECO:0000313|Proteomes:UP000008311}. FT DOMAIN 300 430 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 625 AA; 69798 MW; 12920CB77D57E402 CRC64; MLALSSLRSR LSLNSLALSQ TLTIINPHQS ITHSQFSSKQ HQQNSNEIDT HGVVSIINRD PTSPPRLFVV QPRLRPDSFL QAKLNEALCL ANSLEEQRDG YFDTDFFDKA LPPHVIVQNP ILRSSRARAD TFFGPGTVNT IKCHLNASES KGEVDAVFVN SVLTGVQQRN LERAWGRPVL DRVGLIIEIF NAHAHTKEAK LQSELAALMY KKSRLVRARG LDGRYTXLLQ FLRLKIEIWR GSGGRGFISG AGETELQLQR RRILERRNYL LSQIREVRRT RAVQRAARKR DDGLHNKGLA TVAVVGYTNA GKSTMVSTLS NSDLYSDSRL FATLDPRLKS VVLPSGRKVL FSDTVGFISD LPVQLVEAFR ATLEEVVEAD LLVHVIDSTA PNLEEHHTTV LQVLQQIGVS KEKLQSMIEV WNKIDYEEEE MDVDHSADDV DGSSWSGDED DDIASEISSR IEDNKGNNCL EAQNGEGDIE ETLDSVEGEY SDGWLLSGDE RELVGDNWLK TLDDQQCKAS DNPGVGKDIL SQAEHGPHVK TSAITGVGLQ ELLVLVDERL KTQDEMLKAQ NVVGRDLFYR KWRPSRADDT EAAGLRIGED EDVKNMGTRT QLAALEMIIR VNYSE // ID B9XPW1_PEDPL Unreviewed; 414 AA. AC B9XPW1; DT 14-APR-2009, integrated into UniProtKB/TrEMBL. DT 14-APR-2009, sequence version 1. DT 07-JUN-2017, entry version 41. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=Cflav_PD1486 {ECO:0000313|EMBL:EEF58142.1}; OS Pedosphaera parvula (strain Ellin514). OC Bacteria; Verrucomicrobia; Verrucomicrobiae; Verrucomicrobiales; OC Verrucomicrobia subdivision 3; Pedosphaera. OX NCBI_TaxID=320771 {ECO:0000313|EMBL:EEF58142.1, ECO:0000313|Proteomes:UP000003688}; RN [1] {ECO:0000313|EMBL:EEF58142.1, ECO:0000313|Proteomes:UP000003688} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Ellin514 {ECO:0000313|EMBL:EEF58142.1, RC ECO:0000313|Proteomes:UP000003688}; RX PubMed=21460084; DOI=10.1128/JB.00299-11; RA Kant R., van Passel M.W., Sangwan P., Palva A., Lucas S., Copeland A., RA Lapidus A., Glavina Del Rio T., Dalin E., Tice H., Bruce D., RA Goodwin L., Pitluck S., Chertkov O., Larimer F.W., Land M.L., RA Hauser L., Brettin T.S., Detter J.C., Han S., de Vos W.M., RA Janssen P.H., Smidt H.; RT "Genome sequence of 'Pedosphaera parvula' Ellin514, an aerobic RT Verrucomicrobial isolate from pasture soil."; RL J. Bacteriol. 193:2900-2901(2011). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EEF58142.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABOX02000049; EEF58142.1; -; Genomic_DNA. DR RefSeq; WP_007417847.1; NZ_ABOX02000049.1. DR ProteinModelPortal; B9XPW1; -. DR STRING; 320771.Cflav_PD1486; -. DR EnsemblBacteria; EEF58142; EEF58142; Cflav_PD1486. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000003688; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000003688}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000003688}. FT DOMAIN 191 355 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 414 AA; 46060 MW; 941D8DA32059DD0D CRC64; MFLVGVELKS RNAWEIRESL DELTELAATA GADVIGDGTQ KMEAPMAATF IGSGKAQEFA RHCVSNEVDT VIFDDELTPA QSRNLEQVFN CKILDRTSLI LDIFAQRART KEGKLQIELA QLQHLLPRLT RFWGHLSRQK GGIGMRGDGE TQLETDRRRV QDRIARIARE LEVVRRQRST QRHGRQRNLW PLASIVGYTN AGKSTLLNAV TGADVLAENK LFATLDPTTR RLRLPTNQNV LLTDTVGFIR KLPHNLVEAF KATLEEVVQA DLLIHVVDGS SPQAEEQIAA VNAVLDEIGA AGKPTMMVFN KIDKLVNGER NFIQSVPNAV AISAKTGEGI PELMAELGKQ LKPIREFIEL SVPHENAAVI ARLHAVGQVM ERDYEGEQAR FKVRIPPHLH EEFAPFIVQA LQTV // ID B9YE13_9FIRM Unreviewed; 382 AA. AC B9YE13; DT 14-APR-2009, integrated into UniProtKB/TrEMBL. DT 14-APR-2009, sequence version 1. DT 07-JUN-2017, entry version 42. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:EEF65774.1}; GN ORFNames=HOLDEFILI_04087 {ECO:0000313|EMBL:EEF65774.1}; OS Holdemania filiformis DSM 12042. OC Bacteria; Firmicutes; Erysipelotrichia; Erysipelotrichales; OC Erysipelotrichaceae; Holdemania. OX NCBI_TaxID=545696 {ECO:0000313|EMBL:EEF65774.1, ECO:0000313|Proteomes:UP000005950}; RN [1] {ECO:0000313|EMBL:EEF65774.1, ECO:0000313|Proteomes:UP000005950} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 12042 {ECO:0000313|EMBL:EEF65774.1, RC ECO:0000313|Proteomes:UP000005950}; RA Fulton L., Clifton S., Fulton B., Xu J., Minx P., Pepin K.H., RA Johnson M., Bhonagiri V., Nash W.E., Mardis E.R., Wilson R.K.; RL Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:EEF65774.1, ECO:0000313|Proteomes:UP000005950} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 12042 {ECO:0000313|EMBL:EEF65774.1, RC ECO:0000313|Proteomes:UP000005950}; RA Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., RA Liep D., Gordon J.; RT "Draft genome sequence of Holdemania filiformis DSM 12042."; RL Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EEF65774.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACCF01000257; EEF65774.1; -; Genomic_DNA. DR RefSeq; WP_006061223.1; NZ_GG657562.1. DR ProteinModelPortal; B9YE13; -. DR STRING; 545696.HOLDEFILI_04087; -. DR EnsemblBacteria; EEF65774; EEF65774; HOLDEFILI_04087. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000005950; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000005950}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000005950}. FT DOMAIN 194 359 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 382 AA; 43053 MW; 77FDE46FD0159AE9 CRC64; MKSAVLAGLR TQETEESWAQ KLDEAALLCE ACGIEVKTRL TQKAQKRHPR TLFGSGKVNE LKQACEAQSA EGIVFVNELT GIQTRNLEQE TGFPVIDRSA LILEIFERRA RTRQAHLQVE AARLAYQLPR LIEGQIHADQ QQGGGVRNRG TGETRLERSR RTIEKQIRNI RLELDQLKLQ QAVQSHRRRQ SGLPRVCLIG YSNAGKSSLM NALLSLRSIS PAKQVASADQ LFATLDSATR RIKLAGRAEM LLSDTVGFVR DLPDFLLDAF ESTLQEIQEA DLLMEVIDAS DPQWELQHEI VMRTLHRLHA AHIDRMRIYN KADQVPQWDR KDGLLLSCLT GQGLQELIAG LISRLNLTDR AFPEIGDEFS SQVSYNEDER GE // ID C0ARS5_9GAMM Unreviewed; 428 AA. AC C0ARS5; DT 05-MAY-2009, integrated into UniProtKB/TrEMBL. DT 05-MAY-2009, sequence version 1. DT 30-AUG-2017, entry version 44. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:EEG87221.1}; GN ORFNames=PROPEN_00496 {ECO:0000313|EMBL:EEG87221.1}; OS Proteus penneri ATCC 35198. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; OC Morganellaceae; Proteus. OX NCBI_TaxID=471881 {ECO:0000313|EMBL:EEG87221.1, ECO:0000313|Proteomes:UP000006464}; RN [1] {ECO:0000313|EMBL:EEG87221.1, ECO:0000313|Proteomes:UP000006464} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 35198 {ECO:0000313|EMBL:EEG87221.1, RC ECO:0000313|Proteomes:UP000006464}; RA Fulton L., Clifton S., Fulton B., Xu J., Minx P., Pepin K.H., RA Johnson M., Bhonagiri V., Nash W.E., Mardis E.R., Wilson R.K.; RL Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:EEG87221.1, ECO:0000313|Proteomes:UP000006464} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 35198 {ECO:0000313|EMBL:EEG87221.1, RC ECO:0000313|Proteomes:UP000006464}; RA Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., RA Liep D., Gordon J.; RT "Draft genome sequence of Proteus penneri (ATCC 35198)."; RL Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EEG87221.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABVP01000019; EEG87221.1; -; Genomic_DNA. DR ProteinModelPortal; C0ARS5; -. DR STRING; 471881.PROPEN_00496; -. DR EnsemblBacteria; EEG87221; EEG87221; PROPEN_00496. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR Proteomes; UP000006464; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000006464}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000006464}. FT DOMAIN 199 366 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 428 AA; 48602 MW; BD839CDE0AA298B7 CRC64; MFDRYEGGEL AVLVHVFFSQ EKNVDDLQEF ESLVTSAGVK PVQIITGNRK APHPKYYVGE GKAEEIAEAV KASGADVVLF NHALTPAQER NLERLCECRV VDRTGVILDI FFAQRARTHE GKLQVELAQL RHLSTRLVRG WTHLERQKGG IGLRGPGETQ LETDRRLLRG KISQILMRLG RVERQREQGR QARSKADIPT LSLVGYTNAG KSSLFNHITC SDVYAADQLF ATLDPTLRRI QVEDVGTVVL ADTVGFIRHL PHDLVAAFKA TLQETREATL LLHVIDAADS RFEENIHAVE SVLEEIDAQE IPTLHVMNKI DLLEDFTPRI DRNEENLPVR VWVSAQTGEG IPLLYQALTE RLSGEIAHFE LRLPPEDTGR LRSRFYQLQS IEREWIEKDG KVGLIIRMPM IDWRRLCKQE PNLLDYVV // ID C0BHG3_FLABM Unreviewed; 402 AA. AC C0BHG3; DT 05-MAY-2009, integrated into UniProtKB/TrEMBL. DT 05-MAY-2009, sequence version 1. DT 07-JUN-2017, entry version 47. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=Flav2ADRAFT_0851 {ECO:0000313|EMBL:EEG41547.1}; OS Flavobacteria bacterium (strain MS024-2A). OC Bacteria; Bacteroidetes; Flavobacteriia. OX NCBI_TaxID=487796 {ECO:0000313|EMBL:EEG41547.1, ECO:0000313|Proteomes:UP000003644}; RN [1] {ECO:0000313|EMBL:EEG41547.1, ECO:0000313|Proteomes:UP000003644} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MS024-2A {ECO:0000313|EMBL:EEG41547.1, RC ECO:0000313|Proteomes:UP000003644}; RG US DOE Joint Genome Institute (JGI-PGF); RA Woyke T., Xie G., Copeland A., Gonzalez J., Han C., Kiss H., Saw J., RA Senin P., Chatterji S., Cheng J.-F., Eisen J.A., Sieracki M.E., RA Stepanauskas R.; RT "Assembling the metagenome, one cell at a time."; RL Submitted (AUG-2008) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EEG41547.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABVV01000002; EEG41547.1; -; Genomic_DNA. DR RefSeq; WP_008865822.1; NZ_ABVV01000002.1. DR ProteinModelPortal; C0BHG3; -. DR STRING; 487796.Flav2ADRAFT_0851; -. DR EnsemblBacteria; EEG41547; EEG41547; Flav2ADRAFT_0851. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000003644; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000003644}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000003644}. FT DOMAIN 200 385 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 402 AA; 46324 MW; 61C803E60287967F CRC64; MIEEKSLDVE KTVLVGIINS RQDIQQSKEY LDELAFLAFT AGGEVMQRFT QKIDLPNPKT FIGSGKIQEV LEFVNENDIS SVIFDDELTP AQQGNIEKTL KVKILDRTGL ILDIFAQRAQ TSYARTQVEL AQYEYLLPRL KGLWTHLERQ RGGIGMRGPG ETEIETDRRI VRDKISLLKK KLINIDKQMA TQRGNRGALV RVALVGYTNV GKSTLMNVVA KSNVFAENKL FATLDTTVRK VVIGNLPFLM SDTVGFIRKL PTQLVESFKS TLDEVQEADL LLHVVDISHP NFEDHIDSVN QILKEIKSLD KPTLMVFNKI DVYQPEPWDE TELIEQREEK HFSLEEWKQT WMHRMNGQAL FISAINKDNL EGFRERLYQE VREIHVTRFP YNHFLYPEGL EE // ID C0BL62_9BACT Unreviewed; 402 AA. AC C0BL62; DT 05-MAY-2009, integrated into UniProtKB/TrEMBL. DT 05-MAY-2009, sequence version 1. DT 07-JUN-2017, entry version 38. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=Flav3CDRAFT_1310 {ECO:0000313|EMBL:EEG43832.1}; OS Flavobacteria bacterium MS024-3C. OC Bacteria; Bacteroidetes; Flavobacteriia. OX NCBI_TaxID=487797 {ECO:0000313|EMBL:EEG43832.1, ECO:0000313|Proteomes:UP000003631}; RN [1] {ECO:0000313|EMBL:EEG43832.1, ECO:0000313|Proteomes:UP000003631} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MS024-3C {ECO:0000313|EMBL:EEG43832.1, RC ECO:0000313|Proteomes:UP000003631}; RG US DOE Joint Genome Institute (JGI-PGF); RA Woyke T., Xie G., Copeland A., Gonzalez J., Han C., Kiss H., Saw J., RA Senin P., Chatterji S., Cheng J.-F., Eisen J.A., Sieracki M.E., RA Stepanauskas R.; RT "Assembling the metagenome, one cell at a time."; RL Submitted (AUG-2008) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EEG43832.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABVW01000001; EEG43832.1; -; Genomic_DNA. DR RefSeq; WP_008867392.1; NZ_ABVW01000001.1. DR ProteinModelPortal; C0BL62; -. DR STRING; 487797.Flav3CDRAFT_1310; -. DR EnsemblBacteria; EEG43832; EEG43832; Flav3CDRAFT_1310. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR Proteomes; UP000003631; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000003631}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000003631}. FT DOMAIN 200 385 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 402 AA; 46297 MW; B4CC6E4547CA8616 CRC64; MIEAQDLNYE KSVLIGVITK AQPEEKMKEY LDELEFLTYT AGGEVLKRFV QRIDVPNPKT YIGTGKMLEV AEFVKEHEIG AVIFDDELSP GQQKNIEREL KCKIVDRTSL ILDIFAQRAQ TSYARTQVEL AQYQYLLPRL AGLWTHLERQ KGGIGMRGPG ETEIETDRRI VRDRITLLKK QLHKIDRQME TQRGNRGALV RVALVGYTNV GKSTLMNVVS KSEVFAENKL FATLDTTVRK VVIGNLPFLM TDTVGFIRKL PTQLVESFKG TLDEVREADL LLHIVDISHS DFEDQIAAVN AIMADIKAAD KPTIMVFNKI DQYKPERLDE DDLITERTSK HFTMEEWERT WMQKMDGNAL FISALNKENL DQFRQKVYDA VRDIHVTRFP YNSFLYPEVL EE // ID C0C478_9FIRM Unreviewed; 424 AA. AC C0C478; DT 05-MAY-2009, integrated into UniProtKB/TrEMBL. DT 05-MAY-2009, sequence version 1. DT 07-JUN-2017, entry version 50. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:EEG72871.1}; GN ORFNames=CLOHYLEM_06893 {ECO:0000313|EMBL:EEG72871.1}; OS [Clostridium] hylemonae DSM 15053. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Lachnospiraceae. OX NCBI_TaxID=553973 {ECO:0000313|EMBL:EEG72871.1, ECO:0000313|Proteomes:UP000004893}; RN [1] {ECO:0000313|EMBL:EEG72871.1, ECO:0000313|Proteomes:UP000004893} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 15053 {ECO:0000313|EMBL:EEG72871.1, RC ECO:0000313|Proteomes:UP000004893}; RA Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., RA Liep D., Gordon J.; RT "Draft genome sequence of Clostridium hylemonae (DSM 15053)."; RL Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:EEG72871.1, ECO:0000313|Proteomes:UP000004893} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 15053 {ECO:0000313|EMBL:EEG72871.1, RC ECO:0000313|Proteomes:UP000004893}; RA Fulton L., Clifton S., Fulton B., Xu J., Minx P., Pepin K.H., RA Johnson M., Bhonagiri V., Nash W.E., Mardis E.R., Wilson R.K.; RL Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EEG72871.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABYI02000034; EEG72871.1; -; Genomic_DNA. DR RefSeq; WP_006444250.1; NZ_GG657760.1. DR ProteinModelPortal; C0C478; -. DR STRING; 553973.CLOHYLEM_06893; -. DR EnsemblBacteria; EEG72871; EEG72871; CLOHYLEM_06893. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000004893; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000004893}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000004893}. FT DOMAIN 199 363 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 158 192 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 424 AA; 47406 MW; 916F67BED3B84EA1 CRC64; MIDLKEEIER IILVGVSVSD QDDTEKSLDE LAELAAAAGA ETAGRIIQSR EQAHPATYIG KGKLEELKDL IWETYATGII CDDELSPAQM GNLQDELDVK VMDRTLVILD IFASRASTSE GKIQVELAQL KYRQSRLTGF GKSLSRLGGG IGTRGPGEKK LEMDRRLIKG RIAQLNRELR DVKRHREVTR EQRSRNQVPV AAVVGYTNAG KSTLLNALTG ADILAEDKLF ATLDPTTREL KLPSKQSVLL TDTVGFIRKL PHHLIEAFRS TLEEAKYADM ILHVVDTANP QMDEQMHIVY ETLRSLGVKD KPVITVFNKQ DKEGAQRTVR DFQADYTVRI SAKTTEGLDE LKEMIEAVLR GQKVLIEQLY SYKEAAKIQL IRKYGELTAE EYREDGIFVS AYVPVSIYDK VRSVSLGDSL NNAL // ID C0CXR2_9FIRM Unreviewed; 427 AA. AC C0CXR2; DT 05-MAY-2009, integrated into UniProtKB/TrEMBL. DT 05-MAY-2009, sequence version 1. DT 07-JUN-2017, entry version 49. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:EEG56152.1}; GN ORFNames=CLOSTASPAR_01787 {ECO:0000313|EMBL:EEG56152.1}; OS [Clostridium asparagiforme] DSM 15981. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Lachnospiraceae. OX NCBI_TaxID=518636 {ECO:0000313|EMBL:EEG56152.1, ECO:0000313|Proteomes:UP000004756}; RN [1] {ECO:0000313|EMBL:EEG56152.1, ECO:0000313|Proteomes:UP000004756} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 15981 {ECO:0000313|EMBL:EEG56152.1, RC ECO:0000313|Proteomes:UP000004756}; RA Fulton L., Clifton S., Fulton B., Xu J., Minx P., Pepin K.H., RA Johnson M., Bhonagiri V., Nash W.E., Mardis E.R., Wilson R.K.; RL Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:EEG56152.1, ECO:0000313|Proteomes:UP000004756} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 15981 {ECO:0000313|EMBL:EEG56152.1, RC ECO:0000313|Proteomes:UP000004756}; RA Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., RA Liep D., Gordon J.; RT "Draft genome sequence of Clostridium asparagiforme (DSM 15981)."; RL Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EEG56152.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACCJ01000092; EEG56152.1; -; Genomic_DNA. DR RefSeq; WP_007709148.1; NZ_GG657591.1. DR ProteinModelPortal; C0CXR2; -. DR EnsemblBacteria; EEG56152; EEG56152; CLOSTASPAR_01787. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000004756; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000004756}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000004756}. FT DOMAIN 202 376 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 427 AA; 47560 MW; 3315F484AE353528 CRC64; MAELFDLKEI EERVVLIAVS TGDGDDAEGS LKELAELVKT AGAVTVDKVI QNREKVHPGT YLGKGKIEEV KDLVWELDAT GVVCDDELSP AQLKNLEAAL DTKVMDRTMV ILDIFASRAH TREGKIQVEL AQLKYRAARL VGMRASLSRL GGGIGTRGPG EKKLEVDRRL IHERIGQLKA ELEDVKRHRE VTRQQREQGC AVSAAIVGYT NAGKSTLLNH LTDADILAED KLFATLDPTT RSFTLPGDQQ ILLTDTVGFI RKLPHHLIEA FKSTLEEAKY SDIILHVVDC SNPQMDMQMH VVRETLKDLE IVDKTVVTVF NKTDRLRAMV ESGEAGPLAQ LPRDFSADYQ VRISAKTGEG LDELCGILEQ IIRSRRVHLE KVYPYSQAGR IQTIRKYGQL LKEEYTEDGI AVEAYVPAEL FAKLYAD // ID C0DT38_EIKCO Unreviewed; 394 AA. AC C0DT38; DT 05-MAY-2009, integrated into UniProtKB/TrEMBL. DT 05-MAY-2009, sequence version 1. DT 07-JUN-2017, entry version 40. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:EEG24743.1}; GN ORFNames=EIKCOROL_00515 {ECO:0000313|EMBL:EEG24743.1}; OS Eikenella corrodens ATCC 23834. OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Eikenella. OX NCBI_TaxID=546274 {ECO:0000313|EMBL:EEG24743.1, ECO:0000313|Proteomes:UP000005837}; RN [1] {ECO:0000313|EMBL:EEG24743.1, ECO:0000313|Proteomes:UP000005837} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 23834 {ECO:0000313|EMBL:EEG24743.1, RC ECO:0000313|Proteomes:UP000005837}; RA Fulton L., Clifton S., Chinwalla A.T., Mitreva M., Sodergren E., RA Weinstock G., Clifton S., Dooling D.J., Fulton B., Minx P., RA Pepin K.H., Johnson M., Bhonagiri V., Nash W.E., Mardis E.R., RA Wilson R.K.; RL Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EEG24743.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACEA01000012; EEG24743.1; -; Genomic_DNA. DR RefSeq; WP_003822348.1; NZ_EQ973317.1. DR ProteinModelPortal; C0DT38; -. DR STRING; 546274.EIKCOROL_00515; -. DR EnsemblBacteria; EEG24743; EEG24743; EIKCOROL_00515. DR GeneID; 29690493; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000005837; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000005837}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000005837}. FT DOMAIN 216 385 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 394 AA; 43451 MW; BB27048C834B7593 CRC64; MPRRPPFQPD KSLSRPERVL LVGVMLADSF SGSNEQRARA FQNVLDEAAE LVRAGGGELV HVSTARRDRP SGALFVGSGK AEELAAEVQA HNIELAVFNH ELTPTQERNL EAKLQCRVLD RVGLILAIFA QRAQSQEGRL QVELAQLTHL SGRLVRGYGH LQSQKGGIGL KGPGETQLET DRRLISQKIT TLKKRLADVR RQRATRRKAR QQGSLPTFAL VGYTNTGKSS LFNRLTKADV LAKDQLFATL DTTARRLYLD REHSIILTDT VGFVRDLPHR LVAAFSATLE ETAQADVLLH VADVSQSDYE QRMEDVNRVL AEIGAAEVPQ LLLYNKIDLL PAEQQQPGIL RSKSGQIAAV RLSVTQSLGL EDLRQALIEW ADTHSKASGS KEAS // ID C0EAX6_9FIRM Unreviewed; 439 AA. AC C0EAX6; DT 05-MAY-2009, integrated into UniProtKB/TrEMBL. DT 05-MAY-2009, sequence version 1. DT 07-JUN-2017, entry version 41. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:EEG31444.1}; GN ORFNames=CLOSTMETH_00993 {ECO:0000313|EMBL:EEG31444.1}; OS [Clostridium] methylpentosum DSM 5476. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Ruminococcaceae; OC Ruminiclostridium. OX NCBI_TaxID=537013 {ECO:0000313|EMBL:EEG31444.1, ECO:0000313|Proteomes:UP000003340}; RN [1] {ECO:0000313|EMBL:EEG31444.1, ECO:0000313|Proteomes:UP000003340} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 5476 {ECO:0000313|EMBL:EEG31444.1, RC ECO:0000313|Proteomes:UP000003340}; RA Fulton L., Clifton S., Fulton B., Xu J., Minx P., Pepin K.H., RA Johnson M., Bhonagiri V., Nash W.E., Mardis E.R., Wilson R.K.; RL Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:EEG31444.1, ECO:0000313|Proteomes:UP000003340} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 5476 {ECO:0000313|EMBL:EEG31444.1, RC ECO:0000313|Proteomes:UP000003340}; RA Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., RA Liep D., Gordon J.; RT "Draft genome sequence of Clostridium methylpentosum (DSM 5476)."; RL Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EEG31444.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACEC01000035; EEG31444.1; -; Genomic_DNA. DR ProteinModelPortal; C0EAX6; -. DR STRING; 537013.CLOSTMETH_00993; -. DR EnsemblBacteria; EEG31444; EEG31444; CLOSTMETH_00993. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000003340; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000003340}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000003340}. FT DOMAIN 221 382 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 43 70 {ECO:0000256|SAM:Coils}. FT COILED 180 214 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 439 AA; 48939 MW; 81C42CE413FD329F CRC64; MKFFPFRVII NWKHVQYDKQ GEAMHENTME TTKAVLVSID TGEFDAEQSL KELEELARTA EVEVAGTVTQ RRDAPDSATC IGAGRLDEIK EFCEGNDVDL LIFDLELTAT QTRNIERVTG VRAIDRTTLI LDIFAQRARS REGQIQVELA QQRYRLPRLA GMGVELSRLG GGIGTRGPGE TKLETDKRHI RRRIASLEQE LSQLEKRREM MRTRRKKDNV TSVAIVGYTN AGKSTLLNAL TDAGVLAENK LFATLDPTAR ALELPDGKSV LLIDTVGLIS RLPHHLVEAF KSTLEEAANA DLILHVCDVS NDEVESQVKV VHQLLGELGC GSIPVLTVLN KCDKIPFQPY LSEPDSVMIS AKTGFGFDNL LHKIASSLEQ TSRRMKLLIP YSDTGLIAKI RLEGKIFEER FTDEGTLVDA LVDHKLFDLT APYLIQEDV // ID C0GDR5_9FIRM Unreviewed; 425 AA. AC C0GDR5; DT 05-MAY-2009, integrated into UniProtKB/TrEMBL. DT 05-MAY-2009, sequence version 1. DT 07-JUN-2017, entry version 49. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=DealDRAFT_0478 {ECO:0000313|EMBL:EEG78548.1}; OS Dethiobacter alkaliphilus AHT 1. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Syntrophomonadaceae; OC Dethiobacter. OX NCBI_TaxID=555088 {ECO:0000313|EMBL:EEG78548.1, ECO:0000313|Proteomes:UP000006443}; RN [1] {ECO:0000313|EMBL:EEG78548.1, ECO:0000313|Proteomes:UP000006443} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=AHT 1 {ECO:0000313|EMBL:EEG78548.1, RC ECO:0000313|Proteomes:UP000006443}; RG US DOE Joint Genome Institute (JGI-PGF); RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., RA Tice H., Bruce D., Goodwin L., Pitluck S., Larimer F., Land M.L., RA Hauser L., Muyzer G.; RT "Sequencing of the draft genome and assembly of Dethiobacter RT alkaliphilus AHT 1."; RL Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EEG78548.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACJM01000002; EEG78548.1; -; Genomic_DNA. DR ProteinModelPortal; C0GDR5; -. DR STRING; 555088.DealDRAFT_0478; -. DR EnsemblBacteria; EEG78548; EEG78548; DealDRAFT_0478. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000006443; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000006443}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000006443}. FT DOMAIN 196 362 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 155 192 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 425 AA; 47198 MW; AC70BB6DD9F89442 CRC64; MAQMEKAVLV GLETQDTQWN IEETMHELAL LAETAGAEPV AEIIQKRQRP DSAFYVGKGK AEEIRLIVEE TDAQLVLFDD ELSPSQRRNL EEAVAVRVVD RTALILDIFA QRAKTKEGKL QVELAQLHYL LPRLTGMGVQ LSRLAGGIGT RGPGETKLEV DRRRIRKRIS DLKKEIEEIK KHRTLHRKAR QEVPLPVVTL VGYTNAGKST LLNALTNADV FAEDKLFATL DPTTRQVELP GGSMFLLTDT VGFIQKLPHH LVAAFRATLE EVLEADLLLH VVDTSHPQAA EQMNAVQNIL QQLGAQELPA IVVFNKMDMP EAHANLSALA GEWPEHVAVS AKNKVGLDTL LEAISDNLQK NHVRLDLTLP FGSEKILAII RKYGQLEQEE YKADGIAVRA VMPRPWAEKV KNSLVEGAAE FADDK // ID C0MDJ7_STRS7 Unreviewed; 412 AA. AC C0MDJ7; DT 05-MAY-2009, integrated into UniProtKB/TrEMBL. DT 05-MAY-2009, sequence version 1. DT 30-AUG-2017, entry version 68. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=SZO_07140 {ECO:0000313|EMBL:CAW98827.1}; OS Streptococcus equi subsp. zooepidemicus (strain H70). OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=553483 {ECO:0000313|Proteomes:UP000001368}; RN [1] {ECO:0000313|EMBL:CAW98827.1, ECO:0000313|Proteomes:UP000001368} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=H70 {ECO:0000313|EMBL:CAW98827.1, RC ECO:0000313|Proteomes:UP000001368}; RX PubMed=19325880; DOI=10.1371/journal.ppat.1000346; RA Holden M.T.G., Heather Z., Paillot R., Steward K.F., Webb K., RA Ainslie F., Jourdan T., Bason N.C., Holroyd N.E., Mungall K., RA Quail M.A., Sanders M., Simmonds M., Willey D., Brooks K., RA Aanensen D.M., Spratt B.G., Jolley K.A., Maiden M.C.J., Kehoe M., RA Chanter N., Bentley S.D., Robinson C., Maskell D.J., Parkhill J., RA Waller A.S.; RT "Genomic evidence for the evolution of Streptococcus equi: host RT restriction, increased virulence, and genetic exchange with human RT pathogens."; RL PLoS Pathog. 5:E1000346-E1000346(2009). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; FM204884; CAW98827.1; -; Genomic_DNA. DR RefSeq; WP_012677751.1; NC_012470.1. DR ProteinModelPortal; C0MDJ7; -. DR STRING; 40041.SZO_07140; -. DR EnsemblBacteria; CAW98827; CAW98827; SZO_07140. DR GeneID; 7694162; -. DR KEGG; seq:SZO_07140; -. DR PATRIC; fig|40041.11.peg.762; -. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000001368; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000001368}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000001368}. FT DOMAIN 199 359 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 158 192 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 412 AA; 46812 MW; 7FC3ED6EC3B343BE CRC64; MIETKARQER VILLGVVLEA ADHAELSMTE LASLAKTAGA EVVDCYMQRR ERYDSKTFVG SGKLAEIKEM VAANEIDIVI VNNRLTARQN ANLENALGIK VIDRMQLILD IFAMRARSHE GKLQVHLAQL KYMLPRLVGQ GVMLSRQAGG IGSRGPGESQ LELNRRSIRH QIADIERQLA AVEKNRQTIR DRRISSDAFN IGLIGYTNAG KSTIMNLLTD DKQYEADELF ATLDATTKQI YLQNQFQATL TDTVGFIQDL PTELVAAFKS TLEESRHVDL LLHVIDASDP NHLEHERVVL DILKDLDMLD IPRLAIYNKM DKTASLTATV FPNVRLSARD KNSRSLLRQL LIDQIRDMFE PFSIKLCQDQ AYKCYDLNRL ALLEPYSFDK EIEEISGYIA PKNKWRLEEF YD // ID C0N866_9GAMM Unreviewed; 380 AA. AC C0N866; DT 05-MAY-2009, integrated into UniProtKB/TrEMBL. DT 05-MAY-2009, sequence version 1. DT 07-JUN-2017, entry version 43. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=MDMS009_2339 {ECO:0000313|EMBL:EEF79079.1}; OS Methylophaga thiooxydans DMS010. OC Bacteria; Proteobacteria; Gammaproteobacteria; Thiotrichales; OC Piscirickettsiaceae; Methylophaga. OX NCBI_TaxID=637616 {ECO:0000313|EMBL:EEF79079.1, ECO:0000313|Proteomes:UP000004679}; RN [1] {ECO:0000313|EMBL:EEF79079.1, ECO:0000313|Proteomes:UP000004679} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DMS010 {ECO:0000313|EMBL:EEF79079.1, RC ECO:0000313|Proteomes:UP000004679}; RX PubMed=21478352; DOI=10.1128/JB.00388-11; RA Boden R., Ferriera S., Johnson J., Kelly D.P., Murrell J.C., RA Schafer H.; RT "Draft genome sequence of the chemolithoheterotrophic, halophilic RT methylotroph Methylophaga thiooxydans DMS010."; RL J. Bacteriol. 193:3154-3155(2011). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GG657900; EEF79079.1; -; Genomic_DNA. DR RefSeq; WP_008291806.1; NZ_GG657900.1. DR ProteinModelPortal; C0N866; -. DR STRING; 637616.MDMS009_2339; -. DR EnsemblBacteria; EEF79079; EEF79079; MDMS009_2339. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR Proteomes; UP000004679; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000004679}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000004679}. FT DOMAIN 207 374 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 173 200 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 380 AA; 43088 MW; 6FA20686EDE5F4A7 CRC64; MFDRPDSNAA FDDLSDKEAV VLVHLNFNDP DYDESQMEFK ELVGSTGANI AALVEGKRHR PDPKYFAGSG KVDEVAEFVH ASHAALVIFN HELSPSQERN LEHKLKCRVL GRTGLILDIF ARRARSHEGK LQVELAQLQH LSTRLIRGWT HLERQKGGIG MRGPGETQLE TDRRLLGQRI KTLKKKLDKV RSQREQGRRS RQRGGVPVVS LVGYTNMGKS TLFNKVTSAE VYADDRLFAT LDPTLRRVKL HDTEMLILAD TVGFIRDLPH DLVESFSSTL EETRDAALLL HVVDCASGDR EELIHHVNDV LKQIEAHELP QLIIYNKIDN VDGMKPRIER NADGNIHRIW LSAKSGEGLE LLRQALQEYF PQQDQSDYLN // ID C0QBU9_DESAH Unreviewed; 552 AA. AC C0QBU9; DT 05-MAY-2009, integrated into UniProtKB/TrEMBL. DT 05-MAY-2009, sequence version 1. DT 07-JUN-2017, entry version 64. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=HRM2_18590 {ECO:0000313|EMBL:ACN14961.1}; OS Desulfobacterium autotrophicum (strain ATCC 43914 / DSM 3382 / HRM2). OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfobacterales; OC Desulfobacteraceae; Desulfobacterium. OX NCBI_TaxID=177437 {ECO:0000313|EMBL:ACN14961.1, ECO:0000313|Proteomes:UP000000442}; RN [1] {ECO:0000313|EMBL:ACN14961.1, ECO:0000313|Proteomes:UP000000442} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43914 / DSM 3382 / HRM2 RC {ECO:0000313|Proteomes:UP000000442}; RX PubMed=19187283; DOI=10.1111/j.1462-2920.2008.01825.x; RA Strittmatter A.W., Liesegang H., Rabus R., Decker I., Amann J., RA Andres S., Henne A., Fricke W.F., Martinez-Arias R., Bartels D., RA Goesmann A., Krause L., Puehler A., Klenk H.P., Richter M., RA Schuler M., Gloeckner F.O., Meyerdierks A., Gottschalk G., Amann R.; RT "Genome sequence of Desulfobacterium autotrophicum HRM2, a marine RT sulfate reducer oxidizing organic carbon completely to carbon RT dioxide."; RL Environ. Microbiol. 11:1038-1055(2009). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001087; ACN14961.1; -; Genomic_DNA. DR RefSeq; WP_015903747.1; NC_012108.1. DR ProteinModelPortal; C0QBU9; -. DR STRING; 177437.HRM2_18590; -. DR EnsemblBacteria; ACN14961; ACN14961; HRM2_18590. DR KEGG; dat:HRM2_18590; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; EREVIIT; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000000442; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000000442}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000000442}. FT DOMAIN 387 551 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 552 AA; 62095 MW; A87A5567428B2C4E CRC64; MKKIFGSTTG LSAHQIKALE NLYLFNTTPE DLISRDQLDA LIAVSTDIRR QVGVLIARNG KTVHVIAGEP HRIVIPDTPD FRTLPGRLKG LRCIHTHLNE TDLTRDDLTD LALLRLDFMA AVSIFTPKGI GKTDQNRTPP ITIYSSHILP GDGDEPCAPM APLSKDDLNI GCLERILAIE DELARQDASY TVETGEEKAL LINIFTDQVK DAVASLDELK ELCRSSNIKV LDTALQRRKK IDPKFVVGRG KLADLVIRAL QKHATMLVFD RELNPSQIRS ITDFVEMKVI DRTQLILDIF ARRAKSREGK LQVELAQMKY LLPRLATKNT AMSRLTGGIG GRGPGETKLE INRRRVRDRI TRLSKDISKI RKQRSQQRSQ RNRRGIPVIS IVGYTNAGKS TLLNTLTKSE IIAENRLFAT LDPSSRRLRF PKDLEVIITD TVGFIQDLPE ELMEAFHATL EELEDADILL HVVDISNPRY EQQMGSVERI LKELGLEKTP VLYVFNKQDK IALADFDNPW LLNQGSLVSA TRPETLKPLV SRLESMIRQQ TG // ID C0QJL7_DESAH Unreviewed; 486 AA. AC C0QJL7; DT 05-MAY-2009, integrated into UniProtKB/TrEMBL. DT 05-MAY-2009, sequence version 1. DT 07-JUN-2017, entry version 56. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:ACN13870.1}; GN OrderedLocusNames=HRM2_07560 {ECO:0000313|EMBL:ACN13870.1}; OS Desulfobacterium autotrophicum (strain ATCC 43914 / DSM 3382 / HRM2). OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfobacterales; OC Desulfobacteraceae; Desulfobacterium. OX NCBI_TaxID=177437 {ECO:0000313|EMBL:ACN13870.1, ECO:0000313|Proteomes:UP000000442}; RN [1] {ECO:0000313|EMBL:ACN13870.1, ECO:0000313|Proteomes:UP000000442} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43914 / DSM 3382 / HRM2 RC {ECO:0000313|Proteomes:UP000000442}; RX PubMed=19187283; DOI=10.1111/j.1462-2920.2008.01825.x; RA Strittmatter A.W., Liesegang H., Rabus R., Decker I., Amann J., RA Andres S., Henne A., Fricke W.F., Martinez-Arias R., Bartels D., RA Goesmann A., Krause L., Puehler A., Klenk H.P., Richter M., RA Schuler M., Gloeckner F.O., Meyerdierks A., Gottschalk G., Amann R.; RT "Genome sequence of Desulfobacterium autotrophicum HRM2, a marine RT sulfate reducer oxidizing organic carbon completely to carbon RT dioxide."; RL Environ. Microbiol. 11:1038-1055(2009). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001087; ACN13870.1; -; Genomic_DNA. DR RefSeq; WP_012663114.1; NC_012108.1. DR ProteinModelPortal; C0QJL7; -. DR STRING; 177437.HRM2_07560; -. DR EnsemblBacteria; ACN13870; ACN13870; HRM2_07560. DR KEGG; dat:HRM2_07560; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; VILEIFH; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000000442; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 2. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000000442}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Hydrolase {ECO:0000313|EMBL:ACN13870.1}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000000442}. FT DOMAIN 268 433 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 486 AA; 54038 MW; 00032D8277CF14F0 CRC64; MDSNGTIKTT FLIKYGWSSK KMIEQSNDER EKKTAVLFSV QTYGVSDEEN DSSLLELGRL VKTMGLEVVA TLTQRRPKPE TSTLLGAGKL KELADYTGGT GIVEGFSRKS EDETRDDMDE AYPSGSPTGI YENRSNDDPM AKNSVHANVV IYDGEITTKQ LQNLEKATGV EVLDRTGVIL EIFSRHAKSR EALIQVEIAK LTYLAPRLRA SHMGGDRQGG GIGSKGAGET SHELDKRRIR DRISELKSRL VSIRDEQTRR RSRRRENFQV ALVGYTNAGK SSLMRKLTGS DVLVEDKLFA TLDTRVKALQ PEAYPPILIS DTVGFIKKLP HDLVASFQST LDEALAASLL LFTVDASDPA FRSQLTVTQS VLKEIGGEKI PGLLILNKID KLTTGALEVL RHEFPHGIFI SAHNPKDVAL LRKKILQHFQ ENMIETTMVI PYDKGHILGQ LRTKAGIIQE SYDETGTEVK FKTSQETLTW LEKQMA // ID C0QUG4_PERMH Unreviewed; 373 AA. AC C0QUG4; DT 05-MAY-2009, integrated into UniProtKB/TrEMBL. DT 05-MAY-2009, sequence version 1. DT 07-JUN-2017, entry version 64. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:ACO03106.1}; GN OrderedLocusNames=PERMA_0540 {ECO:0000313|EMBL:ACO03106.1}; OS Persephonella marina (strain DSM 14350 / EX-H1). OC Bacteria; Aquificae; Aquificales; Hydrogenothermaceae; Persephonella. OX NCBI_TaxID=123214 {ECO:0000313|EMBL:ACO03106.1, ECO:0000313|Proteomes:UP000001366}; RN [1] {ECO:0000313|EMBL:ACO03106.1, ECO:0000313|Proteomes:UP000001366} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 14350 / EX-H1 {ECO:0000313|Proteomes:UP000001366}; RX PubMed=19136599; DOI=10.1128/JB.01645-08; RA Reysenbach A.-L., Hamamura N., Podar M., Griffiths E., Ferreira S., RA Hochstein R., Heidelberg J., Johnson J., Mead D., Pohorille A., RA Sarmiento M., Schweighofer K., Seshadri R., Voytek M.A.; RT "Complete and draft genome sequences of six members of the RT Aquificales."; RL J. Bacteriol. 191:1992-1993(2009). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001230; ACO03106.1; -; Genomic_DNA. DR RefSeq; WP_012675345.1; NC_012440.1. DR ProteinModelPortal; C0QUG4; -. DR STRING; 123214.PERMA_0540; -. DR EnsemblBacteria; ACO03106; ACO03106; PERMA_0540. DR KEGG; pmx:PERMA_0540; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000001366; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000001366}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000001366}. FT DOMAIN 195 320 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 373 AA; 42082 MW; A00F36F48B00892A CRC64; MRCILVGIKT KEKKDKELKQ SLSELEGLVE AVEGVTLGKL YQKKDIPDPS TFIGKGKVKQ LKELIEGTKA DTVVFDADLT PVQITNIEKI TQANVLDRTD LILQIFSQRA KTRQAKLQVE LATLQHELPR VYGQKGKALS RIGGGMKTKG AGEKIGEIKV RTIKDRISKI KKELEKIKKQ RYQQRKWRNK DPNILKVSLV GYTNAGKSTL LKKLTKRDTF VSDQLFATLD TKTSYIAFPD IGKKVLITDT VGFVKNMPKE LMDAFMATLE ELEDADLILH VIDISDENWV EKMEAVEDIL KKINVSDKPL VVVLNKIDKL VPSPEYIEEA DHTMLTGDRE TVVISTEKGW NIDKLHNILR KYALRKDTVS VGG // ID C0QXG9_BRAHW Unreviewed; 370 AA. AC C0QXG9; DT 05-MAY-2009, integrated into UniProtKB/TrEMBL. DT 05-MAY-2009, sequence version 1. DT 07-JUN-2017, entry version 67. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=BHWA1_00327 {ECO:0000313|EMBL:ACN82827.1}; OS Brachyspira hyodysenteriae (strain ATCC 49526 / WA1). OC Bacteria; Spirochaetes; Brachyspirales; Brachyspiraceae; Brachyspira. OX NCBI_TaxID=565034 {ECO:0000313|EMBL:ACN82827.1, ECO:0000313|Proteomes:UP000001803}; RN [1] {ECO:0000313|EMBL:ACN82827.1, ECO:0000313|Proteomes:UP000001803} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 49526 / WA1 {ECO:0000313|Proteomes:UP000001803}; RX PubMed=19262690; DOI=10.1371/journal.pone.0004641; RA Bellgard M.I., Wanchanthuek P., La T., Ryan K., Moolhuijzen P., RA Albertyn Z., Shaban B., Motro Y., Dunn D.S., Schibeci D., Hunter A., RA Barrero R., Phillips N.D., Hampson D.J.; RT "Genome sequence of the pathogenic intestinal spirochete Brachyspira RT hyodysenteriae reveals adaptations to its lifestyle in the porcine RT large intestine."; RL PLoS ONE 4:E4641-E4641(2009). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001357; ACN82827.1; -; Genomic_DNA. DR RefSeq; WP_012669880.1; NC_012225.1. DR ProteinModelPortal; C0QXG9; -. DR STRING; 565034.BHWA1_00327; -. DR EnsemblBacteria; ACN82827; ACN82827; BHWA1_00327. DR KEGG; bhy:BHWA1_00327; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000001803; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000001803}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000001803}. FT DOMAIN 201 368 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 162 189 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 370 AA; 41770 MW; 1BD1C321E53C5BD4 CRC64; MNNDNLKKAY IIFVTDSRQY RNSKINIDNI LNELAMLCDT AGYEVVNKYS FIQPKITAGT YIGTGKLESL KESAAIDNVE YFIFDNELSG SQVNAIEEGS NITALTRTEI ILEIFALRAK TMTAKMQVEL AFLEFEYPRL KGKRTNLSQI KGGIGLRGGA GEKQLEYDRR RARERIHKLK SQLSKVEKSA STGRKGRENT FRIAIVGYTN AGKSTLFNLL CKESVYVEDK LFATLDTHTR KLYLTDDTPV EVIISDTVGF IDRLPHTLVA SFKSTLSEVV EADLLLHLSD ASDENIEEKL LHVESIIKEI DASHIKRIVI FNKSDSIDEV QKNKILTSYD DAIFISAKNN TNIELLRKKI LDTILELNNN // ID C0W0F3_9ACTO Unreviewed; 543 AA. AC C0W0F3; DT 26-MAY-2009, integrated into UniProtKB/TrEMBL. DT 26-MAY-2009, sequence version 1. DT 05-JUL-2017, entry version 50. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:EEH64012.1}; GN ORFNames=HMPREF0044_1031 {ECO:0000313|EMBL:EEH64012.1}; OS Actinomyces coleocanis DSM 15436. OC Bacteria; Actinobacteria; Actinomycetales; Actinomycetaceae; OC Actinomyces. OX NCBI_TaxID=525245 {ECO:0000313|EMBL:EEH64012.1, ECO:0000313|Proteomes:UP000010301}; RN [1] {ECO:0000313|EMBL:EEH64012.1, ECO:0000313|Proteomes:UP000010301} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 15436 {ECO:0000313|EMBL:EEH64012.1, RC ECO:0000313|Proteomes:UP000010301}; RA Qin X., Bachman B., Battles P., Bell A., Bess C., Bickham C., RA Chaboub L., Chen D., Coyle M., Deiros D.R., Dinh H., Forbes L., RA Fowler G., Francisco L., Fu Q., Gubbala S., Hale W., Han Y., RA Hemphill L., Highlander S.K., Hirani K., Hogues M., Jackson L., RA Jakkamsetti A., Javaid M., Jiang H., Korchina V., Kovar C., Lara F., RA Lee S., Mata R., Mathew T., Moen C., Morales K., Munidasa M., RA Nazareth L., Ngo R., Nguyen L., Okwuonu G., Ongeri F., Patil S., RA Petrosino J., Pham C., Pham P., Pu L.-L., Puazo M., Raj R., Reid J., RA Rouhana J., Saada N., Shang Y., Simmons D., Thornton R., Warren J., RA Weissenberger G., Zhang J., Zhang L., Zhou C., Zhu D., Muzny D., RA Worley K., Gibbs R.; RL Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EEH64012.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACFG01000030; EEH64012.1; -; Genomic_DNA. DR ProteinModelPortal; C0W0F3; -. DR STRING; 525245.HMPREF0044_1031; -. DR EnsemblBacteria; EEH64012; EEH64012; HMPREF0044_1031. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000010301; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 2. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000010301}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000010301}. FT DOMAIN 316 482 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 543 AA; 58706 MW; BAC15553FD575B54 CRC64; MTENLNPHAD LDQAKAVVDR VLERQKQGVK KLVHTADSSA LIEGLAETHS ENLEGGQVMP KRGGVFANRA ASLQSTQGQV ENSAGAMERE ARQATRRVAS MSTELEDVSE VEYRQIRLEK VVLVGIYATD VEDAENSLHE LAALAETAGS EVLDGMLQRR DMPDPATYLG KGKAKELAEI VADCGADTVI VDGELAPSQR RGLEDAVKVK VVDRTALILD IFAQHAQSRE GKAQVELAQL EYLLPRLRGW GESMSRQAGG RVAGGEGIGS RGPGETKIEL DRRRIRKRMS KLRNEIAAMK PARDTQRQSR RSGEIPSVAI AGYTNAGKST LLNRLTGAEV MVQNALFATL DPTVRQTKTD DGRLYTLTDT VGFVRNLPTQ LVEAFRSTLE EVGDADLIVH VVDAAHPDPM GQIKAVHAVF ETIDGAMEIP EIIALNKADL ATEADLAVLR SLLPNSVAVS AHTGAGMGDL QELIAQMLPR PSVKVDVVVP YAHGDLVHRF HNDGEIELEE YLPEGTHLVG LVSQALAYDL NRVAVATDSG NAE // ID C0W2Q2_9ACTO Unreviewed; 553 AA. AC C0W2Q2; DT 26-MAY-2009, integrated into UniProtKB/TrEMBL. DT 26-MAY-2009, sequence version 1. DT 07-JUN-2017, entry version 41. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:EEH66983.1}; GN ORFNames=HMPREF0058_0146 {ECO:0000313|EMBL:EEH66983.1}; OS Actinomyces urogenitalis DSM 15434. OC Bacteria; Actinobacteria; Actinomycetales; Actinomycetaceae; OC Actinomyces. OX NCBI_TaxID=525246 {ECO:0000313|EMBL:EEH66983.1, ECO:0000313|Proteomes:UP000004778}; RN [1] {ECO:0000313|EMBL:EEH66983.1, ECO:0000313|Proteomes:UP000004778} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 15434 {ECO:0000313|EMBL:EEH66983.1, RC ECO:0000313|Proteomes:UP000004778}; RA Qin X., Bachman B., Battles P., Bell A., Bess C., Bickham C., RA Chaboub L., Chen D., Coyle M., Deiros D.R., Dinh H., Forbes L., RA Fowler G., Francisco L., Fu Q., Gubbala S., Hale W., Han Y., RA Hemphill L., Highlander S.K., Hirani K., Hogues M., Jackson L., RA Jakkamsetti A., Javaid M., Jiang H., Korchina V., Kovar C., Lara F., RA Lee S., Mata R., Mathew T., Moen C., Morales K., Munidasa M., RA Nazareth L., Ngo R., Nguyen L., Okwuonu G., Ongeri F., Patil S., RA Petrosino J., Pham C., Pham P., Pu L.-L., Puazo M., Raj R., Reid J., RA Rouhana J., Saada N., Shang Y., Simmons D., Thornton R., Warren J., RA Weissenberger G., Zhang J., Zhang L., Zhou C., Zhu D., Muzny D., RA Worley K., Gibbs R.; RL Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EEH66983.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACFH01000008; EEH66983.1; -; Genomic_DNA. DR ProteinModelPortal; C0W2Q2; -. DR STRING; 525246.HMPREF0058_0146; -. DR EnsemblBacteria; EEH66983; EEH66983; HMPREF0058_0146. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000004778; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000004778}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000004778}. FT DOMAIN 314 480 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 553 AA; 58491 MW; 6B11CE8E11C2ECEA CRC64; MTDRTDNHTT DTHIAAHAGP GTEAPSAEDI VNRILSRHGT ALASTAGDHT RHDLADDGAL EREARAATRR VASLTTELED VSEVEYRQIR LEKVVLVGLE LPAARPAATT GAAASPSSRH GSALEAADAQ DAETSLAELA ALAETAGSQV LDALIQKRDH PDPATYLGSG KAKELAEMVA AAGADTVIVD GDLAPSQRRA LEDVVRVKVV DRTALILDIF AQHAKSREGK AQVELAQLEY LLPRLRGWGE SMSRQAGGRV AGGQGIGSRG PGETKIELDR RRIRDRMAKL RREIKAMAPS REVKRGSRRR GPIPSVAIAG YTNAGKSSLM NRLTDAGLMV QDALFATLDP TVRKAETSDG RLYTLTDTVG FVRNLPHELI EAFRSTLEEV AGADVLVHVV DAAHPDPLSQ IAAVRAVLAE IPGALEVPEL IVLNKADLAD AVTLAALRTR LPEAVIVSAA TGEGLDELRS RIEEMLPRPD VPVDLVIPYS RGDLVAKVHA DGEIDAIEYV EAGTRVRGRV DAPLAAELRA AAVAEPEPAA GASEPGPAGS AGR // ID C0XSJ5_9CORY Unreviewed; 496 AA. AC C0XSJ5; DT 26-MAY-2009, integrated into UniProtKB/TrEMBL. DT 26-MAY-2009, sequence version 1. DT 07-JUN-2017, entry version 40. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:EEI16794.1}; GN ORFNames=HMPREF0298_1415 {ECO:0000313|EMBL:EEI16794.1}; OS Corynebacterium lipophiloflavum DSM 44291. OC Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae; OC Corynebacterium. OX NCBI_TaxID=525263 {ECO:0000313|EMBL:EEI16794.1, ECO:0000313|Proteomes:UP000006196}; RN [1] {ECO:0000313|EMBL:EEI16794.1, ECO:0000313|Proteomes:UP000006196} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 44291 {ECO:0000313|EMBL:EEI16794.1, RC ECO:0000313|Proteomes:UP000006196}; RA Qin X., Bachman B., Battles P., Bell A., Bess C., Bickham C., RA Chaboub L., Chen D., Coyle M., Deiros D.R., Dinh H., Forbes L., RA Fowler G., Francisco L., Fu Q., Gubbala S., Hale W., Han Y., RA Hemphill L., Highlander S.K., Hirani K., Hogues M., Jackson L., RA Jakkamsetti A., Javaid M., Jiang H., Korchina V., Kovar C., Lara F., RA Lee S., Mata R., Mathew T., Moen C., Morales K., Munidasa M., RA Nazareth L., Ngo R., Nguyen L., Okwuonu G., Ongeri F., Patil S., RA Petrosino J., Pham C., Pham P., Pu L.-L., Puazo M., Raj R., Reid J., RA Rouhana J., Saada N., Shang Y., Simmons D., Thornton R., Warren J., RA Weissenberger G., Zhang J., Zhang L., Zhou C., Zhu D., Muzny D., RA Worley K., Gibbs R.; RL Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EEI16794.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACHJ01000115; EEI16794.1; -; Genomic_DNA. DR RefSeq; WP_006840142.1; NZ_GG667192.1. DR ProteinModelPortal; C0XSJ5; -. DR STRING; 525263.HMPREF0298_1415; -. DR EnsemblBacteria; EEI16794; EEI16794; HMPREF0298_1415. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000006196; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000006196}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000006196}. FT DOMAIN 269 442 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 496 AA; 54502 MW; 229F2395EE089045 CRC64; MTEPIELNHD ELLARAFRHN APQPTDNGEP TVGSLDLEER NAFRRVTVET ELRSEDQAEG FEVEYRKLRL EQVILVGAWI EGTTAEMEAN MLELAALAET AGADVVELLY QKRDKPDPGT YIGSGKVKEL RDIVVSTGAD TVVFDGELSP GQMVALEEAL KIKVIDRTML ILDIFAQHAK SKEGKAQVSL AQMEYLYTRT RGWGGNLSRQ AGGRAGSNGG VGLRGPGETR IEADRRRLRT DMAKLRHELR GMKTAREVKR ARRQRSTIPK IAIAGYTNAG KSSLINAMTN AGVLVEDALF ATLDPSTRKA QLADGRNVVL TDTVGFVRHL PTQLVEAFKS TLEEVTGADL MLHVVDGSDA FPLKQIEAVN KVLSDVTRES GESIPPEIVV VNKIDQADPV VLAELRHTFD NTGHDVVFVS AHTGEGIAEL EGKIEMHLNS VEAHVQMLVP FTRGDVVSRV HEQGTVRSES YEEDGTLIDV RLPHVIAEQY SEFVVS // ID C0ZEX4_BREBN Unreviewed; 430 AA. AC C0ZEX4; DT 26-MAY-2009, integrated into UniProtKB/TrEMBL. DT 26-MAY-2009, sequence version 1. DT 07-JUN-2017, entry version 58. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:BAH44333.1}; GN Synonyms=ynbA {ECO:0000313|EMBL:BAH44333.1}; GN OrderedLocusNames=BBR47_33560 {ECO:0000313|EMBL:BAH44333.1}; OS Brevibacillus brevis (strain 47 / JCM 6285 / NBRC 100599). OC Bacteria; Firmicutes; Bacilli; Bacillales; Paenibacillaceae; OC Brevibacillus. OX NCBI_TaxID=358681 {ECO:0000313|EMBL:BAH44333.1, ECO:0000313|Proteomes:UP000001877}; RN [1] {ECO:0000313|EMBL:BAH44333.1, ECO:0000313|Proteomes:UP000001877} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=47 / JCM 6285 / NBRC 100599 RC {ECO:0000313|Proteomes:UP000001877}; RA Hosoyama A., Yamada R., Hongo Y., Terui Y., Ankai A., Masuyama W., RA Sekiguchi M., Takeda T., Asano K., Ohji S., Ichikawa N., Narita S., RA Aoki N., Miura H., Matsushita S., Sekigawa T., Yamagata H., RA Yoshikawa H., Udaka S., Tanikawa S., Fujita N.; RT "Brevibacillus brevis strain 47, complete genome."; RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AP008955; BAH44333.1; -; Genomic_DNA. DR RefSeq; WP_015891643.1; NC_012491.1. DR ProteinModelPortal; C0ZEX4; -. DR STRING; 358681.BBR47_33560; -. DR EnsemblBacteria; BAH44333; BAH44333; BBR47_33560. DR GeneID; 29260618; -. DR KEGG; bbe:BBR47_33560; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000001877; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000001877}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000001877}. FT DOMAIN 201 363 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 160 194 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 430 AA; 48911 MW; 37511D838C0F9A90 CRC64; MNDLIKTQET AILVGCYLDN RDEERTRLSM EELHELADTA GVEVLDVITQ NRDRVDSAWY LGTGKIDEIA QRAEELDVDV IIFNDELSPS QTRNLDKVFD CKVIDRTQLI LDIFAGRAQS REGKIQVELA QYNYLLPRLA GQGKQLSRLG GGIGTRGPGE TKLESDRRHI RKRISELKQQ LEDTVRTRQL HRERRKKNNV FQIALVGYTN AGKSTILNKL TNANTLQEDK LFATLDPTTR QLELPSGLDV LLTDTVGFIQ DLPTSLVAAF RSTLEGVKEA DLILHVVDSH HPDFQVHMEV VDKILRELKA EEIPHLVVFN KADMLTEGSY LPRADESILI SAMREDDLKQ LLTRIESFAL QSFNAMKLRV PVERGDILSL LHRDGVEMEQ EFNEEEAAYL ITVRVNKDNP IYGRIAPFLL DKPETVEESW // ID C0ZYN9_RHOE4 Unreviewed; 491 AA. AC C0ZYN9; DT 26-MAY-2009, integrated into UniProtKB/TrEMBL. DT 26-MAY-2009, sequence version 1. DT 30-AUG-2017, entry version 60. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:BAH33474.1}; GN OrderedLocusNames=RER_27660 {ECO:0000313|EMBL:BAH33474.1}; OS Rhodococcus erythropolis (strain PR4 / NBRC 100887). OC Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae; OC Rhodococcus. OX NCBI_TaxID=234621 {ECO:0000313|EMBL:BAH33474.1, ECO:0000313|Proteomes:UP000002204}; RN [1] {ECO:0000313|Proteomes:UP000002204} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=PR4 / NBRC 100887 {ECO:0000313|Proteomes:UP000002204}; RA Takarada H., Sekine M., Hosoyama A., Yamada R., Fujisawa T., Omata S., RA Shimizu A., Tsukatani N., Tanikawa S., Fujita N., Harayama S.; RT "Comparison of the complete genome sequences of Rhodococcus RT erythropolis PR4 and Rhodococcus opacus B4."; RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:BAH33474.1, ECO:0000313|Proteomes:UP000002204} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=PR4 / NBRC 100887 {ECO:0000313|Proteomes:UP000002204}; RX PubMed=16423019; DOI=10.1111/j.1462-2920.2005.00899.x; RA Sekine M., Tanikawa S., Omata S., Saito M., Fujisawa T., Tsukatani N., RA Tajima T., Sekigawa T., Kosugi H., Matsuo Y., Nishiko R., Imamura K., RA Ito M., Narita H., Tago S., Fujita N., Harayama S.; RT "Sequence analysis of three plasmids harboured in Rhodococcus RT erythropolis strain PR4."; RL Environ. Microbiol. 8:334-346(2006). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AP008957; BAH33474.1; -; Genomic_DNA. DR RefSeq; WP_003942213.1; NC_012490.1. DR ProteinModelPortal; C0ZYN9; -. DR STRING; 234621.RER_27660; -. DR EnsemblBacteria; BAH33474; BAH33474; RER_27660. DR KEGG; rer:RER_27660; -. DR PATRIC; fig|234621.6.peg.3257; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000002204; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 2. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000002204}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000002204}. FT DOMAIN 267 436 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 226 260 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 491 AA; 53174 MW; 1A355AAD471CA812 CRC64; MTNTHENEES TAHEQSEYAQ AEYTAASASG NPSTGEMQLA DRGALRRVAG LSTELEDVTE VEYRQLRLER VVLVGVWTQG TAEQAEASMT ELAALAETAG SEVLEGLVQR RDKPDAATYI GSGKAQELRE VVLATGADTV VCDGELTPAQ LTALEKIVKV KVIDRTALIL DIFAQHATSR EGKAQVAFAQ MEYMLPRLRG WGESMSRQAG GRAGSNGGVG LRGPGETKIE TDRRRIRERM AKLRREIKGM KAARDTKRTR RLQSDIPSIA IVGYTNAGKS SLLNSLTGSG VLVENALFAT LDPTTRRAAL DDGREYVLTD TVGFVRHLPT QLVEAFRSTL EEVTDADLLL HVVDGSDPLP TEQIKAVREV VTDVLRETDS KAPPELIVVN KIDAADPVTL TQLRGLLPGA VFVSARTGEG IAELRAHLSE VLVRPEVEVD VLVPYTRGDL MARIHSDGTI LESTHEEAGT RVHARVPQML ASALVEYAPS A // ID C1A4C4_GEMAT Unreviewed; 394 AA. AC C1A4C4; DT 26-MAY-2009, integrated into UniProtKB/TrEMBL. DT 26-MAY-2009, sequence version 1. DT 07-JUN-2017, entry version 48. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=GAU_1907 {ECO:0000313|EMBL:BAH38949.1}; OS Gemmatimonas aurantiaca (strain T-27 / DSM 14586 / JCM 11422 / NBRC OS 100505). OC Bacteria; Gemmatimonadetes; Gemmatimonadales; Gemmatimonadaceae; OC Gemmatimonas. OX NCBI_TaxID=379066 {ECO:0000313|EMBL:BAH38949.1, ECO:0000313|Proteomes:UP000002209}; RN [1] {ECO:0000313|Proteomes:UP000002209} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=T-27 / DSM 14586 / JCM 11422 / NBRC 100505 RC {ECO:0000313|Proteomes:UP000002209}; RA Takasaki K., Ichikawa N., Miura H., Matsushita S., Watanabe Y., RA Oguchi A., Ankai A., Yashiro I., Takahashi M., Terui Y., Fukui S., RA Yokoyama H., Tanikawa S., Hanada S., Kamagata Y., Fujita N.; RT "Complete genome sequence of Gemmatimonas aurantiaca T-27 that RT represents a novel phylum Gemmatimonadetes."; RL Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AP009153; BAH38949.1; -; Genomic_DNA. DR ProteinModelPortal; C1A4C4; -. DR STRING; 379066.GAU_1907; -. DR EnsemblBacteria; BAH38949; BAH38949; GAU_1907. DR KEGG; gau:GAU_1907; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000002209; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000002209}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000002209}. FT DOMAIN 156 326 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 394 AA; 44331 MW; 9F807891CBEF1D27 CRC64; MVGTLTQQLD RPHPATYLGT GKVEELKLRI QELGATLVIF DDELTPAQGK NIELIVNTRV MDRAELILDI FATRARSSEA RMQVELAQLE YMLPRLTRMW THLEKMRGGI GMRGPGETQL ETDRRLIQHR IRVLKERLAD VERAREIQRQ GRRSQFRVSL VGYTNAGKSS VLRTLANDGE VFVEDRLFAT LDPLTREVEV GDGYTVLLTD TVGFIRKLPH HLVASFRATL AEAREADLLL HVIDASHPTW EEHRDVVDGV LTDLGLSGRP MRYVMNKMDA VPEELDAGVR ARVANLMPDS LFVSALEPGG LEGLRTELRE SLKRSRPVLE VRIPASNGRL IAEVHRDGEV LEQRTDEELI VIRARLDERA IGRLRQAGVS VTVTQAARPF ANTP // ID C1CXH6_DEIDV Unreviewed; 569 AA. AC C1CXH6; DT 26-MAY-2009, integrated into UniProtKB/TrEMBL. DT 26-MAY-2009, sequence version 1. DT 07-JUN-2017, entry version 55. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:ACO46893.1}; GN OrderedLocusNames=Deide_19040 {ECO:0000313|EMBL:ACO46893.1}; OS Deinococcus deserti (strain VCD115 / DSM 17065 / LMG 22923). OC Bacteria; Deinococcus-Thermus; Deinococci; Deinococcales; OC Deinococcaceae; Deinococcus. OX NCBI_TaxID=546414 {ECO:0000313|EMBL:ACO46893.1, ECO:0000313|Proteomes:UP000002208}; RN [1] {ECO:0000313|EMBL:ACO46893.1, ECO:0000313|Proteomes:UP000002208} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=VCD115 / DSM 17065 / LMG 22923 RC {ECO:0000313|Proteomes:UP000002208}; RX PubMed=19370165; DOI=10.1371/journal.pgen.1000434; RA de Groot A., Dulermo R., Ortet P., Blanchard L., Guerin P., RA Fernandez B., Vacherie B., Dossat C., Jolivet E., Siguier P., RA Chandler M., Barakat M., Dedieu A., Barbe V., Heulin T., Sommer S., RA Achouak W., Armengaud J.; RT "Alliance of proteomics and genomics to unravel the specificities of RT Sahara bacterium Deinococcus deserti."; RL PLoS Genet. 5:E1000434-E1000434(2009). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001114; ACO46893.1; -; Genomic_DNA. DR RefSeq; WP_012694014.1; NC_012526.1. DR ProteinModelPortal; C1CXH6; -. DR STRING; 546414.Deide_19040; -. DR PaxDb; C1CXH6; -. DR EnsemblBacteria; ACO46893; ACO46893; Deide_19040. DR KEGG; ddr:Deide_19040; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; EREVIIT; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000002208; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000002208}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000002208}. FT DOMAIN 382 550 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 341 375 {ECO:0000256|SAM:Coils}. FT COILED 536 563 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 569 AA; 62402 MW; 802A621A777C1CC1 CRC64; MHGNTSGLRP SQLKALGNLY RRRIEPGRIG SPELARNLAE LSHDVRREVG VLIDRRGRVI SVSVADAKAT EFPDLRMGEN RLAGFHLLHA HPKGGPLSKG DLSTLFLKRL DAVSAVEVRQ EGQPGLVHTA HLTPPGTIGE EEDWRILPPV SSHQIDEFDL GAQVSALEEE IARAAVGRES KKDRERAILV QIDQGEFDAE ERLDELAELA RTAGAEVVHK ELVYRRNLKA GTLVGAGKLE ELTSRAYHLD ADLLIFGQEL GPAQAREIEA ATGLKILDRT QLILDIFALH AQGVESRLQV ELAQLRYMKP RLLGAGAALS RIGGSAGSSA GGAIGTRGPG ETKLELDRRR INDRLSFLEK QLENVSQRRE ERRKSRERND VPVVSIVGYT NAGKSTLLNT FTHAAEEPRR VLAENKLFAT LRPTSRQGFI HGVGPVVLTD TVGFIRDLPK DLTRAFRSTL EEIGDADVLL HVVDAASPGA DTRLDAVNRI LEELGFRDMP TVVALNKADA ADPEQLAREV ERTDGIAVSA LRNIGLAELK EALADAIGQV QRAELAQREE ERERSAQYR // ID C1DD50_LARHH Unreviewed; 284 AA. AC C1DD50; DT 26-MAY-2009, integrated into UniProtKB/TrEMBL. DT 26-MAY-2009, sequence version 1. DT 07-JUN-2017, entry version 61. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:ACO73685.1}; GN OrderedLocusNames=LHK_00692 {ECO:0000313|EMBL:ACO73685.1}; OS Laribacter hongkongensis (strain HLHK9). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Chromobacteriaceae; Laribacter. OX NCBI_TaxID=557598 {ECO:0000313|EMBL:ACO73685.1, ECO:0000313|Proteomes:UP000002010}; RN [1] {ECO:0000313|EMBL:ACO73685.1, ECO:0000313|Proteomes:UP000002010} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=HLHK9 {ECO:0000313|EMBL:ACO73685.1, RC ECO:0000313|Proteomes:UP000002010}; RX PubMed=19283063; DOI=10.1371/journal.pgen.1000416; RA Woo P.C., Lau S.K., Tse H., Teng J.L., Curreem S.O., Tsang A.K., RA Fan R.Y., Wong G.K., Huang Y., Loman N.J., Snyder L.A., Cai J.J., RA Huang J.D., Mak W., Pallen M.J., Lok S., Yuen K.Y.; RT "The complete genome and proteome of Laribacter hongkongensis reveal RT potential mechanisms for adaptations to different temperatures and RT habitats."; RL PLoS Genet. 5:E1000416-E1000416(2009). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001154; ACO73685.1; -; Genomic_DNA. DR ProteinModelPortal; C1DD50; -. DR STRING; 557598.LHK_00692; -. DR EnsemblBacteria; ACO73685; ACO73685; LHK_00692. DR KEGG; lhk:LHK_00692; -. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000002010; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000002010}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000002010}. FT DOMAIN 117 282 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 83 110 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 284 AA; 32161 MW; A918018CC0F2FCFA CRC64; MLFPRPQQRN LERALECRVV DRTSLILDIF AQRARSHEGK LQVELAQLEY LSTRLVRGWT HLERQKGGIG LRGPGETQLE TDRRLLGNRV RLLKERLAKL ERQRHVQRRS RERGGVFSVS IVGYTNAGKS TLFNALTKAR AYAADQLFAT LDTTSRRLYL NEQLSVVLSD TVGFIRDLPH SLVEAFKATL EETVRADLLL HVVDCASDTR ETQLAEVNKV LKEIEADGID QLIIWNKCDL KGLSPAIERD ETGRIVAVRL SALKGEGLDL LRQALVERAD IPTY // ID C1DLQ3_AZOVD Unreviewed; 433 AA. AC C1DLQ3; DT 26-MAY-2009, integrated into UniProtKB/TrEMBL. DT 26-MAY-2009, sequence version 1. DT 30-AUG-2017, entry version 57. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:ACO77001.1}; GN OrderedLocusNames=Avin_07550 {ECO:0000313|EMBL:ACO77001.1}; OS Azotobacter vinelandii (strain DJ / ATCC BAA-1303). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Azotobacter. OX NCBI_TaxID=322710 {ECO:0000313|EMBL:ACO77001.1, ECO:0000313|Proteomes:UP000002424}; RN [1] {ECO:0000313|EMBL:ACO77001.1, ECO:0000313|Proteomes:UP000002424} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DJ / ATCC BAA-1303 {ECO:0000313|Proteomes:UP000002424}; RX PubMed=19429624; DOI=10.1128/JB.00504-09; RA Setubal J.C., dos Santos P., Goldman B.S., Ertesvag H., Espin G., RA Rubio L.M., Valla S., Almeida N.F., Balasubramanian D., Cromes L., RA Curatti L., Du Z., Godsy E., Goodner B., Hellner-Burris K., RA Hernandez J.A., Houmiel K., Imperial J., Kennedy C., Larson T.J., RA Latreille P., Ligon L.S., Lu J., Maerk M., Miller N.M., Norton S., RA O'Carroll I.P., Paulsen I., Raulfs E.C., Roemer R., Rosser J., RA Segura D., Slater S., Stricklin S.L., Studholme D.J., Sun J., RA Viana C.J., Wallin E., Wang B., Wheeler C., Zhu H., Dean D.R., RA Dixon R., Wood D.; RT "Genome sequence of Azotobacter vinelandii, an obligate aerobe RT specialized to support diverse anaerobic metabolic processes."; RL J. Bacteriol. 191:4534-4545(2009). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001157; ACO77001.1; -; Genomic_DNA. DR RefSeq; WP_012699426.1; NC_012560.1. DR ProteinModelPortal; C1DLQ3; -. DR STRING; 322710.Avin_07550; -. DR EnsemblBacteria; ACO77001; ACO77001; Avin_07550. DR KEGG; avn:Avin_07550; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000002424; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000002424}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000002424}. FT DOMAIN 199 366 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 165 192 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 433 AA; 48743 MW; 52456DDCB2BB187E CRC64; MFFERPGGGE RAILVHLEGQ DPEAREDPQE FQELARSAGA DVVAFVGVTR HQPSAKYLIG TGKVGELHDL VRTEQAELVI FNHVLTPSQE RNLERAFECR VLDRTGLILD IFAQRARTHE GKLQVELAQL EHMSTRLVRG WTHLERQKGG IGLRGPGETQ LETDRRLLRM RIRQIRQRLE KVRSQREQAR RGRRRAEIPL VSLVGYTNAG KSTLFNALTA SGVYAANQLF ATLDPTLRRL ELDDLGALVL ADTVGFIRHL PHKLVEAFRA TLEESSNSDL LLHVIDAHEP ERMAQIEQVM AVLGEIGADH LPILEVYNKL DLLEGMEPQI QRDVDGKPLR VWVSARDGRG LELLRQAIAE LLGNDLFVGT LRLPQGLGRL RAQFFSLGAV RSETHDEEGG SLLAVRLPRI ELNRLVSREG LRPDEFIAQH TLQ // ID C1DV04_SULAA Unreviewed; 369 AA. AC C1DV04; DT 26-MAY-2009, integrated into UniProtKB/TrEMBL. DT 26-MAY-2009, sequence version 1. DT 07-JUN-2017, entry version 66. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:ACN99255.1}; GN OrderedLocusNames=SULAZ_0968 {ECO:0000313|EMBL:ACN99255.1}; OS Sulfurihydrogenibium azorense (strain Az-Fu1 / DSM 15241 / OCM 825). OC Bacteria; Aquificae; Aquificales; Hydrogenothermaceae; OC Sulfurihydrogenibium. OX NCBI_TaxID=204536 {ECO:0000313|EMBL:ACN99255.1, ECO:0000313|Proteomes:UP000001369}; RN [1] {ECO:0000313|EMBL:ACN99255.1, ECO:0000313|Proteomes:UP000001369} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Az-Fu1 / DSM 15241 / OCM 825 RC {ECO:0000313|Proteomes:UP000001369}; RX PubMed=19136599; DOI=10.1128/JB.01645-08; RA Reysenbach A.-L., Hamamura N., Podar M., Griffiths E., Ferreira S., RA Hochstein R., Heidelberg J., Johnson J., Mead D., Pohorille A., RA Sarmiento M., Schweighofer K., Seshadri R., Voytek M.A.; RT "Complete and draft genome sequences of six members of the RT Aquificales."; RL J. Bacteriol. 191:1992-1993(2009). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001229; ACN99255.1; -; Genomic_DNA. DR RefSeq; WP_012674573.1; NC_012438.1. DR ProteinModelPortal; C1DV04; -. DR STRING; 204536.SULAZ_0968; -. DR EnsemblBacteria; ACN99255; ACN99255; SULAZ_0968. DR KEGG; saf:SULAZ_0968; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000001369; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000001369}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000001369}. FT DOMAIN 194 360 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 159 189 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 369 AA; 42021 MW; 27E7DC17C001396A CRC64; MRSIIVGVNT GLNPARFKYQ IEELEGLVEA AEGVVLGKVY QKRESPDPAY YIGRGKVNEI KQLVEGIGAD TVVFNVNLSP VQISNLSQEI NAQILDRTDL ILQIFFKRAK TKQAKLQVEL AYLQHQLPRV YNQKGKELSR IGGGMKTKGA GEKLGEIKTR AIKDRINKIK KELKEIEKQK KQQRKTREDN PNILNVALVG YTNAGKSSLL NRLTKRDTYI SDQLFATLDT KTSFIHFPDI NKRVIITDTV GFVEDMPQEI MDAFMTTLKE TEEADLILHV IDISDDNWML KKQTVEDVLK KLKLEEKPVI NVMNKVDKVI PSQEYLEPDE SENTITVSAT KGWNIDKLFD ILKKYAIKKG EEYGKLRIL // ID C1E7R5_MICCC Unreviewed; 447 AA. AC C1E7R5; DT 26-MAY-2009, integrated into UniProtKB/TrEMBL. DT 26-MAY-2009, sequence version 1. DT 07-JUN-2017, entry version 40. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:ACO64028.1}; GN ORFNames=MICPUN_82419 {ECO:0000313|EMBL:ACO64028.1}; OS Micromonas commoda (strain RCC299 / NOUM17 / CCMP2709) (Picoplanktonic OS green alga). OC Eukaryota; Viridiplantae; Chlorophyta; prasinophytes; Mamiellophyceae; OC Mamiellales; Mamiellaceae; Micromonas. OX NCBI_TaxID=296587 {ECO:0000313|EMBL:ACO64028.1, ECO:0000313|Proteomes:UP000002009}; RN [1] {ECO:0000313|EMBL:ACO64028.1, ECO:0000313|Proteomes:UP000002009} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=RCC299 / NOUM17 {ECO:0000313|Proteomes:UP000002009}; RX PubMed=19359590; DOI=10.1126/science.1167222; RA Worden A.Z., Lee J.H., Mock T., Rouze P., Simmons M.P., Aerts A.L., RA Allen A.E., Cuvelier M.L., Derelle E., Everett M.V., Foulon E., RA Grimwood J., Gundlach H., Henrissat B., Napoli C., McDonald S.M., RA Parker M.S., Rombauts S., Salamov A., Von Dassow P., Badger J.H., RA Coutinho P.M., Demir E., Dubchak I., Gentemann C., Eikrem W., RA Gready J.E., John U., Lanier W., Lindquist E.A., Lucas S., Mayer K.F., RA Moreau H., Not F., Otillar R., Panaud O., Pangilinan J., Paulsen I., RA Piegu B., Poliakov A., Robbens S., Schmutz J., Toulza E., Wyss T., RA Zelensky A., Zhou K., Armbrust E.V., Bhattacharya D., Goodenough U.W., RA Van de Peer Y., Grigoriev I.V.; RT "Green evolution and dynamic adaptations revealed by genomes of the RT marine picoeukaryotes Micromonas."; RL Science 324:268-272(2009). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001327; ACO64028.1; -; Genomic_DNA. DR RefSeq; XP_002502770.1; XM_002502724.1. DR ProteinModelPortal; C1E7R5; -. DR GeneID; 8244408; -. DR KEGG; mis:MICPUN_82419; -. DR HOGENOM; HOG000260368; -. DR InParanoid; C1E7R5; -. DR KO; K03665; -. DR Proteomes; UP000002009; Chromosome 6. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000002009}; KW Reference proteome {ECO:0000313|Proteomes:UP000002009}. FT DOMAIN 181 354 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 140 167 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 447 AA; 49106 MW; BF58DFDF2BE9D06A CRC64; MEDSLAELAE LAQSAGLEVV ATLTQRMKHP HSGTYVGKGK LRELRRLRDP TVDTVIFDTE LTPRQNRNIE QYLDGKVRVC DRTMLILDIF SQRARTAEGQ LQVEMAQLEY QLPRLSRMWT HLDRTAGGGG AGGQVKGMGE KQIEIDKRLL RDRIQFLKKK LDKVKTHRML YRDRRKETPV PVVSLVGYTN AGKSSLLNAL TAADVYAEDQ LFATLDPTTR RFPLPNGKDV LVTDTVGFIQ NLPTELVAAF RATLEEIVDS TMLVHVVDIS SPLAGAQVAA VDTVLKELGA SDIPRVTVWN KSDASIASGK DPEALAEEAR SRGAVVTSAT TGFGIDSLVH ALQDTLVRVA LVRVEIDVPY DVGGVIGEVR KAGVVESETY WQGGTRVVAH VPSATARRLA HLAVTDSSPR LEDLEAAAEE GEPQWSREDE EAFLAMMLEE EEEEASA // ID C1MZ22_MICPC Unreviewed; 567 AA. AC C1MZ22; DT 26-MAY-2009, integrated into UniProtKB/TrEMBL. DT 26-MAY-2009, sequence version 1. DT 07-JUN-2017, entry version 35. DE SubName: Full=Predicted protein {ECO:0000313|EMBL:EEH54531.1}; GN ORFNames=MICPUCDRAFT_28210 {ECO:0000313|EMBL:EEH54531.1}; OS Micromonas pusilla (strain CCMP1545) (Picoplanktonic green alga). OC Eukaryota; Viridiplantae; Chlorophyta; prasinophytes; Mamiellophyceae; OC Mamiellales; Mamiellaceae; Micromonas. OX NCBI_TaxID=564608 {ECO:0000313|Proteomes:UP000001876}; RN [1] {ECO:0000313|EMBL:EEH54531.1, ECO:0000313|Proteomes:UP000001876} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CCMP1545 {ECO:0000313|EMBL:EEH54531.1, RC ECO:0000313|Proteomes:UP000001876}; RX PubMed=19359590; DOI=10.1126/science.1167222; RA Worden A.Z., Lee J.H., Mock T., Rouze P., Simmons M.P., Aerts A.L., RA Allen A.E., Cuvelier M.L., Derelle E., Everett M.V., Foulon E., RA Grimwood J., Gundlach H., Henrissat B., Napoli C., McDonald S.M., RA Parker M.S., Rombauts S., Salamov A., Von Dassow P., Badger J.H., RA Coutinho P.M., Demir E., Dubchak I., Gentemann C., Eikrem W., RA Gready J.E., John U., Lanier W., Lindquist E.A., Lucas S., Mayer K.F., RA Moreau H., Not F., Otillar R., Panaud O., Pangilinan J., Paulsen I., RA Piegu B., Poliakov A., Robbens S., Schmutz J., Toulza E., Wyss T., RA Zelensky A., Zhou K., Armbrust E.V., Bhattacharya D., Goodenough U.W., RA Van de Peer Y., Grigoriev I.V.; RT "Green evolution and dynamic adaptations revealed by genomes of the RT marine picoeukaryotes Micromonas."; RL Science 324:268-272(2009). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GG663743; EEH54531.1; -; Genomic_DNA. DR RefSeq; XP_003060881.1; XM_003060835.1. DR ProteinModelPortal; C1MZ22; -. DR GeneID; 9686580; -. DR KEGG; mpp:MICPUCDRAFT_28210; -. DR KO; K03665; -. DR OMA; VYAKDQL; -. DR Proteomes; UP000001876; Unassembled WGS sequence. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 2. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000001876}; KW Reference proteome {ECO:0000313|Proteomes:UP000001876}. FT DOMAIN 275 470 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 567 AA; 61026 MW; BBD9B4F0AEA20927 CRC64; MYGWDLPKER VVLVGVGGQR NDEKASPNAY GLDDSLSELA QLAETAGLQV VGRVTQRLRA PHPGTYVGKG KLRELRLACG LTDDVAEEDE EEEAHDDDDD DFDEFEFQWE DVSEDEDEDA SAPPSPRPPA PIPEQPHPKP KPRVVDTVVF DDELTPRQNR NLAKILDDRV QVCDRTMLIL DIFSQRARTA EGQLQVEMAQ LEYQLPRLSK MWTHLERQAG GGAGGGGQVK GMGEKQIEID KRLLRDRIVM LKRKLDKVST HRAAYRDRRA AAPIPVVSLV GYTNAGKSTV LNALVGAGVL AEDKLFATLD PTTRRLSLPN GKDVLLTDTV GFIQRLPTDL IAAFRATLEE IKDSTLLLHV VDISSPLAGA QVAAVEAVLE DLGALDIPRV TVWNKVDALT GFEGGVVLGG GADGGADGGA DAGSETTAEA RTREVLSRAA KCGAVAVSAA TGFGVDALVD VVQSELVRVS LTRVEVLVPY DKGSVLGEIR RAGVVESETW REDGTRVIAH VPVSAARRLA SLGMTAVGGA DLGADSDGAD DVVATWSEED EAELERLLME EEEEANT // ID C2BIB9_9FIRM Unreviewed; 411 AA. AC C2BIB9; DT 16-JUN-2009, integrated into UniProtKB/TrEMBL. DT 16-JUN-2009, sequence version 1. DT 07-JUN-2017, entry version 49. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:EEI85289.1}; GN ORFNames=HMPREF0072_2089 {ECO:0000313|EMBL:EEI85289.1}; OS Anaerococcus lactolyticus ATCC 51172. OC Bacteria; Firmicutes; Tissierellia; Tissierellales; Peptoniphilaceae; OC Anaerococcus. OX NCBI_TaxID=525254 {ECO:0000313|EMBL:EEI85289.1, ECO:0000313|Proteomes:UP000005984}; RN [1] {ECO:0000313|EMBL:EEI85289.1, ECO:0000313|Proteomes:UP000005984} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51172 {ECO:0000313|EMBL:EEI85289.1, RC ECO:0000313|Proteomes:UP000005984}; RA Qin X., Bachman B., Battles P., Bell A., Bess C., Bickham C., RA Chaboub L., Chen D., Coyle M., Deiros D.R., Dinh H., Forbes L., RA Fowler G., Francisco L., Fu Q., Gubbala S., Hale W., Han Y., RA Hemphill L., Highlander S.K., Hirani K., Hogues M., Jackson L., RA Jakkamsetti A., Javaid M., Jiang H., Korchina V., Kovar C., Lara F., RA Lee S., Mata R., Mathew T., Moen C., Morales K., Munidasa M., RA Nazareth L., Ngo R., Nguyen L., Okwuonu G., Ongeri F., Patil S., RA Petrosino J., Pham C., Pham P., Pu L.-L., Puazo M., Raj R., Reid J., RA Rouhana J., Saada N., Shang Y., Simmons D., Thornton R., Warren J., RA Weissenberger G., Zhang J., Zhang L., Zhou C., Zhu D., Muzny D., RA Worley K., Gibbs R.; RL Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EEI85289.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABYO01000282; EEI85289.1; -; Genomic_DNA. DR RefSeq; WP_004828777.1; NZ_GG666047.1. DR ProteinModelPortal; C2BIB9; -. DR STRING; 525254.HMPREF0072_2089; -. DR EnsemblBacteria; EEI85289; EEI85289; HMPREF0072_2089. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000005984; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000005984}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000005984}. FT DOMAIN 189 357 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 157 187 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 411 AA; 47295 MW; B68A674E3B8E251A CRC64; MQEVIQVNVL AKDDDEEIKI YELESLINTA GGKSVAFVSQ VVNKVNPRFY IGKGKLEEIR DLADKLEVKT IIFDVELSAS QLYNLEEELK LKVVDWTSLI LDIFAQRAHT KEARLKIKLA QLKYQLPRIN KWFAYLSRQA GGIGTRGPGE TMLETDRRAI ERDIRSLEKA LKDIEKTKRI NRKSRDNIFN ISLVGYTNAG KSTILNGMMR LFGSEKYVYS DDLLFATLDT STRRLDFSNT KVTLTDTVGF IDNLSKELND SFLTTLEEIK FADMLLIVID ASHNIDGQLA TIDKSLDEIE LDGKQIIYVF NKMDKVEDVT ATSLYKREYE RIFISAKNDE DLHNLKNEIV KVIKEEYREV TMHIPFDKGA VLDYFMTNYD ILKTDYDNTG TIIKLEINKG DYGKYESYID K // ID C2CP16_CORST Unreviewed; 486 AA. AC C2CP16; DT 16-JUN-2009, integrated into UniProtKB/TrEMBL. DT 16-JUN-2009, sequence version 1. DT 07-JUN-2017, entry version 48. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:EEI78614.1}; GN ORFNames=HMPREF0308_1145 {ECO:0000313|EMBL:EEI78614.1}; OS Corynebacterium striatum ATCC 6940. OC Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae; OC Corynebacterium. OX NCBI_TaxID=525268 {ECO:0000313|EMBL:EEI78614.1, ECO:0000313|Proteomes:UP000005820}; RN [1] {ECO:0000313|EMBL:EEI78614.1, ECO:0000313|Proteomes:UP000005820} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 6940 {ECO:0000313|EMBL:EEI78614.1, RC ECO:0000313|Proteomes:UP000005820}; RA Qin X., Bachman B., Battles P., Bell A., Bess C., Bickham C., RA Chaboub L., Chen D., Coyle M., Deiros D.R., Dinh H., Forbes L., RA Fowler G., Francisco L., Fu Q., Gubbala S., Hale W., Han Y., RA Hemphill L., Highlander S.K., Hirani K., Hogues M., Jackson L., RA Jakkamsetti A., Javaid M., Jiang H., Korchina V., Kovar C., Lara F., RA Lee S., Mata R., Mathew T., Moen C., Morales K., Munidasa M., RA Nazareth L., Ngo R., Nguyen L., Okwuonu G., Ongeri F., Patil S., RA Petrosino J., Pham C., Pham P., Pu L.-L., Puazo M., Raj R., Reid J., RA Rouhana J., Saada N., Shang Y., Simmons D., Thornton R., Warren J., RA Weissenberger G., Zhang J., Zhang L., Zhou C., Zhu D., Muzny D., RA Worley K., Gibbs R.; RL Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EEI78614.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACGE01000046; EEI78614.1; -; Genomic_DNA. DR RefSeq; WP_005529030.1; NZ_GG667520.1. DR ProteinModelPortal; C2CP16; -. DR STRING; 525268.HMPREF0308_1145; -. DR EnsemblBacteria; EEI78614; EEI78614; HMPREF0308_1145. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000005820; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000005820}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000005820}. FT DOMAIN 258 429 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 217 244 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 486 AA; 53643 MW; 09B08DA285A6D8EE CRC64; MNENHEELLA QAFGDYQPQD PTTGDLDLAE RNSFRRVSTT IRAEDTTDGY EVEYRKLRLE QVVLVGVWTE GTVAEVEATM AELAALTETA GAEVVEAIYQ RRDKPDPGTY IGRGKVQELK EIVEATGADT VICDGELQPG QLSALERELN TKVIDRTMLI LDIFAQHAKS KEGKAQVSLA QLEYLYTHTR GWGGNLSRQA GGRAGSNGGV GLRGPGETKI ESDRRRIRTE MARLRKELRG MKTAREVKRS KRQSSTIPQI AIAGYTNAGK SSLINAMTGA GVLVEDALFA TLDPTTRRAE LADGRQVVFT DTVGFVRHLP TQLVEAFKST LEEVLAADIM LHVVDGSDPF PIKQIEAVNK VIYDIVKETG EQAPPEIIVI NKIDQADPLV LAEIRHVLDH ENVVYVSAHT GEGIDELTSR IELFLNSRDS HVRLLVPFTR GDVVSRVHAE GTVRYEEYTN EGTLVDVRLP ASIARELSEF VVEEVS // ID C2D383_LACBR Unreviewed; 427 AA. AC C2D383; DT 16-JUN-2009, integrated into UniProtKB/TrEMBL. DT 16-JUN-2009, sequence version 1. DT 07-JUN-2017, entry version 41. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:EEI70833.1}; GN ORFNames=HMPREF0496_2005 {ECO:0000313|EMBL:EEI70833.1}; OS Lactobacillus brevis subsp. gravesensis ATCC 27305. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; OC Lactobacillus. OX NCBI_TaxID=525310 {ECO:0000313|EMBL:EEI70833.1, ECO:0000313|Proteomes:UP000003176}; RN [1] {ECO:0000313|EMBL:EEI70833.1, ECO:0000313|Proteomes:UP000003176} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 27305 {ECO:0000313|EMBL:EEI70833.1, RC ECO:0000313|Proteomes:UP000003176}; RA Qin X., Bachman B., Battles P., Bell A., Bess C., Bickham C., RA Chaboub L., Chen D., Coyle M., Deiros D.R., Dinh H., Forbes L., RA Fowler G., Francisco L., Fu Q., Gubbala S., Hale W., Han Y., RA Hemphill L., Highlander S.K., Hirani K., Hogues M., Jackson L., RA Jakkamsetti A., Javaid M., Jiang H., Korchina V., Kovar C., Lara F., RA Lee S., Mata R., Mathew T., Moen C., Morales K., Munidasa M., RA Nazareth L., Ngo R., Nguyen L., Okwuonu G., Ongeri F., Patil S., RA Petrosino J., Pham C., Pham P., Pu L.-L., Puazo M., Raj R., Reid J., RA Rouhana J., Saada N., Shang Y., Simmons D., Thornton R., Warren J., RA Weissenberger G., Zhang J., Zhang L., Zhou C., Zhu D., Muzny D., RA Worley K., Gibbs R.; RL Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EEI70833.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACGG01000104; EEI70833.1; -; Genomic_DNA. DR RefSeq; WP_004466709.1; NZ_GG669606.1. DR ProteinModelPortal; C2D383; -. DR EnsemblBacteria; EEI70833; EEI70833; HMPREF0496_2005. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000003176; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000003176}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000003176}. FT DOMAIN 203 371 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 427 AA; 47766 MW; AFEA9560CF0BC084 CRC64; MDLTQTLTPV VTIGLNQHPN SFDYSMTELN NLAEANNMEV VETLIQKLDK PDPATYFGKG KIEELTQVVI DDGVDTIVAN DELSPSQIRN IEKATKVRII DRTGLILEIF ANRAQSREAK LQVELAKLKY QLPRLHTSAS QRLDQQTGTS SGGGFTNRGA GESQYELNRR TLENRITHVN RELKESSKAD QTKRKQRDKS DTPTVALVGY TNAGKSTIMN GMINLFGNND DKQVMVKDML FATLDTSVRK LSLPDQKSFL LSDTVGFVSQ LPHQLVQAFK STLAEAANAD LLVQVVDYSD PHREMMIKTT EETLKEIGVD NIPMVVALNK ADKMDIAYPT REGDNLIMAA TDQPSLKELA NIIKEKVFKD YQTRSLLIPF DKGDIVSYLN DNTTILKTDY RENGTVVTAE LNSVDAKRFE KYLLPTE // ID C2EUZ4_9LACO Unreviewed; 424 AA. AC C2EUZ4; DT 16-JUN-2009, integrated into UniProtKB/TrEMBL. DT 16-JUN-2009, sequence version 1. DT 07-JUN-2017, entry version 47. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:EEJ40274.1}; GN ORFNames=HMPREF0549_1280 {ECO:0000313|EMBL:EEJ40274.1}; OS Lactobacillus vaginalis DSM 5837 = ATCC 49540. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; OC Lactobacillus. OX NCBI_TaxID=1423814 {ECO:0000313|EMBL:EEJ40274.1, ECO:0000313|Proteomes:UP000004483}; RN [1] {ECO:0000313|EMBL:EEJ40274.1, ECO:0000313|Proteomes:UP000004483} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 49540 {ECO:0000313|EMBL:EEJ40274.1, RC ECO:0000313|Proteomes:UP000004483}; RA Qin X., Bachman B., Battles P., Bell A., Bess C., Bickham C., RA Chaboub L., Chen D., Coyle M., Deiros D.R., Dinh H., Forbes L., RA Fowler G., Francisco L., Fu Q., Gubbala S., Hale W., Han Y., RA Hemphill L., Highlander S.K., Hirani K., Hogues M., Jackson L., RA Jakkamsetti A., Javaid M., Jiang H., Korchina V., Kovar C., Lara F., RA Lee S., Mata R., Mathew T., Moen C., Morales K., Munidasa M., RA Nazareth L., Ngo R., Nguyen L., Okwuonu G., Ongeri F., Patil S., RA Petrosino J., Pham C., Pham P., Pu L.-L., Puazo M., Raj R., Reid J., RA Rouhana J., Saada N., Shang Y., Simmons D., Thornton R., Warren J., RA Weissenberger G., Zhang J., Zhang L., Zhou C., Zhu D., Muzny D., RA Worley K., Gibbs R.; RL Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EEJ40274.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACGV01000140; EEJ40274.1; -; Genomic_DNA. DR RefSeq; WP_003716548.1; NZ_GG693412.1. DR ProteinModelPortal; C2EUZ4; -. DR EnsemblBacteria; EEJ40274; EEJ40274; HMPREF0549_1280. DR PATRIC; fig|1423814.6.peg.1570; -. DR Proteomes; UP000004483; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000004483}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}. FT DOMAIN 201 370 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 424 AA; 47809 MW; 5CA292FDBE203503 CRC64; MDNIQTEEPV LITGLNTEQE DFDYSMTELA ELTQANHMKV IDRIDQSIDR PNPATYFGSG KVDEIKEAVL AENVSTVITN DELTPSQLRN LEDELGCRVL DRTALILEIF AERAQSKEAK LQVQIAELQY RLPRLQTSAN QRLDQQTGGG SGFTNRGSGE TKLEMNRRTI QNSISHLRKE LRVIDRSEEV KRKQRDKSAI PTAALVGYTN AGKSTIMNGL VEKYGAGEDK TVFEKDMLFA TLDTSVRQLT LPDQKRFLLS DTVGFVSKLP THLVESFKST LAEAANADLL IQVIDASDPH YEDMMKTTQE TLKQIGIENI PMLYVFNKAD KTDMEYPVLE GDDQIVISAK DDESLDLLVS AIRKHLFQDY VEAKMLIPFA DGNVVSYLNE NTNILNTEYQ NSGTVLTVEL SQKDYDKYQK YVIQ // ID C2GI60_9CORY Unreviewed; 505 AA. AC C2GI60; DT 16-JUN-2009, integrated into UniProtKB/TrEMBL. DT 16-JUN-2009, sequence version 1. DT 07-JUN-2017, entry version 39. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:EEI62917.1}; GN ORFNames=HMPREF0293_1603 {ECO:0000313|EMBL:EEI62917.1}; OS Corynebacterium glucuronolyticum ATCC 51866. OC Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae; OC Corynebacterium. OX NCBI_TaxID=548478 {ECO:0000313|EMBL:EEI62917.1, ECO:0000313|Proteomes:UP000006237}; RN [1] {ECO:0000313|EMBL:EEI62917.1, ECO:0000313|Proteomes:UP000006237} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51866 {ECO:0000313|EMBL:EEI62917.1, RC ECO:0000313|Proteomes:UP000006237}; RA Qin X., Bachman B., Battles P., Bell A., Bess C., Bickham C., RA Chaboub L., Chen D., Coyle M., Deiros D.R., Dinh H., Forbes L., RA Fowler G., Francisco L., Fu Q., Gubbala S., Hale W., Han Y., RA Hemphill L., Highlander S.K., Hirani K., Hogues M., Jackson L., RA Jakkamsetti A., Javaid M., Jiang H., Korchina V., Kovar C., Lara F., RA Lee S., Mata R., Mathew T., Moen C., Morales K., Munidasa M., RA Nazareth L., Ngo R., Nguyen L., Okwuonu G., Ongeri F., Patil S., RA Petrosino J., Pham C., Pham P., Pu L.-L., Puazo M., Raj R., Reid J., RA Rouhana J., Saada N., Shang Y., Simmons D., Thornton R., Warren J., RA Weissenberger G., Zhang J., Zhang L., Zhou C., Zhu D., Muzny D., RA Worley K., Gibbs R.; RL Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EEI62917.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACHF01000037; EEI62917.1; -; Genomic_DNA. DR RefSeq; WP_005394173.1; NZ_GG667033.1. DR ProteinModelPortal; C2GI60; -. DR EnsemblBacteria; EEI62917; EEI62917; HMPREF0293_1603. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000006237; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000006237}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000006237}. FT DOMAIN 282 458 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 241 268 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 505 AA; 55338 MW; 485F18419380C4E0 CRC64; MTDSTFGTKN PDHDAVLRDV FRDHEDTTVD RYSAEPLTRP HTPSVGELDL EDRSRLRGVM SHTDMTRTER EDGYDVEYRK LRLERVVLVG VWTEGTAAEI DAAMEELKAL AETAGSEVVD TLYQKRDKPD PGTYIGQGKV SELKVAINAH EADTVVCDGE LSPGQMIALE KALDVKVIDR TMLILDIFAQ HAKSREGKTQ VALAQMEYLI TRVRGWGGAL SRQAGGRAGS NGGVGLRGPG ETKIEADRRR LRSEMAKLRK ELASMKKARD VKAMRRRGST IPKIAIAGYT NSGKSSLINA LTGAGVLVED ALFATLDPTT RRAQLVDGRS IIFSDTVGFV RHLPTQLVEA FRSTLEEVLG ADLILHVVDG SDPFPLKQIE AVRGVILDIV REEGVEAPPE IIVVNKIDQA DPLVLAELRH ALDDVAFVSA RTGEGIAELE SRIELFLNTL DSHVTLHIPF SRGDVVARVH EEGTVLSESY TEQGTVIDAR IPRQLAAQLG EFVAQ // ID C2GIC7_9CORY Unreviewed; 80 AA. AC C2GIC7; DT 16-JUN-2009, integrated into UniProtKB/TrEMBL. DT 16-JUN-2009, sequence version 1. DT 07-SEP-2016, entry version 17. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EEI62843.1}; DE Flags: Fragment; GN ORFNames=HMPREF0293_1670 {ECO:0000313|EMBL:EEI62843.1}; OS Corynebacterium glucuronolyticum ATCC 51866. OC Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae; OC Corynebacterium. OX NCBI_TaxID=548478 {ECO:0000313|EMBL:EEI62843.1, ECO:0000313|Proteomes:UP000006237}; RN [1] {ECO:0000313|EMBL:EEI62843.1, ECO:0000313|Proteomes:UP000006237} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51866 {ECO:0000313|EMBL:EEI62843.1, RC ECO:0000313|Proteomes:UP000006237}; RA Qin X., Bachman B., Battles P., Bell A., Bess C., Bickham C., RA Chaboub L., Chen D., Coyle M., Deiros D.R., Dinh H., Forbes L., RA Fowler G., Francisco L., Fu Q., Gubbala S., Hale W., Han Y., RA Hemphill L., Highlander S.K., Hirani K., Hogues M., Jackson L., RA Jakkamsetti A., Javaid M., Jiang H., Korchina V., Kovar C., Lara F., RA Lee S., Mata R., Mathew T., Moen C., Morales K., Munidasa M., RA Nazareth L., Ngo R., Nguyen L., Okwuonu G., Ongeri F., Patil S., RA Petrosino J., Pham C., Pham P., Pu L.-L., Puazo M., Raj R., Reid J., RA Rouhana J., Saada N., Shang Y., Simmons D., Thornton R., Warren J., RA Weissenberger G., Zhang J., Zhang L., Zhou C., Zhu D., Muzny D., RA Worley K., Gibbs R.; RL Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EEI62843.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACHF01000057; EEI62843.1; -; Genomic_DNA. DR EnsemblBacteria; EEI62843; EEI62843; HMPREF0293_1670. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000006237; Unassembled WGS sequence. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000006237}; KW Reference proteome {ECO:0000313|Proteomes:UP000006237}. FT DOMAIN 1 22 GTP-bdg_N. {ECO:0000259|Pfam:PF13167}. FT DOMAIN 24 80 GTP-bdg_M. {ECO:0000259|Pfam:PF16360}. FT NON_TER 1 1 {ECO:0000313|EMBL:EEI62843.1}. FT NON_TER 80 80 {ECO:0000313|EMBL:EEI62843.1}. SQ SEQUENCE 80 AA; 9310 MW; 48550E8E5577EE20 CRC64; NLERLCECRV IDRTGLILDI FAQRARTHEG KLQVELAQLR HIATRLVRGW THLERQKGGI GLRGPGETQL ETDRRLLRDR // ID C2L0V4_9FIRM Unreviewed; 426 AA. AC C2L0V4; DT 16-JUN-2009, integrated into UniProtKB/TrEMBL. DT 16-JUN-2009, sequence version 1. DT 07-JUN-2017, entry version 40. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:EEJ50335.1}; GN ORFNames=HMPREF6123_2373 {ECO:0000313|EMBL:EEJ50335.1}; OS Oribacterium sinus F0268. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Lachnospiraceae; OC Oribacterium. OX NCBI_TaxID=585501 {ECO:0000313|EMBL:EEJ50335.1, ECO:0000313|Proteomes:UP000004121}; RN [1] {ECO:0000313|EMBL:EEJ50335.1, ECO:0000313|Proteomes:UP000004121} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=F0268 {ECO:0000313|EMBL:EEJ50335.1, RC ECO:0000313|Proteomes:UP000004121}; RA Qin X., Bachman B., Battles P., Bell A., Bess C., Bickham C., RA Chaboub L., Chen D., Coyle M., Deiros D.R., Dinh H., Forbes L., RA Fowler G., Francisco L., Fu Q., Gubbala S., Hale W., Han Y., RA Hemphill L., Highlander S.K., Hirani K., Hogues M., Jackson L., RA Jakkamsetti A., Javaid M., Jiang H., Korchina V., Kovar C., Lara F., RA Lee S., Mata R., Mathew T., Moen C., Morales K., Munidasa M., RA Nazareth L., Ngo R., Nguyen L., Okwuonu G., Ongeri F., Patil S., RA Petrosino J., Pham C., Pham P., Pu L.-L., Puazo M., Raj R., Reid J., RA Rouhana J., Saada N., Shang Y., Simmons D., Thornton R., Warren J., RA Weissenberger G., Zhang J., Zhang L., Zhou C., Zhu D., Muzny D., RA Worley K., Gibbs R.; RL Submitted (APR-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EEJ50335.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACKX01000220; EEJ50335.1; -; Genomic_DNA. DR RefSeq; WP_007157519.1; NZ_GG668534.1. DR ProteinModelPortal; C2L0V4; -. DR STRING; 585501.HMPREF6123_2373; -. DR EnsemblBacteria; EEJ50335; EEJ50335; HMPREF6123_2373. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000004121; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000004121}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000004121}. FT DOMAIN 203 373 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 162 189 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 426 AA; 48071 MW; 249601910F72F361 CRC64; MQSNQIQNKK AVLVGVEFPE NRDFALDMEE LFGLCQALSI ECCTSISQSL AREDSATFIG SGKVEEVRSA VLFHEADLVI FQNALSPSQL HNLSKALSVE VLDRTQVILQ IFAERARSKE AKMQVQYATL QYMLPRLVGL RENLSRQGGS GGAGLSNRGA GEKKIELDKR KIQEEMAFLR RECKKQEEVR RVKRQKREKS NIPRIALVGY TNAGKSSLMN AILDWSKEGQ KEKVEEKDML FATLDTTIRH VKGERGEEFL FADTVGFIRD LPPKLLDAFH STLEEAIEAD LILQVVDYSD PNYQKHMDST LATLKKLEAS HIPMLYVMNK CDKVLPLSEL PKKRGEKLYI SVKEGIGISE LMEAVSEKAS ANLRPLSILL PYSEAAWENS IRKEGKILSL SYEEEGIQME LRLPEALYAK LQKFSV // ID C2W6N2_BACCE Unreviewed; 419 AA. AC C2W6N2; DT 16-JUN-2009, integrated into UniProtKB/TrEMBL. DT 16-JUN-2009, sequence version 1. DT 07-JUN-2017, entry version 47. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=bcere0022_14560 {ECO:0000313|EMBL:EEL51204.1}; OS Bacillus cereus Rock3-44. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=526986 {ECO:0000313|EMBL:EEL51204.1, ECO:0000313|Proteomes:UP000006654}; RN [1] {ECO:0000313|EMBL:EEL51204.1, ECO:0000313|Proteomes:UP000006654} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Rock3-44 {ECO:0000313|EMBL:EEL51204.1, RC ECO:0000313|Proteomes:UP000006654}; RX PubMed=22645259; DOI=10.1101/gr.134437.111; RA Zwick M.E., Joseph S.J., Didelot X., Chen P.E., Bishop-Lilly K.A., RA Stewart A.C., Willner K., Nolan N., Lentz S., Thomason M.K., RA Sozhamannan S., Mateczun A.J., Du L., Read T.D.; RT "Genomic characterization of the Bacillus cereus sensu lato species: RT Backdrop to the evolution of Bacillus anthracis."; RL Genome Res. 22:1512-1524(2012). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EEL51204.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACML01000106; EEL51204.1; -; Genomic_DNA. DR RefSeq; WP_000392009.1; NZ_CM000733.1. DR ProteinModelPortal; C2W6N2; -. DR EnsemblBacteria; EEL51204; EEL51204; bcere0022_14560. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000006654; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000006654}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}. FT DOMAIN 198 366 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 157 191 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 419 AA; 47833 MW; 6A992EFF6BB3DCE6 CRC64; MEELVQKAIL VGVNLNNESD FEYSMEELTN LAEACDVEVV GRVTQNLHRV NPSHYIGKGK IEEVSAFVKE SDANMVIFND ELSPSQIRNL EADLDCKVID RTILILDIFA QRAKTKEAQL QVEVAHLQYM MPRLIGLRES LGRQSGGVGT KNKGVGEKKL ELDRRKIEEQ IAVLNKELEA HVAQRQTQRK QRKKNEIPVV SLVGYTNAGK STIMNTMLEV FNGSTEKQVF EKDMLFATLE TSVRNIELPD NKSFLLTDTV GFVSKLPHHL VKAFRSTLEE VAEADLLIHV VDYANPNYEQ LIEITNQTLK QIGVENIPTI YAYNKSDMMD VEIPKMQEDR VYLSAKQQIG IEELVEMIRS HIYKEYTKCQ MLIPYDQGQV VSYFNDHAHV TSTSYENEGT KISLECKTSD FEKYKRFVI // ID C2WZI6_BACCE Unreviewed; 419 AA. AC C2WZI6; DT 16-JUN-2009, integrated into UniProtKB/TrEMBL. DT 16-JUN-2009, sequence version 1. DT 07-JUN-2017, entry version 43. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=bcere0024_16090 {ECO:0000313|EMBL:EEL60472.1}; OS Bacillus cereus Rock4-18. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=526988 {ECO:0000313|EMBL:EEL60472.1, ECO:0000313|Proteomes:UP000001384}; RN [1] {ECO:0000313|EMBL:EEL60472.1, ECO:0000313|Proteomes:UP000001384} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Rock4-18 {ECO:0000313|EMBL:EEL60472.1, RC ECO:0000313|Proteomes:UP000001384}; RA Read T.D., Akmal A., Bishop-Lilly K., Chen P.E., Cook C., Kiley M.P., RA Lentz S., Mateczun A., Nagarajan N., Nolan N., Osborne B.I., Pop M., RA Sozhamannan S., Stewart A.C., Sulakvelidze A., Thomason B., RA Willner K., Zwick M.E.; RT "Annotation of the Bacillus cereus Rock4-18 genome."; RL Submitted (APR-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EEL60472.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACMN01000035; EEL60472.1; -; Genomic_DNA. DR RefSeq; WP_000391749.1; NZ_CM000735.1. DR ProteinModelPortal; C2WZI6; -. DR STRING; 526988.bcere0024_16090; -. DR EnsemblBacteria; EEL60472; EEL60472; bcere0024_16090. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR Proteomes; UP000001384; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000001384}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000001384}. FT DOMAIN 198 366 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 157 191 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 419 AA; 47847 MW; 679F364BA1ED0359 CRC64; MEELFQRAVL VGVNLGNEDD FVYSMEELTN LAEACDVEVI GQVTQNLQRV NPSHYIGKGK IEEVAAYVNE VEANMVIFND ELSPSQIRNL EEDLDCKVID RTILILDIFA QRAKTKEAQL QVEVAHLQYM MPRLIGLRES LGRQSGGVGT KNKGVGEKKL ELDRRKIEEQ ISVLNKDLEA LVAQRQTQRK QRKKNEVPVV ALVGYTNAGK STTMNAMLEI YNGTEEKQVF EKDMLFATLE TSVRNIDLPD NKSFLLTDTV GFVSKLPHHL VKAFRSTLEE VAEADLLIHV VDYANPNYEQ LIDITNETLK KIGVENIPTI YAYNKSDMID VEIPKVQEDR VYLSAKKHVG IEELVEMIRS YIYKEYTKCE MLIPYDQGQV VSYFNNHAHV LSTSYENEGT KIELECKTSD YEKYKRFAI // ID C2X1R8_BACCE Unreviewed; 424 AA. AC C2X1R8; DT 16-JUN-2009, integrated into UniProtKB/TrEMBL. DT 16-JUN-2009, sequence version 1. DT 05-JUL-2017, entry version 43. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=bcere0024_34220 {ECO:0000313|EMBL:EEL59777.1}; OS Bacillus cereus Rock4-18. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=526988 {ECO:0000313|EMBL:EEL59777.1, ECO:0000313|Proteomes:UP000001384}; RN [1] {ECO:0000313|EMBL:EEL59777.1, ECO:0000313|Proteomes:UP000001384} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Rock4-18 {ECO:0000313|EMBL:EEL59777.1, RC ECO:0000313|Proteomes:UP000001384}; RA Read T.D., Akmal A., Bishop-Lilly K., Chen P.E., Cook C., Kiley M.P., RA Lentz S., Mateczun A., Nagarajan N., Nolan N., Osborne B.I., Pop M., RA Sozhamannan S., Stewart A.C., Sulakvelidze A., Thomason B., RA Willner K., Zwick M.E.; RT "Annotation of the Bacillus cereus Rock4-18 genome."; RL Submitted (APR-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EEL59777.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACMN01000063; EEL59777.1; -; Genomic_DNA. DR ProteinModelPortal; C2X1R8; -. DR STRING; 526988.bcere0024_34220; -. DR EnsemblBacteria; EEL59777; EEL59777; bcere0024_34220. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR Proteomes; UP000001384; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000001384}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000001384}. FT DOMAIN 197 359 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 424 AA; 48396 MW; B1B4B83BCE083895 CRC64; MEEKEKVILV GCQLQQDDDE QFMHSMKELA SLAKTARAKV LVSTTQKRPK FHPVTYIGKG KLEELTMLTE ELEPDVIIFN NELTPSQIRN LSSVLDARVI DRTQLILDIF AQRAKSREGK LQVELAQLQY TMPRLMGQGL SLSRLGGGIG TRGPGETKLE TDRRHIRSRI DEIKKQLAVV VEHRKRYRER RKDNKVFQVS LIGYTNAGKS TLFNRLTEAD TFEENLLFAT LDPTTRKMPL PSGYTVLLTD TVGFIQDLPT SLIAAFRSTL EEAGEADVIL HVVDSADPNY VGHEKTVKKL LSELEINHIP IITLYNKKDT LHQNFIPFPK SDFLMTSAFE ESDLLHIKEA IETKMKEEMD PYQVEIPPSE GKLLTLLKTE TLLTKMEFLE DKFVYHCTGY IFAYSPYNGQ LKRFLVEEGE NDNV // ID C3J7S1_POREA Unreviewed; 413 AA. AC C3J7S1; DT 16-JUN-2009, integrated into UniProtKB/TrEMBL. DT 16-JUN-2009, sequence version 1. DT 07-JUN-2017, entry version 41. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:EEN83621.1}; GN ORFNames=POREN0001_1162 {ECO:0000313|EMBL:EEN83621.1}; OS Porphyromonas endodontalis (strain ATCC 35406 / BCRC 14492 / JCM 8526 OS / NCTC 13058 / HG 370). OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; OC Porphyromonadaceae; Porphyromonas. OX NCBI_TaxID=553175 {ECO:0000313|EMBL:EEN83621.1, ECO:0000313|Proteomes:UP000004295}; RN [1] {ECO:0000313|EMBL:EEN83621.1, ECO:0000313|Proteomes:UP000004295} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 35406 / BCRC 14492 / JCM 8526 / NCTC 13058 / HG 370 RC {ECO:0000313|Proteomes:UP000004295}; RA Sebastian Y., Madupu R., Durkin A.S., Torralba M., Methe B., RA Sutton G.G., Strausberg R.L., Nelson K.E.; RL Submitted (APR-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EEN83621.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACNN01000005; EEN83621.1; -; Genomic_DNA. DR RefSeq; WP_004332088.1; NZ_ACNN01000005.1. DR ProteinModelPortal; C3J7S1; -. DR STRING; 553175.POREN0001_1162; -. DR EnsemblBacteria; EEN83621; EEN83621; POREN0001_1162. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000004295; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000004295}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000004295}. FT DOMAIN 202 387 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 413 AA; 47366 MW; 24AACA8F35FB21E2 CRC64; MKEFILTETS SERAVLVGLI TPKVTERQVQ DYLDELAFLS TTAGISPVKS FVQRLDMPNS ATFVGKGKLE EIASYIQENE IGLAIFDDEL SPKQLRCIEE VLRVRILDRT SLILDIFATR VQTAHAKTQV ELAQYRYMLP RLTRLWTHLE RQRGGVGMRG PGETQLETDK RIILDKISRL KEELVRIDKQ KSVQRKNRGK MVRVALVGYT NVGKSTLMNM LSKSEVFAEN KLFATLDTTV RKVILHNLPF LMSDTVGFIR KLPTELIESF KSTLDEVREA DLLLHVVDLS HPDFESQIAV VEATLREILG NENKPTLLIF NKIDAFTFTP KEEDDLTPKS RENYSREELE RSWMAKMGQN CLFVSAHTGD GIEGLRALLY DKVREIHIKR YPYNDFLFQD YNEAFSEEGL VDN // ID C3KDW4_PSEFS Unreviewed; 433 AA. AC C3KDW4; DT 16-JUN-2009, integrated into UniProtKB/TrEMBL. DT 16-JUN-2009, sequence version 1. DT 30-AUG-2017, entry version 61. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:CAY46796.1}; GN OrderedLocusNames=PFLU_0521 {ECO:0000313|EMBL:CAY46796.1}; OS Pseudomonas fluorescens (strain SBW25). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=216595 {ECO:0000313|EMBL:CAY46796.1, ECO:0000313|Proteomes:UP000002332}; RN [1] {ECO:0000313|EMBL:CAY46796.1, ECO:0000313|Proteomes:UP000002332} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SBW25 {ECO:0000313|EMBL:CAY46796.1, RC ECO:0000313|Proteomes:UP000002332}; RX PubMed=19432983; DOI=10.1186/gb-2009-10-5-r51; RA Silby M.W., Cerdeno-Tarraga A.M., Vernikos G.S., Giddens S.R., RA Jackson R.W., Preston G.M., Zhang X.X., Moon C.D., Gehrig S.M., RA Godfrey S.A., Knight C.G., Malone J.G., Robinson Z., Spiers A.J., RA Harris S., Challis G.L., Yaxley A.M., Harris D., Seeger K., Murphy L., RA Rutter S., Squares R., Quail M.A., Saunders E., Mavromatis K., RA Brettin T.S., Bentley S.D., Hothersall J., Stephens E., Thomas C.M., RA Parkhill J., Levy S.B., Rainey P.B., Thomson N.R.; RT "Genomic and genetic analyses of diversity and plant interactions of RT Pseudomonas fluorescens."; RL Genome Biol. 10:R51.1-R51.16(2009). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AM181176; CAY46796.1; -; Genomic_DNA. DR RefSeq; WP_012721915.1; NC_012660.1. DR ProteinModelPortal; C3KDW4; -. DR STRING; 216595.PFLU0521; -. DR PRIDE; C3KDW4; -. DR EnsemblBacteria; CAY46796; CAY46796; PFLU_0521. DR KEGG; pfs:PFLU_0521; -. DR PATRIC; fig|216595.4.peg.759; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000002332; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000002332}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000002332}. FT DOMAIN 199 366 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 433 AA; 48942 MW; 65B0DE1618F4E648 CRC64; MFFERHGGGE RVILVHLDGQ DPEAREDPQE FQELANSAGA ETVAFFNVPR HRPTAKYLIG SGKVEELRDL VHAEEADLVI FNHTLTPSQE RNLERVFECR VIDRTGLILD IFAQRARTHE GKLQVELAQL DHMSTRLVRG WTHLERQGGG IGMRGPGETQ LETDRRLLRV RLRQIKGRLE KVRSQREQSR RGRSRADIPT VSLVGYTNAG KSTLFNNVTK SDVYAADQLF ATLDPTLRRL DLDDLGPIVL ADTVGFIRHL PHKLVEAFRS TLEESSNSDL LLHVIDAAEP DRMLQIEQVM LVLGEIGAQD LPILEVYNKL DLLEGVEPQI QRDENGKPQR VWLSARDGSG LELLEQAIAE LLGGDLFVGT LRLPQRFARL RAQFFELGAV QKEEHDEEGV SLLAVRLPRS ELNRLVSREG VVPTEFIEQH TLQ // ID C3MBM1_SINFN Unreviewed; 440 AA. AC C3MBM1; DT 16-JUN-2009, integrated into UniProtKB/TrEMBL. DT 16-JUN-2009, sequence version 1. DT 07-JUN-2017, entry version 57. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=NGR_c13020 {ECO:0000313|EMBL:ACP25083.1}; OS Sinorhizobium fredii (strain NBRC 101917 / NGR234). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium. OX NCBI_TaxID=394 {ECO:0000313|EMBL:ACP25083.1, ECO:0000313|Proteomes:UP000001054}; RN [1] {ECO:0000313|EMBL:ACP25083.1, ECO:0000313|Proteomes:UP000001054} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NBRC 101917 / NGR234 {ECO:0000313|Proteomes:UP000001054}; RX PubMed=19376903; DOI=10.1128/AEM.00515-09; RA Schmeisser C., Liesegang H., Krysciak D., Bakkou N., Le Quere A., RA Wollherr A., Heinemeyer I., Morgenstern B., Pommerening-Roeser A., RA Flores M., Palacios R., Brenner S., Gottschalk G., Schmitz R.A., RA Broughton W.J., Perret X., Strittmatter A.W., Streit W.R.; RT "Rhizobium sp. strain NGR234 possesses a remarkable number of RT secretion systems."; RL Appl. Environ. Microbiol. 75:4035-4045(2009). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001389; ACP25083.1; -; Genomic_DNA. DR RefSeq; WP_012707859.1; NC_012587.1. DR RefSeq; YP_002825836.1; NC_012587.1. DR ProteinModelPortal; C3MBM1; -. DR STRING; 394.NGR_c13020; -. DR EnsemblBacteria; ACP25083; ACP25083; NGR_c13020. DR GeneID; 7793175; -. DR KEGG; rhi:NGR_c13020; -. DR PATRIC; fig|394.7.peg.4124; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000001054; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000001054}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000001054}. FT DOMAIN 204 376 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 163 197 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 440 AA; 48355 MW; 3F8C3B84EB893816 CRC64; MRAVVVVPVL KRTGKPAAEL TAASGRSDES RLEEATGLAL AIDLDVVHGT VVPVAQPKPG TLLGSGKIEE IGHILNEKDA GLVIVDHPLT PVQQRNLEKE WNAKVIDRTG LILEIFGRRA STKEGTLQVD LAHLNYQKGR LVRSWTHLER QRGGAGFMGG PGETQIEADR RLLQERIVRL ERELEQVRRT RQLHRSKRKK VPHPIVALVG YTNAGKSTLF NRMTGAGVLA EDMLFATLDP TLRRLKLPHG RMVILSDTVG FISDLPTHLV AAFRATLEEV LEADLILHVR DLSDPDNQAQ ASDVLRILAD LGIDEKEGSE RIVEVWNKID RLAPEVREAL VKKAASADNT VAVSAITGEG VDDLLGEIGG RLSGVMTECT VALGLDQLQL LPWIYEHAIV DGRDDLEDGR ISLDLRLTEA EAAELERRLG NGPKPVEEDW // ID C3PGX3_CORA7 Unreviewed; 492 AA. AC C3PGX3; DT 16-JUN-2009, integrated into UniProtKB/TrEMBL. DT 16-JUN-2009, sequence version 1. DT 05-JUL-2017, entry version 64. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:ACP33077.1}; GN OrderedLocusNames=cauri_1484 {ECO:0000313|EMBL:ACP33077.1}; OS Corynebacterium aurimucosum (strain ATCC 700975 / DSM 44827 / CN-1) OS (Corynebacterium nigricans). OC Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae; OC Corynebacterium. OX NCBI_TaxID=548476 {ECO:0000313|EMBL:ACP33077.1, ECO:0000313|Proteomes:UP000002077}; RN [1] {ECO:0000313|EMBL:ACP33077.1, ECO:0000313|Proteomes:UP000002077} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700975 / DSM 44827 / CN-1 RC {ECO:0000313|Proteomes:UP000002077}; RX PubMed=20137072; DOI=10.1186/1471-2164-11-91; RA Trost E., Gotker S., Schneider J., Schneiker-Bekel S., RA Szczepanowski R., Tilker A., Viehoever P., Arnold W., Bekel T., RA Blom J., Gartemann K.H., Linke B., Goesmann A., Puhler A., RA Shukla S.K., Tauch A.; RT "Complete genome sequence and lifestyle of black-pigmented RT Corynebacterium aurimucosum ATCC 700975 (formerly C. nigricans CN-1) RT isolated from a vaginal swab of a woman with spontaneous abortion."; RL BMC Genomics 11:91-91(2010). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001601; ACP33077.1; -; Genomic_DNA. DR RefSeq; WP_010190267.1; NZ_ACLH01000083.1. DR ProteinModelPortal; C3PGX3; -. DR STRING; 548476.CaurA7_010100009903; -. DR EnsemblBacteria; ACP33077; ACP33077; cauri_1484. DR GeneID; 31924114; -. DR KEGG; car:cauri_1484; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000002077; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000002077}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000002077}. FT DOMAIN 263 434 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 492 AA; 53636 MW; CE460A466F930F18 CRC64; MTKETHDVLL AQAFGEPAPS SQEPTTGDLD LAERNAFRRV TRETTIRAED TTDGYEVEYR KLRLEQVVLV GVWTEGTVAE VEATMSELAA LTETAGAEVV EALYQKRDKP DPGTYIGSGK VNELKDIVAA TGADTVVCDG ELTPGQLSAL ERALNTKVID RTMLILDIFA QHAKSKEGKA QVSLAQLEYL YTHTRGWGGN LSRQAGGRAG SNGGVGLRGP GETKIETDRR RIRTQMALLR KELKAMKTAR EIKRSRRASS TIPQIAIAGY TNAGKSSLIN AMTGAGVLVE DALFATLDPT TRRAELADGR QVVFTDTVGF VRHLPTQLVE AFKSTLEEVL SADLMLHVVD GSDPFPLKQI EAVNAVIYDI VKETGEDAPP EIIVINKIDQ ADPLVLAELR HALDRDNVVY VSAKTGEGID ELTTRVELFL NSRDEHVQLL IPFTRGDVVD RIHTQGTVRS EEYTGEGTLV DVRLPASIAA ELSEFRVSGE DT // ID C3WDR8_FUSMR Unreviewed; 596 AA. AC C3WDR8; DT 16-JUN-2009, integrated into UniProtKB/TrEMBL. DT 16-JUN-2009, sequence version 1. DT 07-JUN-2017, entry version 45. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:EEO36024.1}; GN ORFNames=FMAG_01586 {ECO:0000313|EMBL:EEO36024.1}; OS Fusobacterium mortiferum ATCC 9817. OC Bacteria; Fusobacteria; Fusobacteriales; Fusobacteriaceae; OC Fusobacterium. OX NCBI_TaxID=469616 {ECO:0000313|EMBL:EEO36024.1, ECO:0000313|Proteomes:UP000003415}; RN [1] {ECO:0000313|EMBL:EEO36024.1, ECO:0000313|Proteomes:UP000003415} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 9817 {ECO:0000313|EMBL:EEO36024.1, RC ECO:0000313|Proteomes:UP000003415}; RG The Broad Institute Genome Sequencing Platform; RA Earl A., Ward D., Feldgarden M., Gevers D., Strauss J., Ambrose C.E., RA Allen-Vercoe E., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., RA Haas B., Abouelleil A., Alvarado L., Arachchi H.M., Berlin A., RA Brown A., Chapman S.B., Chen Z., Dunbar C., Freedman E., Gearin G., RA Gellesch M., Goldberg J., Griggs A., Gujja S., Heiman D., Howarth C., RA Larson L., Lui A., MacDonald P.J.P., Mehta T., Montmayeur A., RA Murphy C., Neiman D., Pearson M., Priest M., Roberts A., Saif S., RA Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., Wortman J., RA Nusbaum C., Birren B.; RT "The Genome Sequence of Fusobacterium mortiferum ATCC 9817."; RL Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EEO36024.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACDB02000044; EEO36024.1; -; Genomic_DNA. DR RefSeq; WP_005887272.1; NZ_GL987994.1. DR ProteinModelPortal; C3WDR8; -. DR STRING; 469616.FMAG_01586; -. DR EnsemblBacteria; EEO36024; EEO36024; FMAG_01586. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000003415; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000003415}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000003415}. FT DOMAIN 364 541 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 596 AA; 66966 MW; F2803A0B27FF8754 CRC64; MIRGNTEGIK DYILKELDSL YEINVEKNKL IEPEMLMLIA QISNKINREI NIAIDRRGNV TEISIGDSSS VQLPIMDIQE RRLSGVRVIH THPSGSSNLS NIDISALIKL KLDCIAAIGI TEDKITGVTL GFCNVENNEL THEVVGPLSI EEAVNYPMIN KFDEIESLLR KRDIVENDTE YAVLVGIDTQ ESLDELAELA RACNVQVVGT FMQKKNRVDS CFFIGTGKAQ ELAVYKQLKR ANLIIFDEEL TGMQVKNLEM ITSCKVIDRT TLILEIFARR ARTREAKIQV ELAQLKYRST RLLGLGSTMS RTGGGVGTKG PGEKKLEIDK RRIRETIYDL KQELEKIRKT RVTQREKREE SGIPKISLVG YTNVGKSTLR NLLVDMFPAD NTSKKEAVFA ENMLFATLDI TTRAITLPDK RVASLTDTVG FVRKLPHDLV EAFKSTLEEV SFSDLIIHVV DASSDTAIEQ IIAVEKVLTE LDAMDKPMFL ALNKCDKATE EQLNTIKEKF PAYKTIEISA KSQMNIDGFL EMMVESLPQT TRICTYLIPY SDSSMGAYLH RNAIIQSEEY EGEGLKISAV VNNEVYNKCK KYLIGE // ID C3X7J2_OXAFO Unreviewed; 379 AA. AC C3X7J2; DT 16-JUN-2009, integrated into UniProtKB/TrEMBL. DT 16-JUN-2009, sequence version 1. DT 05-JUL-2017, entry version 41. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:EEO29168.1}; GN ORFNames=BRW84_09820 {ECO:0000313|EMBL:ARQ78874.1}, GN OFBG_00196 {ECO:0000313|EMBL:EEO29168.1}; OS Oxalobacter formigenes OXCC13. OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Oxalobacteraceae; Oxalobacter. OX NCBI_TaxID=556269 {ECO:0000313|EMBL:EEO29168.1, ECO:0000313|Proteomes:UP000005089}; RN [1] {ECO:0000313|EMBL:EEO29168.1, ECO:0000313|Proteomes:UP000005089} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=OXCC13 {ECO:0000313|EMBL:EEO29168.1, RC ECO:0000313|Proteomes:UP000005089}; RG The Broad Institute Genome Sequencing Platform; RA Ward D., Young S.K., Kodira C.D., Zeng Q., Koehrsen M., Alvarado L., RA Berlin A., Borenstein D., Chen Z., Engels R., Freedman E., RA Gellesch M., Goldberg J., Griggs A., Gujja S., Heiman D., Hepburn T., RA Howarth C., Jen D., Larson L., Lewis B., Mehta T., Park D., RA Pearson M., Roberts A., Saif S., Shea T., Shenoy N., Sisk P., RA Stolte C., Sykes S., Walk T., White J., Yandava C., Allison M.J., RA Lander E., Nusbaum C., Galagan J., Birren B.; RT "The Genome Sequence of Oxalobacter formigenes OXCC13."; RL Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:ARQ78874.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=OXCC13 {ECO:0000313|EMBL:ARQ78874.1}; RA Mah S.A., Swanson W.J., Moy G.W., Vacquier V.D.; RL Submitted (JAN-2017) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP019430; ARQ78874.1; -; Genomic_DNA. DR EMBL; GG658170; EEO29168.1; -; Genomic_DNA. DR RefSeq; WP_005879499.1; NZ_GG658170.1. DR ProteinModelPortal; C3X7J2; -. DR STRING; 556269.OFBG_00196; -. DR EnsemblBacteria; EEO29168; EEO29168; OFBG_00196. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000005089; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000005089}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000005089}. FT DOMAIN 191 357 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 379 AA; 42006 MW; C0691D5873C09735 CRC64; MPKAILVGVD FGKGDFSGSL EELMLLAKSA GAEPVLNVTG KRASPDAAYY VGSGKVDEIV AAVHLYKADV VIFNHALSPA QQRNLEKRLE VNVVDRTSLI LDIFAQRAKS HEGKVQVELA QLQHLMTRLV RGWTHLERQK GGIGLRGPGE TQLETDRRLI GTRVRMLRSK LEKLQRQRET QRRSRNRNHV FSVSLVGYTN AGKSTLFNAM TKAGTYVADQ LFATLDTTSR RIYIEETGNV VISDTVGFVR ELPHQLVAAF RATLEETIHA DLLLHVVDAA NPMRKEQIEQ VNLVLKEIGA ENVPQLLVWN KIDLAGLEPG LERDEYGRIS RVFVSAGTGA GLDLLRDAIA EYAKEDKTSR MSDMDEGNGS DHYSDLASH // ID C3ZCM0_BRAFL Unreviewed; 570 AA. AC C3ZCM0; DT 28-JUL-2009, integrated into UniProtKB/TrEMBL. DT 28-JUL-2009, sequence version 1. DT 30-AUG-2017, entry version 42. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EEN49724.1}; GN ORFNames=BRAFLDRAFT_64000 {ECO:0000313|EMBL:EEN49724.1}; OS Branchiostoma floridae (Florida lancelet) (Amphioxus). OC Eukaryota; Metazoa; Chordata; Cephalochordata; Branchiostomidae; OC Branchiostoma. OX NCBI_TaxID=7739 {ECO:0000313|Proteomes:UP000001554}; RN [1] {ECO:0000313|EMBL:EEN49724.1, ECO:0000313|Proteomes:UP000001554} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=S238N-H82 {ECO:0000313|EMBL:EEN49724.1, RC ECO:0000313|Proteomes:UP000001554}; RC TISSUE=Testes {ECO:0000313|EMBL:EEN49724.1}; RX PubMed=18563158; DOI=10.1038/nature06967; RG US DOE Joint Genome Institute (JGI-PGF); RA Putnam N.H., Butts T., Ferrier D.E.K., Furlong R.F., Hellsten U., RA Kawashima T., Robinson-Rechavi M., Shoguchi E., Terry A., Yu J.-K., RA Benito-Gutierrez E.L., Dubchak I., Garcia-Fernandez J., RA Gibson-Brown J.J., Grigoriev I.V., Horton A.C., de Jong P.J., RA Jurka J., Kapitonov V.V., Kohara Y., Kuroki Y., Lindquist E., RA Lucas S., Osoegawa K., Pennacchio L.A., Salamov A.A., Satou Y., RA Sauka-Spengler T., Schmutz J., Shin-I T., Toyoda A., RA Bronner-Fraser M., Fujiyama A., Holland L.Z., Holland P.W.H., RA Satoh N., Rokhsar D.S.; RT "The amphioxus genome and the evolution of the chordate karyotype."; RL Nature 453:1064-1071(2008). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GG666608; EEN49724.1; -; Genomic_DNA. DR RefSeq; XP_002593713.1; XM_002593667.1. DR ProteinModelPortal; C3ZCM0; -. DR STRING; 7739.JGI64000; -. DR GeneID; 7209710; -. DR KEGG; bfo:BRAFLDRAFT_64000; -. DR eggNOG; KOG0410; Eukaryota. DR eggNOG; COG2262; LUCA. DR InParanoid; C3ZCM0; -. DR OMA; MDTVGFM; -. DR Proteomes; UP000001554; Partially assembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR GO; GO:0043022; F:ribosome binding; IBA:GO_Central. DR CDD; cd01878; HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000001554}; KW Reference proteome {ECO:0000313|Proteomes:UP000001554}. FT DOMAIN 340 508 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 570 AA; 64458 MW; 897B1F94157FC833 CRC64; MLQQGSTVCD WFDWPAANRS QHVHVFTRAR GYTELRSSPS FDSRKEEPYN SNRKKRKHSP LTRCFHSSSK RYRKDRKQPK ERAEVTESTE EDRNPDIDLD SDVTYSEDED EEYDSELDEE DLAEELYEEQ VTLVTPKGGH KVVVVQPNVK WGAKKQHLTT GELMLAESVA LVETLPHWKV VHTVLMSTKT PDKKTVFGKG NFQALTEKIK AMKDVTAVFL SVEALTGRQQ KQMEEAWGVS VFDRYTVVLQ IFKDHARTKE ARMQIALAEI PYLKMRISEE VANLDQQRGG VRTRGGGGET FRELRKRVLK QKETAIKKAL VRLKKKRDLL RSGRTKKEIP VVSVVGYTNS GKTTLIKALT GEERIQPQDQ LFATLDVTAH AGQLPSKMTA LYVDTVGFLS QLPHHLIASF NATLEDVRLS DLIVHIRDVS HPDTVNQKHN VLQVLSNLKL PQHLLDNMIE ANNKIDLLDG ESSVPEEDDS TVINISALKG TGLDRLRDVV EERLFEATDT VKTTLRIPMA GQQLSQLYKT ATVQGVQVTE DAEHLDVDVI VGKAAFAKFM HAFKGKVRQA // ID C4F8P0_9ACTN Unreviewed; 429 AA. AC C4F8P0; DT 07-JUL-2009, integrated into UniProtKB/TrEMBL. DT 07-JUL-2009, sequence version 1. DT 07-JUN-2017, entry version 43. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:EEP44912.1}; GN ORFNames=COLINT_02411 {ECO:0000313|EMBL:EEP44912.1}; OS Collinsella intestinalis DSM 13280. OC Bacteria; Actinobacteria; Coriobacteriia; Coriobacteriales; OC Coriobacteriaceae; Collinsella. OX NCBI_TaxID=521003 {ECO:0000313|EMBL:EEP44912.1, ECO:0000313|Proteomes:UP000003295}; RN [1] {ECO:0000313|EMBL:EEP44912.1, ECO:0000313|Proteomes:UP000003295} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 13280 {ECO:0000313|EMBL:EEP44912.1, RC ECO:0000313|Proteomes:UP000003295}; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Nelson J., Hou S., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Nash W.E., Warren W., Chinwalla A., Mardis E.R., RA Wilson R.K.; RL Submitted (APR-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EEP44912.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABXH02000005; EEP44912.1; -; Genomic_DNA. DR RefSeq; WP_006722656.1; NZ_GG692710.1. DR ProteinModelPortal; C4F8P0; -. DR STRING; 521003.COLINT_02411; -. DR EnsemblBacteria; EEP44912; EEP44912; COLINT_02411. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000003295; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000003295}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000003295}. FT DOMAIN 210 375 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 169 203 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 429 AA; 48147 MW; 2DB1A9D54695F5C3 CRC64; MSRFELVDTA PTPERAILVG VDWRSDGWPI ERSLDELERL ADTAGAGTVA RLTQRLDRPV PKSYIGSGKV EELKGFVQRL DADVVIFDDD LSPSQQSYLE RALGEPTKVI DRTALILDIF GLHARTREGR LQVQLAQLQY LLPRLRGMWS HLAKEQTRGG IGSRFGQGES QLEIDRRMIR NRIAQLRHEL REVEKRRDVQ SKKRNDSQTF RIALTGYTNA GKSSLLNQLC GPSVLAQDKL FATLDPTTRS LSLPGGRNVT ITDTVGFIQK LPHGLVEAFK STLSEVRDAD LILRVVDISD ADYPRHVDAV EHVLDEVGAA DQPAVTVYNK IDRLDSSVVE SLRRRDPRAV FFSAVTGEGK EELLNRIIHE ASACDAPISC EIPYREGLLL SSIRTQGNIL IEEYLEDRIR LVCKVPRHIA ARVKPYVTE // ID C4FG19_9BIFI Unreviewed; 547 AA. AC C4FG19; DT 07-JUL-2009, integrated into UniProtKB/TrEMBL. DT 07-JUL-2009, sequence version 1. DT 05-JUL-2017, entry version 45. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:EEP20715.1}; GN ORFNames=BIFANG_03284 {ECO:0000313|EMBL:EEP20715.1}; OS Bifidobacterium angulatum DSM 20098 = JCM 7096. OC Bacteria; Actinobacteria; Bifidobacteriales; Bifidobacteriaceae; OC Bifidobacterium. OX NCBI_TaxID=518635 {ECO:0000313|EMBL:EEP20715.1, ECO:0000313|Proteomes:UP000006408}; RN [1] {ECO:0000313|EMBL:EEP20715.1, ECO:0000313|Proteomes:UP000006408} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 20098 {ECO:0000313|EMBL:EEP20715.1, RC ECO:0000313|Proteomes:UP000006408}; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Nelson J., Hou S., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Nash W.E., Warren W., Chinwalla A., Mardis E.R., RA Wilson R.K.; RL Submitted (APR-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EEP20715.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABYS02000009; EEP20715.1; -; Genomic_DNA. DR ProteinModelPortal; C4FG19; -. DR STRING; 518635.BIFANG_03284; -. DR EnsemblBacteria; EEP20715; EEP20715; BIFANG_03284. DR PATRIC; fig|518635.7.peg.1173; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000006408; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000006408}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000006408}. FT DOMAIN 327 493 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 547 AA; 59214 MW; 109CE776B1B2BE01 CRC64; MIIMNRARMV PRVVAHGRRR TTDDPPRIGS VAEREYKNEV ALTLSDNIDI TGTADAADGE SGRFDANVLA ESSEVLLDNG THGVDFDPSG SEEWAERESR NQLKRVAGLG ELQDITEVEY RKVRLERVVL VGVWSSAVTT QAKAEESLRE LAALAQTAGA EVCDGLLQHR SRPDAATYVG SGKAKEIADI VAREEADTIV VDDDLPPSQR RGLEDAAKVK VVDRTAVILD IFAQHATSRE GKAQVELAQL EYMLPRLRGW GGSLSRQAGG QAAGQNGGIG SRGPGETQIE MDRRVIRTRI ARLKKQIAQM APAREVKRGS RRRYGLPTIA VVGYTNAGKS SLTNRLTGSG ELVENALFAT LDTAVRRTKA GDGRLYAYVD TVGFVRRLPT QLVEAFKSTL EEVAEADVIL HVVDASHPDP FSQIDAVNEI LADIEGTAAI PRILAFNKAD LCDETTLERL AALEPDAHIV SAYSGDGVRQ LREAVEALLP TPGVHVEALL PYSAGALLSQ IREYGHVQDV QWLDDGVRVS ADVDDRLSAQ IVAAAID // ID C4GBV6_9FIRM Unreviewed; 444 AA. AC C4GBV6; DT 07-JUL-2009, integrated into UniProtKB/TrEMBL. DT 07-JUL-2009, sequence version 1. DT 07-JUN-2017, entry version 43. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:EEP28599.1}; GN ORFNames=GCWU000342_01409 {ECO:0000313|EMBL:EEP28599.1}; OS Shuttleworthia satelles DSM 14600. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Lachnospiraceae; OC Shuttleworthia. OX NCBI_TaxID=626523 {ECO:0000313|EMBL:EEP28599.1, ECO:0000313|Proteomes:UP000003494}; RN [1] {ECO:0000313|EMBL:EEP28599.1, ECO:0000313|Proteomes:UP000003494} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 14600 {ECO:0000313|EMBL:EEP28599.1, RC ECO:0000313|Proteomes:UP000003494}; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Nelson J., Hou S., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Nash W.E., Warren W., Chinwalla A., Mardis E.R., RA Wilson R.K.; RL Submitted (APR-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EEP28599.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACIP02000002; EEP28599.1; -; Genomic_DNA. DR ProteinModelPortal; C4GBV6; -. DR STRING; 626523.GCWU000342_01409; -. DR EnsemblBacteria; EEP28599; EEP28599; GCWU000342_01409. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000003494; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000003494}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000003494}. FT DOMAIN 230 394 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 444 AA; 49858 MW; 8B7E7633A3A04189 CRC64; MILDTDSRVD RDRFDLDMEE ENKLNQPLLE HNQRIKEQAE SFLLVSVCTE DESKTQLLLD ELEELLHTAG GQSVGRITQK QDAPNTASYL GRGKIEEIRG YLEMTGADGI ICDDELTPAQ MRNLAMALDC KVMDRTILIL DIFASHAASA EGKIQVELAQ LRYRATHLTG MGLSMSRLGG GIGTRGPGES RLEIDRRRIR SRIGRLKAMS QEAAAHRQLT REHRKRQQMP VAAIVGYTNA GKSTLLNALT GAGVLAQDIL FATLDTTTRI VDLGGSETML LTDTVGFIRK LPHGLIDAFR STLEEAKYAD YIIQLVDASD PDMEERMHVV RQTLDELGVK NKKILTLFNK CDRLEEDLSL HDFRADKSLC ISARTGMGLH EVRQALADFL REDRVLVERV LDYQKMQLLA RIHERGQVLE ESYEEDGIHI KAYVPLAVYG ILDD // ID C4GJE9_9NEIS Unreviewed; 377 AA. AC C4GJE9; DT 07-JUL-2009, integrated into UniProtKB/TrEMBL. DT 07-JUL-2009, sequence version 1. DT 07-JUN-2017, entry version 50. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:EEP67921.1}; GN ORFNames=GCWU000324_02172 {ECO:0000313|EMBL:EEP67921.1}; OS Kingella oralis ATCC 51147. OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Kingella. OX NCBI_TaxID=629741 {ECO:0000313|EMBL:EEP67921.1, ECO:0000313|Proteomes:UP000003009}; RN [1] {ECO:0000313|EMBL:EEP67921.1, ECO:0000313|Proteomes:UP000003009} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51147 {ECO:0000313|EMBL:EEP67921.1, RC ECO:0000313|Proteomes:UP000003009}; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Nelson J., Hou S., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Nash W.E., Warren W., Chinwalla A., Mardis E.R., RA Wilson R.K.; RL Submitted (APR-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EEP67921.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACJW02000003; EEP67921.1; -; Genomic_DNA. DR RefSeq; WP_003797210.1; NZ_GG665872.1. DR ProteinModelPortal; C4GJE9; -. DR STRING; 629741.GCWU000324_02172; -. DR EnsemblBacteria; EEP67921; EEP67921; GCWU000324_02172. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR Proteomes; UP000003009; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000003009}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000003009}. FT DOMAIN 212 377 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 377 AA; 41398 MW; 9C7A2DA20316E387 CRC64; MPHTTNKTLA QAERIMLVSV LLSSQYTGSN QTRERSFQTA CAEAAELVRA TGGELVCSET SKRDKPHTAL FVGTGKAEEL ADLVKQHDIQ LVIFNHELSP TQERNLERTL QCRVLDRVGL ILAIFAQRAQ SQEGKLQVEL AQLTHLSSRL VRGYGHLQSQ KGGIGLKGPG ETQLETDRRL IQTKITALKR QLANVKKQRE TRRKARLSGS LKTMAIVGYT NAGKSTLFNR LTKSDVFAKD QLFATLDTTA RRLYLAPEAS IILSDTVGFV QDLPHQLVSA FSATLEETAL ADVLLHIVDA HDPEHERKIQ DVNAVLAEIK ADKIPQIIVY NKIDLLPEAE QHAGSLKNHA GQTVAVRVSA ASGTGLADLR AALLEWA // ID C4IH48_CLOBU Unreviewed; 596 AA. AC C4IH48; DT 07-JUL-2009, integrated into UniProtKB/TrEMBL. DT 07-JUL-2009, sequence version 1. DT 07-JUN-2017, entry version 41. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=CLP_3007 {ECO:0000313|EMBL:EEP53899.1}; OS Clostridium butyricum E4 str. BoNT E BL5262. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=632245 {ECO:0000313|EMBL:EEP53899.1, ECO:0000313|Proteomes:UP000003081}; RN [1] {ECO:0000313|EMBL:EEP53899.1, ECO:0000313|Proteomes:UP000003081} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=E4 str. BoNT E BL5262 {ECO:0000313|Proteomes:UP000003081}; RA Shrivastava S., Brinkac L.B., Brown J.L., Bruce D.B., Detter C., RA Green L.D., Munk C.A., Rogers Y.C., Tapia R., Sims D.R., Smith L.A., RA Smith T.J., Sutton G., Brettin T.; RL Submitted (AUG-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EEP53899.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACOM01000005; EEP53899.1; -; Genomic_DNA. DR RefSeq; WP_003409327.1; NZ_ACOM01000005.1. DR ProteinModelPortal; C4IH48; -. DR STRING; 632245.CLP_3007; -. DR EnsemblBacteria; EEP53899; EEP53899; CLP_3007. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000003081; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000003081}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000003081}. FT DOMAIN 364 542 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 596 AA; 66905 MW; 17A91FC812FD040A CRC64; MIDGNIEGIK KSLIDELESI HSIKTLKDEV CNLEILNIIS RISSLIEREV SVAINRKGNV TAVAIGDSTS VEVPVINIDE KRLAGVRVIH THPNGYCNLS ALDLTALLKL KLDAIVSVAV IDGSIVDFSL GMLTLYNNKL EYEEKSNLSL DAIMSVNILD KIKFIENLIK TNDVIEDNEE KAILVGSDTR ESLEELKELT EACNIPVLNT VFQSRNKIDA AFYIGRGKVL EIASMRQVER ANVVIFDDEL SGSQVRNLEA AIGAKVIDRT TLILEIFATR AKTKEAKIQV ELAQLKYRLS RLQGLGTILS RTGGGIGTRG PGEKKLETDR RHIMETIYDL RAELKKIKKT REIQREKRNK ENIPKVSLVG YTNAGKSTLR NALCDLAAKK ENKTKEKVFE ADMLFATLDT TTRAITLKNK GVITLTDTVG FVRKLPHDLV EAFKSTLEEV IFSDLLCHVI DTSSDTSVEQ YIAVNEVLTE LGAIDKETII VLNKIDKASK EQINKIKEAL EGNNKIIEVS AAFGTNLEEF LEVIEEKLPY NYRKVEYLIP YEKGDIQSFL HRNGRVFEED YRDNGTYMCV EVDDEVYNKT QEYIIK // ID C4KBV5_THASP Unreviewed; 447 AA. AC C4KBV5; DT 07-JUL-2009, integrated into UniProtKB/TrEMBL. DT 07-JUL-2009, sequence version 1. DT 30-AUG-2017, entry version 57. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Tmz1t_3241 {ECO:0000313|EMBL:ACR01836.1}; OS Thauera sp. (strain MZ1T). OC Bacteria; Proteobacteria; Betaproteobacteria; Rhodocyclales; OC Zoogloeaceae; Thauera. OX NCBI_TaxID=85643 {ECO:0000313|EMBL:ACR01836.1, ECO:0000313|Proteomes:UP000002186}; RN [1] {ECO:0000313|Proteomes:UP000002186} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MZ1T {ECO:0000313|Proteomes:UP000002186}; RG US DOE Joint Genome Institute; RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., RA Tice H., Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T., RA Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N., RA Mikhailova N., Sayler G.S.; RT "Complete sequence of chromosome of Thauera sp. MZ1T."; RL Submitted (MAY-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001281; ACR01836.1; -; Genomic_DNA. DR RefSeq; WP_004309290.1; NC_011662.2. DR ProteinModelPortal; C4KBV5; -. DR STRING; 85643.Tmz1t_3241; -. DR EnsemblBacteria; ACR01836; ACR01836; Tmz1t_3241. DR KEGG; tmz:Tmz1t_3241; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; VILEIFH; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000002186; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000002186}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000002186}. FT DOMAIN 221 391 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 186 213 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 447 AA; 49291 MW; 7F3C2A853B3B08D3 CRC64; MQTDLADEPR KAIVASVQRP NVSDAEFEAS LAELRELAKT LGYRVVHTFT QKRAGFDTTG YLGVGKRQEV REFVAAQAGF DAAPTDTVPR TGAIEALLVD HEISPSQARN LELETGCEVM DRTMVILEIF HRNARSRAAK AQVEIARLGY MAPRLREAAK LAGPQGRQRS GVGGRGAGES HTELDRRKIR DRIAELQLEI VAMEAERKTQ RARRQGRQSP ASVALVGYTN AGKSTLMRAL TGSEVLVANK LFATLDTTVR TLYPESVPRV LVSDTVGFIK NLPHGLVASF KSTLDEALDA GLLLHVIDAS DPGFERQLEV TDSVLQEIGA DELPRIRVFN KIDHVGDAAA QAECEAALRA KYPGCIVMSA RRPDEVARLR QTIVAFFQQD LVEAELLLPW SAQQLRKEIY ANCEVLEERA EDEGAVFRLR GEPDTVERLR AQCALTR // ID C4KCN0_THASP Unreviewed; 385 AA. AC C4KCN0; DT 07-JUL-2009, integrated into UniProtKB/TrEMBL. DT 07-JUL-2009, sequence version 1. DT 30-AUG-2017, entry version 57. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Tmz1t_3384 {ECO:0000313|EMBL:ACR01978.1}; OS Thauera sp. (strain MZ1T). OC Bacteria; Proteobacteria; Betaproteobacteria; Rhodocyclales; OC Zoogloeaceae; Thauera. OX NCBI_TaxID=85643 {ECO:0000313|EMBL:ACR01978.1, ECO:0000313|Proteomes:UP000002186}; RN [1] {ECO:0000313|Proteomes:UP000002186} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MZ1T {ECO:0000313|Proteomes:UP000002186}; RG US DOE Joint Genome Institute; RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., RA Tice H., Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T., RA Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N., RA Mikhailova N., Sayler G.S.; RT "Complete sequence of chromosome of Thauera sp. MZ1T."; RL Submitted (MAY-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001281; ACR01978.1; -; Genomic_DNA. DR RefSeq; WP_012585933.1; NC_011662.2. DR ProteinModelPortal; C4KCN0; -. DR STRING; 85643.Tmz1t_3384; -. DR EnsemblBacteria; ACR01978; ACR01978; Tmz1t_3384. DR KEGG; tmz:Tmz1t_3384; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000002186; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000002186}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000002186}. FT DOMAIN 198 367 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 385 AA; 41993 MW; 0A9F8A114B25D416 CRC64; MFERPASGER AVLVQLDLGQ GAIDERLSEL KLLVLSAGAS VEAVVQGRRA APDSKLFAGS GKVQEIGEAL RAYGADIVIF NHALSPGQQR NLERELRCMV IDRTALILDI FAQRARSHEG KLQVELAQLE HLATRLVRGW THLERQKGGI GLRGPGEKQL ETDRRLLGNR VKMLKSRLAQ IEKQRKVRRR ARERRDVLSV SLVGYTNAGK STLFNALTKA GAYAADQLFA TLDTTSRRLY VGGEGAGASV VLSDTVGFIR DLPHALVAAF QATLEETAQA DLLLHVVDSA SEDRDAQIGA VNQVLAEIGA ADVPQILVWN KIDLTRAAAA VERGDCGTIR RIFLSARTGE GLDLLRDALA EVARQTFGDN ADRPAGRDDE RRQET // ID C4L2T8_EXISA Unreviewed; 415 AA. AC C4L2T8; DT 07-JUL-2009, integrated into UniProtKB/TrEMBL. DT 07-JUL-2009, sequence version 1. DT 07-JUN-2017, entry version 55. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=EAT1b_0414 {ECO:0000313|EMBL:ACQ69346.1}; OS Exiguobacterium sp. (strain ATCC BAA-1283 / AT1b). OC Bacteria; Firmicutes; Bacilli; Bacillales; OC Bacillales Family XII. Incertae Sedis; Exiguobacterium. OX NCBI_TaxID=360911 {ECO:0000313|EMBL:ACQ69346.1, ECO:0000313|Proteomes:UP000000716}; RN [1] {ECO:0000313|Proteomes:UP000000716} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-1283 / AT1b {ECO:0000313|Proteomes:UP000000716}; RG US DOE Joint Genome Institute; RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., RA Tice H., Bruce D., Goodwin L., Pitluck S., Saunders E., Brettin T., RA Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N., RA Ovchinnikova G., Ramaley R.F., Rodrigues D.F., Vishnivetskaya T.A., RA Kathariou S., Tiedje J.M., Richardson P.; RT "Complete sequence of Exiguobacterium sp. AT1b."; RL Submitted (MAY-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001615; ACQ69346.1; -; Genomic_DNA. DR RefSeq; WP_012726465.1; NC_012673.1. DR ProteinModelPortal; C4L2T8; -. DR STRING; 360911.EAT1b_0414; -. DR EnsemblBacteria; ACQ69346; ACQ69346; EAT1b_0414. DR KEGG; eat:EAT1b_0414; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000000716; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000000716}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000000716}. FT DOMAIN 201 359 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 415 AA; 46875 MW; 070E3B24FB4B697D CRC64; MIEREKVVIV GCQLPDTDDW TYEQSMGELV ELVDTAQGEV VARLDQKRQQ IDRRTFIGKG KIEELAMLVE QFEPDLLIFN AELTPAQSKN IRIALNDPDE MKLIDRTQLI LDIFASRAQS REGKLQVELA QMNYLLPRLI GQGTQLSRLG GGIGTRGPGE TKLESDRRHI KRRIDEITKQ LEGTVAHRGR YRERRKENRV FQVALVGYTN AGKSTIFNRL TDADTYEQDE LFATLDPLTR ELELPRGGKV LITDTVGFIR DLPTKLVAAF RSTLEEVVGA DLILHVIDAS NPHYLNQIDT TNAVLEELGA SEVPQLEVYN KKDRLTEDFV GGPLLISAIA SEDIVTLTGA LEDKIADILT RVHVILPVTA FEHYHPAKEA MYRLEESFLD DGSVELVGYM REDTRLYATL KQFEV // ID C4L9M8_TOLAT Unreviewed; 429 AA. AC C4L9M8; DT 07-JUL-2009, integrated into UniProtKB/TrEMBL. DT 07-JUL-2009, sequence version 1. DT 30-AUG-2017, entry version 61. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Tola_2384 {ECO:0000313|EMBL:ACQ93981.1}; OS Tolumonas auensis (strain DSM 9187 / TA4). OC Bacteria; Proteobacteria; Gammaproteobacteria; Aeromonadales; OC Aeromonadaceae; Tolumonas. OX NCBI_TaxID=595494 {ECO:0000313|EMBL:ACQ93981.1, ECO:0000313|Proteomes:UP000009073}; RN [1] {ECO:0000313|Proteomes:UP000009073} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 9187 / TA4 {ECO:0000313|Proteomes:UP000009073}; RG US DOE Joint Genome Institute; RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., RA Bruce D., Goodwin L., Pitluck S., Chertkov O., Brettin T., RA Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N., RA Mikhailova N., Spring S., Beller H.; RT "Complete sequence of Tolumonas auensis DSM 9187."; RL Submitted (MAY-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001616; ACQ93981.1; -; Genomic_DNA. DR RefSeq; WP_015879449.1; NC_012691.1. DR ProteinModelPortal; C4L9M8; -. DR STRING; 595494.Tola_2384; -. DR EnsemblBacteria; ACQ93981; ACQ93981; Tola_2384. DR KEGG; tau:Tola_2384; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000009073; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000009073}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000009073}. FT DOMAIN 198 365 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 429 AA; 48754 MW; 9A89EE9F74A37344 CRC64; MFERYQGGEQ ALLVHVDFRD ETAREDLREL EMLATSAGAT ILGTITTRRD SPQAKFFVGT GKADEIAQEV HRLQADLVIF NHALTPAQER NLERMFECRV LDRTTLILDI FAQRARTHEG KLQVELAQLR HISSRLVRGW THLERQKGGI GLRGPGETQL ETDRRLIREK ISNILGRLEK VEKQREQGRR ARVRNAIPVV SLVGYTNAGK STLFNRMTQS KVYAADQLFA TLDPTLRRIE LERLGPVVLA DTVGFIRHLP HDLVAAFKAT LQETREADLQ LHVIDCADER VQDNMAQVNE VLHEIEADEV PQLLVYNKVD CLPEGIPRIE RDDTGKPVAV WLSALTGEGT DLLLTVLDEL LSVQIVEHQL KLPVSAARLR SRLYELKAIQ RENYAEDGNC IVQIRLSEVE WLRLVKQEGP DILNFIVKQ // ID C4LJ42_CORK4 Unreviewed; 507 AA. AC C4LJ42; DT 07-JUL-2009, integrated into UniProtKB/TrEMBL. DT 07-JUL-2009, sequence version 1. DT 07-JUN-2017, entry version 66. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=ckrop_1096 {ECO:0000313|EMBL:ACR17847.1}; OS Corynebacterium kroppenstedtii (strain DSM 44385 / JCM 11950 / CIP OS 105744 / CCUG 35717). OC Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae; OC Corynebacterium. OX NCBI_TaxID=645127 {ECO:0000313|EMBL:ACR17847.1, ECO:0000313|Proteomes:UP000001473}; RN [1] {ECO:0000313|EMBL:ACR17847.1, ECO:0000313|Proteomes:UP000001473} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 44385 / JCM 11950 / CIP 105744 / CCUG 35717 RC {ECO:0000313|Proteomes:UP000001473}; RX PubMed=18430482; DOI=10.1016/j.jbiotec.2008.03.004; RA Tauch A., Schneider J., Szczepanowski R., Tilker A., Viehoever P., RA Gartemann K.-H., Arnold W., Blom J., Brinkrolf K., Brune I., RA Goetker S., Weisshaar B., Goesmann A., Droege M., Puehler A.; RT "Ultrafast pyrosequencing of Corynebacterium kroppenstedtii DSM44385 RT revealed insights into the physiology of a lipophilic corynebacterium RT that lacks mycolic acids."; RL J. Biotechnol. 136:22-30(2008). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001620; ACR17847.1; -; Genomic_DNA. DR RefSeq; WP_012731734.1; NC_012704.1. DR ProteinModelPortal; C4LJ42; -. DR STRING; 645127.ckrop_1096; -. DR EnsemblBacteria; ACR17847; ACR17847; ckrop_1096. DR KEGG; ckp:ckrop_1096; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000001473; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000001473}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000001473}. FT DOMAIN 280 456 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 239 266 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 507 AA; 56001 MW; 1B2981C570136387 CRC64; MTERSHNYPS YSDNDTHLTD DHGRRGGGLH NDTRVRHADM PTAGELDLSE RDELRALSRG SQAHTTEQSD GYDVEYRKLR LERVILVGVW TSGTTAEFEA NLEELRALAE TAGSEVLESF YQRREKPDAG TYIGSGKVAE LRDAVRSLGA DTVICDGELS PGQLIALEKQ LDVKVIDRTM LILDIFAQHA KSKEGKAQVS LAQMEYLYTR VRGWGDMMSR QAGGRAGSNG GVGLRGPGET KIEADRRRLR KDMARLRAEL RSMTTAREIK RDRRDSSTTP QIAIAGYTNA GKSSLINAIT GAGVLVEDAL FATLDPTTRR AELADGRAVI FSDTVGFVRH LPTQLVEAFR SSLEEVASAD LVLHVVDGSD PFPLKQIAAV HEVLADVRNS RAETMPPEII VVNKIDQADP IVLAQLRHEL DDVVFVSAKT GENIDELASR IELFLNTLDT HVRLHVPYTR GDIVAKVHEY GTVIDEQYDS DGTVLDVRVP ARVAQEVKEF IQADEYS // ID C4SDK9_YERMO Unreviewed; 433 AA. AC C4SDK9; DT 28-JUL-2009, integrated into UniProtKB/TrEMBL. DT 28-JUL-2009, sequence version 1. DT 30-AUG-2017, entry version 43. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=ymoll0001_5770 {ECO:0000313|EMBL:EEQ10423.1}; OS Yersinia mollaretii ATCC 43969. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; OC Yersiniaceae; Yersinia. OX NCBI_TaxID=349967 {ECO:0000313|EMBL:EEQ10423.1, ECO:0000313|Proteomes:UP000003027}; RN [1] {ECO:0000313|EMBL:EEQ10423.1, ECO:0000313|Proteomes:UP000003027} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43969 {ECO:0000313|EMBL:EEQ10423.1, RC ECO:0000313|Proteomes:UP000003027}; RA Read T.D., Akmal A., Bishop-Lilly K., Chen P.E., Cook C., Kiley M.P., RA Lentz S., Mateczun A., Nagarajan N., Nolan N., Osborne B.I., Pop M., RA Sozhamannan S., Stewart A.C., Sulakvelidze A., Thomason B., RA Willner K., Zwick M.E.; RT "Annotation of the Yersinia mollaretii ATCC 43969 genome."; RL Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AALD02000019; EEQ10423.1; -; Genomic_DNA. DR RefSeq; WP_004875466.1; NZ_AALD02000019.1. DR ProteinModelPortal; C4SDK9; -. DR EnsemblBacteria; EEQ10423; EEQ10423; ymoll0001_5770. DR Proteomes; UP000003027; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000003027}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000003027}. FT DOMAIN 198 365 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 433 AA; 48505 MW; 489C65381BAF8459 CRC64; MFDRYEAGEQ AVLVHIYFSQ DKNSEDLREF EALVSSAGVE ALQIVTGSRK APHPKYFVGE GKAVEIADAV KASGASVVLF DHALSPAQER NLERLCECRV IDRTGLILDI FAQRARTHEG KLQVELAQLR HIATRLVRGW THLERQKGGI GLRGPGETQL ETDRRLLRDR ITLILSRLER VAKQREQGRR ARTRADIPTV SLVGYTNAGK SSLFNKITAA DVYAADQLFA TLDPTLRRIN VADVGDTVLA DTVGFIRHLP HDLVAAFKAT LQETRQASLL LHIIDAADPR VTENMAAVDT VLAEIEADEI PTLLVMNKID LLDDFVPRID RNEDNLPVRV WLSAQTGAGI PLLFQALTER LSGEIAHYEL RLPPQAGRLR SRFYQLQAIE KEWIDEDGNV GMVVRMPIVD WRRLCKQEQE LISYITSESG VVN // ID C4Z105_EUBE2 Unreviewed; 413 AA. AC C4Z105; DT 28-JUL-2009, integrated into UniProtKB/TrEMBL. DT 28-JUL-2009, sequence version 1. DT 07-JUN-2017, entry version 58. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=EUBELI_01271 {ECO:0000313|EMBL:ACR72268.1}; OS Eubacterium eligens (strain ATCC 27750 / VPI C15-48). OC Bacteria; Firmicutes; Clostridia; Clostridiales; Eubacteriaceae; OC Eubacterium. OX NCBI_TaxID=515620 {ECO:0000313|EMBL:ACR72268.1, ECO:0000313|Proteomes:UP000001476}; RN [1] {ECO:0000313|EMBL:ACR72268.1, ECO:0000313|Proteomes:UP000001476} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 27750 / VPI C15-48 {ECO:0000313|Proteomes:UP000001476}; RX PubMed=19321416; DOI=10.1073/pnas.0901529106; RA Mahowald M.A., Rey F.E., Seedorf H., Turnbaugh P.J., Fulton R.S., RA Wollam A., Shah N., Wang C., Magrini V., Wilson R.K., Cantarel B.L., RA Coutinho P.M., Henrissat B., Crock L.W., Russell A., Verberkmoes N.C., RA Hettich R.L., Gordon J.I.; RT "Characterizing a model human gut microbiota composed of members of RT its two dominant bacterial phyla."; RL Proc. Natl. Acad. Sci. U.S.A. 106:5859-5864(2009). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001104; ACR72268.1; -; Genomic_DNA. DR RefSeq; WP_012739503.1; NC_012778.1. DR ProteinModelPortal; C4Z105; -. DR STRING; 515620.EUBELI_01271; -. DR EnsemblBacteria; ACR72268; ACR72268; EUBELI_01271. DR KEGG; eel:EUBELI_01271; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000001476; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000001476}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000001476}. FT DOMAIN 201 365 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 413 AA; 45948 MW; C4C81EC7FBEB3285 CRC64; MAVYETDEII ERVILVGVAF DTDDDTERSL DELGELAKTA GAQTVGRMIQ TRDNFHPATY IGKGKIEELR LMIDELDATG IICDDELSPA QFKNLEDELG IKVMDRTMVI LDIFAARATS SEGKIQVEMA QLKYRSIRLA GFGTSMSRLG GGIGTRGPGE KKIETDRRLI RDRISKLSAD LKDMKEHRDV QRSKRAKTST SVAAIVGYTN AGKSTLLNKL TDAGVLSEDK LFATLDPTTR SMELPNGEKV LLTDTVGFIR KLPHNLIEAF KSTLEEAKYA DIIVHVVDVS NPDYEQQMST VYATLKQLGV EGKPVVTLFN KCDVLPEKPA AKDLHADYTY NISAVRGNGL EAFKECLQEI ILKSRIRIER VFSYSEAGKI QLIRQFGQLE SEEYTEDGIK VLAYVPKEIE GKL // ID C4ZF32_AGARV Unreviewed; 415 AA. AC C4ZF32; DT 28-JUL-2009, integrated into UniProtKB/TrEMBL. DT 28-JUL-2009, sequence version 1. DT 07-JUN-2017, entry version 66. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=EUBREC_2422 {ECO:0000313|EMBL:ACR76153.1}; OS Agathobacter rectalis (strain ATCC 33656 / DSM 3377 / JCM 17463 / KCTC OS 5835 / VPI 0990) (Eubacterium rectale). OC Bacteria; Firmicutes; Clostridia; Clostridiales; Lachnospiraceae. OX NCBI_TaxID=515619 {ECO:0000313|EMBL:ACR76153.1, ECO:0000313|Proteomes:UP000001477}; RN [1] {ECO:0000313|EMBL:ACR76153.1, ECO:0000313|Proteomes:UP000001477} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33656 / DSM 3377 / JCM 17463 / KCTC 5835 / VPI 0990 RC {ECO:0000313|Proteomes:UP000001477}; RX PubMed=19321416; DOI=10.1073/pnas.0901529106; RA Mahowald M.A., Rey F.E., Seedorf H., Turnbaugh P.J., Fulton R.S., RA Wollam A., Shah N., Wang C., Magrini V., Wilson R.K., Cantarel B.L., RA Coutinho P.M., Henrissat B., Crock L.W., Russell A., Verberkmoes N.C., RA Hettich R.L., Gordon J.I.; RT "Characterizing a model human gut microbiota composed of members of RT its two dominant bacterial phyla."; RL Proc. Natl. Acad. Sci. U.S.A. 106:5859-5864(2009). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001107; ACR76153.1; -; Genomic_DNA. DR RefSeq; WP_012743247.1; NC_012781.1. DR ProteinModelPortal; C4ZF32; -. DR EnsemblBacteria; ACR76153; ACR76153; EUBREC_2422. DR KEGG; ere:EUBREC_2422; -. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000001477; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000001477}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000001477}. FT DOMAIN 202 366 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 161 195 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 415 AA; 46422 MW; 00C3A0E5D101E7C2 CRC64; MADTIKIEDI EERVVLVGVS EQDGDDADDS LSELAELVKT AGATVVGTLI QRREKIHPGT YVGTGKVAEI AELVESTGAT GIVCDDELSP AQQKNLETYL DTKVMDRTLV ILDIFASRAT TSEGKIQVEL AQLKYRLSRL SGLGKSMSRL GGGIGTRGPG EKKLEVDRRL INDRIAQLRR ELKEVQKHRD ITRAKREKNK VPVVAIVGYT NAGKSTLLNH LTEADVLEED KLFATLDPTT RILALDGKQQ VLLTDTVGFI RKLPHHLIEA FKSTLEEAKY ADIIFHVVDA SNMQREKQMF ITYQTLDDLG VKDKKFVTLF NKQDARTDNE PLHDFRADYT LNISAAKDLG LDEVKSLLEE ILRENKVYIE RIIPYDKAGV IQLIRKQGEL VSEEYVADGI QIKAYVPMEV YGRLD // ID C5A3F9_THEGJ Unreviewed; 431 AA. AC C5A3F9; DT 28-JUL-2009, integrated into UniProtKB/TrEMBL. DT 28-JUL-2009, sequence version 1. DT 07-JUN-2017, entry version 68. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:ACS32771.1}; GN OrderedLocusNames=TGAM_0269 {ECO:0000313|EMBL:ACS32771.1}; OS Thermococcus gammatolerans (strain DSM 15229 / JCM 11827 / EJ3). OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae; OC Thermococcus. OX NCBI_TaxID=593117 {ECO:0000313|EMBL:ACS32771.1, ECO:0000313|Proteomes:UP000001488}; RN [1] {ECO:0000313|EMBL:ACS32771.1, ECO:0000313|Proteomes:UP000001488} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 15229 / JCM 11827 / EJ3 RC {ECO:0000313|Proteomes:UP000001488}; RX PubMed=19558674; DOI=10.1186/gb-2009-10-6-r70; RA Zivanovic Y., Armengaud J., Lagorce A., Leplat C., Guerin P., RA Dutertre M., Anthouard V., Forterre P., Wincker P., Confalonieri F.; RT "Genome analysis and genome-wide proteomics of Thermococcus RT gammatolerans, the most radioresistant organism known amongst the RT Archaea."; RL Genome Biol. 10:R70.1-R70.23(2007). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001398; ACS32771.1; -; Genomic_DNA. DR ProteinModelPortal; C5A3F9; -. DR STRING; 593117.TGAM_0269; -. DR PaxDb; C5A3F9; -. DR EnsemblBacteria; ACS32771; ACS32771; TGAM_0269. DR KEGG; tga:TGAM_0269; -. DR PATRIC; fig|593117.10.peg.272; -. DR eggNOG; arCOG00353; Archaea. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; FNNHAHV; -. DR OrthoDB; POG093Z07D6; -. DR Proteomes; UP000001488; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000001488}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}. FT DOMAIN 189 365 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 431 AA; 49649 MW; 10FA6F3A3753186B CRC64; MRDMKAIGVI RYSRRERLSR EEFEELLRSA GYEVLAVLEQ NREEHPRYNI GRGKLEELKE LVKELRPDKV IFANRLTPSQ AYNLWKELRV EILDRWQLVL EIFEKRAHSK EAKLQVELAS LQYEVPLVKE AIRRIKLGDR AGFKGMGEYQ TQQYLKHIRY RMGKIRKELE RVRADRGVKR KRREELGFLL IALAGYTNAG KSTLLNALAG ESVEARDQMF TTLDTTTRRF KLGRKRVLLT DTVGFIDNLP PFIVEAFHST LEEIVKADIV LLVIDASEPW AEVRRKLLAS IEILRELKAL DKPMVIVLNK IDLTNDEDVE EKRRRIMEIA DELAPSVRAV VKTSAKLGIL EELKRALEEI IPSLPKYRRF KILIPSTVDP GKVLGLLESI GEVLSVSYGD EVEVEGLVQV GMIKELTRLG IKLEHPSNEA H // ID C5AFJ7_BURGB Unreviewed; 398 AA. AC C5AFJ7; DT 28-JUL-2009, integrated into UniProtKB/TrEMBL. DT 28-JUL-2009, sequence version 1. DT 07-JUN-2017, entry version 66. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=bglu_1g14560 {ECO:0000313|EMBL:ACR28604.1}; OS Burkholderia glumae (strain BGR1). OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Burkholderia. OX NCBI_TaxID=626418 {ECO:0000313|EMBL:ACR28604.1, ECO:0000313|Proteomes:UP000002187}; RN [1] {ECO:0000313|EMBL:ACR28604.1, ECO:0000313|Proteomes:UP000002187} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BGR1 {ECO:0000313|EMBL:ACR28604.1, RC ECO:0000313|Proteomes:UP000002187}; RX PubMed=19329631; DOI=10.1128/JB.00349-09; RA Lim J., Lee T.H., Nahm B.H., Choi Y.D., Kim M., Hwang I.; RT "Complete genome sequence of Burkholderia glumae BGR1."; RL J. Bacteriol. 191:3758-3759(2009). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001503; ACR28604.1; -; Genomic_DNA. DR RefSeq; WP_015875496.1; NC_012724.2. DR ProteinModelPortal; C5AFJ7; -. DR STRING; 626418.bglu_1g14560; -. DR EnsemblBacteria; ACR28604; ACR28604; bglu_1g14560. DR KEGG; bgl:bglu_1g14560; -. DR PATRIC; fig|626418.3.peg.4240; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000002187; Chromosome 1. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000002187}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000002187}. FT DOMAIN 196 367 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 162 189 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 398 AA; 43780 MW; F28DEBE418F81EFF CRC64; MTPANLTNAA LVGIDFGKTD FEASLEELSL LASSAGAHPA VTLTGRRSSP DAAMFIGSGK AEELRLACDA NEIDIVIFNH PLAPAQQRNL ERTLNRRVVD RTSLILDIFA QRARSHEGKL QVELAQLQYL STRLIRAWTH LERQKGGIGL RGPGETQLET DRRLIGERIK MLKSRLDKLR RQHNTQRRQR ERNRTMSVSL VGYTNAGKST LFNALTKAQA YAADQLFATL DTTSRRVYLG DEVGQIVVSD TVGFIRELPH QLVAAFRATL EETIHADLLL HVVDASSAVR LEQIEQVNDV LHEIGADAIR QVLVFNKIDA VPELAARGDA VERDEYGNIS RVFLSARSGQ GLDALRSAIA EIATSDQQLS GAVSLPEPTR DGGLAEPRDD HTVSEHGH // ID C5AVT8_METEA Unreviewed; 471 AA. AC C5AVT8; DT 28-JUL-2009, integrated into UniProtKB/TrEMBL. DT 28-JUL-2009, sequence version 1. DT 07-JUN-2017, entry version 57. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=MexAM1_META1p3026 {ECO:0000313|EMBL:ACS40774.1}; OS Methylobacterium extorquens (strain ATCC 14718 / DSM 1338 / JCM 2805 / OS NCIMB 9133 / AM1). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Methylobacteriaceae; Methylobacterium. OX NCBI_TaxID=272630 {ECO:0000313|EMBL:ACS40774.1, ECO:0000313|Proteomes:UP000009081}; RN [1] {ECO:0000313|EMBL:ACS40774.1, ECO:0000313|Proteomes:UP000009081} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 14718 / DSM 1338 / JCM 2805 / NCIMB 9133 / AM1 RC {ECO:0000313|Proteomes:UP000009081}; RX PubMed=19440302; DOI=10.1371/journal.pone.0005584; RA Vuilleumier S., Chistoserdova L., Lee M.-C., Bringel F., Lajus A., RA Zhou Y., Gourion B., Barbe V., Chang J., Cruveiller S., Dossat C., RA Gillett W., Gruffaz C., Haugen E., Hourcade E., Levy R., Mangenot S., RA Muller E., Nadalig T., Pagni M., Penny C., Peyraud R., Robinson D.G., RA Roche D., Rouy Z., Saenampechek C., Salvignol G., Vallenet D., Wu Z., RA Marx C.J., Vorholt J.A., Olson M.V., Kaul R., Weissenbach J., RA Medigue C., Lidstrom M.E.; RT "Methylobacterium genome sequences: a reference blueprint to RT investigate microbial metabolism of C1 compounds from natural and RT industrial sources."; RL PLoS ONE 4:E5584-E5584(2009). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001510; ACS40774.1; -; Genomic_DNA. DR RefSeq; WP_003600263.1; NC_012808.1. DR ProteinModelPortal; C5AVT8; -. DR STRING; 272630.MexAM1_META1p3026; -. DR EnsemblBacteria; ACS40774; ACS40774; MexAM1_META1p3026. DR KEGG; mea:Mex_1p3026; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR Proteomes; UP000009081; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000009081}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000009081}. FT DOMAIN 229 403 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 471 AA; 51289 MW; 25D2683EE96653FC CRC64; MTEILPPGEA RLQAKAAPEG EIAAATRTLV LGPYLTRAAQ RLAPGQTETV RSDEARLDEA VGLAAAIELD VTRAISVHIQ RPRPSTYLGK GRVEEIAGLI KAEEIGLVVM DCALSPVQQR NLEKAWGAKV IDRTGLILEI FGRRASTREG TLQVEHAHLA YQKSRLVRSW THLERQRGGF GFLGGPGETQ IEADRRMIQE RMTRIERDLE AVTRTRGLHR KSRARVPYPI VALVGYTNAG KSTLFNALTK AEVRAQDMLF ATLDPTARAT KLPHGETVIL SDTVGFISDL PTSLIAAFRA TLEDVIEADI LLHVRDVSHG DTQAQADDVE GVLRELGIEA DAERIIEVWN KADLLDEGER TRLLNLSAAH RGAGPAPILV SALTGEGLPE LTERIEGQVA RARSTFAVTL PPEDGAALNW LYENAEVLDR QSETGGAIAL TIRIAPEKEP RFLNRFEAAQ RVGGPQSSPA A // ID C5BDN2_EDWI9 Unreviewed; 426 AA. AC C5BDN2; DT 28-JUL-2009, integrated into UniProtKB/TrEMBL. DT 28-JUL-2009, sequence version 1. DT 30-AUG-2017, entry version 57. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=NT01EI_0410 {ECO:0000313|EMBL:ACR67648.1}; OS Edwardsiella ictaluri (strain 93-146). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; OC Hafniaceae; Edwardsiella. OX NCBI_TaxID=634503 {ECO:0000313|EMBL:ACR67648.1, ECO:0000313|Proteomes:UP000001485}; RN [1] {ECO:0000313|Proteomes:UP000001485} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=93-146 {ECO:0000313|Proteomes:UP000001485}; RA Williams M.L., Gillaspy A.F., Dyer D.W., Thune R.L., Waldbieser G.C., RA Schuster S.C., Gipson J., Zaitshik J., Landry C., Lawrence M.L.; RT "Complete genome sequence of Edwardsiella ictaluri 93-146."; RL Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001600; ACR67648.1; -; Genomic_DNA. DR RefSeq; WP_015869853.1; NC_012779.2. DR ProteinModelPortal; C5BDN2; -. DR STRING; 634503.NT01EI_0410; -. DR EnsemblBacteria; ACR67648; ACR67648; NT01EI_0410. DR GeneID; 7961235; -. DR KEGG; eic:NT01EI_0410; -. DR PATRIC; fig|634503.3.peg.370; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000001485; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000001485}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000001485}. FT DOMAIN 198 365 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 426 AA; 47945 MW; 37F0CE2350869A27 CRC64; MFDRYEAGEQ AVLVHIYFSQ EKDSEDLSEF ESLVSSAGVQ ALRVITGSRK APHPKYFVGE GKAQEIAQAV AETQASVVLF DHPLSPAQER NLERLCQCRV IDRTGLILDI FAQRARTHEG KLQVELAQLR HLATRLVRGW THLERQKGGI GLRGPGETQL ETDRRLLRDR IHLILGRLEK VEKQREQGRR ARVRAEIPTV SLVGYTNAGK STLFNTLTSA TVYAADQLFA TLDPTLRRVE VNDVGPTVLA DTVGFIRHLP HDLVAAFKAT LLETRQASLL LHVVDASDAR VDENIDAVNT VLADIGADEI PVLLVMNKID MLQDFVPRID RDEENRPLRV WVSAQQASGM DLLFQALSER LGGEIASYTL RLPPAAGRLR SRFYQLQAIE KEWIEEDGSI GLQVRMPVVD WRRLCKQQQE LINFIV // ID C5BRH6_TERTT Unreviewed; 444 AA. AC C5BRH6; DT 28-JUL-2009, integrated into UniProtKB/TrEMBL. DT 28-JUL-2009, sequence version 1. DT 07-JUN-2017, entry version 55. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:ACR14113.1}; GN OrderedLocusNames=TERTU_3557 {ECO:0000313|EMBL:ACR14113.1}; OS Teredinibacter turnerae (strain ATCC 39867 / T7901). OC Bacteria; Proteobacteria; Gammaproteobacteria; Cellvibrionales; OC Cellvibrionaceae; Teredinibacter. OX NCBI_TaxID=377629 {ECO:0000313|EMBL:ACR14113.1, ECO:0000313|Proteomes:UP000009080}; RN [1] {ECO:0000313|EMBL:ACR14113.1, ECO:0000313|Proteomes:UP000009080} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 39867 / T7901 {ECO:0000313|Proteomes:UP000009080}; RX PubMed=19568419; DOI=10.1371/journal.pone.0006085; RA Yang J.C., Madupu R., Durkin A.S., Ekborg N.A., Pedamallu C.S., RA Hostetler J.B., Radune D., Toms B.S., Henrissat B., Coutinho P.M., RA Schwarz S., Field L., Trindade-Silva A.E., Soares C.A.G., RA Elshahawi S., Hanora A., Schmidt E.W., Haygood M.G., Posfai J., RA Benner J., Madinger C., Nove J., Anton B., Chaudhary K., Foster J., RA Holman A., Kumar S., Lessard P.A., Luyten Y.A., Slatko B., Wood N., RA Wu B., Teplitski M., Mougous J.D., Ward N., Eisen J.A., Badger J.H., RA Distel D.L.; RT "The complete genome of Teredinibacter turnerae T7901: an RT intracellular endosymbiont of marine wood-boring bivalves RT (shipworms)."; RL PLoS ONE 4:E6085-E6085(2009). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001614; ACR14113.1; -; Genomic_DNA. DR RefSeq; WP_015820229.1; NC_012997.1. DR ProteinModelPortal; C5BRH6; -. DR STRING; 377629.TERTU_3557; -. DR EnsemblBacteria; ACR14113; ACR14113; TERTU_3557. DR GeneID; 29650000; -. DR KEGG; ttu:TERTU_3557; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000009080; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000009080}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000009080}. FT DOMAIN 199 370 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 444 AA; 49745 MW; 79DE1448EFE5DC96 CRC64; MFFDRPDSGE LAVLVHLEIP QSAESDDPRE FEELVLSAGG DPVELLSGQR SAPHPKYFIG TGKLEELQAL VQQHQAELVI FNHELSPSQE RNLEKALECR VLDRTGLILD IFAQRARTHE GKLQVELAQL EHMSTRLIRG WTHLERQKGG IGLRGPGETQ LETDRRLLRA RIKTIGKRLE KVRKQREQGR RARNRADIPT VSLVGYTNAG KSTLFNAITD AGVFAQDQLF ATLDPTMRRI GLPDVGPAVL ADTVGFISNL PHRLVESFRA TLEEASSSDL LLHVIDAADD ERQRNIEQVN LVLEEIDAHE LPCLMVYNKI DLLSDMAPRI DRDDQGRPVA VWLSAKNAAD NPVNISLLFQ ALAELLAEDI FQQSVYLGAA MGSLRARLYR HNAVLNESYT PDGICELEIR IPEADLKRML SAENIALDDL LKQPEQTDYQ QLAV // ID C5BWM0_BEUC1 Unreviewed; 493 AA. AC C5BWM0; DT 28-JUL-2009, integrated into UniProtKB/TrEMBL. DT 28-JUL-2009, sequence version 1. DT 07-JUN-2017, entry version 65. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Bcav_2436 {ECO:0000313|EMBL:ACQ80686.1}; OS Beutenbergia cavernae (strain ATCC BAA-8 / DSM 12333 / NBRC 16432). OC Bacteria; Actinobacteria; Micrococcales; Beutenbergiaceae; OC Beutenbergia. OX NCBI_TaxID=471853 {ECO:0000313|EMBL:ACQ80686.1, ECO:0000313|Proteomes:UP000007962}; RN [1] {ECO:0000313|EMBL:ACQ80686.1, ECO:0000313|Proteomes:UP000007962} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-8 / DSM 12333 / NBRC 16432 RC {ECO:0000313|Proteomes:UP000007962}; RX PubMed=21304633; DOI=10.4056/sigs.1162; RA Land M., Pukall R., Abt B., Goker M., Rohde M., Glavina Del Rio T., RA Tice H., Copeland A., Cheng J.F., Lucas S., Chen F., Nolan M., RA Bruce D., Goodwin L., Pitluck S., Ivanova N., Mavromatis K., RA Ovchinnikova G., Pati A., Chen A., Palaniappan K., Hauser L., RA Chang Y.J., Jefferies C.C., Saunders E., Brettin T., Detter J.C., RA Han C., Chain P., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P., RA Kyrpides N.C., Klenk H.P., Lapidus A.; RT "Complete genome sequence of Beutenbergia cavernae type strain (HKI RT 0122)."; RL Stand. Genomic Sci. 1:21-28(2009). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001618; ACQ80686.1; -; Genomic_DNA. DR RefSeq; WP_015882926.1; NC_012669.1. DR ProteinModelPortal; C5BWM0; -. DR STRING; 471853.Bcav_2436; -. DR EnsemblBacteria; ACQ80686; ACQ80686; Bcav_2436. DR KEGG; bcv:Bcav_2436; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000007962; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 2. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000007962}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000007962}. FT DOMAIN 274 440 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 493 AA; 52511 MW; 911BC7C94E499254 CRC64; MSAHPSGDEQ ADPARDVVAR ILARAGTALQ STDAAPTETD GEQLDVEERS ALRRVTGLST ELQDVTEVEY RQLRLEQVVL VGLWSSGTAE GAEISLRELA ALAETAGSTV LDGVLQRRRT PDPGTYLGSG KAAELADVVA ATGADTVVVD GELAPSQRRG LEDIVKVKVV DRTALILDIF AQHAKSREGK GQVELAQLEY LLPRLRGWGE SMSRQAGGRV AGGAGIGSRG PGETKIELDR RRIRTRMAKL RRQIDQMAPS RATKRASRHR AEVPSVAIAG YTNAGKSSLL NRLTGAGVLV ENALFATLDP TVRRAQTPDG RAYTLADTVG FVRALPHELV EAFRSTLEEV GDADVLLHVV DASHPDPESQ IAAVRTVLAD IEGLTDTPEV LVLNKADIAD AEVLTRLRSA GPHVVTVSAR TGAGIEHLRD VVAGLLPRPA VEVDVVVPYV RGDLVHRAHA TGEVLAEEHT AEGTHLQARV DAELAADLAD ALR // ID C5C9W0_MICLC Unreviewed; 546 AA. AC C5C9W0; DT 28-JUL-2009, integrated into UniProtKB/TrEMBL. DT 28-JUL-2009, sequence version 1. DT 07-JUN-2017, entry version 68. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Mlut_07300 {ECO:0000313|EMBL:ACS30262.1}; OS Micrococcus luteus (strain ATCC 4698 / DSM 20030 / JCM 1464 / NBRC OS 3333 / NCIMB 9278 / NCTC 2665 / VKM Ac-2230) (Micrococcus OS lysodeikticus). OC Bacteria; Actinobacteria; Micrococcales; Micrococcaceae; Micrococcus. OX NCBI_TaxID=465515 {ECO:0000313|EMBL:ACS30262.1, ECO:0000313|Proteomes:UP000000738}; RN [1] {ECO:0000313|Proteomes:UP000000738} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 4698 / DSM 20030 / JCM 1464 / NBRC 3333 / NCIMB 9278 / RC NCTC 2665 / VKM Ac-2230 {ECO:0000313|Proteomes:UP000000738}; RX PubMed=19948807; DOI=10.1128/JB.01254-09; RA Young M., Artsatbanov V., Beller H.R., Chandra G., Chater K.F., RA Dover L.G., Goh E.B., Kahan T., Kaprelyants A.S., Kyrpides N., RA Lapidus A., Lowry S.R., Lykidis A., Mahillon J., Markowitz V., RA Mavromatis K., Mukamolova G.V., Oren A., Rokem J.S., Smith M.C., RA Young D.I., Greenblatt C.L.; RT "Genome sequence of the Fleming strain of Micrococcus luteus, a simple RT free-living actinobacterium."; RL J. Bacteriol. 192:841-860(2010). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001628; ACS30262.1; -; Genomic_DNA. DR RefSeq; WP_010079099.1; NZ_CABC01000044.1. DR ProteinModelPortal; C5C9W0; -. DR STRING; 465515.MlutN2_010100003508; -. DR EnsemblBacteria; ACS30262; ACS30262; Mlut_07300. DR GeneID; 7984926; -. DR KEGG; mlu:Mlut_07300; -. DR PATRIC; fig|465515.4.peg.694; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000000738; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000000738}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000000738}. FT DOMAIN 322 487 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 546 AA; 58720 MW; DF2060ECEF72A80C CRC64; MTEKNQHTPG PQAAHGPEDE IQAVIDRILA ADDARRASER EVTGRGSADS VAADHEGAPD DGTPDRSGAL AGRALALDEG EDGHTDADGD QDELAARHSL KRVQGLSTEL EDMTEVEYRQ LRLERVVLAG VWTEGSAEDA ENSLRELAAL AETAGSEVLD GVIQRRATPD PATFLGKGKA QELAEIVALS GADTVVVDSE LAPSQRRALE DVVRVKVIDR TALILDIFAQ HASSREGRAQ VELAQLEYLL PRLRGWGESM SRQAGGRAAA GEGIGSRGPG ETKIELDRRR IRTRMAKLRR DIAGMKPARE AKRANRRRNR VPSVAIAGYT NAGKSSLLNR LTHAGVLVEN ALFATLDPTV RRAMTPDGIG YTLSDTVGFV RNLPTQLVEA FRSTLEEVAD ADVILHVVDG SHPDPEGQIA AVRSVFAEVD AHRIPEIIVL NKADAADPAV VARIRSKEPH AVVVSARTGE GIDELERAIA ATIPRPDVRL ELLVPFTRGE LVSRLHSADA EILAEGYEEG GTRLSVLVRE DIAPDFAEFV VEADAS // ID C5CD63_KOSOT Unreviewed; 379 AA. AC C5CD63; DT 28-JUL-2009, integrated into UniProtKB/TrEMBL. DT 28-JUL-2009, sequence version 1. DT 07-JUN-2017, entry version 50. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Kole_0282 {ECO:0000313|EMBL:ACR79007.1}; OS Kosmotoga olearia (strain TBF 19.5.1). OC Bacteria; Thermotogae; Kosmotogales; Kosmotogaceae; Kosmotoga. OX NCBI_TaxID=521045 {ECO:0000313|EMBL:ACR79007.1, ECO:0000313|Proteomes:UP000002382}; RN [1] {ECO:0000313|EMBL:ACR79007.1, ECO:0000313|Proteomes:UP000002382} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=TBF 19.5.1 {ECO:0000313|EMBL:ACR79007.1, RC ECO:0000313|Proteomes:UP000002382}; RG US DOE Joint Genome Institute; RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., RA Bruce D., Goodwin L., Pitluck S., Chertkov O., Brettin T., RA Detter J.C., Han C., Schmutz J., Larimer F., Land M., Hauser L., RA Kyrpides N., Ovchinnikova G., Noll K.; RT "Complete sequence of Thermotogales bacterium TBF 19.5.1."; RL Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001634; ACR79007.1; -; Genomic_DNA. DR ProteinModelPortal; C5CD63; -. DR STRING; 521045.Kole_0282; -. DR EnsemblBacteria; ACR79007; ACR79007; Kole_0282. DR KEGG; kol:Kole_0282; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000002382; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000002382}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000002382}. FT DOMAIN 157 322 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 379 AA; 42997 MW; 19D26B1F79ECA086 CRC64; MDKIIQNLDK PDNRRYFGKG KLEQVKKIVS FKNISVVITR HNLTPSQKKN LESFLEVKVL DRTQVILEIF KKHAVTREGK LEVELARLKY ELPSLKGKGT SLSNTGAGIG TRGPGEKILE RDRRLALKRI TVLQKELIKQ RKVREVIRKK RQRNSIPVVS FVGYTNVGKS SLISALTGAD LLVENQLFST LDVKTCRLKL PSGRRVLISD TVGFIRELPQ ELIQSFKSTL EEAKFSDLLV VVLDASDRYL DEKLEIINST LRDIGAENVP KLNVINKIDK CTGERLKELG NSFPDAVFVS AVLKYNLDEL KEKIDIVLSQ SFRKYKLVVP PEKLGEFLKV RDEIKVISQE CYGDSLIVVY KAPERIHKKL VSFIGEGVK // ID C5D9J9_GEOSW Unreviewed; 415 AA. AC C5D9J9; DT 28-JUL-2009, integrated into UniProtKB/TrEMBL. DT 28-JUL-2009, sequence version 1. DT 07-JUN-2017, entry version 63. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=GWCH70_1232 {ECO:0000313|EMBL:ACS24085.1}; OS Geobacillus sp. (strain WCH70). OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus. OX NCBI_TaxID=471223 {ECO:0000313|EMBL:ACS24085.1, ECO:0000313|Proteomes:UP000002386}; RN [1] {ECO:0000313|EMBL:ACS24085.1, ECO:0000313|Proteomes:UP000002386} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=WCH70 {ECO:0000313|EMBL:ACS24085.1, RC ECO:0000313|Proteomes:UP000002386}; RG US DOE Joint Genome Institute; RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., RA Tice H., Bruce D., Goodwin L., Pitluck S., Chertkov O., Brettin T., RA Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N., RA Mikhailova N., Brumm P., Mead D.A., Richardson P.; RT "Complete sequence of chromosome of Geopacillus sp. WCH70."; RL Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001638; ACS24085.1; -; Genomic_DNA. DR RefSeq; WP_015863557.1; NC_012793.1. DR ProteinModelPortal; C5D9J9; -. DR STRING; 471223.GWCH70_1232; -. DR EnsemblBacteria; ACS24085; ACS24085; GWCH70_1232. DR KEGG; gwc:GWCH70_1232; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000002386; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000002386}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000002386}. FT DOMAIN 197 359 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 415 AA; 47707 MW; 12BD68E92D750A1A CRC64; MNEREKVILV GCQLPHIDDE RFFYSMEELA SLVHTANGEV IMTVTQKREA IHPATYIGKG KVEELARLVE QLEPDVVIFN DELSPSQTRN LSRQLSVRII DRTQLILDIF AQRARSKEGK LQVELAQLQY LLPRLSGQGA ELSRLGGGIG TRGPGETKLE TDRRHIYRRI DEIKTQLKLV AEHRERYRER RKKNHVFQIS LVGYTNAGKS TLFNRLTDAD SFEENLLFAT LDPLTRKITL PSGYTALLTD TVGFIQDLPT TLVAAFRSTL EEVKEADLIL HVVDSSNPDY YNHEQTVYEL LDELGVSSIP IVTIYNKRDI AHRNFVPSTK TDAIIISAFN EHDLHRLRQF IEETMMKQMV HYHVSIPSNE GRLLAQLKAE TILRELHYNE ESGMYECKGY MMPKHPLYGQ LQQYQ // ID C5ENK6_9FIRM Unreviewed; 424 AA. AC C5ENK6; DT 28-JUL-2009, integrated into UniProtKB/TrEMBL. DT 28-JUL-2009, sequence version 1. DT 07-JUN-2017, entry version 51. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:EEQ59736.1}; GN ORFNames=CBFG_03446 {ECO:0000313|EMBL:EEQ59736.1}; OS Clostridiales bacterium 1_7_47FAA. OC Bacteria; Firmicutes; Clostridia; Clostridiales. OX NCBI_TaxID=457421 {ECO:0000313|EMBL:EEQ59736.1, ECO:0000313|Proteomes:UP000004695}; RN [1] {ECO:0000313|EMBL:EEQ59736.1, ECO:0000313|Proteomes:UP000004695} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=1_7_47_FAA {ECO:0000313|EMBL:EEQ59736.1, RC ECO:0000313|Proteomes:UP000004695}; RG The Broad Institute Genome Sequencing Platform; RA Allen-Vercoe E., Strauss J., Ambrose C., Ward D., Gujja S., Young S., RA Jaffe D., Gnerre S., Berlin A., Heiman D., Hepburn T., Shea T., RA Sykes S., Alvarado L., Kodira C., Borodovsky M., Lander E., RA Galagan J., Nusbaum C., Birren B.; RT "Annotation of Clostridiales bacterium 1_7_47_FAA."; RL Submitted (AUG-2008) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; DS990261; EEQ59736.1; -; Genomic_DNA. DR ProteinModelPortal; C5ENK6; -. DR STRING; 457421.CBFG_03446; -. DR EnsemblBacteria; EEQ59736; EEQ59736; CBFG_03446. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000004695; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000004695}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000004695}. FT DOMAIN 199 370 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 158 192 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 424 AA; 47751 MW; 9144A7AD7A7D8EA1 CRC64; MIDLEELQEK VILIAVSTGE EDGSDASLDE LEELAATAGA VTVGRVIQNR ERIHPGTYLG KGKIDEVRDL VWELHATGVI CDDELSPAQL RNLEDSLDTK VMDRTMVILD IFASRASTRE GKIQVELAQL KYRAVRLVGM RNSLSRLGGG IGTRGPGEKK LETDRRLIHQ RISQLKEELE AVKRHREVTR QQREKDFALT AAIVGYTNAG KSTLLNRLTG AGILAEDKLF ATLDPTTRSF VMEDGQQILL TDTVGFIRKL PHHLIEAFKS TLEEARYSDI ILHVVDCSNP QMDMQMHVVK ETLRELEIVD KTTVTVFNKT DRLNEEGTED GMHPVPRDFS SDYQVRISAR TGEGIDELEQ ILRTIIRSRR IFLEKVFPYS QTGRIQTIRR YGQLLEEEYR DDGVAVKAYV PAELFAGLYS DGKG // ID C5R972_WEIPA Unreviewed; 437 AA. AC C5R972; DT 01-SEP-2009, integrated into UniProtKB/TrEMBL. DT 01-SEP-2009, sequence version 1. DT 07-JUN-2017, entry version 40. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:EER75304.1}; GN ORFNames=HMPREF0877_0517 {ECO:0000313|EMBL:EER75304.1}; OS Weissella paramesenteroides ATCC 33313. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Leuconostocaceae; OC Weissella. OX NCBI_TaxID=585506 {ECO:0000313|EMBL:EER75304.1, ECO:0000313|Proteomes:UP000004528}; RN [1] {ECO:0000313|EMBL:EER75304.1, ECO:0000313|Proteomes:UP000004528} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33313 {ECO:0000313|EMBL:EER75304.1, RC ECO:0000313|Proteomes:UP000004528}; RA Qin X., Bachman B., Battles P., Bell A., Bess C., Bickham C., RA Chaboub L., Chen D., Coyle M., Deiros D.R., Dinh H., Forbes L., RA Fowler G., Francisco L., Fu Q., Gubbala S., Hale W., Han Y., RA Hemphill L., Highlander S.K., Hirani K., Hogues M., Jackson L., RA Jakkamsetti A., Javaid M., Jiang H., Korchina V., Kovar C., Lara F., RA Lee S., Mata R., Mathew T., Moen C., Morales K., Munidasa M., RA Nazareth L., Ngo R., Nguyen L., Okwuonu G., Ongeri F., Patil S., RA Petrosino J., Pham C., Pham P., Pu L.-L., Puazo M., Raj R., Reid J., RA Rouhana J., Saada N., Shang Y., Simmons D., Thornton R., Warren J., RA Weissenberger G., Zhang J., Zhang L., Zhou C., Zhu D., Muzny D., RA Worley K., Gibbs R.; RL Submitted (APR-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EER75304.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACKU01000007; EER75304.1; -; Genomic_DNA. DR ProteinModelPortal; C5R972; -. DR STRING; 585506.HMPREF0877_0517; -. DR EnsemblBacteria; EER75304; EER75304; HMPREF0877_0517. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000004528; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000004528}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000004528}. FT DOMAIN 213 382 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 437 AA; 48566 MW; 9B6FBDAF7B819044 CRC64; MTQQQNGKKN MIENEQQPTR QVILAGLDQQ NENFDYEMTE LANLAAANNM TVVGRVVQKL EKPNAATYFG KGKVDELKEA LTYYDADMVV TNDELSPSQI RNLEAGTAAD IMDRTALILD IFASRAKTKV AKLQVAIAQL KYQLPRLRTS MNIRLDQQTG GGGSFTSRGA GETKLETNRR HIQHQISLLQ TELANIEADD ETRRAYRAKQ SIRNVALVGY TNAGKSTIMN GLVKRFGDNP EKTVFQADML FATLETSVRK IQLPDKQNFL LSDTVGFVSK LPHGLVAAFR ATLAEAADAD LLIQVVDYSD PHYQEMMTTT AETLKEIGVG NVPMVTVYNK ADKIPEQVYP DRAGDTLILS AIDEASQDLL VEVIKEHIFP DYVTTTLHVP FSDGQVVNEL NEQATVHELD YDESGTILKV TLTPIQAARF AQYEMTK // ID C5T4C3_ACIDE Unreviewed; 375 AA. AC C5T4C3; DT 01-SEP-2009, integrated into UniProtKB/TrEMBL. DT 01-SEP-2009, sequence version 1. DT 07-JUN-2017, entry version 46. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=AcdelDRAFT_1753 {ECO:0000313|EMBL:EER60682.1}; OS Acidovorax delafieldii 2AN. OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Comamonadaceae; Acidovorax. OX NCBI_TaxID=573060 {ECO:0000313|EMBL:EER60682.1, ECO:0000313|Proteomes:UP000003856}; RN [1] {ECO:0000313|EMBL:EER60682.1, ECO:0000313|Proteomes:UP000003856} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=2AN {ECO:0000313|EMBL:EER60682.1, RC ECO:0000313|Proteomes:UP000003856}; RG US DOE Joint Genome Institute (JGI-PGF); RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., RA Bruce D., Goodwin L., Pitluck S., Larimer F., Land M.L., Hauser L., RA Shelobolina E.S., Picardal F., Roden E., Emerson D.; RT "The draft genome of Acidovorax delafieldii 2AN."; RL Submitted (MAY-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EER60682.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACQT01000044; EER60682.1; -; Genomic_DNA. DR ProteinModelPortal; C5T4C3; -. DR EnsemblBacteria; EER60682; EER60682; AcdelDRAFT_1753. DR PATRIC; fig|573060.9.peg.3396; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000003856; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000003856}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000003856}. FT DOMAIN 186 359 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 375 AA; 41665 MW; 4159043FB53F0B41 CRC64; MGVDFGFPHF DADLEELGLL AQTAGLNPVA RLTCKRKAPD AALFVGSGKA DEIRTLAQMQ GAVEILFDQS LSPAQQRNLE RYLELPVNDR TLLILEIFAQ RARSHEGKLQ VELARLQYLS TRLVRRWSHL ERQTGGAGVR GGPGEKQIEL DRRMIDDAIK RIKERLVKVK RQRSTQRRQR ERRETFNISL VGYTNAGKST LFNALVKARA YAADQLFATL DTTTRQLYLG EAGRSVSLSD TVGFIRDLPH GLVDAFQATL QEAVDADLLL HVVDASNPHF PEQIDQVQRV LHEIGAGAVP QLLVFNKLDA MPPESRPALL QDVYELEGRA VDRQFVSARN GEGLDALRQK LARAVLAAQT DMTPGAGTEF PMEAP // ID C5WCI1_9ENTR Unreviewed; 426 AA. AC C5WCI1; DT 03-OCT-2012, integrated into UniProtKB/TrEMBL. DT 03-OCT-2012, sequence version 1. DT 07-JUN-2017, entry version 31. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:BAH83037.1}; GN ORFNames=ICMP_176 {ECO:0000313|EMBL:BAH83037.1}; OS Candidatus Ishikawaella capsulata Mpkobe. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; OC Enterobacteriaceae; Candidatus Ishikawaella. OX NCBI_TaxID=476281 {ECO:0000313|EMBL:BAH83037.1, ECO:0000313|Proteomes:UP000061704}; RN [1] {ECO:0000313|EMBL:BAH83037.1, ECO:0000313|Proteomes:UP000061704} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Mpkobe {ECO:0000313|EMBL:BAH83037.1, RC ECO:0000313|Proteomes:UP000061704}; RX PubMed=21737395; RA Nikoh N., Hosokawa T., Ohshima K., Hattori M., Fukatsu T.; RT "Reductive evolution of bacterial genome in insect gut environment."; RL Genome Biol. Evol. 3:702-714(2011). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AP010872; BAH83037.1; -; Genomic_DNA. DR RefSeq; WP_041068901.1; NZ_AP010872.1. DR EnsemblBacteria; BAH83037; BAH83037; ICMP_176. DR KEGG; icp:ICMP_176; -. DR KO; K03665; -. DR Proteomes; UP000061704; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000061704}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000061704}. FT DOMAIN 198 365 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 426 AA; 48735 MW; FF966916E4EA9604 CRC64; MIYYDIGEYA ILVHIICFPE KDIEYLQEFK KLVFSADMKV VYTVISKCKT LNPKYLVGEG KALEIADLVQ ANRASSVIFN HILTPSQERN LQRLFKCCVV DRTGIILNIF AKRAKTYESK LQVELAQLRH IATRLVCGWT HLERQKGGIG LRGGPGETQL ETDRRLLRKR IRQINWRLQS IKKQREQGRH ARSKANINTI SLIGYTNAGK STLFNNITSA NVYTADQFFA TLDMTLRRLY IANVGEVILA DTIGFISHLP YNLVAAFQAT LQEISHANLL LHVVDATNIR INENIKSVNS VLENIKKKEI TTLIIMNKID KLEYFEPRID RNEENIPVRV WISAHTGHGI PLLLTAISEI LAREMKQCTL LLPANSGKLR SNLYKLKVIQ KEWNEPDGSI ILNINIPIVD WKRLCKKEPY LNSFIV // ID C6A385_THESM Unreviewed; 424 AA. AC C6A385; DT 01-SEP-2009, integrated into UniProtKB/TrEMBL. DT 01-SEP-2009, sequence version 1. DT 07-JUN-2017, entry version 64. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=TSIB_1024 {ECO:0000313|EMBL:ACS90080.1}; OS Thermococcus sibiricus (strain MM 739 / DSM 12597). OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae; OC Thermococcus. OX NCBI_TaxID=604354 {ECO:0000313|EMBL:ACS90080.1, ECO:0000313|Proteomes:UP000009079}; RN [1] {ECO:0000313|EMBL:ACS90080.1, ECO:0000313|Proteomes:UP000009079} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MM 739 / DSM 12597 {ECO:0000313|Proteomes:UP000009079}; RX PubMed=19447963; DOI=10.1128/AEM.00718-09; RA Mardanov A.V., Ravin N.V., Svetlitchnyi V.A., Beletsky A.V., RA Miroshnichenko M.L., Bonch-Osmolovskaya E.A., Skryabin K.G.; RT "Metabolic versatility and indigenous origin of the archaeon RT Thermococcus sibiricus, isolated from a siberian oil reservoir, as RT revealed by genome analysis."; RL Appl. Environ. Microbiol. 75:4580-4588(2009). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001463; ACS90080.1; -; Genomic_DNA. DR RefSeq; WP_015849299.1; NC_012883.1. DR ProteinModelPortal; C6A385; -. DR STRING; 604354.TSIB_1024; -. DR EnsemblBacteria; ACS90080; ACS90080; TSIB_1024. DR GeneID; 8096020; -. DR KEGG; tsi:TSIB_1024; -. DR eggNOG; arCOG00353; Archaea. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG093Z07D6; -. DR Proteomes; UP000009079; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000009079}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000009079}. FT DOMAIN 186 362 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 424 AA; 48970 MW; ADCA2CE7259230FE CRC64; MKAIGIIRHS PNKRVNREEF EELLRSAGYE ILAIVEQVRE EHPKYNIGPG KLQEVKELIK ELNPDRVIFA NPLTPSQSFN ITKELRIDVI DKWQLVLEIF EKRAHSKEAK LQVEFANLQY ELPLVKEAIR RIKLGDRAGF KGMGEYQTQQ YLKHIRYRMG RIKKELEKVK ADREVKRKRR EEVGFILIAL AGYTNAGKST LLNTLANEEI ETKMQMFTTL DTTTRRFMMN GKKTLITDTV GFIDDLPPFI VEAFHSTLEE IIKADIILLI LDISEPWREI KRKFLASIEV LKELKTLDKP LIIVLNKKDL TSKADVEDKK KALEELITRK GIIAHSIIPI SAKENDLGEL KNSLEEVMFT LPKYRLFEVL VRDKEKVPKV MAMINSIGEI LDIKYGDTTK IFAYIQIGMI KSLTKMGVEL KHPS // ID C6C159_DESAD Unreviewed; 531 AA. AC C6C159; DT 01-SEP-2009, integrated into UniProtKB/TrEMBL. DT 01-SEP-2009, sequence version 1. DT 07-JUN-2017, entry version 59. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Desal_1159 {ECO:0000313|EMBL:ACS79222.1}; OS Desulfovibrio salexigens (strain ATCC 14822 / DSM 2638 / NCIB 8403 / OS VKM B-1763). OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfovibrionales; OC Desulfovibrionaceae; Desulfovibrio. OX NCBI_TaxID=526222 {ECO:0000313|EMBL:ACS79222.1, ECO:0000313|Proteomes:UP000002601}; RN [1] {ECO:0000313|EMBL:ACS79222.1, ECO:0000313|Proteomes:UP000002601} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 14822 / DSM 2638 / NCIB 8403 / VKM B-1763 RC {ECO:0000313|Proteomes:UP000002601}; RG US DOE Joint Genome Institute; RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., RA Bruce D., Goodwin L., Pitluck S., Munk A.C., Brettin T., Detter J.C., RA Han C., Tapia R., Larimer F., Land M., Hauser L., Kyrpides N., RA Anderson I., Wall J.D., Arkin A.P., Dehal P., Chivian D., Giles B., RA Hazen T.C.; RT "Complete sequence of Desulfovibrio salexigens DSM 2638."; RL Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001649; ACS79222.1; -; Genomic_DNA. DR RefSeq; WP_015851041.1; NC_012881.1. DR ProteinModelPortal; C6C159; -. DR STRING; 526222.Desal_1159; -. DR EnsemblBacteria; ACS79222; ACS79222; Desal_1159. DR KEGG; dsa:Desal_1159; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; EREVIIT; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000002601; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000002601}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000002601}. FT DOMAIN 363 531 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 531 AA; 59887 MW; 6C0B253E41DFEFD2 CRC64; MKRINRLADR RYNDPNGFTN EQARELSFLS HEIGRQIGLL VNRQGKPEMI LVGDPGSIYI PELPRARQAE GRLRGLRLLH THISGENLSE EDLMDMVFLR LDSVSVIASD PHGEPDFVQY AYLLPPGAGS KPYEQLAPVR WDRADMDLPA QIKALEDEFR RADRTRDTTD KRERAIVVSV SQDPKSVQER SLDELEDLAD TAGLKVEGRL VQRIRKLNPK FIMGKGKLAE LEVIALQADA EVILFDQELS AAQMRNLAKL TERKILDRTQ LILDIFAQHA TTRAGKLQVE MAQLKYTMPR LVGKNRAMSR LMGGIGGRGP GETKLEIDRR RIKDKLTKLG NELKKVSRQR GFTRERRARA GVPVVSLVGY TNAGKSTLLN TLTNSGVLAE DKLFATLDPT SRRIRFPREQ ELILTDTVGF IRQLPKELKE AFRATLEELE AADVLLHVCD SSHPEVDEQI AAVNNIVADM KLGDVATILV LNKWDKLDDE QRELMRNTYP QGIPSSAVDR RSLNLLVEEI LNAIDRLGHK L // ID C6CUR6_PAESJ Unreviewed; 429 AA. AC C6CUR6; DT 01-SEP-2009, integrated into UniProtKB/TrEMBL. DT 01-SEP-2009, sequence version 1. DT 07-JUN-2017, entry version 55. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Pjdr2_2616 {ECO:0000313|EMBL:ACT01270.1}; OS Paenibacillus sp. (strain JDR-2). OC Bacteria; Firmicutes; Bacilli; Bacillales; Paenibacillaceae; OC Paenibacillus. OX NCBI_TaxID=324057 {ECO:0000313|EMBL:ACT01270.1, ECO:0000313|Proteomes:UP000002510}; RN [1] {ECO:0000313|Proteomes:UP000002510} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=JDR-2 {ECO:0000313|Proteomes:UP000002510}; RX PubMed=22675593; DOI=10.4056/sigs.2374349; RA Chow V., Nong G., St John F.J., Rice J.D., Dickstein E., Chertkov O., RA Bruce D., Detter C., Brettin T., Han J., Woyke T., Pitluck S., RA Nolan M., Pati A., Martin J., Copeland A., Land M.L., Goodwin L., RA Jones J.B., Ingram L.O., Shanmugam K.T., Preston J.F.; RT "Complete genome sequence of Paenibacillus sp. strain JDR-2."; RL Stand. Genomic Sci. 6:1-10(2012). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001656; ACT01270.1; -; Genomic_DNA. DR RefSeq; WP_015844214.1; NC_012914.1. DR ProteinModelPortal; C6CUR6; -. DR STRING; 324057.Pjdr2_2616; -. DR EnsemblBacteria; ACT01270; ACT01270; Pjdr2_2616. DR KEGG; pjd:Pjdr2_2616; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000002510; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000002510}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000002510}. FT DOMAIN 208 372 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 429 AA; 47431 MW; 7529150738D22AC8 CRC64; MREKTFNTTA TMLERAVLVS LVTPNIKRGI SDPEHSLEEL VALAETAGTE VLTTMVQNKE APDTKWFIGK GKVEELRAIA DELGATTAIF DQELSGAQVR NLEETLDLKI VDRTQLILDI FAQRAKTREG IIQVELAQLS YLLPRLSGHG KNLSRLGGGI GTRGPGESKL ETDRRHIRGR ITDLKAQLDE VVRHRKLHRE RRKKSGVIQV ALVGYTNAGK STLLRELTSA DVYVENQLFA TLDPTSRTLE LPNGREVVLT DTVGFIQNLP HDLVAAFRAT LEEVLEADLV LHVVDGSSPM REEQMRVVEQ ILGDLGAAGT ASLTIYNKKD LCEVNHVELP TSGTDTLVIS AYQKDDLELV RNKIQDKLTG DTVTFTLPAD RGDLIALAYR SGEVVGNDVS EDGESLRLTV QVSRQAYEQN GYKLQPYLE // ID C6HYT5_9BACT Unreviewed; 518 AA. AC C6HYT5; DT 01-SEP-2009, integrated into UniProtKB/TrEMBL. DT 01-SEP-2009, sequence version 1. DT 07-JUN-2017, entry version 43. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=UBAL3_94240168 {ECO:0000313|EMBL:EES52370.1}; OS Leptospirillum ferrodiazotrophum. OC Bacteria; Nitrospirae; Nitrospirales; Nitrospiraceae; Leptospirillum. OX NCBI_TaxID=412449 {ECO:0000313|EMBL:EES52370.1, ECO:0000313|Proteomes:UP000009374}; RN [1] {ECO:0000313|EMBL:EES52370.1, ECO:0000313|Proteomes:UP000009374} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=19429552; DOI=10.1128/AEM.02943-08; RA Goltsman D.S., Denef V.J., Singer S.W., VerBerkmoes N.C., Lefsrud M., RA Mueller R.S., Dick G.J., Sun C.L., Wheeler K.E., Zemla A., Baker B.J., RA Hauser L., Land M., Shah M.B., Thelen M.P., Hettich R.L., RA Banfield J.F.; RT "Community genomic and proteomic analyses of chemoautotrophic iron- RT oxidizing "Leptospirillum rubarum" (Group II) and "Leptospirillum RT ferrodiazotrophum" (Group III) bacteria in acid mine drainage RT biofilms."; RL Appl. Environ. Microbiol. 75:4599-4615(2009). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GG693878; EES52370.1; -; Genomic_DNA. DR ProteinModelPortal; C6HYT5; -. DR Proteomes; UP000009374; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000009374}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000009374}. FT DOMAIN 344 509 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 518 AA; 57865 MW; 289E13027E681424 CRC64; MARQIAELSH ETGRQIALLI TREGTVAMVV VGTAREIYLE TLPPSRSGSR SLRGLRMVHT HLLGEALSQD DLNDLALLRL DAMVAILVNR SSGLPEKLCV ATIDPDPEAA SPWIVDPPRP VGPEAYDSSG RVEALEDELA RSLSDATKHT TGQERGLLVS VSTASISDQE DALAELSELA RSADVDVLGV VRQRVARYHP TTLMSIDRLK SLLIHALKLH ATLIIFEQEL SPNQVRKIAE MTELKVIDRT QLILDIFARR AHSRDGKLQV ELAQLKYLLP RLFERSTALS RLTGGIGGRG PGETRLEEDR RRVRDRIASL GAKLRHLEVE RAGRKSRRRE AAIPVVSLVG YTNVGKSTLL NRLTKSEVLV EDKMFATLDP TSRRLRFPRE REIILTDTVG FIRDLPADLR RAFMATFDEL RDADLIVHVA DGSHPQCELM IERVTEILRE MELDRIPTLL LFNKSDRLDA GTRETLSLRH PEGVFVSAMD PATLRPLEEI LQRRLFERPL TSLADGSP // ID C6J5X5_9BACL Unreviewed; 428 AA. AC C6J5X5; DT 01-SEP-2009, integrated into UniProtKB/TrEMBL. DT 01-SEP-2009, sequence version 1. DT 07-JUN-2017, entry version 39. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:EES71556.1}; GN ORFNames=POTG_03779 {ECO:0000313|EMBL:EES71556.1}; OS Paenibacillus sp. oral taxon 786 str. D14. OC Bacteria; Firmicutes; Bacilli; Bacillales; Paenibacillaceae; OC Paenibacillus. OX NCBI_TaxID=621372 {ECO:0000313|EMBL:EES71556.1, ECO:0000313|Proteomes:UP000003981}; RN [1] {ECO:0000313|EMBL:EES71556.1, ECO:0000313|Proteomes:UP000003981} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=D14 {ECO:0000313|EMBL:EES71556.1, RC ECO:0000313|Proteomes:UP000003981}; RG The Broad Institute Genome Sequencing Platform; RA Ward D., Young S.K., Kodira C.D., Zeng Q., Koehrsen M., Alvarado L., RA Berlin A., Borenstein D., Chen Z., Engels R., Freedman E., RA Gellesch M., Goldberg J., Griggs A., Gujja S., Heiman D., Hepburn T., RA Howarth C., Jen D., Larson L., Lewis B., Mehta T., Park D., RA Pearson M., Roberts A., Saif S., Shea T., Shenoy N., Sisk P., RA Stolte C., Sykes S., Walk T., White J., Yandava C., Allen-Vercoe E., RA Strauss J., Sibley C., White A., Lander E., Nusbaum C., Galagan J., RA Birren B.; RT "The Genome Sequence of Paenibacillus sp. D14."; RL Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GG695991; EES71556.1; -; Genomic_DNA. DR ProteinModelPortal; C6J5X5; -. DR STRING; 621372.POTG_03779; -. DR EnsemblBacteria; EES71556; EES71556; POTG_03779. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000003981; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000003981}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000003981}. FT DOMAIN 203 371 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 162 189 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 428 AA; 48510 MW; A2BE2EB1EB880DD7 CRC64; MTMTEQQQLE QKAILVGVNL NHQSDFDYSM EELANLAEAC DIEVVGVLTQ NLPKVTPSHY IGTGKIAEVR ALLEAHDGNL VIFNDELSPS QLRNLESDLE CKVIDRTLLI LDIFAERAKT REAQLQVEVA RLKYMLPRLI GLRESLGRQS GGVGTKNRGA GETRLELDRR RIEEKITALS RELETLVAHR QTQRKQRKKN DVPVVSLVGY TNAGKSTIMN ALLETYTPGM EKQVLEKDML FATLETSVRN IPLEDNKSFL LTDTVGFVSR LPHHLVKAFR STLEEVAEAD LLIHVVDYSN PEFARMIEIT HQTLKEIGIT DIPMIYAYNK SDRTEQAFPS VQGDIIYLAA KPRIGIAELV NEIRRRIFKD YVKCTMLIPY DKGSLVSYLN EQANVLETSY EEEGTKLVLE CKQSDYGRYK EYVLEGAE // ID C6J652_9BACL Unreviewed; 146 AA. AC C6J652; DT 01-SEP-2009, integrated into UniProtKB/TrEMBL. DT 01-SEP-2009, sequence version 1. DT 07-JUN-2017, entry version 16. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EES71546.1}; GN ORFNames=POTG_03879 {ECO:0000313|EMBL:EES71546.1}; OS Paenibacillus sp. oral taxon 786 str. D14. OC Bacteria; Firmicutes; Bacilli; Bacillales; Paenibacillaceae; OC Paenibacillus. OX NCBI_TaxID=621372 {ECO:0000313|EMBL:EES71546.1, ECO:0000313|Proteomes:UP000003981}; RN [1] {ECO:0000313|EMBL:EES71546.1, ECO:0000313|Proteomes:UP000003981} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=D14 {ECO:0000313|EMBL:EES71546.1, RC ECO:0000313|Proteomes:UP000003981}; RG The Broad Institute Genome Sequencing Platform; RA Ward D., Young S.K., Kodira C.D., Zeng Q., Koehrsen M., Alvarado L., RA Berlin A., Borenstein D., Chen Z., Engels R., Freedman E., RA Gellesch M., Goldberg J., Griggs A., Gujja S., Heiman D., Hepburn T., RA Howarth C., Jen D., Larson L., Lewis B., Mehta T., Park D., RA Pearson M., Roberts A., Saif S., Shea T., Shenoy N., Sisk P., RA Stolte C., Sykes S., Walk T., White J., Yandava C., Allen-Vercoe E., RA Strauss J., Sibley C., White A., Lander E., Nusbaum C., Galagan J., RA Birren B.; RT "The Genome Sequence of Paenibacillus sp. D14."; RL Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GG695992; EES71546.1; -; Genomic_DNA. DR ProteinModelPortal; C6J652; -. DR STRING; 621372.POTG_03879; -. DR EnsemblBacteria; EES71546; EES71546; POTG_03879. DR OrthoDB; POG091H24Y9; -. DR BioCyc; PSP621372-HMP:GTTW-3944-MONOMER; -. DR Proteomes; UP000003981; Unassembled WGS sequence. DR InterPro; IPR025121; GTPase_HflX_N. DR Pfam; PF13167; GTP-bdg_N; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000003981}; KW Reference proteome {ECO:0000313|Proteomes:UP000003981}. FT DOMAIN 38 81 GTP-bdg_N. {ECO:0000259|Pfam:PF13167}. SQ SEQUENCE 146 AA; 15567 MW; 6303E3CAB7062039 CRC64; MIMSKVHLHE TTTHQTDVAV LVSLVTSETK QSGINSDYSL AELVQLAETG GVEVAVTVVQ YREKPDPRWL IGKGKVLELR DRHTGAGGKP AGNGSPPYPP ADRRVETSAG GGHEAPATAS CASEGQRGSA NRPDKKPLRI SRQTME // ID C6JKP4_FUSVA Unreviewed; 599 AA. AC C6JKP4; DT 01-SEP-2009, integrated into UniProtKB/TrEMBL. DT 01-SEP-2009, sequence version 1. DT 07-JUN-2017, entry version 39. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:EES64313.1}; GN ORFNames=FVAG_01804 {ECO:0000313|EMBL:EES64313.1}; OS Fusobacterium varium ATCC 27725. OC Bacteria; Fusobacteria; Fusobacteriales; Fusobacteriaceae; OC Fusobacterium. OX NCBI_TaxID=469618 {ECO:0000313|EMBL:EES64313.1, ECO:0000313|Proteomes:UP000004505}; RN [1] {ECO:0000313|EMBL:EES64313.1, ECO:0000313|Proteomes:UP000004505} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 27725 {ECO:0000313|EMBL:EES64313.1, RC ECO:0000313|Proteomes:UP000004505}; RG The Broad Institute Genome Sequencing Platform; RA Earl A., Ward D., Feldgarden M., Gevers D., Strauss J., Ambrose C.E., RA Allen-Vercoe E., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., RA Haas B., Abouelleil A., Alvarado L., Arachchi H.M., Berlin A., RA Brown A., Chapman S.B., Chen Z., Dunbar C., Freedman E., Gearin G., RA Gellesch M., Goldberg J., Griggs A., Gujja S., Heiman D., Howarth C., RA Larson L., Lui A., MacDonald P.J.P., Mehta T., Montmayeur A., RA Murphy C., Neiman D., Pearson M., Priest M., Roberts A., Saif S., RA Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., Wortman J., RA Nusbaum C., Birren B.; RT "The Genome Sequence of Fusobacterium varium ATCC 27725."; RL Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EES64313.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACIE02000030; EES64313.1; -; Genomic_DNA. DR RefSeq; WP_005951539.1; NZ_GL988001.1. DR ProteinModelPortal; C6JKP4; -. DR STRING; 469618.FVAG_01804; -. DR EnsemblBacteria; EES64313; EES64313; FVAG_01804. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000004505; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000004505}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000004505}. FT DOMAIN 364 541 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 599 AA; 67256 MW; 8FD42FE1E21F3C98 CRC64; MIKGNTEGIK DFILNELDSL HDITVEKNKI IEPEMLTLIA SVSSRINREI NIAIDRKGNV TEISIGDSSS VQLPFLNVQE KRLSGTRVIH THPSGSSNLS NIDISALTKL KLDCIVAIGI NEDSITGMSI GFCSVDGNDL SHEIVGPLSV EQIVNYDFLS KIEEIESFLK KREIIENDDE YAILVGLDDN ESLDELAELA RACNVKVVAK FFQKKTKIDS CYFIGPGKAQ ELAVFKQLKK ANLIIFDEEL SGLQVRNLEE LTSCKVIDRT VLILEIFATR ARTREAKIQV ELAQLKYRSS RLLGFGSTMS RTGGGVGTKG PGEKKLEIDK RRIRETIYDL KQELEKIRKT RITQREKRDE SGIPKISLVG YTNVGKSTLR NLLVDMYAAD NTSKKEAVFA ENMLFATLDI TTRAIVLPDK RVASLTDTVG FVRKLPHDLV EAFKSTLEEV SFSDLIIHVV DVSSETASEQ ISAVEKVLEE LNALDKPSFL ALNKFEMASP EQLITIKEKF SKYQMIEISA KENKNINEFL QMIVALLPQT TRKCTYLIPY SDTSMSAFLH RNSIIQEEEY EGEGIKITAI VNDEVYNKCK KFMIEENIC // ID C6LAK6_9FIRM Unreviewed; 415 AA. AC C6LAK6; DT 22-SEP-2009, integrated into UniProtKB/TrEMBL. DT 22-SEP-2009, sequence version 1. DT 07-JUN-2017, entry version 48. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:EET62613.1}; GN ORFNames=BRYFOR_05648 {ECO:0000313|EMBL:EET62613.1}; OS Marvinbryantia formatexigens DSM 14469. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Lachnospiraceae; OC Marvinbryantia. OX NCBI_TaxID=478749 {ECO:0000313|EMBL:EET62613.1, ECO:0000313|Proteomes:UP000005561}; RN [1] {ECO:0000313|EMBL:EET62613.1, ECO:0000313|Proteomes:UP000005561} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 14469 {ECO:0000313|EMBL:EET62613.1, RC ECO:0000313|Proteomes:UP000005561}; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Nelson J., Hou S., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Nash W.E., Warren W., Chinwalla A., Mardis E.R., RA Wilson R.K.; RL Submitted (JUL-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EET62613.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACCL02000002; EET62613.1; -; Genomic_DNA. DR RefSeq; WP_006860448.1; NZ_ACCL02000002.1. DR ProteinModelPortal; C6LAK6; -. DR STRING; 478749.BRYFOR_05648; -. DR EnsemblBacteria; EET62613; EET62613; BRYFOR_05648. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000005561; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000005561}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000005561}. FT DOMAIN 201 365 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 160 194 {ECO:0000256|SAM:Coils}. FT COILED 343 370 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 415 AA; 46333 MW; 1F0628782662D4B0 CRC64; MTGIEISTPE ERVILLGVSV TDADGAKQSL DELEELAKTA GAVTVGKMLQ NREQIHPGTY IGRGKIEEVK QMAYALEADA VICDDELSPA QLHNLQQELD MKVLDRTLII LDIFAARAST SEGKIQVELA QLKYRQARLV GLRNSLSRLG GGIGTRGPGE KKLEMDRRLI KDRIAQLNRE LSEVKRHREV TRSRRMRQQT PVAAIVGYTN AGKSTLLNTL TGSQVMEEDK LFATLDPTTR VLELPSGQEM LLTDTVGFIR KLPHHLIDAF RSTLEEAKYA DIILHVVDAS NPQAEQQMAV VYETLENLGV SGKTVITLFN KQDKTLTGET LRDSRADRVI PVSAKYGSRL EELKAVLEEI LNERNVLIER LYSYSDAGLI QLIRRHGQLL QEEYRADGIY VRAYVPMEIY GAVSP // ID C6PW97_9CLOT Unreviewed; 592 AA. AC C6PW97; DT 22-SEP-2009, integrated into UniProtKB/TrEMBL. DT 22-SEP-2009, sequence version 1. DT 07-JUN-2017, entry version 48. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=CcarbDRAFT_3064 {ECO:0000313|EMBL:EET86511.1}; OS Clostridium carboxidivorans P7. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=536227 {ECO:0000313|EMBL:EET86511.1, ECO:0000313|Proteomes:UP000004198}; RN [1] {ECO:0000313|EMBL:EET86511.1, ECO:0000313|Proteomes:UP000004198} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=P7 {ECO:0000313|EMBL:EET86511.1, RC ECO:0000313|Proteomes:UP000004198}; RG US DOE Joint Genome Institute (JGI-PGF); RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., RA Bruce D., Goodwin L., Pitluck S., Larimer F., Land M.L., Hauser L., RA Hemme C.L.; RT "The draft genome of Clostridium carboxidivorans P7."; RL Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EET86511.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACVI01000052; EET86511.1; -; Genomic_DNA. DR RefSeq; WP_007061949.1; NZ_GG770691.1. DR ProteinModelPortal; C6PW97; -. DR STRING; 536227.CLCAR_2636; -. DR EnsemblBacteria; EET86511; EET86511; CcarbDRAFT_3064. DR KEGG; cck:Ccar_17160; -. DR PATRIC; fig|536227.13.peg.3614; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR KO; K03665; -. DR Proteomes; UP000004198; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000004198}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000004198}. FT DOMAIN 362 539 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 592 AA; 66964 MW; EFF638A48F343CB5 CRC64; MIYGNIEGVK SSILARLEKV YEMKMPKDSI CTEELIELLC DVTTYLNREV SVGINRKGTV ISVAIGDSST VEIPEIDIKE RKLSQVRIIH THPNGNSRLS AIDISALIKL KLDCITAIGV EDNKYTDMTL GFCGIENDLF VAESTKPLSI DAGIKFNILD RIKYIEDIIK DENIIDDDSE RAILVGVESE ESIDELEELA KACNVKVVYK VLQKRSIIDS AFYVGKGKVD EIALLRQGYS ANVIIFDDEL SASQVRNLEE NIGAKVIDRT TLILEIFATR ARSREAKIQV ELAQLKYRLP RLSGLGTVLS RTGGGIGTKG PGEKKLETDK RHIREKIYDL IKELKKIKQV RETQRERRNE LQKVSLVGYT NAGKSTLRNK LCEIAMPKEA VHKEKVFEAD MLFATLDITT RAIELSDSRI ITVTDTVGFI RKLPHDLVEA FKSTLEEVIY SDLLLHVVDI SSDYVEEQID AVNSVLGQLG VNNKPMMLVL NKIDKASKER IEEIKEKYNK IEVVCISAKQ EHNLDLLLQE VSKLLPYTLK EAEYLIPYTD QSMVAFLHRN SKVKDEEYRE DGTYICALAD DEVYNRCEKY MI // ID C6RNR5_ACIRA Unreviewed; 446 AA. AC C6RNR5; DT 22-SEP-2009, integrated into UniProtKB/TrEMBL. DT 22-SEP-2009, sequence version 1. DT 30-AUG-2017, entry version 40. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:EET82525.1}; GN ORFNames=ACIRA0001_3243 {ECO:0000313|EMBL:EET82525.1}; OS Acinetobacter radioresistens SK82. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Moraxellaceae; Acinetobacter. OX NCBI_TaxID=596318 {ECO:0000313|EMBL:EET82525.1, ECO:0000313|Proteomes:UP000018419}; RN [1] {ECO:0000313|EMBL:EET82525.1, ECO:0000313|Proteomes:UP000018419} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SK82 {ECO:0000313|EMBL:EET82525.1, RC ECO:0000313|Proteomes:UP000018419}; RA Madupu R., Durkin A.S., Torralba M., Methe B., Sutton G.G., RA Strausberg R.L., Nelson K.E.; RL Submitted (JUL-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EET82525.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACVR01000036; EET82525.1; -; Genomic_DNA. DR RefSeq; WP_005405127.1; NZ_ACVR01000036.1. DR ProteinModelPortal; C6RNR5; -. DR EnsemblBacteria; EET82525; EET82525; ACIRA0001_3243. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000018419; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000018419}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000018419}. FT DOMAIN 199 364 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 446 AA; 50215 MW; 7EAA2D56B1E73B8F CRC64; MEYFERHQGG ERAILVSVSV QLLEDIDTEE FRLLAQSAGA EILHHVTAQR IKPDPKLFIG SGKAEEIAEL VKTEEIDLVI FNHSLSPAQE RNLERVMQCR VIDRTGLILD IFAQRARTHE GKLQVELAQL EHLSTRLVRG WTHLERQKGG IGLRGPGESQ LETDRRLLRI RMGQLKDKLE KVRQTRMQGR AARQKAAIPT VSLVGYTNAG KSTLFNILAN TEVYAANQLF ATLDPTLRRL EWDGIGSLVL ADTVGFVRNL PHSLVESFKA TLEETLEATL LLHVIDSSTP DMMEQIDAVE SVLKEIGADV PVLRVYNKID VSGEAAKIIY AKPHMPERVY VSAHSGQGLE LLRQAVQECL MGQLQQFELV LNPAYGKLRT QLYALNVIQS EAYDDEGQLH LTVNMAPHKL EQLIKQAHLP IDEILGQNSQ QFKRPLEEFE IRDQIG // ID C6W6J5_DYAFD Unreviewed; 411 AA. AC C6W6J5; DT 22-SEP-2009, integrated into UniProtKB/TrEMBL. DT 22-SEP-2009, sequence version 1. DT 07-JUN-2017, entry version 65. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Dfer_3121 {ECO:0000313|EMBL:ACT94335.1}; OS Dyadobacter fermentans (strain ATCC 700827 / DSM 18053 / NS114). OC Bacteria; Bacteroidetes; Cytophagia; Cytophagales; Cytophagaceae; OC Dyadobacter. OX NCBI_TaxID=471854 {ECO:0000313|EMBL:ACT94335.1, ECO:0000313|Proteomes:UP000002011}; RN [1] {ECO:0000313|EMBL:ACT94335.1, ECO:0000313|Proteomes:UP000002011} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700827 / DSM 18053 / NS114 RC {ECO:0000313|Proteomes:UP000002011}; RX PubMed=21304649; DOI=10.4056/sigs.19262; RA Lang E., Lapidus A., Chertkov O., Brettin T., Detter J.C., Han C., RA Copeland A., Glavina Del Rio T., Nolan M., Chen F., Lucas S., Tice H., RA Cheng J.F., Land M., Hauser L., Chang Y.J., Jeffries C.D., Kopitz M., RA Bruce D., Goodwin L., Pitluck S., Ovchinnikova G., Pati A., RA Ivanova N., Mavrommatis K., Chen A., Palaniappan K., Chain P., RA Bristow J., Eisen J.A., Markowitz V., Hugenholtz P., Goker M., RA Rohde M., Kyrpides N.C., Klenk H.P.; RT "Complete genome sequence of Dyadobacter fermentans type strain RT (NS114)."; RL Stand. Genomic Sci. 1:133-140(2009). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001619; ACT94335.1; -; Genomic_DNA. DR RefSeq; WP_015812583.1; NC_013037.1. DR ProteinModelPortal; C6W6J5; -. DR STRING; 471854.Dfer_3121; -. DR EnsemblBacteria; ACT94335; ACT94335; Dfer_3121. DR KEGG; dfe:Dfer_3121; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000002011; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000002011}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000002011}. FT DOMAIN 207 392 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 411 AA; 46966 MW; D786155EFDB69871 CRC64; MIDKKKLYST AAKKETAVLV AVSTQKQNAE KTKEYLEELA FLATTLGVET VQTFTQNLER TDIRTYTGKG KLEEILIYVT ANPVDMIIYD DDLTPSQVRN LEAVFKDIKV IDRSLLILAI FAMRAQTAQA KLQVELAQYQ YMYPRLTRLW THLSRQSGAG VGMRGPGETE LETDRRIVKD RIAFLKEKLE KVDKQSVTRR KERDRLVRVA IVGYTNVGKS TLMRNLSKAD VFAENKLFAT VDSTVRKVNM ENIPFLLTDT VGFIRKLPTT LIESFKSTLD EVREADILMH VVDISHASFE EHLDVVNKTL EEIGAANKPS ILVFNKIDLY KPSYNDEEEE QAAAPSTQEI LDQLKRSYIA EKADHVVFIS AQEKENIDEL KRTLFSLVKE KHFSIYPNWL DLGYTPVETE E // ID C6WAC0_ACTMD Unreviewed; 480 AA. AC C6WAC0; DT 22-SEP-2009, integrated into UniProtKB/TrEMBL. DT 22-SEP-2009, sequence version 1. DT 07-JUN-2017, entry version 55. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Amir_1436 {ECO:0000313|EMBL:ACU35387.1}; OS Actinosynnema mirum (strain ATCC 29888 / DSM 43827 / NBRC 14064 / IMRU OS 3971). OC Bacteria; Actinobacteria; Pseudonocardiales; Pseudonocardiaceae; OC Actinosynnema. OX NCBI_TaxID=446462 {ECO:0000313|EMBL:ACU35387.1, ECO:0000313|Proteomes:UP000002213}; RN [1] {ECO:0000313|EMBL:ACU35387.1, ECO:0000313|Proteomes:UP000002213} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29888 / DSM 43827 / NBRC 14064 / IMRU 3971 RC {ECO:0000313|Proteomes:UP000002213}; RX PubMed=21304636; DOI=10.4056/sigs.21137; RA Land M., Lapidus A., Mayilraj S., Chen F., Copeland A., Del Rio T.G., RA Nolan M., Lucas S., Tice H., Cheng J.F., Chertkov O., Bruce D., RA Goodwin L., Pitluck S., Rohde M., Goker M., Pati A., Ivanova N., RA Mavromatis K., Chen A., Palaniappan K., Hauser L., Chang Y.J., RA Jeffries C.C., Brettin T., Detter J.C., Han C., Chain P., RA Tindall B.J., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P., RA Kyrpides N.C., Klenk H.P.; RT "Complete genome sequence of Actinosynnema mirum type strain (101)."; RL Stand. Genomic Sci. 1:46-53(2009). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001630; ACU35387.1; -; Genomic_DNA. DR RefSeq; WP_015800277.1; NC_013093.1. DR ProteinModelPortal; C6WAC0; -. DR STRING; 446462.Amir_1436; -. DR EnsemblBacteria; ACU35387; ACU35387; Amir_1436. DR KEGG; ami:Amir_1436; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000002213; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000002213}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000002213}. FT DOMAIN 254 423 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 480 AA; 52195 MW; 64D2AA19BEA4EC0F CRC64; MRDNDNHDDD RFDRDEELST GDLALAERAA LRRVAGLSTE LEDVTEVEYR QLRLERVVLV GVWTEGTAAD SEASLAELAL LAETAGSQVL EGLVQRRDRP DPATYIGSGK VEQLRDVVIA TGADTVICDG ELSPGQLRQL EERLKVKVID RTALILDIFA QHASSKEGKA QVELAQLQYL LPRLRGWGES LSRQAGGRAG GGNGGVGLRG PGETKLETDR RRIRARIAKL RREIASMGVI RETKRSGRVA NAVPSVAIAG YTNAGKSSLL NALTSAGVLV QDALFATLDT TTRRTSTPDG LPYTLTDTVG FVRHLPHQLV EAFRSTLEEV ADADLLIHVV DGSDSMPEKQ VAAVREVIGE IVEKREEPMP PELLVVNKVD AVDELVQARL RNLFPGSQLV SAHSGEGVEE LRRVIAGLIP RPEVMVDALV PYARGELVAR VHREGEVLKE RHTEEGTELS ARVHPDLAGA LEQYAVGSRS // ID C6WV51_METML Unreviewed; 378 AA. AC C6WV51; DT 22-SEP-2009, integrated into UniProtKB/TrEMBL. DT 22-SEP-2009, sequence version 1. DT 30-AUG-2017, entry version 54. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Mmol_0891 {ECO:0000313|EMBL:ACT47800.1}; OS Methylotenera mobilis (strain JLW8 / ATCC BAA-1282 / DSM 17540). OC Bacteria; Proteobacteria; Betaproteobacteria; Nitrosomonadales; OC Methylophilaceae; Methylotenera. OX NCBI_TaxID=583345 {ECO:0000313|EMBL:ACT47800.1, ECO:0000313|Proteomes:UP000002742}; RN [1] {ECO:0000313|Proteomes:UP000002742} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=JLW8 / ATCC BAA-1282 / DSM 17540 RC {ECO:0000313|Proteomes:UP000002742}; RG US DOE Joint Genome Institute; RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., RA Bruce D., Goodwin L., Pitluck S., LaButti K.M., Clum A., Larimer F., RA Land M., Hauser L., Kyrpides N., Mikhailova N., Kayluzhnaya M., RA Chistoserdova L.; RT "Complete sequence of Methylotenera mobilis JLW8."; RL Submitted (JUL-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001672; ACT47800.1; -; Genomic_DNA. DR ProteinModelPortal; C6WV51; -. DR STRING; 583345.Mmol_0891; -. DR EnsemblBacteria; ACT47800; ACT47800; Mmol_0891. DR KEGG; mmb:Mmol_0891; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000002742; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000002742}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000002742}. FT DOMAIN 202 371 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 161 188 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 378 AA; 41973 MW; 4B31315AB9CC4BCF CRC64; MKDLFERPSG GDAAILVSVD FGENDYQESL EELRQLSLSA GLAVLGKVEG KRSVPDAKLF IGSGKADELA QMMQATESHV AVFNHDLTPS QQRNLERLLQ ARVVDRTGLI LDIFSQRAQT HEGKLQVELA QLEHLSTRLV RGWTHLERQK GGIGVRGGPG ETQLELDRRM LRVRVKQLRE KLLKLKAQRG MQRRARKRSN VMTVSLVGYT NAGKSTIFNR LTKANIYAAD QLFATLDTTT HKIYIEGCGS VVLSDTVGFI KHLPHALVEA FGATLEEAVQ ADLLLHIVDT ASTNRDEQIA QVNKVLHEIG ASEVPQILVY NQIDRVGLEP AIGRDEYGRI TSLHVSAKTG EGLDFLRAAM AEHYQYVQKQ STEESAFI // ID C6WWM7_METML Unreviewed; 447 AA. AC C6WWM7; DT 22-SEP-2009, integrated into UniProtKB/TrEMBL. DT 22-SEP-2009, sequence version 1. DT 30-AUG-2017, entry version 55. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Mmol_1420 {ECO:0000313|EMBL:ACT48326.1}; OS Methylotenera mobilis (strain JLW8 / ATCC BAA-1282 / DSM 17540). OC Bacteria; Proteobacteria; Betaproteobacteria; Nitrosomonadales; OC Methylophilaceae; Methylotenera. OX NCBI_TaxID=583345 {ECO:0000313|EMBL:ACT48326.1, ECO:0000313|Proteomes:UP000002742}; RN [1] {ECO:0000313|Proteomes:UP000002742} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=JLW8 / ATCC BAA-1282 / DSM 17540 RC {ECO:0000313|Proteomes:UP000002742}; RG US DOE Joint Genome Institute; RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., RA Bruce D., Goodwin L., Pitluck S., LaButti K.M., Clum A., Larimer F., RA Land M., Hauser L., Kyrpides N., Mikhailova N., Kayluzhnaya M., RA Chistoserdova L.; RT "Complete sequence of Methylotenera mobilis JLW8."; RL Submitted (JUL-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001672; ACT48326.1; -; Genomic_DNA. DR RefSeq; WP_015832361.1; NC_012968.1. DR ProteinModelPortal; C6WWM7; -. DR STRING; 583345.Mmol_1420; -. DR EnsemblBacteria; ACT48326; ACT48326; Mmol_1420. DR KEGG; mmb:Mmol_1420; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; VILEIFH; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000002742; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000002742}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000002742}. FT DOMAIN 222 392 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 187 214 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 447 AA; 49732 MW; DFF3821501FEBEB5 CRC64; MQKEVKERSN LALVAAVQLP NVSDAEFEAS LTELRELAKT LGYDVVKTFV QKRAGFDIKA YLGEGKREEI RAFVNHESYD VEFDKAPPNL NDWEIDTVLV DHEISPSQAR NLEKEVGCEV MDRTMVILEI FHRNARSRAA RAQVEIARLG YMAPRLREAA KLAGPQGRQR SGEGGRGAGE SHTELDRRKV RDRIAELQQD IIAMEAERKT QRARRQGRQG LAGVALVGYT NAGKSTLMRA LTGSEVLVAN KLFATLDTTV RALYPESIPR ILVSDTVGFI KNLPHGLVAS FKSTLDEALD ASLLLHVIDA SDSGFERQLE VTNEVLAEIG ADDVPRIRVF NKIDYVGDDA AQAALTLTLQ SRYPDCVVMS AKRPDDVAQL HQKIVAIYQQ DQIEAEIFLP WEAQQLRKNI YATCQVLAET SDDTGAFFKV RGEVDAVRKL SESVKLI // ID C6WZG0_FLAB3 Unreviewed; 403 AA. AC C6WZG0; DT 22-SEP-2009, integrated into UniProtKB/TrEMBL. DT 22-SEP-2009, sequence version 1. DT 07-JUN-2017, entry version 54. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=FIC_00017 {ECO:0000313|EMBL:ACU06495.1}; OS Flavobacteriaceae bacterium (strain 3519-10). OC Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales; OC Flavobacteriaceae. OX NCBI_TaxID=531844 {ECO:0000313|EMBL:ACU06495.1, ECO:0000313|Proteomes:UP000001512}; RN [1] {ECO:0000313|EMBL:ACU06495.1, ECO:0000313|Proteomes:UP000001512} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=3519-10 {ECO:0000313|EMBL:ACU06495.1, RC ECO:0000313|Proteomes:UP000001512}; RX PubMed=18622572; DOI=10.1007/s00792-008-0178-2; RA Raymond J.A., Christner B.C., Schuster S.C.; RT "A bacterial ice-binding protein from the Vostok ice core."; RL Extremophiles 12:713-717(2008). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001673; ACU06495.1; -; Genomic_DNA. DR RefSeq; WP_012781642.1; NC_013062.1. DR ProteinModelPortal; C6WZG0; -. DR STRING; 531844.FIC_00017; -. DR EnsemblBacteria; ACU06495; ACU06495; FIC_00017. DR KEGG; fba:FIC_00017; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000001512; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000001512}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000001512}. FT DOMAIN 200 384 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 403 AA; 46878 MW; 14FAA4DA6448604B CRC64; MLDNKEHLYE KAVLVGVITQ NQDEEKLVEY MDELEFLALT AGATVVKRFT QKLTQPDPKT FIGSGKAQEV RDYIKENDIG TVIFDDELSP SQLKNLEREI EVKILDRTNL ILDIFAQRAQ TSYARTQVEL AQYQYLLPRL TRMWTHLERQ KGGIGMRGPG ETEIETDRRI IRDRISLLKE KLKTIDRQMA TQRNNRGKVV RAALVGYTNV GKSTLMNAIS KSDVFAENKL FATLDTTVRK VVIGNLPFLL TDTVGFIRKL PTQLVESFKS TLDEVREADL LIHVVDISHE SFEDHIDSVN QILMEINAHQ KPMIMVFNKI DDFSYEKKDE FDLTPESRKN IPLAEWQNTW MSKSKFPTVF ISALTKENFE EMKKMIYDEV LKIHISRFPY NDFLFEYFEE EEK // ID C6X7L1_METGS Unreviewed; 444 AA. AC C6X7L1; DT 22-SEP-2009, integrated into UniProtKB/TrEMBL. DT 22-SEP-2009, sequence version 1. DT 30-AUG-2017, entry version 56. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Msip34_0004 {ECO:0000313|EMBL:ACT49253.1}; OS Methylovorus glucosetrophus (strain SIP3-4). OC Bacteria; Proteobacteria; Betaproteobacteria; Nitrosomonadales; OC Methylophilaceae; Methylovorus. OX NCBI_TaxID=582744 {ECO:0000313|EMBL:ACT49253.1, ECO:0000313|Proteomes:UP000002743}; RN [1] {ECO:0000313|Proteomes:UP000002743} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SIP3-4 {ECO:0000313|Proteomes:UP000002743}; RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., RA Bruce D., Goodwin L., Pitluck S., Clum A., Larimer F., Land M., RA Hauser L., Kyrpides N., Mikhailova N., Kayluzhnaya M., RA Chistoserdova L.; RT "Complete sequence of chromosome of Methylovorus sp. SIP3-4."; RL Submitted (JUL-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001674; ACT49253.1; -; Genomic_DNA. DR RefSeq; WP_015829059.1; NC_012969.1. DR ProteinModelPortal; C6X7L1; -. DR STRING; 582744.Msip34_0004; -. DR EnsemblBacteria; ACT49253; ACT49253; Msip34_0004. DR KEGG; mei:Msip34_0004; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR KO; K03665; -. DR OMA; VILEIFH; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000002743; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000002743}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000002743}. FT DOMAIN 220 390 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 185 217 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 444 AA; 49457 MW; 8351E0BF64D7525C CRC64; MQTEVKDAPK YAIVASVQLP SVSDIEFEAS LTELRELAKT LGYHVVHTFV QKRSSFDTTA YLGIGKRQEI QAWVSHENEI AEQEDAPADS HLIEAILVDH EISPSQARNL EKETGCEVMD RTMVILEIFH RNARSRAAKA QVEIARLGYM APRLREAAKL AGPQGRQRSG VGGRGAGESS TELDRRKIRD RIAELQLEIL AMEAERKTQR ARRQQRQGLT SVALVGYTNA GKSTLMRALT GSEVLVANKL FATLDTTVRT LYPESVPRVL VSDTVGFIKN LPHGLVASFK STLDEALDAA LLLHVIDASD PGFERQLEVT DKVLEEINAD DVPRIRVFNK IDHVGDAAAQ AEREAALKAQ YPDCVVMSAR RPDDVARLHK MIVAFFQRDL IETEIFVPWA QQQLLGEIYA TCQVRGERSD EQGTFFQICG EASVLERLQQ KLSD // ID C6XEG1_METGS Unreviewed; 379 AA. AC C6XEG1; DT 22-SEP-2009, integrated into UniProtKB/TrEMBL. DT 22-SEP-2009, sequence version 1. DT 30-AUG-2017, entry version 59. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Msip34_1691 {ECO:0000313|EMBL:ACT50936.1}; OS Methylovorus glucosetrophus (strain SIP3-4). OC Bacteria; Proteobacteria; Betaproteobacteria; Nitrosomonadales; OC Methylophilaceae; Methylovorus. OX NCBI_TaxID=582744 {ECO:0000313|EMBL:ACT50936.1, ECO:0000313|Proteomes:UP000002743}; RN [1] {ECO:0000313|Proteomes:UP000002743} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SIP3-4 {ECO:0000313|Proteomes:UP000002743}; RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., RA Bruce D., Goodwin L., Pitluck S., Clum A., Larimer F., Land M., RA Hauser L., Kyrpides N., Mikhailova N., Kayluzhnaya M., RA Chistoserdova L.; RT "Complete sequence of chromosome of Methylovorus sp. SIP3-4."; RL Submitted (JUL-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001674; ACT50936.1; -; Genomic_DNA. DR RefSeq; WP_015830345.1; NC_012969.1. DR ProteinModelPortal; C6XEG1; -. DR STRING; 582744.Msip34_1691; -. DR EnsemblBacteria; ACT50936; ACT50936; Msip34_1691. DR KEGG; mei:Msip34_1691; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000002743; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000002743}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000002743}. FT DOMAIN 199 365 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 158 192 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 379 AA; 42096 MW; 60348E6BFD2E5430 CRC64; MFDRPSGGDA AVLVSVDFGD SGYEESLQEL RQLAITAGMD IRATIEGKRP KPDAKYFVGS GKADELAESL KSHEAQVAVF NHDLSPSQQR NLERLLESRV VDRTGLILDI FAQRAQSHEG KLQVELAQLE HLSTRLVRGW THLERQKGGI GVRGGPGETQ LELDRRMLRI RVKQLREKLA KLKQQRGMQR RSRKRSLVMS VSLVGYTNAG KSTLFNRLTQ SGVYAADQLF ATLDTTSRKL YIPDGGPVVL SDTVGFIKHL PHALVEAFGA TLEEAVQADL LLHVVDAASP VRDDQIAQVN KVLEEIGAEH VHQVLVLNQI DRAGLEPGLE RDEYGRICRI RISAKTGEGL ELVRQCLREH QQMLFAHQLE TSSPDVVPT // ID C6XJP9_HIRBI Unreviewed; 445 AA. AC C6XJP9; DT 22-SEP-2009, integrated into UniProtKB/TrEMBL. DT 22-SEP-2009, sequence version 1. DT 30-AUG-2017, entry version 63. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Hbal_1656 {ECO:0000313|EMBL:ACT59344.1}; OS Hirschia baltica (strain ATCC 49814 / DSM 5838 / IFAM 1418). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Hyphomonadaceae; Hirschia. OX NCBI_TaxID=582402 {ECO:0000313|EMBL:ACT59344.1, ECO:0000313|Proteomes:UP000002745}; RN [1] {ECO:0000313|Proteomes:UP000002745} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 49814 / DSM 5838 / IFAM 1418 RC {ECO:0000313|Proteomes:UP000002745}; RX PubMed=21705585; DOI=10.1128/JB.05453-11; RG US DOE Joint Genome Institute; RA Brown P.J., Kysela D.T., Buechlein A., Hemmerich C., Brun Y.V.; RT "Genome sequences of eight morphologically diverse RT alphaproteobacteria."; RL J. Bacteriol. 193:4567-4568(2011). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001678; ACT59344.1; -; Genomic_DNA. DR RefSeq; WP_015827494.1; NC_012982.1. DR ProteinModelPortal; C6XJP9; -. DR STRING; 582402.Hbal_1656; -. DR EnsemblBacteria; ACT59344; ACT59344; Hbal_1656. DR KEGG; hba:Hbal_1656; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR BioCyc; HBAL582402:GHMV-1678-MONOMER; -. DR Proteomes; UP000002745; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000002745}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000002745}. FT DOMAIN 206 378 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 445 AA; 49509 MW; B86F017DE7E263E6 CRC64; MNTSNLIDIS VPTQIAGIVI PALFDAPIYD QSRIEETQGL VEALGVELGF TDAVRIRKPN AAKLFGAGQL DLISERLDDC EGNLLVVDCS LSPIQQRNLE NTLNVKVMDR TGLILEIFGV RARSAEGRLQ VEMARQLYER SRLVRTWTHL ERQRGGTGFL AGPGESQLEA DRRMLDGRIA KLKSDLEAVR RTRRLQRAGR KRRGAPIVAL AGYTNAGKST LFNSLTHSSV FAADMPFATL DPTARDVELS SGKKISMIDT VGFITDLPTH LIESFRATIE EAIEADLLLH VRDISHPETD RQSSDVNDVL TKLEQDLNAD RPPVIEVWNK SDALSDDVLT ALKTTVENRD DIALTSATTG EGLDDLMQMV QDKLFASTRE FELKIEPKYG RARSWLHQNC DISNETVDEN GNVIIRVQLS VRELNEFAHE HPDLDMNLVI LSSKS // ID C6XX52_PEDHD Unreviewed; 396 AA. AC C6XX52; DT 22-SEP-2009, integrated into UniProtKB/TrEMBL. DT 22-SEP-2009, sequence version 1. DT 07-JUN-2017, entry version 54. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Phep_4167 {ECO:0000313|EMBL:ACU06358.1}; OS Pedobacter heparinus (strain ATCC 13125 / DSM 2366 / CIP 104194 / JCM OS 7457 / NBRC 12017 / NCIMB 9290 / NRRL B-14731 / HIM 762-3). OC Bacteria; Bacteroidetes; Sphingobacteriia; Sphingobacteriales; OC Sphingobacteriaceae; Pedobacter. OX NCBI_TaxID=485917 {ECO:0000313|EMBL:ACU06358.1, ECO:0000313|Proteomes:UP000000852}; RN [1] {ECO:0000313|EMBL:ACU06358.1, ECO:0000313|Proteomes:UP000000852} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 13125 / DSM 2366 / CIP 104194 / JCM 7457 / NBRC 12017 / RC NCIMB 9290 / NRRL B-14731 / HIM 762-3 RC {ECO:0000313|Proteomes:UP000000852}; RX PubMed=21304637; DOI=10.4056/sigs.22138; RA Han C., Spring S., Lapidus A., Del Rio T.G., Tice H., Copeland A., RA Cheng J.F., Lucas S., Chen F., Nolan M., Bruce D., Goodwin L., RA Pitluck S., Ivanova N., Mavromatis K., Mikhailova N., Pati A., RA Chen A., Palaniappan K., Land M., Hauser L., Chang Y.J., RA Jeffries C.C., Saunders E., Chertkov O., Brettin T., Goker M., RA Rohde M., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P., RA Kyrpides N.C., Klenk H.P., Detter J.C.; RT "Complete genome sequence of Pedobacter heparinus type strain (HIM RT 762-3)."; RL Stand. Genomic Sci. 1:54-62(2009). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001681; ACU06358.1; -; Genomic_DNA. DR RefSeq; WP_015809966.1; NZ_AQGK01000003.1. DR ProteinModelPortal; C6XX52; -. DR STRING; 485917.Phep_4167; -. DR EnsemblBacteria; ACU06358; ACU06358; Phep_4167. DR KEGG; phe:Phep_4167; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000000852; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000000852}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000000852}. FT DOMAIN 204 385 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 396 AA; 45530 MW; 8F906351F8D181FF CRC64; MGRQKYYDTA VKQERAVLVG VIRPGEKPEE TREYLDELAF LVDTAGGLVE HEFTQKMLKP DRATFVGTGK LEEIQAYVKS EEIDMVVFDD ELSPSQLRNI EKELQVKILD RSNLILDIFA GRAQTAQAKT QVELAQLQYL LPRLTRLWTH LERQKGGIGM RGPGETQIES DRRMILEKIS LLKTRLKQID RQNETQRKNR GQLIRVALVG YTNVGKSTIM NMLSKSEVFA ENKLFATLDT TVRKVVIENL PFLLSDTVGF IRKLPHHLVE CFKSTLDEVR EADILIHVVD VSHPNFEDQI NVVNETLKDL GARDKDTIMV FNKIDAYVSP EPDHEDEEKI VLTLDDFKKS WMGAENAPAL FISALHKENL EEFRQLLYGK VLAMHTERYP YDKLLY // ID C7D5J9_9RHOB Unreviewed; 452 AA. AC C7D5J9; DT 22-SEP-2009, integrated into UniProtKB/TrEMBL. DT 22-SEP-2009, sequence version 1. DT 07-JUN-2017, entry version 40. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:EET48181.1}; GN ORFNames=TR2A62_0705 {ECO:0000313|EMBL:EET48181.1}; OS Thalassobium sp. R2A62. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae; Thalassobium. OX NCBI_TaxID=633131 {ECO:0000313|EMBL:EET48181.1, ECO:0000313|Proteomes:UP000004701}; RN [1] {ECO:0000313|EMBL:EET48181.1, ECO:0000313|Proteomes:UP000004701} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=R2A62 {ECO:0000313|EMBL:EET48181.1, RC ECO:0000313|Proteomes:UP000004701}; RA Suzuki M., Ferriera S., Johnson J., Kravitz S., Beeson K., Sutton G., RA Rogers Y.-H., Friedman R., Frazier M., Venter J.C.; RL Submitted (MAY-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GG697169; EET48181.1; -; Genomic_DNA. DR ProteinModelPortal; C7D5J9; -. DR STRING; 633131.TR2A62_0705; -. DR EnsemblBacteria; EET48181; EET48181; TR2A62_0705. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000004701; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000004701}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000004701}. FT DOMAIN 208 377 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 452 AA; 49969 MW; D833285EBF6556DC CRC64; MGEDPNATAD PDTWAWVIRP DIKSDHDRRD PATSLAEAVS LARALPNLVV QGDEVVRLPK AHPGMLFGSG KIAEVKERLH DAEVDLVLID GPVTPVQQRN LEKEWGVKLL DRTGLILEIF SDRARTREGV LQVEMAALSY QRTRLVRAWT HLERQRGGLG FVGGPGETQI EADRRAIDDQ LVRLRKQLGK VEKTRALHRS ARAKVPFPIV ALVGYTNAGK STLFNRLTGA EVFAKDMLFA TLDPTMRKVD LPTGDEIILS DTVGFISDLP TELVASFRAT LEEVLDADLI LHVRDISSAD THEQSRDVME ILTKLGVGQD APLLEVWNKI DQVELDVRKG LNTASDRDDA IFVTSSVTGE GMDPLLAAIS DILNAAMKIE TLTLGFADGR ARAWLHNTGV VEDETQTETG FEITVKWNET DRSRFSSAEP QVLPTVVVDE EKDEAPRGEW LP // ID C7HAY0_9FIRM Unreviewed; 421 AA. AC C7HAY0; DT 13-OCT-2009, integrated into UniProtKB/TrEMBL. DT 13-OCT-2009, sequence version 1. DT 07-JUN-2017, entry version 41. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:EEU94963.1}; GN ORFNames=FAEPRAA2165_03494 {ECO:0000313|EMBL:EEU94963.1}; OS Faecalibacterium prausnitzii A2-165. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Ruminococcaceae; OC Faecalibacterium. OX NCBI_TaxID=411483 {ECO:0000313|EMBL:EEU94963.1, ECO:0000313|Proteomes:UP000004619}; RN [1] {ECO:0000313|EMBL:EEU94963.1, ECO:0000313|Proteomes:UP000004619} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=A2-165 {ECO:0000313|EMBL:EEU94963.1, RC ECO:0000313|Proteomes:UP000004619}; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Nelson J., Hou S., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Nash W.E., Warren W., Chinwalla A., Mardis E.R., RA Wilson R.K.; RL Submitted (AUG-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EEU94963.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACOP02000095; EEU94963.1; -; Genomic_DNA. DR RefSeq; WP_005936530.1; NZ_GG697158.2. DR ProteinModelPortal; C7HAY0; -. DR STRING; 411483.FAEPRAA2165_03494; -. DR EnsemblBacteria; EEU94963; EEU94963; FAEPRAA2165_03494. DR PATRIC; fig|411483.3.peg.2754; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000004619; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000004619}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000004619}. FT DOMAIN 209 368 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 175 202 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 421 AA; 45621 MW; 60CDDD0D75721EC2 CRC64; MSELYDILVE TPPTKVILLA LDQGLWDCER SLNELAALCE ANHMEAVASV TQKRQTPETG IVLGSGKLEE AAAAAGELGA ECAVFDGELT GSQIRNISTA LGGMEVIDRT MLILEIFRSR AVTNEGKLQT ELALLRYRLP RLQGMGESLS RQGGGGGGGG GARRGAGETK LELDRRHVHA RIDALAEKLA EMEKRRGESR KARAKTGMPV VSLVGYTNVG KSSLMNALCG PSVAEADMLF ATLDPTSRKL VLPSGMAVLL VDTVGFVSRL PHNLVEAFKS TLEEAAWSDV IVRVADAGDD QREEQLAVTD EVLDGLDCAD IPRLTVYNKC DKPNALNFDP DILLTSAKTG YGLDALLKKL DELLSDRVHT IRVLLPYDKL GLAAPMRERG SVQVEEYRED GLYLEGIVKT EDLHCFEGYL V // ID C7HUX2_9FIRM Unreviewed; 411 AA. AC C7HUX2; DT 13-OCT-2009, integrated into UniProtKB/TrEMBL. DT 13-OCT-2009, sequence version 1. DT 05-JUL-2017, entry version 51. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:EEU12421.1}; GN ORFNames=HMPREF0078_1029 {ECO:0000313|EMBL:EEU12421.1}; OS Anaerococcus vaginalis ATCC 51170. OC Bacteria; Firmicutes; Tissierellia; Tissierellales; Peptoniphilaceae; OC Anaerococcus. OX NCBI_TaxID=655811 {ECO:0000313|EMBL:EEU12421.1, ECO:0000313|Proteomes:UP000003821}; RN [1] {ECO:0000313|EMBL:EEU12421.1, ECO:0000313|Proteomes:UP000003821} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51170 {ECO:0000313|EMBL:EEU12421.1, RC ECO:0000313|Proteomes:UP000003821}; RA Muzny D., Qin X., Deng J., Jiang H., Liu Y., Qu J., Song X.-Z., RA Zhang L., Thornton R., Coyle M., Francisco L., Jackson L., Javaid M., RA Korchina V., Kovar C., Mata R., Mathew T., Ngo R., Nguyen L., RA Nguyen N., Okwuonu G., Ongeri F., Pham C., Simmons D., RA Wilczek-Boney K., Hale W., Jakkamsetti A., Pham P., Ruth R., RA San Lucas F., Warren J., Zhang J., Zhao Z., Zhou C., Zhu D., Lee S., RA Bess C., Blankenburg K., Forbes L., Fu Q., Gubbala S., Hirani K., RA Jayaseelan J.C., Lara F., Munidasa M., Palculict T., Patil S., RA Pu L.-L., Saada N., Tang L., Weissenberger G., Zhu Y., Hemphill L., RA Shang Y., Youmans B., Ayvaz T., Ross M., Santibanez J., Aqrawi P., RA Gross S., Joshi V., Fowler G., Nazareth L., Reid J., Worley K., RA Petrosino J., Highlander S., Gibbs R., Gibbs R.; RL Submitted (AUG-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EEU12421.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACXU01000015; EEU12421.1; -; Genomic_DNA. DR RefSeq; WP_004839069.1; NZ_GG700527.1. DR ProteinModelPortal; C7HUX2; -. DR STRING; 655811.HMPREF0078_1029; -. DR EnsemblBacteria; EEU12421; EEU12421; HMPREF0078_1029. DR GeneID; 32185563; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000003821; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000003821}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000003821}. FT DOMAIN 188 356 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 156 183 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 411 AA; 47376 MW; 7E096625DC9C8BF4 CRC64; MQEVIQVNVF EKNENPNKEF ELESLINTAG GKSVAKISQV ISKVNPAYYI GSGKVSEIED IAKKLDVKTV VFDVELSASQ LRNLEEKMKL HVVDWTTLIL DIFAQRANTK EAKLKIKLAQ LKYQLPRINK WFAYLSRQSG GIGTRGPGET MLETDKRAIV RDIRSLEEKL KDLEKTKSVN RKSRDKILNI SLLGYTNAGK STILNNMLKI FGKEKYVYSD DLLFATLDTS TRRLDFSNTK VTLTDTVGFI DNLSKELNDS FLTTLEEIKF SDMLLVVIDS SYDIETQLKT IDKALDDIDV GNKKILYVFN KIDKIENDTL LLGYKRKEEK IYISAKNQDD IIKLKEKIVD VIKDDYIKVK MKIPYEDGKV LDYIMTNYDI DNKDYDESSS ILEFDISKKD YNKYERYIEK N // ID C7JC47_ACEP3 Unreviewed; 448 AA. AC C7JC47; DT 13-OCT-2009, integrated into UniProtKB/TrEMBL. DT 13-OCT-2009, sequence version 1. DT 07-JUN-2017, entry version 55. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:BAH99875.1}; GN OrderedLocusNames=APA01_17470 {ECO:0000313|EMBL:BAH99875.1}; OS Acetobacter pasteurianus (strain NBRC 3283 / LMG 1513 / CCTM 1153). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales; OC Acetobacteraceae; Acetobacter. OX NCBI_TaxID=634452 {ECO:0000313|EMBL:BAH99875.1, ECO:0000313|Proteomes:UP000000948}; RN [1] {ECO:0000313|EMBL:BAH99875.1, ECO:0000313|Proteomes:UP000000948} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NBRC 3283 / LMG 1513 / CCTM 1153 RC {ECO:0000313|Proteomes:UP000000948}; RX PubMed=19638423; DOI=10.1093/nar/gkp612; RA Azuma Y., Hosoyama A., Matsutani M., Furuya N., Horikawa H., RA Harada T., Hirakawa H., Kuhara S., Matsushita K., Fujita N., RA Shirai M.; RT "Whole-genome analyses reveal genetic instability of Acetobacter RT pasteurianus."; RL Nucleic Acids Res. 37:5768-5783(2009). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AP011121; BAH99875.1; -; Genomic_DNA. DR ProteinModelPortal; C7JC47; -. DR STRING; 634452.APA01_17470; -. DR EnsemblBacteria; BAH99875; BAH99875; APA01_17470. DR KEGG; apt:APA01_17470; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000000948; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000000948}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000000948}. FT DOMAIN 219 388 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 448 AA; 49549 MW; 4EFDEF1DE578E8C8 CRC64; MRRQTGTFLL ATSFSEKKKK VATRAAVILP WERSAHGQDV RAAEARLEEA VGLTASIGLV IVRKDVLLLR SRRSATLLGK GQVDSLRIAV KADQVDVVVV DAKLSPAQQR NLETECGCKV IDRTGLILDI FGARAATKEG TVQVELAHLE YQRSRLVRLW THLERQRGGF GFLGGPGETQ IEADRRMIGD RIVRLKKDLE QVRRTRGLHR QARKRVPFPV VALVGYTNAG KSTLFNALTG ATVYAQDQLF ATLDPTMRAI DLPSGRRVIL SDTVGFISDL PTELIAAFRA TLEEVAEADI ILHVRDVAHP DSASQKKDVL GVLEGMAKDD MLEQDWPERI IEVLNKVDLL GGPEAIPQTE DTIAISAITG EGLETLLARI DARITQGMET VRYCLPLADG AASAWLYQHG EVVAREDKDE QTDITVRLST EDRARFERQF SHIQPMIA // ID C7LW62_DESBD Unreviewed; 540 AA. AC C7LW62; DT 13-OCT-2009, integrated into UniProtKB/TrEMBL. DT 13-OCT-2009, sequence version 1. DT 07-JUN-2017, entry version 54. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Dbac_3023 {ECO:0000313|EMBL:ACU91098.1}; OS Desulfomicrobium baculatum (strain DSM 4028 / VKM B-1378) OS (Desulfovibrio baculatus). OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfovibrionales; OC Desulfomicrobiaceae; Desulfomicrobium. OX NCBI_TaxID=525897 {ECO:0000313|EMBL:ACU91098.1, ECO:0000313|Proteomes:UP000002216}; RN [1] {ECO:0000313|EMBL:ACU91098.1, ECO:0000313|Proteomes:UP000002216} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 4028 / VKM B-1378 {ECO:0000313|Proteomes:UP000002216}; RX PubMed=21304634; DOI=10.4056/sigs.13134; RA Copeland A., Spring S., Goker M., Schneider S., Lapidus A., RA Del Rio T.G., Tice H., Cheng J.F., Chen F., Nolan M., Bruce D., RA Goodwin L., Pitluck S., Ivanova N., Mavrommatis K., Ovchinnikova G., RA Pati A., Chen A., Palaniappan K., Land M., Hauser L., Chang Y.J., RA Jeffries C.C., Meincke L., Sims D., Brettin T., Detter J.C., Han C., RA Chain P., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P., RA Kyrpides N.C., Klenk H.P., Lucas S.; RT "Complete genome sequence of Desulfomicrobium baculatum type strain RT (X)."; RL Stand. Genomic Sci. 1:29-37(2009). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001629; ACU91098.1; -; Genomic_DNA. DR RefSeq; WP_015775187.1; NC_013173.1. DR ProteinModelPortal; C7LW62; -. DR STRING; 525897.Dbac_3023; -. DR EnsemblBacteria; ACU91098; ACU91098; Dbac_3023. DR KEGG; dba:Dbac_3023; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; EREVIIT; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000002216; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000002216}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000002216}. FT DOMAIN 379 540 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 540 AA; 59414 MW; A19A47F9C21DE2DA CRC64; MASKPLGNLT GLKPSQITAI SRLYNRRFPD QGGCTPDQAR ELAILSRGVS RQLGVLINRK GVPVMVIVGE QDGILIPELS RHRQADSRLS GLRLLHTHLD SSLLTQEDLM DMVFLRLDAV SVLTVSSDGA PITCQIAHIL PPNADELPYQ VHPAMIWDDV DFDFGAGVRA LEDELARTGQ SVATTAREGA AILVSVASES KSAQERSLAE LAELAATAGL DVVGQVVQRV TRVNPKLILG RGKLAELEVL ALQKNAATLV FDQELTPTQQ RNLSEITERK VLDRTQLILD IFAQHAQTRE GKMQVEMAQL KYMMPRLVGQ SRALSRLAGG IGGRGPGESR LEMDRRKIRE RIAQIKTELG SVRKHRKSTR SRRDKAGLPI VSLVGYTNAG KSTLLNTLTK SVVLAENKLF ATLDPTSRRL RFPEDREIIL TDTVGFIRHL PADLREAFMA TLEELESADV LVHVADASHP EMEAQVQAVE SILRDLSIDG IPRILALNKI DRISEETRQT LGYVYPDAVF ISAIERPTLA PLVDRVKALL // ID C7LY04_ACIFD Unreviewed; 425 AA. AC C7LY04; DT 13-OCT-2009, integrated into UniProtKB/TrEMBL. DT 13-OCT-2009, sequence version 1. DT 07-JUN-2017, entry version 60. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Afer_0658 {ECO:0000313|EMBL:ACU53612.1}; OS Acidimicrobium ferrooxidans (strain DSM 10331 / JCM 15462 / NBRC OS 103882 / ICP). OC Bacteria; Actinobacteria; Acidimicrobiia; Acidimicrobiales; OC Acidimicrobiaceae; Acidimicrobium. OX NCBI_TaxID=525909 {ECO:0000313|EMBL:ACU53612.1, ECO:0000313|Proteomes:UP000000771}; RN [1] {ECO:0000313|EMBL:ACU53612.1, ECO:0000313|Proteomes:UP000000771} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 10331 / JCM 15462 / NBRC 103882 / ICP RC {ECO:0000313|Proteomes:UP000000771}; RX PubMed=21304635; DOI=10.4056/sigs.1463; RA Clum A., Nolan M., Lang E., Glavina Del Rio T., Tice H., Copeland A., RA Cheng J.F., Lucas S., Chen F., Bruce D., Goodwin L., Pitluck S., RA Ivanova N., Mavrommatis K., Mikhailova N., Pati A., Chen A., RA Palaniappan K., Goker M., Spring S., Land M., Hauser L., Chang Y.J., RA Jeffries C.C., Chain P., Bristow J., Eisen J.A., Markowitz V., RA Hugenholtz P., Kyrpides N.C., Klenk H.P., Lapidus A.; RT "Complete genome sequence of Acidimicrobium ferrooxidans type strain RT (ICP)."; RL Stand. Genomic Sci. 1:38-45(2009). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001631; ACU53612.1; -; Genomic_DNA. DR RefSeq; WP_015798107.1; NC_013124.1. DR ProteinModelPortal; C7LY04; -. DR STRING; 525909.Afer_0658; -. DR EnsemblBacteria; ACU53612; ACU53612; Afer_0658. DR KEGG; afo:Afer_0658; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; FNNHAHV; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000000771; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000000771}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000000771}. FT DOMAIN 202 364 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 161 195 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 425 AA; 46592 MW; 25B5E55D4A654FB2 CRC64; MTLIERSFRE RILLVGVVHH GERREAVEDS LAELAALVDT AGADVVDREL VRRDAVDPAT YVGSGKAAEL AERSEALDVD TVVFDDPLSP AQQRNLERIL GRTAIDRTAV ILDVFAQNAR SEEGRRQVEL ALLSYRLPRL RGRGVALSQQ VGRIGTRGPG ETKLEEDRRR IQARMAQLRR ELDQLARRRL VQRRARLASR QAQVALVGYT NVGKSALLRA LSGADVLVEN RLFATLDPRT RRVALPGGET ILVTDTVGFI RKLPHELIES FRSTLEQVAE ADLLLHVADA SSPDVAAQIA EVERTLAEIG ADRVPRLVVY NKVDLRPIDT LAAGVPEGVA ISAEHDIGLD DLRAAIAAAL DAMRRPRRYV VPAGRGDVLA LIHREGAVVR EEVDAERVLI DAVLDDASDR LVRRALGEAP PEPLG // ID C7M6Q2_CAPOD Unreviewed; 401 AA. AC C7M6Q2; DT 13-OCT-2009, integrated into UniProtKB/TrEMBL. DT 13-OCT-2009, sequence version 1. DT 07-JUN-2017, entry version 62. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Coch_0477 {ECO:0000313|EMBL:ACU92040.1}; OS Capnocytophaga ochracea (strain ATCC 27872 / DSM 7271 / JCM 12966 / OS NCTC 12371 / VPI 2845) (Bacteroides ochraceus). OC Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales; OC Flavobacteriaceae; Capnocytophaga. OX NCBI_TaxID=521097 {ECO:0000313|EMBL:ACU92040.1, ECO:0000313|Proteomes:UP000006650}; RN [1] {ECO:0000313|EMBL:ACU92040.1, ECO:0000313|Proteomes:UP000006650} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 27872 / DSM 7271 / JCM 12966 / VPI 2845 RC {ECO:0000313|Proteomes:UP000006650}; RX PubMed=21304645; DOI=10.4056/sigs.15195; RA Mavrommatis K., Gronow S., Saunders E., Land M., Lapidus A., RA Copeland A., Glavina Del Rio T., Nolan M., Lucas S., Chen F., Tice H., RA Cheng J.F., Bruce D., Goodwin L., Pitluck S., Pati A., Ivanova N., RA Chen A., Palaniappan K., Chain P., Hauser L., Chang Y.J., RA Jeffries C.D., Brettin T., Detter J.C., Han C., Bristow J., Goker M., RA Rohde M., Eisen J.A., Markowitz V., Kyrpides N.C., Klenk H.P., RA Hugenholtz P.; RT "Complete genome sequence of Capnocytophaga ochracea type strain (VPI RT 2845)."; RL Stand. Genomic Sci. 1:101-109(2009). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001632; ACU92040.1; -; Genomic_DNA. DR RefSeq; WP_002673774.1; NC_013162.1. DR ProteinModelPortal; C7M6Q2; -. DR STRING; 521097.Coch_0477; -. DR EnsemblBacteria; ACU92040; ACU92040; Coch_0477. DR GeneID; 29676244; -. DR KEGG; coc:Coch_0477; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000006650; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000006650}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000006650}. FT DOMAIN 200 385 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 401 AA; 46375 MW; 647EF3C5657DAA2C CRC64; MLEQVNLTYE KVVLVGIINQ TQTEEKSKEY LDELEFLTYT AGGEVLKRFT QKLDVPNPKT FIGTGKMEEV QQFVEENEVG TVIFDDELTP AQQKNIERIL KAKILDRTGL ILDIFAQRAQ TSYSRTQVEL AQYEYLLPRL TGLWTHLERQ RGGIGMRGPG ETEIETDRRI VRDRIALLKK KLTAIDKQMA TQRSNRGALV RVALIGYTNV GKSTLMNVIS KSEVFAENKL FATLDTTVRK VVIENLPFLL SDTVGFIRKL PTQLIESFKS TLDEVREADL LLHVVDISHP NFEEHIQSVN QILAEIHSAD KPTIMVFNKI DAYTNEEIAE DDLATERTKK HFTLEEWKQT WMQRMGRDVL FISALNKNNL EEFREVVYEK VKEIHITRFP FNNFLYEKID E // ID C7MBD5_BRAFD Unreviewed; 521 AA. AC C7MBD5; DT 13-OCT-2009, integrated into UniProtKB/TrEMBL. DT 13-OCT-2009, sequence version 1. DT 07-JUN-2017, entry version 63. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Bfae_10600 {ECO:0000313|EMBL:ACU84908.1}; OS Brachybacterium faecium (strain ATCC 43885 / DSM 4810 / NCIB 9860). OC Bacteria; Actinobacteria; Micrococcales; Dermabacteraceae; OC Brachybacterium. OX NCBI_TaxID=446465 {ECO:0000313|EMBL:ACU84908.1, ECO:0000313|Proteomes:UP000001919}; RN [1] {ECO:0000313|EMBL:ACU84908.1, ECO:0000313|Proteomes:UP000001919} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43885 / DSM 4810 / NCIB 9860 RC {ECO:0000313|Proteomes:UP000001919}; RX PubMed=21304631; DOI=10.4056/sigs.492; RA Lapidus A., Pukall R., Labuttii K., Copeland A., Del Rio T.G., RA Nolan M., Chen F., Lucas S., Tice H., Cheng J.F., Bruce D., RA Goodwin L., Pitluck S., Rohde M., Goker M., Pati A., Ivanova N., RA Mavrommatis K., Chen A., Palaniappan K., D'haeseleer P., Chain P., RA Bristow J., Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., RA Klenk H.P.; RT "Complete genome sequence of Brachybacterium faecium type strain RT (Schefferle 6-10)."; RL Stand. Genomic Sci. 1:3-11(2009). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001643; ACU84908.1; -; Genomic_DNA. DR RefSeq; WP_012804682.1; NC_013172.1. DR RefSeq; YP_003154498.1; NC_013172.1. DR ProteinModelPortal; C7MBD5; -. DR STRING; 446465.Bfae_10600; -. DR EnsemblBacteria; ACU84908; ACU84908; Bfae_10600. DR GeneID; 8399608; -. DR KEGG; bfa:Bfae_10600; -. DR PATRIC; fig|446465.5.peg.1059; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000001919; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000001919}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000001919}. FT DOMAIN 304 469 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 521 AA; 55472 MW; 58DEA3BC500350EB CRC64; MPIAFHPEPA SDADVDGTTP GGAGAAEHSN SADRATSPAP APNRDPLTQR ILDRGDASLS AATYDSETDG EQFDLADRQA LRRVGGLSTE LDDVTEVEYR QLRLERVVLA GLYTSGNAEA AETSLRELAA LADTAGSEVL DGVLQRRAHP DPATFLGKGK AAELADLVAA SGADTVVADG ELAPGQRRAL EDVVKVKVID RTALILDIFA QHAKSREGKA QVELAQLEYL LPRLRGWGES MSRQAGGQVG GAGAGMGSRG PGETKIELDR RRIRDRMSKL RREIKAMAPG RAEQRAHRTR HQVPAVAIAG YTNAGKSSLL NRLTGAGVLV ENALFATLDP TVRRSTTPDG REFTYADTVG FVRHLPTQLV EAFRSTLEEV GGADLLLHVV DASHPDPEGQ ITAVRAVLGE LEGFDVPEIV VLNKADIAEP ETIARLRSQV GDSAVVSART GMGIQELREL IAERLPRPAV EVDVVVPYSR GDLVSRVHST GEVLAEEHLV EGTRVHARVD AALAAELHGT A // ID C7MVB3_SACVD Unreviewed; 482 AA. AC C7MVB3; DT 13-OCT-2009, integrated into UniProtKB/TrEMBL. DT 13-OCT-2009, sequence version 1. DT 07-JUN-2017, entry version 56. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Svir_27610 {ECO:0000313|EMBL:ACU97742.1}; OS Saccharomonospora viridis (strain ATCC 15386 / DSM 43017 / JCM 3036 / OS NBRC 12207 / P101). OC Bacteria; Actinobacteria; Pseudonocardiales; Pseudonocardiaceae; OC Saccharomonospora. OX NCBI_TaxID=471857 {ECO:0000313|EMBL:ACU97742.1, ECO:0000313|Proteomes:UP000000841}; RN [1] {ECO:0000313|EMBL:ACU97742.1, ECO:0000313|Proteomes:UP000000841} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 15386 / DSM 43017 / JCM 3036 / NBRC 12207 / P101 RC {ECO:0000313|Proteomes:UP000000841}; RX PubMed=21304650; DOI=10.4056/sigs.20263; RA Pati A., Sikorski J., Nolan M., Lapidus A., Copeland A., RA Glavina Del Rio T., Lucas S., Chen F., Tice H., Pitluck S., RA Cheng J.F., Chertkov O., Brettin T., Han C., Detter J.C., Kuske C., RA Bruce D., Goodwin L., Chain P., D'haeseleer P., Chen A., RA Palaniappan K., Ivanova N., Mavromatis K., Mikhailova N., Rohde M., RA Tindall B.J., Goker M., Bristow J., Eisen J.A., Markowitz V., RA Hugenholtz P., Kyrpides N.C., Klenk H.P.; RT "Complete genome sequence of Saccharomonospora viridis type strain RT (P101)."; RL Stand. Genomic Sci. 1:141-149(2009). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001683; ACU97742.1; -; Genomic_DNA. DR RefSeq; WP_015787054.1; NC_013159.1. DR ProteinModelPortal; C7MVB3; -. DR STRING; 471857.Svir_27610; -. DR EnsemblBacteria; ACU97742; ACU97742; Svir_27610. DR KEGG; svi:Svir_27610; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000000841; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000000841}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000000841}. FT DOMAIN 255 424 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 482 AA; 51901 MW; 441F8BF099BC45DF CRC64; MTELTQNFLP EADLDGVELS DGELELSDRA SLRRVAGLST ELADVTEVEY RQLRLERVVL VGVWTEGTAE QAEESLAELA RLAETAGSEV LEGLVQRRSR PDPATYIGSG KVKALADIVA STGADTVICD GELSPSQLRQ LEERLHVKVI DRTALILDIF AQHARSREGK AQVELAQLEY LLPRLRGWGQ SLSRQAGGRA GGANGGVGLR GPGETKLETD RRRINKRIAK LRREIAAMDT IRATKRGRRM ANEVPSVALV GYTNAGKSSI LNAVTGAGVL VEDALFATLD PTTRRTETPD GRVYTLTDTV GFVRHLPHQL VDAFRSTLDE AADADLLLHV VDGAAAAPED QVVAVREVLA EIAEKRAEPL PPELVVINKA DIADEMTLAR LRNLLPDAVV VSAHSGQGID TLLSEIAARL PKPETVVDVV VPYTRGELVA KAYAEGEVLA EEHRPEGTHL RARVHPELAA ALADYATNGS GA // ID C7N5C9_SLAHD Unreviewed; 433 AA. AC C7N5C9; DT 13-OCT-2009, integrated into UniProtKB/TrEMBL. DT 13-OCT-2009, sequence version 1. DT 07-JUN-2017, entry version 66. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Shel_10790 {ECO:0000313|EMBL:ACV22114.1}; OS Slackia heliotrinireducens (strain ATCC 29202 / DSM 20476 / NCTC 11029 OS / RHS 1) (Peptococcus heliotrinreducens). OC Bacteria; Actinobacteria; Coriobacteriia; Eggerthellales; OC Eggerthellaceae; Slackia. OX NCBI_TaxID=471855 {ECO:0000313|EMBL:ACV22114.1, ECO:0000313|Proteomes:UP000002026}; RN [1] {ECO:0000313|EMBL:ACV22114.1, ECO:0000313|Proteomes:UP000002026} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29202 / DSM 20476 / NCTC 11029 / RHS 1 RC {ECO:0000313|Proteomes:UP000002026}; RX PubMed=21304663; DOI=10.4056/sigs.37633; RA Pukall R., Lapidus A., Nolan M., Copeland A., Glavina Del Rio T., RA Lucas S., Chen F., Tice H., Cheng J.F., Chertkov O., Bruce D., RA Goodwin L., Kuske C., Brettin T., Detter J.C., Han C., Pitluck S., RA Pati A., Mavrommatis K., Ivanova N., Ovchinnikova G., Chen A., RA Palaniappan K., Schneider S., Rohde M., Chain P., D'haeseleer P., RA Goker M., Bristow J., Eisen J.A., Markowitz V., Kyrpides N.C., RA Klenk H.P., Hugenholtz P.; RT "Complete genome sequence of Slackia heliotrinireducens type strain RT (RHS 1)."; RL Stand. Genomic Sci. 1:234-241(2009). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001684; ACV22114.1; -; Genomic_DNA. DR RefSeq; WP_012798217.1; NC_013165.1. DR ProteinModelPortal; C7N5C9; -. DR STRING; 471855.Shel_10790; -. DR EnsemblBacteria; ACV22114; ACV22114; Shel_10790. DR KEGG; shi:Shel_10790; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000002026; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000002026}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000002026}. FT DOMAIN 214 379 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 433 AA; 47601 MW; EBC355F4707CF660 CRC64; MSFADMDANS VMEDRERAIL VGIDYRDNAS EYSLESSLDE LARLTDTAGA DVVATTSQRL DSPNPRTFIG SGKAEEIASM CRSLSADVVI FDDELTPSQQ SNLEKVLPKD VKVIDRTALI LDIFALHATT KEGRLQVRLA QNQYLLPRLR GMWAHLASNR MGGGVGSRFG EGESQLEVDR RMVRKRITSI RRELEQVAQM RTIQRAARYD SGIFKVAEAG YTNAGKSSLL NRLTNAEVLS YDKLFATLDS TTRKLVLPEG REVTITDTVG FIQKLPTTLV EAFNSTLDEI RGADLIMHVV DASSNERDLQ MNAVGDTLEQ IGAQDIPRLV VFNKIDLVDE GDRAILASRY PMAILVSAET GEGIDGLIDA LARAVAAQEE LMDVLVPYSK GSVVSLVHER CTVLAESYGE DGTRLTLRAP RDLIALLGQY SVQ // ID C7NJ74_KYTSD Unreviewed; 517 AA. AC C7NJ74; DT 13-OCT-2009, integrated into UniProtKB/TrEMBL. DT 13-OCT-2009, sequence version 1. DT 07-JUN-2017, entry version 64. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Ksed_17490 {ECO:0000313|EMBL:ACV06761.1}; OS Kytococcus sedentarius (strain ATCC 14392 / DSM 20547 / CCM 314 / 541) OS (Micrococcus sedentarius). OC Bacteria; Actinobacteria; Micrococcales; Dermacoccaceae; Kytococcus. OX NCBI_TaxID=478801 {ECO:0000313|EMBL:ACV06761.1, ECO:0000313|Proteomes:UP000006666}; RN [1] {ECO:0000313|EMBL:ACV06761.1, ECO:0000313|Proteomes:UP000006666} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 14392 / DSM 20547 / CCM 314 / 541 RC {ECO:0000313|Proteomes:UP000006666}; RX PubMed=21304632; DOI=10.4056/sigs.761; RA Sims D., Brettin T., Detter J.C., Han C., Lapidus A., Copeland A., RA Glavina Del Rio T., Nolan M., Chen F., Lucas S., Tice H., Cheng J.F., RA Bruce D., Goodwin L., Pitluck S., Ovchinnikova G., Pati A., RA Ivanova N., Mavrommatis K., Chen A., Palaniappan K., D'haeseleer P., RA Chain P., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P., RA Schneider S., Goker M., Pukall R., Kyrpides N.C., Klenk H.P.; RT "Complete genome sequence of Kytococcus sedentarius type strain RT (541)."; RL Stand. Genomic Sci. 1:12-20(2009). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001686; ACV06761.1; -; Genomic_DNA. DR RefSeq; WP_015779703.1; NC_013169.1. DR ProteinModelPortal; C7NJ74; -. DR STRING; 478801.Ksed_17490; -. DR EnsemblBacteria; ACV06761; ACV06761; Ksed_17490. DR KEGG; kse:Ksed_17490; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000006666; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 2. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000006666}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000006666}. FT DOMAIN 293 462 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 517 AA; 56765 MW; BE27AE92F4BA6581 CRC64; MTHTPTSPAE FEREDQVNTA TPQDPRGVDE VDGPPALRRA AALSQDPDGY DDREGEHYDG EQYDREERRA LRRIDSLSTE LEDISEVEYR QVRLERVVLA HVQTEGTAEE AENSLAELAA LAETAGSTVL TGVIQRRQKP DPATWMGSGK AAELRDIVAA EGADTVIADD ELAPSQRRAL EDVIKVKVVD RTALILDIFA QHAKSREGRA QVELAQLQYL LPRLRGWGES MSRQAGGRVA GGEGIGSRGP GETKIELDRR RINTQMAKLR KQIAQMKTVR DTKRSSRKDH QVPSVVIAGY TNAGKSSLLN RLTRAGVLVE NQLFATLDPT VRRTETADGR VFTLADTVGF VRSLPHQLVE AFRSTLEEVA DADLVLHVVD GSHPDPENQI SAVREVLSEV LDEKGADSMN EIIVINKADA ADPEVVARLL RTEKRSIAVS ARTGQGITEL RELVESELPR PDIEVDVVVP YERGDLVARI HSEGEVLAER HLPEGTHLVA RINADLAGAL TPVVQAR // ID C7NY54_HALMD Unreviewed; 436 AA. AC C7NY54; DT 13-OCT-2009, integrated into UniProtKB/TrEMBL. DT 13-OCT-2009, sequence version 1. DT 07-JUN-2017, entry version 60. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Hmuk_2404 {ECO:0000313|EMBL:ACV48514.1}; OS Halomicrobium mukohataei (strain ATCC 700874 / DSM 12286 / JCM 9738 / OS NCIMB 13541) (Haloarcula mukohataei). OC Archaea; Euryarchaeota; Halobacteria; Halobacteriales; Haloarculaceae; OC Halomicrobium. OX NCBI_TaxID=485914 {ECO:0000313|EMBL:ACV48514.1, ECO:0000313|Proteomes:UP000001746}; RN [1] {ECO:0000313|EMBL:ACV48514.1, ECO:0000313|Proteomes:UP000001746} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700874 / DSM 12286 / JCM 9738 / NCIMB 13541 RC {ECO:0000313|Proteomes:UP000001746}; RX PubMed=21304667; DOI=10.4056/sigs.42644; RA Tindall B.J., Schneider S., Lapidus A., Copeland A., RA Glavina Del Rio T., Nolan M., Lucas S., Chen F., Tice H., Cheng J.F., RA Saunders E., Bruce D., Goodwin L., Pitluck S., Mikhailova N., Pati A., RA Ivanova N., Mavrommatis K., Chen A., Palaniappan K., Chain P., RA Land M., Hauser L., Chang Y.J., Jeffries C.D., Brettin T., Han C., RA Rohde M., Goker M., Bristow J., Eisen J.A., Markowitz V., RA Hugenholtz P., Klenk H.P., Kyrpides N.C., Detter J.C.; RT "Complete genome sequence of Halomicrobium mukohataei type strain RT (arg-2)."; RL Stand. Genomic Sci. 1:270-277(2009). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001688; ACV48514.1; -; Genomic_DNA. DR RefSeq; WP_015763356.1; NC_013202.1. DR ProteinModelPortal; C7NY54; -. DR STRING; 485914.Hmuk_2404; -. DR EnsemblBacteria; ACV48514; ACV48514; Hmuk_2404. DR GeneID; 8411948; -. DR KEGG; hmu:Hmuk_2404; -. DR eggNOG; arCOG00353; Archaea. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG093Z07D6; -. DR Proteomes; UP000001746; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000001746}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000001746}. FT DOMAIN 193 376 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 109 136 {ECO:0000256|SAM:Coils}. FT COILED 159 189 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 436 AA; 48653 MW; AD85E97DFFB2101E CRC64; MTASTTAERA VIAKRVDSGT ADTEEITDLA RAAGYEAVGE VTQKRTEDPA YHLGEGKVAR LANVVAREGA TAVIFDNELG PYQTYNIGNE LPDGVQVVDR FRLILEIFGQ RAQTRKAQLQ VELAELRYEL PRAEAKASLA KRDERPGFMG LGEYDESREE DIKKQISRIR DELASIEETE QHRRQQRRES GFDLVALAGY TNAGKSTLLR RVADDVDVDE NEELHPDLDP TAESEDRLFT TLGTTTRRAD MDQRDVLVTD TVGFISDLPH WLVESFKSTL DAVYRADLVL LVVDVSEPVE EIREKLVTSH DTLYERNEAP IVTVLNKTDT VDDAEIERKR AALSGLAPNP IAVSAKEGAN VDALLDRIHD ELPDYERERL VLPMTDETMS LVSWIHDHAH VDNVDYGDQV IVEFEGRSAV VERSRAKAGE LVEASA // ID C7PHA9_CHIPD Unreviewed; 396 AA. AC C7PHA9; DT 13-OCT-2009, integrated into UniProtKB/TrEMBL. DT 13-OCT-2009, sequence version 1. DT 07-JUN-2017, entry version 64. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Cpin_0590 {ECO:0000313|EMBL:ACU58088.1}; OS Chitinophaga pinensis (strain ATCC 43595 / DSM 2588 / NCIB 11800 / UQM OS 2034). OC Bacteria; Bacteroidetes; Chitinophagia; Chitinophagales; OC Chitinophagaceae; Chitinophaga. OX NCBI_TaxID=485918 {ECO:0000313|EMBL:ACU58088.1, ECO:0000313|Proteomes:UP000002215}; RN [1] {ECO:0000313|Proteomes:UP000002215} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43595 / DSM 2588 / NCIB 11800 / UQM 2034 RC {ECO:0000313|Proteomes:UP000002215}; RG US DOE Joint Genome Institute (JGI-PGF); RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., RA Tice H., Bruce D., Goodwin L., Pitluck S., Kyrpides N., Mavromatis K., RA Ivanova N., Mikhailova N., Sims D., Meinche L., Brettin T., RA Detter J.C., Han C., Larimer F., Land M., Hauser L., Markowitz V., RA Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Spring S., Klenk H.-P., RA Eisen J.A.; RT "The complete genome of Chitinophaga pinensis DSM 2588."; RL Submitted (AUG-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001699; ACU58088.1; -; Genomic_DNA. DR RefSeq; WP_012788264.1; NC_013132.1. DR ProteinModelPortal; C7PHA9; -. DR STRING; 485918.Cpin_0590; -. DR EnsemblBacteria; ACU58088; ACU58088; Cpin_0590. DR KEGG; cpi:Cpin_0590; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000002215; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000002215}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000002215}. FT DOMAIN 202 384 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 396 AA; 45887 MW; 2694052C7F8E2BB2 CRC64; MIEKKQVVQQ EERAVIVGVI HKEQSDRQVQ EYLDELVFLA ETAGAITVKK FTQKLARPDR ATFVGKGKLE EIRDFIAGRN INLVIFDDEL TGSQIANIEK VLNVKVIDRS DLILDIFARR ARTAQAKVQV ELAQYQYILP RLKGMWSHLE RQGGGIGSRG PGETEIETDR RIIKEKVALL RKRLAEIDKQ SLTQRKDRGE YIRVALVGYT NVGKSTIMNL MSKSEVFAEN KLFATLDTTT RKVVFDQTAF LLSDTVGFIR KLPHHLVESF KSTLDEVRES DILLHVVDVS HPQYEDQVEV VNRTLHELKA FDKPIIMVFN KMDLYEEQTF DKWLTEDIKQ DILNQLKENW QTRTQGNCVF ISATERKNVE ELRATILSKV VELYRVRYPY KSEYFY // ID C7Q5E1_CATAD Unreviewed; 502 AA. AC C7Q5E1; DT 13-OCT-2009, integrated into UniProtKB/TrEMBL. DT 13-OCT-2009, sequence version 1. DT 07-JUN-2017, entry version 64. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Caci_7080 {ECO:0000313|EMBL:ACU75910.1}; OS Catenulispora acidiphila (strain DSM 44928 / NRRL B-24433 / NBRC OS 102108 / JCM 14897). OC Bacteria; Actinobacteria; Catenulisporales; Catenulisporaceae; OC Catenulispora. OX NCBI_TaxID=479433 {ECO:0000313|EMBL:ACU75910.1, ECO:0000313|Proteomes:UP000000851}; RN [1] {ECO:0000313|EMBL:ACU75910.1, ECO:0000313|Proteomes:UP000000851} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 44928 / NRRL B-24433 / NBRC 102108 / JCM 14897 RC {ECO:0000313|Proteomes:UP000000851}; RX PubMed=21304647; RA Copeland A., Lapidus A., Glavina Del Rio T., Nolan M., Lucas S., RA Chen F., Tice H., Cheng J.F., Bruce D., Goodwin L., Pitluck S., RA Mikhailova N., Pati A., Ivanova N., Mavromatis K., Chen A., RA Palaniappan K., Chain P., Land M., Hauser L., Chang Y.J., RA Jeffries C.D., Chertkov O., Brettin T., Detter J.C., Han C., Ali Z., RA Tindall B.J., Goker M., Bristow J., Eisen J.A., Markowitz V., RA Hugenholtz P., Kyrpides N.C., Klenk H.P.; RT "Complete genome sequence of Catenulispora acidiphila type strain (ID RT 139908)."; RL Stand. Genomic Sci. 1:119-125(2009). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001700; ACU75910.1; -; Genomic_DNA. DR ProteinModelPortal; C7Q5E1; -. DR STRING; 479433.Caci_7080; -. DR EnsemblBacteria; ACU75910; ACU75910; Caci_7080. DR KEGG; cai:Caci_7080; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000000851; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 2. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000000851}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000000851}. FT DOMAIN 280 445 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 239 266 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 502 AA; 55194 MW; 9C8C09DABCA550C2 CRC64; MTESHKDAAR DEVYALNDHD TPEAEWDTED AFDAPAPLYR NRWADSRHDG EQFDLEERAS LRRVAGLSTE LEDVTEVEYR QLRLERVVLV GVWTDGTAAD AEVSLRELAA LAETAGSEVL DGVIQRREKP DPATYIGSGK ALELRDIVVA TGADTVICDG ELSPGQLIHL EDVVKVKVID RTALILDIFA QHAKSREGKA QVALAQMQYM LPRLRGWGQS LSRQMGGGRG GLATRGPGET KIETDRRRIR ERMAKLRREI NDMSKGRVTK RAERRRGSVP SVVLAGYTNA GKSSILNRLT GAGVLVENAL FATLDPTVRR TETASGRAYT LSDTVGFVRH LPHQLVEAFR STLEEVGESD LVLHVVDASD EDPEGQISAV RAVFADMGAG DVKELMVLNK ADLADPEVLA RLLRHEPHSI IVSARTGEGI DHLLSAIERD LPRPGVELEA LVPYDRGDLV ARIHAEGEML KEEHTDHGTL VRALIHQNLA AQLEPFRTVG AV // ID C7R3H1_JONDD Unreviewed; 509 AA. AC C7R3H1; DT 13-OCT-2009, integrated into UniProtKB/TrEMBL. DT 13-OCT-2009, sequence version 1. DT 07-JUN-2017, entry version 57. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Jden_1051 {ECO:0000313|EMBL:ACV08707.1}; OS Jonesia denitrificans (strain ATCC 14870 / DSM 20603 / CIP 55134) OS (Listeria denitrificans). OC Bacteria; Actinobacteria; Micrococcales; Jonesiaceae; Jonesia. OX NCBI_TaxID=471856 {ECO:0000313|EMBL:ACV08707.1, ECO:0000313|Proteomes:UP000000628}; RN [1] {ECO:0000313|EMBL:ACV08707.1, ECO:0000313|Proteomes:UP000000628} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 14870 / DSM 20603 / CIP 55134 RC {ECO:0000313|Proteomes:UP000000628}; RX PubMed=21304666; DOI=10.4056/sigs.41646; RA Pukall R., Gehrich-Schroter G., Lapidus A., Nolan M., RA Glavina Del Rio T., Lucas S., Chen F., Tice H., Pitluck S., RA Cheng J.F., Copeland A., Saunders E., Brettin T., Detter J.C., RA Bruce D., Goodwin L., Pati A., Ivanova N., Mavromatis K., RA Ovchinnikova G., Chen A., Palaniappan K., Land M., Hauser L., RA Chang Y.J., Jeffries C.D., Chain P., Goker M., Bristow J., Eisen J.A., RA Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P., Han C.; RT "Complete genome sequence of Jonesia denitrificans type strain (Prevot RT 55134)."; RL Stand. Genomic Sci. 1:262-269(2009). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001706; ACV08707.1; -; Genomic_DNA. DR RefSeq; WP_015771335.1; NC_013174.1. DR ProteinModelPortal; C7R3H1; -. DR STRING; 471856.Jden_1051; -. DR EnsemblBacteria; ACV08707; ACV08707; Jden_1051. DR KEGG; jde:Jden_1051; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000000628; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 2. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000000628}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000000628}. FT DOMAIN 287 453 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 509 AA; 55018 MW; 0233CBDC18993954 CRC64; MHDDNSPRLP TEHTQPGETR AERDVATDVV QRILARAGTA VQDGDTTHSR FDGDQLDLAE RSALRRVQGL STELDDVTEV EYRQLRLERV VLVGLYTRGS AQEAEVSLRE LAALAETAGS QVLDGLLQRR ATPDPGTYLG SGKASELADI VQQVGADTVI VDGELGPSQR RALEDIIKIK VIDRTALILD IFAQHAKSRE GKAQVELAQL EYLLPRLRGW GESMSRQAGG QVGSAGAGMG SRGPGETKIE LDRRRIRTRM AKLRREIAAM KPAREAKRSS RRKNAVPAVA IVGYTNAGKS SLLNALTGAG VLVQNALFAT LDPTVRRTKT PDGRVYTLAD TVGFVRHLPH QLVEAFRSTL EETADADIIV HVVDGAHPDP AGQIAAVRTV LADIDGVSDI PEIIVVNKAD IAPPEAIAQI RSMERDVWAV SAHTGAGIEE LLGHIADILP APGVEIHLTV PYHRGDLLSR MHAEGEIDEL RHTEQGTFVA GRVPEDLAAD LHRVAIDGE // ID C7RDH3_ANAPD Unreviewed; 412 AA. AC C7RDH3; DT 13-OCT-2009, integrated into UniProtKB/TrEMBL. DT 13-OCT-2009, sequence version 1. DT 07-JUN-2017, entry version 64. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Apre_1212 {ECO:0000313|EMBL:ACV29236.1}; OS Anaerococcus prevotii (strain ATCC 9321 / DSM 20548 / JCM 6508 / PC1) OS (Peptostreptococcus prevotii) (Peptococcus prevotii). OC Bacteria; Firmicutes; Tissierellia; Tissierellales; Peptoniphilaceae; OC Anaerococcus. OX NCBI_TaxID=525919 {ECO:0000313|EMBL:ACV29236.1, ECO:0000313|Proteomes:UP000002294}; RN [1] {ECO:0000313|EMBL:ACV29236.1, ECO:0000313|Proteomes:UP000002294} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 9321 / DSM 20548 / JCM 6508 / PC1 RC {ECO:0000313|Proteomes:UP000002294}; RX PubMed=21304652; DOI=10.4056/sigs.24194; RA Labutti K., Pukall R., Steenblock K., Glavina Del Rio T., Tice H., RA Copeland A., Cheng J.F., Lucas S., Chen F., Nolan M., Bruce D., RA Goodwin L., Pitluck S., Ivanova N., Mavromatis K., Ovchinnikova G., RA Pati A., Chen A., Palaniappan K., Land M., Hauser L., Chang Y.J., RA Jeffries C.D., Chain P., Saunders E., Brettin T., Detter J.C., Han C., RA Goker M., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P., RA Kyrpides N.C., Klenk H.P., Lapidus A.; RT "Complete genome sequence of Anaerococcus prevotii type strain RT (PC1)."; RL Stand. Genomic Sci. 1:159-165(2009). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001708; ACV29236.1; -; Genomic_DNA. DR RefSeq; WP_015778135.1; NC_013171.1. DR ProteinModelPortal; C7RDH3; -. DR STRING; 525919.Apre_1212; -. DR EnsemblBacteria; ACV29236; ACV29236; Apre_1212. DR KEGG; apr:Apre_1212; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000002294; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000002294}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}. FT DOMAIN 189 357 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 412 AA; 47638 MW; 3BD66BF8F5C7E674 CRC64; MQRVIQVNAV DKDDDLDNKI YELESLINTA GGKTEAYVSQ KVSKVNPRYY IGKGKVEEIM DLAQKNDIDT VIFDVELSAS QLYNLEEEMK LHVVDWTTLI LDIFAMRANT KEARLKIKLA QLKYQLPRIN KWFSYLSRQA GGIGTRGPGE TMLETDRRAI VRDIKSLEKA LKDLDKTKMI NRKSRKDIHN ISLVGYTNAG KSTILNGMLK LFGEEKYVYS DDLLFATLDT STRRLDFSNT KVTLTDTVGF IDNLSKELND SFLTTLDEVR FADMLLIVID SSHNIDHQIE TIENSLEGID VGNKEILYVF NKMDRVDDEL SVSLYKRDSE KIYMSAHKEE DLIRLKEKIV KIIKEDYELV EMAIPFEDGR VLDYIMSNYD IIERDYDPTS SILKLEISKE DYSKYDRYIK KV // ID C7RU31_ACCPU Unreviewed; 390 AA. AC C7RU31; DT 13-OCT-2009, integrated into UniProtKB/TrEMBL. DT 13-OCT-2009, sequence version 1. DT 07-JUN-2017, entry version 57. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=CAP2UW1_2916 {ECO:0000313|EMBL:ACV36195.1}; OS Accumulibacter phosphatis (strain UW-1). OC Bacteria; Proteobacteria; Betaproteobacteria; OC Candidatus Accumulibacter. OX NCBI_TaxID=522306 {ECO:0000313|EMBL:ACV36195.1, ECO:0000313|Proteomes:UP000001619}; RN [1] {ECO:0000313|EMBL:ACV36195.1, ECO:0000313|Proteomes:UP000001619} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=UW-1 {ECO:0000313|EMBL:ACV36195.1, RC ECO:0000313|Proteomes:UP000001619}; RG US DOE Joint Genome Institute; RA Martin H.G., Ivanova N., Kunin V., Warnecke F., Barry K., He S., RA Salamov A., Szeto E., Dalin E., Pangilinan J.L., Lapidus A., Lowry S., RA Kyrpides N.C., McMahon K.D., Hugenholtz P.; RT "Complete sequence of chromosome of Candidatus Accumulibacter RT phosphatis clade IIA str. UW-1."; RL Submitted (SEP-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001715; ACV36195.1; -; Genomic_DNA. DR RefSeq; WP_015767374.1; NC_013194.1. DR ProteinModelPortal; C7RU31; -. DR STRING; 522306.CAP2UW1_2916; -. DR EnsemblBacteria; ACV36195; ACV36195; CAP2UW1_2916. DR KEGG; app:CAP2UW1_2916; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000001619; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000001619}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000001619}. FT DOMAIN 198 364 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 390 AA; 42552 MW; 7321B63E0ECADA8F CRC64; MHERPSGEER AVIVQLDFGR DDLTEQLEEV RLLTRSAGAA VCAVVHGRRH SPDAATYAGK GKVLEVAAEV AAHEADLVIF NHELSAGQER NLERALQCRV IDRTSLILDI FAQRAQSAEG KLQVELAQLE HLATRLVRGW THLERQKGGI GLRGPGETQL ETDRRLLGIR VRLLKERLGR LERQRGVQRK ARGRGELLNV SLVGYTNAGK STLFNSLTHA GVFAADQLFA TLDTTTRKLW LAEAGHIVLS DTVGFIRDLP HSLVAAFHAT LEATAEADLL LHVVDSASQA RDEQIADVNK VLAEIGAADV PQLLVLNKLD LTGLPPAVER DEYGRIRRVR VSAKGGDGLP LLREALAEVA LAKTGRLRER SSAAATVQAT DLITDSDWSP // ID C7XX39_9LACO Unreviewed; 425 AA. AC C7XX39; DT 13-OCT-2009, integrated into UniProtKB/TrEMBL. DT 13-OCT-2009, sequence version 1. DT 07-JUN-2017, entry version 43. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:EEU29859.1}; GN ORFNames=HMPREF0501_01324 {ECO:0000313|EMBL:EEU29859.1}; OS Lactobacillus coleohominis 101-4-CHN. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; OC Lactobacillus. OX NCBI_TaxID=575594 {ECO:0000313|EMBL:EEU29859.1, ECO:0000313|Proteomes:UP000003987}; RN [1] {ECO:0000313|EMBL:EEU29859.1, ECO:0000313|Proteomes:UP000003987} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=101-4-CHN {ECO:0000313|EMBL:EEU29859.1, RC ECO:0000313|Proteomes:UP000003987}; RG The Broad Institute Genome Sequencing Platform; RA Ward D., Young S.K., Zeng Q., Koehrsen M., Alvarado L., Berlin A., RA Borenstein D., Chen Z., Engels R., Freedman E., Gellesch M., RA Goldberg J., Griggs A., Gujja S., Heiman D., Hepburn T., Howarth C., RA Jen D., Larson L., Lewis B., Mehta T., Park D., Pearson M., RA Roberts A., Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., RA Walk T., White J., Yandava C., Liu Y., Xu Q., Lander E., Nusbaum C., RA Galagan J., Birren B.; RT "The Genome Sequence of Lactobacillus coleohominis strain 101-4-CHN."; RL Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GG698805; EEU29859.1; -; Genomic_DNA. DR RefSeq; WP_006917196.1; NZ_GG698805.1. DR ProteinModelPortal; C7XX39; -. DR STRING; 575594.HMPREF0501_01324; -. DR EnsemblBacteria; EEU29859; EEU29859; HMPREF0501_01324. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000003987; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000003987}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000003987}. FT DOMAIN 202 371 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 425 AA; 47970 MW; B7E97181B2E57913 CRC64; MDTTIQADEK VIVTGLNTGQ EDYDYSMTEL KELAQANQMD VVDRIDQVLD RPNAATYFGS GKIDEIKNIA AAEEATTVIT NDELSPSQLS NLNDEVGVRV IDRTALILEI FAKRAQTKEA KIQVQIAKLE YQLPRLHTAA NQRLDQQTGG GAGFANRGAG ETKIEMDRRV IQKHISHLRH ELKEINKSEA TKRALRDKSA IPTAALVGYT NAGKSTLMNK MIERYGISRE KEVFEKDMLF STLDTSVRQL TLPDQKRFIL SDTVGFVSKL PTHLIEAFKS TLTEAAKADL LIQIIDYSDP HRDEMIKTTE KTLHQIGIDN IPMIYVFNKA DKTNFEYPTM EGDDHLVISA KDDKSLDLFI KTIKDHLFDD YVDAKLLIPF TDGHVVSYLN EHANITDTDY QNDGTLLQVE ISPRDLQRFS QYVVE // ID C8NCL8_CARH6 Unreviewed; 430 AA. AC C8NCL8; DT 03-NOV-2009, integrated into UniProtKB/TrEMBL. DT 03-NOV-2009, sequence version 1. DT 07-JUN-2017, entry version 39. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:EEV87641.1}; GN ORFNames=HMPREF0198_2246 {ECO:0000313|EMBL:EEV87641.1}; OS Cardiobacterium hominis (strain ATCC 15826 / DSM 8339 / NCTC 10426 / OS 6573). OC Bacteria; Proteobacteria; Gammaproteobacteria; Cardiobacteriales; OC Cardiobacteriaceae; Cardiobacterium. OX NCBI_TaxID=638300 {ECO:0000313|EMBL:EEV87641.1, ECO:0000313|Proteomes:UP000004870}; RN [1] {ECO:0000313|EMBL:EEV87641.1, ECO:0000313|Proteomes:UP000004870} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 15826 / DSM 8339 / NCTC 10426 / 6573 RC {ECO:0000313|Proteomes:UP000004870}; RA Qin X., Bachman B., Battles P., Bell A., Bess C., Bickham C., RA Chaboub L., Chen D., Coyle M., Deiros D.R., Dinh H., Forbes L., RA Fowler G., Francisco L., Fu Q., Gubbala S., Hale W., Han Y., RA Hemphill L., Highlander S.K., Hirani K., Hogues M., Jackson L., RA Jakkamsetti A., Javaid M., Jiang H., Korchina V., Kovar C., Lara F., RA Lee S., Mata R., Mathew T., Moen C., Morales K., Munidasa M., RA Nazareth L., Ngo R., Nguyen L., Okwuonu G., Ongeri F., Patil S., RA Petrosino J., Pham C., Pham P., Pu L.-L., Puazo M., Raj R., Reid J., RA Rouhana J., Saada N., Shang Y., Simmons D., Thornton R., Warren J., RA Weissenberger G., Zhang J., Zhang L., Zhou C., Zhu D., Muzny D., RA Worley K., Gibbs R.; RL Submitted (AUG-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EEV87641.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACKY01000117; EEV87641.1; -; Genomic_DNA. DR RefSeq; WP_004142566.1; NZ_GG694027.1. DR ProteinModelPortal; C8NCL8; -. DR STRING; 638300.HMPREF0198_2246; -. DR EnsemblBacteria; EEV87641; EEV87641; HMPREF0198_2246. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000004870; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000004870}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000004870}. FT DOMAIN 198 364 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 157 196 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 430 AA; 48238 MW; 0AB1F66C841A825C CRC64; MFERPKSGER AALVQVDINR TPDPAVEEEF HQLARSAGAQ IIWAERYSRG EAEPRYYIGR GQAEALAEAV KAHDIELVIF NAPLSPSQER NLEKLCSARV LDRSGLVLDI FAQRARSHEG KLQVELAQLN HLATRLVRGW THLERQKGGI GLRGPGETQL ETDRRLLAAR IKQLQRRLAR VQKQREENRK ARLRRDIPTV ALAGYTNSGK STLFNTLTEA DVYAQDQLFA TLDPTWRKLQ HSGPQTILMA DTVGFVSDLP HELVAAFSAT LEETARADLL LHVIDVADPH HLEREEVVED VLKSIDAADV PTLRVYNKID LRGEAPRVKP GADGKAEAVF LSALTGAGVD LLTDAIVAYF KSDEKNGWLH LAPHEGALRA ALYAEHAVLE ERSAADGSQW LHIRLREKHY HQIQSKYNRR LELQTHSDIP // ID C8NEF2_9LACT Unreviewed; 400 AA. AC C8NEF2; DT 03-NOV-2009, integrated into UniProtKB/TrEMBL. DT 03-NOV-2009, sequence version 1. DT 07-JUN-2017, entry version 41. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:EEW38053.1}; GN ORFNames=HMPREF0444_0297 {ECO:0000313|EMBL:EEW38053.1}; OS Granulicatella adiacens ATCC 49175. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Carnobacteriaceae; OC Granulicatella. OX NCBI_TaxID=638301 {ECO:0000313|EMBL:EEW38053.1, ECO:0000313|Proteomes:UP000005926}; RN [1] {ECO:0000313|EMBL:EEW38053.1, ECO:0000313|Proteomes:UP000005926} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 49175 {ECO:0000313|EMBL:EEW38053.1, RC ECO:0000313|Proteomes:UP000005926}; RA Muzny D., Qin X., Deng J., Jiang H., Liu Y., Qu J., Song X.-Z., RA Zhang L., Thornton R., Coyle M., Francisco L., Jackson L., Javaid M., RA Korchina V., Kovar C., Mata R., Mathew T., Ngo R., Nguyen L., RA Nguyen N., Okwuonu G., Ongeri F., Pham C., Simmons D., RA Wilczek-Boney K., Hale W., Jakkamsetti A., Pham P., Ruth R., RA San Lucas F., Warren J., Zhang J., Zhao Z., Zhou C., Zhu D., Lee S., RA Bess C., Blankenburg K., Forbes L., Fu Q., Gubbala S., Hirani K., RA Jayaseelan J.C., Lara F., Munidasa M., Palculict T., Patil S., RA Pu L.-L., Saada N., Tang L., Weissenberger G., Zhu Y., Hemphill L., RA Shang Y., Youmans B., Ayvaz T., Ross M., Santibanez J., Aqrawi P., RA Gross S., Joshi V., Fowler G., Nazareth L., Reid J., Worley K., RA Petrosino J., Highlander S., Gibbs R.; RL Submitted (AUG-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EEW38053.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACKZ01000008; EEW38053.1; -; Genomic_DNA. DR RefSeq; WP_005605305.1; NZ_GG694015.1. DR ProteinModelPortal; C8NEF2; -. DR STRING; 638301.HMPREF0444_0297; -. DR EnsemblBacteria; EEW38053; EEW38053; HMPREF0444_0297. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000005926; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000005926}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000005926}. FT DOMAIN 196 357 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 162 192 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 400 AA; 45725 MW; 7E55941D32F7D3DB CRC64; MEQRERVLIV SMQTTQTDED FAYANQELAQ LVDTAMGEVV ATVTQKRESI SGRTLVGKGK VEEISHLVDE LEVDLVVFYQ SLTGSMVKNL NESINCRIID RVQLILDIFA MRARSKEGKL QVQLAQLNYL LPRLSGQREG LSRQGGGIGT RGPGETRLET DRRYIRKQIQ DIEEQLEQIK KHRERSREKR KSSNGFQLGL IGYTNAGKST ILNQLTQAGT YQMDQLFATL DPLTRQVDLF PNFEVTLTDT VGFIQDLPTT LIHAFESTLE ESADVDLLVH VVDASNTQFS LHEKTVIDLV NDLEMQEILM VTVYNKTDLI EGEFQPNLYP SIQISAVNDA DVERLKAFLK EQVKAQMTYY EEWLEVTETK ELNQLQQRTL VESLNYVEEK NQYCVKGYRK // ID C8PCM2_9LACO Unreviewed; 401 AA. AC C8PCM2; DT 03-NOV-2009, integrated into UniProtKB/TrEMBL. DT 03-NOV-2009, sequence version 1. DT 07-JUN-2017, entry version 42. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:EEW51797.1}; GN ORFNames=HMPREF0520_0842 {ECO:0000313|EMBL:EEW51797.1}; OS Lactobacillus iners DSM 13335. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; OC Lactobacillus. OX NCBI_TaxID=525328 {ECO:0000313|EMBL:EEW51797.1, ECO:0000313|Proteomes:UP000004115}; RN [1] {ECO:0000313|EMBL:EEW51797.1, ECO:0000313|Proteomes:UP000004115} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 13335 {ECO:0000313|EMBL:EEW51797.1, RC ECO:0000313|Proteomes:UP000004115}; RA Qin X., Bachman B., Battles P., Bell A., Bess C., Bickham C., RA Chaboub L., Chen D., Coyle M., Deiros D.R., Dinh H., Forbes L., RA Fowler G., Francisco L., Fu Q., Gubbala S., Hale W., Han Y., RA Hemphill L., Highlander S.K., Hirani K., Hogues M., Jackson L., RA Jakkamsetti A., Javaid M., Jiang H., Korchina V., Kovar C., Lara F., RA Lee S., Mata R., Mathew T., Moen C., Morales K., Munidasa M., RA Nazareth L., Ngo R., Nguyen L., Okwuonu G., Ongeri F., Patil S., RA Petrosino J., Pham C., Pham P., Pu L.-L., Puazo M., Raj R., Reid J., RA Rouhana J., Saada N., Shang Y., Simmons D., Thornton R., Warren J., RA Weissenberger G., Zhang J., Zhang L., Zhou C., Zhu D., Muzny D., RA Worley K., Gibbs R.; RL Submitted (SEP-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EEW51797.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACLN01000008; EEW51797.1; -; Genomic_DNA. DR ProteinModelPortal; C8PCM2; -. DR EnsemblBacteria; EEW51797; EEW51797; HMPREF0520_0842. DR PATRIC; fig|525328.13.peg.335; -. DR Proteomes; UP000004115; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000004115}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000004115}. FT DOMAIN 175 344 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 401 AA; 45710 MW; F5D9AC4105D590B0 CRC64; MDELAKLAEA NQMEVVGRSW QNLETIVTGT YFGLGKINEI KHLAKELHAT VIIINDELTP TQIRNLEKMT KLSILDRTEL ILEIFSNRVR TKQAKLQVQL ARLQYELPRL HPSENRLDQQ RGSGGGFNNR GAGETKLELN RRTIQQQISN IKKDLKKINQ QEIIKATQRN NSFLPQVALV GYTNSGKSTT LNNLLNEYSK SADKKQVFTK DMLFATLDTH VRRIDLENKL SFIISDTVGF VSNLPHNLIE SFKATLQEVR DADLIINVVD ASDPNILQMI QTTTKVLDEL QIGDVPIITA FNKVDKTDRS YPQIEGNGNI LYSAKDPESI RLLAKLIQKK IFSNLQVVEL FLPLQMGDKL NYLHTHGQVI EEKYQDNGIY IKTKICKKIA DKFAKYNYKS K // ID C8Q039_9PROT Unreviewed; 456 AA. AC C8Q039; DT 03-NOV-2009, integrated into UniProtKB/TrEMBL. DT 03-NOV-2009, sequence version 1. DT 07-JUN-2017, entry version 38. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:EEV22087.1}; GN ORFNames=ENHAE0001_0017 {ECO:0000313|EMBL:EEV22087.1}; OS Enhydrobacter aerosaccus SK60. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales; OC unclassified Rhodospirillales; Enhydrobacter. OX NCBI_TaxID=553217 {ECO:0000313|EMBL:EEV22087.1, ECO:0000313|Proteomes:UP000010294}; RN [1] {ECO:0000313|EMBL:EEV22087.1, ECO:0000313|Proteomes:UP000010294} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SK60 {ECO:0000313|EMBL:EEV22087.1, RC ECO:0000313|Proteomes:UP000010294}; RA Madupu R., Yinong S., Durkin A.S., Torralba M., Methe B., Sutton G.G., RA Strausberg R.L., Nelson K.E.; RL Submitted (JUL-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EEV22087.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACYI01000065; EEV22087.1; -; Genomic_DNA. DR RefSeq; WP_007116961.1; NZ_ACYI01000065.1. DR ProteinModelPortal; C8Q039; -. DR STRING; 553217.ENHAE0001_0017; -. DR EnsemblBacteria; EEV22087; EEV22087; ENHAE0001_0017. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000010294; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000010294}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000010294}. FT DOMAIN 200 365 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 456 AA; 51052 MW; A23107A908C1565A CRC64; MEYFERYEGG EKAILVHLNI THLNDPDDLE EFELLVDSAG AQKQALVTGT RSKPDAKYFV GTGKAEEIGE LVKQYEADIV IFNHSLTPSQ ERNIERLVQC RVLDRTGLIL DIFAQRARTY EGKLQVELAQ LNHLATRLVR GWTHLERQKG GIGLRGPGET QLETDRRLLQ VRVGQLKAKL DKVKQTRAQG RAKRQKSSVP TISLVGYTNA GKSTLFNTLT HENIYAANQL FATLDPTLRS VSWSGVGKVV LVDTVGFVRH LPHELVEAFH ATLEETLEAD LLLHVIDSHR EDMHEQIAAV QSVLAEIDNQ VPVLNVFNKI DLTGEPPHIG YSDKAKPNRV YVSAHEQLGI EQLTLAVQQL LVGQLQRFEL TLPANFGQLQ HELHKLEVIE DLSYDETGQT KLTAMMSVDK LKQLLGEFGI APEEVLSQAQ AKLLAPVLEP FEQLLQQQPL DTADET // ID C8RZ29_9RHOB Unreviewed; 412 AA. AC C8RZ29; DT 03-NOV-2009, integrated into UniProtKB/TrEMBL. DT 03-NOV-2009, sequence version 1. DT 07-JUN-2017, entry version 39. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=Rsw2DRAFT_1057 {ECO:0000313|EMBL:EEW25986.1}; OS Rhodobacter sp. SW2. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae; Rhodobacter. OX NCBI_TaxID=371731 {ECO:0000313|EMBL:EEW25986.1, ECO:0000313|Proteomes:UP000010121}; RN [1] {ECO:0000313|EMBL:EEW25986.1, ECO:0000313|Proteomes:UP000010121} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SW2 {ECO:0000313|EMBL:EEW25986.1, RC ECO:0000313|Proteomes:UP000010121}; RG US DOE Joint Genome Institute (JGI-PGF); RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., RA Bruce D., Goodwin L., Pitluck S., Larimer F., Land M.L., Hauser L., RA Emerson D.; RT "The draft genome of Rhodobacter sp. SW2."; RL Submitted (AUG-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EEW25986.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACYY01000005; EEW25986.1; -; Genomic_DNA. DR ProteinModelPortal; C8RZ29; -. DR STRING; 371731.Rsw2DRAFT_1057; -. DR EnsemblBacteria; EEW25986; EEW25986; Rsw2DRAFT_1057. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000010121; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000010121}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000010121}. FT DOMAIN 192 361 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 412 AA; 45613 MW; 71E569F7032B723D CRC64; MLHPDLRADR ERRLAENGLA EAVALAAALP NLEVVGSEVV RVGRMQPGTL FGSGKVDELK ARFAALEVDL VLVDGPVSPV QQRNLEKAWG VKLLDRTGLI LEIFADRART REGVMQVELA ALSYQRTRLV RAWTHLERQR GGFGFVGGPG ETQIEADRRA IDDQVIRIKR QLEKVVKTRE LHRAARRRVP FPLVALVGYT NAGKSTLFNR MTGAEVLAKD MLFATLDPTM RGLVLPSGRK IIISDTVGFI SDLPTQLVAA FRATLEEVLE ADLILHVRDI SHPESAEQAA DVAKILAALG VKAATPQIEI WNKLDLVQGA MRDGLVQQAQ GRDGVMALSA LTGEGLPELL EAISRAFDEA KSDLRLTLPF SEGRRHAWLH AEGVVLAETQ TEDGWQIDLR WTARQEQRYR EF // ID C8VW36_DESAS Unreviewed; 414 AA. AC C8VW36; DT 03-NOV-2009, integrated into UniProtKB/TrEMBL. DT 03-NOV-2009, sequence version 1. DT 07-JUN-2017, entry version 66. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Dtox_3611 {ECO:0000313|EMBL:ACV64323.1}; OS Desulfotomaculum acetoxidans (strain ATCC 49208 / DSM 771 / VKM OS B-1644). OC Bacteria; Firmicutes; Clostridia; Clostridiales; Peptococcaceae; OC Desulfotomaculum. OX NCBI_TaxID=485916 {ECO:0000313|EMBL:ACV64323.1, ECO:0000313|Proteomes:UP000002217}; RN [1] {ECO:0000313|EMBL:ACV64323.1, ECO:0000313|Proteomes:UP000002217} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 49208 / DSM 771 / VKM B-1644 RC {ECO:0000313|Proteomes:UP000002217}; RX PubMed=21304664; DOI=10.4056/sigs.39508; RA Spring S., Lapidus A., Schroder M., Gleim D., Sims D., Meincke L., RA Glavina Del Rio T., Tice H., Copeland A., Cheng J.F., Lucas S., RA Chen F., Nolan M., Bruce D., Goodwin L., Pitluck S., Ivanova N., RA Mavromatis K., Mikhailova N., Pati A., Chen A., Palaniappan K., RA Land M., Hauser L., Chang Y.J., Jeffries C.D., Chain P., Saunders E., RA Brettin T., Detter J.C., Goker M., Bristow J., Eisen J.A., RA Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P., Han C.; RT "Complete genome sequence of Desulfotomaculum acetoxidans type strain RT (5575)."; RL Stand. Genomic Sci. 1:242-253(2009). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001720; ACV64323.1; -; Genomic_DNA. DR RefSeq; WP_015759010.1; NC_013216.1. DR ProteinModelPortal; C8VW36; -. DR STRING; 485916.Dtox_3611; -. DR EnsemblBacteria; ACV64323; ACV64323; Dtox_3611. DR KEGG; dae:Dtox_3611; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000002217; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000002217}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000002217}. FT DOMAIN 195 361 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 156 183 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 414 AA; 45966 MW; B0F345433E4DFB63 CRC64; MENLEKVILV GIELPGMSSE QVEESMNELA ALADTAGAEA VDSFIQRRNR PDSKYFIGKG KAEETSQRCR ELEAQLVIFD HELSPSQIRN LIDLMEVRVL DRTQLILDIF AQRASTKEGK LQVELAQLKY LLPRLTGQGK FLSRLGGGIG TRGPGETKLE TDRRRLRERI VDIQAELEEV KKHRALLRKG RKQVPVVSLV GYTNAGKSTL LNKLTGSDVL VEDKLFATLD PTTRQVILPN NDEILVTDTV GFIQNLPHHL VAAFRATLEE VIEADLLLHV VDSTHPNCFE QYKAVQSVLS SLEVENKPSI LVLNKADGLP KPDLNLWINI AGTPVTAISA LTGEGLPGLL ETIAKNLAYR RVRTTFLIPY AKGYLLSQVH EQGLVLSEEH GNDGVRVEVE IERVWAERIA AGLK // ID C8WAR3_ATOPD Unreviewed; 437 AA. AC C8WAR3; DT 03-NOV-2009, integrated into UniProtKB/TrEMBL. DT 03-NOV-2009, sequence version 1. DT 07-JUN-2017, entry version 66. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Apar_0772 {ECO:0000313|EMBL:ACV51201.1}; OS Atopobium parvulum (strain ATCC 33793 / DSM 20469 / JCM 10300 / VPI OS 0546) (Streptococcus parvulus) (Peptostreptococcus parvulus). OC Bacteria; Actinobacteria; Coriobacteriia; Coriobacteriales; OC Atopobiaceae; Atopobium. OX NCBI_TaxID=521095 {ECO:0000313|EMBL:ACV51201.1, ECO:0000313|Proteomes:UP000000960}; RN [1] {ECO:0000313|EMBL:ACV51201.1, ECO:0000313|Proteomes:UP000000960} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33793 / DSM 20469 / JCM 10300 / VPI 0546 RC {ECO:0000313|Proteomes:UP000000960}; RX PubMed=21304653; DOI=10.4056/sigs.29547; RA Copeland A., Sikorski J., Lapidus A., Nolan M., Del Rio T.G., RA Lucas S., Chen F., Tice H., Pitluck S., Cheng J.F., Pukall R., RA Chertkov O., Brettin T., Han C., Detter J.C., Kuske C., Bruce D., RA Goodwin L., Ivanova N., Mavromatis K., Mikhailova N., Chen A., RA Palaniappan K., Chain P., Rohde M., Goker M., Bristow J., Eisen J.A., RA Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P., Detter J.C.; RT "Complete genome sequence of Atopobium parvulum type strain (IPP RT 1246)."; RL Stand. Genomic Sci. 1:166-173(2009). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001721; ACV51201.1; -; Genomic_DNA. DR RefSeq; WP_012808858.1; NC_013203.1. DR ProteinModelPortal; C8WAR3; -. DR STRING; 521095.Apar_0772; -. DR EnsemblBacteria; ACV51201; ACV51201; Apar_0772. DR KEGG; apv:Apar_0772; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000000960; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000000960}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000000960}. FT DOMAIN 210 375 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 437 AA; 48494 MW; 8E6B0B20F55FF8BF CRC64; MGRFVPFSTA PKVERAILVG VDHGKSDWSL EESMDELERL TQTDGAEVFM RITQKLDAPV PKTFIGKGKT EELVSLVKNT DADVVIFDDE LTPSQQSNLE KLLGEPVKVI DRTALILDIF GIHARTKEGR LQVQLAQLQY VLPRLRGMWS HLVGEQTRGG IGSRFGQGES QLEVDRRLIR KRISTLKNEL KQLGQRREIQ SKSRWNSGTF SVSLVGYTNA GKSTLLNQLT GADVYAKDEL FATLDPTTRA LSLDEGRKIV LTDTVGFIQK LPTNLIESFK STLIEAQEAD LLLLVADATD KNLSKEIAVV RSILKDIEAD KSDQVLVLNK VDLLSEQELQ MLKALYPDAV FISAQKGTGI NGLLHKIQEI ASTGDKVVSA LIPFNKGALV KSVHERCQLL HEQYVAEGLL LSVKADTYMQ ALLEPYVISE DNILTDE // ID C8WHI9_EGGLE Unreviewed; 436 AA. AC C8WHI9; DT 03-NOV-2009, integrated into UniProtKB/TrEMBL. DT 03-NOV-2009, sequence version 1. DT 05-JUL-2017, entry version 61. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Elen_1612 {ECO:0000313|EMBL:ACV55580.1}; OS Eggerthella lenta (strain ATCC 25559 / DSM 2243 / JCM 9979 / NCTC OS 11813 / VPI 0255) (Eubacterium lentum). OC Bacteria; Actinobacteria; Coriobacteriia; Eggerthellales; OC Eggerthellaceae; Eggerthella. OX NCBI_TaxID=479437 {ECO:0000313|EMBL:ACV55580.1, ECO:0000313|Proteomes:UP000001377}; RN [1] {ECO:0000313|EMBL:ACV55580.1, ECO:0000313|Proteomes:UP000001377} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 25559 / DSM 2243 / JCM 9979 / NCTC 11813 / VPI 0255 RC {ECO:0000313|Proteomes:UP000001377}; RX PubMed=21304654; DOI=10.4056/sigs.33592; RA Saunders E., Pukall R., Abt B., Lapidus A., Glavina Del Rio T., RA Copeland A., Tice H., Cheng J.F., Lucas S., Chen F., Nolan M., RA Bruce D., Goodwin L., Pitluck S., Ivanova N., Mavromatis K., RA Ovchinnikova G., Pati A., Chen A., Palaniappan K., Land M., Hauser L., RA Chang Y.J., Jeffries C.D., Chain P., Meincke L., Sims D., Brettin T., RA Detter J.C., Goker M., Bristow J., Eisen J.A., Markowitz V., RA Hugenholtz P., Kyrpides N.C., Klenk H.P., Han C.; RT "Complete genome sequence of Eggerthella lenta type strain (IPP VPI RT 0255)."; RL Stand. Genomic Sci. 1:174-182(2009). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001726; ACV55580.1; -; Genomic_DNA. DR ProteinModelPortal; C8WHI9; -. DR STRING; 479437.Elen_1612; -. DR EnsemblBacteria; ACV55580; ACV55580; Elen_1612. DR KEGG; ele:Elen_1612; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000001377; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000001377}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000001377}. FT DOMAIN 217 382 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 436 AA; 47867 MW; 5FE002BDC6498BFB CRC64; MTEFESVITR GMTPISEERR ERAVLVGVDR PGSTWPLASS LAELERLVDT AGADAVATTT QKLDAPNPRT FVGTGKAEEV AELARAHAAD LVVFDDELTP SQQANLEKAM GRDVKVIDRT ALILDIFALH ATSKEGRLQV RLAQNEYLLP RLRGMWAHLA SNRMGGGVGS RFGEGESQLE VDRRMVRKRI TSIKRELKHL AEVRAVQRES RYESGMFKVA LAGYTNAGKS SLLNRLTNAD VLAYDKLFAT LDSTTRKFEL PEGREITVTD TVGFIQKLPT TLIEAFKSTL DEITGADLVL HVVDASSDEY EAQIAAVEDV LGQIHAQDLS RVLVFNKCDL LGEERLGALK ARHPQAQFVS AATGEGVGEL VEHVARVASA QDEHLDVLIP YNRGDLVSVA HERCHILSET HEEQGTRIVM LAAPSFASMF RPYTVG // ID C8WWW0_ALIAD Unreviewed; 365 AA. AC C8WWW0; DT 03-NOV-2009, integrated into UniProtKB/TrEMBL. DT 03-NOV-2009, sequence version 1. DT 07-JUN-2017, entry version 54. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Aaci_1570 {ECO:0000313|EMBL:ACV58582.1}; OS Alicyclobacillus acidocaldarius subsp. acidocaldarius (strain ATCC OS 27009 / DSM 446 / JCM 5260 / NBRC 15652 / NCIMB 11725 / NRRL B-14509 / OS 104-1A) (Bacillus acidocaldarius). OC Bacteria; Firmicutes; Bacilli; Bacillales; Alicyclobacillaceae; OC Alicyclobacillus. OX NCBI_TaxID=521098 {ECO:0000313|EMBL:ACV58582.1, ECO:0000313|Proteomes:UP000001917}; RN [1] {ECO:0000313|Proteomes:UP000001917} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 27009 / DSM 446 / JCM 5260 / NBRC 15652 / NCIMB 11725 / RC NRRL B-14509 / 104-1A {ECO:0000313|Proteomes:UP000001917}; RG US DOE Joint Genome Institute (JGI-PGF); RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., RA Tice H., Bruce D., Goodwin L., Pitluck S., Kyrpides N., Mavromatis K., RA Ivanova N., Ovchinnikova G., Chertkov O., Sims D., Brettin T., RA Detter J.C., Han C., Larimer F., Land M., Hauser L., Markowitz V., RA Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Pukall R., Klenk H.-P., RA Eisen J.A.; RT "The complete chromosome of Alicyclobacillus acidocaldarius subsp. RT acidocaldarius DSM 446."; RL Submitted (SEP-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001727; ACV58582.1; -; Genomic_DNA. DR RefSeq; WP_012810888.1; NC_013205.1. DR STRING; 521098.Aaci_1570; -. DR EnsemblBacteria; ACV58582; ACV58582; Aaci_1570. DR KEGG; aac:Aaci_1570; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000001917; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000001917}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000001917}. FT DOMAIN 195 361 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 155 189 {ECO:0000256|SAM:Coils}. FT COILED 343 365 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 365 AA; 40856 MW; 5272383CE5E48B0E CRC64; MEAEKALLLV WQRSDETQDD VAYRVEELTG LCEAAGAQVV GTVVQWRRSP DGRWYLGQGK VEVLRHLVES TGADLVVADG ELRPTQARNL EDAVHRRVVD RTVLILDIFA RRAVSREGKL QVEIAQLKYL LPRLSGRGAA WSRLGGGIGT RGPGESKLEL DRRRIRARIA KLERDLAELS AHRSRLRQRR VRDSAVVALV GYTNAGKTTV RARWVADRGR VAEAFGRDRL FDTLDVTARR VFEPGGEPYV VTDTVGFVEH LPHHLIEAFR STLEEVAYAD VIVLVVDASR APDRHLRATR QVLADLRALD KPIITFYNKM DLAAWQPPPD LEAQQTVYGS AVAGDLELLY QAVEARLHQA KEKAD // ID C8X570_DESRD Unreviewed; 549 AA. AC C8X570; DT 03-NOV-2009, integrated into UniProtKB/TrEMBL. DT 03-NOV-2009, sequence version 1. DT 07-JUN-2017, entry version 62. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Dret_2283 {ECO:0000313|EMBL:ACV69567.1}; OS Desulfohalobium retbaense (strain ATCC 49708 / DSM 5692 / JCM 16813 / OS HR100). OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfovibrionales; OC Desulfohalobiaceae; Desulfohalobium. OX NCBI_TaxID=485915 {ECO:0000313|EMBL:ACV69567.1, ECO:0000313|Proteomes:UP000001052}; RN [1] {ECO:0000313|Proteomes:UP000001052} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 5692 {ECO:0000313|Proteomes:UP000001052}; RG US DOE Joint Genome Institute (JGI-PGF); RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., RA Tice H., Bruce D., Goodwin L., Pitluck S., Kyrpides N., Mavromatis K., RA Ivanova N., Mikhailova N., Munk A.C., Brettin T., Detter J.C., Han C., RA Tapia R., Larimer F., Land M., Hauser L., Markowitz V., Cheng J.-F., RA Hugenholtz P., Woyke T., Wu D., Spring S., Klenk H.-P., Eisen J.A.; RT "The complete chromosome of Desulfohalobium retbaense DSM 5692."; RL Submitted (SEP-2009) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:ACV69567.1, ECO:0000313|Proteomes:UP000001052} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 5692 {ECO:0000313|EMBL:ACV69567.1, RC ECO:0000313|Proteomes:UP000001052}; RX PubMed=21304676; RA Spring S., Nolan M., Lapidus A., Glavina Del Rio T., Copeland A., RA Tice H., Cheng J.F., Lucas S., Land M., Chen F., Bruce D., Goodwin L., RA Pitluck S., Ivanova N., Mavromatis K., Mikhailova N., Pati A., RA Chen A., Palaniappan K., Hauser L., Chang Y.J., Jeffries C.D., RA Munk C., Kiss H., Chain P., Han C., Brettin T., Detter J.C., RA Schuler E., Goker M., Rohde M., Bristow J., Eisen J.A., Markowitz V., RA Hugenholtz P., Kyrpides N.C., Klenk H.P.; RT "Complete genome sequence of Desulfohalobium retbaense type strain RT (HR(100))."; RL Stand. Genomic Sci. 2:38-48(2010). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001734; ACV69567.1; -; Genomic_DNA. DR RefSeq; WP_015752708.1; NC_013223.1. DR ProteinModelPortal; C8X570; -. DR STRING; 485915.Dret_2283; -. DR EnsemblBacteria; ACV69567; ACV69567; Dret_2283. DR KEGG; drt:Dret_2283; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; EREVIIT; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000001052; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000001052}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000001052}. FT DOMAIN 386 549 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 549 AA; 60959 MW; 517B8A0FC43F850D CRC64; MSKGAAPIAA KVRGSTSGLK PSQLKKLQRL AQRRYPSQGG LSREQVREVA GLTHEVGRQL GLLIDRQGRL EMVVVGEPGR IVIPELGRQR QHSGRLRGLR LVHTHLGQEG LSEEDLMDMV FLRLDSITVL EVDSHGTPGH MQWAHLLPAN ADAKPYTVSK RQPWDRVDID FNAQAEALEE ELARRQEGIA LQARENTTLL VSVGTKPRAR LEAELDELDD LAQTAGLHVA GRLVQRVARL NPKFILGRGK LAELEVKALQ ANAGIIIFDG ELSPSQMRNL AQVTERKVLD RTQLILDIFA QHATSRAGKL QVEMAQLKYT LPRLVGQNRA LSRLAGGIGG RGPGETKLEL DRRKVRERIT RIRKELDKVR KHRAHTRSRR SDAGVPIVAL VGYTNAGKST LLNTITHSQV VAEDKLFATL DPTSRRIRFP QDREVVLTDT VGFIRELPED LREAFLATLE ELEEADVLIQ VADAGHPELE EQVAAVDAIL QDMGLEDIPR LLALNKWDTL EPEARQRVLN IFPHGLPTTA LDKGGLEDLV QAILKRLPA // ID C8XH42_NAKMY Unreviewed; 487 AA. AC C8XH42; DT 03-NOV-2009, integrated into UniProtKB/TrEMBL. DT 03-NOV-2009, sequence version 1. DT 07-JUN-2017, entry version 63. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Namu_3981 {ECO:0000313|EMBL:ACV80273.1}; OS Nakamurella multipartita (strain ATCC 700099 / DSM 44233 / CIP 104796 OS / JCM 9543 / NBRC 105858 / Y-104) (Microsphaera multipartita). OC Bacteria; Actinobacteria; Nakamurellales; Nakamurellaceae; OC Nakamurella. OX NCBI_TaxID=479431 {ECO:0000313|EMBL:ACV80273.1, ECO:0000313|Proteomes:UP000002218}; RN [1] {ECO:0000313|Proteomes:UP000002218} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700099 / DSM 44233 / CIP 104796 / JCM 9543 / NBRC 105858 / RC Y-104 {ECO:0000313|Proteomes:UP000002218}; RG US DOE Joint Genome Institute (JGI-PGF); RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., RA Tice H., Bruce D., Goodwin L., Pitluck S., Kyrpides N., Mavromatis K., RA Ivanova N., Ovchinnikova G., Sims D., Meincke L., Brettin T., RA Detter J.C., Han C., Larimer F., Land M., Hauser L., Markowitz V., RA Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Klenk H.-P., Eisen J.A.; RT "The complete genome of Nakamurella multipartita DSM 44233."; RL Submitted (SEP-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001737; ACV80273.1; -; Genomic_DNA. DR ProteinModelPortal; C8XH42; -. DR STRING; 479431.Namu_3981; -. DR EnsemblBacteria; ACV80273; ACV80273; Namu_3981. DR KEGG; nml:Namu_3981; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000002218; Chromosome. DR GO; GO:0005840; C:ribosome; IEA:InterPro. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro. DR GO; GO:0006412; P:translation; IEA:InterPro. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR018261; Ribosomal_L27_CS. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. DR PROSITE; PS00831; RIBOSOMAL_L27; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000002218}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000002218}. FT DOMAIN 267 432 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 487 AA; 52772 MW; B87363904E4C025B CRC64; MRIQPTHHDG DGGAPIRLRD EPIEFDDLEH TQGDRDLADR AALRRVAGLS TELTDITEVE YRKLQLERVV LVGVWAGAAS TAVAAEESMA ELARLAETAG SVVLEAVMQR RSHPDSATYV GSGKVTELKE IVEVTGADTV ICDGELTPSQ LRNLEEKLRV KVVDRTALIL DIFAQHARSR EGKAQVELAQ LNYLVPRLRG WGSVLSRQRG GRVAAGAGIG SRGPGETKLE IDRRRIHRRI SQLRSDLKDM RRVRDTKRSQ RRANAVPAVS IAGYTNAGKS SLLNRLTDAG VLVEDALFAT LDPTTRRSRT TDGRVYTLTD TVGFVRHLPH QLVESFRSTL EEIGDADLLL HVVDGSDENP EAQVSAVREV LGEIDALSVA EIIVVNKIDA ADEMTLTRLR HVLPGAVFVS ARTGAGIDEL RDRIAAALPD PAVAVNVLMP FSEGALVSRV HSEGTVLGEE HTPDGTLLQA RVYPDLAGVL APFAAAG // ID C9A583_ENTCA Unreviewed; 414 AA. AC C9A583; DT 03-NOV-2009, integrated into UniProtKB/TrEMBL. DT 03-NOV-2009, sequence version 1. DT 07-JUN-2017, entry version 46. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=ECBG_00044 {ECO:0000313|EMBL:EEV37775.1}; OS Enterococcus casseliflavus EC20. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Enterococcaceae; OC Enterococcus. OX NCBI_TaxID=565655 {ECO:0000313|EMBL:EEV37775.1, ECO:0000313|Proteomes:UP000012675}; RN [1] {ECO:0000313|Proteomes:UP000012675} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=EC20 {ECO:0000313|Proteomes:UP000012675}; RA Ishii A., Suzuki M., Sahara T., Takada Y., Sasaki S., Fukunaga N.; RL Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Proteomes:UP000012675} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=EC20 {ECO:0000313|Proteomes:UP000012675}; RG The Broad Institute Genomics Platform; RG The Broad Institute Genome Sequencing Center for Infectious Disease; RA Russ C., Feldgarden M., Gilmore M., Manson J., Palmer K., Carniol K., RA Walker B., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B., RA Abouelleil A., Allen A.W., Alvarado L., Arachchi H.M., Berlin A.M., RA Chapman S.B., Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., RA Hansen M., Howarth C., Imamovic A., Ireland A., Larimer J., RA McCowan C., Murphy C., Pearson M., Poon T.W., Priest M., Roberts A., RA Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C., RA Birren B.; RT "The Genome Sequence of Enterococcus casseliflavus EC20 (899205)."; RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GG670300; EEV37775.1; -; Genomic_DNA. DR RefSeq; WP_005225165.1; NZ_AKCC01000001.1. DR ProteinModelPortal; C9A583; -. DR STRING; 565655.ECBG_00044; -. DR GeneID; 15141263; -. DR KEGG; ecas:ECBG_00044; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR KO; K03665; -. DR Proteomes; UP000012675; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000012675}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000012675}. FT DOMAIN 195 357 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 414 AA; 47173 MW; BEA57219FAA80936 CRC64; MSQERVILVG VETEKNYLHF DSSMKELKSL TKTANGEVVF SLVQKRQQVD RQTVIGKGKV AELQQLAEAH EADLVIFNHE LTPRQSQLIG DALEVPVIDR VQLILDIFAM RARSKEGKLQ VELAQLDYLL PRLIGQGKNM SRLGGGIGTR GPGETKLETD RRHIRNRITI IKRELKEVAA HRDRTRQKRK DSQVFQMGLI GYTNAGKSTI LNILTSADTY EQDQLFATLD PLTKRWRMPE GFEVTITDTV GFIQELPTQL IDAFHSTLEE SQNMDFLLHV VDASSEERVQ QEETVLKLME ELSLTQLPML TVYNKADRID ADQFVPTLFP NVLISAKSTK GKERLTQAIK MELMQIMQPY HLVLQADEGN ALNRLKRESL VLSNAFDEAT QTYHIKGFAL EDTYPLRRMA QEQE // ID C9KKJ3_9FIRM Unreviewed; 615 AA. AC C9KKJ3; DT 24-NOV-2009, integrated into UniProtKB/TrEMBL. DT 24-NOV-2009, sequence version 1. DT 07-JUN-2017, entry version 51. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:EEX69643.1}; GN ORFNames=MITSMUL_03692 {ECO:0000313|EMBL:EEX69643.1}; OS Mitsuokella multacida DSM 20544. OC Bacteria; Firmicutes; Negativicutes; Selenomonadales; OC Selenomonadaceae; Mitsuokella. OX NCBI_TaxID=500635 {ECO:0000313|EMBL:EEX69643.1, ECO:0000313|Proteomes:UP000003671}; RN [1] {ECO:0000313|EMBL:EEX69643.1, ECO:0000313|Proteomes:UP000003671} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 20544 {ECO:0000313|EMBL:EEX69643.1, RC ECO:0000313|Proteomes:UP000003671}; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Nelson J., Hou S., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Nash W.E., Warren W., Chinwalla A., Mardis E.R., RA Wilson R.K.; RL Submitted (SEP-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EEX69643.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABWK02000009; EEX69643.1; -; Genomic_DNA. DR RefSeq; WP_005839901.1; NZ_GG697141.2. DR ProteinModelPortal; C9KKJ3; -. DR STRING; 500635.MITSMUL_03692; -. DR EnsemblBacteria; EEX69643; EEX69643; MITSMUL_03692. DR PATRIC; fig|500635.8.peg.1076; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000003671; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000003671}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000003671}. FT DOMAIN 381 559 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 347 374 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 615 AA; 68624 MW; DF7DB032FEF57516 CRC64; MQINGDIQNI KQHIVKRLEG LYEKTVPIGQ LSTHELNSEM LEVTHLLGRE VAVYLNRQGK VLQVSVGDTD TVDLPEFKSR RAEGKLTGIR CIHTHPSGDT RLSEPDLSSL RRLRFDCMAA IGFRADREGE IVGSLGFFTG DVAEDGTEAL STVGPLPERA LHMINLTYLI TVVNKKLSAR STKTTADETE RALLAGLDCG KTLWPIDESM AELERLADTA GAVIVGKFIQ RREKPDAAFF LGRGKVAEIA MEVQNRDATL LILDDELTPS QQHNLEQMLG IKVIDRTALI LDIFAQRART REGKLQVELA QLQYNLPRLG GQGLVLSRLG GGIGTRGPGE TKLEVDRRRI YARIHDLEAQ IDAVQKNRHL HRRRRKLSRI PLVALVGYTN AGKSTLLNKL TGAEVFAEDK LFATLDPTTR HLVLPEKQEI LLTDTVGFIQ KLPHTLVKAF RATLEEVQEA DLLLHVVDCS NENYEQQIES VVEVLKELDA VDKPTLYVFN KADRFAVPDA APGQARKGLT PAQEAMMLHG REGICVSART GANLLALQQL IEHFFSEQQV QMELLIPFAQ GRLLTELHEL HAVRETDYCE TGTRVKVSLP ASKRARFEPY EIHKK // ID C9LFZ0_9BACT Unreviewed; 421 AA. AC C9LFZ0; DT 24-NOV-2009, integrated into UniProtKB/TrEMBL. DT 24-NOV-2009, sequence version 1. DT 07-JUN-2017, entry version 52. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:EEX71598.1}; GN ORFNames=GCWU000325_01128 {ECO:0000313|EMBL:EEX71598.1}; OS Alloprevotella tannerae ATCC 51259. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Prevotellaceae; OC Alloprevotella. OX NCBI_TaxID=626522 {ECO:0000313|EMBL:EEX71598.1, ECO:0000313|Proteomes:UP000003460}; RN [1] {ECO:0000313|EMBL:EEX71598.1, ECO:0000313|Proteomes:UP000003460} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51259 {ECO:0000313|EMBL:EEX71598.1, RC ECO:0000313|Proteomes:UP000003460}; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Nelson J., Hou S., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Nash W.E., Warren W., Chinwalla A., Mardis E.R., RA Wilson R.K.; RL Submitted (SEP-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EEX71598.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACIJ02000018; EEX71598.1; -; Genomic_DNA. DR RefSeq; WP_006254905.1; NZ_GG700642.1. DR ProteinModelPortal; C9LFZ0; -. DR STRING; 626522.GCWU000325_01128; -. DR EnsemblBacteria; EEX71598; EEX71598; GCWU000325_01128. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000003460; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000003460}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000003460}. FT DOMAIN 216 400 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 421 AA; 48376 MW; E7B5DBA32C10863E CRC64; MEERNTIRKE NERAVLVALI TKTQDERKTK EYLDELEFLA ETAGATTAKR FTQRLDGPSS VTYVGKGKIE EIRDYIIAEE EAERAIDLVI FDDELSAKQL RNIEKEINVR VVDRTNLILD IFAMRAQTAN AKTQVELAQY KYMLPRLQRM WTHLERQGGG SGSGGGKGSV GLRGPGETQL EMDRRIILNR MALLKQRLAD IDRQKKTQRG NRGKMIRVAL VGYTNVGKST LLNLMSKSEV FAENKLFATL DTTVRKVVID NLPFLLTDTV GFIRKIPTDL VDSFKSTLDE VREADLLLHV VDISHPDFEE QIQVVEKTLA ELGTSGRPSI LVFNKIDAYR WIEKEADDLT PKQKENISLA ELQQTYMAKM QENCIFISAR EKTNIEQLRE LLYQKVRELH VQKYPYNDFL YQHYDQEGQP E // ID C9P981_VIBME Unreviewed; 429 AA. AC C9P981; DT 24-NOV-2009, integrated into UniProtKB/TrEMBL. DT 24-NOV-2009, sequence version 1. DT 30-AUG-2017, entry version 46. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=VIB_003076 {ECO:0000313|EMBL:EEX35597.1}; OS Vibrio metschnikovii CIP 69.14. OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; OC Vibrionaceae; Vibrio. OX NCBI_TaxID=675813 {ECO:0000313|EMBL:EEX35597.1, ECO:0000313|Proteomes:UP000005604}; RN [1] {ECO:0000313|EMBL:EEX35597.1, ECO:0000313|Proteomes:UP000005604} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CIP 69.14 {ECO:0000313|EMBL:EEX35597.1, RC ECO:0000313|Proteomes:UP000005604}; RG Los Alamos National Laboratory (LANL); RG National Microbial Pathogen Data Resource (NMPDR); RA Munk A.C., Tapia R., Green L., Rogers Y., Detter J.C., Bruce D., RA Brettin T.S., Colwell R.R., Huq A., Grim C.J., Hasan N.A., Bartels D., RA Vonstein V.; RL Submitted (OCT-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACZO01000010; EEX35597.1; -; Genomic_DNA. DR RefSeq; WP_004397626.1; NZ_ACZO01000010.1. DR ProteinModelPortal; C9P981; -. DR STRING; 675813.VIB_003076; -. DR EnsemblBacteria; EEX35597; EEX35597; VIB_003076. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000005604; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000005604}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000005604}. FT DOMAIN 198 365 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 429 AA; 48660 MW; 2F75DAD2684D57B5 CRC64; MFDRYEAGER AVLVHINFTQ KGEWENLKEC EMLVSSAGVS TLQIVTGSRQ SPHPKYFVGE GKAQEIAQAV QSTEADVVIF NHSLSPAQER NLEQLCQCRV IDRTGLILDI FAQRARTHEG KLQVELAQLR HISTRLVRGW THLERQKGGI GLRGPGETQL ETDRRLLRER IKAILRRLEK VAKQREQGRR ARNRAEIPTI SLVGYTNAGK STLFNQITSA GVYAADQLFA TLDPTLRKIE LLDVGPAILA DTVGFIRHLP HDLVAAFKAT LQETQQADIL LHVVDASDDR FRENIQAVDD VLLEIDAHEV PSLLVMNKID NLEGQYPRIE RDDEGVPRAV WVSAMDGLGM DQLFTALTER LASNIVQYCL RVPPEHQGRI RSTFFQMNCI EKEEYDPEGN LLISVRMQQV DWSRLEKREE AVLRDFIVT // ID C9R8T8_AMMDK Unreviewed; 408 AA. AC C9R8T8; DT 24-NOV-2009, integrated into UniProtKB/TrEMBL. DT 24-NOV-2009, sequence version 1. DT 07-JUN-2017, entry version 50. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Adeg_1623 {ECO:0000313|EMBL:ACX52717.1}; OS Ammonifex degensii (strain DSM 10501 / KC4). OC Bacteria; Firmicutes; Clostridia; Thermoanaerobacterales; OC Thermoanaerobacteraceae; Moorella group; Ammonifex. OX NCBI_TaxID=429009 {ECO:0000313|EMBL:ACX52717.1, ECO:0000313|Proteomes:UP000002620}; RN [1] {ECO:0000313|EMBL:ACX52717.1, ECO:0000313|Proteomes:UP000002620} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 10501 / KC4 {ECO:0000313|Proteomes:UP000002620}; RG US DOE Joint Genome Institute; RA Kerfeld C., Goodner B., Huber H., Stetter K., Lucas S., Copeland A., RA Lapidus A., Glavina del Rio T., Dalin E., Tice H., Bruce D., RA Goodwin L., Pitluck S., Saunders E., Brettin T., Detter J.C., Han C., RA Larimer F., Land M., Hauser L., Kyrpides N., Ovchinnikova G., RA Richardson P.; RT "Complete sequence of chromosome of Ammonifex degensii KC4."; RL Submitted (OCT-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001785; ACX52717.1; -; Genomic_DNA. DR RefSeq; WP_015739594.1; NC_013385.1. DR ProteinModelPortal; C9R8T8; -. DR STRING; 429009.Adeg_1623; -. DR EnsemblBacteria; ACX52717; ACX52717; Adeg_1623. DR KEGG; adg:Adeg_1623; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000002620; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000002620}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000002620}. FT DOMAIN 194 354 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 8 35 {ECO:0000256|SAM:Coils}. FT COILED 153 187 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 408 AA; 46457 MW; 9D95B9511112A5B9 CRC64; MEKGVICYLA QEEEEEEIEY DLQELKELLR NVDIETVATV VQRRLPDPHY LLGPGKITEV KELVEREKIQ AVVFNRELSP RQVQALEDFF GPEVAVWDRT QVILEIFRRR AQSREGKIQV ELARLTYLYP RLYGLGGTLS RLGGGVGTRG PGETKLEVLR RALRRRITEL RRELEEVRAS RDLLRRHRQR SGIPVVSLVG YTNAGKSTLL NALAGEGKEV LAEDRLFATL DPVSRRVILP SGRVFLLTDT VGFIKDLPPK LKEAFKATLE ELETADLLLH VIDLTSPYLD EQQRAVESLL EELGLAEKPI LKVYNKVDRY TGILPADGVV ISALKKINLD QLLHQIEARL FPEEEMELFL PFTSLGKLEK WRERVRVVAE EYGSEGVKVT VRGRPEDLAR LRVQVAGQ // ID C9RPW3_FIBSS Unreviewed; 398 AA. AC C9RPW3; DT 24-NOV-2009, integrated into UniProtKB/TrEMBL. DT 24-NOV-2009, sequence version 1. DT 07-JUN-2017, entry version 65. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=FSU_0331 {ECO:0000313|EMBL:ADL25373.1}; OS Fibrobacter succinogenes (strain ATCC 19169 / S85). OC Bacteria; Fibrobacteres; Fibrobacterales; Fibrobacteraceae; OC Fibrobacter. OX NCBI_TaxID=59374 {ECO:0000313|EMBL:ADL25373.1, ECO:0000313|Proteomes:UP000000517}; RN [1] {ECO:0000313|Proteomes:UP000000517} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 19169 / S85 {ECO:0000313|Proteomes:UP000000517}; RA Durkin A.S., Nelson K.E., Morrison M., Forsberg C.W., Wilson D.B., RA Russell J.B., Cann I.K.O., Mackie R.I., White B.A.; RT "Complete sequence of Fibrobacter succinogenes subsp. succinogenes RT S85."; RL Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002158; ADL25373.1; -; Genomic_DNA. DR RefSeq; WP_014545163.1; NC_017448.1. DR ProteinModelPortal; C9RPW3; -. DR STRING; 59374.Fisuc_3065; -. DR EnsemblBacteria; ADL25373; ADL25373; FSU_0331. DR KEGG; fsc:FSU_0331; -. DR KEGG; fsu:Fisuc_3065; -. DR PATRIC; fig|59374.8.peg.327; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR Proteomes; UP000000517; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000000517}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000000517}. FT DOMAIN 211 375 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 172 209 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 398 AA; 44895 MW; 1FF076BC32EBC346 CRC64; MEEPKKKGAK PVEHKKEQER CILVGIATPK IRPWLAGEQL AELGRLAETA GAYVTRSFLQ RVQNFSPATL IGEGKVGEVK RALEEDNAKM VVFDDDLSGS QVRNLEERMP GIKVLDRTGL ILDIFAKHAV TAESRLMVEV AQLQYMMPRL TGAWTHLCRQ HNGGIGTKGP GETQLETDRR MIRKRIQELK KKLEKIEDAR EQQADKRNDI FQVGIVGYTN AGKSTLTNRL TGADVYVEDK LFATLDSTTR KLFLDGENII LSDTVGFIRK LPHNLIETFK STLGVAAHAD CILEVVDGSA PDYRDHLEVT HKTLESIIDK DTPRLRVFNK VEVASEARRT ELLQNYPDAI QISAKENIGM ERLRAAFKEQ LERWHEKRAV AEAKEKEIAE APWPPELD // ID C9Z0M8_STRSW Unreviewed; 498 AA. AC C9Z0M8; DT 24-NOV-2009, integrated into UniProtKB/TrEMBL. DT 24-NOV-2009, sequence version 1. DT 07-JUN-2017, entry version 63. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=SCAB_24721 {ECO:0000313|EMBL:CBG69581.1}; OS Streptomyces scabiei (strain 87.22). OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae; OC Streptomyces. OX NCBI_TaxID=680198 {ECO:0000313|EMBL:CBG69581.1, ECO:0000313|Proteomes:UP000001444}; RN [1] {ECO:0000313|EMBL:CBG69581.1, ECO:0000313|Proteomes:UP000001444} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=87.22 {ECO:0000313|EMBL:CBG69581.1, RC ECO:0000313|Proteomes:UP000001444}; RX PubMed=20064060; DOI=10.1094/MPMI-23-2-0161; RA Bignell D.R., Seipke R.F., Huguet-Tapia J.C., Chambers A.H., RA Parry R.J., Loria R.; RT "Streptomyces scabies 87-22 contains a coronafacic acid-like RT biosynthetic cluster that contributes to plant-microbe interactions."; RL Mol. Plant Microbe Interact. 23:161-175(2010). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; FN554889; CBG69581.1; -; Genomic_DNA. DR RefSeq; WP_013000272.1; NC_013929.1. DR ProteinModelPortal; C9Z0M8; -. DR STRING; 680198.SCAB_24721; -. DR EnsemblBacteria; CBG69581; CBG69581; SCAB_24721. DR GeneID; 24306193; -. DR KEGG; scb:SCAB_24721; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000001444; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000001444}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000001444}. FT DOMAIN 276 441 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 498 AA; 54296 MW; 508B6250AFFD62D3 CRC64; MTSSSSPSQA AQSAFAQNNP ENLRADALME EDVAWSFEID GERDGDQFDR SDRAALRRVA GLSTELEDVT EVEYRQLRLE RVVLVGVWTT GTVRDAENSL AELAALAETA GALVLDGVIQ RRDKPDAATY IGSGKANELR DVVLESGADT VICDGELSPG QLIHLEDVVK VKVIDRTALI LDIFAQHAKS REGKAQVALA QMQYMLPRLR GWGQSLSRQM GGGKGGGLAT RGPGETKIET DRRRIREKMA KMRREIAEMK TGREIKRQER RRNKVPSVAI AGYTNAGKSS LLNRLTGAGV LVENALFATL DPTVRRAETP SGRLYTLADT VGFVRHLPHH LVEAFRSTME EVGDADLILH VVDGSHPAPE EQLAAVREVI RDVGATKVPE IVVINKADAA DPLTLQRLLR VEKRSIAVSA RSGQGIQELL ALIDNELPRP SVEIEALVPY THGKLVARTH TEGEVISEEH TPEGTLLKAR VHEELAADLA PYVPAATV // ID D0BJZ6_9LACT Unreviewed; 404 AA. AC D0BJZ6; DT 24-NOV-2009, integrated into UniProtKB/TrEMBL. DT 24-NOV-2009, sequence version 1. DT 05-JUL-2017, entry version 43. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=HMPREF0446_00281 {ECO:0000313|EMBL:EEW93399.1}; OS Granulicatella elegans ATCC 700633. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Carnobacteriaceae; OC Granulicatella. OX NCBI_TaxID=626369 {ECO:0000313|EMBL:EEW93399.1, ECO:0000313|Proteomes:UP000002939}; RN [1] {ECO:0000313|EMBL:EEW93399.1, ECO:0000313|Proteomes:UP000002939} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700633 {ECO:0000313|EMBL:EEW93399.1, RC ECO:0000313|Proteomes:UP000002939}; RG The Broad Institute Genome Sequencing Platform; RA Ward D., Feldgarden M., Earl A., Young S.K., Zeng Q., Koehrsen M., RA Alvarado L., Berlin A., Bochicchio J., Borenstein D., Chapman S.B., RA Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A., RA Gujja S., Heilman E., Heiman D., Hepburn T., Howarth C., Jen D., RA Larson L., Lewis B., Mehta T., Park D., Pearson M., Roberts A., RA Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., Thomson T., RA Walk T., White J., Yandava C., Sibley C.D., Field T.R., Grinwis M., RA Eshaghurshan C.S., Surette M.G., Haas B., Nusbaum C., Birren B.; RL Submitted (SEP-2009) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:EEW93399.1, ECO:0000313|Proteomes:UP000002939} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700633 {ECO:0000313|EMBL:EEW93399.1, RC ECO:0000313|Proteomes:UP000002939}; RG The Broad Institute Genome Sequencing Platform; RG The Broad Institute Genome Sequencing Center for Infectious Disease; RA Earl A., Ward D., Feldgarden M., Gevers D., Sibley C.D., Field T.R., RA Grinwis M., Eshaghurshan C.S., Surette M.G., Young S.K., Zeng Q., RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L., RA Arachchi H.M., Berlin A., Brown A., Chapman S.B., Chen Z., Dunbar C., RA Freedman E., Gearin G., Goldberg J., Griggs A., Gujja S., Heiman D., RA Howarth C., Larson L., Lui A., MacDonald P.J.P., Montmayeur A., RA Murphy C., Neiman D., Pearson M., Priest M., Roberts A., Saif S., RA Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., Wortman J., RA Nusbaum C., Birren B.; RT "The Genome Sequence of Granulicatella elegans ATCC 700633."; RL Submitted (OCT-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EEW93399.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACRF02000014; EEW93399.1; -; Genomic_DNA. DR ProteinModelPortal; D0BJZ6; -. DR STRING; 626369.HMPREF0446_00281; -. DR EnsemblBacteria; EEW93399; EEW93399; HMPREF0446_00281. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000002939; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000002939}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000002939}. FT DOMAIN 197 358 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 404 AA; 46075 MW; E1549002F6DC8F92 CRC64; MENTKERVMI VAVQTTQSDE QFQYALEEMK QLVDTAQGEV VVTVTQKRET YSGRTMIGKG KVEEISHLVD ELEIDLIVFY QSLTGSQTKN LNETINARII DRVQLILDIF AMRARSKEGK LQVQLAQLNY LLPRLSGQGT ALSRQGGGIG TRGPGETQLE TDKRHIRKQI SDIEAQLEQT KLHRQRSRMK RNRSNGFRMG LIGYTNAGKS TVLNQLTDAG TYQMDQLFAT LDPLTRKVDL ADQYDVTLTD TVGFIQDLPT TLIHAFESTL EESADVDLLV HVVDASSPNF LMHEKTVHDL VEDLEMETIP MVTIYNKSDL IVGEFQPNAY PSLVISAENS TDIERLREFL GVQMKAEMDY YEEWVEVYEA QKLSQLQQNI LVEILEFNEE KNQYYVKGYR KKGM // ID D0CPV4_RUELI Unreviewed; 423 AA. AC D0CPV4; DT 24-NOV-2009, integrated into UniProtKB/TrEMBL. DT 24-NOV-2009, sequence version 1. DT 07-JUN-2017, entry version 50. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:EEX10631.1}; GN ORFNames=SL1157_2691 {ECO:0000313|EMBL:EEX10631.1}; OS Ruegeria lacuscaerulensis (strain DSM 11314 / KCTC 2953 / ITI-1157) OS (Silicibacter lacuscaerulensis). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae; Ruegeria. OX NCBI_TaxID=644107 {ECO:0000313|EMBL:EEX10631.1, ECO:0000313|Proteomes:UP000005093}; RN [1] {ECO:0000313|EMBL:EEX10631.1, ECO:0000313|Proteomes:UP000005093} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 11314 / KCTC 2953 / ITI-1157 RC {ECO:0000313|Proteomes:UP000005093}; RA Zinser E., Buchan A., Ferriera S.F., Johnson J.J., Kravitz S.K., RA Beeson K.B., Sutton G.S., Rogers Y.-H.R., Friedman R.F., Frazier M.F., RA Venter J.C.V.; RL Submitted (SEP-2008) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GG704596; EEX10631.1; -; Genomic_DNA. DR RefSeq; WP_005982827.1; NZ_GG704596.1. DR STRING; 644107.SL1157_2691; -. DR EnsemblBacteria; EEX10631; EEX10631; SL1157_2691. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000005093; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000005093}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000005093}. SQ SEQUENCE 423 AA; 47350 MW; B522F193E0C88CDC CRC64; MEHDRRRTRA WVLHPDIKSD DQRRDPVPAL DEAVALAAAL PDLDVIGSEI VRLPRAQPGL LFGSGKIEEL GARFAENEIE LVLIDGPVTP VQQRNLEKAW KVKILDRTGL ILEIFSDRAR TREGVLQVEM AALSYQRTRL VRAWTHLERQ RGGLGFVGGP GETQIEADRR AIDDQLVRLR RQLQKVVKTR TLHRAARAKV PYPIVALVGY TNAGKSTLFN RLTGAEVMAK DMLFATLDPT MRRIELPDGP EVILSDTVGF ISNLPTELVA AFRATLEEVL AADLIVHVRD ISHPETEEQA EDVRSILASL GVDDTRPQLE VWNKIDLLSD EDRQAVQARA ERDPAVFPIS AVTGEGIDPL LTEIATILQG VRWEEVLKLG FADGDKRAWL FRQDVVRDEK QTEDGFEITV LWTDKQAAQF AAL // ID D0D0X8_9RHOB Unreviewed; 417 AA. AC D0D0X8; DT 24-NOV-2009, integrated into UniProtKB/TrEMBL. DT 24-NOV-2009, sequence version 1. DT 07-JUN-2017, entry version 39. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:EEX15637.1}; GN ORFNames=CSE45_1388 {ECO:0000313|EMBL:EEX15637.1}; OS Citreicella sp. SE45. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae; Citreicella. OX NCBI_TaxID=501479 {ECO:0000313|EMBL:EEX15637.1, ECO:0000313|Proteomes:UP000005759}; RN [1] {ECO:0000313|EMBL:EEX15637.1, ECO:0000313|Proteomes:UP000005759} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SE45 {ECO:0000313|EMBL:EEX15637.1, RC ECO:0000313|Proteomes:UP000005759}; RA Buchan A., Ferriera S.F., Johnson J.J., Kravitz S.K., Beeson K.B., RA Sutton G.S., Rogers Y.-H.R., Friedman R.F., Frazier M.F., RA Venter J.C.V.; RL Submitted (SEP-2008) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GG704599; EEX15637.1; -; Genomic_DNA. DR RefSeq; WP_008885595.1; NZ_GG704599.1. DR ProteinModelPortal; D0D0X8; -. DR STRING; 501479.CSE45_1388; -. DR EnsemblBacteria; EEX15637; EEX15637; CSE45_1388. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000005759; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000005759}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000005759}. FT DOMAIN 197 366 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 417 AA; 46849 MW; 911ADACC84DA1AE1 CRC64; MTRAWVLHPD IRSDRDRRDA EMALEEAVAL AVALPDLEVV GSAVVPVRDP HPGHLFGTGK IEELKTLFEE AEVELVLVDG PVSPVQQRNL EKQWKVKLLD RTGLILEIFS DRAATREGVL QVEMAALSYQ RTRLVRAWTH LERQRGGLGF VGGPGETQIE ADRRAIDEQL VRLRRQLDRV VKTRDLHRKA RAKVPFPIVA LVGYTNAGKS TLFNRLTGAE VMAKDMLFAT LDPTMRAVRL PTGIEVILSD TVGFISDLPT ELVAAFRATL EEVLAADVVV HVRDISHPNT EEQSEDVETI LASLGLDEEV PRIEVWNKID RLHPDERDAL LTRAEREEQV YAVSALTGDG LDVMLRAVTD LLQGETVEEE LLLGFDEGRR RSWLFGKGLV TDERQEEDGF VVRVRWSAKD RAQFQSL // ID D0J2Q5_COMT2 Unreviewed; 387 AA. AC D0J2Q5; DT 15-DEC-2009, integrated into UniProtKB/TrEMBL. DT 15-DEC-2009, sequence version 1. DT 07-JUN-2017, entry version 51. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=CtCNB1_3282 {ECO:0000313|EMBL:ACY34028.1}; OS Comamonas testosteroni (strain CNB-2). OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Comamonadaceae; Comamonas. OX NCBI_TaxID=688245 {ECO:0000313|EMBL:ACY34028.1, ECO:0000313|Proteomes:UP000002360}; RN [1] {ECO:0000313|EMBL:ACY34028.1, ECO:0000313|Proteomes:UP000002360} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CNB-2 {ECO:0000313|Proteomes:UP000002360}; RX PubMed=19734336; DOI=10.1128/AEM.00933-09; RA Ma Y.F., Zhang Y., Zhang J.Y., Chen D.W., Zhu Y., Zheng H., Wang S.Y., RA Jiang C.Y., Zhao G.P., Liu S.J.; RT "The complete genome of Comamonas testosteroni reveals its genetic RT adaptations to changing environments."; RL Appl. Environ. Microbiol. 75:6812-6819(2009). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001220; ACY34028.1; -; Genomic_DNA. DR ProteinModelPortal; D0J2Q5; -. DR STRING; 688245.CtCNB1_3282; -. DR EnsemblBacteria; ACY34028; ACY34028; CtCNB1_3282. DR KEGG; ctt:CtCNB1_3282; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR Proteomes; UP000002360; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000002360}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000002360}. FT DOMAIN 189 362 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 155 182 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 387 AA; 43581 MW; C5323D5A913A50C6 CRC64; MLLVGVDFGV PHFDDELEEL GLLAQTAGLQ PVARLTCKRK APDPALFVGS GKADEIRMLA QMHGAKEVWF DQALSPAQQR NLERHIQMPV NDRTMLILEI FAQRARSHEG KLQVELARLQ YISTRLVRRW SHLERQAGGI GGRGGPGEKQ IELDRRMIDD AIKRTKERLK KVKKQRSTQR RQRSRREVFN ISLVGYTNAG KSTLFNAMVK ARAYAADQLF ATLDTTTRQM YLAEAEESVS LSDTVGFIRD LPHGLVDAFQ ATLQEAIDAD LLLHVVDASN PGFPEQIQQV QKVLGEIGAD DVPQILVFNK LDAIEPERQP ALLQDMYELD GTPVPRVFVS ARSGRGLAQL RQMLADRVLQ VREEAAREEV EGQDDTYWMS PDDDAQY // ID D0KVK4_HALNC Unreviewed; 440 AA. AC D0KVK4; DT 15-DEC-2009, integrated into UniProtKB/TrEMBL. DT 15-DEC-2009, sequence version 1. DT 07-JUN-2017, entry version 52. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Hneap_2012 {ECO:0000313|EMBL:ACX96834.1}; OS Halothiobacillus neapolitanus (strain ATCC 23641 / c2) (Thiobacillus OS neapolitanus). OC Bacteria; Proteobacteria; Gammaproteobacteria; Chromatiales; OC Halothiobacillaceae; Halothiobacillus. OX NCBI_TaxID=555778 {ECO:0000313|EMBL:ACX96834.1, ECO:0000313|Proteomes:UP000009102}; RN [1] {ECO:0000313|EMBL:ACX96834.1, ECO:0000313|Proteomes:UP000009102} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 23641 / c2 {ECO:0000313|Proteomes:UP000009102}; RG US DOE Joint Genome Institute; RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., RA Bruce D., Goodwin L., Pitluck S., Davenport K., Brettin T., RA Detter J.C., Han C., Tapia R., Larimer F., Land M., Hauser L., RA Kyrpides N., Mikhailova N., Kerfeld C., Cannon G., Heinhort S.; RT "Complete sequence of Halothiobacillus neapolitanus c2."; RL Submitted (OCT-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001801; ACX96834.1; -; Genomic_DNA. DR RefSeq; WP_012824866.1; NC_013422.1. DR ProteinModelPortal; D0KVK4; -. DR STRING; 555778.Hneap_2012; -. DR EnsemblBacteria; ACX96834; ACX96834; Hneap_2012. DR KEGG; hna:Hneap_2012; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR BioCyc; HNEA555778:GIVV-2059-MONOMER; -. DR Proteomes; UP000009102; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR Gene3D; 3.40.50.620; -; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR014729; Rossmann-like_a/b/a_fold. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000009102}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000009102}. FT DOMAIN 201 368 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 167 194 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 440 AA; 49632 MW; B61CAC96A0049C31 CRC64; MQFFERHEGG ERAVLLHVAS RQQSRAEDLD EFRELVDSAG AEILGECLAS REAPDPRLYI GKGKAEELAD LVKSTEADLV VVNAQLSPSQ ERNLESVLHC RVLDRTGLIL DIFSQRARSH EGKLQVELAQ LKHLSTRLVR GWTHLERQRG GSIGLRGPGE TQLEMDRRLI HDRIKQLQDR IAKVRRQRQE GRKTRQKSQV PMVSLVGYTN AGKSTLFNAL TEAGTFAADQ LFATLDTTLR RLEFAPGEPM VLADTVGFIR HLPHELVTAF RSTLEETLEA DLLIHVVDAA SPERDRQMTD VEVVLKEIGA DTLPRLTVMN KIDQLEDRAP EISRNEAGEI DRVWMSAQSG AGMDLLRQAL GERLRPTRTI INLFLPASLG GLRARWLNEG AIVTEHWQDD RMHDEMPQPG WQLTLSLTEA RWAQWRKHHP ELEACLAAPA // ID D0LBP9_GORB4 Unreviewed; 484 AA. AC D0LBP9; DT 15-DEC-2009, integrated into UniProtKB/TrEMBL. DT 15-DEC-2009, sequence version 1. DT 07-JUN-2017, entry version 51. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Gbro_2215 {ECO:0000313|EMBL:ACY21463.1}; OS Gordonia bronchialis (strain ATCC 25592 / DSM 43247 / JCM 3198 / NCTC OS 10667) (Rhodococcus bronchialis). OC Bacteria; Actinobacteria; Corynebacteriales; Gordoniaceae; Gordonia. OX NCBI_TaxID=526226 {ECO:0000313|EMBL:ACY21463.1, ECO:0000313|Proteomes:UP000001219}; RN [1] {ECO:0000313|Proteomes:UP000001219} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 25592 / DSM 43247 / JCM 3198 / NCTC 10667 RC {ECO:0000313|Proteomes:UP000001219}; RG US DOE Joint Genome Institute (JGI-PGF); RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., RA Tice H., Bruce D., Goodwin L., Pitluck S., Kyrpides N., Mavromatis K., RA Ivanova N., Ovchinnikova G., Saunders E., Brettin T., Detter J.C., RA Han C., Larimer F., Land M., Hauser L., Markowitz V., Cheng J.-F., RA Hugenholtz P., Woyke T., Wu D., Jando M., Schneider S., Goeker M., RA Klenk H.-P., Eisen J.A.; RT "The complete chromosome of Gordonia bronchialis DSM 43247."; RL Submitted (OCT-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001802; ACY21463.1; -; Genomic_DNA. DR ProteinModelPortal; D0LBP9; -. DR STRING; 526226.Gbro_2215; -. DR EnsemblBacteria; ACY21463; ACY21463; Gbro_2215. DR KEGG; gbr:Gbro_2215; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000001219; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000001219}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000001219}. FT DOMAIN 259 429 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 218 245 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 484 AA; 52459 MW; D05E32B82B10F70E CRC64; MSPEIDEPPQ SVDDWLDDHP QSAPTTGELQ LSERASLQRV AGLSTELTDV TEVEYRQLRL ERVVLVGVWT EGSAAAARAN MVELAALAET AGSQVLEALI QRRGKPDPAT YIGSGKAEEL REVVLATGAD TVICDGELTP AQLTALEKVV KVKVIDRTAL ILDIFAQHAT SREGKAQVSL AQMEYMMPRL RGWGESMSRQ AGGRAGSNGG VGLRGPGETK IETDRRRIRE RMAKLRREIR GMKKARTTKR AARRRTEIPA ITVAGYTNAG KSSLVNAMTG SGVLVQDALF ATLDPTTRRA TLDDGRAVVF TDTVGFVRHL PTQLVEAFRS TLEEVVDADL LLHVVDGSDP FPAEQIAAVR RVVNEIVAEE KADAPPEMLV INKIDAIDAT RLTELRGALG ADAVFVSART GEGLPELFDR IREFVGRSDV ELTIAVPFSR GDIISRIHRE GEVLATDHHA DGTTMRVRVP SAFAGELAPL TVDP // ID D0LMD8_HALO1 Unreviewed; 488 AA. AC D0LMD8; DT 15-DEC-2009, integrated into UniProtKB/TrEMBL. DT 15-DEC-2009, sequence version 1. DT 07-JUN-2017, entry version 49. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Hoch_4350 {ECO:0000313|EMBL:ACY16844.1}; OS Haliangium ochraceum (strain DSM 14365 / JCM 11303 / SMP-2). OC Bacteria; Proteobacteria; Deltaproteobacteria; Myxococcales; OC Nannocystineae; Kofleriaceae; Haliangium. OX NCBI_TaxID=502025 {ECO:0000313|EMBL:ACY16844.1, ECO:0000313|Proteomes:UP000001880}; RN [1] {ECO:0000313|EMBL:ACY16844.1, ECO:0000313|Proteomes:UP000001880} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 14365 / JCM 11303 / SMP-2 RC {ECO:0000313|Proteomes:UP000001880}; RX PubMed=21304682; DOI=10.4056/sigs.69.1277; RG US DOE Joint Genome Institute (JGI-PGF); RA Ivanova N., Daum C., Lang E., Abt B., Kopitz M., Saunders E., RA Lapidus A., Lucas S., Glavina Del Rio T., Nolan M., Tice H., RA Copeland A., Cheng J.F., Chen F., Bruce D., Goodwin L., Pitluck S., RA Mavromatis K., Pati A., Mikhailova N., Chen A., Palaniappan K., RA Land M., Hauser L., Chang Y.J., Jeffries C.D., Detter J.C., RA Brettin T., Rohde M., Goker M., Bristow J., Markowitz V., Eisen J.A., RA Hugenholtz P., Kyrpides N.C., Klenk H.P.; RT "Complete genome sequence of Haliangium ochraceum type strain (SMP- RT 2)."; RL Stand. Genomic Sci. 2:96-106(2010). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001804; ACY16844.1; -; Genomic_DNA. DR RefSeq; WP_012829442.1; NC_013440.1. DR ProteinModelPortal; D0LMD8; -. DR STRING; 502025.Hoch_4350; -. DR EnsemblBacteria; ACY16844; ACY16844; Hoch_4350. DR KEGG; hoh:Hoch_4350; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; FNNHAHV; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000001880; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 2. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000001880}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000001880}. FT DOMAIN 267 432 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 488 AA; 52356 MW; 1DDFF824FA38F382 CRC64; MFDNGSNNPP TTPVHPRRAV LVAATAGLSE QMMSASLGEM RQLLRGLGIE VVAEVVQRRA AGNAPGYLGP GKLRELARFT GGSGELRRGP PRPKRAAEPG EDGEDGGDAL RADGAPAAGD DFDHVSGDQA DLAADAAEAG ESLEPVDLVV VDDALDPGQQ RNLERATGAE VLDRGAVILW VFETRAKTRA AQLEIELARL SYELPRLRDD AMVSERSGGG GGRAARGHSN VVLAKQRTRD RIASLKRELA AVQASAATRR QRRASSHRVA LLGYTNAGKS TLMRALTGSE VLVADALFAS LDITVRQLAP PATPPVLVAD TVGFMNRLPH ELMASFRSTL DEVHEASLLL HVVDASDPHL RDQIDVVTEV VSDIGATELP TWLVLNKIDQ VDEETRAALR EAFPEAIELS ALRPEDSAAL RARIVDFFDQ RLVTEEVEIP YAASGVLAEL RSHARVLSEQ YGDALVATVR ASPEVLARLR KRLAEARA // ID D0LYG2_HALO1 Unreviewed; 563 AA. AC D0LYG2; DT 15-DEC-2009, integrated into UniProtKB/TrEMBL. DT 15-DEC-2009, sequence version 1. DT 07-JUN-2017, entry version 50. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Hoch_5344 {ECO:0000313|EMBL:ACY17828.1}; OS Haliangium ochraceum (strain DSM 14365 / JCM 11303 / SMP-2). OC Bacteria; Proteobacteria; Deltaproteobacteria; Myxococcales; OC Nannocystineae; Kofleriaceae; Haliangium. OX NCBI_TaxID=502025 {ECO:0000313|EMBL:ACY17828.1, ECO:0000313|Proteomes:UP000001880}; RN [1] {ECO:0000313|EMBL:ACY17828.1, ECO:0000313|Proteomes:UP000001880} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 14365 / JCM 11303 / SMP-2 RC {ECO:0000313|Proteomes:UP000001880}; RX PubMed=21304682; DOI=10.4056/sigs.69.1277; RG US DOE Joint Genome Institute (JGI-PGF); RA Ivanova N., Daum C., Lang E., Abt B., Kopitz M., Saunders E., RA Lapidus A., Lucas S., Glavina Del Rio T., Nolan M., Tice H., RA Copeland A., Cheng J.F., Chen F., Bruce D., Goodwin L., Pitluck S., RA Mavromatis K., Pati A., Mikhailova N., Chen A., Palaniappan K., RA Land M., Hauser L., Chang Y.J., Jeffries C.D., Detter J.C., RA Brettin T., Rohde M., Goker M., Bristow J., Markowitz V., Eisen J.A., RA Hugenholtz P., Kyrpides N.C., Klenk H.P.; RT "Complete genome sequence of Haliangium ochraceum type strain (SMP- RT 2)."; RL Stand. Genomic Sci. 2:96-106(2010). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001804; ACY17828.1; -; Genomic_DNA. DR RefSeq; WP_012830420.1; NC_013440.1. DR ProteinModelPortal; D0LYG2; -. DR STRING; 502025.Hoch_5344; -. DR EnsemblBacteria; ACY17828; ACY17828; Hoch_5344. DR KEGG; hoh:Hoch_5344; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; EREVIIT; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000001880; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000001880}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000001880}. FT DOMAIN 378 542 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 337 364 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 563 AA; 63128 MW; 6166DEFCE6BCD7E0 CRC64; MKQDVTGNTT GLKASQIKAL ERIYRRRIDQ TEVISAELAA FMCEISAELH RQIGVLVDRR GAIAHVMVGD ASKIMLPDVG RMRGGMGRFR GLRLVHTHLR GEKLTRDDLT DLALLRLDVV AAITVAPGGR PGPMYIGHLL PDNPKGDMWR ELPSESVYEP ETDFAALMDA LEAEFQRKRQ LASTENQHRA LLVHVALGRE EDTEARIAEL RELCRTAGVD ALDILTQRRP SADPRYLVGR GKLEQILLRA MQLGAESVIF NQDLTPGQAR AITNFTELKI LDRTMLILDI FAQHAVSRDG KLQVELAQLK YALPRLAEKN TMMSRLTGGI GGRGPGETKL EINRRRARDR IRFLENKLEG LAKNRRLRRQ RRESRDVPIV AIVGYTNAGK STLLNALTEG NAKAENKLFA TLDPISRRLR FPQEREVVLT DTVGFIRDLP PDLVTAFRAT LEELEDADLL VHVVDLSDPD YEQHVRAVTQ ILSDLELGEK PRLLGFNKCD RLDAEEAGRL AESHDAYAFS ALDHQTFNEL LRAIERELWR EGHAAMAQPP SPDDYTSLPA DSP // ID D0MGM9_RHOM4 Unreviewed; 442 AA. AC D0MGM9; DT 15-DEC-2009, integrated into UniProtKB/TrEMBL. DT 15-DEC-2009, sequence version 1. DT 07-JUN-2017, entry version 61. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Rmar_2721 {ECO:0000313|EMBL:ACY49592.1}; OS Rhodothermus marinus (strain ATCC 43812 / DSM 4252 / R-10) OS (Rhodothermus obamensis). OC Bacteria; Bacteroidetes; Bacteroidetes Order II. Incertae sedis; OC Rhodothermaceae; Rhodothermus. OX NCBI_TaxID=518766 {ECO:0000313|EMBL:ACY49592.1, ECO:0000313|Proteomes:UP000002221}; RN [1] {ECO:0000313|EMBL:ACY49592.1, ECO:0000313|Proteomes:UP000002221} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43812 / DSM 4252 / R-10 RC {ECO:0000313|Proteomes:UP000002221}; RX PubMed=21304669; DOI=10.4056/sigs.46736; RA Nolan M., Tindall B.J., Pomrenke H., Lapidus A., Copeland A., RA Glavina Del Rio T., Lucas S., Chen F., Tice H., Cheng J.F., RA Saunders E., Han C., Bruce D., Goodwin L., Chain P., Pitluck S., RA Ovchinikova G., Pati A., Ivanova N., Mavromatis K., Chen A., RA Palaniappan K., Land M., Hauser L., Chang Y.J., Jeffries C.D., RA Brettin T., Goker M., Bristow J., Eisen J.A., Markowitz V., RA Hugenholtz P., Kyrpides N.C., Klenk H.P., Detter J.C.; RT "Complete genome sequence of Rhodothermus marinus type strain (R- RT 10)."; RL Stand. Genomic Sci. 1:283-291(2009). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001807; ACY49592.1; -; Genomic_DNA. DR RefSeq; WP_012845202.1; NC_013501.1. DR ProteinModelPortal; D0MGM9; -. DR STRING; 518766.Rmar_2721; -. DR EnsemblBacteria; ACY49592; ACY49592; Rmar_2721. DR KEGG; rmr:Rmar_2721; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000002221; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000002221}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000002221}. FT DOMAIN 200 366 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 442 AA; 50155 MW; 36BAD4D15DC1FF96 CRC64; MYTATAPRPE TAILVGVVTP ETTRWDVEDS LEELAQLART AGAEVTDRVL QVLRRVHAAT YVGRGKVEEL KRLVAARKSD LVIFDDDLSP AQMRNLERAL GCKLLDRTGL ILDIFARRAR TAVAKTQVEL AQLEYMRTRL TRQWTHLSRQ KGGIGTKGPG ETQIETDRRL IARRIAVLRE RLERIDRQRT TQRKKRQRYT RVSLVGYTNA GKSTLMNVLA GTNVLAEDRL FATLDATTRL VHLEPGKPVL LSDTVGFIRK LPHRLIESFK STLDEVRESD VLLHLVDATH PRFEDHIQVV HETLAELGAA DKPMLLVFNK IDRLADLGLL QALRTEYPEA VFISALRGIG LEELKRRLQE RIEAEALELD VCVPLTEGRT LSYLYQVADV LEETYLYAHN GHDETPLPAA RLRLRVPVHR QAAVERLLMR FRSLQPLPDM SS // ID D0WQY6_9ACTO Unreviewed; 499 AA. AC D0WQY6; DT 19-JAN-2010, integrated into UniProtKB/TrEMBL. DT 19-JAN-2010, sequence version 1. DT 07-JUN-2017, entry version 38. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:EEZ77145.1}; GN ORFNames=HMPREF0972_02223 {ECO:0000313|EMBL:EEZ77145.1}; OS Actinomyces sp. oral taxon 848 str. F0332. OC Bacteria; Actinobacteria; Actinomycetales; Actinomycetaceae; OC Actinomyces. OX NCBI_TaxID=649743 {ECO:0000313|EMBL:EEZ77145.1, ECO:0000313|Proteomes:UP000003063}; RN [1] {ECO:0000313|EMBL:EEZ77145.1, ECO:0000313|Proteomes:UP000003063} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=F0332 {ECO:0000313|EMBL:EEZ77145.1, RC ECO:0000313|Proteomes:UP000003063}; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Nelson J., Hou S., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Nash W.E., Warren W., Chinwalla A., Mardis E.R., RA Wilson R.K.; RL Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EEZ77145.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACUY02000014; EEZ77145.1; -; Genomic_DNA. DR RefSeq; WP_009199815.1; NZ_GG703880.1. DR ProteinModelPortal; D0WQY6; -. DR STRING; 649743.HMPREF0972_02223; -. DR EnsemblBacteria; EEZ77145; EEZ77145; HMPREF0972_02223. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000003063; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000003063}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000003063}. FT DOMAIN 272 438 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 499 AA; 53686 MW; 084D94F8494934F8 CRC64; MNESTSGAGS SESRIDLHTA EGTALQAVSH EDAGWSGDAL EREERSSLQR IQGLETGISR EEGVDVEYRQ VRLERVVLVG LWSEGSASQA EDSLRELAAL AETAGSKVLD GLIQRRALPD PATYLGSGKA HELADLVASL EADTVIADSE LAPSQRRGLE DIVKVKVIDR TALILDIFAR HAKSREGKAQ VELAQLEYLL PRLRGWGDSM SRQAGGRVAA GAGIGSRGPG ETQLELDRRR IRTRMAKLRR DIKRMGPARQ QQRAERRRAA TPSAVVVGYT NAGKSSLLNR LTGAGVLVEN ALFATLDPTV RRTQTASGRE YTLADTVGFV RQLPTQLVEA FRSTLEEAGE ADVLVHVVDA SHHDPVGQVK AVRKVLAEVP GTREAREIVV LSKSDLADPV DLAALRSRFP GSIAVSCLTG EGVDELRAAI EEALPQPEIE IAVVVPYSAG ALLSRIHDDG ELLAPVEYRG EGVFVHARVP ADIEAAMRRG GMLSPAETK // ID D0Z0G9_PHODD Unreviewed; 429 AA. AC D0Z0G9; DT 19-JAN-2010, integrated into UniProtKB/TrEMBL. DT 19-JAN-2010, sequence version 1. DT 30-AUG-2017, entry version 45. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=VDA_003033 {ECO:0000313|EMBL:EEZ42000.1}; OS Photobacterium damselae subsp. damselae CIP 102761. OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; OC Vibrionaceae; Photobacterium. OX NCBI_TaxID=675817 {ECO:0000313|EMBL:EEZ42000.1, ECO:0000313|Proteomes:UP000003579}; RN [1] {ECO:0000313|EMBL:EEZ42000.1, ECO:0000313|Proteomes:UP000003579} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CIP 102761 {ECO:0000313|EMBL:EEZ42000.1, RC ECO:0000313|Proteomes:UP000003579}; RG Los Alamos National Laboratory (LANL); RG National Microbial Pathogen Data Resource (NMPDR); RA Munk A.C., Tapia R., Green L., Rogers Y., Detter J.C., Bruce D., RA Brettin T.S., Colwell R., Huq A., Grim C.J., Hasan N.A., Vonstein V., RA Bartels D.; RL Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADBS01000001; EEZ42000.1; -; Genomic_DNA. DR RefSeq; WP_005301649.1; NZ_ADBS01000001.1. DR ProteinModelPortal; D0Z0G9; -. DR STRING; 675817.VDA_003033; -. DR EnsemblBacteria; EEZ42000; EEZ42000; VDA_003033. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000003579; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000003579}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000003579}. FT DOMAIN 198 365 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 429 AA; 48502 MW; E75BE3EE11753306 CRC64; MFDRYEAGEQ AVLVHVNFTQ EGEWEDLREF EMLVSSAGVN SLRVVTGSRK TPHPKYYVGE GKALEIADAV RAVDADIVIF NHALSPAQER NLEQLCQCRV VDRTGLILDI FAQRARTHEG KLQVELAQLR HLSTRLIRGW THLERQKGGI GLRGPGETQL ETDRRLLRER IKAILRRLDK VAKQREQGRR ARNRAEIPTI SLVGYTNAGK STLFNRITDA GVYAADQLFA TLDPTLRKVE VADVGTAILA DTVGFIRHLP HDLVAAFKAT LKETQEADLL LHVVDASDDR FRENIDAVES VLEEIEAHEV PSLLVMNKID NLEGAKPRIE RDDDGVPRRV WVSAMEGIGL DLLFQALTER LSGTMVKHTL RLPPELIGRY RSKFYQLGCI LREEYESDGC LTIDIRIQLA DWSRLQKRES TSLDDFIVA // ID D1AA95_THECD Unreviewed; 485 AA. AC D1AA95; DT 19-JAN-2010, integrated into UniProtKB/TrEMBL. DT 19-JAN-2010, sequence version 1. DT 07-JUN-2017, entry version 66. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Tcur_3269 {ECO:0000313|EMBL:ACY98808.1}; OS Thermomonospora curvata (strain ATCC 19995 / DSM 43183 / JCM 3096 / OS NBRC 15933 / NCIMB 10081 / Henssen B9). OC Bacteria; Actinobacteria; Streptosporangiales; Thermomonosporaceae; OC Thermomonospora. OX NCBI_TaxID=471852 {ECO:0000313|EMBL:ACY98808.1, ECO:0000313|Proteomes:UP000001918}; RN [1] {ECO:0000313|EMBL:ACY98808.1, ECO:0000313|Proteomes:UP000001918} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 19995 / DSM 43183 / JCM 3096 / NBRC 15933 / NCIMB 10081 / RC Henssen B9 {ECO:0000313|Proteomes:UP000001918}; RX PubMed=21475583; DOI=10.4056/sigs.1453580; RA Chertkov O., Sikorski J., Nolan M., Lapidus A., Lucas S., RA Del Rio T.G., Tice H., Cheng J.F., Goodwin L., Pitluck S., Liolios K., RA Ivanova N., Mavromatis K., Mikhailova N., Ovchinnikova G., Pati A., RA Chen A., Palaniappan K., Djao O.D., Land M., Hauser L., Chang Y.J., RA Jeffries C.D., Brettin T., Han C., Detter J.C., Rohde M., Goker M., RA Woyke T., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P., RA Klenk H.P., Kyrpides N.C.; RT "Complete genome sequence of Thermomonospora curvata type strain RT (B9)."; RL Stand. Genomic Sci. 1:13-22(2011). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001738; ACY98808.1; -; Genomic_DNA. DR RefSeq; WP_012853592.1; NC_013510.1. DR ProteinModelPortal; D1AA95; -. DR STRING; 471852.Tcur_3269; -. DR EnsemblBacteria; ACY98808; ACY98808; Tcur_3269. DR KEGG; tcu:Tcur_3269; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000001918; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000001918}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000001918}. FT DOMAIN 263 428 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 229 256 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 485 AA; 53043 MW; 6E936222E9548493 CRC64; MTSAFFEDPQ IHRDGRDDGT PEDFRDEPLT GELDLADRQA LRRVAGLSTE LADITEVEYR TLRLERVVLV GVWTEGTAQQ AESSLRELAA LAETAGSQVL EGLIQRRSKP DVATYIGSGK TAELAEIVRA TGADTVICDG ELSPSQLRHL EEIVKVKVID RTALILDIFA QHARSREGKA QVELAQLEYL LPRLRGWGGN LSRQVGGRAA GGVGIGGRGP GETKIELDRR RIRARMAKLR RQIAEMAKTR ETMRSNRRRN RIPSVAIAGY TNAGKSSLLN RLTGAGVLVE DALFATLDPT VRRAQTPSGR PFTLADTVGF VRHLPHQLVE AFRSTLEEVT QADLILHVVD GSDAEPEAQI DAVRQVLREI GADRVPELVV INKADAADPL TLARLRRREP GSVVVSARTG AGIEELMAAI EAELPEVGRE VRVVLPYERG DLVARIHELG EVFSQEHTAE GTRLHARVPA ALAAELDRYV TAEAL // ID D1AML8_SEBTE Unreviewed; 419 AA. AC D1AML8; DT 19-JAN-2010, integrated into UniProtKB/TrEMBL. DT 19-JAN-2010, sequence version 1. DT 07-JUN-2017, entry version 54. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Sterm_2747 {ECO:0000313|EMBL:ACZ09592.1}; OS Sebaldella termitidis (strain ATCC 33386 / NCTC 11300). OC Bacteria; Fusobacteria; Fusobacteriales; Leptotrichiaceae; Sebaldella. OX NCBI_TaxID=526218 {ECO:0000313|EMBL:ACZ09592.1, ECO:0000313|Proteomes:UP000000845}; RN [1] {ECO:0000313|Proteomes:UP000000845} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33386 / NCTC 11300 {ECO:0000313|Proteomes:UP000000845}; RG US DOE Joint Genome Institute (JGI-PGF); RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., RA Tice H., Bruce D., Goodwin L., Pitluck S., Kyrpides N., Mavromatis K., RA Ivanova N., Mikhailova N., Sims D., Meincke L., Brettin T., RA Detter J.C., Han C., Larimer F., Land M., Hauser L., Markowitz V., RA Cheng J.F., Hugenholtz P., Woyke T., Wu D., Eisen J.A.; RT "The complete chromosome of Sebaldella termitidis ATCC 33386."; RL Submitted (SEP-2009) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:ACZ09592.1, ECO:0000313|Proteomes:UP000000845} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33386 / NCTC 11300 {ECO:0000313|Proteomes:UP000000845}; RX PubMed=21304705; RA Harmon-Smith M., Celia L., Chertkov O., Lapidus A., Copeland A., RA Glavina Del Rio T., Nolan M., Lucas S., Tice H., Cheng J.F., Han C., RA Detter J.C., Bruce D., Goodwin L., Pitluck S., Pati A., Liolios K., RA Ivanova N., Mavromatis K., Mikhailova N., Chen A., Palaniappan K., RA Land M., Hauser L., Chang Y.J., Jeffries C.D., Brettin T., Goker M., RA Beck B., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P., RA Kyrpides N.C., Klenk H.P., Chen F.; RT "Complete genome sequence of Sebaldella termitidis type strain (NCTC RT 11300)."; RL Stand. Genomic Sci. 2:220-227(2010). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001739; ACZ09592.1; -; Genomic_DNA. DR RefSeq; WP_012862186.1; NC_013517.1. DR ProteinModelPortal; D1AML8; -. DR STRING; 526218.Sterm_2747; -. DR EnsemblBacteria; ACZ09592; ACZ09592; Sterm_2747. DR KEGG; str:Sterm_2747; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000000845; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000000845}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000000845}. FT DOMAIN 196 364 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 162 189 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 419 AA; 48401 MW; 76657153CD01ED77 CRC64; MTKKAIIVGI KINNQKDFDY MMDELENLVY ANNINVSERL VQNLDKIHAG HYLGSGKIEE LKKIIAETDV DMVIFNDELS PYQIRNLEEF LDIEVIDRTQ LILDIFYKRA KTKEAKLQVE IARLQYELPR MRTSRDEKLD QQSGASGTSN RGAGETKLEI NYRTIKHRIQ LLNKELENVI KERDIQRKQR KKNQISVVSL VGYTNAGKST IMNKFVNKFN KGESKEVFEK DMLFATLETS VRNITLPDRK KFLLTDTVGF VSNLPHHLIK AFRSTLEEVR EADLLIHVVD YSSIHYKNMM QTTDSTLAEV GVKDIPVIYV YNKADLTEKE IPADDGDSIY ISAKNDIGLD LLLEKIYDKI FQDYEKAVFL IPYNKGEIVS HFNENASVLD IKHEENGTKI TAECRKSDIE KYKNYIIND // ID D1B9R2_THEAS Unreviewed; 357 AA. AC D1B9R2; DT 19-JAN-2010, integrated into UniProtKB/TrEMBL. DT 19-JAN-2010, sequence version 1. DT 07-JUN-2017, entry version 63. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Taci_0782 {ECO:0000313|EMBL:ACZ19015.1}; OS Thermanaerovibrio acidaminovorans (strain ATCC 49978 / DSM 6589 / OS Su883) (Selenomonas acidaminovorans). OC Bacteria; Synergistetes; Synergistia; Synergistales; Synergistaceae; OC Thermanaerovibrio. OX NCBI_TaxID=525903 {ECO:0000313|EMBL:ACZ19015.1, ECO:0000313|Proteomes:UP000002030}; RN [1] {ECO:0000313|EMBL:ACZ19015.1, ECO:0000313|Proteomes:UP000002030} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 49978 / DSM 6589 / Su883 RC {ECO:0000313|Proteomes:UP000002030}; RA Chovatia M., Sikorski J., Schroder M., Lapidus A., Nolan M., Tice H., RA Glavina Del Rio T., Copeland A., Cheng J.F., Lucas S., Chen F., RA Bruce D., Goodwin L., Pitluck S., Ivanova N., Mavromatis K., RA Ovchinnikova G., Pati A., Chen A., Palaniappan K., Land M., Hauser L., RA Chang Y.J., Jeffries C.D., Chain P., Saunders E., Detter J.C., RA Brettin T., Rohde M., Goker M., Spring S., Bristow J., Markowitz V., RA Hugenholtz P., Kyrpides N.C., Klenk H.P., Eisen J.A.; RT "Complete genome sequence of Thermanaerovibrio acidaminovorans type RT strain (Su883)."; RL Stand. Genomic Sci. 1:254-261(2009). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001818; ACZ19015.1; -; Genomic_DNA. DR RefSeq; WP_012869530.1; NC_013522.1. DR RefSeq; YP_003317297.1; NC_013522.1. DR ProteinModelPortal; D1B9R2; -. DR STRING; 525903.Taci_0782; -. DR EnsemblBacteria; ACZ19015; ACZ19015; Taci_0782. DR GeneID; 8630601; -. DR KEGG; tai:Taci_0782; -. DR PATRIC; fig|525903.6.peg.783; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000002030; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000002030}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000002030}. FT DOMAIN 190 357 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 149 183 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 357 AA; 39611 MW; 72FD50BD258174AE CRC64; MTDPGAIVLS IDPRDEASIE EVEALLSNLG YRRLKRMVQR RMRPDPASFV GAGFCEAVRE EVRCGGYELV VVDGNLSPTQ RRSLGEALKV EVWDRPYLIM RIFEARAVTA EAKLQVQLAS LRHEIPYLKG LGLQMSRAGG GIGTRGPGET EFERHRRKLE RRARSIEDKL EQLRRRRSSL RQHRRRRALK TVSLVGYTNS GKTTLLSRLS GDRGVVGKDE LFATLDPLVR GVTLPDGKVV LFSDTVGFIR RLPVELVAAF RATLEEVAFA DLVAVVIDGA SKERWEHLKV IGDVLDQIGA GEIPRAILLN KEDLWGSSDE AFEILSEMRG TGLPVFPVSG ITGQGLDSFL GWLQGSL // ID D1BJ28_SANKS Unreviewed; 515 AA. AC D1BJ28; DT 19-JAN-2010, integrated into UniProtKB/TrEMBL. DT 19-JAN-2010, sequence version 1. DT 07-JUN-2017, entry version 63. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Sked_23070 {ECO:0000313|EMBL:ACZ22222.1}; OS Sanguibacter keddieii (strain ATCC 51767 / DSM 10542 / NCFB 3025 / OS ST-74). OC Bacteria; Actinobacteria; Micrococcales; Sanguibacteraceae; OC Sanguibacter. OX NCBI_TaxID=446469 {ECO:0000313|EMBL:ACZ22222.1, ECO:0000313|Proteomes:UP000000322}; RN [1] {ECO:0000313|EMBL:ACZ22222.1, ECO:0000313|Proteomes:UP000000322} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51767 / DSM 10542 / NCFB 3025 / ST-74 RC {ECO:0000313|Proteomes:UP000000322}; RX PubMed=21304646; RA Ivanova N., Sikorski J., Sims D., Brettin T., Detter J.C., Han C., RA Lapidus A., Copeland A., Glavina Del Rio T., Nolan M., Chen F., RA Lucas S., Tice H., Cheng J.F., Bruce D., Goodwin L., Pitluck S., RA Pati A., Mavromatis K., Chen A., Palaniappan K., D'haeseleer P., RA Chain P., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P., RA Goker M., Pukall R., Klenk H.P., Kyrpides N.C.; RT "Complete genome sequence of Sanguibacter keddieii type strain (ST- RT 74)."; RL Stand. Genomic Sci. 1:110-118(2009). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001819; ACZ22222.1; -; Genomic_DNA. DR RefSeq; WP_012867291.1; NC_013521.1. DR ProteinModelPortal; D1BJ28; -. DR STRING; 446469.Sked_23070; -. DR EnsemblBacteria; ACZ22222; ACZ22222; Sked_23070. DR KEGG; ske:Sked_23070; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000000322; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 2. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000000322}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000000322}. FT DOMAIN 294 459 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 515 AA; 55008 MW; 1FABFD1118B31D62 CRC64; MTNSHEPRPE PAQGPSPTTV QRASDAAPSA RDIAGDVVAR VLARAGTARA EGSTQHSSHD GDQLDLAERS ALRRVANLST ELEDVTEVEY RQLRLERVVL VGLWARDATD AEVSLRELAA LAETAGSQVL DGLLQRRQTP DPGTYLGSGK AAELAAVVAS TGADTVIVDG DLAPSQRRAL EDIIKVKVVD RTALILDIFA QHAKSREGKA QVELAQLEYL LPRLRGWGES MSRQAGGQVG GAGAGMGSRG PGETKIELDR RRIRNRMAKL RREIAAMAPS RETKRSSRKR NAIPSVAIAG YTNAGKSSLL NALTGAGVLV ENALFATLDP TVRRTKTPDG RVYTLADTVG FVRSLPHQLV EAFRSTLEEV ADSDLLLHVV DASHPDPEGQ IAAVRHVLEG IPGALDVPEV IVLNKADLAD PDTIARLRSR ERTTLVVSAH TGEGITELLD LISGALPHPG VTVDLIVPYS RGDLVNRVHL EGEIDHLEHV GEGTLLRGRV DDELAAELAA VAVRG // ID D1C097_XYLCX Unreviewed; 515 AA. AC D1C097; DT 19-JAN-2010, integrated into UniProtKB/TrEMBL. DT 19-JAN-2010, sequence version 1. DT 07-JUN-2017, entry version 53. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Xcel_1255 {ECO:0000313|EMBL:ACZ30286.1}; OS Xylanimonas cellulosilytica (strain DSM 15894 / CECT 5975 / LMG 20990 OS / XIL07). OC Bacteria; Actinobacteria; Micrococcales; Promicromonosporaceae; OC Xylanimonas. OX NCBI_TaxID=446471 {ECO:0000313|EMBL:ACZ30286.1, ECO:0000313|Proteomes:UP000002255}; RN [1] {ECO:0000313|Proteomes:UP000002255} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 15894 / CECT 5975 / LMG 20990 / XIL07 RC {ECO:0000313|Proteomes:UP000002255}; RG US DOE Joint Genome Institute (JGI-PGF); RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., RA Tice H., Bruce D., Goodwin L., Pitluck S., Kyrpides N., Mavromatis K., RA Ivanova N., Mikhailova N., Foster B., Clum A., Brettin T., RA Detter J.C., Han C., Larimer F., Land M., Hauser L., Markowitz V., RA Cheng J.F., Hugenholtz P., Woyke T., Wu D., Gehrich-Schroeter G., RA Schneider S., Pukall S.R., Klenk H.P., Eisen J.A.; RT "The complete chromosome of Xylanimonas cellulosilytica DSM 15894."; RL Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:ACZ30286.1, ECO:0000313|Proteomes:UP000002255} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 15894 / CECT 5975 / LMG 20990 / XIL07 RC {ECO:0000313|Proteomes:UP000002255}; RX PubMed=21304672; DOI=10.4056/sigs.571102; RA Foster B., Pukall R., Abt B., Nolan M., Glavina Del Rio T., Chen F., RA Lucas S., Tice H., Pitluck S., Cheng J.-F., Chertkov O., Brettin T., RA Han C., Detter J.C., Bruce D., Goodwin L., Ivanova N., Mavromatis K., RA Pati A., Mikhailova N., Chen A., Palaniappan K., Land M., Hauser L., RA Chang Y.-J., Jeffries C.D., Chain P., Rohde M., Goeker M., Bristow J., RA Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.-P., RA Lapidus A.; RT "Complete genome sequence of Xylanimonas cellulosilytica type strain RT (XIL07)."; RL Stand. Genomic Sci. 2:1-8(2010). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001821; ACZ30286.1; -; Genomic_DNA. DR RefSeq; WP_012878028.1; NC_013530.1. DR ProteinModelPortal; D1C097; -. DR STRING; 446471.Xcel_1255; -. DR EnsemblBacteria; ACZ30286; ACZ30286; Xcel_1255. DR KEGG; xce:Xcel_1255; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000002255; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 2. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000002255}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000002255}. FT DOMAIN 296 462 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 515 AA; 55517 MW; D318252C882F8CCE CRC64; MTHAPQDPTA PDTEHTDDTD GTVDAGRAAQ AIANDVVARV LARAGTARAE GTTVHVAHDG EQLDLEERTA LRRVAGLSTE LDDVTEVEYR QLRLEKVVLI GQYSGGEAAA AEAGVSLREL AALAETAGSE VLDGLLQRRQ KPDPGTYLGS GKAAELAELV RDVGADTVVA DTELAPSQRR ALEDIVKVKV IDRTALILDI FAQHAKSREG KAQVELAQLE YLLPRLRGWG DSMSRQAGGQ VGGQGAGMGS RGPGETKIEL DRRRIRNRMA KLRREIKEMA PARATKRVER KRHAIPNVAI AGYTNAGKSS LLNALTDAGV LVENALFATL DPTVRRATTD DGRVYTLADT VGFVRHLPHQ LVEAFRSTLE EVGDAALLLH VVDASHPDPE GQIAAVREVL AEIPGIDAVR EVVVLNKADV ADPEVIGRIQ RREKRTVVVS AHTGEGIAEL RHLIADELPR PEVAIDLVVP YSRGDLVNRV HQFGELDHEE HLATGTLLRG RVDEALAAEL QRAAV // ID D1C432_SPHTD Unreviewed; 433 AA. AC D1C432; DT 19-JAN-2010, integrated into UniProtKB/TrEMBL. DT 19-JAN-2010, sequence version 1. DT 07-JUN-2017, entry version 61. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Sthe_1564 {ECO:0000313|EMBL:ACZ38999.1}; OS Sphaerobacter thermophilus (strain DSM 20745 / S 6022). OC Bacteria; Chloroflexi; Sphaerobacteridae; Sphaerobacterales; OC Sphaerobacterineae; Sphaerobacteraceae; Sphaerobacter. OX NCBI_TaxID=479434 {ECO:0000313|EMBL:ACZ38999.1, ECO:0000313|Proteomes:UP000002027}; RN [1] {ECO:0000313|Proteomes:UP000002027} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 20745 / S 6022 {ECO:0000313|Proteomes:UP000002027}; RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., RA Tice H., Bruce D., Goodwin L., Pitluck S., Kyrpides N., Mavromatis K., RA Ivanova N., Mikhailova N., LaButti K.M., Clum A., Sun H.I., RA Brettin T., Detter J.C., Han C., Larimer F., Land M., Hauser L., RA Markowitz V., Cheng J.F., Hugenholtz P., Woyke T., Wu D., RA Steenblock K., Schneider S., Pukall R., Goeker M., Klenk H.P., RA Eisen J.A.; RT "The complete chromosome 1 of Sphaerobacter thermophilus DSM 20745."; RL Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:ACZ38999.1, ECO:0000313|Proteomes:UP000002027} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 20745 / S 6022 {ECO:0000313|Proteomes:UP000002027}; RX PubMed=21304676; RA Spring S., Nolan M., Lapidus A., Glavina Del Rio T., Copeland A., RA Tice H., Cheng J.F., Lucas S., Land M., Chen F., Bruce D., Goodwin L., RA Pitluck S., Ivanova N., Mavromatis K., Mikhailova N., Pati A., RA Chen A., Palaniappan K., Hauser L., Chang Y.J., Jeffries C.D., RA Munk C., Kiss H., Chain P., Han C., Brettin T., Detter J.C., RA Schuler E., Goker M., Rohde M., Bristow J., Eisen J.A., Markowitz V., RA Hugenholtz P., Kyrpides N.C., Klenk H.P.; RT "Complete genome sequence of Desulfohalobium retbaense type strain RT (HR(100))."; RL Stand. Genomic Sci. 2:38-48(2010). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001823; ACZ38999.1; -; Genomic_DNA. DR RefSeq; WP_012872046.1; NC_013523.1. DR ProteinModelPortal; D1C432; -. DR STRING; 479434.Sthe_1564; -. DR EnsemblBacteria; ACZ38999; ACZ38999; Sthe_1564. DR KEGG; sti:Sthe_1564; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000002027; Chromosome 1. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000002027}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000002027}. FT DOMAIN 204 373 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 433 AA; 48262 MW; EF1666C3EC282295 CRC64; MGRRLQTNPT AERALLVAVD WRNDGWDLES SLTELAHLAE TDGLVVVGSV TQRLPKPNMT HYVGSGKLEE IRALKDTLHY DVVLVNDELS PGQLRHLEDA LDAKVIDRTA LILDIFARRA QTHEGRLQVE LAQLEYRLPR LTRMWTHLSR QAVGGVGLRG PGETQLEVDR RQARRRIALI KSQLQEVHRH RELYRNRRRR QNIPVIALVG YTNAGKSTLL NRLTDAGVLA EDKLFATLDP TTRRVTLPSG RTVLMTDTVG FIHNLPTFLV AAFRATLEEI LEASVIVHVM DVTHPKAAEQ AETVRTVLED LGADSRPKVT ALNKIDRLGD GLTPDQIAAD LNLPPTYVPI SAATGAGVDL LLQRVEEILT EQQRLVPVRV VVPYSEAGLV DLFHRAGKVD SERFGEHGTL LAGHLPVDLL PRFEPYRETA GTR // ID D1CBZ9_THET1 Unreviewed; 441 AA. AC D1CBZ9; DT 19-JAN-2010, integrated into UniProtKB/TrEMBL. DT 19-JAN-2010, sequence version 1. DT 07-JUN-2017, entry version 61. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Tter_1408 {ECO:0000313|EMBL:ACZ42314.1}; OS Thermobaculum terrenum (strain ATCC BAA-798 / YNP1). OC Bacteria; Thermobaculum. OX NCBI_TaxID=525904 {ECO:0000313|EMBL:ACZ42314.1, ECO:0000313|Proteomes:UP000000323}; RN [1] {ECO:0000313|Proteomes:UP000000323} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-798 / YNP1 {ECO:0000313|Proteomes:UP000000323}; RX DOI=10.4056/sigs.1153107; RA Kiss H., Cleland D., Lapidus A., Lucas S., Glavina Del Rio T., RA Nolan M., Tice H., Han C., Goodwin L., Pitluck S., Liolios K., RA Ivanova N., Mavromatis K., Ovchinnikova G., Pati A., Chen A., RA Palaniappan K., Land M., Hauser L., Chang Y., Jeffries C., Lu M., RA Brettin T., Detter J., Goker M., Tindall B., Beck B., McDermott T., RA Woyke T., Bristow J., Eisen J., Markowitz V., Hugenholtz P., RA Kyrpides N., Klenk H., Cheng J.; RT "Complete genome sequence of Thermobaculum terrenum type strain RT (YNP1T)."; RL Stand. Genomic Sci. 3:153-162(2010). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001825; ACZ42314.1; -; Genomic_DNA. DR ProteinModelPortal; D1CBZ9; -. DR STRING; 525904.Tter_1408; -. DR EnsemblBacteria; ACZ42314; ACZ42314; Tter_1408. DR KEGG; ttr:Tter_1408; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000000323; Chromosome 1. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000000323}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000000323}. FT DOMAIN 213 381 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 441 AA; 49143 MW; 679746156BBE3E1A CRC64; MQDTIDRVGP IKPVSTAQPE ELAILVGVQT PDSKWDVNSS LDELERLADT ADVKVVGRIT QRLAAPDPRT FIGKGKLREL ADMKNATGAT VVLFDDELSP SQERNLEDEL KCKIIDRSAL ILDIFARRAR TKEGRLQVEL AQLEYRLPRL TRMWTHLSRQ GVGGVGLRGP GETQLEVDRR QSRERITHIK REIEQVRKHR KILREHRKAE GLPVVSLVGY TNAGKSTLLN KLAGADVLAE DKLFATLDPT TRQVRLPAGM LSLWTDTVGF IQKLPTDLVA AFRATLEEIL EADVLVHVVD ITHENAEEQA ATVNETLRSL GAADKPTVVA LNKVDKLAPD LDSGLPSLED LPDNYVLISA ELGWGIDTLL SKVEQVLESN LRELDVLLPY SEGALVDLFH KYGQVRTEEF THAGTHIRGK LPEKYVSLMR RYETAESRSG D // ID D1KAU6_9GAMM Unreviewed; 438 AA. AC D1KAU6; DT 19-JAN-2010, integrated into UniProtKB/TrEMBL. DT 19-JAN-2010, sequence version 1. DT 07-JUN-2017, entry version 45. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=Sup05_0718 {ECO:0000313|EMBL:EEZ80744.1}; OS uncultured SUP05 cluster bacterium. OC Bacteria; Proteobacteria; Gammaproteobacteria; Candidatus Thioglobus; OC environmental samples. OX NCBI_TaxID=655186 {ECO:0000313|EMBL:EEZ80744.1, ECO:0000313|Proteomes:UP000009383}; RN [1] {ECO:0000313|EMBL:EEZ80744.1, ECO:0000313|Proteomes:UP000009383} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=19900896; DOI=10.1126/science.1175309; RA Walsh D.A., Zaikova E., Howes C.L., Song Y.C., Wright J.J., RA Tringe S.G., Tortell P.D., Hallam S.J.; RT "Metagenome of a versatile chemolithoautotroph from expanding oceanic RT dead zones."; RL Science 326:578-582(2009). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GG729960; EEZ80744.1; -; Genomic_DNA. DR ProteinModelPortal; D1KAU6; -. DR PATRIC; fig|655186.3.peg.1351; -. DR Proteomes; UP000009383; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000009383}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000009383}. FT DOMAIN 205 372 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 438 AA; 49766 MW; D1F59A82C390FB99 CRC64; MELFDRQKDS VGQGEKTLLV YVELPSNRHI HNGLDEFLEL ANSSGLDVVQ ALKVNRNTAT AQYFIGSGKV DEIAELVKEH EIDLVIFAPE LTPSQERNLE KKLNCQVMDR TGLILDIFAL RAQSFEGKLQ VELAQLRHLS TRLVRGWTHL ERQKGGIGLR GPGETQLETD KRLIAVRIKN ITKRLDKVHK QRDLGRKSRV KSELPMIALA GYTNAGKSTL FNALTKAEVF ADDRLFATLD STIRRVILPA SGEAVIADTV GFIQDLPHEL VAAFKSTLEE TRRANVLLHV VDASDEYNLE KIDQVEDIIN EIDANKIPSI LVMNKIDRLE NFKPRIDRDK DGRIYRVWIS AQNGDGIDLL YQTLAEQLSG MMTRAKIQLD VNAAYIRSEI HNIGYIHNEK VDDFGQWILE INVTNHYLSK LLHKQGVKLL WEQKPQQR // ID D1NSV0_9BIFI Unreviewed; 523 AA. AC D1NSV0; DT 09-FEB-2010, integrated into UniProtKB/TrEMBL. DT 09-FEB-2010, sequence version 1. DT 07-JUN-2017, entry version 52. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:EFA23752.1}; GN ORFNames=BGLCM_0824 {ECO:0000313|EMBL:KFI59231.1}, GN BIFGAL_02860 {ECO:0000313|EMBL:EFA23752.1}; OS Bifidobacterium gallicum DSM 20093 = LMG 11596. OC Bacteria; Actinobacteria; Bifidobacteriales; Bifidobacteriaceae; OC Bifidobacterium. OX NCBI_TaxID=561180 {ECO:0000313|EMBL:EFA23752.1, ECO:0000313|Proteomes:UP000003656}; RN [1] {ECO:0000313|EMBL:EFA23752.1, ECO:0000313|Proteomes:UP000003656} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 20093 {ECO:0000313|EMBL:EFA23752.1, RC ECO:0000313|Proteomes:UP000003656}; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Nelson J., Hou S., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Nash W.E., Warren W., Chinwalla A., Mardis E.R., RA Wilson R.K.; RL Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:KFI59231.1, ECO:0000313|Proteomes:UP000029074} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=LMG 11596 {ECO:0000313|EMBL:KFI59231.1, RC ECO:0000313|Proteomes:UP000029074}; RA Ventura M., Milani C., Lugli G.A.; RT "Genomics of Bifidobacteria."; RL Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EFA23752.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABXB03000001; EFA23752.1; -; Genomic_DNA. DR EMBL; JGYW01000004; KFI59231.1; -; Genomic_DNA. DR STRING; 561180.BIFGAL_02860; -. DR EnsemblBacteria; EFA23752; EFA23752; BIFGAL_02860. DR EnsemblBacteria; KFI59231; KFI59231; BGLCM_0824. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000003656; Unassembled WGS sequence. DR Proteomes; UP000029074; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000003656}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000003656}. FT DOMAIN 292 458 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 523 AA; 57525 MW; E61DEAD34E7805F9 CRC64; MPEQEEVSAT QDHNVQPTSQ RQETERDEPG TGVLGERSDV LLDQHERTDV YAERDDELWR ERESRNQLKH VTGLGELHDV TEVEYRKIRL ERVVLVGVWS SRDTTLTQAE ESLRELAALA ETAGAQVVDG VLQHRSRPDS ATYVGSGKAK EIADIVAVNE ADTIIVDADL PPSQRRALED VTRVKVVDRT AVILDIFAQH AQSREGKAQV ELAQLQYMLP RLRGWGAALS RQAGGRAAGA DAGIGSRGPG ETKIEMDRRV IRTRIARLRK QIAQMAPSRQ VKRGSRRRTG LPTVAVVGYT NAGKSSLTNR LTGSSELVEN ALFATLDTAV RRAQSADGRR YAYVDTVGFV RRLPTQLVEA FKSTLEEVGE ADLIVHVVDS SHPDPFSQID AVNDVLKDID GVGEIPTLTV FNKADLIDNA KRERIASLMP DAFIVSSASG EGIDTLRESV EGLLPRPDVQ VEALLPYTAG SLINRIREFG ELTALDYRDT GIAVIARVDD RLAARIMDEA LPDEPDNRAL EGE // ID D1PR59_9FIRM Unreviewed; 427 AA. AC D1PR59; DT 09-FEB-2010, integrated into UniProtKB/TrEMBL. DT 09-FEB-2010, sequence version 1. DT 12-APR-2017, entry version 39. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:EFB74906.1}; GN ORFNames=SUBVAR_06887 {ECO:0000313|EMBL:EFB74906.1}; OS Subdoligranulum variabile DSM 15176. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Ruminococcaceae; OC Subdoligranulum. OX NCBI_TaxID=411471 {ECO:0000313|EMBL:EFB74906.1, ECO:0000313|Proteomes:UP000003438}; RN [1] {ECO:0000313|EMBL:EFB74906.1, ECO:0000313|Proteomes:UP000003438} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 15176 {ECO:0000313|EMBL:EFB74906.1, RC ECO:0000313|Proteomes:UP000003438}; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Nelson J., Hou S., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Nash W.E., Warren W., Chinwalla A., Mardis E.R., RA Wilson R.K.; RL Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EFB74906.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACBY02000054; EFB74906.1; -; Genomic_DNA. DR ProteinModelPortal; D1PR59; -. DR STRING; 411471.SUBVAR_06887; -. DR EnsemblBacteria; EFB74906; EFB74906; SUBVAR_06887. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000003438; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000003438}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000003438}. FT DOMAIN 215 374 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 181 208 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 427 AA; 46652 MW; 067B18947D93239F CRC64; MSEITLDFGT TAQKQTQGEA IPVVLLALDQ GRYDMARSLD ELRALADANG MEAVAEVVQK RSVPEAATML GEGKVAEARL VCQNLDARAA IFDGELTGSQ IRNLSAALQV EVLDRTMLIL EIFRARATTN EGKLQTELAT LRYQLPRLQG LGESLSRQGG GGGGGAGARR GAGETKLELD RRHLHQRIEH LEGKLREMEK RRGETRRARQ KNNVPVVALV GYTNVGKSSL LNALCGEQIF EADMLFATLD PTARKLTLPS GLQVILVDTV GFVSRLPHHL VEAFKSTLEE AAFADVILKV ADASDPQAAE QLAVTDEVLG TLDCGDIPQL VVYNKCDAAN LTAFDPAMLL TSAKTGRGLP ELLARLDEEL AHRVRTIEVV LPYDKLALAD ILRSRGSVAE EEYREDGVYY RGTVKIDDLH RFEPYLV // ID D1PYX6_9BACT Unreviewed; 411 AA. AC D1PYX6; DT 09-FEB-2010, integrated into UniProtKB/TrEMBL. DT 09-FEB-2010, sequence version 1. DT 07-JUN-2017, entry version 40. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:EFA43392.1}; GN ORFNames=HMPREF0645_2161 {ECO:0000313|EMBL:EFA43392.1}; OS Prevotella bergensis DSM 17361. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Prevotellaceae; OC Prevotella. OX NCBI_TaxID=585502 {ECO:0000313|EMBL:EFA43392.1, ECO:0000313|Proteomes:UP000003160}; RN [1] {ECO:0000313|EMBL:EFA43392.1, ECO:0000313|Proteomes:UP000003160} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 17361 {ECO:0000313|EMBL:EFA43392.1, RC ECO:0000313|Proteomes:UP000003160}; RA Qin X., Bachman B., Battles P., Bell A., Bess C., Bickham C., RA Chaboub L., Chen D., Coyle M., Deiros D.R., Dinh H., Forbes L., RA Fowler G., Francisco L., Fu Q., Gubbala S., Hale W., Han Y., RA Hemphill L., Highlander S.K., Hirani K., Hogues M., Jackson L., RA Jakkamsetti A., Javaid M., Jiang H., Korchina V., Kovar C., Lara F., RA Lee S., Mata R., Mathew T., Moen C., Morales K., Munidasa M., RA Nazareth L., Ngo R., Nguyen L., Okwuonu G., Ongeri F., Patil S., RA Petrosino J., Pham C., Pham P., Pu L.-L., Puazo M., Raj R., Reid J., RA Rouhana J., Saada N., Shang Y., Simmons D., Thornton R., Warren J., RA Weissenberger G., Zhang J., Zhang L., Zhou C., Zhu D., Muzny D., RA Worley K., Gibbs R.; RL Submitted (OCT-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EFA43392.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACKS01000081; EFA43392.1; -; Genomic_DNA. DR RefSeq; WP_007174264.1; NZ_GG704781.1. DR ProteinModelPortal; D1PYX6; -. DR STRING; 585502.HMPREF0645_2161; -. DR EnsemblBacteria; EFA43392; EFA43392; HMPREF0645_2161. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000003160; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000003160}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000003160}. FT DOMAIN 212 396 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 411 AA; 47008 MW; 77797CD0F28FF3DC CRC64; MKEFVISEAK AETAVLVGLV TPQQNEARTK EYLDELEFLA DTAGAVTVKR FTQKVGGVNQ TTYVGKGKLA EIKQYIQEEE DNEREVGMVI FDDELSARQL RNIEAELKVK ILDRTSLILD IFAMRAQTAN AKTQVELAQY RYMLPRLQRL WTHLERQGGG SGNGSVGLRG PGETQLEMDR RIILQRITLL KQRLVDIDKQ KATQRKNRGR LIRVALVGYT NVGKSTIMNL LSKSDVFAEN KLFATLDTTV RKVVIGNLPF LLADTVGFIR KLPTDLVDSF KSTLDEVREA DLLLHVVDIS HPDFEEQISV VNETLKDLGC SDKPQIVVFN KTDNYQWVEK EPDDLTPETK ENLSLDDLQK TWMAKLDENC LFISAKNKDN IDEFRNTLYR QVRMLHVQKY PYNDFLYPMV D // ID D1VRR0_9FIRM Unreviewed; 422 AA. AC D1VRR0; DT 09-FEB-2010, integrated into UniProtKB/TrEMBL. DT 09-FEB-2010, sequence version 1. DT 07-JUN-2017, entry version 41. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:EFA90766.1}; GN ORFNames=HMPREF0628_0353 {ECO:0000313|EMBL:EFA90766.1}; OS Peptoniphilus lacrimalis 315-B. OC Bacteria; Firmicutes; Tissierellia; Tissierellales; Peptoniphilaceae; OC Peptoniphilus. OX NCBI_TaxID=596330 {ECO:0000313|EMBL:EFA90766.1, ECO:0000313|Proteomes:UP000005711}; RN [1] {ECO:0000313|EMBL:EFA90766.1, ECO:0000313|Proteomes:UP000005711} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=315-B {ECO:0000313|EMBL:EFA90766.1, RC ECO:0000313|Proteomes:UP000005711}; RA Durkin A.S., Madupu R., Torralba M., Methe B., Sutton G., RA Strausberg R.L., Nelson K.E.; RT "Genome Sequence of Peptoniphilus lacrimalis 315-B."; RL Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EFA90766.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADDO01000009; EFA90766.1; -; Genomic_DNA. DR RefSeq; WP_004823794.1; NZ_ADDO01000009.1. DR ProteinModelPortal; D1VRR0; -. DR STRING; 596330.HMPREF0628_0353; -. DR EnsemblBacteria; EFA90766; EFA90766; HMPREF0628_0353. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000005711; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000005711}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000005711}. FT DOMAIN 200 368 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 159 193 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 422 AA; 48174 MW; 255761EC6316C2BA CRC64; MEDVSSKKIE RVITVGTDIG AYPNSLETSM KELDELCYAD GAEVIGQMTQ NLEKFNPKYL IGKGKVKEIK EMAENLEADA IVFNDELTGI QLRNLEDTIK KKVVDRTNLI LDIFALRAST YEGKLQVELA QLEYQLPRLL GIKGWSRTGG GIGTRGPGEQ IIETDRRRLL REIDKIKEKL NKAKKTRDTT RSKRMNSKIP TVSLVGYTNA GKSTILNRIK EDDSKEVFVK DMLFATLDPN SRKARLLSGR EFIISDTVGF VSKLPTKLIE AFKSTLEEIK YSDLIVHVID ASSKDLEIAY DTTMNILQEI GIKDKKILTV FNKSDKIDLN STTIPLKIKS QKIYISAKND PDMNKLLKAI EENLPEEYIY TKLNFPYDDT DILYKLIERF DLKPIYKENF IEIELSLSKK EYSKLKRYVA NV // ID D1VYA0_9BACT Unreviewed; 415 AA. AC D1VYA0; DT 09-FEB-2010, integrated into UniProtKB/TrEMBL. DT 09-FEB-2010, sequence version 1. DT 07-JUN-2017, entry version 40. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:EFA97903.1}; GN ORFNames=HMPREF9019_1145 {ECO:0000313|EMBL:EFA97903.1}; OS Prevotella timonensis CRIS 5C-B1. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Prevotellaceae; OC Prevotella. OX NCBI_TaxID=679189 {ECO:0000313|EMBL:EFA97903.1, ECO:0000313|Proteomes:UP000004001}; RN [1] {ECO:0000313|EMBL:EFA97903.1, ECO:0000313|Proteomes:UP000004001} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CRIS 5C-B1 {ECO:0000313|EMBL:EFA97903.1, RC ECO:0000313|Proteomes:UP000004001}; RA Durkin A.S., Madupu R., Torralba M., Methe B., Sutton G., RA Strausberg R.L., Nelson K.E.; RT "Genome Sequence of Prevotella timonensis CRIS 5C-B1."; RL Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EFA97903.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADEF01000019; EFA97903.1; -; Genomic_DNA. DR RefSeq; WP_008123148.1; NZ_ADEF01000019.1. DR ProteinModelPortal; D1VYA0; -. DR STRING; 679189.HMPREF9019_1145; -. DR EnsemblBacteria; EFA97903; EFA97903; HMPREF9019_1145. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000004001; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000004001}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000004001}. FT DOMAIN 216 400 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 415 AA; 47273 MW; F20B2E6AB3751AE7 CRC64; MKEFVISEAK SETAVLVGIV TQEQNEAKTN EYLDELEFLA DTAGAETVKR FTQKAGGPNA VTYVGKGKLE EIKQYIDEEA ENERPVGMVI FDDELSAKQI RNIEKALDVK ILDRTSLILD IFAMRAQTAN AKTQVELAQY RYMLPRLQRL WTHLERQGGG SGSGGGKGSV GLRGPGETQL EMDRRIILQR ITLLKQRLEQ IDKQKTTQRK NRGRMIRVAL VGYTNVGKST LMNLLSKSEV FAENKLFATL DTTVRKVVVE NLPFLLADTV GFIRKLPTDL VDSFKSTLDE VREADLLLHV VDISHPDFEE QIHVVENTLK ELGCAEKPSM IIFNKIDNYT WVPKDADDLT PSTAENITLD ELKQTWMARL NDQCLFISAK KKLNIDEFKE VLYQQVRRLH VQKYPYNDFL YPIEE // ID D1Y146_9BACT Unreviewed; 358 AA. AC D1Y146; DT 09-FEB-2010, integrated into UniProtKB/TrEMBL. DT 09-FEB-2010, sequence version 1. DT 07-JUN-2017, entry version 47. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:EFB91974.1}; GN ORFNames=HMPREF7215_0431 {ECO:0000313|EMBL:EFB91974.1}; OS Pyramidobacter piscolens W5455. OC Bacteria; Synergistetes; Synergistia; Synergistales; Synergistaceae; OC Pyramidobacter. OX NCBI_TaxID=352165 {ECO:0000313|EMBL:EFB91974.1, ECO:0000313|Proteomes:UP000006462}; RN [1] {ECO:0000313|EMBL:EFB91974.1, ECO:0000313|Proteomes:UP000006462} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=W5455 {ECO:0000313|EMBL:EFB91974.1, RC ECO:0000313|Proteomes:UP000006462}; RA Shrivastava S., Madupu R., Durkin A.S., Torralba M., Methe B., RA Sutton G.G., Strausberg R.L., Nelson K.E.; RL Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EFB91974.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADFP01000009; EFB91974.1; -; Genomic_DNA. DR RefSeq; WP_009163578.1; NZ_ADFP01000009.1. DR ProteinModelPortal; D1Y146; -. DR STRING; 352165.HMPREF7215_0431; -. DR EnsemblBacteria; EFB91974; EFB91974; HMPREF7215_0431. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000006462; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000006462}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000006462}. FT DOMAIN 188 358 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 154 181 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 358 AA; 40005 MW; 1A29F29874AA2348 CRC64; MITGLELPLR DDLELLLEEL RLLLANLDVE VVAVATQKKD RPDPAFLLGA GKADELKILA QASEADLVVC NDLLTPIQLS NMRRKTDCEV WDRALVIMKI FERRAATAEA KLQVELARCR YEMPHIRGLG KQMSNAGAGI GTRGPGETEF ERHRRKLQAR IVEASRKLEE MKKRRQGQRK QRRRSGVPTV ALVGYTNSGK TTLLKRLSGD KKLYAADQLF ATLDTTVRSV RLPSGRNILM ADTVGFIREL PPELIAAFRT TLEEACQADM LLVVLDANDP DLTATYDVIQ QTLDEIGAAT LPRAIVLNKI DRSGLFRVER IRAQLRRDGL PVCALSALTG EGVESLWEVF DWLAVRRS // ID D1Z209_METPS Unreviewed; 420 AA. AC D1Z209; DT 09-FEB-2010, integrated into UniProtKB/TrEMBL. DT 09-FEB-2010, sequence version 1. DT 07-JUN-2017, entry version 59. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=MCP_2659 {ECO:0000313|EMBL:BAI62731.1}; OS Methanocella paludicola (strain DSM 17711 / JCM 13418 / NBRC 101707 / OS SANAE). OC Archaea; Euryarchaeota; Methanomicrobia; Methanocellales; OC Methanocellaceae; Methanocella. OX NCBI_TaxID=304371 {ECO:0000313|EMBL:BAI62731.1, ECO:0000313|Proteomes:UP000001882}; RN [1] {ECO:0000313|Proteomes:UP000001882} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 17711 / JCM 13418 / NBRC 101707 / SANAE RC {ECO:0000313|Proteomes:UP000001882}; RX PubMed=21829548; DOI=10.1371/journal.pone.0022898; RA Sakai S., Takaki Y., Shimamura S., Sekine M., Tajima T., Kosugi H., RA Ichikawa N., Tasumi E., Hiraki A.T., Shimizu A., Kato Y., Nishiko R., RA Mori K., Fujita N., Imachi H., Takai K.; RT "Genome sequence of a mesophilic hydrogenotrophic methanogen RT Methanocella paludicola, the first cultivated representative of the RT order Methanocellales."; RL PLoS ONE 6:E22898-E22898(2011). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AP011532; BAI62731.1; -; Genomic_DNA. DR ProteinModelPortal; D1Z209; -. DR STRING; 304371.MCP_2659; -. DR EnsemblBacteria; BAI62731; BAI62731; MCP_2659. DR KEGG; mpd:MCP_2659; -. DR PATRIC; fig|304371.9.peg.2720; -. DR eggNOG; arCOG00353; Archaea. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG093Z07D6; -. DR Proteomes; UP000001882; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000001882}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000001882}. FT DOMAIN 191 360 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 420 AA; 46997 MW; A729AF0873E40E4F CRC64; MNSDVKGVLL VKRIQPGTDG SLEELEELSH SAGYEVLGEV TQVRTPDKAF AVGRGKAEEI AALVQELKPE KVVFDEKLNA VQIYNLSKLC RVEVIDRFNL ILEIFASRAR TREAKLQVEL ASLIYERPKA RMKVTLAKRG EQPGFKGLGR YQADIYESEI TGRIAKIEAE LDVIRKRQHE TRKQRKEKGF DLVALAGYTN AGKSTLMNAL VGETVVAKDQ LFTTLVPTTR SLQIGQRKTL LTDTVGFIKN LPHFMVEAFR STLEEIYLAD VIILVVDVSE PPEALVDKLV TCHDTMWDEI GPVPVITALN KSDLITEEEL EERKQAIVHL APHPVVISAR TGEGLDELKQ KIGKYLPKWT SSEVVLPRTV EGLSMLSQLY DEAIVHHVDY SDSTIKVNLE ARESVLRRLG KRLDSPAINP // ID D2AZK0_STRRD Unreviewed; 494 AA. AC D2AZK0; DT 09-FEB-2010, integrated into UniProtKB/TrEMBL. DT 09-FEB-2010, sequence version 1. DT 07-JUN-2017, entry version 63. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Sros_2263 {ECO:0000313|EMBL:ACZ85245.1}; OS Streptosporangium roseum (strain ATCC 12428 / DSM 43021 / JCM 3005 / OS NI 9100). OC Bacteria; Actinobacteria; Streptosporangiales; Streptosporangiaceae; OC Streptosporangium. OX NCBI_TaxID=479432 {ECO:0000313|EMBL:ACZ85245.1, ECO:0000313|Proteomes:UP000002029}; RN [1] {ECO:0000313|EMBL:ACZ85245.1, ECO:0000313|Proteomes:UP000002029} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 12428 / DSM 43021 / JCM 3005 / NI 9100 RC {ECO:0000313|Proteomes:UP000002029}; RX PubMed=21304675; DOI=10.4056/sigs.631049; RA Nolan M., Sikorski J., Jando M., Lucas S., Lapidus A., RA Glavina Del Rio T., Chen F., Tice H., Pitluck S., Cheng J.F., RA Chertkov O., Sims D., Meincke L., Brettin T., Han C., Detter J.C., RA Bruce D., Goodwin L., Land M., Hauser L., Chang Y.J., Jeffries C.D., RA Ivanova N., Mavromatis K., Mikhailova N., Chen A., Palaniappan K., RA Chain P., Rohde M., Goker M., Bristow J., Eisen J.A., Markowitz V., RA Hugenholtz P., Kyrpides N.C., Klenk H.P.; RT "Complete genome sequence of Streptosporangium roseum type strain (NI RT 9100)."; RL Stand. Genomic Sci. 2:29-37(2010). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001814; ACZ85245.1; -; Genomic_DNA. DR ProteinModelPortal; D2AZK0; -. DR STRING; 479432.Sros_2263; -. DR EnsemblBacteria; ACZ85245; ACZ85245; Sros_2263. DR KEGG; sro:Sros_2263; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000002029; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 2. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000002029}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000002029}. FT DOMAIN 270 436 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 229 256 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 494 AA; 54336 MW; F420662C4CFDB098 CRC64; MFHSVERTHM NHAPEWSNDI DTREPLDIDQ FDDLPGIGEM DLAERQALRR VAGLSTELED VTEVEYRQLR LERVVLVGVW TSGTAIDAEN SLLELKLLAE TAGSEVLEGV IQRRQKPDTA TYIGSGKAQE LADIVSATGA DTVVCDGELS PGQLRQLEEV VKVKVIDRTM LILDIFAQHA KSREGKAQVE LAQLNYLLPR LRGWGGNLSR QVGGRAAGGV GMGGRGPGET KIELDRRRIR ERMAKLRRQI IEMTTSRVTK RARRQEREVP AVAIAGYTNA GKSSLLNRLT GAGVLVEDSL FATLDPTVRR AHTPEGRLFT LADTVGFVRH LPHQLVEAFR STLEEVGDAD LILHVVDGSH PDPESQLAAV REVVADIEGA RDIPEIVVIN KADVADPVVL AQLTAREKHT VVVSARTGAG IDELLAIIER ELPRFDQEVR LLVPYQRGDL ISRAHKEGEV LGVEHTEDGT ILHARVLPAL FAELEKTAKP VETV // ID D2B5Q2_STRRD Unreviewed; 117 AA. AC D2B5Q2; DT 09-FEB-2010, integrated into UniProtKB/TrEMBL. DT 09-FEB-2010, sequence version 1. DT 07-JUN-2017, entry version 30. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:ACZ91356.1}; GN OrderedLocusNames=Sros_8720 {ECO:0000313|EMBL:ACZ91356.1}; OS Streptosporangium roseum (strain ATCC 12428 / DSM 43021 / JCM 3005 / OS NI 9100). OC Bacteria; Actinobacteria; Streptosporangiales; Streptosporangiaceae; OC Streptosporangium. OX NCBI_TaxID=479432 {ECO:0000313|EMBL:ACZ91356.1, ECO:0000313|Proteomes:UP000002029}; RN [1] {ECO:0000313|EMBL:ACZ91356.1, ECO:0000313|Proteomes:UP000002029} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 12428 / DSM 43021 / JCM 3005 / NI 9100 RC {ECO:0000313|Proteomes:UP000002029}; RX PubMed=21304675; DOI=10.4056/sigs.631049; RA Nolan M., Sikorski J., Jando M., Lucas S., Lapidus A., RA Glavina Del Rio T., Chen F., Tice H., Pitluck S., Cheng J.F., RA Chertkov O., Sims D., Meincke L., Brettin T., Han C., Detter J.C., RA Bruce D., Goodwin L., Land M., Hauser L., Chang Y.J., Jeffries C.D., RA Ivanova N., Mavromatis K., Mikhailova N., Chen A., Palaniappan K., RA Chain P., Rohde M., Goker M., Bristow J., Eisen J.A., Markowitz V., RA Hugenholtz P., Kyrpides N.C., Klenk H.P.; RT "Complete genome sequence of Streptosporangium roseum type strain (NI RT 9100)."; RL Stand. Genomic Sci. 2:29-37(2010). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001814; ACZ91356.1; -; Genomic_DNA. DR RefSeq; WP_012895084.1; NC_013595.1. DR STRING; 479432.Sros_8720; -. DR EnsemblBacteria; ACZ91356; ACZ91356; Sros_8720. DR KEGG; sro:Sros_8720; -. DR eggNOG; ENOG4106YMQ; Bacteria. DR eggNOG; ENOG410YUFX; LUCA. DR OMA; REKRYET; -. DR OrthoDB; POG091H3GO5; -. DR BioCyc; SROS479432:GI0V-8370-MONOMER; -. DR Proteomes; UP000002029; Chromosome. DR InterPro; IPR025121; GTPase_HflX_N. DR Pfam; PF13167; GTP-bdg_N; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000002029}; KW Reference proteome {ECO:0000313|Proteomes:UP000002029}. FT DOMAIN 25 111 GTP-bdg_N. {ECO:0000259|Pfam:PF13167}. SQ SEQUENCE 117 AA; 12372 MW; AEB3BAD5C9DB4C13 CRC64; MGLTGRDVLV VGYFSARQKR YAALMDELAD AVTALGARVV GRSVQRRGVS GGGVKAMDRP YSSRTLVSAG KAREIARARE ESGAGAVVFL NPLTGHQRDV LAEILGCPVL SSIDLRT // ID D2MN89_9FIRM Unreviewed; 412 AA. AC D2MN89; DT 02-MAR-2010, integrated into UniProtKB/TrEMBL. DT 02-MAR-2010, sequence version 1. DT 07-JUN-2017, entry version 29. DE SubName: Full=GTP-binding protein HflX {ECO:0000313|EMBL:EFC05911.1}; GN Name=hflX {ECO:0000313|EMBL:EFC05911.1}; GN ORFNames=HMPREF9013_0110 {ECO:0000313|EMBL:EFC05911.1}; OS Bulleidia extructa W1219. OC Bacteria; Firmicutes; Erysipelotrichia; Erysipelotrichales; OC Erysipelotrichaceae; Bulleidia. OX NCBI_TaxID=679192 {ECO:0000313|EMBL:EFC05911.1, ECO:0000313|Proteomes:UP000005017}; RN [1] {ECO:0000313|Proteomes:UP000005017} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=W1219 {ECO:0000313|Proteomes:UP000005017}; RA Madupu R., Durkin A.S., Torralba M., Methe B., Sutton G.G., RA Strausberg R.L., Nelson K.E.; RT "Sequence of Clostridiales genomosp. BVAB3 str. UPII9-5."; RL Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EFC05911.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADFR01000003; EFC05911.1; -; Genomic_DNA. DR RefSeq; WP_006626860.1; NZ_ADFR01000003.1. DR ProteinModelPortal; D2MN89; -. DR STRING; 679192.HMPREF9013_0110; -. DR EnsemblBacteria; EFC05911; EFC05911; HMPREF9013_0110. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000005017; Unassembled WGS sequence. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR CDD; cd01878; HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 4: Predicted; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000005017}; KW Reference proteome {ECO:0000313|Proteomes:UP000005017}. FT DOMAIN 193 354 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 159 186 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 412 AA; 46716 MW; 01886F9AEEAB034E CRC64; MKRCYVVGVE IKGSSDQEII QECVALCQAC EYEVVKTFIQ KLKSRDPKMV YRSGKIQELK EWLIADEVET VVFYHEISVS ASRRLSEELG VEVLDRTAVI LDIFSQRARS KQSKIQTELA RLSYALPKEL ASLEQESDHQ RGGGTITRGS GEQRSEQIVR KYARRKHVLQ EELKLVEKQR QQDEKRRAKT LYPRVGLVGY TNAGKSSLLN AILAYTRQNG QPVMVRDRVF ETLDTAVRLV EYKGFAFYLY DTVGFVSNLP KTLIDAFFST LESAKQADVL IHVVDGSDPL SFEKQEATKS VLVKIGAHPK QSLLVHTKKD LVSSFEDGLW VSSYTQEGIG ELLDQLIGLL FPKEVQFTCL LPYDKMALFD RLSSLAHLQI VGQEETGLIL KVAGDVDHLR PLKPYEIIRK DI // ID D2NNQ7_ROTMD Unreviewed; 571 AA. AC D2NNQ7; DT 02-MAR-2010, integrated into UniProtKB/TrEMBL. DT 02-MAR-2010, sequence version 1. DT 07-JUN-2017, entry version 61. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=RMDY18_14430 {ECO:0000313|EMBL:BAI65275.1}; OS Rothia mucilaginosa (strain DY-18) (Stomatococcus mucilaginosus). OC Bacteria; Actinobacteria; Micrococcales; Micrococcaceae; Rothia. OX NCBI_TaxID=680646 {ECO:0000313|EMBL:BAI65275.1, ECO:0000313|Proteomes:UP000001883}; RN [1] {ECO:0000313|Proteomes:UP000001883} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DY-18 {ECO:0000313|Proteomes:UP000001883}; RA Yamane K., Nambu T., Mashimo C., Sugimori C., Yamanaka T., Leung K., RA Fukushima H.; RT "Complete genome sequence of Rothia mucilaginosa DJ."; RL Submitted (JUL-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AP011540; BAI65275.1; -; Genomic_DNA. DR RefSeq; WP_012903898.1; NC_013715.1. DR ProteinModelPortal; D2NNQ7; -. DR STRING; 680646.RMDY18_14430; -. DR EnsemblBacteria; BAI65275; BAI65275; RMDY18_14430. DR GeneID; 25056012; -. DR KEGG; rmu:RMDY18_14430; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR Proteomes; UP000001883; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000001883}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000001883}. FT DOMAIN 317 482 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 571 AA; 62582 MW; 572B0456B5EC28BB CRC64; MNSKNTPVSD TEKLPSDEQL RRTVDRVLGR SQAAASVTTY DAAGTAHHSD NSSSTHGSHT SRRVLDTRAR EISDVQREHS EYDGDQEDLA ERRALRRIAN LSTELEDVTE VEYRQLRLER VVLAGLWTEG TVEDAENSLR ELAALAETAG SEVLDGLVQR RLKPDPGTFL GSGKALELKD IVEATGADTV IVDSELAPSQ RRALEDIVKV KVIDRTALIL DIFAQHAKSR EGKAQVELAQ LEYMLPRLRG WGASLSRQAG GRAAAGEGIG SRGPGETKIE MDRRRLRARM AKLKREIAAM APARETKRLN RRRNRVPSVA IAGYTNAGKS SLLNRLTDAG VLVENALFAT LDPTVRKAQT PDGIGYTLSD TVGFVRSLPT QLVEAFRSTL EEVADADVIL HVVDASHPDP EGQIRAVREV IAEVDARHIP EIIVLNKADA ADPFVLERMR QREPEHVIVS ARTGEGIEEL KQKIADTIPR PSIEVKLLIP YSHGEIISRL HEWDAEIKST DFVSDGTFVV ALVREDVASE LSEYVLEGDL LEVLEEELAE AHALAEATAS DSAQSSTAEA L // ID D2PZC0_KRIFD Unreviewed; 496 AA. AC D2PZC0; DT 02-MAR-2010, integrated into UniProtKB/TrEMBL. DT 02-MAR-2010, sequence version 1. DT 07-JUN-2017, entry version 57. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Kfla_4712 {ECO:0000313|EMBL:ADB33729.1}; OS Kribbella flavida (strain DSM 17836 / JCM 10339 / NBRC 14399). OC Bacteria; Actinobacteria; Propionibacteriales; Nocardioidaceae; OC Kribbella. OX NCBI_TaxID=479435 {ECO:0000313|EMBL:ADB33729.1, ECO:0000313|Proteomes:UP000007967}; RN [1] {ECO:0000313|Proteomes:UP000007967} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 17836 / JCM 10339 / NBRC 14399 RC {ECO:0000313|Proteomes:UP000007967}; RG US DOE Joint Genome Institute (JGI-PGF); RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., RA Tice H., Bruce D., Goodwin L., Pitluck S., Kyrpides N., Mavromatis K., RA Ivanova N., Saunders E., Brettin T., Detter J.C., Han C., Larimer F., RA Land M., Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P., RA Woyke T., Wu D., Pukall R., Klenk H.-P., Eisen J.A.; RT "The complete genome of Kribbella flavida DSM 17836."; RL Submitted (SEP-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001736; ADB33729.1; -; Genomic_DNA. DR RefSeq; WP_012922283.1; NC_013729.1. DR ProteinModelPortal; D2PZC0; -. DR STRING; 479435.Kfla_4712; -. DR EnsemblBacteria; ADB33729; ADB33729; Kfla_4712. DR KEGG; kfl:Kfla_4712; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000007967; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 2. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000007967}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000007967}. FT DOMAIN 274 439 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 240 267 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 496 AA; 53614 MW; 249847AC39990738 CRC64; MTTHSNAYEE TEDVDLDLIQ DDALDDEDTS STGYDSELGT EGLELEERQA LRRVVGMSTE LTDISEVEYR KLLLERVLLV GVWTEGSAED AENSLAELKL LAETAGSEVL DGVIQRRKKP DPATFIGSGK VSDLRNLVAS LGADTVIADG ELAPAQLRNL EDKLKVKVVD RTALILDIFA QHAKSKEGKA QVELAQLQYM KQRLRGWGGN LSRQAGGRVG AAGGGIGGRG PGETKIETDR RRINTKISKL RRELKEMKGT RTTMRQERRR HSVPSVAIAG YTNAGKSSLL NAITGAGVLV ENALFATLDP TTRKTTTADG RVYTFTDTVG FVRHLPHDIV EAFRSTLEEV ADADLLLHVV DGSHPDPLAQ IQAVREVLHE IGATDVPEII VINKGDVADP MALAPILHRE TGAIVVSART GEGIDKLRAQ VEAALPQPHI TVDALLPYDR GDLVSRVHSE GSVDTLEHTG DGTRLTARVH PQLAGELAPY QVAAAN // ID D2Q5D8_BIFDB Unreviewed; 482 AA. AC D2Q5D8; DT 02-MAR-2010, integrated into UniProtKB/TrEMBL. DT 02-MAR-2010, sequence version 1. DT 07-JUN-2017, entry version 52. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:ADB10153.1}; GN OrderedLocusNames=BDP_1559 {ECO:0000313|EMBL:ADB10153.1}; OS Bifidobacterium dentium (strain ATCC 27534 / DSM 20436 / JCM 1195 / OS Bd1). OC Bacteria; Actinobacteria; Bifidobacteriales; Bifidobacteriaceae; OC Bifidobacterium. OX NCBI_TaxID=401473 {ECO:0000313|EMBL:ADB10153.1, ECO:0000313|Proteomes:UP000008693}; RN [1] {ECO:0000313|EMBL:ADB10153.1, ECO:0000313|Proteomes:UP000008693} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 27534 / DSM 20436 / JCM 1195 / Bd1 RC {ECO:0000313|Proteomes:UP000008693}; RX PubMed=20041198; DOI=10.1371/journal.pgen.1000785; RA Ventura M., Turroni F., Zomer A., Foroni E., Giubellini V., RA Bottacini F., Canchaya C., Claesson M.J., He F., Mantzourani M., RA Mulas L., Ferrarini A., Gao B., Delledonne M., Henrissat B., RA Coutinho P., Oggioni M., Gupta R.S., Zhang Z., Beighton D., RA Fitzgerald G.F., O'Toole P.W., van Sinderen D.; RT "The Bifidobacterium dentium Bd1 genome sequence reflects its genetic RT adaptation to the human oral cavity."; RL PLoS Genet. 5:E1000785-E1000785(2009). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001750; ADB10153.1; -; Genomic_DNA. DR ProteinModelPortal; D2Q5D8; -. DR STRING; 401473.BDP_1559; -. DR EnsemblBacteria; ADB10153; ADB10153; BDP_1559. DR KEGG; bde:BDP_1559; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR Proteomes; UP000008693; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000008693}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000008693}. FT DOMAIN 262 428 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 482 AA; 52308 MW; C2A7DC4E3AAA5618 CRC64; MGGVLADQSE VLLDTGDGGR FHESHDEQWQ ERESRNALKH VAGLGEKQDV TEVEYRKVRL ERVVLVGVWS SRETTQAAAE ESLRELAALA ETAGAVVCDG LLQHRIKPDA ATYVGSGKAR ELAGIVAQED ADTIVVDDDL PPSQRRALED ATKVKVVDRT AVILDIFAQH ATSREGKAQV ELAQLEYMLP RLRGWGGSLS RQAGGRAAGA DAGIGSRGPG ETKIEMDRRV IRSRIAKLRR QIAEMAPARE VKRGSRRRFG LPTVAVVGYT NAGKSSLTNR LTGSAELVEN ALFATLDTAV RRARAKDGRL YAYVDTVGFV RRLPTQLIEA FKSTLEEVAE ADLIVHVVDG SHPDPFSQID AVNDVLADID GVGAIPTIVA FNKSDLMGEA VRERIEALMP DAYVVSAYSG EGVDELRTGI ESMLPTPNVH VEALLPYSAG SLVSRVREYG KVLAVEYRDD GMMLRAEVDD HLAARIVEQA IA // ID D2QTT0_SPILD Unreviewed; 426 AA. AC D2QTT0; DT 02-MAR-2010, integrated into UniProtKB/TrEMBL. DT 02-MAR-2010, sequence version 1. DT 07-JUN-2017, entry version 60. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Slin_6253 {ECO:0000313|EMBL:ADB42212.1}; OS Spirosoma linguale (strain ATCC 33905 / DSM 74 / LMG 10896). OC Bacteria; Bacteroidetes; Cytophagia; Cytophagales; Cytophagaceae; OC Spirosoma. OX NCBI_TaxID=504472 {ECO:0000313|EMBL:ADB42212.1, ECO:0000313|Proteomes:UP000002028}; RN [1] {ECO:0000313|Proteomes:UP000002028} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33905 / DSM 74 / LMG 10896 RC {ECO:0000313|Proteomes:UP000002028}; RG US DOE Joint Genome Institute (JGI-PGF); RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., RA Tice H., Bruce D., Goodwin L., Pitluck S., Kyrpides N., Mavromatis K., RA Mikhailova N., Ovchinnikova G., Saunders E., Brettin T., Detter J.C., RA Han C., Larimer F., Land M., Hauser L., Markowitz V., Cheng J.-F., RA Hugenholtz P., Woyke T., Wu D., Tindal B., Schutze A., Schneider S., RA Goker M., Klenk H.-P., Eisen J.A.; RT "The complete chromosome of Spirosoma linguale DSM 74."; RL Submitted (SEP-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001769; ADB42212.1; -; Genomic_DNA. DR ProteinModelPortal; D2QTT0; -. DR STRING; 504472.Slin_6253; -. DR EnsemblBacteria; ADB42212; ADB42212; Slin_6253. DR KEGG; sli:Slin_6253; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000002028; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 2. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000002028}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000002028}. FT DOMAIN 200 401 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 161 188 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 426 AA; 48387 MW; 6E5D81E225B73CCF CRC64; MIDTHKPAET AILVAVITQK QTAEQTKDYL DELAFLAETS GVKTIQTFTQ KLEHPDNRTF VGKGKLEEIQ TFILDNPVDC VIFDDDLSPS QVRNLEDSFK DIKVLDRSLL ILNIFSMRAQ TAQSRVQVEL AQYQYMYPRL TRMWSHLTSQ KGGVGMRGPG EKELETDRRI VKDRIAFLKE KLAKIDKQSV TRRKERDRLV RVALVGYTNV GKSTLMRTMA KADVFAENKL FATVDSTVRK VTLGNIPFLL TDTVGFIRKL PTMLIESFKS TLDEVREADI LVHVVDVSHP NFEEQIEVVN STLADIKAAD KPMVLVFNKM DRFSPKASWT EKAELPEEDE VFNGGEEVMI PMAVQRKTAL EYLKKTYLSQ KADYVAFISA ETGENVGELR ELLYSLVKEK HFFIYPNWVN VPLTESAEEF GDGLAG // ID D2QZ49_PIRSD Unreviewed; 489 AA. AC D2QZ49; DT 02-MAR-2010, integrated into UniProtKB/TrEMBL. DT 02-MAR-2010, sequence version 1. DT 07-JUN-2017, entry version 50. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Psta_3580 {ECO:0000313|EMBL:ADB18241.1}; OS Pirellula staleyi (strain ATCC 27377 / DSM 6068 / ICPB 4128) (Pirella OS staleyi). OC Bacteria; Planctomycetes; Planctomycetia; Planctomycetales; OC Planctomycetaceae; Pirellula. OX NCBI_TaxID=530564 {ECO:0000313|EMBL:ADB18241.1, ECO:0000313|Proteomes:UP000001887}; RN [1] {ECO:0000313|EMBL:ADB18241.1, ECO:0000313|Proteomes:UP000001887} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 27377 / DSM 6068 / ICPB 4128 RC {ECO:0000313|Proteomes:UP000001887}; RX PubMed=21304671; DOI=10.4056/sigs.51657; RA Clum A., Tindall B.J., Sikorski J., Ivanova N., Mavrommatis K., RA Lucas S., Glavina del Rio T., Nolan M., Chen F., Tice H., Pitluck S., RA Cheng J.F., Chertkov O., Brettin T., Han C., Detter J.C., Kuske C., RA Bruce D., Goodwin L., Ovchinikova G., Pati A., Mikhailova N., Chen A., RA Palaniappan K., Land M., Hauser L., Chang Y.J., Jeffries C.D., RA Chain P., Rohde M., Goker M., Bristow J., Eisen J.A., Markowitz V., RA Hugenholtz P., Kyrpides N.C., Klenk H.P., Lapidus A.; RT "Complete genome sequence of Pirellula staleyi type strain (ATCC RT 27377)."; RL Stand. Genomic Sci. 1:308-316(2009). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001848; ADB18241.1; -; Genomic_DNA. DR ProteinModelPortal; D2QZ49; -. DR STRING; 530564.Psta_3580; -. DR EnsemblBacteria; ADB18241; ADB18241; Psta_3580. DR KEGG; psl:Psta_3580; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000001887; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000001887}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000001887}. FT DOMAIN 229 395 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 190 217 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 489 AA; 54284 MW; B3A02DFC3BB74E99 CRC64; MSIHPSLSSS DTPENNLSRK PSGGKRPHVQ EIQREQGVAR ERAILVRVIL PDQYCGEDPL DEIAGLAKTA GATVVGTCVQ RREIPDTTTY LGKGKVNELK EIVEANEADV VIFDNDLGPA QTRNLEQTIK VKVLDRTELI LDIFASNARS YESRLAVELA QLEYSLPRLK RMWTHLSRIK MGIGMRGPGE KQLEEDRRLV ERRIHELKTE LHGVERRKQR QVASRADRLT VSLVGYTNAG KSTLMNALTD AGVLAADKLF ATLDTRTRRW HLPSWGPVLL SDTVGFIRDL PHGLVASFRA TLEEARQADL LIHVADASNP AVLEQISAVY IVLQELGIEE KDTLLVLNKI DRLADPAQLV AVKQRYPNAI TISAATREGF DRLHDSVSSA LSRSFADLDV QAEVSNGRLL AFLSAHGEVL SKTFSEDRVI VHCRLPHRHL GGLMRERAVV RPHTAAEFLL QDLPEHAAES EVELLEETSQ PSPSVEDVA // ID D2RJY2_ACIFV Unreviewed; 604 AA. AC D2RJY2; DT 02-MAR-2010, integrated into UniProtKB/TrEMBL. DT 02-MAR-2010, sequence version 1. DT 07-JUN-2017, entry version 58. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Acfer_1014 {ECO:0000313|EMBL:ADB47384.1}; OS Acidaminococcus fermentans (strain ATCC 25085 / DSM 20731 / VR4). OC Bacteria; Firmicutes; Negativicutes; Acidaminococcales; OC Acidaminococcaceae; Acidaminococcus. OX NCBI_TaxID=591001 {ECO:0000313|EMBL:ADB47384.1, ECO:0000313|Proteomes:UP000001902}; RN [1] {ECO:0000313|EMBL:ADB47384.1, ECO:0000313|Proteomes:UP000001902} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 25085 / DSM 20731 / VR4 RC {ECO:0000313|Proteomes:UP000001902}; RX PubMed=21304687; DOI=10.4056/sigs.1002553; RA Chang Y.J., Pukall R., Saunders E., Lapidus A., Copeland A., Nolan M., RA Glavina Del Rio T., Lucas S., Chen F., Tice H., Cheng J.F., Han C., RA Detter J.C., Bruce D., Goodwin L., Pitluck S., Mikhailova N., RA Liolios K., Pati A., Ivanova N., Mavromatis K., Chen A., RA Palaniappan K., Land M., Hauser L., Jeffries C.D., Brettin T., RA Rohde M., Goker M., Bristow J., Eisen J.A., Markowitz V., RA Hugenholtz P., Kyrpides N.C., Klenk H.P.; RT "Complete genome sequence of Acidaminococcus fermentans type strain RT (VR4)."; RL Stand. Genomic Sci. 3:1-14(2010). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001859; ADB47384.1; -; Genomic_DNA. DR RefSeq; WP_012938373.1; NC_013740.1. DR ProteinModelPortal; D2RJY2; -. DR STRING; 591001.Acfer_1014; -. DR EnsemblBacteria; ADB47384; ADB47384; Acfer_1014. DR KEGG; afn:Acfer_1014; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000001902; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000001902}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000001902}. FT DOMAIN 384 550 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 343 377 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 604 AA; 67204 MW; 9FFCB5F32210FD18 CRC64; MTQTIYGKTE GLKKQVLTQL EGIYELRADE GQLISQELAL VLRDLSDAIN REISLYIDRK GRVTAVAVGS DCHVELPGTD SRRSQNRLCG VACIHTHPSG APRLSGVDLS ALRDLRFDAM AAMAWETPQS EPLLSFGMIT DLDEDQQPVL QEFGPFKVKD VAAMPFGNVV HTVEKILAKR SRNHNLAEGP ERAMLISLAW GDTASRWSAQ DSVEELAQLA ETAGAEVVGK FVQSRPKPDP VFFIGKGKVQ EMALFAQQED IDLCIFDDEL SPAQQRNLER ALGVRIIDRT GLILDIFAKR ARTSEGKLQV ELAQLQYMLP RIMGQGTSLS RLGGGIGTRG PGETKLEVDR RRIRDRIAFL EDQIRRMKGN RKQQQRARNK NEVKQVCLVG YTNAGKSTLL NTLTHSDIYA QDQLFATLDP TTRQLDLPDG SSCTLTDTVG FIQRLPHQLV AAFKSTLEVV KDADLLLHVV DSSHELAREQ TEAVYQVLQE LGVTDKPILT VYNKVDRLSQ HEGLRRRLEQ EDNALCISAR TGEGVPELLE TLARLLGQDR VEADLCIPYG ESRLAARLHE EAQVLSEEYG ETGILIRARM DKALADRLAP YIQP // ID D2RRN5_HALTV Unreviewed; 433 AA. AC D2RRN5; DT 02-MAR-2010, integrated into UniProtKB/TrEMBL. DT 02-MAR-2010, sequence version 1. DT 07-JUN-2017, entry version 56. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Htur_1710 {ECO:0000313|EMBL:ADB60595.1}; OS Haloterrigena turkmenica (strain ATCC 51198 / DSM 5511 / NCIMB 13204 / OS VKM B-1734) (Halococcus turkmenicus). OC Archaea; Euryarchaeota; Halobacteria; Natrialbales; Natrialbaceae; OC Haloterrigena. OX NCBI_TaxID=543526 {ECO:0000313|EMBL:ADB60595.1, ECO:0000313|Proteomes:UP000001903}; RN [1] {ECO:0000313|EMBL:ADB60595.1, ECO:0000313|Proteomes:UP000001903} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51198 / DSM 5511 / NCIMB 13204 / VKM B-1734 RC {ECO:0000313|Proteomes:UP000001903}; RX PubMed=21304683; DOI=10.4056/sigs.681272; RA Saunders E., Tindall B.J., Fahnrich R., Lapidus A., Copeland A., RA Del Rio T.G., Lucas S., Chen F., Tice H., Cheng J.F., Han C., RA Detter J.C., Bruce D., Goodwin L., Chain P., Pitluck S., Pati A., RA Ivanova N., Mavromatis K., Chen A., Palaniappan K., Land M., RA Hauser L., Chang Y.J., Jeffries C.D., Brettin T., Rohde M., Goker M., RA Bristow J., Eisen J.A., Markowitz V., Hugenholtz P., Klenk H.P., RA Kyrpides N.C.; RT "Complete genome sequence of Haloterrigena turkmenica type strain RT (4k)."; RL Stand. Genomic Sci. 2:107-116(2010). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001860; ADB60595.1; -; Genomic_DNA. DR RefSeq; WP_012942889.1; NC_013743.1. DR ProteinModelPortal; D2RRN5; -. DR STRING; 543526.Htur_1710; -. DR EnsemblBacteria; ADB60595; ADB60595; Htur_1710. DR GeneID; 8742304; -. DR KEGG; htu:Htur_1710; -. DR eggNOG; arCOG00353; Archaea. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG093Z07D6; -. DR Proteomes; UP000001903; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000001903}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000001903}. FT DOMAIN 186 369 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 102 129 {ECO:0000256|SAM:Coils}. FT COILED 152 175 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 433 AA; 48321 MW; 33ADEEACA390BD88 CRC64; MRAIIAKRVD SGTPDTSEIR DLAAAAGYTV VGEITQSRKA DPALQLGEGK AEELADEVAA TDATTVIFDN RLGPYQTYNL GQLLPEGVEV IDRFTLILEI FGQRAQTRKA QLQVELAELR YELPRAEAKT SLAKREEHPG FMGLGEYDES REQDIKDQIS RIKDELERIE QTEQHRRERR RDSGFDLVAL AGYTNAGKST LLRQLADDLT VEENEDLHPD LDATAESQDK LFTTLGTTTR RAAIEPRDVL VTDTVGFISD LPHWLVESFK STLDSVYRAD LVLLVVDVSE PIDEIHEKLV TSHDTLYERN EAPIVTVLNK IDTVDDAELE EKREALSALA PNPVAVSGRE GTNVDTLLER IDEELPDWEE ERLLLPMTED TMSVVSWLHD NAHVEEVTYG DEDVVVSFEA RPAVISQARS RASELRTAAA ESA // ID D2S693_GEOOG Unreviewed; 384 AA. AC D2S693; DT 02-MAR-2010, integrated into UniProtKB/TrEMBL. DT 02-MAR-2010, sequence version 1. DT 07-JUN-2017, entry version 54. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Gobs_0528 {ECO:0000313|EMBL:ADB73310.1}; OS Geodermatophilus obscurus (strain ATCC 25078 / DSM 43160 / JCM 3152 / OS G-20). OC Bacteria; Actinobacteria; Geodermatophilales; Geodermatophilaceae; OC Geodermatophilus. OX NCBI_TaxID=526225 {ECO:0000313|EMBL:ADB73310.1, ECO:0000313|Proteomes:UP000001382}; RN [1] {ECO:0000313|Proteomes:UP000001382} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 25078 / DSM 43160 / JCM 3152 / G-20 RC {ECO:0000313|Proteomes:UP000001382}; RG US DOE Joint Genome Institute (JGI-PGF); RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., RA Tice H., Bruce D., Goodwin L., Pitluck S., Kyrpides N., Mavromatis K., RA Ivanova N., Munk A.C., Brettin T., Detter J.C., Han C., Larimer F., RA Land M., Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P., RA Woyke T., Wu D., Jando M., Schneider S., Klenk H.-P., Eisen J.A.; RT "The complete genome of Geodermatophilus obscurus DSM 43160."; RL Submitted (JAN-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001867; ADB73310.1; -; Genomic_DNA. DR RefSeq; WP_012946751.1; NC_013757.1. DR ProteinModelPortal; D2S693; -. DR STRING; 526225.Gobs_0528; -. DR EnsemblBacteria; ADB73310; ADB73310; Gobs_0528. DR KEGG; gob:Gobs_0528; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR OMA; FNNHAHV; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000001382; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000001382}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000001382}. FT DOMAIN 222 384 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 384 AA; 41429 MW; 4661A615D1A7AC82 CRC64; MPGTWLLGSE VAQDGNRDGD GGPDGARAVL LGLRDGGRGA ADPLDELERL AETDGVAVVG RLVQPRDRPD PATYLGSGKV AELADLVRDR DAGLVIADGE LSPAQVRNLE ERLGARVVDR TALILDIFAQ HARSSEGKAQ VELAQLAYQL PRLTGHGVEM SRVGGGRTAG GAGIGVRGPG EQQLESRRRH LRRRMTLLRR QVQDTARRRE RTRSRRRRNR VPSVALTGYT NAGKSALLNR LAGADVLVQD ALFATLDPTV RRTRTPDGRP YTLTDTVGFV RHLPHQLVDA FRSTLEEVVD ADLVLHVVDA SAPDAMDQVT AVRGVLHEIG ARDHPELLAL NKVDVAPEGW LAALRAAYPD AVPVSALTGE GAEELRRAIG ERLD // ID D2SDQ8_GEOOG Unreviewed; 512 AA. AC D2SDQ8; DT 02-MAR-2010, integrated into UniProtKB/TrEMBL. DT 02-MAR-2010, sequence version 1. DT 07-JUN-2017, entry version 55. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Gobs_3905 {ECO:0000313|EMBL:ADB76474.1}; OS Geodermatophilus obscurus (strain ATCC 25078 / DSM 43160 / JCM 3152 / OS G-20). OC Bacteria; Actinobacteria; Geodermatophilales; Geodermatophilaceae; OC Geodermatophilus. OX NCBI_TaxID=526225 {ECO:0000313|EMBL:ADB76474.1, ECO:0000313|Proteomes:UP000001382}; RN [1] {ECO:0000313|Proteomes:UP000001382} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 25078 / DSM 43160 / JCM 3152 / G-20 RC {ECO:0000313|Proteomes:UP000001382}; RG US DOE Joint Genome Institute (JGI-PGF); RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., RA Tice H., Bruce D., Goodwin L., Pitluck S., Kyrpides N., Mavromatis K., RA Ivanova N., Munk A.C., Brettin T., Detter J.C., Han C., Larimer F., RA Land M., Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P., RA Woyke T., Wu D., Jando M., Schneider S., Klenk H.-P., Eisen J.A.; RT "The complete genome of Geodermatophilus obscurus DSM 43160."; RL Submitted (JAN-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001867; ADB76474.1; -; Genomic_DNA. DR ProteinModelPortal; D2SDQ8; -. DR STRING; 526225.Gobs_3905; -. DR PRIDE; D2SDQ8; -. DR EnsemblBacteria; ADB76474; ADB76474; Gobs_3905. DR KEGG; gob:Gobs_3905; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000001382; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000001382}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000001382}. FT DOMAIN 291 455 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 512 AA; 54420 MW; 1723B684D0EAA803 CRC64; MTIQMPQVLG SATLETMTTA QNRAVLADAE ERALRAAPEP TEEAPRPDAA SDEPDDTTGS YALEARGALR RVAGLSTELA DVTEVEYRQL RLERVVLVGV WTEGTQADAD RSLGELAALA ETAGSEVLEA VSQRRDKPDA GTYVGSGKAA EIRDIVAAAG ADTVICDGEL TPGQLNALEK ILKVKVVDRT ALILDIFAQH ASSREGKAQV ELAQMQYMLP RLRGWGESLS RQAGGRVAGG GGIGTRGPGE TKIETDRRRI RARVSKLRRE IAGMATARAT QRSSRGRNAV PSVAIAGYTN AGKSSLLNRL TGAGVLVENA LFATLDPTVR RAQSPDGREY TLTDTVGFVR HLPHQLVDAF RSTLEEVAAA DLLLHVVDGS DPDPLGQIEA VRVVLGEIEA AAVPELIVVN KVDAMGEEDV LTLRRALPGA IWVSARTGVG IEQLREIVAA RLPHPDVEVD VLVPYDRGDL VARVHRDGEV LNETHEVGGT RLSARVDGAL AAALDGFTAP VA // ID D2TN10_CITRI Unreviewed; 426 AA. AC D2TN10; DT 02-MAR-2010, integrated into UniProtKB/TrEMBL. DT 02-MAR-2010, sequence version 1. DT 30-AUG-2017, entry version 56. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:CBG89953.1}; GN OrderedLocusNames=ROD_32331 {ECO:0000313|EMBL:CBG89953.1}; OS Citrobacter rodentium (strain ICC168) (Citrobacter freundii biotype OS 4280). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; OC Enterobacteriaceae; Citrobacter. OX NCBI_TaxID=637910 {ECO:0000313|EMBL:CBG89953.1, ECO:0000313|Proteomes:UP000001889}; RN [1] {ECO:0000313|EMBL:CBG89953.1, ECO:0000313|Proteomes:UP000001889} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ICC168 {ECO:0000313|EMBL:CBG89953.1, RC ECO:0000313|Proteomes:UP000001889}; RX PubMed=19897651; DOI=10.1128/JB.01144-09; RA Petty N.K., Bulgin R., Crepin V.F., Cerdeno-Tarraga A.M., RA Schroeder G.N., Quail M.A., Lennard N., Corton C., Barron A., RA Clark L., Toribio A.L., Parkhill J., Dougan G., Frankel G., RA Thomson N.R.; RT "The Citrobacter rodentium genome sequence reveals convergent RT evolution with human pathogenic Escherichia coli."; RL J. Bacteriol. 192:525-538(2010). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; FN543502; CBG89953.1; -; Genomic_DNA. DR RefSeq; WP_012907324.1; NC_013716.1. DR ProteinModelPortal; D2TN10; -. DR STRING; 637910.ROD_32331; -. DR EnsemblBacteria; CBG89953; CBG89953; ROD_32331. DR KEGG; cro:ROD_32331; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000001889; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000001889}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000001889}. FT DOMAIN 198 365 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 164 191 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 426 AA; 48165 MW; 2FEBF8356024C45C CRC64; MFDRYDAGEQ AVLVHIYFSQ DKDMEDLQEF ESLVSSAGVE AMQVITGSRK APHPKYFVGE GKAVEIAEAV KATGAAVVLF DHALSPAQER NLERLCECRV IDRTGLILDI FAQRARTHEG KLQVELAQLR HLATRLVRGW THLERQKGGI GLRGPGETQL ETDRRLLRNR ILQIQSRLEK VEKQREQGRQ SRIKADVPTV SLVGYTNAGK STLFNQITEA RVYAADQLFA TLDPTLRRID VADVGETVLA DTVGFIRHLP HDLVAAFKAT LQETRQATLL LHVVDAADVR VQENIDAVDT VLEEIDAHEI PTLMVMNKID MLDDFAPRID RDEENKPIRV WLSAQTGAGI PQLFQALTER LSGEVAQHTL RLPPQEGRLR SRFYQLQAIE KEWMEDDGSV SLQVRMPIVD WRRLCKQEPA LEDYVV // ID D2UDM6_XANAP Unreviewed; 441 AA. AC D2UDM6; DT 02-MAR-2010, integrated into UniProtKB/TrEMBL. DT 02-MAR-2010, sequence version 1. DT 30-AUG-2017, entry version 60. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:CBA15683.1}; GN OrderedLocusNames=XALc_1168 {ECO:0000313|EMBL:CBA15683.1}; OS Xanthomonas albilineans (strain GPE PC73 / CFBP 7063). OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales; OC Xanthomonadaceae; Xanthomonas. OX NCBI_TaxID=380358 {ECO:0000313|EMBL:CBA15683.1, ECO:0000313|Proteomes:UP000001890}; RN [1] {ECO:0000313|EMBL:CBA15683.1, ECO:0000313|Proteomes:UP000001890} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=GPE PC73 / CFBP 7063 {ECO:0000313|Proteomes:UP000001890}; RX PubMed=20017926; DOI=10.1186/1471-2164-10-616; RA Pieretti I., Royer M., Barbe V., Carrere S., Koebnik R., RA Cociancich S., Couloux A., Darrasse A., Gouzy J., Jacques M.A., RA Lauber E., Manceau C., Mangenot S., Poussier S., Segurens B., RA Szurek B., Verdier V., Arlat M., Rott P.; RT "The complete genome sequence of Xanthomonas albilineans provides new RT insights into the reductive genome evolution of the xylem-limited RT Xanthomonadaceae."; RL BMC Genomics 10:616-616(2009). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; FP565176; CBA15683.1; -; Genomic_DNA. DR RefSeq; WP_012915687.1; NC_013722.1. DR ProteinModelPortal; D2UDM6; -. DR EnsemblBacteria; CBA15683; CBA15683; XALC_1168. DR KEGG; xal:XALC_1168; -. DR PATRIC; fig|29447.3.peg.1169; -. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000001890; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000001890}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000001890}. FT DOMAIN 199 369 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 158 192 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 441 AA; 48811 MW; 658A20F5F337AEEC CRC64; MFDRSRRGEH ALLIQPYAGG PLQDDVLEEF ADLARSAGAS IAATVTARID KPSPSTLIGS GKLEEVKAAA DASGADLILV NHALSPGQER NLEKYLERRV IDRTGLILDI FAQRARSHEG KLQVELAQLR HMATRLVRGW THLERQRGGS IGLRGPGETQ LETDRRLLQK RVEQLQKRLE KVEVQHTQMR RARVRSELPR IAVVGYTNAG KSTLFNALTG AEAYAADQLF ATLDPTVRRI ALPGGNAMLA DTVGFVRDLP HELVAAFRST LSEAREADFL LHVVDAADPL REERIAQVDE VLHAVGAGEL PQLLVFNKID RIEGAQARHD AQDGAPDAAR RERVWISARD GRGQDLLQQV LGQRLGLRHV QGRLRLPPSA GRLRSQLHQL QVIRSEQGDE DGWLLQVDIP ITEAERLAAT ADGAPIRALL PPPEQEEWQQ R // ID D2Z4L4_9BACT Unreviewed; 364 AA. AC D2Z4L4; DT 23-MAR-2010, integrated into UniProtKB/TrEMBL. DT 23-MAR-2010, sequence version 1. DT 07-JUN-2017, entry version 41. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=Dpep_2336 {ECO:0000313|EMBL:EFC92358.1}; OS Dethiosulfovibrio peptidovorans DSM 11002. OC Bacteria; Synergistetes; Synergistia; Synergistales; Synergistaceae; OC Dethiosulfovibrio. OX NCBI_TaxID=469381 {ECO:0000313|EMBL:EFC92358.1, ECO:0000313|Proteomes:UP000006427}; RN [1] {ECO:0000313|EMBL:EFC92358.1, ECO:0000313|Proteomes:UP000006427} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 11002 {ECO:0000313|EMBL:EFC92358.1, RC ECO:0000313|Proteomes:UP000006427}; RX PubMed=21304695; RA Labutti K., Mayilraj S., Clum A., Lucas S., Glavina Del Rio T., RA Nolan M., Tice H., Cheng J.F., Pitluck S., Liolios K., Ivanova N., RA Mavromatis K., Mikhailova N., Pati A., Goodwin L., Chen A., RA Palaniappan K., Land M., Hauser L., Chang Y.J., Jeffries C.D., RA Rohde M., Spring S., Goker M., Woyke T., Bristow J., Eisen J.A., RA Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P., Lapidus A.; RT "Permanent draft genome sequence of Dethiosulfovibrio peptidovorans RT type strain (SEBR 4207)."; RL Stand. Genomic Sci. 3:85-92(2010). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EFC92358.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABTR02000001; EFC92358.1; -; Genomic_DNA. DR RefSeq; WP_005662357.1; NZ_ABTR02000001.1. DR ProteinModelPortal; D2Z4L4; -. DR STRING; 469381.Dpep_2336; -. DR EnsemblBacteria; EFC92358; EFC92358; Dpep_2336. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000006427; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000006427}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000006427}. FT DOMAIN 194 364 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 153 187 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 364 AA; 41262 MW; F03DD63840FDE3CC CRC64; MADERRRAVL IALERLEEGE RLLLELELLL ANLDVDVVER VIQKRDSPDP AFFLGSGKAR DLKRVCDVVD AGLIVSDRPL TPRQMANLKA ESGRYVWDRP LVIMKIFEER ARTSEAKLQV ELARCRYELP HLRGLGHQMS RLGGGIGTRG PGETEFERHR RKLERRIRDI TRKLVQVKKR RRNQRKRRSR SDIVTVAMVG YTNSGKSTLL RRLSGDRSIY VADALFATLD TLVRSISMSD GRTILLTDTV GFIRELPPTL IAAFRTTLEE AVAADFLLVM LDGSDPDALE TLRVVRDTLR DIDAIEIPRA VFLNKADLID RSTLDGLLTR IRSEGEDVEA ISASKWDVKE ITPVLEKLVF RTGL // ID D3APJ8_9CLOT Unreviewed; 158 AA. AC D3APJ8; DT 23-MAR-2010, integrated into UniProtKB/TrEMBL. DT 23-MAR-2010, sequence version 1. DT 12-APR-2017, entry version 20. DE SubName: Full=Putative GTP-binding protein HflX {ECO:0000313|EMBL:EFC96259.1}; GN ORFNames=CLOSTHATH_05550 {ECO:0000313|EMBL:EFC96259.1}; OS Hungatella hathewayi DSM 13479. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Hungatella. OX NCBI_TaxID=566550 {ECO:0000313|EMBL:EFC96259.1, ECO:0000313|Proteomes:UP000004968}; RN [1] {ECO:0000313|EMBL:EFC96259.1, ECO:0000313|Proteomes:UP000004968} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 13479 {ECO:0000313|EMBL:EFC96259.1, RC ECO:0000313|Proteomes:UP000004968}; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Nelson J., Hou S., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Nash W.E., Warren W., Chinwalla A., Mardis E.R., RA Wilson R.K.; RL Submitted (JAN-2010) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EFC96259.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACIO01000588; EFC96259.1; -; Genomic_DNA. DR ProteinModelPortal; D3APJ8; -. DR EnsemblBacteria; EFC96259; EFC96259; CLOSTHATH_05550. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000004968; Unassembled WGS sequence. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000004968}. FT DOMAIN 29 116 GTP-bdg_N. {ECO:0000259|Pfam:PF13167}. FT DOMAIN 118 145 GTP-bdg_M. {ECO:0000259|Pfam:PF16360}. SQ SEQUENCE 158 AA; 17511 MW; 3B6D1E8DB0471EF9 CRC64; MADLVELKEI EERVILVAVS TEEGSLAASS LDELEELVET AGAVTVDKMI QNRERIHPGT YLGKGKIEEV KERVWELNAT GIVCDDELSP AQLRNLEDAL DTKVMDRTMV ILDIFASRAT TREGKIQVEL AQLKYRAARL VGLRNSNPFG SNVGTERV // ID D3ARD4_9CLOT Unreviewed; 301 AA. AC D3ARD4; DT 23-MAR-2010, integrated into UniProtKB/TrEMBL. DT 23-MAR-2010, sequence version 1. DT 07-JUN-2017, entry version 32. DE SubName: Full=GTP-binding protein HflX {ECO:0000313|EMBL:EFC95622.1}; DE Flags: Fragment; GN Name=hflX {ECO:0000313|EMBL:EFC95622.1}; GN ORFNames=CLOSTHATH_06190 {ECO:0000313|EMBL:EFC95622.1}; OS Hungatella hathewayi DSM 13479. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Hungatella. OX NCBI_TaxID=566550 {ECO:0000313|EMBL:EFC95622.1, ECO:0000313|Proteomes:UP000004968}; RN [1] {ECO:0000313|EMBL:EFC95622.1, ECO:0000313|Proteomes:UP000004968} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 13479 {ECO:0000313|EMBL:EFC95622.1, RC ECO:0000313|Proteomes:UP000004968}; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Nelson J., Hou S., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Nash W.E., Warren W., Chinwalla A., Mardis E.R., RA Wilson R.K.; RL Submitted (JAN-2010) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EFC95622.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACIO01000712; EFC95622.1; -; Genomic_DNA. DR RefSeq; WP_006776604.1; NZ_GG667812.1. DR ProteinModelPortal; D3ARD4; -. DR EnsemblBacteria; EFC95622; EFC95622; CLOSTHATH_06190. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000004968; Unassembled WGS sequence. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000004968}. FT DOMAIN 182 301 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 141 175 {ECO:0000256|SAM:Coils}. FT NON_TER 1 1 {ECO:0000313|EMBL:EFC95622.1}. FT NON_TER 301 301 {ECO:0000313|EMBL:EFC95622.1}. SQ SEQUENCE 301 AA; 34151 MW; 6B2FDD71990582C1 CRC64; NQDFEVSMKE LNNLVKACDM EPVARIDQNL ASINAAYYIG SGKVGEIREA AETLRADYVV FNDTLSPSQL KNLQREIDVP VWDRTYLILE IFSRRAQTKE ARMQVESARL QYMLPRLMGL RDSLGRQGGA SGSLSNKGSG EKQIELDRRK IEGRISELRR ELERMEQERN VQRRKRSRGT CPQAALVGYT NAGKSTLLNK LVELSNGKEE KMVMAKDMLF ATLDTTVRKI SPNGSQDFLL SDTVGFISRL PHSLVKAFRS TLEEIRYADL LLHVVDFSDE HYKEQMEVTE ETLKELGAGD I // ID D3D4N3_9ACTN Unreviewed; 502 AA. AC D3D4N3; DT 23-MAR-2010, integrated into UniProtKB/TrEMBL. DT 23-MAR-2010, sequence version 1. DT 07-JUN-2017, entry version 45. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=FrEUN1fDRAFT_4755 {ECO:0000313|EMBL:EFC82110.1}; OS Frankia sp. EUN1f. OC Bacteria; Actinobacteria; Frankiales; Frankiaceae; Frankia. OX NCBI_TaxID=102897 {ECO:0000313|EMBL:EFC82110.1, ECO:0000313|Proteomes:UP000004777}; RN [1] {ECO:0000313|EMBL:EFC82110.1, ECO:0000313|Proteomes:UP000004777} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=EUN1f {ECO:0000313|EMBL:EFC82110.1, RC ECO:0000313|Proteomes:UP000004777}; RG US DOE Joint Genome Institute (JGI-PGF); RA Lucas S., Copeland A., Lapidus A., Tice H., Bruce D., Goodwin L., RA Pitluck S., Larimer F., Land M.L., Hauser L., Beauchemin N., Sen A., RA Fernandez M., Tisa L.; RT "The draft genome of Frankia sp. EUN1f."; RL Submitted (JAN-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EFC82110.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADGX01000083; EFC82110.1; -; Genomic_DNA. DR RefSeq; WP_006542616.1; NZ_ADGX01000083.1. DR ProteinModelPortal; D3D4N3; -. DR EnsemblBacteria; EFC82110; EFC82110; FrEUN1fDRAFT_4755. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000004777; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000004777}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000004777}. FT DOMAIN 278 443 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 237 264 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 502 AA; 53733 MW; CFAF8FBBA808421B CRC64; MSLPADAAMA STRYPNPDLS PSFDGDDGGV VLLGDDEGFS FFDEQGDGFD LEERGALRRI PGLTTELEDV TEVEYRQLRL ERVVLIGVWT SGTLLEAEAS MTELAALATT AGSMVLDALV QRRDRPDTAT FVGSGKAREL AEVVASTGAD TVICDGELTP GQLRQLEEVV KVKVIDRTAL ILDIFAQHAT SREGKAQVEL AQLQYMLPRL RGWGESMSRA AASSGGRAPI GTRGPGETKI ETDRRRLRTR MAKLRRELAA MATVRETKRS SRRRGAVPAV AIAGYTNAGK SSLLNRLTGA GVLVEDALFA TLDPTVRRAT LPDGRVFTLA DTVGFVRHLP HQIVEAFRST LEEVVDADLV LHVVDGSAPD PMGQITAVRE VLAEIDAAGV PELVVVNKVD AVDPTTLAVL RKAVPDAIFV SARSGTGLAE LVDALSERIP HPEIEMSLLV PYTRGDLVSR IHRDGEVLSV EHTGAGTAVA ARVPVSLAAE LEPFRVAGAL RS // ID D3DGD2_HYDTT Unreviewed; 370 AA. AC D3DGD2; DT 23-MAR-2010, integrated into UniProtKB/TrEMBL. DT 23-MAR-2010, sequence version 1. DT 07-JUN-2017, entry version 65. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:BAI68884.1}; GN OrderedLocusNames=HTH_0420 {ECO:0000313|EMBL:BAI68884.1}; OS Hydrogenobacter thermophilus (strain DSM 6534 / IAM 12695 / TK-6). OC Bacteria; Aquificae; Aquificales; Aquificaceae; Hydrogenobacter. OX NCBI_TaxID=608538 {ECO:0000313|EMBL:BAI68884.1, ECO:0000313|Proteomes:UP000002574}; RN [1] {ECO:0000313|EMBL:BAI68884.1, ECO:0000313|Proteomes:UP000002574} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 6534 / IAM 12695 / TK-6 [Tokyo] RC {ECO:0000313|Proteomes:UP000002574}; RX PubMed=20348262; DOI=10.1128/JB.00158-10; RA Arai H., Kanbe H., Ishii M., Igarashi Y.; RT "Complete genome sequence of the thermophilic, obligately RT chemolithoautotrophic hydrogen-oxidizing bacterium Hydrogenobacter RT thermophilus TK-6."; RL J. Bacteriol. 192:2651-2652(2010). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AP011112; BAI68884.1; -; Genomic_DNA. DR RefSeq; WP_012963067.1; NC_017161.1. DR ProteinModelPortal; D3DGD2; -. DR STRING; 608538.HTH_0420; -. DR EnsemblBacteria; BAI68884; BAI68884; HTH_0420. DR KEGG; hte:Hydth_0419; -. DR KEGG; hth:HTH_0420; -. DR PATRIC; fig|608538.5.peg.425; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000002574; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000002574}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000002574}. FT DOMAIN 197 367 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 159 193 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 370 AA; 42281 MW; 64B1FE10A1F11FFD CRC64; MKALLVSLSY PDQNKEEVRE YIEELKELVK AVGGKVLGYV VQRRSAPDAR YYIGAGKLEE IKQVIEGVSA DTIIFNTFLS PSQIHNLENA LGVKVLDRAD LVLEIFSRRV RSKTAKLQVE LAKLELELPR LYGRGKELSR LGGGVGTRGP GEQEAEVRRR WIKKRIQQIR EELEEVKKQR KEQRKRRDRW HSDIRIVKVA LVGYTNVGKS SLMRLLTGRE TFVADMPFAT LDTKTSDVYL SKDIKVLITD TVGFIRDLPH ELIESFKATL EELQEADILL HVVDISDKKW LEKIKVVRKV LAELKVDEKP TLYVFNKADK LVESEQDIEL LTEPAFLGEK SVVISAQKGW GIKKLLSTIK EMVEEFIEVS // ID D3E8Q9_GEOS4 Unreviewed; 430 AA. AC D3E8Q9; DT 23-MAR-2010, integrated into UniProtKB/TrEMBL. DT 23-MAR-2010, sequence version 1. DT 07-JUN-2017, entry version 54. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=GYMC10_2358 {ECO:0000313|EMBL:ACX64636.1}; OS Geobacillus sp. (strain Y412MC10). OC Bacteria; Firmicutes; Bacilli; Bacillales; Paenibacillaceae; OC Paenibacillus. OX NCBI_TaxID=481743 {ECO:0000313|EMBL:ACX64636.1, ECO:0000313|Proteomes:UP000002381}; RN [1] {ECO:0000313|Proteomes:UP000002381} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Y412MC10 {ECO:0000313|Proteomes:UP000002381}; RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., RA Tice H., Bruce D., Goodwin L., Pitluck S., Saunders E., Brettin T., RA Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N., RA Ovchinnikova G., Brumm P., Mead D.; RT "Complete sequence of Geobacillus sp. Y412MC10."; RL Submitted (OCT-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001793; ACX64636.1; -; Genomic_DNA. DR RefSeq; WP_015734663.1; NC_013406.1. DR ProteinModelPortal; D3E8Q9; -. DR STRING; 481743.GYMC10_2358; -. DR EnsemblBacteria; ACX64636; ACX64636; GYMC10_2358. DR KEGG; gym:GYMC10_2358; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000002381; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000002381}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000002381}. FT DOMAIN 208 372 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 167 194 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 430 AA; 47797 MW; ACC4EB24787B6002 CRC64; MTNITHDTRT EIEDKAVLVS LVTDAVKRTG INPEHSLQEL VQLAETAGVE VLDVITQNRE VPDSKWFIGK GKVEELRMAI DGLGATTAIF DQELSGAQVR NLEESLDVKI IDRTQLILDI FAQRAKTREG IIQVELAQLT YLLPRLSGHG KNLSRLGAGI GTRGPGESKL ETDRRHIRDR ISDLKRQLDE VTRHRTLHRE RRKKSGAVQV ALVGYTNAGK STLLNRLTAA DVYIENQLFA TLDPTSRVLE LPSGKEVVLT DTVGFIQNLP HDLVAAFRAT LEEANEADLI LHVVDASSPM RDEQMAVVQS ILQDLGASDK PQIVLFNKKD ACEPGQLEML PTGEGQLKIS AYVDQDLESV REAIQDRLSG GNVTFRIPAD RGDLNSVVYR VGDVLEQSFD ENDILYEVRI NKADYEKMGY LLHDYVQNGS // ID D3FE61_CONWI Unreviewed; 450 AA. AC D3FE61; DT 23-MAR-2010, integrated into UniProtKB/TrEMBL. DT 23-MAR-2010, sequence version 1. DT 07-JUN-2017, entry version 57. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Cwoe_3259 {ECO:0000313|EMBL:ADB51677.1}; OS Conexibacter woesei (strain DSM 14684 / JCM 11494 / NBRC 100937 / OS ID131577). OC Bacteria; Actinobacteria; Thermoleophilia; Solirubrobacterales; OC Conexibacteraceae; Conexibacter. OX NCBI_TaxID=469383 {ECO:0000313|EMBL:ADB51677.1, ECO:0000313|Proteomes:UP000008229}; RN [1] {ECO:0000313|Proteomes:UP000008229} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 14684 / JCM 11494 / NBRC 100937 / ID131577 RC {ECO:0000313|Proteomes:UP000008229}; RG US DOE Joint Genome Institute (JGI-PGF); RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., RA Tice H., Bruce D., Goodwin L., Pitluck S., Kyrpides N., Mavromatis K., RA Ivanova N., Mikhailova N., Chertkov O., Brettin T., Detter J.C., RA Han C., Larimer F., Land M., Hauser L., Markowitz V., Cheng J.-F., RA Hugenholtz P., Woyke T., Wu D., Pukall R., Steenblock K., RA Schneider S., Klenk H.-P., Eisen J.A.; RT "The complete genome of Conexibacter woesei DSM 14684."; RL Submitted (JAN-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001854; ADB51677.1; -; Genomic_DNA. DR RefSeq; WP_012934728.1; NC_013739.1. DR ProteinModelPortal; D3FE61; -. DR STRING; 469383.Cwoe_3259; -. DR EnsemblBacteria; ADB51677; ADB51677; Cwoe_3259. DR KEGG; cwo:Cwoe_3259; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; FNNHAHV; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000008229; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000008229}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000008229}. FT DOMAIN 221 387 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 450 AA; 49569 MW; 0BCBFDA4F6D52AE1 CRC64; MTTTRSRNGR MSEPRRDDRQ PVGRARQRAF MIAALESGDD LSELQELLRT AGVAVVGQTV QHRERPHPNT YLGEGKLEEL RALLKEADAN VVAVDDELSP RQERNLERAL DTPVIDRTSI ILDIFAGHAH SAEGKLQVEL AQLQYNLARM RGLWTHLERL GAGAGGPGGG PGIGTRGPGE SQIETDRRLA RDRITALRRR LERVKGSRET MRAERDRARL PTVALVGYTN AGKSTLLNRL TGAEVGVRDR LFHTLDPTTR SYKLGGRDYL LTDTVGFIRK LPHQLVEAFG ATLEETRLAD LLLHVVDASA PEEELDEMMR AVDSVLGDIG AGDQPRLLIL NKADALDDDQ RHEVQLRHPD GMLISAATGE GLDALGERIE EEFARRLRDV ELLLPYSEGG RLAELHEIAG DLAREDTADG VRVTAKLPAT VAARYARYAV SANGDGRVEQ // ID D3HN82_LEGLN Unreviewed; 419 AA. AC D3HN82; DT 23-MAR-2010, integrated into UniProtKB/TrEMBL. DT 23-MAR-2010, sequence version 1. DT 30-AUG-2017, entry version 59. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:CBJ10338.1}; GN OrderedLocusNames=LLO_0017 {ECO:0000313|EMBL:CBJ10338.1}; OS Legionella longbeachae serogroup 1 (strain NSW150). OC Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales; OC Legionellaceae; Legionella. OX NCBI_TaxID=661367 {ECO:0000313|EMBL:CBJ10338.1, ECO:0000313|Proteomes:UP000001060}; RN [1] {ECO:0000313|EMBL:CBJ10338.1, ECO:0000313|Proteomes:UP000001060} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NSW150 {ECO:0000313|EMBL:CBJ10338.1, RC ECO:0000313|Proteomes:UP000001060}; RX PubMed=20174605; DOI=10.1371/journal.pgen.1000851; RA Cazalet C., Gomez-Valero L., Rusniok C., Lomma M., Dervins-Ravault D., RA Newton H., Sansom F., Jarraud S., Zidane N., Ma L., Bouchier C., RA Etienne J., Hartland E., Buchrieser C.; RT "Analysis of the Legionella longbeachae genome and transcriptome RT uncovers unique strategies to cause Legionnaires' disease."; RL PLoS Genet. 6:E1000851-E1000851(2010). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; FN650140; CBJ10338.1; -; Genomic_DNA. DR RefSeq; WP_003633820.1; NC_013861.1. DR ProteinModelPortal; D3HN82; -. DR STRING; 661367.LLO_0017; -. DR EnsemblBacteria; CBJ10338; CBJ10338; LLO_0017. DR KEGG; llo:LLO_0017; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000001060; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000001060}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000001060}. FT DOMAIN 198 363 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 419 AA; 47145 MW; 1A970E796D9B9D53 CRC64; MFERPQGGER AVLVQLALPG IDAGKALQEF EELALSANAE VLECVLGTRA TPDAKYYIGQ GKAEEIAQLV KTCDAELVLV NHELSPSQER NLERLLECRV VDRSGLILDI FAQRARTFEG KLQVELAQLQ HLSTRLIRGW THLERQKGGI GLRGPGETQL ETDRRLLRDR IKYINKRLEK VRSSRDQNRQ ARRKASLRTV SLVGYTNAGK STLFNALTGE SIYVANQLFA TLDPTMRQLN LPGSSSVIVT DTVGFIRDLP HHLVEAFRAT LEETQQADLL LHVIDISDPH WRDNVFSVQQ VLDELEVHDV PIIQVFNKID LKEGWEPKID YQEEKCKVWL SAASNLGLDL LKEAISTQLH GAISTEEVVL KATQAKLRAQ LYQLGSVLSE SINDEGDWLL KIRITKSQKQ RLFANECAS // ID D3IB51_9BACT Unreviewed; 416 AA. AC D3IB51; DT 23-MAR-2010, integrated into UniProtKB/TrEMBL. DT 23-MAR-2010, sequence version 1. DT 07-JUN-2017, entry version 43. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=HMPREF0669_00655 {ECO:0000313|EMBL:EFC70950.1}; OS Prevotella sp. oral taxon 299 str. F0039. OG Plasmid unnamed {ECO:0000313|EMBL:EFC70950.1}. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Prevotellaceae; OC Prevotella. OX NCBI_TaxID=575614 {ECO:0000313|EMBL:EFC70950.1, ECO:0000313|Proteomes:UP000015929}; RN [1] {ECO:0000313|EMBL:EFC70950.1, ECO:0000313|Proteomes:UP000015929} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=F0039 {ECO:0000313|EMBL:EFC70950.1, RC ECO:0000313|Proteomes:UP000015929}; RC PLASMID=unnamed {ECO:0000313|EMBL:EFC70950.1}; RG The Broad Institute Genome Sequencing Platform; RA Ward D., Feldgarden M., Earl A., Young S.K., Zeng Q., Koehrsen M., RA Alvarado L., Berlin A., Bochicchio J., Borenstein D., Chapman S.B., RA Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A., RA Gujja S., Heilman E., Heiman D., Hepburn T., Howarth C., Jen D., RA Larson L., Lewis B., Mehta T., Park D., Pearson M., Roberts A., RA Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., Thomson T., RA Walk T., White J., Yandava C., Izard J., Baranova O.V., Blanton J.M., RA Tanner A.C., Dewhirst F.E., Haas B., Nusbaum C., Birren B.; RL Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:EFC70950.1, ECO:0000313|Proteomes:UP000015929} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=F0039 {ECO:0000313|EMBL:EFC70950.1, RC ECO:0000313|Proteomes:UP000015929}; RG The Broad Institute Genome Sequencing Platform; RG The Broad Institute Genome Sequencing Center for Infectious Disease; RA Earl A., Ward D., Feldgarden M., Gevers D., Izard J., Baranova O.V., RA Blanton J.M., Tanner A.C., Dewhirst F.E., Walker B., Young S.K., RA Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., RA Alvarado L., Arachchi H.M., Berlin A.M., Chapman S.B., Goldberg J., RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Larimer J., RA McCowan C., Montmayeur A., Murphy C., Neiman D., Pearson M., RA Priest M., Roberts A., Saif S., Shea T., Sisk P., Sykes S., RA Wortman J., Nusbaum C., Birren B.; RT "The Genome Sequence of Prevotella sp. Oral Taxon 299 strain F0039."; RL Submitted (JUN-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP003667; EFC70950.1; -; Genomic_DNA. DR RefSeq; WP_009227831.1; NC_022111.1. DR ProteinModelPortal; D3IB51; -. DR STRING; 575614.HMPREF0669_00655; -. DR EnsemblBacteria; EFC70950; EFC70950; HMPREF0669_00655. DR KEGG; pro:HMPREF0669_00655; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR KO; K03665; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000015929; Plasmid. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000015929}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Plasmid {ECO:0000313|EMBL:EFC70950.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000015929}. FT DOMAIN 216 400 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 416 AA; 47802 MW; F998A91502699B89 CRC64; MKEFVISEVK AETAVLVGLI TKEQDENKTK EYLDELEFLA DTAGAITVKR FTQRVQGPNS VTYVGKGKLE EIKEYIVSEE EAERPVGMVI FDDELSPKQM RNIENELQVK ILDRTSLILD IFAMRAQTAN SKTQVELAQY RYMLPRLQRL WTHLERQGGG SGSGGGKGSV GLRGPGETQL EMDRRIILQR ISLLKERLVE IDKQKVTQRK NRGRMIRVAL VGYTNVGKST LMNLLSKSEV FAENKLFATL DTTVRKVVIE NLPFLLADTV GFIRKLPTDL VDSFKSTLDE VREADLLVHV VDISHPEFED HIRVVESTLK DLDAADKPSI MIFNKIDNYR WVEKEEDDLT PQGKENISLE ELERTWMARL KDDCVFISAK ENTNIKKLRE DLYARVKQLH VQKYPYNDFL YNIEEE // ID D3ILC0_9BACT Unreviewed; 414 AA. AC D3ILC0; DT 23-MAR-2010, integrated into UniProtKB/TrEMBL. DT 23-MAR-2010, sequence version 1. DT 07-JUN-2017, entry version 41. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:EFC67593.1}; GN ORFNames=HMPREF0670_02239 {ECO:0000313|EMBL:EFC67593.1}; OS Prevotella sp. oral taxon 317 str. F0108. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Prevotellaceae; OC Prevotella. OX NCBI_TaxID=575615 {ECO:0000313|EMBL:EFC67593.1, ECO:0000313|Proteomes:UP000003829}; RN [1] {ECO:0000313|EMBL:EFC67593.1, ECO:0000313|Proteomes:UP000003829} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=F0108 {ECO:0000313|EMBL:EFC67593.1, RC ECO:0000313|Proteomes:UP000003829}; RG The Broad Institute Genome Sequencing Platform; RA Ward D., Feldgarden M., Earl A., Young S.K., Zeng Q., Koehrsen M., RA Alvarado L., Berlin A., Bochicchio J., Borenstein D., Chapman S.B., RA Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A., RA Gujja S., Heilman E., Heiman D., Hepburn T., Howarth C., Jen D., RA Larson L., Lewis B., Mehta T., Park D., Pearson M., Roberts A., RA Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., Thomson T., RA Walk T., White J., Yandava C., Izard J., Baranova O.V., Blanton J.M., RA Tanner A.C., Dewhirst F.E., Haas B., Nusbaum C., Birren B.; RT "The Genome Sequence of Prevotella sp. Oral Taxon 317 strain F0108."; RL Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GG740075; EFC67593.1; -; Genomic_DNA. DR RefSeq; WP_009231334.1; NZ_GG740075.1. DR ProteinModelPortal; D3ILC0; -. DR STRING; 575615.HMPREF0670_02239; -. DR EnsemblBacteria; EFC67593; EFC67593; HMPREF0670_02239. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000003829; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000003829}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000003829}. FT DOMAIN 216 400 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 414 AA; 47302 MW; 9C712785DCF42AD8 CRC64; MKEFVISEVK AETAVLVGLI TQQQNEAKTK EYLDELEFLA DTAGAVTVKR FTQRLNAPSM VTYVGKGKLE EIKQYILAEE EAEREVGMVI FDDELSAKQM RNIEKELNVK ILDRTSLILD IFAMRAQTAN AKTQVELAQY RYMLPRLQRL WTHLERQGGG SGSGGGKGSV GLRGPGETQL EMDRRIILSR MALLKERLAE IDKQKTTQRK NRGRMVRVAL VGYTNVGKST IMNLLAKSEV FAENKLFATL DTTVRKVVVE NLPFLLADTV GFIRKLPTDL VDSFKSTLDE VREADLLVHV VDISHPDFEE QIAVVEKTLT ELDCADKPSM IVFNKIDNYT FVKKDEDDLT PATKENMTLD DLKRTWMARL NDNCIFISAR EKTNVDELRD RLYAKVRELH VQKYPYNDFL YEME // ID D3P8L1_DEFDS Unreviewed; 576 AA. AC D3P8L1; DT 20-APR-2010, integrated into UniProtKB/TrEMBL. DT 20-APR-2010, sequence version 1. DT 07-JUN-2017, entry version 57. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=DEFDS_1593 {ECO:0000313|EMBL:BAI81051.1}; OS Deferribacter desulfuricans (strain DSM 14783 / JCM 11476 / NBRC OS 101012 / SSM1). OC Bacteria; Deferribacteres; Deferribacterales; Deferribacteraceae; OC Deferribacter. OX NCBI_TaxID=639282 {ECO:0000313|EMBL:BAI81051.1, ECO:0000313|Proteomes:UP000001520}; RN [1] {ECO:0000313|EMBL:BAI81051.1, ECO:0000313|Proteomes:UP000001520} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 14783 / JCM 11476 / NBRC 101012 / SSM1 RC {ECO:0000313|Proteomes:UP000001520}; RX PubMed=20189949; DOI=10.1093/dnares/dsq005; RA Takaki Y., Shimamura S., Nakagawa S., Fukuhara Y., Horikawa H., RA Ankai A., Harada T., Hosoyama A., Oguchi A., Fukui S., Fujita N., RA Takami H., Takai K.; RT "Bacterial lifestyle in a deep-sea hydrothermal vent chimney revealed RT by the genome sequence of the thermophilic bacterium Deferribacter RT desulfuricans SSM1."; RL DNA Res. 17:123-137(2010). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AP011529; BAI81051.1; -; Genomic_DNA. DR ProteinModelPortal; D3P8L1; -. DR STRING; 639282.DEFDS_1593; -. DR EnsemblBacteria; BAI81051; BAI81051; DEFDS_1593. DR KEGG; ddf:DEFDS_1593; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; EREVIIT; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000001520; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000001520}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000001520}. FT DOMAIN 405 570 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 576 AA; 66192 MW; 11662621E8ADF8F0 CRC64; MTYCATTSII CIARKSVTTI IIIKKFRRDD ILTGELKDLK QSFIKRLEKL DRKRFKTDNI ISVELAKQVS ALSKEVNRQI GLLIDRQNEV QYVIVGDNRS IFIPELKRFR LVPGKLRGLR LVHTHLYGEP INDDDITDLA MLRLDSLTAI YVDEAGLPKS MDTIYLLPPN IENKTYDYLD EKDVYNQNIN FLEFIRELEK EIEDKTAALF QVSSGNNAIL AGVFKSKTEA KMALEELKEL ARSAGLNVLD TVYQIRNKVD PKYLLGVGKL KDLAIKAYQI GADYIIFDNN LQPSQAKEIS KIVELKIMDR TQLILDIFAK RAHTDEGKLK VELAQLKYIM PRLSVKDDSL SRLTGGIGGR GPGETKLEID RRRIKDRIAF LNRKLKQISK VRYTQRKRRL QREIPTVSIV GYTNAGKTTL INSLTNSSIY ADNLMFATLD TSSKRLRFPE EKEIIITDTV GFIRDLPEDL KDAFKSTLDE LYDADLFLHV VDISNPEFRK QIESVNKILE ELNLIDVEQI LVFNKIDLLD EESLKELKNE FPKAIFISAI NRKTFNELLN RIFYILFRQK VKNGSS // ID D3PSL5_MEIRD Unreviewed; 560 AA. AC D3PSL5; DT 20-APR-2010, integrated into UniProtKB/TrEMBL. DT 20-APR-2010, sequence version 1. DT 07-JUN-2017, entry version 57. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=K649_14125 {ECO:0000313|EMBL:AGK06111.1}; OS Meiothermus ruber (strain ATCC 35948 / DSM 1279 / VKM B-1258 / 21) OS (Thermus ruber). OC Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; OC Meiothermus. OX NCBI_TaxID=504728 {ECO:0000313|EMBL:AGK06111.1, ECO:0000313|Proteomes:UP000013026}; RN [1] {ECO:0000313|EMBL:AGK06111.1, ECO:0000313|Proteomes:UP000013026} RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 1279 {ECO:0000313|EMBL:AGK06111.1, RC ECO:0000313|Proteomes:UP000013026}; RA Chin J., Alexander D.H., Marks P., Korlach J., Clum A., Copeland A.; RL Submitted (APR-2013) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP005385; AGK06111.1; -; Genomic_DNA. DR RefSeq; WP_013013950.1; NC_021081.1. DR ProteinModelPortal; D3PSL5; -. DR STRING; 504728.Mrub_1687; -. DR EnsemblBacteria; AGK06111; AGK06111; K649_14125. DR KEGG; mrb:Mrub_1687; -. DR KEGG; mre:K649_14125; -. DR PATRIC; fig|504728.9.peg.2901; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; EREVIIT; -. DR Proteomes; UP000013026; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000013026}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000013026}. FT DOMAIN 376 539 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 335 369 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 560 AA; 61173 MW; BF6179D95AC757D9 CRC64; MEKIFGRTNG LKPSEKKRLA NLYNRRVGAN RLLTAELART MAALSGELGK PISLLLDRGG RVMRVAVGDA KELPVPERAL VETRLSGYRI LHTHLGSGGL SRPDLSVLFL HRLDAMAALE VEQGHPGRLH LAQLSPPKAD EEDWQIFPSK PYHEYLEWDL AASVAALEEE LSRQARGLDL RDGSGERAVL VGIDQGEGVQ AEVDLAELAE LARTAGAVVA HKELVFRPSL DPRYAVGRGK VEELVSHAYH QNAGTLIFGI DLSAAQAREL ETITGLKVLD RTQLILDIFA QHARTPEAKV QVELAQLKYL LPRLVGKGKE LSRLGGGIGT RGPGETKLEV DRRRLQDRIA ELTRKLQEIA GRRQETRRQR DKSGLPIVGV VGYTNAGKTT LMHALAKKGD EGENKLFATL RPLTRRGFLP GIGEVLFTDT VGFIRHMPGD LLEAFRSTLE ELRDADVLLH VLDASQEGAL ERYQVVEDLL AELGVESPQV LVLSKADAAD GYDLEFLRER LGGFPVSAVR GQGLGELKQA VAEALLAQGV RPAAWAYPPR EPGVAAALTD // ID D3Q6G5_STANL Unreviewed; 466 AA. AC D3Q6G5; DT 20-APR-2010, integrated into UniProtKB/TrEMBL. DT 20-APR-2010, sequence version 1. DT 07-JUN-2017, entry version 60. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Snas_4564 {ECO:0000313|EMBL:ADD44208.1}; OS Stackebrandtia nassauensis (strain DSM 44728 / NRRL B-16338 / NBRC OS 102104 / LLR-40K-21). OC Bacteria; Actinobacteria; Glycomycetales; Glycomycetaceae; OC Stackebrandtia. OX NCBI_TaxID=446470 {ECO:0000313|EMBL:ADD44208.1, ECO:0000313|Proteomes:UP000000844}; RN [1] {ECO:0000313|EMBL:ADD44208.1, ECO:0000313|Proteomes:UP000000844} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 44728 / NRRL B-16338 / NBRC 102104 / LLR-40K-21 RC {ECO:0000313|Proteomes:UP000000844}; RX PubMed=21304662; DOI=10.4056/sigs.47643; RA Munk C., Lapidus A., Copeland A., Jando M., Mayilraj S., RA Glavina Del Rio T., Nolan M., Chen F., Lucas S., Tice H., Cheng J.F., RA Han C., Detter J.C., Bruce D., Goodwin L., Chain P., Pitluck S., RA Goker M., Ovchinikova G., Pati A., Ivanova N., Mavromatis K., Chen A., RA Palaniappan K., Land M., Hauser L., Chang Y.J., Jeffries C.D., RA Bristow J., Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., RA Klenk H.P.; RT "Complete genome sequence of Stackebrandtia nassauensis type strain RT (LLR-40K-21)."; RL Stand. Genomic Sci. 1:292-299(2009). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001778; ADD44208.1; -; Genomic_DNA. DR RefSeq; WP_013019779.1; NC_013947.1. DR ProteinModelPortal; D3Q6G5; -. DR STRING; 446470.Snas_4564; -. DR EnsemblBacteria; ADD44208; ADD44208; Snas_4564. DR KEGG; sna:Snas_4564; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000000844; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 2. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000000844}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000000844}. FT DOMAIN 245 410 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 466 AA; 50454 MW; 1EB39AF40824A7D6 CRC64; MPTNDTELPD TGQLALEERH ALRRVAGLST ELTDVTEVEY RQLRLERVVL VGVWTKGTLT EAENSLAELA ALAETAGSQV LDGLIQRRKS PDPATFVGRG KVDELTEAVT ASGADTVICD GELSPSQLRN LEAEIKVKVI DRTALILDIF AQHATSREGK AQVELAQLEY LVPRLRGWGE TLSRQAGGRA GGAGGGVGLR GPGETKLETD RRRIRTRIAK LRRDIAKLRT VRDTKRSSRR RHSVPSVAIA GYTNAGKSSL LNRLTGAGVL VEDALFATLD PTTRRARTGD GRDYTLSDTV GFVSHLPHQL VDAFRSTLEE VADADLIVHV IDGSHPDPGA QVRAVREVLN DVGADAVPEV LVVNKIDRAG SEALLTLRTD WPDAVFVSAH TGEGVDKLRD VIEERLPRPA VPLLVCVPYV RGDLAARVRQ RGQVRSIDHR GDGTVMDVLV DEALAAELAP FVIDTP // ID D3QZU8_MAGIU Unreviewed; 403 AA. AC D3QZU8; DT 20-APR-2010, integrated into UniProtKB/TrEMBL. DT 20-APR-2010, sequence version 1. DT 05-JUL-2017, entry version 58. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:ADC90601.1}; GN OrderedLocusNames=HMPREF0868_0103 {ECO:0000313|EMBL:ADC90601.1}; OS Mageeibacillus indolicus (strain UPII9-5) (Clostridiales genomosp. OS BVAB3 (strain UPII9-5)). OC Bacteria; Firmicutes; Clostridia; Clostridiales; Ruminococcaceae; OC Mageeibacillus. OX NCBI_TaxID=699246 {ECO:0000313|EMBL:ADC90601.1, ECO:0000313|Proteomes:UP000008234}; RN [1] {ECO:0000313|Proteomes:UP000008234} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=UPII9-5 {ECO:0000313|Proteomes:UP000008234}; RA Madupu R., Durkin A.S., Torralba M., Methe B., Sutton G.G., RA Strausberg R.L., Nelson K.E.; RT "Sequence of Clostridiales genomosp. BVAB3 str. UPII9-5."; RL Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001850; ADC90601.1; -; Genomic_DNA. DR ProteinModelPortal; D3QZU8; -. DR STRING; 699246.HMPREF0868_0103; -. DR EnsemblBacteria; ADC90601; ADC90601; HMPREF0868_0103. DR KEGG; clo:HMPREF0868_0103; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000008234; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000008234}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000008234}. FT DOMAIN 206 394 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 403 AA; 44744 MW; 3CAE27CE245DBF77 CRC64; MKESKPLFTV GKEKAILMAL APDQRTLEKE VLPSLDELAA LTETCGGEVV AVVTQLRPAR EAAFYLGKGK IDEIKDLGAK LEADILICDD ELTGSQMRRL EAMTGLRVLD RTLVILDIFA KRAQSREGKI QVELAQQEYR LSRLTQEEGE LSRLGGGIGT RGPGETKLES DRRHIHRRIN QLKNDLVSVA EHRERLRAAR RRSGSYTVAV VGYTNAGKTT LVNNLCKADL TAANQLFATL DPAARKMNVT SEEIFAVTQD YSCYFAPVLV DTVGFIRRLP HTLINAFHST LQEATEADIL LHVVNAADKE AVRQFEVAEK LLRELGADKI PGIIVLNKVD LITSPEQQEQ LAALTALAHH TTEAESSCVE ISAKNGEGLS DLRRLILQRC YESRRSVLRR KRV // ID D3RSK5_ALLVD Unreviewed; 443 AA. AC D3RSK5; DT 20-APR-2010, integrated into UniProtKB/TrEMBL. DT 20-APR-2010, sequence version 1. DT 07-JUN-2017, entry version 49. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Alvin_1225 {ECO:0000313|EMBL:ADC62164.1}; OS Allochromatium vinosum (strain ATCC 17899 / DSM 180 / NBRC 103801 / OS NCIMB 10441 / D) (Chromatium vinosum). OC Bacteria; Proteobacteria; Gammaproteobacteria; Chromatiales; OC Chromatiaceae; Allochromatium. OX NCBI_TaxID=572477 {ECO:0000313|EMBL:ADC62164.1, ECO:0000313|Proteomes:UP000001441}; RN [1] {ECO:0000313|EMBL:ADC62164.1, ECO:0000313|Proteomes:UP000001441} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 17899 / DSM 180 / NBRC 103801 / NCIMB 10441 / D RC {ECO:0000313|Proteomes:UP000001441}; RX PubMed=22675582; DOI=10.4056/sigs.2335270; RA Weissgerber T., Zigann R., Bruce D., Chang Y.J., Detter J.C., Han C., RA Hauser L., Jeffries C.D., Land M., Munk A.C., Tapia R., Dahl C.; RT "Complete genome sequence of Allochromatium vinosum DSM 180(T)."; RL Stand. Genomic Sci. 5:311-330(2011). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001896; ADC62164.1; -; Genomic_DNA. DR ProteinModelPortal; D3RSK5; -. DR STRING; 572477.Alvin_1225; -. DR EnsemblBacteria; ADC62164; ADC62164; Alvin_1225. DR KEGG; alv:Alvin_1225; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000001441; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000001441}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000001441}. FT DOMAIN 222 389 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 188 215 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 443 AA; 48790 MW; 38EEC686C782B856 CRC64; MNDTPVAVPS VEARPVAVGP SLVFERPKAG ERAVLVDLDI GRGPASEADE REEFVLLAQA AGAEVVGSIG GSRATPDSRL FIGSGKAEEL RALVAATESE LVIFNHPLSP AQERNLERLL QCRVIDRSGL ILDIFAQRAR SFEGKLQVEL AQLKHLSTRL VRGWTHLERQ KGGIGLRGPG ETQLETDRRL LATRVAMLER RLQRIEGQRA QGRKARAKAE LPVVSLVGYT NAGKSTLFNG LTEAGVLEAD QLFATLDPTL RRLDLPSGGH VLLADTVGFV SRLPHELVAA FRSTLEETRG ASLLLHVIDA AAANRPRLMA DVETVLAEIG SHERPRLEVF NKIDRLEGET ARLERDAEGR PVRVWVSART GEGLDLLRQA LIELTGGERL IETFDLDATD GRRRAWLYQH ARVIEDRPLD SGGWKLRCEI ARVDLERLRA RLP // ID D3SEG7_THISK Unreviewed; 441 AA. AC D3SEG7; DT 20-APR-2010, integrated into UniProtKB/TrEMBL. DT 20-APR-2010, sequence version 1. DT 07-JUN-2017, entry version 49. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=TK90_0497 {ECO:0000313|EMBL:ADC71012.1}; OS Thioalkalivibrio sp. (strain K90mix). OC Bacteria; Proteobacteria; Gammaproteobacteria; Chromatiales; OC Ectothiorhodospiraceae; Thioalkalivibrio. OX NCBI_TaxID=396595 {ECO:0000313|EMBL:ADC71012.1, ECO:0000313|Proteomes:UP000009099}; RN [1] {ECO:0000313|Proteomes:UP000009099} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K90mix {ECO:0000313|Proteomes:UP000009099}; RG US DOE Joint Genome Institute; RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L., RA Pitluck S., Foster B., Sun H., Larimer F., Land M., Hauser L., RA Kyrpides N., Ivanova N., Sorokin D.Y., Muyzer G., Woyke T.; RT "Complete sequence of chromosome of Thioalkalivibrio sp. K90mix."; RL Submitted (FEB-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001905; ADC71012.1; -; Genomic_DNA. DR RefSeq; WP_012981910.1; NC_013889.1. DR ProteinModelPortal; D3SEG7; -. DR STRING; 396595.TK90_0497; -. DR EnsemblBacteria; ADC71012; ADC71012; TK90_0497. DR KEGG; tkm:TK90_0497; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000009099; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000009099}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000009099}. FT DOMAIN 200 367 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 166 193 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 441 AA; 49272 MW; 5B5FCC62CBC591C5 CRC64; MFERPDSAGD RAVLVALAIG ENPDIEAQVQ EFDELVRSAG ADVLELVRGS RDRPHPRLFV GAGKADEIRA AVEAHGADVV IFNHALSPSQ ERNLERHLQC RVLDRAGLIL DIFAQRARSH EGKLQVELAQ LRHMATRLVR GWTHLERQKG GIGLRGPGET QLETDRRLLA ARIKHIERRL EKVERTREQG RQARLRNEIP TVSLVGYTNA GKSTLFNRLT HSDVYEADQL FATLDPTLRR LDLAPHQSLI LADTVGFVRD LPHELVAAFK ATLTETREAA LLLHVIDAAD PEREARIRQV EAVLEEIGAQ DVPCWRVYNK IDRLESTPDA AEARFGSGDD VFWVSAYTGE GIATLEEHLA ETFTESMMRG WVELPASAGR LRAQLYEEKA VEAEQTTADG QIQLRLSLPQ RRFQQLVSDA GLNPEQIEIV FDEPSSTAVG Q // ID D3SNH8_THEAH Unreviewed; 368 AA. AC D3SNH8; DT 20-APR-2010, integrated into UniProtKB/TrEMBL. DT 20-APR-2010, sequence version 1. DT 07-JUN-2017, entry version 56. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Thal_0077 {ECO:0000313|EMBL:ADC88715.1}; OS Thermocrinis albus (strain DSM 14484 / JCM 11386 / HI 11/12). OC Bacteria; Aquificae; Aquificales; Aquificaceae; Thermocrinis. OX NCBI_TaxID=638303 {ECO:0000313|EMBL:ADC88715.1, ECO:0000313|Proteomes:UP000002043}; RN [1] {ECO:0000313|Proteomes:UP000002043} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 14484 / JCM 11386 / HI 11/12 RC {ECO:0000313|Proteomes:UP000002043}; RA Wirth R., Sikorski J., Brambilla E., Misra M., Lapidus A., RA Copeland A., Nolan M., Lucas S., Chen F., Tice H., Cheng J.F., Han C., RA Detter J.C., Tapia R., Bruce D., Goodwin L., Pitluck S., Pati A., RA Anderson I., Ivanova N., Mavromatis K., Mikhailova N., Chen A., RA Palaniappan K., Bilek Y., Hader T., Land M., Hauser L., Chang Y.J., RA Jeffries C.D., Tindall B.J., Rohde M., Goker M., Bristow J., RA Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.; RT "Complete genome sequence of Thermocrinis albus type strain (HI RT 11/12T)."; RL Stand. Genomic Sci. 2:194-202(2010). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001931; ADC88715.1; -; Genomic_DNA. DR RefSeq; WP_012991122.1; NC_013894.1. DR ProteinModelPortal; D3SNH8; -. DR STRING; 638303.Thal_0077; -. DR EnsemblBacteria; ADC88715; ADC88715; Thal_0077. DR KEGG; tal:Thal_0077; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000002043; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000002043}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000002043}. FT DOMAIN 196 366 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 151 192 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 368 AA; 41865 MW; 3366809826644E2F CRC64; MKAILVGIIE REDKKSFRES LEELRELVRA VGGKVIGYIY QRRNSPDVRY FVGAGKAKEI QEVVKGTGAD TVVFDTFLTP SQVQNLEDLI DARIMDRGTL VLEIFSRRVR SKTAKLQVEL ATLTYQLPRL YGKGREMSRL GGGVGTRGPG EQETEIKRRA IKRRIQQIKE ELEEIKRQRR EQRKRRERYG SDLKVVRVAL VGYTNVGKSS LMKVLTGRDV LSADMPFATL DTTTSARLLF PDLKILFTDT VGFIRKLPPE LIESFKATLE EVQEADIILH VVDISDSSWI EKVKVVQQVL ADLSADEKPV IYVFNKADKL VKEEEQLHEL RQQFLMDAPA VIVSAQKGWG IRELLDTIKQ VVQQVVKV // ID D3SSM3_NATMM Unreviewed; 433 AA. AC D3SSM3; DT 20-APR-2010, integrated into UniProtKB/TrEMBL. DT 20-APR-2010, sequence version 1. DT 07-JUN-2017, entry version 58. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:ADD06868.1}; GN OrderedLocusNames=Nmag_3318 {ECO:0000313|EMBL:ADD06868.1}; GN ORFNames=C500_13632 {ECO:0000313|EMBL:ELY28406.1}; OS Natrialba magadii (strain ATCC 43099 / DSM 3394 / CIP 104546 / JCM OS 8861/ NBRC 102185 / NCIMB 2190 / MS3) (Natronobacterium magadii). OC Archaea; Euryarchaeota; Halobacteria; Natrialbales; Natrialbaceae; OC Natrialba. OX NCBI_TaxID=547559 {ECO:0000313|EMBL:ADD06868.1, ECO:0000313|Proteomes:UP000001879}; RN [1] {ECO:0000313|Proteomes:UP000001879} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43099 / DSM 3394 / CIP 104546 / JCM 8861/ NBRC 102185 / RC NCIMB 2190 / MS3 {ECO:0000313|Proteomes:UP000001879}; RG US DOE Joint Genome Institute; RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L., RA Pitluck S., Davenport K., Saunders E., Detter J.C., Han C., Tapia R., RA Land M., Hauser L., Kyrpides N., Mikhailova N., De Castro R.E., RA Maupin-Furlow J.A., Woyke T.; RT "Complete sequence of chromosome of Natrialba magadii ATCC 43099."; RL Submitted (FEB-2010) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:ADD06868.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 43099 {ECO:0000313|EMBL:ADD06868.1}; RX PubMed=22559199; DOI=10.1186/1471-2164-13-165; RA Siddaramappa S., Challacombe J.F., Decastro R.E., Pfeiffer F., RA Sastre D.E., Gimenez M.I., Paggi R.A., Detter J.C., Davenport K.W., RA Goodwin L.A., Kyrpides N., Tapia R., Pitluck S., Lucas S., Woyke T., RA Maupin-Furlow J.A.; RT "A comparative genomics perspective on the genetic content of the RT alkaliphilic haloarchaeon Natrialba magadii ATCC 43099T."; RL BMC Genomics 13:165-165(2012). RN [3] {ECO:0000313|Proteomes:UP000011543} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43099 / DSM 3394 / CIP 104546 / JCM 8861/ NBRC 102185 / RC NCIMB 2190 / MS3 {ECO:0000313|Proteomes:UP000011543}; RA Becker E.A., Seitzer P., Tritt A., Larsen D., Yao A., Wu D., RA Darling A., Eisen J.A., Facciotti M.T.; RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases. RN [4] {ECO:0000313|EMBL:ELY28406.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=MS-3 {ECO:0000313|EMBL:ELY28406.1}; RX PubMed=25393412; RA Becker E.A., Seitzer P.M., Tritt A., Larsen D., Krusor M., Yao A.I., RA Wu D., Madern D., Eisen J.A., Darling A.E., Facciotti M.T.; RT "Phylogenetically driven sequencing of extremely halophilic archaea RT reveals strategies for static and dynamic osmo-response."; RL PLoS Genet. 10:E1004784-E1004784(2014). RN [5] {ECO:0000313|EMBL:ADD06868.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 43099 {ECO:0000313|EMBL:ADD06868.1}; RA Capua I., De Benedictis P., Joannis T., Lombin L.H., Cattoli G.; RL Submitted (SEP-2016) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001932; ADD06868.1; -; Genomic_DNA. DR EMBL; AOHS01000042; ELY28406.1; -; Genomic_DNA. DR RefSeq; WP_004215904.1; NZ_AOHS01000042.1. DR STRING; 547559.Nmag_3318; -. DR EnsemblBacteria; ADD06868; ADD06868; Nmag_3318. DR EnsemblBacteria; ELY28406; ELY28406; C500_13632. DR GeneID; 8826182; -. DR KEGG; nmg:Nmag_3318; -. DR PATRIC; fig|547559.17.peg.2698; -. DR eggNOG; arCOG00353; Archaea. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG093Z07D6; -. DR Proteomes; UP000001879; Chromosome. DR Proteomes; UP000011543; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000001879}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000001879}. FT DOMAIN 186 369 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 102 129 {ECO:0000256|SAM:Coils}. FT COILED 152 175 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 433 AA; 48346 MW; 59FED75A7545454A CRC64; MRAIIAKRVD SGTPDTTEIS DLAAAAGYTV AGEVTQSRRA DPALQLGEGK AEELAEVVEA TEATTVIFDN RLGPYQTYNL GQLLPEGVEV IDRFTLILEI FGQRAQTRKA QLQVELAELR YELPRAEAKT SLAKRDEHPG FMGLGEYDES REQDIKNQIS RINDELERIE QTEEHRRERR RDSGFDLVAL AGYTNAGKST LLRRLSEDLD VDENEDLHQD LDATAESQDK LFTTLGTTTR RAAIEPRDVL VTDTVGFISD LPHWLVESFK STLDSVYRAD LVLLVVDVSE DVDDIHEKLV TSHDTLYERN EAPIVTVLNK IDAVDEAELE EKREALSALA PNPVTVSAQE GQNIDALLDR IDDELPDWEE ERLMLPMTDE TMSVVSWIHD NAHVDDVTYG DEDVLVSFEA RPAVISQART RASELQATVA DSA // ID D3SXQ8_NATMM Unreviewed; 469 AA. AC D3SXQ8; DT 20-APR-2010, integrated into UniProtKB/TrEMBL. DT 20-APR-2010, sequence version 1. DT 07-JUN-2017, entry version 52. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Nmag_2447 {ECO:0000313|EMBL:ADD06007.1}; OS Natrialba magadii (strain ATCC 43099 / DSM 3394 / CIP 104546 / JCM OS 8861/ NBRC 102185 / NCIMB 2190 / MS3) (Natronobacterium magadii). OC Archaea; Euryarchaeota; Halobacteria; Natrialbales; Natrialbaceae; OC Natrialba. OX NCBI_TaxID=547559 {ECO:0000313|EMBL:ADD06007.1, ECO:0000313|Proteomes:UP000001879}; RN [1] {ECO:0000313|Proteomes:UP000001879} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43099 / DSM 3394 / CIP 104546 / JCM 8861/ NBRC 102185 / RC NCIMB 2190 / MS3 {ECO:0000313|Proteomes:UP000001879}; RG US DOE Joint Genome Institute; RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L., RA Pitluck S., Davenport K., Saunders E., Detter J.C., Han C., Tapia R., RA Land M., Hauser L., Kyrpides N., Mikhailova N., De Castro R.E., RA Maupin-Furlow J.A., Woyke T.; RT "Complete sequence of chromosome of Natrialba magadii ATCC 43099."; RL Submitted (FEB-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001932; ADD06007.1; -; Genomic_DNA. DR RefSeq; WP_012996677.1; NZ_AOHS01000030.1. DR ProteinModelPortal; D3SXQ8; -. DR STRING; 547559.Nmag_2447; -. DR EnsemblBacteria; ADD06007; ADD06007; Nmag_2447. DR GeneID; 8825300; -. DR KEGG; nmg:Nmag_2447; -. DR eggNOG; arCOG00353; Archaea. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; FNNHAHV; -. DR OrthoDB; POG093Z07D6; -. DR Proteomes; UP000001879; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000001879}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000001879}. FT DOMAIN 215 410 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 469 AA; 51226 MW; DA3099A0A4220482 CRC64; MSRSRTHNTP NRTVVASRLD AAAKSNETDD TDQTGQVGGT DQTDQTNQTD QTDEIAALVR AAGDEVVATI TQAGRENPGS YLGHGKVDEL AETVAATDAN RVVVDDELTP SQHHTLESAM PADTAVLDRH RLVLEIFEAG AGSRRAKLQV ELAQLRYDLP RLIESADEGL LNKQTEKGSP VYDVRDRIDR LERKLEERPE PAARFRERRR EEGFDLVTCA GYTNAGKSTL LHRLADELSI SDANSSSKSN DDSSDKDATA AVRDRLFETL ETTTRRATID GRPVLVTDTV GFVDDLPHDL VESFSATLSE AGAADVVVLV VDASDPESRF RARLEVALDV LDAQTVADDR IVPALNKVDC LSADESARRL TIAAAHLPDA AADPIPVSVL EGTNLSRLCE TILERLPTET ANLRVPNCDD AMALVSRAYD RTSVETVDYD DTVTIRCRGP PRILEQLRAR ADRITAEHR // ID D3TB77_ACIB4 Unreviewed; 405 AA. AC D3TB77; DT 20-APR-2010, integrated into UniProtKB/TrEMBL. DT 20-APR-2010, sequence version 1. DT 07-JUN-2017, entry version 56. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Aboo_1550 {ECO:0000313|EMBL:ADD09356.1}; OS Aciduliprofundum boonei (strain DSM 19572 / T469). OC Archaea; Euryarchaeota; DHVE2 group; Aciduliprofundum. OX NCBI_TaxID=439481 {ECO:0000313|EMBL:ADD09356.1, ECO:0000313|Proteomes:UP000001400}; RN [1] {ECO:0000313|Proteomes:UP000001400} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 19572 / T469 {ECO:0000313|Proteomes:UP000001400}; RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L., RA Pitluck S., Saunders E., Detter J.C., Han C., Tapia R., Land M., RA Hauser L., Kyrpides N., Mikhailova N., Flores G., Reysenbach A.-L., RA Woyke T.; RT "Complete sequence of Aciduliprofundum boonei T469."; RL Submitted (FEB-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001941; ADD09356.1; -; Genomic_DNA. DR RefSeq; WP_012997489.1; NC_013926.1. DR ProteinModelPortal; D3TB77; -. DR STRING; 439481.Aboo_1550; -. DR EnsemblBacteria; ADD09356; ADD09356; Aboo_1550. DR GeneID; 8828521; -. DR KEGG; abi:Aboo_1550; -. DR eggNOG; arCOG00353; Archaea. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; FNNHAHV; -. DR OrthoDB; POG093Z07D6; -. DR Proteomes; UP000001400; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000001400}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000001400}. FT DOMAIN 180 343 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 146 173 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 405 AA; 47076 MW; 0F549C3074ACE867 CRC64; MPDVIVVFDG NEEFEELVKS LGYEIVAKVY FKNKVNPKYY ISKGKIEEIK NLLKDFNVEK IIIDAILKSS QWYKLEKELK IRVDDRIKLI IDIFADRARS REAMMQVEYA NLKYETSHIK ELIHQIRLGE HPGFMGGGEY EIADYYEQIR RKMARIRKEL EKLKVHREER RKRRKEEGYI LVGIAGYTNT GKSTLLKALS GRDVVIENRM FSTLSTRTSK IGKEKILITD TVGFVENMPP WLIRAFEPTL EEIYKADIVL LLLNCQESIE DFKRKMQVSL EILEGKSEGK IIPVINKIDS CKDLDEKIKI AKEIGEPIAI SALRGIGIED VIRRIKDEMK IEKFYAEVEK DSKAYNFIIK HGKIIKIEAD EMMKIIFEMP ISKYSALKDL IREISTGNDG VLKRI // ID D3UYU4_XENBS Unreviewed; 426 AA. AC D3UYU4; DT 20-APR-2010, integrated into UniProtKB/TrEMBL. DT 20-APR-2010, sequence version 1. DT 30-AUG-2017, entry version 54. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:CBJ79472.1}; GN OrderedLocusNames=XBJ1_0322 {ECO:0000313|EMBL:CBJ79472.1}; OS Xenorhabdus bovienii (strain SS-2004). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; OC Morganellaceae; Xenorhabdus. OX NCBI_TaxID=406818 {ECO:0000313|EMBL:CBJ79472.1, ECO:0000313|Proteomes:UP000002045}; RN [1] {ECO:0000313|Proteomes:UP000002045} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SS-2004 {ECO:0000313|Proteomes:UP000002045}; RA Goodrich-Blair H., Barbazuk B., Bode H.B., Darby C., Du Z., Forst S., RA Gaudriault S., Goldman B.S., Goodner B., Henkhaus J., Latreille P., RA Medigue C., Miller N., Norton S., Ogier J.C., Rouy Z., Slater S., RA Suen G.; RT "Complete genome sequence of Xenorhabdus nematophila (strain ATCC RT 19061 / DSM 3370 / LMG 1036 / NCIB 9965 / AN6)."; RL Submitted (FEB-2010) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:CBJ79472.1, ECO:0000313|Proteomes:UP000002045} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SS-2004 {ECO:0000313|EMBL:CBJ79472.1, RC ECO:0000313|Proteomes:UP000002045}; RX PubMed=22125637; DOI=10.1371/journal.pone.0027909; RA Chaston J.M., Suen G., Tucker S.L., Andersen A.W., Bhasin A., Bode E., RA Bode H.B., Brachmann A.O., Cowles C.E., Cowles K.N., Darby C., RA de Leon L., Drace K., Du Z., Givaudan A., Herbert Tran E.E., RA Jewell K.A., Knack J.J., Krasomil-Osterfeld K.C., Kukor R., Lanois A., RA Latreille P., Leimgruber N.K., Lipke C.M., Liu R., Lu X., RA Martens E.C., Marri P.R., Medigue C., Menard M.L., Miller N.M., RA Morales-Soto N., Norton S., Ogier J.C., Orchard S.S., Park D., RA Park Y., Qurollo B.A., Sugar D.R., Richards G.R., Rouy Z., RA Slominski B., Slominski K., Snyder H., Tjaden B.C., van der Hoeven R., RA Welch R.D., Wheeler C., Xiang B., Barbazuk B., Gaudriault S., RA Goodner B., Slater S.C., Forst S., Goldman B.S., Goodrich-Blair H.; RT "The entomopathogenic bacterial endosymbionts xenorhabdus and RT photorhabdus: convergent lifestyles from divergent genomes."; RL PLoS ONE 6:e27909-e27909(2011). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; FN667741; CBJ79472.1; -; Genomic_DNA. DR RefSeq; WP_012986932.1; NC_013892.1. DR ProteinModelPortal; D3UYU4; -. DR STRING; 406818.XBJ1_0322; -. DR EnsemblBacteria; CBJ79472; CBJ79472; XBJ1_0322. DR GeneID; 8829947; -. DR KEGG; xbo:XBJ1_0322; -. DR PATRIC; fig|406818.4.peg.293; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000002045; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000002045}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Hydrolase {ECO:0000313|EMBL:CBJ79472.1}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Protease {ECO:0000313|EMBL:CBJ79472.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000002045}. FT DOMAIN 198 365 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 426 AA; 47995 MW; B9BFAF176D27185E CRC64; MFDRYEGGEL AVLVHVFFSQ EKDTENLSEF ESLVTSAGVS PVQIVTGSRK APNPKYFVGE GKAEEIAEAV KNSGADVVLF NHALSPAQER NLERLCQCRV VDRTGVILDI FAQRARTHEG KLQVELAQLR HLSTRLVRGW THLERQKGGI GLRGPGETQL ETDRRLLRDK IKQILGRLGK VEKQREQGRQ ARNKADIPTV SLVGYTNAGK SSLFNRITSA EVYTADQLFA TLDPTLRRID VNDVGTVVLA DTVGFIRHLP HDLVAAFKAT LQETRQARLL LHVVDAADSR LDENIVAVDS VLEEIEANEI PSLLVMNKID MLEDFVPRID RDEENRPIRV WLSAQTGAGI PLLFQVLTEC LSGEIAHYEL HLPPEAGRLR SRFYQLQAIE REWIEDGGQI GIEVRMPMVD WRRLCKQELN LLDYVV // ID D3VII0_XENNA Unreviewed; 426 AA. AC D3VII0; DT 20-APR-2010, integrated into UniProtKB/TrEMBL. DT 20-APR-2010, sequence version 1. DT 30-AUG-2017, entry version 52. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:CBJ88530.1}; GN OrderedLocusNames=XNC1_0456 {ECO:0000313|EMBL:CBJ88530.1}; OS Xenorhabdus nematophila (strain ATCC 19061 / DSM 3370 / LMG 1036 / OS NCIB 9965 / AN6). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; OC Morganellaceae; Xenorhabdus. OX NCBI_TaxID=406817 {ECO:0000313|EMBL:CBJ88530.1, ECO:0000313|Proteomes:UP000008075}; RN [1] {ECO:0000313|Proteomes:UP000008075} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 19061 / DSM 3370 / LMG 1036 / NCIB 9965 / AN6 RC {ECO:0000313|Proteomes:UP000008075}; RA Goodrich-Blair H., Barbazuk B., Bode H.B., Darby C., Du Z., Forst S., RA Gaudriault S., Goldman B.S., Goodner B., Henkhaus J., Latreille P., RA Medigue C., Miller N., Norton S., Ogier J.C., Rouy Z., Slater S., RA Suen G.; RT "Complete genome sequence of Xenorhabdus nematophila (strain ATCC RT 19061 / DSM 3370 / LMG 1036 / NCIB 9965 / AN6)."; RL Submitted (FEB-2010) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:CBJ88530.1, ECO:0000313|Proteomes:UP000008075} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 19061 / DSM 3370 / LMG 1036 / NCIB 9965 / AN6 RC {ECO:0000313|Proteomes:UP000008075}; RX PubMed=22125637; DOI=10.1371/journal.pone.0027909; RA Chaston J.M., Suen G., Tucker S.L., Andersen A.W., Bhasin A., Bode E., RA Bode H.B., Brachmann A.O., Cowles C.E., Cowles K.N., Darby C., RA de Leon L., Drace K., Du Z., Givaudan A., Herbert Tran E.E., RA Jewell K.A., Knack J.J., Krasomil-Osterfeld K.C., Kukor R., Lanois A., RA Latreille P., Leimgruber N.K., Lipke C.M., Liu R., Lu X., RA Martens E.C., Marri P.R., Medigue C., Menard M.L., Miller N.M., RA Morales-Soto N., Norton S., Ogier J.C., Orchard S.S., Park D., RA Park Y., Qurollo B.A., Sugar D.R., Richards G.R., Rouy Z., RA Slominski B., Slominski K., Snyder H., Tjaden B.C., van der Hoeven R., RA Welch R.D., Wheeler C., Xiang B., Barbazuk B., Gaudriault S., RA Goodner B., Slater S.C., Forst S., Goldman B.S., Goodrich-Blair H.; RT "The entomopathogenic bacterial endosymbionts xenorhabdus and RT photorhabdus: convergent lifestyles from divergent genomes."; RL PLoS ONE 6:e27909-e27909(2011). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; FN667742; CBJ88530.1; -; Genomic_DNA. DR RefSeq; WP_013183278.1; NC_014228.1. DR ProteinModelPortal; D3VII0; -. DR STRING; 406817.XNC1_0456; -. DR EnsemblBacteria; CBJ88530; CBJ88530; XNC1_0456. DR KEGG; xne:XNC1_0456; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000008075; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000008075}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Hydrolase {ECO:0000313|EMBL:CBJ88530.1}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Protease {ECO:0000313|EMBL:CBJ88530.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008075}. FT DOMAIN 198 365 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 426 AA; 48112 MW; A38181FFDC5D7D57 CRC64; MFDRYEGGEL AVLVHVFFSQ EKDTENLSEF ESLVTSAGVS PVQIVTGSRK APHPKYFVGE GKAEEIAEAV KNSGADVVLF NHTLSPAQER NLERLCQCRV VDRTGVILDI FAQRARTHEG KLQVELAQLR HLSTRLVRGW THLERQKGGI GLRGPGETQL ESDRRMLRDK IKQILGRLSK VEKQREQGRQ ARNKADIPTV SLVGYTNAGK SSLFNSITSA KVYAADQLFA TLDPTLRRID VDDVGTVVLA DTVGFIRHLP HDLVAAFKAT LQETRQAKLL LHVVDAADHR LDENIIAVDS VLEEIESNEI PSLMVMNKID MLEDFTPRID RDEENRPVRV WLSAQTGEGI SLLLQALTER LSGETAHYEL HLPPEAGRLR SRFYQLQAIE REWMEEDGQV GLEVRMPMVD WRRLCKQEPN LPDYVV // ID D3YW02_MOUSE Unreviewed; 221 AA. AC D3YW02; DT 20-APR-2010, integrated into UniProtKB/TrEMBL. DT 20-APR-2010, sequence version 1. DT 05-JUL-2017, entry version 40. DE SubName: Full=Putative GTP-binding protein 6 {ECO:0000313|Ensembl:ENSMUSP00000117817}; DE Flags: Fragment; GN Name=Gtpbp6 {ECO:0000313|Ensembl:ENSMUSP00000117817, GN ECO:0000313|MGI:MGI:1306825}; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090 {ECO:0000313|Ensembl:ENSMUSP00000117817, ECO:0000313|Proteomes:UP000000589}; RN [1] {ECO:0000313|Ensembl:ENSMUSP00000117817, ECO:0000313|Proteomes:UP000000589} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000117817, RC ECO:0000313|Proteomes:UP000000589}; RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112; RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., RA She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., RA Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., RA Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J., RA Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., RA Lindblad-Toh K., Eichler E.E., Ponting C.P.; RT "Lineage-specific biology revealed by a finished genome assembly of RT the mouse."; RL PLoS Biol. 7:E1000112-E1000112(2009). RN [2] {ECO:0000213|PubMed:21183079} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001; RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R., RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.; RT "A tissue-specific atlas of mouse protein phosphorylation and RT expression."; RL Cell 143:1174-1189(2010). RN [3] {ECO:0000313|Ensembl:ENSMUSP00000117817} RP IDENTIFICATION. RC STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000117817}; RG Ensembl; RL Submitted (MAY-2011) to UniProtKB. CC -!- CAUTION: The sequence shown here is derived from an Ensembl CC automatic analysis pipeline and should be considered as CC preliminary data. {ECO:0000313|Ensembl:ENSMUSP00000117817}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AC166747; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR MaxQB; D3YW02; -. DR PaxDb; D3YW02; -. DR PeptideAtlas; D3YW02; -. DR Ensembl; ENSMUST00000135409; ENSMUSP00000117817; ENSMUSG00000033434. DR MGI; MGI:1306825; Gtpbp6. DR eggNOG; KOG0410; Eukaryota. DR eggNOG; COG2262; LUCA. DR GeneTree; ENSGT00390000001397; -. DR HOGENOM; HOG000260368; -. DR Proteomes; UP000000589; Chromosome 5. DR Bgee; ENSMUSG00000033434; -. DR ExpressionAtlas; D3YW02; baseline and differential. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. PE 1: Evidence at protein level; KW Complete proteome {ECO:0000313|Proteomes:UP000000589}; KW Proteomics identification {ECO:0000213|MaxQB:D3YW02, KW ECO:0000213|PeptideAtlas:D3YW02}; KW Reference proteome {ECO:0000313|Proteomes:UP000000589}. FT DOMAIN 46 134 GTP-bdg_N. {ECO:0000259|Pfam:PF13167}. FT DOMAIN 138 216 GTP-bdg_M. {ECO:0000259|Pfam:PF16360}. FT NON_TER 221 221 {ECO:0000313|Ensembl:ENSMUSP00000117817}. SQ SEQUENCE 221 AA; 25193 MW; 2D2A96F5A4CB3437 CRC64; MVWAGDADSA RARFHPRANP VHRRGPRSSR SALDWMDPCV LTAEWQVAEA AALVRALPGW SVASTLVVPS AAPGSRLVFG KGNFQDVTEK IKGCQDITSV FLNVERMAPP TKKELESAWG LRVFDRFTLV LHIFRCNART REARMQLALA EIPLLRSSVN TDSGQQDQQG WGSRYIMGSG ESPTELRARA LRDRELRLRR VLERLRDKRR LMRKERVRRE F // ID D3ZLF0_RAT Unreviewed; 513 AA. AC D3ZLF0; D4A5V5; DT 20-APR-2010, integrated into UniProtKB/TrEMBL. DT 20-APR-2010, sequence version 1. DT 07-JUN-2017, entry version 61. DE SubName: Full=GTP-binding protein 6 (putative) {ECO:0000313|Ensembl:ENSRNOP00000053471}; GN Name=Gtpbp6 {ECO:0000313|Ensembl:ENSRNOP00000053471, GN ECO:0000313|RGD:1305954}; OS Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; OC Muroidea; Muridae; Murinae; Rattus. OX NCBI_TaxID=10116 {ECO:0000313|Ensembl:ENSRNOP00000053471, ECO:0000313|Proteomes:UP000002494}; RN [1] {ECO:0000313|Ensembl:ENSRNOP00000053471, ECO:0000313|Proteomes:UP000002494} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000053471, RC ECO:0000313|Proteomes:UP000002494}; RX PubMed=15057822; DOI=10.1038/nature02426; RG Rat Genome Sequencing Project Consortium; RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J., RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G., RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G., RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G., RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S., RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T., RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., RA Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A., RA Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., RA Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., RA Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S., RA Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J., RA Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y., RA Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A., RA Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J., RA D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R., RA Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A., RA Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E., RA Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E., RA Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J., RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., RA Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., RA Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., RA Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O., RA Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H., RA Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S., RA Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J., RA Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M., RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., RA Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., RA Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., RA Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., RA Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., RA Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M., RA Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A., RA Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S., RA Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G., RA Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H., RA Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R., RA Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M., RA Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H., RA Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S., RA Collins F.S.; RT "Genome sequence of the Brown Norway rat yields insights into RT mammalian evolution."; RL Nature 428:493-521(2004). RN [2] {ECO:0000313|Ensembl:ENSRNOP00000053471} RP IDENTIFICATION. RC STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000053471}; RG Ensembl; RL Submitted (JUL-2011) to UniProtKB. CC -!- CAUTION: The sequence shown here is derived from an Ensembl CC automatic analysis pipeline and should be considered as CC preliminary data. {ECO:0000313|Ensembl:ENSRNOP00000053471}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AABR07036648; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AABR07036649; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR RefSeq; NP_001129312.1; NM_001135840.1. DR UniGene; Rn.98504; -. DR STRING; 10116.ENSRNOP00000059157; -. DR Ensembl; ENSRNOT00000056632; ENSRNOP00000053471; ENSRNOG00000037426. DR Ensembl; ENSRNOT00000063905; ENSRNOP00000059157; ENSRNOG00000048168. DR GeneID; 363931; -. DR KEGG; rno:363931; -. DR UCSC; RGD:1305954; rat. DR CTD; 8225; -. DR RGD; 1305954; Gtpbp6. DR eggNOG; KOG0410; Eukaryota. DR eggNOG; COG2262; LUCA. DR GeneTree; ENSGT00390000001397; -. DR OMA; MDTVGFM; -. DR OrthoDB; EOG091G0852; -. DR TreeFam; TF315022; -. DR Proteomes; UP000002494; Chromosome 12. DR Bgee; ENSRNOG00000037426; -. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR GO; GO:0043022; F:ribosome binding; IBA:GO_Central. DR CDD; cd01878; HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 1: Evidence at protein level; KW Complete proteome {ECO:0000313|Proteomes:UP000002494}; KW Proteomics identification {ECO:0000213|PeptideAtlas:D3ZLF0}; KW Reference proteome {ECO:0000313|Proteomes:UP000002494}. FT DOMAIN 283 447 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 513 AA; 56552 MW; FD347F56EB07D9A5 CRC64; MLFPRVAALP GIWLLRVRRV QHALSLAGTL PRPVRAVSAG SRALGSVWAS DGPVRGGGPE DPREDEEEEE LLRVPPLLPF DAQRVCVLHP DVKRPAGKTP RSTAEWQVAE AAALVRALPG WSVARTLVVS SAAPGSRQVF GKGNFRDLTE KIRGCQDITS VFLNVERMTP QTQKELETAW GLRVFDRFTL VLHIFRCNAR TREARMQLAL AEIPLLRSSV SGDSEQQDQQ GWGSRYIMGS GESFSELRAR ALRDRELRLR RVLERLRDKR RLMRKERVRR EFPVVSVVGY TNCGKTTLIR ALTGEATLQP RDQPFATLDV TVHEGRLPSR LRVLYVDTIG FLSQLPHSLI HAFSATLEDV AYSDVLVHVT DVSHPDAELQ KATVLSTLRG LGLRPALLES AVEVHSKVDL VPGHTTPCSG ALAVSAVSGR GLDELKAALE ASVLRATGRQ LLTIRVRLGG PQLGWLYNEA VVQQVQELPE GGAAHVTVVI TQAAYGRFQK LFPTDITSDP HTD // ID D4BRQ4_BIFBR Unreviewed; 508 AA. AC D4BRQ4; DT 18-MAY-2010, integrated into UniProtKB/TrEMBL. DT 18-MAY-2010, sequence version 1. DT 07-JUN-2017, entry version 43. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:EFE88117.1}; GN ORFNames=BIFBRE_04794 {ECO:0000313|EMBL:EFE88117.1}; OS Bifidobacterium breve DSM 20213 = JCM 1192. OC Bacteria; Actinobacteria; Bifidobacteriales; Bifidobacteriaceae; OC Bifidobacterium. OX NCBI_TaxID=518634 {ECO:0000313|EMBL:EFE88117.1, ECO:0000313|Proteomes:UP000003191}; RN [1] {ECO:0000313|EMBL:EFE88117.1, ECO:0000313|Proteomes:UP000003191} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 20213 {ECO:0000313|EMBL:EFE88117.1, RC ECO:0000313|Proteomes:UP000003191}; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Nelson J., Hou S., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Zhang X., Suruliraj S., Warren W., Chinwalla A., RA Mardis E.R., Wilson R.K.; RL Submitted (FEB-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EFE88117.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACCG02000016; EFE88117.1; -; Genomic_DNA. DR ProteinModelPortal; D4BRQ4; -. DR EnsemblBacteria; EFE88117; EFE88117; BIFBRE_04794. DR PATRIC; fig|518634.7.peg.1732; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000003191; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000003191}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000003191}. FT DOMAIN 288 454 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 508 AA; 55308 MW; ED7DC5F25F13632B CRC64; MTDTEVPLTD NTQYTDLDRS DADEAPSGVL SGQSNVLLDD TQRAAGWHED SNQEWEEREA RNELKHVAGL GELQDVTEVE YRKVRLERVV LVGVWSSAVT TQAKAEESLR ELAALAETAG AVVCDGLLQH RSKPDAATYV GSGKAREIAD IVAREEADTI VVDDDLAPSQ RRALEDAAKV KVVDRTAVIL DIFAQHATSR EGKAQVELAQ LEYMLPRLRG WGGSLSRQAG GRAAGADAGI GSRGPGETKI EMDRRVIRAR IARLRRQIRE MAPAREIKRG SRRRFGLPTV AVVGYTNAGK SSLTNRLTGS AELVENALFA TLDTAVRRAK THDGRAFAYV DTVGFVRRLP TQLVEAFKST LEEVGEADVI VHVVDGSHPD PFSQIDAVND VLADIEGTVS IPRILVFNKA DQIDDAKRER LAALQPDAFI VSAYSGKGLD ALRDAVEELL PVPHVHINAL LPYTAGSLLS RVREYGKVDS VEYRDDGVAL EADVDSHLAA QIMEQSIA // ID D4DY80_SEROD Unreviewed; 426 AA. AC D4DY80; DT 18-MAY-2010, integrated into UniProtKB/TrEMBL. DT 18-MAY-2010, sequence version 1. DT 30-AUG-2017, entry version 43. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:EFE97572.1}; GN ORFNames=HMPREF0758_0863 {ECO:0000313|EMBL:EFE97572.1}; OS Serratia odorifera DSM 4582. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; OC Yersiniaceae; Serratia. OX NCBI_TaxID=667129 {ECO:0000313|EMBL:EFE97572.1, ECO:0000313|Proteomes:UP000005723}; RN [1] {ECO:0000313|EMBL:EFE97572.1, ECO:0000313|Proteomes:UP000005723} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 4582 {ECO:0000313|EMBL:EFE97572.1, RC ECO:0000313|Proteomes:UP000005723}; RA Muzny D., Qin X., Deng J., Jiang H., Liu Y., Qu J., Song X.-Z., RA Zhang L., Thornton R., Coyle M., Francisco L., Jackson L., Javaid M., RA Korchina V., Kovar C., Mata R., Mathew T., Ngo R., Nguyen L., RA Nguyen N., Okwuonu G., Ongeri F., Pham C., Simmons D., RA Wilczek-Boney K., Hale W., Jakkamsetti A., Pham P., Ruth R., RA San Lucas F., Warren J., Zhang J., Zhao Z., Zhou C., Zhu D., Lee S., RA Bess C., Blankenburg K., Forbes L., Fu Q., Gubbala S., Hirani K., RA Jayaseelan J.C., Lara F., Munidasa M., Palculict T., Patil S., RA Pu L.-L., Saada N., Tang L., Weissenberger G., Zhu Y., Hemphill L., RA Shang Y., Youmans B., Ayvaz T., Ross M., Santibanez J., Aqrawi P., RA Gross S., Joshi V., Fowler G., Nazareth L., Reid J., Worley K., RA Petrosino J., Highlander S., Gibbs R.; RL Submitted (JAN-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EFE97572.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADBY01000017; EFE97572.1; -; Genomic_DNA. DR RefSeq; WP_004955986.1; NZ_GG753567.1. DR ProteinModelPortal; D4DY80; -. DR STRING; 667129.HMPREF0758_0863; -. DR EnsemblBacteria; EFE97572; EFE97572; HMPREF0758_0863. DR GeneID; 31791383; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000005723; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000005723}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Hydrolase {ECO:0000313|EMBL:EFE97572.1}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000005723}. FT DOMAIN 198 365 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 426 AA; 48039 MW; 240AF49712A906EA CRC64; MFDRYEAGEQ AVLVHIYFSQ DKDTEDLSEF ESLVSSAGVD ALQVVTGSRK APHPKYFVGE GKAEEIADAV KASGASVVLF DHSLSPAQER NLERLCECRV IDRTGLILDI FAQRARTHEG KLQVELAQLR HIATRLVRGW THLERQKGGI GLRGPGETQL ETDRRLLRDR ISLILRRLER VEKQREQGRR ARTRADVPTV SLVGYTNAGK STLFNRITSA DVYAADQLFA TLDPTLRRID VADVGDTVLA DTVGFIRHLP HDLVAAFKAT LQETRQASLL LHVIDAADTR VDENIEAVNT VLAEIDSDEI PTLLVMNKID MLDDFVPRID RNEENLPIRV WLSAASGEGI PLLFQALTER LSGEIAQHEL RLPPEAGRLR SRFYQLQAIE KEWIEEDGSI GMVVRMPIVE WRRLCKQEQE LINFIV // ID D4GNZ8_PANAM Unreviewed; 426 AA. AC D4GNZ8; DT 18-MAY-2010, integrated into UniProtKB/TrEMBL. DT 18-MAY-2010, sequence version 1. DT 30-AUG-2017, entry version 51. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:ADD78703.1}; GN OrderedLocusNames=PANA_3536 {ECO:0000313|EMBL:ADD78703.1}; OS Pantoea ananatis (strain LMG 20103). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; OC Erwiniaceae; Pantoea. OX NCBI_TaxID=706191 {ECO:0000313|EMBL:ADD78703.1, ECO:0000313|Proteomes:UP000001702}; RN [1] {ECO:0000313|EMBL:ADD78703.1, ECO:0000313|Proteomes:UP000001702} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=LMG 20103 {ECO:0000313|EMBL:ADD78703.1, RC ECO:0000313|Proteomes:UP000001702}; RX PubMed=20348253; DOI=10.1128/JB.00060-10; RA De Maayer P., Chan W.Y., Venter S.N., Toth I.K., Birch P.R., RA Joubert F., Coutinho T.A.; RT "Genome sequence of Pantoea ananatis LMG20103, the causative agent of RT Eucalyptus blight and dieback."; RL J. Bacteriol. 192:2936-2937(2010). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001875; ADD78703.1; -; Genomic_DNA. DR RefSeq; WP_013027403.1; NC_013956.2. DR ProteinModelPortal; D4GNZ8; -. DR STRING; 706191.PANA_3536; -. DR EnsemblBacteria; ADD78703; ADD78703; PANA_3536. DR GeneID; 31512475; -. DR KEGG; pam:PANA_3536; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000001702; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000001702}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000001702}. FT DOMAIN 198 365 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 426 AA; 47863 MW; 15F7894BA78DBB18 CRC64; MFDRYDAGEQ AVLVHIWFSQ DKELEDLQEF ETLVSSAGVE ALQVVTGSRK APHPKYFVGE GKAVEIADAV KTSGASVVLF DHALTPAQER NLERLCECRV IDRTGLILDI FAQRARTHEG KLQVELAQLR HLATRLVRGW THLERQKGGI GLRGPGETQL ETDRRLLRGR ISQILSRLER VEKQREQGRQ ARAKADVPTV SLVGYTNAGK STLFNAITSA NVYAADQLFA TLDPTLRRLN VADVGEVVLA DTVGFIRHLP HDLVAAFKAT LQETRQATLL MHVIDAADVR VNENIGAVNE VLEEIDADEI PTLLIMNKID MLDGFEPRID RDEENMPVRV WLSAQSGVGI PLLWQALSER LSGEIAQYDL RLPPEAGRLR SRFYQLQAIE KEWNEEDGCV GLHVRMPVID WRRLCKQEPS LTSYIV // ID D4GXM6_HALVD Unreviewed; 433 AA. AC D4GXM6; DT 18-MAY-2010, integrated into UniProtKB/TrEMBL. DT 18-MAY-2010, sequence version 1. DT 07-JUN-2017, entry version 61. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:ADE04901.1}; GN OrderedLocusNames=HVO_1346 {ECO:0000313|EMBL:ADE04901.1}; OS Haloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC OS 14742 / NCIMB 2012 / VKM B-1768 / DS2) (Halobacterium volcanii). OC Archaea; Euryarchaeota; Halobacteria; Haloferacales; Haloferacaceae; OC Haloferax. OX NCBI_TaxID=309800 {ECO:0000313|EMBL:ADE04901.1, ECO:0000313|Proteomes:UP000008243}; RN [1] {ECO:0000313|Proteomes:UP000008243} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / RC VKM B-1768 / DS2 {ECO:0000313|Proteomes:UP000008243}; RX PubMed=20333302; DOI=10.1371/journal.pone.0009605; RA Hartman A.L., Norais C., Badger J.H., Delmas S., Haldenby S., RA Madupu R., Robinson J., Khouri H., Ren Q., Lowe T.M., RA Maupin-Furlow J., Pohlschroder M., Daniels C., Pfeiffer F., Allers T., RA Eisen J.A.; RT "The complete genome sequence of Haloferax volcanii DS2, a model RT archaeon."; RL PLoS ONE 5:E9605-E9605(2010). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001956; ADE04901.1; -; Genomic_DNA. DR RefSeq; WP_004043592.1; NZ_AOHU01000091.1. DR STRING; 309800.HVO_1346; -. DR EnsemblBacteria; ADE04901; ADE04901; HVO_1346. DR EnsemblBacteria; ELY27967; ELY27967; C498_12008. DR GeneID; 8925897; -. DR KEGG; hvo:HVO_1346; -. DR PATRIC; fig|309800.29.peg.2293; -. DR eggNOG; arCOG00353; Archaea. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG093Z07D6; -. DR Proteomes; UP000008243; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000008243}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000008243}. FT COILED 153 183 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 433 AA; 48212 MW; 47C9AA1FD456631F CRC64; MSRVVVAKRV DRGDADLTEI SDLARAAGYE VVGELTQTRE EDAAFHFGEG KVGELASLVA REDAVAVVFD NRLGPYQTYN IAQKLPDDAE VIDRFTLILE IFGQRANTRK AQLQVELAEL RYELPRAEAK ASLAKRDERP GFMGLGEYDE SREQDIKAQI SRIKNELDAI ADKEETRREQ RRESGFDLVA LAGYTNAGKS TLMQRLAADL EVGQNDELHP DLDPTAESQD KLFTTLGTTT RRAETGKRDV LLTDTVGFVS DLPHWLVESF KSTLDSVYRA DLVLLVVDAS EPVEEMREKL VTSHDTLYER NEAPIVTVFN KVDKVEAEEL EEKRAALSAL APNPVAVSGL TGENVEELAD RVEGELPAWK RERLLLPMAD DTMSLVSWLY DHAHVEAEEY EGEQVHVEFE ARPAIVEKAR AKAADLSAPT DSA // ID D4H3D5_DENA2 Unreviewed; 597 AA. AC D4H3D5; DT 18-MAY-2010, integrated into UniProtKB/TrEMBL. DT 18-MAY-2010, sequence version 1. DT 07-JUN-2017, entry version 51. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Dacet_0420 {ECO:0000313|EMBL:ADD67219.1}; OS Denitrovibrio acetiphilus (strain DSM 12809 / N2460). OC Bacteria; Deferribacteres; Deferribacterales; Deferribacteraceae; OC Denitrovibrio. OX NCBI_TaxID=522772 {ECO:0000313|EMBL:ADD67219.1, ECO:0000313|Proteomes:UP000002012}; RN [1] {ECO:0000313|EMBL:ADD67219.1, ECO:0000313|Proteomes:UP000002012} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 12809 / N2460 {ECO:0000313|Proteomes:UP000002012}; RX PubMed=21304711; RA Kiss H., Lang E., Lapidus A., Copeland A., Nolan M., RA Glavina Del Rio T., Chen F., Lucas S., Tice H., Cheng J.F., Han C., RA Goodwin L., Pitluck S., Liolios K., Pati A., Ivanova N., RA Mavromatis K., Chen A., Palaniappan K., Land M., Hauser L., RA Chang Y.J., Jeffries C.D., Detter J.C., Brettin T., Spring S., RA Rohde M., Goker M., Woyke T., Bristow J., Eisen J.A., Markowitz V., RA Hugenholtz P., Kyrpides N.C., Klenk H.P.; RT "Complete genome sequence of Denitrovibrio acetiphilus type strain RT (N2460)."; RL Stand. Genomic Sci. 2:270-279(2010). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001968; ADD67219.1; -; Genomic_DNA. DR RefSeq; WP_013009763.1; NC_013943.1. DR ProteinModelPortal; D4H3D5; -. DR STRING; 522772.Dacet_0420; -. DR EnsemblBacteria; ADD67219; ADD67219; Dacet_0420. DR KEGG; dap:Dacet_0420; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; EREVIIT; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000002012; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000002012}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000002012}. FT DOMAIN 388 576 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 354 381 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 597 AA; 67392 MW; A4C320DE0C98A875 CRC64; MQRLTSTVFN RRCNILHGNT GGLKPQQIQK LEKLYTRKAG VNETIQPELA KTICAISHEL NRQIGILADR KGNVHYVIVG DTSEVFIPGL ERFPLVPGSL RGLRLLHTHL SGEDITDDDL TDLALLRLDS VTALHFNQDG HSYGMQTAHL LPPDNVNYYD FLTDKDPHQQ KIDYLAFITE LEAEISSKTK RLHKVDTGSH ALLIGCYKSK VQGSENMAEL SELARSANMY VTGEVVQIKD KLHPKYVIGS GKLKEIVIKS MQNGVEFLVF DNPLSPAQAK AIADFTDLKI LDRPQLILDI FAKRATTNDG KIRVELAQLK YLLPRLSQRD DSLSRLTGGI GGRGPGNTKL EIDRRRTNDR IAMLSRKLKK IEKNRETMRR KRNRNELPIV SIIGYTNAGK STLLNSLTQS GVYADDLMFA TLDTSSKRIR FPQERDVIIT DTVGFIRDLP ENLKGAFKST LEELQDADVL LHVVDISSDG FDSHVHSVET ILQELELTDK ESILVLNKTD LLLQHETDYI QFGEMPDDAD PEMFTRAHRI VNLIERYNKV CMVSALHRKS FRELLELIRL TLFADGIDIE PMGIEDYFGH RSIDGTT // ID D4I1H7_ERWAC Unreviewed; 426 AA. AC D4I1H7; DT 18-MAY-2010, integrated into UniProtKB/TrEMBL. DT 18-MAY-2010, sequence version 1. DT 30-AUG-2017, entry version 51. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:CBA23139.1}; GN OrderedLocusNames=EAMY_3156 {ECO:0000313|EMBL:CBA23139.1}; OS Erwinia amylovora (strain CFBP1430). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; OC Erwiniaceae; Erwinia. OX NCBI_TaxID=665029 {ECO:0000313|EMBL:CBA23139.1, ECO:0000313|Proteomes:UP000001841}; RN [1] {ECO:0000313|EMBL:CBA23139.1, ECO:0000313|Proteomes:UP000001841} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CFBP1430 {ECO:0000313|Proteomes:UP000001841}; RX PubMed=20192826; DOI=10.1094/MPMI-23-4-0384; RA Smits T.H., Rezzonico F., Kamber T., Blom J., Goesmann A., Frey J.E., RA Duffy B.; RT "Complete genome sequence of the fire blight pathogen Erwinia RT amylovora CFBP 1430 and comparison to other Erwinia spp."; RL Mol. Plant Microbe Interact. 23:384-393(2010). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; FN434113; CBA23139.1; -; Genomic_DNA. DR RefSeq; WP_004160133.1; NC_013961.1. DR ProteinModelPortal; D4I1H7; -. DR STRING; 665029.EAMY_3156; -. DR EnsemblBacteria; CBA23139; CBA23139; EAMY_3156. DR GeneID; 8913047; -. DR KEGG; eam:EAMY_3156; -. DR PATRIC; fig|665029.3.peg.3034; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR Proteomes; UP000001841; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000001841}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}. FT DOMAIN 198 365 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 426 AA; 47921 MW; 38755CAA33F42025 CRC64; MFDRYDAGEQ AVLVHIYFSQ DKDTDDLQEF ETLVSSAGVE ALRVVTGSRK APHPKYFVGE GKAVEIADAV KESGATVVLF DHALSPAQER NLEALCECRV IDRTGLILDI FAQRARTHEG KLQVELAQLR HLATRLVRGW THLERQKGGI GLRGPGETQL ETDRRLLRNR ITLILSRLER VSKQREQGRQ ARNKADVPTV SLVGYTNAGK STLFNRLTSA EVYAADQLFA TLDPTLRRVD VADVGEVVLA DTVGFIRHLP HDLVAAFKAT LQETREAALL LHIVDAADLR IEENIDAVNV VLEEIESDDI PSLLVMNKID MLDGFVPRID RDEENLPVRV WLSAQTGEGI PLLFQALTER LAGEIAQFEL RLPPAAGRLR SRFYQLRAIE KEWNEEDGSL GLQIRMPIVD WRRLCKQEPE LVDYIV // ID D4IWI5_BUTFI Unreviewed; 410 AA. AC D4IWI5; DT 18-MAY-2010, integrated into UniProtKB/TrEMBL. DT 18-MAY-2010, sequence version 1. DT 07-JUN-2017, entry version 50. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=CIY_25080 {ECO:0000313|EMBL:CBK75128.1}; OS Butyrivibrio fibrisolvens 16/4. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Lachnospiraceae; OC Butyrivibrio. OX NCBI_TaxID=657324 {ECO:0000313|EMBL:CBK75128.1, ECO:0000313|Proteomes:UP000008796}; RN [1] {ECO:0000313|EMBL:CBK75128.1, ECO:0000313|Proteomes:UP000008796} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=16/4 {ECO:0000313|EMBL:CBK75128.1, RC ECO:0000313|Proteomes:UP000008796}; RG metaHIT consortium -- http://www.metahit.eu/; RA Pajon A., Turner K., Parkhill J., Duncan S., Flint H.; RT "The genome sequence of Butyrivibrio fibrisolvens 16/4."; RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:CBK75128.1, ECO:0000313|Proteomes:UP000008796} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=16/4 {ECO:0000313|EMBL:CBK75128.1, RC ECO:0000313|Proteomes:UP000008796}; RA Pajon A.; RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; FP929036; CBK75128.1; -; Genomic_DNA. DR ProteinModelPortal; D4IWI5; -. DR STRING; 657324.CIY_25080; -. DR EnsemblBacteria; CBK75128; CBK75128; CIY_25080. DR KEGG; bfi:CIY_25080; -. DR PATRIC; fig|657324.3.peg.2294; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR KO; K03665; -. DR BioCyc; BFIB657324:G131C-2140-MONOMER; -. DR Proteomes; UP000008796; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000008796}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000008796}. FT DOMAIN 206 370 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 410 AA; 45521 MW; 051A81F8FAF0108A CRC64; MVNTEKIIEK VILVAVNEGD EAEAWDSLKE LEELCETAGA QVVGQIMQNL ERRNPGTYVG SGKVDEIADL IWETGATGIV CDDELTPAQM RNLADALDTK VMDRTLIILD IFAARAGTAE GKIQVELAQL RYEMTRLTGF GKNMSRVGGT AAGGGGAIGT RGPGEKKLEM DKRLIAGRIS QLKKELADVV SHREITRAKR QRNGVPVAAI VGYTNAGKSS LLNKLTDAHI LEWDALFATL DPTTRELLLD NDQKILLTDT VGFIRKLPHH LVDAFKSTLE EAKYADYIIH VVDVSNPQMD RQMEIVYQTL DKLGVSDKPI LTIFNKVDKV ADEHDYHDLR ADYTVHTSIK TGKGLDRVRE ILAELLRDGK EYVEKLIPYT EAGTIAKIRE NGELISEEYR EDGIFIKAYL // ID D4J9H8_9FIRM Unreviewed; 419 AA. AC D4J9H8; DT 18-MAY-2010, integrated into UniProtKB/TrEMBL. DT 18-MAY-2010, sequence version 1. DT 07-JUN-2017, entry version 43. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=CC1_23250 {ECO:0000313|EMBL:CBK80999.1}; OS Coprococcus catus GD/7. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Lachnospiraceae; OC Coprococcus. OX NCBI_TaxID=717962 {ECO:0000313|EMBL:CBK80999.1, ECO:0000313|Proteomes:UP000008798}; RN [1] {ECO:0000313|EMBL:CBK80999.1, ECO:0000313|Proteomes:UP000008798} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=GD/7 {ECO:0000313|EMBL:CBK80999.1, RC ECO:0000313|Proteomes:UP000008798}; RG metaHIT consortium -- http://www.metahit.eu/; RA Pajon A., Turner K., Parkhill J., Duncan S., Flint H.; RT "The genome sequence of Coprococcus catus GD/7."; RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:CBK80999.1, ECO:0000313|Proteomes:UP000008798} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=GD/7 {ECO:0000313|EMBL:CBK80999.1, RC ECO:0000313|Proteomes:UP000008798}; RA Pajon A.; RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; FP929038; CBK80999.1; -; Genomic_DNA. DR ProteinModelPortal; D4J9H8; -. DR STRING; 717962.CC1_23250; -. DR EnsemblBacteria; CBK80999; CBK80999; CC1_23250. DR KEGG; cct:CC1_23250; -. DR PATRIC; fig|717962.3.peg.2222; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR KO; K03665; -. DR OrthoDB; POG091H0464; -. DR BioCyc; CCAT717962:G134I-2034-MONOMER; -. DR Proteomes; UP000008798; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000008798}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000008798}. FT DOMAIN 202 369 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 161 198 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 419 AA; 47115 MW; FCCBC6FB9D4B878C CRC64; MADFYENKQV TEEIILVGVA LGETSVTDES LDELEELAKT AGAVTVGRLI QNREMIHPGT YLGKGKLEEL AFLISETHAT GIICDDELSP AQMANMEDVL DIKVMDRTLL ILDIFAQRAT TREGKIQVEL AQLRYRATRL VGMRNSLSRL GGGIGTRGPG EKKLEVDRRL IRERISQLKR ELEDVKRHRE VARQQRQRNQ IPVAAIVGYT NAGKSTLLNR LTGAGVLEED KLFATLDPTT RNLTLDDGQE LLLTDTVGFI HKLPHHLVDA FRSTLEEAKY ADILIHMVDA SNPQAEMHMH VVYETLAALD IKDKKIITVF NKTDLIRDQE SLVSLKDFRA DYTVTASVKQ GTGLDALLST VQTILRANKL LIERVFDYAH AGEIAVIRKY GQLLEERYQE DGIYVKAYIP KDIYARLSF // ID D4JVS6_9FIRM Unreviewed; 419 AA. AC D4JVS6; DT 18-MAY-2010, integrated into UniProtKB/TrEMBL. DT 18-MAY-2010, sequence version 1. DT 07-JUN-2017, entry version 49. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=EUS_21890 {ECO:0000313|EMBL:CBK97195.1}; OS [Eubacterium] siraeum 70/3. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Ruminococcaceae; OC Ruminiclostridium. OX NCBI_TaxID=657319 {ECO:0000313|EMBL:CBK97195.1, ECO:0000313|Proteomes:UP000008803}; RN [1] {ECO:0000313|EMBL:CBK97195.1, ECO:0000313|Proteomes:UP000008803} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=70/3 {ECO:0000313|EMBL:CBK97195.1, RC ECO:0000313|Proteomes:UP000008803}; RG metaHIT consortium -- http://www.metahit.eu/; RA Pajon A., Turner K., Parkhill J., Duncan S., Flint H.; RT "The genome sequence of Eubacterium siraeum 70/3."; RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:CBK97195.1, ECO:0000313|Proteomes:UP000008803} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=70/3 {ECO:0000313|EMBL:CBK97195.1, RC ECO:0000313|Proteomes:UP000008803}; RA Pajon A.; RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; FP929044; CBK97195.1; -; Genomic_DNA. DR ProteinModelPortal; D4JVS6; -. DR STRING; 657319.EUS_21890; -. DR EnsemblBacteria; CBK97195; CBK97195; EUS_21890. DR KEGG; esu:EUS_21890; -. DR PATRIC; fig|657319.3.peg.2599; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR KO; K03665; -. DR Proteomes; UP000008803; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000008803}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000008803}. FT DOMAIN 206 366 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 165 199 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 419 AA; 45940 MW; A094E245491D414F CRC64; MNESAVNNPI LKENELTRAI LAGVDTGEYD AEISMDELEE LAETAGAVTV CRIIQKRPAI ESATILGEGK IEELSAAAKD LDAQLIIFDM ELSSSQIRNI EDITSVRVID RTMLILDIFA GRAVTNEGKL QVELAQLKYR LPRLMGIGTS LSRLGGGIGT RGPGETQLET DRRHIRRRID KLSDELKELE KRRDLSRRRR KKDSVCVGAI VGYTNAGKST LLNALTGAGV LAEDKLFATL DLTSRAIELP DGRSFTLVDT VGLIRRLPHH LVEAFKSTLE EAASADIILH VCDASDPEAR EKGQTTLSLL SELGCGEIPV ITVLNKCDKL DYELPPAENT VMISAKNGTG FDELLKAISD NLTDKVSRME MLIPYDKSGL AAALHSHGKV LSEEYLENGI AVTALVDKLH KYEYEEFVI // ID D4KZA1_9FIRM Unreviewed; 414 AA. AC D4KZA1; DT 18-MAY-2010, integrated into UniProtKB/TrEMBL. DT 18-MAY-2010, sequence version 1. DT 07-JUN-2017, entry version 42. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=RO1_21790 {ECO:0000313|EMBL:CBL12691.1}; OS Roseburia intestinalis XB6B4. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Lachnospiraceae; OC Roseburia. OX NCBI_TaxID=718255 {ECO:0000313|EMBL:CBL12691.1, ECO:0000313|Proteomes:UP000008953}; RN [1] {ECO:0000313|EMBL:CBL12691.1, ECO:0000313|Proteomes:UP000008953} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=XB6B4 {ECO:0000313|EMBL:CBL12691.1, RC ECO:0000313|Proteomes:UP000008953}; RG metaHIT consortium -- http://www.metahit.eu/; RA Pajon A., Turner K., Parkhill J., Bernalier A.; RT "The genome sequence of Roseburia intestinalis XB6B4."; RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:CBL12691.1, ECO:0000313|Proteomes:UP000008953} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=XB6B4 {ECO:0000313|EMBL:CBL12691.1, RC ECO:0000313|Proteomes:UP000008953}; RA Pajon A.; RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; FP929050; CBL12691.1; -; Genomic_DNA. DR ProteinModelPortal; D4KZA1; -. DR STRING; 718255.RO1_21790; -. DR EnsemblBacteria; CBL12691; CBL12691; RO1_21790. DR KEGG; rix:RO1_21790; -. DR PATRIC; fig|718255.3.peg.3344; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR KO; K03665; -. DR Proteomes; UP000008953; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000008953}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000008953}. FT DOMAIN 202 366 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 161 195 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 414 AA; 46463 MW; 36196579AC56C947 CRC64; MPEPIKIEEV KERVILVGVS EQDGDDAEDS VAELAELVKT AGAVTVGTLI QKRELIHPGT YVGTGKVQEI ADMIAELGAT GIVCDDELSP TQLKNLEQML DTKVMDRTLI ILDIFAARAT TSEGKIQVEL AQLKYRLSRL TGLGRSMSRL GGGIGTRGPG EKKLEMDRRL IKDRIAQLNR ELKEVRKHRE ITRAQREKKQ IPVAAIVGYT NAGKSTLLNH LTGAGVLEED KLFATLDPTT RVLELPGRQE ILLTDTVGFI RKLPHHLIEA FKSTLEEAKY ADYIVHVVDA SNPQRDKQMH IVYDTLYQLD IREKTVITLF NKQDQVTDEE PIRDFKADYT LAVSAKKGTG LEELKELFCT LLRDNKILVE RTISYQEAGI LQQIRKSGEL LEEEYRPEGI FIRAYVTPEI YGSL // ID D4LFG5_RUMC1 Unreviewed; 417 AA. AC D4LFG5; DT 18-MAY-2010, integrated into UniProtKB/TrEMBL. DT 18-MAY-2010, sequence version 1. DT 07-JUN-2017, entry version 45. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=RUM_23690 {ECO:0000313|EMBL:CBL18360.1}; OS Ruminococcus champanellensis (strain DSM 18848 / JCM 17042 / KCTC OS 15320 / 18P13). OC Bacteria; Firmicutes; Clostridia; Clostridiales; Ruminococcaceae; OC Ruminococcus. OX NCBI_TaxID=213810 {ECO:0000313|EMBL:CBL18360.1, ECO:0000313|Proteomes:UP000007054}; RN [1] {ECO:0000313|Proteomes:UP000007054} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 18848 / JCM 17042 / 18P13 RC {ECO:0000313|Proteomes:UP000007054}; RA Pajon A., Turner K., Parkhill J., Bernalier A.; RT "The genome sequence of Ruminococcus sp. 18P13."; RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; FP929052; CBL18360.1; -; Genomic_DNA. DR RefSeq; WP_015559266.1; NZ_BBEP01000014.1. DR ProteinModelPortal; D4LFG5; -. DR STRING; 213810.RUM_23690; -. DR EnsemblBacteria; CBL18360; CBL18360; RUM_23690. DR KEGG; rch:RUM_23690; -. DR PATRIC; fig|213810.4.peg.2260; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR KO; K03665; -. DR OMA; HPATYIG; -. DR Proteomes; UP000007054; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000007054}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000007054}. FT DOMAIN 198 361 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 164 191 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 417 AA; 45752 MW; 6D443707101F6999 CRC64; MIETEAKRPR VLLAAVDTGE YDAEQSLDEL EELADTAGAD TAARIVQKRP AFDSATCIGP GRLEEMAQLC QSGDIDQIIF DHELTATQIR NIEDACGVHT IDRTMLILDI FAQRATTHEG RLQVELAQQR YRLPRLAGMG IQLSRLGGGI GTRGPGETKL ETDKRHIRTR ISNLSAELKE IEKRRTYARS RRKKDGVLVC AIVGYTNVGK STLLNLLTDA GVLAENKLFA TLETTSRAIE LPDGRSLMLV DTVGLIRRLP HHLVEAFKST LEEAANADVI LHICDASAEN CEEQAQVTLD LLSELGCDGI PVVTVFNKCD LLPEELAFAP ETRNAVLISA KENRGMDQLL AALAKALPDP ARRMRLLLPF SQGSLLNEIR SSGKLFSEEY TPDGVLVDAM VDVRLQKAAA PYETEKA // ID D4LKB7_9FIRM Unreviewed; 411 AA. AC D4LKB7; DT 18-MAY-2010, integrated into UniProtKB/TrEMBL. DT 18-MAY-2010, sequence version 1. DT 07-JUN-2017, entry version 43. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=CK1_23010 {ECO:0000313|EMBL:CBL20278.1}; OS Ruminococcus sp. SR1/5. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Ruminococcaceae; OC Ruminococcus. OX NCBI_TaxID=657323 {ECO:0000313|EMBL:CBL20278.1, ECO:0000313|Proteomes:UP000007055}; RN [1] {ECO:0000313|EMBL:CBL20278.1, ECO:0000313|Proteomes:UP000007055} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SR1/5 {ECO:0000313|EMBL:CBL20278.1, RC ECO:0000313|Proteomes:UP000007055}; RG metaHIT consortium -- http://www.metahit.eu/; RA Pajon A., Turner K., Parkhill J., Duncan S., Flint H.; RT "The genome sequence of Ruminococcus sp. SR1/5."; RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:CBL20278.1, ECO:0000313|Proteomes:UP000007055} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SR1/5 {ECO:0000313|EMBL:CBL20278.1, RC ECO:0000313|Proteomes:UP000007055}; RA Pajon A.; RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; FP929053; CBL20278.1; -; Genomic_DNA. DR ProteinModelPortal; D4LKB7; -. DR STRING; 657323.CK1_23010; -. DR EnsemblBacteria; CBL20278; CBL20278; CK1_23010. DR KEGG; rum:CK1_23010; -. DR PATRIC; fig|657323.3.peg.1915; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR KO; K03665; -. DR Proteomes; UP000007055; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000007055}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000007055}. FT DOMAIN 199 362 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 158 192 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 411 AA; 45757 MW; 492C77B370AD0C69 CRC64; MEYFEEIQDR VILIGVQADR GDDMEESLDE LGELAVTAGA AVAGRIIQNR EAVHPGTYIG KGKIEEVKGL LYALDANGVI CDDELSPAQM NNLERELECK VMDRTLLILD IFAKRAVTSE GKIQVELAQL RYRSARLVGL RSSLSRLGGG IGTRGPGEKK LETDRRLIRN RISALKQELS QVEKHRELIR SRRAVGNLKT AAIVGYTNAG KSTLLNTLTG ASVLSEDKLF ATLDPTTRLL TLDDGQQLLL TDTVGFIRKL PHNLVEAFKS TLEEAKYADY IIHVVDASNP QAEIQMHIVY ETLKELGALG KKTITLFNKQ DRVSGESFRD LRADHTLKIS ARTGEGLEEF KQLLSEILAE GQIYMERLFP YSEAGQIQLI REYGQLLSEE YTEGGIAVKA RVPREIYPKV T // ID D4LQN4_9FIRM Unreviewed; 417 AA. AC D4LQN4; DT 18-MAY-2010, integrated into UniProtKB/TrEMBL. DT 18-MAY-2010, sequence version 1. DT 07-JUN-2017, entry version 42. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=CK5_16860 {ECO:0000313|EMBL:CBL23092.1}; OS Blautia obeum A2-162. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Lachnospiraceae; OC Blautia. OX NCBI_TaxID=657314 {ECO:0000313|EMBL:CBL23092.1, ECO:0000313|Proteomes:UP000008955}; RN [1] {ECO:0000313|EMBL:CBL23092.1, ECO:0000313|Proteomes:UP000008955} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=A2-162 {ECO:0000313|EMBL:CBL23092.1, RC ECO:0000313|Proteomes:UP000008955}; RG metaHIT consortium -- http://www.metahit.eu/; RA Pajon A., Turner K., Parkhill J., Duncan S., Flint H.; RT "The genome sequence of Ruminococcus obeum A2-162."; RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:CBL23092.1, ECO:0000313|Proteomes:UP000008955} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=A2-162 {ECO:0000313|EMBL:CBL23092.1, RC ECO:0000313|Proteomes:UP000008955}; RA Pajon A.; RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; FP929054; CBL23092.1; -; Genomic_DNA. DR ProteinModelPortal; D4LQN4; -. DR STRING; 657314.CK5_16860; -. DR EnsemblBacteria; CBL23092; CBL23092; CK5_16860. DR KEGG; rob:CK5_16860; -. DR PATRIC; fig|657314.3.peg.1541; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR KO; K03665; -. DR Proteomes; UP000008955; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000008955}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000008955}. FT DOMAIN 201 364 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 417 AA; 46346 MW; 3DB4131EC0011098 CRC64; MRFYEFNDVE ERVILIGVQT REDEDVAASL DELEELAETA GAVTVAKVIQ NREAVHPGTY IGKGKIEEVA ALIQEYDANG VICDDELSPA QLNNLERELD CKVMDRTLLI LDIFAARAVS SEGKIQVELA QLRYRAARLV GLRESLSRLG GGIGTRGPGE KKLETDRRLI RTRISALKAE LFQVEKHREL IRGKRSRGNL KTAAIVGYTN AGKSTLLNTL TGAGILAEDK LFATLDPTTR VLELKDGQQI LLTDTVGFIR KLPHHLVEAF KSTLEEAKYA DYIIHVVDAS NPQAELQMHT VYETLRELGA TGKKIITLLN KQDKVKDVRI RDLQADYTVK CSARSGEGLE ELKDVLAKIL AESQIYLEEL FSYKEAGKIQ LIREYGSLLS EEYTADGIAV KARVPAEIFV SVLPESH // ID D4M324_9FIRM Unreviewed; 411 AA. AC D4M324; DT 18-MAY-2010, integrated into UniProtKB/TrEMBL. DT 18-MAY-2010, sequence version 1. DT 07-JUN-2017, entry version 42. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=RTO_09390 {ECO:0000313|EMBL:CBL25636.1}; OS Ruminococcus torques L2-14. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Lachnospiraceae; OC Blautia. OX NCBI_TaxID=657313 {ECO:0000313|EMBL:CBL25636.1, ECO:0000313|Proteomes:UP000008956}; RN [1] {ECO:0000313|EMBL:CBL25636.1, ECO:0000313|Proteomes:UP000008956} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=L2-14 {ECO:0000313|EMBL:CBL25636.1, RC ECO:0000313|Proteomes:UP000008956}; RG metaHIT consortium -- http://www.metahit.eu/; RA Pajon A., Turner K., Parkhill J., Duncan S., Flint H.; RT "The genome sequence of Ruminococcus torques L2-14."; RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:CBL25636.1, ECO:0000313|Proteomes:UP000008956} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=L2-14 {ECO:0000313|EMBL:CBL25636.1, RC ECO:0000313|Proteomes:UP000008956}; RA Pajon A.; RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; FP929055; CBL25636.1; -; Genomic_DNA. DR ProteinModelPortal; D4M324; -. DR STRING; 657313.RTO_09390; -. DR EnsemblBacteria; CBL25636; CBL25636; RTO_09390. DR KEGG; rto:RTO_09390; -. DR PATRIC; fig|657313.3.peg.610; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR KO; K03665; -. DR Proteomes; UP000008956; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR Gene3D; 3.40.50.620; -; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR014729; Rossmann-like_a/b/a_fold. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000008956}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000008956}. FT DOMAIN 199 363 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 158 192 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 411 AA; 45778 MW; 8E2877E663DBD8C2 CRC64; MISMDEIKER VILVAVDTDG SDQAERFLDE LGELAKTAGA EVVGRMIQPR ENIHPGTYIG KGKILELKEL LWETHGTGII CDDELTSVQM GNLEAELDCK IMDRTLLILD IFAARAVSGE GKIQVELAQL KYRASRLAGL GKSLSRLGGG IGTRGPGEKK LEMDRRLIRE RISRLKKELK DVERHRELIR GQRKQSGLKV AALVGYTSAG KSSIENALTQ AGVLEDAMLF STLDTTTRAL TLDNTQEILL TDTVGFINKL PHHLVEAFKS TLEEAKYADI IVHVVDASNP QMDAQMHVVY ETLRQLGAEG KPVITLFNKQ DKVENPVNHK DLQADYSIAT SAKTGQGLEE FKHALLEIIR KEQIYIERLY DFSEAGKIQL IRSKGQLLSE EYVPEGIEVK AYVPQDIYGR L // ID D4MRH3_9FIRM Unreviewed; 417 AA. AC D4MRH3; DT 18-MAY-2010, integrated into UniProtKB/TrEMBL. DT 18-MAY-2010, sequence version 1. DT 07-JUN-2017, entry version 39. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=CL3_19340 {ECO:0000313|EMBL:CBL36359.1}; OS butyrate-producing bacterium SM4/1. OC Bacteria; Firmicutes; Clostridia; Clostridiales. OX NCBI_TaxID=245012 {ECO:0000313|EMBL:CBL36359.1, ECO:0000313|Proteomes:UP000008959}; RN [1] {ECO:0000313|EMBL:CBL36359.1, ECO:0000313|Proteomes:UP000008959} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SM4/1 {ECO:0000313|EMBL:CBL36359.1, RC ECO:0000313|Proteomes:UP000008959}; RG metaHIT consortium -- http://www.metahit.eu/; RA Pajon A., Turner K., Parkhill J., Duncan S., Flint H.; RT "The genome sequence of Clostridiales sp. SM4/1."; RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:CBL36359.1, ECO:0000313|Proteomes:UP000008959} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SM4/1 {ECO:0000313|EMBL:CBL36359.1, RC ECO:0000313|Proteomes:UP000008959}; RA Pajon A.; RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; FP929060; CBL36359.1; -; Genomic_DNA. DR ProteinModelPortal; D4MRH3; -. DR EnsemblBacteria; CBL36359; CBL36359; CL3_19340. DR KEGG; bprm:CL3_19340; -. DR PATRIC; fig|245012.3.peg.1399; -. DR KO; K03665; -. DR Proteomes; UP000008959; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000008959}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000008959}. FT DOMAIN 202 366 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 417 AA; 46764 MW; EFCF22AD423220E3 CRC64; MAELYDMREE AERVILVAVS TDDGDDTEES VDELAELVKT AGATAIDRII QNRERVHPGT YLGKGKIEEV RERAAELHAT GIVCDDELSP AQLRNLEDAL QIKVMDRTMV ILDIFASHAV TREGKIQVEL AQLRYRAARL VGLRNSLSRL GGGIGTRGPG EKKLEVDRRL IHERIGQLKS ELENVKRHRE VARQQRDRNC TVSAAIVGYT NAGKSTLLNY LTDAGILAQD MLFATLDPTT RTLELPSGQK ILLTDTVGFI RKLPHHLIEA FKSTLEEARY SDIILHVVDV SNPQMETQIH IVYETLRQLE ITDKTVITVF NKMDRLTGDV ILRDFRSDFQ VKISAKTGEG IPALLETLEG ILRSRKVYLE KVFPYAQAGK IQSIRRYGEL LSEEYTEEGI AVKAYVPAEI YGSILQG // ID D4MYR9_ANAHA Unreviewed; 412 AA. AC D4MYR9; DT 18-MAY-2010, integrated into UniProtKB/TrEMBL. DT 18-MAY-2010, sequence version 1. DT 05-JUL-2017, entry version 50. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=CL2_07300 {ECO:0000313|EMBL:CBL37764.1}; OS Anaerostipes hadrus. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Lachnospiraceae; OC Anaerostipes. OX NCBI_TaxID=649756 {ECO:0000313|EMBL:CBL37764.1, ECO:0000313|Proteomes:UP000008960}; RN [1] {ECO:0000313|EMBL:CBL37764.1, ECO:0000313|Proteomes:UP000008960} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SSC/2 {ECO:0000313|EMBL:CBL37764.1, RC ECO:0000313|Proteomes:UP000008960}; RG metaHIT consortium -- http://www.metahit.eu/; RA Pajon A., Turner K., Parkhill J., Duncan S., Flint H.; RT "The genome sequence of Clostridiales sp. SSC/2."; RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:CBL37764.1, ECO:0000313|Proteomes:UP000008960} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SSC/2 {ECO:0000313|EMBL:CBL37764.1, RC ECO:0000313|Proteomes:UP000008960}; RA Pajon A.; RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; FP929061; CBL37764.1; -; Genomic_DNA. DR ProteinModelPortal; D4MYR9; -. DR EnsemblBacteria; CBL37764; CBL37764; CL2_07300. DR KEGG; bprl:CL2_07300; -. DR PATRIC; fig|245018.3.peg.920; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR KO; K03665; -. DR Proteomes; UP000008960; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000008960}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000008960}. FT DOMAIN 200 364 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 15 42 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 412 AA; 46045 MW; FE9E5F61ED44C5D3 CRC64; MEEIKKEIIE KVILVAVADQ DTTEAEESLD ELEELVKTAG AEVVARVIQV RETPHPGTYI GKGKIDEVNA LLYGTDATGI VCDDELSPAQ ISNLEEALDT KVMDRTLIIL DIFAKRAFTR EGKIQVELAQ LKYRASKLTG QGRALSRLGG GIGTRGPGEK KLEMDRRLIR TRISRLKAEL RDVVKHREVQ RKQRQKNHLP VVCIVGYTNA GKSTLLNHFT NAGVYEEDQL FATLDPTTKS LDLSGGQTIL MTDTVGFIRK LPHHLVEAFK STLEEAKYSD LILHVVDASN PQKEKQMEAV YDTLKQLGAN ESPIITAFNK IDLLNGDEIL KDPNAEAVVR ISGKNGEGTD QLLEQIEKIL QKQKLYLEKL YGYQEAGKIQ LIRSHGQLLK EEYRDDGIYV EAYIPKEILG SI // ID D4TR23_9CYAN Unreviewed; 602 AA. AC D4TR23; DT 15-JUN-2010, integrated into UniProtKB/TrEMBL. DT 15-JUN-2010, sequence version 1. DT 07-JUN-2017, entry version 40. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=CRD_01586 {ECO:0000313|EMBL:EFA73181.1}; OS Raphidiopsis brookii D9. OC Bacteria; Cyanobacteria; Nostocales; Aphanizomenonaceae; Raphidiopsis. OX NCBI_TaxID=533247 {ECO:0000313|EMBL:EFA73181.1, ECO:0000313|Proteomes:UP000052137}; RN [1] {ECO:0000313|EMBL:EFA73181.1, ECO:0000313|Proteomes:UP000052137} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=D9 {ECO:0000313|EMBL:EFA73181.1, RC ECO:0000313|Proteomes:UP000052137}; RX PubMed=20169071; DOI=10.1371/journal.pone.0009235; RA Stucken K., John U., Cembella A., Murillo A.A., Soto-Liebe K., RA Fuentes-Valdes J.J., Friedel M., Plominsky A.M., Vasquez M., RA Glockner G.; RT "The smallest known genomes of multicellular and toxic cyanobacteria: RT comparison, minimal gene sets for linked traits and the evolutionary RT implications."; RL PLoS ONE 5:E9235-E9235(2010). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EFA73181.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACYB01000031; EFA73181.1; -; Genomic_DNA. DR RefSeq; WP_009342891.1; NZ_ACYB01000031.1. DR ProteinModelPortal; D4TR23; -. DR STRING; 533247.CRD_01586; -. DR EnsemblBacteria; EFA73181; EFA73181; CRD_01586. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000052137; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000052137}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000052137}. FT DOMAIN 423 593 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 382 409 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 602 AA; 66968 MW; D2712E35F9B696C8 CRC64; MLEYEYDLEG QVTGHGPIET IFGNLQGLKS SQLRQLQRLY HQRVPGNFIT TSEFAQRLAA ISTEVNQPIC SYINRKGKVI RVGVGTVRQT QIPPMEIPRY GAERLSGIRC IATNLKSEPP QEAALTAMLL QRLDSLVILN LTGTGFTKRG GGSTGYVKEV YLAHLVCNTT RIPFSQSSFM TVGESRSPDF HISPPLSLDA IAQLDFLGLV EGLEAEFERE YIGQEVNGDH DRVILVGVFT DDVSDQQFQD TIAELARLVD TAGGEVLQSV QQKRSRIHPQ TVIGEGKVQE VALTAQTRGA NLIVFDRDLS PAQVRNLESQ IGVRVIDRTE VILDIFAQRA QSGAGKLQVE LAQLEYMLPR LTGRGRAMSR LGGGIGTRGP GETKLETERR AIQRRISRLQ QEVNQLQAHR CRLRQKRQHR EIPSLALVGY TNAGKSTLLN ALTNAQVYTA DQLFATLDPT TRRLVIPQGE NYPVREALIT DTVGFIHELP YSLMDAFRAT LEEVTEADAL IHLVDLSHPA WLSHIRSVRE ILAQMPITPG PALVVFNKID QVNNEVLVSA REEFPLSVFI SASQRLGLET LRLRLSQLIE YALEPMIQEQ GF // ID D4W952_9FIRM Unreviewed; 422 AA. AC D4W952; DT 15-JUN-2010, integrated into UniProtKB/TrEMBL. DT 15-JUN-2010, sequence version 1. DT 07-JUN-2017, entry version 43. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:EFF62564.1}; GN ORFNames=CUW_1791 {ECO:0000313|EMBL:EFF62564.1}; OS Turicibacter sanguinis PC909. OC Bacteria; Firmicutes; Erysipelotrichia; Erysipelotrichales; OC Erysipelotrichaceae; Turicibacter. OX NCBI_TaxID=702450 {ECO:0000313|EMBL:EFF62564.1, ECO:0000313|Proteomes:UP000002938}; RN [1] {ECO:0000313|EMBL:EFF62564.1, ECO:0000313|Proteomes:UP000002938} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=PC909 {ECO:0000313|EMBL:EFF62564.1, RC ECO:0000313|Proteomes:UP000002938}; RX PubMed=21183674; DOI=10.1128/JB.01328-10; RA Cuiv P.O., Klaassens E.S., Durkin A.S., Harkins D.M., Foster L., RA McCorrison J., Torralba M., Nelson K.E., Morrison M.; RT "Draft genome sequence of Turicibacter sanguinis PC909, isolated from RT human feces."; RL J. Bacteriol. 193:1288-1289(2011). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EFF62564.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADMN01000121; EFF62564.1; -; Genomic_DNA. DR RefSeq; WP_006785910.1; NZ_ADMN01000121.1. DR ProteinModelPortal; D4W952; -. DR STRING; 702450.CUW_1791; -. DR EnsemblBacteria; EFF62564; EFF62564; CUW_1791. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000002938; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000002938}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000002938}. FT DOMAIN 196 365 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 155 182 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 422 AA; 47535 MW; 359254D18C0A0668 CRC64; MEEIMQRAIL VGVDLNSDKN FEYSVEELRN LAEACNVEVV GLLTQKLERV NSACYIGTGK VEEVALLVAQ NDANLVIFND ELSPSQIRNL EAGLQCKVID RTILILDIFA RRAKTREAQL QVEVAQLRYM MPRLIGLNAS LSRQAGGIGS KGPGEKKLEL DRRRIEEQVH RLNKELDSLV LARQNQRKLR KRNATPVVAL VGYTNAGKST TMNALLKISN SQLDKVVFEK NMLFATLETS TRQIQLPDNK QFLLTDTVGF VSKLPHQLVK AFRSTLEEVT EADLLLHVVD LSHPEFETQI EITNKVLAEL GVSETPMVYV YNKSDLAPDE IAPPTDQDSV RISAKNLENI DELINMIKHH IFQNYVKATF LIPYDRGNLV SYLNEVATVF STEYQENGTL ITVECSAHDA QRLSEYIIKT TH // ID D4XAN2_9BURK Unreviewed; 368 AA. AC D4XAN2; DT 15-JUN-2010, integrated into UniProtKB/TrEMBL. DT 15-JUN-2010, sequence version 1. DT 07-JUN-2017, entry version 39. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:EFF76205.1}; GN ORFNames=HMPREF0004_2529 {ECO:0000313|EMBL:EFF76205.1}; OS Achromobacter piechaudii ATCC 43553. OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Alcaligenaceae; Achromobacter. OX NCBI_TaxID=742159 {ECO:0000313|EMBL:EFF76205.1, ECO:0000313|Proteomes:UP000004510}; RN [1] {ECO:0000313|Proteomes:UP000004510} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43553 {ECO:0000313|Proteomes:UP000004510}; RA Muzny D., Qin X., Deng J., Jiang H., Liu Y., Qu J., Song X.-Z., RA Zhang L., Thornton R., Coyle M., Francisco L., Jackson L., Javaid M., RA Korchina V., Kovar C., Mata R., Mathew T., Ngo R., Nguyen L., RA Nguyen N., Okwuonu G., Ongeri F., Pham C., Simmons D., RA Wilczek-Boney K., Hale W., Jakkamsetti A., Pham P., Ruth R., RA San Lucas F., Warren J., Zhang J., Zhao Z., Zhou C., Zhu D., Lee S., RA Bess C., Blankenburg K., Forbes L., Fu Q., Gubbala S., Hirani K., RA Jayaseelan J.C., Lara F., Munidasa M., Palculict T., Patil S., RA Pu L.-L., Saada N., Tang L., Weissenberger G., Zhu Y., Hemphill L., RA Shang Y., Youmans B., Ayvaz T., Ross M., Santibanez J., Aqrawi P., RA Gross S., Joshi V., Fowler G., Nazareth L., Reid J., Worley K., RA Petrosino J., Highlander S., Gibbs R., Gibbs R.; RT "Complete sequence of Mobiluncus curtisii ATCC 43063."; RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EFF76205.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADMS01000054; EFF76205.1; -; Genomic_DNA. DR RefSeq; WP_006218586.1; NZ_GG770409.1. DR ProteinModelPortal; D4XAN2; -. DR STRING; 742159.HMPREF0004_2529; -. DR EnsemblBacteria; EFF76205; EFF76205; HMPREF0004_2529. DR PATRIC; fig|742159.3.peg.3482; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000004510; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000004510}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000004510}. FT DOMAIN 190 354 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 156 183 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 368 AA; 40194 MW; 86CAC1E71399149B CRC64; MRALIISVDL GDPDHAAHAE EFTMLAKGAG AEVVGTLNAR RDRPDAKFFI GSGKADEGVA MAQALLADIV LFDQPLSPAQ QRNLERAFNL RVVDRVALIL DIFALRAKSH EGKLQVELAQ LQHLATRLTR MWSHLERQRG GIGMRGPGES QLEMDRRMIG AKVKTLRERL DRVERQRVTQ RRARARGGAL SVSLVGYTNA GKSTLFNALT RADSYAADQL FATLDTTTRR IWIEGAGSVV VSDTVGFIRD LPHGLIAAFR ATLEETVHAD LLLHVVDAAS PQRDEQIFEV NKVLAEIGAS AIPTILVYNK IDRAGLEPRV ERDAHGTIAR VFVSATERAG LDALRGAIAE TGQIVGNNAA NYQTLQSE // ID D4YG68_9LACT Unreviewed; 410 AA. AC D4YG68; DT 15-JUN-2010, integrated into UniProtKB/TrEMBL. DT 15-JUN-2010, sequence version 1. DT 05-JUL-2017, entry version 47. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:EFG49803.1}; GN ORFNames=HMPREF0061_0857 {ECO:0000313|EMBL:EFG49803.1}; OS Aerococcus viridans ATCC 11563 = CCUG 4311. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Aerococcaceae; OC Aerococcus. OX NCBI_TaxID=655812 {ECO:0000313|EMBL:EFG49803.1, ECO:0000313|Proteomes:UP000003764}; RN [1] {ECO:0000313|EMBL:EFG49803.1, ECO:0000313|Proteomes:UP000003764} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 11563 {ECO:0000313|EMBL:EFG49803.1, RC ECO:0000313|Proteomes:UP000003764}; RA Muzny D., Qin X., Deng J., Jiang H., Liu Y., Qu J., Song X.-Z., RA Zhang L., Thornton R., Coyle M., Francisco L., Jackson L., Javaid M., RA Korchina V., Kovar C., Mata R., Mathew T., Ngo R., Nguyen L., RA Nguyen N., Okwuonu G., Ongeri F., Pham C., Simmons D., RA Wilczek-Boney K., Hale W., Jakkamsetti A., Pham P., Ruth R., RA San Lucas F., Warren J., Zhang J., Zhao Z., Zhou C., Zhu D., Lee S., RA Bess C., Blankenburg K., Forbes L., Fu Q., Gubbala S., Hirani K., RA Jayaseelan J.C., Lara F., Munidasa M., Palculict T., Patil S., RA Pu L.-L., Saada N., Tang L., Weissenberger G., Zhu Y., Hemphill L., RA Shang Y., Youmans B., Ayvaz T., Ross M., Santibanez J., Aqrawi P., RA Gross S., Joshi V., Fowler G., Nazareth L., Reid J., Worley K., RA Petrosino J., Highlander S., Gibbs R., Gibbs R.; RL Submitted (APR-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EFG49803.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADNT01000062; EFG49803.1; -; Genomic_DNA. DR RefSeq; WP_004262313.1; NZ_ADNT01000062.1. DR ProteinModelPortal; D4YG68; -. DR STRING; 655812.HMPREF0061_0857; -. DR EnsemblBacteria; EFG49803; EFG49803; HMPREF0061_0857. DR GeneID; 32030460; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000003764; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000003764}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000003764}. FT DOMAIN 194 358 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 153 187 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 410 AA; 46276 MW; 6598D5B7599E1F0D CRC64; MQKVLLAAVQ TPDTSDRQFD MQIEELEELV NTAGGEVVGL VSQKRERFDA RTLIGKGKVE ELAMHADANE ADLIIFYQQL TPSQNNNLQQ AVDFPVIDRI QLILDIFAMR ATSKEGKLQV ALAQNEYLLP RLAGNYNALS RLGGGIGTRG PGETKIEQDR RVLRNEIQRI KGELKEVEKH RSRTRENREK GAIFQLGLIG YTNAGKSTIT NALSQADTLE ENQLFATLTP LTRVFSLNNH FQMSITDTVG FIQDLPPQII DSFHSTLEES RQVDLMLIVI DASSPYASEQ EAVVLDTLKQ LDMLDIPHLF VYNKMDKVAN TNQAILAFNQ PNVQISAKSE ESIEELLAAI VNELKDQYDE VEIAVSPSQI GNWLGLQDHI YFEKMEFDEV SQQYELHLFK PKYLQLPKSE // ID D4YMF3_9MICO Unreviewed; 510 AA. AC D4YMF3; DT 15-JUN-2010, integrated into UniProtKB/TrEMBL. DT 15-JUN-2010, sequence version 1. DT 07-JUN-2017, entry version 45. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:EFG47614.1}; GN ORFNames=HMPREF0183_1113 {ECO:0000313|EMBL:EFG47614.1}; OS Brevibacterium mcbrellneri ATCC 49030. OC Bacteria; Actinobacteria; Micrococcales; Brevibacteriaceae; OC Brevibacterium. OX NCBI_TaxID=585530 {ECO:0000313|EMBL:EFG47614.1, ECO:0000313|Proteomes:UP000005714}; RN [1] {ECO:0000313|EMBL:EFG47614.1, ECO:0000313|Proteomes:UP000005714} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 49030 {ECO:0000313|EMBL:EFG47614.1, RC ECO:0000313|Proteomes:UP000005714}; RA Qin X., Bachman B., Battles P., Bell A., Bess C., Bickham C., RA Chaboub L., Chen D., Coyle M., Deiros D.R., Dinh H., Forbes L., RA Fowler G., Francisco L., Fu Q., Gubbala S., Hale W., Han Y., RA Hemphill L., Highlander S.K., Hirani K., Hogues M., Jackson L., RA Jakkamsetti A., Javaid M., Jiang H., Korchina V., Kovar C., Lara F., RA Lee S., Mata R., Mathew T., Moen C., Morales K., Munidasa M., RA Nazareth L., Ngo R., Nguyen L., Okwuonu G., Ongeri F., Patil S., RA Petrosino J., Pham C., Pham P., Pu L.-L., Puazo M., Raj R., Reid J., RA Rouhana J., Saada N., Shang Y., Simmons D., Thornton R., Warren J., RA Weissenberger G., Zhang J., Zhang L., Zhou C., Zhu D., Muzny D., RA Worley K., Gibbs R.; RL Submitted (APR-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EFG47614.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADNU01000032; EFG47614.1; -; Genomic_DNA. DR ProteinModelPortal; D4YMF3; -. DR STRING; 585530.HMPREF0183_1113; -. DR EnsemblBacteria; EFG47614; EFG47614; HMPREF0183_1113. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000005714; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 2. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000005714}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000005714}. FT DOMAIN 282 447 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 510 AA; 56489 MW; F03C576008EFC095 CRC64; MLKHQCETIM FLTIYRKSSM QSDKHREMID RVLSRASDSL TEDHLASDDY SQLDLIEREA LRRVSGLSTE LEDITEVEYR QIRLENVVLA GVYSGSSEEA ETSLRELAAL AETAGSRVLD GVLQRRDTPD PSTYLGRGKA QELAEIVASV GADTVITDTE LAPSQRRALE DVVKVKVIDR VALILDIFAQ HAKSREGKAQ VELAQLEYLL PRLRGWGESM SRQAGGRVAG GAGIGSRGPG ETKIELDRRR IRTRMAKLRR EIKAMAPARE TKRSNRTRNK VPSVAIVGYT NAGKSSLLNR LTDAGVMVKN ELFATLDPTV RQAHTADGRV FTYTDTVGFV RNLPHQLVEA FRSTLEEAAD ADLLLHIVDA SHTDPLAQIK AVHEVLDEAQ TIDIPELIVF NKADIADSDT LARVLNTYPN AVVVSAHTGQ GIDELRERID DLLPRPSHHI TALVPFDRGD LIARAHDEGT VESEKYTAQG TLLVAMVDPD LLHELEQFRQ PDMVDPQTFG // ID D4YV91_9LACO Unreviewed; 421 AA. AC D4YV91; DT 15-JUN-2010, integrated into UniProtKB/TrEMBL. DT 15-JUN-2010, sequence version 1. DT 30-AUG-2017, entry version 41. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:EFG54914.1}; GN ORFNames=HMPREF0493_1452 {ECO:0000313|EMBL:EFG54914.1}; OS Lactobacillus amylolyticus DSM 11664. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; OC Lactobacillus. OX NCBI_TaxID=585524 {ECO:0000313|EMBL:EFG54914.1, ECO:0000313|Proteomes:UP000004069}; RN [1] {ECO:0000313|EMBL:EFG54914.1, ECO:0000313|Proteomes:UP000004069} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 11664 {ECO:0000313|EMBL:EFG54914.1, RC ECO:0000313|Proteomes:UP000004069}; RA Muzny D., Qin X., Deng J., Jiang H., Liu Y., Qu J., Song X.-Z., RA Zhang L., Thornton R., Coyle M., Francisco L., Jackson L., Javaid M., RA Korchina V., Kovar C., Mata R., Mathew T., Ngo R., Nguyen L., RA Nguyen N., Okwuonu G., Ongeri F., Pham C., Simmons D., RA Wilczek-Boney K., Hale W., Jakkamsetti A., Pham P., Ruth R., RA San Lucas F., Warren J., Zhang J., Zhao Z., Zhou C., Zhu D., Lee S., RA Bess C., Blankenburg K., Forbes L., Fu Q., Gubbala S., Hirani K., RA Jayaseelan J.C., Lara F., Munidasa M., Palculict T., Patil S., RA Pu L.-L., Saada N., Tang L., Weissenberger G., Zhu Y., Hemphill L., RA Shang Y., Youmans B., Ayvaz T., Ross M., Santibanez J., Aqrawi P., RA Gross S., Joshi V., Fowler G., Nazareth L., Reid J., Worley K., RA Petrosino J., Highlander S., Gibbs R.; RL Submitted (APR-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EFG54914.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADNY01000061; EFG54914.1; -; Genomic_DNA. DR RefSeq; WP_006352601.1; NZ_AZEP01000020.1. DR ProteinModelPortal; D4YV91; -. DR STRING; 585524.HMPREF0493_1452; -. DR EnsemblBacteria; EFG54914; EFG54914; HMPREF0493_1452. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000004069; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000004069}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}. FT DOMAIN 199 368 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 421 AA; 47211 MW; EA87F7B2F83E28FC CRC64; MIDNQPKKTK AFIAGVNLND PNFEYYMTEL ANLTEANNME VVGQARQNAE NIVAGTYFGL GKINEIKAMA HGLKAKVLVL NDELTPVQIR NLEKLTKLRV VDRTELILEI FSNRARTKQA KLQVQLARLQ YELPRLHPSE NNLDQQRGGG FANRGAGESK LEMNRRTIGQ QISAIKKELK AVASQEEIKA SRRNQSCIPK VALVGYTNAG KSTTMNGLLK AFSDEGANKQ VFVKNMLFAT LDTSVRRIDM KDNFSFILSD TVGFISKLPH NLVESFKATL QEAKDADLLV NVVDASDPNM IQMVRTTQQV LGEIGVKDIP TITAYNKADK TDRNYPQIEG DDILYSAIDE RSIKLLANLI VKRVFSNYDK FNLKLPLADG KLLAYLHEHA QVQDEDYRDD GVYVTANIAP ADQNRFKEFL V // ID D4Z1M1_SPHJU Unreviewed; 443 AA. AC D4Z1M1; DT 15-JUN-2010, integrated into UniProtKB/TrEMBL. DT 15-JUN-2010, sequence version 1. DT 07-JUN-2017, entry version 49. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:BAI96503.1}; GN OrderedLocusNames=SJA_C1-16690 {ECO:0000313|EMBL:BAI96503.1}; OS Sphingobium japonicum (strain NBRC 101211 / UT26S). OC Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales; OC Sphingomonadaceae; Sphingobium. OX NCBI_TaxID=452662 {ECO:0000313|EMBL:BAI96503.1, ECO:0000313|Proteomes:UP000007753}; RN [1] {ECO:0000313|EMBL:BAI96503.1, ECO:0000313|Proteomes:UP000007753} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NBRC 101211 / UT26S {ECO:0000313|Proteomes:UP000007753}; RX PubMed=20817768; DOI=10.1128/JB.00961-10; RA Nagata Y., Ohtsubo Y., Endo R., Ichikawa N., Ankai A., Oguchi A., RA Fukui S., Fujita N., Tsuda M.; RT "Complete genome sequence of the representative gamma- RT hexachlorocyclohexane-degrading bacterium Sphingobium japonicum RT UT26."; RL J. Bacteriol. 192:5852-5853(2010). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AP010803; BAI96503.1; -; Genomic_DNA. DR RefSeq; WP_013040001.1; NC_014006.1. DR ProteinModelPortal; D4Z1M1; -. DR STRING; 452662.SJA_C1-16690; -. DR EnsemblBacteria; BAI96503; BAI96503; SJA_C1-16690. DR GeneID; 29273281; -. DR KEGG; sjp:SJA_C1-16690; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000007753; Chromosome 1. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0016810; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds; IEA:InterPro. DR CDD; cd01878; HflX; 1. DR Gene3D; 2.30.40.10; -; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR011059; Metal-dep_hydrolase_composite. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 2. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000007753}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000007753}. FT DOMAIN 209 389 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 443 AA; 48323 MW; B8DF2614C73624D4 CRC64; MAVFNRDSAD EVSRGARAIV VRADVHGPER RDSDARLEEA RGLALAIGID VRAAQAFRVR DRKPATLFGS GQVDQIATLA RMEEAELVIV DNALSPVQQS NLEKATETKV IDRTGLILEI FGERAATNEG RLQVELAHLD YQAGRLVRSW THLERQRGGF GFLGGPGETQ IEADRRMIRD RMAKIRRELD QVTKTRGLHR ARRQRAPWPV IALVGYTNAG KSTLFNRMTG AAVMAEDLLF ATLDPTMRQI ALPGLDKAIL SDTVGFVSDL PTQLIAAFRA TLEEVLSADL IVHVRDIAHP DSDAQRDDVM DVLGELGIAG EGAFEAGEGE EPPPIIEAWN KLDLLDEDAA TLARETATRR SDVVVLSALT GEGVDDLQRA VSARLTAGAQ IHRLHVPLAD GAAMAWLHEH GEVIGSSAEG EDMLVDVRLS DSALARFLKR RGN // ID D4ZFK8_SHEVD Unreviewed; 432 AA. AC D4ZFK8; DT 15-JUN-2010, integrated into UniProtKB/TrEMBL. DT 15-JUN-2010, sequence version 1. DT 30-AUG-2017, entry version 51. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:BAJ00457.1}; GN OrderedLocusNames=SVI_0486 {ECO:0000313|EMBL:BAJ00457.1}; OS Shewanella violacea (strain JCM 10179 / CIP 106290 / LMG 19151 / OS DSS12). OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales; OC Shewanellaceae; Shewanella. OX NCBI_TaxID=637905 {ECO:0000313|EMBL:BAJ00457.1, ECO:0000313|Proteomes:UP000002350}; RN [1] {ECO:0000313|Proteomes:UP000002350} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=JCM 10179 / CIP 106290 / LMG 19151 / DSS12 RC {ECO:0000313|Proteomes:UP000002350}; RX PubMed=20458400; DOI=10.1039/c000396d; RA Aono E., Baba T., Ara T., Nishi T., Nakamichi T., Inamoto E., RA Toyonaga H., Hasegawa M., Takai Y., Okumura Y., Baba M., Tomita M., RA Kato C., Oshima T., Nakasone K., Mori H.; RT "Complete genome sequence and comparative analysis of Shewanella RT violacea, a psychrophilic and piezophilic bacterium from deep sea RT floor sediments."; RL Mol. Biosyst. 6:1216-1226(2010). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AP011177; BAJ00457.1; -; Genomic_DNA. DR RefSeq; WP_013049770.1; NC_014012.1. DR ProteinModelPortal; D4ZFK8; -. DR STRING; 637905.SVI_0486; -. DR EnsemblBacteria; BAJ00457; BAJ00457; SVI_0486. DR KEGG; svo:SVI_0486; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000002350; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000002350}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000002350}. FT DOMAIN 198 364 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 432 AA; 48589 MW; 2A10854B06076F31 CRC64; MFDRYEAGES AVLVHIDFAD EDRREDLVEL KLLVESAGAQ QVGVITTSRR SPDRKFFLGS GKADELAALV AATEANVVIF NHALSPAQER NLEMVCQCRV LDRTALILDI FAQRARTYEG KLQVELAQLR HMSTRLIRGW THLERQKGGI GMRGPGETQL ETDRRLLRGR MGTINKRLAK VDKQREQSRR ARSRSEQPTV SLVGYTNAGK STLFNSLTVS DVYAADQLFA TLDPTLRKLD LPDGAIILAD TVGFIRHLPH DLVAAFKSTL QETREADLLL HIVDCHDDNM EDNFEQVQLV LKEIGADEIP QLVVCNKIDL LEDVSPRIDY NDEGVPTRVW VSAQQQKGLD QLKEAINQIV GRATLELTLR IPATAGHYLG QFYRLDAIQQ KEFDDLGDCI LSVRLLEADW LRLVKQSQGE LEHFIVEDAA VE // ID D5A3Y5_ARTPN Unreviewed; 511 AA. AC D5A3Y5; DT 15-JUN-2010, integrated into UniProtKB/TrEMBL. DT 15-JUN-2010, sequence version 1. DT 07-JUN-2017, entry version 48. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=NIES39_C04130 {ECO:0000313|EMBL:BAI89279.1}; OS Arthrospira platensis (strain NIES-39 / IAM M-135) (Spirulina OS platensis). OC Bacteria; Cyanobacteria; Oscillatoriophycideae; Oscillatoriales; OC Microcoleaceae; Arthrospira. OX NCBI_TaxID=696747 {ECO:0000313|EMBL:BAI89279.1, ECO:0000313|Proteomes:UP000006803}; RN [1] {ECO:0000313|EMBL:BAI89279.1, ECO:0000313|Proteomes:UP000006803} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NIES-39 / IAM M-135 {ECO:0000313|Proteomes:UP000006803}; RX PubMed=20203057; DOI=10.1093/dnares/dsq004; RA Fujisawa T., Narikawa R., Okamoto S., Ehira S., Yoshimura H., RA Suzuki I., Masuda T., Mochimaru M., Takaichi S., Awai K., Sekine M., RA Horikawa H., Yashiro I., Omata S., Takarada H., Katano Y., Kosugi H., RA Tanikawa S., Ohmori K., Sato N., Ikeuchi M., Fujita N., Ohmori M.; RT "Genomic structure of an economically important cyanobacterium, RT Arthrospira (Spirulina) platensis NIES-39."; RL DNA Res. 17:85-103(2010). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AP011615; BAI89279.1; -; Genomic_DNA. DR RefSeq; WP_014274772.1; NC_016640.1. DR ProteinModelPortal; D5A3Y5; -. DR STRING; 696747.NIES39_C04130; -. DR EnsemblBacteria; BAI89279; BAI89279; NIES39_C04130. DR KEGG; arp:NIES39_C04130; -. DR PATRIC; fig|696747.3.peg.5365; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR KO; K03665; -. DR OMA; EREVIIT; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000006803; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000006803}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000006803}. FT DOMAIN 338 508 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 297 334 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 511 AA; 55947 MW; BA97EB530C762413 CRC64; MGVGTVSQTR IPALELPRYG NGRLSGIRCI ATQLKSDLPR ESVLTAMAMQ RLDVLAILTL TGSGFERRGG GGTGYVKEAY LAHLLPQGEG ENQTQLDSPL APVPYYVSSP MSLDVLSNQD FLDLVDGLEA EFQREFVALD VNSDQDRVLL VGVQTDKIST QRFEEGLAEL GRLVDTAGGI VLQTLRQKRS RPHPQTVVGE GKTQEIALAA QTLGATLIVF DRSLSPAQVR NLETRIGVRV VDRTEVILDI FAQRAQSGAG KLQVELAQLE YSLPRLTGRG QAMSRLGGGI GTRGPGETKL ETERRAIQRR IARLQQEVNQ LQAHRARLRQ RRQRQEVPTL AIVGYTNAGK STLLNVLTAS EIYAADQLFA TLDPTSRRLT IPDAVTEEPQ NIVITDTVGF IHELPPALID AFRATLEEVT DADVLLHLVD LSHPAWQAQI QSVMEILTQM PITPGPALLA FNKIDSVDGE TLRFAQEEYP QAVFISAANA LGLETLRLRM AQLIDYAIAN Q // ID D5AUA8_RHOCB Unreviewed; 427 AA. AC D5AUA8; DT 15-JUN-2010, integrated into UniProtKB/TrEMBL. DT 15-JUN-2010, sequence version 1. DT 07-JUN-2017, entry version 52. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:ADE85547.1}; GN OrderedLocusNames=RCAP_rcc01802 {ECO:0000313|EMBL:ADE85547.1}; OS Rhodobacter capsulatus (strain ATCC BAA-309 / NBRC 16581 / SB1003). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae; Rhodobacter. OX NCBI_TaxID=272942 {ECO:0000313|EMBL:ADE85547.1, ECO:0000313|Proteomes:UP000002361}; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=SB1003; RA Strnad H., Lapidus A., Vlcek C., Ulbrich P., Paces J., Maltsev N., RA Kumar V., Kogan Y., Milgram A., Rebrekov D., Mazur M., Cox R., RA Kyrpides N., Kolar M., Sachova J., Ridl J., Ivanova N., Kapatral V., RA Los T., Lykidis A., Mikhailova N., Reznik G., Vasieva O., Fonstein M., RA Paces V., Haselkorn R.; RT "Complete genome sequence of Rhodobacter capsulatus SB1003."; RL Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:ADE85547.1, ECO:0000313|Proteomes:UP000002361} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-309 / NBRC 16581 / SB1003 RC {ECO:0000313|Proteomes:UP000002361}; RX PubMed=20418398; DOI=10.1128/JB.00366-10; RA Strnad H., Lapidus A., Paces J., Ulbrich P., Vlcek C., Paces V., RA Haselkorn R.; RT "Complete genome sequence of the photosynthetic purple nonsulfur RT bacterium Rhodobacter capsulatus SB 1003."; RL J. Bacteriol. 192:3545-3546(2010). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001312; ADE85547.1; -; Genomic_DNA. DR RefSeq; WP_013067526.1; NC_014034.1. DR ProteinModelPortal; D5AUA8; -. DR STRING; 272942.RCAP_rcc01802; -. DR EnsemblBacteria; ADE85547; ADE85547; RCAP_rcc01802. DR GeneID; 31490677; -. DR KEGG; rcp:RCAP_rcc01802; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000002361; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000002361}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000002361}. FT DOMAIN 207 376 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 427 AA; 47350 MW; E578F9B2C50D4D2F CRC64; MSDPILSKDR PTRVWVLHPD LKAVDARREP ELRLAEAVSL AAALPDLQIM GHEIVRLPKP HAGHLFGTGK MAELKERLQA AEVDLVLVDG PVSPIQQRNL EKEWGVKLLD RTGLILEIFA DRARTREGVL QVELAALSYQ RTRLVRAWTH LERQRGGFGF VGGPGETQIE ADRRAIDDQV IRLKRQLAKV VKTRELHRAA RRKVPFPIVA LVGYTNAGKS SLFNRMTGAE VLAKDMLFAT LDPTMRGLVL PSGRRIILSD TVGFISDLPH ELVAAFRATL EEVLEADLIL HVRDISHPET EEQAEDVGEI LESLGVAEDV ALIEVWNKID ALSEAVRQGL LAQDARRSDV QAVSALSGEG IGALVAAIEA RLGEAWIEED LDLPFTAGKE HAWLHAQGVI RTELQGEEGW QLRLRWTEAQ KSKFAAL // ID D5BCQ3_ZUNPS Unreviewed; 406 AA. AC D5BCQ3; DT 15-JUN-2010, integrated into UniProtKB/TrEMBL. DT 15-JUN-2010, sequence version 1. DT 07-JUN-2017, entry version 55. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=ZPR_0205 {ECO:0000313|EMBL:ADF50566.1}; OS Zunongwangia profunda (strain DSM 18752 / CCTCC AB 206139 / SM-A87). OC Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales; OC Flavobacteriaceae; Zunongwangia. OX NCBI_TaxID=655815 {ECO:0000313|EMBL:ADF50566.1, ECO:0000313|Proteomes:UP000001654}; RN [1] {ECO:0000313|EMBL:ADF50566.1, ECO:0000313|Proteomes:UP000001654} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 18752 / CCTCC AB 206139 / SM-A87 RC {ECO:0000313|Proteomes:UP000001654}; RX PubMed=20398413; DOI=10.1186/1471-2164-11-247; RA Qin Q.L., Zhang X.Y., Wang X.M., Liu G.M., Chen X.L., Xie B.B., RA Dang H.Y., Zhou B.C., Yu J., Zhang Y.Z.; RT "The complete genome of Zunongwangia profunda SM-A87 reveals its RT adaptation to the deep-sea environment and ecological role in RT sedimentary organic nitrogen degradation."; RL BMC Genomics 11:247-247(2010). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001650; ADF50566.1; -; Genomic_DNA. DR RefSeq; WP_013069719.1; NC_014041.1. DR ProteinModelPortal; D5BCQ3; -. DR STRING; 655815.ZPR_0205; -. DR EnsemblBacteria; ADF50566; ADF50566; ZPR_0205. DR KEGG; zpr:ZPR_0205; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000001654; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000001654}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000001654}. FT DOMAIN 200 385 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 406 AA; 47070 MW; 5A4832EEC2A8240E CRC64; MIEKTDLSYE KAVLIGIITK DQNEDKLEEY LDELEFLTYT AGGEVAKRFS QKMDFPNPKT FIGSGKMEEV RIYVSENEIG TAIFDDELSP AQQKNIEKIL KCKVLDRTNL ILDIFAQRAQ TSYARTQVEL AQYEYLLPRL AGMWTHLERQ RGGIGMRGPG ETEIETDRRI VRDKISLLKK KLATIDKQME VQRGNRGQLV RVALVGYTNV GKSTLMNTIS KSEVFAENKL FATLDTTVRK VVIRNLPFLL TDTVGFIRKL PTQLVESFKS TLDEVREADL LLHVVDISHP NFEEHIDSVN QILDEIKSSD KPSVMVFNKI DQYVPEEIAE DDLMTERTTA HYTLTEWKQT WMNRLGDNVL FISALEKENM EHFRKKVYEA VRKIHITRFP YNNFLYPEYD KYGEEK // ID D5BRY9_PUNMI Unreviewed; 430 AA. AC D5BRY9; DT 15-JUN-2010, integrated into UniProtKB/TrEMBL. DT 15-JUN-2010, sequence version 1. DT 07-JUN-2017, entry version 49. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=SAR116_0793 {ECO:0000313|EMBL:ADE39036.1}; OS Puniceispirillum marinum (strain IMCC1322). OC Bacteria; Proteobacteria; Alphaproteobacteria; SAR116 cluster; OC Candidatus Puniceispirillum. OX NCBI_TaxID=488538 {ECO:0000313|EMBL:ADE39036.1, ECO:0000313|Proteomes:UP000007460}; RN [1] {ECO:0000313|EMBL:ADE39036.1, ECO:0000313|Proteomes:UP000007460} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=IMCC1322 {ECO:0000313|EMBL:ADE39036.1, RC ECO:0000313|Proteomes:UP000007460}; RX PubMed=20382761; DOI=10.1128/JB.00347-10; RA Oh H.M., Kwon K.K., Kang I., Kang S.G., Lee J.H., Kim S.J., Cho J.C.; RT "Complete genome sequence of "Candidatus Puniceispirillum marinum" RT IMCC1322, a representative of the SAR116 clade in the RT Alphaproteobacteria."; RL J. Bacteriol. 192:3240-3241(2010). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001751; ADE39036.1; -; Genomic_DNA. DR RefSeq; WP_013045665.1; NC_014010.1. DR ProteinModelPortal; D5BRY9; -. DR STRING; 488538.SAR116_0793; -. DR EnsemblBacteria; ADE39036; ADE39036; SAR116_0793. DR KEGG; apb:SAR116_0793; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000007460; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000007460}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Hydrolase {ECO:0000313|EMBL:ADE39036.1}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000007460}. FT DOMAIN 198 374 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 430 AA; 47513 MW; BA5D443534555AE9 CRC64; MGSNNAFVIH PDVKYAPTSR PADMMLEEAC MLVEAIGLDV VVAETVNISQ PRAGSFLGKG YADQLAEMAE AYDHPLIIIN TTLSSVQQRN LETLTSCKVI DRTALILEIF GARAQTHAGR LQVELAALTF QRSRLVRSWT HLERQRGGGG FLGGPGERQI ELDRRMLMDR VMRIKGELRE VERTRHLQRR NRDRSETPTL ALIGYTNAGK STLFNMLTGA DVLSKDMLFA TLDPTMRGMK LPSGRRAVLA DTVGFISQLP TELVEAFKST LEEVVEADIL VHVHDASSPM VAEEYADVCQ ILEELGLDAE MQAERVIHIL NKSDKIDDMA GDMAGETREY LENLVGNGVF VSALTGAGID DALLALDEKI NIDDIRLDVM LAPEDGAPRA WLHAHGTVHN SLFDEAGNET VSLTMSIANR NRFQARWPHL // ID D5C2S2_NITHN Unreviewed; 383 AA. AC D5C2S2; DT 15-JUN-2010, integrated into UniProtKB/TrEMBL. DT 15-JUN-2010, sequence version 1. DT 07-JUN-2017, entry version 48. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Nhal_3727 {ECO:0000313|EMBL:ADE16747.1}; OS Nitrosococcus halophilus (strain Nc4). OC Bacteria; Proteobacteria; Gammaproteobacteria; Chromatiales; OC Chromatiaceae; Nitrosococcus. OX NCBI_TaxID=472759 {ECO:0000313|EMBL:ADE16747.1, ECO:0000313|Proteomes:UP000001844}; RN [1] {ECO:0000313|Proteomes:UP000001844} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Nc4 {ECO:0000313|Proteomes:UP000001844}; RG US DOE Joint Genome Institute; RA Campbell M.A., Malfatti S.A., Chain P.S.G., Heidelberg J.F., RA Ward B.B., Klotz M.G.; RT "Complete genome sequence of Nitrosococcus halophilus Nc4, a salt- RT adapted, aerobic obligate ammonia-oxidizing sulfur purple bacterium."; RL Submitted (APR-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001798; ADE16747.1; -; Genomic_DNA. DR RefSeq; WP_013034596.1; NC_013960.1. DR ProteinModelPortal; D5C2S2; -. DR STRING; 472759.Nhal_3727; -. DR EnsemblBacteria; ADE16747; ADE16747; Nhal_3727. DR KEGG; nhl:Nhal_3727; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000001844; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000001844}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000001844}. FT DOMAIN 204 371 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 383 AA; 43519 MW; 7ECA5F23137211AD CRC64; MFEHPKGSGK YSYSAILVHI HFHVPAYAYR EEQAEFRELV SSTGIEVIRT IAGRRQAPHP KYFIGRGKVD EIRGRVDAEQ ANLVVFNHDL SPAQARNLEQ SLQCRVLDRT ELILDIFSQR ARSHEGKLQV ELAQLQHLST RLVRGWSHLE RQKGGIGLRG PGETQLETDR RLIGNRIRQL HKRLGRVRKQ RHQSRRSRHK AQVPTISLVG YTNAGKSTLF NRLTTAQVLA DSRLFATLDP TLRRLRLAMV RPLVLADTVG FIRNLPHDLV EAFRSTLEET RDAALLLHVV DASSEERQVL IAQVNRVLQT IGAEEVPQLE IYNKIDQIEN CQPRLERDAS GRICRVWLSA ASGEGIELLR QALAEYFPAK ETVVNSQQAI RAC // ID D5CRS2_SIDLE Unreviewed; 380 AA. AC D5CRS2; DT 15-JUN-2010, integrated into UniProtKB/TrEMBL. DT 15-JUN-2010, sequence version 1. DT 30-AUG-2017, entry version 52. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Slit_1421 {ECO:0000313|EMBL:ADE11658.1}; OS Sideroxydans lithotrophicus (strain ES-1). OC Bacteria; Proteobacteria; Betaproteobacteria; Nitrosomonadales; OC Gallionellaceae; Sideroxydans. OX NCBI_TaxID=580332 {ECO:0000313|EMBL:ADE11658.1, ECO:0000313|Proteomes:UP000001625}; RN [1] {ECO:0000313|EMBL:ADE11658.1, ECO:0000313|Proteomes:UP000001625} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ES-1 {ECO:0000313|EMBL:ADE11658.1, RC ECO:0000313|Proteomes:UP000001625}; RG US DOE Joint Genome Institute; RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L., RA Pitluck S., Munk A.C., Detter J.C., Han C., Tapia R., Larimer F., RA Land M., Hauser L., Kyrpides N., Ivanova N., Emerson D., Woyke T.; RT "Complete sequence of Sideroxydans lithotrophicus ES-1."; RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001965; ADE11658.1; -; Genomic_DNA. DR RefSeq; WP_013029556.1; NC_013959.1. DR ProteinModelPortal; D5CRS2; -. DR STRING; 580332.Slit_1421; -. DR EnsemblBacteria; ADE11658; ADE11658; Slit_1421. DR KEGG; slt:Slit_1421; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000001625; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000001625}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000001625}. FT DOMAIN 198 365 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 164 191 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 380 AA; 42030 MW; DA734DB8BED60229 CRC64; MHESTTAANT AVLVSLDFGA PDYAESLEEL RLLAESAGVR TLALVEGKRQ RPDASMFAGS GKVEEIAALV EELEAPLVIF NHDLSPAQMR NLAAKIQTRV IDRTMLILDI FALRAQSHEG KVQVELAQLK YLSTRLVGMN MDMGQQKFAV GARGPGETQL ELDRRKLDRR VHLLNERLKQ LKRHRELQRK ARNRSDVMSV SIVGYTNAGK STLFNRLTNA NVYVANQLFA TLDTTARKIF LEGDSHRQVV LSDTVGFIRH LPHGLVAAFR STLEETAQAD LLLHVVDVNS PERHDQVAEV NKVLAEIGAQ HIPQIVVYNK IDLQGLEAGV KRDEYGKITS IHLSARTGAG LAELRAALAE VRDAPVAAAK VEEWHPLNDN // ID D5DQ13_BACMQ Unreviewed; 416 AA. AC D5DQ13; DT 15-JUN-2010, integrated into UniProtKB/TrEMBL. DT 15-JUN-2010, sequence version 1. DT 05-JUL-2017, entry version 54. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:ADE71114.1}; GN OrderedLocusNames=BMQ_4102 {ECO:0000313|EMBL:ADE71114.1}; OS Bacillus megaterium (strain ATCC 12872 / QMB1551). OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus. OX NCBI_TaxID=545693 {ECO:0000313|EMBL:ADE71114.1, ECO:0000313|Proteomes:UP000000935}; RN [1] {ECO:0000313|Proteomes:UP000000935} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 12872 / QMB1551 {ECO:0000313|Proteomes:UP000000935}; RA Eppinger M., Bunk B., Johns M.A., Edirisinghe J.N., Kutumbaka K.K., RA Riley D.R., Creasy H.H., Koenig S.S.K., Galens K., Orvis J., RA Creasy T., Biedendieck R., Braun C., Grayburn S., Jahn D., Ravel J., RA Vary P.S.; RT "Genome sequences of the industrial vitamin B12-producers B. RT megaterium QM B1551 and DSM319 reveal new insights into the Bacillus RT genome evolution and pan-genome structure."; RL Submitted (FEB-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001983; ADE71114.1; -; Genomic_DNA. DR ProteinModelPortal; D5DQ13; -. DR STRING; 545693.BMQ_4102; -. DR EnsemblBacteria; ADE71114; ADE71114; BMQ_4102. DR KEGG; bmq:BMQ_4102; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000000935; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000000935}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000000935}. FT DOMAIN 197 358 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 156 190 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 416 AA; 47378 MW; 57A59CD4F492F4F8 CRC64; MNTELERVIL VGCQLHDDDE RFEYSMDELA SLTETAKGEV LVRLTQKRDR IHPATYIGKG KVEELVALEE ELEPDLIVFN DELSPSQIRN LSAGLSARII DRTQLILDIF AQRAQTREGK MQVELAQLNY LLPRLVGQGT ALSRLGGGIG TRGPGETKLE SDRRHIRRKI DEIKRQLKTV VSHRERYRER RKRNHVYQIA IVGYTNAGKS TIFNRLTEAG IFEENQLFAT LDPTTRQYTL PSGLTALLTD TVGFIQDLPT TLVAAFRSTL EEVTEADLVL HVVDSSNPDY NNHEKTVHRL LEELNVTDIP MLTVYNKEDM QHELFVPSAS TSLSMSAFKA ADLVKLGERI QEEMKKEMAF FHVLLPAYEG KMLAELKTVS IVESLKFNEE TEKYQCKGYI AKEHPLYKKL QTLEES // ID D5E6X8_METMS Unreviewed; 428 AA. AC D5E6X8; DT 15-JUN-2010, integrated into UniProtKB/TrEMBL. DT 15-JUN-2010, sequence version 1. DT 07-JUN-2017, entry version 50. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Mmah_1418 {ECO:0000313|EMBL:ADE36916.1}; OS Methanohalophilus mahii (strain ATCC 35705 / DSM 5219 / SLP). OC Archaea; Euryarchaeota; Methanomicrobia; Methanosarcinales; OC Methanosarcinaceae; Methanohalophilus. OX NCBI_TaxID=547558 {ECO:0000313|EMBL:ADE36916.1, ECO:0000313|Proteomes:UP000001059}; RN [1] {ECO:0000313|EMBL:ADE36916.1, ECO:0000313|Proteomes:UP000001059} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 35705 / DSM 5219 / SLP RC {ECO:0000313|Proteomes:UP000001059}; RG US DOE Joint Genome Institute (JGI-PGF); RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., RA Tice H., Bruce D., Goodwin L., Pitluck S., Kyrpides N., Mavromatis K., RA Ivanova N., Lykidis A., Saunders E., Brettin T., Detter J.C., Han C., RA Land M., Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P., RA Woyke T., Wu D., Spring S., Schneider S., Schroeder M., Klenk H.-P., RA Eisen J.A.; RT "The complete genome of Methanohalophilus mahii DSM 5219."; RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001994; ADE36916.1; -; Genomic_DNA. DR RefSeq; WP_013037858.1; NC_014002.1. DR ProteinModelPortal; D5E6X8; -. DR STRING; 547558.Mmah_1418; -. DR EnsemblBacteria; ADE36916; ADE36916; Mmah_1418. DR GeneID; 8983591; -. DR KEGG; mmh:Mmah_1418; -. DR eggNOG; arCOG00353; Archaea. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG093Z07D6; -. DR Proteomes; UP000001059; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000001059}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000001059}. FT DOMAIN 191 360 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 428 AA; 48912 MW; B2BB334C74AC19A3 CRC64; MKDVIIVQRR IPRCSESENQ RKLAELRELA WAGNYNVVQE VIQTRYPDRQ YQIGKGKAEE LAELALSQKP AKIICYNPLS VTQVYNLSEM CKCEVIDKFQ LILEIFATRA TTRRSRMQVE LARLEYELPR ARKIVSLLKM EERPGFMGLG GYEDSYEQDI KKRISRIKKE LSTVQRDSEN LRGYRHGEGF SLLCLAGYTN AGKSTLFRAL VDENVEVENM LFTTLSPTTR YLGINGRWTL LTDTVGFIED LPHFLVDAFR STLEDVFRAD IILLVVDISE PVDVIRKKLA VSHEIFWEQL EKATIITAIN KADRLSPEEL SSRLKSIAYL APNPVVVSAK TVEGLDELKD VIYSHLPEWK RFTLELPMSG ESMSAVSWLF EEGIVHSVNY GNNIVMDVEA RNEVYRKARS LEKRLSSGNT AESTSKDL // ID D5EF79_AMICL Unreviewed; 378 AA. AC D5EF79; DT 15-JUN-2010, integrated into UniProtKB/TrEMBL. DT 15-JUN-2010, sequence version 1. DT 07-JUN-2017, entry version 60. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Amico_1087 {ECO:0000313|EMBL:ADE57211.1}; OS Aminobacterium colombiense (strain DSM 12261 / ALA-1). OC Bacteria; Synergistetes; Synergistia; Synergistales; Synergistaceae; OC Aminobacterium. OX NCBI_TaxID=572547 {ECO:0000313|EMBL:ADE57211.1, ECO:0000313|Proteomes:UP000002366}; RN [1] {ECO:0000313|EMBL:ADE57211.1, ECO:0000313|Proteomes:UP000002366} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 12261 / ALA-1 {ECO:0000313|Proteomes:UP000002366}; RX PubMed=21304712; RA Chertkov O., Sikorski J., Brambilla E., Lapidus A., Copeland A., RA Glavina Del Rio T., Nolan M., Lucas S., Tice H., Cheng J.F., Han C., RA Detter J.C., Bruce D., Tapia R., Goodwin L., Pitluck S., Liolios K., RA Ivanova N., Mavromatis K., Ovchinnikova G., Pati A., Chen A., RA Palaniappan K., Land M., Hauser L., Chang Y.J., Jeffries C.D., RA Spring S., Rohde M., Goker M., Bristow J., Eisen J.A., Markowitz V., RA Hugenholtz P., Kyrpides N.C., Klenk H.P.; RT "Complete genome sequence of Aminobacterium colombiense type strain RT (ALA-1)."; RL Stand. Genomic Sci. 2:280-289(2010). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001997; ADE57211.1; -; Genomic_DNA. DR RefSeq; WP_013048474.1; NC_014011.1. DR ProteinModelPortal; D5EF79; -. DR STRING; 572547.Amico_1087; -. DR EnsemblBacteria; ADE57211; ADE57211; Amico_1087. DR KEGG; aco:Amico_1087; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000002366; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000002366}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000002366}. FT DOMAIN 205 376 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 164 191 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 378 AA; 42624 MW; 23D83039C6958C51 CRC64; MKRVIDIDGG ARHQRAVVAA LDIPAQDYTP RILLDELKML LVNLNIDVAG EVIQRRDKPD PAYMLGKGKA EESALFCKEV KADLFVCNEQ LTPGQRLNLQ QILGIEIWDR PFVIMKIFER RARTTEARLQ IELAMCQYEI PHLKGLGRQM SRLGAGIGTR GPGETEFERH RRKLERRVRD INERLVKVRK RRTFQRYRRE KAGIPTVALT GYTNSGKSTL LQQLSHGRNL YVADQLFSTL DTYVRKVELS DGHDVLVSDT VGFIRDLPPA LIAAFRTTLE EISVSSLILL VLDGSMPDVM ETLDVVEETL SDIGAGAIPR LIVLNKIDKI DLSLIPFLQT RLQGRSKAKV LPICALSGVG VTELLQEVEY QLFNKMAK // ID D5EHN5_CORAD Unreviewed; 421 AA. AC D5EHN5; DT 15-JUN-2010, integrated into UniProtKB/TrEMBL. DT 15-JUN-2010, sequence version 1. DT 07-JUN-2017, entry version 55. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Caka_1054 {ECO:0000313|EMBL:ADE54076.1}; OS Coraliomargarita akajimensis (strain DSM 45221 / IAM 15411 / JCM 23193 OS / KCTC 12865 / 04OKA010-24). OC Bacteria; Verrucomicrobia; Opitutae; Puniceicoccales; OC Puniceicoccaceae; Coraliomargarita. OX NCBI_TaxID=583355 {ECO:0000313|EMBL:ADE54076.1, ECO:0000313|Proteomes:UP000000925}; RN [1] {ECO:0000313|EMBL:ADE54076.1, ECO:0000313|Proteomes:UP000000925} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 45221 / IAM 15411 / JCM 23193 / KCTC 12865 RC {ECO:0000313|Proteomes:UP000000925}; RX PubMed=21304713; DOI=10.4056/sigs.952166; RA Mavromatis K., Abt B., Brambilla E., Lapidus A., Copeland A., RA Deshpande S., Nolan M., Lucas S., Tice H., Cheng J.F., Han C., RA Detter J.C., Woyke T., Goodwin L., Pitluck S., Held B., Brettin T., RA Tapia R., Ivanova N., Mikhailova N., Pati A., Liolios K., Chen A., RA Palaniappan K., Land M., Hauser L., Chang Y.J., Jeffries C.D., RA Rohde M., Goker M., Bristow J., Eisen J.A., Markowitz V., RA Hugenholtz P., Klenk H.P., Kyrpides N.C.; RT "Complete genome sequence of Coraliomargarita akajimensis type strain RT (04OKA010-24)."; RL Stand. Genomic Sci. 2:290-299(2010). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001998; ADE54076.1; -; Genomic_DNA. DR RefSeq; WP_013042798.1; NC_014008.1. DR ProteinModelPortal; D5EHN5; -. DR STRING; 583355.Caka_1054; -. DR EnsemblBacteria; ADE54076; ADE54076; Caka_1054. DR KEGG; caa:Caka_1054; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000000925; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000000925}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000000925}. FT DOMAIN 198 364 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 421 AA; 47361 MW; 6D506F76BCE459BB CRC64; MVERAMLIGI TLPDEESSTT LSLLDELREL VNTLGISIAH ERQLSIRKPQ AKFLVGSGKA DELIEEARAH QCDVIVFDNE LTPAQQRNWE QAGNNKILVI DRQEVILDIF GDRAQTKEAV LQVELARLEY NLPRLKRAWT HLDRQRGGGA MQRDAGETQL ELDQRMVRTQ IARVKRELDS VIQHRHLQRK KRMTVPVPTC AIVGYTNAGK SSLLNKLTNS DILAEDKLFA TLDPTSRRCP LPSGQPLVIT DTVGFVRNLP HRLVDAFKAT LEEAVVSNFL LHVLDVNSPE VEAHAETTLS VLHELGAKDK QIITVFNKID ALWDPETMDS LKLRYPDAFF ISAHSGEGVD QLLAAIEAII EANYAQLRLL IPHSRYDLVA RMHREGAVRK EEARDDGTYL VGSVPERMLS AIQEFILQAE D // ID D5EVI1_PRER2 Unreviewed; 443 AA. AC D5EVI1; DT 15-JUN-2010, integrated into UniProtKB/TrEMBL. DT 15-JUN-2010, sequence version 1. DT 07-JUN-2017, entry version 54. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=PRU_0115 {ECO:0000313|EMBL:ADE81131.1}; OS Prevotella ruminicola (strain ATCC 19189 / JCM 8958 / 23). OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Prevotellaceae; OC Prevotella. OX NCBI_TaxID=264731 {ECO:0000313|EMBL:ADE81131.1, ECO:0000313|Proteomes:UP000000927}; RN [1] {ECO:0000313|EMBL:ADE81131.1, ECO:0000313|Proteomes:UP000000927} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 19189 / JCM 8958 / 23 {ECO:0000313|Proteomes:UP000000927}; RX PubMed=20585943; DOI=10.1007/s00248-010-9692-8; RG North American Consortium for Rumen Bacteria; RA Purushe J., Fouts D.E., Morrison M., White B.A., Mackie R.I., RA Coutinho P.M., Henrissat B., Nelson K.E.; RT "Comparative genome analysis of Prevotella ruminicola and Prevotella RT bryantii: insights into their environmental niche."; RL Microb. Ecol. 60:721-729(2010). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002006; ADE81131.1; -; Genomic_DNA. DR RefSeq; WP_013063118.1; NC_014033.1. DR ProteinModelPortal; D5EVI1; -. DR STRING; 264731.PRU_0115; -. DR EnsemblBacteria; ADE81131; ADE81131; PRU_0115. DR GeneID; 31499669; -. DR KEGG; pru:PRU_0115; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000000927; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 2. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000000927}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000000927}. FT DOMAIN 239 428 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 443 AA; 50498 MW; C85956B400503D0E CRC64; MKEFVISEAK AETAVLVGLI TKEQNEAKTK EYLDELEFLA DTAGAVTVKR FTQKVGGPSQ TTYVGSGKLL EIKEYIKQCQ DAYDEWLDEQ DASLFAEGLL DESNAPQPVG MVIFDDELSA KQMRNIEKEL QVKILDRTSL ILDIFAMRAQ TAEAKAQVEL AQHRYMLPRL QRLWTHLERQ GGGSGSGGGK GSVGLRGPGE TQLEMDRRII LQRITLLKQR LAEIDKQKTT QRKNRGRLIR VALVGYTNVG KSTMMNLLAK SEVFAENKLF ATLDTTVRKM TIDNLPFLLA DTVGFIRKLP SDLVESFKST LDEVREADLL VHVVDISHPD FEDQIRVVEE TLKELGCADK PAMLVFNKID AYTWVEKEED DLTPATKENM TLEDLEKTWM ARTGENQHYL ECLFISAKQK DNIDALRDIL YKRVRELHVQ KYPYNDFLYQ DYE // ID D5GZK4_LACCS Unreviewed; 421 AA. AC D5GZK4; DT 15-JUN-2010, integrated into UniProtKB/TrEMBL. DT 15-JUN-2010, sequence version 1. DT 07-JUN-2017, entry version 53. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:CBL51213.1}; GN OrderedLocusNames=LCRIS_01766 {ECO:0000313|EMBL:CBL51213.1}; OS Lactobacillus crispatus (strain ST1). OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; OC Lactobacillus. OX NCBI_TaxID=748671 {ECO:0000313|EMBL:CBL51213.1, ECO:0000313|Proteomes:UP000002371}; RN [1] {ECO:0000313|EMBL:CBL51213.1, ECO:0000313|Proteomes:UP000002371} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ST1 {ECO:0000313|EMBL:CBL51213.1, RC ECO:0000313|Proteomes:UP000002371}; RX PubMed=20435723; DOI=10.1128/JB.00399-10; RA Ojala T., Kuparinen V., Koskinen J.P., Alatalo E., Holm L., RA Auvinen P., Edelman S., Westerlund-Wikstrom B., Korhonen T.K., RA Paulin L., Kankainen M.; RT "Genome sequence of Lactobacillus crispatus ST1."; RL J. Bacteriol. 192:3547-3548(2010). RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ST1; RA Ojala T., Kuparinen V., Koskinen J.P., Alatalo E., Holm L., RA Auvinen P., Edelman S., Westerlund-Wikstroem B., Korhonen T.K., RA Paulin L., Kankainen M.; RT "Genome Sequence of Lactobacillus crispatus ST1."; RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; FN692037; CBL51213.1; -; Genomic_DNA. DR RefSeq; WP_013086893.1; NC_014106.1. DR ProteinModelPortal; D5GZK4; -. DR STRING; 748671.LCRIS_01766; -. DR EnsemblBacteria; CBL51213; CBL51213; LCRIS_01766. DR GeneID; 9106806; -. DR KEGG; lcr:LCRIS_01766; -. DR PATRIC; fig|748671.3.peg.1738; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; FNNHAHV; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000002371; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000002371}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000002371}. FT DOMAIN 199 368 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 421 AA; 47380 MW; D9DF9C9B8CE49CA4 CRC64; MIDNQPKKTK AYIAGVNLND PNFDYYMTEL ANLTEANNME VVGQSFQNAE SIVAGTYFGV GKINEIRTMA QGLKAKVLVL NDELTPVQIR NLEKLTKMRV IDRTELILEI FSNRARTKQA KLQVQLARLQ YELPRLHPSE NNLDQQRGGG FANRGAGESK LELNRRTIGK QISAIKKELK AVASQEEIKA ARRNQSRLPK VALVGYTNAG KSTTMNGLLR EFSKEAADKQ VFVKNMLFAT LDTSVRRIDL KDNFSFILSD TVGFISKLPH NLVESFKATL QETRDADLLI NVVDASDPNM VQMIRTTQNV LDEIGVKGIP MITAYNKADK TDRNYPQIEG DDILYSAIDP KSIKLLADLI TKRVFANYEK FDLILPLSAG KELAYLHDHA QVLREDYQDD GVHIEANIAP DDQGRFRQYL A // ID D5MET7_9BACT Unreviewed; 389 AA. AC D5MET7; DT 15-JUN-2010, integrated into UniProtKB/TrEMBL. DT 15-JUN-2010, sequence version 1. DT 07-JUN-2017, entry version 45. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:CBE68266.1}; GN ORFNames=DAMO_1206 {ECO:0000313|EMBL:CBE68266.1}; OS Candidatus Methylomirabilis oxyfera. OC Bacteria; candidate division NC10; Candidatus Methylomirabilis. OX NCBI_TaxID=671143 {ECO:0000313|EMBL:CBE68266.1, ECO:0000313|Proteomes:UP000006898}; RN [1] {ECO:0000313|EMBL:CBE68266.1, ECO:0000313|Proteomes:UP000006898} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=20336137; DOI=10.1038/nature08883; RA Ettwig K.F., Butler M.K., Le Paslier D., Pelletier E., Mangenot S., RA Kuypers M.M.M., Schreiber F., Dutilh B.E., Zedelius J., de Beer D., RA Gloerich J., Wessels H.J.C.T., van Allen T., Luesken F., Wu M., RA van de Pas-Schoonen K.T., Op den Camp H.J.M., Janssen-Megens E.M., RA Francoijs K-J., Stunnenberg H., Weissenbach J., Jetten M.S.M., RA Strous M.; RT "Nitrite-driven anaerobic methane oxidation by oxygenic bacteria."; RL Nature 464:543-548(2010). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; FP565575; CBE68266.1; -; Genomic_DNA. DR ProteinModelPortal; D5MET7; -. DR KEGG; mox:DAMO_1206; -. DR PATRIC; fig|671143.5.peg.1057; -. DR KO; K03665; -. DR BioCyc; CMET671143:G131O-1148-MONOMER; -. DR Proteomes; UP000006898; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000006898}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000006898}. FT DOMAIN 206 373 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 165 192 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 389 AA; 43002 MW; 7E149B20FD66E930 CRC64; MKGTIASALV GEPRERALLV GIHRKRDPRW EAEDSLDELA RLAGSAGAVV IGTILQDRDV PDPRYLIGKG KAQEIKAQWG GKVDLLVIDE ELSGSQQRSL EELTGWKTVD RPLLILDIFS QRARSREGKL QVELAQLDYR LPRLVGMGTQ LSRLGGGIGT RGPGETQLET DRRTIRRRMA KIREELAKVR RHRALLRRPR KRHAIPIVAL VGYTNAGKST LFNALTHSGV QTDDALFVTL DPILRRVTMA DGFGFLLSDT VGFIRRLPEQ LVTAFKATLE ELDEADLLLH VIDASHPQVM EQKEAVDTIL RELGLSTKPI VEVFNKMDRL TGGIGQSFIG GKTIVPRVAI SALTGYGLDR LLQTVRESLA PTASQARGYD RLPYPAAHA // ID D5PJL7_9MYCO Unreviewed; 484 AA. AC D5PJL7; DT 13-JUL-2010, integrated into UniProtKB/TrEMBL. DT 13-JUL-2010, sequence version 1. DT 07-JUN-2017, entry version 40. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:EFG73730.1}; GN ORFNames=HMPREF0591_6361 {ECO:0000313|EMBL:EFG73730.1}; OS Mycobacterium parascrofulaceum ATCC BAA-614. OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae; OC Mycobacterium. OX NCBI_TaxID=525368 {ECO:0000313|EMBL:EFG73730.1, ECO:0000313|Proteomes:UP000003653}; RN [1] {ECO:0000313|EMBL:EFG73730.1, ECO:0000313|Proteomes:UP000003653} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-614 {ECO:0000313|EMBL:EFG73730.1, RC ECO:0000313|Proteomes:UP000003653}; RA Muzny D., Qin X., Deng J., Jiang H., Liu Y., Qu J., Song X.-Z., RA Zhang L., Thornton R., Coyle M., Francisco L., Jackson L., Javaid M., RA Korchina V., Kovar C., Mata R., Mathew T., Ngo R., Nguyen L., RA Nguyen N., Okwuonu G., Ongeri F., Pham C., Simmons D., RA Wilczek-Boney K., Hale W., Jakkamsetti A., Pham P., Ruth R., RA San Lucas F., Warren J., Zhang J., Zhao Z., Zhou C., Zhu D., Lee S., RA Bess C., Blankenburg K., Forbes L., Fu Q., Gubbala S., Hirani K., RA Jayaseelan J.C., Lara F., Munidasa M., Palculict T., Patil S., RA Pu L.-L., Saada N., Tang L., Weissenberger G., Zhu Y., Hemphill L., RA Shang Y., Youmans B., Ayvaz T., Ross M., Santibanez J., Aqrawi P., RA Gross S., Joshi V., Fowler G., Nazareth L., Reid J., Worley K., RA Petrosino J., Highlander S., Gibbs R.; RL Submitted (APR-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EFG73730.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADNV01000399; EFG73730.1; -; Genomic_DNA. DR ProteinModelPortal; D5PJL7; -. DR EnsemblBacteria; EFG73730; EFG73730; HMPREF0591_6361. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000003653; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 2. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000003653}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}. FT DOMAIN 257 430 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 216 250 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 484 AA; 51990 MW; E34873CA69097140 CRC64; MHHSVLPMTH PDFSNPAVPE PSTGELALEE RSALRRIAGL STELADVSEV EYRQLRLERV VLVGVWTDGT AADSEASMAE LAALAETAGS QVLEGLIQRR DKPDPSTYIG SGKAQELREV VLATGADTVI CDGELSPAQL TALEKAVKVK VIDRTALILD IFAQHATSRE GKAQVSLAQM EYMLPRLRGW GESMSRQAGG RAGGSGGGVG LRGPGETKIE TDRRRIRERM SKLRREIKDM KQVRDTQRSR RLASDAPSIA IVGYTNAGKS SLLNALTGAG VLVQDALFAT LEPTTRRAEF GADSKRAGAY TITDTVGFVR HLPTQLVEAF RSTLEEVVDA DLLLHVVDGS DANPLAQINA VRAVVSDVVA DHHGDPPPEL LVVNKIDAAS DLTLAKLRHA LPGAVFVSAR TGDGIDALRT RMAELAVPAD TAVDVVIPYH RGDLVARLHA DGRVQQEEHN PDGTRIKARV PVALAGRLQE FSAR // ID D5QCI7_KOMHA Unreviewed; 436 AA. AC D5QCI7; DT 13-JUL-2010, integrated into UniProtKB/TrEMBL. DT 13-JUL-2010, sequence version 1. DT 07-JUN-2017, entry version 40. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=GXY_04200 {ECO:0000313|EMBL:EFG85239.1}; OS Komagataeibacter hansenii ATCC 23769. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales; OC Acetobacteraceae; Komagataeibacter. OX NCBI_TaxID=714995 {ECO:0000313|EMBL:EFG85239.1, ECO:0000313|Proteomes:UP000006468}; RN [1] {ECO:0000313|EMBL:EFG85239.1, ECO:0000313|Proteomes:UP000006468} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 23769 {ECO:0000313|EMBL:EFG85239.1, RC ECO:0000313|Proteomes:UP000006468}; RX PubMed=20543071; DOI=10.1128/JB.00588-10; RA Iyer P.R., Geib S.M., Catchmark J., Kao T.H., Tien M.; RT "Genome sequence of a cellulose-producing bacterium, Gluconacetobacter RT hansenii ATCC 23769."; RL J. Bacteriol. 192:4256-4257(2010). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EFG85239.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADTV01000011; EFG85239.1; -; Genomic_DNA. DR RefSeq; WP_003617959.1; NZ_CM000920.1. DR ProteinModelPortal; D5QCI7; -. DR STRING; 714995.GXY_04200; -. DR EnsemblBacteria; EFG85239; EFG85239; GXY_04200. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR Proteomes; UP000006468; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000006468}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000006468}. FT DOMAIN 206 375 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 436 AA; 47882 MW; 388F78EE13083F2B CRC64; MTSAPGPVMT RAAVILPWER PDRQDESRAA EARLEEAVGL AASIGLVIIC KAVLLLRARR PATLLGSGQV ESLHATVRAD NITVVIIDSR LTPVQQRNLE RALGCKVIDR TALILDIFGE RAATKEGSLQ VELAHLEYQR SRLVRTWTHL ERQRGGFGFL GGPGETQIEA DRRMIGDRIV RLKRELEQVR RTRGLHRQAR RRVPFPVVAL VGYTNAGKST LFNALTGASV YAQDQLFATL DPTMRGIRLP SGRQIILSDT VGFISDLPTE LIAAFRATLE EVAEADIILH VRDASHPETS AQRADVVEVL EGMAHSGTIE PDWQSRVIEV LNKADLMGGR DAVGARPGAI VISAITGDGL PDLLAAIDER LTHAMELVRY RVPLSDGAAM AWLYEHGEVV ERTDHEDGVD MHVRLSPANR ARFEMQHATG ITCLDS // ID D5RQ48_9PROT Unreviewed; 393 AA. AC D5RQ48; DT 13-JUL-2010, integrated into UniProtKB/TrEMBL. DT 13-JUL-2010, sequence version 1. DT 07-JUN-2017, entry version 38. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:EFH10574.1}; GN ORFNames=HMPREF0731_3210 {ECO:0000313|EMBL:EFH10574.1}; OS Roseomonas cervicalis ATCC 49957. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales; OC Acetobacteraceae; Roseomonas. OX NCBI_TaxID=525371 {ECO:0000313|EMBL:EFH10574.1, ECO:0000313|Proteomes:UP000005324}; RN [1] {ECO:0000313|EMBL:EFH10574.1, ECO:0000313|Proteomes:UP000005324} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 49957 {ECO:0000313|EMBL:EFH10574.1, RC ECO:0000313|Proteomes:UP000005324}; RA Qin X., Bachman B., Battles P., Bell A., Bess C., Bickham C., RA Chaboub L., Chen D., Coyle M., Deiros D.R., Dinh H., Forbes L., RA Fowler G., Francisco L., Fu Q., Gubbala S., Hale W., Han Y., RA Hemphill L., Highlander S.K., Hirani K., Hogues M., Jackson L., RA Jakkamsetti A., Javaid M., Jiang H., Korchina V., Kovar C., Lara F., RA Lee S., Mata R., Mathew T., Moen C., Morales K., Munidasa M., RA Nazareth L., Ngo R., Nguyen L., Okwuonu G., Ongeri F., Patil S., RA Petrosino J., Pham C., Pham P., Pu L.-L., Puazo M., Raj R., Reid J., RA Rouhana J., Saada N., Shang Y., Simmons D., Thornton R., Warren J., RA Weissenberger G., Zhang J., Zhang L., Zhou C., Zhu D., Muzny D., RA Worley K., Gibbs R.; RL Submitted (APR-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EFH10574.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADVL01000656; EFH10574.1; -; Genomic_DNA. DR ProteinModelPortal; D5RQ48; -. DR EnsemblBacteria; EFH10574; EFH10574; HMPREF0731_3210. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000005324; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000005324}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000005324}. FT DOMAIN 169 342 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 393 AA; 42967 MW; 2D3AD4BAFF539E28 CRC64; MGLAASIGLT IVHSAVFPLR NRRPSTLLGE GQVEMAAEAI EENQIGVVVV DAALTPVQQR NLERQWHCKV IDRTGLILEI FGERARTKEG TLQVELAHLE YQRTRLVRSW THLERQRGGF GFLGGPGESQ IEIDRRLIGE RIVKLKRELE QVRRTRGLHR AARTRVPFPV VALVGYTNAG KSTLFNALTG AGVYAQDQLF ATLDPTMRAI RLPSGRTVIL SDTVGFISDL PTQLIEAFRA TLEEVAAADI ILHVRDVAHP DTTAQRNDVV GVLSEMAKGE HPTLDENWPA RTIEVLNKAD LLGGIAEVPG LDDAASVAVS ALTGEGLDAL RSALDARLAA GMEIADYALP PSDGARIAWL YQHGEVLTRE DGEEVVRLTV RLSPADRARF EQG // ID D5SXH6_PLAL2 Unreviewed; 464 AA. AC D5SXH6; DT 13-JUL-2010, integrated into UniProtKB/TrEMBL. DT 13-JUL-2010, sequence version 1. DT 07-JUN-2017, entry version 54. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Plim_1713 {ECO:0000313|EMBL:ADG67543.1}; OS Planctopirus limnophila (strain ATCC 43296 / DSM 3776 / IFAM 1008 / OS 290) (Planctomyces limnophilus). OC Bacteria; Planctomycetes; Planctomycetia; Planctomycetales; OC Planctomycetaceae; Planctopirus. OX NCBI_TaxID=521674 {ECO:0000313|EMBL:ADG67543.1, ECO:0000313|Proteomes:UP000002220}; RN [1] {ECO:0000313|EMBL:ADG67543.1, ECO:0000313|Proteomes:UP000002220} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43296 / DSM 3776 / IFAM 1008 / 290 RC {ECO:0000313|Proteomes:UP000002220}; RX PubMed=21304691; DOI=10.4056/sigs.1052813; RA Labutti K., Sikorski J., Schneider S., Nolan M., Lucas S., RA Glavina Del Rio T., Tice H., Cheng J.F., Goodwin L., Pitluck S., RA Liolios K., Ivanova N., Mavromatis K., Mikhailova N., Pati A., RA Chen A., Palaniappan K., Land M., Hauser L., Chang Y.J., RA Jeffries C.D., Tindall B.J., Rohde M., Goker M., Woyke T., Bristow J., RA Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P., RA Lapidus A.; RT "Complete genome sequence of Planctomyces limnophilus type strain (Mu RT 290)."; RL Stand. Genomic Sci. 3:47-56(2010). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001744; ADG67543.1; -; Genomic_DNA. DR ProteinModelPortal; D5SXH6; -. DR STRING; 521674.Plim_1713; -. DR EnsemblBacteria; ADG67543; ADG67543; Plim_1713. DR KEGG; plm:Plim_1713; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000002220; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000002220}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000002220}. FT DOMAIN 230 396 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 198 225 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 464 AA; 52004 MW; 38A2675B6BFE4723 CRC64; MNNQHVGHVF LKIKDSDLFL PALDEPLNQP LRNDLQTINK TAVLVAVCLN DNKRSRENVL DELKGLVKTA GVKVVGELVQ FRQMVHPGTC LGPGKIEELK LILEETRAEL VIFDNNLTPG QGRRLEQETG RVIVDRSELI LDIFATHART AEARLQVELA QLQYNRTRLK RLWTHLERID GGIGASRGPG EKQIETDRRL IDQRISELQS SLKEVEQRRE RMVKQRRDHA LVSLVGYTNA GKSTLMRALT GEEVYIADQL FATLDTKTRL WKIPGWGDAL LSDTVGFVRD LPHSLVASFK STLEEARHAD LLLHVVDASN PEAEAQVATV EAVLEEIGVE LKNFILVLNK ADQVPDRMAL DLLRARYEWS VSISARTGDG LDRLAQLVVD RLGDGLESVT VSTGIEDGKL LGWLSEHATI IDTHYSETTA TFRCRISRSM LPRLRQRGTV LEDHHDQSSL EAVG // ID D5U341_THEAM Unreviewed; 355 AA. AC D5U341; DT 13-JUL-2010, integrated into UniProtKB/TrEMBL. DT 13-JUL-2010, sequence version 1. DT 07-JUN-2017, entry version 55. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Tagg_1278 {ECO:0000313|EMBL:ADG91541.1}; OS Thermosphaera aggregans (strain DSM 11486 / M11TL). OC Archaea; Crenarchaeota; Thermoprotei; Desulfurococcales; OC Desulfurococcaceae; Thermosphaera. OX NCBI_TaxID=633148 {ECO:0000313|EMBL:ADG91541.1, ECO:0000313|Proteomes:UP000002376}; RN [1] {ECO:0000313|Proteomes:UP000002376} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 11486 / M11TL {ECO:0000313|Proteomes:UP000002376}; RX DOI=10.4056/sigs.821804; RA Spring S., Rachel R., Lapidus A., Davenport K., Tice H., Copeland A., RA Cheng J.-F., Lucas S., Chen F., Nolan M., Bruce D., Goodwin L., RA Pitluck S., Ivanova N., Mavromatis K., Ovchinnikova G., Pati A., RA Chen A., Palaniappan K., Land M., Hauser L., Chang Y.-J., RA Jeffries C.C., Brettin T., Detter J.C., Tapia R., Han C., Heimerl T., RA Weikl F., Brambilla E., Goker M., Bristow J., Eisen J.A., RA Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.-P.; RT "Complete genome sequence of Thermosphaera aggregans type strain RT (M11TLT)."; RL Stand. Genomic Sci. 2:245-259(2010). RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 11486; RG US DOE Joint Genome Institute (JGI-PGF); RA Spring S., Lapidus A., Munk C., Schroeder M., Glavina Del Rio T., RA Tice H., Copeland A., Cheng J.-F., Lucas S., Chen F., Nolan M., RA Bruce D., Goodwin L., Pitluck S., Ivanova N., Mavromatis K., RA Ovchinnikova G., Pati A., Chen A., Palaniappan K., Land M., Hauser L., RA Chang Y.-J., Jeffries C.C., Brettin T., Detter J.C., Tapia R., Han C., RA Chain P., Heimerl T., Weik F., Goker M., Rachel R., Bristow J., RA Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.-P.; RT "Complete genome sequence of Thermosphaera aggregans type strain RT (M11TL)."; RL Submitted (FEB-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001939; ADG91541.1; -; Genomic_DNA. DR RefSeq; WP_013130134.1; NC_014160.1. DR ProteinModelPortal; D5U341; -. DR STRING; 633148.Tagg_1278; -. DR EnsemblBacteria; ADG91541; ADG91541; Tagg_1278. DR GeneID; 9166323; -. DR KEGG; tag:Tagg_1278; -. DR eggNOG; arCOG00353; Archaea. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; FNNHAHV; -. DR OrthoDB; POG093Z07D6; -. DR Proteomes; UP000002376; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000002376}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000002376}. FT DOMAIN 179 353 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 355 AA; 40648 MW; 8E6671190D1EBB34 CRC64; MIVEVAVPKK YVEYLDEEIS LVKTIYPVVG NVFVVKKPNR KTYISATILD ELREKRFDKL VVMDSLKPTQ IINLVRELRK DVIDRSMLIL EIFANHAGSL EAKLQIELAQ LRHNLPLIKE AIRYAKIGEM HGFLGAGEYG FEKYYFMLKR RENKVRREIE RVRKTRALRR ERRERLGYPH VAIIGYTCAG KTTLFNRLTM LSKPVGPEPF TTLTPKSYKV RFNTIEAVVT DTVGFIRDLP PEVLEAFYAT LEEVAESDLI LNVIDSSKPL KRIIDEVETS MSILGKIGCR GKPLIHVLNK IDLVSSGRLK EVMEGLERAL NNSQDSIIPV SAEKNINIDE LVLLVESTLK RVLKR // ID D5UDQ2_CELFN Unreviewed; 505 AA. AC D5UDQ2; DT 13-JUL-2010, integrated into UniProtKB/TrEMBL. DT 13-JUL-2010, sequence version 1. DT 07-JUN-2017, entry version 52. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Cfla_1562 {ECO:0000313|EMBL:ADG74460.1}; OS Cellulomonas flavigena (strain ATCC 482 / DSM 20109 / NCIB 8073 / NRS OS 134). OC Bacteria; Actinobacteria; Micrococcales; Cellulomonadaceae; OC Cellulomonas. OX NCBI_TaxID=446466 {ECO:0000313|EMBL:ADG74460.1, ECO:0000313|Proteomes:UP000000849}; RN [1] {ECO:0000313|EMBL:ADG74460.1, ECO:0000313|Proteomes:UP000000849} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 482 / DSM 20109 / NCIB 8073 / NRS 134 RC {ECO:0000313|Proteomes:UP000000849}; RX PubMed=21304688; RA Abt B., Foster B., Lapidus A., Clum A., Sun H., Pukall R., Lucas S., RA Glavina Del Rio T., Nolan M., Tice H., Cheng J.F., Pitluck S., RA Liolios K., Ivanova N., Mavromatis K., Ovchinnikova G., Pati A., RA Goodwin L., Chen A., Palaniappan K., Land M., Hauser L., Chang Y.J., RA Jeffries C.D., Rohde M., Goker M., Woyke T., Bristow J., Eisen J.A., RA Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.; RT "Complete genome sequence of Cellulomonas flavigena type strain RT (134)."; RL Stand. Genomic Sci. 3:15-25(2010). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001964; ADG74460.1; -; Genomic_DNA. DR RefSeq; WP_013116794.1; NC_014151.1. DR ProteinModelPortal; D5UDQ2; -. DR STRING; 446466.Cfla_1562; -. DR EnsemblBacteria; ADG74460; ADG74460; Cfla_1562. DR KEGG; cfl:Cfla_1562; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000000849; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 2. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000000849}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000000849}. FT DOMAIN 284 450 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 505 AA; 54247 MW; AAD669008627EB5F CRC64; MDDREHTTDE AREAPVRSAQ EVADDVVARV LARAGTALQD GATAHTTFDG DQLDLEERTS LRRVAGLSTE LEDVTEVEYR QLRLERVVLV GLWGAGTVEE AEISLRELAA LAETAGSQVL DGLLQRRRTP DPGTFLGSGK AAELAGLVAA VGADTVVVDG ELAPSQRRAL EDVVKVKVVD RTALILDIFA QHAKSREGKA QVELAQLEYL LPRLRGWGES MSRQAGGQVG GAGAGMGSRG PGETKIELDR RRIRTRMAKL RREIAAMEPA RQTKRASRRR NAIPSVAIAG YTNAGKSSLL NRLTHAGVLV ENALFATLDP TVRRAEAADG RVYTLADTVG FVRHLPHQLV EAFRSTLEEV ADADLILHVV DAAHPDPEGQ IAAVRHVFAD IPGAMDVPEI IVLNKADLAA PEAVARLRSR EVHSIVVSAH TGEGIDELSA LIADQLPRPG VQVEVVVPYT RGDLVSRVHE HGEIDLEEHT EAGTRLRARV DAGLAAELEE ASGAA // ID D5UMD8_TSUPD Unreviewed; 479 AA. AC D5UMD8; DT 13-JUL-2010, integrated into UniProtKB/TrEMBL. DT 13-JUL-2010, sequence version 1. DT 07-JUN-2017, entry version 47. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Tpau_1800 {ECO:0000313|EMBL:ADG78418.1}; OS Tsukamurella paurometabola (strain ATCC 8368 / DSM 20162 / JCM 10117 / OS NBRC 16120 / NCTC 13040) (Corynebacterium paurometabolum). OC Bacteria; Actinobacteria; Corynebacteriales; Tsukamurellaceae; OC Tsukamurella. OX NCBI_TaxID=521096 {ECO:0000313|EMBL:ADG78418.1, ECO:0000313|Proteomes:UP000001213}; RN [1] {ECO:0000313|Proteomes:UP000001213} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 8368 / DSM 20162 / JCM 10117 / NBRC 16120 / NCTC 13040 RC {ECO:0000313|Proteomes:UP000001213}; RG US DOE Joint Genome Institute (JGI-PGF); RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., RA Tice H., Bruce D., Goodwin L., Pitluck S., Kyrpides N., Mavromatis K., RA Ivanova N., Mikhailova N., Munk A.C., Brettin T., Detter J.C., RA Tapia R., Han C., Larimer F., Land M., Hauser L., Markowitz V., RA Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Jando M., Brambilla E., RA Klenk H.-P., Eisen J.A.; RT "The complete chromosome of Tsukamurella paurometabola DSM 20162."; RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001966; ADG78418.1; -; Genomic_DNA. DR RefSeq; WP_013126446.1; NC_014158.1. DR ProteinModelPortal; D5UMD8; -. DR STRING; 521096.Tpau_1800; -. DR EnsemblBacteria; ADG78418; ADG78418; Tpau_1800. DR KEGG; tpr:Tpau_1800; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000001213; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000001213}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000001213}. FT DOMAIN 250 419 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 209 236 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 479 AA; 51630 MW; 281A7A788DD0D552 CRC64; MTDTDTWEPA PGTQPTVGEL QLQERSSLRR VAGLSTELDD VTEVEYRQLR LEQVVLVGVW TEGSAAQADS SLAELAALAE TAGSVVLDGV VQRRDRPDPA TYIGSGKAHE LREVVLATGA DTVICDGELT PAQLNALEKV VKVKVIDRTA LILDIFAQHA TSREGKAQVS LAQMEYMLPR LRGWGEALSR QAGGRAGSNG GVGLRGPGET KIETDRRRIR ERMAKLRREI KGMKQARDTK RGARRRSGVP AVAIAGYTNA GKSSLLNALT DAGVLVQNAL FATLDPTTRH GTLTDGRDVV FTDTVGFVRH LPTQLVEAFR STLEEVVDAD LLVHVVDGSD PMPQRQIDAV RHVLREVAGE REAALPRELL VINKTDAADP MVLAQLRVAL PEAVFVSAHT REGIDELMQR MTDLITAGDV EVSALVPYER GDLVARIHAE GTILATDHEA DGTRITARVP AALAGMLQQF GADAPAVVE // ID D5VB98_MORCB Unreviewed; 469 AA. AC D5VB98; DT 13-JUL-2010, integrated into UniProtKB/TrEMBL. DT 13-JUL-2010, sequence version 1. DT 07-JUN-2017, entry version 47. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:ADG60951.1}; GN OrderedLocusNames=MCR_0683 {ECO:0000313|EMBL:ADG60951.1}; OS Moraxella catarrhalis (strain BBH18). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Moraxellaceae; Moraxella. OX NCBI_TaxID=1236608 {ECO:0000313|Proteomes:UP000000930}; RN [1] {ECO:0000313|EMBL:ADG60951.1, ECO:0000313|Proteomes:UP000000930} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BBH18 {ECO:0000313|EMBL:ADG60951.1, RC ECO:0000313|Proteomes:UP000000930}; RX PubMed=20453089; DOI=10.1128/JB.00121-10; RA de Vries S.P., van Hijum S.A., Schueler W., Riesbeck K., Hays J.P., RA Hermans P.W., Bootsma H.J.; RT "Genome analysis of Moraxella catarrhalis strain RH4, a human RT respiratory tract pathogen."; RL J. Bacteriol. 192:3574-3583(2010). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002005; ADG60951.1; -; Genomic_DNA. DR RefSeq; WP_013107828.1; NC_014147.1. DR ProteinModelPortal; D5VB98; -. DR EnsemblBacteria; ADG60951; ADG60951; MCR_0683. DR GeneID; 9135388; -. DR KEGG; mct:MCR_0683; -. DR PATRIC; fig|1236608.7.peg.709; -. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000000930; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000000930}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Hydrolase {ECO:0000313|EMBL:ADG60951.1}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000000930}. FT DOMAIN 208 373 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 174 201 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 469 AA; 52546 MW; DC81963F63CBD95E CRC64; MQYFDRHEGG ENAILVHLDI HQITDPDDLE EFRLLVHSAG ANEIEIITGS RSKPHAKYFV GTGKAEEIAE AVKRFRDTND DNTDDVIVIF NHTLTPSQER NLESLIKCRV LDRTGLILDI FAQRARTHEG KLQVELAQLN HLATRLVRGW THLERQKGGI GLRGPGETQL ETDRRLLQIR VTQLKAKLDK VKQTRKQGRA KRQKSDIPTI SLVGYTNAGK STLFNHLTDD NIYAADQLFA TLDPTLRRVK WPGVGNVVLA DTVGFVRHLP HELVESFHAT LEETLEADLL LHVIDAASED MHAQIEAVND VLEQIQADAP ILLVFNKIDK SGEPAKIHYQ DHGVPHRVYV SAKENLGINQ LMLAVQELLS GQLNHYTLTL PHHAGALKNT LHELGVIESE SFDELGHQIL SVQLSPAKLT QLLGQYALNP KQVLPPNEAA SLEPALEPFE EVLKQHDDKS DDQLNPFCL // ID D5VS44_METIM Unreviewed; 400 AA. AC D5VS44; DT 13-JUL-2010, integrated into UniProtKB/TrEMBL. DT 13-JUL-2010, sequence version 1. DT 07-JUN-2017, entry version 56. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Metin_0730 {ECO:0000313|EMBL:ADG13397.1}; OS Methanocaldococcus infernus (strain DSM 11812 / JCM 15783 / ME). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=573063 {ECO:0000313|EMBL:ADG13397.1, ECO:0000313|Proteomes:UP000002061}; RN [1] {ECO:0000313|EMBL:ADG13397.1, ECO:0000313|Proteomes:UP000002061} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 11812 / JCM 15783 / ME {ECO:0000313|Proteomes:UP000002061}; RG US DOE Joint Genome Institute; RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L., RA Pitluck S., Munk A.C., Detter J.C., Han C., Tapia R., Land M., RA Hauser L., Kyrpides N., Mikhailova N., Sieprawska-Lupa M., RA Whitman W.B., Woyke T.; RT "Complete sequence of Methanocaldococcus infernus ME."; RL Submitted (APR-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002009; ADG13397.1; -; Genomic_DNA. DR RefSeq; WP_013100143.1; NC_014122.1. DR ProteinModelPortal; D5VS44; -. DR STRING; 573063.Metin_0730; -. DR EnsemblBacteria; ADG13397; ADG13397; Metin_0730. DR GeneID; 9131741; -. DR KEGG; mif:Metin_0730; -. DR eggNOG; arCOG00353; Archaea. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; FNNHAHV; -. DR OrthoDB; POG093Z07D6; -. DR Proteomes; UP000002061; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000002061}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000002061}. FT DOMAIN 172 341 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 400 AA; 46415 MW; 76D5B1C178842329 CRC64; MDKKSLEELE ELVKVLYNPV KSFVQIRKPD AKFQIGKGLV EKIKNYVREN NIDIVVFGNQ LSPTQKYNLA KEFKVEVIDK IELVLQIFQK HARTKEAQLQ VKLAELQYEL PRAKEKVRLA KKGEQPGFMG YGDYEVERYY QKVKREIASI KKKLEKLREH RRIARKGREK FDSVGLVGYT NAGKTSLLNI LCGEKKEAKN QVFTTLSTTT RRIRGIKRKI LVTDTVGFMD DLPPFMIEAF LSTIEESSDS DLILLVIDAS EDIEEIERKL KVNHEILEKV NCKSPIITVF NKCDLITEEK REEILTKLER YIVNPIFVSA KTGEGIERLK NLILDKLNLS IGVIETNNPK VVSFLYQNTE IIEDIEEEGK RIITFRAKER EVNRILKIHR VVREDGYRVS // ID D5X1Z2_THIK1 Unreviewed; 397 AA. AC D5X1Z2; DT 13-JUL-2010, integrated into UniProtKB/TrEMBL. DT 13-JUL-2010, sequence version 1. DT 07-JUN-2017, entry version 48. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Tint_1768 {ECO:0000313|EMBL:ADG31138.1}; OS Thiomonas intermedia (strain K12) (Thiobacillus intermedius). OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Thiomonas. OX NCBI_TaxID=75379 {ECO:0000313|EMBL:ADG31138.1, ECO:0000313|Proteomes:UP000002185}; RN [1] {ECO:0000313|EMBL:ADG31138.1, ECO:0000313|Proteomes:UP000002185} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 {ECO:0000313|EMBL:ADG31138.1, RC ECO:0000313|Proteomes:UP000002185}; RG US DOE Joint Genome Institute; RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L., RA Pitluck S., Davenport K., Detter J.C., Han C., Tapia R., Land M., RA Hauser L., Kyrpides N., Ovchinnikova G., Kerfeld C.A., Cannon G.C., RA Heinhorst S., Woyke T.; RT "Complete sequence of Thiomonas intermedia K12."; RL Submitted (APR-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002021; ADG31138.1; -; Genomic_DNA. DR ProteinModelPortal; D5X1Z2; -. DR EnsemblBacteria; ADG31138; ADG31138; Tint_1768. DR KEGG; tin:Tint_1768; -. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; FNNHAHV; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000002185; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000002185}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000002185}. FT DOMAIN 206 380 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 397 AA; 43338 MW; 9A450C2D5D0ED0A9 CRC64; MSKKHPQPEG QPQGPERAAL VSVQHRRPSS DDALAELEQL STSAGYALAG ELSCVRARPD AATYIGSGKL DELSELVSTT SADTIIFDNA LSPIQQRNLE KALGKPVIDR TGLILEIFAR RAQSAEGKMQ VELARLEHLA TRLVRGWTHL ERQTGGIGVR GGPGEKQIEL DRRMLDDKIK MLRTRLGKLG RQRMTQRRAR RRTGAFRVAL VGYTNAGKST LFNALTKSKI YAADQLFATL DTTTRKFYLG PQVNVTLSDT VGFIRDLPHT LIEAFKATLE DTLQADLLLH VVDASSPMLR EQMDEVHAVL REIGADDIPQ FLIFNKSDLL PVNLQVTNAH TQSEGIEARA SMPRLVVSAL TGAGVASLKS ALLEAVLADP RFQSSASALS DTTQISA // ID D5ZT08_9ACTN Unreviewed; 601 AA. AC D5ZT08; DT 13-JUL-2010, integrated into UniProtKB/TrEMBL. DT 13-JUL-2010, sequence version 1. DT 07-JUN-2017, entry version 45. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=SSFG_01958 {ECO:0000313|EMBL:EFE66709.2}; OS Streptomyces ghanaensis ATCC 14672. OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae; OC Streptomyces. OX NCBI_TaxID=566461 {ECO:0000313|EMBL:EFE66709.2, ECO:0000313|Proteomes:UP000003824}; RN [1] {ECO:0000313|EMBL:EFE66709.2, ECO:0000313|Proteomes:UP000003824} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 14672 {ECO:0000313|EMBL:EFE66709.2, RC ECO:0000313|Proteomes:UP000003824}; RG The Broad Institute Genome Sequencing Platform; RG Broad Institute Microbial Sequencing Center; RA Fischbach M., Ward D., Young S., Kodira C.D., Zeng Q., Koehrsen M., RA Godfrey P., Alvarado L., Berlin A.M., Borenstein D., Chen Z., RA Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A., Gujja S., RA Heiman D.I., Hepburn T.A., Howarth C., Jen D., Larson L., Lewis B., RA Mehta T., Park D., Pearson M., Roberts A., Saif S., Shea T.D., RA Shenoy N., Sisk P., Stolte C., Sykes S.N., Walk T., White J., RA Yandava C., Straight P., Clardy J., Hung D., Kolter R., Mekalanos J., RA Walker S., Walsh C.T., Wieland B.L.C., Ilzarbe M., Galagan J., RA Nusbaum C., Birren B.; RT "Annotation of Streptomyces ghanaensis ATCC 14672."; RL Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Proteomes:UP000003824} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 14672 {ECO:0000313|Proteomes:UP000003824}; RA Molnar K.; RL Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; DS999641; EFE66709.2; -; Genomic_DNA. DR ProteinModelPortal; D5ZT08; -. DR STRING; 566461.SSFG_01958; -. DR EnsemblBacteria; EFE66709; EFE66709; SSFG_01958. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000003824; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000003824}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000003824}. FT DOMAIN 275 440 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 601 AA; 64919 MW; 3205EC9CF47D851F CRC64; MTSSSSPSQD TKRFAHTHPE GLRADALMEE DVAWSLEIDG ERDGDQFDRS ERAALRRVAG LSTELEDVTE VEYRQLRLER VVLVGVWTSG TVQDAENSLA ELAALAETAG ALVLDGVIQR RDKPDAATYI GSGKAEELRD IVLETGADTV ICDGELSPGQ LIHLEDVVKV KVIDRTALIL DIFAQHAKSR EGKAQVSLAQ MQYMLPRLRG WGQSLSRQMG GGKGGGLATR GPGETKIETD RRRIREKMAK MRREIAEMKT GREVKRQERK RNKVPSVAIA GYTNAGKSSL LNRLTGAGVL VENALFATLD PTVRRAETPS GRLYTLADTV GFVRHLPHHL VEAFRSTMEE VGDSDLILHV VDGSHPNPEE QLAAVREVIR DVGATDVPEI VVINKADAAD PLTLQRLLRV EKRSLAVSAR TGQNIEQLLA FIDAELPRPS VEIEALVPYT HGKLVARAHD EGEVISEEHT PEGTLLKARV HEELAAELAP YVPAAAGCSS PGAKARPRST AGAAFGAPGS PAAVGLALCC GRAPPRPCPA AGPPARCCRA GRSRCWRPAR SRRPPRGPSH RRTNRRSWCG RCGASSAGSG RARTGPGRRG T // ID D6D858_9BACE Unreviewed; 419 AA. AC D6D858; DT 13-JUL-2010, integrated into UniProtKB/TrEMBL. DT 13-JUL-2010, sequence version 1. DT 07-JUN-2017, entry version 46. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=BXY_10490 {ECO:0000313|EMBL:CBK66203.1}; OS Bacteroides xylanisolvens XB1A. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae; OC Bacteroides. OX NCBI_TaxID=657309 {ECO:0000313|EMBL:CBK66203.1, ECO:0000313|Proteomes:UP000008795}; RN [1] {ECO:0000313|EMBL:CBK66203.1, ECO:0000313|Proteomes:UP000008795} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=XB1A {ECO:0000313|EMBL:CBK66203.1, RC ECO:0000313|Proteomes:UP000008795}; RG metaHIT consortium -- http://www.metahit.eu/; RA Pajon A., Turner K., Parkhill J., Bernalier A.; RT "The genome sequence of Bacteriodes xylanisolvens XB1A."; RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:CBK66203.1, ECO:0000313|Proteomes:UP000008795} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=XB1A {ECO:0000313|EMBL:CBK66203.1, RC ECO:0000313|Proteomes:UP000008795}; RA Pajon A.; RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; FP929033; CBK66203.1; -; Genomic_DNA. DR ProteinModelPortal; D6D858; -. DR STRING; 657309.BXY_10490; -. DR EnsemblBacteria; CBK66203; CBK66203; BXY_10490. DR KEGG; bxy:BXY_10490; -. DR PATRIC; fig|657309.4.peg.4629; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR KO; K03665; -. DR Proteomes; UP000008795; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000008795}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000008795}. FT DOMAIN 216 400 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 419 AA; 47936 MW; F1010647EF0BB97B CRC64; MKEFVISEAK VETAVLVGLI TQTQDERKTN EYLDELAFLA ETAGAEVVKR FTQKLPTAHS VTYVGKGKLE EIRQYIRNEE EEEREVGMVI FDDELSAKQI RNIEAELKVK ILDRTSLILD IFAMRAQTAN AKTQVELAQY KYMLPRLQRL WTHLERQGGG SGAGGGKGSV GLRGPGETQL EMDRRIILNR MSLLKERLAE IDKQKATQRK NRGRMIRVAL VGYTNVGKST MMNLLSKSEV FAENKLFATL DTTVRKVIID NLPFLLSDTV GFIRKLPTDL VESFKSTLDE VREADLLVHV VDISHPGFEE QIEVVNKTLA EIGGSGKPMI LVFNKIDAYT YVEKAPDDLT PRTKENLTLE ELMKTWMAKM EDNCLFISAR ERINIDELKN VVYQRVKELH VQKYPYNDFL YQTYEEEEE // ID D6DKX4_CLOSC Unreviewed; 417 AA. AC D6DKX4; DT 13-JUL-2010, integrated into UniProtKB/TrEMBL. DT 13-JUL-2010, sequence version 1. DT 07-JUN-2017, entry version 45. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=CLS_30700 {ECO:0000313|EMBL:CBK78348.1}; OS [Clostridium] cf. saccharolyticum K10. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Lachnospiraceae. OX NCBI_TaxID=717608 {ECO:0000313|EMBL:CBK78348.1, ECO:0000313|Proteomes:UP000008797}; RN [1] {ECO:0000313|EMBL:CBK78348.1, ECO:0000313|Proteomes:UP000008797} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K10 {ECO:0000313|EMBL:CBK78348.1, RC ECO:0000313|Proteomes:UP000008797}; RG metaHIT consortium -- http://www.metahit.eu/; RA Pajon A., Turner K., Parkhill J., Duncan S., Flint H.; RT "The genome sequence of Clostridium saccharolyticum-like K10."; RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:CBK78348.1, ECO:0000313|Proteomes:UP000008797} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K10 {ECO:0000313|EMBL:CBK78348.1, RC ECO:0000313|Proteomes:UP000008797}; RA Pajon A.; RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; FP929037; CBK78348.1; -; Genomic_DNA. DR ProteinModelPortal; D6DKX4; -. DR STRING; 717608.CLS_30700; -. DR EnsemblBacteria; CBK78348; CBK78348; CLS_30700. DR KEGG; cso:CLS_30700; -. DR PATRIC; fig|717608.3.peg.1129; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR KO; K03665; -. DR Proteomes; UP000008797; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000008797}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000008797}. FT DOMAIN 202 366 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 417 AA; 46795 MW; CDBF22166C4BC66D CRC64; MAELYDMREE AERVILVAVS TDDGDDTEES VDELAELVKT AGATAIDRII QNREWVHPGT YLGKGKIEEV RERAAELHAT GIVCDDELSP AQLRNLEDAL QIKVMDRTMV ILDIFASHAV TREGKIQVEL AQLRYRAARL VGLRNSLSRL GGGIGTRGPG EKKLEVDRRL IHERIGQLKS ELENVKRHRE VARQQRDRNC TVSAAIVGYT NAGKSTLLNY LTDAGILAQD MLFATLDPTT RTLELPSGQK ILLTDTVGFI RKLPHHLIEA FKSTLEEARY SDIILHVVDV SNPQMETQIH IVYETLRQLE ITDKTVITVF NKMDRLTGDV ILRDFRSDFQ VKISAKTGEG IPALLETLEG ILRSRKVYLE KVFPYAQAGK IQSIRRYGEL LSEEYTEEGI AVKAYVPAEI YGSILQG // ID D6E6R2_9ACTN Unreviewed; 428 AA. AC D6E6R2; DT 13-JUL-2010, integrated into UniProtKB/TrEMBL. DT 13-JUL-2010, sequence version 1. DT 07-JUN-2017, entry version 46. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=GPA_03700 {ECO:0000313|EMBL:CBL03409.1}; OS Gordonibacter pamelaeae 7-10-1-b. OC Bacteria; Actinobacteria; Coriobacteriia; Eggerthellales; OC Eggerthellaceae; Gordonibacter. OX NCBI_TaxID=657308 {ECO:0000313|EMBL:CBL03409.1, ECO:0000313|Proteomes:UP000008805}; RN [1] {ECO:0000313|EMBL:CBL03409.1, ECO:0000313|Proteomes:UP000008805} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=7-10-1-b {ECO:0000313|Proteomes:UP000008805}; RG metaHIT consortium -- http://www.metahit.eu/; RA Pajon A., Turner K., Parkhill J., Timmis K., Oxley A., Wurdemann D.; RT "The genome sequence of Gordonibacter pamelaeae 7-10-1-bT."; RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:CBL03409.1, ECO:0000313|Proteomes:UP000008805} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=7-10-1-bT {ECO:0000313|EMBL:CBL03409.1}; RA Pajon A.; RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; FP929047; CBL03409.1; -; Genomic_DNA. DR ProteinModelPortal; D6E6R2; -. DR EnsemblBacteria; CBL03409; CBL03409; GPA_03700. DR KEGG; gpa:GPA_03700; -. DR PATRIC; fig|657308.3.peg.3049; -. DR KO; K03665; -. DR Proteomes; UP000008805; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000008805}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Hydrolase {ECO:0000313|EMBL:CBL03409.1}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000008805}. FT DOMAIN 206 371 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 428 AA; 46822 MW; 685145F7EE6A8AD7 CRC64; MTPVSEERRE KAVLVGVDRP GASWPLASSL AELERLVDTA GADVAAVTTQ KLDAPNPRTF VGSGKAEEVA ELARAHAADL VVFDDELTPS QQSNLEKVVG KDVKVIDRTA LILDIFALHA TSKEGRLQVR LAQNEYLLPR LRGMWAHLAS NRMGGGVGSR FGEGESQLEV DRRMVRKRIT SIRRELKHLA EVRAIQRESR YESGMFKVAL AGYTNAGKSS LLNRLTNADV LAYDKLFATL DSTTRKFELP EGREITVTDT VGFIQKLPTT LIEAFKSTLD EITGADLVLH VVDASSDEYE AQIAAVEDVL GQIEAQDLLR VLVFNKCDLL DGEQCGALKA RHPQAQFVSA ATGEGIAELV GHVARVASAQ DEHLDVVIPY NRGDLVSVAH ERCHILSEKH EEDGTHLVML AAPSFAGLFR PYAAEKDR // ID D6GQG8_FILAD Unreviewed; 428 AA. AC D6GQG8; DT 13-JUL-2010, integrated into UniProtKB/TrEMBL. DT 13-JUL-2010, sequence version 1. DT 07-JUN-2017, entry version 47. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=HMPREF0389_00943 {ECO:0000313|EMBL:EFE29021.2}; OS Filifactor alocis (strain ATCC 35896 / D40 B5) (Fusobacterium alocis). OC Bacteria; Firmicutes; Clostridia; Clostridiales; OC Peptostreptococcaceae; Filifactor. OX NCBI_TaxID=546269 {ECO:0000313|EMBL:EFE29021.2, ECO:0000313|Proteomes:UP000007468}; RN [1] {ECO:0000313|Proteomes:UP000007468} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 35896 / D40 B5 {ECO:0000313|Proteomes:UP000007468}; RG The Broad Institute Genome Sequencing Platform; RA Ward D., Earl A., Feldgarden M., Young S.K., Gargeya S., Zeng Q., RA Alvarado L., Berlin A., Bochicchio J., Chapman S.B., Chen Z., RA Freedman E., Gellesch M., Goldberg J., Griggs A., Gujja S., RA Heilman E., Heiman D., Howarth C., Mehta T., Neiman D., Pearson M., RA Roberts A., Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., RA White J., Yandava C., Izard J., Blanton J.M., Baranova O.V., RA Tanner A.C., Dewhirst F.E., Haas B., Nusbaum C., Birren B.; RT "The genome sequence of Filifactor alocis strain ATCC 35896."; RL Submitted (DEC-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GG745527; EFE29021.2; -; Genomic_DNA. DR RefSeq; WP_014262935.1; NC_016630.1. DR ProteinModelPortal; D6GQG8; -. DR STRING; 546269.HMPREF0389_00943; -. DR KEGG; faa:HMPREF0389_00943; -. DR PATRIC; fig|546269.5.peg.1448; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR KO; K03665; -. DR OMA; HPATYIG; -. DR Proteomes; UP000007468; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000007468}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000007468}. FT DOMAIN 204 370 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 26 53 {ECO:0000256|SAM:Coils}. FT COILED 163 190 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 428 AA; 48961 MW; A64D359CCAD1E548 CRC64; MEQDKREVCY SAILVGVDFG KKSEVFAKFE DSMKELEELA QAAEIEVVGQ MTQPRDSVDV KYYIGKGKVE ELRELAENME VNLIVFNNEL SGSQLRNLEE GIGVTVIDRT MLILDIFAKR ARTGEGKLQV ELAQLKYKLP RLINSSTNLS RTGAGIGARG PGEKKLETDK RRIQRKIFEI ERELKEVKHN REVQRKGRLK SELPIVALAG YTNAGKSTLF NELLKEHKEY TEEKEVFVKN MLFATLDTTL RKSQLPNGME YLLTDTVGFV SNLPHDLVNA FHSTLEEIKY ADLILHVVDV SNEKYDLQMN TTQHVLKEIG VGDIPIVTVF NKIDLLEENF VISKESNKIS ISAKTGYHKQ ELLEKIQSIV CKNRRVTMLI PYVDGSVLND LHNKYRIEEE VYEEQGTKVV LSVDETDYHK YRDNIIEE // ID D6K3D4_9ACTN Unreviewed; 496 AA. AC D6K3D4; DT 13-JUL-2010, integrated into UniProtKB/TrEMBL. DT 13-JUL-2010, sequence version 1. DT 07-JUN-2017, entry version 45. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=SSTG_03825 {ECO:0000313|EMBL:EFF93506.2}; OS Streptomyces sp. e14. OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae; OC Streptomyces. OX NCBI_TaxID=645465 {ECO:0000313|EMBL:EFF93506.2, ECO:0000313|Proteomes:UP000004704}; RN [1] {ECO:0000313|EMBL:EFF93506.2, ECO:0000313|Proteomes:UP000004704} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=e14 {ECO:0000313|Proteomes:UP000004704}; RG The Broad Institute Genome Sequencing Platform; RG Broad Institute Microbial Sequencing Center; RA Fischbach M., Godfrey P., Ward D., Young S., Zeng Q., Koehrsen M., RA Alvarado L., Berlin A.M., Bochicchio J., Borenstein D., Chapman S.B., RA Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A., RA Gujja S., Heilman E.R., Heiman D.I., Hepburn T.A., Howarth C., Jen D., RA Larson L., Lewis B., Mehta T., Park D., Pearson M., Richards J., RA Roberts A., Saif S., Shea T.D., Shenoy N., Sisk P., Stolte C., RA Sykes S.N., Thomson T., Walk T., White J., Yandava C., Straight P., RA Clardy J., Hung D., Kolter R., Mekalanos J., Walker S., Walsh C.T., RA Wieland-Brown L.C., Haas B., Nusbaum C., Birren B.; RT "The genome sequence of Streptomyces sp. strain e14."; RL Submitted (OCT-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GG753626; EFF93506.2; -; Genomic_DNA. DR RefSeq; WP_009191048.1; NZ_GG753626.1. DR ProteinModelPortal; D6K3D4; -. DR STRING; 645465.SSTG_03825; -. DR EnsemblBacteria; EFF93506; EFF93506; SSTG_03825. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000004704; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 2. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000004704}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000004704}. FT DOMAIN 274 439 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 496 AA; 54131 MW; AF7E15580F9194F7 CRC64; MTSSSSSSQA TKRLAHTYPE GLRADALMEE DVAWSHEVDT ERDGDQFDRS ERAALRRVAG LSTELEDVTE VEYRQLRLER VVLVGVWTSG TVQDADNSLA ELAALAETAG AMVLDGVIQR RDKPDAATYI GSGKADELRD IVLETGADTV ICDGELSPGQ LIHLEDIVKV KVIDRTALIL DIFAQHAKSR EGKAQVALAQ MQYMLPRLRG WGQSLSRQMG GGSGGLATRG PGETKIETDR RRIREKMAKM RREIAEMKTG RELKRQERRR NKVPSVAIAG YTNAGKSSLL NRLTGAGVLV ENALFATLDP TVRRAETPSG RLYTLADTVG FVRHLPHHLV EAFRSTMEEV GDSDLILHVV DGSHPNPEEQ LAAVREVIRD VGATDVPEIV VVNKADAADP LVLQRLLRVE KHSIAVSART GRGIPELLAL IDAELPRPSV EIEALVPYTH GKLVARAHTE GEVISEEHTA EGTLLKARVH EELAADLAPY VPASAL // ID D6S2J6_9LACO Unreviewed; 423 AA. AC D6S2J6; DT 10-AUG-2010, integrated into UniProtKB/TrEMBL. DT 10-AUG-2010, sequence version 1. DT 07-JUN-2017, entry version 40. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:EFH30376.1}; GN ORFNames=HMPREF0526_10529 {ECO:0000313|EMBL:EFH30376.1}; OS Lactobacillus jensenii JV-V16. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; OC Lactobacillus. OX NCBI_TaxID=525329 {ECO:0000313|EMBL:EFH30376.1, ECO:0000313|Proteomes:UP000005177}; RN [1] {ECO:0000313|EMBL:EFH30376.1, ECO:0000313|Proteomes:UP000005177} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=JV-V16 {ECO:0000313|EMBL:EFH30376.1, RC ECO:0000313|Proteomes:UP000005177}; RA Muzny D., Qin X., Buhay C., Dugan-Rocha S., Ding Y., Chen G., RA Hawes A., Holder M., Jhangiani S., Johnson A., Khan Z., Li Z., Liu W., RA Liu X., Perez L., Shen H., Wang Q., Watt J., Xi L., Xin Y., Zhou J., RA Deng J., Jiang H., Liu Y., Qu J., Song X.-Z., Zhang L., Villasana D., RA Johnson A., Liu J., Liyanage D., Lorensuhewa L., Robinson T., Song A., RA Song B.-B., Dinh H., Thornton R., Coyle M., Francisco L., Jackson L., RA Javaid M., Korchina V., Kovar C., Mata R., Mathew T., Ngo R., RA Nguyen L., Nguyen N., Okwuonu G., Ongeri F., Pham C., Simmons D., RA Wilczek-Boney K., Hale W., Jakkamsetti A., Pham P., Ruth R., RA San Lucas F., Warren J., Zhang J., Zhao Z., Zhou C., Zhu D., Lee S., RA Bess C., Blankenburg K., Forbes L., Fu Q., Gubbala S., Hirani K., RA Jayaseelan J.C., Lara F., Munidasa M., Palculict T., Patil S., RA Pu L.-L., Saada N., Tang L., Weissenberger G., Zhu Y., Hemphill L., RA Shang Y., Youmans B., Ayvaz T., Ross M., Santibanez J., Aqrawi P., RA Gross S., Joshi V., Fowler G., Nazareth L., Reid J., Worley K., RA Petrosino J., Highlander S., Gibbs R.; RL Submitted (MAY-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EFH30376.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACGQ02000001; EFH30376.1; -; Genomic_DNA. DR RefSeq; WP_006586258.1; NZ_CM000953.1. DR ProteinModelPortal; D6S2J6; -. DR EnsemblBacteria; EFH30376; EFH30376; HMPREF0526_10529. DR Proteomes; UP000005177; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000005177}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000005177}. FT DOMAIN 199 367 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 423 AA; 47376 MW; 47EC9A646B5228E3 CRC64; MIDNQPQKTK VVVAGVNLSD PNFDYYMTEL VNLSEANNML VVGQVRQNLE QIYGGTYFGL GKLNEIKNLA HGLHATAVVL NDELTPMQIR NIEKITKLEV IDRTELILEI FANRAKTRQA KLQVQLARLQ YELPRLHPSE NTLDQQRGGG SVNRGSGESK LELNRRTIDK QITTIKKELQ NVATQEEIKS KRRNNSKLPQ VALVGYTNAG KSTTMNGLLK VFGSDTGKEV FVKNMLFATL DTSVRRINFD GTNDFIISDT VGFISKLPHN LIESFKATLK EASDADLIVN VVDSSDSNML QMIKTTQKVL HEIGITNVPI VTAYNKADLT TKKFPEIEGN DILYSAKDSE SIKVLAKFIT KRVFSNYKSL NIKLPLNAGA LLSYLHENGD VKKEEYTNTG ILITVKLSPK DYSKFSIYKQ KSE // ID D6STB1_9DELT Unreviewed; 552 AA. AC D6STB1; DT 10-AUG-2010, integrated into UniProtKB/TrEMBL. DT 10-AUG-2010, sequence version 1. DT 12-APR-2017, entry version 40. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=Dthio_PD1266 {ECO:0000313|EMBL:EFI33927.1}; OS Desulfonatronospira thiodismutans ASO3-1. OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfovibrionales; OC Desulfohalobiaceae; Desulfonatronospira. OX NCBI_TaxID=555779 {ECO:0000313|EMBL:EFI33927.1, ECO:0000313|Proteomes:UP000005496}; RN [1] {ECO:0000313|EMBL:EFI33927.1, ECO:0000313|Proteomes:UP000005496} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ASO3-1 {ECO:0000313|EMBL:EFI33927.1, RC ECO:0000313|Proteomes:UP000005496}; RG US DOE Joint Genome Institute (JGI-PGF); RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L., RA Pitluck S., Chertkov O., Brettin T., Detter J.C., Han C., Land M.L., RA Hauser L., Kyrpides N., Mikhailova N., Muyzer G., Woyke T.; RT "The draft genome of Desulfonatronospira thiodismutans ASO3-1."; RL Submitted (MAY-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EFI33927.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACJN02000003; EFI33927.1; -; Genomic_DNA. DR ProteinModelPortal; D6STB1; -. DR STRING; 555779.Dthio_PD1266; -. DR EnsemblBacteria; EFI33927; EFI33927; Dthio_PD1266. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000005496; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000005496}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000005496}. FT DOMAIN 391 552 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 357 384 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 552 AA; 62340 MW; CC99EA9F286DC064 CRC64; MTLTLKPTRR RLLIAHKPFG NLTGLKPHQL KALSRLYFRK FPASSGFTTE QARELASLTH QTKRQIGLII DRRGHVLMVI VGDQGGILIP ALDRLRESSG RLRGVRLLHT HMGSTCLTDE DLMDMVFLRL DSISVITVDP QGFPDQFQWA HLMPPNRERT PYRIYPSLHW SRAGADHQAS VESLEKELGR EGTAQEVSAE GNALLVSVDT RPRQEQERSL QEVAALAGTA GLEVSDTLIQ RVHRVNPKSI MGKGKVAELE VMALQSNASV IIFDQELSPT QLRNLTSITD RKVIDRTQLI LDIFAQRATS RAGKLQVEMA QLKYTLPRLI QQDRALSRLA GGIGGRGPGE TKLELDRRKI RDRITRIKDE LQKLRRHREN IRARRVETDV PVISLVGYTN AGKSTLLNTL TRSRILAEDK LFATLDPTSR RLRFPDEREV VLTDTVGFIK DLPEDLREAF MATLEELSLA RVLVHVADAS HPEVEEQVEA VQGLLRLLEL EDKPLVMVLN KWDLVTQDRK EILQNVFRDA IPASAQEEET LTPLVQTLER LL // ID D6TDS8_9CHLR Unreviewed; 451 AA. AC D6TDS8; DT 10-AUG-2010, integrated into UniProtKB/TrEMBL. DT 10-AUG-2010, sequence version 1. DT 05-JUL-2017, entry version 46. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=Krac_11821 {ECO:0000313|EMBL:EFH90210.1}; OS Ktedonobacter racemifer DSM 44963. OC Bacteria; Chloroflexi; Ktedonobacteria; Ktedonobacterales; OC Ktedonobacteraceae; Ktedonobacter. OX NCBI_TaxID=485913 {ECO:0000313|EMBL:EFH90210.1, ECO:0000313|Proteomes:UP000004508}; RN [1] {ECO:0000313|EMBL:EFH90210.1, ECO:0000313|Proteomes:UP000004508} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 44963 {ECO:0000313|Proteomes:UP000004508}; RX PubMed=22180814; DOI=10.4056/sigs.2114901; RA Chang Y.J., Land M., Hauser L., Chertkov O., Del Rio T.G., Nolan M., RA Copeland A., Tice H., Cheng J.F., Lucas S., Han C., Goodwin L., RA Pitluck S., Ivanova N., Ovchinikova G., Pati A., Chen A., RA Palaniappan K., Mavromatis K., Liolios K., Brettin T., Fiebig A., RA Rohde M., Abt B., Goker M., Detter J.C., Woyke T., Bristow J., RA Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P., RA Lapidus A.; RT "Non-contiguous finished genome sequence and contextual data of the RT filamentous soil bacterium Ktedonobacter racemifer type strain (SOSP1- RT 21)."; RL Stand. Genomic Sci. 5:97-111(2011). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EFH90210.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADVG01000001; EFH90210.1; -; Genomic_DNA. DR ProteinModelPortal; D6TDS8; -. DR STRING; 485913.Krac_11821; -. DR EnsemblBacteria; EFH90210; EFH90210; Krac_11821. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000004508; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000004508}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000004508}. FT DOMAIN 216 384 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 175 209 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 451 AA; 50372 MW; D3EAB5D224AE09F8 CRC64; MPEEYNSANV YEEKHMSGLL AEAPRRAILV SVDTPENDWP VEESLDELEQ LAQTAGVNCV DRAVQRLPHP HPGTVVGSGK VDEIAELVKS HDCDAVIFDL ELKPVQHRNL ERKLEVQVLD RTALILIIFG QRAQTREGRL QVELAQIEYD LPRLARQWSH LSRQRGGTQQ RGEGEKQIEV DRRLLRRQKE QLEEELELVR SQRQLHRDRR KYAGAPVVAL VGYTNAGKST LLNRLSGAQK LAEDKLFATL DPTTRRARIE GGQEFLLTDT VGFVQRLPHT LVAAFRATLE EVNAADLLVH VVDSSHPHVN HQILAVEEVL EEIGAGGMPI VIALNKSDNL EPGTTLPPLE GIAATLPQVQ VSALKGTGIS DLLRCISQAL VSQFVSLDVL IPYDRGDLVA QFHQFGTMEC EEYEEGGTHI RGYMPENHSS PFFAFRCKPQ ASTRPRKHAT V // ID D6TMZ7_9CHLR Unreviewed; 433 AA. AC D6TMZ7; DT 10-AUG-2010, integrated into UniProtKB/TrEMBL. DT 10-AUG-2010, sequence version 1. DT 07-JUN-2017, entry version 39. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=Krac_8472 {ECO:0000313|EMBL:EFH87147.1}; OS Ktedonobacter racemifer DSM 44963. OC Bacteria; Chloroflexi; Ktedonobacteria; Ktedonobacterales; OC Ktedonobacteraceae; Ktedonobacter. OX NCBI_TaxID=485913 {ECO:0000313|EMBL:EFH87147.1, ECO:0000313|Proteomes:UP000004508}; RN [1] {ECO:0000313|EMBL:EFH87147.1, ECO:0000313|Proteomes:UP000004508} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 44963 {ECO:0000313|Proteomes:UP000004508}; RX PubMed=22180814; DOI=10.4056/sigs.2114901; RA Chang Y.J., Land M., Hauser L., Chertkov O., Del Rio T.G., Nolan M., RA Copeland A., Tice H., Cheng J.F., Lucas S., Han C., Goodwin L., RA Pitluck S., Ivanova N., Ovchinikova G., Pati A., Chen A., RA Palaniappan K., Mavromatis K., Liolios K., Brettin T., Fiebig A., RA Rohde M., Abt B., Goker M., Detter J.C., Woyke T., Bristow J., RA Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P., RA Lapidus A.; RT "Non-contiguous finished genome sequence and contextual data of the RT filamentous soil bacterium Ktedonobacter racemifer type strain (SOSP1- RT 21)."; RL Stand. Genomic Sci. 5:97-111(2011). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EFH87147.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADVG01000002; EFH87147.1; -; Genomic_DNA. DR RefSeq; WP_007912021.1; NZ_ADVG01000002.1. DR ProteinModelPortal; D6TMZ7; -. DR STRING; 485913.Krac_8472; -. DR EnsemblBacteria; EFH87147; EFH87147; Krac_8472. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000004508; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000004508}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000004508}. FT DOMAIN 213 377 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 179 206 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 433 AA; 47321 MW; AB6F75C8997D7549 CRC64; MIDTGIRRGP ERAYLVAVEA DEQEGMWGAE DSLQELEALA TTAGAAVLGR MIQHLSQPDA QTYLGKGKAQ ELVALDQQLQ LDVIIFDDEL TPTQQRSLDK MLNARVIDRT ALILDVFARR AYSHEGRLQV ELAQAEYRLP RLAGSGTYTR QAGGSLGGGG VGGAIGVRGP GETRLELDRR RIRSRISALR KEIEEARSQR ALQRKQRVAQ GLPVVAVVGY TNAGKSTLFN ALTEAGVLAE DKLFATLDPV TRRLLLPNNQ EALLSDTVGF IQKLPTQLIA AFRATLEEVI EADLLLEVVD ISHENAFEQS ETVHDILDEL GAAAKPRVTA LNKIDLLTDP DALDPSLYSH AVPISAAEGK GLEELCAEVA SVLADTMEQL TVLLPFSRGD LVELFHRRGL IAHEEHEDEG TRLVGRLPRS LAGYYFPYIQ PLA // ID D6U4N8_9CHLR Unreviewed; 438 AA. AC D6U4N8; DT 10-AUG-2010, integrated into UniProtKB/TrEMBL. DT 10-AUG-2010, sequence version 1. DT 07-JUN-2017, entry version 44. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=Krac_2193 {ECO:0000313|EMBL:EFH81468.1}; OS Ktedonobacter racemifer DSM 44963. OC Bacteria; Chloroflexi; Ktedonobacteria; Ktedonobacterales; OC Ktedonobacteraceae; Ktedonobacter. OX NCBI_TaxID=485913 {ECO:0000313|EMBL:EFH81468.1, ECO:0000313|Proteomes:UP000004508}; RN [1] {ECO:0000313|EMBL:EFH81468.1, ECO:0000313|Proteomes:UP000004508} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 44963 {ECO:0000313|Proteomes:UP000004508}; RX PubMed=22180814; DOI=10.4056/sigs.2114901; RA Chang Y.J., Land M., Hauser L., Chertkov O., Del Rio T.G., Nolan M., RA Copeland A., Tice H., Cheng J.F., Lucas S., Han C., Goodwin L., RA Pitluck S., Ivanova N., Ovchinikova G., Pati A., Chen A., RA Palaniappan K., Mavromatis K., Liolios K., Brettin T., Fiebig A., RA Rohde M., Abt B., Goker M., Detter J.C., Woyke T., Bristow J., RA Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P., RA Lapidus A.; RT "Non-contiguous finished genome sequence and contextual data of the RT filamentous soil bacterium Ktedonobacter racemifer type strain (SOSP1- RT 21)."; RL Stand. Genomic Sci. 5:97-111(2011). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EFH81468.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADVG01000004; EFH81468.1; -; Genomic_DNA. DR RefSeq; WP_007918859.1; NZ_ADVG01000004.1. DR ProteinModelPortal; D6U4N8; -. DR STRING; 485913.Krac_2193; -. DR EnsemblBacteria; EFH81468; EFH81468; Krac_2193. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000004508; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000004508}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000004508}. FT DOMAIN 213 377 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 172 206 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 438 AA; 48724 MW; 65F9E9C90A94037F CRC64; MSQREGKQTT GGEKERAFLI AVDTGNEEQL LSVEDSLQEL ATLAQTAGAE PVGMMTQKLE HPDSATYIGK GKLEELKALE GQLAFDVVVV DDELRPAQQH NLEDQLHARV IDRTELILDI FAQHARTREG LLQVELAQLA YRLPRLSEHA INFSRVGGGT LGGAIGVRGP GETKLEIDRR RIRRRMSEIK RELEAVRQHR QVSRQQRASH ALPVVAVIGY TNAGKSTLFN ALTDANALVE NKLFATLDPT TRQLTLPNNQ EALLTDTVGF IQKLPTDLVA AFRATLEEVT DADILLEVVD ISHPNMHEQH EEVLRTLKDL HAEHLPRITA LNKIDLLGKT PQVDTSFFPD AVAISALQRQ GLDTLCEKMS QVLAVNMVPI CVTVPYDRGE LVDLFHRKGH IEQELHEEEG TLIVGRLPYS LRGQYLPYLC AVPAHVHV // ID D6W7F4_TRICA Unreviewed; 437 AA. AC D6W7F4; DT 10-AUG-2010, integrated into UniProtKB/TrEMBL. DT 11-MAY-2016, sequence version 2. DT 07-JUN-2017, entry version 37. DE SubName: Full=Putative GTP-binding protein 6-like Protein {ECO:0000313|EMBL:EFA11204.2}; GN ORFNames=TcasGA2_TC005168 {ECO:0000313|EMBL:EFA11204.2}; OS Tribolium castaneum (Red flour beetle). OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; OC Pterygota; Neoptera; Holometabola; Coleoptera; Polyphaga; OC Cucujiformia; Tenebrionidae; Tenebrionidae incertae sedis; Tribolium. OX NCBI_TaxID=7070 {ECO:0000313|EMBL:EFA11204.2, ECO:0000313|Proteomes:UP000007266}; RN [1] {ECO:0000313|EMBL:EFA11204.2, ECO:0000313|Proteomes:UP000007266} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Georgia GA2 {ECO:0000313|EMBL:EFA11204.2, RC ECO:0000313|Proteomes:UP000007266}; RX PubMed=18362917; DOI=10.1038/nature06784; RG Tribolium Genome Sequencing Consortium; RA Richards S., Gibbs R.A., Weinstock G.M., Brown S.J., Denell R., RA Beeman R.W., Gibbs R., Beeman R.W., Brown S.J., Bucher G., RA Friedrich M., Grimmelikhuijzen C.J., Klingler M., Lorenzen M., RA Richards S., Roth S., Schroder R., Tautz D., Zdobnov E.M., Muzny D., RA Gibbs R.A., Weinstock G.M., Attaway T., Bell S., Buhay C.J., RA Chandrabose M.N., Chavez D., Clerk-Blankenburg K.P., Cree A., Dao M., RA Davis C., Chacko J., Dinh H., Dugan-Rocha S., Fowler G., Garner T.T., RA Garnes J., Gnirke A., Hawes A., Hernandez J., Hines S., Holder M., RA Hume J., Jhangiani S.N., Joshi V., Khan Z.M., Jackson L., Kovar C., RA Kowis A., Lee S., Lewis L.R., Margolis J., Morgan M., Nazareth L.V., RA Nguyen N., Okwuonu G., Parker D., Richards S., Ruiz S.J., RA Santibanez J., Savard J., Scherer S.E., Schneider B., Sodergren E., RA Tautz D., Vattahil S., Villasana D., White C.S., Wright R., Park Y., RA Beeman R.W., Lord J., Oppert B., Lorenzen M., Brown S., Wang L., RA Savard J., Tautz D., Richards S., Weinstock G., Gibbs R.A., Liu Y., RA Worley K., Weinstock G., Elsik C.G., Reese J.T., Elhaik E., Landan G., RA Graur D., Arensburger P., Atkinson P., Beeman R.W., Beidler J., RA Brown S.J., Demuth J.P., Drury D.W., Du Y.Z., Fujiwara H., RA Lorenzen M., Maselli V., Osanai M., Park Y., Robertson H.M., Tu Z., RA Wang J.J., Wang S., Richards S., Song H., Zhang L., Sodergren E., RA Werner D., Stanke M., Morgenstern B., Solovyev V., Kosarev P., RA Brown G., Chen H.C., Ermolaeva O., Hlavina W., Kapustin Y., RA Kiryutin B., Kitts P., Maglott D., Pruitt K., Sapojnikov V., RA Souvorov A., Mackey A.J., Waterhouse R.M., Wyder S., Zdobnov E.M., RA Zdobnov E.M., Wyder S., Kriventseva E.V., Kadowaki T., Bork P., RA Aranda M., Bao R., Beermann A., Berns N., Bolognesi R., Bonneton F., RA Bopp D., Brown S.J., Bucher G., Butts T., Chaumot A., Denell R.E., RA Ferrier D.E., Friedrich M., Gordon C.M., Jindra M., Klingler M., RA Lan Q., Lattorff H.M., Laudet V., von Levetsow C., Liu Z., Lutz R., RA Lynch J.A., da Fonseca R.N., Posnien N., Reuter R., Roth S., RA Savard J., Schinko J.B., Schmitt C., Schoppmeier M., Schroder R., RA Shippy T.D., Simonnet F., Marques-Souza H., Tautz D., Tomoyasu Y., RA Trauner J., Van der Zee M., Vervoort M., Wittkopp N., Wimmer E.A., RA Yang X., Jones A.K., Sattelle D.B., Ebert P.R., Nelson D., Scott J.G., RA Beeman R.W., Muthukrishnan S., Kramer K.J., Arakane Y., Beeman R.W., RA Zhu Q., Hogenkamp D., Dixit R., Oppert B., Jiang H., Zou Z., RA Marshall J., Elpidina E., Vinokurov K., Oppert C., Zou Z., Evans J., RA Lu Z., Zhao P., Sumathipala N., Altincicek B., Vilcinskas A., RA Williams M., Hultmark D., Hetru C., Jiang H., Grimmelikhuijzen C.J., RA Hauser F., Cazzamali G., Williamson M., Park Y., Li B., Tanaka Y., RA Predel R., Neupert S., Schachtner J., Verleyen P., Raible F., Bork P., RA Friedrich M., Walden K.K., Robertson H.M., Angeli S., Foret S., RA Bucher G., Schuetz S., Maleszka R., Wimmer E.A., Beeman R.W., RA Lorenzen M., Tomoyasu Y., Miller S.C., Grossmann D., Bucher G.; RT "The genome of the model beetle and pest Tribolium castaneum."; RL Nature 452:949-955(2008). RN [2] {ECO:0000313|EMBL:EFA11204.2, ECO:0000313|Proteomes:UP000007266} RP GENOME REANNOTATION. RC STRAIN=Georgia GA2 {ECO:0000313|EMBL:EFA11204.2, RC ECO:0000313|Proteomes:UP000007266}; RX PubMed=19820115; DOI=10.1093/nar/gkp807; RA Kim H.S., Murphy T., Xia J., Caragea D., Park Y., Beeman R.W., RA Lorenzen M.D., Butcher S., Manak J.R., Brown S.J.; RT "BeetleBase in 2010: revisions to provide comprehensive genomic RT information for Tribolium castaneum."; RL Nucleic Acids Res. 38:D437-D442(2010). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; KQ971307; EFA11204.2; -; Genomic_DNA. DR STRING; 7070.TC005168-PA; -. DR EnsemblMetazoa; TC005168_001; TC005168_001; TC005168. DR eggNOG; KOG0410; Eukaryota. DR eggNOG; COG2262; LUCA. DR InParanoid; D6W7F4; -. DR Proteomes; UP000007266; Linkage group 1. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR CDD; cd01878; HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 4: Predicted; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000007266}; KW Reference proteome {ECO:0000313|Proteomes:UP000007266}. FT DOMAIN 248 347 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 221 244 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 437 AA; 49539 MW; DA84B6176EB1C9F3 CRC64; MLVLNRFAAI SRKLNTVFHA KVAFHLSHRL KNENKNLYDE ILTEDREFLA FSENYFKFES GRNCYIIQPY IKWGPQKLQG ITPIEQLDEA KALVNTLPSW NIQDSISVPL ESFDKKTLFK SGSLDKLRQI IRKNSTINAV FVNLGTLKKA QIVSLEREFG VPILDRYKVV MYILKLHVVS KHAKLQVALA ELYYLQRSTF HEANFGKAER EKVKLMFQTR EQKLKNAIKE LRTERALLRN KRQKIDFPVV AVVGYTNAGK TSLIKALTGE ERLRPKNQLF ATLDVTLHAG LLPSGMKVLY VDTVGFISDI PTNLIECFVA TLEDAVLADV ILHVEDISSS FFEFKRKHVL ATLQDLATNA GTGDVLNKVI SVGNKCDLVP KETDFGILKV SSKDDTGLDV LRMTLEKAIL ENTNRAKIKI RVPVGGDAIR WFLSSLM // ID D6XU49_BACIE Unreviewed; 419 AA. AC D6XU49; DT 10-AUG-2010, integrated into UniProtKB/TrEMBL. DT 10-AUG-2010, sequence version 1. DT 30-AUG-2017, entry version 52. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Bsel_1829 {ECO:0000313|EMBL:ADH99335.1}; OS Bacillus selenitireducens (strain ATCC 700615 / DSM 15326 / MLS10). OC Bacteria; Firmicutes; Bacilli; Bacillales; Sporolactobacillaceae; OC unclassified Sporolactobacillaceae. OX NCBI_TaxID=439292 {ECO:0000313|EMBL:ADH99335.1, ECO:0000313|Proteomes:UP000000271}; RN [1] {ECO:0000313|EMBL:ADH99335.1, ECO:0000313|Proteomes:UP000000271} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700615 / DSM 15326 / MLS10 RC {ECO:0000313|Proteomes:UP000000271}; RG US DOE Joint Genome Institute; RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., RA Tice H., Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T., RA Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N., RA Ovchinnikova G., Stolz J.; RT "Complete sequence of Bacillus selenitireducens MLS10."; RL Submitted (OCT-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001791; ADH99335.1; -; Genomic_DNA. DR RefSeq; WP_013172757.1; NC_014219.1. DR ProteinModelPortal; D6XU49; -. DR STRING; 439292.Bsel_1829; -. DR EnsemblBacteria; ADH99335; ADH99335; Bsel_1829. DR KEGG; bse:Bsel_1829; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000000271; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000000271}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000000271}. FT DOMAIN 200 361 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 419 AA; 47604 MW; 2638DC8C7C8668B7 CRC64; MEQRIAKQTV IIVGVEEKQG DRKAFEHRMD ELESLVKTAG GTVELKVEQA LDHPVAATYI GKGKLFELKQ AMDEISADLV IFNDELSPSQ LRNISTELDA LVLDRTQLIL DIFAQRAQSK EGKLQVELAQ LNYLLPRLRG QGHIMSRLGG GIGTRGPGET QLEVDQRHIR QRMDDIKSQL EQVVRHRTRY RERRKRNQAF QIALVGYTNA GKSTLLNRLS QADVMVEDQL FATLDPTTKK IRLPKGMDVL LSDTVGFIQQ LPTTLIAAFR STLEEVTGAD FIVHVVDASH EDAVNHEESV NRLLDDLDAQ HIPRLTVYNK RDLIQGDFFA LSTPSLLLST MSDDDIQRFL NKLEQTIEDA FVPYQVSVQA YEGKLLHRLK EETIVHEETF VEDGELYRVR GYAQQDSAIY HLMTRSEDK // ID D6Y8G5_THEBD Unreviewed; 501 AA. AC D6Y8G5; DT 10-AUG-2010, integrated into UniProtKB/TrEMBL. DT 10-AUG-2010, sequence version 1. DT 07-JUN-2017, entry version 54. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Tbis_1140 {ECO:0000313|EMBL:ADG87862.1}; OS Thermobispora bispora (strain ATCC 19993 / DSM 43833 / CBS 139.67 / OS JCM 10125 / NBRC 14880 / R51). OC Bacteria; Actinobacteria; Actinobacteria incertae sedis; OC Thermobispora. OX NCBI_TaxID=469371 {ECO:0000313|EMBL:ADG87862.1, ECO:0000313|Proteomes:UP000006640}; RN [1] {ECO:0000313|EMBL:ADG87862.1, ECO:0000313|Proteomes:UP000006640} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 19993 / DSM 43833 / CBS 139.67 / JCM 10125 / NBRC 14880 / RC R51 {ECO:0000313|Proteomes:UP000006640}; RG US DOE Joint Genome Institute (JGI-PGF); RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., RA Tice H., Bruce D., Goodwin L., Pitluck S., Kyrpides N., Mavromatis K., RA Ivanova N., Mikhailova N., Chertkov O., Brettin T., Detter J.C., RA Han C., Larimer F., Land M., Hauser L., Markowitz V., Cheng J.-F., RA Hugenholtz P., Woyke T., Wu D., Jando M., Schneider S., Klenk H.-P., RA Eisen J.A.; RT "The complete genome of Thermobispora bispora DSM 43833."; RL Submitted (JAN-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001874; ADG87862.1; -; Genomic_DNA. DR RefSeq; WP_013131395.1; NC_014165.1. DR ProteinModelPortal; D6Y8G5; -. DR STRING; 469371.Tbis_1140; -. DR EnsemblBacteria; ADG87862; ADG87862; Tbis_1140. DR KEGG; tbi:Tbis_1140; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000006640; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000006640}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000006640}. FT DOMAIN 277 443 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 236 263 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 501 AA; 55282 MW; 445DF3ECEA5EEC11 CRC64; MRYGGEPWDD RGKPGCRRGR DRGAGLFAST EMTFMGNEYE DHTVGDFELE QRQALRRVAG LSTELQDITE VEYRKLRLER VVLVGVWTSG TLEEAENSLR ELKLLAETAG SVVLDGLIQR RDRPDPATYI GSGKAQELAD IVAATGADTV ICDGELTPGQ LRRLEEIVKV KVVDRTALIL DIFAQHAKSR EGKAQVELAQ LEYLLPRLRG WGGNLSRQVG GRAAGGVGIG GRGPGETKIE LDRRRIRERM AKLRKQIKEM SVVRQTKRRR RQNRDVPAVA IAGYTNAGKS SLLNRLTGAG VLVEDALFAT LDPTVRRART PDGRVFTLAD TVGFVRHLPH QLVEAFRSTL EEVADADLIL HVVDGSHPDP ESQIAAVRKV FAEIEGALDI PEIIVINKAD IADPVVLARL SAKERHSVVV SARTGEGIDR LLEAIARELP EPDREVRVLV PYERGDLISR AHTEGTVLSL DHTPEGTILH ARVRPDLYAE LDRVAKPVET V // ID D6YWT0_WADCW Unreviewed; 434 AA. AC D6YWT0; DT 10-AUG-2010, integrated into UniProtKB/TrEMBL. DT 10-AUG-2010, sequence version 1. DT 07-JUN-2017, entry version 56. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:ADI38591.1}; GN OrderedLocusNames=wcw_1234 {ECO:0000313|EMBL:ADI38591.1}; OS Waddlia chondrophila (strain ATCC VR-1470 / WSU 86-1044). OC Bacteria; Chlamydiae; Parachlamydiales; Waddliaceae; Waddlia. OX NCBI_TaxID=716544 {ECO:0000313|EMBL:ADI38591.1, ECO:0000313|Proteomes:UP000001505}; RN [1] {ECO:0000313|EMBL:ADI38591.1, ECO:0000313|Proteomes:UP000001505} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC VR-1470 / WSU 86-1044 {ECO:0000313|Proteomes:UP000001505}; RX PubMed=20531937; DOI=10.1371/journal.pone.0010890; RA Bertelli C., Collyn F., Croxatto A., Ruckert C., Polkinghorne A., RA Kebbi-Beghdadi C., Goesmann A., Vaughan L., Greub G.; RT "The Waddlia genome: a window into chlamydial biology."; RL PLoS ONE 5:E10890-E10890(2010). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001928; ADI38591.1; -; Genomic_DNA. DR RefSeq; WP_013182303.1; NZ_LVEB01000011.1. DR ProteinModelPortal; D6YWT0; -. DR STRING; 716544.wcw_1234; -. DR EnsemblBacteria; ADI38591; ADI38591; wcw_1234. DR KEGG; wch:wcw_1234; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000001505; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000001505}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000001505}. FT DOMAIN 214 380 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 434 AA; 49609 MW; 0775C292B6300F1D CRC64; MYEEIREKLG DEEASKERRA LLVAIYRGTD QLPECKEHLD ELELLCKTYG IETAEKLPCL VRKFNASTLI SSGKVEEIGE TAKELGVDVI VFDDEVTPGQ QRNLEKIYSI PVIDRSEVII GVFAQRAHSK EAKLQVELAR LKYLAPRLKR MWTHLSRQQA TAGGGAYLKG KGEKQIEIDR RLLKTKIFHL QKEINAVQAH RDTQRIQRER SEIPTFAIVG YTNAGKSTLL NALTEAGIFT EDKLFATLDT TTRKFTLPNN QEILLTDTVG FIRKLPHLLV AAFRSTLEEA VQADILIHLI DSSHPMALEQ AEATVEVLHE LGAKDKPVIT VLNKIDRLED RAILKKLRTK FTKTVNLSAL YKQGFDHLTE QMTEELQKRR RVVNLRIPQK DYAVVSEVMR HGNILNQEYE ENDVVMRVDL PSRYLGRISR YIEE // ID D6Z6T6_DESAT Unreviewed; 540 AA. AC D6Z6T6; DT 10-AUG-2010, integrated into UniProtKB/TrEMBL. DT 10-AUG-2010, sequence version 1. DT 07-JUN-2017, entry version 45. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=DaAHT2_0339 {ECO:0000313|EMBL:ADH85045.1}; OS Desulfurivibrio alkaliphilus (strain DSM 19089 / UNIQEM U267 / AHT2). OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfobacterales; OC Desulfobulbaceae; Desulfurivibrio. OX NCBI_TaxID=589865 {ECO:0000313|EMBL:ADH85045.1, ECO:0000313|Proteomes:UP000001508}; RN [1] {ECO:0000313|Proteomes:UP000001508} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 19089 / UNIQEM U267 / AHT2 RC {ECO:0000313|Proteomes:UP000001508}; RG US DOE Joint Genome Institute; RA Pitluck S., Chertkov O., Detter J.C., Han C., Tapia R., Larimer F., RA Land M., Hauser L., Kyrpides N., Mikhailova N., Sorokin D.Y., RA Muyzer G., Woyke T.; RT "Complete sequence of Desulfurivibrio alkaliphilus AHT2."; RL Submitted (FEB-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001940; ADH85045.1; -; Genomic_DNA. DR RefSeq; WP_013162576.1; NC_014216.1. DR ProteinModelPortal; D6Z6T6; -. DR STRING; 589865.DaAHT2_0339; -. DR EnsemblBacteria; ADH85045; ADH85045; DaAHT2_0339. DR KEGG; dak:DaAHT2_0339; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; EREVIIT; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000001508; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000001508}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000001508}. FT DOMAIN 375 540 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 540 AA; 60827 MW; 70EFE1E7C68E97C1 CRC64; MLERLGRRRL DPDHIMTPEM ARPMSELSRE IGRQLGLIID RSGQVELLLV GDHRSIMIPA LPQNRVAGAR LRGLRCLHTH LGGEKLTQDD FMDLLFLRLD LMSALEVDNQ GRPGKLHSAH LNPRAMGERD PGAAAGAAKA EVKPWILLPP QQVSRQPDNL RELISSLEAE FSRLRPVREV DKGRDRAILV SVSSVPRAVA EESMAELKEL AASAGVMVLA EVIQRRDKIN PRLILGRGKL GEIMLQALQL NANLLIFDQE LNPSQVRSIT DHTEMRVIDR TQLILDIFAR RALSREGRLQ IEMAQLKYLL PRLGTRDDAL SRLTGGIGGR GPGETRLEID RRRTRDRLNT LAAKLKAVSK ERYRRRERRR KKEIPVLSLV GYTNAGKSTL LNALTGSDIL AEDKLFATLD PTSRRLRFPE EMEVIITDTV GFIRHLPAEL LQAFKATLEE LGEADVLIHV VDISNPRFTE HIKVVEELLR ELELDLLPRL TVFNKVDLLP DHEWVAAEAA RYDAVVVSAL APETLPPLLE RARQAILKNW // ID D6ZEP7_SEGRD Unreviewed; 511 AA. AC D6ZEP7; DT 10-AUG-2010, integrated into UniProtKB/TrEMBL. DT 10-AUG-2010, sequence version 1. DT 07-JUN-2017, entry version 52. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Srot_0948 {ECO:0000313|EMBL:ADG97421.1}; OS Segniliparus rotundus (strain ATCC BAA-972 / CDC 1076 / CIP 108378 / OS DSM 44985 / JCM 13578). OC Bacteria; Actinobacteria; Corynebacteriales; Segniliparaceae; OC Segniliparus. OX NCBI_TaxID=640132 {ECO:0000313|EMBL:ADG97421.1, ECO:0000313|Proteomes:UP000002247}; RN [1] {ECO:0000313|EMBL:ADG97421.1, ECO:0000313|Proteomes:UP000002247} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-972 / CDC 1076 / CIP 108378 / DSM 44985 / JCM 13578 RC {ECO:0000313|Proteomes:UP000002247}; RX PubMed=21304703; DOI=10.4056/sigs.791633; RA Sikorski J., Lapidus A., Copeland A., Misra M., Glavina Del Rio T., RA Nolan M., Lucas S., Chen F., Tice H., Cheng J.F., Jando M., RA Schneider S., Bruce D., Goodwin L., Pitluck S., Liolios K., RA Mikhailova N., Pati A., Ivanova N., Mavromatis K., Chen A., RA Palaniappan K., Chertkov O., Land M., Hauser L., Chang Y.J., RA Jeffries C.D., Brettin T., Detter J.C., Han C., Rohde M., Goker M., RA Bristow J., Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., RA Klenk H.P.; RT "Complete genome sequence of Segniliparus rotundus type strain (CDC RT 1076)."; RL Stand. Genomic Sci. 2:203-211(2010). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001958; ADG97421.1; -; Genomic_DNA. DR RefSeq; WP_013137877.1; NC_014168.1. DR ProteinModelPortal; D6ZEP7; -. DR STRING; 640132.Srot_0948; -. DR EnsemblBacteria; ADG97421; ADG97421; Srot_0948. DR KEGG; srt:Srot_0948; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000002247; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000002247}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000002247}. FT DOMAIN 279 448 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 511 AA; 54605 MW; 5804163A68294E4E CRC64; MSSFETSSDS SAAPCGQDPD GPLSAEAFGA RPPQSTSGWG VVQEEAEWLW EERDSLRRVQ GLSTELSDVT EVEYRQLRLE RVVLVGVWPK RQSAEADASI KELAALARTA GSQVLEGLVQ RRDKPDAATY IGSGKVAAVK AVVAETEADT VICDGELTPA QLRTLEQQVG VKVIDRTALI LDIFAQHATS KEGKAQVQLA QLQYLLPRLR GWGQTLSRQA GGRAGGANGG VGLRGPGETK IETDRRRIRE RISHLRGELK GMRKVRSTKR SLRERNGVPS AVIVGYTNAG KSSLLGALTG ASVIIRDELF ATLDPTTRKS WGETSGSFTI TDTVGFVRHL PTQLVEAFAS TLEEATGADV LVHVVDASDP RPADQIRVVR EILGDVFAKA QTPWPTEIVA LNKSDAVDEA TLAGLRIAFP EATLVSARTG EGIDELKRRI GEALAVRSGA ACLVELSLAV PEDRPDLLAK VCAAGRVLAS EETESGTLVR ALVPQDLADQ LRGGATSLAE T // ID D6ZGX3_MOBCV Unreviewed; 524 AA. AC D6ZGX3; DT 10-AUG-2010, integrated into UniProtKB/TrEMBL. DT 10-AUG-2010, sequence version 1. DT 07-JUN-2017, entry version 50. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:ADI67881.1}; GN OrderedLocusNames=HMPREF0573_11562 {ECO:0000313|EMBL:ADI67881.1}; OS Mobiluncus curtisii (strain ATCC 43063 / DSM 2711 / V125) (Falcivibrio OS vaginalis). OC Bacteria; Actinobacteria; Actinomycetales; Actinomycetaceae; OC Mobiluncus. OX NCBI_TaxID=548479 {ECO:0000313|EMBL:ADI67881.1, ECO:0000313|Proteomes:UP000006742}; RN [1] {ECO:0000313|Proteomes:UP000006742} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43063 / DSM 2711 / V125 RC {ECO:0000313|Proteomes:UP000006742}; RA Muzny D., Qin X., Deng J., Jiang H., Liu Y., Qu J., Song X.-Z., RA Zhang L., Thornton R., Coyle M., Francisco L., Jackson L., Javaid M., RA Korchina V., Kovar C., Mata R., Mathew T., Ngo R., Nguyen L., RA Nguyen N., Okwuonu G., Ongeri F., Pham C., Simmons D., RA Wilczek-Boney K., Hale W., Jakkamsetti A., Pham P., Ruth R., RA San Lucas F., Warren J., Zhang J., Zhao Z., Zhou C., Zhu D., Lee S., RA Bess C., Blankenburg K., Forbes L., Fu Q., Gubbala S., Hirani K., RA Jayaseelan J.C., Lara F., Munidasa M., Palculict T., Patil S., RA Pu L.-L., Saada N., Tang L., Weissenberger G., Zhu Y., Hemphill L., RA Shang Y., Youmans B., Ayvaz T., Ross M., Santibanez J., Aqrawi P., RA Gross S., Joshi V., Fowler G., Nazareth L., Reid J., Worley K., RA Petrosino J., Highlander S., Gibbs R., Gibbs R.; RT "Complete sequence of Mobiluncus curtisii ATCC 43063."; RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001992; ADI67881.1; -; Genomic_DNA. DR RefSeq; WP_013189472.1; NC_014246.1. DR ProteinModelPortal; D6ZGX3; -. DR EnsemblBacteria; ADI67881; ADI67881; HMPREF0573_11562. DR KEGG; mcu:HMPREF0573_11562; -. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000006742; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000006742}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000006742}. FT DOMAIN 288 454 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 524 AA; 57147 MW; 4FB67EF26FED2A69 CRC64; MHGLGDTLNS RRKDYNLQEN TEDYPNLDFL LPAAVPPAGG EPESDMASWS QLDTAEQAQR WADRYALGRV ESIGSELQDI SEVEYREVRL EKVIVVGIFA ADRDEAELSL QELAALAKTA GAVVLAGLLQ RRDKPDVATF LGRGKAHELQ TQVATLGADT VIVDDELAPS QRRALEDVVK VKVIDRTALI LDIFAQHATS REGKAQVELA QLEYLLPRLR GWGESMSRQA GGRAAAGDGI GARGPGETKI ELDRRRIRSR MARLRRNLKA LAPTREAKRA SRKAGGIPAV AIVGYTNAGK SSLLNRLAGA NLLVHDALFA TLDPSVRRAH TPEGREYTLA DTVGFVRRLP TELVEAFRST LEETAMADLI LHVVDGSNPD PMAQVAAVDA TLELVEGIEE IPVMMVVNKI DQASAPALAL LRHSLPEAYY VSARTGEGIE ALQQSIADRL PWPGQRVRVV VKWENTGLLE RIYRDGKLLT RQNRADGTFI DAWVPPALGA KLLNQAMEDD CGTSEGDDSG ANER // ID D6ZYG8_STAND Unreviewed; 463 AA. AC D6ZYG8; DT 10-AUG-2010, integrated into UniProtKB/TrEMBL. DT 10-AUG-2010, sequence version 1. DT 07-JUN-2017, entry version 46. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Snov_1776 {ECO:0000313|EMBL:ADH89080.1}; OS Starkeya novella (strain ATCC 8093 / DSM 506 / CCM 1077 / IAM 12100 / OS NBRC 12443 / NCIB 9113). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Xanthobacteraceae; Starkeya. OX NCBI_TaxID=639283 {ECO:0000313|EMBL:ADH89080.1, ECO:0000313|Proteomes:UP000006633}; RN [1] {ECO:0000313|Proteomes:UP000006633} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 8093 / DSM 506 / CCM 1077 / IAM 12100 / NBRC 12443 / NCIB RC 9113 {ECO:0000313|Proteomes:UP000006633}; RG US DOE Joint Genome Institute; RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L., RA Pitluck S., Davenport K., Brettin T., Detter J.C., Han C., Tapia R., RA Land M., Hauser L., Kyrpides N., Ivanova N., Beatson S., Kappler U., RA Woyke T.; RT "Complete sequence of Starkeya novella DSM 506."; RL Submitted (MAY-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002026; ADH89080.1; -; Genomic_DNA. DR ProteinModelPortal; D6ZYG8; -. DR STRING; 639283.Snov_1776; -. DR EnsemblBacteria; ADH89080; ADH89080; Snov_1776. DR KEGG; sno:Snov_1776; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000006633; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000006633}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000006633}. FT DOMAIN 226 400 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 463 AA; 51521 MW; 43C4EC75152D3122 CRC64; MEPKGSRRSR DARLPAADGE EARDDTRVVV IVPNLARRGA GEDDHRRSPE ARLEEAVGLA LAIDGLQVVA SMLVGLTQLR PATYLGTGKV EEIAGVVKAE EAGLVFVDAP LTPVQQRNLE KAWSAKVIDR TALILEIFGQ RARTKEGVLQ VELAHLNYQR SRLVRSWTHL ERQRGGFGFL GGPGETQIEA DRRLIGERIL KIERELEQVK RTRALHRASR KKVPYPVVAL VGYTNAGKST LFNRLTRSDV MAQDLLFATL DPTLRAVQLP SGERIILSDT VGFISDLPTQ LVAAFRATLE EVIEADLILH VRDMSHEDAE AQAHDVEAVL SDLDIDPEDD HRVIEVWNKI DRLDEEGRAR LFNTAERREG DARPIPVSAL TGEGVDALLV AIGQRLARER VSLRVDLDAA DGRGLSWLYR HSEVLERRED EGGRLHLAVR VPPDRAEHIE RRFGAKRIKG AGQ // ID D7AYE4_NOCDD Unreviewed; 512 AA. AC D7AYE4; DT 10-AUG-2010, integrated into UniProtKB/TrEMBL. DT 10-AUG-2010, sequence version 1. DT 07-JUN-2017, entry version 56. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Ndas_0684 {ECO:0000313|EMBL:ADH66129.1}; OS Nocardiopsis dassonvillei (strain ATCC 23218 / DSM 43111 / CIP 107115 OS / JCM 7437 / KCTC 9190 / NBRC 14626 / NCTC 10488 / NRRL B-5397 / IMRU OS 509) (Actinomadura dassonvillei). OC Bacteria; Actinobacteria; Streptosporangiales; Nocardiopsaceae; OC Nocardiopsis. OX NCBI_TaxID=446468 {ECO:0000313|EMBL:ADH66129.1, ECO:0000313|Proteomes:UP000002219}; RN [1] {ECO:0000313|EMBL:ADH66129.1, ECO:0000313|Proteomes:UP000002219} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 23218 / DSM 43111 / CIP 107115 / JCM 7437 / KCTC 9190 / RC NBRC 14626 / NCTC 10488 / NRRL B-5397 / IMRU 509 RC {ECO:0000313|Proteomes:UP000002219}; RX PubMed=21304737; DOI=10.4056/sigs.1363462; RA Sun H., Lapidus A., Nolan M., Lucas S., Del Rio T.G., Tice H., RA Cheng J.F., Tapia R., Han C., Goodwin L., Pitluck S., Pagani I., RA Ivanova N., Mavromatis K., Mikhailova N., Pati A., Chen A., RA Palaniappan K., Land M., Hauser L., Chang Y.J., Jeffries C.D., RA Djao O.D., Rohde M., Sikorski J., Goker M., Woyke T., Bristow J., RA Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.; RT "Complete genome sequence of Nocardiopsis dassonvillei type strain RT (IMRU 509)."; RL Stand. Genomic Sci. 3:325-336(2010). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002040; ADH66129.1; -; Genomic_DNA. DR RefSeq; WP_013151736.1; NC_014210.1. DR ProteinModelPortal; D7AYE4; -. DR STRING; 446468.Ndas_0684; -. DR EnsemblBacteria; ADH66129; ADH66129; Ndas_0684. DR KEGG; nda:Ndas_0684; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000002219; Chromosome 1. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR Gene3D; 3.90.1150.10; -; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR015422; PyrdxlP-dep_Trfase_sub2. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 2. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000002219}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000002219}. FT DOMAIN 291 456 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 512 AA; 54854 MW; C72ED857B17AF918 CRC64; MNTADTRGSV HDGHEAEDAF REAITVGDGV DAHDASREAK ATGGDRYDDP DNAPDQGEME LAERHALRRV PGLSTELTDV TEVEYRSLRL ERVILIGVWT SGSQADADNS LTELAALSET AGALVLEGVT QRRSKPDPAT YVGKGKAAEL RDIVEATGAD TVICDGELTP GQLRQLEDVV KVKVIDRTAL ILDIFAQHAR SSEGKAQVEL AQLSYLLPRL RGWGDALSRQ AGGSGGGGAG GGVGLRGPGE TKIETDRRRI NDKMAKLRRQ LAHMRTARDV KRDVRRTRSV PSVAIAGYTN AGKSSLLNRL TGAGVLVENA LFATLDPTVR QARTPDGRGF TLSDTVGFVR HLPHQLVEAF RSTLEEVADS DLVLHVVDGS HPDPESQISA VRHVFADIDA GDVPELIVVN KVDAADPDVL KALRTRYPDM VEVSARTGEG VPALVEAVAA ALPELAHEVR ALVPYSRGDL IARIHEEGRI LSEEHTAEGT AIHAFVPALL AGRLDEYTPS TA // ID D7BIF0_MEISD Unreviewed; 555 AA. AC D7BIF0; DT 10-AUG-2010, integrated into UniProtKB/TrEMBL. DT 10-AUG-2010, sequence version 1. DT 07-JUN-2017, entry version 49. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Mesil_2258 {ECO:0000313|EMBL:ADH64125.1}; OS Meiothermus silvanus (strain ATCC 700542 / DSM 9946 / VI-R2) (Thermus OS silvanus). OC Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; OC Meiothermus. OX NCBI_TaxID=526227 {ECO:0000313|EMBL:ADH64125.1, ECO:0000313|Proteomes:UP000001916}; RN [1] {ECO:0000313|EMBL:ADH64125.1, ECO:0000313|Proteomes:UP000001916} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700542 / DSM 9946 / VI-R2 RC {ECO:0000313|Proteomes:UP000001916}; RX PubMed=21304690; RA Sikorski J., Tindall B.J., Lowry S., Lucas S., Nolan M., Copeland A., RA Glavina Del Rio T., Tice H., Cheng J.F., Han C., Pitluck S., RA Liolios K., Ivanova N., Mavromatis K., Mikhailova N., Pati A., RA Goodwin L., Chen A., Palaniappan K., Land M., Hauser L., Chang Y.J., RA Jeffries C.D., Rohde M., Goker M., Woyke T., Bristow J., Eisen J.A., RA Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P., Lapidus A.; RT "Complete genome sequence of Meiothermus silvanus type strain (VI- RT R2)."; RL Stand. Genomic Sci. 3:37-46(2010). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002042; ADH64125.1; -; Genomic_DNA. DR RefSeq; WP_013158670.1; NC_014212.1. DR ProteinModelPortal; D7BIF0; -. DR STRING; 526227.Mesil_2258; -. DR EnsemblBacteria; ADH64125; ADH64125; Mesil_2258. DR KEGG; msv:Mesil_2258; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; EREVIIT; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000001916; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000001916}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000001916}. FT DOMAIN 378 541 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 555 AA; 60936 MW; D7655A6C40A99373 CRC64; MDKILGRTNG LKPSQLRQLA NLYRRRIPAG RLLNAELART LAHLSSETHK PIALLMDRQG HVLRVAVGDA KEMPMPQMAY VETRLSGYRL LHTHLGGGGL SRPDLTTLFL NRLDVLAALD VDVKNGLPGQ LHIAQLSPPG ALEEDWQVLP SKPYHDYLEW DLTGATAALE EELARRSRTY ELQDGAGERA ILVGVDQGEG VQAEVDLLEL AELARTAGAV AVHKELVFRP TLDPRYAVGR GKLEELQSRA YHENAGTLIF GIDLTPAQAR EIEAVTGLKV LDRTQLILDI FAQHARSPEA KAQVELAQLK YLLPRLVGKG KELSRLGGGI GTRGPGETKL EVDRRRLQER ITLLSDKLRE IAGRRQETRR ARERSGLPVV AVVGYTNAGK TTLMQALAKN GDAGENKLFA TLRPLTRRGF VPGVGEVLYT DTVGFIRHMP EELVEAFRST LEELREADLL LHVLDASSEG ALERHAVVEE LLGRLEVEVP RVLVLAKADR AGGYDLEFIQ ERLGGISVSA LSGAGLPQLK EQIAARLLSS GVRPAEWARA NVWVS // ID D7BN89_ARCHD Unreviewed; 526 AA. AC D7BN89; DT 10-AUG-2010, integrated into UniProtKB/TrEMBL. DT 10-AUG-2010, sequence version 1. DT 07-JUN-2017, entry version 50. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Arch_0654 {ECO:0000313|EMBL:ADH92388.1}; OS Arcanobacterium haemolyticum (strain ATCC 9345 / DSM 20595 / NBRC OS 15585 / NCTC 8452 / 11018). OC Bacteria; Actinobacteria; Actinomycetales; Actinomycetaceae; OC Arcanobacterium. OX NCBI_TaxID=644284 {ECO:0000313|EMBL:ADH92388.1, ECO:0000313|Proteomes:UP000000376}; RN [1] {ECO:0000313|EMBL:ADH92388.1, ECO:0000313|Proteomes:UP000000376} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 9345 / DSM 20595 / NBRC 15585 / NCTC 8452 / 11018 RC {ECO:0000313|Proteomes:UP000000376}; RX PubMed=21304742; RA Yasawong M., Teshima H., Lapidus A., Nolan M., Lucas S., RA Glavina Del Rio T., Tice H., Cheng J.F., Bruce D., Detter C., RA Tapia R., Han C., Goodwin L., Pitluck S., Liolios K., Ivanova N., RA Mavromatis K., Mikhailova N., Pati A., Chen A., Palaniappan K., RA Land M., Hauser L., Chang Y.J., Jeffries C.D., Rohde M., Sikorski J., RA Pukall R., Goker M., Woyke T., Bristow J., Eisen J.A., Markowitz V., RA Hugenholtz P., Kyrpides N.C., Klenk H.P.; RT "Complete genome sequence of Arcanobacterium haemolyticum type strain RT (11018)."; RL Stand. Genomic Sci. 3:126-135(2010). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002045; ADH92388.1; -; Genomic_DNA. DR RefSeq; WP_013169886.1; NC_014218.1. DR ProteinModelPortal; D7BN89; -. DR STRING; 644284.Arch_0654; -. DR EnsemblBacteria; ADH92388; ADH92388; Arch_0654. DR KEGG; ahe:Arch_0654; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000000376; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000000376}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000000376}. FT DOMAIN 303 469 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 526 AA; 57603 MW; 49905C2041B503E1 CRC64; MSTSPWINHA RSEIIKHHHV KGDTKISAHK PTEHNHTPKN TKLGENHVDL STYEGTALQE NPAYEGAWAG ESLEREERSS LRRVTSLATE RDDKVDVEYR QLRLERVVLV GLWREGPYEA AQDSLRELAA LAETAGSTVL DGLIQKRQLP DPATYLGSGK AKELAEIVEF HGADTVIVDS ELAPSQRRAL EDVVKVKVID RTALILDIFA QHAKSREGKA QVELAQLEYL LPRLRGWGDS MSRQAGGRVA GGAGIGSRGP GETQLELDRR RIRTRMAKLR ADIKAMEPAR VTRRASRTKK AVPAVVVVGY TNAGKSSLLN TLTGAGVLVE NALFATLDPT VRRTQTADGR EYTLTDTVGF VRNLPTQLVE AFRSTLEEVG QADLLLHVVD ASHHDPVGQI QAVRSVLADV PGADTVRELI VLSKADLADP IDVAALRSRY PDSVLVSAVS GEGIAELEER IDQLLPRPQI LIDLTIPFSR GDLVSRIHDD GEILSESFTE EGTHVTAHIT EEIAGMLQDA GLMNRE // ID D7CA82_STRBB Unreviewed; 502 AA. AC D7CA82; DT 10-AUG-2010, integrated into UniProtKB/TrEMBL. DT 10-AUG-2010, sequence version 1. DT 07-JUN-2017, entry version 55. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=SBI_03318 {ECO:0000313|EMBL:ADI06439.1}; OS Streptomyces bingchenggensis (strain BCW-1). OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae; OC Streptomyces. OX NCBI_TaxID=749414 {ECO:0000313|EMBL:ADI06439.1, ECO:0000313|Proteomes:UP000000377}; RN [1] {ECO:0000313|EMBL:ADI06439.1, ECO:0000313|Proteomes:UP000000377} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BCW-1 {ECO:0000313|EMBL:ADI06439.1, RC ECO:0000313|Proteomes:UP000000377}; RX PubMed=20581206; DOI=10.1128/JB.00596-10; RA Wang X.J., Yan Y.J., Zhang B., An J., Wang J.J., Tian J., Jiang L., RA Chen Y.H., Huang S.X., Yin M., Zhang J., Gao A.L., Liu C.X., Zhu Z.X., RA Xiang W.S.; RT "Genome sequence of the milbemycin-producing bacterium Streptomyces RT bingchenggensis."; RL J. Bacteriol. 192:4526-4527(2010). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002047; ADI06439.1; -; Genomic_DNA. DR RefSeq; WP_014175916.1; NC_016582.1. DR ProteinModelPortal; D7CA82; -. DR STRING; 749414.SBI_03318; -. DR EnsemblBacteria; ADI06439; ADI06439; SBI_03318. DR KEGG; sbh:SBI_03318; -. DR PATRIC; fig|749414.3.peg.3439; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000000377; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000000377}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000000377}. FT DOMAIN 278 443 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 502 AA; 55047 MW; 0CFD02795BC875B5 CRC64; MTHSSSLPQD RQRIAFAESL RADALMEEDV AWSHEIDQER DGDQYDRSER AALRRVVGLS TELEDVTEVE YRQLRLERVV LVGVWTSGTM QDAENSLSEL AALAETAGAL VLDGVIQRRD KPDPATYIGS GKARELRDIV IESGADTVVC DGELSPGQLI HLEDVVKVKV VDRTALILDI FAQHAKSREG KAQVSLAQMQ YMLPRLRGWG QSLSRQMGGG GSGAAGGGGM ATRGPGETKI ETDRRRIREK MAKMRREIAE MKTGRDIKRQ ERKRHKVPSV AIAGYTNAGK SSLLNRLTGA GVLVENALFA TLDPTVRRAE TPSGRLYTLA DTVGFVRHLP HHLVEAFRST MEEVGDADLI VHVVDGSHPM PEEQLAAVRE VIRDVGAVDV PEIVVINKAD MADPLVLQRL LRVEKRALVV SARTGQGIDE LLGLIDNELP RPQVEIEALV PYTQGKLVAR THAEGEVISE EHTPEGTLLK ARVHEELAAE LRRYVPAGSA QG // ID D7CQW6_TRURR Unreviewed; 568 AA. AC D7CQW6; DT 10-AUG-2010, integrated into UniProtKB/TrEMBL. DT 10-AUG-2010, sequence version 1. DT 07-JUN-2017, entry version 50. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Trad_1986 {ECO:0000313|EMBL:ADI15100.1}; OS Truepera radiovictrix (strain DSM 17093 / CIP 108686 / LMG 22925 / OS RQ-24). OC Bacteria; Deinococcus-Thermus; Deinococci; Deinococcales; OC Trueperaceae; Truepera. OX NCBI_TaxID=649638 {ECO:0000313|EMBL:ADI15100.1, ECO:0000313|Proteomes:UP000000379}; RN [1] {ECO:0000313|Proteomes:UP000000379} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 17093 / CIP 108686 / LMG 22925 / RQ-24 RC {ECO:0000313|Proteomes:UP000000379}; RG US DOE Joint Genome Institute (JGI-PGF); RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., RA Tice H., Bruce D., Goodwin L., Pitluck S., Kyrpides N., Mavromatis K., RA Ovchinnikova G., Munk A.C., Detter J.C., Han C., Tapia R., Land M., RA Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T., Wu D., RA Tindall B., Pomrenke H.G., Brambilla E., Klenk H.-P., Eisen J.A.; RT "The complete genome of Truepera radiovictris DSM 17093."; RL Submitted (MAY-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002049; ADI15100.1; -; Genomic_DNA. DR RefSeq; WP_013178465.1; NC_014221.1. DR ProteinModelPortal; D7CQW6; -. DR STRING; 649638.Trad_1986; -. DR EnsemblBacteria; ADI15100; ADI15100; Trad_1986. DR KEGG; tra:Trad_1986; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; EREVIIT; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000000379; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000000379}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000000379}. FT DOMAIN 383 550 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 342 369 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 568 AA; 61765 MW; B21E8A87DE545520 CRC64; MNKVHGKLSG LKTSQVKRLS NLYRRRLDPS AVVSQELARA LGELSLEFHK PVSVLVDRRG RVVTVALGDA ADTPLPARPG EAEGRLYGLR LVHTHLKGGG LSQGDLSKLF LNRLDAVVAV DVRANARGDA EVTQVHLAQI APPRAEAEDW LISPPMSMQR AEKLDFLELT RALEEELSRS ARARETKRSS QERAVLVGLN TGESPFESDS RLAELAELAR SAGATVAVMS KQQRAAPDPR TLIGRGKLQE LVSRAYHEDA DLLIFDRELN PAQAREIAQE TQLKVVDRTQ LILDIFAQNA RGREAQVQVE LAQLQYQVTR LAGRGRAMSR LGGGIGTRGP GETKLEVDRR RIRDRIAALQ AEVAQISQRR AEGRKGRKAS EVPVIALVGY TNAGKSTLFN ALAKADVLSQ NRLFATLRPT TREGWLPALG AWGGKVLYTD TVGFIRDLPE ELVDAFRATL EELHDAELLL HVVDAATPGA PDRVAAVNRI LDDLGVEVPR TVVLNKADLA APAELKDLAK RYNALGVSAA TGAGLDALKA SLAQLLEGPR HVPLPDDPGR AYGMTFHD // ID D7DP07_METV0 Unreviewed; 450 AA. AC D7DP07; DT 10-AUG-2010, integrated into UniProtKB/TrEMBL. DT 10-AUG-2010, sequence version 1. DT 30-AUG-2017, entry version 49. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=M301_2683 {ECO:0000313|EMBL:ADI31038.1}; OS Methylotenera versatilis (strain 301). OC Bacteria; Proteobacteria; Betaproteobacteria; Nitrosomonadales; OC Methylophilaceae; Methylotenera. OX NCBI_TaxID=666681 {ECO:0000313|EMBL:ADI31038.1, ECO:0000313|Proteomes:UP000000383}; RN [1] {ECO:0000313|Proteomes:UP000000383} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=301 {ECO:0000313|Proteomes:UP000000383}; RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L., RA Pitluck S., Clum A., Land M., Hauser L., Kyrpides N., Ivanova N., RA Chistoservova L., Kalyuzhnaya M., Woyke T.; RT "Complete sequence of Methylotenera sp. 301."; RL Submitted (MAY-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002056; ADI31038.1; -; Genomic_DNA. DR RefSeq; WP_013149343.1; NC_014207.1. DR ProteinModelPortal; D7DP07; -. DR STRING; 666681.M301_2683; -. DR EnsemblBacteria; ADI31038; ADI31038; M301_2683. DR KEGG; meh:M301_2683; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR KO; K03665; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000000383; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000000383}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000000383}. FT DOMAIN 222 392 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 180 214 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 450 AA; 49980 MW; 964DC5DABB0645CD CRC64; MQKEDKEQPN YAIVAAVQIP SVTDIEFEAS LNELRELAKT LGFTVVKTFV QKRAGFDVTA YLGAGKRQEI RDYVNNEYEI TEVDEVAANL GDVEINTLLV DHEISPSQAR NLELEVGCVV MDRTMVILEI FHRNARSRAA RAQVEIARLG YMAPRMREAA KLAGSQGRQR SGEGGRGAGE SQTELDRRKI RDRIAELQLE IVAMDAERKT QRARRQERQG IAGIALVGYT NAGKSTLMRA LTGSEVLVAN KLFATLDTTV RSLYPESVPR ILVSDTVGFI KNLPHGLVAS FKSTLDEALD ASLLLHVIDA SDPGFVRQLE VTNEVLEEIG ADVVPRLRIF NKIDYVGDAA AQAECEATLR EKYPDCIVMS AKRPDDVAKL HQTIVAFFQQ DLIEAELFLP WSAQQWRGKI YASCQVLEER SDNDGAFLMV RGEAEAINKL RAQVQASTLD // ID D7DPV7_METV0 Unreviewed; 375 AA. AC D7DPV7; DT 10-AUG-2010, integrated into UniProtKB/TrEMBL. DT 10-AUG-2010, sequence version 1. DT 30-AUG-2017, entry version 47. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=M301_0944 {ECO:0000313|EMBL:ADI29328.1}; OS Methylotenera versatilis (strain 301). OC Bacteria; Proteobacteria; Betaproteobacteria; Nitrosomonadales; OC Methylophilaceae; Methylotenera. OX NCBI_TaxID=666681 {ECO:0000313|EMBL:ADI29328.1, ECO:0000313|Proteomes:UP000000383}; RN [1] {ECO:0000313|Proteomes:UP000000383} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=301 {ECO:0000313|Proteomes:UP000000383}; RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L., RA Pitluck S., Clum A., Land M., Hauser L., Kyrpides N., Ivanova N., RA Chistoservova L., Kalyuzhnaya M., Woyke T.; RT "Complete sequence of Methylotenera sp. 301."; RL Submitted (MAY-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002056; ADI29328.1; -; Genomic_DNA. DR RefSeq; WP_013147644.1; NC_014207.1. DR ProteinModelPortal; D7DPV7; -. DR STRING; 666681.M301_0944; -. DR EnsemblBacteria; ADI29328; ADI29328; M301_0944. DR KEGG; meh:M301_0944; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR KO; K03665; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000000383; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000000383}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000000383}. FT DOMAIN 199 365 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 158 185 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 375 AA; 41367 MW; 2FC425ABCD542554 CRC64; MFERPSGGDA AIMVSVDFGD NDYEESLNEL RQLSISAGLS IRGTIEGKRA TPDAKLFIGS GKADELAQMM QASESNIAVF NHDLSPSQQR NLERLLKARV VDRTGLILDI FSQRAQSHEG KLQVELAQLE HLSTRLVRGW THLERQKGGI GVRGGPGETQ LELDRRMLRV RVKQLREKLI KLKAQRGMQR RARKRSNVMT VSLVGYTNAG KSTVFNRLTK ADIYVADQLF ATLDTTTHKI YIADAGSVVL SDTVGFIKHL PHALVEAFGA TLEEAAQADL LLHIVDTAST NRDEQIAQVN KVLLEIGAAN VPQILVHNQI DRVGLPPSVS RDEYGRITTI HASASTGEGM DLLRQAMAEH SQYLHKLSTE ESAYA // ID D7DW81_NOSA0 Unreviewed; 583 AA. AC D7DW81; DT 10-AUG-2010, integrated into UniProtKB/TrEMBL. DT 10-AUG-2010, sequence version 1. DT 07-JUN-2017, entry version 52. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Aazo_1906 {ECO:0000313|EMBL:ADI63998.1}; OS Nostoc azollae (strain 0708) (Anabaena azollae (strain 0708)). OC Bacteria; Cyanobacteria; Nostocales; Nostocaceae; Trichormus. OX NCBI_TaxID=551115 {ECO:0000313|EMBL:ADI63998.1, ECO:0000313|Proteomes:UP000001511}; RN [1] {ECO:0000313|EMBL:ADI63998.1, ECO:0000313|Proteomes:UP000001511} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=0708 {ECO:0000313|EMBL:ADI63998.1, RC ECO:0000313|Proteomes:UP000001511}; RX PubMed=20628610; DOI=10.1371/journal.pone.0011486; RA Ran L., Larsson J., Vigil-Stenman T., Nylander J.A., Ininbergs K., RA Zheng W.W., Lapidus A., Lowry S., Haselkorn R., Bergman B.; RT "Genome erosion in a nitrogen-fixing vertically transmitted RT endosymbiotic multicellular cyanobacterium."; RL PLoS ONE 5:E11486-E11486(2010). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002059; ADI63998.1; -; Genomic_DNA. DR ProteinModelPortal; D7DW81; -. DR STRING; 551115.Aazo_1906; -. DR EnsemblBacteria; ADI63998; ADI63998; Aazo_1906. DR KEGG; naz:Aazo_1906; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; EREVIIT; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000001511; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000001511}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000001511}. FT DOMAIN 409 579 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 368 395 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 583 AA; 64429 MW; 7094A9FB026FC6EB CRC64; METIFGNLQG LKSSQRKQLQ RLYHQRISGD RVTTPEFAQR LAAISTELNQ PVCTYLNRRG HVVRVGVGTP CQTQIPPLEL PRYSAQRLSG IRCIATHLKA EPPNEAALTA MALQRLDALV VLNITGTGFT RRGGGSTGYV KEAYLAHLLA NSKQLLFTQS SGQSSGITIP DTNLYSSVSP PLSLDAIADE DFLDLVESLE EEFSREYIAQ EVDADHDRVV IVGVLTDKMT SQQFQDTILE LARLVDTAGG DVLQTLQQKR LRIHPQTVIG EGKVQEVALT AQTLGANLVV FDRDLSPTQV RNLEAQIGIR VVDRTEVILD IFAQRAQSGA GKLQVELAQL EYMLPRLTGR GRAMSRLGGG IGTRGPGETK LETERRAIQK RISRLQQEVN QLQAHRCRLR QRRQHREVPS VALVGYTNAG KSTLLNALTN AEVYTADQLF ATLDPTTRRL IIPHVGTSEL QETLITDTVG FIHELPNSLM DAFRATLEEV TEADALIHLV DLSHPAWLSH IRSVRDILAQ MPITPGPCLV VFNKIDQVDS EALALAREEF PLAVFISASQ RLGLETLRQR LSQLIQYAVD GDC // ID D7E8C0_METEZ Unreviewed; 418 AA. AC D7E8C0; DT 10-AUG-2010, integrated into UniProtKB/TrEMBL. DT 10-AUG-2010, sequence version 1. DT 07-JUN-2017, entry version 57. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Metev_0551 {ECO:0000313|EMBL:ADI73462.1}; OS Methanohalobium evestigatum (strain ATCC BAA-1072 / DSM 3721 / NBRC OS 107634 / OCM 161 / Z-7303). OC Archaea; Euryarchaeota; Methanomicrobia; Methanosarcinales; OC Methanosarcinaceae; Methanohalobium. OX NCBI_TaxID=644295 {ECO:0000313|EMBL:ADI73462.1, ECO:0000313|Proteomes:UP000000391}; RN [1] {ECO:0000313|EMBL:ADI73462.1, ECO:0000313|Proteomes:UP000000391} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-1072 / DSM 3721 / NBRC 107634 / OCM 161 / Z-7303 RC {ECO:0000313|Proteomes:UP000000391}; RG US DOE Joint Genome Institute; RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L., RA Pitluck S., Saunders E., Detter J.C., Han C., Tapia R., Land M., RA Hauser L., Kyrpides N., Mikhailova N., Sieprawska-Lupa M., RA Whitman W.B., Anderson I., Woyke T.; RT "Complete sequence chromosome of Methanohalobium evestigatum Z-7303."; RL Submitted (JUN-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002069; ADI73462.1; -; Genomic_DNA. DR RefSeq; WP_013194030.1; NC_014253.1. DR ProteinModelPortal; D7E8C0; -. DR STRING; 644295.Metev_0551; -. DR EnsemblBacteria; ADI73462; ADI73462; Metev_0551. DR GeneID; 9346173; -. DR KEGG; mev:Metev_0551; -. DR eggNOG; arCOG00353; Archaea. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG093Z07D6; -. DR Proteomes; UP000000391; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000000391}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000000391}. FT DOMAIN 191 360 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 107 141 {ECO:0000256|SAM:Coils}. FT COILED 157 184 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 418 AA; 47690 MW; A755C6A8443DE6D5 CRC64; MKSVILVQRN EPRSNESENS DKLFELEELA KSAGYCIVGE ITQSKNPDRR YQVGRGKVDE LASLVNEYNA EKVIFYNQLS TIQIYNVSET CKCEVIDKFH LILEIFATRA TTKRAKLQVE LAQLEYELPK AKNIVSLLKQ EERPGFMSLG EYEDSYEQDI KNRISRIKNE LKTAKKDRES LRKFRHDKGF SLVALAGYTN AGKSTLFNTI VDEDVRVEDM LFTTLSPVTR SLNLGGRHVL LTDTVGFIED LPHWMIDAFR STLDEIFLTD VILLVVDVAE DAEKIRKKLA TSHEILWNKS EGAPIITVLN KVDAIKSDEL NKKLDKIEYL APNPVFISAK SGYGLDNLKK QINQQVPGWK RTSVSLPMSD DGMAAVSWLF EEGVVHNIDY GDYIEVDLEA RDEIIHKAQI YEREIFVD // ID D7FHX0_ECTSI Unreviewed; 458 AA. AC D7FHX0; DT 10-AUG-2010, integrated into UniProtKB/TrEMBL. DT 10-AUG-2010, sequence version 1. DT 07-JUN-2017, entry version 32. DE SubName: Full=MHflX, mitochondrial HflX GTPase {ECO:0000313|EMBL:CBJ48981.1}; GN Name=MHflX {ECO:0000313|EMBL:CBJ48981.1}; GN ORFNames=Esi_0115_0018 {ECO:0000313|EMBL:CBJ48981.1}; OS Ectocarpus siliculosus (Brown alga) (Conferva siliculosa). OC Eukaryota; Stramenopiles; PX clade; Phaeophyceae; Ectocarpales; OC Ectocarpaceae; Ectocarpus. OX NCBI_TaxID=2880 {ECO:0000313|EMBL:CBJ48981.1, ECO:0000313|Proteomes:UP000002630}; RN [1] {ECO:0000313|EMBL:CBJ48981.1, ECO:0000313|Proteomes:UP000002630} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Ec32 / CCAP1310/4 {ECO:0000313|Proteomes:UP000002630}; RX PubMed=20520714; DOI=10.1038/nature09016; RA Cock J.M., Sterck L., Rouze P., Scornet D., Allen A.E., Amoutzias G., RA Anthouard V., Artiguenave F., Aury J.M., Badger J.H., Beszteri B., RA Billiau K., Bonnet E., Bothwell J.H., Bowler C., Boyen C., RA Brownlee C., Carrano C.J., Charrier B., Cho G.Y., Coelho S.M., RA Collen J., Corre E., Da Silva C., Delage L., Delaroque N., RA Dittami S.M., Doulbeau S., Elias M., Farnham G., Gachon C.M., RA Gschloessl B., Heesch S., Jabbari K., Jubin C., Kawai H., Kimura K., RA Kloareg B., Kupper F.C., Lang D., Le Bail A., Leblanc C., Lerouge P., RA Lohr M., Lopez P.J., Martens C., Maumus F., Michel G., RA Miranda-Saavedra D., Morales J., Moreau H., Motomura T., Nagasato C., RA Napoli C.A., Nelson D.R., Nyvall-Collen P., Peters A.F., Pommier C., RA Potin P., Poulain J., Quesneville H., Read B., Rensing S.A., RA Ritter A., Rousvoal S., Samanta M., Samson G., Schroeder D.C., RA Segurens B., Strittmatter M., Tonon T., Tregear J.W., Valentin K., RA von Dassow P., Yamagishi T., Van de Peer Y., Wincker P.; RT "The Ectocarpus genome and the independent evolution of RT multicellularity in brown algae."; RL Nature 465:617-621(2010). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; FN647841; CBJ48981.1; -; Genomic_DNA. DR HOGENOM; HOG000260368; -. DR InParanoid; D7FHX0; -. DR Proteomes; UP000002630; Chromosome LG26. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR CDD; cd01878; HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 3. DR SUPFAM; SSF52540; SSF52540; 2. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000002630}; KW Reference proteome {ECO:0000313|Proteomes:UP000002630}. FT DOMAIN 170 424 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 458 AA; 49009 MW; 6D9D5B66BBC2C9FA CRC64; MVARTAVAFG RKAKVVQLRN VHPKFVFGSG KTSEMSGAIS AADADTIFVN APLSGQQQKA LSAEWGGATV LDRFAVILDI FADRARTTEA KLQVELAMLK YKAAHLVKGS GSGFDRQGGG VGTMGGSGEK AIDTQRRLLR NRTAEVHRQL KDVERRRGFQ RSSRDRRLEA SVALVGYTNV GKSSLMNQLA LGRHSTRGVG GGGGNREGRG GERGRRFEGA GGGAGKGKGM VQARNRVFDT LDPTVRSVTL PSRVRCVLVD TVGFIQDLPT DLVHSFKSTL EEVKSADVLL HVRDASVEPR VCEAHRKAVQ ETLAELGAGG VPTLEVWNKV DKERRLDPEN RGANTGAGRS DGGGSYMSLP YEAEAEKANR RTEGPAGEGG SRLSHAREGR TGPDDEGAIR VSAASGQGLA HLLERIDAML HLNGGADGEG SGRRFSTKPI DRYEYVRVLP GQSQQGYK // ID D7G4N1_ECTSI Unreviewed; 823 AA. AC D7G4N1; DT 10-AUG-2010, integrated into UniProtKB/TrEMBL. DT 10-AUG-2010, sequence version 1. DT 12-APR-2017, entry version 31. DE SubName: Full=PHflX, plastid HflX GTPase {ECO:0000313|EMBL:CBJ33718.1}; GN Name=PHflX {ECO:0000313|EMBL:CBJ33718.1}; GN ORFNames=Esi_0570_0006 {ECO:0000313|EMBL:CBJ33718.1}; OS Ectocarpus siliculosus (Brown alga) (Conferva siliculosa). OC Eukaryota; Stramenopiles; PX clade; Phaeophyceae; Ectocarpales; OC Ectocarpaceae; Ectocarpus. OX NCBI_TaxID=2880 {ECO:0000313|EMBL:CBJ33718.1, ECO:0000313|Proteomes:UP000002630}; RN [1] {ECO:0000313|EMBL:CBJ33718.1, ECO:0000313|Proteomes:UP000002630} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Ec32 / CCAP1310/4 {ECO:0000313|Proteomes:UP000002630}; RX PubMed=20520714; DOI=10.1038/nature09016; RA Cock J.M., Sterck L., Rouze P., Scornet D., Allen A.E., Amoutzias G., RA Anthouard V., Artiguenave F., Aury J.M., Badger J.H., Beszteri B., RA Billiau K., Bonnet E., Bothwell J.H., Bowler C., Boyen C., RA Brownlee C., Carrano C.J., Charrier B., Cho G.Y., Coelho S.M., RA Collen J., Corre E., Da Silva C., Delage L., Delaroque N., RA Dittami S.M., Doulbeau S., Elias M., Farnham G., Gachon C.M., RA Gschloessl B., Heesch S., Jabbari K., Jubin C., Kawai H., Kimura K., RA Kloareg B., Kupper F.C., Lang D., Le Bail A., Leblanc C., Lerouge P., RA Lohr M., Lopez P.J., Martens C., Maumus F., Michel G., RA Miranda-Saavedra D., Morales J., Moreau H., Motomura T., Nagasato C., RA Napoli C.A., Nelson D.R., Nyvall-Collen P., Peters A.F., Pommier C., RA Potin P., Poulain J., Quesneville H., Read B., Rensing S.A., RA Ritter A., Rousvoal S., Samanta M., Samson G., Schroeder D.C., RA Segurens B., Strittmatter M., Tonon T., Tregear J.W., Valentin K., RA von Dassow P., Yamagishi T., Van de Peer Y., Wincker P.; RT "The Ectocarpus genome and the independent evolution of RT multicellularity in brown algae."; RL Nature 465:617-621(2010). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; FN648786; CBJ33718.1; -; Genomic_DNA. DR ProteinModelPortal; D7G4N1; -. DR InParanoid; D7G4N1; -. DR Proteomes; UP000002630; Unplaced LGUn. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000002630}; KW Reference proteome {ECO:0000313|Proteomes:UP000002630}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1 16 {ECO:0000256|SAM:SignalP}. FT CHAIN 17 823 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5003096186. FT DOMAIN 547 719 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 823 AA; 88655 MW; 45A360689F56618D CRC64; MYPSPALLLA LPCTLAFFQS PNAGLSALQR TGNACTASTR GATTWPAERS DGSAAAAVGR RRRARRPHAV PVLFGKGRKK RGAAVSQDAS SWYDEDEEDA VVGGAAAGDS DGADAAAAAA FSTTPAAAAT AEAGASSGDI QEGRRDVGTR GDKGSSSATM TDDILLPSLD DDGNQIVLEP VWVEGETQGE KPIVEAYGLN DALAGAEDGI DIDNGMMAGG VSGDEALLIP TADGGVLPGG LGDGVGPESW RNGMEVPDDD VVLGERFNMG RGLDDMLMER SVRFYDPKVT GERERCYLVG LEASGWGMGN KRDTKGSFPE KGAAAGNGDG EGGEDDGWTE EQEAAFQEEK QLAYEARKEE REMRFTLEES MAELSELAGT AGLEVAGSTY QRVLEPNPRT YIGTGKVKEI KSAMNQLGVC TVIFDDELSP GQQRSLEVEF GGEAAGIKVL DRTALILDIF AQHAKTREGQ LQVDLALHMY RLPRLTKMWT HLERQQGGVG LRGPGERQLE VDRRLLKDKI IALKKELSGV RRHRDFQRRG RKKLGLPVVA LVGYTNAGKS TLLNTLTRAG VMAENMLFAT LDPTTRKVKL SGLKVHPEVM LTDTVGFIQK LPTNLVAAFR ATLEEVVEAD VIVHIVDVSS PSREKQESAV TGVLGEMKTS DKPRLTMWNK LDLLPEEEQE QVRVDAEERD ELTVAASAMT GEGLDDFVTC LEEAICALLF KVEAVVPYSR GDLLSRVHEL GACDTEEYTD AGTLIQARVP AELLNRLEPF FTPEFKETSR VEASNSGAEE AAALREENTW KQIAKKRLKT SSLDEEAPVA VPK // ID D7GE63_PROFC Unreviewed; 473 AA. AC D7GE63; DT 10-AUG-2010, integrated into UniProtKB/TrEMBL. DT 10-AUG-2010, sequence version 1. DT 07-JUN-2017, entry version 44. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=PFREUD_13060 {ECO:0000313|EMBL:CBL56824.1}; OS Propionibacterium freudenreichii subsp. shermanii (strain ATCC 9614 / OS DSM 4902 / CIP 103027 / NCIMB 8099 / CIRM-BIA1). OC Bacteria; Actinobacteria; Propionibacteriales; Propionibacteriaceae; OC Propionibacterium. OX NCBI_TaxID=754252 {ECO:0000313|EMBL:CBL56824.1, ECO:0000313|Proteomes:UP000000936}; RN [1] {ECO:0000313|EMBL:CBL56824.1, ECO:0000313|Proteomes:UP000000936} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 9614 / DSM 4902 / CIP 103027 / NCIMB 8099 / CIRM-BIA1 RC {ECO:0000313|Proteomes:UP000000936}; RX PubMed=20668525; DOI=10.1371/journal.pone.0011748; RA Falentin H., Deutsch S.M., Jan G., Loux V., Thierry A., Parayre S., RA Maillard M.B., Dherbecourt J., Cousin F.J., Jardin J., Siguier P., RA Couloux A., Barbe V., Vacherie B., Wincker P., Gibrat J.F., RA Gaillardin C., Lortal S.; RT "The complete genome of Propionibacterium freudenreichii CIRM-BIA1, a RT hardy actinobacterium with food and probiotic applications."; RL PLoS ONE 5:E11748-E11748(2010). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; FN806773; CBL56824.1; -; Genomic_DNA. DR RefSeq; WP_013161192.1; NC_014215.1. DR ProteinModelPortal; D7GE63; -. DR STRING; 754252.PFREUD_13060; -. DR EnsemblBacteria; CBL56824; CBL56824; PFREUD_13060. DR GeneID; 29491023; -. DR KEGG; pfr:PFREUD_13060; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000000936; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000000936}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000000936}. FT DOMAIN 254 419 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 473 AA; 52094 MW; 0DA3C20F4CB5C102 CRC64; MTAGVPEPHE RDNEARHDVT DELLDLEERH SLTRVAGMST ELQDESEVEY RQLRLERVVL VSVWTTGTQA DADNAMQELR ALAETAGSQV LEGLVQRRSR PDAATYIGEG KVTELREAVV ATGADTVIAD GELSPAQLRN LEDRVGVKVV DRTALILDIF AQHAKSTEGK TQVELAQLNY MKQRLRGWGE SLSRQVGGRA ASGVGIGGRG PGETKLETDR RRINTRIATL RKKLRAMDAS RALQREERVR HRIPSVALVG YTNAGKSSLL NRLTGAGVLV EDALFATLDP TTRRCRTTDG RVYTLTDTVG FVRHLPTDLV AAFRSTLEES VRADLLLHVV DGSDPDPEGQ ITAVHEVLRD IGAGERPEQI VVNKVDLASS QSLLELRHNH PDAVFVSAVT GEGLEELRTR TESRLPTPQT SVDVVVPWDR GDLVDKVHRF GEISQDEYLA EGTHLVARVY PDLAGELKPY ERA // ID D7GU23_9FIRM Unreviewed; 417 AA. AC D7GU23; DT 10-AUG-2010, integrated into UniProtKB/TrEMBL. DT 10-AUG-2010, sequence version 1. DT 07-JUN-2017, entry version 47. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=CK3_16450 {ECO:0000313|EMBL:CBL41315.1}; OS butyrate-producing bacterium SS3/4. OC Bacteria; Firmicutes; Clostridia; Clostridiales. OX NCBI_TaxID=245014 {ECO:0000313|EMBL:CBL41315.1, ECO:0000313|Proteomes:UP000008961}; RN [1] {ECO:0000313|EMBL:CBL41315.1, ECO:0000313|Proteomes:UP000008961} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SS3/4 {ECO:0000313|EMBL:CBL41315.1, RC ECO:0000313|Proteomes:UP000008961}; RG metaHIT consortium -- http://www.metahit.eu/; RA Pajon A., Turner K., Parkhill J., Duncan S., Flint H.; RT "The genome sequence of Clostridiales sp. SS3/4."; RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:CBL41315.1, ECO:0000313|Proteomes:UP000008961} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SS3/4 {ECO:0000313|EMBL:CBL41315.1, RC ECO:0000313|Proteomes:UP000008961}; RA Pajon A.; RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; FP929062; CBL41315.1; -; Genomic_DNA. DR ProteinModelPortal; D7GU23; -. DR STRING; 245014.CK3_16450; -. DR EnsemblBacteria; CBL41315; CBL41315; CK3_16450. DR KEGG; bprs:CK3_16450; -. DR PATRIC; fig|245014.3.peg.58; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR KO; K03665; -. DR BioCyc; BBAC245014:G1314-1402-MONOMER; -. DR Proteomes; UP000008961; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000008961}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000008961}. FT DOMAIN 202 366 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 168 195 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 417 AA; 46914 MW; 76B7A938E9F15DEE CRC64; MAELIEIGEQ QERVILFAAS TNASDDTEES VEELRELVKT AGAETVGAVI QNRENIHPGT YLGKGKIQEL KEMVWESGAT GVVCDDELSP AQLKNLEDAL DTKVMDRTMI ILDIFAARAK TREGKIQVEL AQLRYRAVRL VGLRNSLSRL GGGIGTRGPG ETKLEVDRRR IHERISQLKS ELQDVERHRD VVRKQREQSG TLTAAIVGYT NAGKSTLLNK LTGAGILAED KLFATLDPTT RALTLPGGEK VLLTDTVGFI RKLPHHLVEA FKSTLEEARY CDVILHVVDC SNPQMDMQMH VVYETLRRLD IKDKEIITVF NKVDRPDADT ACRDMSADYK VKLSAKTGEG IEELLDLFAI ILRNRRIYFE KVFAYRDAGR IQTIRKSGQL LSEEYQDDGI HVKAYVPVEL FEELYRD // ID D7JFE9_9BACT Unreviewed; 421 AA. AC D7JFE9; DT 10-AUG-2010, integrated into UniProtKB/TrEMBL. DT 10-AUG-2010, sequence version 1. DT 07-JUN-2017, entry version 44. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=HMPREF0156_01216 {ECO:0000313|EMBL:EFI17618.1}; OS Bacteroidetes oral taxon 274 str. F0058. OC Bacteria; Bacteroidetes. OX NCBI_TaxID=575590 {ECO:0000313|EMBL:EFI17618.1, ECO:0000313|Proteomes:UP000004685}; RN [1] {ECO:0000313|Proteomes:UP000004685} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=F0058 {ECO:0000313|Proteomes:UP000004685}; RG The Broad Institute Genome Sequencing Platform; RA Ward D., Earl A., Feldgarden M., Gevers D., Young S.K., Zeng Q., RA Koehrsen M., Alvarado L., Berlin A., Bochicchio J., Borenstein D., RA Chapman S.B., Chen Z., Engels R., Freedman E., Gellesch M., RA Goldberg J., Griggs A., Gujja S., Heilman E., Heiman D., Hepburn T., RA Howarth C., Jen D., Larson L., Mehta T., Park D., Pearson M., RA Roberts A., Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., RA Thomson T., Walk T., White J., Yandava C., Izard J., Baranova O.V., RA Blanton J.M., Tanner A.C., Dewhirst F.E., Haas B., Nusbaum C., RA Birren B.; RT "The Genome Sequence of Bacteroidetes bacterium Oral taxon 274 strain RT F0058."; RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GG774889; EFI17618.1; -; Genomic_DNA. DR RefSeq; WP_009217629.1; NZ_GG774889.1. DR ProteinModelPortal; D7JFE9; -. DR STRING; 575590.HMPREF0156_01216; -. DR EnsemblBacteria; EFI17618; EFI17618; HMPREF0156_01216. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000004685; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000004685}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000004685}. FT DOMAIN 217 401 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 421 AA; 48670 MW; 4FB7554B89DEAB4D CRC64; MLFYNKIVPL QKIYEKEFGR SEYLMEKAVL IGIITPQQPE TKAKEYIEEL AFLSETAGAV PVKRFFQNLP YPNPRTFVGE GKLAEIREYI ADNEEITLVI FDDELSPVQL RNIENILKIK ILDRTNLILD IFAQRAQTAN AKTQVELAQC QYMLPRLTRL WTHLERQRGG IGMRGPGETQ IETDRRILLS KISLLKEKLR KIDQQKTIQR KNRENMIRVA LVGYTNAGKS TIMNLIGKSN VLAENKLFAT LDTTVRKVIV DNLPFLLSDT VGFIRKLPHN LIESFKSTLD ELNEADILVH VCDISHPNFE EQFDVVNETI KSIVKTEKPT IVVFNKIDNY SFTEKDEADL SVRTKDNIPL DELQKTYMAK LAGNCLFISA KEKINIDSFK LILYDKVKEL YSQKYPYSNF IFDKYDDLEQ K // ID D7LSX2_ARALL Unreviewed; 1188 AA. AC D7LSX2; DT 10-AUG-2010, integrated into UniProtKB/TrEMBL. DT 10-AUG-2010, sequence version 1. DT 30-AUG-2017, entry version 45. DE SubName: Full=Pentatricopeptide repeat-containing protein {ECO:0000313|EMBL:EFH53955.1}; GN ORFNames=ARALYDRAFT_323555 {ECO:0000313|EMBL:EFH53955.1}; OS Arabidopsis lyrata subsp. lyrata (Lyre-leaved rock-cress). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae; OC Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae; OC Arabidopsis. OX NCBI_TaxID=81972 {ECO:0000313|Proteomes:UP000008694}; RN [1] {ECO:0000313|Proteomes:UP000008694} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. MN47 {ECO:0000313|Proteomes:UP000008694}; RX PubMed=21478890; DOI=10.1038/ng.807; RA Hu T.T., Pattyn P., Bakker E.G., Cao J., Cheng J.-F., Clark R.M., RA Fahlgren N., Fawcett J.A., Grimwood J., Gundlach H., Haberer G., RA Hollister J.D., Ossowski S., Ottilar R.P., Salamov A.A., RA Schneeberger K., Spannagl M., Wang X., Yang L., Nasrallah M.E., RA Bergelson J., Carrington J.C., Gaut B.S., Schmutz J., Mayer K.F.X., RA Van de Peer Y., Grigoriev I.V., Nordborg M., Weigel D., Guo Y.-L.; RT "The Arabidopsis lyrata genome sequence and the basis of rapid genome RT size change."; RL Nat. Genet. 43:476-481(2011). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GL348717; EFH53955.1; -; Genomic_DNA. DR RefSeq; XP_002877696.1; XM_002877650.1. DR ProteinModelPortal; D7LSX2; -. DR STRING; 59689.fgenesh1_pm.C_scaffold_5001099; -. DR EnsemblPlants; fgenesh1_pm.C_scaffold_5001099; fgenesh1_pm.C_scaffold_5001099; fgenesh1_pm.C_scaffold_5001099. DR Gramene; fgenesh1_pm.C_scaffold_5001099; fgenesh1_pm.C_scaffold_5001099; fgenesh1_pm.C_scaffold_5001099. DR KEGG; aly:ARALYDRAFT_323555; -. DR OrthoDB; EOG093608HG; -. DR Proteomes; UP000008694; Unassembled WGS sequence. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR CDD; cd01878; HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR002885; Pentatricopeptide_repeat. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR Pfam; PF01535; PPR; 1. DR Pfam; PF12854; PPR_1; 2. DR Pfam; PF13041; PPR_2; 3. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 2. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00756; PPR; 7. DR PROSITE; PS51705; G_HFLX; 1. DR PROSITE; PS51375; PPR; 11. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008694}; KW Reference proteome {ECO:0000313|Proteomes:UP000008694}. FT REPEAT 133 167 PPR. {ECO:0000256|PROSITE- FT ProRule:PRU00708}. FT REPEAT 169 203 PPR. {ECO:0000256|PROSITE- FT ProRule:PRU00708}. FT REPEAT 204 234 PPR. {ECO:0000256|PROSITE- FT ProRule:PRU00708}. FT REPEAT 238 272 PPR. {ECO:0000256|PROSITE- FT ProRule:PRU00708}. FT REPEAT 273 307 PPR. {ECO:0000256|PROSITE- FT ProRule:PRU00708}. FT REPEAT 308 343 PPR. {ECO:0000256|PROSITE- FT ProRule:PRU00708}. FT REPEAT 344 378 PPR. {ECO:0000256|PROSITE- FT ProRule:PRU00708}. FT REPEAT 379 413 PPR. {ECO:0000256|PROSITE- FT ProRule:PRU00708}. FT REPEAT 414 448 PPR. {ECO:0000256|PROSITE- FT ProRule:PRU00708}. FT REPEAT 449 483 PPR. {ECO:0000256|PROSITE- FT ProRule:PRU00708}. FT REPEAT 523 557 PPR. {ECO:0000256|PROSITE- FT ProRule:PRU00708}. FT DOMAIN 914 1149 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 1188 AA; 134685 MW; C9568EC01DA542F9 CRC64; MRRFSTIVDL LLISKKPSSQ SQANSRIDLI CKRFHISRVL NNDFVESTER KNGLGLVFPE KHEDEFAGDV EKIYRILRNY HSRVPKLELS LNESGIDLRP GLIVRVLSRC GDAGNLGYRF FLWATKQPGY CHSYEVCKSM VKILSKMRQF GAVWGLIEEM RKENPELIEP ELFVVLIRRF ASANMVKKAV EVLDEMPKYG FEPDEYVFGC LLDALCKNGS VKDASKVFED MREKIPPNLR YFTSLLYGWC REGKLMEAKE VLVQMKEAGL EPDIVVFTNL LSGYAHAGKM ADAYDLLNDM RKRGYEPNAN CYTVLIQALC RTEKRMDEAM RVFVEMERYG CEADIVTYTA LISGFCKWGM IDKGYSVLDD MRKKGVMPSQ VTYMQILVAH EKKEQFEECL ELIEKMKQIG CHPDLLIYNV VIRLACNFRE VKEAVRLWNE MEANGLSPGA DMFVIMINGF TSQGYLIEAC SHFKEMVSRG IFSAPQYGTL KSLLNTLLRD DKLEMAKDVW SCISNKTSSC ELNVSAWTIW IHALFAKGHV KEACSYCLDM MEMDLMPQPN TYVKLMKGLN KLYNRTIAAE ITEKVMKMAS EREMSFKMYK KRGEEDLIEK AKPKGNNKEG KKKGTDHHRH KGGVSLARNR LRSETPSSFL ARNHLRSKTP SSSPFSSKRH APKTSEVEEE STPKDSVLLN PKDPSSPPKL FLVQPRLAPP KLLQAKLNEA LCLANSLEEQ RYGYFESDFF DKELPSHVVV QNPVRRSSKP REEVDAVFVN AILTAIQQRN LERIWAKPVL DRVGLIIEIF NAHAHTKEAK LQAELAALMY NKSRLVRVRG TDGRHTFGQF GEAEVVSARG RAGSKGTGGG FVGGAGETEL QLQRRRISDR RLRLLSQIKE AQRTRLLQRA GRNKRVGLEG ESSGTIAVVG YTNAGKSTLI SALTKTALYC NERLFATLDP TLKSAHLPSG KFVLLSDTVG FISDLPIQLV KAFQSTLEEV VEADILLHVV DSTAPNIEEH RSTVFHILKQ IGVSEEKLQN MIEVWNKIDY EEEEEVGDAK YLDDGEGEEE EADLKAEETV DASIAAVNED QIQNQDNDSD GWLLSEDENA DDSELWKVPE VAKVDAAQKK GPDVRVSALT GVGLKELLYL IDDKMKVEEE KKLKSQTVVE RSDLHKRKWR PPRNDDDEEV RVIPLDQR // ID D7MNY2_ARALL Unreviewed; 541 AA. AC D7MNY2; DT 10-AUG-2010, integrated into UniProtKB/TrEMBL. DT 10-AUG-2010, sequence version 1. DT 05-JUL-2017, entry version 47. DE SubName: Full=GTP-binding family protein {ECO:0000313|EMBL:EFH42500.1}; GN ORFNames=ARALYDRAFT_918982 {ECO:0000313|EMBL:EFH42500.1}; OS Arabidopsis lyrata subsp. lyrata (Lyre-leaved rock-cress). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae; OC Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae; OC Arabidopsis. OX NCBI_TaxID=81972 {ECO:0000313|Proteomes:UP000008694}; RN [1] {ECO:0000313|Proteomes:UP000008694} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. MN47 {ECO:0000313|Proteomes:UP000008694}; RX PubMed=21478890; DOI=10.1038/ng.807; RA Hu T.T., Pattyn P., Bakker E.G., Cao J., Cheng J.-F., Clark R.M., RA Fahlgren N., Fawcett J.A., Grimwood J., Gundlach H., Haberer G., RA Hollister J.D., Ossowski S., Ottilar R.P., Salamov A.A., RA Schneeberger K., Spannagl M., Wang X., Yang L., Nasrallah M.E., RA Bergelson J., Carrington J.C., Gaut B.S., Schmutz J., Mayer K.F.X., RA Van de Peer Y., Grigoriev I.V., Nordborg M., Weigel D., Guo Y.-L.; RT "The Arabidopsis lyrata genome sequence and the basis of rapid genome RT size change."; RL Nat. Genet. 43:476-481(2011). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GL348720; EFH42500.1; -; Genomic_DNA. DR RefSeq; XP_002866241.1; XM_002866195.1. DR ProteinModelPortal; D7MNY2; -. DR STRING; 59689.scaffold_802382.1; -. DR EnsemblPlants; scaffold_802382.1; scaffold_802382.1; scaffold_802382.1. DR GeneID; 9300618; -. DR Gramene; scaffold_802382.1; scaffold_802382.1; scaffold_802382.1. DR KEGG; aly:ARALYDRAFT_918982; -. DR KO; K03665; -. DR OrthoDB; EOG093609UJ; -. DR Proteomes; UP000008694; Unassembled WGS sequence. DR GO; GO:0009507; C:chloroplast; IEA:EnsemblPlants. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000008694}; KW Reference proteome {ECO:0000313|Proteomes:UP000008694}. FT DOMAIN 311 477 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 541 AA; 60588 MW; DC0852C5C7C7BF87 CRC64; MSSFYLSSSP IFKLQWHANA KPKPSRPIVS LPLSRLHANC YSWRLSCNLT QHGLQLEETV EEDEIPQVLE LPTEEEPNFD KETTASPSKM LRKKKGDEES LDDRFKLRNG KEIFEEKAYL VGVERKGDGE CLFNIEESLE ELEQLADTAG LAVVGSTYQK LASPNPRTYI GSGKVAEIKS AINALDVETV IFDDELSPGQ LRNLEKAFGG DVRVCDRTAL ILDIFNQRAA THEAALQVAL AQMEYQLPRL TRMWTHLERQ SGGQVKGMGE KQIEVDKRIL RTQIGVLKKE LESVRKHRKQ YRSRRVAIPV PVVSLVGYTN AGKSTLLNQL TGANVLAENR LFATLDPTTR RVQMQNGKEF LLTDTVGFIQ KLPTTLVAAF RATLEEIAES SLLVHVVDIS HPLAEQQIEA VEKVMSELDV SSIPKLVVWN KVDRVDDPQK VKLEAEKSGD TICISALTGE GLDDFCNAVH EKLKDSMVWV EALLPFDKGD LLSTIHKVGM VKETEYTENG TLIRAHVPLR FAQLLKPMRH LVKDTSISQK G // ID D7N0G7_9NEIS Unreviewed; 393 AA. AC D7N0G7; DT 10-AUG-2010, integrated into UniProtKB/TrEMBL. DT 10-AUG-2010, sequence version 1. DT 07-JUN-2017, entry version 39. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:EFI24644.1}; GN ORFNames=HMPREF9016_00824 {ECO:0000313|EMBL:EFI24644.1}; OS Neisseria sp. oral taxon 014 str. F0314. OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=641149 {ECO:0000313|EMBL:EFI24644.1, ECO:0000313|Proteomes:UP000002768}; RN [1] {ECO:0000313|EMBL:EFI24644.1, ECO:0000313|Proteomes:UP000002768} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=F0314 {ECO:0000313|EMBL:EFI24644.1, RC ECO:0000313|Proteomes:UP000002768}; RG The Broad Institute Genome Sequencing Platform; RA Ward D., Feldgarden M., Earl A., Young S.K., Zeng Q., Koehrsen M., RA Alvarado L., Berlin A., Bochicchio J., Borenstein D., Chapman S.B., RA Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A., RA Gujja S., Heilman E., Heiman D., Hepburn T., Howarth C., Jen D., RA Larson L., Mehta T., Park D., Pearson M., Roberts A., Saif S., RA Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., Thomson T., Walk T., RA White J., Yandava C., Izard J., Baranova O.V., Blanton J.M., RA Tanner A.C., Dewhirst F.E., Haas B., Nusbaum C., Birren B.; RT "The Genome Sequence of Neisseria sp. oral taxon 014 strain F0314."; RL Submitted (FEB-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GL349411; EFI24644.1; -; Genomic_DNA. DR RefSeq; WP_009173859.1; NZ_GL349411.1. DR ProteinModelPortal; D7N0G7; -. DR STRING; 641149.HMPREF9016_00824; -. DR EnsemblBacteria; EFI24644; EFI24644; HMPREF9016_00824. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000002768; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000002768}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}. FT DOMAIN 225 393 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 393 AA; 43061 MW; 57F6904EC848C973 CRC64; MSRNKMFQVD KSLEKPERVM LVGVMLDTDY AAGGAGGQVF YSAESRKAHF QTALDEAADL VRAAGGELVA VETSKRDRPH SALFVGTGKA EELAASVRLH DVGLVVFNHE LTPTQERNLE KELQCRVLDR VGLILAIFAK RAQSQEGKLQ VELAQLSHLS GRLVRGYGHL QSQKGGIGLK GPGETQLETD RRLINQKITA LKRQLKNVRQ QRATRRQSRM GGRLKTFAIV GYTNAGKSSL FNRLTKAGVL AENQLFATLD TTARRLFLSH EVSVILTDTV GFVRDLPHKL VSAFSATLEE TALADVLLHV VDVSNPEFGR QMEDVNAVLE EIGAHEIPQL AVYNKIDLQP SEERKTGIVR DAAGKAAAVN ISVAENLGLD DLRQAMIERA LEG // ID D7N7C7_9FIRM Unreviewed; 433 AA. AC D7N7C7; DT 10-AUG-2010, integrated into UniProtKB/TrEMBL. DT 10-AUG-2010, sequence version 1. DT 07-JUN-2017, entry version 38. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:EFI42078.1}; GN ORFNames=HMPREF0629_00712 {ECO:0000313|EMBL:EFI42078.1}; OS Peptoniphilus sp. oral taxon 386 str. F0131. OC Bacteria; Firmicutes; Tissierellia; Tissierellales; Peptoniphilaceae; OC Peptoniphilus. OX NCBI_TaxID=575609 {ECO:0000313|EMBL:EFI42078.1, ECO:0000313|Proteomes:UP000004712}; RN [1] {ECO:0000313|EMBL:EFI42078.1, ECO:0000313|Proteomes:UP000004712} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=F0131 {ECO:0000313|EMBL:EFI42078.1, RC ECO:0000313|Proteomes:UP000004712}; RG The Broad Institute Genome Sequencing Platform; RA Ward D., Feldgarden M., Earl A., Young S.K., Zeng Q., Koehrsen M., RA Alvarado L., Berlin A., Bochicchio J., Borenstein D., Chapman S.B., RA Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A., RA Gujja S., Heilman E., Heiman D., Hepburn T., Howarth C., Jen D., RA Larson L., Mehta T., Park D., Pearson M., Roberts A., Saif S., RA Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., Thomson T., Walk T., RA White J., Yandava C., Izard J., Baranova O.V., Blanton J.M., RA Tanner A.C., Dewhirst F.E., Haas B., Nusbaum C., Birren B.; RT "The Genome Sequence of Peptoniphilus sp. oral taxon 386 strain RT F0131."; RL Submitted (FEB-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GL349422; EFI42078.1; -; Genomic_DNA. DR RefSeq; WP_009222017.1; NZ_GL349422.1. DR ProteinModelPortal; D7N7C7; -. DR STRING; 575609.HMPREF0629_00712; -. DR EnsemblBacteria; EFI42078; EFI42078; HMPREF0629_00712. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000004712; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000004712}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000004712}. FT DOMAIN 209 377 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 175 202 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 433 AA; 49347 MW; C6EA5C3918C50302 CRC64; MENIKDKEKE RVIIVGTDIG AYPNSLETSI RELEELVKAD GAEVVGVVTQ NIDKFSPKYL VGSGKVNEIN DMIPKLEANA VVFNDELSGV QLRNLEDAFN KGCDFFNKKV KVLDRTNLIL DIFALRASTY EGKLQVQLAQ LNYQLPRLIG IQGWSRTGGG IGTRGPGEQI IETDRRRLLR EIETIKAKLK KSEKTRDTMR SKRLENRIST VSLVGYTNAG KSTILNRLKV SDSKDVYVED MLFATLDPNS RRAKLPNGIE FILSDTVGFV SKLPTKLIEA FKSTLEEIKY SDLILHVIDA SSDDLEIQYE TTMNILKDLK IDGDKVITVF NKMDKLEGSD ILINPKYTDK RLYISAKFDD DMDKLLKFIE ENLPEKFKHV KMLIDYKNSV VLSEILDNHK CEELEYLNEG VSFKVILTIE EYNKYKKFVV DYV // ID D7NBR4_9BACT Unreviewed; 415 AA. AC D7NBR4; DT 10-AUG-2010, integrated into UniProtKB/TrEMBL. DT 10-AUG-2010, sequence version 1. DT 07-JUN-2017, entry version 44. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=HMPREF0665_00971 {ECO:0000313|EMBL:EFI49224.1}; OS Prevotella oris C735. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Prevotellaceae; OC Prevotella. OX NCBI_TaxID=563008 {ECO:0000313|EMBL:EFI49224.1, ECO:0000313|Proteomes:UP000003805}; RN [1] {ECO:0000313|EMBL:EFI49224.1, ECO:0000313|Proteomes:UP000003805} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C735 {ECO:0000313|EMBL:EFI49224.1, RC ECO:0000313|Proteomes:UP000003805}; RG The Broad Institute Genome Sequencing Platform; RA Ward D., Feldgarden M., Earl A., Young S.K., Zeng Q., Koehrsen M., RA Alvarado L., Berlin A., Bochicchio J., Borenstein D., Chapman S.B., RA Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A., RA Gujja S., Heilman E., Heiman D., Hepburn T., Howarth C., Jen D., RA Larson L., Mehta T., Park D., Pearson M., Roberts A., Saif S., RA Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., Thomson T., Walk T., RA White J., Yandava C., Sibley C.D., Field T.R., Grinwis M., RA Eshaghurshan C.S., Surette M.G., Haas B., Nusbaum C., Birren B.; RT "The Genome Sequence of Prevotella oris strain C735."; RL Submitted (FEB-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GL349565; EFI49224.1; -; Genomic_DNA. DR RefSeq; WP_004377251.1; NZ_GL349565.1. DR ProteinModelPortal; D7NBR4; -. DR STRING; 563008.HMPREF0665_00971; -. DR EnsemblBacteria; EFI49224; EFI49224; HMPREF0665_00971. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000003805; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000003805}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000003805}. FT DOMAIN 216 400 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 415 AA; 47399 MW; B5514C89F42EC375 CRC64; MKEFVISEVK AETAILVGLI TNNQSEAKTK EYLDELEFLA DTAGAVTVKR FTQKANGPSA VTYVGKGKLE EIKNYIETCE ENEEPIGMVI FDDELSAKQI RNIENELKVK ILDRTSLILD IFAMRAQTAN AKTQVELAQY RYMLPRLQRL WTHLERQGGG SGSGGGKGSV GLRGPGETQL EMDRRIILQR ITLLKQRLVE IDKQKVTQRK NRGRMIRVAL VGYTNVGKST IMNLLAKSEV FAENKLFATL DTTVRKVVVD NLPFLLADTV GFIRKLPTDL VDSFKSTLDE VREADVLLHV VDISHPDFEE QIQVVEKTLA DLGCSDKPSM IIFNKIDNYH WVEKDEDDLT PETRENITLE ELKKTWMARL NDNCLFISAK EKMNIDEFRS TLYKKVRELH VQKYPYNDFL YPEVE // ID D7UZY0_LISGR Unreviewed; 416 AA. AC D7UZY0; DT 05-OCT-2010, integrated into UniProtKB/TrEMBL. DT 05-OCT-2010, sequence version 1. DT 07-JUN-2017, entry version 41. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:EFI82975.1}; GN ORFNames=HMPREF0556_11660 {ECO:0000313|EMBL:EFI82975.1}; OS Listeria grayi DSM 20601. OC Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria. OX NCBI_TaxID=525367 {ECO:0000313|EMBL:EFI82975.1, ECO:0000313|Proteomes:UP000010119}; RN [1] {ECO:0000313|EMBL:EFI82975.1, ECO:0000313|Proteomes:UP000010119} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 20601 {ECO:0000313|EMBL:EFI82975.1, RC ECO:0000313|Proteomes:UP000010119}; RA Muzny D., Qin X., Buhay C., Dugan-Rocha S., Ding Y., Chen G., RA Hawes A., Holder M., Jhangiani S., Johnson A., Khan Z., Li Z., Liu W., RA Liu X., Perez L., Shen H., Wang Q., Watt J., Xi L., Xin Y., Zhou J., RA Deng J., Jiang H., Liu Y., Qu J., Song X.-Z., Zhang L., Villasana D., RA Johnson A., Liu J., Liyanage D., Lorensuhewa L., Robinson T., Song A., RA Song B.-B., Dinh H., Thornton R., Coyle M., Francisco L., Jackson L., RA Javaid M., Korchina V., Kovar C., Mata R., Mathew T., Ngo R., RA Nguyen L., Nguyen N., Okwuonu G., Ongeri F., Pham C., Simmons D., RA Wilczek-Boney K., Hale W., Jakkamsetti A., Pham P., Ruth R., RA San Lucas F., Warren J., Zhang J., Zhao Z., Zhou C., Zhu D., Lee S., RA Bess C., Blankenburg K., Forbes L., Fu Q., Gubbala S., Hirani K., RA Jayaseelan J.C., Lara F., Munidasa M., Palculict T., Patil S., RA Pu L.-L., Saada N., Tang L., Weissenberger G., Zhu Y., Hemphill L., RA Shang Y., Youmans B., Ayvaz T., Ross M., Santibanez J., Aqrawi P., RA Gross S., Joshi V., Fowler G., Nazareth L., Reid J., Worley K., RA Petrosino J., Highlander S., Gibbs R.; RL Submitted (JUN-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EFI82975.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACCR02000005; EFI82975.1; -; Genomic_DNA. DR RefSeq; WP_003754566.1; NZ_GL538352.1. DR ProteinModelPortal; D7UZY0; -. DR STRING; 525367.HMPREF0556_11660; -. DR EnsemblBacteria; EFI82975; EFI82975; HMPREF0556_11660. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000010119; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000010119}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000010119}. FT DOMAIN 194 363 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 416 AA; 47571 MW; EE0382D9E9BFF7C6 CRC64; MQRKVILVGV SHKQAFFDYS MEELENLALA NQYEVCSVMV QNMERENRAT YVGKGKVEEI KLEAEIEGAK LVIFNDELSP SQIRNLEEGL ELQIMDRTGL ILAIFAERAK TREAQIQVEI ARLQYELPRI FGQGEDLDQQ GGGSGVTNRG SGETKLELNR RTIRYQIKNL RKELQDIVAN REVMRRKRKK NNLPVVSLVG YTNAGKSTTM NGLVKLFQGK ENKQVFEKDM LFATLETSIR DIHLTDNKQF LLTDTVGFVS KLPHHLVQAF RSTLEEARDA DLLIHVVDYS DPHYKLMMET TEKTLAELDV KDIPIIYAFN KADKREDTDY PIERGDTIIF SAREEAGLQL LVNRIKKELF ADYEKATFLI PFEESKWVAY LNEVGDVAAT EYLEDGTKIT AEVAPKVIEQ LKAYHV // ID D7VLG8_9SPHI Unreviewed; 396 AA. AC D7VLG8; DT 05-OCT-2010, integrated into UniProtKB/TrEMBL. DT 05-OCT-2010, sequence version 1. DT 07-JUN-2017, entry version 38. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:EFK58441.1}; GN ORFNames=HMPREF0766_11838 {ECO:0000313|EMBL:EFK58441.1}; OS Sphingobacterium spiritivorum ATCC 33861. OC Bacteria; Bacteroidetes; Sphingobacteriia; Sphingobacteriales; OC Sphingobacteriaceae; Sphingobacterium. OX NCBI_TaxID=525373 {ECO:0000313|EMBL:EFK58441.1, ECO:0000313|Proteomes:UP000006258}; RN [1] {ECO:0000313|EMBL:EFK58441.1, ECO:0000313|Proteomes:UP000006258} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33861 {ECO:0000313|EMBL:EFK58441.1, RC ECO:0000313|Proteomes:UP000006258}; RA Muzny D., Qin X., Buhay C., Dugan-Rocha S., Ding Y., Chen G., RA Hawes A., Holder M., Jhangiani S., Johnson A., Khan Z., Li Z., Liu W., RA Liu X., Perez L., Shen H., Wang Q., Watt J., Xi L., Xin Y., Zhou J., RA Deng J., Jiang H., Liu Y., Qu J., Song X.-Z., Zhang L., Villasana D., RA Johnson A., Liu J., Liyanage D., Lorensuhewa L., Robinson T., Song A., RA Song B.-B., Dinh H., Thornton R., Coyle M., Francisco L., Jackson L., RA Javaid M., Korchina V., Kovar C., Mata R., Mathew T., Ngo R., RA Nguyen L., Nguyen N., Okwuonu G., Ongeri F., Pham C., Simmons D., RA Wilczek-Boney K., Hale W., Jakkamsetti A., Pham P., Ruth R., RA San Lucas F., Warren J., Zhang J., Zhao Z., Zhou C., Zhu D., Lee S., RA Bess C., Blankenburg K., Forbes L., Fu Q., Gubbala S., Hirani K., RA Jayaseelan J.C., Lara F., Munidasa M., Palculict T., Patil S., RA Pu L.-L., Saada N., Tang L., Weissenberger G., Zhu Y., Hemphill L., RA Shang Y., Youmans B., Ayvaz T., Ross M., Santibanez J., Aqrawi P., RA Gross S., Joshi V., Fowler G., Nazareth L., Reid J., Worley K., RA Petrosino J., Highlander S., Gibbs R.; RL Submitted (JUL-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EFK58441.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACHA02000006; EFK58441.1; -; Genomic_DNA. DR RefSeq; WP_003000114.1; NZ_GL379773.1. DR ProteinModelPortal; D7VLG8; -. DR STRING; 525373.HMPREF0766_11838; -. DR EnsemblBacteria; EFK58441; EFK58441; HMPREF0766_11838. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000006258; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000006258}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000006258}. FT DOMAIN 204 385 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 396 AA; 45243 MW; B4892FCDA096FF92 CRC64; MARTKIYDTA LKPETAVLIS VITPDTTEAK AREYLEELQF LVETAGGITN GIFTQKLAYP DKATFIGSGK MEEIKSYIDA EEIDMVVFDD ELSPSQLRNI ENFFKVKILD RSNLILDIFA SHAKTAQAKT QVELAQLQYI LPRLTRMWTH LERQRGGIGM RGPGESQIES DRRMILNKIS LFKERLKSID KQNETQRKNR GEMIRVALVG YTNVGKSTIM NMISKSDVLI ENKLFATLDT TVRKVVIDNL PFLLSDTVGF IRKLPHHLVE CFKSTLDEVR EADVLIHVVD ISHPNFEDHI HAVNETLKDL GALDKPVITI FNKIDAYKPA VEEGDEGEER EVTLEEFRNS WMGKNSDPAI FISATNKTNV EEFKQKLYDI IVKMHNARYP YNNLLY // ID D7WFF4_9CORY Unreviewed; 505 AA. AC D7WFF4; DT 05-OCT-2010, integrated into UniProtKB/TrEMBL. DT 05-OCT-2010, sequence version 1. DT 07-JUN-2017, entry version 39. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:EFK53781.1}; GN ORFNames=HMPREF0291_11438 {ECO:0000313|EMBL:EFK53781.1}; OS Corynebacterium genitalium ATCC 33030. OC Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae; OC Corynebacterium. OX NCBI_TaxID=585529 {ECO:0000313|EMBL:EFK53781.1, ECO:0000313|Proteomes:UP000004208}; RN [1] {ECO:0000313|EMBL:EFK53781.1, ECO:0000313|Proteomes:UP000004208} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33030 {ECO:0000313|EMBL:EFK53781.1, RC ECO:0000313|Proteomes:UP000004208}; RA Muzny D., Qin X., Buhay C., Dugan-Rocha S., Ding Y., Chen G., RA Hawes A., Holder M., Jhangiani S., Johnson A., Khan Z., Li Z., Liu W., RA Liu X., Perez L., Shen H., Wang Q., Watt J., Xi L., Xin Y., Zhou J., RA Deng J., Jiang H., Liu Y., Qu J., Song X.-Z., Zhang L., Villasana D., RA Johnson A., Liu J., Liyanage D., Lorensuhewa L., Robinson T., Song A., RA Song B.-B., Dinh H., Thornton R., Coyle M., Francisco L., Jackson L., RA Javaid M., Korchina V., Kovar C., Mata R., Mathew T., Ngo R., RA Nguyen L., Nguyen N., Okwuonu G., Ongeri F., Pham C., Simmons D., RA Wilczek-Boney K., Hale W., Jakkamsetti A., Pham P., Ruth R., RA San Lucas F., Warren J., Zhang J., Zhao Z., Zhou C., Zhu D., Lee S., RA Bess C., Blankenburg K., Forbes L., Fu Q., Gubbala S., Hirani K., RA Jayaseelan J.C., Lara F., Munidasa M., Palculict T., Patil S., RA Pu L.-L., Saada N., Tang L., Weissenberger G., Zhu Y., Hemphill L., RA Shang Y., Youmans B., Ayvaz T., Ross M., Santibanez J., Aqrawi P., RA Gross S., Joshi V., Fowler G., Nazareth L., Reid J., Worley K., RA Petrosino J., Highlander S., Gibbs R.; RL Submitted (JUN-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EFK53781.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACLJ02000003; EFK53781.1; -; Genomic_DNA. DR RefSeq; WP_005289824.1; NZ_CM000961.1. DR ProteinModelPortal; D7WFF4; -. DR STRING; 585529.HMPREF0291_11438; -. DR EnsemblBacteria; EFK53781; EFK53781; HMPREF0291_11438. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000004208; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000004208}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000004208}. FT DOMAIN 278 458 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 505 AA; 55373 MW; 23C676D0756A1D50 CRC64; MTTSSHASSQ PSHDELLAQA FRHNAPQPTD RGRDEAHEPS VGTLDLAERN AFRRVTRETE IRSEEHKDVY EVEYRKLQLE QVILVGVWTE GTTAEVEASM NELAALAETA GAEVVEMIYQ KRDKPDPGTY VGSGKVSELR DIVHATGADT VVCDGGLSPG QLVALEEALK IKVIDRTMLI LDIFAQHAKS KEGKAQVSLA QMEYLYTRTR GWGGNLSRQA GGRAGSNGGV GLRGPGETRI EADRRRLRTD MAKLRRDLSG MKTARDIKRA QRQRSTLPKI AIAGYTNAGK SSLINAMTDA GVLVEDALFA TLDPSTRRAE LADGRTVVLT DTVGFVRHLP TQLVEAFKST LEEVVGADLM LHVVDGSDPF PLKQIKAVND VLAEITRDTG EEIPPEIIVV NKIDEADPVV LAELRHAFAD SKHNVVFVSA VTGEGIDELE GRIEMFLNTL DAHVKLLVPF TRGDVVSRVH EEGTVRSEEY NEEGTLIDVR LPRVLAEQYA EFVVA // ID D8DVN0_PREBR Unreviewed; 415 AA. AC D8DVN0; DT 05-OCT-2010, integrated into UniProtKB/TrEMBL. DT 05-OCT-2010, sequence version 1. DT 07-JUN-2017, entry version 42. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:EFI72487.1}; GN ORFNames=PBR_1637 {ECO:0000313|EMBL:EFI72487.1}, GN SAMN05444375_11185 {ECO:0000313|EMBL:SEQ62105.1}; OS Prevotella bryantii B14. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Prevotellaceae; OC Prevotella. OX NCBI_TaxID=752555 {ECO:0000313|EMBL:EFI72487.1, ECO:0000313|Proteomes:UP000004524}; RN [1] {ECO:0000313|EMBL:EFI72487.1, ECO:0000313|Proteomes:UP000004524} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=B14 {ECO:0000313|EMBL:EFI72487.1, RC ECO:0000313|Proteomes:UP000004524}; RX PubMed=20585943; DOI=10.1007/s00248-010-9692-8; RG North American Consortium for Rumen Bacteria; RA Purushe J., Fouts D.E., Morrison M., White B.A., Mackie R.I., RA Coutinho P.M., Henrissat B., Nelson K.E.; RT "Comparative genome analysis of Prevotella ruminicola and Prevotella RT bryantii: insights into their environmental niche."; RL Microb. Ecol. 60:721-729(2010). RN [2] {ECO:0000313|EMBL:SEQ62105.1, ECO:0000313|Proteomes:UP000183837} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=B14 {ECO:0000313|EMBL:SEQ62105.1, RC ECO:0000313|Proteomes:UP000183837}; RA de Groot N.N.; RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADWO01000042; EFI72487.1; -; Genomic_DNA. DR EMBL; FOEM01000011; SEQ62105.1; -; Genomic_DNA. DR RefSeq; WP_006282070.1; NZ_FOEM01000011.1. DR ProteinModelPortal; D8DVN0; -. DR STRING; 752555.PBR_1637; -. DR EnsemblBacteria; EFI72487; EFI72487; PBR_1637. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000004524; Unassembled WGS sequence. DR Proteomes; UP000183837; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000004524}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000004524}. FT DOMAIN 216 400 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 415 AA; 47517 MW; C424BC6EEC078ACC CRC64; MKEFVISEAK AETAILVGLI TPNQNEEKTK EYLDELEFLA DTAGAVTVKR FTQRVNGPSQ VTYVGKGKLE EIKQYIKDEE DNEREIGMVI FDDELTAKQI RNIEGELGVK ILDRTSLILD IFAMRAQTAN AKTQVELAQH RYMLPRLQRL WTHLERQGGG SGSGGGKGSV GLRGPGETQL EMDRRIILQR ITLLKKRLEE IDRQQSTQRK NRGRLIRVAL VGYTNVGKST TMNLLSKSEV FAENKLFATL DTTVRKVVVK NLPFLLADTV GFIRKLPTDL VDSFKSTLDE TREADLLVHV VDISHPDFEE QINVVEQTLK DIGCTDKPSM IVFNKIDNYT WVEKEEDDLT PSTKENISLD ELKKTWMARM HDNCIFISAK TKENVDEFRD ILYKKVRELH VQKYPYNDFL YPEVE // ID D8FDR6_9DELT Unreviewed; 423 AA. AC D8FDR6; DT 05-OCT-2010, integrated into UniProtKB/TrEMBL. DT 05-OCT-2010, sequence version 1. DT 07-JUN-2017, entry version 42. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:EFK06045.1}; GN ORFNames=NPH_2611 {ECO:0000313|EMBL:EFK06045.1}; OS delta proteobacterium NaphS2. OC Bacteria; Proteobacteria; Deltaproteobacteria. OX NCBI_TaxID=88274 {ECO:0000313|EMBL:EFK06045.1, ECO:0000313|Proteomes:UP000003834}; RN [1] {ECO:0000313|EMBL:EFK06045.1, ECO:0000313|Proteomes:UP000003834} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NaphS2 {ECO:0000313|EMBL:EFK06045.1, RC ECO:0000313|Proteomes:UP000003834}; RX PubMed=21124915; DOI=10.1371/journal.pone.0014072; RA Didonato R.J., Young N.D., Butler J.E., Chin K.J., Hixson K.K., RA Mouser P., Lipton M.S., Deboy R., Methe B.A.; RT "Genome Sequence of the Deltaproteobacterial Strain NaphS2 and RT Analysis of Differential Gene Expression during Anaerobic Growth on RT Naphthalene."; RL PLoS ONE 5:E14072-E14072(2010). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EFK06045.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADZZ01000698; EFK06045.1; -; Genomic_DNA. DR RefSeq; WP_006425136.1; NZ_ADZZ01000698.1. DR ProteinModelPortal; D8FDR6; -. DR EnsemblBacteria; EFK06045; EFK06045; NPH_2611. DR Proteomes; UP000003834; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000003834}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000003834}. FT DOMAIN 205 370 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 165 192 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 423 AA; 47831 MW; DE2577D8289603D1 CRC64; MTLAAAEKEK AILLGYCPLD GETAAKDDSM AELTRLTDTA GILSLGAFVQ RRAKIHPRTF LGEGFIEDSL EKAGAAADLL IFDHDLTGNQ ARNIEKRFML PVMDRTEVIL KIFHDHARTR EARLQVRLAQ LKYELPRVKS MWGHLDRERF GSKAGGRVAF RGMGEKQSEM DRQKLQREIY EIEKNLKRLV KQIDTQKKLR KQTCRNIGLV GYTNAGKSTL FNRLTRADVL MEDKLFATLD STSRALPLHN NKEAVISDTV GFISNLPHHL VASFRATLKE AEEADLLIHV ADISDENYEK HIADVETVLK SIDADQIPHM LVFNKIDRVS KDTIKGTRNA YPNARFISAA TGQNVDLFLR NLSENLYPTT KVTLLIPISE QKRIHDIHNL SKVLETTYED ESVRMTVVIA KEDLSPLVPY LIS // ID D8G608_9CYAN Unreviewed; 539 AA. AC D8G608; DT 05-OCT-2010, integrated into UniProtKB/TrEMBL. DT 05-OCT-2010, sequence version 1. DT 07-JUN-2017, entry version 41. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=OSCI_3600011 {ECO:0000313|EMBL:CBN58048.1}; OS [Oscillatoria] sp. PCC 6506. OC Bacteria; Cyanobacteria; Oscillatoriophycideae; Oscillatoriales; OC Microcoleaceae; Kamptonema. OX NCBI_TaxID=272129 {ECO:0000313|EMBL:CBN58048.1, ECO:0000313|Proteomes:UP000004532}; RN [1] {ECO:0000313|Proteomes:UP000004532} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=PCC 6506 {ECO:0000313|Proteomes:UP000004532}; RX PubMed=20675499; DOI=10.1128/JB.00704-10; RA Mejean A., Mazmouz R., Mann S., Calteau A., Medigue C., Ploux O.; RT "The genome sequence of the cyanobacterium Oscillatoria sp. PCC 6506 RT reveals several gene clusters responsible for the biosynthesis of RT toxins and secondary metabolites."; RL J. Bacteriol. 192:5264-5265(2010). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CACA01000324; CBN58048.1; -; Genomic_DNA. DR ProteinModelPortal; D8G608; -. DR EnsemblBacteria; CBN58048; CBN58048; OSCI_3600011. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000004532; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000004532}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000004532}. FT DOMAIN 366 539 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 325 362 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 539 AA; 59031 MW; A5BAA63A9F3C85D0 CRC64; MIRVGVGTPR QTQIPPLELP RYGQGRLSGI RCIATHLKPE PPGEAALTAM AIQRLDALVW LTLTGGGFQR RGGGGAGYIK ETYLAHLTPE GERGSRGAGE QGGAGDIAPV LNTQNREGLP ETDQSLKAQN FFWSMSAPLS LEVLAELDFQ EWVEAIEAEF EREFVAKQVD VDQDKVLVVG MMTQDMTPQQ FEDGLLELTS LVGTAGGQVL QTVKQKRSRP HPQTVVGEGK VEEIALSAQT VGANLIVFDR DLSPAQVRNL ETKIGIRVVD RTEVILDIFA QRAQSGAGKL QVELAQLEYN LPRLTGRGQA MSRLGGGIGT RGPGETKLET ERRAIAKRIS RLQQEVNQLQ AHRSRMRQQR QHREVPSIAI VGYTNAGKST LLNVLTNAEV YTADQLFATL DPTTRRLVIA DAVTEESLSI VLTDTVGFIH ELPPALIDAF RATLEEVTDA DALLHVVDLS HPAWHSQIRS VMTILTEMPV TPGPALVAFN KIDRVDGDTL RQAQEEFPQA VFISAAKALG LETLRQRLAQ LIYYVAYPR // ID D8IIY2_LACFC Unreviewed; 425 AA. AC D8IIY2; DT 05-OCT-2010, integrated into UniProtKB/TrEMBL. DT 05-OCT-2010, sequence version 1. DT 07-JUN-2017, entry version 49. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=LC40_1047 {ECO:0000313|EMBL:ADJ41611.1}; OS Lactobacillus fermentum (strain CECT 5716). OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; OC Lactobacillus. OX NCBI_TaxID=712938 {ECO:0000313|EMBL:ADJ41611.1, ECO:0000313|Proteomes:UP000006910}; RN [1] {ECO:0000313|EMBL:ADJ41611.1, ECO:0000313|Proteomes:UP000006910} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CECT 5716 {ECO:0000313|EMBL:ADJ41611.1, RC ECO:0000313|Proteomes:UP000006910}; RX PubMed=20639335; DOI=10.1128/JB.00702-10; RA Jimenez E., Langa S., Martin V., Arroyo R., Martin R., Fernandez L., RA Rodriguez J.M.; RT "Complete genome sequence of Lactobacillus fermentum CECT 5716, a RT probiotic strain isolated from human milk."; RL J. Bacteriol. 192:4800-4800(2010). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002033; ADJ41611.1; -; Genomic_DNA. DR RefSeq; WP_014562670.1; NC_017465.1. DR ProteinModelPortal; D8IIY2; -. DR STRING; 712938.LC40_1047; -. DR EnsemblBacteria; ADJ41611; ADJ41611; LC40_1047. DR KEGG; lfr:LC40_1047; -. DR PATRIC; fig|712938.3.peg.2076; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; FNNHAHV; -. DR Proteomes; UP000006910; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000006910}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000006910}. FT DOMAIN 201 370 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 167 197 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 425 AA; 47782 MW; 31E846BA0F1C78A1 CRC64; MDTTVPSEKV IIIGLNTGQA NYEYSMLELA ELAQANHMEV IDRLDQSLDR PNAATYFGKG KVEELTQFAT AEQVTTIIAN DELTPSQLAN LTEATKIRVI DRTALILEIF AQRAQSREAK IQVQIAQLQY RLPRLHTAAN QSLDQQTGGG AGFANRGSGE TQIEMDRRVI QKQIAHLRNE LKEIAKSEET KRAKRDRDTI PTAALVGYTN AGKSTIMNQL VERFGVSSEK KVFEKDMLFA TLDTSVRQLT LPDQKRFLLS DTVGFVSKLP THLIEAFKST LAEAASADLL IQVIDYSDPH HEEMMATTDE TLRQIGIENI PMVYVFNKAD KTEVSFPTME GEDRVIVSAK QDSSIDLIVK VIRQHLFKDY QEATLLVPFA DGHVVSYLNE HTNILDTDYL PDGTKLRLEI APEDLHRFQK YLLTE // ID D8IZU5_HERSS Unreviewed; 374 AA. AC D8IZU5; DT 05-OCT-2010, integrated into UniProtKB/TrEMBL. DT 05-OCT-2010, sequence version 1. DT 07-JUN-2017, entry version 45. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:ADJ64435.1}; GN OrderedLocusNames=Hsero_2947 {ECO:0000313|EMBL:ADJ64435.1}; OS Herbaspirillum seropedicae (strain SmR1). OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Oxalobacteraceae; Herbaspirillum. OX NCBI_TaxID=757424 {ECO:0000313|EMBL:ADJ64435.1, ECO:0000313|Proteomes:UP000000329}; RN [1] {ECO:0000313|EMBL:ADJ64435.1, ECO:0000313|Proteomes:UP000000329} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SmR1 {ECO:0000313|EMBL:ADJ64435.1, RC ECO:0000313|Proteomes:UP000000329}; RA Pedrosa F.O., Monteiro R.A., Wassem R., Cruz L.M., Ayub R.A., RA Colauto N.B., Fernandez M.A., Fungaro M.H.P., Grisard E.C., RA Hungria M., Madeira H.M.F., Nodari R.O., Osaku C.A., Petzl-Erler M.L., RA Terenzi H., Vieira L.G.E., Almeida M.I.M., Alves L.R., Arantes O.M.N., RA Balsanelli E., Barcellos F.G., Baura V.A., Binde D.R., Campo R.J., RA Chubatsu L.S., Chueire L.M.O., Ciferri R.R., Correa L.C., RA da Conceicao Silva J.L., Dabul A.N.G., Dambros B.P., Faoro H., RA Favetti A., Friedermann G., Furlaneto M.C., Gasques L.S., RA Gimenes C.C.T., Gioppo N.M.R., Glienke-Blanco C., Godoy L.P., RA Guerra M.P., Karp S., Kava-Cordeiro V., Margarido V.P., Mathioni S.M., RA Menck-Soares M.A., Murace N.K., Nicolas M.F., Oliveira C.E.C., RA Pagnan N.A.B., Pamphile J.A., Patussi E.V., Pereira L.F.P., RA Pereira-Ferrari L., Pinto F.G.S., Precoma C., Prioli A.J., RA Prioli S.M.A.P., Raittz R.T., Ramos H.J.O., Ribeiro E.M.S.F., RA Rigo L.U., Rocha C.L.M.S.C., Rocha S.N., Santos K., Satori D., RA Silva A.G., Simao R.C.G., Soares M.A.M., Souza E.M., Steffens M.B.R., RA Steindel M., Tadra-Sfeir M.Z., Takahashi E.K., Torres R.A., RA Valle J.S., Vernal J.I., Vilas-Boas L.A., Watanabe M.A.E., Weiss V.A., RA Yates M.A., Souza E.M.; RT "The genome of Herbaspirillum seropedicae SmR1, an endophytic, RT nitrogen-fixing, plant-growth promoting beta-Proteobacteria."; RL Submitted (APR-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002039; ADJ64435.1; -; Genomic_DNA. DR RefSeq; WP_013234908.1; NC_014323.1. DR ProteinModelPortal; D8IZU5; -. DR STRING; 757424.Hsero_2947; -. DR EnsemblBacteria; ADJ64435; ADJ64435; Hsero_2947. DR GeneID; 29393182; -. DR KEGG; hse:Hsero_2947; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000000329; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000000329}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Hydrolase {ECO:0000313|EMBL:ADJ64435.1}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000000329}. FT DOMAIN 190 356 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 156 183 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 374 AA; 40973 MW; 478106CF4C9B8F4E CRC64; MRAALVGLDF GKNDFAASLD ELYLLAKSAG AEPVITITGR RASPDAALFI GTGKAQEVAD AVADLQLELV IFNHALSPAQ QRNLERLLKV RVLDRTSLIL DIFAQRAKSH EGKVQVELAQ LQHLSTRLIR GWTHLERQKG GIGLRGPGET QLETDRRLLG ERVKALRAVL AKLRRQHATQ RRARGRNETF SVSLVGYTNA GKSTIFNALA KAGVYAANQL FATLDTTSRR VYLGEVGHVV ISDTVGFIRE LPHQLVEAFR ATLEETIHAD LLLHVVDAAS PVRMEQIEEV NLVLKEIGAD HVPQILVWNK IDAAGLEPTV EYDEYGKIQR VFVSAKSGAG LDLLREAIAA SLKAALEARG RSRSEPVDSV DMHA // ID D8J3E2_HALJB Unreviewed; 430 AA. AC D8J3E2; DT 05-OCT-2010, integrated into UniProtKB/TrEMBL. DT 05-OCT-2010, sequence version 1. DT 07-JUN-2017, entry version 53. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=HacjB3_09330 {ECO:0000313|EMBL:ADJ15249.1}; GN ORFNames=C497_13346 {ECO:0000313|EMBL:ELY35330.1}; OS Halalkalicoccus jeotgali (strain DSM 18796 / CECT 7217 / JCM 14584 / OS KCTC 4019 / B3). OC Archaea; Euryarchaeota; Halobacteria; Halobacteriales; OC Halobacteriaceae; Halalkalicoccus. OX NCBI_TaxID=795797 {ECO:0000313|EMBL:ADJ15249.1, ECO:0000313|Proteomes:UP000000390}; RN [1] {ECO:0000313|EMBL:ADJ15249.1, ECO:0000313|Proteomes:UP000000390} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=B3 {ECO:0000313|EMBL:ADJ15249.1}, and RC DSM 18796 / CECT 7217 / JCM 14584 / KCTC 4019 / B3 RC {ECO:0000313|Proteomes:UP000000390}; RX PubMed=20601480; DOI=10.1128/JB.00663-10; RA Roh S.W., Nam Y.D., Nam S.H., Choi S.H., Park H.S., Bae J.W.; RT "Complete genome sequence of Halalkalicoccus jeotgali B3(T), an RT extremely halophilic archaeon."; RL J. Bacteriol. 192:4528-4529(2010). RN [2] {ECO:0000313|Proteomes:UP000011645} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=B3 {ECO:0000313|Proteomes:UP000011645}; RA Becker E.A., Seitzer P., Tritt A., Larsen D., Yao A., Wu D., RA Darling A., Eisen J.A., Facciotti M.T.; RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases. RN [3] {ECO:0000313|EMBL:ELY35330.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=B3 {ECO:0000313|EMBL:ELY35330.1}; RX PubMed=25393412; RA Becker E.A., Seitzer P.M., Tritt A., Larsen D., Krusor M., Yao A.I., RA Wu D., Madern D., Eisen J.A., Darling A.E., Facciotti M.T.; RT "Phylogenetically driven sequencing of extremely halophilic archaea RT reveals strategies for static and dynamic osmo-response."; RL PLoS Genet. 10:E1004784-E1004784(2014). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002062; ADJ15249.1; -; Genomic_DNA. DR EMBL; AOHV01000034; ELY35330.1; -; Genomic_DNA. DR RefSeq; WP_008417282.1; NZ_AXZD01000008.1. DR STRING; 795797.HacjB3_09330; -. DR EnsemblBacteria; ADJ15249; ADJ15249; HacjB3_09330. DR EnsemblBacteria; ELY35330; ELY35330; C497_13346. DR GeneID; 9419675; -. DR KEGG; hje:HacjB3_09330; -. DR PATRIC; fig|795797.18.peg.1861; -. DR eggNOG; arCOG00353; Archaea. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG093Z07D6; -. DR Proteomes; UP000000390; Chromosome. DR Proteomes; UP000011645; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000000390}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000000390}. FT DOMAIN 186 368 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 430 AA; 48216 MW; 030394F02CEF5ABA CRC64; MNTVIVKRVD EGTADTNEIR DLARAAGYTV LDELTQTRTE DAAYHIGEGK VAELSSLVAR TGVETVIFDN RLGPYQIYNI GREIPEDVEV IDRFTLILDI FGQRAQTRKA QLQVELAELR YELPRVDAKV SLAKREEHPG FMGLGEYDES RERDIKSQIS RIKEELASIA ETEEHRREER RESGFDLVAL AGYTNAGKST LLRRLAADLA VDENEDLHPD LDTTAESEDR LFTTLGTTTR RADMERDVLL TDTVGFISDL PHWLVESFRS TLDEVYRADL VLLVVDVSEP IEEIREKVVT CHDTLYERNE APIVTVLNKI DAVDEAELEE KRAALSALAP DPVAVSGKEG LNVEALTDRI AADLPPLREE RLVLPMAEDT MSLVSWLYDN ACVEEVTYDA DQVLVEFAAR PSVIERSRSK ASELTIPESA // ID D8K074_DEHLB Unreviewed; 367 AA. AC D8K074; DT 05-OCT-2010, integrated into UniProtKB/TrEMBL. DT 05-OCT-2010, sequence version 1. DT 07-JUN-2017, entry version 50. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Dehly_0695 {ECO:0000313|EMBL:ADJ26002.1}; OS Dehalogenimonas lykanthroporepellens (strain ATCC BAA-1523 / JCM 15061 OS / BL-DC-9). OC Bacteria; Chloroflexi; Dehalococcoidia; Dehalogenimonas. OX NCBI_TaxID=552811 {ECO:0000313|EMBL:ADJ26002.1, ECO:0000313|Proteomes:UP000002349}; RN [1] {ECO:0000313|Proteomes:UP000002349} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-1523 / JCM 15061 / BL-DC-9 RC {ECO:0000313|Proteomes:UP000002349}; RG US DOE Joint Genome Institute; RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L., RA Pitluck S., Daligault H., Detter J.C., Han C., Tapia R., Land M., RA Hauser L., Kyrpides N., Ovchinnikova G., Rainey F.A., Yan J., RA da Costa M.S., Moe W.M., Woyke T.; RT "Complete sequence of Dehalogenimonas lykanthroporepellens BL-DC-9."; RL Submitted (JUN-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002084; ADJ26002.1; -; Genomic_DNA. DR RefSeq; WP_013218148.1; NC_014314.1. DR ProteinModelPortal; D8K074; -. DR STRING; 552811.Dehly_0695; -. DR EnsemblBacteria; ADJ26002; ADJ26002; Dehly_0695. DR KEGG; dly:Dehly_0695; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000002349; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000002349}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000002349}. FT DOMAIN 194 367 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 367 AA; 41290 MW; 2B71F26ED6CBD488 CRC64; MVAVDYVDKS ASSSNWSTED SLSELARLVN TIGIRVTGHL IQKLSSPKRQ TYVGQGKLDE LIGTQETQPI DQLIFDDELT PLQYKTLVAM FPKIEILDRV SVILEIFSRH ARTKEGRLQI ELARAQYLLP RLTGQWKHLE RLGGGIGTRG PGESQLETDR RLIQKRITTI KKDLEKVSKH RALYRKKRQM SYIPIVALVG YTNSGKSSLL KTLTKSDVLV QNQLFATLDP TTRRLCLPNL TKILVTDTVG FIHKLPPTII EAFKSTLEEL QDASILLHVV DISSLHATEQ SITVENILAE LGIADKPVIT VYNKIDLIDY NQFLSSVDRP GTQDFLKSCP ENTVMVSAEK RLGLDRLLHN IESLLLK // ID D8MMA0_ERWBE Unreviewed; 426 AA. AC D8MMA0; DT 05-OCT-2010, integrated into UniProtKB/TrEMBL. DT 05-OCT-2010, sequence version 1. DT 30-AUG-2017, entry version 53. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:CAX57984.1}; GN OrderedLocusNames=EbC_04530 {ECO:0000313|EMBL:CAX57984.1}; OS Erwinia billingiae (strain Eb661). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; OC Erwiniaceae; Erwinia. OX NCBI_TaxID=634500 {ECO:0000313|Proteomes:UP000008793}; RN [1] {ECO:0000313|EMBL:CAX57984.1, ECO:0000313|Proteomes:UP000008793} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Eb661 {ECO:0000313|EMBL:CAX57984.1, RC ECO:0000313|Proteomes:UP000008793}; RX PubMed=20565991; DOI=10.1186/1471-2164-11-393; RA Kube M., Migdoll A.M., Gehring I., Heitmann K., Mayer Y., Kuhl H., RA Knaust F., Geider K., Reinhardt R.; RT "Genome comparison of the epiphytic bacteria Erwinia billingiae and E. RT tasmaniensis with the pear pathogen E. pyrifoliae."; RL BMC Genomics 11:393-393(2010). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; FP236843; CAX57984.1; -; Genomic_DNA. DR RefSeq; WP_013200490.1; NC_014306.1. DR ProteinModelPortal; D8MMA0; -. DR STRING; 634500.EbC_04530; -. DR EnsemblBacteria; CAX57984; CAX57984; EbC_04530. DR KEGG; ebi:EbC_04530; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000008793; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000008793}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Hydrolase {ECO:0000313|EMBL:CAX57984.1}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000008793}. FT DOMAIN 198 365 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 426 AA; 47895 MW; D12A1F904563A069 CRC64; MFDRYEAGEQ AVLVHIYFSQ ERNTEDLQEF ETLVSSAGVE ALSVVTGSRK SPHPKYFVGE GKAVEIAEAV KASGATVVLF DHALSPAQER NLEALCECRV IDRTGLILDI FAQRARTHEG KLQVELAQLR HLATRLVRGW THLERQKGGI GLRGPGETQL ETDRRLLRNR ITLILSRLER VAKQREQGRQ ARNKADVPTL SLVGYTNAGK STLFNRVTAA EVYVADQLFA TLDPTLRRID VADVGEVVLA DTVGFIRHLP HDLVAAFKAT LQETREATLL VHVIDAADLR VDENIKAVEV VLEEIESDEI PTLQVMNKID MLDGFVPRID RDEENKPVRV WVSAQTGEGI PLLFQALTER LAGEIAQYDL RLPPEAGRLR SRFYQLQAIE KEWNEDDGSV GLQVRMPIVD WRRLCKQEPA LVDYIV // ID D8PFY2_9BACT Unreviewed; 538 AA. AC D8PFY2; DT 05-OCT-2010, integrated into UniProtKB/TrEMBL. DT 05-OCT-2010, sequence version 1. DT 30-AUG-2017, entry version 43. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=NIDE2459 {ECO:0000313|EMBL:CBK42169.1}; OS Nitrospira defluvii. OC Bacteria; Nitrospirae; Nitrospirales; Nitrospiraceae; Nitrospira. OX NCBI_TaxID=330214 {ECO:0000313|EMBL:CBK42169.1, ECO:0000313|Proteomes:UP000001660}; RN [1] {ECO:0000313|EMBL:CBK42169.1, ECO:0000313|Proteomes:UP000001660} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX DOI=10.1073/pnas.1003860107 ; RA Lucker S., Wagner M., Maixner F., Pelletier E., Koch H., Vacherie B., RA Rattei T., Sinninghe Damste J., Spieck E., Le Paslier D., Daims H.; RT "A Nitrospira metagenome illuminates the physiology and evolution of RT globally important nitrite-oxidizing bacteria."; RL Proc. Natl. Acad. Sci. U.S.A. 0:0-0(2010). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; FP929003; CBK42169.1; -; Genomic_DNA. DR ProteinModelPortal; D8PFY2; -. DR STRING; 330214.NIDE2459; -. DR EnsemblBacteria; CBK42169; CBK42169; NIDE2459. DR KEGG; nde:NIDE2459; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000001660; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000001660}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000001660}. FT DOMAIN 352 516 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 311 338 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 538 AA; 59645 MW; 14F0AE32DE113091 CRC64; MPSSLVITAE LARTTCQLTR EIRRPIGLLI TRRGVVEQVL VGAGCAPTFE SLVKFRVGSH ALRGLRLIRT HLHDDPLSQD DLTHLALLRL DLIGVLGVDE TGEPSLLHLA HLLPPNQQGE VCRLLKPVPF HDLDLQLDVF LHGLDSDLQR ADSTHDVAGG SESAILVSAA PRSHAEQEEH LEELKELAES AGVRVLDRIA QRTHEGFERY LLGKGKLKEV VMRALQKGAD LVIFDQDLAP AQARAISEVT DLKVIDRTQL ILDIFARRAH TREGKVQVEL AQLRYLLPRL SGHGTSLSRL GGGIGSRGPG ETKLETDRRR IRDRIAHLER EIDDVARHQD QRRSRRVRQG LPILSIVGYT NAGKSTLLNS LTHSQIPAQD RLFETLDTTS RRLRFPHDRE VIVTDTVGFI RDLPKDLVGA FRTTLDELRD ADLLLHVVDA SAPNVDQQIT AVETVLQSLN LDTIPRVMVL NKCDRLSAHE AGVLCERYHA IGISAPNRET LRPLIAHLET LLPAVPTLPG QEEDPDQPPQ DLALASHS // ID D8PGD2_9BACT Unreviewed; 463 AA. AC D8PGD2; DT 05-OCT-2010, integrated into UniProtKB/TrEMBL. DT 05-OCT-2010, sequence version 1. DT 30-AUG-2017, entry version 44. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=NIDE2613 {ECO:0000313|EMBL:CBK42319.1}; OS Nitrospira defluvii. OC Bacteria; Nitrospirae; Nitrospirales; Nitrospiraceae; Nitrospira. OX NCBI_TaxID=330214 {ECO:0000313|EMBL:CBK42319.1, ECO:0000313|Proteomes:UP000001660}; RN [1] {ECO:0000313|EMBL:CBK42319.1, ECO:0000313|Proteomes:UP000001660} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX DOI=10.1073/pnas.1003860107 ; RA Lucker S., Wagner M., Maixner F., Pelletier E., Koch H., Vacherie B., RA Rattei T., Sinninghe Damste J., Spieck E., Le Paslier D., Daims H.; RT "A Nitrospira metagenome illuminates the physiology and evolution of RT globally important nitrite-oxidizing bacteria."; RL Proc. Natl. Acad. Sci. U.S.A. 0:0-0(2010). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; FP929003; CBK42319.1; -; Genomic_DNA. DR RefSeq; WP_013249140.1; NC_014355.1. DR ProteinModelPortal; D8PGD2; -. DR STRING; 330214.NIDE2613; -. DR EnsemblBacteria; CBK42319; CBK42319; NIDE2613. DR KEGG; nde:NIDE2613; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000001660; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 2. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000001660}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000001660}. FT DOMAIN 244 409 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 463 AA; 50792 MW; CE3FB366E82BB770 CRC64; MSKPSQSNAV LVAIRTPRVT AEELDSSLQE LTRLVNTLGY RVVGRVTQKR SSDQYAAVLG QGKLAELALW TGGSGKIESA FERPKHKAAS KREAAASDVT DESDDEDESD DSPEVSPGPD EQAQIVIVDC DLSPSQLKNL ERAAGVPVLD RTGVIIEIFS RHARTRAARL QVEIARLNYL APRLRETGGG SERQGGGVGG KGAGETSLEL DKRRIRDRTK ELRAELAAIG DEHQTRRARR EHELTVALVG YTNAGKSSLM RAMTGSEVLV ADKLFATLDT TIRPLYPETR PKVLLSDTVG FIKKLPHDLV ASFKSTLDEA ASASLLLFVV DASDPSFRSQ LEVTRKVLAE VGATDVPSLL VLNKRDRLGP DELTALKAEY PDAVLLSTRN KEDLQALRER IMGYFESDMI DEELRIPFTA QGVVAEIRAR MRILSEEYDA EGLTIRVRST PENLAAIKRK LAR // ID D8QTQ9_SELML Unreviewed; 462 AA. AC D8QTQ9; DT 05-OCT-2010, integrated into UniProtKB/TrEMBL. DT 05-OCT-2010, sequence version 1. DT 30-AUG-2017, entry version 45. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EFJ36690.1}; GN ORFNames=SELMODRAFT_77541 {ECO:0000313|EMBL:EFJ36690.1}; OS Selaginella moellendorffii (Spikemoss). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Lycopodiopsida; Selaginellales; Selaginellaceae; Selaginella. OX NCBI_TaxID=88036 {ECO:0000313|Proteomes:UP000001514}; RN [1] {ECO:0000313|EMBL:EFJ36690.1, ECO:0000313|Proteomes:UP000001514} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=21551031; DOI=10.1126/science.1203810; RA Banks J.A., Nishiyama T., Hasebe M., Bowman J.L., Gribskov M., RA dePamphilis C., Albert V.A., Aono N., Aoyama T., Ambrose B.A., RA Ashton N.W., Axtell M.J., Barker E., Barker M.S., Bennetzen J.L., RA Bonawitz N.D., Chapple C., Cheng C., Correa L.G., Dacre M., RA DeBarry J., Dreyer I., Elias M., Engstrom E.M., Estelle M., Feng L., RA Finet C., Floyd S.K., Frommer W.B., Fujita T., Gramzow L., RA Gutensohn M., Harholt J., Hattori M., Heyl A., Hirai T., Hiwatashi Y., RA Ishikawa M., Iwata M., Karol K.G., Koehler B., Kolukisaoglu U., RA Kubo M., Kurata T., Lalonde S., Li K., Li Y., Litt A., Lyons E., RA Manning G., Maruyama T., Michael T.P., Mikami K., Miyazaki S., RA Morinaga S., Murata T., Mueller-Roeber B., Nelson D.R., Obara M., RA Oguri Y., Olmstead R.G., Onodera N., Petersen B.L., Pils B., RA Prigge M., Rensing S.A., Riano-Pachon D.M., Roberts A.W., Sato Y., RA Scheller H.V., Schulz B., Schulz C., Shakirov E.V., Shibagaki N., RA Shinohara N., Shippen D.E., Soerensen I., Sotooka R., Sugimoto N., RA Sugita M., Sumikawa N., Tanurdzic M., Theissen G., Ulvskov P., RA Wakazuki S., Weng J.K., Willats W.W., Wipf D., Wolf P.G., Yang L., RA Zimmer A.D., Zhu Q., Mitros T., Hellsten U., Loque D., Otillar R., RA Salamov A., Schmutz J., Shapiro H., Lindquist E., Lucas S., RA Rokhsar D., Grigoriev I.V.; RT "The Selaginella genome identifies genetic changes associated with the RT evolution of vascular plants."; RL Science 332:960-963(2011). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GL377566; EFJ36690.1; -; Genomic_DNA. DR RefSeq; XP_002961430.1; XM_002961384.1. DR UniGene; Smo.9034; -. DR ProteinModelPortal; D8QTQ9; -. DR STRING; 88036.EFJ36690; -. DR EnsemblPlants; EFJ36690; EFJ36690; SELMODRAFT_77541. DR GeneID; 9629695; -. DR Gramene; EFJ36690; EFJ36690; SELMODRAFT_77541. DR KEGG; smo:SELMODRAFT_77541; -. DR eggNOG; KOG0410; Eukaryota. DR eggNOG; COG2262; LUCA. DR InParanoid; D8QTQ9; -. DR KO; K03665; -. DR OMA; VILEIFH; -. DR OrthoDB; EOG093609UJ; -. DR Proteomes; UP000001514; Unassembled WGS sequence. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000001514}; KW Reference proteome {ECO:0000313|Proteomes:UP000001514}. FT DOMAIN 239 404 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 198 232 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 462 AA; 51432 MW; CD4D333734E33230 CRC64; MPPGEEEAPA SSSPGRSITV SSSVTDSEDS SDRFVIRNNR EIYQEKAFLV GVEMKRHRAL FSIDESLKEL EQLADTAGLA VVGSTYQKLG YPNPRTYMAS GKVAEVKTAV QALDVETVIL DDEISPGQLR NLEKAFGDDV RVCDRTALIL DIFSQRAATR EAALQVVLAQ LEYQLPRLTK LWTHLERQAG GMVKGMGEKQ IEVDKRILRT KIAELRKNLE SVRDHRQQYR NRRASVPIPV ISLVGYTNAG KSTLLNKLSN AGVLAEDKLF ATLDPITRRV QLPNGKECLF TDTVGFIQKL PTQLVAAFRA TLEEISDSSL ILHVVDRSHP MAPEQTKAVD EVLAELDVQH IPRLSVWNKI DKAEDPDALR AEAKQQGAIC VSALTGEGIQ EFFDAVETKL KDLLVRVEAI VPYSKGDLVD MIHRRGVVEH EEYTDSGTLV RAHVPLALSK QLLEYRDQVP FM // ID D8REG0_SELML Unreviewed; 334 AA. AC D8REG0; DT 05-OCT-2010, integrated into UniProtKB/TrEMBL. DT 05-OCT-2010, sequence version 1. DT 30-AUG-2017, entry version 33. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EFJ29440.1}; GN ORFNames=SELMODRAFT_91633 {ECO:0000313|EMBL:EFJ29440.1}; OS Selaginella moellendorffii (Spikemoss). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Lycopodiopsida; Selaginellales; Selaginellaceae; Selaginella. OX NCBI_TaxID=88036 {ECO:0000313|Proteomes:UP000001514}; RN [1] {ECO:0000313|EMBL:EFJ29440.1, ECO:0000313|Proteomes:UP000001514} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=21551031; DOI=10.1126/science.1203810; RA Banks J.A., Nishiyama T., Hasebe M., Bowman J.L., Gribskov M., RA dePamphilis C., Albert V.A., Aono N., Aoyama T., Ambrose B.A., RA Ashton N.W., Axtell M.J., Barker E., Barker M.S., Bennetzen J.L., RA Bonawitz N.D., Chapple C., Cheng C., Correa L.G., Dacre M., RA DeBarry J., Dreyer I., Elias M., Engstrom E.M., Estelle M., Feng L., RA Finet C., Floyd S.K., Frommer W.B., Fujita T., Gramzow L., RA Gutensohn M., Harholt J., Hattori M., Heyl A., Hirai T., Hiwatashi Y., RA Ishikawa M., Iwata M., Karol K.G., Koehler B., Kolukisaoglu U., RA Kubo M., Kurata T., Lalonde S., Li K., Li Y., Litt A., Lyons E., RA Manning G., Maruyama T., Michael T.P., Mikami K., Miyazaki S., RA Morinaga S., Murata T., Mueller-Roeber B., Nelson D.R., Obara M., RA Oguri Y., Olmstead R.G., Onodera N., Petersen B.L., Pils B., RA Prigge M., Rensing S.A., Riano-Pachon D.M., Roberts A.W., Sato Y., RA Scheller H.V., Schulz B., Schulz C., Shakirov E.V., Shibagaki N., RA Shinohara N., Shippen D.E., Soerensen I., Sotooka R., Sugimoto N., RA Sugita M., Sumikawa N., Tanurdzic M., Theissen G., Ulvskov P., RA Wakazuki S., Weng J.K., Willats W.W., Wipf D., Wolf P.G., Yang L., RA Zimmer A.D., Zhu Q., Mitros T., Hellsten U., Loque D., Otillar R., RA Salamov A., Schmutz J., Shapiro H., Lindquist E., Lucas S., RA Rokhsar D., Grigoriev I.V.; RT "The Selaginella genome identifies genetic changes associated with the RT evolution of vascular plants."; RL Science 332:960-963(2011). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GL377577; EFJ29440.1; -; Genomic_DNA. DR RefSeq; XP_002969352.1; XM_002969306.1. DR UniGene; Smo.5630; -. DR ProteinModelPortal; D8REG0; -. DR STRING; 88036.EFJ29440; -. DR EnsemblPlants; EFJ29440; EFJ29440; SELMODRAFT_91633. DR GeneID; 9659730; -. DR Gramene; EFJ29440; EFJ29440; SELMODRAFT_91633. DR KEGG; smo:SELMODRAFT_91633; -. DR eggNOG; KOG0410; Eukaryota. DR eggNOG; COG2262; LUCA. DR InParanoid; D8REG0; -. DR OMA; NIRTHLN; -. DR OrthoDB; EOG09360975; -. DR Proteomes; UP000001514; Unassembled WGS sequence. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000001514}; KW Reference proteome {ECO:0000313|Proteomes:UP000001514}. FT DOMAIN 246 334 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 334 AA; 36596 MW; AAB34D75AB4AC9D3 CRC64; MKWLGVAWSG LRRHFSSRAD GVGSIYDKLF VVQPRFHPPL LLKAKLLEAL RLANSLAPLT ATDLKSDFPS YVLVQGRRKI NAGTYFGAGT IDNIRTHLNV IDVEDREIDA VFVNTSLSGV QQRNLEDAWE RPVLDRVGLI IEIFGSRARS KEAKLQVELA ALDFKRTRLI REKGERKAFG AGGEQEVVSA RGASGGGGRG FTSGSGESEL QLQRRRISDQ KHKIQVALAK AKQTRSLHRR NREGIPLVAV VGYTNAGKST LVGALSKSSL YSDDRLFATL DTQVRSVILP SGRRVLVSDT VGFISDLPTQ LVEAFHATLE EVVAADIVLV STLL // ID D8T3S6_SELML Unreviewed; 462 AA. AC D8T3S6; DT 05-OCT-2010, integrated into UniProtKB/TrEMBL. DT 05-OCT-2010, sequence version 1. DT 30-AUG-2017, entry version 43. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EFJ08687.1}; GN ORFNames=SELMODRAFT_131329 {ECO:0000313|EMBL:EFJ08687.1}; OS Selaginella moellendorffii (Spikemoss). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Lycopodiopsida; Selaginellales; Selaginellaceae; Selaginella. OX NCBI_TaxID=88036 {ECO:0000313|Proteomes:UP000001514}; RN [1] {ECO:0000313|EMBL:EFJ08687.1, ECO:0000313|Proteomes:UP000001514} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=21551031; DOI=10.1126/science.1203810; RA Banks J.A., Nishiyama T., Hasebe M., Bowman J.L., Gribskov M., RA dePamphilis C., Albert V.A., Aono N., Aoyama T., Ambrose B.A., RA Ashton N.W., Axtell M.J., Barker E., Barker M.S., Bennetzen J.L., RA Bonawitz N.D., Chapple C., Cheng C., Correa L.G., Dacre M., RA DeBarry J., Dreyer I., Elias M., Engstrom E.M., Estelle M., Feng L., RA Finet C., Floyd S.K., Frommer W.B., Fujita T., Gramzow L., RA Gutensohn M., Harholt J., Hattori M., Heyl A., Hirai T., Hiwatashi Y., RA Ishikawa M., Iwata M., Karol K.G., Koehler B., Kolukisaoglu U., RA Kubo M., Kurata T., Lalonde S., Li K., Li Y., Litt A., Lyons E., RA Manning G., Maruyama T., Michael T.P., Mikami K., Miyazaki S., RA Morinaga S., Murata T., Mueller-Roeber B., Nelson D.R., Obara M., RA Oguri Y., Olmstead R.G., Onodera N., Petersen B.L., Pils B., RA Prigge M., Rensing S.A., Riano-Pachon D.M., Roberts A.W., Sato Y., RA Scheller H.V., Schulz B., Schulz C., Shakirov E.V., Shibagaki N., RA Shinohara N., Shippen D.E., Soerensen I., Sotooka R., Sugimoto N., RA Sugita M., Sumikawa N., Tanurdzic M., Theissen G., Ulvskov P., RA Wakazuki S., Weng J.K., Willats W.W., Wipf D., Wolf P.G., Yang L., RA Zimmer A.D., Zhu Q., Mitros T., Hellsten U., Loque D., Otillar R., RA Salamov A., Schmutz J., Shapiro H., Lindquist E., Lucas S., RA Rokhsar D., Grigoriev I.V.; RT "The Selaginella genome identifies genetic changes associated with the RT evolution of vascular plants."; RL Science 332:960-963(2011). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GL377671; EFJ08687.1; -; Genomic_DNA. DR RefSeq; XP_002990272.1; XM_002990226.1. DR ProteinModelPortal; D8T3S6; -. DR STRING; 88036.EFJ08687; -. DR EnsemblPlants; EFJ08687; EFJ08687; SELMODRAFT_131329. DR GeneID; 9630790; -. DR Gramene; EFJ08687; EFJ08687; SELMODRAFT_131329. DR KEGG; smo:SELMODRAFT_131329; -. DR eggNOG; KOG0410; Eukaryota. DR eggNOG; COG2262; LUCA. DR InParanoid; D8T3S6; -. DR KO; K03665; -. DR OMA; VYAKDQL; -. DR OrthoDB; EOG093609UJ; -. DR Proteomes; UP000001514; Unassembled WGS sequence. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000001514}; KW Reference proteome {ECO:0000313|Proteomes:UP000001514}. FT DOMAIN 239 404 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 462 AA; 51453 MW; ADB0A70E7A089A36 CRC64; MPPREEEAPA SSSPGRSITV SSSVTDSEDS SDRFVIRNNR EIYQEKAFLV GVEMKRHRAL FSIDESLKEL EQLADTAGLA VVGSTYQKLG YPNPRTYMAS GKVAEVKTAV QALDVETVIL DDEISPGQLR NLEKAFGDDV RVCDRTALIL DIFSQRAATR EAALQVVLAQ LEYQLPRLTK LWTHLERQAG GMVKGMGEKQ IEVDKRILRT KASSLRKNLE SVRDHRQQYR NRRASVPIPV ISLVGYTNAG KSTLLNKLSN AGVLAEDKLF ATLDPITRRV QLPNGKECLF TDTVGFIQKL PTQLVAAFRA TLEEISDSSL ILHVVDRSHS MAPEQTKAVD EVLAELDVQH IPRLSVWNKI DKAEDPDALR AEAKQQGAIC VSALTGEGIQ EFFDAVETKL KDLLVRVEAI VPYSKGDLVD MIHRRGVVEH EEYTDSGTLV RAHVPLALSK QLLEYRDQVP FM // ID D8UK55_VOLCA Unreviewed; 548 AA. AC D8UK55; DT 05-OCT-2010, integrated into UniProtKB/TrEMBL. DT 05-OCT-2010, sequence version 1. DT 30-AUG-2017, entry version 32. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EFJ39892.1}; GN ORFNames=VOLCADRAFT_108445 {ECO:0000313|EMBL:EFJ39892.1}; OS Volvox carteri f. nagariensis. OC Eukaryota; Viridiplantae; Chlorophyta; Chlorophyceae; OC Chlamydomonadales; Volvocaceae; Volvox. OX NCBI_TaxID=3068 {ECO:0000313|Proteomes:UP000001058}; RN [1] {ECO:0000313|EMBL:EFJ39892.1, ECO:0000313|Proteomes:UP000001058} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=f. Nagariensis / Eve {ECO:0000313|Proteomes:UP000001058}; RX PubMed=20616280; DOI=10.1126/science.1188800; RA Prochnik S.E., Umen J., Nedelcu A.M., Hallmann A., Miller S.M., RA Nishii I., Ferris P., Kuo A., Mitros T., Fritz-Laylin L.K., RA Hellsten U., Chapman J., Simakov O., Rensing S.A., Terry A., RA Pangilinan J., Kapitonov V., Jurka J., Salamov A., Shapiro H., RA Schmutz J., Grimwood J., Lindquist E., Lucas S., Grigoriev I.V., RA Schmitt R., Kirk D., Rokhsar D.S.; RT "Genomic analysis of organismal complexity in the multicellular green RT alga Volvox carteri."; RL Science 329:223-226(2010). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GL378438; EFJ39892.1; -; Genomic_DNA. DR RefSeq; XP_002959031.1; XM_002958985.1. DR ProteinModelPortal; D8UK55; -. DR GeneID; 9625791; -. DR KEGG; vcn:VOLCADRAFT_108445; -. DR InParanoid; D8UK55; -. DR KO; K03665; -. DR Proteomes; UP000001058; Unassembled WGS sequence. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000001058}; KW Reference proteome {ECO:0000313|Proteomes:UP000001058}. FT DOMAIN 299 468 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 258 292 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 548 AA; 59221 MW; 85A03AA675D69E67 CRC64; MSPGATALGS FGRSRPGPIY SHHLYKQGRL QLPLLVGTPL PARAIKCSVQ VSEESALAQS FESAFLQAQE QQQQSDQRSR TPGRQTELPP EDERERVFLV GAAIKGEQRR HTYDVHESVD ELGRLAETAG LRVMGSTYQL LDAPNMSTYI GSGKVAEVGR AVAALGVETV IFDDELSPGQ LRNLERQLGT AAGGGEGSVR VCDRTALILD IFSQRAQTRE GQLQVELAQT EYQLPRLTRM WTHLDRVGGG GQVKGAGEKQ IEVDKRLLRD RAAALRRELE AVRTHRRQYR DKRSATPIPV VGICGYTNAG KSTLLNTLTN AGVLAEDQLF ATLDPTTRRL RLKGNKEILM SDTVGFIQKL PTELVAAFRA TLEEIRDASI ILHVVDISHP NAAAQNAAVM QVLEELGIGG GDMPPMVTAW NKVDATSNPE EIRRVAAKRS RTVCISGRTG EGLDELLELL GQVLEESMEE VRALLPYSAG DLLNELHTGG RVKCVEYTPG GVAVVAAAPA ALVGRLRHAG VLLESEVKAG CAGGEEDGGE DGDELVLL // ID D9Q060_ACIS3 Unreviewed; 373 AA. AC D9Q060; DT 05-OCT-2010, integrated into UniProtKB/TrEMBL. DT 05-OCT-2010, sequence version 1. DT 07-JUN-2017, entry version 53. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=ASAC_0291 {ECO:0000313|EMBL:ADL18698.1}; OS Acidilobus saccharovorans (strain DSM 16705 / JCM 18335 / VKM B-2471 / OS 345-15). OC Archaea; Crenarchaeota; Thermoprotei; Acidilobales; Acidilobaceae; OC Acidilobus. OX NCBI_TaxID=666510 {ECO:0000313|EMBL:ADL18698.1, ECO:0000313|Proteomes:UP000000346}; RN [1] {ECO:0000313|EMBL:ADL18698.1, ECO:0000313|Proteomes:UP000000346} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 16705 / JCM 18335 / VKM B-2471 / 345-15 RC {ECO:0000313|Proteomes:UP000000346}; RX PubMed=20581186; DOI=10.1128/AEM.00599-10; RA Mardanov A.V., Svetlitchnyi V.A., Beletsky A.V., Prokofeva M.I., RA Bonch-Osmolovskaya E.A., Ravin N.V., Skryabin K.G.; RT "The genome sequence of the crenarchaeon Acidilobus saccharovorans RT supports a new order, Acidilobales, and suggests an important RT ecological role in terrestrial acidic hot springs."; RL Appl. Environ. Microbiol. 76:5652-5657(2010). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001742; ADL18698.1; -; Genomic_DNA. DR RefSeq; WP_013266210.1; NC_014374.1. DR ProteinModelPortal; D9Q060; -. DR STRING; 666510.ASAC_0291; -. DR EnsemblBacteria; ADL18698; ADL18698; ASAC_0291. DR GeneID; 9498514; -. DR KEGG; asc:ASAC_0291; -. DR eggNOG; arCOG00353; Archaea. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; FNNHAHV; -. DR OrthoDB; POG093Z07D6; -. DR Proteomes; UP000000346; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000000346}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000000346}. FT DOMAIN 176 352 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 142 169 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 373 AA; 41806 MW; ACF8B59C37691755 CRC64; MISREYLDHL EEALAIAESA NYEVVDIIKR SRPGRRLSDE AARRISERAH RANAEVIIYY GNLEPSSLYK LEKESKLKVL DRVLIILEIF ALHAGSKESK LQIEMARLKH ELPLIREYIR RAKAGEQVDF LGPGRYAFEA YEKHVITRIA RIRRELDELR RRVKTQEQAR KDSGVVLASI VGYASAGKTS IFNAITGERQ PTGPEYFTTL FAKHKMVNFN NTKIMLIDTV GFVRDVPAEI IESFYSTLQE ASLADVLIFV VDSSEDVSAI REKVAAGVSL LSKLNAINKP IILAMNKIDL VARDDLNKKE SLVRELLSHM GIKADLVEVS AVKKLNLEAL LEKVSESARG AGGPSETLRQ GVRAEARPQA DAR // ID D9QAY4_CORP2 Unreviewed; 546 AA. AC D9QAY4; DT 05-OCT-2010, integrated into UniProtKB/TrEMBL. DT 05-OCT-2010, sequence version 1. DT 07-JUN-2017, entry version 47. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:ADL10710.1}; GN OrderedLocusNames=CpC231_1235 {ECO:0000313|EMBL:ADL10710.1}; OS Corynebacterium pseudotuberculosis (strain C231). OC Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae; OC Corynebacterium. OX NCBI_TaxID=681645 {ECO:0000313|EMBL:ADL10710.1, ECO:0000313|Proteomes:UP000000276}; RN [1] {ECO:0000313|EMBL:ADL10710.1, ECO:0000313|Proteomes:UP000000276} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C231 {ECO:0000313|EMBL:ADL10710.1, RC ECO:0000313|Proteomes:UP000000276}; RX PubMed=21037006; DOI=10.1128/JB.01211-10; RG Consortium: Rede Paraense de Genomica e Proteomica (RPGP); RA Silva A., Schneider M.P., Cerdeira L., Barbosa M.S., Ramos R.T., RA Carneiro A.R., Santos R., Lima M., D'Afonseca V., Almeida S.S., RA Santos A.R., Soares S.C., Pinto A.C., Ali A., Dorella F.A., Rocha F., RA de Abreu V.A., Trost E., Tauch A., Shpigel N., Miyoshi A., Azevedo V.; RT "Complete genome sequence of Corynebacterium pseudotuberculosis I19, a RT strain isolated from a cow in Israel with bovine mastitis."; RL J. Bacteriol. 193:323-324(2011). RN [2] {ECO:0000313|EMBL:ADL10710.1, ECO:0000313|Proteomes:UP000000276} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C231 {ECO:0000313|EMBL:ADL10710.1, RC ECO:0000313|Proteomes:UP000000276}; RX PubMed=21533164; DOI=10.1371/journal.pone.0018551; RA Ruiz J.C., D'Afonseca V., Silva A., Ali A., Pinto A.C., Santos A.R., RA Rocha A.A., Lopes D.O., Dorella F.A., Pacheco L.G., Costa M.P., RA Turk M.Z., Seyffert N., Moraes P.M., Soares S.C., Almeida S.S., RA Castro T.L., Abreu V.A., Trost E., Baumbach J., Tauch A., RA Schneider M.P., McCulloch J., Cerdeira L.T., Ramos R.T., Zerlotini A., RA Dominitini A., Resende D.M., Coser E.M., Oliveira L.M., Pedrosa A.L., RA Vieira C.U., Guimaraes C.T., Bartholomeu D.C., Oliveira D.M., RA Santos F.R., Rabelo E.M., Lobo F.P., Franco G.R., Costa A.F., RA Castro I.M., Dias S.R., Ferro J.A., Ortega J.M., Paiva L.V., RA Goulart L.R., Almeida J.F., Ferro M.I., Carneiro N.P., Falcao P.R., RA Grynberg P., Teixeira S.M., Brommonschenkel S., Oliveira S.C., RA Meyer R., Moore R.J., Miyoshi A., Oliveira G.C., Azevedo V.; RT "Evidence for reductive genome evolution and lateral acquisition of RT virulence functions in two Corynebacterium pseudotuberculosis RT strains."; RL PLoS ONE 6:E18551-E18551(2011). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001829; ADL10710.1; -; Genomic_DNA. DR ProteinModelPortal; D9QAY4; -. DR EnsemblBacteria; ADL10710; ADL10710; CpC231_1235. DR KEGG; cpq:CpC231_1235; -. DR PATRIC; fig|681645.3.peg.1293; -. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR Proteomes; UP000000276; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000000276}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000000276}. FT DOMAIN 321 497 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 280 307 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 546 AA; 59402 MW; 91A0D9CE8EB459D0 CRC64; MRQWSVTMTK NNETPIHDQI LNSAHPSEPR GISHDDLLDR AFKDHRPVAP HEDSGIDQSG LLSSRYTDGA ASSSGASENK QPTVGELDLE ARSSLRSLTR GSSIHATDQD DGYDVEYRKL RLERVILVGG WTQGTTAEVE ATMQELAALA ETAGSEVVDM LYQKRDKPDP GTYIGSGKVA ELKDIVMSTG VDTVVCDGEL SPGQMIALEK ALDVKVIDRT MLILDIFAQH AKSKEGKAQV SLAQMEYLIT RVRGWGGALS RQAGERAGSN GGVGLRGPGE TKIEADRRRL RSDMAKLRKE IAGMKTAREV KRSQRRESTI PQIAIAGYTN AGKSSLINAL TDAGVLVEDA LFATLDPTTR RAELADGRSV VFTDTVGFVR HLPTQLVEAF RSTLEEVVGA DLVLHVVDGS DPFPLEQIKA VNGVISDIVR ELKVEAPPEI IVVNKIDQAD PLVLAELRHA LDDVVFVSAQ EGDGIPELEA RIELFLNTLD AHVHLLIPFT RGDIVSRLHK FGTVLSEEYH AEGTLIDVRL PHSLAAELGE YHVTSA // ID D9QHD1_BRESC Unreviewed; 443 AA. AC D9QHD1; DT 05-OCT-2010, integrated into UniProtKB/TrEMBL. DT 05-OCT-2010, sequence version 1. DT 07-JUN-2017, entry version 54. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Bresu_1786 {ECO:0000313|EMBL:ADL01097.1}; OS Brevundimonas subvibrioides (strain ATCC 15264 / DSM 4735 / LMG 14903 OS / NBRC 16000 / CB 81) (Caulobacter subvibrioides). OC Bacteria; Proteobacteria; Alphaproteobacteria; Caulobacterales; OC Caulobacteraceae; Brevundimonas. OX NCBI_TaxID=633149 {ECO:0000313|EMBL:ADL01097.1, ECO:0000313|Proteomes:UP000002696}; RN [1] {ECO:0000313|Proteomes:UP000002696} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 15264 / DSM 4735 / LMG 14903 / NBRC 16000 / CB 81 RC {ECO:0000313|Proteomes:UP000002696}; RX PubMed=21705585; DOI=10.1128/JB.05453-11; RG US DOE Joint Genome Institute; RA Brown P.J., Kysela D.T., Buechlein A., Hemmerich C., Brun Y.V.; RT "Genome sequences of eight morphologically diverse RT alphaproteobacteria."; RL J. Bacteriol. 193:4567-4568(2011). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002102; ADL01097.1; -; Genomic_DNA. DR RefSeq; WP_013269199.1; NC_014375.1. DR ProteinModelPortal; D9QHD1; -. DR STRING; 633149.Bresu_1786; -. DR EnsemblBacteria; ADL01097; ADL01097; Bresu_1786. DR KEGG; bsb:Bresu_1786; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000002696; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000002696}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000002696}. FT DOMAIN 218 390 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 443 AA; 49290 MW; 6DD93545E2060E7F CRC64; MLPSPLQPVR PSLTTKLIDH SVPLIRAVVI HPDMGERSSR PAQERLEEAA GLARALDLDV RAEEVVRLRK TTPATLFGTG KVEELAALIR AAEAEAAVID DDLTPVQQRN LEKEWDCKVI DRTGLILEIF GRRARTKEGR LQVELARLDY EKSRLVRTWT HLERQRGGTG STGGPGETQI ELDRRLIADR IVKLKGELEE VRRTRGLHRK QRKKAPFPAV ALVGYTNAGK STLFNRLTGS EVLAKDLLFA TLDTTQRTIR LPQGRPAIIA DTVGFISDLP HELVESFRAT LEEVGEADLI LHVRDIASAD TAAQAKDVED VLKQIEQPEG KPRRILEVWN KTDLLDPEAR EAVEGQAARS GNTAVAVSAW TGQGIETLRQ AITDLIDDDP ETELILQPSQ GEALAWLYEH GRVTARDTDD QGRMLLTVRL DPQAMGRFER QFG // ID D9QU24_ACEAZ Unreviewed; 606 AA. AC D9QU24; DT 05-OCT-2010, integrated into UniProtKB/TrEMBL. DT 05-OCT-2010, sequence version 1. DT 07-JUN-2017, entry version 50. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Acear_2260 {ECO:0000313|EMBL:ADL13745.1}; OS Acetohalobium arabaticum (strain ATCC 49924 / DSM 5501 / Z-7288). OC Bacteria; Firmicutes; Clostridia; Halanaerobiales; Halobacteroidaceae; OC Acetohalobium. OX NCBI_TaxID=574087 {ECO:0000313|EMBL:ADL13745.1, ECO:0000313|Proteomes:UP000001661}; RN [1] {ECO:0000313|EMBL:ADL13745.1, ECO:0000313|Proteomes:UP000001661} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 49924 / DSM 5501 / Z-7288 RC {ECO:0000313|Proteomes:UP000001661}; RX PubMed=21304692; RA Sikorski J., Lapidus A., Chertkov O., Lucas S., Copeland A., RA Glavina Del Rio T., Nolan M., Tice H., Cheng J.F., Han C., RA Brambilla E., Pitluck S., Liolios K., Ivanova N., Mavromatis K., RA Mikhailova N., Pati A., Bruce D., Detter C., Tapia R., Goodwin L., RA Chen A., Palaniappan K., Land M., Hauser L., Chang Y.J., RA Jeffries C.D., Rohde M., Goker M., Spring S., Woyke T., Bristow J., RA Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.; RT "Complete genome sequence of Acetohalobium arabaticum type strain (Z- RT 7288)."; RL Stand. Genomic Sci. 3:57-65(2010). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002105; ADL13745.1; -; Genomic_DNA. DR ProteinModelPortal; D9QU24; -. DR STRING; 574087.Acear_2260; -. DR EnsemblBacteria; ADL13745; ADL13745; Acear_2260. DR KEGG; aar:Acear_2260; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; EREVIIT; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000001661; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000001661}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000001661}. FT DOMAIN 380 546 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 342 376 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 606 AA; 68500 MW; 3D90ABAE2D5EF101 CRC64; MVLITDLRGD LSGIKDRYIE ELEMMSSSIF SSGELVAIDF LYQIINIASE IEDKIAVLIN RRGEVLRIKV GELTNDFFAG AKQRRSVKRL SGLRCIYLTF NSQLNRKNKI FLKEYRLDLL VHLSLADRQS KLEALVHYPK VDNGQLVVGS ELKGPFSLTE LTETDYSTEI EDIEDKLQET ETVKVTEAES EAAVLVCLIT EDDTGYNQEE PLAELENLVQ TAGIEVKGKE IQYRKDPDHS YYIGYGKVQE LKELKYRLGI NVIIFDEELS PAQQRNLEDE LGVKVIDRTE VILDIFAQHA NSKEGKLQVE LAQLHYLLPR LTGKGEDLSR LAGGIGTRGP GESKLEIDRR RIRKRIDNLE AEINRVQQTR ATQRSRRKLP TISLVGYTNA GKSTLLNRLT EATAVTKDEL FATLDSNTCR LKLPVGRKVL ISDTVGFIRK LPHQLIAAFR ATLEEVTEAD ILLHVVDVTE ADYKAKMDAV VEVLSELNVL DKPIITILNK IDLLKDQKQV ELIQQNLKNS LVISAKEGQG VDRLLDEISN LLLDTMVELE LLLPYSDAGA LELIHQRGKV LREEYSNEGI SIKARISQQM ANQVDEDYII FRRSLA // ID D9RV44_PREMB Unreviewed; 416 AA. AC D9RV44; DT 05-OCT-2010, integrated into UniProtKB/TrEMBL. DT 05-OCT-2010, sequence version 1. DT 07-JUN-2017, entry version 47. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:ADK97123.1}; GN OrderedLocusNames=HMPREF0659_A6522 {ECO:0000313|EMBL:ADK97123.1}; OS Prevotella melaninogenica (strain ATCC 25845 / DSM 7089 / JCM 6325 / OS VPI 2381 / B282) (Bacteroides melaninogenicus). OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Prevotellaceae; OC Prevotella. OX NCBI_TaxID=553174 {ECO:0000313|EMBL:ADK97123.1, ECO:0000313|Proteomes:UP000001498}; RN [1] {ECO:0000313|Proteomes:UP000001498} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 25845 / DSM 7089 / JCM 6325 / VPI 2381 / B282 RC {ECO:0000313|Proteomes:UP000001498}; RA Harkins D.M., Madupu R., Durkin A.S., Torralba M., Methe B., RA Sutton G.G., Nelson K.E.; RT "Genome sequence of Prevotella melaninogenica strain ATCC 25845."; RL Submitted (JUL-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002123; ADK97123.1; -; Genomic_DNA. DR RefSeq; WP_013265581.1; NC_014371.1. DR ProteinModelPortal; D9RV44; -. DR STRING; 553174.HMPREF0659_A6522; -. DR EnsemblBacteria; ADK97123; ADK97123; HMPREF0659_A6522. DR GeneID; 9497379; -. DR KEGG; pmz:HMPREF0659_A6522; -. DR PATRIC; fig|553174.6.peg.1501; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR Proteomes; UP000001498; Chromosome II. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000001498}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000001498}. FT DOMAIN 216 400 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 416 AA; 47718 MW; C4F02C64484E84F2 CRC64; MKEFIISDVK AETAILVGLI TKDQNEDKTK EYLDELEFLA DTAGAITVKR FTQRVTGPSS VTYVGKGKLE EIRDYIKMKE DEEEPIGMVI FDDELSAKQM RNIEQELGVK ILDRTSLILD IFAMRAQTAN AKTQVELAQY RYMLPRLQRL WTHLERQGGG SGSGGGKGSV GLRGPGETQL EMDRRIILQR MTLLKQRLAE IDKQKVTQRK NRGRMIRVAL VGYTNVGKST TMNLLAKSEV FAENKLFATL DTTVRKVVVD NLPFLLADTV GFIRKLPTDL VDSFKSTLDE VREADLLLHV VDISHPDFEE QIQVVNQTLS ELGCADKPSM IIFNKIDNYH WVEKEEDDLT PATKENITLD ELKKTWMAKE HDNCLFISAK EKENIDEFRE VLYKKVRELH VQKYPYNDFL YNIEEE // ID D9RYW8_THEOJ Unreviewed; 417 AA. AC D9RYW8; DT 05-OCT-2010, integrated into UniProtKB/TrEMBL. DT 05-OCT-2010, sequence version 1. DT 07-JUN-2017, entry version 53. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Toce_1811 {ECO:0000313|EMBL:ADL08542.1}; OS Thermosediminibacter oceani (strain ATCC BAA-1034 / DSM 16646 / OS JW/IW-1228P). OC Bacteria; Firmicutes; Clostridia; Thermoanaerobacterales; OC Thermoanaerobacterales Family III. Incertae Sedis; OC Thermosediminibacter. OX NCBI_TaxID=555079 {ECO:0000313|EMBL:ADL08542.1, ECO:0000313|Proteomes:UP000000272}; RN [1] {ECO:0000313|EMBL:ADL08542.1, ECO:0000313|Proteomes:UP000000272} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-1034 / DSM 16646 / JW/IW-1228P RC {ECO:0000313|Proteomes:UP000000272}; RX PubMed=21304740; RA Pitluck S., Yasawong M., Munk C., Nolan M., Lapidus A., Lucas S., RA Glavina Del Rio T., Tice H., Cheng J.F., Bruce D., Detter C., RA Tapia R., Han C., Goodwin L., Liolios K., Ivanova N., Mavromatis K., RA Mikhailova N., Pati A., Chen A., Palaniappan K., Land M., Hauser L., RA Chang Y.J., Jeffries C.D., Rohde M., Spring S., Sikorski J., Goker M., RA Woyke T., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P., RA Kyrpides N.C., Klenk H.P.; RT "Complete genome sequence of Thermosediminibacter oceani type strain RT (JW/IW-1228P)."; RL Stand. Genomic Sci. 3:108-116(2010). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002131; ADL08542.1; -; Genomic_DNA. DR RefSeq; WP_013276564.1; NC_014377.1. DR ProteinModelPortal; D9RYW8; -. DR STRING; 555079.Toce_1811; -. DR EnsemblBacteria; ADL08542; ADL08542; Toce_1811. DR KEGG; toc:Toce_1811; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000000272; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000000272}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000000272}. FT DOMAIN 196 358 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 165 192 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 417 AA; 46468 MW; BFA6CCE2067A59A9 CRC64; MPSHENIKPK TEAILAGLID DKSCDETLEE LALLSETAGA KVLAKVTQKR ASKDPAYYLG MGKAREIAEL VEGLGANAVI FDDDLTPVQI RNLENLIGVQ IIDRTTLVLD IFAQRARSLE GKIQVELAQL QHMLPRLTGK GVELSREGGG IGTRGPGETK LETDRRHIRR RITHLKKELE RIRKNRKLLR SSRKYPVISL VGYTNAGKST LMNALTGAGV SSNDRLFDTL DPTTRALLLP DGRRVLLSDT VGFIRKLPHE IVEAFKATLE EVKEADLLIH VVDASSPKAD EEISTVKSVL KEIGAENIPT ILALNKIDRV NHRELITGEE NVVEISALCG TNLDILREKI CQLLPQTREH ALLCIPYEYG FLLDEIHETS LVEREEFKQD GIEIEGKIDT ILLRRIKKYL SEKNACS // ID D9SFI1_GALCS Unreviewed; 382 AA. AC D9SFI1; DT 05-OCT-2010, integrated into UniProtKB/TrEMBL. DT 05-OCT-2010, sequence version 1. DT 30-AUG-2017, entry version 51. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Galf_1250 {ECO:0000313|EMBL:ADL55278.1}; OS Gallionella capsiferriformans (strain ES-2) (Gallionella ferruginea OS capsiferriformans (strain ES-2)). OC Bacteria; Proteobacteria; Betaproteobacteria; Nitrosomonadales; OC Gallionellaceae; Gallionella. OX NCBI_TaxID=395494 {ECO:0000313|EMBL:ADL55278.1, ECO:0000313|Proteomes:UP000001235}; RN [1] {ECO:0000313|EMBL:ADL55278.1, ECO:0000313|Proteomes:UP000001235} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ES-2 {ECO:0000313|EMBL:ADL55278.1, RC ECO:0000313|Proteomes:UP000001235}; RG US DOE Joint Genome Institute; RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L., RA Pitluck S., Chertkov O., Davenport K.W., Detter J.C., Han C., RA Tapia R., Land M., Hauser L., Chang Y.-J., Jeffries C., Kyrpides N., RA Ivanova N., Mikhailova N., Shelobolina E.S., Picardal F., Roden E., RA Emerson D., Woyke T.; RT "Complete sequence of Gallionella capsiferriformans ES-2."; RL Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002159; ADL55278.1; -; Genomic_DNA. DR RefSeq; WP_013293217.1; NC_014394.1. DR ProteinModelPortal; D9SFI1; -. DR STRING; 395494.Galf_1250; -. DR EnsemblBacteria; ADL55278; ADL55278; Galf_1250. DR KEGG; gca:Galf_1250; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000001235; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000001235}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000001235}. FT DOMAIN 198 364 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 164 191 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 382 AA; 42270 MW; 4B311D41BCBB9336 CRC64; MQQTSEGTQA AILVSIDLGG ADYRESLAEL RLLAETAGVR TLATFEAKRM RPDAALFAGS GKVAEIAEMV ELKEVPLVIF NHDLSPAQMR NLTARLGTRV IDRTMLILDI FAQRAQSHEG KVQVELAQLK YMATRLVGLN TDMGQQKFAV GARGPGETQL ELDRRKLDKR VHLLKERLEK LKAQRDVMRR SRNRSGVFSV SIVGYTNAGK STLFNRLTKA NVYVANQLFA TLDTTSRRMY SEGAGEIVVS DTVGFIRHLP HGLVAAFRST LEETIQADLL LHVVDASNPN RDDQIAEVNK VLKEIDAGDI PQLMVYNKVD LTEMAAGAER DDCDRIARVF LSAVSGAGMD DLRLALTAAK DAKLVVEQNE NQIRQARNLP WD // ID D9SMX8_CLOC7 Unreviewed; 599 AA. AC D9SMX8; DT 05-OCT-2010, integrated into UniProtKB/TrEMBL. DT 05-OCT-2010, sequence version 1. DT 07-JUN-2017, entry version 54. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Clocel_2101 {ECO:0000313|EMBL:ADL51844.1}; OS Clostridium cellulovorans (strain ATCC 35296 / DSM 3052 / OCM 3 / OS 743B). OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=573061 {ECO:0000313|EMBL:ADL51844.1, ECO:0000313|Proteomes:UP000002730}; RN [1] {ECO:0000313|EMBL:ADL51844.1, ECO:0000313|Proteomes:UP000002730} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 35296 / DSM 3052 / OCM 3 / 743B RC {ECO:0000313|Proteomes:UP000002730}; RG US DOE Joint Genome Institute; RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L., RA Pitluck S., Chertkov O., Detter J.C., Han C., Tapia R., Land M., RA Hauser L., Chang Y.-J., Jeffries C., Kyrpides N., Ivanova N., RA Mikhailova N., Hemme C.L., Woyke T.; RT "Complete sequence of Clostridium cellulovorans 743B."; RL Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002160; ADL51844.1; -; Genomic_DNA. DR RefSeq; WP_010076938.1; NC_014393.1. DR ProteinModelPortal; D9SMX8; -. DR STRING; 573061.Clocel_2101; -. DR EnsemblBacteria; ADL51844; ADL51844; Clocel_2101. DR KEGG; ccb:Clocel_2101; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; EREVIIT; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000002730; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000002730}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000002730}. FT DOMAIN 366 543 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 325 359 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 599 AA; 67056 MW; C4BE5F52C666985B CRC64; MINGNIEGVK NSFLAELEDL YKLKAYKDQI ATVEMVNTIV NVTKAINREV SIAIDRKGNV IDVSIGDSAT VNLPMIDLKE KRLCGVKVLH THPSGNSNLS VVDTSALLKL KLDAMIAVGV TEDGITDVTL GFCALKNEIL VYDKVGPMSL EDSLNFNYLE KVNYVESFLK NSSVTENEEE EEIAIVVGVD NEESLDELEE LANACNVKVV YKVLQKKNKI DNLYYIGSGK AEELALIKQV KGANLIIFDD ELSGIQVKNL EEVTGTKVID RTILILEIFA RRAKSREAKI QVELAQLKYR SARLIAHGIT MSRTGGGIGT RGPGEKKLEI DRRRIKDDIH DLRMELEKIR KNRAVQREKR SKSNVPKISL VGYTNAGKST LRNALAEYAL VEQGKQKDKV FEADMLFATL DVTTRAILLR DKRVAALTDT VGFIRKLSHD LVEAFKSTLE EVIFADLLLH VVDSSSDIIF EQIEATHAVL KELNAFDKPI ILVLNKVDKE NAHTVAEIKE KYKEFQVIPI SAKNGTNFDG LMEMIVEFLP NPMKKVEFLI PYSDGDVGAY LHRNAIIEEE DYLDNGTKVI ATVDIETYNK FNKFIVNEF // ID D9SYS5_MICAI Unreviewed; 487 AA. AC D9SYS5; DT 05-OCT-2010, integrated into UniProtKB/TrEMBL. DT 05-OCT-2010, sequence version 1. DT 05-JUL-2017, entry version 52. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Micau_1552 {ECO:0000313|EMBL:ADL45110.1}; OS Micromonospora aurantiaca (strain ATCC 27029 / DSM 43813 / BCRC 12538 OS / CBS 129.76 / JCM 10878 / NBRC 16125 / NRRL B-16091 / INA 9442). OC Bacteria; Actinobacteria; Micromonosporales; Micromonosporaceae; OC Micromonospora. OX NCBI_TaxID=644283 {ECO:0000313|EMBL:ADL45110.1, ECO:0000313|Proteomes:UP000001908}; RN [1] {ECO:0000313|EMBL:ADL45110.1, ECO:0000313|Proteomes:UP000001908} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 27029 / DSM 43813 / JCM 10878 / NBRC 16125 / INA 9442 RC {ECO:0000313|Proteomes:UP000001908}; RG US DOE Joint Genome Institute; RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L., RA Pitluck S., Chertkov O., Detter J.C., Han C., Tapia R., Land M., RA Hauser L., Chang Y.-J., Jeffries C., Kyrpides N., Ivanova N., RA Ovchinnikova G., Hirsch A.M., Woyke T.; RT "Complete sequence of Micromonospora aurantiaca ATCC 27029."; RL Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002162; ADL45110.1; -; Genomic_DNA. DR RefSeq; WP_013284748.1; NC_014391.1. DR ProteinModelPortal; D9SYS5; -. DR STRING; 644283.Micau_1552; -. DR EnsemblBacteria; ADL45110; ADL45110; Micau_1552. DR GeneID; 32162187; -. DR KEGG; mau:Micau_1552; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000001908; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000001908}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000001908}. FT DOMAIN 255 420 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 487 AA; 53584 MW; 224E877A8B7CDB9C CRC64; MREQETFHPY TDDEFDATTG EYELSERQAL RRVPGLSTEL TDITEVEYRQ LRLERVVLVG VWTEGTQSDA DNSLTELAAL AETAGSQVLE GLIQRRHRPD PATYIGRGKV DDLGAVALST GADTIICDGE LSPSQLRNLE QRTKVKVVDR TALILDIFAQ HAKSKEGKAQ VELAQLEYLL PRLRGWGETL SRQTGGSGRG GGAGGGVGLR GPGETKLETD RRRIRHRIAR LRREIKSMAT VRQTKRARRT RNAVPAVAIA GYTNAGKSSL LNRLTGAGVL VENALFATLD PTTRRATTSD GRLYTLSDTV GFVRHLPHQI VEAFRSTLEE VADADLVVHV VDGTHPDPEE QVRAVREVLA EVGADRLPEL LVVNKTDATD EETMLRLKRL WPDAVFVSAH SGRGIDEMRE AVERRLPRPA VEVRAVLPYD RGDLVSRVHR QGEVLSTAHL PEGTLVHVRV SEGLAAELAP YRAGDRLTSD ERVGAGR // ID D9UVL6_9ACTN Unreviewed; 481 AA. AC D9UVL6; DT 05-OCT-2010, integrated into UniProtKB/TrEMBL. DT 05-OCT-2010, sequence version 1. DT 07-JUN-2017, entry version 44. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=SSMG_01903 {ECO:0000313|EMBL:EFL06232.1}; OS Streptomyces sp. AA4. OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae; OC Streptomyces. OX NCBI_TaxID=591158 {ECO:0000313|EMBL:EFL06232.1, ECO:0000313|Proteomes:UP000003970}; RN [1] {ECO:0000313|EMBL:EFL06232.1, ECO:0000313|Proteomes:UP000003970} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=AA4 {ECO:0000313|EMBL:EFL06232.1, RC ECO:0000313|Proteomes:UP000003970}; RG The Broad Institute Genome Sequencing Platform; RG Broad Institute Microbial Sequencing Center; RA Fischbach M., Godfrey P., Ward D., Young S., Zeng Q., Koehrsen M., RA Alvarado L., Berlin A.M., Bochicchio J., Borenstein D., Chapman S.B., RA Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A., RA Gujja S., Heilman E.R., Heiman D.I., Hepburn T.A., Howarth C., Jen D., RA Larson L., Lewis B., Mehta T., Park D., Pearson M., Richards J., RA Roberts A., Saif S., Shea T.D., Shenoy N., Sisk P., Stolte C., RA Sykes S.N., Thomson T., Walk T., White J., Yandava C., Straight P., RA Clardy J., Hung D., Kolter R., Mekalanos J., Walker S., Walsh C.T., RA Wieland-Brown L.C., Haas B., Nusbaum C., Birren B.; RT "Annotation of Streptomyces sp. strain AA4."; RL Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GG657746; EFL06232.1; -; Genomic_DNA. DR RefSeq; WP_009075123.1; NZ_GG657746.1. DR ProteinModelPortal; D9UVL6; -. DR STRING; 591158.SSMG_01903; -. DR EnsemblBacteria; EFL06232; EFL06232; SSMG_01903. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000003970; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 2. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000003970}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000003970}. FT DOMAIN 254 423 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 481 AA; 52190 MW; CEC3B5F2BD8B0E92 CRC64; MTEQTHEDFY DDNDPYDPSV GEMELEDRAS LRRVAGLSTE LEDITEVEYR QLRLERVVLV GVWTEGTAQQ SEASLAELAR LAETAGSEVL EGLVQRRQKP DPATYVGSGK VRELRDVVVA TGADTVICDG ELSPGQLRQL EEKVKVKVID RTALILDIFA QHARSKEGKA QVELAQLQYL VPRLRGWGSA LSRQAGGRAG GANGGVGLRG PGETKLETDR RRISKRVAKL RREIAAMDTI RETKRGKRVA NEVPSVAIVG YTNAGKSSLL NALTGAGVLV EDALFATLDP TTRRAQTADG RTFTLTDTVG FVRHLPHQLV DAFRSTLEEA ADADLLLHVV DGSDAAPEDQ VNAVREVLAE ITRSRKEPLP PELLVINKAD AADDVTLARL RHALPGSVQI SARTGSGVAD LAEVLAERLP RAELVIDVLV PYSRGELVSR AHAEGEVLEE EHVADGTRLK VRVRADLAAA LRAFETNVSA L // ID D9W1L0_9ACTN Unreviewed; 501 AA. AC D9W1L0; DT 05-OCT-2010, integrated into UniProtKB/TrEMBL. DT 05-OCT-2010, sequence version 1. DT 05-JUL-2017, entry version 45. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=SSNG_05305 {ECO:0000313|EMBL:EFL18053.1}; OS Streptomyces sp. C. OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae; OC Streptomyces. OX NCBI_TaxID=253839 {ECO:0000313|EMBL:EFL18053.1, ECO:0000313|Proteomes:UP000005763}; RN [1] {ECO:0000313|EMBL:EFL18053.1, ECO:0000313|Proteomes:UP000005763} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C {ECO:0000313|EMBL:EFL18053.1, RC ECO:0000313|Proteomes:UP000005763}; RG The Broad Institute Genome Sequencing Platform; RG Broad Institute Microbial Sequencing Center; RA Fischbach M., Godfrey P., Ward D., Young S., Zeng Q., Koehrsen M., RA Alvarado L., Berlin A.M., Bochicchio J., Borenstein D., Chapman S.B., RA Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A., RA Gujja S., Heilman E.R., Heiman D.I., Hepburn T.A., Howarth C., Jen D., RA Larson L., Lewis B., Mehta T., Park D., Pearson M., Richards J., RA Roberts A., Saif S., Shea T.D., Shenoy N., Sisk P., Stolte C., RA Sykes S.N., Thomson T., Walk T., White J., Yandava C., Straight P., RA Clardy J., Hung D., Kolter R., Mekalanos J., Walker S., Walsh C.T., RA Wieland-Brown L.C., Haas B., Nusbaum C., Birren B.; RT "Annotation of Streptomyces sp. strain C."; RL Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GG657750; EFL18053.1; -; Genomic_DNA. DR ProteinModelPortal; D9W1L0; -. DR STRING; 253839.SSNG_05305; -. DR EnsemblBacteria; EFL18053; EFL18053; SSNG_05305. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000005763; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 2. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000005763}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000005763}. FT DOMAIN 280 445 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 501 AA; 54746 MW; 8593861287469A0C CRC64; MTSSSSPSQD PRDAQDVRDS QRFTESLRAD ALMEEDVAWS HEIDGERDGD QFDRSERAAL RRVAGLSTEL EDVTEVEYRQ LRLERVVLVG VWTSGTVQDA ENSLAELAAL AETAGALVLD GVMQRRDKPD PATFIGSGKA RELRDIVLES GADTVVCDGE LSPGQLIALE DVVKVKVVDR TALILDIFAQ HAKSREGKAQ VALAQMQYML PRLRGWGQSL SRQMGGGGGG GMATRGPGET KIETDRRRIR EKMAKMRREI AEMKTGRDIK RQERRRNKIP SVAIAGYTNA GKSSLLNRLT GAGVLVENAL FATLDPTVRR AETPSGRVYT LADTVGFVRH LPHHLVEAFR STMEEVGDSD LILHIVDGSH PAPEEQLAAV REVIREVGAV NVPEIVVINK ADAADPLVLQ RLLRIEKHSI AVSARTGQGI EELLALIDTE LPRPAVEVEA LVPYTRGSLV ARAHADGEVI SEEHTPEGTL LKARVHEELA AELAPYVPAK H // ID D9W9V7_9ACTN Unreviewed; 500 AA. AC D9W9V7; DT 05-OCT-2010, integrated into UniProtKB/TrEMBL. DT 05-OCT-2010, sequence version 1. DT 07-JUN-2017, entry version 45. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=SSOG_02485 {ECO:0000313|EMBL:EFL22771.1}; OS Streptomyces himastatinicus ATCC 53653. OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae; OC Streptomyces. OX NCBI_TaxID=457427 {ECO:0000313|EMBL:EFL22771.1, ECO:0000313|Proteomes:UP000003963}; RN [1] {ECO:0000313|EMBL:EFL22771.1, ECO:0000313|Proteomes:UP000003963} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 53653 {ECO:0000313|EMBL:EFL22771.1, RC ECO:0000313|Proteomes:UP000003963}; RG The Broad Institute Genome Sequencing Platform; RG Broad Institute Microbial Sequencing Center; RA Fischbach M., Godfrey P., Ward D., Young S., Zeng Q., Koehrsen M., RA Alvarado L., Berlin A.M., Bochicchio J., Borenstein D., Chapman S.B., RA Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A., RA Gujja S., Heilman E.R., Heiman D.I., Hepburn T.A., Howarth C., Jen D., RA Larson L., Lewis B., Mehta T., Park D., Pearson M., Richards J., RA Roberts A., Saif S., Shea T.D., Shenoy N., Sisk P., Stolte C., RA Sykes S.N., Thomson T., Walk T., White J., Yandava C., Straight P., RA Clardy J., Hung D., Kolter R., Mekalanos J., Walker S., Walsh C.T., RA Wieland-Brown L.C., Haas B., Nusbaum C., Birren B.; RT "Annotation of Streptomyces hygroscopicus strain ATCC 53653."; RL Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GG657754; EFL22771.1; -; Genomic_DNA. DR RefSeq; WP_009714592.1; NZ_GG657754.1. DR ProteinModelPortal; D9W9V7; -. DR STRING; 457427.SSOG_02485; -. DR EnsemblBacteria; EFL22771; EFL22771; SSOG_02485. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000003963; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 2. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000003963}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000003963}. FT DOMAIN 275 440 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 500 AA; 54671 MW; BAA547FB41C248AC CRC64; MTHSSSLPQD RQSLAESLRA DALMEEDVAW SHEIDGERDG DQYDRSDRAA LRRVAGLSTE LEDVTEVEYR QLRLERVVLV GVWTSGTAQD ADNSLAELAA LAETAGAVVL DGVIQRRNKP DPATYIGSGK AEELREIVIE SGADTVVCDG ELSPGQLIHL EDVVKVKVVD RTALILDIFA QHAKSREGKA QVSLAQMQYM LPRLRGWGQS LSRQMGGGGS GSSGGGMATR GPGETKIETD RRRIREKMAK MRREIAEMKT GRDIKRQERR RHKVPSVAIA GYTNAGKSSL LNRLTGAGVL VENALFATLD PTVRRAETPS GRLYTLADTV GFVRHLPHHL VEAFRSTMEE VGDADLILHV VDGSHPAPEE QLAAVREVIR DVGAVDVPEI VVINKADKAD PLVLQRLLRM ERSAMAVSAR SGQGIDELLE VIDHELPRPQ VEIEALVPYT EGKLVSRTHA DGEVISEEHT PEGTLLKARV HEELAAELRR FVPAAAGARQ // ID D9WY99_STRVT Unreviewed; 497 AA. AC D9WY99; DT 05-OCT-2010, integrated into UniProtKB/TrEMBL. DT 05-OCT-2010, sequence version 1. DT 07-JUN-2017, entry version 45. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=SSQG_05829 {ECO:0000313|EMBL:EFL35311.1}; OS Streptomyces viridochromogenes (strain DSM 40736 / JCM 4977 / BCRC OS 1201 / Tue 494). OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae; OC Streptomyces. OX NCBI_TaxID=591159 {ECO:0000313|EMBL:EFL35311.1, ECO:0000313|Proteomes:UP000004184}; RN [1] {ECO:0000313|EMBL:EFL35311.1, ECO:0000313|Proteomes:UP000004184} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 40736 / JCM 4977 / BCRC 1201 / Tue 494 RC {ECO:0000313|Proteomes:UP000004184}; RG The Broad Institute Genome Sequencing Platform; RG Broad Institute Microbial Sequencing Center; RA Fischbach M., Godfrey P., Ward D., Young S., Zeng Q., Koehrsen M., RA Alvarado L., Berlin A.M., Bochicchio J., Borenstein D., Chapman S.B., RA Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A., RA Gujja S., Heilman E.R., Heiman D.I., Hepburn T.A., Howarth C., Jen D., RA Larson L., Lewis B., Mehta T., Park D., Pearson M., Richards J., RA Roberts A., Saif S., Shea T.D., Shenoy N., Sisk P., Stolte C., RA Sykes S.N., Thomson T., Walk T., White J., Yandava C., Straight P., RA Clardy J., Hung D., Kolter R., Mekalanos J., Walker S., Walsh C.T., RA Wieland-Brown L.C., Haas B., Nusbaum C., Birren B.; RT "Annotation of Streptomyces viridochromogenes strain DSM 40736."; RL Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GG657757; EFL35311.1; -; Genomic_DNA. DR RefSeq; WP_003993435.1; NZ_GG657757.1. DR ProteinModelPortal; D9WY99; -. DR STRING; 591159.SSQG_05829; -. DR EnsemblBacteria; EFL35311; EFL35311; SSQG_05829. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000004184; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000004184}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000004184}. FT DOMAIN 275 440 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 497 AA; 54439 MW; 42B500663C68D787 CRC64; MTSSSSPSQD TKRFAHSHPE GLRADALMEE DVAWSHEIDG ERDGDQFDRS DRAALRRVAG LSTELEDVTE VEYRQLRLER VVLVGVWTTG TAQDADNSLA ELAALAETAG ALVLDGVIQR RDKPDAATYI GSGKAVELRD IVLETGADTV ICDGELSPGQ LIHLEDVVKV KVIDRTALIL DIFAQHAKSR EGKAQVALAQ MQYMLPRLRG WGQSLSRQMG GGKGGGLATR GPGETKIETD RRRIREKMAK MRREIAEMKT GREIKRQERK RHKVPSVAIA GYTNAGKSSL LNRLTGAGVL VENALFATLD PTVRRAETPS GRLYTLADTV GFVRHLPHHL VEAFRSTMEE VGESDLILHV VDGSHPNPEE QLAAVREVVR DVGATDVPEI VVINKADLAD PLTLQRLLRV EKRSIAVSAR TGRNIDQLLA LIDNELPRPS VEVEALVPYT HGKLVARAHD EGEVLSEEHT PEGTLLKVRV HEELAAELAP YVPAPLA // ID D9XTF2_9ACTN Unreviewed; 589 AA. AC D9XTF2; DT 05-OCT-2010, integrated into UniProtKB/TrEMBL. DT 05-OCT-2010, sequence version 1. DT 10-MAY-2017, entry version 44. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=SSRG_01520 {ECO:0000313|EMBL:EFL38716.1}; OS Streptomyces griseoflavus Tu4000. OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae; OC Streptomyces. OX NCBI_TaxID=467200 {ECO:0000313|EMBL:EFL38716.1, ECO:0000313|Proteomes:UP000002968}; RN [1] {ECO:0000313|EMBL:EFL38716.1, ECO:0000313|Proteomes:UP000002968} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Tu4000 {ECO:0000313|EMBL:EFL38716.1, RC ECO:0000313|Proteomes:UP000002968}; RG The Broad Institute Genome Sequencing Platform; RG Broad Institute Microbial Sequencing Center; RA Fischbach M., Godfrey P., Ward D., Young S., Zeng Q., Koehrsen M., RA Alvarado L., Berlin A.M., Bochicchio J., Borenstein D., Chapman S.B., RA Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A., RA Gujja S., Heilman E.R., Heiman D.I., Hepburn T.A., Howarth C., Jen D., RA Larson L., Lewis B., Mehta T., Park D., Pearson M., Richards J., RA Roberts A., Saif S., Shea T.D., Shenoy N., Sisk P., Stolte C., RA Sykes S.N., Thomson T., Walk T., White J., Yandava C., Straight P., RA Clardy J., Hung D., Kolter R., Mekalanos J., Walker S., Walsh C.T., RA Wieland-Brown L.C., Haas B., Nusbaum C., Birren B.; RT "Annotation of Streptomyces griseoflavus strain Tu4000."; RL Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GG657758; EFL38716.1; -; Genomic_DNA. DR ProteinModelPortal; D9XTF2; -. DR STRING; 467200.SSRG_01520; -. DR EnsemblBacteria; EFL38716; EFL38716; SSRG_01520. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000002968; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000002968}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000002968}. FT DOMAIN 275 440 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 589 AA; 63930 MW; 834E92CFC81FF0BF CRC64; MTSSSSPSQD TKRFAHTYPE GLRADALMEE DVAWSLDIDG ERDGDQFDRS ERAALRRVAG LSTELEDVTE VEYRQLRLER VVLVGVWTSG TVQDAENSLA ELAALAETAG ALVLDGVIQR RDKPDAATYI GSGKAEELRD VVLDTGADTV ICDGELSPGQ LIHLEDVVKV KVIDRTALIL DIFAQHAKSR EGKAQVALAQ MQYMLPRLRG WGQSLSRQMG GGKGGGLATR GPGETKIETD RRRIREKMAK MRREIAEMKT GREIKRQERR RHKVPSVAIA GYTNAGKSSL LNRLTGAGVL VENALFATLD PTVRRAETPS GRLYTLADTV GFVRHLPHHL VEAFRSTMEE VGDADLILHV VDGSHPVPEE QLAAVREVIR DVGATGVPEI VVINKADAAD PLTLQRLLRV EKRSIAVSAR TGRGMAELLA LHRRRAAPSV RGDRGTRAVH PRQAGRARPR RGRGDLRGAH RGGHPAQGAG ARGAGGGTHA VRAGPGRLTA RPKARPRTPR GRAFGMVRLT DRRRSCSCSG TAPRRPRRAA GRRARCCPAG RSRCWRPVPS CRPAPGTSRR RTSRRSSSSR CGTSSAGSG // ID E0CQI8_VITVI Unreviewed; 561 AA. AC E0CQI8; DT 05-OCT-2010, integrated into UniProtKB/TrEMBL. DT 05-OCT-2010, sequence version 1. DT 30-AUG-2017, entry version 46. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:CBI19757.3}; GN OrderedLocusNames=VIT_18s0001g13120 {ECO:0000313|EMBL:CBI19757.3}; OS Vitis vinifera (Grape). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae; OC Pentapetalae; rosids; Vitales; Vitaceae; Vitis. OX NCBI_TaxID=29760 {ECO:0000313|Proteomes:UP000009183}; RN [1] {ECO:0000313|Proteomes:UP000009183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Pinot noir / PN40024 {ECO:0000313|Proteomes:UP000009183}; RX PubMed=17721507; DOI=10.1038/nature06148; RG The French-Italian Public Consortium for Grapevine Genome Characterization.; RA Jaillon O., Aury J.-M., Noel B., Policriti A., Clepet C., RA Casagrande A., Choisne N., Aubourg S., Vitulo N., Jubin C., Vezzi A., RA Legeai F., Hugueney P., Dasilva C., Horner D., Mica E., Jublot D., RA Poulain J., Bruyere C., Billault A., Segurens B., Gouyvenoux M., RA Ugarte E., Cattonaro F., Anthouard V., Vico V., Del Fabbro C., RA Alaux M., Di Gaspero G., Dumas V., Felice N., Paillard S., Juman I., RA Moroldo M., Scalabrin S., Canaguier A., Le Clainche I., Malacrida G., RA Durand E., Pesole G., Laucou V., Chatelet P., Merdinoglu D., RA Delledonne M., Pezzotti M., Lecharny A., Scarpelli C., Artiguenave F., RA Pe M.E., Valle G., Morgante M., Caboche M., Adam-Blondon A.-F., RA Weissenbach J., Quetier F., Wincker P.; RT "The grapevine genome sequence suggests ancestral hexaploidization in RT major angiosperm phyla."; RL Nature 449:463-467(2007). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; FN595227; CBI19757.3; -; Genomic_DNA. DR ProteinModelPortal; E0CQI8; -. DR STRING; 29760.VIT_18s0001g13120.t01; -. DR PRIDE; E0CQI8; -. DR EnsemblPlants; VIT_18s0001g13120.t01; VIT_18s0001g13120.t01; VIT_18s0001g13120. DR Gramene; VIT_18s0001g13120.t01; VIT_18s0001g13120.t01; VIT_18s0001g13120. DR eggNOG; KOG0410; Eukaryota. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR InParanoid; E0CQI8; -. DR OMA; VILEIFH; -. DR OrthoDB; EOG093609UJ; -. DR Proteomes; UP000009183; Chromosome 18. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR GO; GO:0043022; F:ribosome binding; IBA:GO_Central. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000009183}; KW Reference proteome {ECO:0000313|Proteomes:UP000009183}. FT DOMAIN 338 504 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 561 AA; 62473 MW; 86839EB9958ECA0F CRC64; MKLRFPEERR GAMKATVSSC FSSISIIPPS SLVHDPHSPF PPVRLRSIPA FTLRTHTTTS FRLVRVLQRG VGLVSPDDLS LPEPVIDVKE EEVFAVVDGV AGTKAEEKTL KAPTRVKKKG GEGESDDNRF KLRNGREVFE EKAYLVAVEL KGDMEYSFGI EESLKELAQL ADTAGLMVVG STSQKLSTPN RRTYIGSGKV AEIKSAIHAL DVETVIFDDE LSAGQLRNLE KAFGGDVRVC DRTALILDIF NQRAATHEAA LQANVALAQM EYQLPRLTKM WTHLERQAGG KVKGMGEKQI EVDKRILRTQ IGALKKELES VRQHRKQYRN RRFSVPVPVV SLVGYTNAGK STLLNRLTGS NVLAEDRLFA TLDPTTRRVQ MKNGREFLLT DTVGFIQKLP TMLVAAFRAT LEEISESSLL VHVVDISHPL AEQQIDAVDK VLSELDVLSI PRLMVWNKVD KASNPQKIKL EAEKREDVVC ISALNGDGLN EFCNAVQEKL KDSMVWVEAL VPFDKGELLS TIHQVGMVER TEYTENGTLV KAHVPLRFAR LLTPMRQLCK S // ID E0DFH4_9CORY Unreviewed; 559 AA. AC E0DFH4; DT 02-NOV-2010, integrated into UniProtKB/TrEMBL. DT 02-NOV-2010, sequence version 1. DT 10-MAY-2017, entry version 39. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:EFM48831.1}; GN ORFNames=HMPREF0299_6618 {ECO:0000313|EMBL:EFM48831.1}; OS Corynebacterium matruchotii ATCC 14266. OC Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae; OC Corynebacterium. OX NCBI_TaxID=553207 {ECO:0000313|EMBL:EFM48831.1, ECO:0000313|Proteomes:UP000004218}; RN [1] {ECO:0000313|EMBL:EFM48831.1, ECO:0000313|Proteomes:UP000004218} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 14266 {ECO:0000313|EMBL:EFM48831.1, RC ECO:0000313|Proteomes:UP000004218}; RA Harkins D.M., Madupu R., Durkin A.S., Torralba M., Methe B., RA Sutton G.G., Nelson K.E.; RL Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EFM48831.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACSH02000005; EFM48831.1; -; Genomic_DNA. DR ProteinModelPortal; E0DFH4; -. DR STRING; 553207.HMPREF0299_6618; -. DR EnsemblBacteria; EFM48831; EFM48831; HMPREF0299_6618. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000004218; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000004218}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000004218}. FT DOMAIN 331 500 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 290 317 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 559 AA; 60288 MW; 7FF6479E3E1CCE05 CRC64; MPKNTSHQPY TQTTHTNTHE ELIKEAFKDH TLTTVSTDAT TPPANIAMVT TDDVVENHGV SVAATGAVSG MSADTAATGV LTASMPMVGV PTTGELDLEE RSSFRRISGS SDIYATDQDD GYDVEYRKLR LERVILVGVW TEGTTAEIEA TMRELAALAQ TAGSEVVDML YQKRDRPDPG TYIGSGKVQE LKDIVQATNI DTVICDGELS PGQMIALEKA LDVKVIDRTM LILDIFAQHA KSKEGKAQVS LAQMEYLITR VRGWGGALSR QAGGRAGGSN GGVGLRGPGE TKIEADRRRL RSDMAKLRKE IAGMQTAREI KRSRRRASTI PQIAIAGYTN AGKSSLINAI TGAGVLVEDA LFATLDPTTR RAELADGRTV VFTDTVGFVR HLPTQLVEAF RSTLEEVVGA DLVLHVVDGS DPFPLKQIAA VNKVIGEIVQ EYGETAPPEI IVVNKIDAAD PLVLVELRHA VDDVVFVSAH TGEGISELEA RIELFLNSLD SHVELLVPFT RGDVVSRVHQ YGTVLREEYT EAGTRIDVRL AAELAAELAE FQVSTDTAS // ID E0E2A8_9FIRM Unreviewed; 437 AA. AC E0E2A8; DT 02-NOV-2010, integrated into UniProtKB/TrEMBL. DT 02-NOV-2010, sequence version 1. DT 07-JUN-2017, entry version 40. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:EFM64961.1}; GN ORFNames=HMPREF0634_1238 {ECO:0000313|EMBL:EFM64961.1}; OS Peptostreptococcus stomatis DSM 17678. OC Bacteria; Firmicutes; Clostridia; Clostridiales; OC Peptostreptococcaceae; Peptostreptococcus. OX NCBI_TaxID=596315 {ECO:0000313|EMBL:EFM64961.1, ECO:0000313|Proteomes:UP000003244}; RN [1] {ECO:0000313|EMBL:EFM64961.1, ECO:0000313|Proteomes:UP000003244} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 17678 {ECO:0000313|EMBL:EFM64961.1, RC ECO:0000313|Proteomes:UP000003244}; RA Harkins D.M., Madupu R., Durkin A.S., Torralba M., Methe B., RA Sutton G.G., Nelson K.E.; RL Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EFM64961.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADGQ01000035; EFM64961.1; -; Genomic_DNA. DR RefSeq; WP_007789097.1; NZ_ADGQ01000035.1. DR ProteinModelPortal; E0E2A8; -. DR STRING; 596315.HMPREF0634_1238; -. DR EnsemblBacteria; EFM64961; EFM64961; HMPREF0634_1238. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000003244; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000003244}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000003244}. FT DOMAIN 212 382 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 437 AA; 49313 MW; 43536956A2B87BBF CRC64; MNDLNINNED IINLKEKALC VGLNLTSLVK KPDDIDIEDS MLELKELVQA AGAEVVGDLI QNRSSIDAAT YMGSGKIEEI KAYADSLNAS MVVFNDELSG AQIRNIEDIV GKKIIDRTTL ILDIFAQRAL SREGKLQVEL AQLKYRLPRL YGMGGQMSRT GAGIGTRGPG EQKLEKDKRH ILNRAANIRK ELKEVVKIRD IQRAQRSKNR VPIVALVGYT NAGKSTLLNE IIKTHPDYEK DKEVFVKDML FATLDVTLRK ALLPNKKEFL VVDTVGFVSK LPHDLVDAFK ATLEEVTYAD LILHIIDATN TSSDIQKSTT ESVLKDLKAD DKYTITVYNK IDKLDLDIYP RNQEDMVYLS AKKNINMDKL MDMIQKALDK DSYKVKLLLP YDQGNIFSSL SDKYAIEAFE YLDTGISVTL SLDEIDYNKY KKYIEIQ // ID E0I531_9BACL Unreviewed; 429 AA. AC E0I531; DT 02-NOV-2010, integrated into UniProtKB/TrEMBL. DT 02-NOV-2010, sequence version 1. DT 07-JUN-2017, entry version 45. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=PaecuDRAFT_0753 {ECO:0000313|EMBL:EFM12073.1}; OS Paenibacillus curdlanolyticus YK9. OC Bacteria; Firmicutes; Bacilli; Bacillales; Paenibacillaceae; OC Paenibacillus. OX NCBI_TaxID=717606 {ECO:0000313|EMBL:EFM12073.1, ECO:0000313|Proteomes:UP000005387}; RN [1] {ECO:0000313|EMBL:EFM12073.1, ECO:0000313|Proteomes:UP000005387} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=YK9 {ECO:0000313|EMBL:EFM12073.1, RC ECO:0000313|Proteomes:UP000005387}; RG US DOE Joint Genome Institute (JGI-PGF); RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L., RA Pitluck S., Land M.L., Hauser L., Chang Y.-J., Jeffries C., RA Anderson I.J., Johnson E., Loganathan U., Mulhopadhyay B., RA Kyrpides N., Woyke T.J.; RT "The draft genome of Paenibacillus curdlanolyticus YK9."; RL Submitted (JUL-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AEDD01000002; EFM12073.1; -; Genomic_DNA. DR RefSeq; WP_006036768.1; NZ_AEDD01000002.1. DR ProteinModelPortal; E0I531; -. DR STRING; 717606.PaecuDRAFT_0753; -. DR EnsemblBacteria; EFM12073; EFM12073; PaecuDRAFT_0753. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000005387; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000005387}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000005387}. FT DOMAIN 208 372 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 429 AA; 47620 MW; FB41D13839F99712 CRC64; MRNITHDVEH GLAECAILVS LVTPDDKRGG MNPEHSLDEL ANLAETAGVE VLATMTQNKE AKDSRWFIGK GKVEELRVIA EELGATTAIF DQELSGAQVR NLEEALDLKI IDRTQLILDI FAQRAKTREG IIQVELAQLS YLLPRLSGHG KNLSRLGGGI GTRGPGESKL ETDRRHIRDR ISDLKGVLEE VVRHRKLHRE RRKKAGVVQV ALVGYTNAGK STLLREMTDA EVYVENQLFA TLDPTSRLLE LPSGKEIVLT DTVGFIQNLP HDLVAAFRAT LEEVCEADLV LHVVDSSSPT RADQMRVVDE VLDQLGAAGK PTLTVYNKRD LCPSEERELL PNGGGSMVIS AYDRSDLDRL RQAIQDHLTG DTRTFAVPAD RGDLIALVYR TGEVQSQEVE EEQLLLTVEL NKADFEKHIK TLEPYMVTE // ID E0ID11_9BACL Unreviewed; 425 AA. AC E0ID11; DT 02-NOV-2010, integrated into UniProtKB/TrEMBL. DT 02-NOV-2010, sequence version 1. DT 07-JUN-2017, entry version 42. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=PaecuDRAFT_3513 {ECO:0000313|EMBL:EFM09466.1}; OS Paenibacillus curdlanolyticus YK9. OC Bacteria; Firmicutes; Bacilli; Bacillales; Paenibacillaceae; OC Paenibacillus. OX NCBI_TaxID=717606 {ECO:0000313|EMBL:EFM09466.1, ECO:0000313|Proteomes:UP000005387}; RN [1] {ECO:0000313|EMBL:EFM09466.1, ECO:0000313|Proteomes:UP000005387} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=YK9 {ECO:0000313|EMBL:EFM09466.1, RC ECO:0000313|Proteomes:UP000005387}; RG US DOE Joint Genome Institute (JGI-PGF); RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L., RA Pitluck S., Land M.L., Hauser L., Chang Y.-J., Jeffries C., RA Anderson I.J., Johnson E., Loganathan U., Mulhopadhyay B., RA Kyrpides N., Woyke T.J.; RT "The draft genome of Paenibacillus curdlanolyticus YK9."; RL Submitted (JUL-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AEDD01000010; EFM09466.1; -; Genomic_DNA. DR RefSeq; WP_006039501.1; NZ_AEDD01000010.1. DR ProteinModelPortal; E0ID11; -. DR STRING; 717606.PaecuDRAFT_3513; -. DR EnsemblBacteria; EFM09466; EFM09466; PaecuDRAFT_3513. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000005387; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000005387}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000005387}. FT DOMAIN 198 366 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 157 191 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 425 AA; 47869 MW; 1DA6C8FA5EF05012 CRC64; MEPVNNRAVI VGVNLQNRPD FAYSMEELRN LADACNIEVV GELTQNAAKV NGPHYIGSGK IQELLALVEG LDASTVIFND ELSPSQIRNL ESSLEKKVID RTILILDIFG ERARTREAQL QVEVAQLQYM LPRLVGLRES LGRQGGGSGM KNKGTGETKL ELDRRRIEER ITALQSELEK LVAQRQVQRK QRQKTGVPVV CLVGYTNAGK SSLLNAVLKE FMPESNKQVL AKDMLFATLE TSVRGIELPD NKSFLLTDTV GFVSKLPHYL IKAFRSTLEE VTEADLLIQV VDFSNEEYER HIQVTNTTLK ELGADHIPMI YAYNKTDLTD EQYPQVNGDK VYLSVKEEAG LSELITLVKQ QIFQDYMSCE VIIPFEEGRL VAYFNANANV IATDYEPNGT RLTMECRKAD YEKYQHLFVE PVTEA // ID E0MK14_9RHOB Unreviewed; 455 AA. AC E0MK14; DT 02-NOV-2010, integrated into UniProtKB/TrEMBL. DT 02-NOV-2010, sequence version 1. DT 07-JUN-2017, entry version 40. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:EFL90143.1}; GN ORFNames=R2A130_0212 {ECO:0000313|EMBL:EFL90143.1}; OS Ahrensia sp. R2A130. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae; Ahrensia. OX NCBI_TaxID=744979 {ECO:0000313|EMBL:EFL90143.1, ECO:0000313|Proteomes:UP000003904}; RN [1] {ECO:0000313|EMBL:EFL90143.1, ECO:0000313|Proteomes:UP000003904} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=R2A130 {ECO:0000313|EMBL:EFL90143.1, RC ECO:0000313|Proteomes:UP000003904}; RA Suzuki M., Ferriera S., Johnson J., Kravitz S., Beeson K., Sutton G., RA Rogers Y.-H., Friedman R., Frazier M., Venter J.C.; RL Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EFL90143.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AEEB01000003; EFL90143.1; -; Genomic_DNA. DR ProteinModelPortal; E0MK14; -. DR STRING; 744979.R2A130_0212; -. DR EnsemblBacteria; EFL90143; EFL90143; R2A130_0212. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000003904; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000003904}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000003904}. FT DOMAIN 233 404 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 192 226 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 455 AA; 49385 MW; 4BF7F168FBA14B98 CRC64; MSSPDSFESA GKPRFQLDTT NERPVTKALV LSPVIASRAT SKADKERVHA RSEAARLDEA VGLARAIDLE IVHSASVPLS KLKAGTLFGT GKVEELKGLI AALDAGLVVV DHPLTPVQQR NLEKEWQAKV VDRTGLILEI FGARAQTKEG RLQVELAHLN YQKGRLVRSW THLERQRGGG GGSGGFLGGP GETQIESDRR QLQGKVNALE KELEKVRRTR TLHRSQRKRI PHPVVALVGY TNAGKSTLFN SLTGAEVMAK DMLFATLDPT LRQLHLPQGT QAILSDTVGF VSDLPTHLVA AFRATLEEVI EAELILHVRD ISDSDTKAQA EDVYTILSQL GVGEDGHSRV VEVWNKIDLL DAEALEAIRA TRTGNDAPLL VSAVTGEGEG SLLELVEDKL GGSENVVDVV LAPAKLGQLN WFYENAHVIE RTDREDGSVA ITVRVAPALR AQMPN // ID E0NI95_PEDAC Unreviewed; 327 AA. AC E0NI95; DT 02-NOV-2010, integrated into UniProtKB/TrEMBL. DT 02-NOV-2010, sequence version 1. DT 07-JUN-2017, entry version 35. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:EFL94858.1}; GN ORFNames=HMPREF0623_1726 {ECO:0000313|EMBL:EFL94858.1}; OS Pediococcus acidilactici DSM 20284. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; OC Pediococcus; Pediococcus acidilactici group. OX NCBI_TaxID=862514 {ECO:0000313|EMBL:EFL94858.1, ECO:0000313|Proteomes:UP000004470}; RN [1] {ECO:0000313|EMBL:EFL94858.1, ECO:0000313|Proteomes:UP000004470} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 20284 {ECO:0000313|EMBL:EFL94858.1, RC ECO:0000313|Proteomes:UP000004470}; RA Muzny D., Qin X., Deng J., Jiang H., Liu Y., Qu J., Song X.-Z., RA Zhang L., Thornton R., Coyle M., Francisco L., Jackson L., Javaid M., RA Korchina V., Kovar C., Mata R., Mathew T., Ngo R., Nguyen L., RA Nguyen N., Okwuonu G., Ongeri F., Pham C., Simmons D., RA Wilczek-Boney K., Hale W., Jakkamsetti A., Pham P., Ruth R., RA San Lucas F., Warren J., Zhang J., Zhao Z., Zhou C., Zhu D., Lee S., RA Bess C., Blankenburg K., Forbes L., Fu Q., Gubbala S., Hirani K., RA Jayaseelan J.C., Lara F., Munidasa M., Palculict T., Patil S., RA Pu L.-L., Saada N., Tang L., Weissenberger G., Zhu Y., Hemphill L., RA Shang Y., Youmans B., Ayvaz T., Ross M., Santibanez J., Aqrawi P., RA Gross S., Joshi V., Fowler G., Nazareth L., Reid J., Worley K., RA Petrosino J., Highlander S., Gibbs R.; RL Submitted (JUL-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EFL94858.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AEEG01000009; EFL94858.1; -; Genomic_DNA. DR ProteinModelPortal; E0NI95; -. DR STRING; 862514.HMPREF0623_1726; -. DR EnsemblBacteria; EFL94858; EFL94858; HMPREF0623_1726. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000004470; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000004470}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}. FT DOMAIN 203 327 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 327 AA; 36797 MW; 666C8D6065F303D9 CRC64; MNEEINEEPI IIAGLELPGV NLDYAMAELK SLASANHMRV MDQLTQKLER PNAATYFGKG KIEELTQVAA AREVETLVVN DELTPSQLSN LEKETQLRVI DRTGLILEIF ANRARSKEAR LQVELAKLQY QLPRLRTSAT QRLDQQTAGN TGGGFTNRGA GETKLELNRR TIRNRINHIN QELKEMSTSA NVQRQRRDKK DIPSVALVGY TNTGKSTTMN GLISMYGRNE DKQVFEKDML FATLDTSVRK LTFPDQKELI LSDTVGFVSN LPHQLVKAFR STLSEAAKAD LLVQVVDVSD PHYRDTITRS PERLPSGLYR SKQSRPE // ID E0NM01_9FIRM Unreviewed; 420 AA. AC E0NM01; DT 02-NOV-2010, integrated into UniProtKB/TrEMBL. DT 02-NOV-2010, sequence version 1. DT 07-JUN-2017, entry version 38. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:EFM25212.1}; GN ORFNames=HMPREF9225_1101 {ECO:0000313|EMBL:EFM25212.1}; OS Peptoniphilus duerdenii ATCC BAA-1640. OC Bacteria; Firmicutes; Tissierellia; Tissierellales; Peptoniphilaceae; OC Peptoniphilus. OX NCBI_TaxID=862517 {ECO:0000313|EMBL:EFM25212.1, ECO:0000313|Proteomes:UP000003280}; RN [1] {ECO:0000313|EMBL:EFM25212.1, ECO:0000313|Proteomes:UP000003280} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-1640 {ECO:0000313|EMBL:EFM25212.1, RC ECO:0000313|Proteomes:UP000003280}; RA Muzny D., Qin X., Deng J., Jiang H., Liu Y., Qu J., Song X.-Z., RA Zhang L., Thornton R., Coyle M., Francisco L., Jackson L., Javaid M., RA Korchina V., Kovar C., Mata R., Mathew T., Ngo R., Nguyen L., RA Nguyen N., Okwuonu G., Ongeri F., Pham C., Simmons D., RA Wilczek-Boney K., Hale W., Jakkamsetti A., Pham P., Ruth R., RA San Lucas F., Warren J., Zhang J., Zhao Z., Zhou C., Zhu D., Lee S., RA Bess C., Blankenburg K., Forbes L., Fu Q., Gubbala S., Hirani K., RA Jayaseelan J.C., Lara F., Munidasa M., Palculict T., Patil S., RA Pu L.-L., Saada N., Tang L., Weissenberger G., Zhu Y., Hemphill L., RA Shang Y., Youmans B., Ayvaz T., Ross M., Santibanez J., Aqrawi P., RA Gross S., Joshi V., Fowler G., Nazareth L., Reid J., Worley K., RA Petrosino J., Highlander S., Gibbs R.; RL Submitted (JUL-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EFM25212.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AEEH01000043; EFM25212.1; -; Genomic_DNA. DR ProteinModelPortal; E0NM01; -. DR STRING; 862517.HMPREF9225_1101; -. DR EnsemblBacteria; EFM25212; EFM25212; HMPREF9225_1101. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000003280; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000003280}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000003280}. FT DOMAIN 201 368 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 160 187 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 420 AA; 47659 MW; 890988E2FBA9121B CRC64; MEYIENLKKK EKVILVGTDL GALPNSLSSS MEELRELVEA DGGEVMGVVT QNIEKFSPKF LIGSGKVNEI KEIAKNMEVE TIIFNDELTG IQLRNLEKEL KLKIVDRTNL ILDIFALRAN TYEGKLQVLL AKREYEMPRL LGIKGWSRTG GGIGTRGPGE QIIETDRRRL QREIDSIRDK LKVAEKNRET RSKRRMESRL PIVSLVGYTN AGKSTILNRI KNSNSREVFV KNMLFATLDP NSRKSKLLNG RDFIISDTVG FVSKLPTKLI EAFKSTLEEI RGSDLIVHVM DASSSDIEIQ YKTTMNILKD IGVMDVPILT VYNKMDRAEL EDIILPQVDG DYIFISAKHD ENMDKLLNAI EKCLNIKYQE VSLLFPYSKT DVLDRFLSGV EAISVEYLAE GTKVRAILNE NEIREYGEFL // ID E0NPN9_9BACT Unreviewed; 417 AA. AC E0NPN9; DT 02-NOV-2010, integrated into UniProtKB/TrEMBL. DT 02-NOV-2010, sequence version 1. DT 07-JUN-2017, entry version 42. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:EFM02998.1}; GN ORFNames=HMPREF0658_0140 {ECO:0000313|EMBL:EFM02998.1}; OS Prevotella marshii DSM 16973 = JCM 13450. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Prevotellaceae; OC Prevotella. OX NCBI_TaxID=862515 {ECO:0000313|EMBL:EFM02998.1, ECO:0000313|Proteomes:UP000004394}; RN [1] {ECO:0000313|EMBL:EFM02998.1, ECO:0000313|Proteomes:UP000004394} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 16973 {ECO:0000313|EMBL:EFM02998.1, RC ECO:0000313|Proteomes:UP000004394}; RA Muzny D., Qin X., Deng J., Jiang H., Liu Y., Qu J., Song X.-Z., RA Zhang L., Thornton R., Coyle M., Francisco L., Jackson L., Javaid M., RA Korchina V., Kovar C., Mata R., Mathew T., Ngo R., Nguyen L., RA Nguyen N., Okwuonu G., Ongeri F., Pham C., Simmons D., RA Wilczek-Boney K., Hale W., Jakkamsetti A., Pham P., Ruth R., RA San Lucas F., Warren J., Zhang J., Zhao Z., Zhou C., Zhu D., Lee S., RA Bess C., Blankenburg K., Forbes L., Fu Q., Gubbala S., Hirani K., RA Jayaseelan J.C., Lara F., Munidasa M., Palculict T., Patil S., RA Pu L.-L., Saada N., Tang L., Weissenberger G., Zhu Y., Hemphill L., RA Shang Y., Youmans B., Ayvaz T., Ross M., Santibanez J., Aqrawi P., RA Gross S., Joshi V., Fowler G., Nazareth L., Reid J., Worley K., RA Petrosino J., Highlander S., Gibbs R.; RL Submitted (JUL-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EFM02998.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AEEI01000004; EFM02998.1; -; Genomic_DNA. DR RefSeq; WP_006947821.1; NZ_GL397214.1. DR ProteinModelPortal; E0NPN9; -. DR STRING; 862515.HMPREF0658_0140; -. DR EnsemblBacteria; EFM02998; EFM02998; HMPREF0658_0140. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000004394; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000004394}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000004394}. FT DOMAIN 216 400 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 417 AA; 47747 MW; 75AB5DD21D75582B CRC64; MKEFVISEVK AETAILVGLI TKEQDEAKTK EYLDELQFLA DTAGAVTVKR FTQKLAAPSQ VTYVGKGKLE EIKQYIIDRE EAEHPVGMVI FDDELSAKQM RNIEKELKVK ILDRTSLILD IFAMRAQTAN AKTQVELAQY RYMLPRLQRL WTHLERQGGG SGSGGGKGSV GLRGPGETQL EMDRRIILQR ITLLKQRLVE IDRQKTTQRK NRGRMIRVAL VGYTNVGKST LMNLISKSEV FAENKLFATL DTTVRKVVIE NLPFLLADTV GFIRKLPTDL VESFKSTLDE VREADMLLHV VDISHPDFEE QIRVVENTLK DLGCSEKPSI IVFNKIDAYT WVEKEDDDLT PPTKENMTLE ELKKTWMARL QENCLFISAK EKTNVEEFKT TLYAKVKELH VQKYPYNDFL YSMEEEA // ID E0QQX8_9ACTO Unreviewed; 513 AA. AC E0QQX8; DT 02-NOV-2010, integrated into UniProtKB/TrEMBL. DT 02-NOV-2010, sequence version 1. DT 07-JUN-2017, entry version 43. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:EFM45971.1}; GN ORFNames=HMPREF0580_1293 {ECO:0000313|EMBL:EFM45971.1}; OS Mobiluncus mulieris ATCC 35239. OC Bacteria; Actinobacteria; Actinomycetales; Actinomycetaceae; OC Mobiluncus. OX NCBI_TaxID=871571 {ECO:0000313|EMBL:EFM45971.1, ECO:0000313|Proteomes:UP000003045}; RN [1] {ECO:0000313|EMBL:EFM45971.1, ECO:0000313|Proteomes:UP000003045} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 35239 {ECO:0000313|EMBL:EFM45971.1, RC ECO:0000313|Proteomes:UP000003045}; RA Muzny D., Qin X., Deng J., Jiang H., Liu Y., Qu J., Song X.-Z., RA Zhang L., Thornton R., Coyle M., Francisco L., Jackson L., Javaid M., RA Korchina V., Kovar C., Mata R., Mathew T., Ngo R., Nguyen L., RA Nguyen N., Okwuonu G., Ongeri F., Pham C., Simmons D., RA Wilczek-Boney K., Hale W., Jakkamsetti A., Pham P., Ruth R., RA San Lucas F., Warren J., Zhang J., Zhao Z., Zhou C., Zhu D., Lee S., RA Bess C., Blankenburg K., Forbes L., Fu Q., Gubbala S., Hirani K., RA Jayaseelan J.C., Lara F., Munidasa M., Palculict T., Patil S., RA Pu L.-L., Saada N., Tang L., Weissenberger G., Zhu Y., Hemphill L., RA Shang Y., Youmans B., Ayvaz T., Ross M., Santibanez J., Aqrawi P., RA Gross S., Joshi V., Fowler G., Nazareth L., Reid J., Worley K., RA Petrosino J., Highlander S., Gibbs R.; RL Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EFM45971.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AEET01000032; EFM45971.1; -; Genomic_DNA. DR RefSeq; WP_004015695.1; NZ_GL405260.1. DR ProteinModelPortal; E0QQX8; -. DR EnsemblBacteria; EFM45971; EFM45971; HMPREF0580_1293. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000003045; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000003045}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000003045}. FT DOMAIN 262 428 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 513 AA; 56336 MW; B9D9ACFD2B718660 CRC64; MDGWRDPGNE TGRKTWPEGG NQREQQYLRD QAARWEERYA LSRGESLGAE LSDISEVEYR EVRLEKVVLV GIFQTDRDKA EYSLRELAAL AQTAGAKVLA GITQRRESPD AATFLGIGKA KELRALVASL EADTVIVDDE LAPSQRRGLE DVVKVKVIDR TAVILDIFAQ HATSREGKAE VELAQLEYLL PRLRGWGESM SRQAGGRAAG GEGIGSRGPG ETKIELDRRR IRTRMSRLRR LLREMAPTRE AKRAARRAGG VPAVAIVGYT NAGKSSLLNR LAGADVLVHD ALFATLDPSV RKTHTATGRV YTLADTVGFV RRLPTQLVEA FRSTLEETAM ADLLLHVVDA ANPDPMGEIE AVNATLDTIE SIRHTPVVMV INKVDAASAP TLALLRRLLP EAVEVSARSG QGIERLQEVI ASRLPWPQQR VRVLVRWENT GLLERIYREG SLVSQETRVD GTFVDAWVEP ALAARLLNQA LGATLDKPVA DEAKCSTPGM APHEPPVNTE RIT // ID E0RWY6_BUTPB Unreviewed; 444 AA. AC E0RWY6; DT 02-NOV-2010, integrated into UniProtKB/TrEMBL. DT 02-NOV-2010, sequence version 1. DT 07-JUN-2017, entry version 52. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:ADL34894.1}; GN OrderedLocusNames=bpr_I2161 {ECO:0000313|EMBL:ADL34894.1}; OS Butyrivibrio proteoclasticus (strain ATCC 51982 / DSM 14932 / B316) OS (Clostridium proteoclasticum). OC Bacteria; Firmicutes; Clostridia; Clostridiales; Lachnospiraceae; OC Butyrivibrio. OX NCBI_TaxID=515622 {ECO:0000313|EMBL:ADL34894.1, ECO:0000313|Proteomes:UP000001299}; RN [1] {ECO:0000313|EMBL:ADL34894.1, ECO:0000313|Proteomes:UP000001299} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51982 / DSM 14932 / B316 RC {ECO:0000313|Proteomes:UP000001299}; RX PubMed=20689770; DOI=10.1371/journal.pone.0011942; RA Kelly W.J., Leahy S.C., Altermann E., Yeoman C.J., Dunne J.C., RA Kong Z., Pacheco D.M., Li D., Noel S.J., Moon C.D., Cookson A.L., RA Attwood G.T.; RT "The glycobiome of the rumen bacterium Butyrivibrio proteoclasticus RT B316(T) highlights adaptation to a polysaccharide-rich environment."; RL PLoS ONE 5:E11942-E11942(2010). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001810; ADL34894.1; -; Genomic_DNA. DR RefSeq; WP_013281548.1; NC_014387.1. DR ProteinModelPortal; E0RWY6; -. DR STRING; 515622.bpr_I2161; -. DR PRIDE; E0RWY6; -. DR EnsemblBacteria; ADL34894; ADL34894; bpr_I2161. DR GeneID; 31783294; -. DR KEGG; bpb:bpr_I2161; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; FNNHAHV; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000001299; Chromosome 1. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000001299}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000001299}. FT DOMAIN 209 348 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 168 202 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 444 AA; 49990 MW; 52483CEE5A57A8B8 CRC64; MKNVIHQIVE DVVETRAVLV GLNTDKTDDE FERSMNELKE LTKALDIIVA CTTTQNLPTP DRSTYVGSGK VEEIKGAVEM FDASIVIFNG DISPMQIRNL EKILDTEVID RTGLILQIFA KRAKTRESRL QVEYAQLQYM LPRLVGMRSS LSRQGGGSGR LSNKGSGEKQ LELDRRRIEH RMAELRRELE AVEKERDTQR GKRVNSGIPK VSLVGYTNAG KSTIMNNLLR LYGGETSDDK QVLEKDMLFA TLDTSVRKIT APGHRPFLLT DTVGFISELP HSLVKAFRST LEEAKYADIL LQVIDFSDPE YRFHMDVTRD TLAEIGAGDI PVIYVFNKSD QVQDEQRENG QLVMEVPRSI DDRAYICAKD QDSLDTLISL IESHLGKADT LCEMLLPYSE GGLLSFLNEA GKIKSTEYLP EGVKVSALLT RTEIDKYEEM IEMD // ID E0SH70_DICD3 Unreviewed; 426 AA. AC E0SH70; DT 02-NOV-2010, integrated into UniProtKB/TrEMBL. DT 02-NOV-2010, sequence version 1. DT 30-AUG-2017, entry version 52. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:ADN00163.1}; GN OrderedLocusNames=Dda3937_00433 {ECO:0000313|EMBL:ADN00163.1}; OS Dickeya dadantii (strain 3937) (Erwinia chrysanthemi (strain 3937)). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; OC Pectobacteriaceae; Dickeya. OX NCBI_TaxID=198628 {ECO:0000313|EMBL:ADN00163.1, ECO:0000313|Proteomes:UP000006859}; RN [1] {ECO:0000313|EMBL:ADN00163.1, ECO:0000313|Proteomes:UP000006859} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=3937 {ECO:0000313|EMBL:ADN00163.1, RC ECO:0000313|Proteomes:UP000006859}; RX PubMed=21217001; DOI=10.1128/JB.01513-10; RA Glasner J.D., Yang C.H., Reverchon S., Hugouvieux-Cotte-Pattat N., RA Condemine G., Bohin J.P., Van Gijsegem F., Yang S., Franza T., RA Expert D., Plunkett G. III, San Francisco M.J., Charkowski A.O., RA Py B., Bell K., Rauscher L., Rodriguez-Palenzuela P., Toussaint A., RA Holeva M.C., He S.Y., Douet V., Boccara M., Blanco C., Toth I., RA Anderson B.D., Biehl B.S., Mau B., Flynn S.M., Barras F., RA Lindeberg M., Birch P.R., Tsuyumu S., Shi X., Hibbing M., Yap M.N., RA Carpentier M., Dassa E., Umehara M., Kim J.F., Rusch M., Soni P., RA Mayhew G.F., Fouts D.E., Gill S.R., Blattner F.R., Keen N.T., RA Perna N.T.; RT "Genome sequence of the plant-pathogenic bacterium Dickeya dadantii RT 3937."; RL J. Bacteriol. 193:2076-2077(2011). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002038; ADN00163.1; -; Genomic_DNA. DR RefSeq; WP_013319582.1; NC_014500.1. DR ProteinModelPortal; E0SH70; -. DR STRING; 198628.Dda3937_00433; -. DR EnsemblBacteria; ADN00163; ADN00163; Dda3937_00433. DR GeneID; 9735442; -. DR KEGG; ddd:Dda3937_00433; -. DR PATRIC; fig|198628.6.peg.3905; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000006859; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000006859}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000006859}. FT DOMAIN 198 365 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 426 AA; 48289 MW; B14A9A29895E01E4 CRC64; MFDRYEAGEQ AILVHIYFSQ EKDTEDLLEF ESLVSSAGID ALQVITGSRK APHSKYFVGE GKAEEIAQAV KATGAFVVLF NHALTPAQER NLERLCECRV IDRTGLILDI FAQRARTHEG KLQVELAQLR HLATRLVRGW THLERQKGGI GLRGPGETQL ETDRRLLRNR ISQILSRLEK VEKQREQGRR ARTRAEVPTV SLVGYTNAGK STLFNRMTSA DVYAADQLFA TLDPTLRRIS VDDVGDTVLA DTVGFIRELP HDLVAAFKAT LQETREATLL LHVVDASDAR VDENIDAVNE VLAEIEADDI PFMLVMNKID RQENVEPRID RDEENRPIRV WLSAQTGEGI PLLLQALTER LSGEIAHYSL HLPPQAGRLR SRFYQLQAIE KEWIEEDGSV GLVVRMPIID WRRLCKQEQK LQDYIV // ID E0SPT3_IGNAA Unreviewed; 359 AA. AC E0SPT3; DT 02-NOV-2010, integrated into UniProtKB/TrEMBL. DT 02-NOV-2010, sequence version 1. DT 07-JUN-2017, entry version 54. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Igag_0103 {ECO:0000313|EMBL:ADM26955.1}; OS Ignisphaera aggregans (strain DSM 17230 / JCM 13409 / AQ1.S1). OC Archaea; Crenarchaeota; Thermoprotei; Desulfurococcales; OC Desulfurococcaceae; Ignisphaera. OX NCBI_TaxID=583356 {ECO:0000313|EMBL:ADM26955.1, ECO:0000313|Proteomes:UP000001304}; RN [1] {ECO:0000313|EMBL:ADM26955.1, ECO:0000313|Proteomes:UP000001304} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 17230 / JCM 13409 / AQ1.S1 RC {ECO:0000313|Proteomes:UP000001304}; RX PubMed=21304693; DOI=10.4056/sigs.1072907; RA Goker M., Held B., Lapidus A., Nolan M., Spring S., Yasawong M., RA Lucas S., Glavina Del Rio T., Tice H., Cheng J.F., Goodwin L., RA Tapia R., Pitluck S., Liolios K., Ivanova N., Mavromatis K., RA Mikhailova N., Pati A., Chen A., Palaniappan K., Brambilla E., RA Land M., Hauser L., Chang Y.J., Jeffries C.D., Brettin T., RA Detter J.C., Han C., Rohde M., Sikorski J., Woyke T., Bristow J., RA Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.; RT "Complete genome sequence of Ignisphaera aggregans type strain RT (AQ1.S1)."; RL Stand. Genomic Sci. 3:66-75(2010). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002098; ADM26955.1; -; Genomic_DNA. DR ProteinModelPortal; E0SPT3; -. DR STRING; 583356.Igag_0103; -. DR EnsemblBacteria; ADM26955; ADM26955; Igag_0103. DR KEGG; iag:Igag_0103; -. DR eggNOG; arCOG00353; Archaea. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; FNNHAHV; -. DR OrthoDB; POG093Z07D6; -. DR Proteomes; UP000001304; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000001304}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000001304}. FT DOMAIN 185 359 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 151 178 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 359 AA; 40985 MW; 1A1283FC12606AC2 CRC64; MKEPAILILR YDDLEYIDEI LSIASEAGLE VKETLTIKKI DSRCFLTPGK ILRLKYLINN NGIKKLCIYD DLKPRQVSCL LKELGIDIID RVMLILSVFQ RHAGSKEALM QIEIARLKHE IPLIRDWIKR AKTGELPGFL SLGRYAIDVY YRHIKRRISK LNKELAQMRI KRESERAKRK DLGFIHVSIV GYTNAGKTTL FNVLSNLDKP TGTEMFTTLS TKISTLKICG KTFALIDTVG FIRKIPVTII ESFKAVLEEI SYSDLILLVV DISKDEEKLL DEIHTSIEIL RTIGAIGKPI VLILNKIDLV NDNSIDKKIY SVLKNVKDKD INIIDYVPIS ALNRTNIDRV KEVLCKYAE // ID E0TDY0_PARBH Unreviewed; 469 AA. AC E0TDY0; DT 02-NOV-2010, integrated into UniProtKB/TrEMBL. DT 02-NOV-2010, sequence version 1. DT 07-JUN-2017, entry version 48. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=PB2503_11929 {ECO:0000313|EMBL:ADM10429.1}; OS Parvularcula bermudensis (strain ATCC BAA-594 / HTCC2503 / KCTC OS 12087). OC Bacteria; Proteobacteria; Alphaproteobacteria; Parvularculales; OC Parvularculaceae; Parvularcula. OX NCBI_TaxID=314260 {ECO:0000313|EMBL:ADM10429.1, ECO:0000313|Proteomes:UP000001302}; RN [1] {ECO:0000313|Proteomes:UP000001302} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-594 / HTCC2503 / KCTC 12087 RC {ECO:0000313|Proteomes:UP000001302}; RA Kang D.-M., Oh H.-M., Cho J.-C.; RT "Genome sequence of Parvularcula bermudensis HTCC2503."; RL Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002156; ADM10429.1; -; Genomic_DNA. DR ProteinModelPortal; E0TDY0; -. DR STRING; 314260.PB2503_11929; -. DR EnsemblBacteria; ADM10429; ADM10429; PB2503_11929. DR KEGG; pbr:PB2503_11929; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000001302; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000001302}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000001302}. FT DOMAIN 212 393 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 178 205 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 469 AA; 51143 MW; ABBDA4214EAE1F21 CRC64; MDFLDEPPKR EGSLHHAIVI HPDWSRAGTV SRTASQRLDE VVGLTAAIGL KVTDALGVGL QDIRPATYFG TGKVKEIGEL IDNADPSPGL VVVNTQLTPV QHRNLERAWQ AKVLDRTALI LEIFGERAQT KEGRLQVDLA HLTYQRSRLV RSWTHLERQR GGAGFLGGPG ERQIEADRRV LAGKIDRLKA QLEQVRRTRT LQRAKRKRAP HPVIALVGYT NAGKSSLFNR MTGAGVTAQD LLFATLDPTM RAVDLPGVGR AILSDTVGFI SDLPTDLVAA FRATLEEVLE ADILLHVRDI SHSEHEAQRL DVLSVLGELG IDEDSPQQVI EVWNKIDLLS PDDQHTAVLT AAHRSTFAEA TLLSPLVSAV SAHSGEGLEG LFGAIDHLLT QDYTLFHVRL GPADGAADAW LHAHGDIREI VETGEVGHRV ISVRLSEKSA GQFRSRFAGL SLASKVDDES FTAMAGFRA // ID E0UER3_CYAP2 Unreviewed; 565 AA. AC E0UER3; DT 02-NOV-2010, integrated into UniProtKB/TrEMBL. DT 02-NOV-2010, sequence version 1. DT 07-JUN-2017, entry version 51. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Cyan7822_4727 {ECO:0000313|EMBL:ADN16631.1}; OS Cyanothece sp. (strain PCC 7822). OC Bacteria; Cyanobacteria; Oscillatoriophycideae; Oscillatoriales; OC Cyanothecaceae; Cyanothece. OX NCBI_TaxID=497965 {ECO:0000313|EMBL:ADN16631.1, ECO:0000313|Proteomes:UP000008206}; RN [1] {ECO:0000313|Proteomes:UP000008206} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=PCC 7822 {ECO:0000313|Proteomes:UP000008206}; RX PubMed=21972240; DOI=10.1128/mBio.00214-11; RA Bandyopadhyay A., Elvitigala T., Welsh E., Stockel J., Liberton M., RA Min H., Sherman L.A., Pakrasi H.B.; RT "Novel metabolic attributes of the genus Cyanothece, comprising a RT group of unicellular nitrogen-fixing Cyanobacteria."; RL MBio 2:E214-E214(2011). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002198; ADN16631.1; -; Genomic_DNA. DR RefSeq; WP_013324671.1; NC_014501.1. DR ProteinModelPortal; E0UER3; -. DR STRING; 497965.Cyan7822_4727; -. DR EnsemblBacteria; ADN16631; ADN16631; Cyan7822_4727. DR KEGG; cyj:Cyan7822_4727; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; EREVIIT; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000008206; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000008206}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000008206}. FT DOMAIN 395 565 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 354 391 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 565 AA; 62396 MW; 4D9FE11EDF85B12D CRC64; MDTIYGNPQG LKASQIKQLQ RLYHQRLPGD RLTTGEFAQR LAAISTDINQ PVCAYINRRG QVIRVGVGTP RQTQIPPLEL PRYGAERLSG IRCIATKLEP VPPKESSLTA MVRQRLDALV VLTLSGMGMV RRGGGATGYV KEAYIAHLLP QSETHNDDQP YWTVSEPLSL DDLSQQDFLE LVEGLEAEFE REFIAQQVDI DHDRVLIVGL MTEDKSDQQF EDGLLEIARL VDTAGGEVLQ TTRQKRPRPH PQTVIGSGKV EEIALQVQTL GANLVVFDRD LSPAQVRNLE NQFGVRVVDR TEVILDIFAQ RAQSQAGKLQ VELAQLEYTL PRLTGRGQAM SRLGGGIGTR GPGETKLETE RRAIGRRIAR LQQQVNELQA HRSRLRKQRQ KQDVPSVAIV GYTNAGKSTL LNALTSAEVY TADQLFATLD PTTRRLAILD PDTGTTETIL LTDTVGFIHE LPPSLVDAFR ATLEEVTEAD ALLHMVDISH AAWESQIQSV STILSEMSMT PGPALIAFNK IDQVEIEVLD LAKEKYPQAV FISAGQGFGL ETLKQKLASL VKVTI // ID E0VHR8_PEDHC Unreviewed; 377 AA. AC E0VHR8; DT 02-NOV-2010, integrated into UniProtKB/TrEMBL. DT 02-NOV-2010, sequence version 1. DT 30-AUG-2017, entry version 40. DE SubName: Full=GTP-binding protein hflx, putative {ECO:0000313|EMBL:EEB12841.1, ECO:0000313|VectorBase:PHUM210680-PA}; GN Name=8237384 {ECO:0000313|VectorBase:PHUM210680-PA}; GN ORFNames=Phum_PHUM210680 {ECO:0000313|EMBL:EEB12841.1}; OS Pediculus humanus subsp. corporis (Body louse). OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; OC Pterygota; Neoptera; Paraneoptera; Psocodea; Phthiraptera; Anoplura; OC Pediculidae; Pediculus. OX NCBI_TaxID=121224 {ECO:0000313|Proteomes:UP000009046}; RN [1] {ECO:0000313|EMBL:EEB12841.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=USDA {ECO:0000313|EMBL:EEB12841.1}; RA Kirkness E., Hannick L., Hass B., Bruggner R., Lawson D., Bidwell S., RA Joardar V., Caler E., Walenz B., Inman J., Schobel S., Galinsky K., RA Amedeo P., Strausberg R.; RT "Annotation of Pediculus humanus corporis strain USDA."; RL Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:EEB12841.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=USDA {ECO:0000313|EMBL:EEB12841.1}; RG The Human Body Louse Genome Consortium; RA Kirkness E., Walenz B., Hass B., Bruggner R., Strausberg R.; RT "The genome of the human body louse."; RL Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases. RN [3] {ECO:0000313|Proteomes:UP000009046, ECO:0000313|VectorBase:PHUM210680-PA} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=USDA {ECO:0000313|Proteomes:UP000009046, RC ECO:0000313|VectorBase:PHUM210680-PA}; RX PubMed=20566863; DOI=10.1073/pnas.1003379107; RA Kirkness E.F., Haas B.J., Sun W., Braig H.R., Perotti M.A., RA Clark J.M., Lee S.H., Robertson H.M., Kennedy R.C., Elhaik E., RA Gerlach D., Kriventseva E.V., Elsik C.G., Graur D., Hill C.A., RA Veenstra J.A., Walenz B., Tubio J.M., Ribeiro J.M., Rozas J., RA Johnston J.S., Reese J.T., Popadic A., Tojo M., Raoult D., Reed D.L., RA Tomoyasu Y., Krause E., Mittapalli O., Margam V.M., Li H.M., RA Meyer J.M., Johnson R.M., Romero-Severson J., Vanzee J.P., RA Alvarez-Ponce D., Vieira F.G., Aguade M., Guirao-Rico S., Anzola J.M., RA Yoon K.S., Strycharz J.P., Unger M.F., Christley S., Lobo N.F., RA Seufferheld M.J., Wang N., Dasch G.A., Struchiner C.J., Madey G., RA Hannick L.I., Bidwell S., Joardar V., Caler E., Shao R., Barker S.C., RA Cameron S., Bruggner R.V., Regier A., Johnson J., Viswanathan L., RA Utterback T.R., Sutton G.G., Lawson D., Waterhouse R.M., Venter J.C., RA Strausberg R.L., Berenbaum M.R., Collins F.H., Zdobnov E.M., RA Pittendrigh B.R.; RT "Genome sequences of the human body louse and its primary endosymbiont RT provide insights into the permanent parasitic lifestyle."; RL Proc. Natl. Acad. Sci. U.S.A. 107:12168-12173(2010). RN [4] {ECO:0000313|VectorBase:PHUM210680-PA} RP IDENTIFICATION. RC STRAIN=USDA {ECO:0000313|VectorBase:PHUM210680-PA}; RG VectorBase; RL Submitted (FEB-2017) to UniProtKB. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; DS235171; EEB12841.1; -; Genomic_DNA. DR RefSeq; XP_002425579.1; XM_002425534.1. DR ProteinModelPortal; E0VHR8; -. DR STRING; 121225.PHUM210680-PA; -. DR EnsemblMetazoa; PHUM210680-RA; PHUM210680-PA; PHUM210680. DR GeneID; 8237384; -. DR KEGG; phu:Phum_PHUM210680; -. DR VectorBase; PHUM210680-RA; PHUM210680-PA; PHUM210680. DR CTD; 8237384; -. DR InParanoid; E0VHR8; -. DR OMA; IMHILRE; -. DR PhylomeDB; E0VHR8; -. DR Proteomes; UP000009046; Partially assembled WGS sequence. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 4: Predicted; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000009046}; KW Reference proteome {ECO:0000313|Proteomes:UP000009046}. FT DOMAIN 261 377 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 230 257 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 377 AA; 43619 MW; F31C825C45066EFB CRC64; MINIRPVLKS YQFFQVSKCQ LTLNKFKHKL RVTDNSESTS EEDDNFLNSN FDKIIERSLL PLGGHHQVFV IQPVIKWGQK KKRNTTPELQ LEESITLVKT LRNWKVVGEA IVKLESFNRK TFFGKGNLQL IRELILKHPT ISAVFLSTEL LKLVQQKILE EMLTVPVFDR YTLIMHILRE HAKTREAKLQ IKLAELPYLY KVMGGLKSGY GIHFFNEITS RSRAARKEIF KEKEAQIRNE LAILRKHREE LRNKRKKNDM PVIAVVGYTN AGKTSLVKAL TGKEKLEPKD YLFATLDVTC HIGTLPSSLP VYFVDTLGFM NDIPTFLIES FVYTLEDVKY ADVIIHVRDI SHPNTVAQND NVIQTLHQLN LSDEDWE // ID E0WUQ1_9ENTR Unreviewed; 396 AA. AC E0WUQ1; DT 02-NOV-2010, integrated into UniProtKB/TrEMBL. DT 02-NOV-2010, sequence version 1. DT 30-AUG-2017, entry version 37. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:EFL91263.1}; GN ORFNames=REG_1820 {ECO:0000313|EMBL:EFL91263.1}; OS Candidatus Regiella insecticola LSR1. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; OC Enterobacteriaceae; aphid secondary symbionts; Candidatus Regiella. OX NCBI_TaxID=663321 {ECO:0000313|EMBL:EFL91263.1, ECO:0000313|Proteomes:UP000005726}; RN [1] {ECO:0000313|EMBL:EFL91263.1, ECO:0000313|Proteomes:UP000005726} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=LSR1 {ECO:0000313|EMBL:EFL91263.1}; RX PubMed=19840097; RA Degnan P.H., Leonardo T.E., Cass B.N., Hurwitz B., Stern D., RA Gibbs R.A., Richards S., Moran N.A.; RT "Dynamics of genome evolution in facultative symbionts of aphids."; RL Environ. Microbiol. 0:0-0(2009). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GL379693; EFL91263.1; -; Genomic_DNA. DR ProteinModelPortal; E0WUQ1; -. DR STRING; 663321.REG_1820; -. DR EnsemblBacteria; EFL91263; EFL91263; REG_1820. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000005726; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 2. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000005726}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000005726}. FT DOMAIN 203 292 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 396 AA; 44501 MW; 28A9A5AEE6260CE8 CRC64; MFDRYEVGER SVLVHISFSP YPDASNKNNE DLQEFESLVF SAGVEVLKTV TGSRKVPDAK YFVGKGKAEE IADTVKTMGA SVVLFNHALS PAQERNLERL CQCRVIDRTG LILDIFAQRA RTHEGKLQVE LAQLRHLATR LVRGWTHLER QKGGIGLRGP GETQLETDRR LLSKRISLIL SRLERVAKQR EQGRQARCRA QIPTVSLIGY TNAGKSSLFN SMTAADVYTA DQLFATLDPT LRSIYVTDVG DTVLADTVGF IRHLPHDLVV AFKATLQETR QASLLLHVID ASXXXXXXXX XXXKYPCSGL AFSANWCGYS VAFQALTERL GGEIAQYELD LPPQEGRLIS RFYQLKAIEK VWPITESGHI GMRFRMPVAK WQRLCKKEKK LVNYIV // ID E1IHX3_9CHLR Unreviewed; 458 AA. AC E1IHX3; DT 30-NOV-2010, integrated into UniProtKB/TrEMBL. DT 30-NOV-2010, sequence version 1. DT 07-JUN-2017, entry version 43. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=OSCT_2911 {ECO:0000313|EMBL:EFO79248.1}; OS Oscillochloris trichoides DG-6. OC Bacteria; Chloroflexi; Chloroflexia; Chloroflexales; Chloroflexineae; OC Oscillochloridaceae; Oscillochloris. OX NCBI_TaxID=765420 {ECO:0000313|EMBL:EFO79248.1, ECO:0000313|Proteomes:UP000054010}; RN [1] {ECO:0000313|EMBL:EFO79248.1, ECO:0000313|Proteomes:UP000054010} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DG-6 {ECO:0000313|EMBL:EFO79248.1, RC ECO:0000313|Proteomes:UP000054010}; RX PubMed=21037015; DOI=10.1128/JB.00931-10; RA Kuznetsov B.B., Ivanovsky R.N., Keppen O.I., Sukhacheva M.V., RA Bumazhkin B.K., Patutina E.O., Beletsky A.V., Mardanov A.V., RA Baslerov R.V., Panteleeva A.N., Kolganova T.V., Ravin N.V., RA Skryabin K.G.; RT "Draft genome sequence of the anoxygenic filamentous phototrophic RT bacterium Oscillochloris trichoides subsp. DG-6."; RL J. Bacteriol. 193:321-322(2011). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EFO79248.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADVR01000120; EFO79248.1; -; Genomic_DNA. DR ProteinModelPortal; E1IHX3; -. DR STRING; 765420.OSCT_2911; -. DR EnsemblBacteria; EFO79248; EFO79248; OSCT_2911. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000054010; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000054010}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000054010}. FT DOMAIN 234 405 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 458 AA; 50655 MW; DA9D52FB1DFBDCA9 CRC64; MYAISHKSKE TIINDIRTHD GKRLHPTTPP RTRALLVGAE VASFSSAWSA EDSLRELALL ADTAGLEVVG SIYQRIDQPF PKYFIGPGKV REVAELREQC GAGLVIFDDE LSPAQTRNLE EALQVGVLDR TALILDIFAQ HARTHEGRLQ VELAQYNYML PRLRRQWSHL ERQAGTGGGT SAGGVVGLRG PGETQLEIDR RLIDQRIAWL KEQLADVHRH RELYRQRRKG SGVPVVALVG YTNAGKSTLL NALSGADVLT QDQLFATLDP TTRQVTLPGN HHILLTDTVG FIQKLPTQLV AAFRATLEEI NEADLLLHVV DLTHPNAQEH AQTVEKTLEE LGVSRKATLT VLNKVDKLEG VAAGEVADLV REMGLPSDVI AVSAQRGWGL DQLGERIVTA LSEGMVALKV LIPYQRNDLV SLWHRRGVID REEYIGEGTH IQGRIPRTLA PQFSQYVD // ID E1KP76_9BACT Unreviewed; 421 AA. AC E1KP76; DT 30-NOV-2010, integrated into UniProtKB/TrEMBL. DT 30-NOV-2010, sequence version 1. DT 07-JUN-2017, entry version 42. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:EFL46931.1}; GN ORFNames=HMPREF9296_2614 {ECO:0000313|EMBL:EFL46931.1}; OS Prevotella disiens FB035-09AN. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Prevotellaceae; OC Prevotella. OX NCBI_TaxID=866771 {ECO:0000313|EMBL:EFL46931.1, ECO:0000313|Proteomes:UP000003610}; RN [1] {ECO:0000313|EMBL:EFL46931.1, ECO:0000313|Proteomes:UP000003610} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=FB035-09AN {ECO:0000313|EMBL:EFL46931.1, RC ECO:0000313|Proteomes:UP000003610}; RA Durkin A.S., Madupu R., Torralba M., Gillis M., Methe B., Sutton G., RA Nelson K.E.; RL Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EFL46931.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AEDO01000013; EFL46931.1; -; Genomic_DNA. DR RefSeq; WP_004355886.1; NZ_AEDO01000013.1. DR ProteinModelPortal; E1KP76; -. DR STRING; 866771.HMPREF9296_2614; -. DR EnsemblBacteria; EFL46931; EFL46931; HMPREF9296_2614. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000003610; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000003610}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000003610}. FT DOMAIN 216 400 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 421 AA; 48414 MW; F6AC72D00D88711B CRC64; MKEFVISEVK AETAILVGLI TQEQNEAKTT EYLDELEFLA DTAGAVTVKR FTQRVGGPNM TSYVGKGKLE EIKQYIKEKE DEEEPIGMVI FDDELSAKQL RNIEAELQVK ILDRTSLILD IFAMRAQTAS AKTQVELAQY RYMLPRLQRL WTHLERQGGG SGSGGGKGSV GLRGPGETQL EMDRRIILQR MTLLKQRLVE IDKQKVTQRK NRGRLIRVAL VGYTNVGKST IMNMLAKSEV FAENKLFATL DTTVRKVVLE NLPFLLADTV GFIRKLPTDL VDSFKSTLDE VREADLLVHV VDISHPDFEE QLQVVNETLK ELECADKPSM IVFNKIDNYT WEEKEEDDLT PMTKENVSLE ELKRTWMAKL NEDCLFISAK EKENVDEFRD VLYKKVRELH VQKYPYNDFL YNIDVENEQF R // ID E1M905_9STRE Unreviewed; 412 AA. AC E1M905; DT 30-NOV-2010, integrated into UniProtKB/TrEMBL. DT 30-NOV-2010, sequence version 1. DT 07-JUN-2017, entry version 43. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:EFO53881.1}; GN ORFNames=SIN_1395 {ECO:0000313|EMBL:EFO53881.1}; OS Streptococcus infantis SK1302. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=871237 {ECO:0000313|EMBL:EFO53881.1, ECO:0000313|Proteomes:UP000003291}; RN [1] {ECO:0000313|EMBL:EFO53881.1, ECO:0000313|Proteomes:UP000003291} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SK1302 {ECO:0000313|EMBL:EFO53881.1, RC ECO:0000313|Proteomes:UP000003291}; RA Daugherty S.C., Kilian M., Tettelin H.; RL Submitted (SEP-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EFO53881.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AEDY01000084; EFO53881.1; -; Genomic_DNA. DR STRING; 871237.SIN_1395; -. DR EnsemblBacteria; EFO53881; EFO53881; SIN_1395. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000003291; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000003291}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000003291}. FT DOMAIN 199 359 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 158 192 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 412 AA; 46753 MW; F87A400C1A97841C CRC64; MIETEKKEER VLLIGVELQG MDNFDLSMEE LASLAKTAGA VVVDSYRQKR EKYDSKTFVG SGKLEEIALM VDAEEITTVI VNNRLTPRQN VNLEEVLGVK VIDRMQLILD IFAMRARSHE GKLQVHLAQL KYLLPRLVGQ GIMLSRQAGG IGSRGPGESQ LELNRRSVRN QITDIERQLK VVEKNRATVR EKRLESSTFK IGLIGYTNAG KSTIMNTLTS KTQYEADELF ATLDATTKSI HLGGNLQVTL TDTVGFIQDL PTELVSSFKS TLEESKHVDL LVHVIDASNP YHEEHEKTVL SIMKDLDMED IPRLTLYNKA DLVEDFTPTQ TPYALISAKS KDSREQLQAL LLDKIKEIFE PFTLRVPFSK SYKIHDLESV AILEERDYQD DGEVITGYIA ERNKWRLEEF YD // ID E1QHQ0_DESB2 Unreviewed; 547 AA. AC E1QHQ0; DT 30-NOV-2010, integrated into UniProtKB/TrEMBL. DT 30-NOV-2010, sequence version 1. DT 07-JUN-2017, entry version 51. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Deba_1726 {ECO:0000313|EMBL:ADK85093.1}; OS Desulfarculus baarsii (strain ATCC 33931 / DSM 2075 / VKM B-1802 / OS 2st14). OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfarculales; OC Desulfarculaceae; Desulfarculus. OX NCBI_TaxID=644282 {ECO:0000313|EMBL:ADK85093.1, ECO:0000313|Proteomes:UP000009047}; RN [1] {ECO:0000313|EMBL:ADK85093.1, ECO:0000313|Proteomes:UP000009047} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33931 / DSM 2075 / VKM B-1802 / 2st14 RC {ECO:0000313|Proteomes:UP000009047}; RX PubMed=21304732; RA Sun H., Spring S., Lapidus A., Davenport K., Del Rio T.G., Tice H., RA Nolan M., Copeland A., Cheng J.F., Lucas S., Tapia R., Goodwin L., RA Pitluck S., Ivanova N., Pagani I., Mavromatis K., Ovchinnikova G., RA Pati A., Chen A., Palaniappan K., Hauser L., Chang Y.J., RA Jeffries C.D., Detter J.C., Han C., Rohde M., Brambilla E., Goker M., RA Woyke T., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P., RA Kyrpides N.C., Klenk H.P., Land M.; RT "Complete genome sequence of Desulfarculus baarsii type strain RT (2st14)."; RL Stand. Genomic Sci. 3:276-284(2010). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002085; ADK85093.1; -; Genomic_DNA. DR RefSeq; WP_013258545.1; NC_014365.1. DR STRING; 644282.Deba_1726; -. DR EnsemblBacteria; ADK85093; ADK85093; Deba_1726. DR KEGG; dbr:Deba_1726; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; EREVIIT; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000009047; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000009047}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000009047}. FT DOMAIN 379 543 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 338 372 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 547 AA; 60052 MW; 69684FA4F8CED7A2 CRC64; MPKLIGSTQG LKPSQINRLN NLYRRRLPPA EVLLPEQARA LAALSHEIGR QIGLVVDRKG EVRQVAVGGP DSLPHIDASR MRHGRARLAG VALVHTALGP SGLSQADQTA LPQRRWDYLA VLNVDDQGLP GLVRVAHLLP QPEDGQDVRL LRPFMAGQTP HDMAALVQSL EDEFARLAPP LDVRAQAAAI LVSVTTGSRQ LAEEHMDELA ELARSAGLEV RGRVVQRRQR LDPRTLMGPG RLAEVLLLAL RQGASVVVFD QDLSPGQAHN LALLTDSDIK VIDRTQLILD IFAQRAATRE GKLQVEMAQL RYLMPRLTSR DDGLSRLTGG IGGRGPGETR LEIDRRRVRE RLHRLEKDLQ EVGKQRQRRR DQRKRGGAPV LSIVGYTNAG KSTLLNTLTG SSVLSEDRLF ATLDPTTRRL RFPQEREVIV TDTVGFIRDL PKELRQAFAA TLEELAQADL LLHVADASNP MVEEQIAAVE RTLDELDLTQ APTILVLNKI DKADPEAVTA LVNRHQGWPV SALDPPSLRP LLAAIEGMAF GQNAGAV // ID E1QRR7_VULDI Unreviewed; 375 AA. AC E1QRR7; DT 30-NOV-2010, integrated into UniProtKB/TrEMBL. DT 30-NOV-2010, sequence version 1. DT 07-JUN-2017, entry version 52. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Vdis_0027 {ECO:0000313|EMBL:ADN49442.1}; OS Vulcanisaeta distributa (strain DSM 14429 / JCM 11212 / NBRC 100878 / OS IC-017). OC Archaea; Crenarchaeota; Thermoprotei; Thermoproteales; OC Thermoproteaceae; Vulcanisaeta. OX NCBI_TaxID=572478 {ECO:0000313|EMBL:ADN49442.1, ECO:0000313|Proteomes:UP000006681}; RN [1] {ECO:0000313|Proteomes:UP000006681} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 14429 / JCM 11212 / NBRC 100878 / IC-017 RC {ECO:0000313|Proteomes:UP000006681}; RX DOI=10.4056/sigs.1113067; RA Mavromatis K., Sikorski J., Pabst E., Teshima H., Lapidus A., RA Lucas S., Nolan M., Glavina Del Rio T., Cheng J., Bruce D., RA Goodwin L., Pitluck S., Liolios K., Ivanova N., Mikhailova N., RA Pati A., Chen A., Palaniappan K., Land M., Hauser L., Chang Y., RA Jeffries C., Rohde M., Spring S., Goker M., Wirth R., Woyke T., RA Bristow J., Eisen J., Markowitz V., Hugenholtz P., Klenk H., RA Kyrpides N.; RT "Complete genome sequence of Vulcanisaeta distributa type strain (IC- RT 017T)."; RL Stand. Genomic Sci. 3:117-125(2010). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002100; ADN49442.1; -; Genomic_DNA. DR RefSeq; WP_013335167.1; NC_014537.1. DR ProteinModelPortal; E1QRR7; -. DR STRING; 572478.Vdis_0027; -. DR EnsemblBacteria; ADN49442; ADN49442; Vdis_0027. DR GeneID; 9750939; -. DR KEGG; vdi:Vdis_0027; -. DR eggNOG; arCOG00353; Archaea. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; FNNHAHV; -. DR OrthoDB; POG093Z07D6; -. DR Proteomes; UP000006681; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000006681}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000006681}. FT DOMAIN 190 360 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 375 AA; 42948 MW; 130ADCC0308469C3 CRC64; MGNNRAKALL LVADDVGENR IREFQLLSEA GGYEVLDTII QRRRPDTRYY LGIGKLGEVE SLVRSLGPDV VITYHQLNPI QYVNLERRLK VRVMDRILLI LEIFERRAGS KEAKLQIELT RLRLEIPRVR EFIRLAKMGE QIGFYGGGEY AIEAYYRYMM RRVAHIRREL SAIKKRREML VIKRRDYGLP QVALTGYTSA GKTTLFNRLA RESKYVDGKP FATLDTYSRL VNFNGLNAIL TDTIGFIDDL PPLLIESFYA TIAEVLNADL VLFMMDISDD YREFSRKFMS SLKIFNDLGI SRTKILPVLN KVDLMDGIDI NDKIGLVESE FGNYVLISAK TGVGIDDLRD AVRSRLEPLV VNKRYGNSKN FNPIG // ID E1R099_OLSUV Unreviewed; 432 AA. AC E1R099; DT 30-NOV-2010, integrated into UniProtKB/TrEMBL. DT 30-NOV-2010, sequence version 1. DT 07-JUN-2017, entry version 50. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Olsu_0952 {ECO:0000313|EMBL:ADK68063.1}; OS Olsenella uli (strain ATCC 49627 / DSM 7084 / CIP 109912 / JCM 12494 / OS NCIMB 702895 / VPI D76D-27C) (Lactobacillus uli). OC Bacteria; Actinobacteria; Coriobacteriia; Coriobacteriales; OC Atopobiaceae; Olsenella. OX NCBI_TaxID=633147 {ECO:0000313|EMBL:ADK68063.1, ECO:0000313|Proteomes:UP000000333}; RN [1] {ECO:0000313|EMBL:ADK68063.1, ECO:0000313|Proteomes:UP000000333} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 49627 / DSM 7084 / CIP 109912 / JCM 12494 / NCIMB 702895 / RC VPI D76D-27C {ECO:0000313|Proteomes:UP000000333}; RX PubMed=21304694; DOI=10.4056/sigs.1082860; RA Goker M., Held B., Lucas S., Nolan M., Yasawong M., RA Glavina Del Rio T., Tice H., Cheng J.F., Bruce D., Detter J.C., RA Tapia R., Han C., Goodwin L., Pitluck S., Liolios K., Ivanova N., RA Mavromatis K., Mikhailova N., Pati A., Chen A., Palaniappan K., RA Land M., Hauser L., Chang Y.J., Jeffries C.D., Rohde M., Sikorski J., RA Pukall R., Woyke T., Bristow J., Eisen J.A., Markowitz V., RA Hugenholtz P., Kyrpides N.C., Klenk H.P., Lapidus A.; RT "Complete genome sequence of Olsenella uli type strain (VPI D76D- RT 27C)."; RL Stand. Genomic Sci. 3:76-84(2010). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002106; ADK68063.1; -; Genomic_DNA. DR RefSeq; WP_013251815.1; NZ_JQCO01000001.1. DR STRING; 633147.Olsu_0952; -. DR EnsemblBacteria; ADK68063; ADK68063; Olsu_0952. DR KEGG; ols:Olsu_0952; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000000333; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000000333}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Hydrolase {ECO:0000313|EMBL:ADK68063.1}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000000333}. FT DOMAIN 210 375 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 432 AA; 47410 MW; 769674E94D7298EC CRC64; MPRFTPHPTA PVPERAVLVG VERRESDWPI GESMAELARL AETDGAVVVA TMVQRLDAPV PRTFIGSGKA GELVRMVHSL DADVVIFDDE LTPSQQSNLE RIVGEPTKVI DRTALILDIF GEHATTREGR LQVQLAQLQY LLPRLRGMWS HLVREQARGG IGSRFGQGES QLEVDRRLVR DRISCLRKEL RRLEGRRKVQ SKARWDSGVF RVALAGYTNA GKSTLLNRLT GAGAYVKDEL FATLDPTTRS MVLDAGRKVT VTDTVGFIQK LPTTLVESFK STLAEVMAAD LVLLVADASD GNVRKEIAAV RRILGDISAS ETPTVVVFNK IDALDDEELA LLRTGAPDAV PISALTGRGI PGLLYRIAEE AARGDEVITA LVPYERGALL RQVHERCRVI REEYRPEGLL ATVSADPRMR EALAPYIEGA GQ // ID E1R4U9_SEDSS Unreviewed; 429 AA. AC E1R4U9; DT 30-NOV-2010, integrated into UniProtKB/TrEMBL. DT 30-NOV-2010, sequence version 1. DT 07-JUN-2017, entry version 49. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Spirs_3087 {ECO:0000313|EMBL:ADK82187.1}; OS Sediminispirochaeta smaragdinae (strain DSM 11293 / JCM 15392 / SEBR OS 4228) (Spirochaeta smaragdinae). OC Bacteria; Spirochaetes; Spirochaetales; Spirochaetaceae; OC Sediminispirochaeta. OX NCBI_TaxID=573413 {ECO:0000313|EMBL:ADK82187.1, ECO:0000313|Proteomes:UP000002318}; RN [1] {ECO:0000313|EMBL:ADK82187.1, ECO:0000313|Proteomes:UP000002318} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 11293 / JCM 15392 / SEBR 4228 RC {ECO:0000313|Proteomes:UP000002318}; RX DOI=10.4056/sigs.1143106; RA Mavromatis K., Yasawong M., Chertkov O., Lapidus A., Lucas S., RA Nolan M., Glavina Del Rio T., Tice H., Cheng J., Pitluck S., RA Liolios K., Ivanova N., Tapia R., Han C., Bruce D., Goodwin L., RA Pati A., Chen A., Palaniappan K., Land M., Hauser L., Chang Y., RA Jeffries C., Detter J., Rohde M., Brambilla E., Spring S., Goker M., RA Sikorski J., Woyke T., Bristow J., Eisen J., Markowitz V., RA Hugenholtz P., Klenk H., Kyrpides N.; RT "Complete genome sequence of Spirochaeta smaragdinae type strain (SEBR RT 4228)."; RL Stand. Genomic Sci. 3:136-144(2010). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002116; ADK82187.1; -; Genomic_DNA. DR RefSeq; WP_013255646.1; NC_014364.1. DR STRING; 573413.Spirs_3087; -. DR EnsemblBacteria; ADK82187; ADK82187; Spirs_3087. DR KEGG; ssm:Spirs_3087; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000002318; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000002318}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000002318}. FT DOMAIN 210 376 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 176 203 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 429 AA; 47591 MW; EC96C7F8723F95FE CRC64; MIETYQRETE DSLPRERRAF LVELRRAEES ERSCEAHLAE LKGLVGTLGL TIAGTTVAPL RSPSPALLLG SGKSEEIADS ADELDAGVII IDDDLTPRQQ RNWERLSGCV VIDRQEVILE IFADRAATRE ASLQVALARM EYSLPRLTRA WTHLSRQRGG SRGTRGEGET QLESDRRIVL AKVAKLKKEL EGVRRQRATA RKQRRSVPLP TVALVGYTNA GKSSLLNALA GSAVNAEDKL FATLDPTTRR LELSGGRSVL LTDTVGFIRK LPHALVDAFR ATLEETLLAD LLIHVIDASD PEAVEHYRTT RQVLSEIGAE DTEQIIVLNK ADLPHDPLLL APLREADPQA LFISTKNGLH LDILKERIAV MLEKHTSGHR YRIPLDRYDL VALLHREGRI ITEEATGQAV CVEAMANEKV DSILKAFRE // ID E1SFK4_PANVC Unreviewed; 426 AA. AC E1SFK4; DT 30-NOV-2010, integrated into UniProtKB/TrEMBL. DT 30-NOV-2010, sequence version 1. DT 30-AUG-2017, entry version 51. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:ADO10950.1}; GN OrderedLocusNames=Pvag_2791 {ECO:0000313|EMBL:ADO10950.1}; OS Pantoea vagans (strain C9-1) (Pantoea agglomerans (strain C9-1)). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; OC Erwiniaceae; Pantoea. OX NCBI_TaxID=712898 {ECO:0000313|EMBL:ADO10950.1, ECO:0000313|Proteomes:UP000006631}; RN [1] {ECO:0000313|EMBL:ADO10950.1, ECO:0000313|Proteomes:UP000006631} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C9-1 {ECO:0000313|EMBL:ADO10950.1, RC ECO:0000313|Proteomes:UP000006631}; RX PubMed=20952567; DOI=10.1128/JB.01122-10; RA Smits T.H., Rezzonico F., Kamber T., Goesmann A., Ishimaru C.A., RA Stockwell V.O., Frey J.E., Duffy B.; RT "The genome sequence of the biocontrol agent Pantoea vagans strain C9- RT 1."; RL J. Bacteriol. 192:6486-6487(2010). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002206; ADO10950.1; -; Genomic_DNA. DR RefSeq; WP_013359181.1; NC_014562.1. DR STRING; 712898.Pvag_2791; -. DR EnsemblBacteria; ADO10950; ADO10950; Pvag_2791. DR KEGG; pva:Pvag_2791; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000006631; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000006631}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}. FT DOMAIN 198 365 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 426 AA; 47695 MW; A2985BB8220AFA7E CRC64; MFDRYDAGEQ AVLVHIWFSQ DKEVEDLQEF ETLVSSAGVE ALQVVTGSRK APHPKYFVGE GKAVEIADAV KTTGASVVLF DHALTPAQER NLERLCECRV IDRTGLILDI FAQRARTHEG KLQVELAQLR HLATRLVRGW THLERQKGGI GLRGPGETQL ETDRRLLRGR ISQILSRLER VEKQREQGRQ SRAKADVPTV SLVGYTNAGK STLFNAMTSA NVFAADQLFA TLDPTLRRLN VADVGDVVLA DTVGFIRHLP HDLVAAFKAT LQETRQATLL LHVIDGADLR VTENIAAVDA VLEEIEADEI PTLLVMNKID MLDGFEPRID RNEENLPIRV WLSAQTGAGI PLLWQALSER LSGEIAQHAL RLPPEAGRLR SRFYQLQAIE KEWNEEDGSV GLQIRMPIIE WMRLCKQEPS LTSYIV // ID E1SPR7_FERBD Unreviewed; 428 AA. AC E1SPR7; DT 30-NOV-2010, integrated into UniProtKB/TrEMBL. DT 30-NOV-2010, sequence version 1. DT 30-AUG-2017, entry version 51. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Fbal_0517 {ECO:0000313|EMBL:ADN74731.1}; OS Ferrimonas balearica (strain DSM 9799 / CCM 4581 / PAT). OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales; OC Ferrimonadaceae; Ferrimonas. OX NCBI_TaxID=550540 {ECO:0000313|EMBL:ADN74731.1, ECO:0000313|Proteomes:UP000006683}; RN [1] {ECO:0000313|EMBL:ADN74731.1, ECO:0000313|Proteomes:UP000006683} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 9799 / CCM 4581 / PAT {ECO:0000313|Proteomes:UP000006683}; RX PubMed=21304747; RA Nolan M., Sikorski J., Davenport K., Lucas S., Del Rio T.G., Tice H., RA Cheng J.F., Goodwin L., Pitluck S., Liolios K., Ivanova N., RA Mavromatis K., Ovchinnikova G., Pati A., Chen A., Palaniappan K., RA Land M., Hauser L., Chang Y.J., Jeffries C.D., Tapia R., Brettin T., RA Detter J.C., Han C., Yasawong M., Rohde M., Tindall B.J., Goker M., RA Woyke T., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P., RA Kyrpides N.C., Klenk H.P., Lapidus A.; RT "Complete genome sequence of Ferrimonas balearica type strain (PAT)."; RL Stand. Genomic Sci. 3:174-182(2010). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002209; ADN74731.1; -; Genomic_DNA. DR RefSeq; WP_013344037.1; NC_014541.1. DR STRING; 550540.Fbal_0517; -. DR EnsemblBacteria; ADN74731; ADN74731; Fbal_0517. DR KEGG; fbl:Fbal_0517; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000006683; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000006683}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Hydrolase {ECO:0000313|EMBL:ADN74731.1}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000006683}. FT DOMAIN 198 365 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 428 AA; 48248 MW; ABC1235D4C327849 CRC64; MFERYEAGER AILVHIDFSA EGEREDLEEL KLLVSSAGVT SCGIVTGRRS SPHPKYFCGT GKAEEIAAVV QAEQAEVVIF NHPLSPAQER NLERICHCRV LDRTGLILDI FAQRARTHEG KLQVELAQLR HLSTRLIRGW THLERQKGGI GLRGPGETQL ETDRRLLRER IKAILRRLDR VARQREQGRR ARQRREVPTV SLVGYTNAGK STLFNRITDS GVYAADQLFA TLDPTLRRIE VADVGPVVLA DTVGFIRHLP HDLVAAFKGT LTETREADLL LHVIDAADER AVENVEAVNE VLAEIEADEV PSLLVYNKLD LLEEAEARID RNDEGEPIRV WLSARNDVGI DLLFEALSER LGNTMVELTV SLPPSEGRWL SRCYELNAVL ATEYDDQGHT QVQLRLPERD WQRLLKASEG KLSDFILK // ID E1T445_BURSG Unreviewed; 390 AA. AC E1T445; DT 30-NOV-2010, integrated into UniProtKB/TrEMBL. DT 30-NOV-2010, sequence version 1. DT 07-JUN-2017, entry version 50. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=BC1003_1210 {ECO:0000313|EMBL:ADN57188.1}; OS Burkholderia sp. (strain CCGE1003). OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Burkholderia. OX NCBI_TaxID=640512 {ECO:0000313|EMBL:ADN57188.1, ECO:0000313|Proteomes:UP000001550}; RN [1] {ECO:0000313|Proteomes:UP000001550} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CCGE1003 {ECO:0000313|Proteomes:UP000001550}; RG US DOE Joint Genome Institute; RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L., RA Pitluck S., Daligault H., Davenport K., Detter J.C., Han C., Tapia R., RA Land M., Hauser L., Jeffries C., Kyrpides N., Ivanova N., RA Ovchinnikova G., Martinez-Romero E., Rogel M.A., Auchtung J., RA Tiedje J.M., Woyke T.; RT "Complete sequence of chromosome 1 of Burkholderia sp. CCGE1003."; RL Submitted (SEP-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002217; ADN57188.1; -; Genomic_DNA. DR RefSeq; WP_013338805.1; NC_014539.1. DR STRING; 640512.BC1003_1210; -. DR EnsemblBacteria; ADN57188; ADN57188; BC1003_1210. DR KEGG; bgf:BC1003_1210; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000001550; Chromosome 1. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000001550}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000001550}. FT DOMAIN 191 362 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 157 184 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 390 AA; 42966 MW; CD27A2F591F25D50 CRC64; MINAALVGID FGKIDFEASL EELSLLAQSA GANPLVTLTG RRSSPDAKMF VGSGKAEELR LACEANDIEL VIFNHALAPA QQRNLEQALN RRVVDRTSLI LDIFAQRARS HEGKLQVELA QLQYLSTRLI RAWTHLERQK GGIGLRGPGE TQLETDRRLI GERIKALKSR LDKLRRQHGT QRRQRSRNQT MSVSLVGYTN AGKSTLFNAL TKAQAYAANQ LFATLDTTSR RVYLGDEAGQ VVVSDTVGFI RELPHQLVAA FRATLEETIH ADLLLHVVDA SSAVRLDQID QVNEVLHAIG ADTIRQVLVF NKIDAVPELA ARGEAVERDE YGNISRVFLS ARTGQGLDTL RAAIAEIATA EPLPDTLLEA SEEDRSAAPR EHRKVPELGH // ID E1V677_HALED Unreviewed; 438 AA. AC E1V677; DT 30-NOV-2010, integrated into UniProtKB/TrEMBL. DT 30-NOV-2010, sequence version 1. DT 30-AUG-2017, entry version 47. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:CBV43247.1}; GN OrderedLocusNames=HELO_3363 {ECO:0000313|EMBL:CBV43247.1}; OS Halomonas elongata (strain ATCC 33173 / DSM 2581 / NBRC 15536 / NCIMB OS 2198 / 1H9). OC Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales; OC Halomonadaceae; Halomonas. OX NCBI_TaxID=768066 {ECO:0000313|EMBL:CBV43247.1, ECO:0000313|Proteomes:UP000008707}; RN [1] {ECO:0000313|Proteomes:UP000008707} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33173 / DSM 2581 / NBRC 15536 / NCIMB 2198 / 1H9 RC {ECO:0000313|Proteomes:UP000008707}; RX PubMed=20849449; DOI=10.1111/j.1462-2920.2010.02336.x; RA Schwibbert K., Marin-Sanguino A., Bagyan I., Heidrich G., Lentzen G., RA Seitz H., Rampp M., Schuster S.C., Klenk H.P., Pfeiffer F., RA Oesterhelt D., Kunte H.J.; RT "A blueprint of ectoine metabolism from the genome of the industrial RT producer Halomonas elongata DSM 2581(T)."; RL Environ. Microbiol. 13:1973-1994(2011). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; FN869568; CBV43247.1; -; Genomic_DNA. DR ProteinModelPortal; E1V677; -. DR STRING; 768066.HELO_3363; -. DR EnsemblBacteria; CBV43247; CBV43247; HELO_3363. DR KEGG; hel:HELO_3363; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000008707; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000008707}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000008707}. FT DOMAIN 199 365 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 438 AA; 49177 MW; 46C22E8FBCA7BF32 CRC64; MFFERPDAGE TAVLVHVDFQ DENEREDSGE FLELVRSAGA EPATLLTGSR GRPDPRFFIG SGKLEEVREA LAVHQAELVI FNHALSPSQE RNVEQALKCR VLDRTGLILD IFAQRARTHE GKLQVELAQL EYMSTRLVRG WTHLERQKGG IGLRGPGETQ LETDRRLLRG RIKAIHKRLD KVRSQRGQNR RARSRAEIPS VSLVGYTNAG KSTLFNALTE SRVYAADQLF ATLDPTLRRL EVEDVGPVVL ADTVGFIRHL PHKLVEAFQA TLQEAAEASL LVHVIDAADP DRDLNVTQVE EVLDEIGALD VPTLKVMNKV DLFDSAPRIE RNAEGRPEAV WLSARDGRGL ELFEQALSEC LADDIIDFDI TLAPAQGKLR ASLHELGAVR EERFDEQGRT LLEIRLPRRD FLQLMARLGE SANDYLPEEL QEGPVWEQ // ID E1VLK6_9GAMM Unreviewed; 430 AA. AC E1VLK6; DT 30-NOV-2010, integrated into UniProtKB/TrEMBL. DT 30-NOV-2010, sequence version 1. DT 07-JUN-2017, entry version 42. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:CBL45698.1}; GN ORFNames=HDN1F_21150 {ECO:0000313|EMBL:CBL45698.1}; OS gamma proteobacterium HdN1. OC Bacteria; Proteobacteria; Gammaproteobacteria. OX NCBI_TaxID=83406 {ECO:0000313|EMBL:CBL45698.1, ECO:0000313|Proteomes:UP000002677}; RN [1] {ECO:0000313|EMBL:CBL45698.1, ECO:0000313|Proteomes:UP000002677} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Widdel F., Rabus R., Grundmann O., Werner I., Schreiber F., RA Ehrenreich P., Behrends A., Wilkes H., Kube M., Reinhardt R., RA Zedelius J.; RT "Alkane degradation by a new type of denitrifying bacterium with RT possible involvement of the electron acceptor in substrate RT activation."; RL Environ. Microbiol. 0:0-0(2010). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; FP929140; CBL45698.1; -; Genomic_DNA. DR RefSeq; WP_013262180.1; NC_014366.1. DR ProteinModelPortal; E1VLK6; -. DR STRING; 83406.HDN1F_21150; -. DR EnsemblBacteria; CBL45698; CBL45698; HDN1F_21150. DR KEGG; gpb:HDN1F_21150; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000002677; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000002677}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000002677}. FT DOMAIN 200 367 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 430 AA; 48487 MW; B7CA9ECAA9094E13 CRC64; MELFERPKSG ERAILVHVDF SAEHIREDVD EFGMLATSAG ATIAAWVRAS RAQPDPRYFI GTGKVEELRQ ALADESADLV MFNHILSPSQ ERNLEKVLQC RVLDRTGLIL DIFAQRARTH EGKLQVELAQ LEHLSTRLIR GWTHLERQRG GIGLRGPGET QLETDRRLIG HRIRTIQKRL EQVRKQRSQA RRSRQRNEVP TVSLVGYTNA GKSTLFNAMT RSDVYAADQL FATLDPTLRR IPIPDVGPIV LADTVGFIRH LPHKLVESFR ATLEESRESD LLLHVVDACS EARDDNIFQV NTVLKETGAG EIPTLMVYNK IDLMGEFPPR VERDADGVSQ AVWLSAQTGA GIQLLLDVLR ERLGKEMVEA GLWLSPAMGE LRAALYRQQG VLNEQVDDTG RCHLQIRIAR KEFEQTLKKL GISAQDLVYE // ID E1VUL8_GLUAR Unreviewed; 553 AA. AC E1VUL8; DT 30-NOV-2010, integrated into UniProtKB/TrEMBL. DT 30-NOV-2010, sequence version 1. DT 07-JUN-2017, entry version 55. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=AARI_11100 {ECO:0000313|EMBL:CBT75321.1}; OS Glutamicibacter arilaitensis (strain DSM 16368 / CIP 108037 / IAM OS 15318 / JCM 13566 / Re117) (Arthrobacter arilaitensis). OC Bacteria; Actinobacteria; Micrococcales; Micrococcaceae; OC Glutamicibacter. OX NCBI_TaxID=861360 {ECO:0000313|Proteomes:UP000006878}; RN [1] {ECO:0000313|EMBL:CBT75321.1, ECO:0000313|Proteomes:UP000006878} RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 16368 / CIP 108037 / IAM 15318 / JCM 13566 / Re117 RC {ECO:0000313|Proteomes:UP000006878}; RX PubMed=21124797; DOI=10.1371/journal.pone.0015489; RA Monnet C., Loux V., Gibrat J.F., Spinnler E., Barbe V., Vacherie B., RA Gavory F., Gourbeyre E., Siguier P., Chandler M., Elleuch R., RA Irlinger F., Vallaeys T.; RT "The Arthrobacter arilaitensis Re117 genome sequence reveals its RT genetic adaptation to the surface of cheese."; RL PLoS ONE 5:E15489-E15489(2010). RN [2] {ECO:0000313|Proteomes:UP000006878} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 16368 / CIP 108037 / IAM 15318 / JCM 13566 / Re117 RC {ECO:0000313|Proteomes:UP000006878}; RA Genoscope.; RT "Complete genome sequence of Arthrobacter arilaitensis (strain DSM RT 16368 / CIP 108037 / JCM 13566 / Re117)."; RL Submitted (JUL-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; FQ311875; CBT75321.1; -; Genomic_DNA. DR STRING; 861360.AARI_11100; -. DR EnsemblBacteria; CBT75321; CBT75321; AARI_11100. DR KEGG; aai:AARI_11100; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000006878; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000006878}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000006878}. FT DOMAIN 332 497 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 553 AA; 60384 MW; 9F84A474FE92DB9F CRC64; MFDEPSETER ATSQSGAHRH YSGKRSTSKE TMTNSESHEH DSASMDDAQI QAAIDRILEA DDAQSPQIQH FGEEESSIFT GQATALNRFS SGLSHFDGDQ EDLDDRRALR RVAGLSTELE DVTEVEYRQL RLERVVLAGI WSEGTVTDAE NSLRELAALA ETAGSEVLDG LVQRRSKPDP STFLGSGKAE ELRAIVASSG ADTVVVDAEL APSQRRALED IVKVKVIDRT SLILDIFAQH AQSREGKAQV ELAQLEYLLP RLRGWGESMS RQAGGRVGAA GGGIGSRGPG ETKIEMDRRR IRDRMAKLRR EIKAMKPARE AKRANRKRNA VPAVAIAGYT NAGKSSLLNR LTNAGVLVEN ALFATLDPTV RQSATEDGLT YTLADTVGFV SNLPTQLVEA FRSTLEEIAD SDLILHVVDG SHPDPEGQIQ AVRTVLGEVD ALNIPEIIVV NKADVADPFV IERIRNRESN TAVVSAHTGE GIEELLEKIS SSIPRPGIQL EVLIPYNRGD LIAKLHQSES EILESEHLEN GTRLIVKVRD SFAAELETFN LHG // ID E1X537_HALMS Unreviewed; 442 AA. AC E1X537; DT 30-NOV-2010, integrated into UniProtKB/TrEMBL. DT 30-NOV-2010, sequence version 1. DT 07-JUN-2017, entry version 50. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=BMS_0601 {ECO:0000313|EMBL:CBW25508.1}; OS Halobacteriovorax marinus (strain ATCC BAA-682 / DSM 15412 / SJ) OS (Bacteriovorax marinus). OC Bacteria; Proteobacteria; Deltaproteobacteria; Bdellovibrionales; OC Halobacteriovoraceae; Halobacteriovorax. OX NCBI_TaxID=862908 {ECO:0000313|EMBL:CBW25508.1, ECO:0000313|Proteomes:UP000008963}; RN [1] {ECO:0000313|Proteomes:UP000008963} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-682 / DSM 15412 / SJ RC {ECO:0000313|Proteomes:UP000008963}; RX PubMed=22955231; DOI=10.1038/ismej.2012.90; RA Crossman L.C., Chen H., Cerdeno-Tarraga A.M., Brooks K., Quail M.A., RA Pineiro S.A., Hobley L., Sockett R.E., Bentley S.D., Parkhill J., RA Williams H.N., Stine O.C.; RT "A small predatory core genome in the divergent marine Bacteriovorax RT marinus SJ and the terrestrial Bdellovibrio bacteriovorus."; RL ISME J. 7:148-160(2013). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; FQ312005; CBW25508.1; -; Genomic_DNA. DR RefSeq; WP_014243295.1; NC_016620.1. DR ProteinModelPortal; E1X537; -. DR STRING; 862908.BMS_0601; -. DR EnsemblBacteria; CBW25508; CBW25508; BMS_0601. DR KEGG; bmx:BMS_0601; -. DR PATRIC; fig|862908.3.peg.576; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR BioCyc; BMAR862908:GJBX-580-MONOMER; -. DR Proteomes; UP000008963; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000008963}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000008963}. FT DOMAIN 208 331 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 442 AA; 50351 MW; A4BFC55E8B376F4E CRC64; MLDNEFHISK DARASLVSLV CPKFAEHSTE KDTMRSLMEL RELLNTLGIE NGEQYVQNRK SVDPATILGS GKIKEIADQA KEEGSSLLVF DCELTSSQIR NIKNLTGLSV VDRCHVILEI FSQHARTKEA KIQIEISRLQ YLLPRLSGFW THLSRQKGGI GVRGGEGEQQ IELDRRIVRE RIEFFKKELD EVRKSREQQK KKRQNKAVTA ALVGYTNAGK SSVMNRLCGV EVLEENKLFA TLDSTYRMLN PDTKPPMILI DTVGFISNLP NTLIDGFKTT LESAIEADLL IIVCDISDPN YKKHLEVTQQ VLSELGVENK EQMIVFNKKD LHPDPLGQKI ILRTNPDSFL VSTYNEEDMV NLKASIINHF LDKQEHYDLF VPYEAGEAHS KVVSKTNVLA THTHERGIFY RVRVPKFIFN PLDLNKYILA PEDPLIEEFI NE // ID E1ZKE5_CHLVA Unreviewed; 415 AA. AC E1ZKE5; DT 30-NOV-2010, integrated into UniProtKB/TrEMBL. DT 30-NOV-2010, sequence version 1. DT 30-AUG-2017, entry version 29. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EFN53678.1}; GN ORFNames=CHLNCDRAFT_32043 {ECO:0000313|EMBL:EFN53678.1}; OS Chlorella variabilis (Green alga). OC Eukaryota; Viridiplantae; Chlorophyta; Trebouxiophyceae; Chlorellales; OC Chlorellaceae; Chlorella. OX NCBI_TaxID=554065 {ECO:0000313|Proteomes:UP000008141}; RN [1] {ECO:0000313|EMBL:EFN53678.1, ECO:0000313|Proteomes:UP000008141} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NC64A {ECO:0000313|EMBL:EFN53678.1, RC ECO:0000313|Proteomes:UP000008141}; RX PubMed=20852019; DOI=10.1105/tpc.110.076406; RA Blanc G., Duncan G., Agarkova I., Borodovsky M., Gurnon J., Kuo A., RA Lindquist E., Lucas S., Pangilinan J., Polle J., Salamov A., Terry A., RA Yamada T., Dunigan D.D., Grigoriev I.V., Claverie J.M., RA Van Etten J.L.; RT "The Chlorella variabilis NC64A genome reveals adaptation to RT photosymbiosis, coevolution with viruses, and cryptic sex."; RL Plant Cell 22:2943-2955(2010). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GL433850; EFN53678.1; -; Genomic_DNA. DR RefSeq; XP_005845780.1; XM_005845718.1. DR GeneID; 17353090; -. DR KEGG; cvr:CHLNCDRAFT_32043; -. DR InParanoid; E1ZKE5; -. DR KO; K03665; -. DR OMA; VILEIFH; -. DR Proteomes; UP000008141; Unassembled WGS sequence. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000008141}; KW Reference proteome {ECO:0000313|Proteomes:UP000008141}. FT DOMAIN 159 325 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 415 AA; 44693 MW; A4D4C111D7BE7285 CRC64; MGSTYQLLDE INPRTYIGSG KVQEIMAAVA NTGATTVVFD DELSPGQLRN LERALGDAVR LCDRTALILD IFSQRAATRE GKLQVELAQS EYQLPRLTRM WSHLERQSGS GQVKGMGEKQ IEVDRRLLKG RMARLRRDIE EVRTHRRAYR ERRAAAPIPV VALVGYTNAG KSTLLNTLTQ AGVLAEDKLF ATLDPTTRRV ELPGGKALLF TDTVGFIQKL PTQLVAAFRA TLEEIKDASL LLHVVDVSHP NAAAQIDAVN GVLAELGVEN MPTLNVWNKV DACADPEVVR AVAARREQTV CVSGLTGEGL GEMLERVSAK LQDSMVAVHV LIPYAQGELV DEIHRTGVVE AAEFGAAGTE VRAYVPLSVA QRLQPLRLQT AAAVEEQQRI EAAAAVAAGA ARAADAAGAA AEAPT // ID E1ZMF1_CHLVA Unreviewed; 609 AA. AC E1ZMF1; DT 30-NOV-2010, integrated into UniProtKB/TrEMBL. DT 30-NOV-2010, sequence version 1. DT 30-AUG-2017, entry version 31. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EFN53099.1}; GN ORFNames=CHLNCDRAFT_137429 {ECO:0000313|EMBL:EFN53099.1}; OS Chlorella variabilis (Green alga). OC Eukaryota; Viridiplantae; Chlorophyta; Trebouxiophyceae; Chlorellales; OC Chlorellaceae; Chlorella. OX NCBI_TaxID=554065 {ECO:0000313|Proteomes:UP000008141}; RN [1] {ECO:0000313|EMBL:EFN53099.1, ECO:0000313|Proteomes:UP000008141} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NC64A {ECO:0000313|EMBL:EFN53099.1, RC ECO:0000313|Proteomes:UP000008141}; RX PubMed=20852019; DOI=10.1105/tpc.110.076406; RA Blanc G., Duncan G., Agarkova I., Borodovsky M., Gurnon J., Kuo A., RA Lindquist E., Lucas S., Pangilinan J., Polle J., Salamov A., Terry A., RA Yamada T., Dunigan D.D., Grigoriev I.V., Claverie J.M., RA Van Etten J.L.; RT "The Chlorella variabilis NC64A genome reveals adaptation to RT photosymbiosis, coevolution with viruses, and cryptic sex."; RL Plant Cell 22:2943-2955(2010). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GL433853; EFN53099.1; -; Genomic_DNA. DR RefSeq; XP_005845201.1; XM_005845139.1. DR GeneID; 17352408; -. DR KEGG; cvr:CHLNCDRAFT_137429; -. DR InParanoid; E1ZMF1; -. DR Proteomes; UP000008141; Unassembled WGS sequence. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000008141}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000008141}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 467 484 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 549 571 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 583 603 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 211 410 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 609 AA; 66741 MW; B880ADFF45F39934 CRC64; MQRLLLSNYS LLEACKLAES LEGTAPEYVQ VGSASRLRPS PSTFFGRGQV EAVQARVAAT QPHRVFVNHV LSGVQQRNLE RALQRPVLDR VALIIEIFSQ RARTAEARLQ VELASLEYKA SRLVRVVDAA TGKRAAFGLA GEASEIVSAR ERGRSGSGAG GLGGAGGQGE SELQLQRRRV ADRRKQLLRK LEEVRKTRGV QRAARRRSGK PQVAIVGYTN AGKSSLLSAL SKCGEAEAGV EDKLFATLDP TLRRVMLPGS GRDVVLSDTV GFISDLPTQL IEAFQATLEE VTEADLLLHV LDASSPQVLQ QRAAVLGVLR GLGVPEARLR EGVIEVWNKM DQLPGQLAAG PVAGEQQLGE RQLPPAVEAL LASDAAAAGY RPTAVATSVL QNEGLSEVLA AVESKPHPAQ QPAEMVAVRQ PAAGAAPAPP AKLTPQVVLH DRANLVALPT IGCMVLAGLL GYIDTLLVTK AFIVYIVGDL FWLILEPKAV PSRPRVIIWH HAVTFLLLQI PLRHPQLGRY TCMDGLIEWN TFFLIARRQF PRCYRAFNFL YWATFYPMRL ALFPLLLPLF WREMQNGYAW WETAAVMGTQ VSLCIFNCWF LIASWTRRR // ID E2ANJ9_CAMFO Unreviewed; 476 AA. AC E2ANJ9; DT 30-NOV-2010, integrated into UniProtKB/TrEMBL. DT 30-NOV-2010, sequence version 1. DT 07-JUN-2017, entry version 26. DE SubName: Full=Putative GTP-binding protein 6 {ECO:0000313|EMBL:EFN64993.1}; GN ORFNames=EAG_08531 {ECO:0000313|EMBL:EFN64993.1}; OS Camponotus floridanus (Florida carpenter ant). OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; OC Pterygota; Neoptera; Holometabola; Hymenoptera; Apocrita; Aculeata; OC Vespoidea; Formicidae; Formicinae; Camponotus. OX NCBI_TaxID=104421 {ECO:0000313|Proteomes:UP000000311}; RN [1] {ECO:0000313|EMBL:EFN64993.1, ECO:0000313|Proteomes:UP000000311} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C129 {ECO:0000313|Proteomes:UP000000311}; RX PubMed=20798317; DOI=10.1126/science.1192428; RA Bonasio R., Zhang G., Ye C., Mutti N.S., Fang X., Qin N., Donahue G., RA Yang P., Li Q., Li C., Zhang P., Huang Z., Berger S.L., Reinberg D., RA Wang J., Liebig J.; RT "Genomic comparison of the ants Camponotus floridanus and Harpegnathos RT saltator."; RL Science 329:1068-1071(2010). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GL441244; EFN64993.1; -; Genomic_DNA. DR RefSeq; XP_011261285.1; XM_011262983.1. DR RefSeq; XP_011261286.1; XM_011262984.2. DR ProteinModelPortal; E2ANJ9; -. DR GeneID; 105254357; -. DR InParanoid; E2ANJ9; -. DR OMA; MDTVGFM; -. DR Proteomes; UP000000311; Unassembled WGS sequence. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR CDD; cd01878; HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000311}; KW Reference proteome {ECO:0000313|Proteomes:UP000000311}. FT DOMAIN 258 418 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 476 AA; 54151 MW; 33DD4C114A5F4FB1 CRC64; MHCIRKILNI AQQNLQGYDK TNTIYKTSRI LLQNIVYRFN HNSEEYADDQ NQEVYTKISN QYLGTALGGH RAFILQPYIK WGRDKKRNTS PELQMAEAVA LINTLSNWCV VGAKYAPLLS LQRKSLLGTG AMENLKKELY KCENPTAIFV STNLLKFIQI AELEKILGLP VYDRYSIVIH IFRQHAKSPE AKLQVAIAEI PYVRKKILET SRTRNGIIMT EKLKLMFDNR EKKLNNELKK LQQHRTVIRS QRKKHGFPTV AVVGYTNAGK TSLIKALTDD KSLQPENKLF ATLDTSAHGG LLPNRMKVLY MDTIGFIQDV PETLIEPFIV TLEDAMIADV IVHIYDVSHP DMKAQYQHVQ QTIKPMIKEA HPIIDVANKC DLVQSDCIPK DAIAISATNL TGIDLLRQKI EKVLLVTTGL LRTRIRVESG SPAASWLYKM TTVMNAQSDP NDAQYLIMDV LATSIDIQKF KKFLRQ // ID E2BH85_HARSA Unreviewed; 477 AA. AC E2BH85; DT 30-NOV-2010, integrated into UniProtKB/TrEMBL. DT 30-NOV-2010, sequence version 1. DT 07-JUN-2017, entry version 24. DE SubName: Full=Putative GTP-binding protein 6 {ECO:0000313|EMBL:EFN85006.1}; GN ORFNames=EAI_17350 {ECO:0000313|EMBL:EFN85006.1}; OS Harpegnathos saltator (Jerdon's jumping ant). OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; OC Pterygota; Neoptera; Holometabola; Hymenoptera; Apocrita; Aculeata; OC Vespoidea; Formicidae; Ponerinae; Ponerini; Harpegnathos. OX NCBI_TaxID=610380 {ECO:0000313|Proteomes:UP000008237}; RN [1] {ECO:0000313|EMBL:EFN85006.1, ECO:0000313|Proteomes:UP000008237} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=R22 G/1 {ECO:0000313|EMBL:EFN85006.1, RC ECO:0000313|Proteomes:UP000008237}; RX PubMed=20798317; DOI=10.1126/science.1192428; RA Bonasio R., Zhang G., Ye C., Mutti N.S., Fang X., Qin N., Donahue G., RA Yang P., Li Q., Li C., Zhang P., Huang Z., Berger S.L., Reinberg D., RA Wang J., Liebig J.; RT "Genomic comparison of the ants Camponotus floridanus and Harpegnathos RT saltator."; RL Science 329:1068-1071(2010). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GL448268; EFN85006.1; -; Genomic_DNA. DR ProteinModelPortal; E2BH85; -. DR InParanoid; E2BH85; -. DR OMA; MDTVGFM; -. DR Proteomes; UP000008237; Unassembled WGS sequence. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR CDD; cd01878; HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008237}; KW Reference proteome {ECO:0000313|Proteomes:UP000008237}. FT DOMAIN 259 419 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 477 AA; 54385 MW; 8A5A3D5CE2D51636 CRC64; MILNITHQNL RICNKVNNVN KICERPRVLL QNIAYRFNHN SEEDASAESE EERKEYVELS SRCIGTAVGH RIFVLQPYIK WGRDKKRNTT PELQLAEAVA LVNTLPYWCV VGTKYAPLLT LQRKSLLGTG SIEDLKKEMR TSENPTAIFV STNQLKFVQM LELEKIFGLP VYDRYSIVIH IFREHAKTPE AKLQVALAEI PYIRRKVLET CITSCGAINM TEKMKLLLDN KEKRLKSDLK KLKQHRQLIR NHRKNTGIPT VAVVGYTNSG KTSLIKALTD DKSLQPKNKL FATLDTTAHR GMLLNRLKIL YMDTIGFIQD VPETLIEPFV VTLEDAIIAD VIIHIFDISH PDMKAQYQHV QQTIKPMIGE DRPVIDVANK CDLVESDCIP KDVIAVSSTK LTGIDLLRLE IEKILLDNIG LLRTRVRVES GSPAASWLYK WTTVTNAAPD PDDAQYLIMN VLATSRDIEE FKKFLRK // ID E2CCW7_9RHOB Unreviewed; 463 AA. AC E2CCW7; DT 30-NOV-2010, integrated into UniProtKB/TrEMBL. DT 30-NOV-2010, sequence version 1. DT 07-JUN-2017, entry version 39. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:EFO33749.1}; GN ORFNames=TRICHSKD4_0859 {ECO:0000313|EMBL:EFO33749.1}; OS Roseibium sp. TrichSKD4. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae; Roseibium. OX NCBI_TaxID=744980 {ECO:0000313|EMBL:EFO33749.1, ECO:0000313|Proteomes:UP000005735}; RN [1] {ECO:0000313|EMBL:EFO33749.1, ECO:0000313|Proteomes:UP000005735} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=TrichSKD4 {ECO:0000313|EMBL:EFO33749.1, RC ECO:0000313|Proteomes:UP000005735}; RA Mann E., Barbeau K., Ferriera S., Johnson J., Kravitz S., Beeson K., RA Sutton G., Rogers Y.-H., Friedman R., Frazier M., Venter J.C.; RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GL476304; EFO33749.1; -; Genomic_DNA. DR ProteinModelPortal; E2CCW7; -. DR STRING; 744980.TRICHSKD4_0859; -. DR EnsemblBacteria; EFO33749; EFO33749; TRICHSKD4_0859. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000005735; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000005735}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000005735}. FT DOMAIN 235 405 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 201 228 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 463 AA; 51610 MW; 183EBA0C3E979EE8 CRC64; MKPKSREEDI SKVKDADHHQ AEKGGIDRRP QPYTAIILEP VLATRSSGED GELRGNRSPE ARLEEAVGLS AAINLQIAMS GIVKVNNPKP ATLFGEGKVS ELTGIVAAQE ADLVVIDHPL TPIQQRNLEK HLKTKVIDRT GLILEIFGDR ARTKEGKLQV DLAHLTWQKS RLVRSWTHLE RQRGGTGFMG GPGETQIESD RRQIQDRITA LQKQLEQVRR TRDLHRKKRK KIPQPVVALV GYTNAGKSTL FNRMTESNVF AKDLLFATLD PTLRKIRLPH GREIILSDTV GFISDLPTHL VAAFRATLEE VLEADLILHV RDISHPDSEA QCEDVKKTLV DLGVDGSHAA PVIEVWNKID ALDPAYREKL LEDAAEEGPV SLSALTGEGV TSLYGRIDAF MAQHDDLFTV KLPVFEGALL AQLYQLSEVM EREDGEEFIT AEVRVTDKQR GPFRDTFATY LSE // ID E2QA49_STRC2 Unreviewed; 496 AA. AC E2QA49; DT 30-NOV-2010, integrated into UniProtKB/TrEMBL. DT 30-NOV-2010, sequence version 1. DT 07-JUN-2017, entry version 43. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=SCLAV_4676 {ECO:0000313|EMBL:EFG09748.1}; OS Streptomyces clavuligerus (strain ATCC 27064 / DSM 738 / JCM 4710 / OS NBRC 13307 / NCIMB 12785 / NRRL 3585 / VKM Ac-602). OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae; OC Streptomyces. OX NCBI_TaxID=443255 {ECO:0000313|EMBL:EFG09748.1, ECO:0000313|Proteomes:UP000002357}; RN [1] {ECO:0000313|EMBL:EFG09748.1, ECO:0000313|Proteomes:UP000002357} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 27064 / DSM 738 / JCM 4710 / NBRC 13307 / NCIMB 12785 / RC NRRL 3585 / VKM Ac-602 {ECO:0000313|Proteomes:UP000002357}; RX PubMed=20624727; DOI=10.1093/gbe/evq013; RA Medema M.H., Trefzer A., Kovalchuk A., van den Berg M., Mueller U., RA Heijne W., Wu L., Alam M.T., Ronning C.M., Nierman W.C., RA Bovenberg R.A.L., Breitling R., Takano E.; RT "The sequence of a 1.8-mb bacterial linear plasmid reveals a rich RT evolutionary reservoir of secondary metabolic pathways."; RL Genome Biol. Evol. 2:212-224(2010). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CM000913; EFG09748.1; -; Genomic_DNA. DR RefSeq; WP_003962097.1; NZ_CM001015.1. DR STRING; 443255.SclaA2_010100022458; -. DR EnsemblBacteria; EFG09748; EFG09748; SCLAV_4676. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR Proteomes; UP000002357; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000002357}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000002357}. FT DOMAIN 275 440 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 496 AA; 54163 MW; 201DA8F9739EA19F CRC64; MTSSSSPSQD EQSFERTRTE SLRADALMEE DVAWSHEIDG ERDGAQYDRA ERAALRRVAG LSTELEDVTE VEYRQLRLER VVLVGVWTSG TVQDADNSLA ELAALAETAG AMVLDGVIQR RDKPDPATYI GSGKAQELRD IVLESGADTV VCDGELSPGQ LIHLEDVVKV KVVDRTALIL DIFAQHAKSR EGKAQVALAQ MQYMLPRLRG WGQSLSRQMG GGGGGGMATR GPGETKIETD RRRIREKMAK MRREIAEMKT GRDLKRQERR RHKVPSVAIA GYTNAGKSSL LNRLTGAGVL VENALFATLD PTVRRAETPS GRLYTLADTV GFVRHLPHHL VEAFRSTMEE VGESDLILHV VDGSHPAPEE QLAAVREVIR DVGAVDVPEI VVVNKADAAD PLVLQRLMRV ERHSIAVSAR TGEGIEELLR LIDDELPRPS VEIEVLVPYT QGGLVARVHA EGEVVSEEHG AEGTLLKARV HEELAAVLAP YAPVAP // ID E2S979_9ACTN Unreviewed; 458 AA. AC E2S979; DT 11-JAN-2011, integrated into UniProtKB/TrEMBL. DT 11-JAN-2011, sequence version 1. DT 07-JUN-2017, entry version 40. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:EFQ83803.1}; GN ORFNames=HMPREF0063_10519 {ECO:0000313|EMBL:EFQ83803.1}; OS Aeromicrobium marinum DSM 15272. OC Bacteria; Actinobacteria; Propionibacteriales; Nocardioidaceae; OC Aeromicrobium. OX NCBI_TaxID=585531 {ECO:0000313|EMBL:EFQ83803.1, ECO:0000313|Proteomes:UP000003111}; RN [1] {ECO:0000313|EMBL:EFQ83803.1, ECO:0000313|Proteomes:UP000003111} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 15272 {ECO:0000313|EMBL:EFQ83803.1, RC ECO:0000313|Proteomes:UP000003111}; RA Muzny D., Qin X., Buhay C., Dugan-Rocha S., Ding Y., Chen G., RA Hawes A., Holder M., Jhangiani S., Johnson A., Khan Z., Li Z., Liu W., RA Liu X., Perez L., Shen H., Wang Q., Watt J., Xi L., Xin Y., Zhou J., RA Deng J., Jiang H., Liu Y., Qu J., Song X.-Z., Zhang L., Villasana D., RA Johnson A., Liu J., Liyanage D., Lorensuhewa L., Robinson T., Song A., RA Song B.-B., Dinh H., Thornton R., Coyle M., Francisco L., Jackson L., RA Javaid M., Korchina V., Kovar C., Mata R., Mathew T., Ngo R., RA Nguyen L., Nguyen N., Okwuonu G., Ongeri F., Pham C., Simmons D., RA Wilczek-Boney K., Hale W., Jakkamsetti A., Pham P., Ruth R., RA San Lucas F., Warren J., Zhang J., Zhao Z., Zhou C., Zhu D., Lee S., RA Bess C., Blankenburg K., Forbes L., Fu Q., Gubbala S., Hirani K., RA Jayaseelan J.C., Lara F., Munidasa M., Palculict T., Patil S., RA Pu L.-L., Saada N., Tang L., Weissenberger G., Zhu Y., Hemphill L., RA Shang Y., Youmans B., Ayvaz T., Ross M., Santibanez J., Aqrawi P., RA Gross S., Joshi V., Fowler G., Nazareth L., Reid J., Worley K., RA Petrosino J., Highlander S., Gibbs R.; RL Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EFQ83803.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACLF03000003; EFQ83803.1; -; Genomic_DNA. DR RefSeq; WP_007077541.1; NZ_CM001024.1. DR ProteinModelPortal; E2S979; -. DR STRING; 585531.HMPREF0063_10519; -. DR EnsemblBacteria; EFQ83803; EFQ83803; HMPREF0063_10519. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000003111; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 2. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000003111}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000003111}. FT DOMAIN 240 405 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 199 233 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 458 AA; 49793 MW; 12FC9636F835EB33 CRC64; MTETQGTDGL ELEERNSLRR VASLRTELQD ITEVEYRQLR LERVVLVGVW TEGSVEDAEN SLAELKLLAE TAGSEVLDAL IQRRPKPDPA TFIGSGKVEE LHAVVESTGA DTVICDGELA PSQLRNLEDR VKVKVVDRTA LILDIFAQHA KSAEGKAQVE LAQLQYQTQR LRGWGGNLSR QAGGRAAGGE GIGGRGPGET KLETDRRRIQ AKMAKLRREL KMLSVTRETK KANRRRHQIP SVAIAGYTNA GKSSLLNRLT DAGVLVEDAL FATLDPTTRR TQTSDGRVYT MSDTVGFVRH LPHQLVEAFR STLEEVAESD LVLHVVDGSH PDPAGQIAAV REVFADVDAL GVPEIIVVNK ADAADPTVIR QLLAREPHAV VVSARTGEGI DELLDAIEAD LPRPASRIEV VLPYARGDLL NQIHATGEIE SIEHEGDGTH VTALVAAELA HQLEPFAV // ID E2SK59_9FIRM Unreviewed; 415 AA. AC E2SK59; DT 11-JAN-2011, integrated into UniProtKB/TrEMBL. DT 11-JAN-2011, sequence version 1. DT 07-JUN-2017, entry version 36. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:EFP62074.1}; GN ORFNames=HMPREF0983_01436 {ECO:0000313|EMBL:EFP62074.1}; OS Erysipelotrichaceae bacterium 3_1_53. OC Bacteria; Firmicutes; Erysipelotrichia; Erysipelotrichales; OC Erysipelotrichaceae. OX NCBI_TaxID=658659 {ECO:0000313|EMBL:EFP62074.1, ECO:0000313|Proteomes:UP000006223}; RN [1] {ECO:0000313|EMBL:EFP62074.1, ECO:0000313|Proteomes:UP000006223} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=3_1_53 {ECO:0000313|EMBL:EFP62074.1, RC ECO:0000313|Proteomes:UP000006223}; RG The Broad Institute Genome Sequencing Platform; RA Ward D., Earl A., Feldgarden M., Young S.K., Pearson M., Zeng Q., RA Alvarado L., Berlin A., Bochicchio J., Chapman S.B., Chen Z., RA Freedman E., Gellesch M., Goldberg J., Griggs A., Gujja S., RA Heilman E., Heiman D., Howarth C., Jen D., Larson L., Mehta T., RA Neiman D., Park D., Roberts A., Saif S., Shea T., Shenoy N., Sisk P., RA Stolte C., Sykes S., Thomson T., Walk T., White J., Yandava C., RA Allen-Vercoe E., Strauss J., Sibley C., Daigneault M., Haas B., RA Nusbaum C., Birren B.; RT "The Genome Sequence of Erysipelotrichaceae bacterium strain 3_1_53."; RL Submitted (JUL-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EFP62074.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACTJ01000034; EFP62074.1; -; Genomic_DNA. DR RefSeq; WP_009272368.1; NZ_GL520135.1. DR ProteinModelPortal; E2SK59; -. DR STRING; 658659.HMPREF0983_01436; -. DR EnsemblBacteria; EFP62074; EFP62074; HMPREF0983_01436. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR Proteomes; UP000006223; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000006223}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000006223}. FT DOMAIN 189 358 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 148 182 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 415 AA; 47971 MW; F9E57EC95B1E4AEB CRC64; MQQVVIVLAD TTEQTEKNEE FIELIQAADM EIRKTFIQNL KSITLKTYIG IGKCEEIREY VQEQKPERIV FNHDLSPLQI RNLEDILQTP VMDRTELILA IFESRAVTRI ARLQIECAQL KKLLPRLIGA NTQLGRQSGS GKNRGAGEKQ LELDRRRINA RIQELQRELK KVEAQRLTQR RSRQKSMLPL VSLVGYTNAG KSTIMNMLLE YSSPYEHDKR VLEKDMLFAT LDTSIRHIDL PDGKSFLLSD TVGFVSDLPH DLVDAFHSTL EEVRYASLLV QVVDVSSEAC ARQMEITQDT LQQINAADIP MITVYNKCDQ SHYPYPREHA HDLYMSAKDK VGLHELLELI HRHLYPDEKH VIMHIPYQQT GIYSLLMKHA RVITRTDEED GIHLEVVISD HLYQKYQKYV TAIRT // ID E2ZMC0_9FIRM Unreviewed; 421 AA. AC E2ZMC0; DT 11-JAN-2011, integrated into UniProtKB/TrEMBL. DT 11-JAN-2011, sequence version 1. DT 07-JUN-2017, entry version 37. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:EFQ05694.1}; GN ORFNames=HMPREF9436_02837 {ECO:0000313|EMBL:EFQ05694.1}; OS Faecalibacterium cf. prausnitzii KLE1255. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Ruminococcaceae; OC Faecalibacterium. OX NCBI_TaxID=748224 {ECO:0000313|EMBL:EFQ05694.1, ECO:0000313|Proteomes:UP000006028}; RN [1] {ECO:0000313|EMBL:EFQ05694.1, ECO:0000313|Proteomes:UP000006028} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=KLE1255 {ECO:0000313|EMBL:EFQ05694.1, RC ECO:0000313|Proteomes:UP000006028}; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Hou S., Chen J., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Zhang X., Suruliraj S., Warren W., Chinwalla A., RA Mardis E.R., Wilson R.K.; RL Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EFQ05694.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AECU01000207; EFQ05694.1; -; Genomic_DNA. DR RefSeq; WP_005945458.1; NZ_GL538344.1. DR STRING; 748224.HMPREF9436_02837; -. DR EnsemblBacteria; EFQ05694; EFQ05694; HMPREF9436_02837. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000006028; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000006028}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000006028}. FT DOMAIN 209 368 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 175 202 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 421 AA; 45623 MW; EC6FDE4228BA5052 CRC64; MSELYDILVE TPPTKVILLA LDQGLWDCER SLAELSALCE ANHMEAVAQV TQKRQTPETG IVLGSGKLEE ASLAAETLGA ECAVFDGELT GSQIRNISNA LGGLEVIDRT MLILEIFRSR AVTNEGKLQT ELALLRYRLP RLQGMGEALS RQGGGGGGGG GARRGAGETK LELDRRHVHA RIDALAEKLA EMEKRRGESR KARAKTGMPV VSLVGYTNVG KSSLMNALCG PSVAEADMLF ATLDPTSRKL ILPSGMAVLL VDTVGFVSRL PHNLVEAFKS TLEEAAWSDV IIRVADAGDE QREEQLAVTD EVLDGLDCAD IPRLTVYNKC DKPGAMSFDP DILLTSAKTG YGLDTLLAKL DEVLSDRVHT LKVLLPYDKL GLAAPMRERG SVQVEEYRED GLYLEGIVKT EDLHCFEGYL V // ID E3BIU0_9VIBR Unreviewed; 429 AA. AC E3BIU0; DT 11-JAN-2011, integrated into UniProtKB/TrEMBL. DT 11-JAN-2011, sequence version 1. DT 30-AUG-2017, entry version 40. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=VIBC2010_11446 {ECO:0000313|EMBL:EFP97026.1}; OS Vibrio caribbeanicus ATCC BAA-2122. OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; OC Vibrionaceae; Vibrio. OX NCBI_TaxID=796620 {ECO:0000313|EMBL:EFP97026.1, ECO:0000313|Proteomes:UP000002943}; RN [1] {ECO:0000313|EMBL:EFP97026.1, ECO:0000313|Proteomes:UP000002943} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-2122 {ECO:0000313|EMBL:EFP97026.1, RC ECO:0000313|Proteomes:UP000002943}; RX PubMed=21930677; DOI=10.1099/ijs.0.032375-0; RA Hoffmann M., Monday S.R., Allard M.W., Strain E.A., Whittaker P., RA Naum M., McCarthy P.J., Lopez J.V., Fischer M., Brown E.W.; RT "Vibrio caribbeanicus sp. nov., isolated from the marine sponge RT Scleritoderma cyanea."; RL Int. J. Syst. Evol. Microbiol. 62:1736-1743(2012). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EFP97026.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AEIU01000067; EFP97026.1; -; Genomic_DNA. DR RefSeq; WP_009600918.1; NZ_AEIU01000067.1. DR ProteinModelPortal; E3BIU0; -. DR STRING; 796620.VIBC2010_11446; -. DR EnsemblBacteria; EFP97026; EFP97026; VIBC2010_11446. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000002943; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000002943}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000002943}. FT DOMAIN 198 365 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 429 AA; 48807 MW; C1D295A3E95448B2 CRC64; MFDRYEAGER AVLVHINFTQ EGEWEDLNEF EMLVSSAGVS ALQVVTGSRQ SPHPKYYVGE GKAQEIAHAV RMMGADIVLF NHSLSPAQER NLEKLCKCRV LDRTGLILDI FAQRARTHEG KLQVELAQLR HISTRLIRGW THLERQKGGI GLRGPGETQL ETDRRLLRDR IKAILRRLEK VAKQREQGRR ARNRAEIPTV SLVGYTNAGK STLFNQITQA SVYAADQLFA TLDPTLRKID VADIGSAILA DTVGFIRHLP HDLVAAFKAT LQETQEADIL LHVVDASDER FRENIHAVHE VLEEIDAHDI PALVVMNKID NLEGQEPRIE RDEDGVASVV WLSAMEGKGT ELLFAALSER LASQMVQYRL RVTPRYQGRI RSTFFQMRCI EREEYDQDGN LLIDVRMQQV DWSRLEKREG AVLRDFIVT // ID E3C858_9LACO Unreviewed; 424 AA. AC E3C858; DT 11-JAN-2011, integrated into UniProtKB/TrEMBL. DT 11-JAN-2011, sequence version 1. DT 07-JUN-2017, entry version 36. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:EFQ53090.1}; GN ORFNames=HMPREF9265_1608 {ECO:0000313|EMBL:EFQ53090.1}; OS Lactobacillus oris PB013-T2-3. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; OC Lactobacillus. OX NCBI_TaxID=908339 {ECO:0000313|EMBL:EFQ53090.1, ECO:0000313|Proteomes:UP000003070}; RN [1] {ECO:0000313|EMBL:EFQ53090.1, ECO:0000313|Proteomes:UP000003070} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=PB013-T2-3 {ECO:0000313|EMBL:EFQ53090.1, RC ECO:0000313|Proteomes:UP000003070}; RA Durkin A.S., Madupu R., Torralba M., Gillis M., Methe B., Sutton G., RA Nelson K.E.; RL Submitted (OCT-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EFQ53090.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AEKL01000051; EFQ53090.1; -; Genomic_DNA. DR RefSeq; WP_003712944.1; NZ_AEKL01000051.1. DR EnsemblBacteria; EFQ53090; EFQ53090; HMPREF9265_1608. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000003070; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000003070}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000003070}. FT DOMAIN 202 371 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 424 AA; 47582 MW; 296E834CE8C7C49C CRC64; MDTTIQNDER VIITGLDTGQ DDYNYSMTEL AELAQANHME VVQRVDQVID RPNPATYFGK GKVAEIAELA AANDVATIIT NDELSPSQLR NLEDETGKRI LDRTALILEI FATRAQTKEA KLQVQIAELQ YRLPRLQTSA SQRLDQQTGG GSGFTNRGAG ETKLEMDRRT IQHQITHLRH ELAAIDKSEE TKRKQRAKSN IPTAALVGYT NAGKSTIMNG LVRRYGTVED KTVFEKDMLF ATLDTSVRRL TLPGKKDFLL SDTVGFVSKL PTNLVESFKS TLAEAANADL LIQVIDYSDP NYEEMMQTTK ETLKQIGIDN IPMVNVFNKA DKTEIEFPVL EGDDQVVISA KQEESLDLLV DVIRKHLFKD YVEAKLLLPF SAGQQVSYLN EHTNILDTEY RNDGTLLTVE MSPQDAQRFA QYQV // ID E3CYA5_9BACT Unreviewed; 380 AA. AC E3CYA5; DT 11-JAN-2011, integrated into UniProtKB/TrEMBL. DT 11-JAN-2011, sequence version 1. DT 07-JUN-2017, entry version 41. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=Apau_1212 {ECO:0000313|EMBL:EFQ23638.1}; OS Aminomonas paucivorans DSM 12260. OC Bacteria; Synergistetes; Synergistia; Synergistales; Synergistaceae; OC Aminomonas. OX NCBI_TaxID=584708 {ECO:0000313|EMBL:EFQ23638.1, ECO:0000313|Proteomes:UP000005096}; RN [1] {ECO:0000313|EMBL:EFQ23638.1, ECO:0000313|Proteomes:UP000005096} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 12260 {ECO:0000313|EMBL:EFQ23638.1}; RX PubMed=21304733; RA Pitluck S., Yasawong M., Held B., Lapidus A., Nolan M., Copeland A., RA Lucas S., Del Rio T.G., Tice H., Cheng J.F., Chertkov O., Goodwin L., RA Tapia R., Han C., Liolios K., Ivanova N., Mavromatis K., RA Ovchinnikova G., Pati A., Chen A., Palaniappan K., Land M., Hauser L., RA Chang Y.J., Jeffries C.D., Pukall R., Spring S., Rohde M., RA Sikorski J., Goker M., Woyke T., Bristow J., Eisen J.A., Markowitz V., RA Hugenholtz P., Kyrpides N.C., Klenk H.P.; RT "Non-contiguous finished genome sequence of Aminomonas paucivorans RT type strain (GLU-3)."; RL Stand. Genomic Sci. 3:285-293(2010). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CM001022; EFQ23638.1; -; Genomic_DNA. DR STRING; 584708.Apau_1212; -. DR EnsemblBacteria; EFQ23638; EFQ23638; Apau_1212. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000005096; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000005096}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000005096}. FT DOMAIN 191 360 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 157 184 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 380 AA; 41792 MW; 7482D5DB0C92FE5C CRC64; MTTPRRAVLA SLVPEGDPAL LELEALLGNL GYEVAGTVFQ KRAAPDPSGF LGQGKAEEIR LFAQAQGARI LVVEGELSPT QRRILGERTK LEVWDRPYLI MKIFEARAVT AEAKWQVQLA AYRYEIPFLK GLGRQMSRPG GGIGTRGPGE TEFERHRRKI ERRIGAIEEK LREVRRRRKE RRERRRKEGR RLVALVGYTN SGKTTLLRRL SGDPKVQGAD RLFATLDTTS RSVLLPSGQR VLFTDTVGFI RRLPPQLVAA FRATLEETRD ADLILVVLDG ADPQVEAHYE VVLETLEALE AAQVPRVVLL NKADLSAAEA SEDCLSLLRA RGERIVSGSA STGEGLEALL EAVENRLDEP RGGPPEPGGE EGGIPACSPA // ID E3D964_GARV3 Unreviewed; 489 AA. AC E3D964; DT 11-JAN-2011, integrated into UniProtKB/TrEMBL. DT 11-JAN-2011, sequence version 1. DT 07-JUN-2017, entry version 47. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:ADP38608.1}; GN OrderedLocusNames=HMPREF0421_20526 {ECO:0000313|EMBL:ADP38608.1}; OS Gardnerella vaginalis (strain ATCC 14019 / 317). OC Bacteria; Actinobacteria; Bifidobacteriales; Bifidobacteriaceae; OC Gardnerella. OX NCBI_TaxID=525284 {ECO:0000313|EMBL:ADP38608.1, ECO:0000313|Proteomes:UP000001453}; RN [1] {ECO:0000313|EMBL:ADP38608.1, ECO:0000313|Proteomes:UP000001453} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 14019 / 317 {ECO:0000313|Proteomes:UP000001453}; RX PubMed=20865041; DOI=10.1371/journal.pone.0012411; RA Yeoman C.J., Yildirim S., Thomas S.M., Durkin A.S., Torralba M., RA Sutton G., Buhay C.J., Ding Y., Dugan-Rocha S.P., Muzny D.M., Qin X., RA Gibbs R.A., Leigh S.R., Stumpf R., White B.A., Highlander S.K., RA Nelson K.E., Wilson B.A.; RT "Comparative genomics of Gardnerella vaginalis strains reveals RT substantial differences in metabolic and virulence potential."; RL PLoS ONE 5:E12411-E12411(2010). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002104; ADP38608.1; -; Genomic_DNA. DR RefSeq; WP_013399502.1; NC_014644.1. DR RefSeq; YP_003985631.1; NC_014644.1. DR ProteinModelPortal; E3D964; -. DR EnsemblBacteria; ADP38608; ADP38608; HMPREF0421_20526. DR GeneID; 9904079; -. DR KEGG; gvg:HMPREF0421_20526; -. DR PATRIC; fig|525284.18.peg.524; -. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000001453; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000001453}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000001453}. FT DOMAIN 268 434 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 489 AA; 53367 MW; E248C2C71285C3C7 CRC64; MPEHKNEHKD VLSGHSEVLL DSTNTGSSLE SNDEAWQERE SRNALKRVAG LGELQDVTEV EYRKLRLERV VLVGVWSSAR GTLSQAEESL RELAALAKTA GAVVCDGMLQ QRYRPDAATY VGSGKARELA AVVAQNDADT IVVDDDLPPS QRRALEDATK VKVVDRTAVI LDIFAQHATS REGKAQVELA QLQYMLPRLR GWGAALSRQA GGRAAGDAGI GSRGPGETKI EMDRRAIRNR ISKLRHDIAL MAPTRETKRG SRRRQDIPTV AVVGYTNAGK SSIINRLTGS KELVENALFA TLDTAVRKSL TKDGRAYTLV DTVGFVRRLP TQLVEAFKST LEEVGNADVI LHVVDGSHPD PVSQIEAVNE VLAQIDGVED IAQIIAFNKS DVMQEPMRLR LQSLYPDSLI VSAASGTNID RLRTRIENLL PSPHVHVKVT LPYSDYSGSL LSRVRENGIV KSAEYKDSGV ELDAFVGDSL AAKLMQIAL // ID E3DPG5_HALPG Unreviewed; 409 AA. AC E3DPG5; DT 11-JAN-2011, integrated into UniProtKB/TrEMBL. DT 11-JAN-2011, sequence version 1. DT 07-JUN-2017, entry version 47. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Hprae_1600 {ECO:0000313|EMBL:ADO77727.1}; OS Halanaerobium praevalens (strain ATCC 33744 / DSM 2228 / GSL). OC Bacteria; Firmicutes; Clostridia; Halanaerobiales; Halanaerobiaceae; OC Halanaerobium. OX NCBI_TaxID=572479 {ECO:0000313|EMBL:ADO77727.1, ECO:0000313|Proteomes:UP000006866}; RN [1] {ECO:0000313|Proteomes:UP000006866} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33744 / DSM 2228 / GSL RC {ECO:0000313|Proteomes:UP000006866}; RG US DOE Joint Genome Institute (JGI-PGF); RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., RA Tice H., Bruce D., Goodwin L., Pitluck S., Kyrpides N., Mavromatis K., RA Ivanova N., Ovchinnikova G., Chertkov O., Detter J.C., Han C., RA Larimer F., Land M., Hauser L., Markowitz V., Cheng J.-F., RA Hugenholtz P., Woyke T., Wu D., Tindall B., Pomrenke H.G., RA Brambilla E., Klenk H.-P., Eisen J.A.; RT "The complete genome of Halanaerobium praevalens DSM 2228."; RL Submitted (OCT-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002175; ADO77727.1; -; Genomic_DNA. DR RefSeq; WP_014553747.1; NC_017455.1. DR ProteinModelPortal; E3DPG5; -. DR STRING; 572479.Hprae_1600; -. DR EnsemblBacteria; ADO77727; ADO77727; Hprae_1600. DR KEGG; hpk:Hprae_1600; -. DR PATRIC; fig|572479.3.peg.1620; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000006866; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000006866}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000006866}. FT DOMAIN 189 354 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 151 178 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 409 AA; 46674 MW; 4FA65C4A37AAF8BC CRC64; MYKIKTKAEK AVLVGLKEEE LTELELLVET AGAETILKMT YHDRKIDPAY YIGSGKVKEI KNAAETLQAN LIVFDNELSP VQQRNLEDQI EIKVIDRSQV ILDIFALHAH SRESKIQVEL AQLEYRLPRL QGRGIEMSRL AGGIGTRGPG ESQLEVDRRR IEEKIHRLKE SLKEIKASRK VQRSNRKDPM VAIVGYTNAG KSTLINNLAA ANSYTADKLF ATLDSTMRKF ELPVGQNIII SDTVGFISKL PHQLIASFRT TLEEIENADL ILHLIDASNS DIEKNIKIVN QEIRKLKKSK AKVIKVFNKI DLIKKSKLAD FKIIYPNSIF ISALKKINIE SIIDKLNEVI KSEMIEIELD LPYEKANWVE KIHNQAQVYQ EKYQKNNIYL KALVPKIMAN KLKKYSREA // ID E3E4P2_PAEPS Unreviewed; 428 AA. AC E3E4P2; DT 11-JAN-2011, integrated into UniProtKB/TrEMBL. DT 11-JAN-2011, sequence version 1. DT 07-JUN-2017, entry version 50. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:ADO56941.1}; GN ORFNames=PPSC2_13935 {ECO:0000313|EMBL:ADO56941.1}; OS Paenibacillus polymyxa (strain SC2) (Bacillus polymyxa). OC Bacteria; Firmicutes; Bacilli; Bacillales; Paenibacillaceae; OC Paenibacillus. OX NCBI_TaxID=886882 {ECO:0000313|EMBL:ADO56941.1, ECO:0000313|Proteomes:UP000006868}; RN [1] {ECO:0000313|EMBL:ADO56941.1, ECO:0000313|Proteomes:UP000006868} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SC2 {ECO:0000313|EMBL:ADO56941.1, RC ECO:0000313|Proteomes:UP000006868}; RX PubMed=21037012; DOI=10.1128/JB.01234-10; RA Ma M., Wang C., Ding Y., Li L., Shen D., Jiang X., Guan D., Cao F., RA Chen H., Feng R., Wang X., Ge Y., Yao L., Bing X., Yang X., Li J., RA Du B.; RT "Complete genome sequence of Paenibacillus polymyxa SC2, a strain of RT plant growth-promoting Rhizobacterium with broad-spectrum RT antimicrobial activity."; RL J. Bacteriol. 193:311-312(2011). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002213; ADO56941.1; -; Genomic_DNA. DR RefSeq; WP_013371541.1; NC_014622.2. DR ProteinModelPortal; E3E4P2; -. DR STRING; 886882.PPSC2_c2980; -. DR EnsemblBacteria; ADO56941; ADO56941; PPSC2_13935. DR GeneID; 25387424; -. DR KEGG; ppm:PPSC2_13935; -. DR PATRIC; fig|886882.15.peg.2977; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000006868; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000006868}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000006868}. FT DOMAIN 208 372 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 167 194 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 428 AA; 47983 MW; 9F387F8D09DBCB22 CRC64; MANSTHDTQT EMQDKAVLVS LITDEVKRSG INTEYSLEEL VKLAETAGVE VLSVLTQNRE SKDSKWFIGK GKVDELRAVA EELGANTAIF DQELSGAQVR NLEESLDLKI IDRTQLILDI FAQRAKTREG IIQVELAQLS YLLPRLSGHG KNLSRLGGGI GTRGPGESKL ETDRRHIRDR ISDLKRQLEE VTRHRYLHRE RRQKAGIVQV ALVGYTNAGK STLLKQLTAA DVYIENQLFA TLDPTSRTME LPSGKEVILT DTVGFIQNLP HDLVASFRAT LEEANEAHLI LHVVDASSDM RDEQMKVVES ILQQLGAADK PQIVLFNKKD ACTPEQLEML PSGEGYLKIS AFDEADLLRI RELVQEHLSG DTLRFRIPAE RGDLTSVLYR IGDVLLTEYD GNDVIYEVEI QRGEYEKYGH ALSEFTES // ID E3F1K9_KETVY Unreviewed; 432 AA. AC E3F1K9; DT 11-JAN-2011, integrated into UniProtKB/TrEMBL. DT 11-JAN-2011, sequence version 1. DT 07-JUN-2017, entry version 49. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=EIO_1410 {ECO:0000313|EMBL:ADO42543.1}; OS Ketogulonicigenium vulgare (strain Y25). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae; Ketogulonicigenium. OX NCBI_TaxID=880591 {ECO:0000313|EMBL:ADO42543.1, ECO:0000313|Proteomes:UP000006871}; RN [1] {ECO:0000313|EMBL:ADO42543.1, ECO:0000313|Proteomes:UP000006871} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Y25 {ECO:0000313|EMBL:ADO42543.1, RC ECO:0000313|Proteomes:UP000006871}; RX PubMed=21037005; DOI=10.1128/JB.01189-10; RA Xiong X.H., Han S., Wang J.H., Jiang Z.H., Chen W., Jia N., Wei H.L., RA Cheng H., Yang Y.X., Zhu B., You S., He J.Y., Hou W., Chen M.X., RA Yu C.J., Jiao Y.H., Zhang W.C.; RT "Complete genome sequence of the bacterium Ketogulonicigenium vulgare RT Y25."; RL J. Bacteriol. 193:315-316(2011). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002224; ADO42543.1; -; Genomic_DNA. DR RefSeq; WP_013384194.1; NC_014625.1. DR ProteinModelPortal; E3F1K9; -. DR EnsemblBacteria; ADO42543; ADO42543; EIO_1410. DR KEGG; kvu:EIO_1410; -. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000006871; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000006871}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000006871}. FT DOMAIN 204 373 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 170 197 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 432 AA; 47914 MW; BD52D0C9C53C9897 CRC64; MLNHQQVDTP AWIVHPEIKS DVSRREADAA LDEAKALADA LPGLDVLGAE IVRLPKVHAG MLFGSGKVQE LKERITAHGV KLVLIDGALS PVQQRNLERE WGVKILDRMS LILEIFSDRA RTREGVLQVE IAALSYQRTR LVRAWTHLER QRGGFGFVGG PGETQRENDR RAIDEQLLRL ERQLEKVQKT RALHRAARAK VPYPIVALVG YTNAGKSSLF NRVTGADVLA KDQLFATLDP TMRRLTLPDG QEVIMSDTVG FISDLPTQLV AAFRATLEEV LEADLILHVR DISHPQTAQQ ARDVMQILHQ IGVPEDAPML EVLNKIDLLD EAGREAFQTE AARKDAKIAV SALTGEGVEA LLEQISAALA PPFLIEDLRL PHTAGKLRAW LYAEGVVEGE VRDDFGMTLS LKWTQVQSAR FNKMRDGMGK AE // ID E3GP41_EUBLK Unreviewed; 603 AA. AC E3GP41; DT 11-JAN-2011, integrated into UniProtKB/TrEMBL. DT 11-JAN-2011, sequence version 1. DT 07-JUN-2017, entry version 48. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=ELI_2664 {ECO:0000313|EMBL:ADO37645.1}; OS Eubacterium limosum (strain KIST612). OC Bacteria; Firmicutes; Clostridia; Clostridiales; Eubacteriaceae; OC Eubacterium. OX NCBI_TaxID=903814 {ECO:0000313|EMBL:ADO37645.1, ECO:0000313|Proteomes:UP000006873}; RN [1] {ECO:0000313|Proteomes:UP000006873} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=KIST612 {ECO:0000313|Proteomes:UP000006873}; RA Roh H., Ko H.-J., Kim D., Choi D.G., Park S., Kim S., Kim K.H., RA Chang I.S., Choi I.-G.; RT "The genome sequence of Eubacterium limosum (strain KIST612)."; RL Submitted (SEP-2010) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=KIST612; RA Roh H., Ko H.-J., Kim D., Choi D.G., Park S., Kim S., Kim K.H., RA Chang I.S., Choi I.-G.; RL Submitted (SEP-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002273; ADO37645.1; -; Genomic_DNA. DR RefSeq; WP_013380966.1; NC_014624.2. DR ProteinModelPortal; E3GP41; -. DR STRING; 903814.ELI_2664; -. DR EnsemblBacteria; ADO37645; ADO37645; ELI_2664. DR KEGG; elm:ELI_2664; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; EREVIIT; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000006873; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000006873}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000006873}. FT DOMAIN 379 546 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 338 368 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 603 AA; 67137 MW; A9135CEF7C5613EE CRC64; MTEVKAEGVR RSILEELNKL IGYTMENQVL LDEDVLAVLV RLTKTLGREI LVMTNDKSKI EYVGIGDASK VPLDHSRVQE NRKGLNRIRV IHTHPGGNPH LSEEDFSASD HLSVECMVAV GVGEDKPVLF GIGAPVVKDG QVVYGMGICE SLGQLNRFPL ENYVLAANRA LRRDPGAGFD LEGERERALL IGVEVNGSRG GIDLEESMEE LARLVETAEG DVAEVVTQHR PQVDPVFYVG RGKLLEILKI IQNKDINLIV ANDELSANQI GNIEGITGVK TIDRTTIILD IFARQAKTRE GKLQVELAQQ KYRLSHLKGL GIVLSRTGGG IGTRGPGEKK LETDRRHIRR QIDELERKNA KINQTNELNA KGRKKNNIRT VSLIGYTNSG KSTLFNVLTE SDAVIKDGLF ITLDSTIRKV RPEAGDYLVS DTVGFIEKLP HELIKAFKTT LKEVETADLL LHVVDASNPN YKSQIEVVNQ VLRDIGSGHK KVLMVYNKMD RLPPEERERF ENRAARAGDA ICISAREKWH IGALTEIIDG DLRGMSLEKT YCIPYEDSRA MAVLHEKSTV LDTRYDEGGT RVRVSINADF PAHQYEKYEV EAE // ID E3H0F0_ROTDC Unreviewed; 549 AA. AC E3H0F0; DT 11-JAN-2011, integrated into UniProtKB/TrEMBL. DT 11-JAN-2011, sequence version 1. DT 07-JUN-2017, entry version 52. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:ADP41044.1}; GN OrderedLocusNames=HMPREF0733_11587 {ECO:0000313|EMBL:ADP41044.1}; OS Rothia dentocariosa (strain ATCC 17931 / CDC X599 / XDIA). OC Bacteria; Actinobacteria; Micrococcales; Micrococcaceae; Rothia. OX NCBI_TaxID=762948 {ECO:0000313|EMBL:ADP41044.1, ECO:0000313|Proteomes:UP000000387}; RN [1] {ECO:0000313|Proteomes:UP000000387} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 17931 / CDC X599 / XDIA RC {ECO:0000313|Proteomes:UP000000387}; RA Muzny D., Qin X., Buhay C., Dugan-Rocha S., Ding Y., Chen G., RA Hawes A., Holder M., Jhangiani S., Johnson A., Khan Z., Li Z., Liu W., RA Liu X., Perez L., Shen H., Wang Q., Watt J., Xi L., Xin Y., Zhou J., RA Deng J., Jiang H., Liu Y., Qu J., Song X.-Z., Zhang L., Villasana D., RA Johnson A., Liu J., Liyanage D., Lorensuhewa L., Robinson T., Song A., RA Song B.-B., Dinh H., Thornton R., Coyle M., Francisco L., Jackson L., RA Javaid M., Korchina V., Kovar C., Mata R., Mathew T., Ngo R., RA Nguyen L., Nguyen N., Okwuonu G., Ongeri F., Pham C., Simmons D., RA Wilczek-Boney K., Hale W., Jakkamsetti A., Pham P., Ruth R., RA San Lucas F., Warren J., Zhang J., Zhao Z., Zhou C., Zhu D., Lee S., RA Bess C., Blankenburg K., Forbes L., Fu Q., Gubbala S., Hirani K., RA Jayaseelan J.C., Lara F., Munidasa M., Palculict T., Patil S., RA Pu L.-L., Saada N., Tang L., Weissenberger G., Zhu Y., Hemphill L., RA Shang Y., Youmans B., Ayvaz T., Ross M., Santibanez J., Aqrawi P., RA Gross S., Joshi V., Fowler G., Nazareth L., Reid J., Worley K., RA Petrosino J., Highlander S., Gibbs R.; RT "The complete genome of Rothia dentocariosa ATCC 17931."; RL Submitted (OCT-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002280; ADP41044.1; -; Genomic_DNA. DR RefSeq; WP_013398767.1; NC_014643.1. DR ProteinModelPortal; E3H0F0; -. DR STRING; 762948.HMPREF0733_11587; -. DR EnsemblBacteria; ADP41044; ADP41044; HMPREF0733_11587. DR GeneID; 29742375; -. DR KEGG; rdn:HMPREF0733_11587; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000000387; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000000387}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000000387}. FT DOMAIN 304 469 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 549 AA; 60355 MW; F59AE18EBD80C3B3 CRC64; MKLTDTSFSS EKLPSDEQLR RTVERVLGRA DAAAQTTIYP ESTGSTAQRR VLDTRAREIS DNQREHSEFD GEQEDLAERR ALRRVAGLST ELDDVTEVEY RQLRLERVVL AGLWTEGTVE DAENSLRELA ALAETAGSEV LDGLVQRRLK PDPGTFLGSG KALELKDIVE ASGADTVIVD SELAPSQRRA LEDIVKVKVI DRTALILDIF AQHAKSREGK AQVELAQLEY MLPRLRGWGA SLSRQAGGRA ASGEGIGSRG PGETKIEMDR RRLRARMAKL KREIAAMAPA RETKRLSRKR NRVPSVAIAG YTNAGKSSLL NRLTDAGVLV ENALFATLDP TVRKAQTPDG IGYTLSDTVG FVRSLPTQLV EAFRSTLEEV ADADVILHVV DASHPDPEGQ IRAVREVIAD LDARRIPEII ALNKADAADP FILERMRQRE SNHVIVSART GEGIDELKQK IADTIPRPSL EVKLLIPYNH GEVISRLHAW DAEIKSTAFV SDGTFVTALV REDVAAELSD YVIDGELLEV LELELQDSAS EPENVCELA // ID E3HD59_ILYPC Unreviewed; 441 AA. AC E3HD59; DT 11-JAN-2011, integrated into UniProtKB/TrEMBL. DT 11-JAN-2011, sequence version 1. DT 07-JUN-2017, entry version 52. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Ilyop_2780 {ECO:0000313|EMBL:ADO84535.1}; OS Ilyobacter polytropus (strain DSM 2926 / CuHBu1). OG Plasmid pILYOP01 {ECO:0000313|EMBL:ADO84535.1, OG ECO:0000313|Proteomes:UP000006875}. OC Bacteria; Fusobacteria; Fusobacteriales; Fusobacteriaceae; Ilyobacter. OX NCBI_TaxID=572544 {ECO:0000313|EMBL:ADO84535.1, ECO:0000313|Proteomes:UP000006875}; RN [1] {ECO:0000313|EMBL:ADO84535.1, ECO:0000313|Proteomes:UP000006875} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 2926 / CuHBu1 {ECO:0000313|Proteomes:UP000006875}; RX PubMed=21304735; RA Sikorski J., Chertkov O., Lapidus A., Nolan M., Lucas S., RA Del Rio T.G., Tice H., Cheng J.F., Tapia R., Han C., Goodwin L., RA Pitluck S., Liolios K., Ivanova N., Mavromatis K., Mikhailova N., RA Pati A., Chen A., Palaniappan K., Land M., Hauser L., Chang Y.J., RA Jeffries C.D., Brambilla E., Yasawong M., Rohde M., Pukall R., RA Spring S., Goker M., Woyke T., Bristow J., Eisen J.A., Markowitz V., RA Hugenholtz P., Kyrpides N.C., Klenk H.P.; RT "Complete genome sequence of Ilyobacter polytropus type strain RT (CuHbu1)."; RL Stand. Genomic Sci. 3:304-314(2010). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002282; ADO84535.1; -; Genomic_DNA. DR RefSeq; WP_013389187.1; NC_014633.1. DR ProteinModelPortal; E3HD59; -. DR EnsemblBacteria; ADO84535; ADO84535; Ilyop_2780. DR KEGG; ipo:Ilyop_2780; -. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000006875; Plasmid pILYOP01. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000006875}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Plasmid {ECO:0000313|EMBL:ADO84535.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000006875}. FT DOMAIN 209 382 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 175 202 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 441 AA; 50296 MW; 4049E6D135543665 CRC64; MINISSEYIF NKNIRGRAIL AGLDVYQKGE SINLEDSLNE LKELAGAASI EVIDIITQSR EKMESSTYMG KGKIEEIRDQ AIRKNADMVI FDDELSGIQI RNLERIIGVE IIDRTSLILD IFGHRAKSKE GKLQVELAML KYQKPRLIGL GGELSRTGAG IGTRGLGETK LELDRRVISK RISDIEKELE EVKKQREVQR KQRKRTSIPT VALVGYTNAG KSTIMNHLMQ MEEEEDTRTK SFVKDMLFAT LDPFHRKIKL EDNLEFILID TVGFVSKLPH DLVESFKSTL EEVEEASLLL YVVDISREDY KHQLKVTRNV VEELNVKDTP FLVVYNKIDK LSSEELEKTG DIFEKSVYIS AIEGKGIGEL LKEIEKEIFK TSKEVTLLIP FSRGDISSYI LDSTRVIQQE YTGDGLLVTT FLKPEDVEKY KQYILKDSDK D // ID E3I5Y7_RHOVT Unreviewed; 462 AA. AC E3I5Y7; DT 11-JAN-2011, integrated into UniProtKB/TrEMBL. DT 11-JAN-2011, sequence version 1. DT 07-JUN-2017, entry version 48. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Rvan_1318 {ECO:0000313|EMBL:ADP70580.1}; OS Rhodomicrobium vannielii (strain ATCC 17100 / ATH 3.1.1 / DSM 162 / OS LMG 4299). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Hyphomicrobiaceae; Rhodomicrobium. OX NCBI_TaxID=648757 {ECO:0000313|EMBL:ADP70580.1, ECO:0000313|Proteomes:UP000001399}; RN [1] {ECO:0000313|Proteomes:UP000001399} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 17100 / ATH 3.1.1 / DSM 162 / LMG 4299 RC {ECO:0000313|Proteomes:UP000001399}; RX PubMed=21705585; DOI=10.1128/JB.05453-11; RG US DOE Joint Genome Institute; RA Brown P.J., Kysela D.T., Buechlein A., Hemmerich C., Brun Y.V.; RT "Genome sequences of eight morphologically diverse RT alphaproteobacteria."; RL J. Bacteriol. 193:4567-4568(2011). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002292; ADP70580.1; -; Genomic_DNA. DR RefSeq; WP_013418982.1; NC_014664.1. DR ProteinModelPortal; E3I5Y7; -. DR STRING; 648757.Rvan_1318; -. DR EnsemblBacteria; ADP70580; ADP70580; Rvan_1318. DR KEGG; rva:Rvan_1318; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000001399; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000001399}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000001399}. FT DOMAIN 231 404 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 462 AA; 50036 MW; 00C1F50EAF68B783 CRC64; MKTLERSERA AQRAGINDGE TTAGDDDGAT RAIVIVPVLK GQSGPQGAFA LALSSEERLE EAVGLAIAIG LDVAFSGTVP LAQIKPAALL GTGKVEEIGA IIAAEGVSVA IVDHPLTPIQ QRNLEKAWNA KVLDRTGLIL EIFAERARSK EGRLQVELAR LTYQKSRLVR SWTHLERQRG GFGFLGGPGE TQIEADRRAI GERIDVIKND LAVSERTRRL HRKRRKETDQ QIVSLVGYTN AGKSTLFNAL SGAGVLAKDM LFATLDPTLR RVEFADGGAF ILSDTVGFIS DLPTQLIVAF HATLEEILEA DLILHVRDIA SASSEAQKIE VERVLAEIGI DAAAQASRVI EVWNKSDLLS EDERSAVGKR AENAAHPAGL VSAQTGEGVP ELAAAIRIRL QAHLRTRDVV VGEADGAFIH WLYENTEVID RQGREDGSQL FQVRVAPERE HDLDLHIARP GS // ID E3J143_FRAIE Unreviewed; 482 AA. AC E3J143; DT 11-JAN-2011, integrated into UniProtKB/TrEMBL. DT 11-JAN-2011, sequence version 1. DT 05-JUL-2017, entry version 50. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=FraEuI1c_1148 {ECO:0000313|EMBL:ADP79221.1}; OS Frankia inefficax (strain DSM 45817 / CECT 9037 / EuI1c). OC Bacteria; Actinobacteria; Frankiales; Frankiaceae; Frankia. OX NCBI_TaxID=298654 {ECO:0000313|EMBL:ADP79221.1, ECO:0000313|Proteomes:UP000002484}; RN [1] {ECO:0000313|EMBL:ADP79221.1, ECO:0000313|Proteomes:UP000002484} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 45817 / CECT 9037 / EuI1c RC {ECO:0000313|Proteomes:UP000002484}; RG US DOE Joint Genome Institute; RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L., RA Pitluck S., Chertkov O., Detter J.C., Han C., Tapia R., Land M., RA Hauser L., Jeffries C., Kyrpides N., Ivanova N., Mikhailova N., RA Beauchemin N., Sen A., Sur S.A., Gtari M., Wall L., Tisa L., Woyke T.; RT "Complete sequence of Frankia sp. EuI1c."; RL Submitted (OCT-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002299; ADP79221.1; -; Genomic_DNA. DR ProteinModelPortal; E3J143; -. DR STRING; 298654.FraEuI1c_1148; -. DR EnsemblBacteria; ADP79221; ADP79221; FraEuI1c_1148. DR KEGG; fri:FraEuI1c_1148; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000002484; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000002484}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000002484}. FT DOMAIN 260 424 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 219 253 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 482 AA; 51840 MW; 7B74E6DD7A0E9AD9 CRC64; MLATDNALED AADSGEITFT GLGFYDDAGD ELAVEERGAL RRMQGLATEL TDVTEVEYRQ LRLERVVLIG VWTVGTIVDA ETSMAELAQL AETAGSVVLD ALVQRRDKPD TATYVGSGKA KELAEVVRAA GADTVICDGE LTPGQLRQLE EVVKVKVIDR TALILDIFAQ HATSKEGKAQ VELAQLQYML PRLRGWGESM SRQAASGGRA PIGTRGPGET KIETDRRRLR ARIAKLRREL REMETVRETK RSSRKRGEVP SVAIAGYTNA GKSSLLNRLT GAGVLVEDAL FATLDPTVRR ATLPDGRAFT LTDTVGFVRH LPHQIVEAFR STLEEVADAD LILHVVDGSH ADPVGQLSAV REVLNDIDAG DVPELVIVNK TDIADKTTVA AIRRVAPDAV CVSARTGAGI AELVEALATR VPHPQVEVDV VVPYNRGDLV ARVHESGEVL HQGHNATGTE LRARVSAALA AELGAYRAPA RV // ID E3MHB2_CAERE Unreviewed; 453 AA. AC E3MHB2; DT 11-JAN-2011, integrated into UniProtKB/TrEMBL. DT 11-JAN-2011, sequence version 1. DT 30-AUG-2017, entry version 37. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EFP01947.1}; GN ORFNames=CRE_22804 {ECO:0000313|EMBL:EFP01947.1}; OS Caenorhabditis remanei (Caenorhabditis vulgaris). OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida; OC Rhabditoidea; Rhabditidae; Peloderinae; Caenorhabditis. OX NCBI_TaxID=31234 {ECO:0000313|Proteomes:UP000008281}; RN [1] {ECO:0000313|Proteomes:UP000008281} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=PB4641 {ECO:0000313|Proteomes:UP000008281}; RG Caenorhabditis remanei Sequencing Consortium; RA Wilson R.K.; RT "PCAP assembly of the Caenorhabditis remanei genome."; RL Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; DS268445; EFP01947.1; -; Genomic_DNA. DR RefSeq; XP_003104346.1; XM_003104298.1. DR ProteinModelPortal; E3MHB2; -. DR STRING; 31234.CRE22804; -. DR EnsemblMetazoa; CRE22804; CRE22804; WBGene00062883. DR GeneID; 9803177; -. DR CTD; 9803177; -. DR eggNOG; KOG0410; Eukaryota. DR eggNOG; COG2262; LUCA. DR InParanoid; E3MHB2; -. DR OMA; MDTVGFM; -. DR OrthoDB; EOG091G0852; -. DR Proteomes; UP000008281; Unassembled WGS sequence. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR CDD; cd01878; HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008281}; KW Reference proteome {ECO:0000313|Proteomes:UP000008281}. FT DOMAIN 222 392 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 453 AA; 50430 MW; EC45248327080751 CRC64; MGRADVATTS SKFANGQWSV LVVHPKVRWG SGSASVLKQA DRQLEEAVAL VNNLPNMIAV DSLIMPVDYN TKRKSIWAAG NLEKLVARRE TARATALMVN VDVLSPAQQE ELFGIFEVPI FDRYNIVLST FKEFARTDEA RLQISLAEIP YIKHRIHALA SKRLHSRPEI LHVEQQYAEI EGGDLNEILR KREQDLRRDL KEATRRATEQ QSGGSKHSSD AAVIAVVGYT NTGKTSLVKR LTGAESLKPK DQLFATLDTT RHVAKLPSGR SAVFTDTIGF LSDLPIHLIA AFEATLAHVK SADVIIHLRD VSNPDWKAQE EDVVATLKSI GVAREVMAER MITVDNKIDK DTSVDSPESS LSESSSIRIS CKTGDGMAEL IGVINEKVSI ATKCKTIRLR LDVRSPVIEW LYHNEFVVVE PISDGNMLIF DVVMNESEIG RFRKKFAHLK RKN // ID E3MHM7_CAERE Unreviewed; 731 AA. AC E3MHM7; DT 11-JAN-2011, integrated into UniProtKB/TrEMBL. DT 11-JAN-2011, sequence version 1. DT 30-AUG-2017, entry version 28. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EFP01963.1}; GN ORFNames=CRE_22870 {ECO:0000313|EMBL:EFP01963.1}; OS Caenorhabditis remanei (Caenorhabditis vulgaris). OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida; OC Rhabditoidea; Rhabditidae; Peloderinae; Caenorhabditis. OX NCBI_TaxID=31234 {ECO:0000313|Proteomes:UP000008281}; RN [1] {ECO:0000313|Proteomes:UP000008281} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=PB4641 {ECO:0000313|Proteomes:UP000008281}; RG Caenorhabditis remanei Sequencing Consortium; RA Wilson R.K.; RT "PCAP assembly of the Caenorhabditis remanei genome."; RL Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; DS268445; EFP01963.1; -; Genomic_DNA. DR RefSeq; XP_003104362.1; XM_003104314.1. DR ProteinModelPortal; E3MHM7; -. DR STRING; 31234.CRE22870; -. DR EnsemblMetazoa; CRE22870; CRE22870; WBGene00062888. DR GeneID; 9803213; -. DR CTD; 9803213; -. DR eggNOG; KOG0410; Eukaryota. DR eggNOG; KOG1066; Eukaryota. DR eggNOG; COG1501; LUCA. DR eggNOG; COG2262; LUCA. DR OrthoDB; EOG091G0852; -. DR Proteomes; UP000008281; Unassembled WGS sequence. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR025887; Glyco_hydro_31_N_dom. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR Pfam; PF13802; Gal_mutarotas_2; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 4: Predicted; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000008281}; KW Reference proteome {ECO:0000313|Proteomes:UP000008281}. FT DOMAIN 222 297 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 662 689 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 731 AA; 83100 MW; 0EA374BBCF58689C CRC64; MGIADVATTS SKFANGQWSV LVVHPKVRWG SGSASVLKQA DRQLEEAVAL VNNLPNMIAV DSLIMPVDYN TKRKSIGATG NLEKLVARRE TARATALMVN VDVLSPAQQE ELFGIFEVPI FDRYNIVLST FKEFARTDEA RLQISLAEIP YIKHRIHALA SKRLNSRPEI LHVEQQCAEI EGGDLNEILR KRGQDLRRNL KEATRRATEQ QSGGSKHSSD AAVIAVVGYT NAGKTSLVKR LTGAESLKPK DQLFATLDTT RHVAKLPSGR STVFTDTIGF LSDLPIHLIA AFEATLAHVK SAVNMIHVLL LLLLFPSTIN TVTQDDASHY ELLPKSIQHD AAVWSAVLRN SQNMMMLNVV GMTNSTMRIQ IDNSETAIRK RYIKRTSSLT LPEELAFESV ENGQQEAEIV GGNKKLKVVV TYKPFLVNVI NEYDELVLQV NKYQKLKIEE FKSFIDRKQY GSNSVGVDIA FVNFKTAYGL PEHADAFALR NTVGNTDPYQ LYNYAEYTSV LYGFNYPYFM AHFNDRAAGF LWYNSLKTVF SSYNGNRTCQ HDSKKNAKNW SEDSVCSLVS EDGRADILLF LGPLRSLPKS HTRVGAILND KYFLEFYAKS NLEKAVPIMT LEQQIRKLNQ PEDARTQIDC LETPLVKYFI DKEYRRRSDY DVRKAKRELK KAEKHKNPLR RRLQEASEDF EMKANRVMTE KEKEKLEKIE ARRKEKNAIR KQKFWRKRRG N // ID E3PRE3_ACESD Unreviewed; 432 AA. AC E3PRE3; DT 11-JAN-2011, integrated into UniProtKB/TrEMBL. DT 11-JAN-2011, sequence version 1. DT 07-JUN-2017, entry version 44. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=CLOST_1327 {ECO:0000313|EMBL:CBH21447.1}; OS Acetoanaerobium sticklandii (strain ATCC 12662 / DSM 519 / JCM 1433 / OS NCIMB 10654) (Clostridium sticklandii). OC Bacteria; Firmicutes; Clostridia; Clostridiales; OC Peptostreptococcaceae; Acetoanaerobium. OX NCBI_TaxID=499177 {ECO:0000313|EMBL:CBH21447.1, ECO:0000313|Proteomes:UP000007041}; RN [1] {ECO:0000313|Proteomes:UP000007041} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 12662 / DSM 519 / JCM 1433 / NCIMB 10654 RC {ECO:0000313|Proteomes:UP000007041}; RX PubMed=20937090; DOI=10.1186/1471-2164-11-555; RA Fonknechten N., Chaussonnerie S., Tricot S., Lajus A., Andreesen J.R., RA Perchat N., Pelletier E., Gouyvenoux M., Barbe V., Salanoubat M., RA Le Paslier D., Weissenbach J., Cohen G.N., Kreimeyer A.; RT "Clostridium sticklandii, a specialist in amino acid RT degradation:revisiting its metabolism through its genome sequence."; RL BMC Genomics 11:555-555(2010). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; FP565809; CBH21447.1; -; Genomic_DNA. DR ProteinModelPortal; E3PRE3; -. DR STRING; 499177.CLOST_1327; -. DR EnsemblBacteria; CBH21447; CBH21447; CLOST_1327. DR KEGG; cst:CLOST_1327; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR BioCyc; CSTI499177:GJE9-1375-MONOMER; -. DR Proteomes; UP000007041; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000007041}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000007041}. FT DOMAIN 206 376 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 432 AA; 49396 MW; 16CF788E8F5FB01D CRC64; MEDNMNKLEE RMILVGLNVT DYKKNTSSTK IEESMIELEE LAKAAGGNVL GSIIQNRDNY DVAYYLGKGK AEEIKEYANN MQANLIVFNE ELSGAQIRNL EEIIGLDIID RTALILDIFA KRALSREGKL QVELAQYKYR LPRLIGVGKE MSRLGGGIGT KGPGEKKLET DKRHIRERIY DIQRELKEIK KNREIQRSKR LKSNLPIVAL VGYTNSGKST LLNKLIQSHR EYSADKDVFV KDMLFATLDV SLRKAILPSN KEYLITDTVG FVSDLPHYLV EAFKATLEEV SYADLLLHVV DSSNEHFNLQ IDTTLGVLKE IGAADKPMIY VFNKADKVNY ELDYKPKDEY VFISAKTGYN NEQLLQKIEC HINSNLKKVK LLIPFSNGEV INSLHKKYNF EENYSEEGIL VQIDITEEDY GRYKKYIVEE VL // ID E4KNI5_9LACT Unreviewed; 409 AA. AC E4KNI5; DT 08-FEB-2011, integrated into UniProtKB/TrEMBL. DT 08-FEB-2011, sequence version 1. DT 07-JUN-2017, entry version 41. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:EFR31487.1}; GN ORFNames=HMPREF9257_0348 {ECO:0000313|EMBL:EFR31487.1}; OS Eremococcus coleocola ACS-139-V-Col8. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Aerococcaceae; OC Eremococcus. OX NCBI_TaxID=908337 {ECO:0000313|EMBL:EFR31487.1, ECO:0000313|Proteomes:UP000005990}; RN [1] {ECO:0000313|EMBL:EFR31487.1, ECO:0000313|Proteomes:UP000005990} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ACS-139-V-Col8 {ECO:0000313|EMBL:EFR31487.1, RC ECO:0000313|Proteomes:UP000005990}; RA Durkin A.S., Madupu R., Torralba M., Gillis M., Methe B., Sutton G., RA Nelson K.E.; RL Submitted (OCT-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EFR31487.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AENN01000011; EFR31487.1; -; Genomic_DNA. DR ProteinModelPortal; E4KNI5; -. DR STRING; 908337.HMPREF9257_0348; -. DR EnsemblBacteria; EFR31487; EFR31487; HMPREF9257_0348. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000005990; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000005990}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000005990}. FT DOMAIN 204 362 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 409 AA; 46420 MW; B64025BEBBE109DA CRC64; MHQTNQTHKA MDRVLIVAVQ TPEMADKNMS VLLNEMKDLV KAAGGEVLAS VQQNLPHVDG RTLVGSGKLE EIQAQIEVED IDLVVTYNQL SPRVNQNLSQ NLGVNVIDRI QLILDIFALR ARSREGKLQV ELAQYNYLLP RIIGQGQAMS RLGAGIGTRG PGETKLETDR RHIRQRMLTI KRELAKVESK RQQTRQRRRQ GKEFNLGLVG YTNAGKSTLL SQLTETETFI KDQVFATLDP LTRKLSLHGN DRFTITDTVG FIEDLPQELV QSFKSTLEEI RDVDLLLHVV DGSDPARVYH EQTVVDLLRE LDMLDIPTLT VYNKKDQMPS DFQATLFPNV ILSALDLSDI KALKEEIWRQ SMKLAQAFET YIDADQAQQI YALKQEAFVE SVDFDSDRNQ YKVKGYQMP // ID E4KY18_9FIRM Unreviewed; 429 AA. AC E4KY18; DT 08-FEB-2011, integrated into UniProtKB/TrEMBL. DT 08-FEB-2011, sequence version 1. DT 07-JUN-2017, entry version 37. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:EFR33173.1}; GN ORFNames=HMPREF9286_1426 {ECO:0000313|EMBL:EFR33173.1}; OS Peptoniphilus harei ACS-146-V-Sch2b. OC Bacteria; Firmicutes; Tissierellia; Tissierellales; Peptoniphilaceae; OC Peptoniphilus. OX NCBI_TaxID=908338 {ECO:0000313|EMBL:EFR33173.1, ECO:0000313|Proteomes:UP000003705}; RN [1] {ECO:0000313|EMBL:EFR33173.1, ECO:0000313|Proteomes:UP000003705} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ACS-146-V-Sch2b {ECO:0000313|EMBL:EFR33173.1, RC ECO:0000313|Proteomes:UP000003705}; RA Durkin A.S., Madupu R., Torralba M., Gillis M., Methe B., Sutton G., RA Nelson K.E.; RL Submitted (OCT-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EFR33173.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AENP01000012; EFR33173.1; -; Genomic_DNA. DR RefSeq; WP_005956086.1; NZ_AENP01000012.1. DR ProteinModelPortal; E4KY18; -. DR STRING; 908338.HMPREF9286_1426; -. DR EnsemblBacteria; EFR33173; EFR33173; HMPREF9286_1426. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000003705; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000003705}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000003705}. FT DOMAIN 206 375 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 165 199 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 429 AA; 49226 MW; B62C7EAC2E278399 CRC64; MDNVYLENLN SNKKLEKVIT VGTNIGAYPH SLETSMKELA ELVYADGAEV VGEVTQNIYK FNPKYLIGSG KVDEIKEMVE LLEVDAVVFN DELSGIQVRN LEKRIKKKVI DRTNLILDIF GLRATTYEAK LQVELARLEY QLPRLLGIDG WSRTGGGIGT RGPGEQIIET DRRRLKREID KIKEKLEKAK RTRDTTRERR IDSNIPIVSL VGYTNAGKST ILNRLKDEES GEVSVKNMLF ETLDPSSRKA RLLSGREFII SDTVGFVSKL PTKIVEAFKS TLEEIKYSDL ILHVIDASSE DLEIQYNTTM AILKDIEVLD KNIITVFNKV DRVDLYDINL PLRVMPDKKV YISALKDENM DSLLKIIEDN LDEKYFDVKL KFAYNDTDLL YKLVEKFDAK PIYEEDGIYL DLKLEEREYE KVKDYVVNV // ID E4NI22_KITSK Unreviewed; 499 AA. AC E4NI22; DT 08-FEB-2011, integrated into UniProtKB/TrEMBL. DT 08-FEB-2011, sequence version 1. DT 07-JUN-2017, entry version 46. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=KSE_53770 {ECO:0000313|EMBL:BAJ31152.1}; OS Kitasatospora setae (strain ATCC 33774 / DSM 43861 / JCM 3304 / KCC OS A-0304 / NBRC 14216 / KM-6054) (Streptomyces setae). OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae; OC Kitasatospora. OX NCBI_TaxID=452652 {ECO:0000313|EMBL:BAJ31152.1, ECO:0000313|Proteomes:UP000007076}; RN [1] {ECO:0000313|EMBL:BAJ31152.1, ECO:0000313|Proteomes:UP000007076} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33774 / DSM 43861 / JCM 3304 / KCC A-0304 / NBRC 14216 / RC KM-6054 {ECO:0000313|Proteomes:UP000007076}; RX PubMed=21059706; DOI=10.1093/dnares/dsq026; RA Ichikawa N., Oguchi A., Ikeda H., Ishikawa J., Kitani S., Watanabe Y., RA Nakamura S., Katano Y., Kishi E., Sasagawa M., Ankai A., Fukui S., RA Hashimoto Y., Kamata S., Otoguro M., Tanikawa S., Nihira T., RA Horinouchi S., Ohnishi Y., Hayakawa M., Kuzuyama T., Arisawa A., RA Nomoto F., Miura H., Takahashi Y., Fujita N.; RT "Genome sequence of Kitasatospora setae NBRC 14216T: an evolutionary RT snapshot of the family Streptomycetaceae."; RL DNA Res. 17:393-406(2010). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AP010968; BAJ31152.1; -; Genomic_DNA. DR RefSeq; WP_014138449.1; NC_016109.1. DR ProteinModelPortal; E4NI22; -. DR STRING; 452652.KSE_53770; -. DR EnsemblBacteria; BAJ31152; BAJ31152; KSE_53770. DR KEGG; ksk:KSE_53770; -. DR PATRIC; fig|452652.3.peg.5375; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000007076; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000007076}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000007076}. FT DOMAIN 278 442 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 237 271 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 499 AA; 54163 MW; D065DD858E9D154D CRC64; MTSTFDSRTR SGESANRLAD LKAEALMDED LAAIDEGLGN YDGAQYDRTE RAALRRVAGL STELQDVTEV EYRQLRLERV VLVGVWTDGT LEEAENSMAE LAALAETAGS EVLDGVIQRR DKPDAATYIG SGKAKELRDI VASTGADTVV CDGELTPGQL IHLEDVVKVK VVDRTALILD IFAQHAKSRE GKAQVSLAQM QYMLPRLRGW GQSLSRQMGG GGSGTSGGGM ATRGPGETKI ETDRRRIREK MAKLRKEIAE MKKGRDTKRQ ERRRNHVPSV AIAGYTNAGK SSLLNRLTGA GVLVENALFA TLDPTVRRAE TPSGRLYTLA DTVGFVRHLP HHLVEAFRST MEEVGDADLI LHVVDGSHPE PETQLAAVRE VIVSVDAQNV PEIVVINKAD AADPLVLQRL LRREPHAIVV SARSGQGIEE LLALIDRELP HPAVEVTVLV PYTRGDLVSR VHAEGELLST EHTADGTLLH AKVATVLAAE LERYAVVTA // ID E4NNB7_HALBP Unreviewed; 450 AA. AC E4NNB7; DT 08-FEB-2011, integrated into UniProtKB/TrEMBL. DT 08-FEB-2011, sequence version 1. DT 07-JUN-2017, entry version 57. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Hbor_18880 {ECO:0000313|EMBL:ADQ67455.1}; GN ORFNames=C499_18982 {ECO:0000313|EMBL:ELY23270.1}; OS Halogeometricum borinquense (strain ATCC 700274 / DSM 11551 / JCM OS 10706 / PR3). OC Archaea; Euryarchaeota; Halobacteria; Haloferacales; Haloferacaceae; OC Halogeometricum. OX NCBI_TaxID=469382 {ECO:0000313|EMBL:ADQ67455.1, ECO:0000313|Proteomes:UP000006663}; RN [1] {ECO:0000313|EMBL:ADQ67455.1, ECO:0000313|Proteomes:UP000006663} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700274 / DSM 11551 / JCM 10706 / PR3 RC {ECO:0000313|Proteomes:UP000006663}, and RC PR 3 {ECO:0000313|EMBL:ADQ67455.1}; RX PubMed=21304651; DOI=10.4056/sigs.23264; RA Malfatti S., Tindall B.J., Schneider S., Fahnrich R., Lapidus A., RA Labuttii K., Copeland A., Glavina Del Rio T., Nolan M., Chen F., RA Lucas S., Tice H., Cheng J.F., Bruce D., Goodwin L., Pitluck S., RA Anderson I., Pati A., Ivanova N., Mavromatis K., Chen A., RA Palaniappan K., D'haeseleer P., Goker M., Bristow J., Eisen J.A., RA Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P., Chain P.; RT "Complete genome sequence of Halogeometricum borinquense type strain RT (PR3)."; RL Stand. Genomic Sci. 1:150-159(2009). RN [2] {ECO:0000313|Proteomes:UP000011585} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 11551 {ECO:0000313|Proteomes:UP000011585}; RA Becker E.A., Seitzer P., Tritt A., Larsen D., Yao A., Wu D., RA Darling A., Eisen J.A., Facciotti M.T.; RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases. RN [3] {ECO:0000313|EMBL:ELY23270.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 11551 {ECO:0000313|EMBL:ELY23270.1}; RX PubMed=25393412; RA Becker E.A., Seitzer P.M., Tritt A., Larsen D., Krusor M., Yao A.I., RA Wu D., Madern D., Eisen J.A., Darling A.E., Facciotti M.T.; RT "Phylogenetically driven sequencing of extremely halophilic archaea RT reveals strategies for static and dynamic osmo-response."; RL PLoS Genet. 10:E1004784-E1004784(2014). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001690; ADQ67455.1; -; Genomic_DNA. DR EMBL; AOHT01000052; ELY23270.1; -; Genomic_DNA. DR RefSeq; WP_006057090.1; NZ_AOHT01000052.1. DR STRING; 469382.Hbor_18880; -. DR EnsemblBacteria; ADQ67455; ADQ67455; Hbor_18880. DR EnsemblBacteria; ELY23270; ELY23270; C499_18982. DR GeneID; 9993707; -. DR KEGG; hbo:Hbor_18880; -. DR PATRIC; fig|469382.19.peg.3749; -. DR eggNOG; arCOG00353; Archaea. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG093Z07D6; -. DR Proteomes; UP000006663; Chromosome. DR Proteomes; UP000011585; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000006663}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Hydrolase {ECO:0000313|EMBL:ADQ67455.1}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000006663}. FT DOMAIN 191 374 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 157 187 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 450 AA; 49691 MW; BDA4D6FCE042F0F7 CRC64; MSDGTNAIVA KRVNSGESAD LSEITDLARA AGYEVVGTLS QSRKEDAAFH FGEGKVDELT ALVAETDAAA VIVDNRLGPY QTYNIGGKLP EGVEVIDRFT LILEIFGQRA NTRKAQLQVE LAELRYELPR AEAKASLAKR DERPGFMGLG EYDESREQDI KNQISRIKNE LDSIAEKEET RREQRRESGF DLVALAGYTN AGKSTLMRRL AEDLEVGENE DLHPDLDPTA ESEDRLFTTL GTTTRRADTG TRDVLLTDTV GFVSDLPHWL VESFKSTLDS VYRADLVLLV VDASEPVEEM RDKLVTCHDT LYERNEAPIV TVLNKIDKVD ADELGRKMDA LQALAPNPVS VSGLTGENVG ALADRIEREL PDWREERLLL PMSDDTMSLV SWLYDHGNVK NEAYEGENVL VEFEARPAIV EKARAKAAEV QAGTDGEAEA EAEPDGGYQT // ID E4NP09_HALBP Unreviewed; 455 AA. AC E4NP09; DT 08-FEB-2011, integrated into UniProtKB/TrEMBL. DT 08-FEB-2011, sequence version 1. DT 07-JUN-2017, entry version 57. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Hbor_08440 {ECO:0000313|EMBL:ADQ66440.1}; GN ORFNames=C499_01750 {ECO:0000313|EMBL:ELY31160.1}; OS Halogeometricum borinquense (strain ATCC 700274 / DSM 11551 / JCM OS 10706 / PR3). OC Archaea; Euryarchaeota; Halobacteria; Haloferacales; Haloferacaceae; OC Halogeometricum. OX NCBI_TaxID=469382 {ECO:0000313|EMBL:ADQ66440.1, ECO:0000313|Proteomes:UP000006663}; RN [1] {ECO:0000313|EMBL:ADQ66440.1, ECO:0000313|Proteomes:UP000006663} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700274 / DSM 11551 / JCM 10706 / PR3 RC {ECO:0000313|Proteomes:UP000006663}, and RC PR 3 {ECO:0000313|EMBL:ADQ66440.1}; RX PubMed=21304651; DOI=10.4056/sigs.23264; RA Malfatti S., Tindall B.J., Schneider S., Fahnrich R., Lapidus A., RA Labuttii K., Copeland A., Glavina Del Rio T., Nolan M., Chen F., RA Lucas S., Tice H., Cheng J.F., Bruce D., Goodwin L., Pitluck S., RA Anderson I., Pati A., Ivanova N., Mavromatis K., Chen A., RA Palaniappan K., D'haeseleer P., Goker M., Bristow J., Eisen J.A., RA Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P., Chain P.; RT "Complete genome sequence of Halogeometricum borinquense type strain RT (PR3)."; RL Stand. Genomic Sci. 1:150-159(2009). RN [2] {ECO:0000313|Proteomes:UP000011585} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 11551 {ECO:0000313|Proteomes:UP000011585}; RA Becker E.A., Seitzer P., Tritt A., Larsen D., Yao A., Wu D., RA Darling A., Eisen J.A., Facciotti M.T.; RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases. RN [3] {ECO:0000313|EMBL:ELY31160.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 11551 {ECO:0000313|EMBL:ELY31160.1}; RX PubMed=25393412; RA Becker E.A., Seitzer P.M., Tritt A., Larsen D., Krusor M., Yao A.I., RA Wu D., Madern D., Eisen J.A., Darling A.E., Facciotti M.T.; RT "Phylogenetically driven sequencing of extremely halophilic archaea RT reveals strategies for static and dynamic osmo-response."; RL PLoS Genet. 10:E1004784-E1004784(2014). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001690; ADQ66440.1; -; Genomic_DNA. DR EMBL; AOHT01000006; ELY31160.1; -; Genomic_DNA. DR RefSeq; WP_006053665.1; NZ_AOHT01000006.1. DR STRING; 469382.Hbor_08440; -. DR EnsemblBacteria; ADQ66440; ADQ66440; Hbor_08440. DR EnsemblBacteria; ELY31160; ELY31160; C499_01750. DR GeneID; 9992664; -. DR KEGG; hbo:Hbor_08440; -. DR PATRIC; fig|469382.19.peg.338; -. DR eggNOG; arCOG00353; Archaea. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; FNNHAHV; -. DR OrthoDB; POG093Z07D6; -. DR Proteomes; UP000006663; Chromosome. DR Proteomes; UP000011585; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000006663}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Hydrolase {ECO:0000313|EMBL:ADQ66440.1}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000006663}. FT DOMAIN 209 394 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 455 AA; 49626 MW; 38FA9193A4BCE3C6 CRC64; MSRQTDQQSA QTTEHDATTT KREPSRTDDG IPAIIAKRSS ETPVETEEIR ALASAAGYRV IDEVTQVRRE DPGTHFGSGK VDSLSDRIEA TDASVLVIDG GLTPSQTTNL RDCLPDETEI FDRYRLVLSI FAAQAGTRRA QLQVELAQLK YALPRIETES DPQAMNIALE KGTRVKGVRD RIAELESKLA DLPNPAAQYR SRRREQGFDL VTVAGYTNAG KSTLLHRLAD DLSLDSTERH PDEANSVAAV EDRLFKTLQT TTRRATLEGR PVLATDTVGF VDDLPHWLVE SFSTTISEAA AADIVVLVAD ASDDVETLRE KIRVSLSVFD AQGVETQNVV TALNKTDLLT DAECESRVAA AESLAPRVVP VSVVEETNLE TLVEVVCDRL PTATETVSMS TGDEAMSVVS WAYDHARVES VEYGAETVTL TLQGRPEILE RMRGKVESVG ESDPG // ID E4PHX4_MARAH Unreviewed; 432 AA. AC E4PHX4; DT 08-FEB-2011, integrated into UniProtKB/TrEMBL. DT 08-FEB-2011, sequence version 1. DT 30-AUG-2017, entry version 50. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=HP15_2498 {ECO:0000313|EMBL:ADP98262.1}; OS Marinobacter adhaerens (strain HP15). OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales; OC Alteromonadaceae; Marinobacter. OX NCBI_TaxID=225937 {ECO:0000313|EMBL:ADP98262.1, ECO:0000313|Proteomes:UP000007077}; RN [1] {ECO:0000313|Proteomes:UP000007077} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=HP15 {ECO:0000313|Proteomes:UP000007077}; RA Gaerdes A.A.M., Kaeppel E., Shezad A., Seebah S., Teeling H., RA Yarza P., Gloeckner F.O., Ullrich M.S.; RT "Complete genome sequence of Marinobacter adhaerens type strain RT (HP15)."; RL Submitted (FEB-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001978; ADP98262.1; -; Genomic_DNA. DR RefSeq; WP_008170060.1; NC_017506.1. DR ProteinModelPortal; E4PHX4; -. DR STRING; 225937.HP15_2498; -. DR EnsemblBacteria; ADP98262; ADP98262; HP15_2498. DR KEGG; mad:HP15_2498; -. DR PATRIC; fig|225937.3.peg.2522; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000007077; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000007077}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}. FT DOMAIN 198 365 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 432 AA; 48642 MW; 9E54ECF84C5FF512 CRC64; MFERPDVGER AVLVHIDFTA HDGTEDPGEF RELVTSAGVE PVSTVTGSRK QPSPRFFVGE GKLEEIRDAV AANEADVVLF NHALSPRQER NIEHELKCRV LDRTGVILDI FAQRARTHEG KLQVELAQLE HMSTRLVRGW THLERQKGGI GLRGPGETQL ETDRRLLRER IKSIHKRLEK VRRQRNQGRR ARQRADIPTV SLVGYTNAGK STLFNRITTS SVYAADQLFA TLDPTLRRLE LPDVGPVVMA DTVGFIRHLP HKLVEAFRAT LEETTQATLL LHIIDSHDPR REENIEQVEE VLAEIGADDI PMLQVFNKID LLENFTPRVE RNEEGIPVRA WVSAVTGEGL DGLFDAIVER VAEDVVHHFV LLGPADGKLR ALLHEAGSVI SEEYRDTGDT VVEVRLQNRD WHQLLSRAGV NEKSVRLDVG HA // ID E4RJ36_HALHG Unreviewed; 410 AA. AC E4RJ36; DT 08-FEB-2011, integrated into UniProtKB/TrEMBL. DT 08-FEB-2011, sequence version 1. DT 07-JUN-2017, entry version 45. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Halsa_1838 {ECO:0000313|EMBL:ADQ15256.1}; OS Halanaerobium hydrogeniformans (Halanaerobium sp. (strain OS sapolanicus)). OC Bacteria; Firmicutes; Clostridia; Halanaerobiales; Halanaerobiaceae; OC Halanaerobium. OX NCBI_TaxID=656519 {ECO:0000313|EMBL:ADQ15256.1, ECO:0000313|Proteomes:UP000007434}; RN [1] {ECO:0000313|EMBL:ADQ15256.1, ECO:0000313|Proteomes:UP000007434} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=sapolanicus {ECO:0000313|Proteomes:UP000007434}; RG US DOE Joint Genome Institute; RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L., RA Pitluck S., Davenport K., Detter J.C., Han C., Tapia R., Land M., RA Hauser L., Jeffries C., Kyrpides N., Ivanova N., Mikhailova N., RA Begemann M.B., Mormile M.R., Wall J.D., Elias D.A., Woyke T.; RT "Complete sequence of Halanaerobium sp. sapolanicus."; RL Submitted (NOV-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002304; ADQ15256.1; -; Genomic_DNA. DR RefSeq; WP_013406327.1; NC_014654.1. DR ProteinModelPortal; E4RJ36; -. DR STRING; 656519.Halsa_1838; -. DR EnsemblBacteria; ADQ15256; ADQ15256; Halsa_1838. DR KEGG; has:Halsa_1838; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000007434; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000007434}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000007434}. FT DOMAIN 189 354 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 151 178 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 410 AA; 46680 MW; 46D5E6DFF0D98BE1 CRC64; MYKVDQLKEK ALLVGVDESD LEELKLLVDT AGAKAKLTMT YHDRKIDPAF YVGKGKVNEI KNTAESTDIN LIVFDNELSP VQQRNLEDYI GIKVIDRSQV ILDIFARHAH SKESKIQVEL AQLEYRLPRL RGRGIEMSRL AGGIGTRGPG ESKLEVDRRR IEKKIHRLKE KLKDIKSSRD VQRSQRKDPL AALVGYTNAG KSTIMNLLSG ANSHVADQLF ATLDSTMRQL ELPVGRTIIL SDTVGFISKL PHQLFASFRT TLEEIENADI ILHVIDSSDP KMEKNIKVVE EELENLNSSK SKRIKIFNKI DLLKQSEIND LKLIYPDAIF ISALKGIGKD KLLAKLNQII RQNMVEIELD LPYSKGKWIE KIHNNGQVIK EEYQKNNIYL KALISEETAS RLERYSREHS // ID E4RYY7_LEAB4 Unreviewed; 414 AA. AC E4RYY7; DT 08-FEB-2011, integrated into UniProtKB/TrEMBL. DT 08-FEB-2011, sequence version 1. DT 07-JUN-2017, entry version 49. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Lbys_2544 {ECO:0000313|EMBL:ADQ18206.1}; OS Leadbetterella byssophila (strain DSM 17132 / KACC 11308 / 4M15). OC Bacteria; Bacteroidetes; Cytophagia; Cytophagales; Cytophagaceae; OC Leadbetterella. OX NCBI_TaxID=649349 {ECO:0000313|EMBL:ADQ18206.1, ECO:0000313|Proteomes:UP000007435}; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 17132; RG US DOE Joint Genome Institute (JGI-PGF); RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., RA Tice H., Bruce D., Goodwin L., Pitluck S., Kyrpides N., Mavromatis K., RA Ivanova N., Teshima H., Brettin T., Detter J.C., Han C., Tapia R., RA Land M., Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P., RA Woyke T., Wu D., Tindall B., Pomrenke H.G., Brambilla E., Klenk H.-P., RA Eisen J.A.; RT "The complete genome of Leadbetterella byssophila DSM 17132."; RL Submitted (NOV-2010) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:ADQ18206.1, ECO:0000313|Proteomes:UP000007435} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 17132 / KACC 11308 / 4M15 RC {ECO:0000313|Proteomes:UP000007435}; RX PubMed=21475582; DOI=10.4056/sigs.1413518; RA Abt B., Teshima H., Lucas S., Lapidus A., Del Rio T.G., Nolan M., RA Tice H., Cheng J.F., Pitluck S., Liolios K., Pagani I., Ivanova N., RA Mavromatis K., Pati A., Tapia R., Han C., Goodwin L., Chen A., RA Palaniappan K., Land M., Hauser L., Chang Y.J., Jeffries C.D., RA Rohde M., Goker M., Tindall B.J., Detter J.C., Woyke T., Bristow J., RA Eisen J.A., Markowitz V., Hugenholtz P., Klenk H.P., Kyrpides N.C.; RT "Complete genome sequence of Leadbetterella byssophila type strain RT (4M15)."; RL Stand. Genomic Sci. 4:2-12(2011). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002305; ADQ18206.1; -; Genomic_DNA. DR ProteinModelPortal; E4RYY7; -. DR STRING; 649349.Lbys_2544; -. DR EnsemblBacteria; ADQ18206; ADQ18206; Lbys_2544. DR KEGG; lby:Lbys_2544; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000007435; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000007435}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Hydrolase {ECO:0000313|EMBL:ADQ18206.1}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000007435}. FT DOMAIN 205 391 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 166 193 {ECO:0000256|SAM:Coils}. FT COILED 336 363 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 414 AA; 47805 MW; 9B87B823A73AACA3 CRC64; MLNTPLISTH KEQETAILVG LITQKQNAEK TREYLEELAF LAETSGVKTL KTFLQRLNFP DQRTFVGKGK LEEIKTWVAI NPVDTIIFDD ELTPSQVRNL EREFENKKVL DRSLLILNIF SQRARTDQAK RQVELAQYKY LLPRLTRMWS HLSKQKGGIG MRGPGEKELE TDKRIVQDRI AFLKEKLDKI DKQAATRRKE RSRLVRVSLV GYTNVGKSTL MRKLTKSDVF AENKLFATID STVRKVVLGH IPFLLTDTVG FIRKLPTTLV ESFKSTLDEI READILIHVV DISHPSFEEQ IEIVNSTLGE IGAQDKPTLL VFNKLDQYQP ESEEGLDKHL ATEEDLKKNL ERLETSYLKK NAKYVAFISA EKNENMDKLR EVLLDLVREK HFGIYPNWDA TKNDLYNWQE DASI // ID E4T879_PALPW Unreviewed; 404 AA. AC E4T879; DT 08-FEB-2011, integrated into UniProtKB/TrEMBL. DT 08-FEB-2011, sequence version 1. DT 30-AUG-2017, entry version 52. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Palpr_2794 {ECO:0000313|EMBL:ADQ80923.1}; OS Paludibacter propionicigenes (strain DSM 17365 / JCM 13257 / WB4). OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; OC Paludibacteraceae; Paludibacter. OX NCBI_TaxID=694427 {ECO:0000313|EMBL:ADQ80923.1, ECO:0000313|Proteomes:UP000008718}; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=WB4; RG US DOE Joint Genome Institute (JGI-PGF); RA Lucas S., Copeland A., Lapidus A., Bruce D., Goodwin L., Pitluck S., RA Kyrpides N., Mavromatis K., Ivanova N., Munk A.C., Brettin T., RA Detter J.C., Han C., Tapia R., Land M., Hauser L., Markowitz V., RA Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Gronow S., Wellnitz S., RA Brambilla E., Klenk H.-P., Eisen J.A.; RT "The complete genome of Paludibacter propionicigenes DSM 17365."; RL Submitted (NOV-2010) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:ADQ80923.1, ECO:0000313|Proteomes:UP000008718} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 17365 / JCM 13257 / WB4 RC {ECO:0000313|Proteomes:UP000008718}; RX PubMed=21475585; DOI=10.4056/sigs.1503846; RA Gronow S., Munk C., Lapidus A., Nolan M., Lucas S., Hammon N., RA Deshpande S., Cheng J.F., Tapia R., Han C., Goodwin L., Pitluck S., RA Liolios K., Ivanova N., Mavromatis K., Mikhailova N., Pati A., RA Chen A., Palaniappan K., Land M., Hauser L., Chang Y.J., RA Jeffries C.D., Brambilla E., Rohde M., Goker M., Detter J.C., RA Woyke T., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P., RA Kyrpides N.C., Klenk H.P.; RT "Complete genome sequence of Paludibacter propionicigenes type strain RT (WB4)."; RL Stand. Genomic Sci. 4:36-44(2011). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002345; ADQ80923.1; -; Genomic_DNA. DR RefSeq; WP_013446292.1; NC_014734.1. DR ProteinModelPortal; E4T879; -. DR STRING; 694427.Palpr_2794; -. DR EnsemblBacteria; ADQ80923; ADQ80923; Palpr_2794. DR KEGG; ppn:Palpr_2794; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000008718; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000008718}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Hydrolase {ECO:0000313|EMBL:ADQ80923.1}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000008718}. FT DOMAIN 198 382 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 404 AA; 46556 MW; 8862EF13A8BD8EE8 CRC64; MKTEIYEEKA VLVGVITQLQ SEEKAKEYLN ELAFLAETAG ASPEKLYFQR LDYPNPKTYV GPGKLIEIKA FVDENEIGVV IFDDELSPKQ LRNIEAELKV LILDRTSLIL DIFAKRAQTA SAKTQVELAQ LQYTLPRLTR LWTHLERQQG GIGMRGPGET QIETDRRIIL TKISLLKQNL KDIDKQMSTQ RKNRGKMVRV ALVGYTNVGK STLMNLISKS EIFAENKLFA TLDTTVRKVI IDNLPFLLSD TVGFIRKLPH HLVQSFKSTL DEVREADLLL HVVDVSHPNF EEQLEVVNQT LKEIDPLEKP MILIFNKIDA FTYTPKDEDD LAPIKRENLS LEELKKTWMG KMHDNCIFIS AREKQNIDSL KALMYEKIKA IHVERYPYND FLFQDYTEIE PENE // ID E4TGD3_CALNY Unreviewed; 552 AA. AC E4TGD3; DT 08-FEB-2011, integrated into UniProtKB/TrEMBL. DT 08-FEB-2011, sequence version 1. DT 07-JUN-2017, entry version 50. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Calni_0703 {ECO:0000313|EMBL:ADR18614.1}; OS Calditerrivibrio nitroreducens (strain DSM 19672 / NBRC 101217 / OS Yu37-1). OC Bacteria; Deferribacteres; Deferribacterales; Deferribacteraceae. OX NCBI_TaxID=768670 {ECO:0000313|EMBL:ADR18614.1, ECO:0000313|Proteomes:UP000007039}; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 19672; RG US DOE Joint Genome Institute (JGI-PGF); RA Lucas S., Copeland A., Lapidus A., Bruce D., Goodwin L., Pitluck S., RA Kyrpides N., Mavromatis K., Ivanova N., Mikhailova N., Zeytun A., RA Brettin T., Detter J.C., Tapia R., Han C., Land M., Hauser L., RA Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Spring S., RA Schroeder M., Brambilla E., Klenk H.-P., Eisen J.A.; RT "The complete genome of chromosome of Calditerrivibrio nitroreducens RT DSM 19672."; RL Submitted (NOV-2010) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:ADR18614.1, ECO:0000313|Proteomes:UP000007039} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 19672 / NBRC 101217 / Yu37-1 RC {ECO:0000313|Proteomes:UP000007039}; RX PubMed=21475587; DOI=10.4056/sigs.1523807; RA Pitluck S., Sikorski J., Zeytun A., Lapidus A., Nolan M., Lucas S., RA Hammon N., Deshpande S., Cheng J.F., Tapia R., Han C., Goodwin L., RA Liolios K., Pagani I., Ivanova N., Mavromatis K., Pati A., Chen A., RA Palaniappan K., Hauser L., Chang Y.J., Jeffries C.D., Detter J.C., RA Brambilla E., Djao O.D., Rohde M., Spring S., Goker M., Woyke T., RA Bristow J., Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., RA Klenk H.P., Land M.; RT "Complete genome sequence of Calditerrivibrio nitroreducens type RT strain (Yu37-1)."; RL Stand. Genomic Sci. 4:54-62(2011). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002347; ADR18614.1; -; Genomic_DNA. DR RefSeq; WP_013450827.1; NC_014758.1. DR ProteinModelPortal; E4TGD3; -. DR STRING; 768670.Calni_0703; -. DR EnsemblBacteria; ADR18614; ADR18614; Calni_0703. DR KEGG; cni:Calni_0703; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; EREVIIT; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000007039; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000007039}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Hydrolase {ECO:0000313|EMBL:ADR18614.1}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000007039}. FT DOMAIN 373 538 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 552 AA; 63476 MW; 4A9DA0073AD2D53A CRC64; MLYGYTDNVK VGYLRTLEKF IKKKNISDTL ISNELLKRIS SISFEMGRQI GLLIDRNNII QIVLVGTNKE VLIPKLERFA ITPGKLRGLR LLHTHLYGED LDEDDITDLK LLRLDAVSVI KLNDRGEPYK LQMAYLYPSH EKEYDIIEYK DPYNIKDNFI EFISAIESEL SRKIKERYEV KKGFSGVLIG VYKDKKEAEE SLFELKELCR TAEIIPEEAF IQIKGAIHPK FVVGPGKLKE IVIYAMQNNI DYLIFDNILS PAQSRSIAEQ TEMKILDRTQ LILDIFARRA KSNEGKIRVE LAQLKHILPR LTGRDDSLSR LTGGIGGRGP GETKLEIDKR RIRDRIAFLT NKLKDIESVR QTQRVKRTRK NLPIVSIVGY TNAGKSTLLN NLTKSDVYAD NLMFATLDTT SKRLRFPEDR ECILTDTVGF IRNLPESLKG AFKSTLEELE ESDLFIHLVD ISNTQYKKQI DAVNQIFEEL KLNDKPKIMV FNKIDLVDKQ VITEAQKDYP EAIFISALNK KTFEELIIKI NHILFVGGKK LGIPVRDYFE KV // ID E4TQD6_MARTH Unreviewed; 392 AA. AC E4TQD6; DT 08-FEB-2011, integrated into UniProtKB/TrEMBL. DT 08-FEB-2011, sequence version 1. DT 07-JUN-2017, entry version 51. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Ftrac_2681 {ECO:0000313|EMBL:ADR22659.1}; OS Marivirga tractuosa (strain ATCC 23168 / DSM 4126 / NBRC 15989 / NCIMB OS 1408 / VKM B-1430 / H-43) (Microscilla tractuosa) (Flexibacter OS tractuosus). OC Bacteria; Bacteroidetes; Cytophagia; Cytophagales; Flammeovirgaceae; OC Marivirga. OX NCBI_TaxID=643867 {ECO:0000313|EMBL:ADR22659.1, ECO:0000313|Proteomes:UP000008720}; RN [1] {ECO:0000313|Proteomes:UP000008720} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 23168 / DSM 4126 / NBRC 15989 / NCIMB 1408 / VKM B-1430 / RC H-43 {ECO:0000313|Proteomes:UP000008720}; RG US DOE Joint Genome Institute (JGI-PGF); RA Lucas S., Copeland A., Lapidus A., Bruce D., Goodwin L., Pitluck S., RA Kyrpides N., Mavromatis K., Pagani I., Ivanova N., Ovchinnikova G., RA Chertkov O., Held B., Detter J.C., Han C., Tapia R., Land M., RA Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T., Wu D., RA Spring S., Schroeder M., Schneider S., Klenk H.-P., Eisen J.A.; RT "The complete genome of chromosome of Marivirga tractuosa DSM 4126."; RL Submitted (NOV-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002349; ADR22659.1; -; Genomic_DNA. DR RefSeq; WP_013454802.1; NC_014759.1. DR ProteinModelPortal; E4TQD6; -. DR STRING; 643867.Ftrac_2681; -. DR EnsemblBacteria; ADR22659; ADR22659; Ftrac_2681. DR KEGG; mtt:Ftrac_2681; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000008720; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000008720}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Hydrolase {ECO:0000313|EMBL:ADR22659.1}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000008720}. FT DOMAIN 203 379 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 171 198 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 392 AA; 45226 MW; FDC549D36279CDDA CRC64; MQYNSAEEKN EKKAVLVAII TQNQNEEKVN EYLDELAFLT STLGAKTIKR FTQRLEKPDV RSFIGKGKLE EINAYAQAEK ADWVVFDDDL TPSQLRNLEK ELKVKIYDRS LLILDIFLNR AQTAQAKTQV ELARNQYLLP RLTRMWTHLE RQRGGTATRG GAGEKEIETD KRIIRNTITK LKERLAKIEK QSRTQRKSRG KIVRVAIVGY TNVGKSTLMT RLSKSDILAE NKLFATVDST VRKVNFEDIP FLLSDTVGFI RKLPTHLIES FKSTLDEIRE ADILIHVVDV SHPTLDDHIS VVNQTLTDID AGDKPTLLVF NKVDLLEEEE EISVEEKIKN LKNTYWNKEQ NDVVFISATN KENIEELKNK LRKLVEAKHF TIFPNYLKNT YY // ID E4U882_OCEP5 Unreviewed; 554 AA. AC E4U882; DT 08-FEB-2011, integrated into UniProtKB/TrEMBL. DT 08-FEB-2011, sequence version 1. DT 07-JUN-2017, entry version 49. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Ocepr_0840 {ECO:0000313|EMBL:ADR36297.1}; OS Oceanithermus profundus (strain DSM 14977 / NBRC 100410 / VKM B-2274 / OS 506). OC Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; OC Oceanithermus. OX NCBI_TaxID=670487 {ECO:0000313|EMBL:ADR36297.1, ECO:0000313|Proteomes:UP000008722}; RN [1] {ECO:0000313|Proteomes:UP000008722} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 14977 / NBRC 100410 / VKM B-2274 / 506 RC {ECO:0000313|Proteomes:UP000008722}; RG US DOE Joint Genome Institute (JGI-PGF); RA Lucas S., Copeland A., Lapidus A., Bruce D., Goodwin L., Pitluck S., RA Kyrpides N., Mavromatis K., Pagani I., Ivanova N., Zhang X., RA Brettin T., Detter J.C., Tapia R., Han C., Land M., Hauser L., RA Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Tindall B., RA Faehnrich R., Brambilla E., Klenk H.-P., Eisen J.A.; RT "The complete sequence of chromosome of Oceanithermus profundus DSM RT 14977."; RL Submitted (NOV-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002361; ADR36297.1; -; Genomic_DNA. DR RefSeq; WP_013457467.1; NC_014761.1. DR STRING; 670487.Ocepr_0840; -. DR EnsemblBacteria; ADR36297; ADR36297; Ocepr_0840. DR KEGG; opr:Ocepr_0840; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; EREVIIT; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000008722; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000008722}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Hydrolase {ECO:0000313|EMBL:ADR36297.1}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000008722}. FT DOMAIN 376 539 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 342 369 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 554 AA; 61344 MW; 5AB676F099645612 CRC64; MNKLYGNVQG LKPSLKKKLG NLYRRRVPAN RLYTAELART LAQLSAEVGR PVSLLLARNG QMRAVAVGDA AALPVPEHAY LESRLSGYRI VHTHLGGGGL SAPDLSTLFL HRYDSIVALD VEEGRPTRAH LAHLVPPEAE EEDWRIYPAR PWDAYLQWDY GAALAALEEE LARRADLREL EDGSGERVIL VGIDEGQGPE AELRLDELAE LARTAGGVVV HRELVYRPTL DPRYAVGRGK LDELTSVAYH ENAGTLIFGV DLTPAQAGAI EQATQLKVLD RTQLILDIFA RHARTPQAEA QVELAQLRYL LPRLVGKGKQ LSRLGGGIGT RGPGETKLEV DRRRIGERIH RLTREIERIA KQRREARKSR KRNRVPVVAI VGYTNAGKTT LLRALTRKGD AGENKLFATL RPLTRRGYLP GYGEVLFTDT VGFIRDMPPA LVTAFRATLE ELFEADLVLH VVDATADGAL EHHRVVEDRL VEMGLEAPRL VVVNKIDRAD PFDRMRLEEQ LDGVAVSALE GRGLEDLASR IVRVLIGSGL PAQPWAQYDV RPMG // ID E5AQJ5_PARRH Unreviewed; 415 AA. AC E5AQJ5; DT 08-FEB-2011, integrated into UniProtKB/TrEMBL. DT 08-FEB-2011, sequence version 1. DT 07-JUN-2017, entry version 48. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=RBRH_03726 {ECO:0000313|EMBL:CBW74877.1}; OS Paraburkholderia rhizoxinica (strain DSM 19002 / CIP 109453 / HKI 454) OS (Burkholderia rhizoxinica). OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Paraburkholderia. OX NCBI_TaxID=882378 {ECO:0000313|EMBL:CBW74877.1, ECO:0000313|Proteomes:UP000007437}; RN [1] {ECO:0000313|EMBL:CBW74877.1, ECO:0000313|Proteomes:UP000007437} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 19002 / CIP 109453 / HKI 454 RC {ECO:0000313|Proteomes:UP000007437}; RX PubMed=21131495; DOI=10.1128/JB.01318-10; RA Lackner G., Moebius N., Partida-Martinez L., Hertweck C.; RT "Complete genome sequence of Burkholderia rhizoxinica, an endosymbiont RT of Rhizopus microsporus."; RL J. Bacteriol. 193:783-784(2011). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; FR687359; CBW74877.1; -; Genomic_DNA. DR RefSeq; WP_013435106.1; NC_014722.1. DR ProteinModelPortal; E5AQJ5; -. DR STRING; 882378.RBRH_03726; -. DR EnsemblBacteria; CBW74877; CBW74877; RBRH_03726. DR KEGG; brh:RBRH_03726; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000007437; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000007437}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000007437}. FT DOMAIN 191 361 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 415 AA; 45541 MW; D040E7633993C826 CRC64; MINAALVSID FGKIDFQASL EELSLLATSA GAHPVLTLTG RRSSPDAAHF IGSGKVEELR LGAQANDVDI VIFNHALSPA QQRNLEHELE RRVVDRTSLI LDIFAQRARS HEGKLQVELA QLQYLSTRLV RAWTHLERQK GGIGLRGPGE TQLETDRRLI GERIKMLRGK LRKLQRQHGT QRRQRERNRT LSVSLVGYTN AGKSTLFNAL TKAQAYAADQ LFATLDTTSR RVYLGEAGNV VVSDTVGFIR DLPHQLVAAF RATLEETVHA DLLLHIVDAA SAVRADQIEQ VNDVLREIGA ASIPQILVFN KIDQVPELAS RADRVERNEY GNITRVFLSA RTGQGLDALR DAVAEVALGA QAFKRDPDGM GADDHGPRCD AEGSHSDEAG ATAGANASDD ERVRQASRSV HQQRI // ID E5BG81_9FUSO Unreviewed; 602 AA. AC E5BG81; DT 08-FEB-2011, integrated into UniProtKB/TrEMBL. DT 08-FEB-2011, sequence version 1. DT 12-APR-2017, entry version 38. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:EFS21504.1}; GN ORFNames=FSBG_01001 {ECO:0000313|EMBL:EFS21504.1}; OS Fusobacterium gonidiaformans 3-1-5R. OC Bacteria; Fusobacteria; Fusobacteriales; Fusobacteriaceae; OC Fusobacterium. OX NCBI_TaxID=469605 {ECO:0000313|EMBL:EFS21504.1, ECO:0000313|Proteomes:UP000002975}; RN [1] {ECO:0000313|EMBL:EFS21504.1, ECO:0000313|Proteomes:UP000002975} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=3_1_5R {ECO:0000313|EMBL:EFS21504.1, RC ECO:0000313|Proteomes:UP000002975}; RG The Broad Institute Genome Sequencing Platform; RA Ward D., Young S.K., Kodira C.D., Zeng Q., Koehrsen M., Alvarado L., RA Berlin A., Borenstein D., Chen Z., Engels R., Freedman E., RA Gellesch M., Goldberg J., Griggs A., Gujja S., Heiman D., Hepburn T., RA Howarth C., Jen D., Larson L., Lewis B., Mehta T., Park D., RA Pearson M., Roberts A., Saif S., Shea T., Shenoy N., Sisk P., RA Stolte C., Sykes S., Walk T., White J., Yandava C., Allen-Vercoe E., RA Strauss J., Ambrose C., Lander E., Nusbaum C., Galagan J., Birren B.; RT "The Genome Sequence of Fusobacterium sp. 3_1_5R."; RL Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GG657972; EFS21504.1; -; Genomic_DNA. DR EnsemblBacteria; EFS21504; EFS21504; FSBG_01001. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000002975; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000002975}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000002975}. FT DOMAIN 372 548 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 331 365 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 602 AA; 68526 MW; D662643E0B73CD66 CRC64; MKQSWRKIMI YGNTEGMKEF TLQQLEQLYE IKLNKGQLIS EEIAIFLANI STKINKEINL CIDRNGNITE ISIGDSSTVS LPFIPVYEKK LSGKRIVHTH PNGNPKLSSV DISALLKLKL DAILAIGCIE EKVTGIGLAL CNLEEDVIHY EEHLYSSFEE LENFPFLEKL QSIETALRRK NIVEDDKEYA VLVGIDSKTS LQELEELAYA CNIEVVGHFF QNRSKADKVL FLGPGKAREL SLFQQIKRAN LIIADEELSG LQVKNLEEVT GCKVIDRTTL ILEIFARRAR SREAKIQVEL AQLKYRSNRL IGYGVTMSRL GGGVGSKGPG EKKLEIDRRR IRENISFLKK ELENIKKTRS VQREKRENSN IPKIALVGYT NVGKSTLRNL LAAEYNPNSN TKEDVFAENM LFATLDTTTR TILLDDKRLI SLTDTVGFIR KLPHDLIEAF KSTLEEVIFS DLILHVVDSS SEEALSQMEA VYQVLEELQC QNKKNILVLN KCDLARPEQI LAIREKYSHI TAVEISAKEH KNIEFLLEEI KKELPQNTKT CTYLIPYSDS SMVAYLHKTS TIQEEKYEAE GTFIKAIVNQ ETENRCKQFE IE // ID E5S6W9_TRISP Unreviewed; 512 AA. AC E5S6W9; DT 08-MAR-2011, integrated into UniProtKB/TrEMBL. DT 08-MAR-2011, sequence version 1. DT 05-JUL-2017, entry version 33. DE SubName: Full=Putative GTP-binding protein 6 {ECO:0000313|EMBL:EFV59470.1}; GN ORFNames=Tsp_07064 {ECO:0000313|EMBL:EFV59470.1}; OS Trichinella spiralis (Trichina worm). OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia; OC Trichocephalida; Trichinellidae; Trichinella. OX NCBI_TaxID=6334 {ECO:0000313|EMBL:EFV59470.1, ECO:0000313|Proteomes:UP000006823}; RN [1] {ECO:0000313|EMBL:EFV59470.1, ECO:0000313|Proteomes:UP000006823} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ISS 195 {ECO:0000313|EMBL:EFV59470.1, RC ECO:0000313|Proteomes:UP000006823}; RX PubMed=21336279; DOI=10.1038/ng.769; RA Mitreva M., Jasmer D.P., Zarlenga D.S., Wang Z., Abubucker S., RA Martin J., Taylor C.M., Yin Y., Fulton L., Minx P., Yang S.P., RA Warren W.C., Fulton R.S., Bhonagiri V., Zhang X., Hallsworth-Pepin K., RA Clifton S.W., McCarter J.P., Appleton J., Mardis E.R., Wilson R.K.; RT "The draft genome of the parasitic nematode Trichinella spiralis."; RL Nat. Genet. 43:228-235(2011). CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EFV59470.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABIR02000611; EFV59470.1; -; Genomic_DNA. DR RefSeq; XP_003380920.1; XM_003380872.1. DR ProteinModelPortal; E5S6W9; -. DR EnsemblMetazoa; EFV59470; EFV59470; EFV59470. DR GeneID; 10903358; -. DR KEGG; tsp:Tsp_07064; -. DR CTD; 10903358; -. DR eggNOG; KOG0410; Eukaryota. DR eggNOG; COG2262; LUCA. DR InParanoid; E5S6W9; -. DR OMA; MDTVGFM; -. DR OrthoDB; EOG091G0852; -. DR Proteomes; UP000006823; Unassembled WGS sequence. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR SUPFAM; SSF52540; SSF52540; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000006823}; KW Reference proteome {ECO:0000313|Proteomes:UP000006823}. FT DOMAIN 119 206 GTP-bdg_N. {ECO:0000259|Pfam:PF13167}. SQ SEQUENCE 512 AA; 58908 MW; AB0C872A91BC76D4 CRC64; MYMYMYSTRL LNQQFHLLLC FHLQINGFVG DHPTLPMAVR IFIRQIQHTP ISYNRLNSSK SIHKDDDLPA ILPLEDYRDL QRKLDVPLQG VKKALFVLQP KVPKPDLLRL ATSNESLEQE ALQLVKSVPG WNVAGVYERY VKVNRSRPSI LGKGTIEELI SYFTNLHHRD GVFLNVARLT PIQHFYLSCA FKMPVYDRYT VALQIFKHYA ISKEAKLQAA LAELAYMKER LQPYINGEID LKEAVKLGAL QMKMPDKKRR KLLDEQEIAI RGKLDKLKTQ RHYLRQNTRR KQCPMIAVIG YTNAEDRRIS SEDRFFATLD VTVHHGQLPC RLDVLYADTV GFFSDLPMGL MPCFDATMEE IASSVDALLH VVDRSHESWL SQRLIVVHNL NKLNVEHVIE VWNKCDKLNE IPNSTASQAL LISCLNGEGI DELKMQIERE ILNLCNFHHV TLEVPITGDY INQLYNVAAV KQAVPSEDGQ KMLISAVLRP YQLESFLKNY DCVKVLPVKD KE // ID E5UH69_NEIMU Unreviewed; 386 AA. AC E5UH69; DT 08-MAR-2011, integrated into UniProtKB/TrEMBL. DT 08-MAR-2011, sequence version 1. DT 07-JUN-2017, entry version 39. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=HMPREF0604_00064 {ECO:0000313|EMBL:EFV81485.1}; OS Neisseria mucosa C102. OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=435832 {ECO:0000313|EMBL:EFV81485.1, ECO:0000313|Proteomes:UP000003612}; RN [1] {ECO:0000313|EMBL:EFV81485.1, ECO:0000313|Proteomes:UP000003612} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C102 {ECO:0000313|EMBL:EFV81485.1, RC ECO:0000313|Proteomes:UP000003612}; RG The Broad Institute Genome Sequencing Platform; RA Earl A., Ward D., Feldgarden M., Gevers D., Sibley C.D., Field T.R., RA Grinwis M., Eshaghurshan C.S., Surette M., Young S.K., Zeng Q., RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L., RA Arachchi H.M., Berlin A., Brown A., Chapman S.B., Chen Z., Dunbar C., RA Freedman E., Gearin G., Gellesch M., Goldberg J., Griggs A., Gujja S., RA Heilman E., Heiman D., Howarth C., Larson L., Lui A., RA MacDonald P.J.P., Mehta T., Montmayeur A., Murphy C., Neiman D., RA Pearson M., Priest M., Roberts A., Saif S., Shea T., Shenoy N., RA Sisk P., Stolte C., Sykes S., White J., Yandava C., Nusbaum C., RA Birren B.; RT "The Genome Sequence of Neisseria mucosa strain C102."; RL Submitted (DEC-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EFV81485.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACRG01000001; EFV81485.1; -; Genomic_DNA. DR RefSeq; WP_003745635.1; NZ_GL635793.1. DR STRING; 435832.HMPREF0604_00064; -. DR EnsemblBacteria; EFV81485; EFV81485; HMPREF0604_00064. DR GeneID; 25046904; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000003612; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000003612}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000003612}. FT DOMAIN 216 385 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 386 AA; 42160 MW; 46296CF129044084 CRC64; MSKRNLFSVD KSLEKSERVL LVGVMLTADY SGANETRERG FQTALAEAAE LVGAAGGDLV SIETSRRDKP HPALFVGTGK AEELAAVVKQ HDVGLVVFNH ELTPTQERNL EKELQCRVLD RVGLILAIFA KRAQSQEGKL QVELAQLNHL SGRLVRGYGH LQSQKGGIGL KGPGETQLET DRRLIGQKIT ALKKQLADVR KQRATRRKSR MSGRLKTFAI VGYTNAGKSS LFNRLTKADV LAKDQLFATL DTTARRLFLS HEASVILTDT VGFVRDLPHK LVSAFSATLE ETAMADVLLH VVDASNPDFE RQMDDVNEVL EEIGAHEIPQ LVVYNKIDLL PSGMREAGIL RDNSGQAVGV NISVAESLGL DGLREAMIEL AVQPNA // ID E5WCI5_9BACI Unreviewed; 418 AA. AC E5WCI5; DT 08-MAR-2011, integrated into UniProtKB/TrEMBL. DT 08-MAR-2011, sequence version 1. DT 07-JUN-2017, entry version 38. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=HMPREF1013_00152 {ECO:0000313|EMBL:EFV79704.1}; OS Bacillus sp. 2_A_57_CT2. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus. OX NCBI_TaxID=665959 {ECO:0000313|EMBL:EFV79704.1, ECO:0000313|Proteomes:UP000003283}; RN [1] {ECO:0000313|EMBL:EFV79704.1, ECO:0000313|Proteomes:UP000003283} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=2_A_57_CT2 {ECO:0000313|EMBL:EFV79704.1, RC ECO:0000313|Proteomes:UP000003283}; RG The Broad Institute Genome Sequencing Platform; RA Earl A., Ward D., Feldgarden M., Gevers D., Daigneault M., Strauss J., RA Allen-Vercoe E., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., RA Haas B., Abouelleil A., Alvarado L., Arachchi H.M., Berlin A., RA Brown A., Chapman S.B., Chen Z., Dunbar C., Freedman E., Gearin G., RA Gellesch M., Goldberg J., Griggs A., Gujja S., Heilman E., Heiman D., RA Howarth C., Larson L., Lui A., MacDonald P.J.P., Mehta T., RA Montmayeur A., Murphy C., Neiman D., Pearson M., Priest M., RA Roberts A., Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., RA White J., Yandava C., Nusbaum C., Birren B.; RT "The Genome Sequence of Bacillus sp. strain 2_A_57_CT2."; RL Submitted (DEC-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EFV79704.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACWD01000002; EFV79704.1; -; Genomic_DNA. DR RefSeq; WP_009330571.1; NZ_GL635750.1. DR ProteinModelPortal; E5WCI5; -. DR STRING; 665959.HMPREF1013_00152; -. DR EnsemblBacteria; EFV79704; EFV79704; HMPREF1013_00152. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000003283; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000003283}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000003283}. FT DOMAIN 199 361 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 418 AA; 48131 MW; 2ED93AE99BEE69EB CRC64; MERKPDYEKV ILVGCHTDED DQRFEYSMEE LESLTETANG KVLASITQKR ERVHPSTYIG KGKVEELAAL QEEMEADIII FNDELSPSQV RNLSADLDAR IIDRTQLILD IFAQRALSKE GKLQVELAQL QYLLPRLSGQ GVQLSRLGAG IGTRGPGETK LESDRRHIRR RIDDIKTQLS VIVQHRDRYR ERRKKNKAFQ IALVGYTNAG KSTIFNRLSE AESYEENQLF ATLDPMTRKL ILPSGFITLV TDTVGFIQDL PTTLIAAFRS TLEEVNEADL LLHVVDMSNP DYYQHEQTVN KLIEDLENDK IPQLTVYNKR DLKHPDFVPT ARTETIQISA FEEDDRNELK RKIEQMILGM MKHYHVEVPS TEGKLLSQLK NETILRELTF NEDKELYVCK GYYLEDHQIS GPLMKYTV // ID E5Y6K1_BILWA Unreviewed; 542 AA. AC E5Y6K1; DT 08-MAR-2011, integrated into UniProtKB/TrEMBL. DT 08-MAR-2011, sequence version 1. DT 07-JUN-2017, entry version 39. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=HMPREF0179_01814 {ECO:0000313|EMBL:EFV44332.1}; OS Bilophila wadsworthia 3_1_6. OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfovibrionales; OC Desulfovibrionaceae; Bilophila. OX NCBI_TaxID=563192 {ECO:0000313|EMBL:EFV44332.1, ECO:0000313|Proteomes:UP000006034}; RN [1] {ECO:0000313|EMBL:EFV44332.1, ECO:0000313|Proteomes:UP000006034} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=3_1_6 {ECO:0000313|EMBL:EFV44332.1, RC ECO:0000313|Proteomes:UP000006034}; RG The Broad Institute Genome Sequencing Platform; RA Ward D., Earl A., Feldgarden M., Young S.K., Gargeya S., Zeng Q., RA Alvarado L., Berlin A., Bochicchio J., Chapman S.B., Chen Z., RA Freedman E., Gellesch M., Goldberg J., Griggs A., Gujja S., RA Heilman E., Heiman D., Howarth C., Mehta T., Neiman D., Pearson M., RA Roberts A., Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., RA White J., Yandava C., Allen-Vercoe E., Sibley C., Ambrose C.E., RA Strauss J., Daigneault M., Haas B., Nusbaum C., Birren B.; RL Submitted (OCT-2010) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:EFV44332.1, ECO:0000313|Proteomes:UP000006034} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=3_1_6 {ECO:0000313|EMBL:EFV44332.1, RC ECO:0000313|Proteomes:UP000006034}; RG The Broad Institute Genomics Platform; RA Earl A., Ward D., Feldgarden M., Gevers D., Sibley C., Strauss J., RA Allen-Vercoe E., Walker B., Young S., Zeng Q., Gargeya S., RA Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L., RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., RA Goldberg J., Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., RA Ireland A., Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., RA Priest M., Roberts A., Saif S., Shea T., Sisk P., Sykes S., RA Wortman J., Nusbaum C., Birren B.; RT "The Genome Sequence of Bilophila wadsworthia 3_1_6."; RL Submitted (APR-2013) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EFV44332.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADCP02000003; EFV44332.1; -; Genomic_DNA. DR STRING; 563192.HMPREF0179_01814; -. DR EnsemblBacteria; EFV44332; EFV44332; HMPREF0179_01814. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000006034; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000006034}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000006034}. FT DOMAIN 363 513 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 322 356 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 542 AA; 60408 MW; 591274624288BC5C CRC64; MKALTRLGQR RYPVQGGYTT EQARELALLS RALGRQVGLV IDRQGKVDMV IVGDPASILI PELPRGRGAA GRLRGIRLMH THLSPDGLSQ EDLMDMLFLR LDSVSVLTVN DYGDPVSFQS GHLLPPNADS KPYRIHPMTA WDRVDIDFNA EAVSLEEELG RVLSEASEAG DSPRAILVSV SPLPRAIQET HIEELRELAR SAGIVVTGTL IQRVADIHPR HILGKGKLTE LEILALQGQA SLIIFDGELT PAQLNSLSEV TERKVLDRTQ LILDIFAQRA TTRAGKLQVE MAQLKYTQPR LVGKNRAMDR LMGGIGGRGP GETKLETDRR RIRERIAKIK KELDGLRQQR AFTRARRARQ GLPVAALVGY TNAGKSTLLN ALTRSEVLAE DKLFATLDPT TRRLRFPEEH ELVLADTVGF IRNLPKELTE AFQATLEELE AADLLLHVAD ASHPELDRQI AAVDGILADM ELNEVPRVLI LNKWDRLEDE MRDILRDRWP DALPISAETR DSLNVLSRCI ENTIHWETTA NIEITGPMPK VY // ID E6J5I8_9ACTN Unreviewed; 483 AA. AC E6J5I8; DT 08-MAR-2011, integrated into UniProtKB/TrEMBL. DT 08-MAR-2011, sequence version 1. DT 07-JUN-2017, entry version 38. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=ES5_02379 {ECO:0000313|EMBL:EFV93140.1}; OS Dietzia cinnamea P4. OC Bacteria; Actinobacteria; Corynebacteriales; Dietziaceae; Dietzia. OX NCBI_TaxID=910954 {ECO:0000313|EMBL:EFV93140.1, ECO:0000313|Proteomes:UP000004165}; RN [1] {ECO:0000313|EMBL:EFV93140.1, ECO:0000313|Proteomes:UP000004165} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=P4 {ECO:0000313|EMBL:EFV93140.1, RC ECO:0000313|Proteomes:UP000004165}; RX PubMed=21901521; DOI=10.1007/s10482-011-9633-7; RA Procopio L., Alvarez V.M., Jurelevicius D.A., Hansen L., RA Sorensen S.J., Cardoso J.S., Padula M., Leitao A.C., Seldin L., RA van Elsas J.D.; RT "Insight from the draft genome of Dietzia cinnamea P4 reveals RT mechanisms of survival in complex tropical soil habitats and RT biotechnology potential."; RL Antonie Van Leeuwenhoek 101:289-302(2012). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EFV93140.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AEKG01000063; EFV93140.1; -; Genomic_DNA. DR RefSeq; WP_007626985.1; NZ_AEKG01000063.1. DR ProteinModelPortal; E6J5I8; -. DR EnsemblBacteria; EFV93140; EFV93140; ES5_02379. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000004165; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000004165}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000004165}. FT DOMAIN 252 421 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 211 238 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 483 AA; 52411 MW; D8B8AECD56596148 CRC64; MTIDHTAVER PTRDLDPSIG ELQLEERSSL RRVAGLSTEL QDVNDAEYRQ LRLERVVLVG VWTEGSAAQA DAAMAELAQL AETAGSEVCD ALIQRRDKPD AATFIGSGKV SVLKDVIAAT GADTVICDGE LTPGQLLALE KAVNVKVIDR TALILDIFAQ HATSREGKAQ VSLAQMEYML PRLRGWGESL SRQAGGRAGS NGGVGLRGPG ETKIETDRRR IRERMAKLRR EIKGMKQSRD TKRYRRRATP VPSIAIAGYT NAGKSSLLNR ITGAGVLVQN ALFATLDPTT RRADLPDGRS VVFTDTVGFV RHLPTQLVEA FRSTLEEVVD SELLLHVVDG SDAFPLRQIE AVRKVINEVV EEQNAERPRE LVVINKIDAA DPVVLTELHH ALPDAVFVSA ATGQGVDELL ERIMQIVASG DMEMTLEVPY ARGDVVARVH TEGAVVEEEH TDRGTRLVVR LPASVAGELG EFVSDSSTRD GAA // ID E6K041_PARDN Unreviewed; 615 AA. AC E6K041; DT 08-MAR-2011, integrated into UniProtKB/TrEMBL. DT 08-MAR-2011, sequence version 1. DT 07-JUN-2017, entry version 42. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:EFT84153.1}; GN ORFNames=HMPREF0620_1158 {ECO:0000313|EMBL:EFT84153.1}; OS Parascardovia denticolens DSM 10105 = JCM 12538. OC Bacteria; Actinobacteria; Bifidobacteriales; Bifidobacteriaceae; OC Parascardovia. OX NCBI_TaxID=864564 {ECO:0000313|EMBL:EFT84153.1, ECO:0000313|Proteomes:UP000004946}; RN [1] {ECO:0000313|EMBL:EFT84153.1, ECO:0000313|Proteomes:UP000004946} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 10105 {ECO:0000313|EMBL:EFT84153.1, RC ECO:0000313|Proteomes:UP000004946}; RA Muzny D., Qin X., Buhay C., Dugan-Rocha S., Ding Y., Chen G., RA Hawes A., Holder M., Jhangiani S., Johnson A., Khan Z., Li Z., Liu W., RA Liu X., Perez L., Shen H., Wang Q., Watt J., Xi L., Xin Y., Zhou J., RA Deng J., Jiang H., Liu Y., Qu J., Song X.-Z., Zhang L., Villasana D., RA Johnson A., Liu J., Liyanage D., Lorensuhewa L., Robinson T., Song A., RA Song B.-B., Dinh H., Thornton R., Coyle M., Francisco L., Jackson L., RA Javaid M., Korchina V., Kovar C., Mata R., Mathew T., Ngo R., RA Nguyen L., Nguyen N., Okwuonu G., Ongeri F., Pham C., Simmons D., RA Wilczek-Boney K., Hale W., Jakkamsetti A., Pham P., Ruth R., RA San Lucas F., Warren J., Zhang J., Zhao Z., Zhou C., Zhu D., Lee S., RA Bess C., Blankenburg K., Forbes L., Fu Q., Gubbala S., Hirani K., RA Jayaseelan J.C., Lara F., Munidasa M., Palculict T., Patil S., RA Pu L.-L., Saada N., Tang L., Weissenberger G., Zhu Y., Hemphill L., RA Shang Y., Youmans B., Ayvaz T., Ross M., Santibanez J., Aqrawi P., RA Gross S., Joshi V., Fowler G., Nazareth L., Reid J., Worley K., RA Petrosino J., Highlander S., Gibbs R.; RL Submitted (DEC-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EFT84153.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AEON01000001; EFT84153.1; -; Genomic_DNA. DR RefSeq; WP_006289870.1; NZ_CM001148.1. DR ProteinModelPortal; E6K041; -. DR STRING; 864564.HMPREF0620_1158; -. DR EnsemblBacteria; EFT84153; EFT84153; HMPREF0620_1158. DR KEGG; pdo:PSDT_0501; -. DR PATRIC; fig|864564.6.peg.553; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR KO; K03665; -. DR Proteomes; UP000004946; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000004946}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000004946}. FT DOMAIN 351 517 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 615 AA; 66417 MW; 87CF58BCE6356D9F CRC64; MAGKTGKQAY KSKASYKSVR KAGGRHRADR ILDEDKTKAS DNDQASQING QALRGNDRTF VDQVSQGKGT ESEGSLGGGI LSGSSEVLIS DDRQAGASAR SDFARKVNGE IGDDGEAWEE RESRNQLRHI TGLGELQDVT EVEYRQVRLE KVVLVGVWSS KETTFAQAEE SLRELAALAQ TAGAQVMDGV LQHRFKPDSA TYVGKGKANE IASIVAATEA DTIVVDADLP PSQRRALEDV TKVKVVDRTA VILDIFAQHA TSREGKAQVE LAQLEYMLPR LRGWGAALSR QAGGQAAGVN GGIGSRGPGE TQIELDRRII RTRMARLRKQ IAQMAPSREI KRGSRRRNAL PTVAVVGYTN AGKSSLINRL TGSHELVENA LFATLDTAVR QSETAENRRF MYVDTVGFVR RLPTQLIEAF KSTLEEAADA SLIIHVVDAS HPDPFAQIDA VNAVLSDVPG VAGIPSLMVF NKIDRIDAAT LERLRNLAPE AHFVSAATGQ GLEELKAAVE AGLPKPDVHV DALVPYTAGS LISQVREFGH IDQIDYEEEG IHLVADVDDR LAVHLIAASE DLASERGSDR AVDQPVHQPA GQLDSASTSP RPRPVADQNR QIQPL // ID E6K3J8_9BACT Unreviewed; 416 AA. AC E6K3J8; DT 08-MAR-2011, integrated into UniProtKB/TrEMBL. DT 08-MAR-2011, sequence version 1. DT 07-JUN-2017, entry version 39. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:EFU31766.1}; GN ORFNames=HMPREF6485_0151 {ECO:0000313|EMBL:EFU31766.1}; OS Prevotella buccae ATCC 33574. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Prevotellaceae; OC Prevotella. OX NCBI_TaxID=873513 {ECO:0000313|EMBL:EFU31766.1, ECO:0000313|Proteomes:UP000003112}; RN [1] {ECO:0000313|EMBL:EFU31766.1, ECO:0000313|Proteomes:UP000003112} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33574 {ECO:0000313|EMBL:EFU31766.1, RC ECO:0000313|Proteomes:UP000003112}; RA Muzny D., Qin X., Deng J., Jiang H., Liu Y., Qu J., Song X.-Z., RA Zhang L., Thornton R., Coyle M., Francisco L., Jackson L., Javaid M., RA Korchina V., Kovar C., Mata R., Mathew T., Ngo R., Nguyen L., RA Nguyen N., Okwuonu G., Ongeri F., Pham C., Simmons D., RA Wilczek-Boney K., Hale W., Jakkamsetti A., Pham P., Ruth R., RA San Lucas F., Warren J., Zhang J., Zhao Z., Zhou C., Zhu D., Lee S., RA Bess C., Blankenburg K., Forbes L., Fu Q., Gubbala S., Hirani K., RA Jayaseelan J.C., Lara F., Munidasa M., Palculict T., Patil S., RA Pu L.-L., Saada N., Tang L., Weissenberger G., Zhu Y., Hemphill L., RA Shang Y., Youmans B., Ayvaz T., Ross M., Santibanez J., Aqrawi P., RA Gross S., Joshi V., Fowler G., Nazareth L., Reid J., Worley K., RA Petrosino J., Highlander S., Gibbs R.; RL Submitted (OCT-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EFU31766.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AEPD01000006; EFU31766.1; -; Genomic_DNA. DR RefSeq; WP_004344033.1; NZ_GL586311.1. DR EnsemblBacteria; EFU31766; EFU31766; HMPREF6485_0151. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000003112; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000003112}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000003112}. FT DOMAIN 216 400 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 416 AA; 47750 MW; E186BFBD084C2796 CRC64; MKEFVISEVK AETAILVGLI TQEQNEAKTN EYLDELEFLA DTAGAVTVKR FTQRVGGPNQ TTYVGKGKLE EIKQYIQQEE DEEREIGMVI FDDELSAKQM RNIENELKVK ILDRTSLILD IFAMRAQTAN AKTQVELAQY RYMLPRLQRL WTHLERQGGG SGSGGGKGSV GLRGPGETQL EMDRRIILQR MSLLKQRLVE IDRQKVTQRK NRGRMIRVAL VGYTNVGKST IMNLLAKSEV FAENKLFATL DTTVRKVVVD NLPFLLADTV GFIRKLPTDL VDSFKSTLDE VREADLLIHV VDISHPDFEE QIKVVENTLG ELGCADKPSM IVFNKIDNYT WVEKEEDDLT PATKENITLD ELKRTWMARL NENCLFISAR EKENIDEFRN TLYTKVRELH VQKYPYNDFL YPMVEE // ID E6KPV1_9ACTO Unreviewed; 515 AA. AC E6KPV1; DT 08-MAR-2011, integrated into UniProtKB/TrEMBL. DT 08-MAR-2011, sequence version 1. DT 07-JUN-2017, entry version 36. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:EFU62202.1}; GN ORFNames=HMPREF9006_0331 {ECO:0000313|EMBL:EFU62202.1}; OS Actinomyces sp. oral taxon 180 str. F0310. OC Bacteria; Actinobacteria; Actinomycetales; Actinomycetaceae; OC Actinomyces. OX NCBI_TaxID=888052 {ECO:0000313|EMBL:EFU62202.1, ECO:0000313|Proteomes:UP000006252}; RN [1] {ECO:0000313|EMBL:EFU62202.1, ECO:0000313|Proteomes:UP000006252} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=F0310 {ECO:0000313|EMBL:EFU62202.1, RC ECO:0000313|Proteomes:UP000006252}; RA Muzny D., Qin X., Deng J., Jiang H., Liu Y., Qu J., Song X.-Z., RA Zhang L., Thornton R., Coyle M., Francisco L., Jackson L., Javaid M., RA Korchina V., Kovar C., Mata R., Mathew T., Ngo R., Nguyen L., RA Nguyen N., Okwuonu G., Ongeri F., Pham C., Simmons D., RA Wilczek-Boney K., Hale W., Jakkamsetti A., Pham P., Ruth R., RA San Lucas F., Warren J., Zhang J., Zhao Z., Zhou C., Zhu D., Lee S., RA Bess C., Blankenburg K., Forbes L., Fu Q., Gubbala S., Hirani K., RA Jayaseelan J.C., Lara F., Munidasa M., Palculict T., Patil S., RA Pu L.-L., Saada N., Tang L., Weissenberger G., Zhu Y., Hemphill L., RA Shang Y., Youmans B., Ayvaz T., Ross M., Santibanez J., Aqrawi P., RA Gross S., Joshi V., Fowler G., Nazareth L., Reid J., Worley K., RA Petrosino J., Highlander S., Gibbs R.; RL Submitted (NOV-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EFU62202.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AEPP01000001; EFU62202.1; -; Genomic_DNA. DR STRING; 888052.HMPREF9006_0331; -. DR EnsemblBacteria; EFU62202; EFU62202; HMPREF9006_0331. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR Proteomes; UP000006252; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000006252}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000006252}. FT DOMAIN 284 450 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 515 AA; 55548 MW; 2EE1883D7DADBCB8 CRC64; MRRTDMDTTP NGSDDATARR DQRVNDVVAR ILARSGTALA STSGQDHSGD AGELEREARA GTRRVDTGAS DRDDISEVEY RQVRLEKVVL VGLRTTQSEE EAENSLRELA ALAETAGSRV LDGIIQRRSK PDPATYLGSG KARELAEIVR AVEADTVIVD EELAPSQRRG LEDVVDAKVV DRTALILDIF AQHAKSREGK AQVELAQLEY LLPRLRGWGE SMSRQAGGRV AGGAGIGSRG PGETKIELDR RRIRTRMAKL KADIARMEPA RRTQRQSRRR GAVPSVAIAG YTNAGKSTLL NRLTDAGVLV QDALFATLDP TVRRARAADG REYTLTDTVG FVRNLPTQLV EAFRSTLEEV GQADLIVHVV DAAHPDPVSQ VQAVRSVIDT IEGARDIPEL IALNKADLAS PEQIALLRTV FPGAVALSAR TGWGVDALRA AVEDMLPRPR VCVDAVLPYS AGSLVHRIHE EGEVEREEYV EAGTRIVARV DVALAAVVAR EAVRGTVAGT AVTGA // ID E6LHG7_9ENTE Unreviewed; 407 AA. AC E6LHG7; DT 08-MAR-2011, integrated into UniProtKB/TrEMBL. DT 08-MAR-2011, sequence version 1. DT 07-JUN-2017, entry version 39. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:EFU73366.1}; GN ORFNames=HMPREF9088_1807 {ECO:0000313|EMBL:EFU73366.1}; OS Enterococcus italicus DSM 15952. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Enterococcaceae; OC Enterococcus. OX NCBI_TaxID=888064 {ECO:0000313|EMBL:EFU73366.1, ECO:0000313|Proteomes:UP000010296}; RN [1] {ECO:0000313|EMBL:EFU73366.1, ECO:0000313|Proteomes:UP000010296} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 15952 {ECO:0000313|EMBL:EFU73366.1, RC ECO:0000313|Proteomes:UP000010296}; RA Muzny D., Qin X., Deng J., Jiang H., Liu Y., Qu J., Song X.-Z., RA Zhang L., Thornton R., Coyle M., Francisco L., Jackson L., Javaid M., RA Korchina V., Kovar C., Mata R., Mathew T., Ngo R., Nguyen L., RA Nguyen N., Okwuonu G., Ongeri F., Pham C., Simmons D., RA Wilczek-Boney K., Hale W., Jakkamsetti A., Pham P., Ruth R., RA San Lucas F., Warren J., Zhang J., Zhao Z., Zhou C., Zhu D., Lee S., RA Bess C., Blankenburg K., Forbes L., Fu Q., Gubbala S., Hirani K., RA Jayaseelan J.C., Lara F., Munidasa M., Palculict T., Patil S., RA Pu L.-L., Saada N., Tang L., Weissenberger G., Zhu Y., Hemphill L., RA Shang Y., Youmans B., Ayvaz T., Ross M., Santibanez J., Aqrawi P., RA Gross S., Joshi V., Fowler G., Nazareth L., Reid J., Worley K., RA Petrosino J., Highlander S., Gibbs R.; RL Submitted (DEC-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EFU73366.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AEPV01000069; EFU73366.1; -; Genomic_DNA. DR RefSeq; WP_007208820.1; NZ_JXKT01000027.1. DR ProteinModelPortal; E6LHG7; -. DR STRING; 888064.HMPREF9088_1807; -. DR EnsemblBacteria; EFU73366; EFU73366; HMPREF9088_1807. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000010296; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000010296}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000010296}. FT DOMAIN 196 324 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 407 AA; 46390 MW; 04A81BCF2613180C CRC64; MISREKVMLV GVETEENYRQ FDSSMQELVQ LAKTANGEII DTITQKRATV DRQSLIGKGK LQELHQWVDA EEIDVVIFNQ ELSPRQQQII SQELGVLVLD RVQLILDIFA LRARSKEGKL QVELAQLNYL LPRLVGQGTS MSRLGAGIGT RGPGETKLET DRRHIRDRIA KIKRELKQVA AHRERTRSRR KQQATVQIGL IGYTNAGKST VLNRLTAADT YEQDQLFATL DPLTKKWRLT EGLTVTLTDT VGFIQELPTQ LVDAFHSTLE ESKDMDILLH VVDASSPDRT QHEATVLQLM KELELENIPT LTIYNKADKL EDDQFVPTLF PNVVVSAKNF QGKEVLSQAV KRFLMTIWEP YECWLPAEQA GQLSDLERQT LVIAKDFDEK RNSYHLRGFQ EKPSDKE // ID E6MI31_9FIRM Unreviewed; 438 AA. AC E6MI31; DT 08-MAR-2011, integrated into UniProtKB/TrEMBL. DT 08-MAR-2011, sequence version 1. DT 07-JUN-2017, entry version 39. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:EFV01355.1}; GN ORFNames=HMP0721_1736 {ECO:0000313|EMBL:EFV01355.1}; OS Pseudoramibacter alactolyticus ATCC 23263. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Eubacteriaceae; OC Pseudoramibacter. OX NCBI_TaxID=887929 {ECO:0000313|EMBL:EFV01355.1, ECO:0000313|Proteomes:UP000004754}; RN [1] {ECO:0000313|EMBL:EFV01355.1, ECO:0000313|Proteomes:UP000004754} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 23263 {ECO:0000313|EMBL:EFV01355.1, RC ECO:0000313|Proteomes:UP000004754}; RA Muzny D., Qin X., Deng J., Jiang H., Liu Y., Qu J., Song X.-Z., RA Zhang L., Thornton R., Coyle M., Francisco L., Jackson L., Javaid M., RA Korchina V., Kovar C., Mata R., Mathew T., Ngo R., Nguyen L., RA Nguyen N., Okwuonu G., Ongeri F., Pham C., Simmons D., RA Wilczek-Boney K., Hale W., Jakkamsetti A., Pham P., Ruth R., RA San Lucas F., Warren J., Zhang J., Zhao Z., Zhou C., Zhu D., Lee S., RA Bess C., Blankenburg K., Forbes L., Fu Q., Gubbala S., Hirani K., RA Jayaseelan J.C., Lara F., Munidasa M., Palculict T., Patil S., RA Pu L.-L., Saada N., Tang L., Weissenberger G., Zhu Y., Hemphill L., RA Shang Y., Youmans B., Ayvaz T., Ross M., Santibanez J., Aqrawi P., RA Gross S., Joshi V., Fowler G., Nazareth L., Reid J., Worley K., RA Petrosino J., Highlander S., Gibbs R.; RL Submitted (DEC-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EFV01355.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AEQN01000022; EFV01355.1; -; Genomic_DNA. DR RefSeq; WP_006599158.1; NZ_GL622359.1. DR STRING; 887929.HMP0721_1736; -. DR EnsemblBacteria; EFV01355; EFV01355; HMP0721_1736. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000004754; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000004754}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000004754}. FT DOMAIN 203 369 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 162 189 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 438 AA; 47907 MW; E1AB8B19642AD1BD CRC64; MKQSFYTTAP QPERALLIGI ASADDQAASP AMAELARLAQ TAGCDVFATL VQPRQKPDPK TFLGKGKIAE AAQLVTANEL DLIIADDELT PGQIAAIEAA AGCKVIDRTT LILDIFARHA STREGKLQVE LAQQRYRLSH LKGLGQVLSR TGGGIGTRGP GEKKLETDRR HIRRQIDRLQ RQLDQLAQTG AIRAQRRRRS GVRAVSLVGY TNAGKSTLFN RLTSAAVHTR DAPFVTLDTT TRRINPEYGH CLLSDTVGFI DKLPHELIRA FRATLAAAAD ADLLLHVVDA SDSRAAENIA VVERVLKEIG AIHLPRLLVY NKIDRLPPDA RTAVMARCAR ADTFAISAKT GEGLGPLAAA VIETLSAQDR IRSYLLPYRD GKRLEQLYRH AEILSREDRP EGICLTVKIG STFPDTAYRP FLIASDHSDD LEAMHDPL // ID E6MNG8_9BACT Unreviewed; 415 AA. AC E6MNG8; DT 08-MAR-2011, integrated into UniProtKB/TrEMBL. DT 08-MAR-2011, sequence version 1. DT 30-AUG-2017, entry version 42. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:EFV04882.1}; GN ORFNames=HMPREF9420_1036 {ECO:0000313|EMBL:EFV04882.1}; OS Prevotella salivae DSM 15606. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Prevotellaceae; OC Prevotella. OX NCBI_TaxID=888832 {ECO:0000313|EMBL:EFV04882.1, ECO:0000313|Proteomes:UP000003874}; RN [1] {ECO:0000313|EMBL:EFV04882.1, ECO:0000313|Proteomes:UP000003874} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 15606 {ECO:0000313|EMBL:EFV04882.1, RC ECO:0000313|Proteomes:UP000003874}; RA Muzny D., Qin X., Deng J., Jiang H., Liu Y., Qu J., Song X.-Z., RA Zhang L., Thornton R., Coyle M., Francisco L., Jackson L., Javaid M., RA Korchina V., Kovar C., Mata R., Mathew T., Ngo R., Nguyen L., RA Nguyen N., Okwuonu G., Ongeri F., Pham C., Simmons D., RA Wilczek-Boney K., Hale W., Jakkamsetti A., Pham P., Ruth R., RA San Lucas F., Warren J., Zhang J., Zhao Z., Zhou C., Zhu D., Lee S., RA Bess C., Blankenburg K., Forbes L., Fu Q., Gubbala S., Hirani K., RA Jayaseelan J.C., Lara F., Munidasa M., Palculict T., Patil S., RA Pu L.-L., Saada N., Tang L., Weissenberger G., Zhu Y., Hemphill L., RA Shang Y., Youmans B., Ayvaz T., Ross M., Santibanez J., Aqrawi P., RA Gross S., Joshi V., Fowler G., Nazareth L., Reid J., Worley K., RA Petrosino J., Highlander S., Gibbs R.; RL Submitted (DEC-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EFV04882.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AEQO01000106; EFV04882.1; -; Genomic_DNA. DR RefSeq; WP_007134305.1; NZ_GL629647.1. DR STRING; 888832.HMPREF9420_1036; -. DR EnsemblBacteria; EFV04882; EFV04882; HMPREF9420_1036. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000003874; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000003874}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000003874}. FT DOMAIN 216 400 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 415 AA; 47433 MW; EAFD2948009BBEC7 CRC64; MKEFVISEVK AETAILVGLI TNTQSEAKTK EYLDELEFLA DTAGAVTVKR FTQKANGPSS VTYVGKGKLE EIREYIEMCA ENEDPIGMVI FDDELSAKQI RNIENELKVK ILDRTSLILD IFAMRAQTAN AKTQVELAQH RYMLPRLQRL WTHLERQGGG SGSGGGKGSV GLRGPGETQL EMDRRIILQR ITLLKQRLEE IDKQKNTQRK NRGRMIRVAL VGYTNVGKST IMNLLSKSEV FAENKLFATL DTTVRKVVID NLPFLLADTV GFIRKLPTDL VDSFKSTLDE VREADLLLHV VDISHPDFEE QIQVVEKTLS DLGCSEKPSM IIFNKIDNYH WIEKDEDDLT PETRENIALE DLEKTWMARL NDNCLFISAK AKINIDEFRR TLYTKVRELH VQKYPYNDFL YPEVE // ID E6N3L6_9ARCH Unreviewed; 412 AA. AC E6N3L6; DT 08-MAR-2011, integrated into UniProtKB/TrEMBL. DT 08-MAR-2011, sequence version 1. DT 12-APR-2017, entry version 44. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=CSUB_C0149 {ECO:0000313|EMBL:BAJ50012.1}, GN HGMM_F32H09C31 {ECO:0000313|EMBL:BAJ49092.1}, GN HGMM_F37B02C05 {ECO:0000313|EMBL:BAJ46922.1}; OS Candidatus Caldiarchaeum subterraneum. OC Archaea; Thaumarchaeota; unclassified Thaumarchaeota; OC Candidatus Caldiarchaeum. OX NCBI_TaxID=311458 {ECO:0000313|EMBL:BAJ46922.1, ECO:0000313|Proteomes:UP000008120}; RN [1] {ECO:0000313|EMBL:BAJ46922.1, ECO:0000313|Proteomes:UP000008120} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16309394; DOI=10.1111/j.1462-2920.2005.00881.x; RA Nunoura T., Hirayama H., Takami H., Oida H., Nishi S., Shimamura S., RA Suzuki Y., Inagaki F., Takai K., Nealson K.H., Horikoshi K.; RT "Genetic and functional properties of uncultivated thermophilic RT crenarchaeotes from a subsurface gold mine as revealed by analysis of RT genome fragments."; RL Environ. Microbiol. 7:1967-1984(2005). RN [2] {ECO:0000313|EMBL:BAJ46922.1, ECO:0000313|Proteomes:UP000008120} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=21169198; DOI=10.1093/nar/gkq1228; RA Nunoura T., Takaki Y., Kakuta J., Nishi S., Sugahara J., Kazama H., RA Chee G., Hattori M., Kanai A., Atomi H., Takai K., Takami H.; RT "Insights into the evolution of Archaea and eukaryotic protein RT modifier systems revealed by the genome of a novel archaeal group."; RL Nucleic Acids Res. 39:3204-3223(2011). RN [3] {ECO:0000313|EMBL:BAJ46922.1} RP NUCLEOTIDE SEQUENCE. RA Takami H., Noguchi H., Takaki Y., Uchiyama I., Toyoda A., Nishi S., RA Chee G.-J., Arai W., Nunoura T., Itoh T., Hattori M., Takai K.; RT "A Deeply Branching Thermophilic Bacterium with an Ancient Acetyl-CoA RT Pathway Dominates a Subsurface Ecosystem."; RL PLoS ONE 7:e30559-e30559(2012). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AP011745; BAJ46922.1; -; Genomic_DNA. DR EMBL; AP011882; BAJ49092.1; -; Genomic_DNA. DR EMBL; BA000048; BAJ50012.1; -; Genomic_DNA. DR ProteinModelPortal; E6N3L6; -. DR KEGG; csu:CSUB_C0149; -. DR KO; K03665; -. DR OrthoDB; POG093Z07D6; -. DR Proteomes; UP000008120; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000008120}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000008120}. FT DOMAIN 186 353 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 108 135 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 412 AA; 46731 MW; A35B10AC5B69B499 CRC64; MKVALVQRLD DWAEYNLDEL EELCRSAGYT PVYKLVQRRP PHSKYMIGPG KVEELRRAVK SLKIEKIVTE NELKPVQEYN LAKALSIPVI TRTQLILETF ARRAASTEAK LQIKLAELQY ELSRAKEKVR LAKKGEQPGF HGLGAYEADV YYNEVFRRIS TIKQKLKQIR MRKNLVRQRR LEGGLPTVAL TGYTNAGKTT LFNRFSGEEH PAGPQLFTTL STTARIVKFR GRKAYLSDTV GFIKNLPHLL VESFHSTLSE FIYADLLLLV VDISEEKSVV ESKLNTCLNV LDEVGVKNVP ILVVFNKIDA AADYREKIES INPEFRYVAV SAWTGQGLDT LEEAVADMMG GYIRVRAQLE NGETTPSLLN EIKQFCNVLK IEYNSSGYEI ECETPLQLAE KIKRLAAEFH VV // ID E6N4D8_9ARCH Unreviewed; 412 AA. AC E6N4D8; DT 08-MAR-2011, integrated into UniProtKB/TrEMBL. DT 08-MAR-2011, sequence version 1. DT 12-APR-2017, entry version 38. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=HGMM_F42C08C10 {ECO:0000313|EMBL:BAJ47157.1}, GN HGMM_F43G04C10 {ECO:0000313|EMBL:BAJ49109.1}; OS Candidatus Caldiarchaeum subterraneum. OC Archaea; Thaumarchaeota; unclassified Thaumarchaeota; OC Candidatus Caldiarchaeum. OX NCBI_TaxID=311458 {ECO:0000313|EMBL:BAJ47157.1, ECO:0000313|Proteomes:UP000008120}; RN [1] {ECO:0000313|EMBL:BAJ47157.1, ECO:0000313|Proteomes:UP000008120} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16309394; DOI=10.1111/j.1462-2920.2005.00881.x; RA Nunoura T., Hirayama H., Takami H., Oida H., Nishi S., Shimamura S., RA Suzuki Y., Inagaki F., Takai K., Nealson K.H., Horikoshi K.; RT "Genetic and functional properties of uncultivated thermophilic RT crenarchaeotes from a subsurface gold mine as revealed by analysis of RT genome fragments."; RL Environ. Microbiol. 7:1967-1984(2005). RN [2] {ECO:0000313|EMBL:BAJ47157.1, ECO:0000313|Proteomes:UP000008120} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=21169198; DOI=10.1093/nar/gkq1228; RA Nunoura T., Takaki Y., Kakuta J., Nishi S., Sugahara J., Kazama H., RA Chee G., Hattori M., Kanai A., Atomi H., Takai K., Takami H.; RT "Insights into the evolution of Archaea and eukaryotic protein RT modifier systems revealed by the genome of a novel archaeal group."; RL Nucleic Acids Res. 39:3204-3223(2011). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AP011829; BAJ47157.1; -; Genomic_DNA. DR EMBL; AP011883; BAJ49109.1; -; Genomic_DNA. DR OrthoDB; POG093Z07D6; -. DR Proteomes; UP000008120; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000008120}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000008120}. FT DOMAIN 186 353 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 108 135 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 412 AA; 46791 MW; 7AB4C970F9598645 CRC64; MKVALVQRLD DWAEYNLDEL EELCRSAGYT PVYKLVQRRP PHSKYMIGPG KVEELRRAVK SLKIEKIVTE NELKPVQEYN LAKALAIPVI TRTQLILETF ARRAASTEAK LQIKLAELQY ELSRAKEKVR LAKKGEQPGF HGLGAYEADV YYNEVFRRIS TIKQKLKQIR MRKNLVRQRR LEGGLPTVAL TGYTNAGKTT LFNRFSGEEH PAGPQLFTTL STTARIVKFR GRKAYLSDTV GFIKNLPHLL VESFHSTLSE FIYADLLLLV VDISEEKSVV ESKLNTCLNV LDEVGVKNVP ILVVFNKIDS TADYREKIES IKPEYRYVAV SAWTGQGLDT LEEAVADMMG GYIRVRAQLE NGETTPSLLN EIKQFCNVLK IEYNSSGYEI ECETPLQLAE KIKRLAAEFH VV // ID E6SDL8_INTC7 Unreviewed; 495 AA. AC E6SDL8; DT 08-MAR-2011, integrated into UniProtKB/TrEMBL. DT 08-MAR-2011, sequence version 1. DT 07-JUN-2017, entry version 48. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Intca_2161 {ECO:0000313|EMBL:ADU48670.1}; OS Intrasporangium calvum (strain ATCC 23552 / DSM 43043 / JCM 3097 / OS NBRC 12989 / 7 KIP). OC Bacteria; Actinobacteria; Micrococcales; Intrasporangiaceae; OC Intrasporangium. OX NCBI_TaxID=710696 {ECO:0000313|EMBL:ADU48670.1, ECO:0000313|Proteomes:UP000008914}; RN [1] {ECO:0000313|EMBL:ADU48670.1, ECO:0000313|Proteomes:UP000008914} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 23552 / DSM 43043 / JCM 3097 / NBRC 12989 / 7 KIP RC {ECO:0000313|Proteomes:UP000008914}; RX PubMed=21304734; DOI=10.4056/sigs.1263355; RA Del Rio T.G., Chertkov O., Yasawong M., Lucas S., Deshpande S., RA Cheng J.F., Detter C., Tapia R., Han C., Goodwin L., Pitluck S., RA Liolios K., Ivanova N., Mavromatis K., Pati A., Chen A., RA Palaniappan K., Land M., Hauser L., Chang Y.J., Jeffries C.D., RA Rohde M., Pukall R., Sikorski J., Goker M., Woyke T., Bristow J., RA Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P., RA Lapidus A.; RT "Complete genome sequence of Intrasporangium calvum type strain (7 RT KIP)."; RL Stand. Genomic Sci. 3:294-303(2010). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002343; ADU48670.1; -; Genomic_DNA. DR STRING; 710696.Intca_2161; -. DR EnsemblBacteria; ADU48670; ADU48670; Intca_2161. DR KEGG; ica:Intca_2161; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000008914; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 2. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000008914}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Hydrolase {ECO:0000313|EMBL:ADU48670.1}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000008914}. FT DOMAIN 276 441 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 495 AA; 54084 MW; FAB5849E46767A75 CRC64; MKNMNRSHSI KPSAADDLLA TRAEALADET LEADPAAHGL YDGDQLDREE RAALRRVTGL STELEDITEV EYRQLRLERV VLAKVWSEGT AADAENSLRE LAALAETAGS DVLAGVIQRR QRPDPASYLG KGKAIELRDI VIAEGADTVI ADDELAPSQR RALEDVVKVK VIDRTALILD IFAQHAKSRE GKAQVELAQL QYLLPRLRGW GESMSRQAGG QAAGGQGMGS RGPGETKIEL DRRRINTRMA KLRREIADMK THRDTKRSTR KKGGVPSVAI AGYTNAGKSS LLNRLTGAGV LVENQLFATL DTTVRRSETK DGREFTLTDT VGFVRSLPTH LVEAFRSTLE EVGDADLLLH VVDGSHPDPE GQITAVREVL ADVEAADVKE VIVVNKADIA DPDVLDRIRR HEKHSIAVSA RTGAGIQELI DLIARELPKP DIEVDVLVPY HRGDLISRIH DEGEILESEH VADGTRVRAR VTPAVEADLS DYVVA // ID E6SK53_THEM7 Unreviewed; 611 AA. AC E6SK53; DT 08-MAR-2011, integrated into UniProtKB/TrEMBL. DT 08-MAR-2011, sequence version 1. DT 07-JUN-2017, entry version 48. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Tmar_1081 {ECO:0000313|EMBL:ADU51194.1}; OS Thermaerobacter marianensis (strain ATCC 700841 / DSM 12885 / JCM OS 10246 / 7p75a). OC Bacteria; Firmicutes; Clostridia; Clostridiales; OC Clostridiales Family XVII. Incertae Sedis; Thermaerobacter. OX NCBI_TaxID=644966 {ECO:0000313|EMBL:ADU51194.1, ECO:0000313|Proteomes:UP000008915}; RN [1] {ECO:0000313|Proteomes:UP000008915} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700841 / DSM 12885 / JCM 10246 / 7p75a RC {ECO:0000313|Proteomes:UP000008915}; RX DOI=10.4056/sigs.1373474; RA Han C., Gu W., Zhang X., Lapidus A., Nolan M., Copeland A., Lucas S., RA Glavina Del Rio T., Tice H., Cheng J., Tapia R., Goodwin L., RA Pitluck S., Pagani I., Ivanova N., Mavromatis K., Mikhailova N., RA Pati A., Chen A., Palaniappan K., Land M., Hauser L., Chang Y., RA Jeffries C., Schneider S., Rohde M., Goker M., Pukall R., Woyke T., RA Bristow J., Eisen J., Markowitz V., Hugenholtz P., Kyrpides N., RA Klenk H., Detter J.; RT "Complete genome sequence of Thermaerobacter marianensis type strain RT (7p75aT)."; RL Stand. Genomic Sci. 3:337-345(2010). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002344; ADU51194.1; -; Genomic_DNA. DR RefSeq; WP_013495499.1; NC_014831.1. DR STRING; 644966.Tmar_1081; -. DR EnsemblBacteria; ADU51194; ADU51194; Tmar_1081. DR KEGG; tmr:Tmar_1081; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000008915; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 2. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000008915}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000008915}. FT DOMAIN 299 544 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 611 AA; 64859 MW; 5B255C2C4BA7CC2D CRC64; MAPVRRVAGR TGQDGTGAAE GNGPEGRPVP ERPDPIPEGG QVRARLDPGA PGRQVRARPD APAEGGQARK QAGPAGKGGS RRARQDPAAE DRDPPDERAR RRAGGPERAL LVGVAWERDG RLSFDERMDE LKELARSAGA QVVGEIRQRR GRPEPATLIG PGKVAEVADA RRRLDADVVI FDRDLTPAQL RNLERAIGGK VIDRTQLILD IFAARARSRE GQLQVELAQL QYLLPRLAGM GEALSRLGGG IGTRGPGETR LEVDRRRIRR RIADLRRMLA EVRRHRSVQR KGRQRAGIPV VALVGYTNAG KTTLHAALVR RFGVAAGPVA QGRDRLFDTL DPTVRRVKWP GVGPVLVADT VGFIHDLPPH LIAAFRATLE EVLEADLLLH VVDASQPRWP VDVETVDAIL DDLGARQPRL LVMNKMDAVA AGVEDAGAGW GEGRGGEEPG IAQPATHAEA ALGGDSTADW AAAGAASPVP DGVVPAASQG TAPATGGGAA RVGRGVMPAP RTGRAGGVVR VSAWTGQGLD DLAAAVAAFL QQGLRRVTVL VPYHRPDLRT RIHDAGTVEA EEPGSDGWTL TARLPEAEVG RLRRAGCRFE DQAAPESGAV F // ID E6SSU0_BACT6 Unreviewed; 418 AA. AC E6SSU0; DT 08-MAR-2011, integrated into UniProtKB/TrEMBL. DT 08-MAR-2011, sequence version 1. DT 07-JUN-2017, entry version 48. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Bache_1193 {ECO:0000313|EMBL:ADV43203.1}; OS Bacteroides helcogenes (strain ATCC 35417 / DSM 20613 / JCM 6297 / P OS 36-108). OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae; OC Bacteroides. OX NCBI_TaxID=693979 {ECO:0000313|EMBL:ADV43203.1, ECO:0000313|Proteomes:UP000008630}; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=P 36-108; RG US DOE Joint Genome Institute (JGI-PGF); RA Lucas S., Copeland A., Lapidus A., Bruce D., Goodwin L., Pitluck S., RA Kyrpides N., Mavromatis K., Ivanova N., Zeytun A., Brettin T., RA Detter J.C., Tapia R., Han C., Land M., Hauser L., Markowitz V., RA Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Gronow S., Wellnitz S., RA Brambilla E., Klenk H.-P., Eisen J.A.; RT "The complete genome of Bacteroides helcogenes P 36-108."; RL Submitted (NOV-2010) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:ADV43203.1, ECO:0000313|Proteomes:UP000008630} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 35417 / DSM 20613 / JCM 6297 / P 36-108 RC {ECO:0000313|Proteomes:UP000008630}; RX PubMed=21475586; RA Pati A., Gronow S., Zeytun A., Lapidus A., Nolan M., Hammon N., RA Deshpande S., Cheng J.F., Tapia R., Han C., Goodwin L., Pitluck S., RA Liolios K., Pagani I., Ivanova N., Mavromatis K., Chen A., RA Palaniappan K., Land M., Hauser L., Chang Y.J., Jeffries C.D., RA Detter J.C., Brambilla E., Rohde M., Goker M., Woyke T., Bristow J., RA Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P., RA Lucas S.; RT "Complete genome sequence of Bacteroides helcogenes type strain (P 36- RT 108)."; RL Stand. Genomic Sci. 4:45-53(2011). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002352; ADV43203.1; -; Genomic_DNA. DR RefSeq; WP_013546797.1; NC_014933.1. DR STRING; 693979.Bache_1193; -. DR EnsemblBacteria; ADV43203; ADV43203; Bache_1193. DR KEGG; bhl:Bache_1193; -. DR PATRIC; fig|693979.3.peg.1262; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000008630; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000008630}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000008630}. FT DOMAIN 216 400 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 418 AA; 47599 MW; AE4B92A2456418D0 CRC64; MKEFVISEVQ AETAVLVGLI TKIQDERRTN EYLDELAFLA ETAGAEVVKR FTQKLDQANS VTYVGTGKLA EIKEYIRNEE EAEREVGMVI FDDELSAKQI RNIEAELKIK ILDRTSLILD IFAMRAQTAN AKTQVELAQY KYMLPRLQRL WTHLERQGGG SGAGGGKGSV GLRGPGETQL EMDRRIILNR MSLLKERLAE IDRQKSTQRK NRGRMIRVAL VGYTNVGKST LMNLLAKSEV FAENKLFATL DTTVRKVIIE NLPFLLSDTV GFIRKLPTDL VDSFKSTLDE VREADLLLHI VDISHPDFEE QIEVVNKTLA DIGAAGKPMI LVFNKIDAYT YVEKAADDLT PRTKENLTLE ELMKTWMAKM EDNCLFISAR ERINMEGLKS VVYGRVKELH VQKYPYNDFL YQTYEEEV // ID E6TS13_BACCJ Unreviewed; 420 AA. AC E6TS13; DT 08-MAR-2011, integrated into UniProtKB/TrEMBL. DT 08-MAR-2011, sequence version 1. DT 07-JUN-2017, entry version 52. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Bcell_2409 {ECO:0000313|EMBL:ADU30667.1}; OS Bacillus cellulosilyticus (strain ATCC 21833 / DSM 2522 / FERM P-1141 OS / JCM 9156 / N-4). OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus. OX NCBI_TaxID=649639 {ECO:0000313|EMBL:ADU30667.1, ECO:0000313|Proteomes:UP000001401}; RN [1] {ECO:0000313|EMBL:ADU30667.1, ECO:0000313|Proteomes:UP000001401} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 21833 / DSM 2522 / FERM P-1141 / JCM 9156 / N-4 RC {ECO:0000313|Proteomes:UP000001401}; RG US DOE Joint Genome Institute; RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L., RA Pitluck S., Chertkov O., Detter J.C., Han C., Tapia R., Land M., RA Hauser L., Jeffries C., Kyrpides N., Ivanova N., Mikhailova N., RA Brumm P., Mead D., Woyke T.; RT "Complete sequence of Bacillus cellulosilyticus DSM 2522."; RL Submitted (DEC-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002394; ADU30667.1; -; Genomic_DNA. DR RefSeq; WP_013489001.1; NC_014829.1. DR ProteinModelPortal; E6TS13; -. DR STRING; 649639.Bcell_2409; -. DR EnsemblBacteria; ADU30667; ADU30667; Bcell_2409. DR KEGG; bco:Bcell_2409; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000001401; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000001401}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000001401}. FT DOMAIN 196 358 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 420 AA; 48025 MW; D4B58A0BF3B18FA1 CRC64; MNKENVLIVG LKTQKIDEEQ FQYRMEELEA LTNTAGGNVV MQVTQNRERP DSATYIGRGK VDEIITILEE LEVELVIFND ELSPSQLRNL TSQLDVKVID RTQLILDIFA GRARSKEGKL QVELAQLGYL LPRLRGQGAM LSRLGGGIGT RGPGETQLET DQRHIRNRMT DIRMQLEQIV SHRERYRARR KKNQAFQISL VGYTNAGKST LLHRLSEADI YVEDQLFATL DPTTKKIKLP SGMEVLLTDT VGFIQQLPTT LIAAFRSTLE EVKEADLILH VVDAANPDYP NHEKTVYKLL EELEAEKIPV LTVYNKRDLL HGDFFSYTKS ASILISSKEK ADLDKLQEKI ESVMEEIFSP YIFHVDANEG KWLHRLQRET IQVEQYFDEQ SEQYVVRGYA APDSAIFHEM QAKQLDTRGE // ID E6VRH7_DESAO Unreviewed; 535 AA. AC E6VRH7; DT 08-MAR-2011, integrated into UniProtKB/TrEMBL. DT 08-MAR-2011, sequence version 1. DT 07-JUN-2017, entry version 45. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Daes_2006 {ECO:0000313|EMBL:ADU63014.1}; OS Desulfovibrio aespoeensis (strain ATCC 700646 / DSM 10631 / Aspo-2). OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfovibrionales; OC Desulfovibrionaceae; Desulfovibrio. OX NCBI_TaxID=643562 {ECO:0000313|EMBL:ADU63014.1, ECO:0000313|Proteomes:UP000002191}; RN [1] {ECO:0000313|Proteomes:UP000002191} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700646 / DSM 10631 / Aspo-2 RC {ECO:0000313|Proteomes:UP000002191}; RG US DOE Joint Genome Institute; RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L., RA Pitluck S., Chertkov O., Misra M., Detter J.C., Han C., Tapia R., RA Land M., Hauser L., Kyrpides N., Ivanova N., Ovchinnikova G., RA Pedersen K., Jagevall S., Hazen T., Woyke T.; RT "Complete sequence of Desulfovibrio aespoeensis Aspo-2."; RL Submitted (DEC-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002431; ADU63014.1; -; Genomic_DNA. DR ProteinModelPortal; E6VRH7; -. DR STRING; 643562.Daes_2006; -. DR EnsemblBacteria; ADU63014; ADU63014; Daes_2006. DR KEGG; das:Daes_2006; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; EREVIIT; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000002191; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000002191}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000002191}. FT DOMAIN 367 532 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 333 360 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 535 AA; 59841 MW; 59D0D3A0512EC022 CRC64; MKPNQIKRLV RLYQRQFPPD SNYTIEQARE LADLSADTGR QIALLIDRQG RVEMVLVGDN RSIYIPELPR ARMSSGRLRG LRLLHTHLAG ESLSQEDLMD MVFLRLDSVT ALTVAEGGPQ TAQVAHLLPP NPDDKSYEVF DQVRWDRLDL DLAKLIEALE DEFSRQIGAR DLDSSEERVL LVSVDDTPQT VQQLSLEELA ELADTAGLVA AGTMIQRVRK KNPKFIMGKG KLAELEVKAL QTNASVVIFD QELSPTQIRN LAEITERKIL DRTQLILDIF AQHATSASGK LQVEMAQLKY TLPRLVGKNR AMSRLMGGIG GRGPGETKLE IDRRRIDDRL TRLKKELEQV RKRRTQTRER RAKAGLPIVS LVGYTNAGKS TLLNTLTQSK VLAEDKLFAT LDPTSRRIRF PQEREVVLTD TVGFIRRLPP DLKEAFRATL EELESADLLV LVCDAAHPEA EQQVEAVRSI LADMELDAIP SILVLNKWDR LDEEGREAMG NVFPGGIPAS ALNRSSLEPV VEAILAAIPW GRLAD // ID E6W206_DESIS Unreviewed; 433 AA. AC E6W206; DT 08-MAR-2011, integrated into UniProtKB/TrEMBL. DT 08-MAR-2011, sequence version 1. DT 07-JUN-2017, entry version 48. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Selin_1905 {ECO:0000313|EMBL:ADU66632.1}; OS Desulfurispirillum indicum (strain ATCC BAA-1389 / S5). OC Bacteria; Chrysiogenetes; Chrysiogenales; Chrysiogenaceae; OC Desulfurispirillum. OX NCBI_TaxID=653733 {ECO:0000313|EMBL:ADU66632.1, ECO:0000313|Proteomes:UP000002572}; RN [1] {ECO:0000313|EMBL:ADU66632.1, ECO:0000313|Proteomes:UP000002572} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-1389 / S5 {ECO:0000313|Proteomes:UP000002572}; RG US DOE Joint Genome Institute; RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L., RA Pitluck S., Chertkov O., Held B., Detter J.C., Han C., Tapia R., RA Land M., Hauser L., Kyrpides N., Ivanova N., Mikhailova N., RA Haggblom M., Rauschenbach I., Bini E., Woyke T.; RT "Complete sequence of Desulfurispirillum indicum S5."; RL Submitted (DEC-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002432; ADU66632.1; -; Genomic_DNA. DR ProteinModelPortal; E6W206; -. DR STRING; 653733.Selin_1905; -. DR EnsemblBacteria; ADU66632; ADU66632; Selin_1905. DR KEGG; din:Selin_1905; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000002572; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000002572}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000002572}. FT DOMAIN 209 377 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 182 209 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 433 AA; 49798 MW; 38F5F15975F7D03A CRC64; MYQEELKGYF LFDRYQRGEQ AIIVHVNFSR QTMDAEDLNE CMELAQSAGA SVLSVFQCNR DEPDSRLYIG SGKAQEIAQY VEEQAVEIAI FNHTLSPTQE RNLEKLFQCR VIDRTGLILD IFAQRARTFE GKLQVELAQL RYMSTRLVRG WTHLERQKGG IGMRGPGETQ LETDRRLIRK RIEYIQQRLE KVTRQRQQVR QHRTRHEKAT ISLVGYTNAG KSTLFNALTT STVYAHDQLF ATLDPTIRSL SLPGMPDAFL ADTVGFIRHL PHTLVAAFRS TLQETRESTL LLHVMDASHE ELERNRESVL KVLEDIEAIE VAQLEVMNKI DRIPEGIEPH IDYDDEGKPR RVWISALRGQ GLDLLRQAVA QLLEPQLKRS HIVLGPAQGK LRALLYERNA IVNETLDDEG NWILEVFLAR EHLERLLESH PPC // ID E6WFZ2_PANSA Unreviewed; 426 AA. AC E6WFZ2; DT 08-MAR-2011, integrated into UniProtKB/TrEMBL. DT 08-MAR-2011, sequence version 1. DT 30-AUG-2017, entry version 50. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Pat9b_3557 {ECO:0000313|EMBL:ADU70847.1}; OS Pantoea sp. (strain At-9b). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; OC Erwiniaceae; Pantoea. OX NCBI_TaxID=592316 {ECO:0000313|EMBL:ADU70847.1, ECO:0000313|Proteomes:UP000001624}; RN [1] {ECO:0000313|EMBL:ADU70847.1, ECO:0000313|Proteomes:UP000001624} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=At-9b {ECO:0000313|EMBL:ADU70847.1, RC ECO:0000313|Proteomes:UP000001624}; RG US DOE Joint Genome Institute; RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L., RA Pitluck S., Davenport K., Detter J.C., Han C., Tapia R., Land M., RA Hauser L., Kyrpides N., Ivanova N., Ovchinnikova G., Pinto A., RA Currie C., Woyke T.; RT "Complete sequence chromosome of Pantoea sp. At-9b."; RL Submitted (DEC-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002433; ADU70847.1; -; Genomic_DNA. DR RefSeq; WP_013510697.1; NC_014837.1. DR ProteinModelPortal; E6WFZ2; -. DR STRING; 592316.Pat9b_3557; -. DR EnsemblBacteria; ADU70847; ADU70847; Pat9b_3557. DR KEGG; pao:Pat9b_3557; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000001624; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000001624}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000001624}. FT DOMAIN 198 365 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 426 AA; 47809 MW; F4C92B6A7686410C CRC64; MFDRYDAGEQ AVLVHIWFSQ DKELEDLQEF ETLVSSAGVE ALQVITGSRK APHPKYFVGE GKAVEIADAV KASGASVVLF DHALSPAQER NLERLCECRV VDRTGLILDI FAQRARTHEG KLQVELAQLR HLATRLVRGW THLERQKGGI GLRGPGETQL ETDRRLLRNR ISLILSRLER VEKQREQGRQ ARAKADVPTV SLVGYTNAGK STLFNAITSA DVYAADQLFA TLDPTLRRLN VADVGEVVLA DTVGFIRHLP HDLVAAFKAT LQETRQATLL MHVIDAADLR VNDNIEAVNE VLAEIEADEI PTLLIMNKID MLDGFVPRID RDEENKPIRV WLSAQTGVGL PLLWQALSER LAGEIAQYDL RLPPEAGRLR SRFYQLQAIE KEWNEDDGSV GLHVRMPIVD WRRLCKQEPS LASYIV // ID E6WQY6_PSEUU Unreviewed; 444 AA. AC E6WQY6; DT 08-MAR-2011, integrated into UniProtKB/TrEMBL. DT 08-MAR-2011, sequence version 1. DT 30-AUG-2017, entry version 50. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Psesu_0805 {ECO:0000313|EMBL:ADV26658.1}; OS Pseudoxanthomonas suwonensis (strain 11-1). OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales; OC Xanthomonadaceae; Pseudoxanthomonas. OX NCBI_TaxID=743721 {ECO:0000313|EMBL:ADV26658.1, ECO:0000313|Proteomes:UP000008632}; RN [1] {ECO:0000313|EMBL:ADV26658.1, ECO:0000313|Proteomes:UP000008632} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=11-1 {ECO:0000313|Proteomes:UP000008632}; RG US DOE Joint Genome Institute; RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L., RA Pitluck S., Teshima H., Detter J.C., Han C., Tapia R., Land M., RA Hauser L., Kyrpides N., Ivanova N., Ovchinnikova G., Siebers A.K., RA Allgaier M., Thelen M.P., Hugenholtz P., Gladden J., Woyke T.; RT "Complete sequence of Pseudoxanthomonas suwonensis 11-1."; RL Submitted (JAN-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002446; ADV26658.1; -; Genomic_DNA. DR RefSeq; WP_013534488.1; NC_014924.1. DR STRING; 743721.Psesu_0805; -. DR EnsemblBacteria; ADV26658; ADV26658; Psesu_0805. DR KEGG; psu:Psesu_0805; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000008632; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000008632}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000008632}. FT DOMAIN 198 369 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 157 191 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 444 AA; 48722 MW; 8B551347530E186A CRC64; MFERSRKGEH ALLIQPHSGG LAEDVLEEFA DLARSAGASV AATLTARIDR PNPATLIGSG KLEEVKAAAE ATGADLILVN HPLSPVQERN LERALQRRVV DRTGLILDIF AQRARSHEGK LQVELAQLKH LATRLVRGWT HLERQRGGSI GLRGPGETQL ETDRRLLQKR LEQLQKRLEK VEVQHTQMRR ARVRSELPRV ALVGYTNAGK STLFNALTGA DAYAADQLFA TLDPTVRRIS LPGGSVVLAD TVGFVRDLPH ELVAAFRSTL SEAREADLLL HVVDAADPLR EERIAQVDSV LSEVGAGELP QLLVFNKIDR IERAEPRHDH AAAAADEPGH RERVWLSARD GRGLELLQAA LAQRLDLQRA TGELRLPPAA GRLRAQLHAL GAVRSEQADE DGWLLQLDLP RGEAERLAAR EGGEPLRALL PPPAPEDWET DAGR // ID E6XBS8_CELAD Unreviewed; 403 AA. AC E6XBS8; DT 08-MAR-2011, integrated into UniProtKB/TrEMBL. DT 08-MAR-2011, sequence version 1. DT 07-JUN-2017, entry version 46. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Celal_1621 {ECO:0000313|EMBL:ADV48930.1}; OS Cellulophaga algicola (strain DSM 14237 / IC166 / ACAM 630). OC Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales; OC Flavobacteriaceae; Cellulophaga. OX NCBI_TaxID=688270 {ECO:0000313|EMBL:ADV48930.1, ECO:0000313|Proteomes:UP000008634}; RN [1] {ECO:0000313|EMBL:ADV48930.1, ECO:0000313|Proteomes:UP000008634} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 14237 / IC166 / ACAM 630 RC {ECO:0000313|Proteomes:UP000008634}; RX PubMed=21475589; RA Abt B., Lu M., Misra M., Han C., Nolan M., Lucas S., Hammon N., RA Deshpande S., Cheng J.F., Tapia R., Goodwin L., Pitluck S., RA Liolios K., Pagani I., Ivanova N., Mavromatis K., Ovchinikova G., RA Pati A., Chen A., Palaniappan K., Land M., Hauser L., Chang Y.J., RA Jeffries C.D., Detter J.C., Brambilla E., Rohde M., Tindall B.J., RA Goker M., Woyke T., Bristow J., Eisen J.A., Markowitz V., RA Hugenholtz P., Kyrpides N.C., Klenk H.P., Lapidus A.; RT "Complete genome sequence of Cellulophaga algicola type strain RT (IC166)."; RL Stand. Genomic Sci. 4:72-80(2010). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002453; ADV48930.1; -; Genomic_DNA. DR RefSeq; WP_013550411.1; NC_014934.1. DR ProteinModelPortal; E6XBS8; -. DR STRING; 688270.Celal_1621; -. DR EnsemblBacteria; ADV48930; ADV48930; Celal_1621. DR KEGG; cao:Celal_1621; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000008634; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000008634}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Hydrolase {ECO:0000313|EMBL:ADV48930.1}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000008634}. FT DOMAIN 200 385 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 403 AA; 46920 MW; F6AFD7CC2A42A9E8 CRC64; MLEQKEIDYE RTILIGVINK DQNEVKVKEF LDELEFLTYT AGGEVYKRFV QKVDLPNPKT YIGSGKMMDV EAYVEEHEIG CVIFDDELSP AQQRNIEKQL KCKILDRTHL ILDIFSQRAQ TSYARTQVEL AQYEYLLPRL KGLWTHLERQ KGGIGMRGPG ETEIETDRRI VRDRITLLKK KLLKIDRQME TQRGNRGALV RVALVGYTNV GKSTLMNVVS KSDVFAENKL FATLDTTVRK VVVGNLPFLL SDTVGFIRKL PTQLVESFKS TLDEVREADL LLHVVDISHP QFEEHIASVN KILGEIGSGD KKTIMVFNKI DQFTHETIDD DDLITERTEE HFTLDEWRQT WMRKVGDRAL FISAINKENL DEFRKRIYDE VRDIHVTRFP YNNFLYPEHL DEY // ID E7G5W9_9FIRM Unreviewed; 419 AA. AC E7G5W9; DT 05-APR-2011, integrated into UniProtKB/TrEMBL. DT 05-APR-2011, sequence version 1. DT 07-JUN-2017, entry version 41. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=HMPREF9488_00157 {ECO:0000313|EMBL:EFW06620.1}; OS Coprobacillus sp. 29_1. OC Bacteria; Firmicutes; Erysipelotrichia; Erysipelotrichales; OC Erysipelotrichaceae; Coprobacillus. OX NCBI_TaxID=469596 {ECO:0000313|EMBL:EFW06620.1, ECO:0000313|Proteomes:UP000003157}; RN [1] {ECO:0000313|EMBL:EFW06620.1, ECO:0000313|Proteomes:UP000003157} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=29_1 {ECO:0000313|EMBL:EFW06620.1, RC ECO:0000313|Proteomes:UP000003157}; RG The Broad Institute Genome Sequencing Platform; RA Earl A., Ward D., Feldgarden M., Gevers D., Daigneault M., RA Sibley C.D., White A., Strauss J., Allen-Vercoe E., Young S.K., RA Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., RA Alvarado L., Arachchi H.M., Berlin A., Brown A., Chapman S.B., RA Chen Z., Dunbar C., Freedman E., Gearin G., Gellesch M., Goldberg J., RA Griggs A., Gujja S., Heilman E., Heiman D., Howarth C., Larson L., RA Lui A., MacDonald P.J.P., Mehta T., Montmayeur A., Murphy C., RA Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T., RA Shenoy N., Sisk P., Stolte C., Sykes S., White J., Yandava C., RA Nusbaum C., Birren B.; RT "The Genome Sequence of Coprobacillus sp. strain 29_1."; RL Submitted (DEC-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EFW06620.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADKX01000001; EFW06620.1; -; Genomic_DNA. DR ProteinModelPortal; E7G5W9; -. DR STRING; 469596.HMPREF9488_00157; -. DR EnsemblBacteria; EFW06620; EFW06620; HMPREF9488_00157. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000003157; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000003157}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000003157}. FT DOMAIN 201 362 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 419 AA; 49238 MW; 3C23AE92BF8AEBF7 CRC64; MTPYNRERGE NVKAILVGVE YDHMYYDLHI SMEELKELAR ACQIEVKDVM IQRLSQISPK YYIGKGKVQE LKDMLTDDDM VIFNEELSPM QIKNLTDELD VEVSDRSDLI LRIFESRAQT KEAKLQVEIA RNQYLLPRLA GMKEELYSQQ GGSGFRGSGE KQIELDRRVI HRQLVQARRE LQSIVKQRQT QRQLRKRNQQ KVVCLVGYTN SGKSSLLNYF TDKKVFQEDM LFASLQTASR KVTLKGHKEI IMSDTVGFIN QLPHHLVQAF RSTLEEVKEA DLLLHVVDSS SAYSDIQIET TQQVLEALGV KDTPVIYVYN KVDKDRYAFL QPHQPYVFVS VKEQINLDKL EELMIETLFK DYELIELYIP YDHGEIFQQI QQTYEFIKEE YLETGIYISF FIDMKQKHKY QQYIYHPLN // ID E7GS46_CLOSY Unreviewed; 418 AA. AC E7GS46; DT 05-APR-2011, integrated into UniProtKB/TrEMBL. DT 05-APR-2011, sequence version 1. DT 07-JUN-2017, entry version 37. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=HMPREF9474_03741 {ECO:0000313|EMBL:EGA92427.1}; OS [Clostridium] symbiosum WAL-14163. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Lachnospiraceae. OX NCBI_TaxID=742740 {ECO:0000313|EMBL:EGA92427.1, ECO:0000313|Proteomes:UP000002970}; RN [1] {ECO:0000313|EMBL:EGA92427.1, ECO:0000313|Proteomes:UP000002970} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=WAL-14163 {ECO:0000313|EMBL:EGA92427.1, RC ECO:0000313|Proteomes:UP000002970}; RA Earl A., Ward D., Feldgarden M., Gevers D., Finegold S.M., RA Summanen P.H., Molitoris D.R., Vaisanen M.L., Daigneault M., RA Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B., RA Abouelleil A., Alvarado L., Arachchi H.M., Berlin A., Brown A., RA Chapman S.B., Chen Z., Dunbar C., Freedman E., Gearin G., Gellesch M., RA Goldberg J., Griggs A., Gujja S., Heilman E., Heiman D., Howarth C., RA Larson L., Lui A., MacDonald P.J.P., Mehta T., Montmayeur A., RA Murphy C., Neiman D., Pearson M., Priest M., Roberts A., Saif S., RA Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., White J., RA Yandava C., Nusbaum C., Birren B.; RT "The Genome Sequence of Clostridium symbiosum strain WAL-14163."; RL Submitted (DEC-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EGA92427.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADLQ01000081; EGA92427.1; -; Genomic_DNA. DR RefSeq; WP_003503546.1; NZ_GL834316.1. DR STRING; 742740.HMPREF9474_03741; -. DR EnsemblBacteria; EGA92427; EGA92427; HMPREF9474_03741. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR Proteomes; UP000002970; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000002970}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000002970}. FT DOMAIN 202 366 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 418 AA; 46970 MW; D53FDDCFD22CB58F CRC64; MAELIDLKEL EERVILIAVS TSDEDDTRQS LDELEELADT AGAVTVDKII QNRERIHPGT YLGKGKIEEV RERVFELGAT GVICDDELSP AQLRNLENAL DTKVMDRTMV ILDIFASHAV TSEGKIQVEL AQLKYRAARL VGLRNSLSRL GGGIGTRGPG EKKLEVDRRL IHDRIGQLKA ELLEVKRHRE VARKQRDRNY TLSAAIVGYT NAGKSTLLNK LTGAGILAED KLFATLDPTT RGMELPSGQK ILLTDTVGFI RKLPHHLIEA FRSTLEEARY SDIILHVVDC VSPQMDSQIH IVYETLRKLE IKDKTIVTVF NKIDCLEQEV ILKDLQSDYQ VKISARTGEG LEELTEILET ILRGRKIFLE KLYTYKDAGK IQTIRKFGQL LSEEYRDDGI LVTAYVPTEL YAGLMAEA // ID E7MPC4_9FIRM Unreviewed; 413 AA. AC E7MPC4; DT 05-APR-2011, integrated into UniProtKB/TrEMBL. DT 05-APR-2011, sequence version 1. DT 07-JUN-2017, entry version 39. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:EFW24029.1}; GN ORFNames=HMPREF9430_01405 {ECO:0000313|EMBL:EFW24029.1}; OS Solobacterium moorei F0204. OC Bacteria; Firmicutes; Erysipelotrichia; Erysipelotrichales; OC Erysipelotrichaceae; Solobacterium. OX NCBI_TaxID=706433 {ECO:0000313|EMBL:EFW24029.1, ECO:0000313|Proteomes:UP000004097}; RN [1] {ECO:0000313|EMBL:EFW24029.1, ECO:0000313|Proteomes:UP000004097} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=F0204 {ECO:0000313|EMBL:EFW24029.1, RC ECO:0000313|Proteomes:UP000004097}; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Hou S., Chen J., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Zhang X., Suruliraj S., Warren W., Chinwalla A., RA Mardis E.R., Wilson R.K.; RL Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EFW24029.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AECQ01000028; EFW24029.1; -; Genomic_DNA. DR RefSeq; WP_006526212.1; NZ_GL637665.1. DR ProteinModelPortal; E7MPC4; -. DR STRING; 706433.HMPREF9430_01405; -. DR EnsemblBacteria; EFW24029; EFW24029; HMPREF9430_01405. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000004097; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000004097}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000004097}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1 23 {ECO:0000256|SAM:SignalP}. FT CHAIN 24 413 GTPase HflX. {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5003219114. FT DOMAIN 194 357 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 160 187 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 413 AA; 46585 MW; 782095A41B66C647 CRC64; MRKIILAGVC LQASSSIFTS AMQECEALCK ACDLEVLGTI TQQSKSMDPH TAFRIGKLET LKVMCEELEA DGIIFYNPLK IQVSDRISAY CGVNVIDRTA LILDIFSKRA RSRQAKLQTE VARLQYDLPR VLHSDNDNER SRGGAVTNRG AGEMRSSIIA TRYQKKISDL KEELRKIEVR RYQDERRRQK TLLKRVALVG YTNAGKSSLM NAILSMQDAG GQEVLEQDML FATLDTSVRM VQSKHKKFLL YDTVGFVSDL PHGLIEAFKS TLDAARDADL LVHVIDAADP SWQEKSAITQ ETLKEIHAAD IPQIHVFNKI DKLAHPERVD GLSISCYTKE GLDTLLEEII EMIYPAEESI VCKLGYDKIS MFDTYKAILD MDILEYHQNG LIARITGEKK MLHVFAKYQI KGE // ID E7NDY7_9ACTO Unreviewed; 532 AA. AC E7NDY7; DT 05-APR-2011, integrated into UniProtKB/TrEMBL. DT 05-APR-2011, sequence version 1. DT 07-JUN-2017, entry version 37. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:EFW25623.1}; GN ORFNames=HMPREF9057_03033 {ECO:0000313|EMBL:EFW25623.1}; OS Actinomyces sp. oral taxon 171 str. F0337. OC Bacteria; Actinobacteria; Actinomycetales; Actinomycetaceae; OC Actinomyces. OX NCBI_TaxID=706439 {ECO:0000313|EMBL:EFW25623.1, ECO:0000313|Proteomes:UP000005722}; RN [1] {ECO:0000313|EMBL:EFW25623.1, ECO:0000313|Proteomes:UP000005722} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=F0337 {ECO:0000313|EMBL:EFW25623.1, RC ECO:0000313|Proteomes:UP000005722}; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Hou S., Chen J., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Zhang X., Suruliraj S., Warren W., Chinwalla A., RA Mardis E.R., Wilson R.K.; RL Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EFW25623.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AECW01000551; EFW25623.1; -; Genomic_DNA. DR RefSeq; WP_009398584.1; NZ_GL637946.1. DR EnsemblBacteria; EFW25623; EFW25623; HMPREF9057_03033. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000005722; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 2. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000005722}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}. FT DOMAIN 308 473 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 532 AA; 56707 MW; 0C9E6C577EE80FCE CRC64; MTQHHSSTPS IPDDVCDAQE GRDVRDVVAR VLSRTGTALA STSAQHEHAD DFEDGDDDGA LEREARAARR RVAGLSTELE DVSEVEYRQV RLEKVVLVGL ELPRPHGSAT GAPGGSGLQV RDTQDADTSL RELAALAQTA GSQVLDALIQ RRDHPDPATY LGSGKARELA EVVAAAGADT VIVDGELAPS QRRALEDVVG VKVVDRTALI LDIFAQHAKS REGKAQVELA QLEYLLPRLR GWGESMSRQA GGRVAAGQGI GSRGPGETKI ELDRRRIRQR MARLRREIQA MAPSRETKRG SRRRGAIPSV AIAGYTNAGK SSLMNRLTEA GIMVEDALFA TLDPTVRRAE TSEGRTYTLT DTVGFVRNLP HELIEAFRST LEEVAGADLV LHVVDAAHPD PLSQVAAVRT VLSEIPGALD VPELIVLNKT DLADAVTLAA LRTGLPGAVA VSARTGEGIE ELRARIEQML PHPQVSIDVV VPYSRGDLVS RVHAEGEIDT VDYVETGTHV VARVGAALAA EIEGAAAGVT VG // ID E7NWS8_TREPH Unreviewed; 386 AA. AC E7NWS8; DT 05-APR-2011, integrated into UniProtKB/TrEMBL. DT 05-APR-2011, sequence version 1. DT 07-JUN-2017, entry version 39. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:EFW36994.1}; GN ORFNames=HMPREF9554_02543 {ECO:0000313|EMBL:EFW36994.1}; OS Treponema phagedenis F0421. OC Bacteria; Spirochaetes; Spirochaetales; Spirochaetaceae; Treponema. OX NCBI_TaxID=754027 {ECO:0000313|EMBL:EFW36994.1, ECO:0000313|Proteomes:UP000004157}; RN [1] {ECO:0000313|EMBL:EFW36994.1, ECO:0000313|Proteomes:UP000004157} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=F0421 {ECO:0000313|EMBL:EFW36994.1, RC ECO:0000313|Proteomes:UP000004157}; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Hou S., Chen J., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Zhang X., Suruliraj S., Warren W., Chinwalla A., RA Mardis E.R., Wilson R.K.; RL Submitted (SEP-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EFW36994.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AEFH01000216; EFW36994.1; -; Genomic_DNA. DR RefSeq; WP_002700364.1; NZ_GL638102.1. DR ProteinModelPortal; E7NWS8; -. DR STRING; 754027.HMPREF9554_02543; -. DR EnsemblBacteria; EFW36994; EFW36994; HMPREF9554_02543. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000004157; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000004157}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000004157}. FT DOMAIN 214 383 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 173 200 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 386 AA; 43525 MW; 14E69E0F87E6DEB5 CRC64; MNLQELKQEQ KKALLIFTDV YSEKIIGNYN VKSFAALKAI EEEELKNLTE TIFVNPVFSL RFNINTRNPA TFVGSGQLEK IAETASEENA DVIIFNSDLS PRVQRNLEAA LDLCVIDRRE VIIQIFADRA QTREAVVQAQ LARLEYSMPR LTRRWTGLAQ QRGGVKGSRG AGEKKLELDR RRVRTEITRL KNEVEKVRVQ RTVQRKNRIF GSKKIGAIVG YTNSGKSSLL KKLSGTEIFT EDKLFATLDA ETRKIYFENE LGSAQFLLTD TVGFVSNLPH QLIDAFRSTL EEAAIADFLL IICDASHPAM RECLNVTMEV LHELNCADKP TVIAINKMDA PFDPTEIMAL KTQHPEAVEI SVKTGLGIEN LKTALFKQVQ NRTKTH // ID E7RPZ3_9BACT Unreviewed; 414 AA. AC E7RPZ3; DT 05-APR-2011, integrated into UniProtKB/TrEMBL. DT 05-APR-2011, sequence version 1. DT 07-JUN-2017, entry version 40. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:EFZ37186.1}; GN ORFNames=HMPREF0663_11244 {ECO:0000313|EMBL:EFZ37186.1}; OS Prevotella oralis ATCC 33269. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Prevotellaceae; OC Prevotella. OX NCBI_TaxID=873533 {ECO:0000313|EMBL:EFZ37186.1, ECO:0000313|Proteomes:UP000005580}; RN [1] {ECO:0000313|EMBL:EFZ37186.1, ECO:0000313|Proteomes:UP000005580} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33269 {ECO:0000313|EMBL:EFZ37186.1, RC ECO:0000313|Proteomes:UP000005580}; RA Muzny D., Qin X., Buhay C., Dugan-Rocha S., Ding Y., Chen G., RA Hawes A., Holder M., Jhangiani S., Johnson A., Khan Z., Li Z., Liu W., RA Liu X., Perez L., Shen H., Wang Q., Watt J., Xi L., Xin Y., Zhou J., RA Deng J., Jiang H., Liu Y., Qu J., Song X.-Z., Zhang L., Villasana D., RA Johnson A., Liu J., Liyanage D., Lorensuhewa L., Robinson T., Song A., RA Song B.-B., Dinh H., Thornton R., Coyle M., Francisco L., Jackson L., RA Javaid M., Korchina V., Kovar C., Mata R., Mathew T., Ngo R., RA Nguyen L., Nguyen N., Okwuonu G., Ongeri F., Pham C., Simmons D., RA Wilczek-Boney K., Hale W., Jakkamsetti A., Pham P., Ruth R., RA San Lucas F., Warren J., Zhang J., Zhao Z., Zhou C., Zhu D., Lee S., RA Bess C., Blankenburg K., Forbes L., Fu Q., Gubbala S., Hirani K., RA Jayaseelan J.C., Lara F., Munidasa M., Palculict T., Patil S., RA Pu L.-L., Saada N., Tang L., Weissenberger G., Zhu Y., Hemphill L., RA Shang Y., Youmans B., Ayvaz T., Ross M., Santibanez J., Aqrawi P., RA Gross S., Joshi V., Fowler G., Nazareth L., Reid J., Worley K., RA Petrosino J., Highlander S., Gibbs R.; RL Submitted (JAN-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EFZ37186.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AEPE02000004; EFZ37186.1; -; Genomic_DNA. DR RefSeq; WP_004368527.1; NZ_GL833118.1. DR STRING; 873533.HMPREF0663_11244; -. DR EnsemblBacteria; EFZ37186; EFZ37186; HMPREF0663_11244. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000005580; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000005580}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000005580}. FT DOMAIN 216 400 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 414 AA; 47457 MW; FE4BC682CCF3F724 CRC64; MKEFVISEVK AETAVLVGLI TKEQDEAKTK EYLDELEFLA DTAGAVTVRR FTQKVGGPNS VTYVGTGKLE EIKQYIKDEE EAERPVGMVI FDDELSAKQI RVIEKELGVK ILDRTSLILD IFAMRAQTAN AKTQVELAQY RYMLPRLQRL WTHLERQGGG SGSGGGKGSV GLRGPGETQL EMDRRIILQR MSLLKRRLEE IDKQKTTQRK NRGRMIRVAL VGYTNVGKST IMNLLAKSEV FAENKLFATL DTTVRKVVVD NLPFLLADTV GFIRKLPTDL VDSFKSTLDE VREADLLLHV VDISHPDFEE QITVVENTLK ELGCAEKPSM IVFNKIDNYK WVEKEEDDLT PMTKENVTLD ELKRTWMARL NENCLFISAR ERLNIDEFRE ILYKKVRELH VQKYPYNDFL YPVE // ID E7RVP0_9BURK Unreviewed; 393 AA. AC E7RVP0; DT 05-APR-2011, integrated into UniProtKB/TrEMBL. DT 05-APR-2011, sequence version 1. DT 05-JUL-2017, entry version 39. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:EFV95373.1}; GN ORFNames=HMPREF0551_0861 {ECO:0000313|EMBL:EFV95373.1}; OS Lautropia mirabilis ATCC 51599. OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Lautropia. OX NCBI_TaxID=887898 {ECO:0000313|EMBL:EFV95373.1, ECO:0000313|Proteomes:UP000011021}; RN [1] {ECO:0000313|EMBL:EFV95373.1, ECO:0000313|Proteomes:UP000011021} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51599 {ECO:0000313|EMBL:EFV95373.1, RC ECO:0000313|Proteomes:UP000011021}; RA Muzny D., Qin X., Deng J., Jiang H., Liu Y., Qu J., Song X.-Z., RA Zhang L., Thornton R., Coyle M., Francisco L., Jackson L., Javaid M., RA Korchina V., Kovar C., Mata R., Mathew T., Ngo R., Nguyen L., RA Nguyen N., Okwuonu G., Ongeri F., Pham C., Simmons D., RA Wilczek-Boney K., Hale W., Jakkamsetti A., Pham P., Ruth R., RA San Lucas F., Warren J., Zhang J., Zhao Z., Zhou C., Zhu D., Lee S., RA Bess C., Blankenburg K., Forbes L., Fu Q., Gubbala S., Hirani K., RA Jayaseelan J.C., Lara F., Munidasa M., Palculict T., Patil S., RA Pu L.-L., Saada N., Tang L., Weissenberger G., Zhu Y., Hemphill L., RA Shang Y., Youmans B., Ayvaz T., Ross M., Santibanez J., Aqrawi P., RA Gross S., Joshi V., Fowler G., Nazareth L., Reid J., Worley K., RA Petrosino J., Highlander S., Gibbs R.; RL Submitted (DEC-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EFV95373.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AEQP01000003; EFV95373.1; -; Genomic_DNA. DR STRING; 887898.HMPREF0551_0861; -. DR EnsemblBacteria; EFV95373; EFV95373; HMPREF0551_0861. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000011021; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000011021}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000011021}. FT DOMAIN 185 351 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 393 AA; 43524 MW; 58C2B3EAE04C4043 CRC64; MATQGERLEA HDLDELDALA RSAGLQPVLR EVLRRNRPDP ALYLGSGAAE RIADQLRTER VGLVLFDHAI SAIQQRNLER LWKVQVADRT ELIIEIFSQR ARSTEGKLQV ELARMQHQAS RLVRMWSHLE RQRGGIGVRG GPGETQLELD RRMLDDKIRR LRTRLQKVDR QRRTRRRARQ RGEALRVSLI GYTNAGKSTL FNRLTRAGAL AADQLFATLD PLTRRLGLGN GLEVVLSDTV GFIRNLPHGL VAAFRATLEE TAEADLLLHV VDAGSPDRER QIEAVNQVIA EIGAGEVEQL MIYNKIDLTG NVPEVRLDPY GRISGLALSA GTGAGVDALR DLLRERAQAR AQAVDETAWY GDEAFTAEAP DPSDVSDEAD PSADEDGPDH PSS // ID E8JFZ6_9ACTO Unreviewed; 500 AA. AC E8JFZ6; DT 05-APR-2011, integrated into UniProtKB/TrEMBL. DT 05-APR-2011, sequence version 1. DT 07-JUN-2017, entry version 36. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:EFW10568.1}; GN ORFNames=HMPREF9005_0443 {ECO:0000313|EMBL:EFW10568.1}; OS Actinomyces sp. oral taxon 178 str. F0338. OC Bacteria; Actinobacteria; Actinomycetales; Actinomycetaceae; OC Actinomyces. OX NCBI_TaxID=888051 {ECO:0000313|EMBL:EFW10568.1, ECO:0000313|Proteomes:UP000003389}; RN [1] {ECO:0000313|EMBL:EFW10568.1, ECO:0000313|Proteomes:UP000003389} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=F0338 {ECO:0000313|EMBL:EFW10568.1, RC ECO:0000313|Proteomes:UP000003389}; RA Muzny D., Qin X., Deng J., Jiang H., Liu Y., Qu J., Song X.-Z., RA Zhang L., Thornton R., Coyle M., Francisco L., Jackson L., Javaid M., RA Korchina V., Kovar C., Mata R., Mathew T., Ngo R., Nguyen L., RA Nguyen N., Okwuonu G., Ongeri F., Pham C., Simmons D., RA Wilczek-Boney K., Hale W., Jakkamsetti A., Pham P., Ruth R., RA San Lucas F., Warren J., Zhang J., Zhao Z., Zhou C., Zhu D., Lee S., RA Bess C., Blankenburg K., Forbes L., Fu Q., Gubbala S., Hirani K., RA Jayaseelan J.C., Lara F., Munidasa M., Palculict T., Patil S., RA Pu L.-L., Saada N., Tang L., Weissenberger G., Zhu Y., Hemphill L., RA Shang Y., Youmans B., Ayvaz T., Ross M., Santibanez J., Aqrawi P., RA Gross S., Joshi V., Fowler G., Nazareth L., Reid J., Worley K., RA Petrosino J., Highlander S., Gibbs R.; RL Submitted (NOV-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EFW10568.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AEUH01000054; EFW10568.1; -; Genomic_DNA. DR RefSeq; WP_009743082.1; NZ_GL636934.1. DR EnsemblBacteria; EFW10568; EFW10568; HMPREF9005_0443. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000003389; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000003389}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000003389}. FT DOMAIN 276 442 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 500 AA; 53695 MW; 5A79240F8AF28B73 CRC64; MTPTQSGDDE ARDARIDEVV ARILSRQAQA LSSTAGQDRS GDAGAMEREA RAATRRVDTS ASDRADISEV EYRQVRLERV VLVGLRTTQS EEEAENSLRE LAALAETAGS RVMDGVIQRR SLPDPATYLG SGKAKELADI VRAHEADTVI VDEELAPSQR RGLEDVVDAK VVDRTALILD IFAQHAKSRE GKAQVELAQL EYLLPRLRGW GESMSRQAGG RVAGGAGIGS RGPGETKIEL DRRRIRARMA KLKAEIARME PARRTQRGAR RRGGVPSVAI AGYTNAGKST LLNRLTDAGV LVEDALFATL DPTVRRARTA DGREYTLTDT VGFVRNLPTQ LVEAFRSTLE EVGAADVLLH VVDAAHPDPV SQVEAVRAVL SGIEGADRVP ELIALNKADL ATPEQLAVLR TAFPGSVALS AKTGYGVGTL RAALEDLLPR PSVLIDAVIP YSAGSLVHRV HEEGEVEREE YAAEGTRLVA RVDEALAAAV RAATAPRADE // ID E8LCX1_9FIRM Unreviewed; 610 AA. AC E8LCX1; DT 05-APR-2011, integrated into UniProtKB/TrEMBL. DT 05-APR-2011, sequence version 1. DT 07-JUN-2017, entry version 38. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:EFY05281.1}; GN ORFNames=HMPREF9443_00694 {ECO:0000313|EMBL:EFY05281.1}; OS Phascolarctobacterium succinatutens YIT 12067. OC Bacteria; Firmicutes; Negativicutes; Acidaminococcales; OC Acidaminococcaceae; Phascolarctobacterium. OX NCBI_TaxID=626939 {ECO:0000313|EMBL:EFY05281.1, ECO:0000313|Proteomes:UP000004923}; RN [1] {ECO:0000313|EMBL:EFY05281.1, ECO:0000313|Proteomes:UP000004923} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=YIT 12067 {ECO:0000313|EMBL:EFY05281.1, RC ECO:0000313|Proteomes:UP000004923}; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Hou S., Chen J., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Zhang X., Suruliraj S., Warren W., Chinwalla A., RA Mardis E.R., Wilson R.K.; RL Submitted (JAN-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EFY05281.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AEVN01000028; EFY05281.1; -; Genomic_DNA. DR RefSeq; WP_009145078.1; NZ_GL830870.1. DR ProteinModelPortal; E8LCX1; -. DR STRING; 626939.HMPREF9443_00694; -. DR EnsemblBacteria; EFY05281; EFY05281; HMPREF9443_00694. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000004923; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000004923}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000004923}. FT DOMAIN 386 552 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 610 AA; 66784 MW; C0C59C53849EDAD1 CRC64; MANEIYGNLK GIRNSVIEEL KTFYDIRLEG GQLLTSELAL RMADVTDFIN REVSVYVARN GQVLAVSVGN DQSVELPPVE GRRGASRLSG VRCVHTHPNG NPLLSGVDIS ALKNNRFDAM IAVGVTSPDI SQSQMSFGMI TGIDDNEQYQ VECYGPLTLQ EAEGVFFPNL AAMVERILDK QTGSASLAQG TERAIIVGME YGAPNSSGWT AEDSLEELKQ LADTAGAEVV ARFLQKRPKP DPAFFIGRGK VQELALYVQQ ENVDLCIFDD ELSPAQQRNI EQSMGVRVLD RTALILDIFA QRAHTNEGKL QVELAQLQYT LPRIMGKGLA LSRLGGGIGT RGPGETKLEV DRRRIRDRIA YIKECIGKVK SVRTLHRAGR AKASVPTVSL VGYTNAGKST LLNTLTNSDI YAQDQLFATL DPTTRQLDLP NKQQAILTDT VGFIQRLPHQ LVAAFQSTLE EVVQSDVLLH VIDVSHELYK EQAAAVYQVL DELGAKDKTI ITVYNKIDKL PPDSGLAERL SKEENSICIS AKARYNLDGL LALIAENLKL KAVEESFLVP YSDSAAVGRL HDAGTVLEQE YLAEGTLLKV LLDAEQVQQF AKYLAADAKA // ID E8LK05_SUCHY Unreviewed; 454 AA. AC E8LK05; DT 05-APR-2011, integrated into UniProtKB/TrEMBL. DT 05-APR-2011, sequence version 1. DT 30-AUG-2017, entry version 38. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:EFY07121.1}; GN ORFNames=HMPREF9444_01042 {ECO:0000313|EMBL:EFY07121.1}; OS Succinatimonas hippei (strain DSM 22608 / JCM 16073 / KCTC 15190 / YIT OS 12066). OC Bacteria; Proteobacteria; Gammaproteobacteria; Aeromonadales; OC Succinivibrionaceae; Succinatimonas. OX NCBI_TaxID=762983 {ECO:0000313|EMBL:EFY07121.1, ECO:0000313|Proteomes:UP000018458}; RN [1] {ECO:0000313|EMBL:EFY07121.1, ECO:0000313|Proteomes:UP000018458} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 22608 / JCM 16073 / KCTC 15190 / YIT 12066 RC {ECO:0000313|Proteomes:UP000018458}; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Hou S., Chen J., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Zhang X., Suruliraj S., Warren W., Chinwalla A., RA Mardis E.R., Wilson R.K.; RL Submitted (JAN-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EFY07121.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AEVO01000051; EFY07121.1; -; Genomic_DNA. DR ProteinModelPortal; E8LK05; -. DR STRING; 762983.HMPREF9444_01042; -. DR EnsemblBacteria; EFY07121; EFY07121; HMPREF9444_01042. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000018458; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000018458}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000018458}. FT DOMAIN 200 366 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 454 AA; 50126 MW; E84D4B9F3834C0CD CRC64; MSDQKIEALG PTLLVHVELP QAESQEDLDE LYRLAESAGG NVRDAIVCKR DVPDAKTFIG KGKVVEVADA VRAHDVSCVI FNSPLTPAQE RNLEKEFSVR VMDRIALILQ IFAQRARTYE GKLQVELAML RYEQARLVRG WTHLERQKGG FGLRGGPGET QIELDRRALR ERIAAIKADL DVVASRREQN RRQRVKNAVP VVSFVGYTNA GKSTLFNRLT KSAVYEADQL FATLDPTLRT VSLDVVGKAV FADTVGFIRH LPHDLIAAFK STLEETVKAD LLLHIIDAAD KRVEENIKAV NAVLKQIGAD EVPTLLVFNK ADLLDTPYDK VVRDETGKPV RVNVSAKTGS GLSDLLSCVS ELLSSNLCTF AVKIYPQDGK LRSMLYESKA VSKESYADDG SLILELKILA ADAARIDKKT AGRLRASCVD GKAPWITTEA KEDLDLDLVF DDID // ID E8N5K8_ANATU Unreviewed; 451 AA. AC E8N5K8; DT 05-APR-2011, integrated into UniProtKB/TrEMBL. DT 05-APR-2011, sequence version 1. DT 07-JUN-2017, entry version 44. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:BAJ63722.1}; GN OrderedLocusNames=ANT_16960 {ECO:0000313|EMBL:BAJ63722.1}; OS Anaerolinea thermophila (strain DSM 14523 / JCM 11388 / NBRC 100420 / OS UNI-1). OC Bacteria; Chloroflexi; Anaerolineae; Anaerolineales; Anaerolineaceae; OC Anaerolinea. OX NCBI_TaxID=926569 {ECO:0000313|EMBL:BAJ63722.1, ECO:0000313|Proteomes:UP000008922}; RN [1] {ECO:0000313|EMBL:BAJ63722.1, ECO:0000313|Proteomes:UP000008922} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 14523 / JCM 11388 / NBRC 100420 / UNI-1 RC {ECO:0000313|Proteomes:UP000008922}; RA Narita-Yamada S., Kishi E., Watanabe Y., Takasaki K., Ankai A., RA Oguchi A., Fukui S., Takahashi M., Yashiro I., Hosoyama A., RA Sekiguchi Y., Hanada S., Fujita N.; RT "Whole genome sequence of Anaerolinea thermophila UNI-1."; RL Submitted (DEC-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AP012029; BAJ63722.1; -; Genomic_DNA. DR RefSeq; WP_013560101.1; NC_014960.1. DR ProteinModelPortal; E8N5K8; -. DR STRING; 926569.ANT_16960; -. DR EnsemblBacteria; BAJ63722; BAJ63722; ANT_16960. DR KEGG; atm:ANT_16960; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000008922; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000008922}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000008922}. FT DOMAIN 219 386 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 178 212 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 451 AA; 50247 MW; 2C02C3B42D32D5F2 CRC64; MAKKVPEPTV PPRERAFLVG VELRNEPSLL PLEDSLEELA LLAQTAGLEV VGQTTQKLDA PHPDTYIGSG KIEEIKILVE ETLAQVVLFD NELSPRHLRE LEERLGPHVR ILDRTALILD IFAQHAHTRE GILQVELAQY EYRLPRLTRA WTHLARQAGG GGGRTGSMGG VGLRGPGETQ LEVDRREIRK RIATLKAELE KVRAHRMRYR AQRQRSQIPV VALVGYTNAG KSTLLNRLAN AEVYVADQLF ATLDPTTRRV ELPGGHLALF TDTVGFIQKL PTQLVAAFRA TLEEIAEADL LLHVVDITHP NAFEQAQAVH ATLKEIQADH IPVITLLNKI DRLPDPKAAE EAIAYFSGSV LAISALKGMG INEMLTLVNQ ELFETYQPVK VRIPYQEGNL ISLFHDQGQV KRIEHTRGGV LIDGNLPGRL LARFQPFLYT DDKLSQKEET T // ID E8N9L4_MICTS Unreviewed; 505 AA. AC E8N9L4; DT 05-APR-2011, integrated into UniProtKB/TrEMBL. DT 05-APR-2011, sequence version 1. DT 05-JUL-2017, entry version 43. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:BAJ73261.1}; GN OrderedLocusNames=MTES_0297 {ECO:0000313|EMBL:BAJ73261.1}; OS Microbacterium testaceum (strain StLB037). OC Bacteria; Actinobacteria; Micrococcales; Microbacteriaceae; OC Microbacterium. OX NCBI_TaxID=979556 {ECO:0000313|EMBL:BAJ73261.1, ECO:0000313|Proteomes:UP000008975}; RN [1] {ECO:0000313|EMBL:BAJ73261.1, ECO:0000313|Proteomes:UP000008975} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=StLB037 {ECO:0000313|EMBL:BAJ73261.1, RC ECO:0000313|Proteomes:UP000008975}; RX PubMed=21357489; DOI=10.1128/JB.00180-11; RA Morohoshi T., Wang W.-Z., Someya N., Ikeda T.; RT "Genome sequence of Microbacterium testaceum StLB037, an N- RT acylhomoserine lactone-degrading bacterium isolated from potato RT leaves."; RL J. Bacteriol. 193:2072-2073(2011). RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=StLB037; RA Morohoshi T., Wang W.Z., Someya N., Ikeda T.; RT "Genome sequence of Microbacterium testaceum StLB037."; RL Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AP012052; BAJ73261.1; -; Genomic_DNA. DR RefSeq; WP_013583388.1; NC_015125.1. DR STRING; 979556.MTES_0297; -. DR EnsemblBacteria; BAJ73261; BAJ73261; MTES_0297. DR GeneID; 32512627; -. DR KEGG; mts:MTES_0297; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000008975; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000008975}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000008975}. FT DOMAIN 287 452 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 505 AA; 54605 MW; C936651319EE612A CRC64; MTEQTTPPNT DAAPVDPVDR VLSRAEAHRG VRVFGAAQAL QDAATAYGGS TDGDQWDREE RAALRRVPGL STELEDVTEV EYRQLRLENV VLVGVHPQGY QSDAENSLRE LAALAETAGA VVLDGVLQRR PHPDPATYVG RGKAEELRDI VAAVGADTVI ADTELAPSQR RALEDVVKVK VIDRTTVILD IFSQHAKSRE GKAQVELAQL EYLLPRLRGW GDSMSRQAGG QVGAGGAGMG SRGPGETKIE LDRRRIRTKM ALLRKQLRDF APARAAKRAE RKRHTIPSVA IAGYTNAGKS SLLNRLTSAG VLVENALFAT LDATVRRSET TDGRVYTLTD TVGFVRNLPH QLVEAFRSTL EEVGDADVIL HVVDASHPDP AAQLATVRDV MGDVEADFGH EIVVFNKADL VSDDDRLVLR GLAPHAHFVS SRTGEGIDEL RAAIEEALPR PAVEVQAVVP YDRGDLVSAV HESGLILAQE HRETGTFLHA HVGARLAAEL EPYAA // ID E8R4P2_ISOPI Unreviewed; 468 AA. AC E8R4P2; DT 05-APR-2011, integrated into UniProtKB/TrEMBL. DT 05-APR-2011, sequence version 1. DT 07-JUN-2017, entry version 50. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Isop_0036 {ECO:0000313|EMBL:ADV60633.1}; OS Isosphaera pallida (strain ATCC 43644 / DSM 9630 / IS1B). OC Bacteria; Planctomycetes; Planctomycetia; Planctomycetales; OC Isosphaeraceae; Isosphaera. OX NCBI_TaxID=575540 {ECO:0000313|EMBL:ADV60633.1, ECO:0000313|Proteomes:UP000008631}; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 43644; RG US DOE Joint Genome Institute (JGI-PGF); RA Lucas S., Copeland A., Lapidus A., Bruce D., Goodwin L., Pitluck S., RA Kyrpides N., Mavromatis K., Pagani I., Ivanova N., Saunders E., RA Brettin T., Detter J.C., Han C., Tapia R., Land M., Hauser L., RA Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Eisen J.A.; RT "The complete sequence of chromosome of Isophaera pallida ATCC RT 43644."; RL Submitted (NOV-2010) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:ADV60633.1, ECO:0000313|Proteomes:UP000008631} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43644 / DSM 9630 / IS1B RC {ECO:0000313|Proteomes:UP000008631}; RX PubMed=21475588; DOI=10.4056/sigs.1533840; RG US DOE Joint Genome Institute (JGI-PGF); RA Goker M., Cleland D., Saunders E., Lapidus A., Nolan M., Lucas S., RA Hammon N., Deshpande S., Cheng J.F., Tapia R., Han C., Goodwin L., RA Pitluck S., Liolios K., Pagani I., Ivanova N., Mavromatis K., Pati A., RA Chen A., Palaniappan K., Land M., Hauser L., Chang Y.J., RA Jeffries C.D., Detter J.C., Beck B., Woyke T., Bristow J., Eisen J.A., RA Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.; RT "Complete genome sequence of Isosphaera pallida type strain (IS1B)."; RL Stand. Genomic Sci. 4:63-71(2011). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002353; ADV60633.1; -; Genomic_DNA. DR RefSeq; WP_013562922.1; NC_014962.1. DR ProteinModelPortal; E8R4P2; -. DR STRING; 575540.Isop_0036; -. DR EnsemblBacteria; ADV60633; ADV60633; Isop_0036. DR KEGG; ipa:Isop_0036; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000008631; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000008631}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Hydrolase {ECO:0000313|EMBL:ADV60633.1}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000008631}. FT DOMAIN 203 369 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 468 AA; 51868 MW; 309F92FAE51F3206 CRC64; MAELKSTQPR NRRERAILVG VLLPDGQYNP DDPLDEIRGL AETAGLVVLA GLLQNRREVD PATYIGSGKV AELKELVEAH EADLVLFDND LGPAQTRNLE QQLKVKVIDR TEVILDIFAT RARTYEARLQ VELAQLEYAM PRLKRMWTHL SRYKGGVGVR GPGEKQLEED RRLVAKRIQD LKAKLAVVQA RKEREVAART EVPTVSLVGY TNAGKSTLMN ALTGAGVYTA DQLFATLDTR TRQWHFKGGG HVLLSDTVGF IRNLPHSLVA SFKATLEEAR QADVLLHVVD ASSHEAERQI EAVEAVLHEL ALSDVPTLLV LNKCDRVRDQ DSLAILRARH PEVVEISAAT GTGLAELEAA VRAKLNETAL DVEIHTHAGD GKVLAYLAQH AHIHSQDYSN TDDLHVRLLC RLPRKCLGFL SEQGVNLHIT TLVDQTPMRE DQKEMISKRR DLSNSNPLGL SLTWTATA // ID E8RIR6_DESPD Unreviewed; 561 AA. AC E8RIR6; DT 05-APR-2011, integrated into UniProtKB/TrEMBL. DT 05-APR-2011, sequence version 1. DT 07-JUN-2017, entry version 48. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Despr_1316 {ECO:0000313|EMBL:ADW17480.1}; OS Desulfobulbus propionicus (strain ATCC 33891 / DSM 2032 / 1pr3). OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfobacterales; OC Desulfobulbaceae; Desulfobulbus. OX NCBI_TaxID=577650 {ECO:0000313|EMBL:ADW17480.1, ECO:0000313|Proteomes:UP000006365}; RN [1] {ECO:0000313|EMBL:ADW17480.1, ECO:0000313|Proteomes:UP000006365} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33891 / DSM 2032 / 1pr3 RC {ECO:0000313|Proteomes:UP000006365}; RX PubMed=21475592; RA Pagani I., Lapidus A., Nolan M., Lucas S., Hammon N., Deshpande S., RA Cheng J.F., Chertkov O., Davenport K., Tapia R., Han C., Goodwin L., RA Pitluck S., Liolios K., Mavromatis K., Ivanova N., Mikhailova N., RA Pati A., Chen A., Palaniappan K., Land M., Hauser L., Chang Y.J., RA Jeffries C.D., Detter J.C., Brambilla E., Kannan K.P., Djao O.D., RA Rohde M., Pukall R., Spring S., Goker M., Sikorski J., Woyke T., RA Bristow J., Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., RA Klenk H.P.; RT "Complete genome sequence of Desulfobulbus propionicus type strain RT (1pr3)."; RL Stand. Genomic Sci. 4:100-110(2011). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002364; ADW17480.1; -; Genomic_DNA. DR RefSeq; WP_015724022.1; NC_014972.1. DR ProteinModelPortal; E8RIR6; -. DR STRING; 577650.Despr_1316; -. DR EnsemblBacteria; ADW17480; ADW17480; Despr_1316. DR KEGG; dpr:Despr_1316; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; EREVIIT; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000006365; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000006365}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Hydrolase {ECO:0000313|EMBL:ADW17480.1}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000006365}. FT DOMAIN 378 561 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 561 AA; 62138 MW; 226868017761A744 CRC64; MATVTGNTNG LKPKQLRDLE RLAQKKVAPD EIVGRETARA LAAISTELNR RVGLLIHRSG QIETVIVGDY DRITIPALAH VGASGGRLRG LRCVHTVLGG AAAINEEDIM DLACLRLDLM ATLTLRDGLP DLLHPVHLIP RQVDGRDWTT LSPVHPANQQ QSCIELIEAL EDEFVRERPV REVDRGKDRA ILVSVTTGSR GEAEDSMAEL VELARSAGVE VLAEVIQRRK HIHPRFILGR GKLVEIVLMS LRLGANLLLF DQELSPSQIR SVTDHTDLRV IDRTQLILDI FASRARSREG KLQIEMAQLK YMLPKLTTRD DALSRLTGGI GARGPGETRL EIDKRRINDR ITRLGKELKA VGDQRFHRRN RRRKRDVPVI SLVGYTNAGK STLLNTLTKS EIQAEDLLFA TLDPTSRRLR FPEDMEVIIT DTVGFIRNLP ADLLKAFEST LEELFEADLL LHVIDVSNPA WRQQVAVVEG LLAELELDGI PCLKVFNKID RLAPEDQAEL ADSAEGVGIS ALDAHTLPPL LIRAQEILRT VAGKAAVSTA NGKRREEEGE G // ID E8RSN3_ASTEC Unreviewed; 448 AA. AC E8RSN3; DT 05-APR-2011, integrated into UniProtKB/TrEMBL. DT 05-APR-2011, sequence version 1. DT 07-JUN-2017, entry version 44. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Astex_2867 {ECO:0000313|EMBL:ADU14504.1}; OS Asticcacaulis excentricus (strain ATCC 15261 / DSM 4724 / VKM B-1370 / OS CB 48). OC Bacteria; Proteobacteria; Alphaproteobacteria; Caulobacterales; OC Caulobacteraceae; Asticcacaulis. OX NCBI_TaxID=573065 {ECO:0000313|EMBL:ADU14504.1, ECO:0000313|Proteomes:UP000001492}; RN [1] {ECO:0000313|Proteomes:UP000001492} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 15261 / DSM 4724 / VKM B-1370 / CB 48 RC {ECO:0000313|Proteomes:UP000001492}; RG US DOE Joint Genome Institute; RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L., RA Pitluck S., Teshima H., Davenport K., Detter J.C., Han C., Tapia R., RA Land M., Hauser L., Jeffries C., Kyrpides N., Ivanova N., RA Ovchinnikova G., Brun Y.V., Woyke T.; RT "Complete sequence of chromosome 2 of Asticcacaulis excentricus CB RT 48."; RL Submitted (DEC-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002396; ADU14504.1; -; Genomic_DNA. DR RefSeq; WP_013480328.1; NC_014817.1. DR ProteinModelPortal; E8RSN3; -. DR STRING; 573065.Astex_2867; -. DR EnsemblBacteria; ADU14504; ADU14504; Astex_2867. DR KEGG; aex:Astex_2867; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000001492; Chromosome 2. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000001492}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000001492}. FT DOMAIN 219 392 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 448 AA; 50117 MW; B28BA2A82A6FF889 CRC64; MTTKFVNRTP ETQRAVIIDP DMAAPHAPSS PRQPQGVPAT RRYDESRLDE AAGLAIALDL DIVAADTARV RKPNPATLFG SGKVEEIVTL CEEVEADLVI VNTTLTPIQQ RNLEKAWERK VIDRTGLILE IFGRRARTRE GKLQVELARL EYERSRLVRT WTHLERQRAT GTTGGPGETQ IELDRRMIAD KIKLLKGELD DVRRTRSLHR SARKKVPYPI VALVGYTNAG KSTLFNHLTR AEVLAKDMLF ATLDTTLRTL KLPGGRAAII SDTVGFISDL PHELVAAFRA TLEEVLEADL ILHVRDMSNP ESDAQAQDVM QVLTHIHPDL DKSRLIEVWN KIDLLDEEAR DILYSRAVLD RAMNKPIMVS AITGEGIEKL LSDIALKVDE AGTEIDVELA PQDGQLLAFL YTQGRVLDRF DDETGHIHLK VKLSDQALGR YEQMTGRA // ID E8T432_THEA1 Unreviewed; 366 AA. AC E8T432; DT 05-APR-2011, integrated into UniProtKB/TrEMBL. DT 05-APR-2011, sequence version 1. DT 07-JUN-2017, entry version 54. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Theam_1398 {ECO:0000313|EMBL:ADU97361.1}; OS Thermovibrio ammonificans (strain DSM 15698 / JCM 12110 / HB-1). OC Bacteria; Aquificae; Desulfurobacteriales; Desulfurobacteriaceae; OC Thermovibrio. OX NCBI_TaxID=648996 {ECO:0000313|EMBL:ADU97361.1, ECO:0000313|Proteomes:UP000006362}; RN [1] {ECO:0000313|EMBL:ADU97361.1, ECO:0000313|Proteomes:UP000006362} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 15698 / JCM 12110 / HB-1 RC {ECO:0000313|Proteomes:UP000006362}; RG US DOE Joint Genome Institute; RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L., RA Pitluck S., Davenport K., Detter J.C., Han C., Tapia R., Land M., RA Hauser L., Kyrpides N., Ivanova N., Ovchinnikova G., Vetriani C., RA Woyke T.; RT "Complete sequence of chromosome of Thermovibrio ammonificans HB-1."; RL Submitted (JAN-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002444; ADU97361.1; -; Genomic_DNA. DR RefSeq; WP_013538147.1; NC_014926.1. DR ProteinModelPortal; E8T432; -. DR STRING; 648996.Theam_1398; -. DR EnsemblBacteria; ADU97361; ADU97361; Theam_1398. DR KEGG; tam:Theam_1398; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000006362; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000006362}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000006362}. FT DOMAIN 189 363 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 366 AA; 41428 MW; A879DA971AE7AA26 CRC64; MELEKERVAL IAVKRPKEEV DLEELKGLVE ALGGEVVQEV VQKRRSFSPS TYIGKGKLKE VDTERATMIV AYHPLTYSQK RNIEELTGLK VSDRTEVILE IFARRARTKE AKLQVELAKS YYQLSHIRGM GKQLSRLGGG VGTRGPGETK TEVEARAIRR RIHKLRKELE EVLSRQELQR YNRKRRGQKT VAVVGYTNVG KSTLVRALTR KEVFVKDMPF ATLDVRTGSL YLNGETVLIS DTVGFIKNLP HELVASFRAT LSEVKEADLL LVVFDASSET AEEELNSVKE VLKRLRSWDK PKIFVANKTD KLVSSPQELE ELKGELLLKI PEENPKLVLI SAVKGWGLEE LKRAIEEALK SSPQER // ID E8TNF0_MESCW Unreviewed; 463 AA. AC E8TNF0; DT 05-APR-2011, integrated into UniProtKB/TrEMBL. DT 05-APR-2011, sequence version 1. DT 07-JUN-2017, entry version 51. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Mesci_3713 {ECO:0000313|EMBL:ADV12832.1}; OS Mesorhizobium ciceri biovar biserrulae (strain HAMBI 2942 / LMG 23838 OS / WSM1271). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Phyllobacteriaceae; Mesorhizobium. OX NCBI_TaxID=765698 {ECO:0000313|EMBL:ADV12832.1, ECO:0000313|Proteomes:UP000007471}; RN [1] {ECO:0000313|Proteomes:UP000007471} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=HAMBI 2942 / LMG 23838 / WSM1271 RC {ECO:0000313|Proteomes:UP000007471}; RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L., RA Pitluck S., Teshima H., Detter J.C., Han C., Tapia R., Land M., RA Hauser L., Kyrpides N., Ivanova N., Nandasena K., Reeve W.G., RA Howieson J.G., O'Hara G., Tiwari R.P., Woyke T.; RT "Complete sequence of chromosome of Mesorhizobium ciceri bv. RT biserrulae WSM1271."; RL Submitted (JAN-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002447; ADV12832.1; -; Genomic_DNA. DR RefSeq; WP_013531499.1; NC_014923.1. DR RefSeq; YP_004142882.1; NC_014923.1. DR STRING; 765698.Mesci_3713; -. DR EnsemblBacteria; ADV12832; ADV12832; Mesci_3713. DR GeneID; 10119199; -. DR KEGG; mci:Mesci_3713; -. DR PATRIC; fig|765698.3.peg.4218; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000007471; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000007471}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000007471}. FT DOMAIN 231 404 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 190 224 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 463 AA; 51017 MW; ECB64116E589862C CRC64; MAREKDADAT VRGKPAHHPG TEAKGPTRAV VIVPVLTRHQ RNDDETNRPR LMRSADARHD EAVGLARAIN LDLIHTAVVT VNDPRPATLL GSGKVAEFAE IVKEGHAEVV VVDHPLTPVQ QRNLEKELNA KVLDRTGLIL EIFGERARTK EGTLQVELAH LNYQKGRLVR SWTHLERQRG GAGFLGGPGE TQIESDRRQL QEKIIKLKQE LETVRRTRDL HRAKRRKVPF PVVAIVGYTN AGKSTLFNRL TGADVLAQDM LFATLDPTLR RVRLPHGTPI ILSDTVGFIS DLPTHLIAAF RATLEEVVEA DLVLHLRDIS DPDTAAQAED VERILADLGV DAGDAKRVIE VWNKIDRLDE GNRTRLLADG ADANKAPPIA VSAVTGEGID ALKAIIETRM AGELEDLTVT IEPAQFGLVD WLYRNGDVVS RSDNDDGSAT ISLKATQSAR EEIENRLRRK NNG // ID E8UAX9_DEIML Unreviewed; 562 AA. AC E8UAX9; DT 05-APR-2011, integrated into UniProtKB/TrEMBL. DT 05-APR-2011, sequence version 1. DT 07-JUN-2017, entry version 44. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Deima_2585 {ECO:0000313|EMBL:ADV68218.1}; OS Deinococcus maricopensis (strain DSM 21211 / LMG 22137 / NRRL B-23946 OS / LB-34). OC Bacteria; Deinococcus-Thermus; Deinococci; Deinococcales; OC Deinococcaceae; Deinococcus. OX NCBI_TaxID=709986 {ECO:0000313|EMBL:ADV68218.1, ECO:0000313|Proteomes:UP000008635}; RN [1] {ECO:0000313|Proteomes:UP000008635} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 21211 / LMG 22137 / NRRL B-23946 / LB-34 RC {ECO:0000313|Proteomes:UP000008635}; RG US DOE Joint Genome Institute (JGI-PGF); RA Lucas S., Copeland A., Lapidus A., Goodwin L., Pitluck S., RA Kyrpides N., Mavromatis K., Pagani I., Ivanova N., Ovchinnikova G., RA Zeytun A., Detter J.C., Han C., Land M., Hauser L., Markowitz V., RA Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Pukall R., RA Gehrich-Schroeter G., Brambilla E., Klenk H.-P., Eisen J.A.; RT "The complete genome of Deinococcus maricopensis DSM 21211."; RL Submitted (JAN-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002454; ADV68218.1; -; Genomic_DNA. DR STRING; 709986.Deima_2585; -. DR EnsemblBacteria; ADV68218; ADV68218; Deima_2585. DR KEGG; dmr:Deima_2585; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; EREVIIT; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000008635; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000008635}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000008635}. FT DOMAIN 370 539 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 329 356 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 562 AA; 61397 MW; EF62B623B5AF4BF1 CRC64; MKQLSNLYRR RIEPGRVGSP ELARNLSELS HDIRREISVL IDRRGRVVSV SVADAKGAEL PSVRMGETRL AGFHLLHTHP KGGPLSKGDL TTLFMKRLDA VAAVEVKGDG LPGNVHVAHL TPPGSTGEEE DWRVYPPVSP YDIDELDLGA QVSALEEEIA RASTLREAKK DRERAILVQI DSGQFDAEER LAELAELART AGADVAYKEL VYRRHLKPGT LVGAGKLEEL TSKAYHLDAD VLVFGQELNP AQAREIEAAT GLKVIDRTQL ILDIFALHAQ GVESRLQVEL AQLRYMKPRL LGQGTQLSRI GGSAGSAAGG AIGTRGPGET KLELDRRRIN DRIAFLEAQL REVATRRGER RKRRERNAIP VISIVGYTNA GKSTLLNAFT HAAEEPRRVL AENKLFATLR PTSRQGFLPG VGPVVFTDTV GFIRDLPTDL TRAFRSTLEE IGDADVLLHV VDAATPGADT RHDAVTRILQ ELEVADLPTV VALNKADAAD PDLLAREMER LHGLPVSAAR ETGLDALKAR LAEVVADVDA QRVNDEHTRE ANLTAERQAY GL // ID E8UE70_TAYEM Unreviewed; 355 AA. AC E8UE70; DT 05-APR-2011, integrated into UniProtKB/TrEMBL. DT 05-APR-2011, sequence version 1. DT 07-JUN-2017, entry version 51. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=TEQUI_1527 {ECO:0000313|EMBL:ADU92439.1}; OS Taylorella equigenitalis (strain MCE9). OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Alcaligenaceae; Taylorella. OX NCBI_TaxID=937774 {ECO:0000313|EMBL:ADU92439.1, ECO:0000313|Proteomes:UP000007472}; RN [1] {ECO:0000313|EMBL:ADU92439.1, ECO:0000313|Proteomes:UP000007472} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MCE9 {ECO:0000313|EMBL:ADU92439.1, RC ECO:0000313|Proteomes:UP000007472}; RX PubMed=21278298; DOI=10.1128/JB.01547-10; RA Hebert L., Moumen B., Duquesne F., Breuil M.F., Laugier C., RA Batto J.M., Renault P., Petry S.; RT "Genome sequence of Taylorella equigenitalis MCE9, the causative agent RT of contagious equine metritis."; RL J. Bacteriol. 193:1785-1785(2011). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002456; ADU92439.1; -; Genomic_DNA. DR RefSeq; WP_013522674.1; NC_014914.1. DR ProteinModelPortal; E8UE70; -. DR STRING; 937774.TEQUI_1527; -. DR EnsemblBacteria; ADU92439; ADU92439; TEQUI_1527. DR KEGG; teq:TEQUI_1527; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000007472; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000007472}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000007472}. FT DOMAIN 190 355 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 156 183 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 355 AA; 39953 MW; 856B783199E2CF4C CRC64; MKAIVISVNF NDSNFDSHLS EFQMLATGAG AQILETVVAK RDKPDAKFFI GSGKVEEVVG LISIYKPEII LFDQALSPAQ QRNLERAFGL RVIDRVTLIL DIFALRAKSH EGKLQVELAQ LQHLITRLTR LWTHLERQRG GIGMRGPGES QLEMDRRMIG DKVKQLKERL AKLDTQRLTQ RRARARSNML SVSLVGYTNA GKSTLFNALT RAGTYEADQL FATLDTTTRR IWIEDVGQVT ISDTVGFIRD LPTTLIAAFK ATLEETVHAD LLFHVVDAAN PQRDEQILEV NKVLKEINAE DIPTILVYNK IDLLEQGARI ETDEQGKINR IFVSSKTREG MNLLRKAIAE FKSNI // ID E8V842_TERSS Unreviewed; 500 AA. AC E8V842; DT 05-APR-2011, integrated into UniProtKB/TrEMBL. DT 05-APR-2011, sequence version 1. DT 07-JUN-2017, entry version 46. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=AciPR4_3268 {ECO:0000313|EMBL:ADV84024.1}; OS Terriglobus saanensis (strain ATCC BAA-1853 / DSM 23119 / SP1PR4). OC Bacteria; Acidobacteria; Acidobacteriales; Acidobacteriaceae; OC Terriglobus. OX NCBI_TaxID=401053 {ECO:0000313|EMBL:ADV84024.1, ECO:0000313|Proteomes:UP000006844}; RN [1] {ECO:0000313|EMBL:ADV84024.1, ECO:0000313|Proteomes:UP000006844} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC BAA-1853 / DSM 23119 / SP1PR4 RC {ECO:0000313|Proteomes:UP000006844}; RX PubMed=23450133; DOI=10.4056/sigs.3036810; RA Rawat S.R., Mannisto M.K., Starovoytov V., Goodwin L., Nolan M., RA Hauser L., Land M., Davenport K.W., Woyke T., Haggblom M.M.; RT "Complete genome sequence of Terriglobus saanensis type strain RT SP1PR4(T), an Acidobacteria from tundra soil."; RL Stand. Genomic Sci. 7:59-69(2012). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002467; ADV84024.1; -; Genomic_DNA. DR RefSeq; WP_013569755.1; NC_014963.1. DR STRING; 401053.AciPR4_3268; -. DR EnsemblBacteria; ADV84024; ADV84024; AciPR4_3268. DR KEGG; tsa:AciPR4_3268; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000006844; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000006844}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000006844}. FT DOMAIN 250 414 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 500 AA; 54767 MW; 7F51321744E788EE CRC64; MEHAASERSA AVTAVAEKAV LVAVEITGSR RSIPAAALMA RSAASIGNSS DDSIEDDDED FVVPKAKAVE SDVDFESSLA EFEELARSAG ATIAATLVQR RGRPDPATLI GIGKVEELAA MAESTEADVV LFDHDLTPTQ LRNLEKEMPC RVIDRTQLIL DIFARHARTR EGHLQVELAQ LEYQLPRLAG KGKSMSQLGG GIGTRGPGET RIETDRRVIR GRIDHVKAQL EQVRRIRRQQ RQRRESVPVP TVALVGYTNA GKSTLFNALT EAGVLASSRM FATLDPKLRQ FVLPSRRKVL LSDTVGFIRN LPHALVTSFR ATLEEVERAE LLLHVRDASS AILEEQKMQV EAVLAELEVA RTPRIEVLNK IDLLSEPEQQ ALLGRKDVIA ISAAKGVGLD VLIAAIEDRI GGEKAPDPTA EAEFRIPQRE GRTIAALEAG CSIESKRFDG SFVVMLARGP ASLLNRYRRF QEADVAKPDT GPVARPKRRV RRIETATKTR // ID E8X348_GRATM Unreviewed; 467 AA. AC E8X348; DT 05-APR-2011, integrated into UniProtKB/TrEMBL. DT 05-APR-2011, sequence version 1. DT 07-JUN-2017, entry version 43. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=AciX9_2230 {ECO:0000313|EMBL:ADW69272.1}; OS Granulicella tundricola (strain ATCC BAA-1859 / DSM 23138 / MP5ACTX9). OC Bacteria; Acidobacteria; Acidobacteriales; Acidobacteriaceae; OC Granulicella. OX NCBI_TaxID=1198114 {ECO:0000313|Proteomes:UP000000343}; RN [1] {ECO:0000313|Proteomes:UP000000343} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MP5ACTX9 {ECO:0000313|Proteomes:UP000000343}; RG US DOE Joint Genome Institute; RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L., RA Pitluck S., Teshima H., Detter J.C., Han C., Tapia R., Land M., RA Hauser L., Kyrpides N., Ivanova N., Ovchinnikova G., Pagani I., RA Rawat S.R., Mannisto M., Haggblom M.M., Woyke T.; RT "Complete sequence of chromosome of Acidobacterium sp. MP5ACTX9."; RL Submitted (JAN-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002480; ADW69272.1; -; Genomic_DNA. DR ProteinModelPortal; E8X348; -. DR EnsemblBacteria; ADW69272; ADW69272; AciX9_2230. DR KEGG; acm:AciX9_2230; -. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000000343; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000000343}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000000343}. FT DOMAIN 248 410 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 467 AA; 51208 MW; 33EA7AB24E3BC13F CRC64; MEASAAQDAA LLARELRTSQ TQEELAVIVV VEFTGELRKR KQLTAAARSA RTAAAVMAGE DEGELPEGSA LDFEAGRAEF EELARSAGAT IAATLVQRRQ KPDPSSLVGQ GKLDEIVGVV ASTNASLVLF DHDLTPSQLR NIEARLPCHV IDRSQLILDI FARHAKTREG QLQVELAQLE YQLPRLAGRG RAMSQLGGGI GTRGPGETQL ETDRRKINVR IDHIKTQLDG VRRIRQQQRQ RREAVPVPVV ALVGYTNAGK STLFNALTEA GVLESARMFA TLDPKLRQLQ LPSRRKILLS DTVGFIRNLP HTLVTSFRAT LEEVERAEIL LHVQDASSPI VEEQKMQVEK VLAEIMAAKK PVIEVLNKID LVPERGRLPH ERGAVAVSSI QKTGLEELLL AIDKALVADP LVESSFRLPQ SEGAVLASLE GGAVIEEKRF EGNLVYLKVK GPASLLGRYR RFRDRSA // ID E9CME4_9GAMM Unreviewed; 426 AA. AC E9CME4; DT 05-APR-2011, integrated into UniProtKB/TrEMBL. DT 05-APR-2011, sequence version 1. DT 30-AUG-2017, entry version 39. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:EFW12303.1}; GN ORFNames=SSYM_1481 {ECO:0000313|EMBL:EFW12303.1}; OS Serratia symbiotica str. Tucson. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; OC Yersiniaceae; Serratia; Serratia symbiotica. OX NCBI_TaxID=914128 {ECO:0000313|EMBL:EFW12303.1, ECO:0000313|Proteomes:UP000013568}; RN [1] {ECO:0000313|Proteomes:UP000013568} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Tucson {ECO:0000313|Proteomes:UP000013568}; RX PubMed=21266540; RA Burke G.R., Moran N.A.; RT "Massive genomic decay in Serratia symbiotica, a recently evolved RT symbiont of aphids."; RL Genome Biol. Evol. 3:195-208(2011). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GL636112; EFW12303.1; -; Genomic_DNA. DR RefSeq; WP_006708863.1; NZ_GL636112.1. DR EnsemblBacteria; EFW12303; EFW12303; SSYM_1481. DR Proteomes; UP000013568; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000013568}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000013568}. FT DOMAIN 198 365 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 426 AA; 48091 MW; 9C5FAA14B8020799 CRC64; MFDRYKTGEQ AVLVHIYFSQ DKDTEDFSEF ESLVSSAGVE ALQVVTGSRK APHPKYFVGE GKAEEIADVV KASGASVVLF NHSLSPAQER NLERRCECRV IDRTGLILDI FAQRARTHEG KLQVELAQLR HIATRLVRGW THLERQKGGI GLRGPGETQL ETDRRLLRDR ISLILRRLGR VEKQREQGRR VRTRADVPTV SLVGYTNAGK STLFNRMTSP GVYAADQLFA TLDPTLRRIS VADVGDTVLA DTVGFIRHLP HDLVAAFKAT LQETRQASLL LHVIDAVDIR VNENMEAVNT VLAEIDSDEI PTLLVMNKID MLDDFVPRID RNDENLPIRV WLSAASGEGL SLLYQALTER LSGEIAHYEL RLPPQAGRLR SRFYQLQAIE KEWNEKDGSI GVVVRMTSVE WHRLCKQEQS LIHFIV // ID E9G6X2_DAPPU Unreviewed; 439 AA. AC E9G6X2; DT 05-APR-2011, integrated into UniProtKB/TrEMBL. DT 05-APR-2011, sequence version 1. DT 30-AUG-2017, entry version 33. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EFX84360.1}; GN ORFNames=DAPPUDRAFT_46890 {ECO:0000313|EMBL:EFX84360.1}; OS Daphnia pulex (Water flea). OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Crustacea; Branchiopoda; OC Diplostraca; Cladocera; Anomopoda; Daphniidae; Daphnia. OX NCBI_TaxID=6669 {ECO:0000313|Proteomes:UP000000305}; RN [1] {ECO:0000313|EMBL:EFX84360.1, ECO:0000313|Proteomes:UP000000305} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=21292972; DOI=10.1126/science.1197761; RA Colbourne J.K., Pfrender M.E., Gilbert D., Thomas W.K., Tucker A., RA Oakley T.H., Tokishita S., Aerts A., Arnold G.J., Basu M.K., RA Bauer D.J., Caceres C.E., Carmel L., Casola C., Choi J.H., RA Detter J.C., Dong Q., Dusheyko S., Eads B.D., Frohlich T., RA Geiler-Samerotte K.A., Gerlach D., Hatcher P., Jogdeo S., RA Krijgsveld J., Kriventseva E.V., Kultz D., Laforsch C., Lindquist E., RA Lopez J., Manak J.R., Muller J., Pangilinan J., Patwardhan R.P., RA Pitluck S., Pritham E.J., Rechtsteiner A., Rho M., Rogozin I.B., RA Sakarya O., Salamov A., Schaack S., Shapiro H., Shiga Y., RA Skalitzky C., Smith Z., Souvorov A., Sung W., Tang Z., Tsuchiya D., RA Tu H., Vos H., Wang M., Wolf Y.I., Yamagata H., Yamada T., Ye Y., RA Shaw J.R., Andrews J., Crease T.J., Tang H., Lucas S.M., RA Robertson H.M., Bork P., Koonin E.V., Zdobnov E.M., Grigoriev I.V., RA Lynch M., Boore J.L.; RT "The ecoresponsive genome of Daphnia pulex."; RL Science 331:555-561(2011). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GL732534; EFX84360.1; -; Genomic_DNA. DR ProteinModelPortal; E9G6X2; -. DR STRING; 6669.DappuP46890; -. DR EnsemblMetazoa; EFX84360; EFX84360; DAPPUDRAFT_46890. DR KEGG; dpx:DAPPUDRAFT_46890; -. DR eggNOG; KOG0410; Eukaryota. DR eggNOG; COG2262; LUCA. DR InParanoid; E9G6X2; -. DR OMA; MDTVGFM; -. DR PhylomeDB; E9G6X2; -. DR Proteomes; UP000000305; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR GO; GO:0043022; F:ribosome binding; IBA:GO_Central. DR CDD; cd01878; HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000305}; KW Reference proteome {ECO:0000313|Proteomes:UP000000305}. FT DOMAIN 213 375 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 439 AA; 49119 MW; A6A8D247560EC769 CRC64; MHLLPDAGHQ VAILQPFVKW GPKKNLLTTP DLMLEEAKAL VDSLPNWKCV DAIKVPVESL EKKTIFGSGQ FESLQKNIVA NPNISAVFVS TNVLRGIQRR ELMMTFGVPV FDRYSVVLQI FKDRARTREA KLQVAFAEIP YLRSSLVGLQ KGTKNNLPVE NTSRGSKGGS GESFCDSQLH LLDRREIKIK KELEKLAKKR TLLKCERKKR EFPVVAIVGY TNCGKTTLIK SLTGDSKITP RDALFATLDV TVHGMKLPCN LTVLLVDTVG FISNIPVNLI AAFNSTLRDA IDADVLVHLQ DISHPDVENQ VATVKDTLEQ LNIDSTKTVI QVANKIDKMS SEELDDYSDL HISAKDGTGL EEFVDLIQTK VLEITNRRYL RLMVLSGGTE YSWLHKEATV VKYSNTKDPQ YLALDVLVTP STFGKLRFNF PDIRVLNKQ // ID E9I7R8_DAPPU Unreviewed; 106 AA. AC E9I7R8; DT 05-APR-2011, integrated into UniProtKB/TrEMBL. DT 05-APR-2011, sequence version 1. DT 30-AUG-2017, entry version 14. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EFX59963.1}; DE Flags: Fragment; GN ORFNames=DAPPUDRAFT_346145 {ECO:0000313|EMBL:EFX59963.1}; OS Daphnia pulex (Water flea). OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Crustacea; Branchiopoda; OC Diplostraca; Cladocera; Anomopoda; Daphniidae; Daphnia. OX NCBI_TaxID=6669 {ECO:0000313|Proteomes:UP000000305}; RN [1] {ECO:0000313|EMBL:EFX59963.1, ECO:0000313|Proteomes:UP000000305} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=21292972; DOI=10.1126/science.1197761; RA Colbourne J.K., Pfrender M.E., Gilbert D., Thomas W.K., Tucker A., RA Oakley T.H., Tokishita S., Aerts A., Arnold G.J., Basu M.K., RA Bauer D.J., Caceres C.E., Carmel L., Casola C., Choi J.H., RA Detter J.C., Dong Q., Dusheyko S., Eads B.D., Frohlich T., RA Geiler-Samerotte K.A., Gerlach D., Hatcher P., Jogdeo S., RA Krijgsveld J., Kriventseva E.V., Kultz D., Laforsch C., Lindquist E., RA Lopez J., Manak J.R., Muller J., Pangilinan J., Patwardhan R.P., RA Pitluck S., Pritham E.J., Rechtsteiner A., Rho M., Rogozin I.B., RA Sakarya O., Salamov A., Schaack S., Shapiro H., Shiga Y., RA Skalitzky C., Smith Z., Souvorov A., Sung W., Tang Z., Tsuchiya D., RA Tu H., Vos H., Wang M., Wolf Y.I., Yamagata H., Yamada T., Ye Y., RA Shaw J.R., Andrews J., Crease T.J., Tang H., Lucas S.M., RA Robertson H.M., Bork P., Koonin E.V., Zdobnov E.M., Grigoriev I.V., RA Lynch M., Boore J.L.; RT "The ecoresponsive genome of Daphnia pulex."; RL Science 331:555-561(2011). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GL737445; EFX59963.1; -; Genomic_DNA. DR EnsemblMetazoa; EFX59963; EFX59963; DAPPUDRAFT_346145. DR KEGG; dpx:DAPPUDRAFT_346145; -. DR Proteomes; UP000000305; Unassembled WGS sequence. DR InterPro; IPR025121; GTPase_HflX_N. DR Pfam; PF13167; GTP-bdg_N; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000305}; KW Reference proteome {ECO:0000313|Proteomes:UP000000305}. FT DOMAIN 30 75 GTP-bdg_N. {ECO:0000259|Pfam:PF13167}. FT NON_TER 106 106 {ECO:0000313|EMBL:EFX59963.1}. SQ SEQUENCE 106 AA; 11321 MW; 2FE5F1F88B32BB53 CRC64; MGPTGNEPKK SRAILAAVQL PGISDVEHQA SLSELERLCN TLGFVVIGRV TQKRKSIATG TILGEGKLKE LAAWTGGTGV VQGFRKAGSE RDEDDEDELS PSDRNE // ID E9IIY3_SOLIN Unreviewed; 483 AA. AC E9IIY3; DT 05-APR-2011, integrated into UniProtKB/TrEMBL. DT 05-APR-2011, sequence version 1. DT 30-AUG-2017, entry version 28. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EFZ19478.1}; DE Flags: Fragment; GN ORFNames=SINV_09654 {ECO:0000313|EMBL:EFZ19478.1}; OS Solenopsis invicta (Red imported fire ant) (Solenopsis wagneri). OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; OC Pterygota; Neoptera; Holometabola; Hymenoptera; Apocrita; Aculeata; OC Vespoidea; Formicidae; Myrmicinae; Solenopsis. OX NCBI_TaxID=13686 {ECO:0000313|Proteomes:UP000006539}; RN [1] {ECO:0000313|EMBL:EFZ19478.1, ECO:0000313|Proteomes:UP000006539} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=21282665; DOI=10.1073/pnas.1009690108; RA Wurm Y., Wang J., Riba-Grognuz O., Corona M., Nygaard S., Hunt B.G., RA Ingram K.K., Falquet L., Nipitwattanaphon M., Gotzek D., RA Dijkstra M.B., Oettler J., Comtesse F., Shih C.J., Wu W.J., Yang C.C., RA Thomas J., Beaudoing E., Pradervand S., Flegel V., Cook E.D., RA Fabbretti R., Stockinger H., Long L., Farmerie W.G., Oakey J., RA Boomsma J.J., Pamilo P., Yi S.V., Heinze J., Goodisman M.A., RA Farinelli L., Harshman K., Hulo N., Cerutti L., Xenarios I., RA Shoemaker D., Keller L.; RT "The genome of the fire ant Solenopsis invicta."; RL Proc. Natl. Acad. Sci. U.S.A. 108:5679-5684(2011). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GL763562; EFZ19478.1; -; Genomic_DNA. DR RefSeq; XP_011157469.1; XM_011159167.1. DR RefSeq; XP_011157470.1; XM_011159168.1. DR ProteinModelPortal; E9IIY3; -. DR EnsemblMetazoa; XM_011159167.1; XP_011157469.1; LOC105194312. DR EnsemblMetazoa; XM_011159168.1; XP_011157470.1; LOC105194312. DR GeneID; 105194312; -. DR KEGG; soc:105194312; -. DR InParanoid; E9IIY3; -. DR OMA; MDTVGFM; -. DR Proteomes; UP000006539; Unassembled WGS sequence. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR CDD; cd01878; HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 4: Predicted; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000006539}; KW Reference proteome {ECO:0000313|Proteomes:UP000006539}. FT DOMAIN 261 420 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 230 257 {ECO:0000256|SAM:Coils}. FT NON_TER 483 483 {ECO:0000313|EMBL:EFZ19478.1}. SQ SEQUENCE 483 AA; 54514 MW; D6BD0529365ADB30 CRC64; MLCVRKILNI AQRNLQVRIK VDTVYKSSGI LLQNIICRLN HDSEEYISAE DEGQQDAYSE IASRYLSIAV GGHRTFILQP YIKWGRDKKR NTSPELQMAE AVALINTLPN WCVVGTKYAP LLTLQKKQLL GTGAMKDLKT ELHKCQPTAV FISTNLLKFV QIIELEKIFN LPVYDRYSIV IHIFREHAKT AEAKLQVALA EIPYIRKKIL ETSITRSGAV NMTEEAKLLL DGKEKKLKNE LKKLKQHRQT IRSQRKKRGF PTVAVVGYTN AGKTSLIKAL TDDSSLQPKD KLFATLDTTA HQGILPNKLK VLYMDTIGFI QDVPETLIEP FIVTLEDAII ADVIVHIYDV SHPDMKAQYQ HIQETIKPML DDRPIIDVAN KCDLVESDYI PKDAIAVSAK NLTGIDLLRF KIQEVLLATT GLLSIRARVK SGSPAASWLY KMTTVINAES DPNDAQYLIM EVLTTSVDIQ KFKKFLATNN LKQ // ID E9SVD4_RHOHA Unreviewed; 492 AA. AC E9SVD4; DT 31-MAY-2011, integrated into UniProtKB/TrEMBL. DT 31-MAY-2011, sequence version 1. DT 30-AUG-2017, entry version 39. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:EGD26268.1}; GN ORFNames=HMPREF0724_10202 {ECO:0000313|EMBL:EGD26268.1}; OS Rhodococcus hoagii ATCC 33707. OC Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae; OC Rhodococcus. OX NCBI_TaxID=525370 {ECO:0000313|EMBL:EGD26268.1, ECO:0000313|Proteomes:UP000004245}; RN [1] {ECO:0000313|EMBL:EGD26268.1, ECO:0000313|Proteomes:UP000004245} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33707 {ECO:0000313|EMBL:EGD26268.1, RC ECO:0000313|Proteomes:UP000004245}; RA Muzny D., Qin X., Buhay C., Dugan-Rocha S., Ding Y., Chen G., RA Hawes A., Holder M., Jhangiani S., Johnson A., Khan Z., Li Z., Liu W., RA Liu X., Perez L., Shen H., Wang Q., Watt J., Xi L., Xin Y., Zhou J., RA Deng J., Jiang H., Liu Y., Qu J., Song X.-Z., Zhang L., Villasana D., RA Johnson A., Liu J., Liyanage D., Lorensuhewa L., Robinson T., Song A., RA Song B.-B., Dinh H., Thornton R., Coyle M., Francisco L., Jackson L., RA Javaid M., Korchina V., Kovar C., Mata R., Mathew T., Ngo R., RA Nguyen L., Nguyen N., Okwuonu G., Ongeri F., Pham C., Simmons D., RA Wilczek-Boney K., Hale W., Jakkamsetti A., Pham P., Ruth R., RA San Lucas F., Warren J., Zhang J., Zhao Z., Zhou C., Zhu D., Lee S., RA Bess C., Blankenburg K., Forbes L., Fu Q., Gubbala S., Hirani K., RA Jayaseelan J.C., Lara F., Munidasa M., Palculict T., Patil S., RA Pu L.-L., Saada N., Tang L., Weissenberger G., Zhu Y., Hemphill L., RA Shang Y., Youmans B., Ayvaz T., Ross M., Santibanez J., Aqrawi P., RA Gross S., Joshi V., Fowler G., Nazareth L., Reid J., Worley K., RA Petrosino J., Highlander S., Gibbs R.; RL Submitted (JAN-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EGD26268.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADNW02000001; EGD26268.1; -; Genomic_DNA. DR RefSeq; WP_005513698.1; NZ_CM001149.1. DR ProteinModelPortal; E9SVD4; -. DR EnsemblBacteria; EGD26268; EGD26268; HMPREF0724_10202. DR GeneID; 32491446; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000004245; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 2. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000004245}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000004245}. FT DOMAIN 268 437 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 227 254 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 492 AA; 53525 MW; C0A2CCA1046A8E3D CRC64; MTKTHRTHSQ SADDTAEHTA SDEADYFDDH SAPSVGEMQL DERSALRRVQ GLSTELTDVT EVEYRQLRLE RVVLVGVWTS GTAAQADASM AELAALAETA GSEVLEGLVQ RRDKPDAATY IGSGKADELR QVVLATGADT VICDGELTPA QLTALEKVVK VKVIDRTALI LDIFAQHATS REGKAQVALA QMEYMLPRLR GWGESMSRQA GGRAGSNGGV GLRGPGETKI ETDRRRIRER MAKLRREIKG MKAARDTKRS HRLRSEIPSV AIVGYTNAGK SSLLNALTGS GVLVQNALFA TLDPTTRQAS FEDGREYVLT DTVGFVRHLP TQLVEAFRST LEEVTDADLL LHVVDGSDPL PTDQIKAVRE VVTEVIREND TTAPPELIVV NKIDAADPVV LTQLRGLLPG AVFVSARTGE GIDELRTRLG EIVRRPEVEV DVLVPYSRGD LVARIHSDGQ ILDTTHEEDG TRMRVRVPES LASALDEFAG RG // ID F0EYN8_9NEIS Unreviewed; 380 AA. AC F0EYN8; DT 03-MAY-2011, integrated into UniProtKB/TrEMBL. DT 03-MAY-2011, sequence version 1. DT 07-JUN-2017, entry version 37. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:EGC17646.1}; GN ORFNames=HMPREF9098_0972 {ECO:0000313|EMBL:EGC17646.1}; OS Kingella denitrificans ATCC 33394. OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Kingella. OX NCBI_TaxID=888741 {ECO:0000313|EMBL:EGC17646.1, ECO:0000313|Proteomes:UP000004088}; RN [1] {ECO:0000313|EMBL:EGC17646.1, ECO:0000313|Proteomes:UP000004088} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33394 {ECO:0000313|EMBL:EGC17646.1, RC ECO:0000313|Proteomes:UP000004088}; RA Muzny D., Qin X., Deng J., Jiang H., Liu Y., Qu J., Song X.-Z., RA Zhang L., Thornton R., Coyle M., Francisco L., Jackson L., Javaid M., RA Korchina V., Kovar C., Mata R., Mathew T., Ngo R., Nguyen L., RA Nguyen N., Okwuonu G., Ongeri F., Pham C., Simmons D., RA Wilczek-Boney K., Hale W., Jakkamsetti A., Pham P., Ruth R., RA San Lucas F., Warren J., Zhang J., Zhao Z., Zhou C., Zhu D., Lee S., RA Bess C., Blankenburg K., Forbes L., Fu Q., Gubbala S., Hirani K., RA Jayaseelan J.C., Lara F., Munidasa M., Palculict T., Patil S., RA Pu L.-L., Saada N., Tang L., Weissenberger G., Zhu Y., Hemphill L., RA Shang Y., Youmans B., Ayvaz T., Ross M., Santibanez J., Aqrawi P., RA Gross S., Joshi V., Fowler G., Nazareth L., Reid J., Worley K., RA Petrosino J., Highlander S., Gibbs R.; RL Submitted (JAN-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EGC17646.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AEWV01000015; EGC17646.1; -; Genomic_DNA. DR RefSeq; WP_003782350.1; NZ_GL870929.1. DR ProteinModelPortal; F0EYN8; -. DR STRING; 888741.HMPREF9098_0972; -. DR EnsemblBacteria; EGC17646; EGC17646; HMPREF9098_0972. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000004088; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000004088}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000004088}. FT DOMAIN 213 380 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 380 AA; 42130 MW; E713AA10E92C7CCE CRC64; MPRFHTDKTL EHAERIMLVS AHFANSHTGS SETRERAFQA ACTEAAELVR ATGGELVCQH TVKRDKAHPA LLVGTGKAEE LAQLVRQNDI ELVVFNHELS PTQERNLERA LQCRVLDRVG LILAIFAQRA QSQEGRLQVE LAQLTHLAGR LVRGYGHLQS QKGGIGLKGP GETQLETDRR LIQTKITALR RQLAQVKKQR ETRRKARQSG RMKTFAIVGY TNAGKSTLFN RLTKADVLAK DQLFATLDTT ARKLYLAPEH SIILTDTVGF VQNLPHKLVA AFSATLEETA LADVLLHVVD AADPEHERKI EDVNNVLAEI HADHLPQILL YNKIDLLPEA EQNAGCLRNH NGQITAVRLS ATQAQGLDDL RQALLETLTA // ID F0F8U5_9BACT Unreviewed; 415 AA. AC F0F8U5; DT 03-MAY-2011, integrated into UniProtKB/TrEMBL. DT 03-MAY-2011, sequence version 1. DT 07-JUN-2017, entry version 38. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:EGC19472.1}; GN ORFNames=HMPREF9141_2012 {ECO:0000313|EMBL:EGC19472.1}; OS Prevotella multiformis DSM 16608. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Prevotellaceae; OC Prevotella. OX NCBI_TaxID=888743 {ECO:0000313|EMBL:EGC19472.1, ECO:0000313|Proteomes:UP000005697}; RN [1] {ECO:0000313|EMBL:EGC19472.1, ECO:0000313|Proteomes:UP000005697} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 16608 {ECO:0000313|EMBL:EGC19472.1, RC ECO:0000313|Proteomes:UP000005697}; RA Muzny D., Qin X., Deng J., Jiang H., Liu Y., Qu J., Song X.-Z., RA Zhang L., Thornton R., Coyle M., Francisco L., Jackson L., Javaid M., RA Korchina V., Kovar C., Mata R., Mathew T., Ngo R., Nguyen L., RA Nguyen N., Okwuonu G., Ongeri F., Pham C., Simmons D., RA Wilczek-Boney K., Hale W., Jakkamsetti A., Pham P., Ruth R., RA San Lucas F., Warren J., Zhang J., Zhao Z., Zhou C., Zhu D., Lee S., RA Bess C., Blankenburg K., Forbes L., Fu Q., Gubbala S., Hirani K., RA Jayaseelan J.C., Lara F., Munidasa M., Palculict T., Patil S., RA Pu L.-L., Saada N., Tang L., Weissenberger G., Zhu Y., Hemphill L., RA Shang Y., Youmans B., Ayvaz T., Ross M., Santibanez J., Aqrawi P., RA Gross S., Joshi V., Fowler G., Nazareth L., Reid J., Worley K., RA Petrosino J., Highlander S., Gibbs R.; RL Submitted (JAN-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EGC19472.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AEWX01000027; EGC19472.1; -; Genomic_DNA. DR RefSeq; WP_007366765.1; NZ_GL872282.1. DR STRING; 888743.HMPREF9141_2012; -. DR EnsemblBacteria; EGC19472; EGC19472; HMPREF9141_2012. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000005697; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000005697}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000005697}. FT DOMAIN 216 400 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 415 AA; 47501 MW; 72F646A2E0BB3B3E CRC64; MKEFILSDVK AETAVLVGLI TKEQDEAKTK EYLDELEFLA DTAGAVTVKR FTQRLNGPSA VTYVGKGKLE EIKEYIQQKE DEDDPVGMVI FDDELSAKQM RNIEHELGVK ILDRTSLILD IFAMRAQTAN AKTQVELAQY RYMLPRLQRL WTHLERQGGG SGSGGGKGSV GLRGPGETQL EMDRRIILQR MSLLKQRLVE IEKQKSTQRK NRGRLIRVAL VGYTNVGKST TMNLLAKSEV FAENKLFATL DTTVRKVVVE NLPFLLADTV GFIRKLPTDL VDSFKSTLDE VREADLLLHI VDISHPDFEE QIQVVNKTLA DLGCADKPSM IVFNKIDNYH WVEKEEDDLT PATKENITLD ELKRTWMAKE HDNCLFISAK KKENIDEFRE VLYKKVRELH VQKYPYNDFL YNIEE // ID F0H0X0_9FIRM Unreviewed; 415 AA. AC F0H0X0; DT 03-MAY-2011, integrated into UniProtKB/TrEMBL. DT 03-MAY-2011, sequence version 1. DT 07-JUN-2017, entry version 37. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:EGC83867.1}; GN ORFNames=HMPREF9246_1787 {ECO:0000313|EMBL:EGC83867.1}; OS Anaerococcus hydrogenalis ACS-025-V-Sch4. OC Bacteria; Firmicutes; Tissierellia; Tissierellales; Peptoniphilaceae; OC Anaerococcus. OX NCBI_TaxID=879306 {ECO:0000313|EMBL:EGC83867.1, ECO:0000313|Proteomes:UP000005277}; RN [1] {ECO:0000313|EMBL:EGC83867.1, ECO:0000313|Proteomes:UP000005277} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ACS-025-V-Sch4 {ECO:0000313|EMBL:EGC83867.1, RC ECO:0000313|Proteomes:UP000005277}; RA Durkin A.S., Madupu R., Torralba M., Gillis M., Methe B., Sutton G., RA Nelson K.E.; RL Submitted (JAN-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EGC83867.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AEXN01000023; EGC83867.1; -; Genomic_DNA. DR RefSeq; WP_004817283.1; NZ_AEXN01000023.1. DR ProteinModelPortal; F0H0X0; -. DR EnsemblBacteria; EGC83867; EGC83867; HMPREF9246_1787. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000005277; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000005277}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}. FT DOMAIN 188 356 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 156 183 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 415 AA; 47889 MW; 9FE389E7B0A95655 CRC64; MQEVIQVNVF ENKENPNKDF ELESLINTAG GKSVAKISQV VSKVNPAYYI GSGKVSEIED IAKKLNVNTV VFDVELSASQ LRNLEERMKL HVVDWTTLIL DIFAQRANTK EAKLKIKLAQ LKYQLPRINK WFAYLSRQSG GIGTRGPGET MLETDKRAIV RDIRSLEEKL KDLEKTKVVN RKSREKILNI SLLGYTNAGK STILNNMLKI FGKDKFVYSD DLLFATLDTS TRRLDFSNTK VTLTDTVGFI DNLSKELNDS FLTTLEEIKF SDMLLVVIDS SYDIQTQLDT IDKALDDIDI GEKKILYVFN KIDKIEDQMI LLGYKNKEEK IYISARDEAD IIRLKDKIVD VIKNDYVRVM MKIPYEDGKV LDYIMTNYDI DKKDYDENSS ILEFDISKKD YNKYERYIEK NQSEL // ID F0IG44_9FLAO Unreviewed; 401 AA. AC F0IG44; DT 03-MAY-2011, integrated into UniProtKB/TrEMBL. DT 03-MAY-2011, sequence version 1. DT 07-JUN-2017, entry version 37. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:EGD33810.1}; GN ORFNames=HMPREF9071_1527 {ECO:0000313|EMBL:EGD33810.1}; OS Capnocytophaga sp. oral taxon 338 str. F0234. OC Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales; OC Flavobacteriaceae; Capnocytophaga. OX NCBI_TaxID=888059 {ECO:0000313|EMBL:EGD33810.1, ECO:0000313|Proteomes:UP000003023}; RN [1] {ECO:0000313|EMBL:EGD33810.1, ECO:0000313|Proteomes:UP000003023} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=F0234 {ECO:0000313|EMBL:EGD33810.1, RC ECO:0000313|Proteomes:UP000003023}; RA Muzny D., Qin X., Deng J., Jiang H., Liu Y., Qu J., Song X.-Z., RA Zhang L., Thornton R., Coyle M., Francisco L., Jackson L., Javaid M., RA Korchina V., Kovar C., Mata R., Mathew T., Ngo R., Nguyen L., RA Nguyen N., Okwuonu G., Ongeri F., Pham C., Simmons D., RA Wilczek-Boney K., Hale W., Jakkamsetti A., Pham P., Ruth R., RA San Lucas F., Warren J., Zhang J., Zhao Z., Zhou C., Zhu D., Lee S., RA Bess C., Blankenburg K., Forbes L., Fu Q., Gubbala S., Hirani K., RA Jayaseelan J.C., Lara F., Munidasa M., Palculict T., Patil S., RA Pu L.-L., Saada N., Tang L., Weissenberger G., Zhu Y., Hemphill L., RA Shang Y., Youmans B., Ayvaz T., Ross M., Santibanez J., Aqrawi P., RA Gross S., Joshi V., Fowler G., Nazareth L., Reid J., Worley K., RA Petrosino J., Highlander S., Gibbs R.; RL Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EGD33810.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AEXX01000038; EGD33810.1; -; Genomic_DNA. DR RefSeq; WP_009745969.1; NZ_GL872413.1. DR STRING; 888059.HMPREF9071_1527; -. DR EnsemblBacteria; EGD33810; EGD33810; HMPREF9071_1527. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000003023; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000003023}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000003023}. FT DOMAIN 200 385 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 401 AA; 46528 MW; 6D15DF86080C5050 CRC64; MLEKKNLDYE RVVLVGVITT TQNEEKSHEY LDELEFLTYT AGGEVVKRFT QRLETPNPKT FIGTGKMDEL IQFVEENEIG AVIFDDELTP AQQNNIEKIL RIKVLDRTTL ILDIFAQRAQ TSYARTQVEL AQYEYLLPRL TGLWTHLERQ RGGIGMRGPG ETEIETDRRI VRDRIALLKK KLETIDRQMS TQRSNRGALV RVALIGYTNV GKSTLMNLIS KSEVFAENKL FATLDTTVRK VVIGNLPFLL SDTVGFIRKL PTQLIESFKS TLDEVRDADL LLHIVDISHP NFEEHIASVN QILGEIKSIN KPTIMVFNKI DAYTHQTIED DDLMIEKTSR HFSLEEWKQT WMNRMNGDVI FISALNKENI QEFREKVYKK VREIHITRFP YNNFLYPEIE E // ID F0JBH4_DESDE Unreviewed; 557 AA. AC F0JBH4; DT 03-MAY-2011, integrated into UniProtKB/TrEMBL. DT 03-MAY-2011, sequence version 1. DT 07-JUN-2017, entry version 46. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=DND132_1080 {ECO:0000313|EMBL:EGB14293.1}; OS Desulfovibrio desulfuricans ND132. OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfovibrionales; OC Desulfovibrionaceae; Desulfovibrio. OX NCBI_TaxID=641491 {ECO:0000313|EMBL:EGB14293.1, ECO:0000313|Proteomes:UP000007845}; RN [1] {ECO:0000313|EMBL:EGB14293.1, ECO:0000313|Proteomes:UP000007845} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ND132 {ECO:0000313|EMBL:EGB14293.1}; RX PubMed=21357488; DOI=10.1128/JB.00170-11; RA Brown S.D., Gilmour C.C., Kucken A.M., Wall J.D., Elias D.A., RA Brandt C.C., Podar M., Chertkov O., Held B., Bruce D.C., Detter J.C., RA Tapia R., Han C.S., Goodwin L.A., Cheng J.F., Pitluck S., Woyke T., RA Mikhailova N., Ivanova N.N., Han J., Lucas S., Lapidus A.L., RA Land M.L., Hauser L.J., Palumbo A.V.; RT "Genome sequence of the mercury-methylating strain Desulfovibrio RT desulfuricans ND132."; RL J. Bacteriol. 193:2078-2079(2011). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP003220; EGB14293.1; -; Genomic_DNA. DR ProteinModelPortal; F0JBH4; -. DR STRING; 641491.DND132_1080; -. DR EnsemblBacteria; EGB14293; EGB14293; DND132_1080. DR KEGG; ddn:DND132_1080; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR KO; K03665; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000007845; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000007845}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000007845}. FT DOMAIN 389 557 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 348 382 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 557 AA; 62073 MW; E1ABFC5448F9B7B6 CRC64; MAESDLTGST IIAQKPKGNL QGLKPNQIKR LSRLYQRQFP TGAVYTTEQA RELAELSQDT GRQLGLLIDR QGKVEMVLVG DNRSIYIPEL PRARMASGRL RGLRLLHTHL AEESLSQEDL MDMVFLRLDS VAALTVREGF PVAVEAAHLL PPNPDEKSYE LFPPVRWDRF EHDLGAITAA LEDEFGRQAD GQGTGSDEDR ALLVSVDETP RPVQELSLAE LAELADTAGL VAAGTMIQRV RKQNPKFILG KGKLADLEVR ALQANASIII FDQELSPTQM RNLAEITERK ILDRTQLILD IFAQHATSKS GKLQVEMAQL KYTLPRLVGK NRAMSRLMGG IGGRGPGETK LEIDRRRAND RLTRLKDELK QVRRHRSQTR ERRAKAGLPV VSLVGYTNAG KSTLLNTLTS SRVLAEDKLF ATLDPTSRRI RFPEEREVVL TDTVGFIRRL PPDLKEAFRA TLEELDSADL LVLVCDASHP EVEEQVEAVR AILDEMELSS IPSILVLNKW DKLDEEGRAA MRNVYPEGIP AVAVDRPTLE PVVQAILANL PWDKQVS // ID F0LIT5_THEBM Unreviewed; 428 AA. AC F0LIT5; DT 03-MAY-2011, integrated into UniProtKB/TrEMBL. DT 03-MAY-2011, sequence version 1. DT 07-JUN-2017, entry version 50. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=TERMP_01562 {ECO:0000313|EMBL:ADT84537.1}; OS Thermococcus barophilus (strain DSM 11836 / MP). OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae; OC Thermococcus. OX NCBI_TaxID=391623 {ECO:0000313|EMBL:ADT84537.1, ECO:0000313|Proteomes:UP000007478}; RN [1] {ECO:0000313|EMBL:ADT84537.1, ECO:0000313|Proteomes:UP000007478} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 11836 / MP {ECO:0000313|Proteomes:UP000007478}; RX PubMed=21217005; DOI=10.1128/JB.01490-10; RA Vannier P., Marteinsson V.T., Fridjonsson O.H., Oger P., Jebbar M.; RT "Complete genome sequence of the hyperthermophilic, piezophilic, RT heterotrophic, and carboxydotrophic archaeon Thermococcus barophilus RT MP."; RL J. Bacteriol. 193:1481-1482(2011). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002372; ADT84537.1; -; Genomic_DNA. DR RefSeq; WP_013467835.1; NC_014804.1. DR ProteinModelPortal; F0LIT5; -. DR STRING; 391623.TERMP_01562; -. DR EnsemblBacteria; ADT84537; ADT84537; TERMP_01562. DR GeneID; 10041878; -. DR KEGG; tba:TERMP_01562; -. DR PATRIC; fig|391623.17.peg.1562; -. DR eggNOG; arCOG00353; Archaea. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG093Z07D6; -. DR Proteomes; UP000007478; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000007478}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}. FT DOMAIN 186 362 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 428 AA; 49145 MW; DDB51DC764DA39C2 CRC64; MKAIGVIRHS PRKRINKAEF EELLRSAGYE VLAIVEQVRE EHPKYNIGPG KLQEIKKLAE ELKPDKVIFA NQLTPSQAFN IAKELRVDII DKWQLVLEIF EKRAHSKEAK LQVELANLRY ELPLVREAIR RAKMGEQPGF KGMGEYQIHQ YLKHIRYRMG KIRKELERIR EDREVKRKRR EEVGFIIVAL AGYTNAGKST LLNALAREEI PAKDQMFTTL DTTTRRFKVN QKRVLVTDTV GFIDDLPPFI VEAFHSTLEE ITKADIILLV LDVSEPWSEI KRKFLASLKI LRELKALDKP IIVVLNKQDL TTNVDVEDKK GAIKELADKR GVVIFDVVSI SAKLNRLEEL YRALERAILT LPKYKSFEIV VKEKGKVSQV IALINSIGEI LDIEYGEATK ILAYIQVGMI KSLTKLGVEI KYSPIDLK // ID F0LNP5_VIBFN Unreviewed; 429 AA. AC F0LNP5; DT 03-MAY-2011, integrated into UniProtKB/TrEMBL. DT 03-MAY-2011, sequence version 1. DT 30-AUG-2017, entry version 43. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=vfu_A00014 {ECO:0000313|EMBL:ADT85257.1}; OS Vibrio furnissii (strain DSM 14383 / NCTC 11218). OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; OC Vibrionaceae; Vibrio. OX NCBI_TaxID=903510 {ECO:0000313|EMBL:ADT85257.1, ECO:0000313|Proteomes:UP000007456}; RN [1] {ECO:0000313|EMBL:ADT85257.1, ECO:0000313|Proteomes:UP000007456} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 14383 / NCTC 11218 {ECO:0000313|Proteomes:UP000007456}; RX PubMed=21217006; DOI=10.1128/JB.01512-10; RA Lux T.M., Lee R., Love J.; RT "Complete genome sequence of a free-living Vibrio furnissii sp. nov. RT strain (NCTC 11218)."; RL J. Bacteriol. 193:1487-1488(2011). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002377; ADT85257.1; -; Genomic_DNA. DR RefSeq; WP_004728279.1; NC_016602.1. DR ProteinModelPortal; F0LNP5; -. DR STRING; 903510.vfu_A00014; -. DR EnsemblBacteria; ADT85257; ADT85257; vfu_A00014. DR KEGG; vfu:vfu_A00014; -. DR PATRIC; fig|903510.3.peg.13; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000007456; Chromosome 1. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000007456}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000007456}. FT DOMAIN 198 365 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 429 AA; 48784 MW; DB13F197DE7D7D35 CRC64; MFDRYEAGER AVLVHINFTQ EGEWEDLREC EMLVSSAGVS TLQVITGSRQ SPHPKYYVGE GKAQEIAQAV QTTDADVVIF NHALSPAQER NLEHLCQCRV IDRTGLILDI FAQRARTHEG KLQVELAQLR HISTRLIRGW THLERQKGGI GLRGPGETQL ETDRRLLRER IKAILRRLER VAKQREQGRR ARNRAEIPTV SLVGYTNAGK STLFNRITSA GVYAADQLFA TLDPTLRKID LADVGPAILA DTVGFIRHLP HDLVAAFKAT LQETQEADIL LHVVDASDER FRENIQAVDD VLLEIEANEV PTLLVMNKID NLEGQQPRIE RDDEGVPRAV WVSAMDGLGI DLLFAALTER LVSQIVEYRL RVPPQHQGRI RSTFFQMKCI QHEEYDQEGN LLITVRMQQV DWSRLEKREE AVLRDFIVT // ID F0P150_WEEVC Unreviewed; 411 AA. AC F0P150; DT 03-MAY-2011, integrated into UniProtKB/TrEMBL. DT 03-MAY-2011, sequence version 1. DT 07-JUN-2017, entry version 47. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Weevi_0836 {ECO:0000313|EMBL:ADX67549.1}; OS Weeksella virosa (strain ATCC 43766 / DSM 16922 / JCM 21250 / NBRC OS 16016 / NCTC 11634 / CL345/78). OC Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales; OC Flavobacteriaceae; Weeksella. OX NCBI_TaxID=865938 {ECO:0000313|EMBL:ADX67549.1, ECO:0000313|Proteomes:UP000008641}; RN [1] {ECO:0000313|Proteomes:UP000008641} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43766 / DSM 16922 / JCM 21250 / NBRC 16016 / NCTC 11634 / RC CL345/78 {ECO:0000313|Proteomes:UP000008641}; RX DOI=10.4056/sigs.1603927; RA Lang E., Teshima H., Lucas S., Lapidus A., Hammon N., Deshpande S., RA Nolan M., Cheng J., Pitluck S., Liolios K., Pagani I., Mikhailova N., RA Ivanova N., Mavromatis K., Pati A., Tapia R., Han C., Goodwin L., RA Chen A., Palaniappan K., Land M., Hauser L., Chang Y., Jeffries C., RA Brambilla E., Kopitz M., Rohde M., Goker M., Tindall B., Detter J., RA Woyke T., Bristow J., Eisen J., Markowitz V., Hugenholtz P., Klenk H., RA Kyrpides N.; RT "Complete genome sequence of Weeksella virosa type strain (9751T)."; RL Stand. Genomic Sci. 4:81-90(2011). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002455; ADX67549.1; -; Genomic_DNA. DR RefSeq; WP_013597940.1; NC_015144.1. DR ProteinModelPortal; F0P150; -. DR STRING; 865938.Weevi_0836; -. DR EnsemblBacteria; ADX67549; ADX67549; Weevi_0836. DR KEGG; wvi:Weevi_0836; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000008641; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000008641}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000008641}. FT DOMAIN 200 384 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 411 AA; 47965 MW; 24532006CA6713A0 CRC64; MLEKKEAQYE KVVLVGLITR DQTEEKLTEY MDELRFLAYT AGAEVDKRFI QKLDRPDPKY FVGSGKLEEI TSYVEENNID TVIFDDELTP SQLKNIEKVV NRKIIDRTQL ILDIFAQRAQ TSYARTQVEL AQYQYLLPRL TRMWTHLERQ RGGIGMRGPG ETEIETDRRI IRDRITLLRE KLKSIDKQMA TQRTNRGAMV RVALVGYTNV GKSTLMNVLS KSDVFAEDKL FATLDTTVRK VVIGNLPFLL TDTVGFIRKL PTQLVESFKS TLDEVREADL LIHVVDISHA SFEDHINSVN KILDEINSKD KPTVMVFNKI DNFSYIEKPE DDLTVMHFEN YSLEHWKKTW MAKTSYPTLF ISATEKENIE ELRKTIYEEV KKLHIQRFPY NNFLFQYYNE DGENISEGEN L // ID F0R1F8_BACSH Unreviewed; 421 AA. AC F0R1F8; DT 03-MAY-2011, integrated into UniProtKB/TrEMBL. DT 03-MAY-2011, sequence version 1. DT 07-JUN-2017, entry version 48. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Bacsa_2871 {ECO:0000313|EMBL:ADY37402.1}; OS Bacteroides salanitronis (strain DSM 18170 / JCM 13567 / BL78). OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae; OC Bacteroides. OX NCBI_TaxID=667015 {ECO:0000313|EMBL:ADY37402.1, ECO:0000313|Proteomes:UP000007486}; RN [1] {ECO:0000313|EMBL:ADY37402.1, ECO:0000313|Proteomes:UP000007486} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 18170 / JCM 13567 / BL78 RC {ECO:0000313|Proteomes:UP000007486}; RX PubMed=21677856; DOI=10.4056/sigs.1704212; RA Gronow S., Held B., Lucas S., Lapidus A., Del Rio T.G., Nolan M., RA Tice H., Deshpande S., Cheng J.F., Pitluck S., Liolios K., Pagani I., RA Ivanova N., Mavromatis K., Pati A., Tapia R., Han C., Goodwin L., RA Chen A., Palaniappan K., Land M., Hauser L., Chang Y.J., RA Jeffries C.D., Brambilla E.M., Rohde M., Goker M., Detter J.C., RA Woyke T., Bristow J., Markowitz V., Hugenholtz P., Kyrpides N.C., RA Klenk H.P., Eisen J.A.; RT "Complete genome sequence of Bacteroides salanitronis type strain RT (BL78)."; RL Stand. Genomic Sci. 4:191-199(2011). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002530; ADY37402.1; -; Genomic_DNA. DR RefSeq; WP_013618775.1; NC_015164.1. DR ProteinModelPortal; F0R1F8; -. DR STRING; 667015.Bacsa_2871; -. DR EnsemblBacteria; ADY37402; ADY37402; Bacsa_2871. DR KEGG; bsa:Bacsa_2871; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000007486; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000007486}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000007486}. FT DOMAIN 217 401 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 421 AA; 47948 MW; FEF47191A53EA737 CRC64; MKEFVISEAQ TEKAVLVGLI TQTQNERKTN EYLDELAFLA ETAGAEVVKR FTQKLDTPNS VTYVGKGKLQ EIKEYLEMQN ESEETEVGMV IFDDELSAKQ IRNIENELKV KILDRTSLIL DIFAMRAQTA NAKTQVELAQ YKYMLPRLQR LWTHLERQGG GSGAGGGKGS VGLRGPGETQ LEMDRRIILN RMSLLKQRLA EIDTQKSTQR KNRGRLIRVA LVGYTNVGKS TLMNLLAKSD VFAENKLFAT LDTTVRKVII DNLPFLLSDT VGFIRKLPTD LVDSFKSTLD EVREADLLVH VVDISHSDFE EQIQVVDKTV SELGAGGKPT MIVFNKIDAY TYIEKDADDL TPKTKENVTL EELMHTWMAK MNDNCIFISA RNKTNLEELR RLLYNKVREL HVQKYPYNDF LYQTYDEEGS L // ID F0R9R2_CELLC Unreviewed; 403 AA. AC F0R9R2; DT 03-MAY-2011, integrated into UniProtKB/TrEMBL. DT 03-MAY-2011, sequence version 1. DT 07-JUN-2017, entry version 45. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Celly_1570 {ECO:0000313|EMBL:ADY29394.1}; OS Cellulophaga lytica (strain ATCC 23178 / DSM 7489 / JCM 8516 / NBRC OS 14961 / NCIMB 1423 / VKM B-1433 / Cy l20). OC Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales; OC Flavobacteriaceae; Cellulophaga. OX NCBI_TaxID=867900 {ECO:0000313|EMBL:ADY29394.1, ECO:0000313|Proteomes:UP000007487}; RN [1] {ECO:0000313|EMBL:ADY29394.1, ECO:0000313|Proteomes:UP000007487} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 23178 / DSM 7489 / JCM 8516 / NBRC 14961 / NCIMB 1423 / RC VKM B-1433 / Cy l20 {ECO:0000313|Proteomes:UP000007487}; RX PubMed=21677859; DOI=10.4056/sigs.1774329; RA Pati A., Abt B., Teshima H., Nolan M., Lapidus A., Lucas S., RA Hammon N., Deshpande S., Cheng J.F., Tapia R., Han C., Goodwin L., RA Pitluck S., Liolios K., Pagani I., Mavromatis K., Ovchinikova G., RA Chen A., Palaniappan K., Land M., Hauser L., Jeffries C.D., RA Detter J.C., Brambilla E.M., Kannan K.P., Rohde M., Spring S., RA Goker M., Woyke T., Bristow J., Eisen J.A., Markowitz V., RA Hugenholtz P., Kyrpides N.C., Klenk H.P., Ivanova N.; RT "Complete genome sequence of Cellulophaga lytica type strain (LIM- RT 21)."; RL Stand. Genomic Sci. 4:221-232(2011). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002534; ADY29394.1; -; Genomic_DNA. DR RefSeq; WP_013621139.1; NC_015167.1. DR ProteinModelPortal; F0R9R2; -. DR STRING; 867900.Celly_1570; -. DR EnsemblBacteria; ADY29394; ADY29394; Celly_1570. DR KEGG; cly:Celly_1570; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000007487; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000007487}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000007487}. FT DOMAIN 200 385 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 403 AA; 46773 MW; C4CDE8470792BE2B CRC64; MLEKKVVEYE RAVLIGVISS TQTEQKVKEY LDELEFLTYT AGGEVYKRFV QKIDKPNPKT YIGSGKMDEV AQYVEEHKIG SVIFDDELTP GQQRNIERHL KCKIVDRTTL ILDIFAQRAQ TSYSRTQVEL AQYEYLLPRL TGLWTHLERQ KGGIGMRGPG ETEIETDRRI VRDRITLLKK KLSKIDRQME TQRGNRGALV RVALVGYTNV GKSTLMNVVS KSDVFAEDKL FATLDTTVRK VVLGNLPFLL SDTVGFIRKL PTQLVESFKS TLDEVREADL LLHIVDISHP NFEDHIASVH KILEEIKADD KKTIIVFNKI DQFTHETIDD DDLVTEKTKI HFTLEEWKKT WMQKVGDRAL FISALNNENL DTFRKRVYDE VRDIHVTRFP YNNFLYPEHL DEY // ID F0RP25_DEIPM Unreviewed; 577 AA. AC F0RP25; DT 03-MAY-2011, integrated into UniProtKB/TrEMBL. DT 03-MAY-2011, sequence version 1. DT 07-JUN-2017, entry version 45. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Deipr_0167 {ECO:0000313|EMBL:ADY25340.1}; OS Deinococcus proteolyticus (strain ATCC 35074 / DSM 20540 / JCM 6276 / OS NBRC 101906 / NCIMB 13154 / VKM Ac-1939 / CCM 2703 / MRP). OC Bacteria; Deinococcus-Thermus; Deinococci; Deinococcales; OC Deinococcaceae; Deinococcus. OX NCBI_TaxID=693977 {ECO:0000313|EMBL:ADY25340.1, ECO:0000313|Proteomes:UP000007718}; RN [1] {ECO:0000313|Proteomes:UP000007718} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 35074 / DSM 20540 / JCM 6276 / NBRC 101906 / NCIMB 13154 / RC VKM Ac-1939 / CCM 2703 / MRP {ECO:0000313|Proteomes:UP000007718}; RG US DOE Joint Genome Institute (JGI-PGF); RA Lucas S., Copeland A., Lapidus A., Bruce D., Goodwin L., Pitluck S., RA Kyrpides N., Mavromatis K., Pagani I., Ivanova N., Ovchinnikova G., RA Zeytun A., Detter J.C., Han C., Land M., Hauser L., Markowitz V., RA Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Pukall R., Steenblock K., RA Brambilla E., Klenk H.-P., Eisen J.A.; RT "The complete sequence of chromosome of Deinococcus proteolyticus DSM RT 20540."; RL Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002536; ADY25340.1; -; Genomic_DNA. DR RefSeq; WP_013613949.1; NC_015161.1. DR STRING; 693977.Deipr_0167; -. DR EnsemblBacteria; ADY25340; ADY25340; Deipr_0167. DR KEGG; dpt:Deipr_0167; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR KO; K03665; -. DR OMA; EREVIIT; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000007718; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000007718}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000007718}. FT DOMAIN 385 559 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 577 AA; 62998 MW; AAFEBF7FBF57F898 CRC64; MTKVHGNTSG LKKAQLKSLE NLYRRRIEPG RIGSPELARN LAELSADVRR EVSVLIDRRG RVLSVSVADA KGTELPENRQ GENRLSGYHL LHTHPRGGEL SKSDLSTLFM RRLDAVSAIE VDSEGRPGRV HTAHLTPPGS AAEEEDWRIL PAVPSYEIDE FDLGAQVSAL EEEIARAART REAQKEREQA ILVQIDTGEV DAEERLAELG ELARTAGAAV VYRELVYRRN LKAGTLVGAG KLEELTSRAY HLDADLVIFG QELGPAQARE IEAATGLKVV DRTQLILDIF AQHAQGQESR LQVELAQLRY MKPRLLGAGA QLSRIGASGG SAASGAIGTR GPGETKLELD RRRINDRIAF LEGQLREVAV RREQRRKSRA RNDVPVVGIV GYTNAGKSTL LNALTHAAEE PRRVLAENKL FATLRPTSRQ GYLSGVGQVV LTDTVGFIRD LPADLSRAFR ATLEEIGDSD VLVHVLDASS DAAELHFEAV TRILDDLELA DLPAVVALNK VDQARPAELA RLQERLEQAG VQTVAISAFK RQGLDELRDA VATALHRQGF AQPGYAEMQS QLAHGAD // ID F0RSY9_SPHGB Unreviewed; 440 AA. AC F0RSY9; DT 03-MAY-2011, integrated into UniProtKB/TrEMBL. DT 03-MAY-2011, sequence version 1. DT 07-JUN-2017, entry version 41. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=SpiBuddy_2115 {ECO:0000313|EMBL:ADY13936.1}; OS Sphaerochaeta globosa (strain ATCC BAA-1886 / DSM 22777 / Buddy) OS (Spirochaeta sp. (strain Buddy)). OC Bacteria; Spirochaetes; Spirochaetales; Spirochaetaceae; OC Sphaerochaeta. OX NCBI_TaxID=158189 {ECO:0000313|EMBL:ADY13936.1, ECO:0000313|Proteomes:UP000008466}; RN [1] {ECO:0000313|Proteomes:UP000008466} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-1886 / DSM 22777 / Buddy RC {ECO:0000313|Proteomes:UP000008466}; RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L., RA Pitluck S., Zeytun A., Detter J.C., Han C., Tapia R., Land M., RA Hauser L., Kyrpides N., Ivanova N., Mikhailova N., Pagani I., RA Ritalahti K.M., Loeffler F.E., Woyke T.; RT "Complete sequence of Spirochaeta sp. Buddy."; RL Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002541; ADY13936.1; -; Genomic_DNA. DR RefSeq; WP_013607785.1; NC_015152.1. DR ProteinModelPortal; F0RSY9; -. DR STRING; 158189.SpiBuddy_2115; -. DR EnsemblBacteria; ADY13936; ADY13936; SpiBuddy_2115. DR KEGG; sbu:SpiBuddy_2115; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000008466; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000008466}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000008466}. FT DOMAIN 220 386 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 440 AA; 49085 MW; C29C317AF40EDD30 CRC64; MGIEQLTGSE EPISKGKRVY EIKDEDQRAL LLILVSHGES EQSSKRRADE LKALVDTMGA LTIRVEYIPM RQTNSATLIG SGKVEAIKLL VEELSIDVVI FDQGINPRVQ RNLEKEMETC VIDRDEVILQ IFADRAATKE ANLQVELARL EYSLPRLTRR WTNLNRQKGG VKGTKGEGET QLELDRRQIQ DRVVALKLLL EKVVQQRNIQ RNQRMNGNIP TGAIVGYTNS GKSSLLNALT NAGVLVEDKL FATLDPTTRL VKLPGGEEIL LSDTVGFISD LPHNLVDAFK STLEEAKYAD FLIIVCDASH PDMLANYATT VQVLEELGCT DKPAIVLANK MDKVEDAFAV SRLKSMYNPV LETSIKTGEG LDALLTQIGI TLHELCATTT YLLPNTRHDL VAHIHRFGQV ESIDYTEEGI LVKSRIQGRF QGPLQNYRHD // ID F0S2K5_DESTD Unreviewed; 357 AA. AC F0S2K5; DT 03-MAY-2011, integrated into UniProtKB/TrEMBL. DT 03-MAY-2011, sequence version 1. DT 07-JUN-2017, entry version 41. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Dester_0423 {ECO:0000313|EMBL:ADY73077.1}; OS Desulfurobacterium thermolithotrophum (strain DSM 11699 / BSA). OC Bacteria; Aquificae; Desulfurobacteriales; Desulfurobacteriaceae; OC Desulfurobacterium. OX NCBI_TaxID=868864 {ECO:0000313|EMBL:ADY73077.1, ECO:0000313|Proteomes:UP000007102}; RN [1] {ECO:0000313|Proteomes:UP000007102} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 11699 / BSA {ECO:0000313|Proteomes:UP000007102}; RG US DOE Joint Genome Institute (JGI-PGF); RA Lucas S., Copeland A., Lapidus A., Bruce D., Goodwin L., Pitluck S., RA Kyrpides N., Mavromatis K., Pagani I., Ivanova N., Mikhailova N., RA Daligault H., Detter J.C., Tapia R., Han C., Land M., Hauser L., RA Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Spring S., RA Brambilla E., Klenk H.-P., Eisen J.A.; RT "The complete genome of Desulfurobacterium thermolithotrophum DSM RT 11699."; RL Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002543; ADY73077.1; -; Genomic_DNA. DR STRING; 868864.Dester_0423; -. DR EnsemblBacteria; ADY73077; ADY73077; Dester_0423. DR KEGG; dte:Dester_0423; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000007102; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000007102}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000007102}. FT DOMAIN 187 357 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 153 180 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 357 AA; 40178 MW; D691EBB85AF93C79 CRC64; MNKEKVVIVG VKTPRKEIDT EELKGLIEAL GGEVIQIVIQ KRKAPSPSTY IGKGKVREID TQNATLIVAY HTLSYSQKRN LENLTGLPVI DRTEVILEIF ARRARTKEAK LQVELAKASY QLSHLRGKGK ELSRLGGGIG TRGPGETKTE VEARVLRKKI HKLKKEIEEI EKRYSLVRES RKRKNFITIA VVGYTNVGKS TLVKALTKKD VFIKNIPFAT LDVKTGSLYL EDKKVLISDT VGFIRNLPHE LIASFKATLG EVKESDILLI VFDVSSKKLE EELKSVKEVL KKLGAWNKPK IFVANKTDCI VDSYEKSQIL YTELLGKLPE EDAPTVFISA KFGWGFENLK LEITKFL // ID F0SA27_PSESL Unreviewed; 410 AA. AC F0SA27; DT 03-MAY-2011, integrated into UniProtKB/TrEMBL. DT 03-MAY-2011, sequence version 1. DT 07-JUN-2017, entry version 49. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Pedsa_3052 {ECO:0000313|EMBL:ADY53591.1}; OS Pseudopedobacter saltans (strain ATCC 51119 / DSM 12145 / JCM 21818 / OS LMG 10337 / NBRC 100064 / NCIMB 13643) (Pedobacter saltans). OC Bacteria; Bacteroidetes; Sphingobacteriia; Sphingobacteriales; OC Sphingobacteriaceae; Pseudopedobacter. OX NCBI_TaxID=762903 {ECO:0000313|EMBL:ADY53591.1, ECO:0000313|Proteomes:UP000000310}; RN [1] {ECO:0000313|Proteomes:UP000000310} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51119 / DSM 12145 / JCM 21818 / LMG 10337 / NBRC 100064 / RC NCIMB 13643 {ECO:0000313|Proteomes:UP000000310}; RG US DOE Joint Genome Institute (JGI-PGF); RA Lucas S., Copeland A., Lapidus A., Bruce D., Goodwin L., Pitluck S., RA Kyrpides N., Mavromatis K., Pagani I., Ivanova N., Ovchinnikova G., RA Lu M., Detter J.C., Han C., Land M., Hauser L., Markowitz V., RA Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Tindall B., RA Pomrenke H.G., Brambilla E., Klenk H.-P., Eisen J.A.; RT "The complete genome of Pedobacter saltans DSM 12145."; RL Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002545; ADY53591.1; -; Genomic_DNA. DR RefSeq; WP_013634076.1; NC_015177.1. DR ProteinModelPortal; F0SA27; -. DR STRING; 762903.Pedsa_3052; -. DR EnsemblBacteria; ADY53591; ADY53591; Pedsa_3052. DR KEGG; psn:Pedsa_3052; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000000310; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000000310}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Hydrolase {ECO:0000313|EMBL:ADY53591.1}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000000310}. FT DOMAIN 214 399 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 410 AA; 47015 MW; A9C53EDE7E4CDE7B CRC64; MARKSLLKKL HDTAPKKETA VLIGLITPET SEVREKEYLE ELAFLVDTAG GETKHVFTQK LQKPDRATFV GSGKLEEIKE YVIAEEIDMV VFDDELSPMQ VRNIENELKV KEELTVKVLD RSNLILDIFA SRAQTAQAKT QVELAQLQYL LPRLTRMWTH LERQKGGIGM RGPGESQIES DRRMINNKVA LLKEKLKTID KQNLTQRKNR KEMVRVALVG YTNVGKSTIM NMLSKSEVFA ENKLFATLDT TVRKVVIENV PFLLSDTVGF IRKLPHHLVE CFKSTLDETR EADILIHVVD ISHPNFEDHI RTVNETLKDL GVIDKETITV FNKIDAYQGV EAEQEWMVDN EEAPKMTLED FKKSWMAKNA SPAVFISATE KENTDELKDV IYERVKAVNE KIYPFNNFLY // ID F0SQG6_RUBBR Unreviewed; 462 AA. AC F0SQG6; DT 03-MAY-2011, integrated into UniProtKB/TrEMBL. DT 03-MAY-2011, sequence version 1. DT 07-JUN-2017, entry version 43. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Plabr_0312 {ECO:0000313|EMBL:ADY57941.1}; OS Rubinisphaera brasiliensis (strain ATCC 49424 / DSM 5305 / JCM 21570 / OS NBRC 103401 / IFAM 1448) (Planctomyces brasiliensis). OC Bacteria; Planctomycetes; Planctomycetia; Planctomycetales; OC Planctomycetaceae; Rubinisphaera. OX NCBI_TaxID=756272 {ECO:0000313|EMBL:ADY57941.1, ECO:0000313|Proteomes:UP000006860}; RN [1] {ECO:0000313|Proteomes:UP000006860} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 49424 / DSM 5305 / JCM 21570 / NBRC 103401 / IFAM 1448 RC {ECO:0000313|Proteomes:UP000006860}; RA Lucas S., Copeland A., Lapidus A., Bruce D., Goodwin L., Pitluck S., RA Kyrpides N., Mavromatis K., Pagani I., Ivanova N., Ovchinnikova G., RA Lu M., Detter J.C., Han C., Land M., Hauser L., Markowitz V., RA Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Tindall B., RA Pomrenke H.G., Brambilla E., Klenk H.-P., Eisen J.A.; RT "The complete genome of Planctomyces brasiliensis DSM 5305."; RL Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002546; ADY57941.1; -; Genomic_DNA. DR RefSeq; WP_013626685.1; NC_015174.1. DR STRING; 756272.Plabr_0312; -. DR EnsemblBacteria; ADY57941; ADY57941; Plabr_0312. DR KEGG; pbs:Plabr_0312; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000006860; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000006860}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Hydrolase {ECO:0000313|EMBL:ADY57941.1}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000006860}. FT DOMAIN 204 395 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 165 199 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 462 AA; 51644 MW; 8126E76572102AA8 CRC64; MGQPLRETLK VQAKKAVLVG MVSPQTSLEK GHYLDELSGL VKTAGCEIVG RLTQFRDKPD PATYLGKGKI EELHQLMQST GAELAVFDNN LSPSQGKNIE AAIKTIVVDR SEVILDIFAS HAKTYEARLQ VELAQLLYMR PRLKRMWTHL ERIEGGIGSG RGPGEKQLEL DRRMLDKRVS ELRKKLETVE KRRERLVASR NESFTVSLVG YTNAGKSTLM RALTGEEVYI ANQLFATLDT KTRKWSIPNW GEVLLSDTVG FVRDLPHHLV ASFKSTLEEA LQADLLLHVV DASNPEAQLQ IDTVEHVLEE IGASDKETLL VFNKVDRLPG HTPAEQTETS EDDIPEPEGD GEPLDRSWYD IMRNKYRSAI SVSAASGEGL ELLRAAVIER LSRSHQLVDI VADVGDGKLS SLLARMTTVE STTYDESTAT YRCRLAEGAI NRIEREHEVE VRRIDELAET SY // ID F0T1R4_SYNGF Unreviewed; 597 AA. AC F0T1R4; DT 03-MAY-2011, integrated into UniProtKB/TrEMBL. DT 03-MAY-2011, sequence version 1. DT 07-JUN-2017, entry version 43. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Sgly_3224 {ECO:0000313|EMBL:ADY57488.1}; OS Syntrophobotulus glycolicus (strain DSM 8271 / FlGlyR). OC Bacteria; Firmicutes; Clostridia; Clostridiales; Peptococcaceae; OC Syntrophobotulus. OX NCBI_TaxID=645991 {ECO:0000313|EMBL:ADY57488.1, ECO:0000313|Proteomes:UP000007488}; RN [1] {ECO:0000313|Proteomes:UP000007488} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 8271 / FlGlyR {ECO:0000313|Proteomes:UP000007488}; RA Lucas S., Copeland A., Lapidus A., Bruce D., Goodwin L., Pitluck S., RA Kyrpides N., Mavromatis K., Pagani I., Ivanova N., Mikhailova N., RA Chertkov O., Held B., Detter J.C., Tapia R., Han C., Land M., RA Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T., Wu D., RA Spring S., Schroeder M., Brambilla E., Klenk H.-P., Eisen J.A.; RT "The complete genome of Syntrophobotulus glycolicus DSM 8271."; RL Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002547; ADY57488.1; -; Genomic_DNA. DR RefSeq; WP_013626213.1; NC_015172.1. DR STRING; 645991.Sgly_3224; -. DR EnsemblBacteria; ADY57488; ADY57488; Sgly_3224. DR KEGG; sgy:Sgly_3224; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR KO; K03665; -. DR OMA; EREVIIT; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000007488; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000007488}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000007488}. FT DOMAIN 379 543 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 597 AA; 65572 MW; E36AD977BB82C8A6 CRC64; MRVHGETEGL KSSVLERLDA LYDLRIPQNQ LWTESLVEEI SSVSSGINRE IAVYLDRKGN VTDVSIGDHQ TVTLTEVAGK RNTRRLTGTR CLHTHPGGSG MLSSVDISSL KILRLDAMIA VSVRDGCPGE LFVGVLSPEN PDGIELFGPL SPGQTSFAEL LESIRHTDDT LRKTLPENLS EAERTVLVGV QTQESRDLNG ISEADVSLGE LEELAKTAGA TVVGKILQKR DSLSSSTIIG RGKLNELRLL AQALEADTVI FDCEISGTQQ RNIEQILGIK VLSRPSLILD IFAQRARSRE GMLQVELAQM EYRLPRLMGM GLSLSRLGGG IGTRGPGETK LETDRRHIRT RITHLRAQLA GIRKQRGVLR SERQKSGIPV VSIVGYTNAG KSTLLNTLCQ TAVFAEDKLF ATLDPTTRKL EFSDDRTVLL TDTVGFIRKL PHHLLEAFKS TLEEVVLSDL ILIVVDASDP QVEDHIRIVD EILGELGASA KPAIIVLNKI DKLADNPVIL SRENRPVIEI SARTGLGLDH LKHGIEKILY SNRVRVKLAV PFQDGAVMAW LYANSKVLSA TYDENVNIVQ AELDKALLKK VSPYRIN // ID F0Y0L5_AURAN Unreviewed; 437 AA. AC F0Y0L5; DT 03-MAY-2011, integrated into UniProtKB/TrEMBL. DT 03-MAY-2011, sequence version 1. DT 30-AUG-2017, entry version 31. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EGB11728.1}; DE Flags: Fragment; GN ORFNames=AURANDRAFT_21487 {ECO:0000313|EMBL:EGB11728.1}; OS Aureococcus anophagefferens (Harmful bloom alga). OC Eukaryota; Stramenopiles; Pelagophyceae; Pelagomonadales; Aureococcus. OX NCBI_TaxID=44056 {ECO:0000313|Proteomes:UP000002729}; RN [1] {ECO:0000313|EMBL:EGB11728.1, ECO:0000313|Proteomes:UP000002729} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CCMP 1984 {ECO:0000313|Proteomes:UP000002729}; RX PubMed=21368207; DOI=10.1073/pnas.1016106108; RA Gobler C.J., Berry D.L., Dyhrman S.T., Wilhelm S.W., Salamov A., RA Lobanov A.V., Zhang Y., Collier J.L., Wurch L.L., Kustka A.B., RA Dill B.D., Shah M., VerBerkmoes N.C., Kuo A., Terry A., Pangilinan J., RA Lindquist E.A., Lucas S., Paulsen I.T., Hattenrath-Lehmann T.K., RA Talmage S.C., Walker E.A., Koch F., Burson A.M., Marcoval M.A., RA Tang Y.Z., Lecleir G.R., Coyne K.J., Berg G.M., Bertrand E.M., RA Saito M.A., Gladyshev V.N., Grigoriev I.V.; RT "Niche of harmful alga Aureococcus anophagefferens revealed through RT ecogenomics."; RL Proc. Natl. Acad. Sci. U.S.A. 108:4352-4357(2011). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GL833122; EGB11728.1; -; Genomic_DNA. DR RefSeq; XP_009034067.1; XM_009035819.1. DR ProteinModelPortal; F0Y0L5; -. DR EnsemblProtists; EGB11728; EGB11728; AURANDRAFT_21487. DR GeneID; 20219448; -. DR KEGG; aaf:AURANDRAFT_21487; -. DR InParanoid; F0Y0L5; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR Proteomes; UP000002729; Unassembled WGS sequence. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000002729}; KW Reference proteome {ECO:0000313|Proteomes:UP000002729}. FT DOMAIN 200 382 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT NON_TER 1 1 {ECO:0000313|EMBL:EGB11728.1}. SQ SEQUENCE 437 AA; 46604 MW; 623B4FDAC8B6E5DE CRC64; GGAAWTVADS LAELARLCET ARVRAVDATF QRADAANGQY LVGKGKIEEV ARKVLDHGAD AVVFDDELSL AQQRSVLAVL AEAGCDDKVQ ILDRTQLVLQ IFSERAQTRE AKAQIALARA EYMLPRLTTF LTGAAAGTDA KSGGRGAGGG AYLRGAGESQ LEMDRRLFGK RIAKLKAELG AIASKRAVAR SKKLDKEDLP LVALIGYTNA GKTSLLNALS EAAPLYADDR LFATLDPATR RVTLPSGRAC KLTDTVGFIQ KLPTKLVASF RATLEEIADA SADACLLVHV VDASSPLADG QMRAVYAILH ELDCFDMPQI TVYNKQDRVG GAPAPPGDDV ASATTLLDLM PPEADEVRVS CQDGTGIRPL LGYVDAALGK MNAKVHCLLP FDQGTLVEEI HRTATVDEVE HLAQGTRIVA RVPPSLEQRL RPFAVPV // ID F0Z097_9CLOT Unreviewed; 413 AA. AC F0Z097; DT 03-MAY-2011, integrated into UniProtKB/TrEMBL. DT 03-MAY-2011, sequence version 1. DT 07-JUN-2017, entry version 38. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=HMPREF0240_02527 {ECO:0000313|EMBL:EGB92518.1}; OS Clostridium sp. D5. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=556261 {ECO:0000313|EMBL:EGB92518.1, ECO:0000313|Proteomes:UP000003978}; RN [1] {ECO:0000313|EMBL:EGB92518.1, ECO:0000313|Proteomes:UP000003978} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=D5 {ECO:0000313|EMBL:EGB92518.1, RC ECO:0000313|Proteomes:UP000003978}; RG The Broad Institute Genome Sequencing Platform; RA Ward D., Earl A., Feldgarden M., Gevers D., Young S., Zeng Q., RA Koehrsen M., Alvarado L., Berlin A.M., Borenstein D., Chapman S.B., RA Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A., RA Gujja S., Heilman E.R., Heiman D.I., Hepburn T.A., Howarth C., Jen D., RA Larson L., Mehta T., Park D., Pearson M., Richards J., Roberts A., RA Saif S., Shea T.D., Shenoy N., Sisk P., Stolte C., Sykes S.N., RA Walk T., White J., Yandava C., Sibley C.D., White A.P., Crowley S., RA Surette M.G., Strauss J.C., Ambrose C.E., Allen-Vercoe E., Haas B., RA Nusbaum C., Birren B.; RT "The Genome Sequence of Clostridium sp. D5."; RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GL870813; EGB92518.1; -; Genomic_DNA. DR RefSeq; WP_009003829.1; NZ_GL870813.1. DR ProteinModelPortal; F0Z097; -. DR STRING; 556261.HMPREF0240_02527; -. DR EnsemblBacteria; EGB92518; EGB92518; HMPREF0240_02527. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000003978; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000003978}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000003978}. FT DOMAIN 201 365 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 160 197 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 413 AA; 46615 MW; E656E89A7B8D7B16 CRC64; MTLFEIEEQR EAVILVGIQL NENEQTEESL DELAELVKTA RAEVAGRVIQ KREAIHPTTY VGKGKLLELK EVLWETEATG IVCDDELTSV QLHNLERELQ CKVIDRTLLI LDIFAARAVS SEGKIQVELA QLKYRASRLV GLRDSLSRLG GGIGTRGPGE KKLEMDRRLI RERISKLKKE LREVEQHREL IRTQRKASHK KIAALVGYTS AGKSSIENAL TGAGILADAM LFSTLDTTTR VLELDKKQEI LLTDTVGFIR KLPHHLIEAF KSTLEEAKYA DIIIHVVDAS NPQMDSQMYV VYETLRQLGV EGKPVITLFN KQDKLEEPGS FRDFQAEYSI LTSAKTGQGL EELKTALLEI IRSGQIYIEK MYPFEEAGKI QLIRKHGQLL EEEYVPEGIS VKAYVTKEIY GKI // ID F1NEZ7_CHICK Unreviewed; 536 AA. AC F1NEZ7; DT 03-MAY-2011, integrated into UniProtKB/TrEMBL. DT 15-FEB-2017, sequence version 4. DT 30-AUG-2017, entry version 46. DE SubName: Full=GTP binding protein 6 (putative) {ECO:0000313|Ensembl:ENSGALP00000026928}; GN Name=GTPBP6 {ECO:0000313|Ensembl:ENSGALP00000026928}; OS Gallus gallus (Chicken). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda; OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; OC Phasianidae; Phasianinae; Gallus. OX NCBI_TaxID=9031 {ECO:0000313|Ensembl:ENSGALP00000026928, ECO:0000313|Proteomes:UP000000539}; RN [1] {ECO:0000313|Ensembl:ENSGALP00000026928, ECO:0000313|Proteomes:UP000000539} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Red jungle fowl {ECO:0000313|Ensembl:ENSGALP00000026928, RC ECO:0000313|Proteomes:UP000000539}; RX PubMed=15592404; DOI=10.1038/nature03154; RG International Chicken Genome Sequencing Consortium; RA Hillier L.W., Miller W., Birney E., Warren W., Hardison R.C., RA Ponting C.P., Bork P., Burt D.W., Groenen M.A.M., Delany M.E., RA Dodgson J.B., Chinwalla A.T., Cliften P.F., Clifton S.W., RA Delehaunty K.D., Fronick C., Fulton R.S., Graves T.A., Kremitzki C., RA Layman D., Magrini V., McPherson J.D., Miner T.L., Minx P., Nash W.E., RA Nhan M.N., Nelson J.O., Oddy L.G., Pohl C.S., Randall-Maher J., RA Smith S.M., Wallis J.W., Yang S.-P., Romanov M.N., Rondelli C.M., RA Paton B., Smith J., Morrice D., Daniels L., Tempest H.G., RA Robertson L., Masabanda J.S., Griffin D.K., Vignal A., Fillon V., RA Jacobbson L., Kerje S., Andersson L., Crooijmans R.P., Aerts J., RA van der Poel J.J., Ellegren H., Caldwell R.B., Hubbard S.J., RA Grafham D.V., Kierzek A.M., McLaren S.R., Overton I.M., Arakawa H., RA Beattie K.J., Bezzubov Y., Boardman P.E., Bonfield J.K., RA Croning M.D.R., Davies R.M., Francis M.D., Humphray S.J., Scott C.E., RA Taylor R.G., Tickle C., Brown W.R.A., Rogers J., Buerstedde J.-M., RA Wilson S.A., Stubbs L., Ovcharenko I., Gordon L., Lucas S., RA Miller M.M., Inoko H., Shiina T., Kaufman J., Salomonsen J., RA Skjoedt K., Wong G.K.-S., Wang J., Liu B., Wang J., Yu J., Yang H., RA Nefedov M., Koriabine M., Dejong P.J., Goodstadt L., Webber C., RA Dickens N.J., Letunic I., Suyama M., Torrents D., von Mering C., RA Zdobnov E.M., Makova K., Nekrutenko A., Elnitski L., Eswara P., RA King D.C., Yang S.-P., Tyekucheva S., Radakrishnan A., Harris R.S., RA Chiaromonte F., Taylor J., He J., Rijnkels M., Griffiths-Jones S., RA Ureta-Vidal A., Hoffman M.M., Severin J., Searle S.M.J., Law A.S., RA Speed D., Waddington D., Cheng Z., Tuzun E., Eichler E., Bao Z., RA Flicek P., Shteynberg D.D., Brent M.R., Bye J.M., Huckle E.J., RA Chatterji S., Dewey C., Pachter L., Kouranov A., Mourelatos Z., RA Hatzigeorgiou A.G., Paterson A.H., Ivarie R., Brandstrom M., RA Axelsson E., Backstrom N., Berlin S., Webster M.T., Pourquie O., RA Reymond A., Ucla C., Antonarakis S.E., Long M., Emerson J.J., RA Betran E., Dupanloup I., Kaessmann H., Hinrichs A.S., Bejerano G., RA Furey T.S., Harte R.A., Raney B., Siepel A., Kent W.J., Haussler D., RA Eyras E., Castelo R., Abril J.F., Castellano S., Camara F., Parra G., RA Guigo R., Bourque G., Tesler G., Pevzner P.A., Smit A., Fulton L.A., RA Mardis E.R., Wilson R.K.; RT "Sequence and comparative analysis of the chicken genome provide RT unique perspectives on vertebrate evolution."; RL Nature 432:695-716(2004). RN [2] {ECO:0000313|Ensembl:ENSGALP00000026928} RP IDENTIFICATION. RC STRAIN=Red jungle fowl {ECO:0000313|Ensembl:ENSGALP00000026928}; RG Ensembl; RL Submitted (JUL-2011) to UniProtKB. CC -!- CAUTION: The sequence shown here is derived from an Ensembl CC automatic analysis pipeline and should be considered as CC preliminary data. {ECO:0000313|Ensembl:ENSGALP00000026928}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AADN04000081; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR RefSeq; XP_416868.3; XM_416868.5. DR STRING; 9031.ENSGALP00000026928; -. DR PaxDb; F1NEZ7; -. DR Ensembl; ENSGALT00000026979; ENSGALP00000026928; ENSGALG00000016717. DR GeneID; 418672; -. DR CTD; 8225; -. DR eggNOG; KOG0410; Eukaryota. DR eggNOG; COG2262; LUCA. DR GeneTree; ENSGT00390000001397; -. DR InParanoid; F1NEZ7; -. DR OMA; MDTVGFM; -. DR OrthoDB; EOG091G0852; -. DR TreeFam; TF315022; -. DR Proteomes; UP000000539; Chromosome 1. DR Bgee; ENSGALG00000016717; -. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR GO; GO:0043022; F:ribosome binding; IBA:GO_Central. DR CDD; cd01878; HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 4: Predicted; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000000539}; KW Reference proteome {ECO:0000313|Proteomes:UP000000539}. FT DOMAIN 309 473 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 271 305 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 536 AA; 59762 MW; 50EE6789096FE8EB CRC64; MGPGRLSRAL LLHCRRALGA ARCPLKPPYG RSLGAAAAFR LCAPQRPPDG RAGGRGRWKG AAGAGRDDDN NDDDEDEEEE EEGDEDEEDD AELEELLGPS PLGPQFGAHR VAVVHPAVRW GPKKPLLTTA ELQMAEAVAL VDTLQNWTVL DKIIIPTKNP DKKFVFGKGN FEALTERIKK LPHVTAVFLN VERISSVTKK ELEDAWGVKV FDRYTVVLHI FRCNARTKEA KLQIALAEIP LLRSNLKTEV SHLDQQRGGS RYIMGSGETF METQNRLLRE KELKIRNALE KLRKKRSLLR TQRRKREFPI ISVMGYTNCG KTTLIKALTG DAGIQPRDQL FATLDITAHA GYLPSHMAVI YVDTIGFLSE LPHNLVESFS ATLEEVAYSD LIVHVRDITH PETILQKASV LSVLKDLNLP SHLLESMVEV HNKVDLIESY QPTEENALAI SALHGHGLEE LKEEIEKKIL KATGKKILTI TVNLQGPQLS WLYKESAVQE VDVMPDDGTA RVKVIISNSA FGKYRNLFPN SKFFVS // ID F1PX47_CANLF Unreviewed; 526 AA. AC F1PX47; DT 03-MAY-2011, integrated into UniProtKB/TrEMBL. DT 31-OCT-2012, sequence version 2. DT 30-AUG-2017, entry version 39. DE SubName: Full=GTP binding protein 6 (putative) {ECO:0000313|Ensembl:ENSCAFP00000016099}; GN Name=GTPBP6 {ECO:0000313|Ensembl:ENSCAFP00000016099}; OS Canis lupus familiaris (Dog) (Canis familiaris). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; OC Canis. OX NCBI_TaxID=9615 {ECO:0000313|Ensembl:ENSCAFP00000016099, ECO:0000313|Proteomes:UP000002254}; RN [1] {ECO:0000313|Ensembl:ENSCAFP00000016099, ECO:0000313|Proteomes:UP000002254} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Boxer {ECO:0000313|Ensembl:ENSCAFP00000016099, RC ECO:0000313|Proteomes:UP000002254}; RX PubMed=16341006; DOI=10.1038/nature04338; RG Broad Sequencing Platform; RA Lindblad-Toh K., Wade C.M., Mikkelsen T.S., Karlsson E.K., Jaffe D.B., RA Kamal M., Clamp M., Chang J.L., Kulbokas E.J. III, Zody M.C., RA Mauceli E., Xie X., Breen M., Wayne R.K., Ostrander E.A., RA Ponting C.P., Galibert F., Smith D.R., deJong P.J., Kirkness E.F., RA Alvarez P., Biagi T., Brockman W., Butler J., Chin C.-W., Cook A., RA Cuff J., Daly M.J., DeCaprio D., Gnerre S., Grabherr M., Kellis M., RA Kleber M., Bardeleben C., Goodstadt L., Heger A., Hitte C., Kim L., RA Koepfli K.-P., Parker H.G., Pollinger J.P., Searle S.M.J., RA Sutter N.B., Thomas R., Webber C., Baldwin J., Abebe A., RA Abouelleil A., Aftuck L., Ait-Zahra M., Aldredge T., Allen N., An P., RA Anderson S., Antoine C., Arachchi H., Aslam A., Ayotte L., RA Bachantsang P., Barry A., Bayul T., Benamara M., Berlin A., RA Bessette D., Blitshteyn B., Bloom T., Blye J., Boguslavskiy L., RA Bonnet C., Boukhgalter B., Brown A., Cahill P., Calixte N., RA Camarata J., Cheshatsang Y., Chu J., Citroen M., Collymore A., RA Cooke P., Dawoe T., Daza R., Decktor K., DeGray S., Dhargay N., RA Dooley K., Dooley K., Dorje P., Dorjee K., Dorris L., Duffey N., RA Dupes A., Egbiremolen O., Elong R., Falk J., Farina A., Faro S., RA Ferguson D., Ferreira P., Fisher S., FitzGerald M., Foley K., RA Foley C., Franke A., Friedrich D., Gage D., Garber M., Gearin G., RA Giannoukos G., Goode T., Goyette A., Graham J., Grandbois E., RA Gyaltsen K., Hafez N., Hagopian D., Hagos B., Hall J., Healy C., RA Hegarty R., Honan T., Horn A., Houde N., Hughes L., Hunnicutt L., RA Husby M., Jester B., Jones C., Kamat A., Kanga B., Kells C., RA Khazanovich D., Kieu A.C., Kisner P., Kumar M., Lance K., Landers T., RA Lara M., Lee W., Leger J.-P., Lennon N., Leuper L., LeVine S., Liu J., RA Liu X., Lokyitsang Y., Lokyitsang T., Lui A., Macdonald J., Major J., RA Marabella R., Maru K., Matthews C., McDonough S., Mehta T., RA Meldrim J., Melnikov A., Meneus L., Mihalev A., Mihova T., Miller K., RA Mittelman R., Mlenga V., Mulrain L., Munson G., Navidi A., Naylor J., RA Nguyen T., Nguyen N., Nguyen C., Nguyen T., Nicol R., Norbu N., RA Norbu C., Novod N., Nyima T., Olandt P., O'Neill B., O'Neill K., RA Osman S., Oyono L., Patti C., Perrin D., Phunkhang P., Pierre F., RA Priest M., Rachupka A., Raghuraman S., Rameau R., Ray V., Raymond C., RA Rege F., Rise C., Rogers J., Rogov P., Sahalie J., Settipalli S., RA Sharpe T., Shea T., Sheehan M., Sherpa N., Shi J., Shih D., Sloan J., RA Smith C., Sparrow T., Stalker J., Stange-Thomann N., Stavropoulos S., RA Stone C., Stone S., Sykes S., Tchuinga P., Tenzing P., Tesfaye S., RA Thoulutsang D., Thoulutsang Y., Topham K., Topping I., Tsamla T., RA Vassiliev H., Venkataraman V., Vo A., Wangchuk T., Wangdi T., RA Weiand M., Wilkinson J., Wilson A., Yadav S., Yang S., Yang X., RA Young G., Yu Q., Zainoun J., Zembek L., Zimmer A., Lander E.S.; RT "Genome sequence, comparative analysis and haplotype structure of the RT domestic dog."; RL Nature 438:803-819(2005). RN [2] {ECO:0000313|Ensembl:ENSCAFP00000016099} RP IDENTIFICATION. RC STRAIN=Boxer {ECO:0000313|Ensembl:ENSCAFP00000016099}; RG Ensembl; RL Submitted (JUL-2011) to UniProtKB. CC -!- CAUTION: The sequence shown here is derived from an Ensembl CC automatic analysis pipeline and should be considered as CC preliminary data. {ECO:0000313|Ensembl:ENSCAFP00000016099}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AAEX03026084; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR RefSeq; XP_850911.3; XM_845818.5. DR STRING; 9615.ENSCAFP00000016099; -. DR PaxDb; F1PX47; -. DR Ensembl; ENSCAFT00000017390; ENSCAFP00000016099; ENSCAFG00000010931. DR GeneID; 608710; -. DR CTD; 8225; -. DR eggNOG; KOG0410; Eukaryota. DR eggNOG; COG2262; LUCA. DR GeneTree; ENSGT00390000001397; -. DR InParanoid; F1PX47; -. DR OMA; MDTVGFM; -. DR OrthoDB; EOG091G0852; -. DR TreeFam; TF315022; -. DR Proteomes; UP000002254; Chromosome X. DR Bgee; ENSCAFG00000010931; -. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR GO; GO:0043022; F:ribosome binding; IBA:GO_Central. DR CDD; cd01878; HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 4: Predicted; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000002254}; KW Reference proteome {ECO:0000313|Proteomes:UP000002254}. FT DOMAIN 305 469 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 267 294 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 526 AA; 58071 MW; 59CF54A598FD71AA CRC64; MWALRAAVRP GPGLCRLARG RRLPRAKPLP PPPPPPACPE RALAAFGPGG VKRRGGEGRG RRDDDGPRSR AGEQEEEEED PGDAEQEEEE EALLRTEPLL PLGTQRVCLI HPEVKRGPEK PKLTRAEWQV AEAEALVHTL DGWSVVESMV VPSKSSDGKL IFGKGTLEHL TEKIRGTPEI TAVFLNVERL AAPTKKELEA AWGVQVCDRF TVVLHIFRCN ARTKEARLQV ALAELPLLRS RLKTSMALPD RRGWGSRYIM GSGESFVQVQ QRLLKDQEMK IRKALERLRN KRRLLGRQRR RQEFPVISVV GYTNCGKTTL IKALTGDDAV QPRDQLFATL DITAHAGWLP SRVAVIYMDT IGFLSQLPHS LIESFSATLE DVAHSDLIVH VRDMSHPETE LQKASVLSTL RGLRLPAALL DSVLEVHNKV DLVPGYRPAG PQAVAVSALL GQGLPELKAR LEDAVLRATG RQVLTLRVQL AGAQLSWLHQ EATVQDVDVI PEAGVADVTV VISSSAYGRF RKLFPE // ID F1R368_DANRE Unreviewed; 533 AA. AC F1R368; DT 03-MAY-2011, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 2. DT 05-JUL-2017, entry version 47. DE SubName: Full=GTP-binding protein 6 (putative) {ECO:0000313|Ensembl:ENSDARP00000081167}; GN Name=gtpbp6 {ECO:0000313|Ensembl:ENSDARP00000081167, GN ECO:0000313|ZFIN:ZDB-GENE-031118-62}; OS Danio rerio (Zebrafish) (Brachydanio rerio). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes; OC Cyprinidae; Danio. OX NCBI_TaxID=7955 {ECO:0000313|Ensembl:ENSDARP00000081167, ECO:0000313|Proteomes:UP000000437}; RN [1] {ECO:0000313|Ensembl:ENSDARP00000081167} RP IDENTIFICATION. RC STRAIN=Tuebingen {ECO:0000313|Ensembl:ENSDARP00000081167}; RG Ensembl; RL Submitted (JUN-2011) to UniProtKB. RN [2] {ECO:0000313|Ensembl:ENSDARP00000081167, ECO:0000313|Proteomes:UP000000437} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Tuebingen {ECO:0000313|Ensembl:ENSDARP00000081167, RC ECO:0000313|Proteomes:UP000000437}; RX PubMed=23594743; DOI=10.1038/nature12111; RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., RA Muffato M., Collins J.E., Humphray S., McLaren K., Matthews L., RA McLaren S., Sealy I., Caccamo M., Churcher C., Scott C., Barrett J.C., RA Koch R., Rauch G.J., White S., Chow W., Kilian B., Quintais L.T., RA Guerra-Assuncao J.A., Zhou Y., Gu Y., Yen J., Vogel J.H., Eyre T., RA Redmond S., Banerjee R., Chi J., Fu B., Langley E., Maguire S.F., RA Laird G.K., Lloyd D., Kenyon E., Donaldson S., Sehra H., RA Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M., RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J., RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G., RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P., RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., RA Clark S., Pelan S., Griffiths G., Smith M., Glithero R., Howden P., RA Barker N., Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., RA Lovell J., Beasley H., Henderson C., Gordon D., Auger K., Wright D., RA Collins J., Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., RA Leongamornlert D., McGuire S., Gilderthorp R., Griffiths C., RA Manthravadi D., Nichol S., Barker G., Whitehead S., Kay M., Brown J., RA Murnane C., Gray E., Humphries M., Sycamore N., Barker D., RA Saunders D., Wallis J., Babbage A., Hammond S., RA Mashreghi-Mohammadi M., Barr L., Martin S., Wray P., Ellington A., RA Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J., RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E., RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., RA Bird C., Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., RA Eser C., Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., RA Konantz M., Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., RA Raddatz G., Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., RA Yang F., Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., RA Searle S.M., Enright A., Geisler R., Plasterk R.H., Lee C., RA Westerfield M., de Jong P.J., Zon L.I., Postlethwait J.H., RA Nusslein-Volhard C., Hubbard T.J., Roest Crollius H., Rogers J., RA Stemple D.L.; RT "The zebrafish reference genome sequence and its relationship to the RT human genome."; RL Nature 496:498-503(2013). CC -!- CAUTION: The sequence shown here is derived from an Ensembl CC automatic analysis pipeline and should be considered as CC preliminary data. {ECO:0000313|Ensembl:ENSDARP00000081167}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BX323016; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BX324166; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR RefSeq; XP_009300799.1; XM_009302524.2. DR UniGene; Dr.106694; -. DR UniGene; Dr.79040; -. DR PaxDb; F1R368; -. DR Ensembl; ENSDART00000086732; ENSDARP00000081167; ENSDARG00000061091. DR GeneID; 563225; -. DR KEGG; dre:563225; -. DR CTD; 8225; -. DR ZFIN; ZDB-GENE-031118-62; gtpbp6. DR eggNOG; KOG0410; Eukaryota. DR eggNOG; COG2262; LUCA. DR GeneTree; ENSGT00390000001397; -. DR InParanoid; F1R368; -. DR TreeFam; TF315022; -. DR Proteomes; UP000000437; Chromosome 6. DR Bgee; ENSDARG00000061091; -. DR ExpressionAtlas; F1R368; baseline. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR CDD; cd01878; HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 1: Evidence at protein level; KW Complete proteome {ECO:0000313|Proteomes:UP000000437}; KW Proteomics identification {ECO:0000213|PeptideAtlas:F1R368}; KW Reference proteome {ECO:0000313|Proteomes:UP000000437}. FT DOMAIN 310 474 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 533 AA; 60307 MW; 7D9747D9821020EF CRC64; MNLNKISVLT RHVFLCKHVL SRSYVRFAKC EVVRFPQCAS KLIVNTLPSQ SLKPGLVVPV LPARTLSLTA RMFKYDNTDD NNVEEDEIDD AEIEKLFQEQ IPSGIGKEDH RVFIVHPDVK WGSRKQYLTT AALQMEEAVG LVKTLHKWSV VDKLILSTKT PEKKRIFGKG NFQMLTEKIR ATPGVTAVFV NVERLSPSSE KDLEEAWGVK VLDRYSLVLH IFRCNAKTKE AKLQISLAEI PLFRSRLRNE VANLDQQGGG PRYIMGSGET LYEMQQRLLK ERELKIRSAL ERLRRKRNLL RSQRKHKDFP IISVMGYTNC GKTTLIKALT GDDGLQPKDQ LFATLDVTVH AGQLPCHMTV LYVDTIGFLS QLPHQLIDSF SATLEDVIHS DLIIHVRDIS HPETVSQKVN VLNVLNNLQI PERLLTSIIE VHNKIDLIEG YESSDPEVIP ISALKQCGLE ALKEKIEEAV LKCTGKQMMT LKVQLNTSQL SWLYKEATVQ AVDNVGDDCT ANVKVIISQA AYGRYRKLFQ VTS // ID F1T516_9ACTN Unreviewed; 461 AA. AC F1T516; DT 31-MAY-2011, integrated into UniProtKB/TrEMBL. DT 31-MAY-2011, sequence version 1. DT 07-JUN-2017, entry version 39. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:EGF23782.1}; GN ORFNames=HMPREF0091_10729 {ECO:0000313|EMBL:EGF23782.1}; OS Atopobium vaginae DSM 15829. OC Bacteria; Actinobacteria; Coriobacteriia; Coriobacteriales; OC Atopobiaceae; Atopobium. OX NCBI_TaxID=525256 {ECO:0000313|EMBL:EGF23782.1, ECO:0000313|Proteomes:UP000005947}; RN [1] {ECO:0000313|EMBL:EGF23782.1, ECO:0000313|Proteomes:UP000005947} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 15829 {ECO:0000313|EMBL:EGF23782.1, RC ECO:0000313|Proteomes:UP000005947}; RA Muzny D., Qin X., Buhay C., Dugan-Rocha S., Ding Y., Chen G., RA Hawes A., Holder M., Jhangiani S., Johnson A., Khan Z., Li Z., Liu W., RA Liu X., Perez L., Shen H., Wang Q., Watt J., Xi L., Xin Y., Zhou J., RA Deng J., Jiang H., Liu Y., Qu J., Song X.-Z., Zhang L., Villasana D., RA Johnson A., Liu J., Liyanage D., Lorensuhewa L., Robinson T., Song A., RA Song B.-B., Dinh H., Thornton R., Coyle M., Francisco L., Jackson L., RA Javaid M., Korchina V., Kovar C., Mata R., Mathew T., Ngo R., RA Nguyen L., Nguyen N., Okwuonu G., Ongeri F., Pham C., Simmons D., RA Wilczek-Boney K., Hale W., Jakkamsetti A., Pham P., Ruth R., RA San Lucas F., Warren J., Zhang J., Zhao Z., Zhou C., Zhu D., Lee S., RA Bess C., Blankenburg K., Forbes L., Fu Q., Gubbala S., Hirani K., RA Jayaseelan J.C., Lara F., Munidasa M., Palculict T., Patil S., RA Pu L.-L., Saada N., Tang L., Weissenberger G., Zhu Y., Hemphill L., RA Shang Y., Youmans B., Ayvaz T., Ross M., Santibanez J., Aqrawi P., RA Gross S., Joshi V., Fowler G., Nazareth L., Reid J., Worley K., RA Petrosino J., Highlander S., Gibbs R.; RL Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EGF23782.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACGK02000001; EGF23782.1; -; Genomic_DNA. DR RefSeq; WP_006302911.1; NZ_ADNA01000008.1. DR ProteinModelPortal; F1T516; -. DR STRING; 525256.AvagD15_010100000167; -. DR EnsemblBacteria; EGF23782; EGF23782; HMPREF0091_10729. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000005947; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000005947}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000005947}. FT DOMAIN 212 336 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 461 AA; 51041 MW; 67F0C2C721135C00 CRC64; MARFSFYNPH ENSSRALVVA VETPSAACDF TTQESLSELS HLAETLNITT VGKLVQKLVA PVHSTYIGSG KLLELKHMAQ SLMCDFIIFD DELSPSQQSN ICHAVGKSFQ VIDRCSLILD IFAAHATTKE GKLQVKLAHM QYMLPRLKGM WSHLLGEQTR GGIGSRFGQG ESQLEIDRRL SREKIAHVKQ QLAALEIQRK VQRSIRSSSP LYKIALVGYT NAGKSTLLNR ISHSSTYVKD ELFATLDSTT RSITLPDTRR AVLSDTVGFI QKLPTELIDA FKSTLLDVVS ADLLLCVVDV SSAHAEKEMN VVLSILNDIG AGSIPYLIVA NKIDRIASNS YAHASEHEVS PCVEYLTPSN SSSAHTQPNE LALFNSIDPT NVAYISAETG QGIETLLQMI SHKLMSQETY MVLHVAYKDS SFISLIHTYG RVVHETYDEQ GTQLCVYVPR KLVERLKPFE L // ID F1VX34_9BURK Unreviewed; 373 AA. AC F1VX34; DT 31-MAY-2011, integrated into UniProtKB/TrEMBL. DT 31-MAY-2011, sequence version 1. DT 07-JUN-2017, entry version 39. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=IMCC9480_1796 {ECO:0000313|EMBL:EGF32838.1}; OS Oxalobacteraceae bacterium IMCC9480. OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Oxalobacteraceae. OX NCBI_TaxID=937450 {ECO:0000313|EMBL:EGF32838.1, ECO:0000313|Proteomes:UP000004494}; RN [1] {ECO:0000313|EMBL:EGF32838.1, ECO:0000313|Proteomes:UP000004494} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=IMCC9480 {ECO:0000313|EMBL:EGF32838.1, RC ECO:0000313|Proteomes:UP000004494}; RX PubMed=21572000; DOI=10.1128/JB.05088-11; RA Oh H.M., Lee K., Jang Y., Kang I., Kim H.J., Kang T.W., Kim S.Y., RA Cho J.C.; RT "Genome sequence of strain IMCC9480, a xanthorhodopsin-bearing RT betaproteobacterium isolated from the Arctic Ocean."; RL J. Bacteriol. 193:3421-3421(2011). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EGF32838.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AEPR01000155; EGF32838.1; -; Genomic_DNA. DR RefSeq; WP_009665449.1; NZ_AEPR01000155.1. DR ProteinModelPortal; F1VX34; -. DR EnsemblBacteria; EGF32838; EGF32838; IMCC9480_1796. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000004494; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000004494}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000004494}. FT DOMAIN 190 356 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 156 183 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 373 AA; 40812 MW; 900920792615AA36 CRC64; MRAALVGVDF GKGDFVASLE ELALLAKSAG AIPVTRITCK RSSPDAAFFV GSGKASEIGD AVIDDELELV IFNHALTPAQ QRNLERHMKV RVIDRTSLIL DIFAQRAQSH VGKVQVELAQ LQHLATRLIR GWTHLERQKG GIGLRGPGET QLETDRRLLG ERVKALRAKL DKLQQQHATQ RRARGRGQVF SVSLVGYTNA GKSTLFNTMC KARVYAADQL FATLDTTSRR VYMGDAGNVV LSDTVGFIRE LPHQLVAAFR ATLEETVHAD LLLHVVDAAS PNRMEQIEQV NNVLKEIGAD HIPQILVWNK IDAAGLEPAL ERDEYDKIRR VFVSAQSGLG VDLLRSAIGE IAKSSRGVTP GEDPVILPCD APV // ID F1Z9Y5_9SPHN Unreviewed; 448 AA. AC F1Z9Y5; DT 31-MAY-2011, integrated into UniProtKB/TrEMBL. DT 31-MAY-2011, sequence version 1. DT 07-JUN-2017, entry version 38. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=Y88_0664 {ECO:0000313|EMBL:EGD58607.1}; OS Novosphingobium nitrogenifigens DSM 19370. OC Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales; OC Sphingomonadaceae; Novosphingobium. OX NCBI_TaxID=983920 {ECO:0000313|EMBL:EGD58607.1, ECO:0000313|Proteomes:UP000004728}; RN [1] {ECO:0000313|EMBL:EGD58607.1, ECO:0000313|Proteomes:UP000004728} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 19370 {ECO:0000313|EMBL:EGD58607.1, RC ECO:0000313|Proteomes:UP000004728}; RX PubMed=22156397; DOI=10.1128/JB.06381-11; RA Strabala T.J., Macdonald L., Liu V., Smit A.M.; RT "Draft Genome Sequence of Novosphingobium nitrogenifigens Y88T."; RL J. Bacteriol. 194:201-201(2012). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EGD58607.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AEWJ01000041; EGD58607.1; -; Genomic_DNA. DR RefSeq; WP_008066504.1; NZ_GL876926.1. DR ProteinModelPortal; F1Z9Y5; -. DR STRING; 983920.Y88_0664; -. DR EnsemblBacteria; EGD58607; EGD58607; Y88_0664. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000004728; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000004728}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000004728}. FT DOMAIN 216 392 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 448 AA; 48968 MW; 3356E3D8FD2CE88C CRC64; MSGFEFGRNP DDLKGEVTHG AKALVVLPDL RQRGGLGVDA EARLDEGQGL ARAIGIVVVD AFILPIRAVR PATLFGEGQV DKIAVACEQS DAELVIVDGA LSAIQQRNLE DRLKRKVIDR TGLILEIFGE RAATAEGRLQ VELAHLDYQA GRLVRSWTHL ERQRGGFGFL GGPGETQIEA DRRLIRGRMA RIRRELEQVR RTRGLHRERR QRAPWPIIAL VGYTNAGKST LFNRLTGATV MAEDLLFATL DPTMRAIRLP GVDKAILSDT VGFISDLPTQ LVAAFRATLE EVTAADVIVH VRDVANPASA QQKREVEDIL TDLGVIGEEG TSIPIVEAWN KIDLLAPDER ALREDLITHG VPDRPVVPIS AATGEGVDAL VERLGTMLTG GAQTLEITVP MAEGQKLAWL HAHGEILSEH EIEDAEGLPA SRIRVRLTPR ELGRFARL // ID F2AAR8_RHIET Unreviewed; 441 AA. AC F2AAR8; DT 31-MAY-2011, integrated into UniProtKB/TrEMBL. DT 31-MAY-2011, sequence version 1. DT 07-JUN-2017, entry version 41. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=RHECNPAF_3040022 {ECO:0000313|EMBL:EGE58458.1}; OS Rhizobium etli CNPAF512. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium. OX NCBI_TaxID=993047 {ECO:0000313|EMBL:EGE58458.1, ECO:0000313|Proteomes:UP000003712}; RN [1] {ECO:0000313|EMBL:EGE58458.1, ECO:0000313|Proteomes:UP000003712} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CNPAF512 {ECO:0000313|EMBL:EGE58458.1, RC ECO:0000313|Proteomes:UP000003712}; RX PubMed=21515775; DOI=10.1128/JB.00310-11; RA Fauvart M., Sanchez-Rodriguez A., Beullens S., Marchal K., RA Michiels J.; RT "Genome sequence of Rhizobium etli CNPAF512, a nitrogen-fixing RT symbiont isolated from bean root nodules in Brazil."; RL J. Bacteriol. 193:3158-3159(2011). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EGE58458.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AEYZ01000193; EGE58458.1; -; Genomic_DNA. DR RefSeq; WP_004674827.1; NZ_AEYZ01000193.1. DR ProteinModelPortal; F2AAR8; -. DR EnsemblBacteria; EGE58458; EGE58458; RHECNPAF_3040022. DR PATRIC; fig|993047.3.peg.3282; -. DR Proteomes; UP000003712; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000003712}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}. FT DOMAIN 203 375 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 162 196 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 441 AA; 48848 MW; CBE6919AE6306229 CRC64; MRATVVVPVL KSRSRGGQTE SASTRTPESR LEEATGLAQA IDLDVVNGQV VPVNDPRPAT LLGTGKIEEI KALLDERDSG LVIVDHPLTP VQQRNLEKEW NAKVIDRTGL ILEIFGRRAS TKEGTLQVDL AHLNYQKGRL VRSWTHLERQ RGGGGFMGGP GETQIEADRR LLQDRIIKLE RELEQVVRTR QLHRAKRRKV PHPIVALVGY TNAGKSTLFN RITGAGVLAE DMLFATLDPT LRRMKLPHGR TVILSDTVGF ISDLPTHLVA AFRATLEEVL EADLILHVRD MSDPDNQAQS SDVMRILGDL GIDEAEAGKR LIEVWNKIDR LEPEVHDAMV QKAAGASNVV AVSAVSGEGV DTLMDEISRR LSGVMTETTI RLPVDKLALL PWLYDHAIVD GREDNEDGSI TLDLRLSETE AAELERRIGN GPKPPREDWE R // ID F2BCX1_9NEIS Unreviewed; 392 AA. AC F2BCX1; DT 31-MAY-2011, integrated into UniProtKB/TrEMBL. DT 31-MAY-2011, sequence version 1. DT 07-JUN-2017, entry version 37. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:EGF10720.1}; GN ORFNames=HMPREF9123_1601 {ECO:0000313|EMBL:EGF10720.1}; OS Neisseria bacilliformis ATCC BAA-1200. OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=888742 {ECO:0000313|EMBL:EGF10720.1, ECO:0000313|Proteomes:UP000004105}; RN [1] {ECO:0000313|EMBL:EGF10720.1, ECO:0000313|Proteomes:UP000004105} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-1200 {ECO:0000313|EMBL:EGF10720.1, RC ECO:0000313|Proteomes:UP000004105}; RA Muzny D., Qin X., Deng J., Jiang H., Liu Y., Qu J., Song X.-Z., RA Zhang L., Thornton R., Coyle M., Francisco L., Jackson L., Javaid M., RA Korchina V., Kovar C., Mata R., Mathew T., Ngo R., Nguyen L., RA Nguyen N., Okwuonu G., Ongeri F., Pham C., Simmons D., RA Wilczek-Boney K., Hale W., Jakkamsetti A., Pham P., Ruth R., RA San Lucas F., Warren J., Zhang J., Zhao Z., Zhou C., Zhu D., Lee S., RA Bess C., Blankenburg K., Forbes L., Fu Q., Gubbala S., Hirani K., RA Jayaseelan J.C., Lara F., Munidasa M., Palculict T., Patil S., RA Pu L.-L., Saada N., Tang L., Weissenberger G., Zhu Y., Hemphill L., RA Shang Y., Youmans B., Ayvaz T., Ross M., Santibanez J., Aqrawi P., RA Gross S., Joshi V., Fowler G., Nazareth L., Reid J., Worley K., RA Petrosino J., Highlander S., Gibbs R.; RL Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EGF10720.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFAY01000031; EGF10720.1; -; Genomic_DNA. DR ProteinModelPortal; F2BCX1; -. DR STRING; 888742.HMPREF9123_1601; -. DR EnsemblBacteria; EGF10720; EGF10720; HMPREF9123_1601. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000004105; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000004105}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000004105}. FT DOMAIN 212 381 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 392 AA; 42810 MW; E5CC3CA070C0689E CRC64; MSKQPDKSLS KPERIMLVGM MLDADYTGAN ESRERAFAAA MAEAEELVCA TGGELVCRQT AKRDRAHPAL FVGTGKAEEL AQAVSEQQID LAVFNHELTP TQERNLEKAL QCRVLDRVGL ILAIFAQRAQ SQEGRLQVEL AQLTHLSGRL VRGYGHLQSQ KGGIGLKGPG ETQLETDRRL IAQKITALKK RLEAVKRQRA TRRKARQSGS LPTFALAGYT NTGKSSLFNR LTKADVLAKD QLFATLDTTA RRLYLAPGTE VILTDTVGFV RDLPHSLVAA FSATLEETAL ADLILHVIDA SRPDHERQAD DVNRVLEEIG AGDIPRLLVY NKTDLLPADS RPAGLLRRAD GRPAAVSISV KTGAGLEDLR QALTELALSD GLRMRQARQE AV // ID F2F697_SOLSS Unreviewed; 426 AA. AC F2F697; DT 31-MAY-2011, integrated into UniProtKB/TrEMBL. DT 31-MAY-2011, sequence version 1. DT 07-JUN-2017, entry version 40. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:BAK14791.1}; GN OrderedLocusNames=SSIL_0368 {ECO:0000313|EMBL:BAK14791.1}; OS Solibacillus silvestris (strain StLB046) (Bacillus silvestris). OC Bacteria; Firmicutes; Bacilli; Bacillales; Planococcaceae; OC Solibacillus. OX NCBI_TaxID=1002809 {ECO:0000313|EMBL:BAK14791.1, ECO:0000313|Proteomes:UP000006691}; RN [1] {ECO:0000313|Proteomes:UP000006691} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=StLB046 {ECO:0000313|Proteomes:UP000006691}; RA Morohoshi T., Someya N., Ikeda T.; RT "Genome sequence of Solibacillus silvestris StLB046."; RL Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:BAK14791.1, ECO:0000313|Proteomes:UP000006691} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=StLB046 {ECO:0000313|EMBL:BAK14791.1, RC ECO:0000313|Proteomes:UP000006691}; RX PubMed=22019407; DOI=10.1016/j.jbiosc.2011.09.006; RA Morohoshi T., Tominaga Y., Someya N., Ikeda T.; RT "Complete genome sequence and characterization of the N-acylhomoserine RT lactone-degrading gene of the potato leaf-associated Solibacillus RT silvestris."; RL J. Biosci. Bioeng. 113:20-25(2012). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AP012157; BAK14791.1; -; Genomic_DNA. DR RefSeq; WP_008405847.1; NC_018065.1. DR EnsemblBacteria; BAK14791; BAK14791; SSIL_0368. DR KEGG; siv:SSIL_0368; -. DR PATRIC; fig|1002809.3.peg.371; -. DR KO; K03665; -. DR OMA; FNNHAHV; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000006691; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000006691}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000006691}. FT DOMAIN 203 371 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 162 196 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 426 AA; 48537 MW; 6E682D310BBE7582 CRC64; MKDVEVLIER GVLVGVNLQK DEHFDYSMEE LANLAQALDV EVVGMVTQNL ERVTPSHYVG TGKIEEIKAF FDETDANIVI FNDELSPSQI RNLERDLQCK VIDRTMLILD IFSRRAKTRE AQLQVELAQL QYMLPRLVGL HASLSRQGGG TGGGFKNRGA GETKLELDRR KIEDQISKIK KELEVVKEQR ETQRKQRRKN AVPVVSIVGY TNAGKSTIMN QLLAKAGQDD TKQVFEKDML FATLETSVRN IDLEDNKSFL LTDTVGFVSK LPHHLVKAFR STLEEARESD LLLHVVDVSN EEYRFMMDVT NETLKAIDVE NIPTVYVYNK SDLADVEYPL VSGDNIWLSA KEDVGLEELL QLIRQQIFAN YITCQMLIPY NQGGIVSYLN EQATVLETEY EEEGTLLTLE LKEADYQKYE IYVVKQ // ID F2I4A7_AERUA Unreviewed; 410 AA. AC F2I4A7; DT 31-MAY-2011, integrated into UniProtKB/TrEMBL. DT 31-MAY-2011, sequence version 1. DT 07-JUN-2017, entry version 42. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:AEA00898.1}; GN OrderedLocusNames=HMPREF9243_0845 {ECO:0000313|EMBL:AEA00898.1}; OS Aerococcus urinae (strain ACS-120-V-Col10a). OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Aerococcaceae; OC Aerococcus. OX NCBI_TaxID=866775 {ECO:0000313|EMBL:AEA00898.1, ECO:0000313|Proteomes:UP000008129}; RN [1] {ECO:0000313|Proteomes:UP000008129} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ACS-120-V-Col10a {ECO:0000313|Proteomes:UP000008129}; RA Durkin A.S., Madupu R., Radune D., Hostetler J., Torralba M., RA Gillis M., Methe B., Sutton G., Nelson K.E.; RT "Complete genome sequence of Aerococcus urinae strain ACS-120-V- RT Col10a."; RL Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002512; AEA00898.1; -; Genomic_DNA. DR RefSeq; WP_013669143.1; NC_015278.1. DR ProteinModelPortal; F2I4A7; -. DR STRING; 866775.HMPREF9243_0845; -. DR EnsemblBacteria; AEA00898; AEA00898; HMPREF9243_0845. DR KEGG; aur:HMPREF9243_0845; -. DR PATRIC; fig|866775.3.peg.800; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000008129; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000008129}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000008129}. FT DOMAIN 195 358 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 154 188 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 410 AA; 46472 MW; 8C492D447C293175 CRC64; MPENVLIIGL QLPQTTDLRF TMQMDELAAL VETAGGQVVS RQSQKRDQED ARYLIGSGKV REIHDLAQEL DIDLVIFYQQ LSPSQNRNLQ AAIDCPVIDR VQLILDIFAS RATSKEGKLQ VALAQNEYLL PRLAGMGTVL SRLGGGIGTR GPGETKLEQD RRVLRNEIQK IRHELKEVEK QRELTRERRQ KSGLFKIGLL GYTNAGKSTI INALTDAQTY QADQLFATLT PLTRKFSLPN HFEITLTDTV GFIQDLPPMI IDAFHSTLEE SRNVDLLMIV VDASSPFALE QEEVVNQLLE DLDMQDLPKL YIYNKRDQVE PGQQVLTPSS PHLLISAQDD QDIETLRQAI VDQVKTIYQP FAVQVAPQAA NEWLGWQNRF YIESFEFDKD SESYQIMGYK PDYLPLPKSE // ID F2IK10_FLUTR Unreviewed; 400 AA. AC F2IK10; DT 31-MAY-2011, integrated into UniProtKB/TrEMBL. DT 31-MAY-2011, sequence version 1. DT 07-JUN-2017, entry version 44. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Fluta_0908 {ECO:0000313|EMBL:AEA42909.1}; OS Fluviicola taffensis (strain DSM 16823 / NCIMB 13979 / RW262). OC Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales; OC Crocinitomicaceae; Fluviicola. OX NCBI_TaxID=755732 {ECO:0000313|EMBL:AEA42909.1, ECO:0000313|Proteomes:UP000007463}; RN [1] {ECO:0000313|Proteomes:UP000007463} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 16823 / RW262 / RW262 {ECO:0000313|Proteomes:UP000007463}; RG US DOE Joint Genome Institute (JGI-PGF); RA Lucas S., Copeland A., Lapidus A., Bruce D., Goodwin L., Pitluck S., RA Kyrpides N., Mavromatis K., Ivanova N., Mikhailova N., Pagani I., RA Chertkov O., Detter J.C., Han C., Tapia R., Land M., Hauser L., RA Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Tindall B., RA Pomrenke H.G., Brambilla E., Klenk H.-P., Eisen J.A.; RT "The complete genome of Fluviicola taffensis DSM 16823."; RL Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002542; AEA42909.1; -; Genomic_DNA. DR RefSeq; WP_013685681.1; NC_015321.1. DR ProteinModelPortal; F2IK10; -. DR STRING; 755732.Fluta_0908; -. DR EnsemblBacteria; AEA42909; AEA42909; Fluta_0908. DR KEGG; fte:Fluta_0908; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000007463; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000007463}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Hydrolase {ECO:0000313|EMBL:AEA42909.1}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000007463}. FT DOMAIN 203 389 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 400 AA; 45794 MW; 4F2E636BD0D28270 CRC64; MDEGHVLVDA VEETCVLVGI ITSTVTDEQA HEYLDELEFL AETAGATSVK RFTQKLPMAN PRTFVGTGKL EEIKEYVKEN GVELVIFDDE LSPSQLRNIE RELECKILDR NILILDIFAS RARTSHAKTQ VELAQMQYML PRLKRLWTHL ERQKGGIGLR GPGESQIETD RRIIQTRIAL LKEKLKEIDK QMSVQRGNRG QLVRVALVGY TNVGKSTMMN MLSKSEVFAE NKLFATLDTT VRKVVIENLP FLLTDTVGFI RKLPHQLVES FKSTLDEVRE ADLLIHVVDI SHPNFEDQLN IVNETLAELD NKDKPMILVF NKIDAYKHNP GIDSDGNLEE ESANMTLEEL KRTWMNRLPA TKCVFISATD KDNVEELKET MYSEIKRIFA VRYPHNNFLY // ID F2J0N7_POLGS Unreviewed; 458 AA. AC F2J0N7; DT 31-MAY-2011, integrated into UniProtKB/TrEMBL. DT 31-MAY-2011, sequence version 1. DT 07-JUN-2017, entry version 43. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=SL003B_2298 {ECO:0000313|EMBL:ADZ70723.1}; OS Polymorphum gilvum (strain LMG 25793 / CGMCC 1.9160 / SL003B-26A1). OC Bacteria; Proteobacteria; Alphaproteobacteria; Polymorphum. OX NCBI_TaxID=991905 {ECO:0000313|EMBL:ADZ70723.1, ECO:0000313|Proteomes:UP000008130}; RN [1] {ECO:0000313|EMBL:ADZ70723.1, ECO:0000313|Proteomes:UP000008130} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=LMG 25793 / CGMCC 1.9160 / SL003B-26A1 RC {ECO:0000313|Proteomes:UP000008130}; RX PubMed=21478361; DOI=10.1128/JB.00333-11; RA Li S.G., Tang Y.Q., Nie Y., Cai M., Wu X.L.; RT "Complete genome sequence of Polymorphum gilvum SL003B-26A1T, a crude RT oil-degrading bacterium from oil-polluted saline soil."; RL J. Bacteriol. 193:2894-2895(2011). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002568; ADZ70723.1; -; Genomic_DNA. DR ProteinModelPortal; F2J0N7; -. DR STRING; 991905.SL003B_2298; -. DR EnsemblBacteria; ADZ70723; ADZ70723; SL003B_2298. DR KEGG; pgv:SL003B_2298; -. DR PATRIC; fig|991905.3.peg.2354; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000008130; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000008130}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000008130}. FT DOMAIN 230 400 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 189 223 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 458 AA; 49875 MW; 227270482C82D91A CRC64; MAQGSRKGDP SSAPDDGAPT GDEGGGARAL VVEPVLPDRP ARTHEPEILV GRSPEARLEE AIGLCAAIDL TIVAALIVKI SAPRPATLLG TGKVEDLAAQ VEAEEVDVVV VDHALTPIQQ RNLERALKTK VIDRTGLILE IFGARARTKE GRLQVDLAHL TWQKSRLVRS WTHLERQRGG VGFMGGPGET QIEADRRQIQ DKIMRLEKEL DQVRRTRDLH RKKRKKIPQP VVALVGYTNA GKSTLFNRLT EAQVLAKDLL FATLDPTLRR IKLPHGREVI LSDTVGFISE LPTHLVAAFR ATLEEVLEAD LILHVRDIAH PDTDAQAADV ARTLEDLGVG PTTGAPIVEV WNKIDCLDAE RRARLLAGQT DSGPVALSAL TGEGIGALLA RIEAFMAQGD DTFELALPVE EGELLAGLYQ IGEVLAREDG ETGIILRVRV SDKQKGPFRE RYKAFIDG // ID F2JRI8_CELLD Unreviewed; 418 AA. AC F2JRI8; DT 31-MAY-2011, integrated into UniProtKB/TrEMBL. DT 31-MAY-2011, sequence version 1. DT 07-JUN-2017, entry version 42. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Clole_2196 {ECO:0000313|EMBL:ADZ83909.1}; OS Cellulosilyticum lentocellum (strain ATCC 49066 / DSM 5427 / NCIMB OS 11756 / RHM5) (Clostridium lentocellum). OC Bacteria; Firmicutes; Clostridia; Clostridiales; Lachnospiraceae; OC Cellulosilyticum. OX NCBI_TaxID=642492 {ECO:0000313|EMBL:ADZ83909.1, ECO:0000313|Proteomes:UP000008467}; RN [1] {ECO:0000313|EMBL:ADZ83909.1, ECO:0000313|Proteomes:UP000008467} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 49066 / DSM 5427 / NCIMB 11756 / RHM5 RC {ECO:0000313|Proteomes:UP000008467}; RX PubMed=21398547; DOI=10.1128/JB.00239-11; RG US DOE Joint Genome Institute; RA Miller D.A., Suen G., Bruce D., Copeland A., Cheng J.F., Detter C., RA Goodwin L.A., Han C.S., Hauser L.J., Land M.L., Lapidus A., Lucas S., RA Meincke L., Pitluck S., Tapia R., Teshima H., Woyke T., Fox B.G., RA Angert E.R., Currie C.R.; RT "Complete genome sequence of the cellulose-degrading bacterium RT Cellulosilyticum lentocellum."; RL J. Bacteriol. 193:2357-2358(2011). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002582; ADZ83909.1; -; Genomic_DNA. DR RefSeq; WP_013657203.1; NC_015275.1. DR ProteinModelPortal; F2JRI8; -. DR STRING; 642492.Clole_2196; -. DR EnsemblBacteria; ADZ83909; ADZ83909; Clole_2196. DR KEGG; cle:Clole_2196; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000008467; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000008467}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000008467}. FT DOMAIN 201 364 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 160 194 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 418 AA; 47430 MW; 75536654ACDB3084 CRC64; MITHKEQIER LILVAAQKKQ YKEEEAWESL DELAELVKTA GGEVITQVLQ RLDHINPGFY IGSGKVEEIK EMAQLHGATG IVFDDELSPI QMRNLAEALQ IKVMDRTMVI LDIFASRALS KEGKLQVEMA QLKYQSSRLI GFGTMLSRQA GGIGSRGPGE KKLELDKRHL KVRMEILQAE LAEVEKHRQL IRSRRDKNNT PVVAIVGYTN AGKSTLLNQL SGSDVYVQNQ LFATLDPTTR GITLPSGSEI LLTDTVGFIR KLPHHLVKAF YSTLEEAKYA DIILHVMDVS SPHLETHQQV VYETLSRLQI SDIPIVAVYN KIDTHVEDYP KDEHATYETY ISAKEGIGCE HLLSVLEEIL YSNMQAFDID VPYTNQDIVR YCHEYGERLE EEYTNEGVKV KGYMPKDKFY KIEAYILS // ID F2JWL5_MARM1 Unreviewed; 429 AA. AC F2JWL5; DT 31-MAY-2011, integrated into UniProtKB/TrEMBL. DT 31-MAY-2011, sequence version 1. DT 30-AUG-2017, entry version 42. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Marme_2547 {ECO:0000313|EMBL:ADZ91779.1}; OS Marinomonas mediterranea (strain ATCC 700492 / JCM 21426 / NBRC 103028 OS / MMB-1). OC Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales; OC Marinomonas. OX NCBI_TaxID=717774 {ECO:0000313|EMBL:ADZ91779.1, ECO:0000313|Proteomes:UP000001062}; RN [1] {ECO:0000313|Proteomes:UP000001062} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700492 / JCM 21426 / NBRC 103028 / MMB-1 RC {ECO:0000313|Proteomes:UP000001062}; RG US DOE Joint Genome Institute; RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L., RA Pitluck S., Teshima H., Detter J.C., Han C., Tapia R., Land M., RA Hauser L., Kyrpides N., Ivanova N., Ovchinnikova G., Pagani I., RA Lucas-Elio P., Johnston A.W.B., Sanchez-Amat A., Woyke T.; RT "Complete sequence of Marinomonas mediterranea MMB-1."; RL Submitted (MAR-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002583; ADZ91779.1; -; Genomic_DNA. DR RefSeq; WP_013661683.1; NC_015276.1. DR ProteinModelPortal; F2JWL5; -. DR STRING; 717774.Marme_2547; -. DR EnsemblBacteria; ADZ91779; ADZ91779; Marme_2547. DR KEGG; mme:Marme_2547; -. DR PATRIC; fig|717774.3.peg.2632; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000001062; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000001062}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000001062}. FT DOMAIN 199 366 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 165 192 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 429 AA; 48065 MW; 57CB3669461965FD CRC64; MFFERPDSGE IAVLVHIDFY DQAEKYGPEE FIELSISAGA DPVAVVVGSR QRPDPKYFIG SGKLEEIKDI VLREEAQVVL FDHALSPSQE RNLEAHLNCR VLDRTGLILD IFAQRARTHE GKLQVELAQL QHMSTRLIRG WTHLERQKGG IGMRGPGETQ LETDRRLLRE RIKTIQKRLD KVNSQRDQSR RSRSRSAMPT VSLVGYTNAG KSTLFNKATG AEVYAADQLF ATLDPTLRRL EVEQIGSVVL ADTVGFIRQL PHRLVKAFQA TLKESSEADL LLHVIDCADI ARDDNIKEVD AVLEEIGASE VPTLKVFNKI DALATGEPRI DRDENGKPYR VWVSAKEGLG IDLLQQSIAE LVGEDIINDK LIISSDQGRF RAMLFEQGAV RSEEYDEHGR SVLEVSLPKK DFMQLLARAG ISEEQVMAA // ID F2LCM9_BURGS Unreviewed; 400 AA. AC F2LCM9; DT 31-MAY-2011, integrated into UniProtKB/TrEMBL. DT 31-MAY-2011, sequence version 1. DT 07-JUN-2017, entry version 48. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=bgla_1g22830 {ECO:0000313|EMBL:AEA60910.1}; OS Burkholderia gladioli (strain BSR3). OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Burkholderia. OX NCBI_TaxID=999541 {ECO:0000313|EMBL:AEA60910.1, ECO:0000313|Proteomes:UP000008316}; RN [1] {ECO:0000313|EMBL:AEA60910.1, ECO:0000313|Proteomes:UP000008316} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BSR3 {ECO:0000313|EMBL:AEA60910.1, RC ECO:0000313|Proteomes:UP000008316}; RX PubMed=21478339; DOI=10.1128/JB.00420-11; RA Seo Y.S., Lim J., Choi B.S., Kim H., Goo E., Lee B., Lim J.S., RA Choi I.Y., Moon J.S., Kim J., Hwang I.; RT "Complete genome sequence of Burkholderia gladioli BSR3."; RL J. Bacteriol. 193:3149-3149(2011). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002599; AEA60910.1; -; Genomic_DNA. DR RefSeq; WP_013698241.1; NC_015381.1. DR ProteinModelPortal; F2LCM9; -. DR STRING; 999541.bgla_1g22830; -. DR EnsemblBacteria; AEA60910; AEA60910; bgla_1g22830. DR KEGG; bgd:bgla_1g22830; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000008316; Chromosome 1. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000008316}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}. FT DOMAIN 196 367 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 162 189 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 400 AA; 44131 MW; BD240216EAF9B5BA CRC64; MTPDNLINAA LVGIDFGKTD FEASLEELSL LASSAGARPA VTLTGRRSSP DAAMFIGSGK AEELRLACDA NDVDIVIFNH PLAPAQQRNL ERTLNRRVVD RTSLILDIFA QRARSHEGKL QVELAQLQYL STRLIRAWTH LERQKGGIGL RGPGETQLET DRRLIGERIK MLKSRLDKLR RQHNTQRRQR ERNRTMSMSL VGYTNAGKST LFNALTKAQA YAADQLFATL DTTSRRVYIG DEVGQIVVSD TVGFIRELPH QLVAAFRATL EETIHADLLL HVVDASSAVR LEQIEQVNDV LHEIGADAIR QVLVFNKIDA VPELAARGDA VERDEYGNIS RVFLSARTGQ GLDTLRAAIA EIASSDALAG TGLLPERDVR FDGNGLTEPH DDHTVSEHGH // ID F2N7X3_CORGP Unreviewed; 443 AA. AC F2N7X3; DT 31-MAY-2011, integrated into UniProtKB/TrEMBL. DT 31-MAY-2011, sequence version 1. DT 07-JUN-2017, entry version 43. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Corgl_0974 {ECO:0000313|EMBL:AEB07082.1}; OS Coriobacterium glomerans (strain ATCC 49209 / DSM 20642 / JCM 10262 / OS PW2). OC Bacteria; Actinobacteria; Coriobacteriia; Coriobacteriales; OC Coriobacteriaceae; Coriobacterium. OX NCBI_TaxID=700015 {ECO:0000313|EMBL:AEB07082.1, ECO:0000313|Proteomes:UP000006851}; RN [1] {ECO:0000313|Proteomes:UP000006851} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 49209 / DSM 20642 / JCM 10262 / PW2 RC {ECO:0000313|Proteomes:UP000006851}; RX PubMed=23961308; DOI=10.4056/sigs.3507020; RA Stackebrandt E., Zeytun A., Lapidus A., Nolan M., Lucas S., Hammon N., RA Deshpande S., Cheng J.F., Tapia R., Goodwin L.A., Pitluck S., RA Liolios K., Pagani I., Ivanova N., Mavromatis K., Mikhailova N., RA Huntemann M., Pati A., Chen A., Palaniappan K., Chang Y.J., Land M., RA Hauser L., Rohde M., Pukall R., Goker M., Detter J.C., Woyke T., RA Bristow J., Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., RA Klenk H.P.; RT "Complete genome sequence of Coriobacterium glomerans type strain RT (PW2(T)) from the midgut of Pyrrhocoris apterus L. (red soldier RT bug)."; RL Stand. Genomic Sci. 8:15-25(2013). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002628; AEB07082.1; -; Genomic_DNA. DR RefSeq; WP_013708825.1; NC_015389.1. DR ProteinModelPortal; F2N7X3; -. DR STRING; 700015.Corgl_0974; -. DR EnsemblBacteria; AEB07082; AEB07082; Corgl_0974. DR KEGG; cgo:Corgl_0974; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000006851; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000006851}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Hydrolase {ECO:0000313|EMBL:AEB07082.1}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000006851}. FT DOMAIN 210 375 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 443 AA; 49411 MW; EDB5BD78689F8017 CRC64; MTHFRPVSTE LIPERALLVG VDLHDGGWPT ESSLDELARL VESAGANPVG RMVQRMARPN PRSMIGSGKL EELKSTVSRL DVDVVIFDED LTPSQQNNIE RAIGASVKII DRTALILDIF GMRAQTREGS IQVQLAQLEY LLPRLRGMWT HLAKEQTRGG IGSRFGQGES QLEVDRRLIR KRISALKRSL LQIETRRDVQ SRARRESPAF RIALAGYTNA GKSTLMNRLT GSDIMSADKL FATLDPTTRA FKLPGGRLCT LTDTVGFIQK LPHGLVDAFK STLAEARDSD IILEVVDASD ENYLRQMSAV DVVLDEIGAS EQRRVTVLNK IDLIDPLDRA DLERRHPDAE LVSSVNGLGI ERLLERLSCE ASTLDSVISL RIPYREAALI SLVHEQGHVL QEVFDEDAVR LVADIPPRVA ERLIRYRDAS TDQLSEPEME KKQ // ID F2NGK7_DESAR Unreviewed; 569 AA. AC F2NGK7; DT 31-MAY-2011, integrated into UniProtKB/TrEMBL. DT 31-MAY-2011, sequence version 1. DT 07-JUN-2017, entry version 44. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Desac_0015 {ECO:0000313|EMBL:AEB07914.1}; OS Desulfobacca acetoxidans (strain ATCC 700848 / DSM 11109 / ASRB2). OC Bacteria; Proteobacteria; Deltaproteobacteria; Syntrophobacterales; OC Syntrophaceae; Desulfobacca. OX NCBI_TaxID=880072 {ECO:0000313|EMBL:AEB07914.1, ECO:0000313|Proteomes:UP000000483}; RN [1] {ECO:0000313|Proteomes:UP000000483} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700848 / DSM 11109 / ASRB2 RC {ECO:0000313|Proteomes:UP000000483}; RG US DOE Joint Genome Institute (JGI-PGF); RA Lucas S., Copeland A., Lapidus A., Bruce D., Goodwin L., Pitluck S., RA Peters L., Kyrpides N., Mavromatis K., Ivanova N., Ovchinnikova G., RA Teshima H., Detter J.C., Han C., Land M., Hauser L., Markowitz V., RA Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Spring S., Schueler E., RA Brambilla E., Klenk H.-P., Eisen J.A.; RT "The complete genome of Desulfobacca acetoxidans DSM 11109."; RL Submitted (MAR-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002629; AEB07914.1; -; Genomic_DNA. DR RefSeq; WP_013705029.1; NC_015388.1. DR STRING; 880072.Desac_0015; -. DR EnsemblBacteria; AEB07914; AEB07914; Desac_0015. DR KEGG; dao:Desac_0015; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR KO; K03665; -. DR OMA; EREVIIT; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000000483; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000000483}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000000483}. FT DOMAIN 378 542 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 337 364 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 569 AA; 64747 MW; 4237EB4C2F4063BD CRC64; MDRVQGNLAG LKPQQLRHLE RLYRRKIPPT SLITPELARQ LTEITGDIKR QVGILVDRQG TVAMVIVGDR KGLVIPPLKR ERQTGWRLKG LRLIHTHLNA EPLNQDDLMD LALLRLDCIA ALETLPSGLP GHLHGAYLLP QRLEGRDWGF ITIDHVAHLD MDFAAFVRSL EEELARAGHS GTEHDRRERA ILIGVTTRPR QTAEDSLLEL RELARTAGLN VVEVILQQRQ RIDPRFLMGR GKLMELVIRA LQMDAELLIF DADLNPSQVR SITDFTELKV IDRTQLILDI FAQRARSREG KLQVEMAQLK YLLPRLGKRD DALSRLTGGI GGRGPGETKL EIDRRRVRER LHRLAQELDQ VRDERRVRRG PRQRQGLPII SIVGYTNAGK STLLNTLTRA EVLAEDRLFA TLDPTSRRLR FPKEREVIIT DTVGFIRDLP KDLLEAFKAT LEELEDADLL LHVIDLSNPR FEEQMETVDT ILASLELSDK PVLKVFNKID LIAPEIAQWQ CRRHNGVAIS ALDGGTLRPL LTRMEEIIDR ILPREQISSA EQDAVAEAMR ERRDTGLLH // ID F2NQB7_MARHT Unreviewed; 549 AA. AC F2NQB7; DT 31-MAY-2011, integrated into UniProtKB/TrEMBL. DT 31-MAY-2011, sequence version 1. DT 07-JUN-2017, entry version 43. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Marky_0898 {ECO:0000313|EMBL:AEB11644.1}; OS Marinithermus hydrothermalis (strain DSM 14884 / JCM 11576 / T1). OC Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; OC Marinithermus. OX NCBI_TaxID=869210 {ECO:0000313|EMBL:AEB11644.1, ECO:0000313|Proteomes:UP000007030}; RN [1] {ECO:0000313|EMBL:AEB11644.1, ECO:0000313|Proteomes:UP000007030} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 14884 / JCM 11576 / T1 {ECO:0000313|Proteomes:UP000007030}; RX PubMed=22675595; DOI=10.4056/sigs.2435521; RA Copeland A., Gu W., Yasawong M., Lapidus A., Lucas S., Deshpande S., RA Pagani I., Tapia R., Cheng J.F., Goodwin L.A., Pitluck S., Liolios K., RA Ivanova N., Mavromatis K., Mikhailova N., Pati A., Chen A., RA Palaniappan K., Land M., Pan C., Brambilla E.M., Rohde M., RA Tindall B.J., Sikorski J., Goker M., Detter J.C., Bristow J., RA Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P., RA Woyke T.; RT "Complete genome sequence of the aerobic, heterotroph Marinithermus RT hydrothermalis type strain (T1(T)) from a deep-sea hydrothermal vent RT chimney."; RL Stand. Genomic Sci. 6:21-30(2012). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002630; AEB11644.1; -; Genomic_DNA. DR RefSeq; WP_013703694.1; NC_015387.1. DR STRING; 869210.Marky_0898; -. DR EnsemblBacteria; AEB11644; AEB11644; Marky_0898. DR KEGG; mhd:Marky_0898; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR KO; K03665; -. DR OMA; EREVIIT; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000007030; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000007030}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000007030}. FT DOMAIN 376 539 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 342 369 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 549 AA; 60939 MW; AE09D94C89DB7468 CRC64; MNKVYGRTNG LKPSARKRLA NLYRRRVPDD RLYTAELART LAQLSYEIHK PISLLLDRRG SVRAVTVGDA REVPIPPMAY VETRLSGYRI LHTHLGGGGL SRPDLSTLFL NRLDAVVALD VAEGRPTNAH LAHLVPPHAE EEDWRVYPAR PYHAYLDWDF GAVLKALEEE LAKAARVREM ADGSGERVIL VGVDRGEGPQ AEVDLVELAE LARTAGGVVV HRELVYRPEL DARYVVGRGK LEELTTVAYH ENAGTLIFGL DLAPAQAREI ETVTQLKVLD RTQLILDIFA QHARTPQAKA QVELAQLRYL LPRLVGRGRE MSRLGGGIGT RGPGETKLEV DRRRIQARIA HLTRDLEKYA QQRREARKAR KRHGLPVIGI VGYTNAGKTT LLQALAKRGE PGENKLFATL RPLTRKGFLP GLGEVLYTDT VGFIRHMPAD LMAAFRATLE ELLDADVLVH VLDVSQEGAL ERHATVEDVL RELGVEQPRV LALNKADRAD PYDVDFVQER LGGLVISATK REGLEALKQA LVQALVARGV RPQAWAQYG // ID F2NWZ8_TRES6 Unreviewed; 439 AA. AC F2NWZ8; DT 31-MAY-2011, integrated into UniProtKB/TrEMBL. DT 31-MAY-2011, sequence version 1. DT 07-JUN-2017, entry version 44. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Tresu_0234 {ECO:0000313|EMBL:AEB13197.1}; OS Treponema succinifaciens (strain ATCC 33096 / DSM 2489 / 6091). OC Bacteria; Spirochaetes; Spirochaetales; Spirochaetaceae; Treponema. OX NCBI_TaxID=869209 {ECO:0000313|EMBL:AEB13197.1, ECO:0000313|Proteomes:UP000006852}; RN [1] {ECO:0000313|Proteomes:UP000006852} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33096 / DSM 2489 / 6091 RC {ECO:0000313|Proteomes:UP000006852}; RA Lucas S., Copeland A., Lapidus A., Bruce D., Goodwin L., Pitluck S., RA Peters L., Kyrpides N., Mavromatis K., Ivanova N., Ovchinnikova G., RA Teshima H., Detter J.C., Tapia R., Han C., Land M., Hauser L., RA Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Gronow S., RA Wellnitz S., Brambilla E., Klenk H.-P., Eisen J.A.; RT "The complete genome of chromosome of Treponema succinifaciens DSM RT 2489."; RL Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002631; AEB13197.1; -; Genomic_DNA. DR ProteinModelPortal; F2NWZ8; -. DR STRING; 869209.Tresu_0234; -. DR EnsemblBacteria; AEB13197; AEB13197; Tresu_0234. DR KEGG; tsu:Tresu_0234; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000006852; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000006852}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000006852}. FT DOMAIN 211 378 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 170 197 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 439 AA; 49355 MW; 00362D7570464736 CRC64; MFILKCIINF MIEIQQEQER KVKCLLVGAP DKKNGNPEPK ELQSLVQTLD MEIAGTIVLT RIEPTPAYGM GTGKAQEIVD KAKEVFADCI VFDWEIDPSK QRNWEKLANM PVFDRNEVII RIFDSRAQTK EASLQVELAK LQYSLPRLSH TYGDMARQRG GSFGNKGSGE TQLELDRRQI EDKIVQIKKE LAQVAINRNI QRKQRERTAT ATCSLVGYTN AGKSSLLNAL TGADVLVENK LFATLDPTTR KFALSEASSV LMTDTVGFIS NLPHTLIDAF KSTLEETSLS DFLLIVVDAS DPDCEKQYQQ VQKVLKEIHA EEIPQTVVLN KFDLVKEKFI TVSQLNKAFP NAIHASAKTE LGFEEIISVL TENLLGTKRK FKIPMEKADL VELARKNGTI EKEEWLENFI ELTARIPGTF DETGNATTRT LSLLKEFIV // ID F2R7U8_STRVP Unreviewed; 497 AA. AC F2R7U8; DT 31-MAY-2011, integrated into UniProtKB/TrEMBL. DT 31-MAY-2011, sequence version 1. DT 07-JUN-2017, entry version 43. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=SVEN_5471 {ECO:0000313|EMBL:CCA58757.1}; OS Streptomyces venezuelae (strain ATCC 10712 / CBS 650.69 / DSM 40230 / OS JCM 4526 / NBRC 13096 / PD 04745). OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae; OC Streptomyces. OX NCBI_TaxID=953739 {ECO:0000313|EMBL:CCA58757.1, ECO:0000313|Proteomes:UP000006854}; RN [1] {ECO:0000313|EMBL:CCA58757.1, ECO:0000313|Proteomes:UP000006854} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 10712 / CBS 650.69 / DSM 40230 / JCM 4526 / NBRC 13096 / RC PD 04745 {ECO:0000313|Proteomes:UP000006854}; RX PubMed=21463507; DOI=10.1186/1471-2164-12-175; RA Pullan S.T., Bibb M.J., Merrick M.; RT "Genome-wide analysis of the role of GlnR in Streptomyces venezuelae RT provides new insights into global nitrogen regulation in RT actinomycetes."; RL BMC Genomics 12:175-175(2011). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; FR845719; CCA58757.1; -; Genomic_DNA. DR RefSeq; WP_015036653.1; NC_018750.1. DR EnsemblBacteria; CCA58757; CCA58757; SVEN_5471. DR GeneID; 28673350; -. DR KEGG; sve:SVEN_5471; -. DR PATRIC; fig|953739.5.peg.615; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000006854; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 2. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000006854}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000006854}. FT DOMAIN 276 441 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 497 AA; 54317 MW; C29D02DAA92B55A8 CRC64; MTSSSSPSQD EQRFAETSRT ESLRADALME EDVAWSHEID GERDGDQFDR SERAALRRVA GLSTELEDVT EVEYRQLRLE RVVLVGVWTS GTVQDAENSL AELAALAETA GALVLDGVIQ RRDKPDPATF IGSGKARELR DIVVETGADT VVCDGELSPG QLIALEDVVK VKVVDRTALI LDIFAQHAKS REGKAQVALA QMQYMLPRLR GWGQSLSRQM GGGGGGGMAT RGPGETKIET DRRRIREKMA KMRREIAEMK TGRDIKRQER RRNKVPSVAI AGYTNAGKSS LLNRLTGAGV LVENALFATL DPTVRRAETP TGRVYTLADT VGFVRHLPHH LVEAFRSTME EVGDSDLILH VVDGSHPAPE EQLAAVREVF RDVGAVNVPE IVVINKADAA DPLVLQRLLR MEKHSIVVSA RSGQGIEQLL ALIDSELPRP EVELEALVPY TQGGLVSRVH AEGEVESEEH TPEGTLLKAR VHEELAAMLA PYVPAAH // ID F2UCB3_SALR5 Unreviewed; 865 AA. AC F2UCB3; DT 31-MAY-2011, integrated into UniProtKB/TrEMBL. DT 31-MAY-2011, sequence version 1. DT 07-JUN-2017, entry version 26. DE SubName: Full=GTP-binding protein HflX {ECO:0000313|EMBL:EGD74220.1}; GN ORFNames=PTSG_06231 {ECO:0000313|EMBL:EGD74220.1}; OS Salpingoeca rosetta (strain ATCC 50818 / BSB-021). OC Eukaryota; Choanoflagellida; Craspedida; Salpingoecidae; Salpingoeca. OX NCBI_TaxID=946362 {ECO:0000313|Proteomes:UP000007799}; RN [1] {ECO:0000313|Proteomes:UP000007799} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 50818 {ECO:0000313|Proteomes:UP000007799}; RA Russ C., Cuomo C., Burger G., Gray M.W., Holland P.W.H., King N., RA Lang F.B.F., Roger A.J., Ruiz-Trillo I., Young S.K., Zeng Q., RA Gargeya S., Alvarado L., Berlin A., Chapman S.B., Chen Z., RA Freedman E., Gellesch M., Goldberg J., Griggs A., Gujja S., RA Heilman E., Heiman D., Howarth C., Mehta T., Neiman D., Pearson M., RA Roberts A., Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., RA White J., Yandava C., Haas B., Nusbaum C., Birren B.; RT "Annotation of Salpingoeca rosetta."; RL Submitted (AUG-2009) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GL832968; EGD74220.1; -; Genomic_DNA. DR RefSeq; XP_004993120.1; XM_004993063.1. DR EnsemblProtists; EGD74220; EGD74220; PTSG_06231. DR GeneID; 16073695; -. DR KEGG; sre:PTSG_06231; -. DR InParanoid; F2UCB3; -. DR Proteomes; UP000007799; Unassembled WGS sequence. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 2. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 4: Predicted; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000007799}; KW Reference proteome {ECO:0000313|Proteomes:UP000007799}. FT DOMAIN 435 532 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 307 338 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 865 AA; 93008 MW; 0D93BA9BE87E9263 CRC64; MLPVVVLARQ RCRQRCLLLA TEAAEAAAAA AAAAQCQRRG ATARRTPLAG VLATRRWKSS RSSSDSHSAP RAGTTTAGAA SDRARVLVLQ PHFHHYRHRS RRHPLLQLDE AVALASATPS LQPTAALLVP VRDVAHDVFF TRGKMEEMTA IVEAHSAAAV ADDDAEHDGN CGAGVADDDD LSFLEGHVAR KDDPARRRVD AVFVNTLALT PRQQLALEEA WGVPVLDRFR VILDIFRARA STREAKLQVE LAQIPYARAR LSTTFRALPG DTFGLGAAAT LFDHQHGHGE RQRGGQHAVS GAGETPLEKE KRRLNMRQKR IKQELAEIKK RRAEMHKRTH VTHSSEHVVA SDEGVDGDRG RLLVDDADSG RDGGEMHFDA LMDDLQGATS KRRHAKAKAK GEKRRAEQPH STSSNNNGSS GGGGGGGGAH RTGLPVVAVV GYTNAGKTAL VQALSGAGDL TPRDMLFATL DTAARVGRLP GGLEAIFVDT VGFVSDLPHQ LVEAFMSTLE EVAYADLIVH VTDSTDPDRL DQQVCVLDVL SSDLHLDPAL LRNRIQVNSK ADILQQQQRR QQQQQQQQQL GGVEGVAETS SPETTATAPT APTAPTAPTA PRAERGGLPP PPHVFAYDWR ANIRAGDVAV LNEACGYFSQ QYQRLVAQVE GTGDGCHDDE HDEHGGAGGE HGEHGRGGDD GYFSAGEVYA ANADDGGGDV KGDGVDREAN RSKRQQHSEL IDDSNALNIS VHTGTNMDLL RGEIEKRLNA LLGRTTYDVL FPVHFGQGTQ FLHNAGTVHA TEVLTSVFDD EHIARMLEGD GSDTAGDDRV EDVDELADSG PLMKLRVTLD DAGTNRVAAF FSKEGIPLHM HAGPR // ID F2Z6G1_SULAC Unreviewed; 352 AA. AC F2Z6G1; DT 31-MAY-2011, integrated into UniProtKB/TrEMBL. DT 31-MAY-2011, sequence version 1. DT 07-JUN-2017, entry version 38. DE SubName: Full=GTP-binding protein hflX {ECO:0000313|EMBL:AAY80038.1}; GN OrderedLocusNames=Saci_0654 {ECO:0000313|EMBL:AAY80038.1}; OS Sulfolobus acidocaldarius (strain ATCC 33909 / DSM 639 / JCM 8929 / OS NBRC 15157 / NCIMB 11770). OC Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae; OC Sulfolobus. OX NCBI_TaxID=330779 {ECO:0000313|EMBL:AAY80038.1, ECO:0000313|Proteomes:UP000001018}; RN [1] {ECO:0000313|EMBL:AAY80038.1, ECO:0000313|Proteomes:UP000001018} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770 RC {ECO:0000313|Proteomes:UP000001018}; RX PubMed=15995215; DOI=10.1128/JB.187.14.4992-4999.2005; RA Chen L., Brugger K., Skovgaard M., Redder P., She Q., Torarinsson E., RA Greve B., Awayez M., Zibat A., Klenk H.-P., Garrett R.A.; RT "The genome of Sulfolobus acidocaldarius, a model organism of the RT Crenarchaeota."; RL J. Bacteriol. 187:4992-4999(2005). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000077; AAY80038.1; -; Genomic_DNA. DR RefSeq; WP_011277540.1; NC_007181.1. DR ProteinModelPortal; F2Z6G1; -. DR STRING; 330779.Saci_0654; -. DR EnsemblBacteria; AAY80038; AAY80038; Saci_0654. DR GeneID; 3473225; -. DR KEGG; sai:Saci_0654; -. DR PATRIC; fig|330779.12.peg.625; -. DR eggNOG; arCOG00353; Archaea. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; FNNHAHV; -. DR OrthoDB; POG093Z07D6; -. DR BioCyc; SACI330779:GH9J-639-MONOMER; -. DR Proteomes; UP000001018; Chromosome. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR CDD; cd01878; HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 4: Predicted; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000001018}; KW Reference proteome {ECO:0000313|Proteomes:UP000001018}. FT DOMAIN 177 352 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 146 177 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 352 AA; 39975 MW; 6AC7C36462E442F2 CRC64; MNFAVLFTAE EYEDEAKALA EAALYNVLEV IKLPRKPNPN FYISQTKLLE LKNNSDVDTI IIFETLKSRH FINLIRELKN KKILDKILLL LEIFALHAGS KEAKLQIELA RLKHQLPVLK DMYKRMKVSE QQGPLGAGVY GIESTVRLYQ RRIVKIREEL NNIKKIKEDQ IRKTELKTTA IVGYTNAGKT TLFNALTGLK QKTDSSMFTT TLPKRYGISV NGDKLLLVDT VGFIRGIPPQ IVEAFYVTLS EAKYADSLLL VVDSSVEDTL FIDMILSSFK ILRDIGISGK PMIIVLNKAD LVNNSDVDQK IDITWKIVKD LYTPIYDVIP ISALKGYNIN TIRDRLLELV LK // ID F3APN7_9FIRM Unreviewed; 417 AA. AC F3APN7; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 07-JUN-2017, entry version 37. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=HMPREF0987_02411 {ECO:0000313|EMBL:EGG88926.1}; OS Lachnospiraceae bacterium 9_1_43BFAA. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Lachnospiraceae. OX NCBI_TaxID=658088 {ECO:0000313|EMBL:EGG88926.1, ECO:0000313|Proteomes:UP000003620}; RN [1] {ECO:0000313|EMBL:EGG88926.1, ECO:0000313|Proteomes:UP000003620} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=9_1_43BFAA {ECO:0000313|EMBL:EGG88926.1, RC ECO:0000313|Proteomes:UP000003620}; RG The Broad Institute Genome Sequencing Platform; RA Earl A., Ward D., Feldgarden M., Gevers D., Daigneault M., Strauss J., RA Ambrose C., Allen-Vercoe E., Young S.K., Zeng Q., Gargeya S., RA Fitzgerald M., Haas B., Abouelleil A., Alvarado L., Arachchi H.M., RA Berlin A., Brown A., Chapman S.B., Chen Z., Dunbar C., Freedman E., RA Gearin G., Gellesch M., Goldberg J., Griggs A., Gujja S., RA Heilman E.R., Heiman D., Howarth C., Larson L., Lui A., RA MacDonald P.J.P., Mehta T., Montmayeur A., Murphy C., Neiman D., RA Pearson M., Priest M., Roberts A., Saif S., Shea T., Shenoy N., RA Sisk P., Stolte C., Sykes S., White J., Yandava C., Wortman J., RA Nusbaum C., Birren B.; RT "The Genome Sequence of Lachnospiraceae bacterium 9_1_43BFAA."; RL Submitted (MAR-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EGG88926.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACTX01000014; EGG88926.1; -; Genomic_DNA. DR RefSeq; WP_009263608.1; NZ_GL890575.1. DR STRING; 658088.HMPREF0987_02411; -. DR EnsemblBacteria; EGG88926; EGG88926; HMPREF0987_02411. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR Proteomes; UP000003620; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000003620}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000003620}. FT DOMAIN 201 365 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 160 194 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 417 AA; 47102 MW; 9958EBFE958B1DF9 CRC64; MQLYDLKETK ERVILVGVQA DDNEDTEKSL DELEELAQTA GAETVGRIIQ NREQIHPGTY VGKGKLDEIK NLLWETDATG IICDDELSPA QLGNLQDALD TKVMDRTLII LDIFAERAST NEGKIQVELA QLKYRQSRLV GLGKSLSRLG GGIGTRGPGE KKLEMDRRLI KGRIAQLNRE LKDVKRHREV TREQRSRNHI PVIAIVGYTN AGKSTLLNRL TGASVLEEDK LFATLDPTTR GLKLPSGQEV LLTDTVGFIR KLPHHLIEAF KSTLEEAKYA DMILHVVDVS NPQMDEQMYT VYETLQNLDV KDKVVITAFN KQDRLTEVPI IRDFKADHIA NISARTGQGL DALQSVIEQI LRERKIEISR TYSYADAGKI QLIRKYGELL EEEYREDGIF VHAFVPKELY GKIEGRE // ID F3BCI5_9FIRM Unreviewed; 415 AA. AC F3BCI5; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 07-JUN-2017, entry version 40. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=HMPREF9477_01640 {ECO:0000313|EMBL:EGG81513.1}; OS Lachnospiraceae bacterium 2_1_46FAA. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Lachnospiraceae. OX NCBI_TaxID=742723 {ECO:0000313|EMBL:EGG81513.1, ECO:0000313|Proteomes:UP000018451}; RN [1] {ECO:0000313|EMBL:EGG81513.1, ECO:0000313|Proteomes:UP000018451} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=2_1_46FAA {ECO:0000313|EMBL:EGG81513.1, RC ECO:0000313|Proteomes:UP000018451}; RG The Broad Institute Genome Sequencing Platform; RA Earl A., Ward D., Feldgarden M., Gevers D., Daigneault M., Strauss J., RA Ambrose C., Allen-Vercoe E., Walker B., Young S.K., Zeng Q., RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L., RA Arachchi H.M., Berlin A.M., Chapman S.B., Dewar J., Goldberg J., RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Larimer J., RA McCowan C., Murphy C., Neiman D., Pearson M., Priest M., Roberts A., RA Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C., RA Birren B.; RT "The Genome Sequence of Lachnospiraceae bacterium 2_1_46FAA."; RL Submitted (DEC-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EGG81513.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADLB02000006; EGG81513.1; -; Genomic_DNA. DR RefSeq; WP_009461992.1; NZ_KE150017.1. DR ProteinModelPortal; F3BCI5; -. DR STRING; 742723.HMPREF9477_01640; -. DR EnsemblBacteria; EGG81513; EGG81513; HMPREF9477_01640. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000018451; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000018451}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000018451}. FT DOMAIN 202 366 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 161 195 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 415 AA; 46714 MW; 1C4E91CA8584CF7C CRC64; MAEMIELSKE IEKVILVGVS VEENDDTEKS LDELEELART AGAVTVGRVI QKREQIHPGT YVGKGKIDEI KELLWETEAT GIICDDELSP AQLGNLQDAL DTKVMDRTLI ILDIFAERAS TSEGKIQVEL AQLKYRQSRL VGLGKSLSRL GGGIGTRGPG EKKLEMDRRL IKGRIAQLNR ELKEVKRHRE VTREQRNRNH LPVVAIVGYT NAGKSTLLNK LTGASVLEED KLFATLDPTT RGLKLQSKQE ILLTDTVGFI RKLPHHLIEA FKSTLEEAKY ADIILHVVDA SNPQLDEQMH IVYETLQQLE VVNKPIITAF NKQDKADGEM IIRDFKADYI VKISAKTGEG LSGLLETIEE VLRQQKVLVE RIYSYAEAGK IQLIRKYGEL LTEEYREEGI FVKAYVPVEI YGKIQ // ID F3KER2_9GAMM Unreviewed; 426 AA. AC F3KER2; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 30-AUG-2017, entry version 38. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=imdm_1462 {ECO:0000313|EMBL:EGG99139.1}; OS gamma proteobacterium IMCC2047. OC Bacteria; Proteobacteria; Gammaproteobacteria. OX NCBI_TaxID=434085 {ECO:0000313|EMBL:EGG99139.1, ECO:0000313|Proteomes:UP000004485}; RN [1] {ECO:0000313|EMBL:EGG99139.1, ECO:0000313|Proteomes:UP000004485} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=imcc2047 {ECO:0000313|Proteomes:UP000004485}; RX PubMed=21602327; DOI=10.1128/JB.05226-11; RA Kang I., Kang D., Oh H.M., Kim H., Kim H.J., Kang T.W., Kim S.Y., RA Cho J.C.; RT "Genome sequence of strain IMCC2047, a novel marine member of the RT Gammaproteobacteria."; RL J. Bacteriol. 193:3688-3689(2011). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EGG99139.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AEGL01000350; EGG99139.1; -; Genomic_DNA. DR ProteinModelPortal; F3KER2; -. DR EnsemblBacteria; EGG99139; EGG99139; imdm_1462. DR PATRIC; fig|434085.3.peg.1260; -. DR Proteomes; UP000004485; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000004485}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000004485}. FT DOMAIN 199 366 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 426 AA; 48271 MW; 705EBEC9CD9CEE00 CRC64; MFFERPDAGE RAILVHLEMS DEAEQEDSRE FKELVLSAGA EPVEMLVARR SQPSPKYFVG SGKVEEIRQA VVAHEAEVVL FNHALTPTQE RNLEKEFQCR VLDRTGLILD IFAQRARTYE GKLQVELAQL EHVSTRLVRG WTHLERQKGG IGLRGPGETQ LETDRRLLRV RLNTITRKLE KVRKQRDQGR QARKRAEIPT ASLAGYTNAG KSTLFNRLTD ASVYAQDQLF ATLDPTMRRL EVEGVGSVVL ADTVGFIRHL PHKLVEAFRA TLQEAAEASL LLHVIDAADE NRDGNIEQVN DVLREIKADE VPSLLVYNKI DLIEDKLPRL DRDDQGVPRR VWVSAETGAG IDLLLQAIGE RLAGEMVNEE LCLPASDGRL RAKFYQQGAV VDERISDEGE FILQIRMSRQ DYDRILGRKP EPLENW // ID F3KLI3_9ARCH Unreviewed; 373 AA. AC F3KLI3; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 30-AUG-2017, entry version 40. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=Nlim_1364 {ECO:0000313|EMBL:EGG41747.1}; OS Candidatus Nitrosoarchaeum limnia SFB1. OC Archaea; Thaumarchaeota; Nitrosopumilales; Nitrosopumilaceae; OC Candidatus Nitrosoarchaeum. OX NCBI_TaxID=886738 {ECO:0000313|EMBL:EGG41747.1, ECO:0000313|Proteomes:UP000004348}; RN [1] {ECO:0000313|EMBL:EGG41747.1, ECO:0000313|Proteomes:UP000004348} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SFB1 {ECO:0000313|EMBL:EGG41747.1, RC ECO:0000313|Proteomes:UP000004348}; RX PubMed=21364937; DOI=10.1371/journal.pone.0016626; RA Blainey P.C., Mosier A.C., Potanina A., Francis C.A., Quake S.R.; RT "Genome of a low-salinity ammonia-oxidizing archaeon determined by RT single-cell and metagenomic analysis."; RL PLoS ONE 6:E16626-E16626(2011). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EGG41747.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AEGP01000048; EGG41747.1; -; Genomic_DNA. DR STRING; 886738.Nlim_1364; -. DR EnsemblBacteria; EGG41747; EGG41747; Nlim_1364. DR PATRIC; fig|886738.10.peg.1491; -. DR eggNOG; arCOG00353; Archaea. DR eggNOG; COG2262; LUCA. DR Proteomes; UP000004348; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR Gene3D; 3.20.20.450; -; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR001633; EAL_dom. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000004348}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000004348}. FT DOMAIN 184 355 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 373 AA; 42418 MW; ECDCA73105782CCF CRC64; MNSAILITYD KEDAVNEAIG LCDAAGIQVI HTIKQNFLKR PKYGIGGGVL EKLEEISEKL KPDIIVFDEI LKPSQNYNLA SVLHREILDR EALILEIFES RASSAESKLQ VKLAQLRYEM VRAKEKIRLS SMGEQPGFMG IGKFEIDVYH NDIKHRMQTV KEKLERAGKQ RELHRQGRKR LGFKTISLAG YTSSGKTTLF NKITGETKEQ SKSLFTTLST TTRRFSIDHE PYLIADTVGF ISKLPAYMID AFKSTLEELV HTDVIIVVVD ISDTLFELKK KFASCMRTLS ELGVEMDKII FTLNKSDLLS VDEIEEKIEL LNLKDYKKRI AVSAKTGNNI GELKELAKNI IQSQKSPEYK KDSWKEFHKS YGT // ID F3KTY5_9BURK Unreviewed; 404 AA. AC F3KTY5; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 07-JUN-2017, entry version 39. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=HGR_09585 {ECO:0000313|EMBL:EGI76737.1}; OS Hylemonella gracilis ATCC 19624. OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Comamonadaceae; Hylemonella. OX NCBI_TaxID=887062 {ECO:0000313|EMBL:EGI76737.1, ECO:0000313|Proteomes:UP000016368}; RN [1] {ECO:0000313|EMBL:EGI76737.1, ECO:0000313|Proteomes:UP000016368} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 19624 {ECO:0000313|EMBL:EGI76737.1, RC ECO:0000313|Proteomes:UP000016368}; RX PubMed=21673657; DOI=10.1038/emboj.2011.186; RA Chen S., Beeby M., Murphy G.E., Leadbetter J.R., Hendrixson D.R., RA Briegel A., Li Z., Shi J., Tocheva E.I., Muller A., Dobro M.J., RA Jensen G.J.; RT "Structural diversity of bacterial flagellar motors."; RL EMBO J. 30:2972-2981(2011). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EGI76737.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AEGR01000058; EGI76737.1; -; Genomic_DNA. DR RefSeq; WP_006297982.1; NZ_AEGR01000058.1. DR STRING; 887062.HGR_09585; -. DR EnsemblBacteria; EGI76737; EGI76737; HGR_09585. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000016368; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 2. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000016368}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000016368}. FT DOMAIN 194 384 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 404 AA; 44571 MW; D441E157B8A830E8 CRC64; MPDTGAILVG VDFGAPHFDG ELEELGLLAE TAGLHPLGRI TCKRKAPDAA LFVGSGKAEE IKLLAQQLGA SEILFDQALS PAQQRNLERV LERPVNDRTL LILEIFAQRA RSHEGKLQVE LARLQYLSTR LVRRWSHLER QTGGQGLRGG PGEKQIELDR RMIADAIKRT KDRLVKVKRQ RQTQRRQRER RDAYNISLVG YTNAGKSTLF NALVKARAYA ADQLFATLDT TTRQLYLAAD EAAAGQAPDP LLMGAPAGRS VSLSDTVGFI RDLPHGLIDA FQATLQEAVD ADLLLHVVDA ANPNFPEQIA EVQRVLAEIG AEGIPQILVF NKLDALAEDR RPTVLQDRYE LDGFETPRVF VSARSGEGLA NLRQMLSARV LSLARQVEAQ RLESLAQDQT IQSV // ID F3L1V2_9GAMM Unreviewed; 428 AA. AC F3L1V2; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 30-AUG-2017, entry version 40. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=IMCC3088_1442 {ECO:0000313|EMBL:EGG29714.1}; OS gamma proteobacterium IMCC3088. OC Bacteria; Proteobacteria; Gammaproteobacteria; Cellvibrionales; OC Halieaceae. OX NCBI_TaxID=876044 {ECO:0000313|EMBL:EGG29714.1, ECO:0000313|Proteomes:UP000005615}; RN [1] {ECO:0000313|EMBL:EGG29714.1, ECO:0000313|Proteomes:UP000005615} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=IMCC3088 {ECO:0000313|EMBL:EGG29714.1, RC ECO:0000313|Proteomes:UP000005615}; RX PubMed=21551310; DOI=10.1128/JB.05111-11; RA Jang Y., Oh H.M., Kang I., Lee K., Yang S.J., Cho J.C.; RT "Genome sequence of strain IMCC3088, a proteorhodopsin-containing RT marine bacterium belonging to the OM60/NOR5 clade."; RL J. Bacteriol. 193:3415-3416(2011). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EGG29714.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AEIG01000035; EGG29714.1; -; Genomic_DNA. DR RefSeq; WP_009575739.1; NZ_AEIG01000035.1. DR ProteinModelPortal; F3L1V2; -. DR STRING; 876044.IMCC3088_1442; -. DR EnsemblBacteria; EGG29714; EGG29714; IMCC3088_1442. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000005615; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000005615}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000005615}. FT DOMAIN 199 365 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 428 AA; 48139 MW; 3695D47DBE0B5CDB CRC64; MFFERPESGE RAVLVHLHLD SEVNREDPRE FEELVLSAGG DPVEFVFGSR ATPHAGTFVG SGKLEEIRQI KERHEAEIVM FNHALTPSQE RNLERVLQCR VLDRTGLILD IFAQRARTHE GKLQVELAQL QHMSTRLVRG WTHLERQKGG IGLRGPGETQ LETDRRLLRA RIKSILARLD KVQRQRDQGR RSRKRAEIPT VSLVGYTNAG KSTLFNHLTD ADVYAADQLF ATLDPTLRQL ELDAIGQVIL ADTVGFIAHL PHKLVDAFNA TLEETLNAEL LCIVVDAASD QRDDNLHQVL DVLAEIGADK IPRLYVYNKL DLLEQEPRIE RDADGVPERV WLSAKTGAGL DLLLEAVAER LGDDMLNATI SLKPEQGRLR ASLYRMNAVM QEATDERGCS QLNVRLPRSD WNRLIAKETG SVELIQSA // ID F3LCP3_9GAMM Unreviewed; 451 AA. AC F3LCP3; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 30-AUG-2017, entry version 41. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=IMCC1989_759 {ECO:0000313|EMBL:EGG95342.1}; OS gamma proteobacterium IMCC1989. OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales. OX NCBI_TaxID=937772 {ECO:0000313|EMBL:EGG95342.1, ECO:0000313|Proteomes:UP000010300}; RN [1] {ECO:0000313|EMBL:EGG95342.1, ECO:0000313|Proteomes:UP000010300} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=IMCC1989 {ECO:0000313|EMBL:EGG95342.1, RC ECO:0000313|Proteomes:UP000010300}; RX PubMed=21602334; DOI=10.1128/JB.05202-11; RA Jang Y., Oh H.M., Kim H., Kang I., Cho J.C.; RT "Genome sequence of strain IMCC1989, a novel member of the marine RT gammaproteobacteria."; RL J. Bacteriol. 193:3672-3673(2011). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EGG95342.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AEVK01000016; EGG95342.1; -; Genomic_DNA. DR RefSeq; WP_009668617.1; NZ_AEVK01000016.1. DR ProteinModelPortal; F3LCP3; -. DR EnsemblBacteria; EGG95342; EGG95342; IMCC1989_759. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000010300; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000010300}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000010300}. FT DOMAIN 199 365 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 165 192 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 451 AA; 50687 MW; 58513455B415A851 CRC64; MFFERPKSGE RAILVHLQLP HSHIRDDPRE FEELVLSAGG DPVEFVTGQR SSVVAKTFVG SGKAEELREL VVLHEAEIVI FNHTLTPTQE RNLEAIFECR VLDRTGLILD IFAQRARTHE GKLQVELAQL HHMSTRLIRG WTHLERQKGG IGLRGPGETQ LETDRRLLRV RVKSIEARLD KVRKQRDQSR RSRLRTSTPT VSLVGYTNAG KSTLFNHITD AGVYAEDKLF ATLDPTMRQI NLPNVGKAVL ADTVGFISHL PHRLIDAFRA TLEEAAHSSL LLHVIDAADE ERPRNIEQVQ EVLTEIGAAD LPQLKIYNKI DLLEHAPRID RDEHGVPVAV WLSAQTGEGV ELMFEALAEC LGDRMIQATL RFPVVLPTEL SRLRARLYSV EAIEDESYDE EGNSEVQINI PQVELLKILG SEGIAEKDLE WAGVIPILST SEAWETAEQP E // ID F3MTD5_LACRH Unreviewed; 240 AA. AC F3MTD5; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 12-APR-2017, entry version 21. DE SubName: Full=HflX subfamily GTP-binding protein {ECO:0000313|EMBL:EGF48536.1}; DE Flags: Fragment; GN ORFNames=AAULR_16174 {ECO:0000313|EMBL:EGF48536.1}; OS Lactobacillus rhamnosus MTCC 5462. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; OC Lactobacillus. OX NCBI_TaxID=947828 {ECO:0000313|EMBL:EGF48536.1, ECO:0000313|Proteomes:UP000003637}; RN [1] {ECO:0000313|EMBL:EGF48536.1, ECO:0000313|Proteomes:UP000003637} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MTCC 5462 {ECO:0000313|EMBL:EGF48536.1, RC ECO:0000313|Proteomes:UP000003637}; RX PubMed=22328760; DOI=10.1128/JB.06644-11; RA Prajapati J.B., Khedkar C.D., Chitra J., Suja S., Mishra V., RA Sreeja V., Patel R.K., Ahir V.B., Bhatt V.D., Sajnani M.R., RA Jakhesara S.J., Koringa P.G., Joshi C.G.; RT "Whole-Genome Shotgun Sequencing of Lactobacillus rhamnosus MTCC 5462, RT a Strain with Probiotic Potential."; RL J. Bacteriol. 194:1264-1265(2012). CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EGF48536.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AEYM01000539; EGF48536.1; -; Genomic_DNA. DR EnsemblBacteria; EGF48536; EGF48536; AAULR_16174. DR Proteomes; UP000003637; Unassembled WGS sequence. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000003637}; KW Reference proteome {ECO:0000313|Proteomes:UP000003637}. FT DOMAIN 29 115 GTP-bdg_N. {ECO:0000259|Pfam:PF13167}. FT DOMAIN 117 198 GTP-bdg_M. {ECO:0000259|Pfam:PF16360}. FT NON_TER 240 240 {ECO:0000313|EMBL:EGF48536.1}. SQ SEQUENCE 240 AA; 26613 MW; 0A6B806FC445FE0B CRC64; MTEQISNEVT SENVLIAGIS RQQPDFNYTM TELGELAKAD NYTVVGEVRQ NLDRAVAATY FGSGKVDDIR QLADVREAST VIINDELSPS QLRNLEKQTK LHVIDRTQLI LDIFADRARS KAAKTQVEIA QLQYALPRLH PSANRLDQQV GGGAGFATRG AGETQLELDR RVLNKRISHL RQELKDASVG DQVRRARRED NAIPVVALVG YTNAGKSTTM NGLLQLFADR PEDKQVSKKT // ID F3NNN4_9ACTN Unreviewed; 497 AA. AC F3NNN4; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 07-JUN-2017, entry version 39. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=SGM_4748 {ECO:0000313|EMBL:EGG44696.1}; OS Streptomyces griseoaurantiacus M045. OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae; OC Streptomyces. OX NCBI_TaxID=996637 {ECO:0000313|EMBL:EGG44696.1, ECO:0000313|Proteomes:UP000003022}; RN [1] {ECO:0000313|EMBL:EGG44696.1, ECO:0000313|Proteomes:UP000003022} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=M045 {ECO:0000313|EMBL:EGG44696.1, RC ECO:0000313|Proteomes:UP000003022}; RX PubMed=21551298; DOI=10.1128/JB.05053-11; RA Li F., Jiang P., Zheng H., Wang S., Zhao G., Qin S., Liu Z.; RT "Draft genome sequence of the marine bacterium Streptomyces RT griseoaurantiacus M045, which produces novel manumycin-type RT antibiotics with a pABA core component."; RL J. Bacteriol. 193:3417-3418(2011). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EGG44696.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AEYX01000042; EGG44696.1; -; Genomic_DNA. DR RefSeq; WP_006142579.1; NZ_AEYX01000042.1. DR STRING; 996637.SGM_4748; -. DR EnsemblBacteria; EGG44696; EGG44696; SGM_4748. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000003022; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 2. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000003022}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000003022}. FT DOMAIN 275 440 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 497 AA; 54175 MW; 645F46DC38B94D0A CRC64; MTSSSSSSQA TKRLARTHPE GLRADALMEE DVTWSHEIDG ERDGDQLDRS ERAALRRVAG LSTELEDVTE VEYRRLRLER VVLVGVWTTG TIKDADNSLA ELAALAETAG ALVLDGVTQR RDKPDAATYI GSGKAEELRD IVLESGADTV ICDGELSPGQ LIHLEDVVKV KVIDRTALIL DIFAQHAKSR EGKAQVALAQ MQYMLPRLRG WGQSLSRQMG GGKGGGLATR GPGETKIETD RRRIREKMAK MRREIAEMKT GREIKRQERR RNKVPSVAIA GYTNAGKSSL LNRLTGAGVL VENALFATLD PTVRRAETPG GRLYTLADTV GFVRHLPHHL VEAFRSTMEE VGDSDLILHV VDGSHPVPEE QLAAVREVIR DVGATDVPEI VVVNKADAAD PLVLQRLLRN EKRAIAVSAR TGRGIDELLA VIDAELPRPA IEVEALVPYT QGKLVARAHA EGEVLSEEHT PEGTLLKVRV HEELAADLGP YTPAPLA // ID F3PRS0_9BACE Unreviewed; 420 AA. AC F3PRS0; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 07-JUN-2017, entry version 39. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=HMPREF9446_01422 {ECO:0000313|EMBL:EGF58121.1}; OS Bacteroides fluxus YIT 12057. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae; OC Bacteroides. OX NCBI_TaxID=763034 {ECO:0000313|EMBL:EGF58121.1, ECO:0000313|Proteomes:UP000003416}; RN [1] {ECO:0000313|EMBL:EGF58121.1, ECO:0000313|Proteomes:UP000003416} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=YIT 12057 {ECO:0000313|EMBL:EGF58121.1, RC ECO:0000313|Proteomes:UP000003416}; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Hou S., Chen J., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Zhang X., Suruliraj S., Warren W., Chinwalla A., RA Mardis E.R., Wilson R.K.; RL Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EGF58121.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFBN01000025; EGF58121.1; -; Genomic_DNA. DR STRING; 763034.HMPREF9446_01422; -. DR EnsemblBacteria; EGF58121; EGF58121; HMPREF9446_01422. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000003416; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000003416}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000003416}. FT DOMAIN 218 402 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 420 AA; 47932 MW; A4EDDD50DFEE8803 CRC64; MAMKEFIISE VQAETAVLVG LITKTQDERR TNEYLDELAF LAETAGAEVV RRFTQKLDQA NSVTYVGKGK LEEIKEYIKG EEEAEREVGM VIFDDELSAK QIRNIEAELK IKILDRTSLI LDIFAMRAQT ANAKTQVELA QYKYMLPRLQ RLWTHLERQG GGSGAGGGKG SVGLRGPGET QLEMDRRIIL NRMSLLKERL AEIDKQKSTQ RKNRGRMIRV ALVGYTNVGK STLMNLLAKS EVFAENKLFA TLDTTVRKVI IENLPFLLSD TVGFIRKLPT DLVDSFKSTL DEVREADLLL HIVDISHPDF EEQIEVVNKT LADIGAAGKP MILVFNKIDA YTYIEKAADD LTPRTKENLT LEELMKTWMA KMEDNCLFIS AREKINMEEL KSVVYQRVKE LHVQKYPYND FLYQTYEEEV // ID F3SAT3_9PROT Unreviewed; 436 AA. AC F3SAT3; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 07-JUN-2017, entry version 38. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=SXCC_03163 {ECO:0000313|EMBL:EGG76174.1}; OS Gluconacetobacter sp. SXCC-1. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales; OC Acetobacteraceae; Gluconacetobacter. OX NCBI_TaxID=1004836 {ECO:0000313|EMBL:EGG76174.1, ECO:0000313|Proteomes:UP000005513}; RN [1] {ECO:0000313|EMBL:EGG76174.1, ECO:0000313|Proteomes:UP000005513} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SXCC-1 {ECO:0000313|EMBL:EGG76174.1, RC ECO:0000313|Proteomes:UP000005513}; RX PubMed=21551293; DOI=10.1128/JB.05147-11; RA Du X.J., Jia S.R., Yang Y., Wang S.; RT "Genome sequence of Gluconacetobacter sp. strain SXCC-1, isolated from RT Chinese vinegar fermentation starter."; RL J. Bacteriol. 193:3395-3396(2011). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EGG76174.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFCH01000047; EGG76174.1; -; Genomic_DNA. DR RefSeq; WP_007399053.1; NZ_AFCH01000047.1. DR STRING; 1004836.SXCC_03163; -. DR EnsemblBacteria; EGG76174; EGG76174; SXCC_03163. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000005513; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000005513}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000005513}. FT DOMAIN 206 375 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 436 AA; 47794 MW; E3EDFCAF395E7918 CRC64; MTAGQPSSAT RAAVILPWER PDRHDDARAA EARLEEAVGL AASIGLVVVC QAVLLLRARR PATLLGGGQV ESLKETVKAD NITVVIIDSR LTPVQQRNLE RALGCKVIDR TALILDIFGE RAATREGTLQ VELAHLEYQR SRLVRTWTHL ERQRGGFGFL GGPGETQIEA DRRMIGDRIV RLKRELEQVR RTRGLHRQAR RRVPFPIVAL VGYTNAGKST LFNALTGASV YAQDQLFATL DPTMRGIQLP SGRRVILSDT VGFISDLPTE LIAAFRATLE EVAEADIILH VRDVSHPDSA SQRQDVIEVL EGMARNGTIE EDWQGRVIEV LNKADLVGGR EAVGARPGNV VISAITGDGL PDLLAAIDER MTRAMEVALY RVPLAEGAAM AWLYEHGEVT ARTDGEQGAD MTVRLSPANR ARFEMQFGRV VTCQAL // ID F3Y9W6_MELPT Unreviewed; 408 AA. AC F3Y9W6; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 07-JUN-2017, entry version 43. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=MPTP_0830 {ECO:0000313|EMBL:BAK21294.1}; OS Melissococcus plutonius (strain ATCC 35311 / CIP 104052 / LMG 20360 / OS NCIMB 702443). OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Enterococcaceae; OC Melissococcus. OX NCBI_TaxID=940190 {ECO:0000313|EMBL:BAK21294.1, ECO:0000313|Proteomes:UP000008456}; RN [1] {ECO:0000313|EMBL:BAK21294.1, ECO:0000313|Proteomes:UP000008456} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 35311 / CIP 104052 / LMG 20360 / NCIMB 702443 RC {ECO:0000313|Proteomes:UP000008456}; RX PubMed=21622755; DOI=10.1128/JB.05151-11; RA Okumura K., Arai R., Okura M., Kirikae T., Takamatsu D., Osaki M., RA Miyoshi-Akiyama T.; RT "Complete genome sequence of Melissococcus plutonius ATCC 35311."; RL J. Bacteriol. 193:4029-4030(2011). RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 35311; RA Okumura K., Arai R., Osaki M., Okura M., Kirikae T., Takamatsu D., RA Akiyama T.; RT "Whole genome sequence of Melissococcus plutonius ATCC 35311."; RL Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AP012200; BAK21294.1; -; Genomic_DNA. DR RefSeq; WP_013773732.1; NC_015516.1. DR ProteinModelPortal; F3Y9W6; -. DR STRING; 940190.MPTP_0830; -. DR EnsemblBacteria; BAK21294; BAK21294; MPTP_0830. DR GeneID; 24963361; -. DR KEGG; mps:MPTP_0830; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000008456; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000008456}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000008456}. FT DOMAIN 196 322 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 408 AA; 46228 MW; B57BF7052D2683FB CRC64; MITKERVILI GVETAENYQI FDESMEELGN LVETAGGEVI SVLTQKLLRI DRKTIVGKGK MEELQELVDN EQADLVIFNH ELTPGQIHTI SLLIAVPIID RVQLIMDIFA LRARSKEGKL QVELAQLNYL LPRLGGQGKQ LSRLGGGIGT RGPGETKLET DRRHVRDKIT KVKQDIKKIT AHRERNRKNR QQTELFQIGL IGYTNAGKST ILNLLTNANT YAENQLFATL DPLTKKWQLP QGMVVTLTDT VGFIQELPTQ LIEAFQSTLE ESNEMDLLLH VVNASSENRL EQEKTVNHLL HELHLDKLPI LTIYNKMDQV NQQTFQPIHF PNVQLSAIQV NSKAILTEAI VGQIKKELSP YCYRIPAEQG KLLNKLKQQT LVVSEEYNEI ENCYYLNGFA KKTFNLNG // ID F3Z2D7_DESAF Unreviewed; 552 AA. AC F3Z2D7; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 07-JUN-2017, entry version 44. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=Desaf_1844 {ECO:0000313|EMBL:EGJ50177.1}; OS Desulfovibrio africanus str. Walvis Bay. OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfovibrionales; OC Desulfovibrionaceae; Desulfovibrio. OX NCBI_TaxID=690850 {ECO:0000313|EMBL:EGJ50177.1, ECO:0000313|Proteomes:UP000007844}; RN [1] {ECO:0000313|EMBL:EGJ50177.1, ECO:0000313|Proteomes:UP000007844} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Walvis Bay {ECO:0000313|EMBL:EGJ50177.1}; RX PubMed=21642452; DOI=10.1128/JB.05223-11; RA Brown S.D., Wall J.D., Kucken A.M., Gilmour C.C., Podar M., RA Brandt C.C., Teshima H., Detter J.C., Han C.S., Land M.L., Lucas S., RA Han J., Pennacchio L., Nolan M., Pitluck S., Woyke T., Goodwin L., RA Palumbo A.V., Elias D.A.; RT "Genome sequence of the mercury-methylating and pleomorphic RT Desulfovibrio africanus Strain Walvis Bay."; RL J. Bacteriol. 193:4037-4038(2011). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP003221; EGJ50177.1; -; Genomic_DNA. DR RefSeq; WP_014259933.1; NC_016629.1. DR STRING; 690850.Desaf_1844; -. DR EnsemblBacteria; EGJ50177; EGJ50177; Desaf_1844. DR KEGG; daf:Desaf_1844; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR KO; K03665; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000007844; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000007844}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000007844}. FT DOMAIN 377 542 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 552 AA; 61413 MW; 4D9D01EFD6937B9C CRC64; MAKVQGNTEG LKASQLKGLE RLYQRRYPPL GGYSVDQARE LAMLSAASGR QIGLLLDRQG RPEMVIVGNA HSILIPELGR ERAVGGRLRG LRLLHTHLTD SGLSEEDLTD MLFLRLDSMA ALSVDKLGQP QTLHVAHLLP SNPENRSWEI LPPRRWDRLD LDFTAMAESL EDELARGVDV KAVAGEERAL LISVSTESRA VQEASLNELA ELARTAGLSV MGRMTQRMRQ MNPKTVLGKG KIAELEVQAL QQDAQVLVFD RELTPAQQRT LADMTERKVL DRTQLILDIF AQRATSRSGK LQVEMAQLKY LQPRLVGQNR ALSRLAGGIG GRGPGETKLE IDRRRVRERI TRIKSELEDL RRRRGYTRER RAKSGVPVVA LVGYTNAGKS TLLNTLTGSV VLAEDKLFAT LDPTSRRIRF PREREVVLTD TVGFIRQLPD ELREAFQATL EELESADLLV HVADAGSPEL ESQVAAVEFI LGEMELGKIA RVLVLNKWDT LREEGRQIVR NIYPEGIPVV AKDRSSLEPL VEAVLAKLPE AGDTEVTQSD QQ // ID F3ZJP0_9ACTN Unreviewed; 520 AA. AC F3ZJP0; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 05-JUL-2017, entry version 38. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=STTU_1536 {ECO:0000313|EMBL:EGJ74325.1}; OS Streptomyces sp. Tu6071. OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae; OC Streptomyces. OX NCBI_TaxID=355249 {ECO:0000313|EMBL:EGJ74325.1, ECO:0000313|Proteomes:UP000003955}; RN [1] {ECO:0000313|Proteomes:UP000003955} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=21705604; DOI=10.1128/JB.00377-11; RA Erxleben A., Wunsch-Palasis J., Gruning B.A., Luzhetska M., RA Bechthold A., Gunther S.; RT "Genome sequence of Streptomyces sp. strain Tu6071."; RL J. Bacteriol. 193:4278-4279(2011). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CM001165; EGJ74325.1; -; Genomic_DNA. DR EnsemblBacteria; EGJ74325; EGJ74325; STTU_1536. DR Proteomes; UP000003955; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 2. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000003955}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000003955}. FT DOMAIN 298 463 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 520 AA; 56600 MW; 694226848E956791 CRC64; MTHTPPFSQD TSGDQDAPLG AEDTVNETHP RGQQPSHSHG LRADALMEED AAWSHGADGA RDGEQYDREE RAALRRVAGL STELEDVTEV EYRQLRLERV ILVGVWTSGT VHDAENSLAE LAALAETAGA LVLDGVIQRR DKPDPATYIG SGKAVELRDL VLETGADTVV CDGELSPGQL IHLEDVVKVK VVDRTALILD IFAQHAKSRE GKAQVSLAQM QYMLPRLRGW GQSLSRQMGG GGSGSSGGGM ATRGPGETKI ETDRRRIREK MAKMRREIAE MKTGRDLKRQ ERRRNKVPSV AIAGYTNAGK SSLLNRLTGA GVLVENALFA TLDPTVRRAE TPSGRLYTLA DTVGFVRHLP HHLVEAFRST MEEVGDSDLI LHVVDGSHPA PEEQLAAVRE VIREVGATDV PEIVVINKAD AADPVVLQRL LRVEKHSIAV SARSGQGIEE LLALIDEELP RPAVEVDVLV PYTEGKYIAR AHVEGEVLSE EHTPEGTRLK ALVHEELAAE LHRFSPVGSH // ID F3ZSD8_9BACE Unreviewed; 420 AA. AC F3ZSD8; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 07-JUN-2017, entry version 39. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=Bcop_0657 {ECO:0000313|EMBL:EGJ70875.1}; OS Bacteroides coprosuis DSM 18011. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae; OC Bacteroides. OX NCBI_TaxID=679937 {ECO:0000313|EMBL:EGJ70875.1, ECO:0000313|Proteomes:UP000018439}; RN [1] {ECO:0000313|EMBL:EGJ70875.1, ECO:0000313|Proteomes:UP000018439} RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 18011 {ECO:0000313|EMBL:EGJ70875.1}; RX PubMed=21677860; DOI=10.4056/sigs.1784330; RA Land M., Held B., Gronow S., Abt B., Lucas S., Del Rio T.G., Nolan M., RA Tice H., Cheng J.F., Pitluck S., Liolios K., Pagani I., Ivanova N., RA Mavromatis K., Mikhailova N., Pati A., Tapia R., Han C., Goodwin L., RA Chen A., Palaniappan K., Hauser L., Brambilla E.M., Rohde M., RA Goker M., Detter J.C., Woyke T., Bristow J., Eisen J.A., Markowitz V., RA Hugenholtz P., Kyrpides N.C., Klenk H.P., Lapidus A.; RT "Non-contiguous finished genome sequence of Bacteroides coprosuis type RT strain (PC139)."; RL Stand. Genomic Sci. 4:233-243(2011). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CM001167; EGJ70875.1; -; Genomic_DNA. DR RefSeq; WP_006744031.1; NZ_CM001167.1. DR ProteinModelPortal; F3ZSD8; -. DR STRING; 679937.Bcop_0657; -. DR EnsemblBacteria; EGJ70875; EGJ70875; Bcop_0657. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000018439; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000018439}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000018439}. FT DOMAIN 210 393 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 420 AA; 48137 MW; EF5117120557363C CRC64; MKDFVISEVQ VETAVLVGLV TPFQDERKTD EYLEELEFLA DTAGAEVVGK FTQKLDKENP TTYVGKGKLE EIRDYVKDHE VGMVIFDDEL SAKQIRNIEK ELQVKILDRT SLILDIFAMR AQTASAKTQV ELAQYQYMLP RLTRLWTHLE RQAGGSGSGK GGSVGLRGPG ETQLEMDKRI IGDRISFLKK QLEKIDRQKA TQRKNRGRLI RVALVGYTNV GKSTIMNMLA KSEVFAEDKL FATLDTTVRK VVVGNLPFLL SDTVGFIRKL PTDLVDSFKS TLDEVREADL LIHVVDISHP SFEDQIKVVN QTLADIDSSD KPTFLVFNKI DAYSYIKKDE DDLTPITRAN WSLEELMNTW MAKNADCIFI SAKERTNIEE LRRKIYDRVR ELHVQRFPYN DFLYPVYDEE DWSGEEVEQE // ID F4B1W9_DOKS4 Unreviewed; 409 AA. AC F4B1W9; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 07-JUN-2017, entry version 41. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Krodi_0867 {ECO:0000313|EMBL:AEE18851.1}; OS Dokdonia sp. (strain 4H-3-7-5) (Krokinobacter sp. (strain 4H-3-7-5)). OC Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales; OC Flavobacteriaceae; Dokdonia. OX NCBI_TaxID=983548 {ECO:0000313|EMBL:AEE18851.1, ECO:0000313|Proteomes:UP000008290}; RN [1] {ECO:0000313|EMBL:AEE18851.1, ECO:0000313|Proteomes:UP000008290} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=4H-3-7-5 {ECO:0000313|EMBL:AEE18851.1, RC ECO:0000313|Proteomes:UP000008290}; RX PubMed=21725025; DOI=10.1128/JB.05518-11; RA Klippel B., Lochner A., Bruce D.C., Walston Davenport K., Detter C., RA Goodwin L.A., Han J., Han S., Hauser L., Land M.L., Nolan M., RA Ovchinnikova G., Pennacchio L., Pitluck S., Tapia R., Woyke T., RA Wiebusch S., Basner A., Abe F., Horikoshi K., Keller M., RA Antranikian G.; RT "Complete genome sequences of Krokinobacter sp. strain 4H-3-7-5 and RT Lacinutrix sp. strain 5H-3-7-4, polysaccharide-degrading members of RT the family Flavobacteriaceae."; RL J. Bacteriol. 193:4545-4546(2011). RN [2] {ECO:0000313|Proteomes:UP000008290} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=4H-3-7-5 {ECO:0000313|Proteomes:UP000008290}; RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L., RA Pitluck S., Davenport K., Detter J.C., Han C., Tapia R., Land M., RA Hauser L., Kyrpides N., Ivanova N., Ovchinnikova G., Pagani I., RA Piela B., Lochner A., Antranikian F.I., Woyke T.; RT "Complete sequence of Krokinobacter diaphorus 4H-3-7-5."; RL Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE. RC STRAIN=4H-3-7-5; RG US DOE Joint Genome Institute; RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L., RA Pitluck S., Davenport K., Detter J.C., Han C., Tapia R., Land M., RA Hauser L., Kyrpides N., Ivanova N., Ovchinnikova G., Pagani I., RA Piela B., Lochner A., Antranikian F.I., Woyke T.; RT "Complete sequence of Krokinobacter sp. 4H-3-7-5."; RL Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002528; AEE18851.1; -; Genomic_DNA. DR RefSeq; WP_013750359.1; NC_015496.1. DR ProteinModelPortal; F4B1W9; -. DR STRING; 983548.Krodi_0867; -. DR EnsemblBacteria; AEE18851; AEE18851; Krodi_0867. DR KEGG; kdi:Krodi_0867; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000008290; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000008290}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000008290}. FT DOMAIN 200 385 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 409 AA; 47178 MW; E3CEDE8A79BA98DD CRC64; MIETEKIDYE KCVLVGLVTQ KQSHDKMTEY LDELEFLAYT AGGEVLKRFF QKLEKPNPKT FIGTGKMEDV AAYVEQHDVG TVIFDDELTP GQQRNIEAIL KCKIVDRTYL ILDIFAQRAQ TSYARTQVEL AQYEYLLPRL TGLWTHLERQ RGGIGMRGPG ETEIETDRRI VRDRITLLKK KMLTIDKQMA TQRGNRGALV RVALVGYTNV GKSTLMNVIS KSKVFAENKL FATLDTTVRK VVVGNLPFLL SDTVGFIRKL PTQLVDSFKS TLDEVREADL LLHVVDISHP QFEDHINAVN QILDEIESMD KPTLMVFNKI DAYTAEAYDD EDLMVERTGA HYTLDEWKET WMSRTNGDAI FISALNKNNF EEFRKKIYER VREIHVTRFP YNAFLYPEYE EQVGNSEEE // ID F4B817_ACIHW Unreviewed; 364 AA. AC F4B817; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 07-JUN-2017, entry version 35. DE SubName: Full=GTP-binding proten HflX {ECO:0000313|EMBL:AEE93694.1}; GN OrderedLocusNames=Ahos_0808 {ECO:0000313|EMBL:AEE93694.1}; OS Acidianus hospitalis (strain W1). OC Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae; OC Acidianus. OX NCBI_TaxID=933801 {ECO:0000313|EMBL:AEE93694.1, ECO:0000313|Proteomes:UP000008458}; RN [1] {ECO:0000313|EMBL:AEE93694.1, ECO:0000313|Proteomes:UP000008458} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=W1 {ECO:0000313|EMBL:AEE93694.1, RC ECO:0000313|Proteomes:UP000008458}; RX PubMed=21607549; DOI=10.1007/s00792-011-0379-y; RA You X.Y., Liu C., Wang S.Y., Jiang C.Y., Shah S.A., Prangishvili D., RA She Q., Liu S.J., Garrett R.A.; RT "Genomic analysis of Acidianus hospitalis W1 a host for studying RT crenarchaeal virus and plasmid life cycles."; RL Extremophiles 15:487-497(2011). RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=W1; RA You X.Y., Liu C., Wang S.Y., Jiang C.Y., Shah S.A., Prangishvili D., RA Liu S.J., Garrett R.A.; RT "Genomic analyses of Acidianus hospitalis W1 a host for studying RT crenarchaeal virus and plasmid life cycles."; RL Extremophiles 0:0-0(2011). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002535; AEE93694.1; -; Genomic_DNA. DR RefSeq; WP_013775610.1; NC_015518.1. DR ProteinModelPortal; F4B817; -. DR STRING; 933801.Ahos_0808; -. DR EnsemblBacteria; AEE93694; AEE93694; Ahos_0808. DR GeneID; 10600269; -. DR KEGG; aho:Ahos_0808; -. DR eggNOG; arCOG00353; Archaea. DR eggNOG; COG2262; LUCA. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG093Z07D6; -. DR Proteomes; UP000008458; Chromosome. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR CDD; cd01878; HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008458}; KW Reference proteome {ECO:0000313|Proteomes:UP000008458}. FT DOMAIN 179 364 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 364 AA; 41365 MW; C9FAEC1361DFE008 CRC64; MKAILFSSDE YLDEAKTLSE TAGYEIVSIY KLPKKPNPSY YIQEDKLNKL KNENIDAIIV FDLLKPRHFI NLNKELGGKM KILDKLLLLL EIFALHAGSK EAQLQIELAK LKYELPIIKD VYKKHKISEQ QGLLGAGVYG VESILRLYHR KIAKISKELM HIKELRESQV KQHESNGIPT VAITGYTNAG KTSIFNILTG LHQKVDSSMF TTTAPKRFKI SINGQKIMLV DTVGFIRGIP PQIIEAFFVT LSEIKYADII LLVVDISLED TLILEMLKSS FSTLRELGIS GKPILIVANK TDKIPYEEID RRSDLIYKIS NEIYSPIIGI IPFSAKTLYN LSNLKIKIAE SLLMYYNQEK REIT // ID F4BYQ6_METCG Unreviewed; 415 AA. AC F4BYQ6; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 07-JUN-2017, entry version 45. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:AEB67683.1}; GN OrderedLocusNames=MCON_0914 {ECO:0000313|EMBL:AEB67683.1}; OS Methanosaeta concilii (strain ATCC 5969 / DSM 3671 / JCM 10134 / NBRC OS 103675 / OCM 69 / GP-6) (Methanothrix concilii). OC Archaea; Euryarchaeota; Methanomicrobia; Methanosarcinales; OC Methanosaetaceae; Methanosaeta. OX NCBI_TaxID=990316 {ECO:0000313|EMBL:AEB67683.1, ECO:0000313|Proteomes:UP000007807}; RN [1] {ECO:0000313|EMBL:AEB67683.1, ECO:0000313|Proteomes:UP000007807} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 5969 / DSM 3671 / JCM 10134 / NBRC 103675 / OCM 69 / GP-6 RC {ECO:0000313|Proteomes:UP000007807}; RX PubMed=21571998; DOI=10.1128/JB.05031-11; RA Barber R.D., Zhang L., Harnack M., Olson M.V., Kaul R., RA Ingram-Smith C., Smith K.S.; RT "Complete genome sequence of Methanosaeta concilii, a specialist in RT aceticlastic methanogenesis."; RL J. Bacteriol. 193:3668-3669(2011). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002565; AEB67683.1; -; Genomic_DNA. DR RefSeq; WP_013718737.1; NC_015416.1. DR ProteinModelPortal; F4BYQ6; -. DR STRING; 990316.MCON_0914; -. DR EnsemblBacteria; AEB67683; AEB67683; MCON_0914. DR GeneID; 10460594; -. DR KEGG; mcj:MCON_0914; -. DR eggNOG; arCOG00353; Archaea. DR eggNOG; COG2262; LUCA. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG093Z07D6; -. DR Proteomes; UP000007807; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000007807}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000007807}. FT DOMAIN 188 357 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 415 AA; 47061 MW; 96B5AD03E7C2F90E CRC64; MDNDKTAVLL MRENPANPID PYRMIELRGL ANAVGYRVLQ EIKQRRERDH RFQIGRGKIE EALSCHPKKL IFYNPLSPTQ VFNIRSEFPA QVLDRFNLIL EIFASRASTR EAKLQVELAR LSYDAPQVRS ELALKKRGEQ PGFRGAGAYE QSMYHDIRGR MAKIRGELKE VEAMGEGRRK RRRELGFDLI ALAGYTNAGK STLLNTLTGS VVNAQDQPFT TLSPTTRALE INGRRTMLTD TVGFIDDLPH FLIKAFQSTL SEIAQADLVL LVADLSDPLE LLRRKLVASH KALWDCQVTA PMITVLNKMD RLDEFDARMR FDQIKDLAPN PVMVSAHSSQ GQESLKECIY QHLPPLKEYQ IRLPYTSRSF GVLSRLYGTA ELLDVSYEDE LVLSLQGRAE DVARLSKAAE DERAK // ID F4CDJ3_SPHS2 Unreviewed; 400 AA. AC F4CDJ3; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 07-JUN-2017, entry version 43. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Sph21_1159 {ECO:0000313|EMBL:ADZ77728.1}; OS Sphingobacterium sp. (strain 21). OC Bacteria; Bacteroidetes; Sphingobacteriia; Sphingobacteriales; OC Sphingobacteriaceae; Sphingobacterium. OX NCBI_TaxID=743722 {ECO:0000313|EMBL:ADZ77728.1, ECO:0000313|Proteomes:UP000007808}; RN [1] {ECO:0000313|Proteomes:UP000007808} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=21 {ECO:0000313|Proteomes:UP000007808}; RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L., RA Pitluck S., Davenport K., Detter J.C., Han C., Tapia R., Land M., RA Hauser L., Kyrpides N., Ivanova N., Ovchinnikova G., Pagani I., RA Siebers A.K., Allgaier M., Thelen M.P., Hugenholtz P., Woyke T.; RT "Complete sequence of Sphingobacterium sp. 21."; RL Submitted (MAR-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002584; ADZ77728.1; -; Genomic_DNA. DR RefSeq; WP_013664456.1; NC_015277.1. DR ProteinModelPortal; F4CDJ3; -. DR STRING; 743722.Sph21_1159; -. DR EnsemblBacteria; ADZ77728; ADZ77728; Sph21_1159. DR KEGG; shg:Sph21_1159; -. DR PATRIC; fig|743722.3.peg.1241; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000007808; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000007808}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000007808}. FT DOMAIN 204 389 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 400 AA; 45700 MW; 217E1B799563D18B CRC64; MAIRKIYDTA IKPERAVLVG IITPNETEDQ EKEYLEELAF LVETAGGETI NTFTQRMQKP DRATFVGSGK LDEIKAYVNA EEADIVVFDD ELSPSQLRNI ENELKIKILD RSNLILDIFA NRAKTAQAKT QVELAQLQYL LPRLTRMWTH LERQKGGIGM RGPGETQIES DRRMILNKIS LLKEKLKQID KQNETQRKNR GELIRVALVG YTNVGKSTIM NMISKSEVFA ENKLFATLDT TVRKVVIDNL PFLLSDTVGF IRKLPHHLVE CFKSTLDEVR EADILVHVVD ISHPNFEDHI NTVNETLKDL GAIDKPVITV FNKIDAYKPA EVARDDNGDE QAKKNITIDD FKNSWMAKHS SPAVFISATE KKNVEEFRQL LYDKVIKIHT ARYPYNNLLY // ID F4CJA5_PSEUX Unreviewed; 493 AA. AC F4CJA5; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 07-JUN-2017, entry version 42. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Psed_2119 {ECO:0000313|EMBL:AEA24344.1}; OS Pseudonocardia dioxanivorans (strain ATCC 55486 / DSM 44775 / JCM OS 13855 / CB1190). OC Bacteria; Actinobacteria; Pseudonocardiales; Pseudonocardiaceae; OC Pseudonocardia. OX NCBI_TaxID=675635 {ECO:0000313|EMBL:AEA24344.1, ECO:0000313|Proteomes:UP000007809}; RN [1] {ECO:0000313|EMBL:AEA24344.1, ECO:0000313|Proteomes:UP000007809} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 55486 / DSM 44775 / JCM 13855 / CB1190 RC {ECO:0000313|Proteomes:UP000007809}; RX PubMed=21725009; DOI=10.1128/JB.00415-11; RA Sales C.M., Mahendra S., Grostern A., Parales R.E., Goodwin L.A., RA Woyke T., Nolan M., Lapidus A., Chertkov O., Ovchinnikova G., RA Sczyrba A., Alvarez-Cohen L.; RT "Genome sequence of the 1,4-dioxane-degrading Pseudonocardia RT dioxanivorans strain CB1190."; RL J. Bacteriol. 193:4549-4550(2011). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002593; AEA24344.1; -; Genomic_DNA. DR RefSeq; WP_013674275.1; NC_015312.1. DR STRING; 675635.Psed_2119; -. DR EnsemblBacteria; AEA24344; AEA24344; Psed_2119. DR KEGG; pdx:Psed_2119; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000007809; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 2. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000007809}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000007809}. FT DOMAIN 268 437 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 493 AA; 53263 MW; 913935710403D766 CRC64; MTESRLDISG MFAPRSDGAG LDTAVAAAAG REPSTGDMEL EERTSLRRVA GLSTELTDVT EVEYRQLRLE RVVLVGVWTT GTAQQAEASL VELARLAETA GSQVLDGLVQ RRSRPDPATF IGSGKVDELR AAVQGAGADT VIADGELSPG QLRQLEEKLK VKVIDRTALI LDIFAQHARS RDGKAQVELA QLSYLLPRLR GWGEALSRQV GGRAAGGVGI GGRGPGETKI ELDRRRIRHR MSKLRREIAA MRTVRETQRG SRRRNEVPGV AIVGYTNAGK SSLLNALTDA GVLVEDALFA TLDPTTRRAE TPDGRDYTLT DTVGFVRHLP HQLVEAFRST LEETAQADLL VHVVDASDPL PEDQIAAVRK VLVEIGEEQQ GRMPPELLVV NKIDAAGDLQ LARLRHLLPD AVFVSAHTGA GVSLLRRRIA ELLPNPEVEV ELLVPYAEGA LVARVHSDGV VLEEEHVADG TRMRARVGPE LATAVSAHLV APR // ID F4EVP2_SELS3 Unreviewed; 647 AA. AC F4EVP2; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 05-JUL-2017, entry version 44. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=Selsp_2153 {ECO:0000313|EMBL:AEC01100.1}; OS Selenomonas sputigena (strain ATCC 35185 / DSM 20758 / VPI D19B-28). OC Bacteria; Firmicutes; Negativicutes; Selenomonadales; OC Selenomonadaceae; Selenomonas. OX NCBI_TaxID=546271 {ECO:0000313|EMBL:AEC01100.1, ECO:0000313|Proteomes:UP000011124}; RN [1] {ECO:0000313|EMBL:AEC01100.1, ECO:0000313|Proteomes:UP000011124} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 35185 / DSM 20758 / VPI D19B-28 RC {ECO:0000313|Proteomes:UP000011124}; RG US DOE Joint Genome Institute (JGI-PGF); RA Lucas S., Copeland A., Lapidus A., Bruce D., Goodwin L., Pitluck S., RA Peters L., Kyrpides N., Mavromatis K., Ivanova N., Ovchinnikova G., RA Teshima H., Detter J.C., Tapia R., Han C., Land M., Hauser L., RA Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Gronow S., RA Wellnitz S., Schneider S., Klenk H.-P., Eisen J.A.; RT "The complete genome of Selenomonas sputigena DSM 20758."; RL Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002637; AEC01100.1; -; Genomic_DNA. DR RefSeq; WP_013741050.1; NZ_GG698597.1. DR EnsemblBacteria; AEC01100; AEC01100; Selsp_2153. DR KEGG; ssg:Selsp_2153; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR KO; K03665; -. DR OMA; EREVIIT; -. DR Proteomes; UP000011124; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 2. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000011124}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000011124}. FT DOMAIN 382 593 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 348 375 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 647 AA; 71287 MW; E4CC1161169A9D06 CRC64; MKDKRIQGEI QNLKPHIMRE LQSLYDLSVP VGQLSTKELN ERLIAVTEEI GREVAVYVDR KGRIIEISVG NTWTVDLPAV DARSEVRLSG VRCIHTHPSG DTELSDPDIS SLRRLRFDAM AAIGRLSGES VGCLGFFTGE KEEDGTLEVQ LFGPVRADHL NRIRLTPLIQ SINKRLSRER TQATDDEEER AVLAGIDAPM ACALWMTEDS LAELAELART AGATVVGTFI QKKAKPDTAL FLGRGKVEEM AMFIQNERAT LVIFDDELTP SQQRNLEMAL GVKILDRTAL ILDIFAQRAR TAAGKLQVEL AQMKYSLPRI LGQGLVLSRL GGGIGTRGPG ETKLEVDRRR IRRRIHDIEG EIERLKKERL LHRERRRAAR IPVAALVGYT NAGKSTLLNA LTGADVFAED KLFATLDPTT RSLRLADGRE ILVTDTVGFI QKLPHTLVQA FHATLEEVVE ADILLHVVDV SNEAAEFQIE AVTEVLKELG AAEKPMLYVL NKLDRLTNGA GGTGGGEAAA HVDTMGDARY EAAGSDAAGG FSEGEIPSLE EVHLPPAVLR LLRGREGCAI SARTGAGLVE LQERIASFFR TGEVELTLHI PFTENAAVTR LHEAGRVLQT DYDERGTRVR VRLSEEEAAR FRRYEIS // ID F4FCU6_VERMA Unreviewed; 480 AA. AC F4FCU6; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 07-JUN-2017, entry version 42. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=VAB18032_12380 {ECO:0000313|EMBL:AEB43590.1}; OS Verrucosispora maris (strain AB-18-032). OC Bacteria; Actinobacteria; Micromonosporales; Micromonosporaceae; OC Verrucosispora. OX NCBI_TaxID=263358 {ECO:0000313|EMBL:AEB43590.1, ECO:0000313|Proteomes:UP000008308}; RN [1] {ECO:0000313|EMBL:AEB43590.1, ECO:0000313|Proteomes:UP000008308} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=AB-18-032 {ECO:0000313|EMBL:AEB43590.1, RC ECO:0000313|Proteomes:UP000008308}; RX PubMed=21551311; DOI=10.1128/JB.05041-11; RA Roh H., Uguru G.C., Ko H.J., Kim S., Kim B.Y., Goodfellow M., RA Bull A.T., Kim K.H., Bibb M.J., Choi I.G., Stach J.E.; RT "Genome sequence of the abyssomicin- and proximicin-producing marine RT actinomycete Verrucosispora maris AB-18-032."; RL J. Bacteriol. 193:3391-3392(2011). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002638; AEB43590.1; -; Genomic_DNA. DR RefSeq; WP_013732259.1; NC_015434.1. DR STRING; 263358.VAB18032_12380; -. DR EnsemblBacteria; AEB43590; AEB43590; VAB18032_12380. DR KEGG; vma:VAB18032_12380; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000008308; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000008308}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000008308}. FT DOMAIN 253 418 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 480 AA; 52744 MW; 7B6410EB6241290F CRC64; MRDQETHVSN DEFETTPGEY ELSERQALRR VPGLSTELTD VTEVEYRQLR LERVVLVGVW TEGTQADADN SLTELAALAE TAGSQVLEGL IQRRTRPDPA TYIGRGKVDD LSAVVLAAGA DTVICDGELS PSQLRNLEQR TKVKVVDRTA LILDIFAQHA KSKEGRAQVE LAQLEYLLPR LRGWGETLSR QTGGSGRGGG AGGGVGVRGP GETKLETDRR RIRHRIARLR REIKAMSTVR ETKRSRRTRN AVPAVAIAGY TNAGKSSLLN RLTGAGVLVE DALFATLDPT TRRATTSEGR VYTLSDTVGF VRHLPHQIVE AFRSTLEEIA EADLVVHVVD GTHPDPQEQV RAVREVLTEV GADRLPELLV VNKTDAADEE TLLQLKRIWP EAVFVSAYSG RGIDDLRATI EQRLPRPAVD VRVVLPYDRG DLVARLHRQG EVLSTAHLPE GTMLHVRVNE ALAAELAPYR DTAEAVSTAR // ID F4GEL5_ALIDK Unreviewed; 392 AA. AC F4GEL5; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 07-JUN-2017, entry version 42. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Alide2_1417 {ECO:0000313|EMBL:AEB83817.1}; OS Alicycliphilus denitrificans (strain DSM 14773 / CIP 107495 / K601). OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Comamonadaceae; Alicycliphilus. OX NCBI_TaxID=596154 {ECO:0000313|EMBL:AEB83817.1, ECO:0000313|Proteomes:UP000007938}; RN [1] {ECO:0000313|EMBL:AEB83817.1, ECO:0000313|Proteomes:UP000007938} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 14773 / CIP 107495 / K601 RC {ECO:0000313|Proteomes:UP000007938}; RG US DOE Joint Genome Institute; RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S., RA Peters L., Zeytun A., Detter J.C., Han C., Tapia R., Land M., RA Hauser L., Kyrpides N., Ivanova N., Mikhailova N., Pagani I., RA Oosterkamp M., Pieper D., van Berkel W., Langenhoff A., Smidt H., RA Stams A., Woyke T.; RT "Complete sequence of chromosome of Alicycliphilus denitrificans RT K601."; RL Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002657; AEB83817.1; -; Genomic_DNA. DR RefSeq; WP_013519840.1; NC_015422.1. DR ProteinModelPortal; F4GEL5; -. DR STRING; 596154.Alide2_1417; -. DR EnsemblBacteria; AEB83817; AEB83817; Alide2_1417. DR KEGG; adk:Alide2_1417; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000007938; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000007938}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000007938}. FT DOMAIN 202 375 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 392 AA; 43232 MW; 51CB075F3C76D775 CRC64; MSSNPSSDTD FTPVLLVGVD FGLPHFDAEL QELGLLAQTA GLKPVARLTC KRKAPDAALF VGSGKAGEIQ TLAQMHGAKE VLFDQALSPA QQRNLERHLQ MPVNDRTLLI LEIFAQRARS HEGKLQVELA RLQYLSTRLV RRWSHLERQR GGIGTRGGPG ETQIELDRRM IGEAIKRTRE RLVKVKRQRA TQRRQRERRD TFNISLVGYT NAGKSTLFNA LVKARAYAAD QLFATLDTTT RQLYLGEAVG SVSLSDTVGF IRDLPHGLVD AFQATLQEAV DADLLLHVVD AANPGYPEQI AQVQLVLAEI GAAEIPQLLV FNKFDAMPAE TRPARLQDMY ELDGRQVPRI FVSARQGEGI PALRELLAHM VQEAAARDMT PGETAELPGP PG // ID F4GKC4_SPHCD Unreviewed; 474 AA. AC F4GKC4; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 07-JUN-2017, entry version 39. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Spico_1099 {ECO:0000313|EMBL:AEC02320.1}; OS Sphaerochaeta coccoides (strain ATCC BAA-1237 / DSM 17374 / SPN1) OS (Spirochaeta coccoides). OC Bacteria; Spirochaetes; Spirochaetales; Spirochaetaceae; OC Sphaerochaeta. OX NCBI_TaxID=760011 {ECO:0000313|EMBL:AEC02320.1, ECO:0000313|Proteomes:UP000007939}; RN [1] {ECO:0000313|Proteomes:UP000007939} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-1237 / DSM 17374 / SPN1 RC {ECO:0000313|Proteomes:UP000007939}; RA Lucas S., Copeland A., Lapidus A., Bruce D., Goodwin L., Pitluck S., RA Peters L., Kyrpides N., Mavromatis K., Pagani I., Ivanova N., RA Ovchinnikova G., Lu M., Detter J.C., Tapia R., Han C., Land M., RA Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T., Wu D., RA Spring S., Schroeder M., Brambilla E., Klenk H.-P., Eisen J.A.; RT "The complete genome of Spirochaeta coccoides DSM 17374."; RL Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002659; AEC02320.1; -; Genomic_DNA. DR RefSeq; WP_013739715.1; NC_015436.1. DR STRING; 760011.Spico_1099; -. DR EnsemblBacteria; AEC02320; AEC02320; Spico_1099. DR KEGG; scc:Spico_1099; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000007939; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000007939}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000007939}. FT DOMAIN 255 421 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 474 AA; 52569 MW; 5A0D467B783DCBCD CRC64; MEKRDADEKQ PLAFLLDGSI SYTSMRGNNP GQRMPCTKKR LDDQDFFPSH DSRLHDTEED SLSVFLVGLR TPDESVPRAQ LRLQELDSLV RTAGMEPLGA RILPLRTGRA ATLIGSGQAL EIKELAEYHA ADAIVFDRDI PPRAQRNLED IIGLPIHDRQ GIIITIFGQR ASTKEAVLQV ELARLHYVLP RLTGSREDLS RQQGGVKGTR GGGEAQLELD RRRISDRIAC LKTELTAVRT RRERQRTQRK SGEIPVGAIV GYTNSGKSSL LKALSGADIL VEDKLFATLD PTTRRIRLPE SGEVLLSDTV GFVSDLPHHL VDAFRSTLEE ATDADFLVIV CDASHPDMLS CYQATLDVLH NMGADGKPTV TMLNKMDVPF EDFAVAKLRD MIPDLVETSI KKRQGLNALL EAMAKAAYAS CPLRSFLIPA DRHDLVSRTR QSGRIETLEY TDDGILLSAR LIPVMLGDFL PFQQ // ID F4GUV2_PUSST Unreviewed; 365 AA. AC F4GUV2; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 07-JUN-2017, entry version 45. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=PT7_1394 {ECO:0000313|EMBL:AEC19934.1}; OS Pusillimonas sp. (strain T7-7). OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Alcaligenaceae; Pusillimonas. OX NCBI_TaxID=1007105 {ECO:0000313|EMBL:AEC19934.1, ECO:0000313|Proteomes:UP000008737}; RN [1] {ECO:0000313|EMBL:AEC19934.1, ECO:0000313|Proteomes:UP000008737} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=T7-7 {ECO:0000313|EMBL:AEC19934.1, RC ECO:0000313|Proteomes:UP000008737}; RX PubMed=21622753; DOI=10.1128/JB.05242-11; RA Cao B., Ma T., Ren Y., Ren Y., Li G., Li P., Guo X., Ding P., Feng L.; RT "Complete genome sequence of Pusillimonas sp. T7-7, a cold-tolerant RT diesel oil-degrading bacterium isolated from the Bohai Sea in China."; RL J. Bacteriol. 193:4021-4022(2011). RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=T7-7; RA Cao B., Ma T., Li P., Jiang L., Li Y., Guo X., Feng L.; RT "Genome Announcement Complete Genome Sequence of Pusillimonas sp. T7- RT 7, a novel species isolated from the Bohai Sea, China."; RL Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002663; AEC19934.1; -; Genomic_DNA. DR RefSeq; WP_013742470.1; NC_015458.1. DR ProteinModelPortal; F4GUV2; -. DR STRING; 1007105.PT7_1394; -. DR EnsemblBacteria; AEC19934; AEC19934; PT7_1394. DR KEGG; put:PT7_1394; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000008737; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000008737}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000008737}. FT DOMAIN 190 354 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 365 AA; 40129 MW; 90ADC2484BA80F52 CRC64; MKALIISVDL GESDYPAHAE EFAMLAKGAG AEIVGTIVAR RARPDAAHFI GSGKLEEAIL VAEAEQAELV LFDQALTPAQ QRNLERGFKL RVVDRVALIL DIFALRAQSH EGKLQVELAQ LQHLSTRLTR MWSHLERQRG GIGMRGPGEA QLEMDRRMIG DKVRLLRERL ARVQRQRTTQ RRARSRSNTL SVSLVGYTNA GKSTLFNALT RAGAYAADQL FATLDTTTRR VWIEGAGQVV ISDTVGFIRD LPPTLIAAFR ATLEETVQAD LLLHVVDAAS PQRDEQIVEV NKVLADIGAA DIPRILVYNK IDLAGYEPRM ERNEHGTIAR VFVSAVGRTG LDDLRGAIVE SGQIAGNNAF NVENI // ID F4H783_CELFA Unreviewed; 506 AA. AC F4H783; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 07-JUN-2017, entry version 43. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Celf_1583 {ECO:0000313|EMBL:AEE45717.1}; OS Cellulomonas fimi (strain ATCC 484 / DSM 20113 / JCM 1341 / NBRC 15513 OS / NCIMB 8980 / NCTC 7547). OC Bacteria; Actinobacteria; Micrococcales; Cellulomonadaceae; OC Cellulomonas. OX NCBI_TaxID=590998 {ECO:0000313|EMBL:AEE45717.1, ECO:0000313|Proteomes:UP000008460}; RN [1] {ECO:0000313|EMBL:AEE45717.1, ECO:0000313|Proteomes:UP000008460} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 484 / DSM 20113 / JCM 1341 / NBRC 15513 / NCIMB 8980 / RC NCTC 7547 {ECO:0000313|Proteomes:UP000008460}; RG US DOE Joint Genome Institute; RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S., RA Peters L., Chertkov O., Detter J.C., Han C., Tapia R., Land M., RA Hauser L., Kyrpides N., Ivanova N., Ovchinnikova G., Pagani I., RA Mead D., Brumm P., Woyke T.; RT "Complete sequence of Cellulomonas fimi ATCC 484."; RL Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002666; AEE45717.1; -; Genomic_DNA. DR RefSeq; WP_013770743.1; NC_015514.1. DR STRING; 590998.Celf_1583; -. DR EnsemblBacteria; AEE45717; AEE45717; Celf_1583. DR KEGG; cfi:Celf_1583; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000008460; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 2. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000008460}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000008460}. FT DOMAIN 285 451 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 506 AA; 54378 MW; 69E96E2ECBD2B5FF CRC64; MNDPQHTTHE AEAYDPPRSV QDVADDVVAR VLARAGTALQ DGATVHSSFD GDQLDLEERT SLRRVAGLST ELEDVTEVEY RQLRLEKVVL VGVWGTGTAE DAEISLRELA ALAETAGSEV LDGVIQRRRT PDPGTYLGSG KAAELAMLVA SVGADTVVVD GELAPSQRRA LEDIVRVKVV DRTALILDIF AQHAKSREGK AQVELAQLEY LLPRLRGWGE SMSRQAGGQV GGAGAGMGSR GPGETKIELD RRRIRNRMAK LRREIAAMEP ARRTKRASRK KNAIPSVAIA GYTNAGKSSL LNRLTNAGVL VENALFATLD PTVRRAETTD GRVYTLADTV GFVRALPHQL VEAFRSTLEE VADADLLLHV VDASHPDPEG QIAAVRHVFA DIPGAMDVPE IIVLNKADRA SAEAIARLRS REVHSVVVSA HTGEGIAELQ ALIADQLPRP GVAVDVVVPY DRGDLVSRVH EHGDIDAEEH TPLGTALRAR VDEALAAELE AASVAR // ID F4KNH5_PORAD Unreviewed; 411 AA. AC F4KNH5; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 07-JUN-2017, entry version 45. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Poras_0492 {ECO:0000313|EMBL:AEE12446.1}; OS Porphyromonas asaccharolytica (strain ATCC 25260 / DSM 20707 / BCRC OS 10618 / JCM 6326 / LMG 13178 / VPI 4198) (Bacteroides OS asaccharolyticus). OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; OC Porphyromonadaceae; Porphyromonas. OX NCBI_TaxID=879243 {ECO:0000313|EMBL:AEE12446.1, ECO:0000313|Proteomes:UP000006545}; RN [1] {ECO:0000313|Proteomes:UP000006545} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 25260 / DSM 20707 / VPI 4198 RC {ECO:0000313|Proteomes:UP000006545}; RA Lucas S., Han J., Lapidus A., Bruce D., Goodwin L., Pitluck S., RA Peters L., Kyrpides N., Mavromatis K., Ivanova N., Ovchinnikova G., RA Pagani I., Lu M., Detter J.C., Tapia R., Han C., Land M., Hauser L., RA Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Gronow S., RA Wellnitz S., Brambilla E., Klenk H.-P., Eisen J.A.; RT "The complete genome of Porphyromonas asaccharolytica DSM 20707."; RL Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002689; AEE12446.1; -; Genomic_DNA. DR RefSeq; WP_004330695.1; NC_015501.1. DR STRING; 879243.Poras_0492; -. DR EnsemblBacteria; AEE12446; AEE12446; Poras_0492. DR KEGG; pah:Poras_0492; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000006545; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000006545}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000006545}. FT DOMAIN 203 388 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 171 198 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 411 AA; 46912 MW; 3B39DE4914C3CCD1 CRC64; MKEFIKTSQS SERTILVGLI TPDVSETQAE EYLDELAFLS ETAGAEPVAR FLQRLDTPHP ATFVGKGKLD EIAEYVSAHE VGLAIFDDEL APNQLRNIER QLGIRILDRT SLILDIFATR AQTAHAKTQV EMAQYQYMLP RLTRLWTHLE RQRGGNIGLR GPGETQLETD RRIILRKISQ LKEQLKKIDK QKSVQRQNRG KMVRVALVGY TNVGKSTLMN VLAKSDIFAE NKLFATLDTT VRKVVLGNLP FLLADTVGFI RKLPTQLVES FKSTLDEVRE SDLILHVVDI SHPEFEDQIA VVTETLREIE ALGDKPQILV FNKIDAYQHI PKDPDDLTPA TKLNRTREEL EKSWMARMGN DCVFISARTG EGMDELRRLL YERVKAIHIQ RYPYNDFLYQ DYSDLLDDGA E // ID F4L6P4_HALH1 Unreviewed; 404 AA. AC F4L6P4; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 07-JUN-2017, entry version 45. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Halhy_3012 {ECO:0000313|EMBL:AEE50875.1}; OS Haliscomenobacter hydrossis (strain ATCC 27775 / DSM 1100 / LMG 10767 OS / O). OC Bacteria; Bacteroidetes; Saprospiria; Saprospirales; OC Haliscomenobacteraceae; Haliscomenobacter. OX NCBI_TaxID=760192 {ECO:0000313|EMBL:AEE50875.1, ECO:0000313|Proteomes:UP000008461}; RN [1] {ECO:0000313|EMBL:AEE50875.1, ECO:0000313|Proteomes:UP000008461} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 27775 / DSM 1100 / LMG 10767 / O RC {ECO:0000313|Proteomes:UP000008461}; RX PubMed=21886862; DOI=10.4056/sigs.1964579; RG US DOE Joint Genome Institute (JGI-PGF); RA Daligault H., Lapidus A., Zeytun A., Nolan M., Lucas S., Del Rio T.G., RA Tice H., Cheng J.F., Tapia R., Han C., Goodwin L., Pitluck S., RA Liolios K., Pagani I., Ivanova N., Huntemann M., Mavromatis K., RA Mikhailova N., Pati A., Chen A., Palaniappan K., Land M., Hauser L., RA Brambilla E.M., Rohde M., Verbarg S., Goker M., Bristow J., RA Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P., RA Woyke T.; RT "Complete genome sequence of Haliscomenobacter hydrossis type strain RT (O)."; RL Stand. Genomic Sci. 4:352-360(2011). RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 1100; RG US DOE Joint Genome Institute (JGI-PGF); RA Lucas S., Han J., Lapidus A., Bruce D., Goodwin L., Pitluck S., RA Peters L., Kyrpides N., Mavromatis K., Ivanova N., Ovchinnikova G., RA Pagani I., Daligault H., Detter J.C., Han C., Land M., Hauser L., RA Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Verbarg S., RA Frueling A., Brambilla E., Klenk H.-P., Eisen J.A.; RT "Complete sequence of chromosome of Haliscomenobacter hydrossis DSM RT 1100."; RL Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002691; AEE50875.1; -; Genomic_DNA. DR RefSeq; WP_013765418.1; NC_015510.1. DR ProteinModelPortal; F4L6P4; -. DR STRING; 760192.Halhy_3012; -. DR EnsemblBacteria; AEE50875; AEE50875; Halhy_3012. DR KEGG; hhy:Halhy_3012; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000008461; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000008461}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000008461}. FT DOMAIN 211 393 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 404 AA; 46725 MW; 20D3DFB777D4F383 CRC64; MANEWNIGEQ RKKGIAQEAE FALLVGVIHK TQTEELVEEY LDELEFLALT AGAVTVKRYT QKLVAPDPRT YIGKGKLEEI ADYIERHEEI TMVIFDDDLT GKQTNALEEA LKVKIIDRSS LILDIFATRA QTAQAKTQVE LAQMQYLLPR LRGLWTHLER QRGGIGMRGP GEKEIETDRR IIRDKIALLK EKLKVIDRQA VTQRKNRGEL IRVSLVGYTN VGKSTLMNLL SKSDVFAENK LFATLDTTVR KVAWDSVPFL LSDTVGFIRK LPHHLIESFK STLDEVLESD ILLHVVDVSH PQHEDQIRTV NETLDELKAL QKPTLFIFNK IDRYREQHYD PFLEDDAKEE IEMSIRGNLK HLFLHDNVLV SALSKEGINE LREKVLKMVK EQYHIRYPYQ SRQW // ID F4LPF2_TREBD Unreviewed; 422 AA. AC F4LPF2; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 07-JUN-2017, entry version 44. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Trebr_0520 {ECO:0000313|EMBL:AEE15963.1}; OS Treponema brennaborense (strain DSM 12168 / CIP 105900 / DD5/3). OC Bacteria; Spirochaetes; Spirochaetales; Spirochaetaceae; Treponema. OX NCBI_TaxID=906968 {ECO:0000313|EMBL:AEE15963.1, ECO:0000313|Proteomes:UP000006546}; RN [1] {ECO:0000313|Proteomes:UP000006546} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 12168 / CIP 105900 / DD5/3 RC {ECO:0000313|Proteomes:UP000006546}; RA Lucas S., Han J., Lapidus A., Bruce D., Goodwin L., Pitluck S., RA Peters L., Kyrpides N., Mavromatis K., Ivanova N., Mikhailova N., RA Pagani I., Teshima H., Detter J.C., Tapia R., Han C., Land M., RA Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T., Wu D., RA Gronow S., Wellnitz S., Brambilla E., Klenk H.-P., Eisen J.A.; RT "The complete genome of Treponema brennaborense DSM 12168."; RL Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002696; AEE15963.1; -; Genomic_DNA. DR RefSeq; WP_013757682.1; NC_015500.1. DR STRING; 906968.Trebr_0520; -. DR EnsemblBacteria; AEE15963; AEE15963; Trebr_0520. DR KEGG; tbe:Trebr_0520; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000006546; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000006546}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000006546}. FT DOMAIN 199 366 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 165 192 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 422 AA; 45941 MW; B5D37B50D68818C5 CRC64; MIDIHAEQTA KIKAYLVAAA GTSPAELKGL VSTLDMETVG VLVLSRAEPD GSVARFGIGS GKAQEIADLA SELEADCIIF DFEISPTRQR NWEKLAGVPV FDRHEVILRI FAARARTKEA VLQVELARLT YSLPRLAHSY GDMARQRGGS YGSKGAGETK LELDRRTVQD RIAQVRRELT KVVRERETQR RRRDRVPLPS CALVGYTNAG KSSLLNALTG ASVLAEDKLF ATLDPTTRRL SIAGGTSLLL TDTVGFISNL PHNLVDAFKS TLEEAVRADL LVVVIDAADP AAAEQYATVC RVLEEIGADS KPRIAVLNKT DKLAEFDVRR PALRAQFSDA VEVSAHTKAG FDVLIPRICN ALAGVERRYR IPLDQHALLT QVRKGGTIAD EQWLDGFIEF AARIGGSASG KLLSLLAPYE VE // ID F4LQS3_TEPAE Unreviewed; 413 AA. AC F4LQS3; L0S181; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 07-JUN-2017, entry version 52. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:CCP26921.1}; GN OrderedLocusNames=TEPIRE1_2097 {ECO:0000313|EMBL:CCP26921.1}; OS Tepidanaerobacter acetatoxydans (strain DSM 21804 / JCM 16047 / Re1). OC Bacteria; Firmicutes; Clostridia; Thermoanaerobacterales; OC Thermoanaerobacteraceae; Tepidanaerobacter. OX NCBI_TaxID=1209989 {ECO:0000313|EMBL:CCP26921.1, ECO:0000313|Proteomes:UP000010802}; RN [1] {ECO:0000313|Proteomes:UP000010802} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Re1 {ECO:0000313|Proteomes:UP000010802}; RX PubMed=23469343; DOI=10.1128/genomeA.00213-12; RA Manzoor S., Bongcam-Rudloff E., Schnurer A., Muller B.; RT "First genome sequence of a syntrophic acetate-oxidizing bacterium, RT Tepidanaerobacter acetatoxydans strain Re1."; RL Genome Announc. 1:E00213-E00213(2013). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; HF563609; CCP26921.1; -; Genomic_DNA. DR RefSeq; WP_013778998.1; NC_019954.2. DR ProteinModelPortal; F4LQS3; -. DR EnsemblBacteria; CCP26921; CCP26921; TepiRe1_2097. DR KEGG; tae:TepiRe1_2097; -. DR KEGG; tep:TepRe1_1948; -. DR PATRIC; fig|1209989.3.peg.2418; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR Proteomes; UP000010802; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000010802}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000010802}. FT DOMAIN 194 359 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 413 AA; 45702 MW; BD3EB9931476E6CC CRC64; MISTSDKSTR ALLLSMCNDI SDEDSFQELR LLAQTAAVEV VGEAVQKRNK IDPAYYVGRG KAEEVAQAVK ALGANAVICD DELSPVQIRN LENLTGVQII DRTMLILDIF AQRAKTSEGK IQVELAQLQY MMPRLTGKGI ELSQEGGGIG TRGPGETKLE TDRRHIRRRI HHLKEELKNV QKSRKIIIQS RSYPVISLVG YTNAGKSTLM NALTDADVKT GDRLFETLDT TTRNLVLPDG RKVLLSDTVG FIRKLPHHLV EAFRATLEEV KEADLLIHVA DGSSPTIDED IFVVNSVLKE LGAEQTPIII AINKIDISGD ASVFIEGYNK DNTIGISALT GKNLDKLLEA ICRILPSNRR KAELFIPYDS GSAVDEIHKN GLINEIEYKD DGVKIKGEID IAILKKYEKY LIN // ID F4QQS4_9CAUL Unreviewed; 441 AA. AC F4QQS4; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 07-JUN-2017, entry version 39. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:EGF90561.1}; GN ORFNames=ABI_35850 {ECO:0000313|EMBL:EGF90561.1}; OS Asticcacaulis biprosthecum C19. OC Bacteria; Proteobacteria; Alphaproteobacteria; Caulobacterales; OC Caulobacteraceae; Asticcacaulis. OX NCBI_TaxID=715226 {ECO:0000313|EMBL:EGF90561.1, ECO:0000313|Proteomes:UP000006512}; RN [1] {ECO:0000313|Proteomes:UP000006512} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C19 {ECO:0000313|Proteomes:UP000006512}; RA Brown P.J.B., Buechlein A., Hemmerich C., Brun Y.V.; RT "Draft genome sequence of Brevundimonas diminuta."; RL Submitted (MAR-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GL883079; EGF90561.1; -; Genomic_DNA. DR RefSeq; WP_006274369.1; NZ_GL883079.1. DR ProteinModelPortal; F4QQS4; -. DR STRING; 715226.ABI_35850; -. DR EnsemblBacteria; EGF90561; EGF90561; ABI_35850. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000006512; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000006512}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000006512}. FT DOMAIN 211 384 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 177 204 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 441 AA; 49377 MW; 0E035438307EC856 CRC64; MTDKYIDNAP DIVRAVVIDP DIAHAAEQRA APRLLEDSRL DEAIGLALAL DLEIAGSLSV RVRKLNPATL FGAGKVEEIK ALCEEVDASL CVVNGSLTPI QQRNLEKELE RKVIDRTGMI LEIFGRRART REGKLQVELA RLEYEKSRLV RTWTHLERQR ATGTTGGPGE TQIELDRRMI ADKIKQLKTE LDEVRRTRAL HRVQRKKVPY PIVALVGYTN AGKSTLFNHL TRAEVVAKDL LFATLDTTLR TLKLPNGRSA MLSDTVGFIS DLPHELVAAF RATLEEVEQA DLILHVRDVS NPETEAQRQD VEQVLQHILP DLDRGRMFEV WNKIDLLDPD SKEVLYARSV TSRDAQKPLP VSAVTGEGIE ALLARVANLV DADGEEIDLV LEPHQGDALA FLYQHGRVIA RHEDEDGKVH VKVKLSDMAY GRYERLSNAQ S // ID F4WWS9_ACREC Unreviewed; 479 AA. AC F4WWS9; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 07-JUN-2017, entry version 24. DE SubName: Full=Putative GTP-binding protein 6 {ECO:0000313|EMBL:EGI61401.1}; GN ORFNames=G5I_10399 {ECO:0000313|EMBL:EGI61401.1}; OS Acromyrmex echinatior (Panamanian leafcutter ant) (Acromyrmex OS octospinosus echinatior). OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; OC Pterygota; Neoptera; Holometabola; Hymenoptera; Apocrita; Aculeata; OC Vespoidea; Formicidae; Myrmicinae; Acromyrmex. OX NCBI_TaxID=103372 {ECO:0000313|Proteomes:UP000007755}; RN [1] {ECO:0000313|Proteomes:UP000007755} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=21719571; DOI=10.1101/gr.121392.111; RA Nygaard S., Zhang G., Schiott M., Li C., Wurm Y., Hu H., Zhou J., RA Ji L., Qiu F., Rasmussen M., Pan H., Hauser F., Krogh A., RA Grimmelikhuijzen C.J., Wang J., Boomsma J.J.; RT "The genome of the leaf-cutting ant Acromyrmex echinatior suggests key RT adaptations to advanced social life and fungus farming."; RL Genome Res. 0:0-0(2011). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GL888412; EGI61401.1; -; Genomic_DNA. DR RefSeq; XP_011061189.1; XM_011062887.1. DR ProteinModelPortal; F4WWS9; -. DR GeneID; 105150067; -. DR KEGG; aec:105150067; -. DR InParanoid; F4WWS9; -. DR Proteomes; UP000007755; Unassembled WGS sequence. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR CDD; cd01878; HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 2. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 4: Predicted; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000007755}; KW Reference proteome {ECO:0000313|Proteomes:UP000007755}. FT DOMAIN 262 421 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 228 258 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 479 AA; 54454 MW; 02503122B9C2FA5D CRC64; MHCIHKIINI TQRNLQVFNK VDTVDKRSGI LLQNIICRLN HNSEEYLSEE DEKKQNAYVK ITSRYLGIAV GGHRTFILQP YIKWGRDKKR NTSPELQMAE AVALINTLPN WCVVGTKYSP LLTLQRKHLL GTGAIENLKK DLRQCPNPTA IFISTNQLKF VQISELEKIF GLPVYDRYSI VIHIFREHAK TAEARLQVAL AEIPYIRKKI FETCITRSGA INVTEETKLL LDSKEKKLKN ELKKLQQHRR TIRSHRKKHG FPTVAVVGYT NAGKTSLIKV LTDDNSLQPR DKLFATLDTT AHQGILPNRL KILYMDTIGF IQDVPETLIE PFIVTLEDAM IADVVVHIYD VSHPDMKAQY QHVQQTIKPM LDARPIIDVA NKCDLVQSDC IPKDVIAVSA KDLTGIDLLR LKIQEVLLAS TGLLSIRVRV KVGSSAASWL YKMTTVTNAE SDPNDTQYLI MEVIATAVDI QKFRKFLKQ // ID F4X9B7_9FIRM Unreviewed; 429 AA. AC F4X9B7; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 07-JUN-2017, entry version 40. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=HMPREF0866_01122 {ECO:0000313|EMBL:EGJ48164.1}; OS Ruminococcaceae bacterium D16. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Ruminococcaceae; OC unclassified Ruminococcaceae. OX NCBI_TaxID=552398 {ECO:0000313|EMBL:EGJ48164.1, ECO:0000313|Proteomes:UP000002801}; RN [1] {ECO:0000313|Proteomes:UP000002801} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=D16 {ECO:0000313|Proteomes:UP000002801}; RG The Broad Institute Genome Sequencing Platform; RA Ward D., Earl A., Feldgarden M., Gevers D., Young S., Zeng Q., RA Koehrsen M., Alvarado L., Berlin A.M., Borenstein D., Chapman S.B., RA Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A., RA Gujja S., Heilman E.R., Heiman D.I., Hepburn T.A., Howarth C., Jen D., RA Larson L., Mehta T., Park D., Pearson M., Richards J., Roberts A., RA Saif S., Shea T.D., Shenoy N., Sisk P., Stolte C., Sykes S.N., RA Walk T., White J., Yandava C., Sibley C.D., White A.P., Crowley S., RA Surette M.G., Strauss J.C., Ambrose C.E., Allen-Vercoe E., Haas B., RA Nusbaum C., Birren B.; RT "The Genome Sequence of Clostridium sp. D5."; RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:EGJ48164.1, ECO:0000313|Proteomes:UP000002801} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=D16 {ECO:0000313|EMBL:EGJ48164.1, RC ECO:0000313|Proteomes:UP000002801}; RG The Broad Institute Genomics Platform; RA Earl A., Ward D., Feldgarden M., Gevers D., Sibley C.D., White A.P., RA Crowley S., Surette M.G., Strauss J.C., Ambrose C.E., Allen-Vercoe E., RA Walker B., Young S., Zeng Q., Gargeya S., Fitzgerald M., Haas B., RA Abouelleil A., Allen A.W., Alvarado L., Arachchi H.M., Berlin A.M., RA Chapman S.B., Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., RA Hansen M., Howarth C., Imamovic A., Ireland A., Larimer J., RA McCowan C., Murphy C., Pearson M., Poon T.W., Priest M., Roberts A., RA Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C., RA Birren B.; RT "The Genome Sequence of Ruminococcaceae bacterium D16."; RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EGJ48164.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADDX02000002; EGJ48164.1; -; Genomic_DNA. DR RefSeq; WP_008980957.1; NZ_KI391947.1. DR ProteinModelPortal; F4X9B7; -. DR STRING; 552398.HMPREF0866_01122; -. DR EnsemblBacteria; EGJ48164; EGJ48164; HMPREF0866_01122. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000002801; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000002801}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000002801}. FT DOMAIN 205 366 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 20 43 {ECO:0000256|SAM:Coils}. FT COILED 164 198 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 429 AA; 48207 MW; 82380F33F1C871ED CRC64; MTENFTKDKL NRAVLVGLSA HSLSREENAT EESMEELKDL LETAGGESVG MVLQQKDSPD PRTFIGQGKV DEVRQLVRTM GADMVIFDNA LSPSQQRVLG EELKVGVLDR SALILDIFAQ RARTREGRLQ VELAQYKYLL PRLIGMWSHL ERQEGAIGTR GPGETQLETD RRHIRRKISK LEEELRDVRR VRATQRQRRE KNEVPVVAIV GYTNAGKSTL LNKLTGAEIP ANNRLFDTLD TTTRTLEISD TCTVLLSDTV GFIRKLPHHL VEAFKATLEE LSFADLLLHV IDASNPEWRE QAQVVDQLIL ELGAEQTPRI EVFNKCDKWT GEIRPHGEDI VSISAKTGEG LDKLLEAIGK RLDSGAKRVT IHLPYDKGGI LDQLYQEAKV EQVEYAETID VVAVCTPKTI GQLGPLVEGW QPHKEPWED // ID F4XQ56_9CYAN Unreviewed; 542 AA. AC F4XQ56; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 07-JUN-2017, entry version 42. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=LYNGBM3L_37690 {ECO:0000313|EMBL:EGJ33285.1}; OS Moorea producens 3L. OC Bacteria; Cyanobacteria; Oscillatoriophycideae; Oscillatoriales; OC Oscillatoriaceae; Moorea. OX NCBI_TaxID=489825 {ECO:0000313|EMBL:EGJ33285.1, ECO:0000313|Proteomes:UP000003959}; RN [1] {ECO:0000313|Proteomes:UP000003959} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=3L {ECO:0000313|Proteomes:UP000003959}; RX PubMed=21555588; DOI=10.1073/pnas.1101137108; RA Jones A.C., Monroe E.A., Podell S., Hess W.R., Klages S., RA Esquenazi E., Niessen S., Hoover H., Rothmann M., Lasken R.S., RA Yates J.R.III., Reinhardt R., Kube M., Burkart M.D., Allen E.E., RA Dorrestein P.C., Gerwick W.H., Gerwick L.; RT "Genomic insights into the physiology and ecology of the marine RT filamentous cyanobacterium Lyngbya majuscula."; RL Proc. Natl. Acad. Sci. U.S.A. 108:8815-8820(2011). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GL890852; EGJ33285.1; -; Genomic_DNA. DR STRING; 489825.LYNGBM3L_37690; -. DR EnsemblBacteria; EGJ33285; EGJ33285; LYNGBM3L_37690. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000003959; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000003959}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000003959}. FT DOMAIN 369 539 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 328 365 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 542 AA; 59830 MW; 2896F2A553D272F3 CRC64; MTTPEFAQRV AAISTDIQQP LCTYINRRGQ VIRVAVGTPT QTKIPPLELP RYGAERLCGI RCIATQLKSE IPRESTLTAM AIQRLDALVV LTITGSGMIR RGGGATGYIK ETYLAHLLPP SNSEGNNQVD SQLLNWSVSS PMSLDILTKQ DFQELVEELE AEFRRQFVAQ QVDVDQDRVL IIGLMTEKIS PERFEDGLAE IGRLVETAGG EVLGVIQQKR SHPHPQTVVG SGKVEEIALT TQTLAANLVV FDRDLSPAQA RNLESQIGVR VVDRTEVILD IFAQRAQSRA GKLQVELAQL EYMLPRLTGR GQAMSRLGGG IGTRGPGETK LETERRSIQR RITRLQQEVN QLQAHRSRLR QRRQQQDVPT VAVVGYTNAG KSTLLNTLTN AEVYTADQLF ATLDPTTRRL PIIDSVTGKS SAMLLIDTVG FIHELPPPLV DSFRATLEEV TEADALLHLV DLSHSAWASH IRSVMGILRD MPITPGPILV VFNKIDQVDS DTLALAKEEF PQGVFISASK RLGLETLRQK LVELVHYAIA TQ // ID F5J244_9BACT Unreviewed; 408 AA. AC F5J244; DT 27-JUL-2011, integrated into UniProtKB/TrEMBL. DT 27-JUL-2011, sequence version 1. DT 30-AUG-2017, entry version 39. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=HMPREF9455_03439 {ECO:0000313|EMBL:EGK00300.1}; OS Dysgonomonas gadei ATCC BAA-286. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; OC Dysgonamonadaceae; Dysgonomonas. OX NCBI_TaxID=742766 {ECO:0000313|EMBL:EGK00300.1, ECO:0000313|Proteomes:UP000004913}; RN [1] {ECO:0000313|EMBL:EGK00300.1, ECO:0000313|Proteomes:UP000004913} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-286 {ECO:0000313|EMBL:EGK00300.1, RC ECO:0000313|Proteomes:UP000004913}; RG The Broad Institute Genome Sequencing Platform; RA Earl A., Ward D., Feldgarden M., Gevers D., Pudlo N., Martens E., RA Allen-Vercoe E., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., RA Haas B., Abouelleil A., Alvarado L., Arachchi H.M., Berlin A., RA Brown A., Chapman S.B., Chen Z., Dunbar C., Freedman E., Gearin G., RA Gellesch M., Goldberg J., Griggs A., Gujja S., Heiman D., Howarth C., RA Larson L., Lui A., MacDonald P.J.P., Mehta T., Montmayeur A., RA Murphy C., Neiman D., Pearson M., Priest M., Roberts A., Saif S., RA Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., Yandava C., RA Wortman J., Nusbaum C., Birren B.; RT "The Genome Sequence of Dysgonomonas gadei ATCC BAA-286."; RL Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EGK00300.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADLV01000039; EGK00300.1; -; Genomic_DNA. DR RefSeq; WP_006800972.1; NZ_GL891988.1. DR ProteinModelPortal; F5J244; -. DR STRING; 742766.HMPREF9455_03439; -. DR EnsemblBacteria; EGK00300; EGK00300; HMPREF9455_03439. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000004913; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000004913}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000004913}. FT DOMAIN 203 387 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 171 198 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 408 AA; 47275 MW; 85FB0277337EAB52 CRC64; MRDFIISESK NKEAVLVGLI TQYQTEEQVN EYLDELAFLA ETAGIIPVKN FTQKLEHSNP VTFVGTGKLQ EIKQYMEDNE IDLVIFDDEL SPKQIRNIEK ELQVKILDRT SLILDIFAMR AQTAYAKTQV ELAQYQYLLP RLTRMWTHLD RQRGGGVMMR GVGETQLETD RRIILNKIAL LKEELKNIDK QMASQRKNRG KMVRVALVGY TNVGKSTLMN LLSKSEVFAE NKLFATLDTT VRKVIIDNLP FLLSDTVGFI RKLPTHLVES FKSTLDEVRE ADLLVHVVDI SHPNFEEQIE VVNKTLLEID KEEKPTILVF NKVDAFTYTP KDEDDLTPAT KENISLEELE KSWMHKLHDD CIFISAKQKI NIDELKKKVY ERVKAIHIER YPYNDFLFQK YDDEANDA // ID F5L3N5_9BACI Unreviewed; 415 AA. AC F5L3N5; DT 27-JUL-2011, integrated into UniProtKB/TrEMBL. DT 27-JUL-2011, sequence version 1. DT 12-APR-2017, entry version 39. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=CathTA2_0394 {ECO:0000313|EMBL:EGL84048.1}; OS Caldalkalibacillus thermarum TA2.A1. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; OC Caldalkalibacillus. OX NCBI_TaxID=986075 {ECO:0000313|EMBL:EGL84048.1, ECO:0000313|Proteomes:UP000010716}; RN [1] {ECO:0000313|EMBL:EGL84048.1, ECO:0000313|Proteomes:UP000010716} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=TA2.A1 {ECO:0000313|EMBL:EGL84048.1, RC ECO:0000313|Proteomes:UP000010716}; RX PubMed=21685297; DOI=10.1128/JB.05035-11; RA Kalamorz F., Keis S., McMillan D.G., Olsson K., Stanton J.A., RA Stockwell P., Black M.A., Klingeman D.M., Land M.L., Han C.S., RA Martin S.L., Becher S.A., Peddie C.J., Morgan H.W., Matthies D., RA Preiss L., Meier T., Brown S.D., Cook G.M.; RT "Draft genome sequence of the thermoalkaliphilic Caldalkalibacillus RT thermarum strain TA2.A1."; RL J. Bacteriol. 193:4290-4291(2011). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EGL84048.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFCE01000052; EGL84048.1; -; Genomic_DNA. DR STRING; 986075.CathTA2_0394; -. DR EnsemblBacteria; EGL84048; EGL84048; CathTA2_0394. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000010716; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000010716}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000010716}. FT DOMAIN 195 356 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 415 AA; 47395 MW; CDC3F4C59D4D55B7 CRC64; MIEKAVLVGC LLPHQQEREV ESSLYELSLL AETAQAQAVC TVIQKRDRVD PAYYIGKGKV LEVASLVETY QADLVIFNDE LSPSQVNNLE QLLPCKVIDR TQLILDIFAL RARSKEGKLQ VELAQLNYLL PRIVGKGTEL SRLGGGIGTR GPGETKLELD RRHIRRRIQD IRQELDKIVA HRERYRSRRK KKQMFQVALV GYTNAGKSTL LNQLTEAEAY TENQLFATLD PLTKQMRLPS GHIVLLTDTV GFIRDLPTTL VAAFRSTLEE VKEADLILHV IDSHDDNHQD QIDVVESLLT ELDAGHIPVV RIFNKKDLPP APELKVRPED LYITALDPHD CWRVKERIET VLKQQMHTYQ LLLPASEAQL ISKLRQVGFV EQLTWDEGQQ GYRVTLHLPV YHPLKNKIEP FRIQH // ID F5LIA6_9BACL Unreviewed; 430 AA. AC F5LIA6; DT 27-JUL-2011, integrated into UniProtKB/TrEMBL. DT 27-JUL-2011, sequence version 1. DT 07-JUN-2017, entry version 40. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:EGL17971.1}; GN ORFNames=HMPREF9413_4276 {ECO:0000313|EMBL:EGL17971.1}; OS Paenibacillus sp. HGF7. OC Bacteria; Firmicutes; Bacilli; Bacillales; Paenibacillaceae; OC Paenibacillus. OX NCBI_TaxID=944559 {ECO:0000313|EMBL:EGL17971.1, ECO:0000313|Proteomes:UP000003445}; RN [1] {ECO:0000313|EMBL:EGL17971.1, ECO:0000313|Proteomes:UP000003445} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=HGF7 {ECO:0000313|EMBL:EGL17971.1, RC ECO:0000313|Proteomes:UP000003445}; RA Durkin A.S., Madupu R., Torralba M., Gillis M., Methe B., Sutton G., RA Nelson K.E.; RL Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EGL17971.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFDH01000056; EGL17971.1; -; Genomic_DNA. DR RefSeq; WP_009673822.1; NZ_AFDH01000056.1. DR STRING; 944559.HMPREF9413_4276; -. DR EnsemblBacteria; EGL17971; EGL17971; HMPREF9413_4276. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000003445; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000003445}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000003445}. FT DOMAIN 198 366 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 157 184 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 430 AA; 48320 MW; ED74B297D774F52B CRC64; MERQKQKAIL IGIHPGNRTD FGYFMEELAN LAAAAGIEEA GMLTQKLARS NPSHYIGKGK IEELLELIET HGADLVICND ELTPSQLRNL EAALNRTVMD RTALILAIFA ERARTREAQL QVEVARLHYM LPRLVGLRES LGRQGGGSGL KNRGAGETKL ELDRRRIEER IVMLQKELEQ LVSHRQTQRK KRRKTEVPVV CLVGYTNAGK SSLMNAMMEA HNPGPGKQVM AEDRLFATLE TSVRSIRLQD GRSFLLTDTV GFVSQLPHHL VKAFRSTLEE VAEADLLLHV VDSSSPVYER QMAVTEETLK ELGADHIPKL LVYNKADLSS LEFPCADNGN VVISAKRRAG ISELTEQIRK RVFRHEVRCE LLVPYDQSHV AAYFNEFARV RSIRYEADGA RLTVECPESV LERYRGSYIP LSEGQAYPGH // ID F5LK42_9BACL Unreviewed; 439 AA. AC F5LK42; DT 27-JUL-2011, integrated into UniProtKB/TrEMBL. DT 27-JUL-2011, sequence version 1. DT 07-JUN-2017, entry version 39. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:EGL17242.1}; GN ORFNames=HMPREF9413_3087 {ECO:0000313|EMBL:EGL17242.1}; OS Paenibacillus sp. HGF7. OC Bacteria; Firmicutes; Bacilli; Bacillales; Paenibacillaceae; OC Paenibacillus. OX NCBI_TaxID=944559 {ECO:0000313|EMBL:EGL17242.1, ECO:0000313|Proteomes:UP000003445}; RN [1] {ECO:0000313|EMBL:EGL17242.1, ECO:0000313|Proteomes:UP000003445} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=HGF7 {ECO:0000313|EMBL:EGL17242.1, RC ECO:0000313|Proteomes:UP000003445}; RA Durkin A.S., Madupu R., Torralba M., Gillis M., Methe B., Sutton G., RA Nelson K.E.; RL Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EGL17242.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFDH01000074; EGL17242.1; -; Genomic_DNA. DR RefSeq; WP_009674337.1; NZ_AFDH01000074.1. DR ProteinModelPortal; F5LK42; -. DR STRING; 944559.HMPREF9413_3087; -. DR EnsemblBacteria; EGL17242; EGL17242; HMPREF9413_3087. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000003445; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000003445}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000003445}. FT DOMAIN 208 372 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 439 AA; 49352 MW; 1BF2B80A1B26A134 CRC64; MKQTGHEVRT GMKDRAILVS LVTDKMKKHE ELVAYSLQEL IQLAETAGVE VLETLTQNRE SADTKWFIGK GKVEELKALI DEHQATTAIF DQELSGAQVR NLEESLDVKI IDRTQLILDI FAGRARTREG IVQVELAQLS YLLPRLSGHG KNLSRLGGGI GTRGPGESKL ETDRRHIRGR IGELKAHLQE MVRHRTLHRE RRRKTGVYQV ALVGYTNSGK STLLRQLTNA DVYVQNELFA TLDPTSRTLE LPSGKEVVLT DTVGFIQNLP HDVVAAFRAT LEEACEADFL LHVVDSSSPM REEQMRVVNE VLGDLGASGK PQAVLFNKID LCTEQELQML TTNLPHLRIS AYDEADQERV RLLIQETLMG DSRTFRIPAD KGDIIALVYR VGDVAESGAE EDVLTFRVNI NKEDYDKVQY LLAPYEVKEE KDKQDKQGE // ID F5R8W0_METUF Unreviewed; 421 AA. AC F5R8W0; DT 27-JUL-2011, integrated into UniProtKB/TrEMBL. DT 27-JUL-2011, sequence version 1. DT 30-AUG-2017, entry version 42. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=METUNv1_00761 {ECO:0000313|EMBL:EGK72927.1}; OS Methyloversatilis universalis (strain ATCC BAA-1314 / JCM 13912 / OS FAM5). OC Bacteria; Proteobacteria; Betaproteobacteria; Nitrosomonadales; OC Sterolibacteriaceae; Methyloversatilis. OX NCBI_TaxID=1000565 {ECO:0000313|EMBL:EGK72927.1, ECO:0000313|Proteomes:UP000005019}; RN [1] {ECO:0000313|EMBL:EGK72927.1, ECO:0000313|Proteomes:UP000005019} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-1314 / JCM 13912 / FAM5 RC {ECO:0000313|Proteomes:UP000005019}; RX PubMed=21725020; DOI=10.1128/JB.05331-11; RA Kittichotirat W., Good N.M., Hall R., Bringel F., Lajus A., RA Medigue C., Smalley N.E., Beck D., Bumgarner R., Vuilleumier S., RA Kalyuzhnaya M.G.; RT "Genome sequence of Methyloversatilis universalis FAM5T, a RT methylotrophic representative of the order Rhodocyclales."; RL J. Bacteriol. 193:4541-4542(2011). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EGK72927.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFHG01000030; EGK72927.1; -; Genomic_DNA. DR RefSeq; WP_008058982.1; NZ_AFHG01000030.1. DR ProteinModelPortal; F5R8W0; -. DR STRING; 1000565.METUNv1_00761; -. DR EnsemblBacteria; EGK72927; EGK72927; METUNv1_00761. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000005019; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000005019}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000005019}. FT DOMAIN 198 365 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 421 AA; 45168 MW; 0C5102A3CD0DDB78 CRC64; MFDRPSGGER AVIVQLDLGA GDYENRLDEF TLLVRSAGAE PVARVGGRRQ SPDPATFAGK GKVAEILDLA NAGEADIVLF NHELSPAQQR NLERALQRRV IDRNALILDI FALRARSHEG KLQVELAQLE HLSTRLVRGW THLERQKGGI GLRGPGETQL ETDRRLLGVR VKALKERLAK VERQRGVRRK SRERRATPVV ALVGYTNAGK STLFNALTKA GTYAADQLFA TLDTTSRQLY LGEFGQVVLS DTVGFIRDLP HTLVAAFHAT LEETAGADLL LHVIDASAPD RDAQIEAVDR VLAEVGADAV PQIRVLNKID LMPALAPGAD AGGCDTIQTV RVSARTGAGL AELRAAVAQR LADEKAAAAL RRPPNDDPRG LELEPSAGSA LRAIAAPEAD NAGASGADEA PYDPSILTYP V // ID F5S872_9NEIS Unreviewed; 378 AA. AC F5S872; DT 27-JUL-2011, integrated into UniProtKB/TrEMBL. DT 27-JUL-2011, sequence version 1. DT 07-JUN-2017, entry version 37. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:EGK08393.1}; GN ORFNames=HMPREF0476_1405 {ECO:0000313|EMBL:EGK08393.1}; OS Kingella kingae ATCC 23330. OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Kingella. OX NCBI_TaxID=887327 {ECO:0000313|EMBL:EGK08393.1, ECO:0000313|Proteomes:UP000004207}; RN [1] {ECO:0000313|EMBL:EGK08393.1, ECO:0000313|Proteomes:UP000004207} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 23330 {ECO:0000313|EMBL:EGK08393.1, RC ECO:0000313|Proteomes:UP000004207}; RA Muzny D., Qin X., Deng J., Jiang H., Liu Y., Qu J., Song X.-Z., RA Zhang L., Thornton R., Coyle M., Francisco L., Jackson L., Javaid M., RA Korchina V., Kovar C., Mata R., Mathew T., Ngo R., Nguyen L., RA Nguyen N., Okwuonu G., Ongeri F., Pham C., Simmons D., RA Wilczek-Boney K., Hale W., Jakkamsetti A., Pham P., Ruth R., RA San Lucas F., Warren J., Zhang J., Zhao Z., Zhou C., Zhu D., Lee S., RA Bess C., Blankenburg K., Forbes L., Fu Q., Gubbala S., Hirani K., RA Jayaseelan J.C., Lara F., Munidasa M., Palculict T., Patil S., RA Pu L.-L., Saada N., Tang L., Weissenberger G., Zhu Y., Hemphill L., RA Shang Y., Youmans B., Ayvaz T., Ross M., Santibanez J., Aqrawi P., RA Gross S., Joshi V., Fowler G., Nazareth L., Reid J., Worley K., RA Petrosino J., Highlander S., Gibbs R.; RL Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EGK08393.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFHS01000046; EGK08393.1; -; Genomic_DNA. DR RefSeq; WP_003787541.1; NZ_GL891961.1. DR ProteinModelPortal; F5S872; -. DR STRING; 887327.HMPREF0476_1405; -. DR EnsemblBacteria; EGK08393; EGK08393; HMPREF0476_1405. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000004207; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000004207}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000004207}. FT DOMAIN 213 378 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 378 AA; 42090 MW; 69FDC5184D2F355E CRC64; MTRFRTDKTL EHAERIMLVS VILSSSYTGT NELREQQFKA ACTEAAELVH ATGGKLVCSE TAKRDKAHSA LFVGTGKAEE LAQVVQQNNI ELVIFNHELS PTQERNLEKI LQCRVLDRVG LILAIFAQRA QSQEGKLQVE LAQLSHLSSR LVRGYKHLQS QKGGIGLKGP GETQLETDRR LIQTKITQLR HQLDNVKKQR ETRRKARLQG NIKTFAIVGY TNAGKSTLFN RLTKSDVLAK DQLFATLDTT ARRLYLNPEA SIILTDTVGF VQDLPHKLVS AFSATLEETA LADVLLHLVD ASDPELERKI QDVNNVLAEI KADKIPQILV YNKIDLLPKT EQSAGYLRDL QQQITAVRVS ASSGAGLDDL RLALIERV // ID F5SC01_9BACL Unreviewed; 408 AA. AC F5SC01; DT 27-JUL-2011, integrated into UniProtKB/TrEMBL. DT 27-JUL-2011, sequence version 1. DT 07-JUN-2017, entry version 38. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:EGK13752.1}; GN ORFNames=HMPREF9374_0632 {ECO:0000313|EMBL:EGK13752.1}; OS Desmospora sp. 8437. OC Bacteria; Firmicutes; Bacilli; Bacillales; Thermoactinomycetaceae; OC Desmospora. OX NCBI_TaxID=997346 {ECO:0000313|EMBL:EGK13752.1, ECO:0000313|Proteomes:UP000004046}; RN [1] {ECO:0000313|EMBL:EGK13752.1, ECO:0000313|Proteomes:UP000004046} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=8437 {ECO:0000313|EMBL:EGK13752.1, RC ECO:0000313|Proteomes:UP000004046}; RA Muzny D., Qin X., Deng J., Jiang H., Liu Y., Qu J., Song X.-Z., RA Zhang L., Thornton R., Coyle M., Francisco L., Jackson L., Javaid M., RA Korchina V., Kovar C., Mata R., Mathew T., Ngo R., Nguyen L., RA Nguyen N., Okwuonu G., Ongeri F., Pham C., Simmons D., RA Wilczek-Boney K., Hale W., Jakkamsetti A., Pham P., Ruth R., RA San Lucas F., Warren J., Zhang J., Zhao Z., Zhou C., Zhu D., Lee S., RA Bess C., Blankenburg K., Forbes L., Fu Q., Gubbala S., Hirani K., RA Jayaseelan J.C., Lara F., Munidasa M., Palculict T., Patil S., RA Pu L.-L., Saada N., Tang L., Weissenberger G., Zhu Y., Hemphill L., RA Shang Y., Youmans B., Ayvaz T., Ross M., Santibanez J., Aqrawi P., RA Gross S., Joshi V., Fowler G., Nazareth L., Reid J., Worley K., RA Petrosino J., Highlander S., Gibbs R.; RL Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EGK13752.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFHT01000044; EGK13752.1; -; Genomic_DNA. DR RefSeq; WP_009708700.1; NZ_GL892032.1. DR ProteinModelPortal; F5SC01; -. DR STRING; 997346.HMPREF9374_0632; -. DR EnsemblBacteria; EGK13752; EGK13752; HMPREF9374_0632. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000004046; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000004046}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000004046}. FT DOMAIN 187 348 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 146 180 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 408 AA; 46007 MW; AC753213CF1D3280 CRC64; MGCGSGRETA SIHSSLTELE RLAHTAGAIV VDTVIQHRDA PDPGWLIGRG KVEELAQTVE EEKIDLILFD RELSPVQLVN LERRIPCKVL DRTQLILDIF AMRARTKEGS LQVELAQLEY SLPRLIGRGK EMSRLGGGIG TRGPGEKKLE TDRRHIRRRI RDLKRELEGV RKHRRLHQNR RRKMDMIQVA LVGYTNAGKS TLLNRLTGAG VMEEDRLFAT LDPTSRFLDL PSGEKVLLTD TVGFIRNLPH HLVAAFRSTL EQVGEADLLL HVVDASHPEA MEQMKSVERV LEDLGAGEVP VLTVFNKADR EGGAILSAEG ETIRISAYDA DDRERLKEKI DRVLNAAQIH GSAEIPVSRG EMISRLYRVA EIVHSEVTDL TLRVEFRLPL RRYERMSPEM KSLIRKDI // ID F5SZI8_9GAMM Unreviewed; 381 AA. AC F5SZI8; DT 27-JUL-2011, integrated into UniProtKB/TrEMBL. DT 27-JUL-2011, sequence version 1. DT 07-JUN-2017, entry version 38. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=MAMP_01810 {ECO:0000313|EMBL:EGL54816.1}; OS Methylophaga aminisulfidivorans MP. OC Bacteria; Proteobacteria; Gammaproteobacteria; Thiotrichales; OC Piscirickettsiaceae; Methylophaga. OX NCBI_TaxID=1026882 {ECO:0000313|EMBL:EGL54816.1, ECO:0000313|Proteomes:UP000003544}; RN [1] {ECO:0000313|EMBL:EGL54816.1, ECO:0000313|Proteomes:UP000003544} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MP(T) {ECO:0000313|Proteomes:UP000003544}; RX PubMed=21685284; DOI=10.1128/JB.05403-11; RA Han G.H., Kim W., Chun J., Kim S.W.; RT "Draft genome sequence of Methylophaga aminisulfidivorans MP T."; RL J. Bacteriol. 193:4265-4265(2011). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EGL54816.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFIG01000001; EGL54816.1; -; Genomic_DNA. DR RefSeq; WP_007144702.1; NZ_AFIG01000001.1. DR ProteinModelPortal; F5SZI8; -. DR STRING; 1026882.MAMP_01810; -. DR EnsemblBacteria; EGL54816; EGL54816; MAMP_01810. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000003544; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000003544}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000003544}. FT DOMAIN 207 374 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 381 AA; 43256 MW; 24794792476FF953 CRC64; MFERPDIQTA FDDSSEKEAV VLVHLNFNDP DYEDSQQEFI ELVGSTGAKI AAIIQGKRHR PDPKFFAGSG KVDEIAENVM ASHAALVIFN HELSPSQERN LEQQLKCRVL GRTGLILDIF ARRARSHEGK LQVELAQLQH LSTRLVRGWT HLERQKGGIG LRGPGETQLE TDRRLLGQRI KSLKKRLGKV QSQREQGRRS RQRGGVPVVS LVGYTNVGKS TLFNKITSAK VYADDRLFAT LDPTLRRVKL HDTQLLILAD TVGFIRDLPH DLVESFRSTL EETRDAELLL HVVDCGANDR DDLIHHVNEV LKQIDADEVR QLIVYNKIDN VEDISPRIER DDEGNIDRIW LSAKTGEGLE LLREALKEYF PEESFSEYVE A // ID F5WRH4_ERYRF Unreviewed; 426 AA. AC F5WRH4; DT 27-JUL-2011, integrated into UniProtKB/TrEMBL. DT 27-JUL-2011, sequence version 1. DT 07-JUN-2017, entry version 40. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:BAK31356.1}; GN OrderedLocusNames=ERH_0297 {ECO:0000313|EMBL:BAK31356.1}; OS Erysipelothrix rhusiopathiae (strain Fujisawa). OC Bacteria; Firmicutes; Erysipelotrichia; Erysipelotrichales; OC Erysipelotrichaceae; Erysipelothrix. OX NCBI_TaxID=650150 {ECO:0000313|EMBL:BAK31356.1, ECO:0000313|Proteomes:UP000007944}; RN [1] {ECO:0000313|EMBL:BAK31356.1, ECO:0000313|Proteomes:UP000007944} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Fujisawa {ECO:0000313|EMBL:BAK31356.1, RC ECO:0000313|Proteomes:UP000007944}; RX PubMed=21478354; DOI=10.1128/JB.01500-10; RA Ogawa Y., Ooka T., Shi F., Ogura Y., Nakayama K., Hayashi T., RA Shimoji Y.; RT "The genome of Erysipelothrix rhusiopathiae, the causative agent of RT swine erysipelas, reveals new insights into the evolution of RT firmicutes and the organism's intracellular adaptations."; RL J. Bacteriol. 193:2959-2971(2011). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AP012027; BAK31356.1; -; Genomic_DNA. DR RefSeq; WP_003775630.1; NC_015601.1. DR ProteinModelPortal; F5WRH4; -. DR STRING; 650150.ERH_0297; -. DR EnsemblBacteria; BAK31356; BAK31356; ERH_0297. DR KEGG; erh:ERH_0297; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000007944; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000007944}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000007944}. FT DOMAIN 200 373 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 426 AA; 48083 MW; 7315AEF0E5E8D04C CRC64; MLDTKTIKER VVLVGVDFGK KDFDLESSMI ELGDLVEAAE GTVVYQITQN RDRPESATYI GIGKIEEVMR AVATYDADTV VFNDELSGSQ IRNLESLIGC KIVDRTNLIL DIFALRATTA EGKLQVKLAQ LKYRLPRLIG YSDYLSRTGG GIGTRGPGEQ KLELDRRHIQ REILHVQNAL TKSEENREIT RSKRLNSNLP IISFVGYTNA GKSTLMNAIL TNGDPQANDK HVFVKDMLFA TLEPSMRKAR LNNGLNVILT DTVGFVSKLP HTLVEAFKGT LEEIKYSDLI IHVVDASNPD LNIQMDTTYK MLRDLDVLDR KIITVFNKMD QAMDQDIVFY QSEFGNRMYI SALDIEDIDR LVDAIEVELE SSFKKVSFEI PFADLGILDA IASNYEIIGL NYTEKGAQFR AVIRESDQNR YKKYII // ID F5XDX2_MICPN Unreviewed; 469 AA. AC F5XDX2; DT 27-JUL-2011, integrated into UniProtKB/TrEMBL. DT 27-JUL-2011, sequence version 1. DT 07-JUN-2017, entry version 43. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=MLP_21310 {ECO:0000313|EMBL:BAK35145.1}; OS Microlunatus phosphovorus (strain ATCC 700054 / DSM 10555 / JCM 9379 / OS NBRC 101784 / NCIMB 13414 / VKM Ac-1990 / NM-1). OC Bacteria; Actinobacteria; Propionibacteriales; Propionibacteriaceae; OC Microlunatus. OX NCBI_TaxID=1032480 {ECO:0000313|EMBL:BAK35145.1, ECO:0000313|Proteomes:UP000007947}; RN [1] {ECO:0000313|EMBL:BAK35145.1, ECO:0000313|Proteomes:UP000007947} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700054 / DSM 10555 / JCM 9379 / NBRC 101784 / NCIMB 13414 RC / VKM Ac-1990 / NM-1 {ECO:0000313|Proteomes:UP000007947}; RA Hosoyama A., Sasaki K., Harada T., Igarashi R., Kawakoshi A., RA Sasagawa M., Fukada J., Nakamura S., Katano Y., Hanada S., RA Kamagata Y., Nakamura N., Yamazaki S., Fujita N.; RT "Whole genome sequence of Microlunatus phosphovorus NM-1."; RL Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AP012204; BAK35145.1; -; Genomic_DNA. DR RefSeq; WP_013863017.1; NC_015635.1. DR ProteinModelPortal; F5XDX2; -. DR STRING; 1032480.MLP_21310; -. DR EnsemblBacteria; BAK35145; BAK35145; MLP_21310. DR KEGG; mph:MLP_21310; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000007947; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 2. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000007947}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000007947}. FT DOMAIN 247 412 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 213 240 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 469 AA; 50747 MW; B01ECE5B72335DB8 CRC64; MSVPESEYAP DYDGEQLDLQ ERHSLRRVAG MSTELTDVTE VEYRQLRLER VVLVSVWTTG SEVDAENAMA ELKLLAETAG SEVLEGLVQR RLRPDPATYI GRGKVAELRE IVVATGADTV ICDGELAPAQ LRNLEDRVKV KVIDRTALIL DIFAQHAKSA EGQAQVELAQ LQYLKQRLRG WGGNLSRQAG GRASGGAGIG GRGPGETKLE TDRRRIHSRI AKLRATLREL DANRQLKRAE RQRHQVPSVA IVGYTNAGKS SVLNRLTGAG VLVEDALFAT LDPTTRRAQT SDGRVYTLTD TVGFVRHLPH DLVEAFASTL EESAQADLLV HVVDASDPDP VGQIKAVRSV LADIGAGDVP ELIVLNKADK ASREAITTLR TAAPGAVVTS ARTGEGIDEL RAAVESGLPR PERELRVLLP YERGDLVDRI HTSGELLSVE HTEHGSLVTA RVHPDLAGEL GPYTLAASS // ID F5XX47_RAMTT Unreviewed; 399 AA. AC F5XX47; DT 27-JUL-2011, integrated into UniProtKB/TrEMBL. DT 27-JUL-2011, sequence version 1. DT 07-JUN-2017, entry version 41. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:AEG92991.1}; GN OrderedLocusNames=Rta_19000 {ECO:0000313|EMBL:AEG92991.1}; OS Ramlibacter tataouinensis (strain ATCC BAA-407 / DSM 14655 / LMG 21543 OS / TTB310). OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Comamonadaceae; Ramlibacter. OX NCBI_TaxID=365046 {ECO:0000313|EMBL:AEG92991.1, ECO:0000313|Proteomes:UP000008385}; RN [1] {ECO:0000313|Proteomes:UP000008385} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-407 / DSM 14655 / LMG 21543 / TTB310 RC {ECO:0000313|Proteomes:UP000008385}; RA Barakat M., Ortet P., De Luca G., Jourlin-Castelli C., Ansaldi M., RA Py B., Fichant G., Coutinho P., Voulhoux R., Bastien O., Roy S., RA Marechal E., Henrissat B., Quentin Y., Noirot P., Filloux A., RA Mejean V., DuBow M., Barras F., Heulin T.; RT "Genome of the cyst-dividing bacterium Ramlibacter tataouinensis."; RL Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000245; AEG92991.1; -; Genomic_DNA. DR RefSeq; WP_013901223.1; NC_015677.1. DR ProteinModelPortal; F5XX47; -. DR STRING; 365046.Rta_19000; -. DR EnsemblBacteria; AEG92991; AEG92991; Rta_19000. DR KEGG; rta:Rta_19000; -. DR PATRIC; fig|365046.3.peg.1937; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000008385; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000008385}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000008385}. FT DOMAIN 202 382 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 399 AA; 43394 MW; 70A121FFD6B13B82 CRC64; MSETPQTQRP AASAILVGVD LGHPHFDAEL EELGLLAQTA GLEPVARVTC KRKAPDAALF IGSGKADEIK LLAEQAGASE VLFDQSLSPA QQRNLERHLG LPVNDRTLLI LEIFAQRARS HEGKLQVELA RLQYVSTRLV RRWSHLERQT GGAGVRGGPG EKQIELDRRM IGEAIKRTRE RLEKVKKQRH TQRRQRERQG AFNISLVGYT NAGKSTLFNS LVKARAYAAD QLFATLDTTT RQLYLGPNPD DPQGGGRSVS LSDTVGFIRD LPHGLIDAFE ATLQEAADAD LLLHVVDAAN PNHPEQIAEV QRVLREIGAD QVPQLLVFNK VDALDAGQHP RQAEDVFELE GTPVPRLFVS GRSGHGLPAL RSRLAEAAAG ARGAALALPG DPEMQGTVA // ID F5YCG7_TREAZ Unreviewed; 423 AA. AC F5YCG7; DT 27-JUL-2011, integrated into UniProtKB/TrEMBL. DT 27-JUL-2011, sequence version 1. DT 07-JUN-2017, entry version 41. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:AEF80145.1}; GN OrderedLocusNames=TREAZ_2843 {ECO:0000313|EMBL:AEF80145.1}; OS Treponema azotonutricium (strain ATCC BAA-888 / DSM 13862 / ZAS-9). OC Bacteria; Spirochaetes; Spirochaetales; Spirochaetaceae; Treponema. OX NCBI_TaxID=545695 {ECO:0000313|EMBL:AEF80145.1, ECO:0000313|Proteomes:UP000009222}; RN [1] {ECO:0000313|Proteomes:UP000009222} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-888 / DSM 13862 / ZAS-9 RC {ECO:0000313|Proteomes:UP000009222}; RA Tetu S.G., Matson E., Ren Q., Seshadri R., Elbourne L., Hassan K.A., RA Durkin A., Radune D., Mohamoud Y., Shay R., Jin S., Zhang X., RA Lucey K., Ballor N.R., Ottesen E., Rosenthal R., Allen A., RA Leadbetter J.R., Paulsen I.T.; RT "Complete sequence of Treponema azotonutricium strain ZAS-9."; RL Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001841; AEF80145.1; -; Genomic_DNA. DR RefSeq; WP_015712695.1; NC_015577.1. DR ProteinModelPortal; F5YCG7; -. DR STRING; 545695.TREAZ_2843; -. DR EnsemblBacteria; AEF80145; AEF80145; TREAZ_2843. DR KEGG; taz:TREAZ_2843; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000009222; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000009222}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000009222}. FT DOMAIN 205 371 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 164 198 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 423 AA; 47236 MW; D9FA6202DD7D035F CRC64; MKETLSTEEK APRAFLIGIR DNKISKKEAE SLGRELLDLC GTLGLEIAGQ ETVHIRENHA QYGMGTGKAA ELSEKAIELA ADCLVFDRDI SPSQQRNWEE LTGISVIDRQ ELIIQIFSGR ARTREADLQV SLAELYYSLP RLQHKYIDLN RQRGGRYGTK GSGETRLETD RRLVEQRIHR LEEELETVRR QRDTQRKQRQ KQGMQVCAIV GYTNAGKSTL LNALTGAEVL AEDKLFATLD STSRRLLLPG GLPILLVDTV GFIRRLPHNL VNAFRSTLEE ASLSDLLIHV LDASDPDAPA YYDTTLQVLR ELGADKVPML TVLNKADRPE ASAYIEDLKT RYEGAIPLSA STGEGLSDLL ARMESLLAGA VQSFRFPHAR SDLAAMLHRS GTVLSEKYED EFIEMDARVD ERTAGKLKEF VVG // ID F5YK46_TREPZ Unreviewed; 447 AA. AC F5YK46; DT 27-JUL-2011, integrated into UniProtKB/TrEMBL. DT 27-JUL-2011, sequence version 1. DT 07-JUN-2017, entry version 43. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:AEF84513.1}; GN OrderedLocusNames=TREPR_0639 {ECO:0000313|EMBL:AEF84513.1}; OS Treponema primitia (strain ATCC BAA-887 / DSM 12427 / ZAS-2). OC Bacteria; Spirochaetes; Spirochaetales; Spirochaetaceae; Treponema. OX NCBI_TaxID=545694 {ECO:0000313|EMBL:AEF84513.1, ECO:0000313|Proteomes:UP000009223}; RN [1] {ECO:0000313|Proteomes:UP000009223} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-887 / DSM 12427 / ZAS-2 RC {ECO:0000313|Proteomes:UP000009223}; RA Tetu S.G., Matson E., Ren Q., Seshadri R., Elbourne L., Hassan K.A., RA Durkin A., Radune D., Mohamoud Y., Shay R., Jin S., Zhang X., RA Lucey K., Ballor N.R., Ottesen E., Rosenthal R., Allen A., RA Leadbetter J.R., Paulsen I.T.; RT "Complete sequence of Treponema primitia strain ZAS-2."; RL Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001843; AEF84513.1; -; Genomic_DNA. DR RefSeq; WP_015709388.1; NC_015578.1. DR ProteinModelPortal; F5YK46; -. DR STRING; 545694.TREPR_0639; -. DR EnsemblBacteria; AEF84513; AEF84513; TREPR_0639. DR KEGG; tpi:TREPR_0639; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000009223; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000009223}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000009223}. FT DOMAIN 204 381 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 164 198 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 447 AA; 49743 MW; 0EF34300A1B9957B CRC64; MAELYETEIA PKRALLISIR SGKSGAVETE SMAKELAGLV KTLGFEIAAQ ETVHIRENHP KFGMGTGKAE EMAEKAAELE ADCLVFDGDL SPSQQRNWER LTGISAVDRQ ELIIQIFAGR AKTREAELQV SLAELYYTLP RLTHKYIDLS RQRGGRYGTK GSGETKLETD RRQIEQRIHR LKEELEGVRK NRETQRKKRD RDSASCALVG YTNSGKSSLL NALTGADVLA EDKLFATLDA TTRVLPSKGR TLVISDTVGF IRRLPHALIN AFRSTLEETA QADLLIHVLD ASDPDIDQYF ETTLSVLREL GAVSSVEAAG RPSPPDKKPM LTVLNKIDRL EPPSLDYLLK RYPGSIPVSA LTGAGLEELV LRIDEALSGP ARRFRFPPNR SDLAAMVHRN GTVLSESYED TYIEIEARLE ESITEKLREY LDTELNDPGR IPAWNGK // ID F5YW56_MYCSD Unreviewed; 466 AA. AC F5YW56; DT 27-JUL-2011, integrated into UniProtKB/TrEMBL. DT 27-JUL-2011, sequence version 1. DT 07-JUN-2017, entry version 40. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:AEF36467.1}; GN OrderedLocusNames=JDM601_2467 {ECO:0000313|EMBL:AEF36467.1}; OS Mycobacterium sinense (strain JDM601). OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae; OC Mycobacterium. OX NCBI_TaxID=875328 {ECO:0000313|EMBL:AEF36467.1, ECO:0000313|Proteomes:UP000009224}; RN [1] {ECO:0000313|EMBL:AEF36467.1, ECO:0000313|Proteomes:UP000009224} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=JDM601 {ECO:0000313|EMBL:AEF36467.1, RC ECO:0000313|Proteomes:UP000009224}; RX PubMed=21685274; DOI=10.1128/JB.05291-11; RA Zhang Z.Y., Sun Z.Q., Wang Z.L., Wen Z.L., Sun Q.W., Zhu Z.Q., RA Song Y.Z., Zhao J.W., Wang H.H., Zhang S.L., Guo X.K.; RT "Complete gnome sequence of a novel clinical isolate, the RT nontuberculous Mycobacterium strain JDM601."; RL J. Bacteriol. 193:4300-4301(2011). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002329; AEF36467.1; -; Genomic_DNA. DR RefSeq; WP_013829397.1; NC_015576.1. DR ProteinModelPortal; F5YW56; -. DR STRING; 875328.JDM601_2467; -. DR EnsemblBacteria; AEF36467; AEF36467; JDM601_2467. DR KEGG; mjd:JDM601_2467; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000009224; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 2. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000009224}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000009224}. FT DOMAIN 243 412 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 202 236 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 466 AA; 49955 MW; 1B83DFFBC628FEDD CRC64; MSHPELPSTG ELALDDRTAL RRVAGLSTEL ADVSEVEYRQ LRLERVVLVG VWTEGSAAEA DASMVELAAL AETAGSQVLE GLIQRRDRPD PSTYIGSGKA VELREVVLAT GADTVICDGE LSPAQLTALE KAVKVKVIDR TALILDIFAQ HATSAEGKAQ VALAQMAYML PRLRGWGESM SRQAGGRAGG SGGGVGLRGP GETKIETDRR RIRERMAKLR REIKAMKQVR DTQRSRRLHS DVPSVAIVGY TNAGKSSLLN ALTGAGVLVQ DALFATLEPT TRRGLFEDDR PFVLTDTVGF VRHLPTQLVE AFRSTLEEVA DADLLLHVVD GADPAPLAQI SAVRQVISEV IAERDAKPAP ELLVVNKIDA AGDLALAQLR RALPDAVFVS AHTGDGIESL RRRMGQLVAP ADTAVDVVIP YERGDLVARV HEQGRLTQAE HGEGGTRIRA RVPAALAASL REFGQA // ID F5Z6E9_ALTNA Unreviewed; 429 AA. AC F5Z6E9; DT 27-JUL-2011, integrated into UniProtKB/TrEMBL. DT 27-JUL-2011, sequence version 1. DT 30-AUG-2017, entry version 42. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=ambt_19855 {ECO:0000313|EMBL:AEF05462.1}; OS Alteromonas naphthalenivorans. OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales; OC Alteromonadaceae; Alteromonas. OX NCBI_TaxID=715451 {ECO:0000313|EMBL:AEF05462.1, ECO:0000313|Proteomes:UP000000683}; RN [1] {ECO:0000313|EMBL:AEF05462.1, ECO:0000313|Proteomes:UP000000683} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=JCM 17741 / KACC 18427 / KCTC 11700BP / SN2 RC {ECO:0000313|Proteomes:UP000000683}; RX PubMed=21705606; DOI=10.1128/JB.05252-11; RA Jin H.M., Jeong H., Moon E.J., Math R.K., Lee K., Kim H.J., Jeon C.O., RA Oh T.K., Kim J.F.; RT "Complete genome sequence of the polycyclic aromatic hydrocarbon- RT degrading bacterium Alteromonas sp. strain SN2."; RL J. Bacteriol. 193:4292-4293(2011). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002339; AEF05462.1; -; Genomic_DNA. DR RefSeq; WP_013786372.1; NC_015554.1. DR ProteinModelPortal; F5Z6E9; -. DR STRING; 715451.ambt_19855; -. DR EnsemblBacteria; AEF05462; AEF05462; ambt_19855. DR KEGG; alt:ambt_19855; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000000683; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000000683}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000000683}. FT DOMAIN 198 365 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 164 191 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 429 AA; 48141 MW; 5F0AEAE088226680 CRC64; MFDRYEAGEQ AVLVHVNFTD ENSKEDLAEL ELLVSSAGVN AVEVITTSRS APQAKFFVGS GKAEEIAAAV KAHDANVVIF NHSLSPSQER NLEAVCQCRV LDRTGLILDI FAQRARTHEG KLQVELAQLR HISTRLIRGW THLERQKGGI GLRGPGETQL ETDRRLLRGR IKAILRRLEK VQKQREQGRR SRKRAEIPTV SLVGYTNAGK STLFNTITDA HVYAADQLFA TLDPTLRKID LKDVGPAILA DTVGFIRHLP HDLVAAFKAT LQETQEADLL LHVVDIADAK YRETIDEVND VLEEIDANEI QQLLICNKID KLDDIKPRIE RNEDGVPTRV WLSAQTGEGT ELLGQALTEC LSKSMVNYTL KIPPAQSSLR GVLFELNCIS SEEYDNQGDW VVDVRMPMAD WNRLEKRLEN GISEYVVRH // ID F6AJW8_PSEF1 Unreviewed; 433 AA. AC F6AJW8; DT 27-JUL-2011, integrated into UniProtKB/TrEMBL. DT 27-JUL-2011, sequence version 1. DT 30-AUG-2017, entry version 45. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Psefu_4105 {ECO:0000313|EMBL:AEF24060.1}; OS Pseudomonas fulva (strain 12-X). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=743720 {ECO:0000313|EMBL:AEF24060.1, ECO:0000313|Proteomes:UP000000686}; RN [1] {ECO:0000313|EMBL:AEF24060.1, ECO:0000313|Proteomes:UP000000686} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=12-X {ECO:0000313|Proteomes:UP000000686}; RG US DOE Joint Genome Institute; RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S., RA Peters L., Mikhailova N., Pagani I., Davenport K., Han C., Tapia R., RA Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Lcollab F.I., RA Woyke T.; RT "Complete sequence of Pseudomonas fulva 12-X."; RL Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002727; AEF24060.1; -; Genomic_DNA. DR RefSeq; WP_013793182.1; NC_015556.1. DR ProteinModelPortal; F6AJW8; -. DR STRING; 743720.Psefu_4105; -. DR EnsemblBacteria; AEF24060; AEF24060; Psefu_4105. DR GeneID; 31811865; -. DR KEGG; pfv:Psefu_4105; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000000686; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000000686}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000000686}. FT DOMAIN 199 366 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 165 192 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 433 AA; 48996 MW; 80B0F30E2909F0E0 CRC64; MFFERHEGGE RAILVHLDSQ NTEASEDPQE FQELALSAGA DTVAFFSVPN SRPTAKFLIG SGKVEELRDQ VKAHEADLVI FNHVLTPSQE RNLERMFECR VLDRTGLILD IFAQRARTHE GKLQVELAQL DHMSTRLVRG WTHLERQKGG IGLRGPGETQ LETDRRLLRV RIRQIKQKLE KVRSQREQAR RGRKRADIPS VSLVGYTNAG KSTLFNALTE SEVYAADQLF ATLDPTLRRL QLDDLGPVVL ADTVGFIRHL PHKLVEAFRA TLEESSNSDL LLHVIDSHEP ERDAQIEQVL EVLGEIGAQD LPVLEVYNKL DLLEGVEPQI QRNADGRPER VWLSARDGRG LPLLKQAIAE LLGDDLFVAT LRLPQRLARL RAQFFELGAV LQESYAEDGS SLLQVRIPRV ELNRLVSREG LQPVEFIEQH TLQ // ID F6CIJ0_DESK7 Unreviewed; 427 AA. AC F6CIJ0; DT 27-JUL-2011, integrated into UniProtKB/TrEMBL. DT 27-JUL-2011, sequence version 1. DT 07-JUN-2017, entry version 41. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Desku_0259 {ECO:0000313|EMBL:AEG13894.1}; OS Desulfotomaculum kuznetsovii (strain DSM 6115 / VKM B-1805 / 17). OC Bacteria; Firmicutes; Clostridia; Clostridiales; Peptococcaceae; OC Desulfotomaculum. OX NCBI_TaxID=760568 {ECO:0000313|EMBL:AEG13894.1, ECO:0000313|Proteomes:UP000009229}; RN [1] {ECO:0000313|EMBL:AEG13894.1, ECO:0000313|Proteomes:UP000009229} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 6115 / VKM B-1805 / 17 {ECO:0000313|Proteomes:UP000009229}; RG US DOE Joint Genome Institute; RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S., RA Peters L., Mikhailova N., Lu M., Saunders E., Han C., Tapia R., RA Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Nazina T., RA Ivanova A., Parshina S., Kuever J., Muyzer G., Plugge C., Stams A., RA Woyke T.; RT "Complete sequence of Desulfotomaculum kuznetsovii DSM 6115."; RL Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002770; AEG13894.1; -; Genomic_DNA. DR STRING; 760568.Desku_0259; -. DR EnsemblBacteria; AEG13894; AEG13894; Desku_0259. DR KEGG; dku:Desku_0259; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000009229; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR Gene3D; 3.40.50.620; -; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR014729; Rossmann-like_a/b/a_fold. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000009229}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000009229}. FT DOMAIN 201 365 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 160 194 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 427 AA; 47755 MW; DFC7E776EC5AED5C CRC64; MQKLPDYEKV LLITLQLPHE DEREVEESLD ELARLADTAG ARVVGRVVQR ARRPDPATFL GRGKVREEIA PACRELGVDL VICDHELSPA QVRNLEEELG VRVIDRTQLI LDIFARRART REGKLQVELA QLEYLYPRLA GKGTELSRLG GGIGTRGPGE TKLETDRRRI KRRITELRRE LDEVRRHRTL LRTRRQDVPV TLVSLVGYTN AGKSTLLNAL TGAGVPAEDK LFATLDPTTR RLVLPNNDVV LLTDTVGFIR RLPHHLVAAF RATLEEVTEA DLLLHVVDVS NPDYPDQVKA VEDVLASLGA GEKPAILVFN KVDRLTAEEP WLLPSGRPAV AVSALTGQGL DELRRLIMEV LRDQRVRREF LVPYQRGDVL NLLYEKGEVL SREYTPEGVR LEVELGAVWA SRAAARLGKD NPGRISG // ID F6CXC9_MARPP Unreviewed; 429 AA. AC F6CXC9; DT 27-JUL-2011, integrated into UniProtKB/TrEMBL. DT 27-JUL-2011, sequence version 1. DT 30-AUG-2017, entry version 40. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Mar181_1439 {ECO:0000313|EMBL:AEF54482.1}; OS Marinomonas posidonica (strain CECT 7376 / NCIMB 14433 / IVIA-Po-181). OC Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales; OC Marinomonas. OX NCBI_TaxID=491952 {ECO:0000313|EMBL:AEF54482.1, ECO:0000313|Proteomes:UP000009230}; RN [1] {ECO:0000313|EMBL:AEF54482.1, ECO:0000313|Proteomes:UP000009230} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CECT 7376 / NCIMB 14433 / IVIA-Po-181 RC {ECO:0000313|Proteomes:UP000009230}; RX PubMed=23458837; DOI=10.4056/sigs.2976373; RA Lucas-Elio P., Goodwin L., Woyke T., Pitluck S., Nolan M., RA Kyrpides N.C., Detter J.C., Copeland A., Lu M., Bruce D., Detter C., RA Tapia R., Han S., Land M.L., Ivanova N., Mikhailova N., Johnston A.W., RA Sanchez-Amat A.; RT "Complete genome sequence of Marinomonas posidonica type strain (IVIA- RT Po-181(T))."; RL Stand. Genomic Sci. 7:31-43(2012). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002771; AEF54482.1; -; Genomic_DNA. DR RefSeq; WP_013795957.1; NC_015559.1. DR ProteinModelPortal; F6CXC9; -. DR STRING; 491952.Mar181_1439; -. DR EnsemblBacteria; AEF54482; AEF54482; Mar181_1439. DR KEGG; mpc:Mar181_1439; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR KO; K03665; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000009230; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000009230}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000009230}. FT DOMAIN 199 366 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 429 AA; 47953 MW; DCE35FF584BBD756 CRC64; MFFERPDSGE IAVVVHIDFN DQSESYGPEE FVELAMSAGA DPVAVVTGSR QRPDAKYFVG SGKLDEIKDI VDQEEAQVVL FDHALSPSQE RNLESVLKCR VLDRTGLILD IFAQRARTHE GKLQVELAQL QHMSTRLIRG WTHLERQKGG IGMRGPGETQ LETDRRLLRV RIKSIQKRLE KVGTQRDQSR RSRARSAVPT VSLVGYTNAG KSTLFNRITG SEVYAADQLF ATLDPTLRRL DIEQIGSVVL ADTVGFIRQL PHRLIKAFQA TLKESAEADL LLHVVDAADI SRDDNMLHVG TVLEEIGADE VPTLLVFNKI DALPTAEPRI DRDEHGNPRR VWLSARDGDG LELLKQAIAE LLAVDVFTET LNLPSHYGRL RAMLFEHGAV RSERFDENGH FVLDVKLPKK DYLQILARAG MSEDQIVAA // ID F6DS13_DESRL Unreviewed; 417 AA. AC F6DS13; DT 27-JUL-2011, integrated into UniProtKB/TrEMBL. DT 27-JUL-2011, sequence version 1. DT 07-JUN-2017, entry version 39. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Desru_2823 {ECO:0000313|EMBL:AEG61037.1}; OS Desulfotomaculum ruminis (strain ATCC 23193 / DSM 2154 / NCIB 8452 / OS DL). OC Bacteria; Firmicutes; Clostridia; Clostridiales; Peptococcaceae; OC Desulfotomaculum. OX NCBI_TaxID=696281 {ECO:0000313|EMBL:AEG61037.1, ECO:0000313|Proteomes:UP000009234}; RN [1] {ECO:0000313|Proteomes:UP000009234} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 23193 / DSM 2154 / NCIB 8452 / DL RC {ECO:0000313|Proteomes:UP000009234}; RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L., RA Pitluck S., Lu M., Detter J.C., Han C., Tapia R., Land M., Hauser L., RA Kyrpides N., Ivanova N., Mikhailova N., Pagani I., Stams A.J.M., RA Plugge C.M., Muyzer G., Kuever J., Parshina S.N., Ivanova A.E., RA Nazina T.N., Brambilla E., Spring S., Klenk H.-P., Woyke T.; RT "Complete sequence of Desulfotomaculum ruminis DSM 2154."; RL Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002780; AEG61037.1; -; Genomic_DNA. DR RefSeq; WP_013842789.1; NC_015589.1. DR ProteinModelPortal; F6DS13; -. DR EnsemblBacteria; AEG61037; AEG61037; Desru_2823. DR KEGG; dru:Desru_2823; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000009234; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000009234}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000009234}. FT DOMAIN 202 365 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 161 195 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 417 AA; 46416 MW; 8B90D71540A2A155 CRC64; MHEIAVVLDE QAVIVGVKLA GEEDGQLTES LEELVSLVDT AGATVSGRFV QNRQRPDTAT FIGRGKVEEL ADYCQEVGAN LIIFDRELSP AQARNLEERI GHKVIDRTQL ILDIFARRAQ TKEGKLQVEL AQLKYLLPRL TGQGNQLSRL GGGIGTRGPG ETKLETDRRR IRKRISDLEQ ELKEVQRHRA LLRQDRKVEP LPLVSLVGYT NAGKSTLLRT LTGAEVLVED KLFATLDPTT RRVVLPNNDI ILLTDTVGFI QNLPHHLVAA FRATLEEVQE ADLLLHVVDV SHPYCEEQIR AVDGVLESLK ASHKPVIMVY NKMDLVKDSR SLPITGHPAV AISALSGQDI QQLLAKITEV LKERYSIIEL TLPYAKTSLI SLLHEKGKVL TEEYGETGIH IKVEISTVWA DRVMSQL // ID F6EKN8_HOYSD Unreviewed; 498 AA. AC F6EKN8; DT 27-JUL-2011, integrated into UniProtKB/TrEMBL. DT 27-JUL-2011, sequence version 1. DT 07-JUN-2017, entry version 39. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:AEF40174.1}; GN OrderedLocusNames=AS9A_1725 {ECO:0000313|EMBL:AEF40174.1}; OS Hoyosella subflava (strain DSM 45089 / JCM 17490 / NBRC 109087 / OS DQS3-9A1) (Amycolicicoccus subflavus). OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae; OC Hoyosella. OX NCBI_TaxID=443218 {ECO:0000313|EMBL:AEF40174.1, ECO:0000313|Proteomes:UP000009235}; RN [1] {ECO:0000313|EMBL:AEF40174.1, ECO:0000313|Proteomes:UP000009235} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 45089 / DQS3-9A1 {ECO:0000313|Proteomes:UP000009235}; RX PubMed=21725023; DOI=10.1128/JB.05388-11; RA Cai M., Chen W.M., Nie Y., Chi C.Q., Wang Y.N., Tang Y.Q., Li G.Y., RA Wu X.L.; RT "Complete genome sequence of Amycolicicoccus subflavus DQS3-9A1T, an RT actinomycete isolated from crude oil-polluted soil."; RL J. Bacteriol. 193:4538-4539(2011). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002786; AEF40174.1; -; Genomic_DNA. DR STRING; 443218.AS9A_1725; -. DR EnsemblBacteria; AEF40174; AEF40174; AS9A_1725. DR KEGG; asd:AS9A_1725; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000009235; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000009235}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000009235}. FT DOMAIN 276 445 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 235 269 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 498 AA; 53663 MW; AA5445FE7B842686 CRC64; MRQSTNSLGH NDFTPDDGAI ELNGDPLAEP GGQASDARTD VSVGELQLED RTSLRRVAGL STELTDITEV EYRQLRLEKV VLAGVWTQGT SAQAEASLRE LAALAETAGS AVLDGVIQRR DKPDAATYLG SGKAAELREI VLSTGADTVI CDGELTPAQL TALEKIVKVK VIDRTALILD IFAQHATSRE GKAQVTLAQM EYMLPRLRGW GEALSRQAGG RAGSNGGVGL RGPGETKIET DRRRIRERMA KLKREIRAMK SARDTKRARR QRNQVPSVAI VGYTNAGKSS LLNALTGAGV LVQNALFATL DPTTRRASLD DGREYVLTDT VGFVRHLPTQ LVEAFRSTLE EVTDADVLVH VVDGSDEFPL GQIKAVREVI NEVVEEQGTT PPPELLVINK TDAADPMALA QLRRALPGAV FVSAHSGAGL TALREQLADR LGRKDVEVLV EVPYARGELV ARIHTEGTVT GETHEAEGTR IRAHVPYSLA ASLQEFAL // ID F6EZC7_SPHCR Unreviewed; 443 AA. AC F6EZC7; DT 27-JUL-2011, integrated into UniProtKB/TrEMBL. DT 27-JUL-2011, sequence version 1. DT 07-JUN-2017, entry version 42. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=Sphch_0708 {ECO:0000313|EMBL:AEG48403.1}; OS Sphingobium chlorophenolicum L-1. OC Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales; OC Sphingomonadaceae; Sphingobium. OX NCBI_TaxID=690566 {ECO:0000313|EMBL:AEG48403.1, ECO:0000313|Proteomes:UP000007150}; RN [1] {ECO:0000313|EMBL:AEG48403.1, ECO:0000313|Proteomes:UP000007150} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=L-1 {ECO:0000313|EMBL:AEG48403.1, RC ECO:0000313|Proteomes:UP000007150}; RG US DOE Joint Genome Institute; RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S., RA Peters L., Daligault H., Han C., Tapia R., Land M., Hauser L., RA Kyrpides N., Ivanova N., Pagani I., Turner P., Copley S., Woyke T.; RT "Complete sequence of chromosome 1 of Sphingobium chlorophenolicum L- RT 1."; RL Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002798; AEG48403.1; -; Genomic_DNA. DR RefSeq; WP_013846668.1; NC_015593.1. DR ProteinModelPortal; F6EZC7; -. DR STRING; 690566.Sphch_0708; -. DR EnsemblBacteria; AEG48403; AEG48403; Sphch_0708. DR KEGG; sch:Sphch_0708; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR KO; K03665; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000007150; Chromosome 1. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0016810; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds; IEA:InterPro. DR CDD; cd01878; HflX; 1. DR Gene3D; 2.30.40.10; -; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR011059; Metal-dep_hydrolase_composite. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 2. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000007150}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000007150}. FT DOMAIN 209 389 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 443 AA; 48277 MW; 568627E348A4BB99 CRC64; MAVFNRDSAD EVSRGARAIV VRADVHGPER RDSDARLEEA RGLALAIGID VRAAQAFRVR DRKPATLFGS GQVDQIATLA RMEEAELVIV DNALSPVQQS NLEKATETKV IDRTGLILEI FGERAATNEG RLQVELAHLD YQAGRLVRSW THLERQRGGF GFLGGPGETQ IEADRRMIRD RMAKIRRELD QVTKTRGLHR ARRQRAPWPV IALVGYTNAG KSTLFNRMTG ADVMAEDLLF ATLDPTMRQI ALPGLDKAIL SDTVGFVSDL PTQLIAAFRA TLEEVLSADL IVHVRDIAHP DSDAQRDDVI DVLSELGVAG EGALEAGEGN DPPPIIEAWN KLDLLDGEAA ALARETAARR DDVVILSALT GEGVDDLQRT ISARLTSGAQ VHQLRVPVAD GAAMAWLHEH GEVIASRADG EDMLVEARLS DSALARFLKR RGS // ID F6FSG2_ISOV2 Unreviewed; 510 AA. AC F6FSG2; DT 27-JUL-2011, integrated into UniProtKB/TrEMBL. DT 27-JUL-2011, sequence version 1. DT 07-JUN-2017, entry version 41. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Isova_1260 {ECO:0000313|EMBL:AEG44029.1}; OS Isoptericola variabilis (strain 225). OC Bacteria; Actinobacteria; Micrococcales; Promicromonosporaceae; OC Isoptericola. OX NCBI_TaxID=743718 {ECO:0000313|Proteomes:UP000009236}; RN [1] {ECO:0000313|EMBL:AEG44029.1, ECO:0000313|Proteomes:UP000009236} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=225 {ECO:0000313|Proteomes:UP000009236}; RG US DOE Joint Genome Institute; RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S., RA Peters L., Mikhailova N., Zeytun A., Han C., Tapia R., Land M., RA Hauser L., Kyrpides N., Ivanova N., Pagani I., Siebers A., RA Allgaier M., Thelen M., Hugenholtz P., Gladden J., Woyke T.; RT "Complete sequence of Isoptericola variabilis 225."; RL Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002810; AEG44029.1; -; Genomic_DNA. DR RefSeq; WP_013838421.1; NC_015588.1. DR STRING; 743718.Isova_1260; -. DR EnsemblBacteria; AEG44029; AEG44029; Isova_1260. DR KEGG; iva:Isova_1260; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR KO; K03665; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000009236; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 2. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000009236}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000009236}. FT DOMAIN 291 457 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 510 AA; 54772 MW; FF9BED15921645C3 CRC64; MTHTPTNPDT PFTGSTPSDA DRDAQAIAND VVARVLARAG TARAEGGTVH TDHDGDQLDL EERSALRRVV GLSTELEDVT EVEYRQLRLE KVVLVGLYSG GEAAAAEAEV SLRELAALAE TAGSQVLDGL LQRRQKPDPG TYLGSGKAAE LADVVAAVGA DTVIADTELA PSQRRALEDI VKVKVVDRTA LILDIFAQHA KSREGKAQVE LAQLEYLLPR LRGWGESMSR QAGGQVGSAG AGMGSRGPGE TKIELDRRRI RNRMAKLRRE IAAMAPARVT KRLERKRHSI PNVAIAGYTN AGKSSLLNAL TDAGVLVENA LFATLDPTVR RARTDDGRVY TLADTVGFVR HLPHQLVEAF RSTLEEVADA ALLLHVVDAS HPDPEGQIAA VREVLSEIPG VEDVPEVVVL NKADVADPAV VGRIQRRERR TVVVSAHTGE GIAELKALIA DELPRPDVEI DVVVPYSRGD LVHRVHEAGE IDAEEHLADG TRLRGRVDPS LAAELERAAV // ID F6GGX9_LACS5 Unreviewed; 409 AA. AC F6GGX9; DT 27-JUL-2011, integrated into UniProtKB/TrEMBL. DT 27-JUL-2011, sequence version 1. DT 07-JUN-2017, entry version 41. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Lacal_1167 {ECO:0000313|EMBL:AEH01015.1}; OS Lacinutrix sp. (strain 5H-3-7-4). OC Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales; OC Flavobacteriaceae; Lacinutrix. OX NCBI_TaxID=983544 {ECO:0000313|EMBL:AEH01015.1, ECO:0000313|Proteomes:UP000008297}; RN [1] {ECO:0000313|EMBL:AEH01015.1, ECO:0000313|Proteomes:UP000008297} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=5H-3-7-4 {ECO:0000313|EMBL:AEH01015.1, RC ECO:0000313|Proteomes:UP000008297}; RX PubMed=21725025; DOI=10.1128/JB.05518-11; RA Klippel B., Lochner A., Bruce D.C., Walston Davenport K., Detter C., RA Goodwin L.A., Han J., Han S., Hauser L., Land M.L., Nolan M., RA Ovchinnikova G., Pennacchio L., Pitluck S., Tapia R., Woyke T., RA Wiebusch S., Basner A., Abe F., Horikoshi K., Keller M., RA Antranikian G.; RT "Complete genome sequences of Krokinobacter sp. strain 4H-3-7-5 and RT Lacinutrix sp. strain 5H-3-7-4, polysaccharide-degrading members of RT the family Flavobacteriaceae."; RL J. Bacteriol. 193:4545-4546(2011). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002825; AEH01015.1; -; Genomic_DNA. DR RefSeq; WP_013869795.1; NC_015638.1. DR ProteinModelPortal; F6GGX9; -. DR STRING; 983544.Lacal_1167; -. DR EnsemblBacteria; AEH01015; AEH01015; Lacal_1167. DR KEGG; lan:Lacal_1167; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000008297; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000008297}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000008297}. FT DOMAIN 200 386 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 409 AA; 47176 MW; 9188F22B852D8E09 CRC64; MLEKKDVELE SAVLIGIITK DQDEERSKEY LDELEFLTYT AGGDVKKRFT QKMDMPNPKT FIGTGKMEDV RQYIEANNIS TAIFDDELSA AQERNISKIL NCKVLDRTNL ILDIFAQRAQ TSAARTQVEL AQFEYLLPRL KGMWTHLERQ KGGIGMRGPG ETEIETDRRI VRDRIALLKA KIKTIDKQMS VQRGNRGKMV RVALVGYTNV GKSTLMNTIS KSKVFAENKL FATLDTTVRK VVIQNLPFLL SDTVGFIRKL PTQLVESFKS TLDEVREADL LLHVVDISHP NFEDHIASVN KILGEIDSSN KPTIMVFNKI DAYQAKPYDE TDLIAERTEE HYSLAEWKRT WMNRVGEDNA LFISALNKKN LEDFKKRVYD EVRQIHITRF PYNHFLYPDY DYENMGEEE // ID F6GUT6_VITVI Unreviewed; 129 AA. AC F6GUT6; DT 27-JUL-2011, integrated into UniProtKB/TrEMBL. DT 27-JUL-2011, sequence version 1. DT 30-AUG-2017, entry version 27. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:CCB43494.1}; GN OrderedLocusNames=VIT_06s0004g06200 {ECO:0000313|EMBL:CCB43494.1}; OS Vitis vinifera (Grape). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae; OC Pentapetalae; rosids; Vitales; Vitaceae; Vitis. OX NCBI_TaxID=29760 {ECO:0000313|Proteomes:UP000009183}; RN [1] {ECO:0000313|Proteomes:UP000009183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Pinot noir / PN40024 {ECO:0000313|Proteomes:UP000009183}; RX PubMed=17721507; DOI=10.1038/nature06148; RG The French-Italian Public Consortium for Grapevine Genome Characterization.; RA Jaillon O., Aury J.-M., Noel B., Policriti A., Clepet C., RA Casagrande A., Choisne N., Aubourg S., Vitulo N., Jubin C., Vezzi A., RA Legeai F., Hugueney P., Dasilva C., Horner D., Mica E., Jublot D., RA Poulain J., Bruyere C., Billault A., Segurens B., Gouyvenoux M., RA Ugarte E., Cattonaro F., Anthouard V., Vico V., Del Fabbro C., RA Alaux M., Di Gaspero G., Dumas V., Felice N., Paillard S., Juman I., RA Moroldo M., Scalabrin S., Canaguier A., Le Clainche I., Malacrida G., RA Durand E., Pesole G., Laucou V., Chatelet P., Merdinoglu D., RA Delledonne M., Pezzotti M., Lecharny A., Scarpelli C., Artiguenave F., RA Pe M.E., Valle G., Morgante M., Caboche M., Adam-Blondon A.-F., RA Weissenbach J., Quetier F., Wincker P.; RT "The grapevine genome sequence suggests ancestral hexaploidization in RT major angiosperm phyla."; RL Nature 449:463-467(2007). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; FN594951; CCB43494.1; -; Genomic_DNA. DR ProteinModelPortal; F6GUT6; -. DR STRING; 29760.VIT_06s0004g06200.t01; -. DR PRIDE; F6GUT6; -. DR EnsemblPlants; VIT_06s0004g06200.t01; VIT_06s0004g06200.t01; VIT_06s0004g06200. DR Gramene; VIT_06s0004g06200.t01; VIT_06s0004g06200.t01; VIT_06s0004g06200. DR eggNOG; KOG0410; Eukaryota. DR eggNOG; COG2262; LUCA. DR InParanoid; F6GUT6; -. DR OrthoDB; EOG09370C81; -. DR Proteomes; UP000009183; Chromosome 6. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR GO; GO:0043022; F:ribosome binding; IBA:GO_Central. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000009183}; KW Reference proteome {ECO:0000313|Proteomes:UP000009183}. FT DOMAIN 8 97 GTP-bdg_N. {ECO:0000259|Pfam:PF13167}. FT DOMAIN 100 126 GTP-bdg_M. {ECO:0000259|Pfam:PF16360}. SQ SEQUENCE 129 AA; 14305 MW; 01140FC1657103E2 CRC64; MEYSFGIEES LKKLAQLADT VGLMVVGSTS QKLRAPNPRT CIRSSKVAEI KSIIHALDVE TITFDYEFST GQLHDLEKAF GGNVRVYDHS VLILDIFNQR ATTHEATLQV ALAQMEYSSP RLSKMGDSP // ID F6GUT8_VITVI Unreviewed; 149 AA. AC F6GUT8; DT 27-JUL-2011, integrated into UniProtKB/TrEMBL. DT 27-JUL-2011, sequence version 1. DT 30-AUG-2017, entry version 27. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:CCB43496.1}; GN OrderedLocusNames=VIT_06s0004g06180 {ECO:0000313|EMBL:CCB43496.1}; OS Vitis vinifera (Grape). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae; OC Pentapetalae; rosids; Vitales; Vitaceae; Vitis. OX NCBI_TaxID=29760 {ECO:0000313|Proteomes:UP000009183}; RN [1] {ECO:0000313|Proteomes:UP000009183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Pinot noir / PN40024 {ECO:0000313|Proteomes:UP000009183}; RX PubMed=17721507; DOI=10.1038/nature06148; RG The French-Italian Public Consortium for Grapevine Genome Characterization.; RA Jaillon O., Aury J.-M., Noel B., Policriti A., Clepet C., RA Casagrande A., Choisne N., Aubourg S., Vitulo N., Jubin C., Vezzi A., RA Legeai F., Hugueney P., Dasilva C., Horner D., Mica E., Jublot D., RA Poulain J., Bruyere C., Billault A., Segurens B., Gouyvenoux M., RA Ugarte E., Cattonaro F., Anthouard V., Vico V., Del Fabbro C., RA Alaux M., Di Gaspero G., Dumas V., Felice N., Paillard S., Juman I., RA Moroldo M., Scalabrin S., Canaguier A., Le Clainche I., Malacrida G., RA Durand E., Pesole G., Laucou V., Chatelet P., Merdinoglu D., RA Delledonne M., Pezzotti M., Lecharny A., Scarpelli C., Artiguenave F., RA Pe M.E., Valle G., Morgante M., Caboche M., Adam-Blondon A.-F., RA Weissenbach J., Quetier F., Wincker P.; RT "The grapevine genome sequence suggests ancestral hexaploidization in RT major angiosperm phyla."; RL Nature 449:463-467(2007). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; FN594951; CCB43496.1; -; Genomic_DNA. DR ProteinModelPortal; F6GUT8; -. DR STRING; 29760.VIT_06s0004g06180.t01; -. DR EnsemblPlants; VIT_06s0004g06180.t01; VIT_06s0004g06180.t01; VIT_06s0004g06180. DR Gramene; VIT_06s0004g06180.t01; VIT_06s0004g06180.t01; VIT_06s0004g06180. DR eggNOG; KOG0410; Eukaryota. DR eggNOG; COG2262; LUCA. DR InParanoid; F6GUT8; -. DR OrthoDB; EOG09370C81; -. DR Proteomes; UP000009183; Chromosome 6. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR GO; GO:0043022; F:ribosome binding; IBA:GO_Central. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF13167; GTP-bdg_N; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000009183}; KW Reference proteome {ECO:0000313|Proteomes:UP000009183}. FT DOMAIN 24 113 GTP-bdg_N. {ECO:0000259|Pfam:PF13167}. SQ SEQUENCE 149 AA; 16542 MW; 19CB86DFECAB254E CRC64; MEFHLLRTLR SIILGDMEYS FGIEESLKEL AQLADIVGLM VVGSTSQKLS VPNPRTYIES GKVAEIKSAI HALDVETVTF DDEFSAMQLR DLEKAFGGDV RVCDCPVLIL DIFNKRVATH EAALQVTLAQ MEYPLPCLIK MGTHLQCQA // ID F6HD86_VITVI Unreviewed; 619 AA. AC F6HD86; DT 27-JUL-2011, integrated into UniProtKB/TrEMBL. DT 27-JUL-2011, sequence version 1. DT 30-AUG-2017, entry version 37. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:CCB50181.1}; GN ORFNames=VIT_00s0734g00020 {ECO:0000313|EMBL:CCB50181.1}; OS Vitis vinifera (Grape). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae; OC Pentapetalae; rosids; Vitales; Vitaceae; Vitis. OX NCBI_TaxID=29760 {ECO:0000313|Proteomes:UP000009183}; RN [1] {ECO:0000313|Proteomes:UP000009183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Pinot noir / PN40024 {ECO:0000313|Proteomes:UP000009183}; RX PubMed=17721507; DOI=10.1038/nature06148; RG The French-Italian Public Consortium for Grapevine Genome Characterization.; RA Jaillon O., Aury J.-M., Noel B., Policriti A., Clepet C., RA Casagrande A., Choisne N., Aubourg S., Vitulo N., Jubin C., Vezzi A., RA Legeai F., Hugueney P., Dasilva C., Horner D., Mica E., Jublot D., RA Poulain J., Bruyere C., Billault A., Segurens B., Gouyvenoux M., RA Ugarte E., Cattonaro F., Anthouard V., Vico V., Del Fabbro C., RA Alaux M., Di Gaspero G., Dumas V., Felice N., Paillard S., Juman I., RA Moroldo M., Scalabrin S., Canaguier A., Le Clainche I., Malacrida G., RA Durand E., Pesole G., Laucou V., Chatelet P., Merdinoglu D., RA Delledonne M., Pezzotti M., Lecharny A., Scarpelli C., Artiguenave F., RA Pe M.E., Valle G., Morgante M., Caboche M., Adam-Blondon A.-F., RA Weissenbach J., Quetier F., Wincker P.; RT "The grapevine genome sequence suggests ancestral hexaploidization in RT major angiosperm phyla."; RL Nature 449:463-467(2007). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; FN595563; CCB50181.1; -; Genomic_DNA. DR RefSeq; XP_010647313.1; XM_010649011.2. DR UniGene; Vvi.13999; -. DR STRING; 29760.VIT_00s0734g00020.t01; -. DR PRIDE; F6HD86; -. DR EnsemblPlants; VIT_00s0734g00020.t01; VIT_00s0734g00020.t01; VIT_00s0734g00020. DR GeneID; 100260987; -. DR Gramene; VIT_00s0734g00020.t01; VIT_00s0734g00020.t01; VIT_00s0734g00020. DR KEGG; vvi:100260987; -. DR eggNOG; KOG0410; Eukaryota. DR eggNOG; KOG4197; Eukaryota. DR eggNOG; COG2262; LUCA. DR InParanoid; F6HD86; -. DR OrthoDB; EOG09360975; -. DR Proteomes; UP000009183; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR GO; GO:0043022; F:ribosome binding; IBA:GO_Central. DR CDD; cd01878; HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000009183}; KW Reference proteome {ECO:0000313|Proteomes:UP000009183}. FT DOMAIN 324 595 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 619 AA; 68896 MW; 6A612BB5ECD6C419 CRC64; MFRTISFLLS PLRSLPQTLN FITQPSLYLK PYHSPLKLPT NPSSIPPNLQ FPPISILSSS FSQTPLLQKK EDPYNDASLF NRDPKSPPKL FVVQPRLRPD TLLQAKLDEA INLANSLEEQ RDGYYDTELC EKGLPPHVVV QNPAVRSSKY RSDTYFGPGT VDTVKCHLNA VESKGEIDAV YVNTILSGIQ QRNLERAWGK PVLDRVGLII EIFNAHAQTK EAKLQAELAA LMYKRTRLVR VRGPDGRYTF GATGETEVVS ARGRGSGGRG FISGAGETEL QLQRRRILER RNHLLSQIEA VRRTRALQRA SRKRRGGSNG QGLATVAIVG YTNAGKSTLV SALSESDLFS DDRLFATVDP RLRSVILPSG RKVLLSDTVG FISDLPVQLV EAFHATLEEV VEADLLVHVL DSSASDLDEQ RSVVLQVLQQ IGVSEEKLQN MLEVWNKIDL QEEEMGADKY LDNGEDDVVD SLSGAEDDDM PSELPAEPVD DDDENDIVSE LSSGDVQETM DDHEGDYSDG WLSRGGEGSE DDQGNPSRWK TMDDQQSESF KDRRMTEKDS CSQPQCIPHV KTSAVMGVGL QELLALIDEK LETQKVPERN YFDRKWRPPH TEDVGVAVE // ID F6IPN7_9SPHN Unreviewed; 425 AA. AC F6IPN7; DT 27-JUL-2011, integrated into UniProtKB/TrEMBL. DT 27-JUL-2011, sequence version 1. DT 12-APR-2017, entry version 40. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=PP1Y_AT26054 {ECO:0000313|EMBL:CCA93389.1}; OS Novosphingobium sp. PP1Y. OC Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales; OC Sphingomonadaceae; Novosphingobium. OX NCBI_TaxID=702113 {ECO:0000313|EMBL:CCA93389.1, ECO:0000313|Proteomes:UP000009242}; RN [1] {ECO:0000313|EMBL:CCA93389.1, ECO:0000313|Proteomes:UP000009242} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=PP1Y {ECO:0000313|EMBL:CCA93389.1}; RX PubMed=21685292; DOI=10.1128/JB.05349-11; RA D'Argenio V., Petrillo M., Cantiello P., Naso B., Cozzuto L., RA Notomista E., Paolella G., Di Donato A., Salvatore F.; RT "De novo sequencing and assembly of the whole genome of RT Novosphingobium sp. strain PP1Y."; RL J. Bacteriol. 193:4296-4296(2011). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; FR856862; CCA93389.1; -; Genomic_DNA. DR STRING; 702113.PP1Y_AT26054; -. DR EnsemblBacteria; CCA93389; CCA93389; PP1Y_AT26054. DR KEGG; npp:PP1Y_AT26054; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR KO; K03665; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000009242; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000009242}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000009242}. FT DOMAIN 185 369 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 425 AA; 46532 MW; 25EE77C201F720D2 CRC64; MRGKGDLDPE ARLDEAKGLA LAIGLVIADA VAIPIREPRA GTLFGEGQIQ NIGTACELNE AELIIVDGSL SAIQQRNLEE KLKRKVIDRT GLILEIFGER AATAEGRLQV ELAHLDYQAG RLVRSWTHLE RQRGGFGFLG GPGETQIEAD RRMIRDRMAK IRRELEQVRR TRGLHRDRRE KAPWPIVALV GYTNAGKSTL FNRLTGAGVM AQDLLFATLD PTMRAIRLPG VEKAILSDTV GFISDLPTQL VAAFRATLEE VTAADLILHV RDIANPDTDA QKRQVLDVLG DLGVLGSVVD DDVEEGAEPG IPIIELWNKW DLLGPEHAEK LHEAIAHRKD ETIVPISAVT GEGCENLLEV VSHALTADSK VYSFLIPAAD GQRLAFLHAR GEVISEDDAG EGSEGPLLRL QVRLAERELG RFQAL // ID F6PZD7_CIOIN Unreviewed; 519 AA. AC F6PZD7; DT 27-JUL-2011, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 2. DT 07-JUN-2017, entry version 39. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSCINP00000023840}; OS Ciona intestinalis (Transparent sea squirt) (Ascidia intestinalis). OC Eukaryota; Metazoa; Chordata; Tunicata; Ascidiacea; Enterogona; OC Phlebobranchia; Cionidae; Ciona. OX NCBI_TaxID=7719 {ECO:0000313|Ensembl:ENSCINP00000023840, ECO:0000313|Proteomes:UP000008144}; RN [1] {ECO:0000313|Ensembl:ENSCINP00000023840} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15114417; DOI=10.1007/s00239-003-2559-6; RA Gissi C., Iannelli F., Pesole G.; RT "Complete mtDNA of Ciona intestinalis reveals extensive gene RT rearrangement and the presence of an atp8 and an extra trnM gene in RT ascidians."; RL J. Mol. Evol. 58:376-389(2004). RN [2] {ECO:0000313|Ensembl:ENSCINP00000023840} RP IDENTIFICATION. RG Ensembl; RL Submitted (JUL-2011) to UniProtKB. CC -!- CAUTION: The sequence shown here is derived from an Ensembl CC automatic analysis pipeline and should be considered as CC preliminary data. {ECO:0000313|Ensembl:ENSCINP00000023840}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; EAAA01003003; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR STRING; 7719.ENSCINP00000023840; -. DR Ensembl; ENSCINT00000024086; ENSCINP00000023840; ENSCING00000012867. DR eggNOG; KOG0410; Eukaryota. DR eggNOG; COG2262; LUCA. DR GeneTree; ENSGT00390000001397; -. DR InParanoid; F6PZD7; -. DR OMA; MDTVGFM; -. DR OrthoDB; EOG091G0852; -. DR TreeFam; TF315022; -. DR Proteomes; UP000008144; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR GO; GO:0043022; F:ribosome binding; IBA:GO_Central. DR CDD; cd01878; HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008144}; KW Reference proteome {ECO:0000313|Proteomes:UP000008144}. FT DOMAIN 298 429 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 519 AA; 59189 MW; 5E6FA84994111F7C CRC64; MLRNFISINT LQYKEVKRIG AKICNFAQQA NRKTQTNLTP SRSGSVWSRR RNLKDQLISP SNWRRYTSEV FDESETEDLN TEKVDWYLGS TRAVFVIQPY EAEDVSKDVY ISTPHITNPQ LELDESVALV ETLPDWKVHG SVILRIRNKN SNEIFSKKNF QNLMEKLKEK QTVNSLFVSV EKLTNIQKAT LQQASGLEHI FDRYSLVLQI FKLRAKTKEA KLQVALAQLP MDKATMKVPN ETSKHQSQHQ QGKGSGETYS ELVRREFNLK EQRLMKRLKH VKRIRNEHRE ARKRNAVPVA AVIGYTNAGK TSLIKALSVL SERIQPKDYL FATLDVTAHA AILPNNLRYV LVDTVGFLSK LPHSLIDAFK ATMEDMLQAD LLIHVRDISH PHSKNQLRNV LKVLSQLKLP PSLLENIIEV RNKVDLVKPV RNISKDECDV SATEGTGLSS LAIQIQNGIM KATDRKVCTL RVPAVGGHLE WLREHYAVHE VRGSGNFNLE LEVIVADWQL AKFTSAFED // ID F6VU77_MONDO Unreviewed; 470 AA. AC F6VU77; DT 27-JUL-2011, integrated into UniProtKB/TrEMBL. DT 09-JAN-2013, sequence version 2. DT 30-AUG-2017, entry version 31. DE SubName: Full=GTP binding protein 6 (putative) {ECO:0000313|Ensembl:ENSMODP00000000388}; GN Name=GTPBP6 {ECO:0000313|Ensembl:ENSMODP00000000388}; OS Monodelphis domestica (Gray short-tailed opossum). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Metatheria; Didelphimorphia; Didelphidae; Monodelphis. OX NCBI_TaxID=13616 {ECO:0000313|Ensembl:ENSMODP00000000388, ECO:0000313|Proteomes:UP000002280}; RN [1] {ECO:0000313|Ensembl:ENSMODP00000000388, ECO:0000313|Proteomes:UP000002280} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=17495919; DOI=10.1038/nature05805; RA Mikkelsen T.S., Wakefield M.J., Aken B., Amemiya C.T., Chang J.L., RA Duke S., Garber M., Gentles A.J., Goodstadt L., Heger A., Jurka J., RA Kamal M., Mauceli E., Searle S.M., Sharpe T., Baker M.L., Batzer M.A., RA Benos P.V., Belov K., Clamp M., Cook A., Cuff J., Das R., Davidow L., RA Deakin J.E., Fazzari M.J., Glass J.L., Grabherr M., Greally J.M., RA Gu W., Hore T.A., Huttley G.A., Kleber M., Jirtle R.L., Koina E., RA Lee J.T., Mahony S., Marra M.A., Miller R.D., Nicholls R.D., Oda M., RA Papenfuss A.T., Parra Z.E., Pollock D.D., Ray D.A., Schein J.E., RA Speed T.P., Thompson K., VandeBerg J.L., Wade C.M., Walker J.A., RA Waters P.D., Webber C., Weidman J.R., Xie X., Zody M.C., Baldwin J., RA Abdouelleil A., Abdulkadir J., Abebe A., Abera B., Abreu J., RA Acer S.C., Aftuck L., Alexander A., An P., Anderson E., Anderson S., RA Arachi H., Azer M., Bachantsang P., Barry A., Bayul T., Berlin A., RA Bessette D., Bloom T., Bloom T., Boguslavskiy L., Bonnet C., RA Boukhgalter B., Bourzgui I., Brown A., Cahill P., Channer S., RA Cheshatsang Y., Chuda L., Citroen M., Collymore A., Cooke P., RA Costello M., D'Aco K., Daza R., De Haan G., DeGray S., DeMaso C., RA Dhargay N., Dooley K., Dooley E., Doricent M., Dorje P., Dorjee K., RA Dupes A., Elong R., Falk J., Farina A., Faro S., Ferguson D., RA Fisher S., Foley C.D., Franke A., Friedrich D., Gadbois L., Gearin G., RA Gearin C.R., Giannoukos G., Goode T., Graham J., Grandbois E., RA Grewal S., Gyaltsen K., Hafez N., Hagos B., Hall J., Henson C., RA Hollinger A., Honan T., Huard M.D., Hughes L., Hurhula B., Husby M.E., RA Kamat A., Kanga B., Kashin S., Khazanovich D., Kisner P., Lance K., RA Lara M., Lee W., Lennon N., Letendre F., LeVine R., Lipovsky A., RA Liu X., Liu J., Liu S., Lokyitsang T., Lokyitsang Y., Lubonja R., RA Lui A., MacDonald P., Magnisalis V., Maru K., Matthews C., RA McCusker W., McDonough S., Mehta T., Meldrim J., Meneus L., Mihai O., RA Mihalev A., Mihova T., Mittelman R., Mlenga V., Montmayeur A., RA Mulrain L., Navidi A., Naylor J., Negash T., Nguyen T., Nguyen N., RA Nicol R., Norbu C., Norbu N., Novod N., O'Neill B., Osman S., RA Markiewicz E., Oyono O.L., Patti C., Phunkhang P., Pierre F., RA Priest M., Raghuraman S., Rege F., Reyes R., Rise C., Rogov P., RA Ross K., Ryan E., Settipalli S., Shea T., Sherpa N., Shi L., Shih D., RA Sparrow T., Spaulding J., Stalker J., Stange-Thomann N., RA Stavropoulos S., Stone C., Strader C., Tesfaye S., Thomson T., RA Thoulutsang Y., Thoulutsang D., Topham K., Topping I., Tsamla T., RA Vassiliev H., Vo A., Wangchuk T., Wangdi T., Weiand M., Wilkinson J., RA Wilson A., Yadav S., Young G., Yu Q., Zembek L., Zhong D., Zimmer A., RA Zwirko Z., Jaffe D.B., Alvarez P., Brockman W., Butler J., Chin C., RA Gnerre S., MacCallum I., Graves J.A., Ponting C.P., Breen M., RA Samollow P.B., Lander E.S., Lindblad-Toh K.; RT "Genome of the marsupial Monodelphis domestica reveals innovation in RT non-coding sequences."; RL Nature 447:167-177(2007). RN [2] {ECO:0000313|Ensembl:ENSMODP00000000388} RP IDENTIFICATION. RG Ensembl; RL Submitted (JUL-2011) to UniProtKB. CC -!- CAUTION: The sequence shown here is derived from an Ensembl CC automatic analysis pipeline and should be considered as CC preliminary data. {ECO:0000313|Ensembl:ENSMODP00000000388}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR STRING; 13616.ENSMODP00000000388; -. DR Ensembl; ENSMODT00000000396; ENSMODP00000000388; ENSMODG00000000326. DR eggNOG; KOG0410; Eukaryota. DR eggNOG; COG2262; LUCA. DR GeneTree; ENSGT00390000001397; -. DR InParanoid; F6VU77; -. DR OMA; MDTVGFM; -. DR OrthoDB; EOG091G0852; -. DR TreeFam; TF315022; -. DR Proteomes; UP000002280; Chromosome 7. DR Bgee; ENSMODG00000000326; -. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR GO; GO:0043022; F:ribosome binding; IBA:GO_Central. DR CDD; cd01878; HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 4: Predicted; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000002280}; KW Reference proteome {ECO:0000313|Proteomes:UP000002280}. FT DOMAIN 249 413 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 10 40 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 470 AA; 53003 MW; E638F7165E4175CA CRC64; MDSNDIGGGR ATARRGRKEE QEEQDEAEEE EEDEELLLEK EPLLPQGAQR VFLLHPDVKW GAKKQTMTRA ELQVAEAKAL VHTLMNWSVE ETMIVSTKTP DKKLVFGKGN FELLTEKIRG SPQITCVFLN IERMSPLTKK ELKAAWGIEV FDRFTIVLHI FRCNAKTKEA KLQIALAEIP LLRSNLKNEI AQLDQQGGGS RYIMGSGETF MQIQQRVLKE KEIKIKKALE KLKKRRHLLR SQRKKRELPI ISVMGYTNCG KTTLIKALTG DTSIQPRDQL FATLDITAHS GSLPSRMNVV YVDTIGFLSQ LPHDLIESFS ATLEDVAYSD VIIHVRDISH PETDLQKASV LSVLKNLHLP NQLLDSVLEV HNKVDLVERY EPTEPNAITI SALFGHGLEK LKEEIENAVL KATGKKLLTL KIKLEGAQLS WLYKEATVQE VDVIPENGTA NVKVIISNSA YGKYRKLFPV // ID F7BFX3_XENTR Unreviewed; 530 AA. AC F7BFX3; DT 27-JUL-2011, integrated into UniProtKB/TrEMBL. DT 27-JUL-2011, sequence version 1. DT 07-JUN-2017, entry version 39. DE SubName: Full=GTP-binding protein 6 (putative) {ECO:0000313|Ensembl:ENSXETP00000008922}; GN Name=gtpbp6 {ECO:0000313|Ensembl:ENSXETP00000008922, GN ECO:0000313|Xenbase:XB-GENE-967567}; OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Amphibia; Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; OC Silurana. OX NCBI_TaxID=8364 {ECO:0000313|Ensembl:ENSXETP00000008922, ECO:0000313|Proteomes:UP000008143}; RN [1] {ECO:0000313|Ensembl:ENSXETP00000008922} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Nigerian {ECO:0000313|Ensembl:ENSXETP00000008922}; RX PubMed=20431018; DOI=10.1126/science.1183670; RA Hellsten U., Harland R.M., Gilchrist M.J., Hendrix D., Jurka J., RA Kapitonov V., Ovcharenko I., Putnam N.H., Shu S., Taher L., RA Blitz I.L., Blumberg B., Dichmann D.S., Dubchak I., Amaya E., RA Detter J.C., Fletcher R., Gerhard D.S., Goodstein D., Graves T., RA Grigoriev I.V., Grimwood J., Kawashima T., Lindquist E., Lucas S.M., RA Mead P.E., Mitros T., Ogino H., Ohta Y., Poliakov A.V., Pollet N., RA Robert J., Salamov A., Sater A.K., Schmutz J., Terry A., Vize P.D., RA Warren W.C., Wells D., Wills A., Wilson R.K., Zimmerman L.B., RA Zorn A.M., Grainger R., Grammer T., Khokha M.K., Richardson P.M., RA Rokhsar D.S.; RT "The genome of the Western clawed frog Xenopus tropicalis."; RL Science 328:633-636(2010). RN [2] {ECO:0000313|Ensembl:ENSXETP00000008922} RP IDENTIFICATION. RG Ensembl; RL Submitted (JUN-2011) to UniProtKB. CC -!- CAUTION: The sequence shown here is derived from an Ensembl CC automatic analysis pipeline and should be considered as CC preliminary data. {ECO:0000313|Ensembl:ENSXETP00000008922}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AAMC01064598; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR RefSeq; XP_002937028.1; XM_002936982.3. DR ProteinModelPortal; F7BFX3; -. DR STRING; 8364.ENSXETP00000008922; -. DR PaxDb; F7BFX3; -. DR Ensembl; ENSXETT00000008922; ENSXETP00000008922; ENSXETG00000004125. DR GeneID; 100487881; -. DR KEGG; xtr:100487881; -. DR CTD; 8225; -. DR Xenbase; XB-GENE-967567; gtpbp6. DR eggNOG; KOG0410; Eukaryota. DR eggNOG; COG2262; LUCA. DR GeneTree; ENSGT00390000001397; -. DR InParanoid; F7BFX3; -. DR OMA; MDTVGFM; -. DR OrthoDB; EOG091G0852; -. DR TreeFam; TF315022; -. DR Proteomes; UP000008143; Unassembled WGS sequence. DR Bgee; ENSXETG00000004125; -. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR GO; GO:0043022; F:ribosome binding; IBA:GO_Central. DR CDD; cd01878; HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 4: Predicted; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000008143}; KW Reference proteome {ECO:0000313|Proteomes:UP000008143}. FT DOMAIN 309 473 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 271 305 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 530 AA; 59498 MW; 90200C5C2FB20DF4 CRC64; MLPVRVLRAV RGCLGYWRYP PYYTTELRAG SSLYSSRTVP CNGRLDFSLS GLRCFSGGLP YWKAKKHGGD HSKSGNLTAS DDFWVEEEDE ELDDLDLSPH TASLLQGAHR VFLVHPDVKW GAKKQHLSSA DLQVAEAVAL IHSLPNWSVV NTLIMSTKSP DSKLIFGKGN FQTLTDVIKG HPQITAVFLN VERLSSLTEK EMEEAWGVKV FDRYTVVLNI FRFNAHTKEA KLQIALAELP LLRSNLKNET AHMDQQGGGS RYIMGSGETF LEVQQRLLKE REIKIKNALE KVKKKRNLLR TQRRRREFPI ISVLGYTNSG KTTLIKALTG DEGLQPRDQL FATLDVTSHA GLLPCRMPVI YVDTIGFLSQ LPHNLIESFS ATLEDVVHSD LLIHVRDISH PETLKQKASV LSVLKNLRLP QQLLDTMIEV HNKIDLVDMP ENIDASVLSV SALLGHGLED LKQQVETAVM KSTGRNVLTI NVKLESPQLS WLYKESSVQE VKVLPEDGTA RVRVIITNSA YGKYKKLFCK // ID F7CX02_ORNAN Unreviewed; 466 AA. AC F7CX02; DT 27-JUL-2011, integrated into UniProtKB/TrEMBL. DT 27-JUL-2011, sequence version 1. DT 05-JUL-2017, entry version 32. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSOANP00000011164}; OS Ornithorhynchus anatinus (Duckbill platypus). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Monotremata; Ornithorhynchidae; Ornithorhynchus. OX NCBI_TaxID=9258 {ECO:0000313|Ensembl:ENSOANP00000011164, ECO:0000313|Proteomes:UP000002279}; RN [1] {ECO:0000313|Ensembl:ENSOANP00000011164, ECO:0000313|Proteomes:UP000002279} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Glennie {ECO:0000313|Ensembl:ENSOANP00000011164, RC ECO:0000313|Proteomes:UP000002279}; RX PubMed=18464734; DOI=10.1038/nature06936; RA Warren W.C., Hillier L.W., Marshall Graves J.A., Birney E., RA Ponting C.P., Grutzner F., Belov K., Miller W., Clarke L., RA Chinwalla A.T., Yang S.P., Heger A., Locke D.P., Miethke P., RA Waters P.D., Veyrunes F., Fulton L., Fulton B., Graves T., Wallis J., RA Puente X.S., Lopez-Otin C., Ordonez G.R., Eichler E.E., Chen L., RA Cheng Z., Deakin J.E., Alsop A., Thompson K., Kirby P., RA Papenfuss A.T., Wakefield M.J., Olender T., Lancet D., Huttley G.A., RA Smit A.F., Pask A., Temple-Smith P., Batzer M.A., Walker J.A., RA Konkel M.K., Harris R.S., Whittington C.M., Wong E.S., Gemmell N.J., RA Buschiazzo E., Vargas Jentzsch I.M., Merkel A., Schmitz J., Zemann A., RA Churakov G., Kriegs J.O., Brosius J., Murchison E.P., RA Sachidanandam R., Smith C., Hannon G.J., Tsend-Ayush E., McMillan D., RA Attenborough R., Rens W., Ferguson-Smith M., Lefevre C.M., Sharp J.A., RA Nicholas K.R., Ray D.A., Kube M., Reinhardt R., Pringle T.H., RA Taylor J., Jones R.C., Nixon B., Dacheux J.L., Niwa H., Sekita Y., RA Huang X., Stark A., Kheradpour P., Kellis M., Flicek P., Chen Y., RA Webber C., Hardison R., Nelson J., Hallsworth-Pepin K., Delehaunty K., RA Markovic C., Minx P., Feng Y., Kremitzki C., Mitreva M., Glasscock J., RA Wylie T., Wohldmann P., Thiru P., Nhan M.N., Pohl C.S., Smith S.M., RA Hou S., Nefedov M., de Jong P.J., Renfree M.B., Mardis E.R., RA Wilson R.K.; RT "Genome analysis of the platypus reveals unique signatures of RT evolution."; RL Nature 453:175-183(2008). RN [2] {ECO:0000313|Ensembl:ENSOANP00000011164} RP IDENTIFICATION. RC STRAIN=Glennie {ECO:0000313|Ensembl:ENSOANP00000011164}; RG Ensembl; RL Submitted (JUL-2011) to UniProtKB. CC -!- CAUTION: The sequence shown here is derived from an Ensembl CC automatic analysis pipeline and should be considered as CC preliminary data. {ECO:0000313|Ensembl:ENSOANP00000011164}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR STRING; 9258.ENSOANP00000011164; -. DR Ensembl; ENSOANT00000011166; ENSOANP00000011164; ENSOANG00000007007. DR eggNOG; KOG0410; Eukaryota. DR eggNOG; COG2262; LUCA. DR GeneTree; ENSGT00390000001397; -. DR InParanoid; F7CX02; -. DR OMA; MDTVGFM; -. DR OrthoDB; EOG091G0852; -. DR TreeFam; TF315022; -. DR Proteomes; UP000002279; Unplaced. DR Bgee; ENSOANG00000007007; -. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR GO; GO:0043022; F:ribosome binding; IBA:GO_Central. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 2. DR SUPFAM; SSF52540; SSF52540; 1. PE 4: Predicted; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000002279}; KW Reference proteome {ECO:0000313|Proteomes:UP000002279}. FT DOMAIN 66 154 GTP-bdg_N. {ECO:0000259|Pfam:PF13167}. FT DOMAIN 158 236 GTP-bdg_M. {ECO:0000259|Pfam:PF16360}. FT DOMAIN 244 301 G (guanine nucleotide-binding). FT {ECO:0000259|Pfam:PF01926}. FT COILED 208 238 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 466 AA; 51235 MW; D45842CD6CFB7EA7 CRC64; MWASGAVCRR GAARDPRGRE QTREDELLRT EPLLPLGSQR VFLVHPDIKR GPKKPTLTRG PEVDLQVAEA TALVRTLADW SVEETAVVST KTPGEKLVFG KGNFALLTEK IKSCPQITSV FLNVERMTPV TKRELEAAWG VEVFDRFTVV LHIFRCNART REAKLQLALA EIPLLRSNLR NEVAHLDQQG GGSRYILGSG ETFVEVRRRL LKEKEIKIKK ALEKLREKRH LLRSQRRKCE FPVIAVMGYT NSGKTSLIRA LTGDPAAEPR DQPFATDITA RAGALPSRLT VIYVDTIGFL SQLPQARMGS WCATRSPVAH GAPPSLIPPL GSPLAPGRRL SAVFLEHGLV FHTTLTGAPA QPASRPDFTG RSPSPRYAPA EPNAVAVSAL LGHGLGELKA EIDRVVLKAT GRKVLTLKID LAGAQLSWLY KEATVQEVDV IPEDGTANVR VIMSHSAYGK YRSRFP // ID F7CX09_ORNAN Unreviewed; 459 AA. AC F7CX09; DT 27-JUL-2011, integrated into UniProtKB/TrEMBL. DT 27-JUL-2011, sequence version 1. DT 05-JUL-2017, entry version 29. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSOANP00000011163}; OS Ornithorhynchus anatinus (Duckbill platypus). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Monotremata; Ornithorhynchidae; Ornithorhynchus. OX NCBI_TaxID=9258 {ECO:0000313|Ensembl:ENSOANP00000011163, ECO:0000313|Proteomes:UP000002279}; RN [1] {ECO:0000313|Ensembl:ENSOANP00000011163, ECO:0000313|Proteomes:UP000002279} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Glennie {ECO:0000313|Ensembl:ENSOANP00000011163, RC ECO:0000313|Proteomes:UP000002279}; RX PubMed=18464734; DOI=10.1038/nature06936; RA Warren W.C., Hillier L.W., Marshall Graves J.A., Birney E., RA Ponting C.P., Grutzner F., Belov K., Miller W., Clarke L., RA Chinwalla A.T., Yang S.P., Heger A., Locke D.P., Miethke P., RA Waters P.D., Veyrunes F., Fulton L., Fulton B., Graves T., Wallis J., RA Puente X.S., Lopez-Otin C., Ordonez G.R., Eichler E.E., Chen L., RA Cheng Z., Deakin J.E., Alsop A., Thompson K., Kirby P., RA Papenfuss A.T., Wakefield M.J., Olender T., Lancet D., Huttley G.A., RA Smit A.F., Pask A., Temple-Smith P., Batzer M.A., Walker J.A., RA Konkel M.K., Harris R.S., Whittington C.M., Wong E.S., Gemmell N.J., RA Buschiazzo E., Vargas Jentzsch I.M., Merkel A., Schmitz J., Zemann A., RA Churakov G., Kriegs J.O., Brosius J., Murchison E.P., RA Sachidanandam R., Smith C., Hannon G.J., Tsend-Ayush E., McMillan D., RA Attenborough R., Rens W., Ferguson-Smith M., Lefevre C.M., Sharp J.A., RA Nicholas K.R., Ray D.A., Kube M., Reinhardt R., Pringle T.H., RA Taylor J., Jones R.C., Nixon B., Dacheux J.L., Niwa H., Sekita Y., RA Huang X., Stark A., Kheradpour P., Kellis M., Flicek P., Chen Y., RA Webber C., Hardison R., Nelson J., Hallsworth-Pepin K., Delehaunty K., RA Markovic C., Minx P., Feng Y., Kremitzki C., Mitreva M., Glasscock J., RA Wylie T., Wohldmann P., Thiru P., Nhan M.N., Pohl C.S., Smith S.M., RA Hou S., Nefedov M., de Jong P.J., Renfree M.B., Mardis E.R., RA Wilson R.K.; RT "Genome analysis of the platypus reveals unique signatures of RT evolution."; RL Nature 453:175-183(2008). RN [2] {ECO:0000313|Ensembl:ENSOANP00000011163} RP IDENTIFICATION. RC STRAIN=Glennie {ECO:0000313|Ensembl:ENSOANP00000011163}; RG Ensembl; RL Submitted (JUL-2011) to UniProtKB. CC -!- CAUTION: The sequence shown here is derived from an Ensembl CC automatic analysis pipeline and should be considered as CC preliminary data. {ECO:0000313|Ensembl:ENSOANP00000011163}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR Ensembl; ENSOANT00000011165; ENSOANP00000011163; ENSOANG00000007007. DR eggNOG; KOG0410; Eukaryota. DR eggNOG; COG2262; LUCA. DR GeneTree; ENSGT00390000001397; -. DR Proteomes; UP000002279; Unplaced. DR Bgee; ENSOANG00000007007; -. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 2. DR SUPFAM; SSF52540; SSF52540; 1. PE 4: Predicted; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000002279}; KW Reference proteome {ECO:0000313|Proteomes:UP000002279}. FT DOMAIN 59 147 GTP-bdg_N. {ECO:0000259|Pfam:PF13167}. FT DOMAIN 151 229 GTP-bdg_M. {ECO:0000259|Pfam:PF16360}. FT DOMAIN 237 294 G (guanine nucleotide-binding). FT {ECO:0000259|Pfam:PF01926}. FT COILED 201 231 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 459 AA; 50359 MW; 4EF2C2FC24B316B3 CRC64; GGGPAEEDPR GREQTREDEL LRTEPLLPLG SQRVFLVHPD IKRGPKKPTL TRGPEVDLQV AEATALVRTL ADWSVEETAV VSTKTPGEKL VFGKGNFALL TEKIKSCPQI TSVFLNVERM TPVTKRELEA AWGVEVFDRF TVVLHIFRCN ARTREAKLQL ALAEIPLLRS NLRNEVAHLD QQGGGSRYIL GSGETFVEVR RRLLKEKEIK IKKALEKLRE KRHLLRSQRR KCEFPVIAVM GYTNSGKTSL IRALTGDPAA EPRDQPFATD ITARAGALPS RLTVIYVDTI GFLSQLPQAR MGSWCATRSP VAHGAPPSLI PPLGSPLAPG RRLSAVFLEH GLVFHTTLTG APAQPASRPD FTGRSPSPRY APAEPNAVAV SALLGHGLGE LKAEIDRVVL KATGRKVLTL KIDLAGAQLS WLYKEATVQE VDVIPEDGTA NVRVIMSHSA YGKYRSRFP // ID F7KK82_9FIRM Unreviewed; 432 AA. AC F7KK82; DT 21-SEP-2011, integrated into UniProtKB/TrEMBL. DT 21-SEP-2011, sequence version 1. DT 07-JUN-2017, entry version 38. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=HMPREF0994_06261 {ECO:0000313|EMBL:EGN30530.1}; OS Lachnospiraceae bacterium 3_1_57FAA_CT1. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Lachnospiraceae. OX NCBI_TaxID=658086 {ECO:0000313|EMBL:EGN30530.1, ECO:0000313|Proteomes:UP000003336}; RN [1] {ECO:0000313|Proteomes:UP000003336} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=3_1_57FAA_CT1 {ECO:0000313|Proteomes:UP000003336}; RG The Broad Institute Genome Sequencing Platform; RA Earl A., Ward D., Feldgarden M., Gevers D., Daigneault M., Strauss J., RA Allen-Vercoe E., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., RA Haas B., Abouelleil A., Alvarado L., Arachchi H.M., Berlin A., RA Brown A., Chapman S.B., Chen Z., Dunbar C., Freedman E., Gearin G., RA Gellesch M., Goldberg J., Griggs A., Gujja S., Heiman D., Howarth C., RA Larson L., Lui A., MacDonald P.J.P., Mehta T., Montmayeur A., RA Murphy C., Neiman D., Pearson M., Priest M., Roberts A., Saif S., RA Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., Wortman J., RA Nusbaum C., Birren B.; RT "The Genome Sequence of Lachnospiraceae bacterium 2_1_58FAA."; RL Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:EGN30530.1, ECO:0000313|Proteomes:UP000003336} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=3_1_57FAA_CT1 {ECO:0000313|EMBL:EGN30530.1, RC ECO:0000313|Proteomes:UP000003336}; RG The Broad Institute Genomics Platform; RA Earl A., Ward D., Feldgarden M., Gevers D., Daigneault M., Strauss J., RA Allen-Vercoe E., Walker B., Young S., Zeng Q., Gargeya S., RA Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L., RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., RA Goldberg J., Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., RA Ireland A., Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., RA Priest M., Roberts A., Saif S., Shea T., Sisk P., Sykes S., RA Wortman J., Nusbaum C., Birren B.; RT "The Genome Sequence of Lachnospiraceae bacterium 3-1-57FAA CT1."; RL Submitted (APR-2013) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EGN30530.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACTP02000007; EGN30530.1; -; Genomic_DNA. DR RefSeq; WP_009256037.1; NZ_KE150405.1. DR ProteinModelPortal; F7KK82; -. DR STRING; 658086.HMPREF0994_06261; -. DR EnsemblBacteria; EGN30530; EGN30530; HMPREF0994_06261. DR PATRIC; fig|658086.3.peg.6862; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000003336; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000003336}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000003336}. FT DOMAIN 206 376 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 165 199 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 432 AA; 49376 MW; A0EDD1EB8A0B7DDA CRC64; MNENNNTQQE NISRVLLVGV NVDDNPDFET SMEELESLAE ACEMEVAAKI EQNLSSLNPA YYIGSGKVKE VQETVEQLDL DYVIFDETLS PSQLKNLQKE VGVPIMDRTN LILEIFSRRA KTREARLQVE SANLQYMLPR LVGMREALGR QAGASGSMSN KGTGEKQIEL DRRKIEKRIS ELRRELEAIE HDRNTQRKRR NDSSLPQVAL VGYTNAGKST LMNKMVETYV GKEEKMVVAR DMLFATLDTT VRKINQNDRK DFLLSDTVGF ISKLPHGLVK AFRSTLDEVR YADLLLQIVD ASDEHYREHI QVTEETLREL GAEKIPCIYV MNKADLIMEK EELPRIDGNK IFMSARDGIG LQELLQMIKK RVFSGNREGI FLIPYEKGEI VSYLNSNATV SSQEYLAEGV KLFVDCRESD YSKYREYLFP ED // ID F7KRE0_9FIRM Unreviewed; 426 AA. AC F7KRE0; DT 21-SEP-2011, integrated into UniProtKB/TrEMBL. DT 21-SEP-2011, sequence version 1. DT 07-JUN-2017, entry version 36. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=HMPREF0993_01532 {ECO:0000313|EMBL:EGN39285.1}; OS Lachnospiraceae bacterium 5_1_57FAA. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Lachnospiraceae. OX NCBI_TaxID=658085 {ECO:0000313|EMBL:EGN39285.1, ECO:0000313|Proteomes:UP000005617}; RN [1] {ECO:0000313|EMBL:EGN39285.1, ECO:0000313|Proteomes:UP000005617} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=5_1_57FAA {ECO:0000313|EMBL:EGN39285.1, RC ECO:0000313|Proteomes:UP000005617}; RG The Broad Institute Genome Sequencing Platform; RA Earl A., Ward D., Feldgarden M., Gevers D., Daigneault M., Strauss J., RA Allen-Vercoe E., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., RA Haas B., Abouelleil A., Alvarado L., Arachchi H.M., Berlin A., RA Brown A., Chapman S.B., Chen Z., Dunbar C., Freedman E., Gearin G., RA Gellesch M., Goldberg J., Griggs A., Gujja S., Heiman D., Howarth C., RA Larson L., Lui A., MacDonald P.J.P., Mehta T., Montmayeur A., RA Murphy C., Neiman D., Pearson M., Priest M., Roberts A., Saif S., RA Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., Wortman J., RA Nusbaum C., Birren B.; RT "The Genome Sequence of Lachnospiraceae bacterium 5_1_57FAA."; RL Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EGN39285.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACTR01000011; EGN39285.1; -; Genomic_DNA. DR RefSeq; WP_004605650.1; NZ_GL945249.1. DR ProteinModelPortal; F7KRE0; -. DR EnsemblBacteria; EGN39285; EGN39285; HMPREF0993_01532. DR PATRIC; fig|658085.3.peg.1579; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000005617; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000005617}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000005617}. FT DOMAIN 202 366 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 161 195 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 426 AA; 47790 MW; 2F78DC0A7557D4BA CRC64; MGNMIDLEKE TERVILVGVS VTDEDDTQKS LEELKDLAST AGAATVGVVI QNREQVHPGT YVGKGKIEEI KGLMWELEAT GIICDDELSP AQMKNLQDEL DAKVMDRTLV ILDIFASRAS TSEGKIQVEL AQLKYRQSRL TGFGTALSRL GGGIGTRGPG EKKLEMDRRL IKGRIAQLNR ELRDVKRHRE VTREQRSRNR IPVAAIVGYT NAGKSTLLNT LTGAGILAED KLFATLDPTT RELKLPSGQE ILLTDTVGFI RKLPHHLIEA FRSTLEEARY ADIILHVVDA ANPQMDEQMY IVYETLQNLG VTDKPIVTIF NKQDKAQDDV IIRDFHADYT VKISAKTREG IPELLKTIEA VLRQQKVAIE NLYPYQDAAK IQMIRRFGEL QEEEYREDGI FVRAYVPVDI YEKVKVSRGD SPKSAL // ID F7NPC5_9FIRM Unreviewed; 619 AA. AC F7NPC5; DT 21-SEP-2011, integrated into UniProtKB/TrEMBL. DT 21-SEP-2011, sequence version 1. DT 07-JUN-2017, entry version 42. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=ALO_19842 {ECO:0000313|EMBL:EGO62087.1}; OS Acetonema longum DSM 6540. OC Bacteria; Firmicutes; Negativicutes; Selenomonadales; Sporomusaceae; OC Acetonema. OX NCBI_TaxID=1009370 {ECO:0000313|EMBL:EGO62087.1, ECO:0000313|Proteomes:UP000003240}; RN [1] {ECO:0000313|EMBL:EGO62087.1, ECO:0000313|Proteomes:UP000003240} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 6540 {ECO:0000313|EMBL:EGO62087.1, RC ECO:0000313|Proteomes:UP000003240}; RX PubMed=21673657; DOI=10.1038/emboj.2011.186; RA Chen S., Beeby M., Murphy G.E., Leadbetter J.R., Hendrixson D.R., RA Briegel A., Li Z., Shi J., Tocheva E.I., Muller A., Dobro M.J., RA Jensen G.J.; RT "Structural diversity of bacterial flagellar motors."; RL EMBO J. 30:2972-2981(2011). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EGO62087.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFGF01000241; EGO62087.1; -; Genomic_DNA. DR RefSeq; WP_004099263.1; NZ_AFGF01000241.1. DR ProteinModelPortal; F7NPC5; -. DR STRING; 1009370.ALO_19842; -. DR EnsemblBacteria; EGO62087; EGO62087; ALO_19842. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000003240; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000003240}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000003240}. FT DOMAIN 384 550 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 619 AA; 68494 MW; B36C7A31DD926F59 CRC64; MSQNKIISGE LDGIRQNVIQ ELQRIYDMQV PANQPVSQEV AAKAAQLSAQ IRREVVLYIN RRGKVTHIAI GDIQSATLPE IDLRRSNTKL NGFRCIHTHP GGDSRLSRLD ISSLKQLRFD LIAALGVEAD GGISSVSMGF ISNLASSPGD TVVQSIELMG FNEFADLNVT DFIAFLERQF SVTQMHDVAQ RKERVLLAGL ETKGSEWDIA DSLAELVQLA ETAGGCVVGQ VSQVREKPDA AFFLGKGKVD EIQHLIQETE ADVLVLDDEL TPAQQRNLEQ YLKIKVIDRT ALILDIFAQR ARSYEGKLQV ELAQLRYNLP RLSGQGLVLS RLGGGIGTRG PGETKLEMDK RRIRSRIHDV EKEIETVKAN RALQRIRRKK SSIPSVVLIG YTNAGKSTLL NSLSEAGVLA EDKLFATLDP TTRNVKLSNG QEILLTDTVG FIQKLPHHLV AAFRATLEEV KQADLLLHVL DISHPRFRAQ SDAVFHVLRE LESDSKDIIT VCNKVDRLES GDALREKLLK QEHAVAISAL TGEGSDDLFA AIEQVLNQRT QIIEMLIPYE ASGLVSNLYG FAVVQSVDYQ ESGIRVKVSV SSEYIKRYHQ FIVGEEENND SISGYDSPG // ID F7NY35_9GAMM Unreviewed; 428 AA. AC F7NY35; DT 21-SEP-2011, integrated into UniProtKB/TrEMBL. DT 21-SEP-2011, sequence version 1. DT 12-APR-2017, entry version 37. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=Rhein_2710 {ECO:0000313|EMBL:EGM77176.1}; OS Rheinheimera sp. A13L. OC Bacteria; Proteobacteria; Gammaproteobacteria; Chromatiales; OC Chromatiaceae; Rheinheimera. OX NCBI_TaxID=506534 {ECO:0000313|EMBL:EGM77176.1, ECO:0000313|Proteomes:UP000004282}; RN [1] {ECO:0000313|EMBL:EGM77176.1, ECO:0000313|Proteomes:UP000004282} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=A13L {ECO:0000313|EMBL:EGM77176.1, RC ECO:0000313|Proteomes:UP000004282}; RX PubMed=21742876; DOI=10.1128/JB.05636-11; RA Gupta H.K., Gupta R.D., Singh A., Chauhan N.S., Sharma R.; RT "Genome Sequence of Rheinheimera sp. Strain A13L, Isolated from RT Pangong Lake, India."; RL J. Bacteriol. 193:5873-5874(2011). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EGM77176.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFHI01000024; EGM77176.1; -; Genomic_DNA. DR ProteinModelPortal; F7NY35; -. DR STRING; 506534.Rhein_2710; -. DR EnsemblBacteria; EGM77176; EGM77176; Rhein_2710. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000004282; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000004282}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000004282}. FT DOMAIN 198 364 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 428 AA; 48126 MW; 9B0111476BB20377 CRC64; MFDSDMVPEQ AILVHIYLSQ DSASEDLQEL EMLVSSAGVE SRAVMTANRS TIDAKFFLGS GKAAELAQAV AELQVDLIIF NHSLTPAQTR NLELLCQCRV IDRTTLILDI FAQRARSYEG KLQVELAQLK HLSSRLVRGW DNAERQKGGI GMRGPGETRL ETDRRLLRDK ITALLLKLDK VSKQREQGRK ARQRAEIPVV SLVGYTNAGK STLFNRLTSS DVYAADQLFA TLDPTLRQVK LQEFGSIIFA DTVGFIRHLP HDLVAAFKST LQESRDADLQ LHVIDVADQR MADNIKQVQL VLHEIDADQV PQLLVFNKID QTEQQARIEY NEQAEPIAVY ISAKQGVGIE LLLQVIRERL ADDYMQLDLK LPADAAVWRA RLHELSAVQT ESFTDLGETQ VRIALSKAEW ARLLKQSDGL LQNYIVRT // ID F7PPD2_9EURY Unreviewed; 439 AA. AC F7PPD2; DT 21-SEP-2011, integrated into UniProtKB/TrEMBL. DT 21-SEP-2011, sequence version 1. DT 07-JUN-2017, entry version 46. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX2 {ECO:0000313|EMBL:ERJ04561.1}; GN Synonyms=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:CCQ32843.1}; GN ORFNames=HLRTI_003472 {ECO:0000313|EMBL:ERJ04561.1}, GN HTIA_0703 {ECO:0000313|EMBL:CCQ32843.1}; OS Halorhabdus tiamatea SARL4B. OC Archaea; Euryarchaeota; Halobacteria; Halobacteriales; Haloarculaceae; OC Halorhabdus. OX NCBI_TaxID=1033806 {ECO:0000313|EMBL:ERJ04561.1, ECO:0000313|Proteomes:UP000003861}; RN [1] {ECO:0000313|EMBL:ERJ04561.1, ECO:0000313|Proteomes:UP000003861} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SARL4B {ECO:0000313|EMBL:ERJ04561.1, RC ECO:0000313|Proteomes:UP000003861}; RX PubMed=21705593; DOI=10.1128/JB.05462-11; RA Antunes A., Alam I., Bajic V.B., Stingl U.; RT "Genome sequence of Halorhabdus tiamatea, the first archaeon isolated RT from a deep-sea anoxic brine lake."; RL J. Bacteriol. 193:4553-4554(2011). RN [2] {ECO:0000313|EMBL:ERJ04561.1, ECO:0000313|Proteomes:UP000003861} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SARL4B {ECO:0000313|EMBL:ERJ04561.1, RC ECO:0000313|Proteomes:UP000003861}; RX PubMed=24324765; RA Alam I., Antunes A., Kamau A.A., Ba Alawi W., Kalkatawi M., Stingl U., RA Bajic V.B.; RT "INDIGO - INtegrated Data Warehouse of MIcrobial GenOmes with Examples RT from the Red Sea Extremophiles."; RL PLoS ONE 8:E82210-E82210(2013). RN [3] {ECO:0000313|EMBL:CCQ32843.1, ECO:0000313|Proteomes:UP000015381} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SARL4B {ECO:0000313|Proteomes:UP000015381}, and RC Type strain: SARL4B {ECO:0000313|EMBL:CCQ32843.1}; RX DOI=10.1111/1462-2920.12393; RA Werner J., Ferrer M., Michel G., Mann A.J., Huang S., Juarez S., RA Ciordia S., Albar J.P., Alcaide M., La Cono V., Yakimov M.M., RA Antunes A., Taborda M., Da Costa M.S., Amann R.I., Gloeckner F.O., RA Golyshina O.V., Golyshin P.N., Teeling H.; RT "Halorhabdus tiamatea: proteogenomics and glycosidase activity RT measurements identify the first cultivated euryarchaeon from a deep- RT sea anoxic brine lake as potential polysaccharide degrader."; RL Environ. Microbiol. 0:0-0(2014). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; HF571520; CCQ32843.1; -; Genomic_DNA. DR EMBL; AFNT02000070; ERJ04561.1; -; Genomic_DNA. DR RefSeq; WP_008527825.1; NZ_AFNT02000070.1. DR STRING; 1033806.HLRTI_16055; -. DR EnsemblBacteria; CCQ32843; CCQ32843; HTIA_0703. DR EnsemblBacteria; ERJ04561; ERJ04561; HLRTI_003472. DR GeneID; 23797965; -. DR KEGG; hti:HTIA_0703; -. DR PATRIC; fig|1033806.12.peg.696; -. DR eggNOG; arCOG00353; Archaea. DR eggNOG; COG2262; LUCA. DR KO; K03665; -. DR OrthoDB; POG093Z07D6; -. DR Proteomes; UP000003861; Unassembled WGS sequence. DR Proteomes; UP000015381; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0016746; F:transferase activity, transferring acyl groups; IEA:UniProtKB-KW. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Acyltransferase {ECO:0000313|EMBL:ERJ04561.1}; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000015381}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000015381}; KW Transferase {ECO:0000313|EMBL:ERJ04561.1}. FT DOMAIN 194 377 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 110 144 {ECO:0000256|SAM:Coils}. FT COILED 160 190 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 439 AA; 49067 MW; 026640147397FD26 CRC64; MTGTDRPTDG ALVVKRVEAG SADTTEIERL ADAAGYDVLA TLTQTRTEDP AYHVGEGKAA EIADQLRARD AAVVIFDNQL GPYQTYNLGT EFPEGVRLLD RFRLILEIFG QRAQTRKAQL QVELAELRYE LPRAEAKASL ARREEHPGFM GLGEYDESRE QDIKNRIARI RDELEKIERT DEHRREQRRE SGFDLVALAG YTNAGKSTLL RRLAEDLDVD ENEDIHPDLD ETAASEDRLF TTLGTTTRRA DFDRRDVLVT DTVGFISDLP HWLVESFKST LGSVYQADLV LLVVDVGESV ESIREKLVTA HDTLYERNEA PILTVLNKID TVEAAELDRK REALSALAPN PVAVSAKTGE NVDALRERID ESLPELERER LVLPMTDDAM SVVSWIHDHA NVETVDYGEQ VVVEFEGRPA VIEQSRAKAS DLVPAESAS // ID F7QN31_9BRAD Unreviewed; 436 AA. AC F7QN31; DT 21-SEP-2011, integrated into UniProtKB/TrEMBL. DT 21-SEP-2011, sequence version 1. DT 12-APR-2017, entry version 36. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:EGP07246.1}; GN ORFNames=CSIRO_2974 {ECO:0000313|EMBL:EGP07246.1}; OS Bradyrhizobiaceae bacterium SG-6C. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Bradyrhizobiaceae. OX NCBI_TaxID=709797 {ECO:0000313|EMBL:EGP07246.1, ECO:0000313|Proteomes:UP000003148}; RN [1] {ECO:0000313|EMBL:EGP07246.1, ECO:0000313|Proteomes:UP000003148} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SG-6C {ECO:0000313|EMBL:EGP07246.1}; RX PubMed=21742875; DOI=10.1128/JB.05647-11; RA Pearce S.L., Pandey R., Dorrian S.J., Russell R.J., Oakeshott J.G., RA Pandey G.; RT "Genome Sequence of the Newly Isolated Chemolithoautotrophic RT Bradyrhizobiaceae Strain SG-6C."; RL J. Bacteriol. 193:5057-5057(2011). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EGP07246.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFOF01000028; EGP07246.1; -; Genomic_DNA. DR ProteinModelPortal; F7QN31; -. DR STRING; 709797.CSIRO_2974; -. DR EnsemblBacteria; EGP07246; EGP07246; CSIRO_2974. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000003148; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000003148}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000003148}. FT DOMAIN 203 377 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 436 AA; 48327 MW; B53C9DFD7A85996F CRC64; MLVIGPYRRV RRGDPDAPSM SHGIRNPEAR LEEAAGLARA IDLTVAEAVI APLSDIRPAT YLGKGKVEEM LGLIKANDVD LVVMDCALSP VQQRNLEKEW KAKVLDRTGL ILEIFGRRAK TREGALQVEL AHLNYQRSRL VRSWTHLERQ RGGFGFMGGP GETQIEADRR MISERISKIE SELKKVQATR RLHRAGRQRV PYRVVALVGY TNAGKSTLFN RLTRADVQAA DMLFATLDPT LRALTLPHGG KAMLSDTVGF ISDLPTMLVA AFRATLEEVI EADVILHVRD ISHEDAEAQQ HDVEGVLRQL GIDTDGGQRI LEVWNKIDRF DEEGRANLMN IAARRPPERP CFPVSAETGE GLDALLAAIE DRLAATRVTL DLTIDPSDGA GISWLHRNAE VLDKHLENGR FAMTVRVDIS KRDITIAKFG AVPSVQ // ID F7S0L0_9GAMM Unreviewed; 427 AA. AC F7S0L0; DT 21-SEP-2011, integrated into UniProtKB/TrEMBL. DT 21-SEP-2011, sequence version 1. DT 30-AUG-2017, entry version 38. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=A28LD_2054 {ECO:0000313|EMBL:EGN74560.1}; OS Idiomarina sp. A28L. OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales; OC Idiomarinaceae; Idiomarina. OX NCBI_TaxID=1036674 {ECO:0000313|EMBL:EGN74560.1, ECO:0000313|Proteomes:UP000053031}; RN [1] {ECO:0000313|EMBL:EGN74560.1, ECO:0000313|Proteomes:UP000053031} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=A28L {ECO:0000313|EMBL:EGN74560.1, RC ECO:0000313|Proteomes:UP000053031}; RX PubMed=21742887; DOI=10.1128/JB.05648-11; RA Gupta H.K., Singh A., Sharma R.; RT "Genome Sequence of Idiomarina sp. Strain A28L, Isolated from Pangong RT Lake, India."; RL J. Bacteriol. 193:5875-5876(2011). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EGN74560.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFPO01000024; EGN74560.1; -; Genomic_DNA. DR RefSeq; WP_007421016.1; NZ_AFPO01000024.1. DR ProteinModelPortal; F7S0L0; -. DR STRING; 1036674.A28LD_2054; -. DR EnsemblBacteria; EGN74560; EGN74560; A28LD_2054. DR PATRIC; fig|1036674.4.peg.2050; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000053031; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000053031}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000053031}. FT DOMAIN 198 365 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 427 AA; 48211 MW; D44E3AF2392180B2 CRC64; MFERYEGGEQ AVLVHVEFSN ESAREDLEEL KLLVSSAGVE AVSVITTSRH APDARLFIGS GKTEEVAAMV EATGAEIVIF NHSLSPSQER NIEREVKCRV LDRTGLILDI FAQRARTHEG KLQVELAQLR HISTRLIRGW THLERQKGGI GLRGPGETQL ETDRRLIRGR IKNILARLEK VSKQREQGRR SRQRAEIPTI ALVGYTNAGK STLFNRLTDS DVYAADQLFA TLDPTLRKYE LPDVGSLIFA DTVGFIRHLP HDLVAAFKAT LQETRDAELL LHVMDCHDER MLDNQHEVDK VLTEIAASEV PQLLVMNKLD LVPDLQPRIV RDDDGKPKEV WLSAQTGEGI DLLREALHEI LVPKLMIEEL RLGPNQGKLR SSLYELQCVT DERPQDDGDV LVSVRVPVVE WQRLLKQFGE QLTRSLC // ID F7T4X9_9BURK Unreviewed; 368 AA. AC F7T4X9; DT 21-SEP-2011, integrated into UniProtKB/TrEMBL. DT 21-SEP-2011, sequence version 1. DT 07-JUN-2017, entry version 39. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=AXXA_20007 {ECO:0000313|EMBL:EGP44601.1}; OS Achromobacter insuavis AXX-A. OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Alcaligenaceae; Achromobacter. OX NCBI_TaxID=1003200 {ECO:0000313|EMBL:EGP44601.1, ECO:0000313|Proteomes:UP000004853}; RN [1] {ECO:0000313|EMBL:EGP44601.1, ECO:0000313|Proteomes:UP000004853} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=AXX-A {ECO:0000313|EMBL:EGP44601.1, RC ECO:0000313|Proteomes:UP000004853}; RA Bador J., Amoureux L., Neuwirth C.; RL Submitted (JUN-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EGP44601.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFRQ01000077; EGP44601.1; -; Genomic_DNA. DR RefSeq; WP_006393981.1; NZ_GL982453.1. DR STRING; 1003200.AXXA_20007; -. DR EnsemblBacteria; EGP44601; EGP44601; AXXA_20007. DR PATRIC; fig|1003200.3.peg.3977; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000004853; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000004853}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}. FT DOMAIN 190 354 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 156 183 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 368 AA; 40276 MW; 14293382CF567B88 CRC64; MRALIISVDL GDPDFAAHAE EFAMLAKGAG AEIVGTLTAR RDRPDAKFFI GSGKADEGVG MAQALLADIV LFDQPLSPAQ QRNLERVFNL RVVDRVALIL DIFALRAKSH EGKLQVELAQ LQHLATRLTR MWSHLERQRG GIGMRGPGES QLEMDRRMIG AKVKTLRERL DRVERQRVTQ RRARARGGAL SVSLVGYTNA GKSTLFNALT RADTYAADQL FATLDTTTRR IWIEGAGNVV VSDTVGFIRD LPHDLIAAFR ATLEETVHAD LLLHVVDAAS PQRDEQIFEV NKVLAEIGAA SIPTILVYNK IDRAGLEPRA ERDAHGTIAR VFVSATERAG LDALRGAIAE TGQIVGNNAS NYQTLQSE // ID F7V1B4_EEGSY Unreviewed; 442 AA. AC F7V1B4; DT 21-SEP-2011, integrated into UniProtKB/TrEMBL. DT 21-SEP-2011, sequence version 1. DT 05-JUL-2017, entry version 41. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=HflX {ECO:0000313|EMBL:BAK44557.1}; GN Synonyms=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=EGYY_14060 {ECO:0000313|EMBL:BAK44557.1}; OS Eggerthella sp. (strain YY7918). OC Bacteria; Actinobacteria; Coriobacteriia; Eggerthellales; OC Eggerthellaceae; Eggerthella. OX NCBI_TaxID=502558 {ECO:0000313|EMBL:BAK44557.1, ECO:0000313|Proteomes:UP000008929}; RN [1] {ECO:0000313|Proteomes:UP000008929} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=YY7918 {ECO:0000313|Proteomes:UP000008929}; RA Yokoyama S., Oshima K., Nomura I., Hattori M., Suzuki T.; RT "Complete genome sequence of the equol-producing bacterium Eggerthella RT sp. strain YY7918 isolated from adult human intestine."; RL Submitted (JUN-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AP012211; BAK44557.1; -; Genomic_DNA. DR ProteinModelPortal; F7V1B4; -. DR STRING; 502558.EGYY_14060; -. DR EnsemblBacteria; BAK44557; BAK44557; EGYY_14060. DR KEGG; eyy:EGYY_14060; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR KO; K03665; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000008929; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000008929}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000008929}. FT DOMAIN 217 382 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 442 AA; 48663 MW; 74C329328430CCF9 CRC64; MSEFESVITR GMTTVAEQRR ERAVLVGVDR PGTTWPLASS LAELERLVDT AGADVVATTS QRLEAPNPKT FVGTGKAEEV AALARANAAD LVVFDDELTP SQQANLEKIV GKDVKIIDRT ALILDIFALH ATSKEGRLQV RLAQNEYLLP RLRGMWAHLA SNRMGGGVGS RFGEGESQLE VDRRMVRKRI TSIKRELKHL AAVRALQRES RYESGMFKVA LAGYTNAGKS SLLNRLTNAE VLAYDKLFAT LDSTTRKFEL PEGREITLTD TVGFIQKLPT TLVEAFKSTL DEITGADLIL HIVDASSDEY EEQIAAVDDI LGQIEAQKIK RVLVFNKCDL LDEEHRNALR ARHTQAQFVS AATGEGIPIL VEHIARVASA HDAHLDVLIP YDRGDLVSIA HERCHILSES HEEAGTHIVM LAGASYAGLF RPFLVESEHE AE // ID F7V589_CLOSS Unreviewed; 416 AA. AC F7V589; DT 21-SEP-2011, integrated into UniProtKB/TrEMBL. DT 21-SEP-2011, sequence version 1. DT 07-JUN-2017, entry version 39. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=HflX {ECO:0000313|EMBL:BAK47918.1}; GN Synonyms=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=CXIVA_19510 {ECO:0000313|EMBL:BAK47918.1}; OS Clostridium sp. (strain SY8519). OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=1042156 {ECO:0000313|EMBL:BAK47918.1, ECO:0000313|Proteomes:UP000008937}; RN [1] {ECO:0000313|Proteomes:UP000008937} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SY8519 {ECO:0000313|Proteomes:UP000008937}; RX PubMed=21914882; DOI=10.1128/JB.05637-11; RA Yokoyama S., Oshima K., Nomura I., Hattori M., Suzuki T.; RT "Complete genomic sequence of the O-desmethylangolensin-producing RT bacterium Clostridium rRNA cluster XIVa strain SY8519, isolated from RT adult human intestine."; RL J. Bacteriol. 193:5568-5569(2011). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AP012212; BAK47918.1; -; Genomic_DNA. DR STRING; 1042156.CXIVA_19510; -. DR EnsemblBacteria; BAK47918; BAK47918; CXIVA_19510. DR KEGG; cls:CXIVA_19510; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000008937; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000008937}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000008937}. FT DOMAIN 202 366 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 161 195 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 416 AA; 46630 MW; 630A24E0DC43EEF6 CRC64; MSEMIQIRQE QESFVLVAAA LEEEQAAWDS LEELQELAET SGAAVVGQVL QNRSAFDPAT YVGSGKIEEI HSLLLQTGAT GILCDDELSP AQIANLNDLL HTKVIDRTLV ILDIFARRAS SAEGKAQVEL AQQRYNLTHL AGLGRSLSRL GGGIGTRGPG EKKLEMDRRR IRSRISQLKR EIREIQQHRQ VTRENRQRSS IRQAAVVGYT NAGKSTLLNC LTGAGVLEED RLFATLDPTT RLLQLEGGQE ILLTDTVGFI SKLPHHLIEA FRSTLEEAKY ADYIIHVVDA SSPQMEEHIR VVYETLEQLG IGRHRIITLL NKMDLVEGPL YYRDPHAVKT IRTSLRKGEG TELVKQALTE LLLEESVYLE HCFPYASAGS IQLIRKYGNL LAEEYTPEGI RVRAYVPREI YRKVKP // ID F7VH02_9PROT Unreviewed; 438 AA. AC F7VH02; DT 21-SEP-2011, integrated into UniProtKB/TrEMBL. DT 21-SEP-2011, sequence version 1. DT 05-JUL-2017, entry version 35. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=ATPR_2651 {ECO:0000313|EMBL:GAA09647.1}; OS Acetobacter tropicalis NBRC 101654. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales; OC Acetobacteraceae; Acetobacter. OX NCBI_TaxID=749388 {ECO:0000313|EMBL:GAA09647.1, ECO:0000313|Proteomes:UP000004319}; RN [1] {ECO:0000313|EMBL:GAA09647.1, ECO:0000313|Proteomes:UP000004319} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NBRC 101654 {ECO:0000313|EMBL:GAA09647.1, RC ECO:0000313|Proteomes:UP000004319}; RX PubMed=21554859; DOI=10.1016/j.bbrc.2011.04.126; RA Matsutani M., Hirakawa H., Nishikura M., Soemphol W., Ali I.A.I., RA Yakushi T., Matsushita K.; RT "Increased number of Arginine-based salt bridges contributes to the RT thermotolerance of thermotolerant acetic acid bacteria, Acetobacter RT tropicalis SKU1100."; RL Biochem. Biophys. Res. Commun. 409:120-124(2011). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:GAA09647.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BABS01000109; GAA09647.1; -; Genomic_DNA. DR ProteinModelPortal; F7VH02; -. DR EnsemblBacteria; GAA09647; GAA09647; ATPR_2651. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000004319; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000004319}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000004319}. FT DOMAIN 209 378 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 438 AA; 48049 MW; A9AD02D208E44309 CRC64; MATTLSDTKP SATRGAVILP WEKSSHDQDI RAAEARLEEA VGLAASIGLV IVRQAVLLVR AKRSATLLGS GQVDSLKVAV KADKIDVLVV DARLTPGQQR NLETEFGCKV IDRTGLILDI FGARAATKEG TLQVELAHLE YQRSRLVRLW THLERQRGGF GFLGGPGETQ IEADRRMIGD RIVRLKKELE QVRRTRGLHR QARKRVPFPV VALVGYTNAG KSTLFNALTG ATVYAKDQLF ATLDPTMRAI TLPSGRRIIL SDTVGFISDL PTELIAAFRA TLEEVAEADI ILHVRDIAHP DSAAQKKDVF GVLDGMARDD MIESDWASRM IEVMNKADLL GGPDAVPQTE DTVAISAITG DGLPALMDVI DRRITSSMEN VRYRVPLSDG AASAWLYQHG EVTDRQDDDT CTTITVRLLA EDRARFESLF KHVEPLVA // ID F7XPR8_METZD Unreviewed; 425 AA. AC F7XPR8; DT 21-SEP-2011, integrated into UniProtKB/TrEMBL. DT 21-SEP-2011, sequence version 1. DT 07-JUN-2017, entry version 46. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Mzhil_0464 {ECO:0000313|EMBL:AEH60338.1}; OS Methanosalsum zhilinae (strain DSM 4017 / NBRC 107636 / OCM 62 / WeN5) OS (Methanohalophilus zhilinae). OC Archaea; Euryarchaeota; Methanomicrobia; Methanosarcinales; OC Methanosarcinaceae; Methanosalsum. OX NCBI_TaxID=679901 {ECO:0000313|EMBL:AEH60338.1, ECO:0000313|Proteomes:UP000006622}; RN [1] {ECO:0000313|EMBL:AEH60338.1, ECO:0000313|Proteomes:UP000006622} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 4017 / NBRC 107636 / OCM 62 / WeN5 RC {ECO:0000313|Proteomes:UP000006622}; RG US DOE Joint Genome Institute (JGI-PGF); RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., RA Tice H., Bruce D., Goodwin L., Pitluck S., Kyrpides N., Mavromatis K., RA Ovchinnikova G., Daligault H., Detter J.C., Han C., Tapia R., RA Larimer F., Land M., Hauser L., Markowitz V., Cheng J.-F., RA Hugenholtz P., Woyke T., Wu D., Spring S., Schueler E., Brambilla E., RA Klenk H.-P., Eisen J.A.; RT "The complete genome of Methanosalsum zhilinae DSM 4017."; RL Submitted (JUL-2010) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:AEH60338.1, ECO:0000313|Proteomes:UP000006622} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 4017 / NBRC 107636 / OCM 62 / WeN5 RC {ECO:0000313|Proteomes:UP000006622}; RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., RA Tice H., Bruce D., Goodwin L., Pitluck S., Kyrpides N., Mavromatis K., RA Ovchinnikova G., Daligault H., Detter J.C., Han C., Tapia R., RA Larimer F., Land M., Hauser L., Markowitz V., Cheng J.-F., RA Hugenholtz P., Woyke T., Wu D., Spring S., Schueler E., Brambilla E., RA Klenk H.-P., Eisen J.A.; RT "The complete genome of Methanosalsum zhilinae DSM 4017."; RL Submitted (JUL-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002101; AEH60338.1; -; Genomic_DNA. DR RefSeq; WP_013897777.1; NC_015676.1. DR ProteinModelPortal; F7XPR8; -. DR STRING; 679901.Mzhil_0464; -. DR EnsemblBacteria; AEH60338; AEH60338; Mzhil_0464. DR GeneID; 10822071; -. DR KEGG; mzh:Mzhil_0464; -. DR eggNOG; arCOG00353; Archaea. DR eggNOG; COG2262; LUCA. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG093Z07D6; -. DR Proteomes; UP000006622; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000006622}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000006622}. FT DOMAIN 191 360 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 157 184 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 425 AA; 48671 MW; DEE57A76AE079336 CRC64; MKKAVLVQRN EPESEEYRNS SRLQELKELA ESAGYLVVDE VTQTKNPDRN YQIGRGKADE LSRIVAETGA NKIIFYNQLS IMQIYNISQT CRCETIDKFH LILEIFATKA KTKRAKYQVE LAKLHYELPK AKTIVSLLKK KERPGFMGLG SYEDSYEKDI KNRISRLRNE LGRMQKDYEN LRTTRHNKGF SIVALAGYTN AGKSTLFSEM VDENVEVENR LFTTLSPTTR SFQVNGRKLL LTDTVGFIED LPHWLIDAFK STLDEIFLAD VILLVVDVSE PVEIIKKKLV ACHDTLWEQI EDAPIIAVLN KVDRISEEDL VCRISEIEYL TPNPIIISAS EGTGIETLKQ KIFSYLPVWK RKDLQLPISD SGMSIASWLF DEGIVHNIKY TDRILVDVEA RDEVINKAKA VERELHAYGH PKNQL // ID F7YIT0_VIBA7 Unreviewed; 429 AA. AC F7YIT0; DT 21-SEP-2011, integrated into UniProtKB/TrEMBL. DT 21-SEP-2011, sequence version 1. DT 30-AUG-2017, entry version 44. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=VAA_00119 {ECO:0000313|EMBL:AEH34367.1}; OS Vibrio anguillarum (strain ATCC 68554 / 775) (Listonella anguillarum). OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; OC Vibrionaceae; Vibrio. OX NCBI_TaxID=882102 {ECO:0000313|EMBL:AEH34367.1, ECO:0000313|Proteomes:UP000006800}; RN [1] {ECO:0000313|EMBL:AEH34367.1, ECO:0000313|Proteomes:UP000006800} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 68554 / 775 {ECO:0000313|Proteomes:UP000006800}; RX PubMed=21576332; DOI=10.1128/IAI.05138-11; RA Naka H., Dias G.M., Thompson C.C., Dubay C., Thompson F.L., RA Crosa J.H.; RT "Complete genome sequence of the marine fish pathogen Vibrio RT anguillarum harboring the pJM1 virulence plasmid and genomic RT comparison with other virulent strains of V. anguillarum and V. RT ordalii."; RL Infect. Immun. 79:2889-2900(2011). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002284; AEH34367.1; -; Genomic_DNA. DR RefSeq; WP_010318941.1; NC_015633.1. DR ProteinModelPortal; F7YIT0; -. DR STRING; 882102.VAA_00119; -. DR EnsemblBacteria; AEH34367; AEH34367; VAA_00119. DR GeneID; 10776650; -. DR KEGG; van:VAA_00119; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000006800; Chromosome I. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000006800}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000006800}. FT DOMAIN 198 365 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 429 AA; 48752 MW; ABE5A136C80647CE CRC64; MFDRYEAGER AVLVHINFTQ KGEWDDLSEC EMLVSSAGVS TLQIITGSRQ TPHPKYYVGE GKAQEIAHAV QLVEADVVIF NHALSPAQER NLEQLCQCRV IDRTGLILDI FAQRARTHEG KLQVELAQLR HISTRLIRGW THLERQKGGI GLRGPGETQL ETDRRLLRER IKAILRRLEK VAKQREQGRR ARNRAEIPTI SLVGYTNAGK STLFNRITEA GVYAADQLFA TLDPTLRKIE LADVGTAVLA DTVGFIRHLP HDLVAAFKAT LQETQEADIL LHVVDASDER FRENIKAVHD VLEEIDAHEV PTLVVMNKID NLEGQQPRIE KDDEGIPRTV WLSAMDGQGI DLLFEALTER LASQVIQYQL CIPPLHQGRI RSAFSQMKCI QQEEYDPDGN LLINIRMQQV DWFRLEKREE AVLRDFIVT // ID F7YXR6_9THEM Unreviewed; 420 AA. AC F7YXR6; DT 21-SEP-2011, integrated into UniProtKB/TrEMBL. DT 21-SEP-2011, sequence version 1. DT 07-JUN-2017, entry version 44. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=Theth_0623 {ECO:0000313|EMBL:AEH50710.1}; OS Pseudothermotoga thermarum DSM 5069. OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; OC Pseudothermotoga. OX NCBI_TaxID=688269 {ECO:0000313|EMBL:AEH50710.1, ECO:0000313|Proteomes:UP000006804}; RN [1] {ECO:0000313|EMBL:AEH50710.1, ECO:0000313|Proteomes:UP000006804} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 5069 {ECO:0000313|EMBL:AEH50710.1, RC ECO:0000313|Proteomes:UP000006804}; RG US DOE Joint Genome Institute (JGI-PGF); RA Lucas S., Copeland A., Lapidus A., Bruce D., Goodwin L., Pitluck S., RA Kyrpides N., Mavromatis K., Ivanova N., Zeytun A., Brettin T., RA Detter J.C., Tapia R., Han C., Land M., Hauser L., Markowitz V., RA Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Spring S., Schroeder M., RA Brambilla E., Klenk H.-P., Eisen J.A.; RT "The complete genome of Thermotoga thermarum DSM 5069."; RL Submitted (NOV-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002351; AEH50710.1; -; Genomic_DNA. DR STRING; 688269.Theth_0623; -. DR EnsemblBacteria; AEH50710; AEH50710; Theth_0623. DR KEGG; tta:Theth_0623; -. DR PATRIC; fig|688269.3.peg.646; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR KO; K03665; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000006804; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000006804}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000006804}. FT DOMAIN 197 362 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 16 39 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 420 AA; 47557 MW; 8EBE6AA01D645CC4 CRC64; MKVKEIDTAL KQSAILVSIK KDLDSLEELK QLLANLEVEV ITTFVQSRLE PDPVTYLGKG KLEELKALVQ AYQPSFVVID GEVKPLQAKN IEKILQVPLK DRTQVILDIF AKHATTEESI LQVELAKLSY ELPRLVGEGK SLSRTGGGIG TRGPGEQKIE ERRRYIKRRI AWIRKKLEEI RLNREIQRRK RLESDLPMVS FVGYTNAGKS SLLKVLSKSD IVVSEKMFSS LSPVIRRVKL PNGRVVLMKD TVGFIRNVPH TIIEAFKSTL EEILYSDLLA LVVDVSEENF AEKMKTSIMV LKELSAESIP RLIVFNKIDL VSPEVLEKLT TIYPEAVFVS AKTGKGIDEF LQKVTEKLFQ NEAEEIFEID PSALPTVMKY CELLTIVQEE WCNGKIRLKL KGSKDVLERL RKVVLGGIEE // ID F7ZZN3_CELGA Unreviewed; 507 AA. AC F7ZZN3; DT 21-SEP-2011, integrated into UniProtKB/TrEMBL. DT 21-SEP-2011, sequence version 1. DT 07-JUN-2017, entry version 41. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Celgi_2025 {ECO:0000313|EMBL:AEI12526.1}; OS Cellulomonas gilvus (strain ATCC 13127 / NRRL B-14078) (Cellvibrio OS gilvus). OC Bacteria; Actinobacteria; Micrococcales; Cellulomonadaceae; OC Cellulomonas. OX NCBI_TaxID=593907 {ECO:0000313|EMBL:AEI12526.1, ECO:0000313|Proteomes:UP000000485}; RN [1] {ECO:0000313|Proteomes:UP000000485} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 13127 / NRRL B-14078 {ECO:0000313|Proteomes:UP000000485}; RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S., RA Peters L., Munk A., Detter J.C., Han C., Tapia R., Land M., Hauser L., RA Kyrpides N., Ivanova N., Ovchinnikova G., Pagani I., Mead D., RA Brumm P., Woyke T.; RT "Complete sequence of Cellvibrio gilvus ATCC 13127."; RL Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002665; AEI12526.1; -; Genomic_DNA. DR RefSeq; WP_013884044.1; NC_015671.1. DR STRING; 593907.Celgi_2025; -. DR EnsemblBacteria; AEI12526; AEI12526; Celgi_2025. DR KEGG; cga:Celgi_2025; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000000485; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 2. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000000485}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000000485}. FT DOMAIN 285 451 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 507 AA; 54684 MW; 81BEF1047F817F57 CRC64; MSETHHTTTP SRTPDEPRSP QQVADDVVAR VLARAGTALQ AGGTVHSSYD GQQLDLEERT SLRRVAGLST ELQDVTEVEY RELRLENVVL VGVWGQGTVQ DAEVSLRELA ALAETAGSRV LEGVLQRRAK PDPSTYLGSG KAAELATVVA AVGADTVVVD GELAPSQRRA LEDVVRVKVV DRTALILDIF AQHAKSREGK AQVELAQLEY LLPRLRGWGE SMSRQAGGQV GGAGAGMGSR GPGETKIELD RRRIRNRMAK LRREIAAMEP ARLTKRASRK RNAIPSVAIA GYTNAGKSSL LNRLTHAGVL VENALFATLD PTVRRAETVD GRVYTLADTV GFVRALPHQL VEAFRSTLEE VADADLILHV VDASHPDPEG QIAAVRHVFA DIPGAMDVPE IIVLNKADLA TPEAIARLRS RELHSIVVSA HSGEGIEELQ DLIADQLPRP GVAVDLVVPY GRGDLVSRVH EHGDIELEEH TPDGTHLRAR VDETLAAELE TSAARRA // ID F8A9F0_THEID Unreviewed; 559 AA. AC F8A9F0; DT 21-SEP-2011, integrated into UniProtKB/TrEMBL. DT 21-SEP-2011, sequence version 1. DT 07-JUN-2017, entry version 45. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Thein_0206 {ECO:0000313|EMBL:AEH44091.1}; OS Thermodesulfatator indicus (strain DSM 15286 / JCM 11887 / CIR29812). OC Bacteria; Thermodesulfobacteria; Thermodesulfobacteriales; OC Thermodesulfobacteriaceae; Thermodesulfatator. OX NCBI_TaxID=667014 {ECO:0000313|EMBL:AEH44091.1, ECO:0000313|Proteomes:UP000006793}; RN [1] {ECO:0000313|Proteomes:UP000006793} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 15286 / JCM 11887 / CIR29812 RC {ECO:0000313|Proteomes:UP000006793}; RA Lucas S., Copeland A., Lapidus A., Bruce D., Goodwin L., Pitluck S., RA Peters L., Kyrpides N., Mavromatis K., Pagani I., Ivanova N., RA Saunders L., Detter J.C., Tapia R., Han C., Land M., Hauser L., RA Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Spring S., RA Schroeder M., Brambilla E., Klenk H.-P., Eisen J.A.; RT "The complete genome of Thermodesulfatator indicus DSM 15286."; RL Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002683; AEH44091.1; -; Genomic_DNA. DR RefSeq; WP_013906838.1; NC_015681.1. DR STRING; 667014.Thein_0206; -. DR EnsemblBacteria; AEH44091; AEH44091; Thein_0206. DR KEGG; tid:Thein_0206; -. DR PATRIC; fig|667014.3.peg.211; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR KO; K03665; -. DR OMA; EREVIIT; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000006793; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000006793}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000006793}. FT DOMAIN 379 543 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 338 372 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 559 AA; 64136 MW; DA515C83F92B7994 CRC64; MSKTLYGNTS GLKPSQIKRL ERLYRRRVSP SQIISHELSK ELAALSHELN RQLGILINRR GEIEFVIVGE HGRIVIPAIT RYRESAGRLR GLRLIHTHLS HEGLDQDDLL DLAFLRLDLI GALMVKEDGF PGKIYLAHLL PAGENGRHYG YLPTVYPWEL KEDFLKLISS LEDELERQRP AKEVADACDR AILISVTTRS RAEAEESLAE LKELARSAGV TVLDTIIQRR HKVDPRYLMG KGKLSELIIR AMQVSANLLI FDQELTPSQM RSITEVTEMR VIDRTQLILD IFAQRAKSRE GKIQVEMAQL RYLLPRLRSR DDAFSRLTGG IGGRGPGETK LEIDRRRIKD RIARLERELK NISSQRKLRR KRRQREGLPV VAIVGYTNAG KTTFLNQLTK SDLLAEDKLF ATLDPASRRV RLPDGSLAIF TDTVGFIKDL PKDLERAFRA TLEELYEADL LLHLVDASNP YFEEHIQAVE KILEEMNLEH LPRILVLNKI DLLDELEVEV LKRRYQAEAI SALDKETFAP LLEKINFMLL PQKKNTEREI EYQFELLSN // ID F8AIJ0_PYRYC Unreviewed; 426 AA. AC F8AIJ0; DT 21-SEP-2011, integrated into UniProtKB/TrEMBL. DT 21-SEP-2011, sequence version 1. DT 07-JUN-2017, entry version 42. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=PYCH_06680 {ECO:0000313|EMBL:AEH24356.1}; OS Pyrococcus yayanosii (strain CH1 / JCM 16557). OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae; OC Pyrococcus. OX NCBI_TaxID=529709 {ECO:0000313|EMBL:AEH24356.1, ECO:0000313|Proteomes:UP000008386}; RN [1] {ECO:0000313|EMBL:AEH24356.1, ECO:0000313|Proteomes:UP000008386} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CH1 / JCM 16557 {ECO:0000313|Proteomes:UP000008386}; RX PubMed=21705594; DOI=10.1128/JB.05345-11; RA Jun X., Lupeng L., Minjuan X., Oger P., Fengping W., Jebbar M., RA Xiang X.; RT "Complete genome sequence of the obligate piezophilic RT hyperthermophilic archaeon Pyrococcus yayanosii CH1."; RL J. Bacteriol. 193:4297-4298(2011). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002779; AEH24356.1; -; Genomic_DNA. DR RefSeq; WP_013905413.1; NC_015680.1. DR STRING; 529709.PYCH_06680; -. DR EnsemblBacteria; AEH24356; AEH24356; PYCH_06680. DR GeneID; 10837244; -. DR KEGG; pya:PYCH_06680; -. DR eggNOG; arCOG00353; Archaea. DR eggNOG; COG2262; LUCA. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG093Z07D6; -. DR Proteomes; UP000008386; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000008386}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}. FT DOMAIN 186 362 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 426 AA; 48956 MW; CB4C16EE2CED5D2D CRC64; MKVVGVIRHE PRRRASREEF EELLRSAGYE VLAIVEQVRE EHPRYNIGPG KLEEVKKLVK ALRPDRVVFA NRLTPSQAYN LWRELRVEIM DKWQLVLEIF EKRAHSKEAK LQVELANLQY ELPLVKEAIR RIRLGDRAGF KGMGEYQTQQ YLKHIRYRMG KIREELEKIR AERAVRRKKR EEEGFVLIAL AGYTNAGKST LLNILTNEDV DAKNQMFTTL DTTTRRFRLR GKKVLITDTV GFIDDLPPFI VEAFHSTLEE IVKADVVVLV VDASEPWPEV RRKFLASLDV LRELKALDRP IIVALNKVDL VGEEDAGEKE ALILELAERR SVTLSGTAKI SARLGRVEEL LEVLERTILS LPKFRLFEIK IREPEKVGKV LSIVRSIGEL VAVEYGPETT IRAYIQAGMI RELTKLGVEL RAAQPP // ID F8B383_FRADG Unreviewed; 464 AA. AC F8B383; DT 21-SEP-2011, integrated into UniProtKB/TrEMBL. DT 21-SEP-2011, sequence version 1. DT 07-JUN-2017, entry version 44. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=FsymDg_3604 {ECO:0000313|EMBL:AEH10883.1}; OS Frankia symbiont subsp. Datisca glomerata. OC Bacteria; Actinobacteria; Frankiales; Frankiaceae; Frankia. OX NCBI_TaxID=656024 {ECO:0000313|EMBL:AEH10883.1, ECO:0000313|Proteomes:UP000001549}; RN [1] {ECO:0000313|EMBL:AEH10883.1, ECO:0000313|Proteomes:UP000001549} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=4085684 {ECO:0000313|EMBL:AEH10883.1}; RG US DOE Joint Genome Institute; RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S., RA Peters L., Mikhailova N., Chertkov O., Teshima H., Han C., Tapia R., RA Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Berry A., RA Pawlowski K., Persson T., Vanden Heuvel B., Benson D., Woyke T.; RT "Complete sequence of chromosome of Frankia symbiont of Datisca RT glomerata."; RL Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002801; AEH10883.1; -; Genomic_DNA. DR RefSeq; WP_013874766.1; NC_015656.1. DR ProteinModelPortal; F8B383; -. DR STRING; 656024.FsymDg_3604; -. DR EnsemblBacteria; AEH10883; AEH10883; FsymDg_3604. DR KEGG; fsy:FsymDg_3604; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000001549; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000001549}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000001549}. FT DOMAIN 243 407 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 202 229 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 464 AA; 49919 MW; 20DA667F9FD17D1B CRC64; MTFPAIFDAS DEDLGLGLGL DLADRLALRR VPGLATELDD VTEVEYRQLR LERVVLIGVW TSGTAAEAET SMAELAALAA TAGSVILDAL IQRRDTPDSA TYVGSGKARE LRDVVTATGA DTVVCDGELT PGQLRQLEDV VKVKVIDRTA LILDIFAQHA TSREGKAQVE LAQLQYMLPR LRGWGESMSR AGGGIGTRGP GETKIETDRR RLRARMARLR RELAGMKTVR TTKRSARQRS GIPAVAITGY TNAGKSSLLN RLTGAGVLVE DALFATLDPA VRRATLPDGR TFTLADTVGF VRHLPHQIVE AFRSTLEEVA DANLLLHVVD GSHPDPMSQI SAVRTVINDI GAGDVPELLV VNKIDAADPD VLARVRRTVP DAILVSARTG DGLTALVEEL TERVPHPDVE VCVLLPFTRG DLVSRVYARG EVLGLEHTAT GTVLRARVPA ELASQLTSFF LEPA // ID F8BUY6_OLICO Unreviewed; 463 AA. AC F8BUY6; DT 21-SEP-2011, integrated into UniProtKB/TrEMBL. DT 21-SEP-2011, sequence version 1. DT 07-JUN-2017, entry version 48. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:AEI06639.1}; GN OrderedLocusNames=OCA5_c19270 {ECO:0000313|EMBL:AEI06639.1}; OS Oligotropha carboxidovorans (strain ATCC 49405 / DSM 1227 / KCTC 32145 OS / OM5). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Bradyrhizobiaceae; Oligotropha. OX NCBI_TaxID=504832 {ECO:0000313|EMBL:AEI06639.1, ECO:0000313|Proteomes:UP000007730}; RN [1] {ECO:0000313|EMBL:AEI06639.1, ECO:0000313|Proteomes:UP000007730} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 49405 / DSM 1227 / KCTC 32145 / OM5 RC {ECO:0000313|Proteomes:UP000007730}; RX PubMed=21742883; DOI=10.1128/JB.05619-11; RA Volland S., Rachinger M., Strittmatter A., Daniel R., Gottschalk G., RA Meyer O.; RT "Complete genome sequences of the chemolithoautotrophic Oligotropha RT carboxidovorans strains OM4 and OM5."; RL J. Bacteriol. 193:5043-5043(2011). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002826; AEI06639.1; -; Genomic_DNA. DR RefSeq; WP_013913116.1; NC_015684.1. DR ProteinModelPortal; F8BUY6; -. DR STRING; 504832.OCA5_c19270; -. DR EnsemblBacteria; AEI06639; AEI06639; OCA5_c19270. DR KEGG; ocg:OCA5_c19270; -. DR PATRIC; fig|504832.7.peg.2050; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR KO; K03665; -. DR Proteomes; UP000007730; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000007730}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000007730}. FT DOMAIN 230 404 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 463 AA; 51168 MW; D3F9CFE4BFBB3C73 CRC64; MDPRSFGGAA DRPGSGGPAQ GQTTGRVLVV GPYLRARRGS ADIATIGSDA VRDPQARLDE AAGLARAIDL TVAEALIAPL SEIRPATYLG KGKVEDILGL IKAHDVDLVV MDCALSPIQQ RNLEKEWNAK VLDRTGLILE IFGRRAKTRE GTLQVELAHL IYQRSRLVRS WTHLERQRGG FGFMGGPGET QIEADRRMIG ERITRIENDL KKVQATRRLH RAGRKRVPYR VVALVGYTNA GKSTLFNRLT RADVQAADML FATLDPTLRA LRLPHGGKAM ISDTVGFISD LPTMLVAAFR ATLEEVIEAD VILHVRDISH EDAEAQERDV DHVLRQLGIG TESGHRIIEV WNKIDCFSPE ERENLARIAA RRPADHPCFL VSAETGEGID ALLAAIEERL AALRTVLELR IDAADGEGIS WIHRNAEVLE KTLDDDHFDM VIRVDETKRD TAIARFQAVP REA // ID F8C2Q5_THEGP Unreviewed; 592 AA. AC F8C2Q5; DT 21-SEP-2011, integrated into UniProtKB/TrEMBL. DT 21-SEP-2011, sequence version 1. DT 07-JUN-2017, entry version 44. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=TOPB45_1377 {ECO:0000313|EMBL:AEH23458.1}; OS Thermodesulfobacterium geofontis (strain OPF15). OC Bacteria; Thermodesulfobacteria; Thermodesulfobacteriales; OC Thermodesulfobacteriaceae; Thermodesulfobacterium. OX NCBI_TaxID=795359 {ECO:0000313|EMBL:AEH23458.1, ECO:0000313|Proteomes:UP000006583}; RN [1] {ECO:0000313|Proteomes:UP000006583} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=OPB45 {ECO:0000313|Proteomes:UP000006583}; RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S., RA Peters L., Mikhailova N., Davenport K., Detter J.C., Han C., Tapia R., RA Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., RA Hamilton-Brehm S., Elkins J., Woyke T.; RT "Complete sequence of Thermodesulfobacterium sp. OPB45."; RL Submitted (JUN-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002829; AEH23458.1; -; Genomic_DNA. DR RefSeq; WP_013910156.1; NC_015682.1. DR STRING; 795359.TOPB45_1377; -. DR EnsemblBacteria; AEH23458; AEH23458; TOPB45_1377. DR KEGG; top:TOPB45_1377; -. DR PATRIC; fig|795359.3.peg.1398; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR KO; K03665; -. DR OMA; EREVIIT; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000006583; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000006583}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000006583}. FT DOMAIN 396 566 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 355 389 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 592 AA; 68111 MW; 8CC4854A2FED5BE8 CRC64; MGSQIFGNTI GLKPSELKKL EKLYRRKVPP TSIITHELAK EISQISAEIN RQVGILINRK GEIDYVIVGT FNRIEIPELK GYRDHIARLK GLRCIHTHLI NSQNDKTKPS GLDQDDLIDL AFLRLDLIGA LEVKPDGEPG KIYIAHILPD PEFFKGALLD QEEKFFYFLK PCYVWELKEN FLELIKNLED ELDRIRPLKE IGENKDRAIL IFIKEPKDIY LEEKMEELEE LARTAGVSVV GKVVQKRVSP DPKYVIGKGK LVEVMILAMR NRANLLIFDR ELTPSQVRAL TEVTDLRVID RTQLILDIFA QRASSREGKI QVEIAQLRYA LPRLRAKDDA FSRLTGGIGG RGPGETKLEI DRRRIKDKIA KLERELSKIS QERELRRKRR KKLNFKVVSL IGYTNAGKTT LLNTLAKTNY LAEDKLFATL DPVTKLIKTK NGKVFLLTDT VGFIRDLPED LKKAFKATLE ELYSADILLH IVDISHPDFE NHIKAVEQIL EEMDLLHIPK ILVFNKIDLL ENKENFSPLW LKNLVSKYNA IPISAKKGIN LDLLIEAIEN WLTILEKEKP ENFPVFSEEE NLPKVPREHR FF // ID F8D6L0_HALXS Unreviewed; 433 AA. AC F8D6L0; DT 21-SEP-2011, integrated into UniProtKB/TrEMBL. DT 21-SEP-2011, sequence version 1. DT 07-JUN-2017, entry version 44. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Halxa_3136 {ECO:0000313|EMBL:AEH37750.1}; OS Halopiger xanaduensis (strain DSM 18323 / JCM 14033 / SH-6). OC Archaea; Euryarchaeota; Halobacteria; Natrialbales; Natrialbaceae; OC Halopiger. OX NCBI_TaxID=797210 {ECO:0000313|EMBL:AEH37750.1, ECO:0000313|Proteomes:UP000006794}; RN [1] {ECO:0000313|EMBL:AEH37750.1, ECO:0000313|Proteomes:UP000006794} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 18323 / JCM 14033 / SH-6 RC {ECO:0000313|Proteomes:UP000006794}; RX PubMed=22675596; DOI=10.4056/sigs.2505605; RA Anderson I., Tindall B.J., Rohde M., Lucas S., Han J., Lapidus A., RA Cheng J.F., Goodwin L., Pitluck S., Peters L., Pati A., Mikhailova N., RA Pagani I., Teshima H., Han C., Tapia R., Land M., Woyke T., RA Klenk H.P., Kyrpides N., Ivanova N.; RT "Complete genome sequence of Halopiger xanaduensis type strain (SH- RT 6(T))."; RL Stand. Genomic Sci. 6:31-42(2012). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002839; AEH37750.1; -; Genomic_DNA. DR RefSeq; WP_013880640.1; NC_015666.1. DR STRING; 797210.Halxa_3136; -. DR EnsemblBacteria; AEH37750; AEH37750; Halxa_3136. DR GeneID; 10798087; -. DR KEGG; hxa:Halxa_3136; -. DR eggNOG; arCOG00353; Archaea. DR eggNOG; COG2262; LUCA. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG093Z07D6; -. DR Proteomes; UP000006794; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000006794}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000006794}. FT DOMAIN 186 369 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 102 129 {ECO:0000256|SAM:Coils}. FT COILED 152 182 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 433 AA; 48610 MW; 1AE0ECEC09A56C4C CRC64; MNAIIAKRVD SGTPDTTEIR DLATAAGYTV VGEITQSRKA DPALQLGEGK AEELAEVAER TEATTVIFDN RLGPYQTYNL GQLLPEGVEV IDRFTLILEI FGQRAQTRKA QLQVELAELR YELPRAEAKT SLAKRDEHPG FMGLGEYDES REQDIKDQIS RIKDELERIE QTEEQRRERR RDSGFDLVAL AGYTNAGKST LLRRLAADLD VDENEGLHRD LDATAESQDK LFTTLGTTTR RADIEPRDVL VTDTVGFISD LPHWLVESFK STLDWVYRAD LVLLVVDVSE DIDEIHEKLV TCHDTLYERN EAPIVTVLNK IDTVDDDELA EKRRALSSLA PNPVTVSARE GTNVEALLDR IDSELPDWEE ERLMLPMTDD TMSLVSWIHD NAHVDDVTYG DQDVIVSFEA RPAVISQARS RASELRTTAA ESA // ID F8DXZ5_CORRG Unreviewed; 490 AA. AC F8DXZ5; DT 21-SEP-2011, integrated into UniProtKB/TrEMBL. DT 21-SEP-2011, sequence version 1. DT 07-JUN-2017, entry version 42. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:AEI09553.1}; GN OrderedLocusNames=CRES_1198 {ECO:0000313|EMBL:AEI09553.1}; OS Corynebacterium resistens (strain DSM 45100 / JCM 12819 / GTC 2026). OC Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae; OC Corynebacterium. OX NCBI_TaxID=662755 {ECO:0000313|EMBL:AEI09553.1, ECO:0000313|Proteomes:UP000000492}; RN [1] {ECO:0000313|EMBL:AEI09553.1, ECO:0000313|Proteomes:UP000000492} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 45100 / JCM 12819 / GTC 2026 RC {ECO:0000313|Proteomes:UP000000492}; RX PubMed=22524407; DOI=10.1186/1471-2164-13-141; RA Schroder J., Maus I., Meyer K., Wordemann S., Blom J., Jaenicke S., RA Schneider J., Trost E., Tauch A.; RT "Complete genome sequence, lifestyle, and multi-drug resistance of the RT human pathogen Corynebacterium resistens DSM 45100 isolated from blood RT samples of a leukemia patient."; RL BMC Genomics 13:141-141(2012). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002857; AEI09553.1; -; Genomic_DNA. DR RefSeq; WP_013888566.1; NC_015673.1. DR STRING; 662755.CRES_1198; -. DR EnsemblBacteria; AEI09553; AEI09553; CRES_1198. DR KEGG; crd:CRES_1198; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000000492; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000000492}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000000492}. FT DOMAIN 266 435 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 225 252 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 490 AA; 53453 MW; FFACF385DE23B441 CRC64; MTEESKLYPG ARRATDEDSS LIDATKPTTG ELDLEARSSL RRLTRGTSAY TDEQADGYDV EYRKLRLEKV ILVGVWTEGT VQQIEARLEE LAALAETAGS EIADITYQKR DKPDAGTYIG RGKVDELRHI VVETGADTVI ADGELSPGQM IALEKALDVK VIDRTMLILD IFAQHAKSKE GKAQVALAQM EYLITRVRGW GGALSRQAGG RAGANGGVGL RGPGETKIEA DRRRLRADMA RLRKEIASMK TSRDIKRERR DSAAIAQVAI AGYTNAGKSS LINALTGAGV LVEDALFATL DPTTRRAELA DGRAVIFTDT VGFVRHLPTQ LVEAFRSTLE EVMAADVVLH VVDGSDPFPL EQIVAVNKVI GEIVEETGEH APPEILVVNK IDKADPLVLA ELRHRLDDVV FVSAHSGEGI SELETRLELF LNSLDSQVDL HVPFDRGDVV ARVHELGTVL SESYDEHGTH LEVRLPAQVA AELKEFTVEQ // ID F8E3S4_FLESM Unreviewed; 548 AA. AC F8E3S4; DT 21-SEP-2011, integrated into UniProtKB/TrEMBL. DT 21-SEP-2011, sequence version 1. DT 07-JUN-2017, entry version 44. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Flexsi_0671 {ECO:0000313|EMBL:AEI14347.1}; OS Flexistipes sinusarabici (strain DSM 4947 / MAS 10). OC Bacteria; Deferribacteres; Deferribacterales; Deferribacteraceae; OC Flexistipes. OX NCBI_TaxID=717231 {ECO:0000313|EMBL:AEI14347.1, ECO:0000313|Proteomes:UP000006621}; RN [1] {ECO:0000313|Proteomes:UP000006621} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 4947 / MAS 10 {ECO:0000313|Proteomes:UP000006621}; RA Lucas S., Han J., Lapidus A., Bruce D., Goodwin L., Pitluck S., RA Peters L., Kyrpides N., Mavromatis K., Ivanova N., Mikhailova N., RA Chertkov O., Detter J.C., Tapia R., Han C., Land M., Hauser L., RA Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Spring S., RA Schroeder M., Brambilla E., Klenk H.-P., Eisen J.A.; RT "The complete genome of Flexistipes sinusarabici DSM 4947."; RL Submitted (JUN-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002858; AEI14347.1; -; Genomic_DNA. DR RefSeq; WP_013885851.1; NC_015672.1. DR ProteinModelPortal; F8E3S4; -. DR STRING; 717231.Flexsi_0671; -. DR EnsemblBacteria; AEI14347; AEI14347; Flexsi_0671. DR KEGG; fsi:Flexsi_0671; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR KO; K03665; -. DR OMA; EREVIIT; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000006621; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000006621}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000006621}. FT DOMAIN 374 539 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 340 367 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 548 AA; 62076 MW; AFCBE605BD3E6760 CRC64; MLYGYTENLK AKFLKRFEKL DKRKSKSTAI ISNDLIKNIT SLSYETGQQV GLLIDRNNTI QYVLVGTNKE VLIPKLHRFA LVPGKLRGLR LVHTHLYNEE LTDDDFTDLV LLRLDSVSAV TMDENGNPLK MHSAHIMPPD ADKPYEVFTD KDPYDQKLDY LSFIKSLEEE VESKTKQLHE TKLYESAILI GVYSNKYEAG ESMAELRELA ASAKIEVMDT FYQIKNKPNP KYIVGSGKLK EIVIKALSSG VDYLIFDNQL SPAQSKAVAN FTELKVIDRT QLILDIFAAR AKSNEGKLRV ELAQLKHILP KLSARDDSLS RLTGGIGGRG PGETKLEVDR RRINDRIAFL NKKLKNIEKN RNVQKGKRLK NNLPIVSIIG YTNAGKSTLL NALTKCDTYS DNLMFATLDT SSKRIRFPRE RDVIITDTVG FIRDLPAGLK GAFKSTLEEL DDSDLLLEVV DASSYHYKQH IQSVSEILNE LGLNEKRKIL VFNKIDKLSE DEIFEIEREY PEAVLVSAIK KHSLDPLLKK IQSVLFQEGK EVLFSGQH // ID F8EAD3_RUNSL Unreviewed; 411 AA. AC F8EAD3; DT 21-SEP-2011, integrated into UniProtKB/TrEMBL. DT 21-SEP-2011, sequence version 1. DT 07-JUN-2017, entry version 42. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Runsl_1040 {ECO:0000313|EMBL:AEI47471.1}; OS Runella slithyformis (strain ATCC 29530 / DSM 19594 / LMG 11500 / OS NCIMB 11436 / LSU 4). OC Bacteria; Bacteroidetes; Cytophagia; Cytophagales; Cytophagaceae; OC Runella. OX NCBI_TaxID=761193 {ECO:0000313|EMBL:AEI47471.1, ECO:0000313|Proteomes:UP000000493}; RN [1] {ECO:0000313|Proteomes:UP000000493} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29530 / DSM 19594 / LMG 11500 / NCIMB 11436 / LSU 4 RC {ECO:0000313|Proteomes:UP000000493}; RG US DOE Joint Genome Institute (JGI-PGF); RA Lucas S., Han J., Lapidus A., Bruce D., Goodwin L., Pitluck S., RA Peters L., Kyrpides N., Mavromatis K., Ivanova N., Ovchinnikova G., RA Zhang X., Misra M., Detter J.C., Tapia R., Han C., Land M., Hauser L., RA Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Tindall B., RA Faehrich R., Brambilla E., Klenk H.-P., Eisen J.A.; RT "The complete genome of chromosome of Runella slithyformis DSM RT 19594."; RL Submitted (JUN-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002859; AEI47471.1; -; Genomic_DNA. DR RefSeq; WP_013926790.1; NC_015703.1. DR ProteinModelPortal; F8EAD3; -. DR STRING; 761193.Runsl_1040; -. DR EnsemblBacteria; AEI47471; AEI47471; Runsl_1040. DR KEGG; rsi:Runsl_1040; -. DR PATRIC; fig|761193.3.peg.1098; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000000493; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000000493}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000000493}. FT DOMAIN 200 392 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 161 188 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 411 AA; 47226 MW; 3B16FDBFC93A1680 CRC64; MNSTAKKQET AVLVAITTQR QTAEQTQEYL HELAFLASTL GVETVRTFTQ KLEYSDNRTF VGKGRLEDIK TFVSANPVDM IIFDDELIPS QVRNLEAEFK DIKVLDRSLL ILDIFAMRAQ TAQAKTQVEL AQYQYMYPRL TRMWSHLSRQ KGGVGMRGPG EKELETDRRI VQDRIAFLKE KLEKIDKQSV TRRKERNRLV RVALVGYTNV GKSTLMRRLA KTDVFAENKL FATVDSTVRK VVLDNIPFLL TDTVGFIRKL PTKLIESFKS TLDEVREADV LLHVVDISHP SFEEQIEVVN QTLAEIGAGD KATIMVFNKI DAYHPKKEAF DEVIETEEGE VVVEQTKERV LEKLKKSYYN GSAEHVVFIS AQNNENLAEL RDKVFELIKR KHYVIYPNWV NMPLTDVDFA E // ID F8EZZ1_TRECH Unreviewed; 423 AA. AC F8EZZ1; DT 21-SEP-2011, integrated into UniProtKB/TrEMBL. DT 21-SEP-2011, sequence version 1. DT 07-JUN-2017, entry version 43. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Spica_0340 {ECO:0000313|EMBL:AEJ18504.1}; OS Treponema caldarium (strain ATCC 51460 / DSM 7334 / H1) (Spirochaeta OS caldaria). OC Bacteria; Spirochaetes; Spirochaetales; Spirochaetaceae; Treponema. OX NCBI_TaxID=744872 {ECO:0000313|EMBL:AEJ18504.1, ECO:0000313|Proteomes:UP000000503}; RN [1] {ECO:0000313|Proteomes:UP000000503} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 51460 / DSM 7334 / H1 {ECO:0000313|Proteomes:UP000000503}; RX PubMed=23961314; DOI=10.4056/sigs.3096473; RA Abt B., Goker M., Scheuner C., Han C., Lu M., Misra M., Lapidus A., RA Nolan M., Lucas S., Hammon N., Deshpande S., Cheng J.F., Tapia R., RA Goodwin L.A., Pitluck S., Liolios K., Pagani I., Ivanova N., RA Mavromatis K., Mikhailova N., Huntemann M., Pati A., Chen A., RA Palaniappan K., Land M., Hauser L., Jeffries C.D., Rohde M., RA Spring S., Gronow S., Detter J.C., Bristow J., Eisen J.A., RA Markowitz V., Hugenholtz P., Kyrpides N.C., Woyke T., Klenk H.P.; RT "Genome sequence of the thermophilic fresh-water bacterium Spirochaeta RT caldaria type strain (H1(T)), reclassification of Spirochaeta RT caldaria, Spirochaeta stenostrepta, and Spirochaeta zuelzerae in the RT genus Treponema as Treponema caldaria comb. nov., Treponema RT stenostrepta comb. nov., and Treponema zuelzerae comb. nov., and RT emendation of the genus Treponema."; RL Stand. Genomic Sci. 8:88-105(2013). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002868; AEJ18504.1; -; Genomic_DNA. DR RefSeq; WP_013967816.1; NC_015732.1. DR ProteinModelPortal; F8EZZ1; -. DR STRING; 744872.Spica_0340; -. DR EnsemblBacteria; AEJ18504; AEJ18504; Spica_0340. DR KEGG; scd:Spica_0340; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000000503; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000000503}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000000503}. FT DOMAIN 205 371 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 164 198 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 423 AA; 47696 MW; C406F463D8CEAFA1 CRC64; MQELISIEPE PQKAYLIGIR DGSMDDAEAQ SLARELAGLA ETLGVCILDQ SIVKIREKHP KYGMGLGKAE EIAERARELG VDCLIFDQDI TPSQQRNWEE LTGISAIDRQ ELIIQIFASR ARTREAELQI ELAQLKHSLP RLTHKYIDLS RQRGGRYGTK GAGETKLELD RRSILRRIHQ LEAEIKEVRQ HRSTQRKKRE KIPIPTCALV GYTNAGKSSL LNAMTNAEVL AEDKLFATLD PTTRRLEIGR GQPVLLTDTV GFIRRLPHDL VDAFHATLEE AALADILLIV LDAADPDVDR HYDTTLGVLK ELGAEQTPKI IILNKIDKVS SPERLQELEK QYSDSVSISA LNRTGLDTLA RRIDLLISGA SCRFRFPVNR HDLVAQLHRS GTVLAEHYEE TYIEVEARLG QRMLGTLQEW RID // ID F8GGU6_NITSI Unreviewed; 450 AA. AC F8GGU6; DT 21-SEP-2011, integrated into UniProtKB/TrEMBL. DT 21-SEP-2011, sequence version 1. DT 07-JUN-2017, entry version 39. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Nit79A3_1506 {ECO:0000313|EMBL:AEJ01336.1}; OS Nitrosomonas sp. (strain Is79A3). OC Bacteria; Proteobacteria; Betaproteobacteria; Nitrosomonadales; OC Nitrosomonadaceae; Nitrosomonas. OX NCBI_TaxID=261292 {ECO:0000313|EMBL:AEJ01336.1, ECO:0000313|Proteomes:UP000000501}; RN [1] {ECO:0000313|EMBL:AEJ01336.1, ECO:0000313|Proteomes:UP000000501} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Is79A3 {ECO:0000313|EMBL:AEJ01336.1, RC ECO:0000313|Proteomes:UP000000501}; RG US DOE Joint Genome Institute; RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S., RA Peters L., Ovchinnikova G., Lu M., Detter J.C., Han C., Tapia R., RA Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Bollmann A., RA Norton J., Suwa Y., Klotz M., Stein L., Laanbroek H., Arp D., RA Woyke T.; RT "Complete sequence of Nitrosomonas sp. Is79A3."; RL Submitted (JUN-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002876; AEJ01336.1; -; Genomic_DNA. DR RefSeq; WP_013965606.1; NC_015731.1. DR STRING; 261292.Nit79A3_1506; -. DR EnsemblBacteria; AEJ01336; AEJ01336; Nit79A3_1506. DR KEGG; nii:Nit79A3_1506; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR KO; K03665; -. DR OMA; VILEIFH; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000000501; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000000501}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000000501}. FT DOMAIN 224 394 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 189 216 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 450 AA; 50163 MW; 23C9ED79AD3B6A14 CRC64; MQKETQEKPK RAVVAAVQLP SVTDMEFEAS LTELRELAKT LGFEVVHTFT QKRSSFDFTA YLGTGKREEI RQFVSNEFGS AGWQETGQTA PLDADGIDVI LVDHEISPSQ ARNLEKEIAC AVMDRTMVIL EIFHRNARSP AARAQVEIAR LGYMAPRLRE MARLAGPQGR QRSGVGGRGA GESHTELDRR KIRDRIAELQ LEIVAMDAER QIQRARRLER RGIACVALVG YTNAGKSTLM RALTGSEVLV ANKLFATLDT TVRTLHPESV PRVLVSDTVG FIKNLPHGLV ASFKSTLDEA LDAALLLHVI DASDPGFERQ LEVTDEVLNE IGAQDIPRIR IFNKIDHVGD AAAQTECEVA LKTKYPACMV MSARRPDEVA KLHQAIVAFF QKDLIEDELF LPWSAQQLRG EIYTSCKVLE ERADGEGAFF RVRGEPNVVK SLREQFEQVR // ID F8GKX9_NITSI Unreviewed; 395 AA. AC F8GKX9; DT 21-SEP-2011, integrated into UniProtKB/TrEMBL. DT 21-SEP-2011, sequence version 1. DT 07-JUN-2017, entry version 40. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Nit79A3_0797 {ECO:0000313|EMBL:AEJ00672.1}; OS Nitrosomonas sp. (strain Is79A3). OC Bacteria; Proteobacteria; Betaproteobacteria; Nitrosomonadales; OC Nitrosomonadaceae; Nitrosomonas. OX NCBI_TaxID=261292 {ECO:0000313|EMBL:AEJ00672.1, ECO:0000313|Proteomes:UP000000501}; RN [1] {ECO:0000313|EMBL:AEJ00672.1, ECO:0000313|Proteomes:UP000000501} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Is79A3 {ECO:0000313|EMBL:AEJ00672.1, RC ECO:0000313|Proteomes:UP000000501}; RG US DOE Joint Genome Institute; RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S., RA Peters L., Ovchinnikova G., Lu M., Detter J.C., Han C., Tapia R., RA Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Bollmann A., RA Norton J., Suwa Y., Klotz M., Stein L., Laanbroek H., Arp D., RA Woyke T.; RT "Complete sequence of Nitrosomonas sp. Is79A3."; RL Submitted (JUN-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002876; AEJ00672.1; -; Genomic_DNA. DR RefSeq; WP_013964970.1; NC_015731.1. DR ProteinModelPortal; F8GKX9; -. DR STRING; 261292.Nit79A3_0797; -. DR EnsemblBacteria; AEJ00672; AEJ00672; Nit79A3_0797. DR KEGG; nii:Nit79A3_0797; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR KO; K03665; -. DR OMA; FNNHAHV; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000000501; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000000501}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000000501}. FT DOMAIN 202 371 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 168 195 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 395 AA; 43872 MW; E72B3B3DBD0B6C5D CRC64; MPESGMEKIK AVNPAILVGL DFGSVMHKDS LQELKQLAIS AKLQVLTIVE GKRSHPDPTT YIGSGKVNEI AQLIAQNEAS LVIFNHDLSP AQQRNLSLRL NCNVIDRTSL ILDIFSQRAK SHEGKLQVEL AQLEHLVTRL VRGWTHLERQ KGGIGLRGPG ETQLETDRRL IKKRVKLLKE KLSALQRQRN VQRRSRQRTD VLSVSIVGYT NAGKSTLFNK LTRAQSYAAD QLFATLDTTT RKLFLAESGS AVISDTVGFI RELPHTLVAA FRATLEETAQ ADILLHVIDA SNPNWNEQVE EVNKILKEIG ADTIPQVLIL NKIDLTDFAA GCKSCARDEY GRISRIRLSA KTGEGIEFVR SALTEALIEN SKKMYEQSTG IKREIGGCAT VQELF // ID F8HY26_WEIKK Unreviewed; 434 AA. AC F8HY26; DT 21-SEP-2011, integrated into UniProtKB/TrEMBL. DT 21-SEP-2011, sequence version 1. DT 07-JUN-2017, entry version 45. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=WKK_02190 {ECO:0000313|EMBL:AEJ23312.1}; OS Weissella koreensis (strain KACC 15510). OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Leuconostocaceae; OC Weissella. OX NCBI_TaxID=1045854 {ECO:0000313|EMBL:AEJ23312.1, ECO:0000313|Proteomes:UP000008930}; RN [1] {ECO:0000313|EMBL:AEJ23312.1, ECO:0000313|Proteomes:UP000008930} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=KACC 15510 {ECO:0000313|EMBL:AEJ23312.1, RC ECO:0000313|Proteomes:UP000008930}; RX PubMed=21914863; DOI=10.1128/JB.05704-11; RA Lee S.H., Jung J.Y., Lee S.H., Jeon C.O.; RT "Complete genome sequence of Weissella koreensis KACC 15510, isolated RT from Kimchi."; RL J. Bacteriol. 193:5534-5534(2011). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002899; AEJ23312.1; -; Genomic_DNA. DR ProteinModelPortal; F8HY26; -. DR STRING; 1045854.WKK_02190; -. DR EnsemblBacteria; AEJ23312; AEJ23312; WKK_02190. DR KEGG; wko:WKK_02190; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000008930; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000008930}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000008930}. FT DOMAIN 211 380 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 120 147 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 434 AA; 48886 MW; CF16E86D1A7E92AB CRC64; MRKYGDRMHE NEENPRVAVL LIGLDRNDPQ FDYQMTELAN LTEANQMEVV STLTQKLDRP VAATYFGKGK VEELKEAVAF HEVTMVVAND ELSPSQIRNL EAQTGASILD RTALILDIFA SRAKTRLAQL QIEMAQLQYQ LPRLRTSMNV RLDQQTGGGG GSFTSRGSGE TKLETNRRLI EHQISMIKKE ITEIEADDQN RRKYRDKQAI KSVALVGYTN AGKSTYMNEL VKRYGENQEK TVFQADMLFA TLETSVRKLN LPDNQTFLLS DTVGFVSKLP HNLVAAFRAT LAEAAQADVL LQVVDYSDPN YKAMMDTTTQ TLKEIGITDL PMITVYNKAD RMIDIKYPER TDDTLILSAL DSSSLDMLVD TLHQKLFADL KEYTLLIPFS DGQIVAELND DANVTSTEYL EEGTQMKVIL TPVQASRLAQ YIQE // ID F8J7H5_HYPSM Unreviewed; 470 AA. AC F8J7H5; DT 21-SEP-2011, integrated into UniProtKB/TrEMBL. DT 21-SEP-2011, sequence version 1. DT 07-JUN-2017, entry version 38. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=HYPMC_2068 {ECO:0000313|EMBL:CCB65290.1}; OS Hyphomicrobium sp. (strain MC1). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Hyphomicrobiaceae; Hyphomicrobium. OX NCBI_TaxID=717785 {ECO:0000313|EMBL:CCB65290.1, ECO:0000313|Proteomes:UP000000494}; RN [1] {ECO:0000313|Proteomes:UP000000494} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC1 {ECO:0000313|Proteomes:UP000000494}; RA Genoscope.; RT "The complete genome of Hyphomicrobium sp. MC1."; RL Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; FQ859181; CCB65290.1; -; Genomic_DNA. DR ProteinModelPortal; F8J7H5; -. DR STRING; 717785.HYPMC_2068; -. DR EnsemblBacteria; CCB65290; CCB65290; HYPMC_2068. DR KEGG; hmc:HYPMC_2068; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000000494; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000000494}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000000494}. FT DOMAIN 237 410 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 470 AA; 52026 MW; E4C33C08F4688992 CRC64; MIARPENGED ERREGEGKRK RRKASEETRA PRTRTLVVVP ALKRPLKTRG VANADAQIHS PENRLAEAVG LAKAIDLDII DSAVVPIAEP RPSTLLGSGK VEEIKDRVAE LEIGLVVVDY NITPVQQRNL EKAWNAKVLD RTGLILEIFG ERARTREGVL QVELAHLTYQ KGRLVRAWTH LERQRGGGGF LGGPGEAQIE LDRRMLQDRI DAIKKDLAEV VKTRDLHRKG RRKVPYPIVA IVGYTNAGKS TLFNKITGAG VVAMDQVFAT LDPTMREVKL PSARRIILSD TVGFISDLPT MLVAAFRATL EEVVEADLIL HVRDIAHEET EAQAQDVEKV LSELGIDTLP IESNILEVWN KIDLLSSDRR SELQHEVQRN ARPPVLVSAE TGEGMAPLLE TIDTRLGASD EIIDVIVPGS AGALLNWLHE TTDVLAREAR KDGGIELRLR IPSEKKDRVI GQLRKNGISV // ID F8JUU2_STREN Unreviewed; 504 AA. AC F8JUU2; G8X0L2; DT 21-SEP-2011, integrated into UniProtKB/TrEMBL. DT 21-SEP-2011, sequence version 1. DT 07-JUN-2017, entry version 48. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=SCATT_45560 {ECO:0000313|EMBL:AEW96927.1}; OS Streptomyces cattleya (strain ATCC 35852 / DSM 46488 / JCM 4925 / NBRC OS 14057 / NRRL 8057). OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae; OC Streptomyces. OX NCBI_TaxID=1003195 {ECO:0000313|EMBL:AEW96927.1, ECO:0000313|Proteomes:UP000007842}; RN [1] {ECO:0000313|Proteomes:UP000007842} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 35852 / DSM 46488 / JCM 4925 / NBRC 14057 / NRRL 8057 RC {ECO:0000313|Proteomes:UP000007842}; RA Ou H.-Y., Li P., Zhao C., O'Hagan D., Deng Z.; RT "Complete genome sequence of Streptomyces cattleya strain DSM 46488."; RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP003219; AEW96927.1; -; Genomic_DNA. DR RefSeq; WP_014145272.1; NC_017586.1. DR STRING; 1003195.SCAT_4568; -. DR EnsemblBacteria; AEW96927; AEW96927; SCATT_45560. DR KEGG; sct:SCAT_4568; -. DR KEGG; scy:SCATT_45560; -. DR PATRIC; fig|1003195.11.peg.6001; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR KO; K03665; -. DR OMA; HPATYIG; -. DR Proteomes; UP000007842; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000007842}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000007842}. FT DOMAIN 282 447 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 241 275 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 504 AA; 54541 MW; 5A6DE1C02101FA23 CRC64; MTNSTSSSSA ARSAAADRQR LPESLRATAL MEEDVAWSLD VDGERDGDQF DRSERASLRR VAGLSTELQD VTEVEYRQLR LERVVLVGVW TDGTVQDAEN SLAELAALAE TAGALVLDGV IQRRDKPDPA TYIGSGKAQE LRDIVLESGA DTVVCDGELS PGQLIHLEDV VKVKVVDRTA LILDIFAQHA KSREGKAQVA LAQMQYMLPR LRGWGQSLSR QMGGGGSGSA GGGMATRGPG ETKIETDRRR IREKMAKLRR EIAEMKTSRD LKRQERRRHQ VPSVAIAGYT NAGKSSLLNR LTGAGVLVEN ALFATLDPTV RRAETPSGRL YTLADTVGFV RHLPHHLVEA FRSTMEEVAD ADLVLHVVDG AHPVPEEQLA AVREVLRDVG AADVPEIVVI NKADAADPLV VQRLLTHEKH AIAVSARSGE GVAELLALLD AELPRPRVEI EALVPYTHGA LVSRVHVGGE VISEEHTAEG TLLKARVHDQ LAAELGPFAL AVQR // ID F8KZT5_PARAV Unreviewed; 436 AA. AC F8KZT5; DT 21-SEP-2011, integrated into UniProtKB/TrEMBL. DT 21-SEP-2011, sequence version 1. DT 07-JUN-2017, entry version 47. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:CCB86444.1}; GN OrderedLocusNames=PUV_14940 {ECO:0000313|EMBL:CCB86444.1}; OS Parachlamydia acanthamoebae (strain UV7). OC Bacteria; Chlamydiae; Parachlamydiales; Parachlamydiaceae; OC Parachlamydia. OX NCBI_TaxID=765952 {ECO:0000313|EMBL:CCB86444.1, ECO:0000313|Proteomes:UP000000495}; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=UV7; RA Collingro A., Tischler P., Weinmaier T., Penz T., Heinz E., RA Brunham R.C., Read T.D., Bavoil P.M., Sachse K., Kahane S., RA Friedman M.G., Rattei T., Myers G.S.A., Horn M.; RT "Unity in variety -- the pan-genome of the Chlamydiae."; RL Mol. Biol. Evol. 0:0-0(2011). RN [2] {ECO:0000313|EMBL:CCB86444.1, ECO:0000313|Proteomes:UP000000495} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=UV7 {ECO:0000313|Proteomes:UP000000495}; RX PubMed=21690563; DOI=10.1093/molbev/msr161; RA Collingro A., Tischler P., Weinmaier T., Penz T., Heinz E., RA Brunham R.C., Read T.D., Bavoil P.M., Sachse K., Kahane S., RA Friedman M.G., Rattei T., Myers G.S., Horn M.; RT "Unity in variety--the pan-genome of the chlamydiae."; RL Mol. Biol. Evol. 28:3253-3270(2011). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; FR872580; CCB86444.1; -; Genomic_DNA. DR RefSeq; WP_013924981.1; NC_015702.1. DR STRING; 765952.PUV_14940; -. DR EnsemblBacteria; CCB86444; CCB86444; PUV_14940. DR KEGG; puv:PUV_14940; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000000495; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000000495}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000000495}. FT DOMAIN 216 382 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 175 209 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 436 AA; 49291 MW; DC0431F37F3E5F10 CRC64; MQKGTKISSE EENAQEKRKA LLVSAFNGND QRAICEEHLD ELELLAETYG VEIVAKVPCL IRKVDAATFV TQGKLEELIT LSKECAADLI IFDDEISPSQ QRNLEKAFQL TVMDRTEVIL EVFAQRAKTK EARLQIEYAR VKYQAPRLKR LWSHLSRQHG SGGAGGGAYL KGEGEKQIEI DRRLIKKRLE QLQSEIQEVK EHREIQRVAR TRSAIPVFAL VGYTNAGKST LLNALTDADV FVEDKLFATL DTTTRKFPLS TGQEVLVTDT VGFIRKLPHL LVAAFKSTLE EAIQADILLH VIDATHPMAL EQARTTIQVL KELGVGDKPI ITVLNKIDQA EQNELTTRLR LEYPRTVPIS ALHRRGFEEL EEMMLRELSQ QRKTLNLRIP QSEYALVSEI RRSGNVISQD YEENDVLIEV DLPVALANKL KNYVIS // ID F8L771_SIMNZ Unreviewed; 435 AA. AC F8L771; DT 21-SEP-2011, integrated into UniProtKB/TrEMBL. DT 21-SEP-2011, sequence version 1. DT 07-JUN-2017, entry version 43. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:CCB88586.1}; GN OrderedLocusNames=SNE_A07090 {ECO:0000313|EMBL:CCB88586.1}; OS Simkania negevensis (strain ATCC VR-1471 / Z). OC Bacteria; Chlamydiae; Parachlamydiales; Simkaniaceae; Simkania. OX NCBI_TaxID=331113 {ECO:0000313|EMBL:CCB88586.1, ECO:0000313|Proteomes:UP000000496}; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=Z; RA Collingro A., Tischler P., Weinmaier T., Penz T., Heinz E., RA Brunham R.C., Read T.D., Bavoil P.M., Sachse K., Kahane S., RA Friedman M.G., Rattei T., Myers G.S.A., Horn M.; RT "Unity in variety -- the pan-genome of the Chlamydiae."; RL Mol. Biol. Evol. 0:0-0(2011). RN [2] {ECO:0000313|EMBL:CCB88586.1, ECO:0000313|Proteomes:UP000000496} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC VR-1471 / Z {ECO:0000313|Proteomes:UP000000496}; RX PubMed=21690563; DOI=10.1093/molbev/msr161; RA Collingro A., Tischler P., Weinmaier T., Penz T., Heinz E., RA Brunham R.C., Read T.D., Bavoil P.M., Sachse K., Kahane S., RA Friedman M.G., Rattei T., Myers G.S., Horn M.; RT "Unity in variety--the pan-genome of the chlamydiae."; RL Mol. Biol. Evol. 28:3253-3270(2011). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; FR872582; CCB88586.1; -; Genomic_DNA. DR RefSeq; WP_013943053.1; NC_015713.1. DR ProteinModelPortal; F8L771; -. DR STRING; 331113.SNE_A07090; -. DR EnsemblBacteria; CCB88586; CCB88586; SNE_A07090. DR KEGG; sng:SNE_A07090; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000000496; Chromosome gsn.131. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000000496}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000000496}. FT DOMAIN 213 379 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 179 206 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 435 AA; 50067 MW; 663D50AE66C6D6CC CRC64; MVDEKRLYED VRYEISDLNT ALLIGCYTKS SDLMLCKEHI DELESLADTY GFEVVSKNPC PLRKIEASTY IGKGKIEELQ AAADESKADV VIFDDEISPN QQRNLEKIFK RPVIDRTELI LEIFSQRAQT REAKLQVELA KSHYQLPRLK RLWTHLSRQV ASGKGFLKGA GERQIELDRR MVRDRISRLK NEIEEVRHQR DVQRHARIRS GVPTFAIIGY TNVGKSTLLH ALTQAEVLIE DKLFATLDTT TRKFTLPNHQ EILLIDTVGF IRKIPHTLVA AFKSTLEEAM YTDILLHLVD INHPLAEEHA ESTYEVLKEL GAEGKPMITV LNKIDAIENK GIIGRFKLKY PRVVGISALK ELGFDDLMRT MMDTIKDLRT VLKLRIPQKE YALVSRLLNE GRLIHQEYEE NDILIEIEIP KHLLHKVEPY IIVES // ID F8N5M0_9BACT Unreviewed; 419 AA. AC F8N5M0; DT 21-SEP-2011, integrated into UniProtKB/TrEMBL. DT 21-SEP-2011, sequence version 1. DT 07-JUN-2017, entry version 38. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=Premu_2832 {ECO:0000313|EMBL:EGN58178.1}; OS Prevotella multisaccharivorax DSM 17128. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Prevotellaceae; OC Prevotella. OX NCBI_TaxID=688246 {ECO:0000313|EMBL:EGN58178.1, ECO:0000313|Proteomes:UP000002772}; RN [1] {ECO:0000313|Proteomes:UP000002772} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 17128 {ECO:0000313|Proteomes:UP000002772}; RX PubMed=22180809; DOI=10.4056/sigs.2164949; RA Pati A., Gronow S., Lu M., Lapidus A., Nolan M., Lucas S., Hammon N., RA Deshpande S., Cheng J.F., Tapia R., Han C., Goodwin L., Pitluck S., RA Liolios K., Pagani I., Mavromatis K., Mikhailova N., Huntemann M., RA Chen A., Palaniappan K., Land M., Hauser L., Detter J.C., RA Brambilla E.M., Rohde M., Goker M., Woyke T., Bristow J., Eisen J.A., RA Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P., Ivanova N.; RT "Non-contiguous finished genome sequence of the opportunistic oral RT pathogen Prevotella multisaccharivorax type strain (PPPA20)."; RL Stand. Genomic Sci. 5:41-49(2011). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GL945017; EGN58178.1; -; Genomic_DNA. DR RefSeq; WP_007576212.1; NZ_GL945017.1. DR ProteinModelPortal; F8N5M0; -. DR STRING; 688246.Premu_2832; -. DR EnsemblBacteria; EGN58178; EGN58178; Premu_2832. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000002772; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000002772}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000002772}. FT DOMAIN 219 403 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 419 AA; 48100 MW; E9E1C6A9B9399B54 CRC64; MKEFEYSEAE ANKAETAILV GLITPQQDEA KTKEYLDELE FLADTAGAVT VKRFTQRTGG PSQTSYVGKG KLEEIHQYIK DEEDNEREIG MVIFDDELSA KQLRNIENEL HVKILDRTSL ILDIFAMRAQ TANAKTQVEL AQYRYMLPRL QRMWTHLERQ GGGSGSGGGK GSVGLRGPGE TQLEMDRRII LNRMSLLKQR LTEIDKQKST QRKNRGRLIR AALVGYTNVG KSTLMNLLAK SEVFAENKLF ATLDTTVRKV VIRNLPFLLA DTVGFIRKLP TDLVESFKST LDEVREADLL LHVVDISHPD FEEQIQVVNN TLKDLGCSDK PTILIFNKID NYHWTEKDPE DLTPATRENI TLDELRQTWM ARLGDDCIFI SARRKENIDE LRDVLYRKVR ELHVQKYPYN DFLYPEEDD // ID F8WX22_9BACT Unreviewed; 406 AA. AC F8WX22; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 30-AUG-2017, entry version 36. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=HMPREF9456_00053 {ECO:0000313|EMBL:EGK06179.1}; OS Dysgonomonas mossii DSM 22836. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; OC Dysgonamonadaceae; Dysgonomonas. OX NCBI_TaxID=742767 {ECO:0000313|EMBL:EGK06179.1, ECO:0000313|Proteomes:UP000006420}; RN [1] {ECO:0000313|EMBL:EGK06179.1, ECO:0000313|Proteomes:UP000006420} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 22836 {ECO:0000313|EMBL:EGK06179.1, RC ECO:0000313|Proteomes:UP000006420}; RG The Broad Institute Genome Sequencing Platform; RA Earl A., Ward D., Feldgarden M., Gevers D., Pudlo N., Martens E., RA Allen-Vercoe E., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., RA Haas B., Abouelleil A., Alvarado L., Arachchi H.M., Berlin A., RA Brown A., Chapman S.B., Chen Z., Dunbar C., Freedman E., Gearin G., RA Gellesch M., Goldberg J., Griggs A., Gujja S., Heiman D., Howarth C., RA Larson L., Lui A., MacDonald P.J.P., Mehta T., Montmayeur A., RA Murphy C., Neiman D., Pearson M., Priest M., Roberts A., Saif S., RA Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., Yandava C., RA Wortman J., Nusbaum C., Birren B.; RT "The Genome Sequence of Dysgonomonas mossii DSM 22836."; RL Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EGK06179.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADLW01000001; EGK06179.1; -; Genomic_DNA. DR RefSeq; WP_006841427.1; NZ_GL892004.1. DR STRING; 742767.HMPREF9456_00053; -. DR EnsemblBacteria; EGK06179; EGK06179; HMPREF9456_00053. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000006420; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000006420}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000006420}. FT DOMAIN 203 387 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 406 AA; 47189 MW; 859D2312CEFF0EA9 CRC64; MKDFIISESK NEQAVLVGLI TQYQTEEQVK EYLDELAFLA ETASIVPVKK FTQKLEKANP VTFVGTGKLQ EIKQYMEDNE IGLVIFDDEL SPKQIRNIEK ELQVKILDRT SLILDIFAMR AQTAYAKTQV ELAQYQYLLP RLTRLWTHLD RQRGGGVMMR GVGETQLETD RRIILTKIAF LKEELKGIDK QMASQRKNRG KMVRAALVGY TNVGKSTLMT LLSKSEVFAE NKLFATLDTT VRKVIIDNLP FLLSDTVGFI RKLPTHLVES FKSTLDEVRE ADLLLHVVDI SHPNFEEQIE VVNKTLLEID KEEKPTILIF NKVDSFSYKP KDEDDLTPKT KENISLEELK NSWMNKMHND CIFISATEKL NFDELKQKLY DRIKEIHIER YPYNDFLFQK YDEEME // ID F9D4C9_PREDD Unreviewed; 415 AA. AC F9D4C9; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 07-JUN-2017, entry version 50. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:EGQ14172.1}; GN OrderedLocusNames=Prede_1533 {ECO:0000313|EMBL:AGB28843.1}; GN ORFNames=HMPREF9136_1707 {ECO:0000313|EMBL:EGQ14172.1}; OS Prevotella dentalis (strain ATCC 49559 / DSM 3688 / JCM 13448 / NCTC OS 12043 / ES 2772) (Mitsuokella dentalis). OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Prevotellaceae; OC Prevotella. OX NCBI_TaxID=908937 {ECO:0000313|EMBL:EGQ14172.1, ECO:0000313|Proteomes:UP000007820}; RN [1] {ECO:0000313|EMBL:EGQ14172.1, ECO:0000313|Proteomes:UP000007820} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 3688 {ECO:0000313|EMBL:EGQ14172.1, RC ECO:0000313|Proteomes:UP000007820}; RA Muzny D., Qin X., Deng J., Jiang H., Liu Y., Qu J., Song X.-Z., RA Zhang L., Thornton R., Coyle M., Francisco L., Jackson L., Javaid M., RA Korchina V., Kovar C., Mata R., Mathew T., Ngo R., Nguyen L., RA Nguyen N., Okwuonu G., Ongeri F., Pham C., Simmons D., RA Wilczek-Boney K., Hale W., Jakkamsetti A., Pham P., Ruth R., RA San Lucas F., Warren J., Zhang J., Zhao Z., Zhou C., Zhu D., Lee S., RA Bess C., Blankenburg K., Forbes L., Fu Q., Gubbala S., Hirani K., RA Jayaseelan J.C., Lara F., Munidasa M., Palculict T., Patil S., RA Pu L.-L., Saada N., Tang L., Weissenberger G., Zhu Y., Hemphill L., RA Shang Y., Youmans B., Ayvaz T., Ross M., Santibanez J., Aqrawi P., RA Gross S., Joshi V., Fowler G., Nazareth L., Reid J., Worley K., RA Petrosino J., Highlander S., Gibbs R.; RL Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:AGB28843.1, ECO:0000313|Proteomes:UP000010862} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 49559 / DSM 3688 / JCM 13448 / NCTC 12043 / ES 2772 RC {ECO:0000313|Proteomes:UP000010862}, and RC DSM 3688 {ECO:0000313|EMBL:AGB28843.1}; RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., RA Tice H., Bruce D., Goodwin L., Pitluck S., Peters L., Mikhailova N., RA Chertkov O., Kyrpides N., Mavromatis K., Ivanova N., Brettin T., RA Detter J.C., Han C., Larimer F., Land M., Hauser L., Markowitz V., RA Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Gronow S., Wellnitz S., RA Brambilla E., Klenk H.-P., Eisen J.A.; RT "Complete sequence of chromosome 2 of Prevotella dentalis DSM 3688."; RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP003369; AGB28843.1; -; Genomic_DNA. DR EMBL; AFPW01000023; EGQ14172.1; -; Genomic_DNA. DR RefSeq; WP_005846154.1; NZ_GL982489.1. DR STRING; 908937.HMPREF9136_1707; -. DR EnsemblBacteria; AGB28843; AGB28843; Prede_1533. DR EnsemblBacteria; EGQ14172; EGQ14172; HMPREF9136_1707. DR KEGG; pdt:Prede_1533; -. DR PATRIC; fig|908937.9.peg.1611; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR KO; K03665; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000007820; Unassembled WGS sequence. DR Proteomes; UP000010862; Chromosome 2. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000010862}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000010862}. FT DOMAIN 216 400 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 415 AA; 47713 MW; B614CD61AC7EABBC CRC64; MKEFVISEVK AETAVLVGLI TPGQDEAKTK EYLDELEFLA DTAGAVTVRR FTQRVGGPSA VTYVGKGKLE EIRQYIKDEE ENEREVGMVI FDDELSAKQM RNIENALQVK ILDRTSLILD IFAMRAQTAN AKTQVELAQY RYMLPRLQRL WTHLERQGGG SGSGGGKGSV GLRGPGETQL EMDRRIILQR ITLLKQRLVE IDRQKTTQRK NRGRLIRVAL VGYTNVGKST IMNLMAKSEV FAEDKLFATL DTTVRKVVVE NLPFLLADTV GFIRKLPTDL VDSFKSTLDE VREADLLLHV VDISHPDFEE QIEVVNQTLK ELDCAEKPTM MVFNKTDKYR WVDKEPDDLT PETRENVTLD ELRRTWMARL EDNCLFISAK QKDNVDEFRN TLYRRVRELH VQKYPYNDFL YPVED // ID F9DTX2_9BACL Unreviewed; 422 AA. AC F9DTX2; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 07-JUN-2017, entry version 37. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:EGQ25156.1}; GN ORFNames=HMPREF9372_2253 {ECO:0000313|EMBL:EGQ25156.1}; OS Sporosarcina newyorkensis 2681. OC Bacteria; Firmicutes; Bacilli; Bacillales; Planococcaceae; OC Sporosarcina. OX NCBI_TaxID=1027292 {ECO:0000313|EMBL:EGQ25156.1, ECO:0000313|Proteomes:UP000005316}; RN [1] {ECO:0000313|EMBL:EGQ25156.1, ECO:0000313|Proteomes:UP000005316} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=2681 {ECO:0000313|EMBL:EGQ25156.1, RC ECO:0000313|Proteomes:UP000005316}; RA Muzny D., Qin X., Deng J., Jiang H., Liu Y., Qu J., Song X.-Z., RA Zhang L., Thornton R., Coyle M., Francisco L., Jackson L., Javaid M., RA Korchina V., Kovar C., Mata R., Mathew T., Ngo R., Nguyen L., RA Nguyen N., Okwuonu G., Ongeri F., Pham C., Simmons D., RA Wilczek-Boney K., Hale W., Jakkamsetti A., Pham P., Ruth R., RA San Lucas F., Warren J., Zhang J., Zhao Z., Zhou C., Zhu D., Lee S., RA Bess C., Blankenburg K., Forbes L., Fu Q., Gubbala S., Hirani K., RA Jayaseelan J.C., Lara F., Munidasa M., Palculict T., Patil S., RA Pu L.-L., Saada N., Tang L., Weissenberger G., Zhu Y., Hemphill L., RA Shang Y., Youmans B., Ayvaz T., Ross M., Santibanez J., Aqrawi P., RA Gross S., Joshi V., Fowler G., Nazareth L., Reid J., Worley K., RA Petrosino J., Highlander S., Gibbs R.; RL Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EGQ25156.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFPZ01000070; EGQ25156.1; -; Genomic_DNA. DR RefSeq; WP_009498927.1; NZ_GL982999.1. DR ProteinModelPortal; F9DTX2; -. DR STRING; 1027292.HMPREF9372_2253; -. DR EnsemblBacteria; EGQ25156; EGQ25156; HMPREF9372_2253. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000005316; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000005316}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000005316}. FT DOMAIN 200 368 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 159 193 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 422 AA; 47888 MW; BBC4920D8D3669C2 CRC64; MDVLVEEAVI VGVHEQKDLH FEYAMEELRN LAEAIDVKVI GEVTQNLERR NPSHYLGKGK IDEIRQVYEE TGANLLIFND ELSPSQLRNL EKELECKIID RTMLILDIFA RRARNREAQM QVELAQLQYT LPRLVGLRAS LSRQGGGTGG GLQNKGAGET KLELDRRKIE DQIAKLRREL EHVKDQRETQ RKQRVRSGIP VVSIVGYTNA GKSTLMNRLL QYTDADQSKQ VSEKNMLFAT LETAVRKIKL PDKKEFILTD TVGFVSKLPH HLVQAFRSTL EEAKNADLLL HVVDVSDEEH GHMMDVTNET LEDIGVESIP TVNVYNKADL AGITYPRTQE QSIWMSAGKN EGIPELLKLI EQNLFRQYIT CKLLIPYDRG EIVSHLNETA AIKETAYEEE GTLITVEIPE SECERLAEFV VG // ID F9EHN8_9ACTO Unreviewed; 533 AA. AC F9EHN8; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 07-JUN-2017, entry version 34. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:EGQ73409.1}; GN ORFNames=HMPREF9062_1960 {ECO:0000313|EMBL:EGQ73409.1}; OS Actinomyces sp. oral taxon 448 str. F0400. OC Bacteria; Actinobacteria; Actinomycetales; Actinomycetaceae; OC Actinomyces. OX NCBI_TaxID=888056 {ECO:0000313|EMBL:EGQ73409.1, ECO:0000313|Proteomes:UP000005351}; RN [1] {ECO:0000313|EMBL:EGQ73409.1, ECO:0000313|Proteomes:UP000005351} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=F0400 {ECO:0000313|EMBL:EGQ73409.1, RC ECO:0000313|Proteomes:UP000005351}; RA Muzny D., Qin X., Deng J., Jiang H., Liu Y., Qu J., Song X.-Z., RA Zhang L., Thornton R., Coyle M., Francisco L., Jackson L., Javaid M., RA Korchina V., Kovar C., Mata R., Mathew T., Ngo R., Nguyen L., RA Nguyen N., Okwuonu G., Ongeri F., Pham C., Simmons D., RA Wilczek-Boney K., Hale W., Jakkamsetti A., Pham P., Ruth R., RA San Lucas F., Warren J., Zhang J., Zhao Z., Zhou C., Zhu D., Lee S., RA Bess C., Blankenburg K., Forbes L., Fu Q., Gubbala S., Hirani K., RA Jayaseelan J.C., Lara F., Munidasa M., Palculict T., Patil S., RA Pu L.-L., Saada N., Tang L., Weissenberger G., Zhu Y., Hemphill L., RA Shang Y., Youmans B., Ayvaz T., Ross M., Santibanez J., Aqrawi P., RA Gross S., Joshi V., Fowler G., Nazareth L., Reid J., Worley K., RA Petrosino J., Highlander S., Gibbs R.; RL Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EGQ73409.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFQC01000051; EGQ73409.1; -; Genomic_DNA. DR STRING; 888056.HMPREF9062_1960; -. DR EnsemblBacteria; EGQ73409; EGQ73409; HMPREF9062_1960. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000005351; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 2. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000005351}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000005351}. FT DOMAIN 307 473 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 533 AA; 56259 MW; F6E042C40C9BBAC9 CRC64; MTASNDPALQ SDDDVEPARP QSLTDPQVRA PSPEEIVDRI LSRGGTALAS TAGEHASREA LDDGALEREA RAGTRRVATL STELQDVSEV EYRQVRLEKV VLVGLDLPRA AARVPAFGTA DAQDAETSLA ELAALAETAG SQVLDALIQK RDHPDPATYL GSGKAGELAE TVAAAGADTV IVDGELAPSQ RRSLEDVVGV KVVDRTAVIL DIFAQHAKSR EGKAQVELAQ LEYLLPRLRG WGESMSRQAG GRVAGGAGIG SRGPGETKIE LDRRRIRARM AKLRRQIRSM TPSREVKRGS RRRGPIPSVA IAGYTNAGKS SLMNALTGAG LLVQDALFAT LDPTVRRAET SDGRVYTLTD TVGFMRDLPH ELIEAFRSTL EEVGGADLVL HVVDAAHPDP VGQVTAVRAV LADIPGGLDV PELVVLNKVD LADAVTLAAL RTRLPGAIGV CARTGGGLET LRRRIEEMLP RPEADVDLVV PYARGDLVSR VHADGEIDAI DYLEAGTRVV ARVAAPLAAE LRAAAVSAAS ASG // ID F9EPJ3_FUSNU Unreviewed; 392 AA. AC F9EPJ3; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 07-JUN-2017, entry version 31. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:EGQ79124.1}; GN ORFNames=HMPREF9094_1848 {ECO:0000313|EMBL:EGQ79124.1}; OS Fusobacterium nucleatum subsp. animalis ATCC 51191. OC Bacteria; Fusobacteria; Fusobacteriales; Fusobacteriaceae; OC Fusobacterium. OX NCBI_TaxID=997347 {ECO:0000313|EMBL:EGQ79124.1, ECO:0000313|Proteomes:UP000005392}; RN [1] {ECO:0000313|EMBL:EGQ79124.1, ECO:0000313|Proteomes:UP000005392} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51191 {ECO:0000313|EMBL:EGQ79124.1, RC ECO:0000313|Proteomes:UP000005392}; RA Muzny D., Qin X., Deng J., Jiang H., Liu Y., Qu J., Song X.-Z., RA Zhang L., Thornton R., Coyle M., Francisco L., Jackson L., Javaid M., RA Korchina V., Kovar C., Mata R., Mathew T., Ngo R., Nguyen L., RA Nguyen N., Okwuonu G., Ongeri F., Pham C., Simmons D., RA Wilczek-Boney K., Hale W., Jakkamsetti A., Pham P., Ruth R., RA San Lucas F., Warren J., Zhang J., Zhao Z., Zhou C., Zhu D., Lee S., RA Bess C., Blankenburg K., Forbes L., Fu Q., Gubbala S., Hirani K., RA Jayaseelan J.C., Lara F., Munidasa M., Palculict T., Patil S., RA Pu L.-L., Saada N., Tang L., Weissenberger G., Zhu Y., Hemphill L., RA Shang Y., Youmans B., Ayvaz T., Ross M., Santibanez J., Aqrawi P., RA Gross S., Joshi V., Fowler G., Nazareth L., Reid J., Worley K., RA Petrosino J., Highlander S., Gibbs R.; RL Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EGQ79124.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFQD01000316; EGQ79124.1; -; Genomic_DNA. DR EnsemblBacteria; EGQ79124; EGQ79124; HMPREF9094_1848. DR PATRIC; fig|997347.4.peg.1714; -. DR Proteomes; UP000005392; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000005392}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000005392}. FT DOMAIN 153 338 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 293 320 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 392 AA; 44947 MW; DD6DB13E54A604B0 CRC64; MQKRSKPDPV FLIGSGKIQE LALVRQVRKA NLLIFDEELS GLQLKMIEEV TGCKVIDRTT LILEIFARRA KTREAKLQVE LAQLKYRSNR LIGFGVTMSR LGGGVGTKGP GEKKLEIDRR VIKKTISYLN NELENIKKVR NTQRSKREDS GIPRVSLVGY TNVGKSTLRN VLVDMYQNDK TLKKEEVLSQ DMLFATLDTT TRTIELKDKR IVSLTDTVGF IQKLPHDLVE SFKSTLEEVI FSDLIIHVAD ISSKNVIEQI EAVEKVLEEL NCLNKTKILL LNKIDNATKN NSYMLIEQKI DEIKEKYSNY QTLIISAKNR FNIDELMDLI KKNLTVKTYD CKLLIPYSNT DIAARVHRNT IVRSESFVDE GIILEVVMNE KEYNKFKDFI LN // ID F9EUZ3_9NEIS Unreviewed; 396 AA. AC F9EUZ3; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 07-JUN-2017, entry version 31. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:EGQ77548.1}; GN ORFNames=HMPREF9418_0970 {ECO:0000313|EMBL:EGQ77548.1}; OS Neisseria macacae ATCC 33926. OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=997348 {ECO:0000313|EMBL:EGQ77548.1, ECO:0000313|Proteomes:UP000004982}; RN [1] {ECO:0000313|EMBL:EGQ77548.1, ECO:0000313|Proteomes:UP000004982} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33926 {ECO:0000313|EMBL:EGQ77548.1, RC ECO:0000313|Proteomes:UP000004982}; RA Muzny D., Qin X., Deng J., Jiang H., Liu Y., Qu J., Song X.-Z., RA Zhang L., Thornton R., Coyle M., Francisco L., Jackson L., Javaid M., RA Korchina V., Kovar C., Mata R., Mathew T., Ngo R., Nguyen L., RA Nguyen N., Okwuonu G., Ongeri F., Pham C., Simmons D., RA Wilczek-Boney K., Hale W., Jakkamsetti A., Pham P., Ruth R., RA San Lucas F., Warren J., Zhang J., Zhao Z., Zhou C., Zhu D., Lee S., RA Bess C., Blankenburg K., Forbes L., Fu Q., Gubbala S., Hirani K., RA Jayaseelan J.C., Lara F., Munidasa M., Palculict T., Patil S., RA Pu L.-L., Saada N., Tang L., Weissenberger G., Zhu Y., Hemphill L., RA Shang Y., Youmans B., Ayvaz T., Ross M., Santibanez J., Aqrawi P., RA Gross S., Joshi V., Fowler G., Nazareth L., Reid J., Worley K., RA Petrosino J., Highlander S., Gibbs R.; RL Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EGQ77548.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFQE01000044; EGQ77548.1; -; Genomic_DNA. DR RefSeq; WP_003777332.1; NZ_GL985618.1. DR ProteinModelPortal; F9EUZ3; -. DR EnsemblBacteria; EGQ77548; EGQ77548; HMPREF9418_0970. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000004982; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000004982}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}. FT DOMAIN 216 385 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 396 AA; 43305 MW; A6062F4EB343DE4B CRC64; MSKRNIFPVD KSLEQPERVM LVGVMLSADY SGANEVRERT FQTTLDEAAE LVAAAGGELV LRETAKRDKA HTAYFVGTGK AEELAAAVKL HDIGLAVFNH ELTPTQERNL EKILQCRVLD RVGLILAIFA KRAQSQEGKL QVELAQLNHL SGRLVRGYGH LQSQKGGIGL KGPGETQLET DRRLIGQKIT ALKKQLVQVK KQRATRRKSR MEGRLKTFAI VGYTNAGKSS LFNRLTKADV LAKDQLFATL DTTARRLFLS QEAGVILTDT VGFVRDLPHK LVSAFSATLE ETALADVLLH VVDASNPDFE RQMDDVNAVL EEIGADEVPQ LVVYNKIDLL PEGVRDAGVL RDNSGRAVGV NISVTKSLGL DALREAMIER ALENGGKGSS ENCEAE // ID F9HFV7_9STRE Unreviewed; 412 AA. AC F9HFV7; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 07-JUN-2017, entry version 39. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:EGP66355.1}; GN ORFNames=HMPREF9182_0264 {ECO:0000313|EMBL:EGP66355.1}; OS Streptococcus sp. oral taxon 056 str. F0418. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=904294 {ECO:0000313|EMBL:EGP66355.1, ECO:0000313|Proteomes:UP000004514}; RN [1] {ECO:0000313|Proteomes:UP000004514} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=F0418 {ECO:0000313|Proteomes:UP000004514}; RA Durkin A.S., Kim M., Radune D., Hostetler J., Torralba M., Gillis M., RA Methe B., Sutton G., Nelson K.E.; RT "Complete sequence of Bifidobacterium breves ACS-071-V-Sch8b."; RL Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EGP66355.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFQU01000001; EGP66355.1; -; Genomic_DNA. DR RefSeq; WP_009443796.1; NZ_AFQU01000001.1. DR STRING; 904294.HMPREF9182_0264; -. DR EnsemblBacteria; EGP66355; EGP66355; HMPREF9182_0264. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR Proteomes; UP000004514; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000004514}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000004514}. FT DOMAIN 199 359 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 158 192 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 412 AA; 46709 MW; 954DB63A0453C623 CRC64; MIETEKKIER VFLVGVELAD TENFDLSMEE LQSLAKTAGA EVIGSYSQKR EKYDSKTFVG SGKLEEIRQM VDAEEISTVI VNNRLTPRQN VNLEESLGVK VIDRMQLILD IFAMRARSHE GKLQVHLAQL KYLLPRLVGQ GIMLSRQAGG IGSRGPGESQ LELNRRSVRN QIHDIERQLK EVEKNRATVR EKRLESSIFK IGLIGYTNAG KSTIMNCLTS KSQYEADELF ATLDATTKNI NLSGHLNVTL TDTVGFIQDL PTELVSSFKS TLEESRNVDL LVHVIDASDP HHEEHEKTVL DIMKELDMLD IPRLTLYNKA DKAEDFTPTL TPYSLISAKA DNSRALLQQV LLERMKELFL PFTIKVAPAK AYKIHDLEKV AIMGNREYID DVETISGWIA EKNKWKLEEF YD // ID F9MX01_9FIRM Unreviewed; 408 AA. AC F9MX01; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 07-JUN-2017, entry version 35. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:EGS29797.1}; GN ORFNames=HMPREF9130_1557 {ECO:0000313|EMBL:EGS29797.1}; OS Peptoniphilus sp. oral taxon 375 str. F0436. OC Bacteria; Firmicutes; Tissierellia; Tissierellales; Peptoniphilaceae; OC Peptoniphilus. OX NCBI_TaxID=879308 {ECO:0000313|EMBL:EGS29797.1, ECO:0000313|Proteomes:UP000003680}; RN [1] {ECO:0000313|EMBL:EGS29797.1, ECO:0000313|Proteomes:UP000003680} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=F0436 {ECO:0000313|EMBL:EGS29797.1, RC ECO:0000313|Proteomes:UP000003680}; RA Harkins D.M., Madupu R., Durkin A.S., Torralba M., Methe B., RA Sutton G.G., Nelson K.E.; RL Submitted (JUN-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EGS29797.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFUH01000001; EGS29797.1; -; Genomic_DNA. DR RefSeq; WP_009430201.1; NZ_AFUH01000001.1. DR STRING; 879308.HMPREF9130_1557; -. DR EnsemblBacteria; EGS29797; EGS29797; HMPREF9130_1557. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000003680; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0051087; F:chaperone binding; IEA:InterPro. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR Gene3D; 1.20.58.120; -; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR003103; BAG_domain. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000003680}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000003680}. FT DOMAIN 188 355 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 154 181 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 408 AA; 46219 MW; 306D3E18D8DC76F2 CRC64; MDQKEGVILL TTNLSPSSPE ETRALIQADN GRVLAELSQN LKEPGPYYIG KGKLEELKAL IQSLDPDLVL VNDDLKGFQL RNLERELDIQ VMDRTHLILD IFASRARTKQ AKLQVLLAQL TYGKSRLIGS YSLSKTGGGI GTRGPGEQKL ELDRRKIDRQ IHQIQSRLDE IKSQRQEQLK QRKKSQVPLV SFVGYTNAGK STMMNALLGQ ESDKQVFVKD MVFATLDTSL RSVKLLDKRP VILADTVGFI SDLPETLMEA FQSTLDELKN SSALVHVLDG QSESLQKDYM ETLKILKDLD LMDIPRLTVF NKIDRPDMRP QIIQPRPDKL LFYSALNDPV EKLEEALVDL LGDQWVQGEI FFSFQDQGLL NQALKDYPQA QVSYNEKGSL LRGEFLKEDM ERWTGGKQ // ID F9PJC5_9ACTO Unreviewed; 550 AA. AC F9PJC5; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 07-JUN-2017, entry version 36. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:EGV14384.1}; GN ORFNames=HMPREF9058_2041 {ECO:0000313|EMBL:EGV14384.1}; OS Actinomyces sp. oral taxon 175 str. F0384. OC Bacteria; Actinobacteria; Actinomycetales; Actinomycetaceae; OC Actinomyces. OX NCBI_TaxID=944560 {ECO:0000313|EMBL:EGV14384.1, ECO:0000313|Proteomes:UP000004281}; RN [1] {ECO:0000313|EMBL:EGV14384.1, ECO:0000313|Proteomes:UP000004281} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=F0384 {ECO:0000313|EMBL:EGV14384.1, RC ECO:0000313|Proteomes:UP000004281}; RA Harkins D.M., Madupu R., Durkin A.S., Torralba M., Methe B., RA Sutton G.G., Nelson K.E.; RL Submitted (JUL-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EGV14384.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFUR01000001; EGV14384.1; -; Genomic_DNA. DR RefSeq; WP_009406504.1; NZ_AFUR01000001.1. DR STRING; 944560.HMPREF9058_2041; -. DR EnsemblBacteria; EGV14384; EGV14384; HMPREF9058_2041. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000004281; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000004281}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000004281}. FT DOMAIN 322 487 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 550 AA; 58417 MW; 1A3C3C9053CEC158 CRC64; MTHHHSTTPS TPSTPEDAAD TRDAHEGRDV RDVQDVHDVH DVVARVLSRT GTALASTAAQ HEHAGGYADG LDDGALEREA RAARRRVAGL STELEDVSEV EYRQVRLEKV VLVGLELPRP HGPAAGAPGG SDQVRDAQDA DTSLRELAAL AQTAGSEVLD ALIQKRDHPD PATYLGSGKA RELADVVAAA GADTVIVDGE LAPSQRRALE DVVGVKVVDR TALILDIFAQ HAKSREGKAQ VELAQLEYLL PRLRGWGESM SRQAGGRVAA GQGIGSRGPG ETKIELDRRR IRQRMARLRR EIQAMAPSRE TKRGSRRRGA IPSVAIAGYT NAGKSSLMNR LTAAGIMVED ALFATLDPTV RRAETSEGRT YTLTDTVGFV RNLPHELIEA FRSTLEEVAG ADLVLHVVDA AHPDPLSQVA AVRTVLSEIP GALDVPELIV LNKTDLADAV TLAALRTGLP GAVAVSARTG EGIEELRARI EQMLPHPQVS IDVVVPYSRG DLVSRVHAEG EIDTVDYVEA GTHVVARVGA ALAAEIEGAS AGVTVDSDAP // ID F9PW66_9STRE Unreviewed; 412 AA. AC F9PW66; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 07-JUN-2017, entry version 36. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:EGV03852.1}; GN ORFNames=HMPREF9954_1576 {ECO:0000313|EMBL:EGV03852.1}; OS Streptococcus infantis SK970. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=1035189 {ECO:0000313|EMBL:EGV03852.1, ECO:0000313|Proteomes:UP000005460}; RN [1] {ECO:0000313|EMBL:EGV03852.1, ECO:0000313|Proteomes:UP000005460} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SK970 {ECO:0000313|EMBL:EGV03852.1, RC ECO:0000313|Proteomes:UP000005460}; RA Harkins D.M., Madupu R., Durkin A.S., Torralba M., Methe B., RA Sutton G.G., Nelson K.E.; RL Submitted (JUL-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EGV03852.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFUT01000003; EGV03852.1; -; Genomic_DNA. DR RefSeq; WP_006154223.1; NZ_AFUT01000003.1. DR STRING; 1035189.HMPREF9954_1576; -. DR EnsemblBacteria; EGV03852; EGV03852; HMPREF9954_1576. DR PATRIC; fig|1035189.4.peg.1044; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR Proteomes; UP000005460; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000005460}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000005460}. FT DOMAIN 199 359 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 412 AA; 46818 MW; 4C9B8021216EAC0B CRC64; MIETEKKEER VLLIGVELQG MDNFDLSMEE LASLAKTAGA VVVDSYRQKR EKYDSKTFVG SGKLEEIAQM VDAEEITTVI VNNRLTPRQN VNLEQVLGVK VIDRMQLILD IFAMRARSHE GKLQVHLAQL KYLLPRLVGQ GIMLSRQAGG IGSRGPGESQ LELNRRSVRN QITDIEYQLK VVEKNRATVR EKRLESSTFK IGLIGYTNAG KSTIMNTLTS KTQYEADELF ATLDATTKSI HLGGNLQVTL TDTVGFIQDL PTELVSSFKS TLEESKHVDL LVHVIDASNP YHEEHEKTVL SIMKDLDMED IPHLTLYNKA DLVEDFTPTQ TPYALISAKS KDSREQLQAL LLDKIKEIFE AFTLRVPFSK SYKIHDLESV AILEERDYQD DCEVIRGYIS EKNKWRLEEF YD // ID F9QB98_9PAST Unreviewed; 443 AA. AC F9QB98; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 30-AUG-2017, entry version 36. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:EGV05205.1}; GN ORFNames=HMPREF9952_1445 {ECO:0000313|EMBL:EGV05205.1}; OS Haemophilus pittmaniae HK 85. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=1035188 {ECO:0000313|EMBL:EGV05205.1, ECO:0000313|Proteomes:UP000006235}; RN [1] {ECO:0000313|EMBL:EGV05205.1, ECO:0000313|Proteomes:UP000006235} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=HK 85 {ECO:0000313|EMBL:EGV05205.1, RC ECO:0000313|Proteomes:UP000006235}; RA Harkins D.M., Madupu R., Durkin A.S., Torralba M., Methe B., RA Sutton G.G., Nelson K.E.; RL Submitted (JUL-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EGV05205.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFUV01000020; EGV05205.1; -; Genomic_DNA. DR ProteinModelPortal; F9QB98; -. DR STRING; 1035188.HMPREF9952_1445; -. DR EnsemblBacteria; EGV05205; EGV05205; HMPREF9952_1445. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000006235; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000006235}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000006235}. FT DOMAIN 215 382 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 181 211 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 443 AA; 49647 MW; 207B2B071A03898B CRC64; MSQTQIINAV ENANVSTAFS LSSMSMETAI AVQVWFDKEN NDDLQEFLLL AESAKVNVLQ IMTTRRNVPQ ARYFVGSGKA EEIADAVHQL DISVVLVNHQ LTPAQTRNLE NLCQCRVIDR TALILDIFAQ RARSHEGKLQ VELAQLKHLS SRLVGRKTGL DQQKGAVGLR GPGETQLETD RRLIKVRIAQ LQNRLAKVEK QRNQNRQTRQ KADIPTISLV GYTNAGKSTL FNFITQANVY AADQLFATLD PTLRRLQIQD VGTAILADTV GFVRDLPHDL VSAFKSTLQE TVEASLLLHI IDASDNRKLE NIEAVNSVLE EIKADNVPVL LVYNKIDLLE NVAPHIEYDD ENKPVAVYLS AHSGGGIALL LEAIKVRLTN EILSFTLTLL PQEGKIRHAL YQLDSICEEK ISDKGEFILR VRVDKVEWLR LCKQFPQLSE IIY // ID F9RCB9_VIBSN Unreviewed; 459 AA. AC F9RCB9; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 07-JUN-2017, entry version 35. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=VIBRN418_15708 {ECO:0000313|EMBL:EGU33772.1}; OS Vibrio sp. (strain N418). OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; OC Vibrionaceae; Vibrio. OX NCBI_TaxID=701176 {ECO:0000313|EMBL:EGU33772.1, ECO:0000313|Proteomes:UP000003627}; RN [1] {ECO:0000313|EMBL:EGU33772.1, ECO:0000313|Proteomes:UP000003627} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=N418 {ECO:0000313|EMBL:EGU33772.1, RC ECO:0000313|Proteomes:UP000003627}; RA Strain E.A., Brown E., Allard M.W.; RL Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EGU33772.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFWD01000051; EGU33772.1; -; Genomic_DNA. DR RefSeq; WP_009386085.1; NZ_AFWD01000051.1. DR STRING; 701176.VIBRN418_15708; -. DR EnsemblBacteria; EGU33772; EGU33772; VIBRN418_15708. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR Proteomes; UP000003627; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 2. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000003627}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000003627}. FT DOMAIN 241 406 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 202 236 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 459 AA; 51607 MW; CFDFD94AB1F8AD5A CRC64; MQLTAKPLQN NALLISICTP QFKGAEAKES LAELARLVTT LGFNVVGTQS QNLASTQKQN VLGVGKMAEI ARLTGNRGEM EEDLDTEDLF DDESFGDMAF DAPIYDEMRF DDLPSENLPL YCADVVVFDC DLSPSQLRNV ENQLGVEVFD RTGIIIEIFS RHARTRTARL QVEIARLNYL APRLRESTSG NKERQMGKGA GETTLELDRR KVRDQIAELR RELVSVQHEL KNRRSQRSEL FSVALVGYTN AGKSSMMRAL TGSEVLVENK LFATLDTTVR ALYPTTQPRI LVSDTVGFIK KLPHDLVASF HSTLAEAHDA SLLLYVVDAS DATFRTQLDV VHEVLGEVGV DDIKKLLVLN KSDQLSLEQQ QALMEEFPDA MMTSTRNPLD VAKLHQYIVD SSQQDMIEEE FIIQYDAQGI IGEIRTSMSV IKEEYEYDHI KLTVRSNAIE LARLKKRMK // ID F9REW0_VIBSN Unreviewed; 429 AA. AC F9REW0; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 30-AUG-2017, entry version 37. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=VIBRN418_12350 {ECO:0000313|EMBL:EGU32058.1}; OS Vibrio sp. (strain N418). OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; OC Vibrionaceae; Vibrio. OX NCBI_TaxID=701176 {ECO:0000313|EMBL:EGU32058.1, ECO:0000313|Proteomes:UP000003627}; RN [1] {ECO:0000313|EMBL:EGU32058.1, ECO:0000313|Proteomes:UP000003627} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=N418 {ECO:0000313|EMBL:EGU32058.1, RC ECO:0000313|Proteomes:UP000003627}; RA Strain E.A., Brown E., Allard M.W.; RL Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EGU32058.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFWD01000066; EGU32058.1; -; Genomic_DNA. DR RefSeq; WP_005595155.1; NZ_AFWD01000066.1. DR STRING; 701176.VIBRN418_12350; -. DR EnsemblBacteria; EGU32058; EGU32058; VIBRN418_12350. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR Proteomes; UP000003627; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000003627}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000003627}. FT DOMAIN 198 365 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 429 AA; 48694 MW; E7F35CB5E7F51CEA CRC64; MFDRYEAGER AVLVHINFTQ EGEWEDLSEF EMLVSSAGVS SLQVVTGSRQ SPLPKYYVGE GKAQEIAQIV QSTDADIVIF NHALSPAQER NLEALCQCRV VDRTGLILDI FAQRARTHEG KLQVELAQLR HISTRLIRGW THLERQKGGI GLRGPGETQL ETDRRLLRER IKAILRRLDK VAKQREQGRR ARNRAEIPTI SLVGYTNAGK STLFNRITAA GVYAADQLFA TLDPTLRKIE LADVGPAILA DTVGFIRHLP HDLVAAFKAT LQETQEADIL LHVVDASDER FRENMQAVQI VLEEIDAHEV PSLVVMNKID NLENQKPRIE RDEEGMPRTV WVSAMEGIGI DLLFEALTER LASQMVQYQL CVPPQHQGRL RSTFFQMKSI QQEEYDQDGN LLINIRMQQV DWSRLEKREG AVLRDFIVT // ID F9T158_9VIBR Unreviewed; 429 AA. AC F9T158; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 30-AUG-2017, entry version 41. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=IX91_13810 {ECO:0000313|EMBL:AIW15223.1}; OS Vibrio tubiashii ATCC 19109. OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; OC Vibrionaceae; Vibrio; Vibrio oreintalis group. OX NCBI_TaxID=1051646 {ECO:0000313|EMBL:AIW15223.1, ECO:0000313|Proteomes:UP000030071}; RN [1] {ECO:0000313|EMBL:AIW15223.1, ECO:0000313|Proteomes:UP000030071} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 19109 {ECO:0000313|EMBL:AIW15223.1, RC ECO:0000313|Proteomes:UP000030071}; RA Richards G.P., Needleman D.S., Watson M.A., Bono J.L.; RT "First Complete Genome Sequence of the Shellfish Pathogen Vibrio RT tubiashii."; RL Submitted (AUG-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP009354; AIW15223.1; -; Genomic_DNA. DR RefSeq; WP_004743152.1; NZ_CP009354.1. DR STRING; 1051646.VITU9109_02550; -. DR EnsemblBacteria; AIW15223; AIW15223; IX91_13810. DR GeneID; 23445799; -. DR KEGG; vtu:IX91_13810; -. DR PATRIC; fig|1051646.9.peg.2713; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR KO; K03665; -. DR Proteomes; UP000030071; Chromosome 1. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000030071}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}. FT DOMAIN 198 365 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 429 AA; 48772 MW; 01A990A3E8EEAA55 CRC64; MFDRYEAGER AVLVHINFTQ EGEWEDLSEF EMLVSSAGVS ALQVVTGSRQ SPHPKYYVGE GKAQEIAQAV QLSGADIVIF NHALSPAQER NLEQLCKCRV VDRTGLILDI FAQRARTHEG KLQVELAQLR HISTRLIRGW THLERQKGGI GLRGPGETQL ETDRRLLRDR IKAILRRLEK VAKQREQGRR ARNRAEIPTV SLVGYTNAGK STLFNRITEA GVYAADQLFA TLDPTLRKIE LADVGPAILA DTVGFIRHLP HDLVAAFKAT LQETQEADIL LHVVDASDDR FRENIQAVHE VLEEIDAHEV PSLVVMNKID NLEDQKPRIE RDEEGIPRAV WVSAMEGIGI ELLFDALTER LASQMVQYQL RIPPQHQGRI RSTFFQMKCI QREEYDQEGN LLINVRMQQV DWSRLEKREG AVLRDFIVT // ID F9UFS8_9GAMM Unreviewed; 428 AA. AC F9UFS8; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 07-JUN-2017, entry version 33. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=ThimaDRAFT_3781 {ECO:0000313|EMBL:EGV16952.1}; OS Thiocapsa marina 5811. OC Bacteria; Proteobacteria; Gammaproteobacteria; Chromatiales; OC Chromatiaceae; Thiocapsa. OX NCBI_TaxID=768671 {ECO:0000313|EMBL:EGV16952.1, ECO:0000313|Proteomes:UP000005459}; RN [1] {ECO:0000313|EMBL:EGV16952.1, ECO:0000313|Proteomes:UP000005459} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=5811 {ECO:0000313|EMBL:EGV16952.1, RC ECO:0000313|Proteomes:UP000005459}; RG US DOE Joint Genome Institute (JGI-PGF); RA Lucas S., Han J., Cheng J.-F., Goodwin L., Pitluck S., Peters L., RA Land M.L., Hauser L., Vogl K., Liu Z., Imhoff J., Thiel V., RA Frigaard N.-U., Bryant D., Woyke T.J.; RT "The draft genome of Thiocapsa marina 5811."; RL Submitted (JUN-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFWV01000013; EGV16952.1; -; Genomic_DNA. DR RefSeq; WP_007194653.1; NZ_AFWV01000013.1. DR ProteinModelPortal; F9UFS8; -. DR EnsemblBacteria; EGV16952; EGV16952; ThimaDRAFT_3781. DR PATRIC; fig|768671.3.peg.3990; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000005459; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000005459}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000005459}. FT DOMAIN 198 365 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 428 AA; 47267 MW; ECD0C662537A4D18 CRC64; MFERPSAGER AVLVHLDIGS TAEPDEREEF RRLAVAAGAE VVGTLGGSRS APDPKLFIGT GKCDELIALV AGTGAELVIV NHPLSPGQER NLERLVKCRV VDRSGLILDI FAQRARSFEG KLQVELAQLK HMSTRLVRGW THLERQKGGI GLRGPGETQL ETDRRLLAKR MTVLDRRLDR IQVQRAQGRK ARDKAELPVL SLVGYTNAGK STLFNRLTEA GVFQADQLFA TLDPTLRRLT LADGGRVLVA DTVGFVGRLP HELVAAFRST LEETRNASLL LHVVEASAPH RSRLAADVEQ VLAEIGSDEI PRLEVYNKVD LLPDESPRIE RDSAGFPSRV WLSAHTGAGV DLLLQAISEW LGRDRIRCSL DLEPDEGRLR AWLFEHAQIL SDVPKPAGGW SMDLIIGRPD RERLAARNTR FSEDKEGV // ID F9UM99_LACPL Unreviewed; 431 AA. AC F9UM99; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 30-AUG-2017, entry version 47. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=lp_0896 {ECO:0000313|EMBL:CCC78338.1}; OS Lactobacillus plantarum (strain ATCC BAA-793 / NCIMB 8826 / WCFS1). OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; OC Lactobacillus. OX NCBI_TaxID=220668 {ECO:0000313|EMBL:CCC78338.1, ECO:0000313|Proteomes:UP000000432}; RN [1] {ECO:0000313|EMBL:CCC78338.1, ECO:0000313|Proteomes:UP000000432} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-793 / NCIMB 8826 / WCFS1 RC {ECO:0000313|Proteomes:UP000000432}; RX PubMed=12566566; DOI=10.1073/pnas.0337704100; RA Kleerebezem M., Boekhorst J., van Kranenburg R., Molenaar D., RA Kuipers O.P., Leer R., Tarchini R., Peters S.A., Sandbrink H.M., RA Fiers M.W.E.J., Stiekema W., Klein Lankhorst R.M., Bron P.A., RA Hoffer S.M., Nierop Groot M.N., Kerkhoven R., De Vries M., Ursing B., RA De Vos W.M., Siezen R.J.; RT "Complete genome sequence of Lactobacillus plantarum WCFS1."; RL Proc. Natl. Acad. Sci. U.S.A. 100:1990-1995(2003). RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=WCFS1; RA Siezen R.J., Francke C., Renckens B., Boekhorst J., Wels M., RA Kleerebezem M., van Hijum S.A.F.T.; RT "Complete resequencing and reannotation of the Lactobacillus plantarum RT WCFS1 genome."; RL Submitted (JUN-2011) to the EMBL/GenBank/DDBJ databases. RN [3] {ECO:0000313|EMBL:CCC78338.1, ECO:0000313|Proteomes:UP000000432} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-793 / NCIMB 8826 / WCFS1 RC {ECO:0000313|Proteomes:UP000000432}; RX PubMed=22156394; DOI=10.1128/JB.06275-11; RA Siezen R.J., Francke C., Renckens B., Boekhorst J., Wels M., RA Kleerebezem M., van Hijum S.A.F.T.; RT "Complete resequencing and reannotation of the Lactobacillus plantarum RT WCFS1 genome."; RL J. Bacteriol. 194:195-196(2012). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AL935263; CCC78338.1; -; Genomic_DNA. DR RefSeq; WP_003641141.1; NC_004567.2. DR RefSeq; YP_004888852.1; NC_004567.2. DR ProteinModelPortal; F9UM99; -. DR STRING; 220668.lp_0896; -. DR DNASU; 1062774; -. DR EnsemblBacteria; CCC78338; CCC78338; lp_0896. DR GeneID; 1062774; -. DR KEGG; lpl:lp_0896; -. DR PATRIC; fig|220668.9.peg.759; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR KO; K03665; -. DR OMA; FNNHAHV; -. DR BioCyc; LPLA220668:G137Z-772-MONOMER; -. DR Proteomes; UP000000432; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000000432}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000000432}. FT DOMAIN 207 375 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 431 AA; 47764 MW; F2514DE3865A4ECF CRC64; MSETNAQKVQ EVIIAGMSKT VANYDYAMSE LEALVAANNM HAALRIDQGL EKPNPATFFG KGKVVEIKEV AAANDLHIMV INADLTPSQV RNLEEQTDIQ IIDRTGLILE IFGNRARSKE AKLQVKIAQL QYQLPRLRTS ISNRLDQQAG AAAGGGGGFT NRGAGETQLE LNRRTIQDRI SHAKHELKEL NKDEVVRRSQ RDKAGLPNVA LVGYTNAGKS TTMNGLVKLF GKGEDKQVFE KDMLFATLDT SIRQLTFPDN KQLLLSDTVG FVSDLPHNLI NAFRSTLAEA ANADLLIQVI DYADPHYKEM MATTEKTLKE IGVHDVPMIY AFNKADLTEA DYPNQQDDQL IYTARDEASL QALTSMIKAK VFKNYVTTTL LIPFNDGEVV AYLNDHANIL KTDYLADGTQ LTVELNTVDA QRYEKYVVTP A // ID F9VG86_LACGL Unreviewed; 411 AA. AC F9VG86; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 07-JUN-2017, entry version 42. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=LCGL_1877 {ECO:0000313|EMBL:BAK61337.1}; OS Lactococcus garvieae (strain Lg2) (Enterococcus seriolicida). OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Lactococcus. OX NCBI_TaxID=420890 {ECO:0000313|EMBL:BAK61337.1, ECO:0000313|Proteomes:UP000008520}; RN [1] {ECO:0000313|EMBL:BAK61337.1, ECO:0000313|Proteomes:UP000008520} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Lg2 {ECO:0000313|EMBL:BAK61337.1, RC ECO:0000313|Proteomes:UP000008520}; RX PubMed=21829716; DOI=10.1371/journal.pone.0023184; RA Morita H., Toh H., Oshima K., Yoshizaki M., Kawanishi M., Nakaya K., RA Suzuki T., Miyauchi E., Ishii Y., Tanabe S., Murakami M., Hattori M.; RT "Complete genome sequence and comparative analysis of the fish RT pathogen Lactococcus garvieae."; RL PLoS ONE 6:E23184-E23184(2011). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AP009333; BAK61337.1; -; Genomic_DNA. DR RefSeq; WP_014025486.1; NC_017490.1. DR ProteinModelPortal; F9VG86; -. DR STRING; 420890.LCGL_1877; -. DR EnsemblBacteria; BAK61337; BAK61337; LCGL_1877. DR GeneID; 12480469; -. DR KEGG; lgv:LCGL_1877; -. DR PATRIC; fig|420890.5.peg.1850; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000008520; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000008520}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000008520}. FT DOMAIN 200 360 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 173 196 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 411 AA; 46647 MW; 146F62AA9D7BC4D2 CRC64; MINLEEKQER VLLAGVETFE NSENFESSML ELAELTKTAG GIVVDAFTQK RDRYDTKFLI GTGKLEQMKW AIEVGEIDTV IFNDRLTPRQ NINLEEALGI KVIDRMQLIL DIFALRARSH EGMLQVEQAQ LSYLLPRLVG QGIMLSRQGG GIGSKGPGES KLETDRRYIR TRIENIDKQL KKVEKTRETI RKKRKESSIF KIGLIGYTNA GKSSIMNALT EKTQYEKDEL FATLDATTKL VKIKEDFTVS LTDTVGFIQD LPTELIKAFK STLEESTHVD LLIHVIDASN PHHEVHEKTV QKLMEEMDIQ GIPVLNVYNK MDIAQDFVPT LAPAVQLSIK SDEGVQWLRT AILEKLHELF VAFELDLPYA MAYKLPELKK IAMVNDVIEG ETAYKVKGLI APNMTWKLDN Y // ID F9VKI4_ARTSS Unreviewed; 604 AA. AC F9VKI4; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 07-JUN-2017, entry version 40. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=SFBM_0875 {ECO:0000313|EMBL:BAK56642.1}; OS Arthromitus sp. (strain SFB-mouse-Japan). OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Candidatus Arthromitus. OX NCBI_TaxID=1029718 {ECO:0000313|EMBL:BAK56642.1, ECO:0000313|Proteomes:UP000001636}; RN [1] {ECO:0000313|EMBL:BAK56642.1, ECO:0000313|Proteomes:UP000001636} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SFB-mouse-Japan {ECO:0000313|Proteomes:UP000001636}; RX PubMed=21791478; DOI=10.1093/dnares/dsr022; RA Kuwahara T., Ogura Y., Oshima K., Kurokawa K., Ooka T., Hirakawa H., RA Itoh T., Nakayama-Imaohji H., Ichimura M., Itoh K., Ishifune C., RA Maekawa Y., Yasutomo K., Hattori M., Hayashi T.; RT "The lifestyle of the segmented filamentous bacterium: a non- RT culturable gut-associated immunostimulating microbe inferred by whole- RT genome sequencing."; RL DNA Res. 18:291-303(2011). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AP012202; BAK56642.1; -; Genomic_DNA. DR RefSeq; WP_014017966.1; NC_015913.1. DR ProteinModelPortal; F9VKI4; -. DR STRING; 1029718.SFBM_0875; -. DR EnsemblBacteria; BAK56642; BAK56642; SFBM_0875. DR KEGG; asf:SFBM_0875; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR KO; K03665; -. DR OMA; EREVIIT; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000001636; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000001636}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000001636}. FT DOMAIN 364 546 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 604 AA; 69535 MW; 0FAD44E8DB2B1F17 CRC64; MIYGDTNGIK RSYLNELEDI YDIRLDKNLI ISEEILYKIC EISFKINKEI CIVLLRNGNV HSISIGTNAD AKIHIDLKDK KKLSGCRVIH THLNSSPKLS DVDIASLKNL RLDAISAVNV TDENLFNGFS IGMLNNGDNE YEEYVFYNLK DYLDFNIFSK IQDIEKNFKV EIYENEISDN CVLIGCDTLE SLEELRELAY ACNINVKDMF FQNRDKADSV YYIGKGKIKE ILNSIYHRNI TLLIFDDDLS GSQIRVLEEM SGIRVIDRTT LILEIFNRRA KSKVSKYQVE LAMLKYKYSK LRGLSSDLNR TSGGIGLRGG SGETKLETDR RYVRSKIDYL KKEIEKIKLE RSVQRDARIK NNIPQVSIVG YTNAGKSTLR NYIYSTSNVG EVDLDKKLVI EADMLFATLD TTVRKILLPR KTLISLTDTV GFIKKLPHDL VDAFKSTLEE VIYSSLLLHV VDISSNNFEV EINTTDNVLK EIGIKNLNRI LIFNKIDKLK NSELEELKSK IYKLYPSDKI VFISVIEKIN IDKLLNLVEE TLSLNYQNVS LLIPYDDYSI LNSVYESYKI IKEKHLDKGT FVNFDIPKSE LDRFKKYIIE DLEN // ID F9YTN0_CAPCC Unreviewed; 408 AA. AC F9YTN0; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 07-JUN-2017, entry version 41. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Ccan_19590 {ECO:0000313|EMBL:AEK24075.1}; OS Capnocytophaga canimorsus (strain 5). OC Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales; OC Flavobacteriaceae; Capnocytophaga. OX NCBI_TaxID=860228 {ECO:0000313|EMBL:AEK24075.1, ECO:0000313|Proteomes:UP000008895}; RN [1] {ECO:0000313|EMBL:AEK24075.1, ECO:0000313|Proteomes:UP000008895} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=5 {ECO:0000313|Proteomes:UP000008895}; RX PubMed=21914877; DOI=10.1128/JB.05853-11; RA Manfredi P., Pagni M., Cornelis G.R.; RT "Complete genome sequence of the dog commensal and human pathogen RT Capnocytophaga canimorsus strain 5."; RL J. Bacteriol. 193:5558-5559(2011). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002113; AEK24075.1; -; Genomic_DNA. DR RefSeq; WP_013998059.1; NC_015846.1. DR ProteinModelPortal; F9YTN0; -. DR STRING; 860228.Ccan_19590; -. DR EnsemblBacteria; AEK24075; AEK24075; Ccan_19590. DR KEGG; ccm:Ccan_19590; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000008895; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000008895}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000008895}. FT DOMAIN 200 385 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 408 AA; 46998 MW; F5303AA39329C28A CRC64; MLEQINLNYE KVVLVGIINQ MQDEEKSKEY LDELEFLTYT AGGEVLQRFT QKLDVPNPKT FIGTGKMEEV QQFVEENGVG TVIFDDELSP AQQKNIERIL KAKILDRTGL ILDIFAQRAQ TSYSRTQVEL AQYQYLLPRL TGLWTHLERQ RGGIGMRGPG ETEIETDRRI VRDRIALLKK KLATIDRQMA VQRGNRGAMV RVALIGYTNV GKSTLMNVIS KSEVFAENKL FATLDTTVRK VVIGNLPFLL SDTVGFIRKL PTQLIESFKS TLDEVREADL LLHIVDISHP NFEEHIHSVN QILSEIKSAD KPTIMVFNKI DAYKHQTIAE DDLITEPTSK HFTLEQWKQT WMNKVGNDVL FISALNKDNL EEFREKVYAK VREIHITRFP YNNFLYPEFI EDNTETEN // ID F9Z5T8_ODOSD Unreviewed; 430 AA. AC F9Z5T8; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 07-JUN-2017, entry version 41. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Odosp_2863 {ECO:0000313|EMBL:ADY33839.1}; OS Odoribacter splanchnicus (strain ATCC 29572 / DSM 20712 / CIP 104287 / OS JCM 15291 / NCTC 10825 / 1651/6) (Bacteroides splanchnicus). OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Odoribacteraceae; OC Odoribacter. OX NCBI_TaxID=709991 {ECO:0000313|EMBL:ADY33839.1, ECO:0000313|Proteomes:UP000006657}; RN [1] {ECO:0000313|EMBL:ADY33839.1, ECO:0000313|Proteomes:UP000006657} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29572 / DSM 20712 / JCM 15291 / NCTC 10825 / 1651/6 RC {ECO:0000313|Proteomes:UP000006657}; RX PubMed=21677857; DOI=10.4056/sigs.1714269; RG US DOE Joint Genome Institute (JGI-PGF); RA Goker M., Gronow S., Zeytun A., Nolan M., Lucas S., Lapidus A., RA Hammon N., Deshpande S., Cheng J.F., Pitluck S., Liolios K., RA Pagani I., Ivanova N., Mavromatis K., Ovchinikova G., Pati A., RA Tapia R., Han C., Goodwin L., Chen A., Palaniappan K., Land M., RA Hauser L., Jeffries C.D., Brambilla E.M., Rohde M., Detter J.C., RA Woyke T., Bristow J., Markowitz V., Hugenholtz P., Eisen J.A., RA Kyrpides N.C., Klenk H.P.; RT "Complete genome sequence of Odoribacter splanchnicus type strain RT (1651/6)."; RL Stand. Genomic Sci. 4:200-209(2011). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002544; ADY33839.1; -; Genomic_DNA. DR RefSeq; WP_013613031.1; NC_015160.1. DR ProteinModelPortal; F9Z5T8; -. DR STRING; 709991.Odosp_2863; -. DR EnsemblBacteria; ADY33839; ADY33839; Odosp_2863. DR KEGG; osp:Odosp_2863; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000006657; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000006657}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000006657}. FT DOMAIN 223 407 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 430 AA; 49475 MW; 606A4512818547F0 CRC64; MPKQQASVLR YCSSLQILLF YMYYTDQEAE KAILVGVALQ SEGITYEQMT EYLDELSFLA ETAGAETVKI FTQNLDKPVH ATFIGKGKLE EIKAYTEENP VDMVIFDDEL SPTQLRNIES VFPGIKVLDR TNLILDIFAS RARTAHAKTQ VELAQYQYLL PRLTGMWTHL ERQKGGIGLR GPGETEIETD RRIIRDKISR LKNELTKIDK QKVIQRKNRG KLVRVALVGY TNVGKSTLMN LLSKSDVFAE NKLFATLDTT VRKIAIKNVP FLLADTVGFI RKLPHHLVES FKSTLDEVRE ADVILHVVDI SHPQFEDQMK VVNATLAELI KEPKPTIIIF NKIDAFHYVQ KEEDDLTPVT RENYSLNDLK QMWMSRQGSE TVYISAVKKE NIEELKEKLY DIVKEIHSAR FPYNDFLYQD YTENNPETEE // ID F9ZFG9_9PROT Unreviewed; 390 AA. AC F9ZFG9; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 07-JUN-2017, entry version 41. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=NAL212_2173 {ECO:0000313|EMBL:ADZ27001.1}; OS Nitrosomonas sp. AL212. OC Bacteria; Proteobacteria; Betaproteobacteria; Nitrosomonadales; OC Nitrosomonadaceae; Nitrosomonas. OX NCBI_TaxID=153948 {ECO:0000313|EMBL:ADZ27001.1, ECO:0000313|Proteomes:UP000001629}; RN [1] {ECO:0000313|EMBL:ADZ27001.1, ECO:0000313|Proteomes:UP000001629} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=AL212 {ECO:0000313|EMBL:ADZ27001.1, RC ECO:0000313|Proteomes:UP000001629}; RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L., RA Pitluck S., Chertkov O., Held B., Detter J.C., Han C., Tapia R., RA Land M., Hauser L., Kyrpides N., Ivanova N., Mikhailova N., Pagani I., RA Suwa Y., Klotz M.G., Bollmann A., Stein L.Y., Laanbroek H.J., RA Arp D.J., Norton J.M., Woyke T.; RT "Complete sequence of chromosome of Nitrosomonas sp. AL212."; RL Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002552; ADZ27001.1; -; Genomic_DNA. DR RefSeq; WP_013648016.1; NC_015222.1. DR ProteinModelPortal; F9ZFG9; -. DR STRING; 153948.NAL212_2173; -. DR EnsemblBacteria; ADZ27001; ADZ27001; NAL212_2173. DR KEGG; nit:NAL212_2173; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR KO; K03665; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000001629; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000001629}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000001629}. FT DOMAIN 197 366 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 390 AA; 43643 MW; 81BC1AC2BB0EAB65 CRC64; MNKLIASDTA ILVGVDFGCG THQDSLLELQ LLASSDKLEV IAIVTGKRSR PDSTTYIGRG KVEEIVRVMQ QTEAGLVIFN HDLSPAQQRN LSLRLNCNVI DRTNLILDIF ARRAHSHEGK LQVELAQLEY LLTRLVRGWT HLERQKGGIG LRGPGETQLE TDRRLIKKRV KLLKGKLSDL QCQRNVQRRS RQRSNSLTVS IVGYTNAGKS TFFNKLTRAQ SYAADQLFAT LDTTTRKLFI EEGSTVVISD TVGFIRELPH TLIAAFRATL EETVQADLLL HVIDASNSNS DEQIKEVNKI LKEIGADVIP QILIFNKIDL IDATLRSAGC VRDEYGRISR IRLSAETGEG VEFVRQALTE TILENSKKLN KESMEINNGL RDCASVQDFF // ID F9ZHU5_9PROT Unreviewed; 449 AA. AC F9ZHU5; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 07-JUN-2017, entry version 41. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=NAL212_1347 {ECO:0000313|EMBL:ADZ26243.1}; OS Nitrosomonas sp. AL212. OC Bacteria; Proteobacteria; Betaproteobacteria; Nitrosomonadales; OC Nitrosomonadaceae; Nitrosomonas. OX NCBI_TaxID=153948 {ECO:0000313|EMBL:ADZ26243.1, ECO:0000313|Proteomes:UP000001629}; RN [1] {ECO:0000313|EMBL:ADZ26243.1, ECO:0000313|Proteomes:UP000001629} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=AL212 {ECO:0000313|EMBL:ADZ26243.1, RC ECO:0000313|Proteomes:UP000001629}; RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L., RA Pitluck S., Chertkov O., Held B., Detter J.C., Han C., Tapia R., RA Land M., Hauser L., Kyrpides N., Ivanova N., Mikhailova N., Pagani I., RA Suwa Y., Klotz M.G., Bollmann A., Stein L.Y., Laanbroek H.J., RA Arp D.J., Norton J.M., Woyke T.; RT "Complete sequence of chromosome of Nitrosomonas sp. AL212."; RL Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002552; ADZ26243.1; -; Genomic_DNA. DR RefSeq; WP_013647294.1; NC_015222.1. DR ProteinModelPortal; F9ZHU5; -. DR STRING; 153948.NAL212_1347; -. DR EnsemblBacteria; ADZ26243; ADZ26243; NAL212_1347. DR KEGG; nit:NAL212_1347; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR KO; K03665; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000001629; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000001629}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000001629}. FT DOMAIN 223 393 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 449 AA; 50064 MW; 49E3C65F3947343D CRC64; MQNESQEKSR CVVVAAVQLS SVTDAEFEAS LTELCELAKT LGFRVVHRFT QKRSGFDATA YLGAGKRQEI REFVNNEFDG DGQEAPQNAK PDAKVIDVIL VNHEISPSQA RNLEKETGCE VMDRTMVIVE IFHRNARSPA ARAQVEIARL SYLAPRLREM AKLAGPQGRQ RSGTGGRGAG ESHTELDRRK IRDRIAELQL EIVAMDAERQ IQRTRRLERR GNASVALVGY TNAGKSTLMR ALTGSEVLVA NKLFATLDTT VRTLHPASVP RILVSDTVGF IKNLPHGLVA SFKSTLDEAL DASLLLHIID ASDPGYERQL EVTNTVLEEI AAQDIPRIRI FNKIDHVGDT AAQAECEAVL KTLYPACIVM SARRPDDVAN LHQQIVAFFQ QDLVEDELFL PWTAQQLRSQ IYANCKVLEE RADGEGAFFR IRGESDVVKS LRERFEQMR // ID F9ZP36_ACICS Unreviewed; 426 AA. AC F9ZP36; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 07-JUN-2017, entry version 37. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Atc_1789 {ECO:0000313|EMBL:AEK58437.1}; OS Acidithiobacillus caldus (strain SM-1). OC Bacteria; Proteobacteria; Acidithiobacillia; Acidithiobacillales; OC Acidithiobacillaceae; Acidithiobacillus. OX NCBI_TaxID=990288 {ECO:0000313|EMBL:AEK58437.1, ECO:0000313|Proteomes:UP000006135}; RN [1] {ECO:0000313|EMBL:AEK58437.1, ECO:0000313|Proteomes:UP000006135} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SM-1 {ECO:0000313|EMBL:AEK58437.1, RC ECO:0000313|Proteomes:UP000006135}; RX PubMed=21703548; DOI=10.1016/j.jgg.2011.04.006; RA You X.Y., Guo X., Zheng H.J., Zhang M.J., Liu L.J., Zhu Y.Q., Zhu B., RA Wang S.Y., Zhao G.P., Poetsch A., Jiang C.Y., Liu S.J.; RT "Unraveling the Acidithiobacillus caldus complete genome and its RT central metabolisms for carbon assimilation."; RL J. Genet. Genomics 38:243-252(2011). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002573; AEK58437.1; -; Genomic_DNA. DR RefSeq; WP_004872417.1; NC_015850.1. DR ProteinModelPortal; F9ZP36; -. DR EnsemblBacteria; AEK58437; AEK58437; Atc_1789. DR KEGG; acu:Atc_1789; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000006135; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000006135}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000006135}. FT DOMAIN 188 355 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 426 AA; 47577 MW; DD3D22BAA3C8369B CRC64; MVLVHVPLAS EQSEDHGEEF RHLAEGAGAE VVAFLSAQRQ RLDPATCIGR GKIDEIRALA DAHSADLVLF DRPLSPVQER NLERELRRPV VDRVGLILDI FARRARTHEG KLQVELAQLD RLRTRLVRGW THLERQRGGI GLRGPGETQL ETDRRLIGER IRALRARLLR IQSQRATQRR ARQRAPVPTV ALVGYTNAGK STLFNRLTAN HQYVADQLFA TLDPAVRRLQ FGKGRGEWLL ADTVGFLRDL PTELIAAFRA TLEEVNRADL LLHVVDASAV DRELQMAAVD AVLAEIGAAE VPRLVVYNKV DRTGERVGPV RDSSGAVQAL RLSAVTGEGL SELVATVRER IAPARLRSHW SLGPEEGALR AKLYALGEVL DERFDEAGRD QLLVELDSAA LQRLQREYGQ HSCQRRRAAP TMHEEH // ID G0A0W9_METMM Unreviewed; 421 AA. AC G0A0W9; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 07-JUN-2017, entry version 40. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Metme_2844 {ECO:0000313|EMBL:AEG01225.1}; OS Methylomonas methanica (strain MC09). OC Bacteria; Proteobacteria; Gammaproteobacteria; Methylococcales; OC Methylococcaceae; Methylomonas. OX NCBI_TaxID=857087 {ECO:0000313|EMBL:AEG01225.1, ECO:0000313|Proteomes:UP000008888}; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=MC09; RA Boden R., Cunliffe M., Scanlan J., Moussard H., Kits K.D., Klotz M., RA Jetten M., Vuilleumier S., Han J., Peters L., Mikhailova N., RA Teshima H., Tapia R., Kyrpides N., Ivanova N., Pagani I., Cheng J.-F., RA Goodwin L., Han C., Hauser L., Land M., Lapidus A., Lucas S., RA Pitluck S., Woyke T., Stein L.Y., Murrell C.; RT "Complete genome sequence of the aerobic marine methanotroph RT Methylomonas methanica MC09."; RL Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Proteomes:UP000008888} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC09 {ECO:0000313|Proteomes:UP000008888}; RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S., RA Peters L., Mikhailova N., Teshima H., Han C., Tapia R., Land M., RA Hauser L., Kyrpides N., Ivanova N., Pagani I., Stein L., Woyke T.; RT "Complete sequence of Methylomonas methanica MC09."; RL Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002738; AEG01225.1; -; Genomic_DNA. DR RefSeq; WP_013819458.1; NC_015572.1. DR ProteinModelPortal; G0A0W9; -. DR STRING; 857087.Metme_2844; -. DR EnsemblBacteria; AEG01225; AEG01225; Metme_2844. DR KEGG; mmt:Metme_2844; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000008888; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000008888}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000008888}. FT DOMAIN 196 363 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 162 189 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 421 AA; 46946 MW; E0484426F7F355F2 CRC64; MFERPEAGER AVLVHLNLQV GQEDLDELKE LTKSAGAQPI CVVTGSRHRP DPKYFVGKGK LDEIKTVVSE QQADIVIVNH PLSPSQERNL EKALEVRVVD RNGLILDIFA QRAQTFEGKL QVELAQLKHL STRLIRGWTH LERQKGGIGL RGPGETQLET DRRLLAVRIK QIQQRLEKVQ KQRHQGRSKR KKAEIPTVSL VGYTNAGKST LFNTLTGADI YAADQLFATL DPTLRHLAIG DSGEVVLADT VGFIRHLPHE LVAAFRSTLQ EASEADLLLH VIDAHAEDRD DTIFQVNQVL DDIEAGKIPQ LRVFNKIDLL DGVLPHIDYD DQGRPVNVWI SAQSGAGCEL LRQALSAFFA SSKIIKKCFL PASQAGLKAK WFGLVRFIDE TVNDRGDCEL TIEIDKKNLG LLKDIRVEEV A // ID G0AK68_COLFT Unreviewed; 373 AA. AC G0AK68; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 07-JUN-2017, entry version 39. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:AEK61753.1}; GN OrderedLocusNames=CFU_1921 {ECO:0000313|EMBL:AEK61753.1}; OS Collimonas fungivorans (strain Ter331). OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Oxalobacteraceae; Collimonas. OX NCBI_TaxID=1005048 {ECO:0000313|EMBL:AEK61753.1, ECO:0000313|Proteomes:UP000008392}; RN [1] {ECO:0000313|Proteomes:UP000008392} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Ter331 {ECO:0000313|Proteomes:UP000008392}; RA Leveau J.H.; RT "Complete sequence of Collimonas fungivorans Ter331."; RL Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002745; AEK61753.1; -; Genomic_DNA. DR ProteinModelPortal; G0AK68; -. DR STRING; 1005048.CFU_1921; -. DR EnsemblBacteria; AEK61753; AEK61753; CFU_1921. DR KEGG; cfu:CFU_1921; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000008392; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000008392}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000008392}. FT DOMAIN 190 356 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 156 183 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 373 AA; 40628 MW; 703B78F4100194D5 CRC64; MRAALVGVDF GKGDFAASLE ELSLLAKSAG AVPLVTITGK RSSPDAALFV GSGKAQEIAD AVFDDELEIV IFNHALSPAQ QRNLERVLKV RVLDRTSLIL DIFAQRAKSH EGKVQVELAQ LQHLATRLIR GWTHLERQKG GIGLRGPGET QLETDRRLLG DRVKALRARL DKLHRQHATQ RRARGRSATI SISLVGYTNA GKSTLFNALA KAGVYAADQL FATLDTTSRR VYLGEAGSVV ISDTVGFIRE LPHQLVAAFR ATLEETIHAD LLLHVVDAAS PARMEQIEQV NLVLKEIGAD HIPQILVWNK IDAAELEPAV ERDEYDKIQR VFVSAQKGLG LDLLRQAIAE FVTGNPPAAA YSAPAAENTQ QQV // ID G0G783_AMYMS Unreviewed; 482 AA. AC G0G783; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 07-JUN-2017, entry version 50. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=RAM_12155 {ECO:0000313|EMBL:AEK40921.1}; OS Amycolatopsis mediterranei (strain S699) (Nocardia mediterranei). OC Bacteria; Actinobacteria; Pseudonocardiales; Pseudonocardiaceae; OC Amycolatopsis. OX NCBI_TaxID=713604 {ECO:0000313|EMBL:AEK40921.1, ECO:0000313|Proteomes:UP000006138}; RN [1] {ECO:0000313|EMBL:AEK40921.1, ECO:0000313|Proteomes:UP000006138} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=S699 {ECO:0000313|EMBL:AEK40921.1, RC ECO:0000313|Proteomes:UP000006138}; RX PubMed=21914879; DOI=10.1128/JB.05819-11; RA Verma M., Kaur J., Kumar M., Kumari K., Saxena A., Anand S., Nigam A., RA Ravi V., Raghuvanshi S., Khurana P., Tyagi A.K., Khurana J.P., Lal R.; RT "Whole genome sequence of the rifamycin B-producing strain RT Amycolatopsis mediterranei S699."; RL J. Bacteriol. 193:5562-5563(2011). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002896; AEK40921.1; -; Genomic_DNA. DR RefSeq; WP_013224262.1; NC_018266.1. DR ProteinModelPortal; G0G783; -. DR EnsemblBacteria; AEK40921; AEK40921; RAM_12155. DR KEGG; amm:AMES_2362; -. DR KEGG; amn:RAM_12155; -. DR PATRIC; fig|713604.12.peg.2505; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000006138; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 2. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000006138}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000006138}. FT DOMAIN 255 424 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 482 AA; 52479 MW; 51AE207AE564E73B CRC64; MTELTHTEDH DDDLYDGDPS TGEMELEDRA SLRRVRGLST ELDDVTEVEY RQLRLERVVL VGVWTEGTAL QSEASLAELA RLAETAGSEV LEGLIQRRTK PDPATYIGSG KVRELRDIVG STGADTVICD GELSPGQLRQ LEEKVKVKVI DRTALILDIF AQHARSKEGK AQVELAQLQY LIPRLRGWGA SLSRQAGGRA GGANGGVGLR GPGETKLETD RRRINKRVAK LRREIAAMDT IRETKRGRRL ANEVPSVAIV GYTNAGKSSL LNALTGAGVL VEDALFATLD PTTRRAQTPD GRGYTLTDTV GFVRHLPHQL VDAFRSTLEE AADADLLVHV VDGSDPAPEE QVSAVREVLG EITRKRKEPL PPELLVINKT DASDEVSLAR LRHALAGSVQ VSARTGAGIA ELVEVIADRL PRPEVTVDVL VPYSRGELVA RAHADGEVLE EEHAEDGTRL LVRVRPDLAA ALREYETNST RA // ID G0GF04_SPITZ Unreviewed; 408 AA. AC G0GF04; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 07-JUN-2017, entry version 35. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Spith_2092 {ECO:0000313|EMBL:AEJ62348.1}; OS Spirochaeta thermophila (strain ATCC 700085 / DSM 6578 / Z-1203). OC Bacteria; Spirochaetes; Spirochaetales; Spirochaetaceae; Spirochaeta. OX NCBI_TaxID=869211 {ECO:0000313|EMBL:AEJ62348.1, ECO:0000313|Proteomes:UP000007254}; RN [1] {ECO:0000313|EMBL:AEJ62348.1, ECO:0000313|Proteomes:UP000007254} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700085 / DSM 6578 / Z-1203 RC {ECO:0000313|Proteomes:UP000007254}; RG US DOE Joint Genome Institute (JGI-PGF); RA Lucas S., Lapidus A., Bruce D., Goodwin L., Pitluck S., Peters L., RA Kyrpides N., Mavromatis K., Ivanova N., Mikailova N., Pagani I., RA Chertkov O., Detter J.C., Tapia R., Han C., Land M., Hauser L., RA Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Spring S., RA Merkhoffer B., Schneider S., Klenk H.-P., Eisen J.A.; RT "The complete genome of Spirochaeta thermophila DSM 6578."; RL Submitted (JUN-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002903; AEJ62348.1; -; Genomic_DNA. DR RefSeq; WP_014625665.1; NC_017583.1. DR EnsemblBacteria; AEJ62348; AEJ62348; Spith_2092. DR KEGG; stq:Spith_2092; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000007254; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000007254}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000007254}. FT DOMAIN 198 361 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 408 AA; 46453 MW; 007B510133525003 CRC64; MYDTGQEAPR CILVGRKTGR EETSSLPELS LLVEELGYIP ETILSFPLRT PERKFLFGPG QAEVVAREAR MRGIDLVVFD EDLTPAQQRN WEHLVKSRVM DRTEVIIEIF SRHARTKQAQ LQTEKARLEY LLPRLRGAWS HLDRQRGGAR GTRGEGERQI ELDRRMILSR LARIRREMEA IERHQTTTRS RRLEAGIPRV SLVGYTNAGK SSLFTRLTGQ AVRIQDRPFV TLDTTTRTCL IPGWGRVVVS DTVGFIQHLP HTLVDAFHAT LEEVRDAHLL LEVVDLSSPN LLLHLSTTEE VLTEIGAHHI PRIRVYNKVD RSSPHPLLPP SNHPEILVSA KTGEGIEGLL SLIVREMERH YPIETLELPY HRLGESHEVL SRAAIIHQEY TDVGLFVRYA PSVPSVHE // ID G0HEH2_CORVD Unreviewed; 483 AA. AC G0HEH2; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 07-JUN-2017, entry version 41. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:AEK36958.1}; GN OrderedLocusNames=CVAR_1604 {ECO:0000313|EMBL:AEK36958.1}; OS Corynebacterium variabile (strain DSM 44702 / JCM 12073 / NCIMB 30131) OS (Corynebacterium mooreparkense). OC Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae; OC Corynebacterium. OX NCBI_TaxID=858619 {ECO:0000313|EMBL:AEK36958.1, ECO:0000313|Proteomes:UP000006659}; RN [1] {ECO:0000313|EMBL:AEK36958.1, ECO:0000313|Proteomes:UP000006659} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 44702 / JCM 12073 / NCIMB 30131 RC {ECO:0000313|Proteomes:UP000006659}; RX PubMed=22053731; DOI=10.1186/1471-2164-12-545; RA Schroeder J., Maus I., Trost E., Tauch A.; RT "Complete genome sequence of Corynebacterium variabile DSM 44702 RT isolated from the surface of smear-ripened cheeses and insights into RT cheese ripening and flavor generation."; RL BMC Genomics 12:545-545(2011). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002917; AEK36958.1; -; Genomic_DNA. DR RefSeq; WP_014010123.1; NC_015859.1. DR STRING; 858619.CVAR_1604; -. DR EnsemblBacteria; AEK36958; AEK36958; CVAR_1604. DR KEGG; cva:CVAR_1604; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000006659; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000006659}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Hydrolase {ECO:0000313|EMBL:AEK36958.1}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000006659}. FT DOMAIN 259 435 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 218 245 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 483 AA; 52301 MW; BED090C1BD4E5F52 CRC64; MNDINRTDGT EPTPAPTGTP TVGDLDLEQR SSLRRLTRGT ADHSTEQSDG YDVEYRRLRL ERVVLVGVWT EGTVEQVEAR LAELSALAET AGSEVVDMLY QRRDKPDSGT YIGSGKVEEL RQVVVETGAD TVVADGELSP GQMIALEKLL DVKVIDRTML ILDIFAQHAK SREGKAQVQL AQLEYLITRV RGWGGALSRQ AGGRAGSNGG VGLRGPGETK IEADRQRIRN DMAKLRREIT GMKKARDIKR RQRDSSAVAQ VAIAGYTNAG KSSLLNALTG AGVLVEDALF ATLDPTTRRA ELADGRTVVF SDTVGFIRFL PTQLVEAFRS TLEEVMAADV VLHVVDGSDP FPMEQIAAVN KVIGEIAEET GEDAPPEILV VNKVDAADPL VLADLRNRLD DVIFVSASTG EGIAELESRL ELFLNSMDAR VTLSVPFSRG EVVSRVHELG TVLSEEYTSD GTVLDVRLPK VLAAELAAFV VQP // ID G0J3L3_CYCMS Unreviewed; 421 AA. AC G0J3L3; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 07-JUN-2017, entry version 40. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Cycma_1450 {ECO:0000313|EMBL:AEL25219.1}; OS Cyclobacterium marinum (strain ATCC 25205 / DSM 745) (Flectobacillus OS marinus). OC Bacteria; Bacteroidetes; Cytophagia; Cytophagales; Cyclobacteriaceae; OC Cyclobacterium. OX NCBI_TaxID=880070 {ECO:0000313|EMBL:AEL25219.1, ECO:0000313|Proteomes:UP000001635}; RN [1] {ECO:0000313|Proteomes:UP000001635} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 25205 / DSM 745 {ECO:0000313|Proteomes:UP000001635}; RA Lucas S., Han J., Lapidus A., Bruce D., Goodwin L., Pitluck S., RA Peters L., Kyrpides N., Mavromatis K., Ivanova N., Ovchinnikova G., RA Chertkov O., Detter J.C., Tapia R., Han C., Land M., Hauser L., RA Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Tindall B., RA Schuetze A., Brambilla E., Klenk H.-P., Eisen J.A.; RT "The complete genome of Cyclobacterium marinum DSM 745."; RL Submitted (JUL-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002955; AEL25219.1; -; Genomic_DNA. DR RefSeq; WP_014019514.1; NC_015914.1. DR STRING; 880070.Cycma_1450; -. DR EnsemblBacteria; AEL25219; AEL25219; Cycma_1450. DR KEGG; cmr:Cycma_1450; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR BioCyc; CMAR880070:GHDK-1459-MONOMER; -. DR Proteomes; UP000001635; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000001635}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000001635}. FT DOMAIN 210 399 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 171 198 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 421 AA; 48199 MW; DC8B7DBA5835E29A CRC64; MSKHSRKLAK LVDTSPKEET AILVALIHQN ETEKLVQDHL DELAFLTETL GAKAIHRFTQ RMDKPDTRSF VGTGKLEEIK AYVEYFDVDM VIFDEDLSPS QVKILENELK IKVYDRSMLI LDIFLNRAQT AQAKTQVELA RFQYLLPRLT RMWTHLERQR GGTATRGGAG EKEIETDKRD IRRKIDILKD KLKKIEKQGQ TQRKGRQGIV RVALVGYTNV GKSTLMNLLT KENILAENKL FATVDSTVRK VVLENIPFLI SDTVGFIRKL PTHLIESFKS TLSEIEEADL LVHVVDIAHP GFEDQIAVVN QTLRELGAGD KPMIMVFNKI DIAPKMPSEE ELMEMSEFEV EEANFIDFEK LKVSYAKKSA INPVFMAAGD GTNIDELRKT IIEEVKKIHK KMYPHYLEDE VVDFSQYSDE E // ID G0LBA1_ZOBGA Unreviewed; 403 AA. AC G0LBA1; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 07-JUN-2017, entry version 38. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hfiX {ECO:0000313|EMBL:CAZ95901.1}; GN Synonyms=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=zobellia_1848 {ECO:0000313|EMBL:CAZ95901.1}; OS Zobellia galactanivorans (strain DSM 12802 / CCUG 47099 / CIP 106680 / OS NCIMB 13871 / Dsij). OC Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales; OC Flavobacteriaceae; Zobellia. OX NCBI_TaxID=63186 {ECO:0000313|EMBL:CAZ95901.1, ECO:0000313|Proteomes:UP000008898}; RN [1] {ECO:0000313|Proteomes:UP000008898} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 12802 / CCUG 47099 / CIP 106680 / NCIMB 13871 / Dsij RC {ECO:0000313|Proteomes:UP000008898}; RG Genoscope - CEA; RT "Complete genome sequence of Zobellia galactanivorans Dsij."; RL Submitted (JUL-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; FP476056; CAZ95901.1; -; Genomic_DNA. DR RefSeq; WP_013993209.1; NC_015844.1. DR ProteinModelPortal; G0LBA1; -. DR EnsemblBacteria; CAZ95901; CAZ95901; ZOBELLIA_1848. DR KEGG; zga:ZOBELLIA_1848; -. DR PATRIC; fig|63186.3.peg.1823; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR Proteomes; UP000008898; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000008898}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000008898}. FT DOMAIN 200 385 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 403 AA; 46676 MW; 81578B7B83843CD4 CRC64; MLEKKTIDHE KAVLIGIINR EQSEGKVTEY LDELEFLTYT AGGEVVKRFV QRMDVPNPKT LIGTGKMEEV EAFVKANDIG SVIFDDELTP AQQRNIEKLL RCKIVDRTSL ILDIFAQRAQ TSYARTQVEL AQYEYLLPRL TGLWTHLERQ RGGIGMRGPG ETEIETDRRI VRDRISLLKK KLLKIDRQME TQRGNRGALV RVALVGYTNV GKSTLMNVIS KSDVFAENKL FATLDTTVRK VVIGNLPFLL SDTVGFIRKL PTQLVESFKS TLDEVREADL LLHVVDISHP QFEEHIESVN KILDEIDSAD KNTIMVFNKI DLYKHAEIDE DDLVTERSER HFTIDEWKKT WMQRVGDKAL FISALNKENL DEFRKRVYDE VRDIHVTRFP YNNFLYPEHL DEY // ID G0NPM2_CAEBE Unreviewed; 465 AA. AC G0NPM2; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 30-AUG-2017, entry version 32. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EGT35308.1}; GN ORFNames=CAEBREN_11668 {ECO:0000313|EMBL:EGT35308.1}; OS Caenorhabditis brenneri (Nematode worm). OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida; OC Rhabditoidea; Rhabditidae; Peloderinae; Caenorhabditis. OX NCBI_TaxID=135651 {ECO:0000313|Proteomes:UP000008068}; RN [1] {ECO:0000313|Proteomes:UP000008068} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=PB2801 {ECO:0000313|Proteomes:UP000008068}; RG Caenorhabditis brenneri Sequencing and Analysis Consortium; RA Wilson R.K.; RL Submitted (JUL-2011) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GL379921; EGT35308.1; -; Genomic_DNA. DR STRING; 135651.CBN11668; -. DR EnsemblMetazoa; CBN11668; CBN11668; WBGene00150393. DR eggNOG; KOG0410; Eukaryota. DR eggNOG; COG2262; LUCA. DR InParanoid; G0NPM2; -. DR OMA; MDTVGFM; -. DR OrthoDB; EOG091G0852; -. DR Proteomes; UP000008068; Unassembled WGS sequence. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR CDD; cd01878; HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008068}; KW Reference proteome {ECO:0000313|Proteomes:UP000008068}. FT DOMAIN 236 402 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 465 AA; 52223 MW; A92DA68D2F40D32B CRC64; MIFGRFTQCS LISIRSLSIG RPEVATTSSK FANERWSVLV VHPKVRWGSG SASVLKQADR QLDEAVALVN NLPNMIAVDS LIMPVDYNTK RKSIWATGNL EKLVARREEA RATALMVNVD VLSPTQQEEL FRIFEVPIFD RYNIVLSTFK EFARTDEARL QIALAEIPYI KHRIHALSSK RLHSRPEILH IEQQYSEIEG DLNEILRKRE QDLRRDLKEA TRKSAEQVGV KNSSDAVVAV VGYTNAGKTS LVKRLTGAVS LTPKDQLFAT LDTTRHVAKL PSGRSAVFTD TIGFLSDLPM HLISAFEATL AHVKSADVII HLRDVSNPDW KAQEEDVVAT LKSIGIADNV LTERMITVDN KIDKEGATNA SESINSVRIS CKTGDGMSEL VELLNEKVTM ATRCKTIRLR LDVRSPVINW LYHNEFVVVE PIVDGNNLIF DVVMNESEVG RFRKTFAHLR KKSHE // ID G0QU66_ICHMG Unreviewed; 707 AA. AC G0QU66; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 30-AUG-2017, entry version 19. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EGR31247.1}; GN ORFNames=IMG5_115070 {ECO:0000313|EMBL:EGR31247.1}; OS Ichthyophthirius multifiliis (strain G5) (White spot disease agent) OS (Ich). OC Eukaryota; Alveolata; Ciliophora; Intramacronucleata; OC Oligohymenophorea; Hymenostomatida; Ophryoglenina; Ichthyophthirius. OX NCBI_TaxID=857967 {ECO:0000313|Proteomes:UP000008983}; RN [1] {ECO:0000313|EMBL:EGR31247.1, ECO:0000313|Proteomes:UP000008983} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=G5 {ECO:0000313|EMBL:EGR31247.1, RC ECO:0000313|Proteomes:UP000008983}; RA Coyne R., Brami D., Johnson J., Hostetler J., Hannick L., Clark T., RA Cassidy-Hanley D., Inman J.; RL Submitted (JUL-2011) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GL983901; EGR31247.1; -; Genomic_DNA. DR RefSeq; XP_004034733.1; XM_004034685.1. DR EnsemblProtists; EGR31247; EGR31247; IMG5_115070. DR GeneID; 14907377; -. DR InParanoid; G0QU66; -. DR Proteomes; UP000008983; Unassembled WGS sequence. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR CDD; cd01878; HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008983}; KW Reference proteome {ECO:0000313|Proteomes:UP000008983}. FT DOMAIN 421 592 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 707 AA; 82663 MW; B36F367DA1FD37CA CRC64; MIKFLQQKII QFQNKSLFNL PRQLYQSKEQ LDFRKQKQIH SFGFAPEIKC LIIHPVLYPN KGPEIELYLA EEAIGLAKSL NWAIEQGPFW KQEQKQIELK EKNQDENYAN DDDQYDLTPG GRIKKPNNQL KNHPGWELAG EANLKDGDYI YTPYFKGTYY KSGIIVDLES ESDEDADLQH EWQNRLLRES IAKSSLMKVK RIIGKTYFTK GKLLDLGLYI KDKNIDCVFI NSEITTTQQK NLEKIWSNIV NGKEEEAFFK KNPQQSSDTE VESDDGLMEK KEDNQYQDND DRKIKVFDRF TIILQIFAKR AQTQISKLQI EISFLNYMKT KVQRDGGQTF SSVYSIFKGD LMSVNELNIE IVSAKSRATR GKASGQGETQ LELQKRLIDE KLSKLKKDLS GVQQQQTFIR EKRNKQHNNI PKISLIGYTN SGKSALMNAL VKKEVVESKD NLFQTLSTTS RKIQLIQGQK AIILDTIGFI TNLPHELVES FKSTLEEVQN SDLFLHVRDI SHPQTEQQKQ TVLQVLKDLK FDQSFYSNKM IEVWNKMDLV KNKVDYKDAL KQDFPSIPVS ALYNTNIGKL VEVMEQKVNE LMNKKYYNLI NPLEQHKQRF DWLYLNGNIT RIENEVYNYD QTKQYPYGCV QFSALLDDVT YRRYCTTFGI QLEEKIYKKN LPPKEWLQGS QSYFEKKKKD KIQEDQEFFK NAKNKKQ // ID G1KLK2_ANOCA Unreviewed; 522 AA. AC G1KLK2; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 26-JUN-2013, sequence version 2. DT 30-AUG-2017, entry version 36. DE SubName: Full=GTP binding protein 6 (putative) {ECO:0000313|Ensembl:ENSACAP00000011603}; GN Name=GTPBP6 {ECO:0000313|Ensembl:ENSACAP00000011603}; OS Anolis carolinensis (Green anole) (American chameleon). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; OC Toxicofera; Iguania; Iguanidae; Polychrotinae; Anolis. OX NCBI_TaxID=28377 {ECO:0000313|Ensembl:ENSACAP00000011603, ECO:0000313|Proteomes:UP000001646}; RN [1] {ECO:0000313|Ensembl:ENSACAP00000011603, ECO:0000313|Proteomes:UP000001646} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=JBL SC #1 {ECO:0000313|Ensembl:ENSACAP00000011603}; RG The Genome Sequencing Platform; RA Di Palma F., Alfoldi J., Heiman D., Young S., Grabherr M., Johnson J., RA Lander E.S., Lindblad-Toh K.; RT "The Genome Sequence of Anolis carolinensis (Green Anole Lizard)."; RL Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Ensembl:ENSACAP00000011603} RP IDENTIFICATION. RG Ensembl; RL Submitted (SEP-2011) to UniProtKB. CC -!- CAUTION: The sequence shown here is derived from an Ensembl CC automatic analysis pipeline and should be considered as CC preliminary data. {ECO:0000313|Ensembl:ENSACAP00000011603}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR RefSeq; XP_003218826.1; XM_003218778.3. DR STRING; 28377.ENSACAP00000011603; -. DR Ensembl; ENSACAT00000011843; ENSACAP00000011603; ENSACAG00000011834. DR GeneID; 100565760; -. DR KEGG; acs:100565760; -. DR CTD; 8225; -. DR eggNOG; KOG0410; Eukaryota. DR eggNOG; COG2262; LUCA. DR GeneTree; ENSGT00390000001397; -. DR InParanoid; G1KLK2; -. DR OrthoDB; EOG091G0852; -. DR TreeFam; TF315022; -. DR Proteomes; UP000001646; Chromosome 3. DR Bgee; ENSACAG00000011834; -. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR GO; GO:0043022; F:ribosome binding; IBA:GO_Central. DR CDD; cd01878; HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 4: Predicted; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000001646}; KW Reference proteome {ECO:0000313|Proteomes:UP000001646}. FT DOMAIN 296 460 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 258 285 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 522 AA; 58476 MW; 86ECDA1AC2D9E44F CRC64; MSSRWRHVLR LGGKLSTISP HPRAACLPRG PWRFLRATAA SYRPPGNGKR GGNDHGRRWG PEETEEEGEE DEDERNFEEE EALAESGLPA VPPGHQKVFI VHPAVKWGPG KPQLTTAELQ LAEAVALINT IQNWTVLDKI ILSTKVPDKK FIFGKGNFQL LTEKIKGLPE ISSVFVNVER LSPPTKKELE QAWEVQVFDR YSVVLHIFRC NAQTKEAKLQ IALAEIPLLR SNIRNEVAQL DQQRGGSRYI MGSGETFMEL QLRLLKEKEL KIRKALERLR RKRRLLRSQR MKREFPTVSV MGYTNCGKTT LIKALTGDAG LQPQDQLFAT LDITAHAGSL PSRLTVLYVD TIGFLSQLPH DLVESFSATL EDVACSDLIL HVRDVSHPET NLQKESVLTV LRNLSLPSHL LKSIIEVHNK VDLIDGHHPT EPNTIAISAL LGHGLEELKE EIEKKILEVT GKNILTIKVN LSGTQLSWLY KEATVQDVDV VPEDGTANVK VVISNSALGK YKRLFPRSSY SS // ID G1L5A7_AILME Unreviewed; 473 AA. AC G1L5A7; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 30-AUG-2017, entry version 30. DE SubName: Full=GTP binding protein 6 (putative) {ECO:0000313|Ensembl:ENSAMEP00000002068}; GN Name=GTPBP6 {ECO:0000313|Ensembl:ENSAMEP00000002068}; OS Ailuropoda melanoleuca (Giant panda). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Carnivora; Caniformia; Ursidae; OC Ailuropoda. OX NCBI_TaxID=9646 {ECO:0000313|Ensembl:ENSAMEP00000002068, ECO:0000313|Proteomes:UP000008912}; RN [1] {ECO:0000313|Ensembl:ENSAMEP00000002068} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=20010809; DOI=10.1038/nature08696; RA Li R., Fan W., Tian G., Zhu H., He L., Cai J., Huang Q., Cai Q., RA Li B., Bai Y., Zhang Z., Zhang Y., Wang W., Li J., Wei F., Li H., RA Jian M., Li J., Zhang Z., Nielsen R., Li D., Gu W., Yang Z., Xuan Z., RA Ryder O.A., Leung F.C., Zhou Y., Cao J., Sun X., Fu Y., Fang X., RA Guo X., Wang B., Hou R., Shen F., Mu B., Ni P., Lin R., Qian W., RA Wang G., Yu C., Nie W., Wang J., Wu Z., Liang H., Min J., Wu Q., RA Cheng S., Ruan J., Wang M., Shi Z., Wen M., Liu B., Ren X., Zheng H., RA Dong D., Cook K., Shan G., Zhang H., Kosiol C., Xie X., Lu Z., RA Zheng H., Li Y., Steiner C.C., Lam T.T., Lin S., Zhang Q., Li G., RA Tian J., Gong T., Liu H., Zhang D., Fang L., Ye C., Zhang J., Hu W., RA Xu A., Ren Y., Zhang G., Bruford M.W., Li Q., Ma L., Guo Y., An N., RA Hu Y., Zheng Y., Shi Y., Li Z., Liu Q., Chen Y., Zhao J., Qu N., RA Zhao S., Tian F., Wang X., Wang H., Xu L., Liu X., Vinar T., Wang Y., RA Lam T.W., Yiu S.M., Liu S., Zhang H., Li D., Huang Y., Wang X., RA Yang G., Jiang Z., Wang J., Qin N., Li L., Li J., Bolund L., RA Kristiansen K., Wong G.K., Olson M., Zhang X., Li S., Yang H., RA Wang J., Wang J.; RT "The sequence and de novo assembly of the giant panda genome."; RL Nature 463:311-317(2010). RN [2] {ECO:0000313|Ensembl:ENSAMEP00000002068} RP IDENTIFICATION. RG Ensembl; RL Submitted (SEP-2011) to UniProtKB. CC -!- CAUTION: The sequence shown here is derived from an Ensembl CC automatic analysis pipeline and should be considered as CC preliminary data. {ECO:0000313|Ensembl:ENSAMEP00000002068}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACTA01004792; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; ACTA01012792; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; ACTA01020792; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; ACTA01196779; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR ProteinModelPortal; G1L5A7; -. DR STRING; 9646.ENSAMEP00000002068; -. DR Ensembl; ENSAMET00000002152; ENSAMEP00000002068; ENSAMEG00000001958. DR eggNOG; KOG0410; Eukaryota. DR eggNOG; COG2262; LUCA. DR GeneTree; ENSGT00390000001397; -. DR InParanoid; G1L5A7; -. DR OMA; MDTVGFM; -. DR OrthoDB; EOG091G0852; -. DR TreeFam; TF315022; -. DR Proteomes; UP000008912; Unassembled WGS sequence. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR CDD; cd01878; HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 4: Predicted; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000008912}; KW Reference proteome {ECO:0000313|Proteomes:UP000008912}. FT DOMAIN 253 417 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 222 249 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 473 AA; 52191 MW; AB91C2E54830FFCB CRC64; RAAAAEGRVW GSTLADGTRS RAGEEEEEPE DAEEEEEEEE LLRRDPLLPV GTQRVCLIHP EVKQGPGKPQ LTRAEWQVAE GEALVHTLDG WSVAETMVVP SNAPDGKLIF GKGTLEHLTE KIRGLPEITA VFLNVERLAT PTKKELEAAW GVQVFDRFTV VLHIFRCNAR TKEARLQVAL AELPLLRSHL KSSMARPDGR GGGSRYIMGS GESFMQVQQR LFKEKEMKIR KALERLKKKR RLLGRQRRRQ EFPVISVVGY TNCGKTTLIK ALTGDDGVQP RDQLFATLDV TAHAGWLPSC MAVIYMDTIG FLSQLPHSLI ESFSATLEDM AHSDLIVHVR DVSHPETELQ KASVLSALHG LCLPAPLLDS MLEVHNKVDL VPGYSPPGPQ AVAVSALLGH GLLELKARLE DAVLRATGRQ VLTLRVRLVG AQLSWLHREA TVQEVDVVPE AGVADVKVVI SSSAYGKFRK LFP // ID G1NPH5_MELGA Unreviewed; 404 AA. AC G1NPH5; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 2. DT 30-AUG-2017, entry version 35. DE SubName: Full=GTP binding protein 6 (putative) {ECO:0000313|Ensembl:ENSMGAP00000015632}; GN Name=GTPBP6 {ECO:0000313|Ensembl:ENSMGAP00000015632}; OS Meleagris gallopavo (Common turkey). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda; OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; OC Phasianidae; Meleagridinae; Meleagris. OX NCBI_TaxID=9103 {ECO:0000313|Ensembl:ENSMGAP00000015632, ECO:0000313|Proteomes:UP000001645}; RN [1] {ECO:0000313|Ensembl:ENSMGAP00000015632, ECO:0000313|Proteomes:UP000001645} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=20838655; DOI=10.1371/journal.pbio.1000475; RA Dalloul R.A., Long J.A., Zimin A.V., Aslam L., Beal K., Blomberg L.A., RA Bouffard P., Burt D.W., Crasta O., Crooijmans R.P., Cooper K., RA Coulombe R.A., De S., Delany M.E., Dodgson J.B., Dong J.J., Evans C., RA Frederickson K.M., Flicek P., Florea L., Folkerts O., Groenen M.A., RA Harkins T.T., Herrero J., Hoffmann S., Megens H.J., Jiang A., RA de Jong P., Kaiser P., Kim H., Kim K.W., Kim S., Langenberger D., RA Lee M.K., Lee T., Mane S., Marcais G., Marz M., McElroy A.P., RA Modise T., Nefedov M., Notredame C., Paton I.R., Payne W.S., RA Pertea G., Prickett D., Puiu D., Qioa D., Raineri E., Ruffier M., RA Salzberg S.L., Schatz M.C., Scheuring C., Schmidt C.J., Schroeder S., RA Searle S.M., Smith E.J., Smith J., Sonstegard T.S., Stadler P.F., RA Tafer H., Tu Z.J., Van Tassell C.P., Vilella A.J., Williams K.P., RA Yorke J.A., Zhang L., Zhang H.B., Zhang X., Zhang Y., Reed K.M.; RT "Multi-platform next-generation sequencing of the domestic turkey RT (Meleagris gallopavo): genome assembly and analysis."; RL PLoS Biol. 8:E1000475-E1000475(2010). RN [2] {ECO:0000313|Ensembl:ENSMGAP00000015632} RP IDENTIFICATION. RG Ensembl; RL Submitted (SEP-2011) to UniProtKB. CC -!- CAUTION: The sequence shown here is derived from an Ensembl CC automatic analysis pipeline and should be considered as CC preliminary data. {ECO:0000313|Ensembl:ENSMGAP00000015632}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR STRING; 9103.ENSMGAP00000015632; -. DR Ensembl; ENSMGAT00000016591; ENSMGAP00000015632; ENSMGAG00000014752. DR eggNOG; KOG0410; Eukaryota. DR eggNOG; COG2262; LUCA. DR GeneTree; ENSGT00390000001397; -. DR InParanoid; G1NPH5; -. DR OMA; MDTVGFM; -. DR OrthoDB; EOG091G0852; -. DR TreeFam; TF315022; -. DR Proteomes; UP000001645; Chromosome 1. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR CDD; cd01878; HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 4: Predicted; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000001645}; KW Reference proteome {ECO:0000313|Proteomes:UP000001645}. FT DOMAIN 183 347 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 145 172 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 404 AA; 45837 MW; FBC5FBB2CAC41323 CRC64; VSKAELQIAE AVALVDTLQN WTVLDKIIIP TKNPDKKFIF GKGNFEALTE KIKKLPHVTA VFLNVERISS VTKKELEDAW GVKVFDRYTV VLHIFRCNAR TKEAKLQIAL AEIPLLRSNL KTEVSHLDQQ RGGSRYIMGS GETFMETQNR LLREKELKIR NALEKLRRKR SLLRTQRKKR EFPIISVMGY TNCGKTTLIK ALTGEAGIQP RNQLFATLDI TAHAGYLPSR MAVIYVDTIG FLSDLPHNLV ESFSATLEEV AYSDLIVHVR DITHPETILQ KASVLSVLKN LNLPSHLLES MVEVHNKVDL IESYEPTEEN ALAISALHGH GLEELKEEIE KKILKATGKK ILTITVNLQG PQLRKTWTNM KLIVLQVLNL PKHTTLILIF FKNCCDNYQS LIVY // ID G1SUS2_RABIT Unreviewed; 514 AA. AC G1SUS2; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 13-NOV-2013, sequence version 2. DT 30-AUG-2017, entry version 35. DE SubName: Full=GTP binding protein 6 (putative) {ECO:0000313|Ensembl:ENSOCUP00000007124}; GN Name=GTPBP6 {ECO:0000313|Ensembl:ENSOCUP00000007124}; OS Oryctolagus cuniculus (Rabbit). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; OC Oryctolagus. OX NCBI_TaxID=9986 {ECO:0000313|Ensembl:ENSOCUP00000007124, ECO:0000313|Proteomes:UP000001811}; RN [1] {ECO:0000313|Ensembl:ENSOCUP00000007124, ECO:0000313|Proteomes:UP000001811} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Thorbecke {ECO:0000313|Proteomes:UP000001811}; RX PubMed=21993624; DOI=10.1038/nature10530; RA Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J., RA Washietl S., Kheradpour P., Ernst J., Jordan G., Mauceli E., RA Ward L.D., Lowe C.B., Holloway A.K., Clamp M., Gnerre S., Alfoldi J., RA Beal K., Chang J., Clawson H., Cuff J., Di Palma F., Fitzgerald S., RA Flicek P., Guttman M., Hubisz M.J., Jaffe D.B., Jungreis I., RA Kent W.J., Kostka D., Lara M., Martins A.L., Massingham T., Moltke I., RA Raney B.J., Rasmussen M.D., Robinson J., Stark A., Vilella A.J., RA Wen J., Xie X., Zody M.C., Baldwin J., Bloom T., Chin C.W., Heiman D., RA Nicol R., Nusbaum C., Young S., Wilkinson J., Worley K.C., Kovar C.L., RA Muzny D.M., Gibbs R.A., Cree A., Dihn H.H., Fowler G., Jhangiani S., RA Joshi V., Lee S., Lewis L.R., Nazareth L.V., Okwuonu G., RA Santibanez J., Warren W.C., Mardis E.R., Weinstock G.M., Wilson R.K., RA Delehaunty K., Dooling D., Fronik C., Fulton L., Fulton B., Graves T., RA Minx P., Sodergren E., Birney E., Margulies E.H., Herrero J., RA Green E.D., Haussler D., Siepel A., Goldman N., Pollard K.S., RA Pedersen J.S., Lander E.S., Kellis M.; RT "A high-resolution map of human evolutionary constraint using 29 RT mammals."; RL Nature 478:476-482(2011). RN [2] {ECO:0000313|Ensembl:ENSOCUP00000007124} RP IDENTIFICATION. RC STRAIN=Thorbecke {ECO:0000313|Ensembl:ENSOCUP00000007124}; RG Ensembl; RL Submitted (SEP-2011) to UniProtKB. CC -!- CAUTION: The sequence shown here is derived from an Ensembl CC automatic analysis pipeline and should be considered as CC preliminary data. {ECO:0000313|Ensembl:ENSOCUP00000007124}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AAGW02072985; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR RefSeq; XP_002716902.1; XM_002716856.3. DR STRING; 9986.ENSOCUP00000007124; -. DR Ensembl; ENSOCUT00000008242; ENSOCUP00000007124; ENSOCUG00000008245. DR GeneID; 100358022; -. DR KEGG; ocu:100358022; -. DR CTD; 8225; -. DR eggNOG; KOG0410; Eukaryota. DR eggNOG; COG2262; LUCA. DR GeneTree; ENSGT00390000001397; -. DR InParanoid; G1SUS2; -. DR OMA; MDTVGFM; -. DR OrthoDB; EOG091G0852; -. DR TreeFam; TF315022; -. DR Proteomes; UP000001811; Chromosome 14. DR Bgee; ENSOCUG00000008245; -. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR CDD; cd01878; HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 4: Predicted; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000001811}; KW Reference proteome {ECO:0000313|Proteomes:UP000001811}. FT DOMAIN 293 457 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 255 289 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 514 AA; 56719 MW; AEB0D00D43E74656 CRC64; MWALRAAVRP LLPRSRACRG LPTPRAAPPQ PRHSRALAAF RPWGPGGPGS ERWGPRTEAP KSPAGEDEGD PEGAEEEEEE LLRRDPLLPS GTQRVCLVHP DVKWGAGKPQ LTRAEWQVAE AAALVRSLDG WSVVLTLVVP TKTPERKLIF GRGNLERLTE TIRGAADITC VFLNLERMAA PTKKELEAAW GIQVFDRFTI VLHIFRAHAR TREARLQVAL AELPLLRSGL KSDITQWDRQ RGGSRYILGS GESARQVQQR ELREKEAGIR KALERLRRKR QLLRQQRARR ELPVVSVVGY TNCGKTTLIQ ALTGDQAMQP QDRLFATLDV TVHAGWLPSR LPVLYVDTVG FLSQLPHGLL ESFTATLEDV AHSDLIVHVR DVSHPETELQ KASVLSALQG LHLPSSLLDS MLEVHNKVDL VPGYSPSGPS AVAVSALLGH GLEELKAGLE AAILRATGRH MVTLRVGLQG AQLSWLHREA TVQQVHVVPG AQAADVDVII SDSAHRRFRK LFPE // ID G1UWY4_9DELT Unreviewed; 549 AA. AC G1UWY4; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 1. DT 07-JUN-2017, entry version 36. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=HMPREF1022_03107 {ECO:0000313|EMBL:EGW49806.1}; OS Desulfovibrio sp. 6_1_46AFAA. OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfovibrionales; OC Desulfovibrionaceae; Desulfovibrio. OX NCBI_TaxID=665942 {ECO:0000313|EMBL:EGW49806.1, ECO:0000313|Proteomes:UP000006424}; RN [1] {ECO:0000313|EMBL:EGW49806.1, ECO:0000313|Proteomes:UP000006424} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=6_1_46AFAA {ECO:0000313|EMBL:EGW49806.1, RC ECO:0000313|Proteomes:UP000006424}; RG The Broad Institute Genome Sequencing Platform; RA Earl A., Ward D., Feldgarden M., Gevers D., Daigneault M., Strauss J., RA Ambrose C.E., Allen-Vercoe E., Young S.K., Zeng Q., Gargeya S., RA Fitzgerald M., Haas B., Abouelleil A., Alvarado L., Arachchi H.M., RA Berlin A., Brown A., Chapman S.B., Chen Z., Dunbar C., Freedman E., RA Gearin G., Gellesch M., Goldberg J., Griggs A., Gujja S., Heiman D., RA Howarth C., Larson L., Lui A., MacDonald P.J.P., Mehta T., RA Montmayeur A., Murphy C., Neiman D., Pearson M., Priest M., RA Roberts A., Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., RA Wortman J., Nusbaum C., Birren B.; RT "The Genome Sequence of Desulfovibrio sp. 6_1_46AFAA."; RL Submitted (JUN-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EGW49806.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACWM01000082; EGW49806.1; -; Genomic_DNA. DR RefSeq; WP_009303861.1; NZ_JH114305.1. DR EnsemblBacteria; EGW49806; EGW49806; HMPREF1022_03107. DR PATRIC; fig|665942.3.peg.3211; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000006424; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000006424}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000006424}. FT DOMAIN 371 536 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 337 364 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 549 AA; 60899 MW; 41A690649CC42273 CRC64; MQGLKPSQLN ALNRLFNRRF PSEDVYTIEQ ARELALLSRA LGRQVGLLID RKGRVQMVLV GEAGSILIPE LPRGRTGQER LRGLRLLHTH LSPDGISQED LMDMLFLRLD AVIALSVNPT GDPVQWQAAH LLPSGATGKP HHLDAPQPWD RTAAQFTATA EALEEELARR GEDAREAADA PRALLVSVAA QPRILQERNL DELAELARTA GLTVAGRMAQ RVAQVNPRLI LGKGKVAELE VLALQGRAGM LVFDGELSPA QLHNLADITE RKVIDRTQLI LDIFAQHAVT RAGKLQVELA QLRYTQPRLV GKNRAMDRLM GGIGGRGPGE TKLETDRRKS RERMARIRKE LDQLRRQRAF TRARRSRQGI PLAALVGYTN AGKSTLLNRL TRSDVLAENK LFATLDPTTR RLRFPAEREI ILADTVGFIR NLPKELMDAF RATLEELEAA DLLVHVADAS HPDLLQQISA VETILAEMEL DRVPRLLVLN KWDQLAAPAR AELADAFPLA LPVSAKSGDG LNYLLEQLET DLLTRNRPPV IPDMPFSLN // ID G1WBJ5_9BACT Unreviewed; 415 AA. AC G1WBJ5; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 1. DT 07-JUN-2017, entry version 36. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=HMPREF9431_01196 {ECO:0000313|EMBL:EGV31449.1}; OS Prevotella oulorum F0390. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Prevotellaceae; OC Prevotella. OX NCBI_TaxID=702438 {ECO:0000313|EMBL:EGV31449.1, ECO:0000313|Proteomes:UP000005141}; RN [1] {ECO:0000313|EMBL:EGV31449.1, ECO:0000313|Proteomes:UP000005141} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=F0390 {ECO:0000313|EMBL:EGV31449.1, RC ECO:0000313|Proteomes:UP000005141}; RG The Broad Institute Genome Sequencing Platform; RG The Broad Institute Genome Sequencing Center for Infectious Disease; RA Earl A., Ward D., Feldgarden M., Gevers D., Izard J., Ganesan A., RA Baranova O.V., Blanton J.M., Tanner A.C., Dewhirst F.E., Young S.K., RA Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., RA Alvarado L., Arachchi H.M., Berlin A., Brown A., Chapman S.B., RA Chen Z., Dunbar C., Freedman E., Gearin G., Gellesch M., Goldberg J., RA Griggs A., Gujja S., Heiman D., Howarth C., Larson L., Lui A., RA MacDonald P.J.P., Mehta T., Montmayeur A., Murphy C., Neiman D., RA Pearson M., Priest M., Roberts A., Saif S., Shea T., Shenoy N., RA Sisk P., Stolte C., Sykes S., Wortman J., Nusbaum C., Birren B.; RT "The Genome Sequence of Prevotella oulorum F0390."; RL Submitted (JUL-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EGV31449.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADGI01000044; EGV31449.1; -; Genomic_DNA. DR RefSeq; WP_004380227.1; NZ_JH114215.1. DR STRING; 702438.HMPREF9431_01196; -. DR EnsemblBacteria; EGV31449; EGV31449; HMPREF9431_01196. DR PATRIC; fig|702438.4.peg.1237; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000005141; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000005141}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000005141}. FT DOMAIN 216 400 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 415 AA; 47439 MW; 01671E8D24B9F6E1 CRC64; MKEFVISEVK AESAILVGLI TETQNEAKTK EYLDELEFLA DTAGAVTVKR FTQKVNGPSA VTYVGKGKLE EIKAYIEQCE DNEEPIGMVI FDDELSAKQI RNIENELKVK ILDRTSLILD IFAMRAQTAN AKTQVELAQY RYMLPRLQRL WTHLERQGGG SGSGGGKGSV GLRGPGETQL EMDRRIILQR ITLLKQRLQE IDKQKTTQRK NRGRMIRVAL VGYTNVGKST IMNLLAKSEV FAENKLFATL DTTVRKVVVD NLPFLLADTV GFIRKLPTDL VDSFKSTLDE VREADLLVHV VDISHPDFEE QIRVVDNTLK ELGCSDKPSM IIFNKIDNYH WIEKEKDDLT PATKENIPLE ELERTWMARL NDNCLFISAK TKCNIETFRK TLYIRVRELH VQKYPYNDFL YPAME // ID G1WG27_9ACTN Unreviewed; 354 AA. AC G1WG27; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 1. DT 07-JUN-2017, entry version 36. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=HMPREF9452_00290 {ECO:0000313|EMBL:EGX67606.1}; OS Collinsella tanakaei YIT 12063. OC Bacteria; Actinobacteria; Coriobacteriia; Coriobacteriales; OC Coriobacteriaceae; Collinsella. OX NCBI_TaxID=742742 {ECO:0000313|EMBL:EGX67606.1, ECO:0000313|Proteomes:UP000004830}; RN [1] {ECO:0000313|EMBL:EGX67606.1, ECO:0000313|Proteomes:UP000004830} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=YIT 12063 {ECO:0000313|EMBL:EGX67606.1, RC ECO:0000313|Proteomes:UP000004830}; RG The Broad Institute Genome Sequencing Platform; RA Earl A., Ward D., Feldgarden M., Gevers D., Morotomi M., Young S.K., RA Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., RA Alvarado L., Arachchi H.M., Berlin A., Brown A., Chapman S.B., RA Chen Z., Dunbar C., Freedman E., Gearin G., Gellesch M., Goldberg J., RA Griggs A., Gujja S., Heiman D., Howarth C., Larson L., Lui A., RA MacDonald P.J.P., Mehta T., Montmayeur A., Murphy C., Neiman D., RA Pearson M., Priest M., Roberts A., Saif S., Shea T., Shenoy N., RA Sisk P., Stolte C., Sykes S., Wortman J., Nusbaum C., Birren B.; RT "The Genome Sequence of Collinsella tanakaei YIT 12063."; RL Submitted (JUN-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EGX67606.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADLS01000005; EGX67606.1; -; Genomic_DNA. DR EnsemblBacteria; EGX67606; EGX67606; HMPREF9452_00290. DR PATRIC; fig|742742.3.peg.284; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000004830; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000004830}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000004830}. FT DOMAIN 135 300 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 354 AA; 39198 MW; 9EC877828E2AF93D CRC64; MVHSLDIDVV IFDDELSPSQ QSYLEKAVGE PVKIIDRTAL ILDIFGLHAK TREGRLQVQL AQLQYLLPRL RGMWSHLAKE QTRGGIGSRF GQGESQLEVD RRLIRNKISA LRKQLRLVEK RRGVQSKDRL ESSAFRVALA GYTNAGKSTL LNRLTGADVF TQDKLFATLD PTTRAYALPG GRLITVTDTV GFIQKLPHGL VEAFKSTLSE VLNADLILKV VDISDDDWIR QMDAVESVLS EIGAGDKLSV TVFNKVDLLD PIELGILKSR YSDSIFFSAL TGEGIDSLTS RIANEASASD TVLSATIPYK EAALISLIRE QGQVVHEEFL GEGVRLIARV PSRIAPRIER YITE // ID G2DIJ0_9NEIS Unreviewed; 391 AA. AC G2DIJ0; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 1. DT 07-JUN-2017, entry version 34. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=l11_01830 {ECO:0000313|EMBL:EGV38736.1}; OS Neisseria weaveri LMG 5135. OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=1051985 {ECO:0000313|EMBL:EGV38736.1, ECO:0000313|Proteomes:UP000004938}; RN [1] {ECO:0000313|EMBL:EGV38736.1, ECO:0000313|Proteomes:UP000004938} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=LMG 5135 {ECO:0000313|EMBL:EGV38736.1}; RX PubMed=22188430; DOI=10.1111/j.1574-6968.2011.02485.x; RA Yi H., Cho Y.J., Yoon S.H., Park S.C., Chun J.; RT "Comparative genomics of Neisseria weaveri clarifies the taxonomy of RT this species and identifies genetic determinants that may be RT associated with virulence."; RL FEMS Microbiol. Lett. 328:100-105(2012). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EGV38736.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFWQ01000003; EGV38736.1; -; Genomic_DNA. DR RefSeq; WP_004282672.1; NZ_AFWQ01000003.1. DR EnsemblBacteria; EGV38736; EGV38736; l11_01830. DR PATRIC; fig|1051985.3.peg.184; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000004938; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000004938}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000004938}. FT DOMAIN 216 385 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 391 AA; 42614 MW; DAA2468162D96FFE CRC64; MAGPALFQVD KSLEKPERVM LVGVMLSADF SGANETRERS FQTALDEAAD LVRASGGDLV HIETAKRDKP HTALFVGTGK AEELADAVAR HEIELVVFNH ELTPTQERNL EKTLQCRVLD RVGLILAIFA RRAQSQEGKL QVELAQLTHL SGRLVRGYGH LKSQKGGIGL KGPGETQLET DRRLIGQKIT ALKKQLQNVQ KQRATRRKSR LSGALPTFAL VGYTNAGKSS LFNRLTKADV LAKDQLFATL DTTARRLYLS PEASVILTDT VGFVRDLPHK LVSAFSATLE ETALADVLLH VVDASNADFE RQMDDVNLVL KEIGADKVPQ LVVYNKIDLP SDLPRAPGIL RDAEGVAAAV NISVTEGLGL AQLREAVIER AVAVKLQNQS K // ID G2E5K1_9GAMM Unreviewed; 450 AA. AC G2E5K1; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 1. DT 07-JUN-2017, entry version 32. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=ThidrDRAFT_3564 {ECO:0000313|EMBL:EGV28670.1}; OS Thiorhodococcus drewsii AZ1. OC Bacteria; Proteobacteria; Gammaproteobacteria; Chromatiales; OC Chromatiaceae; Thiorhodococcus. OX NCBI_TaxID=765913 {ECO:0000313|EMBL:EGV28670.1, ECO:0000313|Proteomes:UP000004200}; RN [1] {ECO:0000313|EMBL:EGV28670.1, ECO:0000313|Proteomes:UP000004200} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=AZ1 {ECO:0000313|EMBL:EGV28670.1, RC ECO:0000313|Proteomes:UP000004200}; RG US DOE Joint Genome Institute (JGI-PGF); RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S., RA Peters L., Land M.L., Hauser L., Vogl K., Liu Z., Imhoff J., Thiel V., RA Frigaard N.-U., Bryant D.A., Woyke T.J.; RT "The draft genome of Thiorhodococcus drewsii AZ1."; RL Submitted (JUN-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EGV28670.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFWT01000032; EGV28670.1; -; Genomic_DNA. DR EnsemblBacteria; EGV28670; EGV28670; ThidrDRAFT_3564. DR PATRIC; fig|765913.3.peg.3633; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000004200; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR Gene3D; 3.40.50.1220; -; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR029035; DHS-like_NAD/FAD-binding_dom. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000004200}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000004200}. FT DOMAIN 219 386 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 450 AA; 49556 MW; 2BE929D417691E51 CRC64; MNEQPGTNST ATTPGRDATL VFERPKVGER AVLVHLDMGG GAAAPDEREE FRLLASAAGA EVLGTLGGSR SAPDSRLFIG SGKADELKMF VEANEADLVI FNHTLSPAQE RNLERLLQCR VLDRSGLILD IFAQRARSFE GKLQVELAQL RHLSTRLVRG WTHLERQKGG IGLRGPGETQ LETDRRLLGT RVAMLERRLS RIEGQRAQGR KARAKAELPV VSLVGYTNAG KSTLFNRLTQ AGVFQADQLF ATLDPTLRRL ELPTGDRVVV ADTVGFVSQL PHELVAAFRS TLEETRNAAL LLHVIDTAAP HRARLIEDVE DVLAEIGSHE IPRLEVFNKI DLLGEEAPRL ERDSEGRPIR VWLSAQSGLG IDLLLQALAE LTGGERVRSR IHLDPSEGKR RAWLYRHAQI LSDQAADTGG WDLELMIGRI DLDRLCAHDR ELGQRLGAAS // ID G2EH71_9FLAO Unreviewed; 403 AA. AC G2EH71; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 1. DT 07-JUN-2017, entry version 36. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=BZARG_458 {ECO:0000313|EMBL:EGV42187.1}; OS Bizionia argentinensis JUB59. OC Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales; OC Flavobacteriaceae; Bizionia. OX NCBI_TaxID=1046627 {ECO:0000313|EMBL:EGV42187.1, ECO:0000313|Proteomes:UP000003730}; RN [1] {ECO:0000313|EMBL:EGV42187.1, ECO:0000313|Proteomes:UP000003730} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=JUB59 {ECO:0000313|EMBL:EGV42187.1, RC ECO:0000313|Proteomes:UP000003730}; RX PubMed=18842857; DOI=10.1099/ijs.0.65599-0; RA Bercovich A., Vazquez S.C., Yankilevich P., Coria S.H., Foti M., RA Hernandez E., Vidal A., Ruberto L., Melo C., Marenssi S., RA Criscuolo M., Memoli M., Arguelles M., Mac Cormack W.P.; RT "Bizionia argentinensis sp. nov., isolated from surface marine water RT in Antarctica."; RL Int. J. Syst. Evol. Microbiol. 58:2363-2367(2008). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EGV42187.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFXZ01000067; EGV42187.1; -; Genomic_DNA. DR RefSeq; WP_008639619.1; NZ_AFXZ01000067.1. DR STRING; 1046627.BZARG_458; -. DR EnsemblBacteria; EGV42187; EGV42187; BZARG_458. DR PATRIC; fig|1046627.3.peg.2848; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000003730; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000003730}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000003730}. FT DOMAIN 200 385 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 403 AA; 46628 MW; 17D5ADCE7221FBD9 CRC64; MIEKVDISHE RAVLIGVVTK NQGEEQSKEY LDELEFLTFT AGGEVIKRFT QKMDIPNPKT FIGTGKMEEV RQFIEDNDIG TAIFDDELSA AQERNISKIL ECKVLDRTNL ILDIFAQRAQ TSYARTQVEL AQCEYLLPRL KGMWTHLERQ RGGIGMRGPG ETEIETDRRI VRDRISLLKD KIKVIDKQMG VQRGNRGKMV RVALVGYTNV GKSTLMNTIS KSDVFAEDKL FATLDTTVRK VVIQNLPFLL TDTVGFIRKL PTQLVDSFKS TLDEVREADL LLHVVDISHH NFEEQINSVN KILGEIDSGD KPTIMVFNKI DAYKAEPYDE TDLEVERTEL HYSLEEWRKT WMNRVGDNAL FISALNKQNM EEFKKRIYDE VREIHVTRFP YNNFLYPDYE EEE // ID G2FJ98_9GAMM Unreviewed; 427 AA. AC G2FJ98; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 1. DT 07-JUN-2017, entry version 36. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:EGW53139.1}; GN ORFNames=TevJSym_bl00190 {ECO:0000313|EMBL:EGW53139.1}; OS endosymbiont of Tevnia jerichonana (vent Tica). OC Bacteria; Proteobacteria; Gammaproteobacteria; OC sulfur-oxidizing symbionts. OX NCBI_TaxID=1049564 {ECO:0000313|EMBL:EGW53139.1, ECO:0000313|Proteomes:UP000005167}; RN [1] {ECO:0000313|EMBL:EGW53139.1, ECO:0000313|Proteomes:UP000005167} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Gardebrecht A., Markert S., Felbeck H., Thuermer A., Albrecht D., RA Wollherr A., Kabisch J., Lehmann R., Daniel R., Liesegang H., RA Hecker M., Sievert S.M., Schweder T.; RT "The endosymbionts of the deep-sea tubeworms Riftia pachyptila and RT Tevnia jerichonana share an identical physiology as revealed by RT proteogenomic analyses."; RL ISME J. 0:0-0(2011). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EGW53139.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFZB01000038; EGW53139.1; -; Genomic_DNA. DR RefSeq; WP_005961351.1; NZ_AFZB01000038.1. DR EnsemblBacteria; EGW53139; EGW53139; TevJSym_bl00190. DR PATRIC; fig|1049564.3.peg.2979; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000005167; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000005167}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000005167}. FT DOMAIN 198 365 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 157 191 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 427 AA; 47923 MW; 8EB799FFFD0B625F CRC64; MFERPKSGER AILVHLDLGR VSDPEEIEEF SDLALSAGAQ PVAMVGGSRS HPDPRLFVGR GKSEEIRQQV EAEAAELVIF DHTLSPSQER NLEREFKCRV IDRTGLILDI FAQRARSFEG KLQVELAQLR HLSTRLVRGW THLERQKGGI GLRGPGETQL ETDRRLLNQR IEQIRKRLAK VEMQREQGRR SRAKADVPTV SLVGYTNAGK STLFNTLVGS GVYVADQLFA TLDPTLRRLQ LKGEGAVVLA DTVGFISKLP HDLVAAFKST LQETTEASLL LHVIDVASHQ REHCIAEVND VLQQIGAHEI DQIEIYNKID LQEGAASRLE RDENGRIRRV WLSARSGEGI GLLRQALTEF FRRNHVQKGV RLQAGDGRLR SLLYNRSDVL ADTGCDDGGW EMQVDMAELE FERLLKEVPE LKGRLIG // ID G2FQ96_9FIRM Unreviewed; 535 AA. AC G2FQ96; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 1. DT 07-JUN-2017, entry version 34. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:EGW40258.1}; GN ORFNames=DOT_1903 {ECO:0000313|EMBL:EGW40258.1}; OS Desulfosporosinus sp. OT. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Peptococcaceae; OC Desulfosporosinus. OX NCBI_TaxID=913865 {ECO:0000313|EMBL:EGW40258.1, ECO:0000313|Proteomes:UP000004928}; RN [1] {ECO:0000313|EMBL:EGW40258.1, ECO:0000313|Proteomes:UP000004928} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=OT {ECO:0000313|EMBL:EGW40258.1, RC ECO:0000313|Proteomes:UP000004928}; RX PubMed=21994931; DOI=10.1128/JB.06018-11; RA Abicht H.K., Mancini S., Karnachuk O.V., Solioz M.; RT "Genome Sequence of Desulfosporosinus sp. OT, an Acidophilic Sulfate- RT Reducing Bacterium from Copper Mining Waste in Norilsk, Northern RT Siberia."; RL J. Bacteriol. 193:6104-6105(2011). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EGW40258.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGAF01000085; EGW40258.1; -; Genomic_DNA. DR EnsemblBacteria; EGW40258; EGW40258; DOT_1903. DR PATRIC; fig|913865.3.peg.1720; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000004928; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000004928}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000004928}. FT DOMAIN 366 535 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 535 AA; 59532 MW; 2EC8D9A242A44749 CRC64; MDMDISGDLA GIRASQIQEL KNLSEFGTER SELIHPEILD RLIYLTQLWN REIALYLSRP GTLLAAAVGR HATVTLPPIK GRSVSKHLRC IHTHPNGDYR LSPLDYSALD SLQLESMSAV GVRDGKLTGI QIAYRTGESD PYIVNLSPET WHSFDYNESL ANFSRGATKK QSASGKERAF LIALEDSEQE TNEDLTELRE LARSAGVDVV GQLVQLRRYG QSRSYLGSGK LEELVHRLQE TEANVVICDD ELSPTQLRTL ETETGLKVLD RTGLILDIFA QRAQSREGKL QVELAQLKHL LPYLSGQGQA LSRLGGGVGS RGPGETKLEL DRRRMRDRIT LLEKELKLVL QHRDVQRKQR TKSGLPIIAL VGYTNAGKTT FMKKAMEQAG SRSDIPIGEN KLFATLDPIV RSIRVNSSLE ILLSDTVGFI RKLPTQLLRA FLATLEEVQQ ADVLLHVVDA SHPQALQHAE TVHEVLKQLG CQDKPIITLL NKVDKVLGED DLTELSQSLP YPIEISLKRG DSLKQVWKLL SSVLA // ID G2G5M6_9ACTN Unreviewed; 470 AA. AC G2G5M6; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 1. DT 07-JUN-2017, entry version 36. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=SZN_03899 {ECO:0000313|EMBL:EGX61193.1}; OS Streptomyces zinciresistens K42. OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae; OC Streptomyces. OX NCBI_TaxID=700597 {ECO:0000313|EMBL:EGX61193.1, ECO:0000313|Proteomes:UP000004217}; RN [1] {ECO:0000313|EMBL:EGX61193.1, ECO:0000313|Proteomes:UP000004217} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K42 {ECO:0000313|EMBL:EGX61193.1, RC ECO:0000313|Proteomes:UP000004217}; RA Lin Y., Hao X., Johnstone L., Miller S.J., Wei G., Rensing C.; RL Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EGX61193.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGBF01000006; EGX61193.1; -; Genomic_DNA. DR EnsemblBacteria; EGX61193; EGX61193; SZN_03899. DR PATRIC; fig|700597.3.peg.757; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000004217; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000004217}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000004217}. FT DOMAIN 248 413 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 470 AA; 51288 MW; DF27A7516011A061 CRC64; MEEDVAWSHE IDGERDGHQF DRSDRAALRR VAGLSTELED VTEVEYRQLR LERVVLVGVW TSGTSQDADN SLAELAALAE TAGALVLDGV IQRRDKPDAA TYIGSGKAQE LRDIVLESGA DTVICDGELS PGQLIHLEDV VKVKVIDRTA LILDIFAQHA KSREGKAQVA LAQMQYMLPR LRGWGQSLSR QMGGGKGGGL ATRGPGETKI ETDRRRIREK MAKMRREIAE MKTGRDIQRQ VRRRNKVPSV AIAGYTNAGK SSLLNRLTGA GVLVENALFA TLDPTVRRAE TPGGRLYTLA DTVGFVRHLP HHLVEAFRST MEEVGDSDLI LHVVDGAHPN PEEQLAAVRE VIRDVGATGV PEIVVINKAD AADPLTLQRL LRIEKRALAV SARTGQGIDE LLALIDNELP RPSVEIEALV PYTHGKLVAR AHTEGEVISE EHTPEGTLLK VRVHEELAAD LAPYVPTATA // ID G2GZL1_9ENTR Unreviewed; 432 AA. AC G2GZL1; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 1. DT 30-AUG-2017, entry version 35. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=Rin_00012340 {ECO:0000313|EMBL:EGY28818.1}; OS Candidatus Regiella insecticola 5.15. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; OC Enterobacteriaceae; aphid secondary symbionts; Candidatus Regiella. OX NCBI_TaxID=1005043 {ECO:0000313|EMBL:EGY28818.1, ECO:0000313|Proteomes:UP000004116}; RN [1] {ECO:0000313|EMBL:EGY28818.1, ECO:0000313|Proteomes:UP000004116} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=R5.15 {ECO:0000313|Proteomes:UP000004116}; RX PubMed=21948522; DOI=10.1101/gr.125351.111; RA Hansen A.K., Vorburger C., Moran N.A.; RT "Genomic basis of endosymbiont-conferred protection against an insect RT parasitoid."; RL Genome Res. 22:106-114(2012). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EGY28818.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGCA01000304; EGY28818.1; -; Genomic_DNA. DR RefSeq; WP_006706898.1; NZ_AGCA01000304.1. DR EnsemblBacteria; EGY28818; EGY28818; Rin_00012340. DR PATRIC; fig|1005043.3.peg.1121; -. DR Proteomes; UP000004116; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000004116}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000004116}. FT DOMAIN 203 370 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 432 AA; 48316 MW; 157F06FFFE3B5164 CRC64; MFDRYEVGEQ SVLVHISFSP YPDASNKNNE DLQEFESLVF SAGVEVLKTV TGSRNAPDAK YFVGKGKAEE IADTVKTMGA SVVLFNHALS PAQERNLERL CQCRVIDRTG LILDIFAQRA RTHEGKLQVE LAQLRHLATR LVRGWTHLER QKGGIGLRGP GETQLETDRR LLSKRISLIL SRLERVAKQR EQGRQARCRA QIPTVSLIGY TNAGKSSLFN SMTAADVYTA DQLFATLDPT LRGIYVTDVG DAVLADTVGF IRHLPHDLVV AFKATLQETR QASLLLHVID ASDPRVDENI TAVDAVLAEI AADEIPRLLV MNKIDRLADF TPRIDRNEEN TPVRVWLSAQ TGAGVPLLFQ ALTECLGGEI AQYELDLPPQ EGRLISRFYQ LKAIEKVWPI TESGHIGMRV RMPVAKWQRL CKKEKKLVNY IV // ID G2ISV8_9SPHN Unreviewed; 439 AA. AC G2ISV8; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 1. DT 12-APR-2017, entry version 38. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:BAK66468.1}; GN ORFNames=SLG_17930 {ECO:0000313|EMBL:BAK66468.1}; OS Sphingobium sp. SYK-6. OC Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales; OC Sphingomonadaceae; Sphingobium. OX NCBI_TaxID=627192 {ECO:0000313|EMBL:BAK66468.1, ECO:0000313|Proteomes:UP000001275}; RN [1] {ECO:0000313|EMBL:BAK66468.1, ECO:0000313|Proteomes:UP000001275} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SYK-6 {ECO:0000313|EMBL:BAK66468.1, RC ECO:0000313|Proteomes:UP000001275}; RX PubMed=22207743; DOI=10.1128/JB.06254-11; RA Masai E., Kamimura N., Kasai D., Oguchi A., Ankai A., Fukui S., RA Takahashi M., Yashiro I., Sasaki H., Harada T., Nakamura S., RA Katano Y., Narita-Yamada S., Nakazawa H., Hara H., Katayama Y., RA Fukuda M., Yamazaki S., Fujita N.; RT "Complete genome sequence of Sphingobium sp. strain SYK-6, a degrader RT of lignin-derived biaryls and monoaryls."; RL J. Bacteriol. 194:534-535(2012). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AP012222; BAK66468.1; -; Genomic_DNA. DR STRING; 627192.SLG_17930; -. DR EnsemblBacteria; BAK66468; BAK66468; SLG_17930. DR KEGG; ssy:SLG_17930; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR KO; K03665; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000001275; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000001275}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000001275}. FT DOMAIN 189 381 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 439 AA; 47718 MW; CFF82506C3286790 CRC64; MHADLGGRQR RDVSARLEEA RGLALAIGLD VVETGVWRVR QSRPAALFGS GQVEEIGALV AQAEAELVVV DNNLTPVQQS NLEKAWSAKV IDRTGLILEI FGERAATAEG RLQVELAHLD YQAGRLVRSW THLERQRGGF GFLGGPGETQ IEADRRMIRD RMARIRRELD QVTRTRGLHR ARRQRAPWPV IALVGYTNAG KSTLFNRLTG ADVMAQDMLF ATLDPTMRQI SLPGIDKAIL SDTVGFVSDL PHQLIAAFRA TLEEVLSADL ILHVRDIAHP DTEAQKADVL DVLADLGAAP ADEDGSAGKA EAPDAAHEGG GPVAPIIEIW NKADLIEDPE RLAAVRARAE QEGNVAIVSA LTGEGVDALR RMLSDILAKG HRRYEITLDG GDGAALAWLH AHGDVLLEEH DTSGETATVH VSVRMAPADH ERFLRLHSN // ID G2IXJ1_PSEUL Unreviewed; 378 AA. AC G2IXJ1; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 1. DT 07-JUN-2017, entry version 37. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=NH8B_3151 {ECO:0000313|EMBL:BAK77924.1}; OS Pseudogulbenkiania sp. (strain NH8B). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Chromobacteriaceae; Pseudogulbenkiania. OX NCBI_TaxID=748280 {ECO:0000313|EMBL:BAK77924.1, ECO:0000313|Proteomes:UP000001274}; RN [1] {ECO:0000313|Proteomes:UP000001274} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NH8B {ECO:0000313|Proteomes:UP000001274}; RX PubMed=22038961; DOI=10.1128/JB.06127-11; RA Ishii S., Tago T., Nishizawa T., Oshima K., Hattori M., Senoo K.; RT "Complete genome sequence of the denitrifying and N(2)O-reducing RT bacterium Pseudogulbenkiania sp. strain NH8B."; RL J. Bacteriol. 193:6395-6396(2011). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AP012224; BAK77924.1; -; Genomic_DNA. DR RefSeq; WP_014088085.1; NC_016002.1. DR EnsemblBacteria; BAK77924; BAK77924; NH8B_3151. DR KEGG; pse:NH8B_3151; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000001274; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000001274}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000001274}. FT DOMAIN 198 364 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 378 AA; 41937 MW; C04488223F47D431 CRC64; MFDRPDLGDQ AIIVCLDFGD PDFQENVDEC VDLVKSAGVE VLGLIHGKRQ RPDAALFAGK GKVEEIAALV RATSANVVIF NHQLSPGQER NIERVLQCRV IDRSSLILDI FAQRARSHEG KLQVELAQLS HLATRLVRGW THLERQKGGI GLRGPGETQL ETDRRLLGNR VKLLKTRLEQ VQKQRKTQRR GRLRNGIASV SIVGYTNAGK STLFNALTKA KSYAADQLFA TLDTTSRKLY LNEQASIVVS DTVGFIRDLP HTLVAAFRAT LEETVQADLL LHVVDSANPM RDMQIEEVNR VLEEIGADEI PQLIVWNKSD LRGLEPLIER DADNLPQAVR VSALTGDGLE LLREALAERV QLLAPPHPSE DRNNNVAA // ID G2J5B3_PSEUL Unreviewed; 462 AA. AC G2J5B3; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 1. DT 07-JUN-2017, entry version 35. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=NH8B_2444 {ECO:0000313|EMBL:BAK77258.1}; OS Pseudogulbenkiania sp. (strain NH8B). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Chromobacteriaceae; Pseudogulbenkiania. OX NCBI_TaxID=748280 {ECO:0000313|EMBL:BAK77258.1, ECO:0000313|Proteomes:UP000001274}; RN [1] {ECO:0000313|Proteomes:UP000001274} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NH8B {ECO:0000313|Proteomes:UP000001274}; RX PubMed=22038961; DOI=10.1128/JB.06127-11; RA Ishii S., Tago T., Nishizawa T., Oshima K., Hattori M., Senoo K.; RT "Complete genome sequence of the denitrifying and N(2)O-reducing RT bacterium Pseudogulbenkiania sp. strain NH8B."; RL J. Bacteriol. 193:6395-6396(2011). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AP012224; BAK77258.1; -; Genomic_DNA. DR RefSeq; WP_014087508.1; NC_016002.1. DR EnsemblBacteria; BAK77258; BAK77258; NH8B_2444. DR KEGG; pse:NH8B_2444; -. DR KO; K03665; -. DR OMA; VILEIFH; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000001274; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000001274}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000001274}. FT DOMAIN 226 396 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 189 221 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 462 AA; 51934 MW; 50C78EA49240FFA5 CRC64; MQTEVKEKPR YALVTSVQLP DVSDSEFEAS LNELSELAKT LGFQVMQTFV QKRNSFDRTA YLGVGKLEEI SMFVNRGIRN DELEEDPQEL DSSTVEFDVL LVDHEISPSQ ARNLELAVGC EVMDRTMVIL EIFHRNARSR AARAQVEIAR LGYMAPRLRE AAKLAGPQGR QRSGTGGRGA GESHTELDRR KVRDRIAELQ REIIAMELER KTQRARRLER QGLGLGGVSL VGYTNAGKST LMRALTGSEV LVANKLFATL DTTVRALYPE SVPRVLVSDT VGFIKNLPHG LVASFKSTLE EALDAALLLH VIDASDPGFQ RQLDVTDEVL QEIGADDVPR IRVFNKIDHV GDEAEQAAWT AELQERYPGC VVMSARRPEE VASLHATIVS FFQQDLVEDE LLLPWSAQQL RGEIYSHCQV LEERAEEEGS WFRVRGEPEK LRSLHEQLNP GLQGREKEYW EV // ID G2JA96_9BURK Unreviewed; 365 AA. AC G2JA96; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 1. DT 12-APR-2017, entry version 33. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:CCD29697.1}; GN ORFNames=CAGGBEG34_280042 {ECO:0000313|EMBL:CCD29697.1}; OS Candidatus Glomeribacter gigasporarum BEG34. OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Candidatus Glomeribacter. OX NCBI_TaxID=1070319 {ECO:0000313|EMBL:CCD29697.1, ECO:0000313|Proteomes:UP000054051}; RN [1] {ECO:0000313|EMBL:CCD29697.1, ECO:0000313|Proteomes:UP000054051} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BEG34 {ECO:0000313|EMBL:CCD29697.1, RC ECO:0000313|Proteomes:UP000054051}; RA Ghignone S., Salvioli A., Anca I., Lumini E., Ortu G., Petiti L., RA Cruveiller S., Bianciotto V., Piffanelli P., Lanfranco L., RA Bonfante P.; RT "The genome of the obligate endobacterium of an arbuscular mycorrhizal RT fungus reveals an interphylum network of nutritional interactions."; RL Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:CCD29697.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CAFB01000045; CCD29697.1; -; Genomic_DNA. DR EnsemblBacteria; CCD29697; CCD29697; CAGGBEG34_280042. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000054051; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000054051}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000054051}. FT DOMAIN 191 364 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 365 AA; 40241 MW; D3952D8B7BB8FE31 CRC64; MINAALVGID FGTGGFQASL DELRLLARSA GAIPAALITA RRRAPDAALF LPGGKTDELK SALGLQNIDL VIFNHALTPA QQRNLEYRLE RRVVDRTTLI LDIFAQRARS HEGKCQVELA QLHYLKTRLV RAWTHLERQK GGIGLRGPGE TQLETDRRLI GERIKTLKAR LDRLHRQRRT QRRRRVRNAV FSVSLVGYTN AGKSTLFNAL TRAQAYCADQ LFATLDTTSR RFYLSDATQG VLSDTVGFIQ DLPHELVAAF RATLEEMVHA DLLLHVVDAS NPARREQAEQ VQQVLSALDA ADIPQILVWN KMDAVPEAVP ELASSGAAER DAHGRIRRVF LSARTGQGLG ALRGAMAEAV ATAPL // ID G2KRN7_MICAA Unreviewed; 440 AA. AC G2KRN7; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 1. DT 07-JUN-2017, entry version 37. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:AEP09599.1}; GN OrderedLocusNames=MICA_1277 {ECO:0000313|EMBL:AEP09599.1}; OS Micavibrio aeruginosavorus (strain ARL-13). OC Bacteria; Proteobacteria; Alphaproteobacteria; Micavibrio. OX NCBI_TaxID=856793 {ECO:0000313|EMBL:AEP09599.1, ECO:0000313|Proteomes:UP000009286}; RN [1] {ECO:0000313|EMBL:AEP09599.1, ECO:0000313|Proteomes:UP000009286} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ARL-13 {ECO:0000313|EMBL:AEP09599.1, RC ECO:0000313|Proteomes:UP000009286}; RX PubMed=21936919; DOI=10.1186/1471-2164-12-453; RA Wang Z., Kadouri D., Wu M.; RT "Genomic insights into an obligate epibiotic bacterial predator: RT Micavibrio aeruginosavorus ARL-13."; RL BMC Genomics 12:453-453(2011). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002382; AEP09599.1; -; Genomic_DNA. DR RefSeq; WP_014102822.1; NC_016026.1. DR STRING; 856793.MICA_1277; -. DR EnsemblBacteria; AEP09599; AEP09599; MICA_1277. DR KEGG; mai:MICA_1277; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000009286; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000009286}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000009286}. FT DOMAIN 210 382 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 440 AA; 49149 MW; 0C48F95CFCE4306B CRC64; MSDSQQTPDD EGPGTAIVLH PTLPGSFARH DRDPEDALEE AVGLIHAIFM DVCESRVVPV RKIDAGALFG KGTREMIAAQ VEVMKPDVVF VNHALSPVQQ RNLEQEWKVK VIDRTGLILE IFGARAQTRE GKIQVQLAAL EYQKSRLVKS WSHLERQRGG MGKTGGPGET QLEIDRRLVT DRITQLKRDL EQISRTRDLQ RKGREKVPFP VVSLVGYTNA GKSTLFNRLT GANVFAEDLP FATLDPTMRR VKLEDGNEII LADTVGFIAD LPTHLVASFR ATLEQVQYAD VIIHVRDMSR HDRAAQKNDV VSILHDLGIE YASDRRVVEV LNKMDAIAEE NRPGILREAR EHVENTAAIS ALTGEGIDDL MQMISRMLAH GRNIVTYHLH PAEGEALAWL YARCNIIERI DGEDAMIAMR VEIDPADQGR FAERFGKHAA // ID G2KTG3_LACSM Unreviewed; 425 AA. AC G2KTG3; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 1. DT 07-JUN-2017, entry version 38. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=LSA_03240 {ECO:0000313|EMBL:AEN98779.1}; OS Lactobacillus sanfranciscensis (strain TMW 1.1304). OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; OC Lactobacillus. OX NCBI_TaxID=714313 {ECO:0000313|EMBL:AEN98779.1, ECO:0000313|Proteomes:UP000001285}; RN [1] {ECO:0000313|EMBL:AEN98779.1, ECO:0000313|Proteomes:UP000001285} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=TMW 1.1304 {ECO:0000313|EMBL:AEN98779.1, RC ECO:0000313|Proteomes:UP000001285}; RX PubMed=21995419; DOI=10.1186/1475-2859-10-S1-S6; RA Vogel R.F., Pavlovic M., Ehrmann M.A., Wiezer A., Liesegang H., RA Offschanka S., Voget S., Angelov A., Bocker G., Liebl W.; RT "Genomic analysis reveals Lactobacillus sanfranciscensis as stable RT element in traditional sourdoughs."; RL Microb. Cell Fact. 10:S6-S6(2011). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002461; AEN98779.1; -; Genomic_DNA. DR STRING; 714313.LSA_03240; -. DR EnsemblBacteria; AEN98779; AEN98779; LSA_03240. DR KEGG; lsn:LSA_03240; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR KO; K03665; -. DR OMA; FNNHAHV; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000001285; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000001285}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000001285}. FT DOMAIN 202 370 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 425 AA; 47797 MW; 911FBE8AB23F58EF CRC64; MRSTMEKTTT PVITIGLNVN NQAFDYSMEE LKNLVMANNM ENVETVTQKL DHPDSRAYFG KGKIEYLAQL VTTTGAQVIV ANDELSPSQI RNIENETNAT VIDRTGLILE IFANRAQTRE AKLQVQMAKL KYQLPRLRTS ASQRLDQQSA GGGLANRGAG ETKLELNRRT IEHQIDHVRH ELKEIDKAYE TQSKRRKENK IPTVALIGYT NAGKSTIMNQ LVTKFGENDE KQVFVKNMLF ATLDTSVRDL HLPDHKQFLL SDTVGFVSNL PHQLVQAFKS TLAEAASANL LVQVVDYSDP DQQLMMETTE TTLKEIGVPD LPMIKVFNKA DLAGTNYPTR EGDNLIISAL DDQSIELLTS VISEKLFKNY VTKTFLFPFD KGDLVSTLNH KFNVQSTDYT EDGTKLTVEL PEPDVARYSQ YLDKD // ID G2LJ34_CHLTF Unreviewed; 573 AA. AC G2LJ34; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 1. DT 07-JUN-2017, entry version 40. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Cabther_A2057 {ECO:0000313|EMBL:AEP12802.1}; OS Chloracidobacterium thermophilum (strain B). OC Bacteria; Acidobacteria; Blastocatellia; Chloracidobacterium. OX NCBI_TaxID=981222 {ECO:0000313|EMBL:AEP12802.1, ECO:0000313|Proteomes:UP000006791}; RN [1] {ECO:0000313|EMBL:AEP12802.1, ECO:0000313|Proteomes:UP000006791} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=B {ECO:0000313|EMBL:AEP12802.1, RC ECO:0000313|Proteomes:UP000006791}; RX PubMed=21951563; DOI=10.1111/j.1462-2920.2011.02592.x; RA Garcia Costas A.M., Liu Z., Tomsho L.P., Schuster S.C., Ward D.M., RA Bryant D.A.; RT "Complete genome of Candidatus Chloracidobacterium thermophilum, a RT chlorophyll-based photoheterotroph belonging to the phylum RT Acidobacteria."; RL Environ. Microbiol. 14:177-190(2012). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002514; AEP12802.1; -; Genomic_DNA. DR RefSeq; WP_014100539.1; NC_016024.1. DR STRING; 981222.Cabther_A2057; -. DR EnsemblBacteria; AEP12802; AEP12802; Cabther_A2057. DR KEGG; ctm:Cabther_A2057; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR KO; K03665; -. DR OMA; EREVIIT; -. DR Proteomes; UP000006791; Chromosome 1. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000006791}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000006791}. FT DOMAIN 385 573 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 344 371 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 573 AA; 63455 MW; 88D8B8A2830B837D CRC64; MPISKVEGNT QGLKSSQVKR LERLLARRVP PRDIITPELA RQMTELSAEI RRQVGVLISR HGQVECVMVG DAGGIVIPDL KRVRVGQGRF RGLRCLHTQL SGPGLTRDDL NDLALLRLDL MGVISVGDNG LPNWIHAAHL LPATDAVTDD TAEPWAYLDK VHPSQLQVDF LDLIEYLEAE FARTRRLRDA RDLRDRAMLV VVTTGALADA EASMEELVEL AESCDLVVVD KLIQRRRELD PKTLLGKGKL QEVIIRSLQH AADVLLFDQD LSPAQVRTIE AATDLKILDR TQLILDIFAQ RARSREGKVQ VELAQLKYLL PRLAGHGADM SRLAGGIGAR GPGETKLEVD RRRARDRIAD LEKLITSLRS QRQTRRAQRD RQQLPVVSIV GYTNAGKSTL LNTLTSSEVV AERRMFATLD PTSRRLRLPR DRDIIINDTV GFIRDLPPTL MAAFKATLEE IETSDLLLHL VDIAAPDYER RIAAVEDILA QLGLSHLPRQ LVFNKADLLP AEQVAALCVR HQAIAIVAYD RATLPPLLQS IDAWLSSPGN REAGVGAGYA PWEPVGNASV LVS // ID G2MI22_9ARCH Unreviewed; 416 AA. AC G2MI22; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 1. DT 12-APR-2017, entry version 24. DE SubName: Full=GTP-binding proten HflX {ECO:0000313|EMBL:AEN07133.1}; GN ORFNames=Halar_3539 {ECO:0000313|EMBL:AEN07133.1}; OS halophilic archaeon DL31. OC Archaea. OX NCBI_TaxID=756883 {ECO:0000313|EMBL:AEN07133.1, ECO:0000313|Proteomes:UP000010096}; RN [1] {ECO:0000313|EMBL:AEN07133.1, ECO:0000313|Proteomes:UP000010096} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DL31 {ECO:0000313|EMBL:AEN07133.1, RC ECO:0000313|Proteomes:UP000010096}; RG US DOE Joint Genome Institute; RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S., RA Peters L., Mikhailova N., Teshima H., Detter J.C., Han C., Tapia R., RA Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., RA Dyall-Smith M., Cavicchioli R., Woyke T.; RT "Complete sequence of chromosome of halophilic archaeon DL31."; RL Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002988; AEN07133.1; -; Genomic_DNA. DR STRING; 756883.Halar_3539; -. DR EnsemblBacteria; AEN07133; AEN07133; Halar_3539. DR KEGG; hah:Halar_3539; -. DR eggNOG; arCOG00353; Archaea. DR eggNOG; COG2262; LUCA. DR KO; K03665; -. DR OrthoDB; POG093Z07D6; -. DR BioCyc; HARC756883:GJDQ-2694-MONOMER; -. DR Proteomes; UP000010096; Chromosome. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 4: Predicted; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000010096}; KW Reference proteome {ECO:0000313|Proteomes:UP000010096}. FT DOMAIN 174 358 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 133 160 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 416 AA; 45114 MW; DF11E3798C048A3E CRC64; MARDAEQQPE TDEIRRLADV AGYAVVSELT QRRREDPTYN VGRGKAEALS RRVAATAADA VLFDAELTPG QYRDLVGLLP DGTSVIDRHR LVLDIFERGT GDKAARLQVE LAKLRYGLPR VQEIEERTHM QEAAETGSQL VDLEKRIRVV ENKLDRVTDR AAERRADRRE AGFGLVAIAG YTNAGKSTLL HRLADDLSVQ EADPGHGDLS GSAAVADQLF ETLETTTRRA TIDGRRILLT DTVGLVDGLP HDLVASFSAT LSAVADSDIG LLVVDASDPL DRVREKLWVS LGELNQPRGR LVAVLNKTDL LDGADVAARV DAVAAEAAVD TVVPVSAMDG TGVERLQSAI IDGLPGRSEQ FDLPNTGETQ AFLAWAHDQG RVETSYEGQR VTVRFEASPQ VIERAEARVA SLRGTD // ID G2MIM2_9ARCH Unreviewed; 440 AA. AC G2MIM2; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 1. DT 05-JUL-2017, entry version 38. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=Halar_1040 {ECO:0000313|EMBL:AEN04803.1}; OS halophilic archaeon DL31. OC Archaea. OX NCBI_TaxID=756883 {ECO:0000313|EMBL:AEN04803.1, ECO:0000313|Proteomes:UP000010096}; RN [1] {ECO:0000313|EMBL:AEN04803.1, ECO:0000313|Proteomes:UP000010096} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DL31 {ECO:0000313|EMBL:AEN04803.1, RC ECO:0000313|Proteomes:UP000010096}; RG US DOE Joint Genome Institute; RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S., RA Peters L., Mikhailova N., Teshima H., Detter J.C., Han C., Tapia R., RA Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., RA Dyall-Smith M., Cavicchioli R., Woyke T.; RT "Complete sequence of chromosome of halophilic archaeon DL31."; RL Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002988; AEN04803.1; -; Genomic_DNA. DR RefSeq; WP_014050584.1; NC_015954.1. DR STRING; 756883.Halar_1040; -. DR EnsemblBacteria; AEN04803; AEN04803; Halar_1040. DR GeneID; 11094384; -. DR KEGG; hah:Halar_1040; -. DR eggNOG; arCOG00353; Archaea. DR eggNOG; COG2262; LUCA. DR KO; K03665; -. DR OrthoDB; POG093Z07D6; -. DR Proteomes; UP000010096; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000010096}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000010096}. FT DOMAIN 189 372 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 105 132 {ECO:0000256|SAM:Coils}. FT COILED 155 185 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 440 AA; 48993 MW; 72FBA040B298C5EF CRC64; MPEQRAVVAK RVDAGDADLS EIRELARAAG YEVVGELSQS RTQDAAFNFG EGKADELAAL ARETRADTVI VDNELGAYQT FNIGEKLPEG AEVVDRFALI LDIFGQRAQT RKAQLQVELA ELRYELPRAE AKASLAKRDE RPGFMGLGEY DESREQDIKN QISRISEELD RIAEEEEKRR AKRRDQGFDL VALAGYTNAG KSTLLRRLAA ELDVDENEER HPDLEKTAES EDRLFTTLDT TTRKADTGTR EILLTDTVGF VSDLPHWLVE SFQSTLSSVY HADLVLLVVD ASDPVDEMRE KLVTSHDTLM DRNEAPIVTV FNKADKSTEP ELERRKRALS ALAPDPIVVS GLTGENVGDL RARVERELPA WERERLVLPV CDDAMSLVSW IHDNGHVREE NYGDEQVIVE FEAPPVVVSK ARAKAAEAEP AGADAGRREA // ID G2NPQ0_STREK Unreviewed; 506 AA. AC G2NPQ0; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 1. DT 07-JUN-2017, entry version 42. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=SACTE_4958 {ECO:0000313|EMBL:AEN12784.1}; OS Streptomyces sp. (strain SirexAA-E / ActE). OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae; OC Streptomyces. OX NCBI_TaxID=862751 {ECO:0000313|EMBL:AEN12784.1, ECO:0000313|Proteomes:UP000001397}; RN [1] {ECO:0000313|EMBL:AEN12784.1, ECO:0000313|Proteomes:UP000001397} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SirexAA-E / ActE {ECO:0000313|Proteomes:UP000001397}; RG US DOE Joint Genome Institute; RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S., RA Peters L., Ovchinnikova G., Davenport K., Detter J.C., Han C., RA Tapia R., Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., RA Adams A., Raffa K., Adams S., Book A., Currie C., Woyke T.; RT "Complete sequence of Streptomyces sp. SirexAA-E."; RL Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002993; AEN12784.1; -; Genomic_DNA. DR RefSeq; WP_014048735.1; NC_015953.1. DR ProteinModelPortal; G2NPQ0; -. DR STRING; 862751.SACTE_4958; -. DR EnsemblBacteria; AEN12784; AEN12784; SACTE_4958. DR KEGG; ssx:SACTE_4958; -. DR PATRIC; fig|862751.12.peg.5142; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR KO; K03665; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000001397; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 2. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000001397}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000001397}. FT DOMAIN 285 450 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 506 AA; 54872 MW; C38E36F68FFC7775 CRC64; MTSSSSLPQD ARDAQSATDT ASESLTESLR ADALMEEDVA WSHAIDTERD GEQLDRSERA ALRRVAGLST ELEDVTEVEY RQLRLERVVL VGVWTSGTVT DAQNSLAELA ALAETAGAMV LDAVFQRRDK PDPATYIGSG KALELRDIVL ESGADTVVCD GELSPGQLIH LEDVVKVKVV DRTALILDIF AQHAKSREGK AQVSLAQMQY MLPRLRGWGQ SLSRQMGGGG SSGGGGMATR GPGETKIETD RRRIREKMAK MRREIAEMKT GREIKRQERK RNKVPSVAIA GYTNAGKSSL LNRLTGAGVL VENALFATLD PTVRRAETPS GRLYTLADTV GFVRHLPHHL VEAFRSTMEE VGDSDLILHV VDGAHPVPEE QLAAVREVIR DVGAVDVREI VVVNKADAAD PEVLQRLLRN EKYAIAVSAR TGAGIDELLA LIDAELPRPS VEIEALVPYV QGALVSRVHA EGEVVSEEHT SEGTLLKARV HEELAAELST FALAAH // ID G2NYE0_STRVO Unreviewed; 500 AA. AC G2NYE0; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 1. DT 05-JUL-2017, entry version 43. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=Strvi_2123 {ECO:0000313|EMBL:AEM81855.1}; OS Streptomyces violaceusniger Tu 4113. OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae; OC Streptomyces. OX NCBI_TaxID=653045 {ECO:0000313|EMBL:AEM81855.1, ECO:0000313|Proteomes:UP000008703}; RN [1] {ECO:0000313|EMBL:AEM81855.1, ECO:0000313|Proteomes:UP000008703} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Tu 4133 {ECO:0000313|Proteomes:UP000008703}; RG US DOE Joint Genome Institute; RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S., RA Peters L., Ivanova N., Daligault H., Detter J.C., Han C., Tapia R., RA Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Hagen A., RA Katz L., Fiedler H.-P., Keasling J., Fortman J., Woyke T.; RT "Complete sequence of chromosome of Streptomyces violaceusniger Tu RT 4113."; RL Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002994; AEM81855.1; -; Genomic_DNA. DR RefSeq; WP_014055361.1; NC_015957.1. DR ProteinModelPortal; G2NYE0; -. DR STRING; 653045.Strvi_2123; -. DR EnsemblBacteria; AEM81855; AEM81855; Strvi_2123. DR GeneID; 32479144; -. DR KEGG; svl:Strvi_2123; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR KO; K03665; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000008703; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000008703}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000008703}. FT DOMAIN 275 440 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 500 AA; 54840 MW; 1F85379A88BCEDD1 CRC64; MTHSSSLPQD RQRPAESLRA DALMEEDVAW SHEIDEERDG DQYDRSDRAA LRRVVGLSTE LEDITEVEYR QLRLERVVLV GVWTSGTAQD AENSLAELAA LAETAGALVL DGVIQRRNKP DPATYIGSGK AEELRDIVVE SGADTVVCDG ELSPGQLIHL EDVVKVKVVD RTALILDIFA QHAKSREGKA QVSLAQMQYM LPRLRGWGQS LSRQMGGGGS GSSGGGMATR GPGETKIETD RRRIREKMAK MRREIAEMKT GRDIKRQERR RHKVPSVAIA GYTNAGKSSL LNRLTGAGVL VENALFATLD PTVRRAETPS GRLYTLADTV GFVRHLPHHL VEAFRSTMEE VGDADLIVHV VDGSHPAPEE QLAAVREVIR DVGAVDVPEI VVINKADLAD PLVVQRLLRM ERRAMAVSAR SGLGIDELLA VIDEELPRPQ VEIEVLLPYT HGKLVARTHV EGEVLSEEHT PEGTLLKARV HEELAAELRR FVPAAAAGQH // ID G2PQ49_MURRD Unreviewed; 403 AA. AC G2PQ49; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 1. DT 07-JUN-2017, entry version 41. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Murru_1473 {ECO:0000313|EMBL:AEM70514.1}; OS Muricauda ruestringensis (strain DSM 13258 / CIP 107369 / LMG 19739 / OS B1). OC Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales; OC Flavobacteriaceae; Muricauda. OX NCBI_TaxID=886377 {ECO:0000313|EMBL:AEM70514.1, ECO:0000313|Proteomes:UP000008908}; RN [1] {ECO:0000313|Proteomes:UP000008908} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 13258 / LMG 19739 / B1 {ECO:0000313|Proteomes:UP000008908}; RA Lucas S., Han J., Lapidus A., Bruce D., Goodwin L., Pitluck S., RA Peters L., Kyrpides N., Mavromatis K., Ivanova N., Ovchinnikova G., RA Teshima H., Detter J.C., Tapia R., Han C., Land M., Hauser L., RA Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Spring S., RA Schroeder M., Brambilla E., Klenk H.-P., Eisen J.A.; RT "The complete genome of Muricauda ruestringensis DSM 13258."; RL Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002999; AEM70514.1; -; Genomic_DNA. DR RefSeq; WP_014032795.1; NC_015945.1. DR STRING; 886377.Murru_1473; -. DR EnsemblBacteria; AEM70514; AEM70514; Murru_1473. DR KEGG; mrs:Murru_1473; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000008908; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000008908}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000008908}. FT DOMAIN 200 385 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 403 AA; 46635 MW; 4F16B0DA070A233B CRC64; MLEKKSIEYE KAVLIGVMNQ HQDEDKVKEY LDELEFLTYT AGGEVEKRFV QRIDVPNPKT YIGSGKMEEV RQFVKENEIG SVIFDDELSP AQQNNVEKLL RCKVLDRTSL ILDIFAQRAK TSYARTQVEL AQYEYLLPRL TGLWTHLERQ RGGIGMRGPG ETEIETDRRI VRDRIALLKK KLAKIDRQME TQRGNRGSLV RVALVGYTNV GKSTLMNVIS KSDVFAENKL FATLDTTVRK VVLGNLPFLL SDTVGFIRKL PTQLVESFKS TLDEVREADL LLHVVDISHP NFEEHIASVN QILDEIDSSG KPCIMVFNKI DQYRPETIDE DDLVTERTTA HFTLEEWKKT YFNKLGDKAL FISALNKENM DEFRKRVYDA VRDIHVTRFP YNNFLYPEHL DEY // ID G2SQG6_LACRR Unreviewed; 419 AA. AC G2SQG6; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 1. DT 07-JUN-2017, entry version 40. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:AEN77515.1}; GN OrderedLocusNames=LRC_01870 {ECO:0000313|EMBL:AEN77515.1}; OS Lactobacillus ruminis (strain ATCC 27782 / RF3). OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; OC Lactobacillus. OX NCBI_TaxID=1069534 {ECO:0000313|EMBL:AEN77515.1, ECO:0000313|Proteomes:UP000001279}; RN [1] {ECO:0000313|EMBL:AEN77515.1, ECO:0000313|Proteomes:UP000001279} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 27782 / RF3 {ECO:0000313|Proteomes:UP000001279}; RX PubMed=21995554; DOI=10.1186/1475-2859-10-S1-S13; RA Forde B.M., Neville B.A., O'Donnell M.M., Riboulet-Bisson E., RA Claesson M.J., Coghlan A., Ross R.P., O'Toole P.W.; RT "Genome sequences and comparative genomics of two Lactobacillus RT ruminis strains from the bovine and human intestinal tracts."; RL Microb. Cell Fact. 10:S13-S13(2011). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP003032; AEN77515.1; -; Genomic_DNA. DR RefSeq; WP_014072796.1; NC_015975.1. DR EnsemblBacteria; AEN77515; AEN77515; LRC_01870. DR GeneID; 29803032; -. DR KEGG; lrm:LRC_01870; -. DR PATRIC; fig|1069534.5.peg.215; -. DR KO; K03665; -. DR OMA; FNNHAHV; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000001279; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000001279}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000001279}. FT DOMAIN 197 365 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 419 AA; 46938 MW; ADDA01068463E839 CRC64; MTPVIICGAD LNQPDFDYTM QELANLAEAC DMEVKNTVIQ KLERPVSASY VGRGKAEEIK TQGKIHDAKI LIVNDELTPM QIRNLGDLTD MKIIDRTALI LEIFASRARS KEAKLQVQIA QLRISLPRLH TDNDKVKLDQ QTGGGGGSFN SRGGGETKLE KDRRVIGKRI SILKKELKDI EEKQNVTRKQ RDASGLRSVA LVGYTNAGKS TTMNGLLRVC GKDDDKQVFE KDMLFATLDT SVRRLHFKDN KDFLISDTVG FVSHLPHQLV QAFKSTLSEA AKADLLVQVI DVSDPNYCDM IKTTETTLKE IGVENIPMIY AFNKADLTEA PYPEILGNQI TYSAKDPASI EKIVELIKEN IFKDDRIVTF KIPFSEGRYL DELNVRGTVL ETTYEEDGTV ISANVSPELH SRLSRFEMH // ID G2T0D0_ROSHA Unreviewed; 414 AA. AC G2T0D0; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 1. DT 07-JUN-2017, entry version 40. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=RHOM_04015 {ECO:0000313|EMBL:AEN95925.1}; OS Roseburia hominis (strain DSM 16839 / NCIMB 14029 / A2-183). OC Bacteria; Firmicutes; Clostridia; Clostridiales; Lachnospiraceae; OC Roseburia. OX NCBI_TaxID=585394 {ECO:0000313|EMBL:AEN95925.1, ECO:0000313|Proteomes:UP000008178}; RN [1] {ECO:0000313|Proteomes:UP000008178} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 16839 / NCIMB 14029 / A2-183 RC {ECO:0000313|Proteomes:UP000008178}; RA Mulder I.E., Aminov R.I., Travis A.J., Lan A., Gaboriau-Routhiau V., RA Garden K., Logan E., Delday M., Coutts A.G.P., Grant G., RA Patterson A.M., Cerf-Bensussan N., Kelly D.; RT "Bi-directional cross-talk between a Clostridium symbiont, Roseburia RT hominis, the gut immune system and appetite regulation."; RL Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP003040; AEN95925.1; -; Genomic_DNA. DR RefSeq; WP_014078970.1; NC_015977.1. DR STRING; 585394.RHOM_04015; -. DR EnsemblBacteria; AEN95925; AEN95925; RHOM_04015. DR KEGG; rho:RHOM_04015; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000008178; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000008178}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000008178}. FT DOMAIN 202 366 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 161 195 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 414 AA; 46322 MW; 6F43B9E35B24455D CRC64; MAEIIELEDQ IEKVILVGVS EQDGDDAEDS VAELAELVRT AGAVVVGTLI QKRELMHPGT YVGTGKVAEI AAMIAERGAT GIVCDDELSP AQLKNLEQML DTKVMDRTLI ILDIFAARAT TSEGKIQVEL AQLKYRLSRL TGLGRSMSRL GGGIGTRGPG EKKLEMDRRL IKDRIAQLNR ELKEVRQHRE ITRAKRTRNG MPVAAIVGYT NAGKSTLLNR LTDAGVLEED KLFATLDPTT RVLELPGRQE ILLTDTVGFI RKLPHHLIEA FKSTLEEAKY ADYILHVVDA SNPQHEKQMH IVYDTLYQLD IREKMVITLF NKQDAVTERE PLHDLRADHT LAVSAREGTG LDELKELLAE LLRENKVLIE RTIAYADAGI LQQIRKQGEL LEEDYRPEGI YVKAYVPLEL YGKL // ID G2TMH6_BACCO Unreviewed; 416 AA. AC G2TMH6; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 1. DT 07-JUN-2017, entry version 41. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=Bcoa_3302 {ECO:0000313|EMBL:AEP02474.1}; OS Bacillus coagulans 36D1. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus. OX NCBI_TaxID=345219 {ECO:0000313|EMBL:AEP02474.1, ECO:0000313|Proteomes:UP000009283}; RN [1] {ECO:0000313|EMBL:AEP02474.1, ECO:0000313|Proteomes:UP000009283} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=36D1 {ECO:0000313|EMBL:AEP02474.1, RC ECO:0000313|Proteomes:UP000009283}; RX PubMed=22675583; DOI=10.4056/sigs.2365342; RA Rhee M.S., Moritz B.E., Xie G., Glavina Del Rio T., Dalin E., Tice H., RA Bruce D., Goodwin L., Chertkov O., Brettin T., Han C., Detter C., RA Pitluck S., Land M.L., Patel M., Ou M., Harbrucker R., Ingram L.O., RA Shanmugam K.T.; RT "Complete Genome Sequence of a thermotolerant sporogenic lactic acid RT bacterium, Bacillus coagulans strain 36D1."; RL Stand. Genomic Sci. 5:331-340(2011). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP003056; AEP02474.1; -; Genomic_DNA. DR RefSeq; WP_014098479.1; NC_016023.1. DR ProteinModelPortal; G2TMH6; -. DR STRING; 345219.Bcoa_3302; -. DR EnsemblBacteria; AEP02474; AEP02474; Bcoa_3302. DR KEGG; bag:Bcoa_3302; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR KO; K03665; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000009283; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000009283}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000009283}. FT DOMAIN 198 359 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 416 AA; 47066 MW; 205FDCC4FFF96DE4 CRC64; MENKKERAIL VGCEWSGISH SRFAYSMEEL KRLVETAQGE AVLEVVQKRD RVDAATYIGK GKVAELRALV SELQADLIVF NAELSPSQLR NLQAAVDCRV LDRTQLILDI FATRARSKEG KLQVELAQLE YLLPRLGGRG TELSRLGGGI GTRGPGETQL ETDRRHIRRR ISEIKAQLET VVHHRERYRE RRKKNHVFQI ALVGYTNAGK STLFNRLSAA NSYEENQLFA TLDPMTRKVV LPSGYTALLT DTVGFIQDLP TTLIAAFRST LEEVREADLL LHVIDSSNPD YDNHQKTVQR LLSELEMNHL PQLAVYNKMD IKDSHFVPNA QNSIMISAKD EKDIHRLLLE IEKQVLAEMV PYRALVPQTE GKLLSVLKSD TILRELIFKE ENEAYQCKGY ALPGHPVLGA IQQYAE // ID G2Z011_FLABF Unreviewed; 406 AA. AC G2Z011; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 1. DT 07-JUN-2017, entry version 44. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:CCB69276.1}; GN OrderedLocusNames=FBFL15_1191 {ECO:0000313|EMBL:CCB69276.1}; OS Flavobacterium branchiophilum (strain FL-15). OC Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales; OC Flavobacteriaceae; Flavobacterium. OX NCBI_TaxID=1034807 {ECO:0000313|EMBL:CCB69276.1, ECO:0000313|Proteomes:UP000009186}; RN [1] {ECO:0000313|EMBL:CCB69276.1, ECO:0000313|Proteomes:UP000009186} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=FL-15 {ECO:0000313|EMBL:CCB69276.1, RC ECO:0000313|Proteomes:UP000009186}; RX PubMed=21926215; DOI=10.1128/AEM.05625-11; RG 1:IP; RG Microbial Evolutionary Genomics,F-75015 Paris; RG France 2:CNRS; RG URA2171; RG F-75015 Paris,France 3:Unite de Virologie et Immunologie Mol.; RG INRA,78352 Jouy en Josas Cedex; RG France. 4:Unite de Mathemathique; RG Informatique et Genome,INRA; RG 78352 Jouy en Josas Cedex; RG France. 5:CEA/Genoscope; RG Evry; RG France; RA Touchon M., Barbier P., Bernardet J.F., Loux V., Vacherie B., RA Barbe V., Rocha E.P., Duchaud E.; RT "Complete Genome Sequence of the Fish Pathogen Flavobacterium RT branchiophilum."; RL Appl. Environ. Microbiol. 77:7656-7662(2011). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; FQ859183; CCB69276.1; -; Genomic_DNA. DR RefSeq; WP_014083744.1; NC_016001.1. DR STRING; 1034807.FBFL15_1191; -. DR EnsemblBacteria; CCB69276; CCB69276; FBFL15_1191. DR KEGG; fbr:FBFL15_1191; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000009186; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000009186}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Hydrolase {ECO:0000313|EMBL:CCB69276.1}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000009186}. FT DOMAIN 200 386 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 406 AA; 46850 MW; C89414ECCBA19CA4 CRC64; MLEKEIITFE KTVLVGIVTQ KQDEEKLKEY LDELEFLTYT AGGEVVKRFF QKMDKPNPKT FLGTGKIDEI NLYVKENNVS TIVFDDELSP SQQKNISRII DCKILDRTHL ILDIFAQRAE TSYARTQVEL AQCIYLLPRL SGMWTHLERQ KGGIGMRGPG ETEIETDRRI VRDRIALLKD KIKIIDKQMS VQRSNRGAMV RVALVGYTNV GKSTLMNTVG KSDVFVENKL FATLDTTVRK IVIKNLPFLL SDTVGFIRKL PTQLIDSFKS TLDEVREADL LLHVVDIAHP DFEDHIASVN QILAEIKCDD KPVIMVFNKI DAYRFLTIED DDLITEKTSK HYTLEEWKQT WMNRVGVSNA LFISATNKEN FEDFRACVYQ AVREIHITRF PYNNFLYPDY KDAVED // ID G3J2A4_METTV Unreviewed; 421 AA. AC G3J2A4; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 1. DT 07-JUN-2017, entry version 34. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=Mettu_2980 {ECO:0000313|EMBL:EGW19860.1}; OS Methylobacter tundripaludum (strain ATCC BAA-1195 / SV96). OC Bacteria; Proteobacteria; Gammaproteobacteria; Methylococcales; OC Methylococcaceae; Methylobacter. OX NCBI_TaxID=697282 {ECO:0000313|EMBL:EGW19860.1, ECO:0000313|Proteomes:UP000004664}; RN [1] {ECO:0000313|EMBL:EGW19860.1, ECO:0000313|Proteomes:UP000004664} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-1195 / SV96 {ECO:0000313|Proteomes:UP000004664}; RG US DOE Joint Genome Institute; RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S., RA Held B., Detter J.C., Han C., Tapia R., Land M., Hauser L., RA Kyrpides N., Ivanova N., Ovchinnikova G., Pagani I., Klotz M.G., RA Dispirito A.A., Murrell J.C., Dunfield P., Kalyuzhnaya M.G., RA Svenning M., Trotsenko Y.A., Stein L.Y., Woyke T.; RT "Genomic sequence of Methylobacter tundripaludum SV96."; RL Submitted (JUN-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JH109154; EGW19860.1; -; Genomic_DNA. DR RefSeq; WP_006894070.1; NZ_JH109154.1. DR STRING; 697282.Mettu_2980; -. DR EnsemblBacteria; EGW19860; EGW19860; Mettu_2980. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000004664; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000004664}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000004664}. FT DOMAIN 196 363 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 421 AA; 47292 MW; 7A52FBD2FE596530 CRC64; MFDRPESGER AVLVHLTLRS MHEDLLELKE LAKSAGTDPV YVVTGSRKKP DPKYFVGKGK LEELKAIIET YEADIVLFNH PLSPSQERNL EGFLGVRVVD RNGLILDIFA QRAQTFEGKL QVELAQLQHL STRLVRGWTH LERQKGGIGL RGPGETQLET DRRLLGLRIK QIQQRLDKVD KQRHQGRSKR KKAEVPSVSL VGYTNAGKST LFNKLTGADI YVADQLFATL DPTLRNCKLP NSSEIVLADT VGFIRHLPHE LVAAFKSTLQ EASEADLLLH VIDASSDDRA ETIYQVNQVL EDIKANEVRQ LEVFNKIDLL TDIQPRIERD DVGNPVRVWL SAETGAGVDL LYQALAEIFS NTKVKRTCYL QPDQGDIRAK LFACARIISE KTDDFGGCEL AIEIDTKYLG LLKSVEIEEM L // ID G3PL21_GASAC Unreviewed; 406 AA. AC G3PL21; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 1. DT 30-AUG-2017, entry version 29. DE SubName: Full=GTP binding protein 6 (putative) {ECO:0000313|Ensembl:ENSGACP00000018301}; OS Gasterosteus aculeatus (Three-spined stickleback). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata; OC Eupercaria; Perciformes; Cottioidei; Gasterosteales; Gasterosteidae; OC Gasterosteus. OX NCBI_TaxID=69293 {ECO:0000313|Ensembl:ENSGACP00000018301, ECO:0000313|Proteomes:UP000007635}; RN [1] {ECO:0000313|Ensembl:ENSGACP00000018301} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Lindblad-Toh K., Mauceli E., Grabherr M., Chang J.L., Lander E.S.; RL Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Ensembl:ENSGACP00000018301} RP IDENTIFICATION. RG Ensembl; RL Submitted (SEP-2011) to UniProtKB. CC -!- CAUTION: The sequence shown here is derived from an Ensembl CC automatic analysis pipeline and should be considered as CC preliminary data. {ECO:0000313|Ensembl:ENSGACP00000018301}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR STRING; 69293.ENSGACP00000018301; -. DR Ensembl; ENSGACT00000018336; ENSGACP00000018301; ENSGACG00000013857. DR eggNOG; KOG0410; Eukaryota. DR eggNOG; COG2262; LUCA. DR GeneTree; ENSGT00390000001397; -. DR InParanoid; G3PL21; -. DR OMA; MDTVGFM; -. DR TreeFam; TF315022; -. DR Proteomes; UP000007635; Unassembled WGS sequence. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR CDD; cd01878; HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000007635}; KW Reference proteome {ECO:0000313|Proteomes:UP000007635}. FT DOMAIN 185 349 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 406 AA; 45324 MW; EEAAA58CE7EDD2F4 CRC64; RSAAELMMAE AVGLVNTLDS WSVVDRVIMS TKTPEKKKIF GKGNFQTLTD RIRQTAGITA VFVNVERLSA LSEKREFEEA WGVKVFDRYS VVLHIFRRNA RTKEAKLQIS LAEIPLLSRS RLKNEMANLD QQGGGSRYIG GSGETLMEVQ QRLLRERELK IRSALETLRR KRRLLRSQRR DKELPSVSVL GYTNCGKTTL IKALTGDAGL QPRNQLFATL DVTVHAGQLP SHMTVLYVDT IGFLSQLPHQ LIDSFSATLE DIKHSDLLVH VRDVSHPETA NQKANVLRVL ENMRVPDRLL SSMIEVHNKT DLVDNYRLTE PGALPISALE QRGLDALRAA VEEELVASTG KRVMDLAVDL GSPQLSWLYK EAAVQDVRVN ADEGSAVVKV IISAAAYGRY RKLFAG // ID G3WSD9_SARHA Unreviewed; 515 AA. AC G3WSD9; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 1. DT 30-AUG-2017, entry version 26. DE SubName: Full=GTP binding protein 6 (putative) {ECO:0000313|Ensembl:ENSSHAP00000018344}; GN Name=GTPBP6 {ECO:0000313|Ensembl:ENSSHAP00000018344}; OS Sarcophilus harrisii (Tasmanian devil) (Sarcophilus laniarius). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Metatheria; Dasyuromorphia; Dasyuridae; Sarcophilus. OX NCBI_TaxID=9305 {ECO:0000313|Ensembl:ENSSHAP00000018344, ECO:0000313|Proteomes:UP000007648}; RN [1] {ECO:0000313|Ensembl:ENSSHAP00000018344} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=21709235; DOI=10.1073/pnas.1102838108; RA Miller W., Hayes V.M., Ratan A., Petersen D.C., Wittekindt N.E., RA Miller J., Walenz B., Knight J., Qi J., Zhao F., Wang Q., RA Bedoya-Reina O.C., Katiyar N., Tomsho L.P., Kasson L.M., Hardie R.A., RA Woodbridge P., Tindall E.A., Bertelsen M.F., Dixon D., Pyecroft S., RA Helgen K.M., Lesk A.M., Pringle T.H., Patterson N., Zhang Y., RA Kreiss A., Woods G.M., Jones M.E., Schuster S.C.; RT "Genetic diversity and population structure of the endangered RT marsupial Sarcophilus harrisii (Tasmanian devil)."; RL Proc. Natl. Acad. Sci. U.S.A. 108:12348-12353(2011). RN [2] {ECO:0000313|Ensembl:ENSSHAP00000018344} RP IDENTIFICATION. RG Ensembl; RL Submitted (SEP-2011) to UniProtKB. CC -!- CAUTION: The sequence shown here is derived from an Ensembl CC automatic analysis pipeline and should be considered as CC preliminary data. {ECO:0000313|Ensembl:ENSSHAP00000018344}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AEFK01127282; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AEFK01127283; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AEFK01127284; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AEFK01127285; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AEFK01127286; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AEFK01127287; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AEFK01127288; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR Ensembl; ENSSHAT00000018494; ENSSHAP00000018344; ENSSHAG00000015570. DR eggNOG; KOG0410; Eukaryota. DR eggNOG; COG2262; LUCA. DR GeneTree; ENSGT00390000001397; -. DR Proteomes; UP000007648; Unassembled WGS sequence. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR CDD; cd01878; HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000007648}; KW Reference proteome {ECO:0000313|Proteomes:UP000007648}. FT DOMAIN 297 461 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 515 AA; 57324 MW; 148DA532BC1AF6FF CRC64; MWTLRAAVRR GLPLLRAACS FREVLAPAPQ DRCVRALSTF GGKNPDKSRL LSGSGGEAIA RKGWKEEGEE EDETGVEDEE VEELLLEREP LLPQGAQRVF LLHPDVKWGA KKQTLTRAEL QVAEAKTLVH TLLNWSVEET MIVSTKTPDK KLVFGKGNFE LLTEKIRGSP QITSVFLNVE RMSPLTKKEL EAAWGVEVFD RFTIVLHIFR CNAKTKEAKL QIALAEIPLL RSNLKNEVAH LDQQGGGSRY IMGSGETFLQ IQQRVLKEKE IKIKKALEKL KKRRHLLRSQ RKKRELPIIS IMGYTNCGKT TLIKALTGDA AIQPRDQLFA TLDITAHSGS LPSHMTVVYV DTIGFLSQLP HDLIESFSAT LEDVAHSDVI IHVRDISHPE TDLQKASVLS VLKNLNLPNQ LLDSIIEVHN KVDLVESYES TEPNAITISA LLGHGLEKLK AEIESAVLKA TGKKLLTLNI KLEGAQLSWL YKEATVQEVD VIPENGTANV KVIISNSAYA MWQTG // ID G3WSE0_SARHA Unreviewed; 520 AA. AC G3WSE0; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 1. DT 30-AUG-2017, entry version 31. DE SubName: Full=GTP binding protein 6 (putative) {ECO:0000313|Ensembl:ENSSHAP00000018345}; GN Name=GTPBP6 {ECO:0000313|Ensembl:ENSSHAP00000018345}; OS Sarcophilus harrisii (Tasmanian devil) (Sarcophilus laniarius). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Metatheria; Dasyuromorphia; Dasyuridae; Sarcophilus. OX NCBI_TaxID=9305 {ECO:0000313|Ensembl:ENSSHAP00000018345, ECO:0000313|Proteomes:UP000007648}; RN [1] {ECO:0000313|Ensembl:ENSSHAP00000018345} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=21709235; DOI=10.1073/pnas.1102838108; RA Miller W., Hayes V.M., Ratan A., Petersen D.C., Wittekindt N.E., RA Miller J., Walenz B., Knight J., Qi J., Zhao F., Wang Q., RA Bedoya-Reina O.C., Katiyar N., Tomsho L.P., Kasson L.M., Hardie R.A., RA Woodbridge P., Tindall E.A., Bertelsen M.F., Dixon D., Pyecroft S., RA Helgen K.M., Lesk A.M., Pringle T.H., Patterson N., Zhang Y., RA Kreiss A., Woods G.M., Jones M.E., Schuster S.C.; RT "Genetic diversity and population structure of the endangered RT marsupial Sarcophilus harrisii (Tasmanian devil)."; RL Proc. Natl. Acad. Sci. U.S.A. 108:12348-12353(2011). RN [2] {ECO:0000313|Ensembl:ENSSHAP00000018345} RP IDENTIFICATION. RG Ensembl; RL Submitted (SEP-2011) to UniProtKB. CC -!- CAUTION: The sequence shown here is derived from an Ensembl CC automatic analysis pipeline and should be considered as CC preliminary data. {ECO:0000313|Ensembl:ENSSHAP00000018345}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AEFK01127282; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AEFK01127283; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AEFK01127284; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AEFK01127285; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AEFK01127286; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AEFK01127287; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AEFK01127288; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR STRING; 9305.ENSSHAP00000018345; -. DR Ensembl; ENSSHAT00000018495; ENSSHAP00000018345; ENSSHAG00000015570. DR eggNOG; KOG0410; Eukaryota. DR eggNOG; COG2262; LUCA. DR GeneTree; ENSGT00390000001397; -. DR InParanoid; G3WSE0; -. DR OMA; MDTVGFM; -. DR OrthoDB; EOG091G0852; -. DR TreeFam; TF315022; -. DR Proteomes; UP000007648; Unassembled WGS sequence. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR CDD; cd01878; HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000007648}; KW Reference proteome {ECO:0000313|Proteomes:UP000007648}. FT DOMAIN 299 463 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 520 AA; 58010 MW; E44E73EBC9CEE51A CRC64; MWTLRAAVRR GLPLLRAACS FREVLAPAPQ DRCVRALSTF GGKNPDKSRL LSGSGGEAIA RKGWKEEGEE EDETGVEDEE VEELLLEREP LLPQGAQRVF LLHPDVKWGA KKQTLTREKA ELQVAEAKTL VHTLLNWSVE ETMIVSTKTP DKKLVFGKGN FELLTEKIRG SPQITSVFLN VERMSPLTKK ELEAAWGVEV FDRFTIVLHI FRCNAKTKEA KLQIALAEIP LLRSNLKNEV AHLDQQGGGS RYIMGSGETF LQIQQRVLKE KEIKIKKALE KLKKRRHLLR SQRKKRELPI ISIMGYTNCG KTTLIKALTG DAAIQPRDQL FATLDITAHS GSLPSHMTVV YVDTIGFLSQ LPHDLIESFS ATLEDVAHSD VIIHVRDISH PETDLQKASV LSVLKNLNLP NQLLDSIIEV HNKVDLVESY ESTEPNAITI SALLGHGLEK LKAEIESAVL KATGKKLLTL NIKLEGAQLS WLYKEATVQE VDVIPENGTA NVKVIISNSA YGKYRKLFPI // ID G4CI69_9NEIS Unreviewed; 401 AA. AC G4CI69; DT 14-DEC-2011, integrated into UniProtKB/TrEMBL. DT 14-DEC-2011, sequence version 1. DT 07-JUN-2017, entry version 33. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:EGY52470.1}; GN ORFNames=HMPREF9371_1308 {ECO:0000313|EMBL:EGY52470.1}; OS Neisseria shayeganii 871. OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=1032488 {ECO:0000313|EMBL:EGY52470.1, ECO:0000313|Proteomes:UP000003019}; RN [1] {ECO:0000313|EMBL:EGY52470.1, ECO:0000313|Proteomes:UP000003019} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=871 {ECO:0000313|EMBL:EGY52470.1, RC ECO:0000313|Proteomes:UP000003019}; RA Muzny D., Qin X., Deng J., Jiang H., Liu Y., Qu J., Song X.-Z., RA Zhang L., Thornton R., Coyle M., Francisco L., Jackson L., Javaid M., RA Korchina V., Kovar C., Mata R., Mathew T., Ngo R., Nguyen L., RA Nguyen N., Okwuonu G., Ongeri F., Pham C., Simmons D., RA Wilczek-Boney K., Hale W., Jakkamsetti A., Pham P., Ruth R., RA San Lucas F., Warren J., Zhang J., Zhao Z., Zhou C., Zhu D., Lee S., RA Bess C., Blankenburg K., Forbes L., Fu Q., Gubbala S., Hirani K., RA Jayaseelan J.C., Lara F., Munidasa M., Palculict T., Patil S., RA Pu L.-L., Saada N., Tang L., Weissenberger G., Zhu Y., Hemphill L., RA Shang Y., Youmans B., Ayvaz T., Ross M., Santibanez J., Aqrawi P., RA Gross S., Joshi V., Fowler G., Nazareth L., Reid J., Worley K., RA Petrosino J., Highlander S., Gibbs R.; RL Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EGY52470.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGAY01000048; EGY52470.1; -; Genomic_DNA. DR RefSeq; WP_009119000.1; NZ_JH164926.1. DR EnsemblBacteria; EGY52470; EGY52470; HMPREF9371_1308. DR PATRIC; fig|1032488.3.peg.1234; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000003019; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000003019}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000003019}. FT DOMAIN 226 393 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 401 AA; 44014 MW; 383444200E805696 CRC64; MSRRTLFQLD KSLERPERVM LVGVMLSDSF SGSNESREHA FRAALQEAAE LVAATGGELV HTETAKRDRA HSALFVGSGK AEELAEAVRR HNIELAVFNH ELTPTQERNL EKILQCRVLD RVGLILAIFA QRARSQEGRL QVELAQLTHL SGRLVRGYGH LKSQKGGIGL KGPGETQLET DRRLIQTKIT TLRRQLEAVK KQRETRRKSR LKAGTTSSDG RFHAVKTFAI VGYTNAGKSS LFNRLTKADV LAKDQLFATL DTTARRLYLN ADTSIILTDT VGFVRDLPHQ LVAAFSATLE ETALADVLLH VVDVSHPDHE RQIQDVNAVL AEIGADGLPQ LLVYNKTDLL PPALRREGIL RNAAGQAVAV GISVLTGSGL DELRQALGEW AQTPAPTQQA T // ID G4CSP0_9NEIS Unreviewed; 382 AA. AC G4CSP0; DT 14-DEC-2011, integrated into UniProtKB/TrEMBL. DT 14-DEC-2011, sequence version 1. DT 07-JUN-2017, entry version 31. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:EGZ44596.1}; GN ORFNames=HMPREF9370_2122 {ECO:0000313|EMBL:EGZ44596.1}; OS Neisseria wadsworthii 9715. OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=1030841 {ECO:0000313|EMBL:EGZ44596.1, ECO:0000313|Proteomes:UP000005336}; RN [1] {ECO:0000313|EMBL:EGZ44596.1, ECO:0000313|Proteomes:UP000005336} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=9715 {ECO:0000313|EMBL:EGZ44596.1, RC ECO:0000313|Proteomes:UP000005336}; RA Muzny D., Qin X., Deng J., Jiang H., Liu Y., Qu J., Song X.-Z., RA Zhang L., Thornton R., Coyle M., Francisco L., Jackson L., Javaid M., RA Korchina V., Kovar C., Mata R., Mathew T., Ngo R., Nguyen L., RA Nguyen N., Okwuonu G., Ongeri F., Pham C., Simmons D., RA Wilczek-Boney K., Hale W., Jakkamsetti A., Pham P., Ruth R., RA San Lucas F., Warren J., Zhang J., Zhao Z., Zhou C., Zhu D., Lee S., RA Bess C., Blankenburg K., Forbes L., Fu Q., Gubbala S., Hirani K., RA Jayaseelan J.C., Lara F., Munidasa M., Palculict T., Patil S., RA Pu L.-L., Saada N., Tang L., Weissenberger G., Zhu Y., Hemphill L., RA Shang Y., Youmans B., Ayvaz T., Ross M., Santibanez J., Aqrawi P., RA Gross S., Joshi V., Fowler G., Nazareth L., Reid J., Worley K., RA Petrosino J., Highlander S., Gibbs R.; RL Submitted (JUN-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EGZ44596.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGAZ01000070; EGZ44596.1; -; Genomic_DNA. DR EnsemblBacteria; EGZ44596; EGZ44596; HMPREF9370_2122. DR PATRIC; fig|1030841.3.peg.2112; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000005336; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000005336}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000005336}. FT DOMAIN 213 382 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 172 206 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 382 AA; 42204 MW; 1E13BB0FBA5F7B50 CRC64; MSKYQPDKSL SKPERVMLVG VMLAADYSGA NEIRERDFQA ALEEAAELVR ATGGELVQVE SAKRDRAHSA LFVGTGKAQE LAEAVRLNEI ELVVFNHELT PTQERNLEKA LQCRVLDRVG LILAIFAQRA QSQEGRLQVE LAQLTHLSGR LVRGYGHLQS QRGGIGLKGP GETQLETDRR LINQKIAALK RQLKNVEKQR ATRRKARLRG SLKTFALVGY TNTGKSSLFN RLTKADVLAK DQLFATLDTT ARRLYLSPEC SLIITDTVGF VRDLPHSLVA AFSATLEETA LADVLLHVAD VSHPQVERQE DDVNLVLEEI GAGDVPQLMV YNKTDLLPAE KRPKGILRNA RGMPVAVYLS VKEGWGLEDL RDAMVELAQA GD // ID G4D3N2_9FIRM Unreviewed; 420 AA. AC G4D3N2; DT 14-DEC-2011, integrated into UniProtKB/TrEMBL. DT 14-DEC-2011, sequence version 1. DT 07-JUN-2017, entry version 34. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:EGY79874.1}; GN ORFNames=HMPREF9129_1012 {ECO:0000313|EMBL:EGY79874.1}; OS Peptoniphilus indolicus ATCC 29427. OC Bacteria; Firmicutes; Tissierellia; Tissierellales; Peptoniphilaceae; OC Peptoniphilus. OX NCBI_TaxID=997350 {ECO:0000313|EMBL:EGY79874.1, ECO:0000313|Proteomes:UP000003422}; RN [1] {ECO:0000313|EMBL:EGY79874.1, ECO:0000313|Proteomes:UP000003422} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29427 {ECO:0000313|EMBL:EGY79874.1, RC ECO:0000313|Proteomes:UP000003422}; RA Muzny D., Qin X., Deng J., Jiang H., Liu Y., Qu J., Song X.-Z., RA Zhang L., Thornton R., Coyle M., Francisco L., Jackson L., Javaid M., RA Korchina V., Kovar C., Mata R., Mathew T., Ngo R., Nguyen L., RA Nguyen N., Okwuonu G., Ongeri F., Pham C., Simmons D., RA Wilczek-Boney K., Hale W., Jakkamsetti A., Pham P., Ruth R., RA San Lucas F., Warren J., Zhang J., Zhao Z., Zhou C., Zhu D., Lee S., RA Bess C., Blankenburg K., Forbes L., Fu Q., Gubbala S., Hirani K., RA Jayaseelan J.C., Lara F., Munidasa M., Palculict T., Patil S., RA Pu L.-L., Saada N., Tang L., Weissenberger G., Zhu Y., Hemphill L., RA Shang Y., Youmans B., Ayvaz T., Ross M., Santibanez J., Aqrawi P., RA Gross S., Joshi V., Fowler G., Nazareth L., Reid J., Worley K., RA Petrosino J., Highlander S., Gibbs R.; RL Submitted (JUN-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EGY79874.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGBB01000092; EGY79874.1; -; Genomic_DNA. DR EnsemblBacteria; EGY79874; EGY79874; HMPREF9129_1012. DR PATRIC; fig|997350.3.peg.976; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000003422; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000003422}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000003422}. FT DOMAIN 200 367 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 420 AA; 47514 MW; C5F6133841A2243C CRC64; MENNINNKIE RVIIVGTDIG ARPHSLATSI NELEELVKAA GAEVVGVVTQ NIDKYSPKFL IGTGKLQEIK DMIPKLEANV VVFNDELSGV QLRNIEDELK VKILDRTSLI LDIFAIRAST YEAKLQVQLA QLSYQLPRLL GIDGWSRTGG GIGTRGPGEQ IIETDRRRIL REIQTIKEKL KKAEKTRETQ RTGRKNSMIP IVSLVGYTNA GKSTILNRIK ISDAKEVFVK DMLFATLDPS SRKAKLLNGM DFIISDTVGF VSKLPTKLVE AFKSTLEEIK HSDLILHVID ASNEDLEIQY KTTMDILEEL KVDRSRILTV FNKMDKVGGD LMINPRHGEN RIYISATHDE SMDKLLEAIE ENLPERFYNV KLLIGYADSD TLSEILNKHN HENLEYREDG VSLEVVLSEA EFRKYERFVM // ID G4E8M2_9GAMM Unreviewed; 429 AA. AC G4E8M2; DT 14-DEC-2011, integrated into UniProtKB/TrEMBL. DT 14-DEC-2011, sequence version 1. DT 07-JUN-2017, entry version 34. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=ThisiDRAFT_2651 {ECO:0000313|EMBL:EGZ42800.1}; OS Thiorhodospira sibirica ATCC 700588. OC Bacteria; Proteobacteria; Gammaproteobacteria; Chromatiales; OC Ectothiorhodospiraceae; Thiorhodospira. OX NCBI_TaxID=765914 {ECO:0000313|EMBL:EGZ42800.1, ECO:0000313|Proteomes:UP000003058}; RN [1] {ECO:0000313|EMBL:EGZ42800.1, ECO:0000313|Proteomes:UP000003058} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700588 {ECO:0000313|EMBL:EGZ42800.1, RC ECO:0000313|Proteomes:UP000003058}; RG US DOE Joint Genome Institute (JGI-PGF); RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S., RA Peters L., Land M.L., Hauser L., Vogl K., Liu Z., Imhoff J., RA Frigaard N.-U., Bryant D., Woyke T.; RT "The draft genome of Thiorhodospira sibirica ATCC 700588."; RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EGZ42800.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGFD01000080; EGZ42800.1; -; Genomic_DNA. DR EnsemblBacteria; EGZ42800; EGZ42800; ThisiDRAFT_2651. DR PATRIC; fig|765914.3.peg.2622; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000003058; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000003058}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000003058}. FT DOMAIN 199 366 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 429 AA; 48021 MW; 486F60CB9A99DCC0 CRC64; MFVFERPRSG EKALLVHMEL SGALAEDRQE FIELVRSAGA QILDCLGGSL RSIDPRHFIG SGKAEELREA VALHQAELAI FDHTLSPSQE RNLERLLQCR VLDRTGLILD IFAQRARSHE GKLQVELAQL RHLSTRLVRG WTHLERQKGG IGLRGPGETQ LETDRRLLAA RIKQIERRLS KVASSREQNR QARQRAETPT VALVGYTNAG KSTLFNRLTG AQVYAADQLF ATLDPTLRRL DLPLQQSLIL ADTVGFIRHL PHDLVAAFKA TLTETREAAL LLHVIDAADE QRDRYIEQVN AVLAEIDAAE VPQILVYNKI DLLESVSVRS EAAAHGQPAR VWLSAQTGEG IEQLRELLAE HFSQAVFHGT VELPAHAGKL RAALFAQHAV LAESFTEAGG WRLEIRLTQR RLEALWREHQ RIAPEIINP // ID G4KR80_OSCVS Unreviewed; 429 AA. AC G4KR80; DT 14-DEC-2011, integrated into UniProtKB/TrEMBL. DT 14-DEC-2011, sequence version 1. DT 07-JUN-2017, entry version 37. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hlfX {ECO:0000313|EMBL:BAK99903.1}; GN Synonyms=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=OBV_27050 {ECO:0000313|EMBL:BAK99903.1}; OS Oscillibacter valericigenes (strain DSM 18026 / NBRC 101213 / OS Sjm18-20). OC Bacteria; Firmicutes; Clostridia; Clostridiales; Oscillospiraceae; OC Oscillibacter. OX NCBI_TaxID=693746 {ECO:0000313|EMBL:BAK99903.1, ECO:0000313|Proteomes:UP000005219}; RN [1] {ECO:0000313|Proteomes:UP000005219} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 18026 / NBRC 101213 / Sjm18-20 RC {ECO:0000313|Proteomes:UP000005219}; RA Katano Y., Fujinami S., Kawakoshi A., Ohji S., Nakazawa H., Ankai A., RA Oguchi A., Fukui S., Terui Y., Harada T., Takahashi M., Suzuki K., RA Fujita N.; RT "Whole genome sequence of Oscillibacter valericigenes Sjm18-20."; RL Submitted (JAN-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AP012044; BAK99903.1; -; Genomic_DNA. DR RefSeq; WP_014118556.1; NC_016048.1. DR STRING; 693746.OBV_27050; -. DR EnsemblBacteria; BAK99903; BAK99903; OBV_27050. DR KEGG; ova:OBV_27050; -. DR PATRIC; fig|693746.9.peg.2922; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000005219; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000005219}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000005219}. FT DOMAIN 208 369 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 429 AA; 47455 MW; DA4474F51FB8CADA CRC64; MQETNEIRDK VVLVGLNSPV LNKDEDADEA TMEELSALVE TAGGETEGIV LQNREKPDPR TFIGEGKVAE VQLYCENVGA TMVIFDNDLS PSQQRVLTEL LGIQVLDRCG LILDIFAQRA KTKEGRLQVE LAEYQYLLPR LTGMWTHLER QGGTSGKGAI GSKGPGETQL ETDRRLIHKK IDKLRSDLED VRRVRGTQRQ QRQKNEIPVV SIVGYTNAGK STLLNQLTGA SIPANNRLFD TLDTTSRLLT VSDTLDVVLS DTVGFIRKLP HQLVEAFKAT LEELEYADLL LHVIDVSNPG WQQQAQVVED LIAELGASGI PRIEVFNKCD LSGGEILPRG EDMVTISAKT GEGVQELLQL IDRRLDKGAR RVSIHLPYDR GGLLDILFRE AKVEKVDYAQ TIDVTAVCAP RVLGQVAPYV QEAEDPLDL // ID G4L6Y6_TETHN Unreviewed; 414 AA. AC G4L6Y6; DT 14-DEC-2011, integrated into UniProtKB/TrEMBL. DT 14-DEC-2011, sequence version 1. DT 07-JUN-2017, entry version 42. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:BAK94310.1}; GN OrderedLocusNames=TEH_09830 {ECO:0000313|EMBL:BAK94310.1}; OS Tetragenococcus halophilus (strain DSM 20338 / JCM 20259 / NCIMB 9735 OS / NBRC 12172) (Pediococcus halophilus). OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Enterococcaceae; OC Tetragenococcus. OX NCBI_TaxID=945021 {ECO:0000313|EMBL:BAK94310.1, ECO:0000313|Proteomes:UP000002663}; RN [1] {ECO:0000313|EMBL:BAK94310.1, ECO:0000313|Proteomes:UP000002663} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 20338 / JCM 20259 / NCIMB 9735 / NBRC 12172 RC {ECO:0000313|Proteomes:UP000002663}; RA Nakazawa H., Omata S., Koga C., Watanabe Y., Katano Y., Ito N., RA Tsukatani N., Ankai A., Oguchi A., Fukui S., Yashiro I., Kamata S., RA Hashimoto Y., Yamazaki J., Taguchi H., Tanaka A., Koyama T., RA Ichige A., Hanya Y., Tanikawa S., Yamazaki S., Fujita N.; RT "Whole genome sequence of Tetragenococcus halophilus NBRC 12172."; RL Submitted (JAN-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AP012046; BAK94310.1; -; Genomic_DNA. DR RefSeq; WP_014124370.1; NC_016052.1. DR STRING; 945021.TEH_09830; -. DR EnsemblBacteria; BAK94310; BAK94310; TEH_09830. DR KEGG; thl:TEH_09830; -. DR PATRIC; fig|945021.8.peg.1006; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000002663; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000002663}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000002663}. FT DOMAIN 196 358 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 169 192 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 414 AA; 47326 MW; D77665EF61B6D851 CRC64; MVKKERVILV GVQTPENHHN FAESMLELKN LAQTANGTMI SSIEQNREQF DHQTIIGKGK LEELRQTIDK EAIDLVIFNH ELTPRQGQII EDALEAPTID RIQLILDIFA KRARSKEGKL QVELAQLEYS FPRIIGQGKT LSRLGGGIGT RGPGETKLET DRRLIRKKMT SIRRELKEVE QHRQRTRQQR NEQQVYQIGL VGYTNSGKST LLNLLTSADA YEENQLFATL DPLTKKWRLP EGFEVTITDT VGFIQDLPTQ LIDAFHSTLE ESQNMDLLLH VIDASAENRQ QQEQTVLKLM DDLQLRQIPV LVVYNKADLI DKEQFVPTLF PYVLVSAKDP ASKDKLIEAI QSIMKEKLQP YTLVLAPDEG RLLEKLKQNT LLVSTDFEEE KQQYVAKGFA KEHSFAITRM EQAK // ID G4Q7N1_ACIIR Unreviewed; 605 AA. AC G4Q7N1; DT 14-DEC-2011, integrated into UniProtKB/TrEMBL. DT 14-DEC-2011, sequence version 1. DT 07-JUN-2017, entry version 38. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Acin_1144 {ECO:0000313|EMBL:AEQ22370.1}; OS Acidaminococcus intestini (strain RyC-MR95). OC Bacteria; Firmicutes; Negativicutes; Acidaminococcales; OC Acidaminococcaceae; Acidaminococcus. OX NCBI_TaxID=568816 {ECO:0000313|EMBL:AEQ22370.1, ECO:0000313|Proteomes:UP000007093}; RN [1] {ECO:0000313|EMBL:AEQ22370.1, ECO:0000313|Proteomes:UP000007093} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=RyC-MR95 {ECO:0000313|EMBL:AEQ22370.1, RC ECO:0000313|Proteomes:UP000007093}; RX PubMed=22123762; DOI=10.1128/JB.06301-11; RA D'Auria G., Galan J.C., Rodriguez-Alcayna M., Moya A., Baquero F., RA Latorre A.; RT "Complete genome sequence of Acidaminococcus intestini RYC-MR95, a RT Gram-negative bacterium from the phylum Firmicutes."; RL J. Bacteriol. 193:7008-7009(2011). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP003058; AEQ22370.1; -; Genomic_DNA. DR RefSeq; WP_009016293.1; NC_016077.1. DR ProteinModelPortal; G4Q7N1; -. DR STRING; 568816.Acin_1144; -. DR EnsemblBacteria; AEQ22370; AEQ22370; Acin_1144. DR KEGG; ain:Acin_1144; -. DR PATRIC; fig|568816.4.peg.1101; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR KO; K03665; -. DR OMA; EREVIIT; -. DR Proteomes; UP000007093; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000007093}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000007093}. FT DOMAIN 384 549 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 605 AA; 66924 MW; CE9E406BC2F0FFA6 CRC64; MDNIVYGKTE GIKKRVLEQL QSLYDLHLDQ GQLISEELAL LLRDISESIG REVSVYVDRK GIISSVSVGS DHAVSLQDTG SRRSLWRLSG ITAIHTHPSG TSRLSGVDIS TLKNLRLDGM AALAWKDAEA MPLLSLGLIT DLTDDGVPVA EEFGPYSAKE AARIPYGTLL QTIERILGKK TRSEKTGKEV ERAMLVSLHW GEDCSRYCVE DSVEELAQLA ETAGAIVAAK FVQSRPKPDP VFFIGKGKVE EMALFAQQED IDLCLVDDDL SPAQQRNLEQ ALGVRIIDRT GLILDIFAKR ARTSEGKLQV ELAQLQYLLP RIMGQGASLS RLGGGIGTRG PGETKLEVDR RRIRDRIGFL EAQIEKMKGA RRTQQKAREK SRIKQVCLVG YTNAGKSSLL NALTHSEIYA ENQLFATLDP TTRQLSLPNK EVCTLTDTVG FIQRLPHQLV AAFRSTLEVV KGADLLLHVI DVSHELHEKQ EEAVLSVLKE LGVTDTPILT VYNKIDKLPD HEGLKKRLDR EESLAISARS GEGIPALIKK IASFLNEGKT EVTLLIPYTE TKLSAQLHEK ATVLSESYGE KGALMKVRLD KHDVKHYAPY LKEET // ID G4QJ92_GLANF Unreviewed; 427 AA. AC G4QJ92; DT 14-DEC-2011, integrated into UniProtKB/TrEMBL. DT 14-DEC-2011, sequence version 1. DT 30-AUG-2017, entry version 39. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:AEP31235.1}; GN OrderedLocusNames=GNIT_3140 {ECO:0000313|EMBL:AEP31235.1}; OS Glaciecola nitratireducens (strain JCM 12485 / KCTC 12276 / FR1064). OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales; OC Alteromonadaceae; Glaciecola. OX NCBI_TaxID=1085623 {ECO:0000313|EMBL:AEP31235.1, ECO:0000313|Proteomes:UP000009282}; RN [1] {ECO:0000313|EMBL:AEP31235.1, ECO:0000313|Proteomes:UP000009282} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=JCM 12485 / KCTC 12276 / FR1064 RC {ECO:0000313|Proteomes:UP000009282}; RX PubMed=22123761; DOI=10.1128/JB.06296-11; RA Bian F., Qin Q.L., Xie B.B., Shu Y.L., Zhang X.Y., Yu Y., Chen B., RA Chen X.L., Zhou B.C., Zhang Y.Z.; RT "Complete genome sequence of seawater bacterium Glaciecola RT nitratireducens FR1064T."; RL J. Bacteriol. 193:7006-7007(2011). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP003060; AEP31235.1; -; Genomic_DNA. DR RefSeq; WP_014110106.1; NC_016041.1. DR STRING; 1085623.GNIT_3140; -. DR EnsemblBacteria; AEP31235; AEP31235; GNIT_3140. DR KEGG; gni:GNIT_3140; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR KO; K03665; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000009282; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000009282}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000009282}. FT DOMAIN 198 365 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 427 AA; 48116 MW; FA99C35E4773D754 CRC64; MFDRYEAGEQ AVLVHVDFSD ESNKEDVNEL QMLVSSAGVK TASVLTTSRR APHAKYFVGS GKAQEIADTV QAVGADVVIF NHQLTPSQER NLEALICCRV LDRTSLILDI FAQRARTHEG KLQVELAQLR HLSTRLIRGW THLERQKGGI GLRGPGETQL ETDRRLLRAR VKGILKRLEK VKKQREQGRR SRKRAEIPTV SLVGYTNAGK STLFNTITDA GVYAADQLFA TLDPTLRKIE LPEVGHAILA DTVGFIRHLP HDLVAAFKAT LQETQEADIL LHVIDYADDK YLEYIDQVND VLDEIDAGDV PQLIVCNKID RLEGVEPKID RDDTGRPIRV WVSAQDGLGI DLLRSALTEC LHKAMVEYQL KVPANEGRLR GMLYNLNCIA QQSYSDDGDW LVDIKMLESD WNKMNKQLEN RLTNYIL // ID G4R906_PELHB Unreviewed; 451 AA. AC G4R906; DT 14-DEC-2011, integrated into UniProtKB/TrEMBL. DT 14-DEC-2011, sequence version 1. DT 07-JUN-2017, entry version 40. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=KKY_1401 {ECO:0000313|EMBL:AEQ51423.1}; OS Pelagibacterium halotolerans (strain DSM 22347 / JCM 15775 / CGMCC OS 1.7692 / B2). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Hyphomicrobiaceae; Pelagibacterium. OX NCBI_TaxID=1082931 {ECO:0000313|EMBL:AEQ51423.1, ECO:0000313|Proteomes:UP000008850}; RN [1] {ECO:0000313|EMBL:AEQ51423.1, ECO:0000313|Proteomes:UP000008850} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 22347 / JCM 15775 / CGMCC 1.7692 / B2 RC {ECO:0000313|Proteomes:UP000008850}; RX PubMed=22156395; DOI=10.1128/JB.06343-11; RA Huo Y.Y., Cheng H., Han X.F., Jiang X.W., Sun C., Zhang X.Q., RA Zhu X.F., Liu Y.F., Li P.F., Ni P.X., Wu M.; RT "Complete genome sequence of Pelagibacterium halotolerans B2T."; RL J. Bacteriol. 194:197-198(2012). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP003075; AEQ51423.1; -; Genomic_DNA. DR RefSeq; WP_014130572.1; NC_016078.1. DR STRING; 1082931.KKY_1401; -. DR EnsemblBacteria; AEQ51423; AEQ51423; KKY_1401. DR KEGG; phl:KKY_1401; -. DR PATRIC; fig|1082931.4.peg.1380; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000008850; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000008850}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000008850}. FT DOMAIN 215 387 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 451 AA; 49364 MW; F1A391F859414C6D CRC64; MIDREDDDDG KGFVDLREVP TRTGLVTPDV RHNRYSRPAE ARHAEFIGLA AAIALDLVFT EIFRIREIKP ATYLGGGQVQ QLAEWAKEKD IELLVVDAPL SPIQQRNLER EIGVKVLDRT ALILEIFGER AATREGVLQV ELAHLNYQKG RLVRSWTHLE RQRGGGGFLG GPGETQIESD RRQIQDRILV LERRLDKVRR TRQLQRGPRD SVPFPVVALV GYTNAGKSSL FNAITGSGVM AENLLFATLD TTVRRATLPH GRDIILSDTV GFISDLPTDL VAAFRGTLEE VTQAQVILHV RDVSNPDHPA QANDVLSVLA SLGVTGEATP IIEVWNKIDN LPADAVDGLT SIAPAGKVAA AIPVSAVTGQ GLPDLLLAVE KTLAQDSRLF SVLIPHESSS ETGWLYANAE VVERGEPDDE GTRYTVRVLP RHRAEFSEKF AGRITGLDGS S // ID G4RLV6_THETK Unreviewed; 399 AA. AC G4RLV6; DT 14-DEC-2011, integrated into UniProtKB/TrEMBL. DT 14-DEC-2011, sequence version 1. DT 07-JUN-2017, entry version 38. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=TTX_1937 {ECO:0000313|EMBL:CCC82551.1}; OS Thermoproteus tenax (strain ATCC 35583 / DSM 2078 / JCM 9277 / NBRC OS 100435 / Kra 1). OC Archaea; Crenarchaeota; Thermoprotei; Thermoproteales; OC Thermoproteaceae; Thermoproteus. OX NCBI_TaxID=768679 {ECO:0000313|EMBL:CCC82551.1, ECO:0000313|Proteomes:UP000002654}; RN [1] {ECO:0000313|EMBL:CCC82551.1, ECO:0000313|Proteomes:UP000002654} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 35583 / DSM 2078 / JCM 9277 / NBRC 100435 / Kra 1 RC {ECO:0000313|Proteomes:UP000002654}; RX PubMed=22003381; DOI=10.1371/journal.pone.0024222; RA Siebers B., Zaparty M., Raddatz G., Tjaden B., Albers S.V., Bell S.D., RA Blombach F., Kletzin A., Kyrpides N., Lanz C., Plagens A., Rampp M., RA Rosinus A., von Jan M., Makarova K.S., Klenk H.P., Schuster S.C., RA Hensel R.; RT "The complete genome sequence of Thermoproteus tenax: a RT physiologically versatile member of the Crenarchaeota."; RL PLoS ONE 6:E24222-E24222(2011). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; FN869859; CCC82551.1; -; Genomic_DNA. DR RefSeq; WP_014127804.1; NC_016070.1. DR STRING; 768679.TTX_1937; -. DR EnsemblBacteria; CCC82551; CCC82551; TTX_1937. DR GeneID; 11262820; -. DR KEGG; ttn:TTX_1937; -. DR PATRIC; fig|768679.9.peg.1960; -. DR eggNOG; arCOG00353; Archaea. DR eggNOG; COG2262; LUCA. DR KO; K03665; -. DR OMA; FNNHAHV; -. DR Proteomes; UP000002654; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000002654}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000002654}. FT DOMAIN 186 338 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 399 AA; 45331 MW; 68D69A7628564DA2 CRC64; MRNRALLAYV GPKDKSLARR LNEFRVLAEL AGYEPIDVVV QYGEPDSRFY FGSGKLKEIA GRDFDVLITY HGLSPLQMYN LRSTTRAEVL DRVMVILKIF EKRAGNIESK LQIELASLRY QLPILKEYVR RAKMGEQLGF MGAGEYAIDS LYRHTVRRIA TIKRKLDLMR ANRTSLIKKR RDLGVPEVVL TGYTSVGKTT LFNRLTAEHK YVDGKPFATL DTYSRRISLW GKELIITDTI GFIEDLPPVL IESFYSTLEE VSQADLILLV ADVSDDVDSF TRELQTSLDV LSTLGVYRER ILPVLNKVDR VSAIELIAKA YIVRKYFDVF VPVSAMTGFG ITTLKILLFW RTPGYAIYEA RPPAGGLILD GKSYIPVKVG EAESFEREAS LYTNLRRVL // ID G4T2J9_META2 Unreviewed; 420 AA. AC G4T2J9; DT 14-DEC-2011, integrated into UniProtKB/TrEMBL. DT 14-DEC-2011, sequence version 1. DT 07-JUN-2017, entry version 43. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:CCE24728.1}; GN OrderedLocusNames=MEALZ_3062 {ECO:0000313|EMBL:CCE24728.1}; OS Methylomicrobium alcaliphilum (strain DSM 19304 / NCIMB 14124 / VKM OS B-2133 / 20Z). OC Bacteria; Proteobacteria; Gammaproteobacteria; Methylococcales; OC Methylococcaceae; Methylomicrobium. OX NCBI_TaxID=1091494 {ECO:0000313|Proteomes:UP000008315}; RN [1] {ECO:0000313|Proteomes:UP000008315} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 19304 / NCIMB 14124 / VKM B-2133 / 20Z RC {ECO:0000313|Proteomes:UP000008315}; RX PubMed=22207753; DOI=10.1128/JB.06392-11; RA Vuilleumier S., Khmelenina V.N., Bringel F., Reshetnikov A.S., RA Lajus A., Mangenot S., Rouy Z., Op den Camp H.J., Jetten M.S., RA Dispirito A.A., Dunfield P., Klotz M.G., Semrau J.D., Stein L.Y., RA Barbe V., Medigue C., Trotsenko Y.A., Kalyuzhnaya M.G.; RT "Genome sequence of the haloalkaliphilic methanotrophic bacterium RT Methylomicrobium alcaliphilum 20Z."; RL J. Bacteriol. 194:551-552(2012). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; FO082060; CCE24728.1; -; Genomic_DNA. DR RefSeq; WP_014149490.1; NC_016112.1. DR EnsemblBacteria; CCE24728; CCE24728; MEALZ_3062. DR KEGG; mah:MEALZ_3062; -. DR PATRIC; fig|271065.3.peg.3156; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR Proteomes; UP000008315; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000008315}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000008315}. FT DOMAIN 196 363 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 420 AA; 46924 MW; 3735E7E37ADE0FDC CRC64; MFERPNAGER AVLVHLTLHT SPEDLSELKE LAKSAGADPV YVLTGSRQSP DSKYFIGTGK LEELKQAISE YSADIVLFNH PLSPSQERNL EKALEVRVVD RNGLILDIFA QRAQTFEGKL QVELAQLRHL STRLIRGWTH LERQKGGIGL RGPGETQLET DRRLLGVRIK QIQRRLNKVA KQRHQGRSKR KKAEVPSVSL VGYTNAGKST LFNTMTGAEI YAADQLFATL DPTLRQCVLP NNAEIVLADT VGFIRHLPHE LVAAFRSTLQ EASEANLLLH VIDANAEDRD ETIAQVNQVL EDIEADEIRQ LQIFNKIDLL PDIEPHIDRD DEGNVLRVWL SAETGAGIDL LYQVLAEIFA SSKVRRQLSL LPTQGDVRAK LFRLGTVLEE EASDTGGWDL LVEIDKKHLG VLKSLDKLEA // ID G5C619_HETGA Unreviewed; 901 AA. AC G5C619; DT 14-DEC-2011, integrated into UniProtKB/TrEMBL. DT 14-DEC-2011, sequence version 1. DT 10-MAY-2017, entry version 18. DE SubName: Full=Putative GTP-binding protein 6 {ECO:0000313|EMBL:EHB16980.1}; GN ORFNames=GW7_12231 {ECO:0000313|EMBL:EHB16980.1}; OS Heterocephalus glaber (Naked mole rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; OC Hystricomorpha; Bathyergidae; Heterocephalus. OX NCBI_TaxID=10181 {ECO:0000313|EMBL:EHB16980.1, ECO:0000313|Proteomes:UP000006813}; RN [1] {ECO:0000313|EMBL:EHB16980.1, ECO:0000313|Proteomes:UP000006813} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=21993625; DOI=10.1038/nature10533; RA Kim E.B., Fang X., Fushan A.A., Huang Z., Lobanov A.V., Han L., RA Marino S.M., Sun X., Turanov A.A., Yang P., Yim S.H., Zhao X., RA Kasaikina M.V., Stoletzki N., Peng C., Polak P., Xiong Z., Kiezun A., RA Zhu Y., Chen Y., Kryukov G.V., Zhang Q., Peshkin L., Yang L., RA Bronson R.T., Buffenstein R., Wang B., Han C., Li Q., Chen L., RA Zhao W., Sunyaev S.R., Park T.J., Zhang G., Wang J., Gladyshev V.N.; RT "Genome sequencing reveals insights into physiology and longevity of RT the naked mole rat."; RL Nature 479:223-227(2011). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JH173471; EHB16980.1; -; Genomic_DNA. DR InParanoid; G5C619; -. DR Proteomes; UP000006813; Unassembled WGS sequence. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR CDD; cd01878; HflX; 1. DR InterPro; IPR011992; EF-hand-dom_pair. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR SUPFAM; SSF47473; SSF47473; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 4: Predicted; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000006813}; KW Reference proteome {ECO:0000313|Proteomes:UP000006813}. FT DOMAIN 720 884 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 237 286 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 901 AA; 99110 MW; EA5EA6598B45F75A CRC64; MCCAERPPSA SGLTLLLREP AALAQLKATP GLCASLPPGQ ADREREDKAG PAALEFVPTV PVPPKRPDPN LVSATPATRP AEVSCPCLTV VSITLTLCRT RELDKWTHTG RGPHGGHATP NMAPMADDGA TGNQGLGAAG ELGPLPDVLA GDTGTPGAAS VCLCSPGAML RAEHQPHQSP ASLLGARVAV CGARELIQSA VQCEGHQPGG WGREQHGTER AASMEMERRV MRGGGGKKKK KKKKKKKKKK KKKKKKKKKK KKKKKKKKKK KKKKKKKKKK KKKRKKKGSP LVFSCPLAAL RGLQPRDMKG SWPPSTGLAL LRFLWAFPGT CALVRRACGC PLYWKGPLFY GAGGERTGSV SVHKFDVVNT HPGLAFLKEA SEFHSRYITT VIQRIFYTVN RSWSGKITCA ELRRSSFLQN VALLEEEADI NQLPEFFSYE HFYVIYCKFW ELDTDHDLLI DAQDLARHSE HAEWQVAEAA ALVHTLDGWS VVQTVVVPTK TPHKKLIFGR GSLERLTERI RASPEITSVF LNVERMASPT KKELEAAWAV EVFDRFTIVL HIFRCNARTK EAKLQVALAE IPLLRSNLKH NVTRLDRKVG ASRYIMGSAP VVHELIRPLM SIQPAAGPRP VAFGTGVPEC EIQGAGIIVA HWGRPGTRPV FWGQDVDSPS RPPPWREGSP SCRSSSGWLK EKEMKIRRAL EQLRGKRVLL RKQRTRREFP VVSVLGYTNS GKTSLIRALT EDPAAQPRDQ LFATLDVTAH GAWLPSRVPV LYMDTVGFLS QLPHSLIQSF SATLEDVAHA DVLMHVRDIS HPESEQQKAT VLSTLRGLRL PAQLLDSMLE VHNKVDLVPG YSTAEPGALA VSARLGLGLR ELEASLDATV MEATGRRVLT LRVPLAGPQL R // ID G5F4V6_9ACTN Unreviewed; 436 AA. AC G5F4V6; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 07-JUN-2017, entry version 34. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=HMPREF1008_01466 {ECO:0000313|EMBL:EHF01842.1}; OS Olsenella sp. oral taxon 809 str. F0356. OC Bacteria; Actinobacteria; Coriobacteriia; Coriobacteriales; OC Atopobiaceae; Olsenella. OX NCBI_TaxID=661087 {ECO:0000313|EMBL:EHF01842.1, ECO:0000313|Proteomes:UP000003446}; RN [1] {ECO:0000313|EMBL:EHF01842.1, ECO:0000313|Proteomes:UP000003446} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=F0356 {ECO:0000313|EMBL:EHF01842.1, RC ECO:0000313|Proteomes:UP000003446}; RG The Broad Institute Genome Sequencing Platform; RA Earl A., Ward D., Feldgarden M., Gevers D., Izard J., Blanton J.M., RA Baranova O.V., Tanner A.C., Dewhirst F.E., Young S.K., Zeng Q., RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L., RA Arachchi H.M., Berlin A., Brown A., Chapman S.B., Chen Z., Dunbar C., RA Freedman E., Gearin G., Gellesch M., Goldberg J., Griggs A., Gujja S., RA Heiman D., Howarth C., Larson L., Lui A., MacDonald P.J.P., RA Montmayeur A., Murphy C., Neiman D., Pearson M., Priest M., RA Roberts A., Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., RA Wortman J., Nusbaum C., Birren B.; RT "The Genome Sequence of Olsenella sp. oral taxon 809 strain F0356."; RL Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EHF01842.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACVE01000009; EHF01842.1; -; Genomic_DNA. DR RefSeq; WP_009279256.1; NZ_JH376563.1. DR EnsemblBacteria; EHF01842; EHF01842; HMPREF1008_01466. DR PATRIC; fig|661087.3.peg.1478; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000003446; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000003446}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000003446}. FT DOMAIN 210 375 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 436 AA; 48055 MW; D840641D962A3310 CRC64; MSRFEPLSTV PVPERAILVG VDLGRGGWPL EDSLAELGRL AKTDGAEVVS TVTQRLDSPV PRTFIGSGKA QELVSLVRNL SADVVIFDDE LSPSQQSNLE RILGEPTKVI DRTALILDIF GQHATTHEGR LQVQLAQLQY VLPRLRGMWG HLVGEQTRGG IGSRFGQGES QLEVDRRLVR DRISWLRREL RELEGRRRVQ SKARWDSGIY RVALVGYTNA GKSTLLNQLT GSEVYAKDEL FATLDPTTRR LELEEGRKIT LTDTVGFIQK LPTTLVESFK STLAEVRAAD LVLKVVDASD SNARKQLAAV DDVLADIESD KIPSVVVYNK CDLLDADERN VLSASHPDAV LLSALGSWGL RGLLYRIAQE ASRDDVTITA LVPYDKGLLM KMVHERCQVV REEYVQGGLM ATVRASSRMA ETLAPYVVRA SDVAGS // ID G5GD40_9BACT Unreviewed; 421 AA. AC G5GD40; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 07-JUN-2017, entry version 36. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=HMPREF9332_01588 {ECO:0000313|EMBL:EHG22073.1}; OS Alloprevotella rava F0323. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Prevotellaceae; OC Alloprevotella. OX NCBI_TaxID=679199 {ECO:0000313|EMBL:EHG22073.1, ECO:0000313|Proteomes:UP000015993}; RN [1] {ECO:0000313|EMBL:EHG22073.1, ECO:0000313|Proteomes:UP000015993} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=F0323 {ECO:0000313|EMBL:EHG22073.1, RC ECO:0000313|Proteomes:UP000015993}; RG The Broad Institute Genome Sequencing Platform; RA Earl A., Ward D., Feldgarden M., Gevers D., Izard J., Blanton J.M., RA Baranova O.V., Tanner A.C., Dewhirst F.E., Young S.K., Zeng Q., RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L., RA Arachchi H.M., Berlin A., Brown A., Chapman S.B., Chen Z., Dunbar C., RA Freedman E., Gearin G., Gellesch M., Goldberg J., Griggs A., Gujja S., RA Heiman D., Howarth C., Larson L., Lui A., MacDonald P.J.P., RA Montmayeur A., Murphy C., Neiman D., Pearson M., Priest M., RA Roberts A., Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., RA Wortman J., Nusbaum C., Birren B.; RT "The Genome Sequence of Prevotella sp. oral taxon 302 str. F0323."; RL Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EHG22073.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACZK01000025; EHG22073.1; -; Genomic_DNA. DR RefSeq; WP_009348100.1; NZ_JH376832.1. DR EnsemblBacteria; EHG22073; EHG22073; HMPREF9332_01588. DR PATRIC; fig|679199.3.peg.1778; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000015993; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000015993}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000015993}. FT DOMAIN 216 400 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 421 AA; 48247 MW; 6A17FA9BCB80B6C2 CRC64; MFEIEKIENR VEKAVLVALI TKTQDERQAN EYLDELAFLA ETAGAECVKR FTQKLDGPHS VTYVGKGKLE EMRRWIESEL EAERDVDMVV FDDELSAKQI RNIENELKVR VIDRTQLILD IFAMRAQTAN AKTQVELAQY KYMLPRLQRM WTHLERQGGG SGSGGGKGAV GLRGPGETQL EMDRRIILNR MALLKSRLSE IDKQKRTQRS NRGRMIRVAL VGYTNVGKST LLNLMAKTEV FAENKLFATL DTTVRKVVID NLPFLLSDTV GFIRKIPTDL VDSFKSTLDE VREADLLLHV VDISHPDFEE QIDVVNRTLA DLGCAEKPVI IVFNKVDAYT WTEKEADDLT PAGSENVSLV ELQQTWMNKM GENCIFISAR ERLNIDELRD LLYNRVRQLH VQKYPYNDFL FNQYDNDGRP L // ID G5GG63_9FIRM Unreviewed; 429 AA. AC G5GG63; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 07-JUN-2017, entry version 32. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=HMPREF9333_00552 {ECO:0000313|EMBL:EHI56273.1}; OS Johnsonella ignava ATCC 51276. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Lachnospiraceae; OC Johnsonella. OX NCBI_TaxID=679200 {ECO:0000313|EMBL:EHI56273.1, ECO:0000313|Proteomes:UP000003011}; RN [1] {ECO:0000313|EMBL:EHI56273.1, ECO:0000313|Proteomes:UP000003011} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51276 {ECO:0000313|EMBL:EHI56273.1, RC ECO:0000313|Proteomes:UP000003011}; RG The Broad Institute Genome Sequencing Platform; RA Earl A., Ward D., Feldgarden M., Gevers D., Izard J., Blanton J.M., RA Baranova O.V., Dewhirst F.E., Young S.K., Zeng Q., Gargeya S., RA Fitzgerald M., Haas B., Abouelleil A., Alvarado L., Arachchi H.M., RA Berlin A., Brown A., Chapman S.B., Chen Z., Dunbar C., Freedman E., RA Gearin G., Gellesch M., Goldberg J., Griggs A., Gujja S., Heiman D., RA Howarth C., Larson L., Lui A., MacDonald P.J.P., Montmayeur A., RA Murphy C., Neiman D., Pearson M., Priest M., Roberts A., Saif S., RA Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., Wortman J., RA Nusbaum C., Birren B.; RT "The Genome Sequence of Johnsonella ignava ATCC 51276."; RL Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EHI56273.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACZL01000011; EHI56273.1; -; Genomic_DNA. DR RefSeq; WP_005539683.1; NZ_JH378830.1. DR EnsemblBacteria; EHI56273; EHI56273; HMPREF9333_00552. DR PATRIC; fig|679200.3.peg.583; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000003011; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000003011}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000003011}. FT DOMAIN 209 374 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 429 AA; 48127 MW; 9936E9DE20571485 CRC64; MENRYNKLKE NKLIETSDIQ ERVILVGVSL GDLASTEDSL DELEQLADTA GAVTVGKLVQ NLDRINPATY IGKGKLDELK LAIFELDATG VICDDELSPA QLKNLENELE IKVMDRTLLI LDIFAQRAST SEGKIQVELA QLKYLSARLA GMRASLSRLG GGIGTRGPGE KKIDIDKRII HNRIGILKAQ LQEIKKHREI TRKTRKNIVT AAIWGYTNAG KSTLLNALAD SDVFVENKLF ATLDPSTRRV KLKSGQEILV TDTVGFIRKL PHNLIEAFRS TFEEAAYADI IIHLVDASNP AADEHMLVVY EALKSFDISD KDIITVYNKI DIAGTEFTLP RDFHSDYSIK ISAKTGYGID ELKDLIEKIV RGRRVYIDRV FAYKDAGIIN EIHSKGEMVF EEFLKDGIHI KAWIDARIYE RIISKTINR // ID G5H7H8_9BACT Unreviewed; 401 AA. AC G5H7H8; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 07-JUN-2017, entry version 32. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=HMPREF9450_01021 {ECO:0000313|EMBL:EHB92817.1}; OS Alistipes indistinctus YIT 12060. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Rikenellaceae; OC Alistipes. OX NCBI_TaxID=742725 {ECO:0000313|EMBL:EHB92817.1, ECO:0000313|Proteomes:UP000006008}; RN [1] {ECO:0000313|EMBL:EHB92817.1, ECO:0000313|Proteomes:UP000006008} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=YIT 12060 {ECO:0000313|EMBL:EHB92817.1, RC ECO:0000313|Proteomes:UP000006008}; RG The Broad Institute Genome Sequencing Platform; RA Earl A., Ward D., Feldgarden M., Gevers D., Morotomi M., Young S.K., RA Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., RA Alvarado L., Arachchi H.M., Berlin A., Brown A., Chapman S.B., RA Chen Z., Dunbar C., Freedman E., Gearin G., Gellesch M., Goldberg J., RA Griggs A., Gujja S., Heiman D., Howarth C., Larson L., Lui A., RA MacDonald P.J.P., Montmayeur A., Murphy C., Neiman D., Pearson M., RA Priest M., Roberts A., Saif S., Shea T., Shenoy N., Sisk P., RA Stolte C., Sykes S., Wortman J., Nusbaum C., Birren B.; RT "The Genome Sequence of Alistipes indistinctus YIT 12060."; RL Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EHB92817.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADLD01000009; EHB92817.1; -; Genomic_DNA. DR RefSeq; WP_009133827.1; NZ_JH370371.1. DR EnsemblBacteria; EHB92817; EHB92817; HMPREF9450_01021. DR PATRIC; fig|742725.3.peg.1079; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000006008; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000006008}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000006008}. FT DOMAIN 206 390 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 174 201 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 401 AA; 45762 MW; B2D2A5DCE471B817 CRC64; MGETKTTNTT DGRGQTAVLV AVMNDRQDET QVTEYLDELE FLAETAGVRT LKRFVQRLAN PNSRTFVGEG KLAEIAAYVE ENEVDFVIFD DELSPSQIRN LDKVFSRKIY DRTSLILEIF AQRATTAYAK TQVELAQCQY LLPRLTGMWT HLERQRGGTG TRGGAGEREI ETDRRIVRDR ISRLKEQLKK IDKQMAVQRS NRGQLVRVAL VGYTNVGKST IMNLISKSEV FAENKLFATL DTTVRKVVLD NLPFLLSDTV GFIRKLPHQL VESFKSTLDE VREADLLLHV VDISHPNFEE QIAVVKETLQ EIGAGEKPVF LIFNKIDAYS FIQKDEDDLT PATKENMTLD ELKNSWIAKA NTPCIFISAR ERINIDKLRK DLYGMVREIH AGRYPFNNFL Y // ID G5IDB0_9CLOT Unreviewed; 417 AA. AC G5IDB0; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 07-JUN-2017, entry version 35. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=HMPREF9473_01487 {ECO:0000313|EMBL:EHI60522.1}; OS Hungatella hathewayi WAL-18680. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Hungatella. OX NCBI_TaxID=742737 {ECO:0000313|EMBL:EHI60522.1, ECO:0000313|Proteomes:UP000005384}; RN [1] {ECO:0000313|EMBL:EHI60522.1, ECO:0000313|Proteomes:UP000005384} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=WAL-18680 {ECO:0000313|EMBL:EHI60522.1, RC ECO:0000313|Proteomes:UP000005384}; RG The Broad Institute Genome Sequencing Platform; RA Earl A., Ward D., Feldgarden M., Gevers D., Finegold S.M., RA Summanen P.H., Molitoris D.R., Song M., Daigneault M., RA Allen-Vercoe E., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., RA Haas B., Abouelleil A., Alvarado L., Arachchi H.M., Berlin A., RA Brown A., Chapman S.B., Chen Z., Dunbar C., Freedman E., Gearin G., RA Gellesch M., Goldberg J., Griggs A., Gujja S., Heiman D., Howarth C., RA Larson L., Lui A., MacDonald P.J.P., Montmayeur A., Murphy C., RA Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T., RA Shenoy N., Sisk P., Stolte C., Sykes S., Wortman J., Nusbaum C., RA Birren B.; RT "The Genome Sequence of Clostridium hathewayi WAL-18680."; RL Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EHI60522.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADLN01000016; EHI60522.1; -; Genomic_DNA. DR RefSeq; WP_006779473.1; NZ_JH379027.1. DR EnsemblBacteria; EHI60522; EHI60522; HMPREF9473_01487. DR PATRIC; fig|742737.3.peg.1504; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000005384; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000005384}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000005384}. FT DOMAIN 202 368 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 417 AA; 47001 MW; 15371C5ED1921979 CRC64; MAELIDLKEV EERVILIGVQ TSEEDDTMNC LNELEELVKT AGAATVDKII QNRERIHPGT YLGKGKIEEV KERIWELDAT GVVCDDELSP AQLRNLEQAL DTKVMDRTMV ILDIFASRAN TSEGKIQVEL AQLKYRAARL VGLRSSLSRL GGGIGTRGPG EKKLEMDRRL IHERIGQLKA ELRDVERHRD VMRQQRSKNH TTVAAIVGYT NAGKSTLLNL LTDAGILAED KLFATLDPTT RNLELPSGQQ ILLTDTVGFI RKLPHHLIEA FKSTLEEARY SDIILHVVDC SNPQMDMQMY TVYETLKQLE VTGKIMVTIY NKIDKIEEEE RRLPKDLSAD YQLAISAKTG EGIGELKDTL EMILRNQKVY LEKIYPYNEA GRIQAIRKYG ELLSEEYGED GITVKAYVPA AVYGQLV // ID G5K695_9STRE Unreviewed; 387 AA. AC G5K695; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 05-JUL-2017, entry version 37. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:EHI68755.1}; GN ORFNames=STRIC_0582 {ECO:0000313|EMBL:EHI68755.1}; OS Streptococcus ictaluri 707-05. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=764299 {ECO:0000313|EMBL:EHI68755.1, ECO:0000313|Proteomes:UP000003330}; RN [1] {ECO:0000313|EMBL:EHI68755.1, ECO:0000313|Proteomes:UP000003330} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=707-05 {ECO:0000313|EMBL:EHI68755.1, RC ECO:0000313|Proteomes:UP000003330}; RX PubMed=24625962; DOI=10.1093/gbe/evu048; RA Richards V.P., Palmer S.R., Pavinski Bitar P.D., Qin X., RA Weinstock G.M., Highlander S.K., Town C.D., Burne R.A., Stanhope M.J.; RT "Phylogenomics and the dynamic genome evolution of the genus RT Streptococcus."; RL Genome Biol. Evol. 6:741-753(2014). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EHI68755.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AEUX02000008; EHI68755.1; -; Genomic_DNA. DR STRING; 764299.STRIC_0582; -. DR EnsemblBacteria; EHI68755; EHI68755; STRIC_0582. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000003330; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000003330}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000003330}. FT DOMAIN 174 334 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 133 167 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 387 AA; 44098 MW; 9452D6F21F049491 CRC64; MSMTELANLA KTAGAQVVDS YTQKRERYDS KTFIGSGKLA EIKEIVDANE IDTVIVNNRL TARQNANLEA ALEVKVIDRM QLILDIFAMR ARSHEGKLQV HLAQLKYMLP RLVGQGIMLS RQAGGIGSRG PGESQLELNR RSIRHQIADI ERQLGLVEKN RQTIRDRRVS SDTFKIGLIG YTNAGKSTIM NLLTDNKQYE ANELFATLDA TTKQLYLQNQ FQATLTDTVG FIQDLPTELV AAFKSTLEES RHVDLLLHVI DASDPNHAEQ EKVVLDLLKD LEMLEIPRLA IYNKMDMTDS LTATVFPNVR LSAREKGISH QLRRLLIDQI RDLFDPFSIK VHQDKAYKLY DLNKVALLDS YSFDIEIEEI SGYISPKNRW RLEEFYE // ID G5KH30_9STRE Unreviewed; 418 AA. AC G5KH30; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 07-JUN-2017, entry version 35. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:EHJ57593.1}; GN ORFNames=STRUR_1424 {ECO:0000313|EMBL:EHJ57593.1}; OS Streptococcus urinalis 2285-97. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=764291 {ECO:0000313|EMBL:EHJ57593.1, ECO:0000313|Proteomes:UP000005388}; RN [1] {ECO:0000313|EMBL:EHJ57593.1, ECO:0000313|Proteomes:UP000005388} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=2285-97 {ECO:0000313|EMBL:EHJ57593.1}; RX PubMed=24625962; DOI=10.1093/gbe/evu048; RA Richards V.P., Palmer S.R., Pavinski Bitar P.D., Qin X., RA Weinstock G.M., Highlander S.K., Town C.D., Burne R.A., Stanhope M.J.; RT "Phylogenomics and the dynamic genome evolution of the genus RT Streptococcus."; RL Genome Biol. Evol. 6:741-753(2014). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EHJ57593.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AEUZ02000001; EHJ57593.1; -; Genomic_DNA. DR RefSeq; WP_006740295.1; NZ_AEUZ02000001.1. DR STRING; 764291.STRUR_1424; -. DR EnsemblBacteria; EHJ57593; EHJ57593; STRUR_1424. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000005388; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000005388}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000005388}. FT DOMAIN 205 365 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 164 198 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 418 AA; 47998 MW; 9850735DAE46EA07 CRC64; MKRGTKMIDT SQKEERVILL GVSLQNTQNF EMSMQELANL AKTAGANVVA TYYQNREKYD SKTFIGSGKL TELKNMIDAD EIDSVIVNNR LTPRQNSNLE NLLEVKVIDR MQLILDIFAL RARSHEGKLQ VHLAQLKYML PRLVGQGVML SRQAGGIGSR GPGESQLELN RRSIRNQIND IERQLKIVEK NRQTIREKRL DAKTFKIGLI GYTNAGKSTI MNLLVDDFQY EADELFATLN ATTKQIYLQN QFQATLTDTV GFIQDLPTEL IAAFRSTLEE SRHVDLLLHV IDASDPSHTE HEKVVNDILE DLGMNDIPKL AIYNKMDKVE QLTATAFPNV RLSAYKSDST DRLRKLIIDE IRDIFIPFSI KVHQKDLYKL YELNKIALIE PYQFENEVEE ISGYISEKNR WYLEAFYD // ID G5LXB4_SALET Unreviewed; 440 AA. AC G5LXB4; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 30-AUG-2017, entry version 34. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=LTSEALA_6077 {ECO:0000313|EMBL:EHC28705.1}; OS Salmonella enterica subsp. enterica serovar Alachua str. R6-377. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; OC Enterobacteriaceae; Salmonella. OX NCBI_TaxID=913241 {ECO:0000313|EMBL:EHC28705.1, ECO:0000313|Proteomes:UP000004642}; RN [1] {ECO:0000313|EMBL:EHC28705.1, ECO:0000313|Proteomes:UP000004642} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=R6-377 {ECO:0000313|EMBL:EHC28705.1, RC ECO:0000313|Proteomes:UP000004642}; RX PubMed=21859443; DOI=10.1186/1471-2164-12-425; RA den Bakker H.C., Moreno Switt A.I., Govoni G., Cummings C.A., RA Ranieri M.L., Degoricija L., Hoelzer K., Rodriguez-Rivera L.D., RA Brown S., Bolchacova E., Furtado M.R., Wiedmann M.; RT "Genome sequencing reveals diversification of virulence factor content RT and possible host adaptation in distinct subpopulations of Salmonella RT enterica."; RL BMC Genomics 12:425-425(2011). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EHC28705.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFCJ01002568; EHC28705.1; -; Genomic_DNA. DR EnsemblBacteria; EHC28705; EHC28705; LTSEALA_6077. DR PATRIC; fig|913241.3.peg.4670; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000004642; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000004642}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}. FT DOMAIN 198 365 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 164 191 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 440 AA; 49855 MW; 4FC3C18F214A95C1 CRC64; MFDRYDAGEQ AVLVHIYFSQ DKDMEDLQEF ESLVSSAGVE AMQVITGSRK APHPKYFVGE GKAVEIAEAV KATGAAVVLF DHALSPAQER NLERLCECRV IDRTGLILDI FAQRARTHEG KLQVELAQLR HLATRLVRGW THLERQKGGI GLRGPGETQL ETDRRLLRNR IVQIQSRLEK VEKQREQGRQ SRIKADVPTV SLVGYTNAGK STLFNQITEA RVYAADQLFA TLDPTLRRID VADVGETVLA DTVGFIRHLP HDLVAAFKAT LQETRQATLL LHVVDAADVR VQENIEAVNT VLEEIDAHEI PTLMVMNKID MLDDFEPRID RDEENKPIRV WLSAQSGVGI PQLFQALTER LSGEVAQHTL HTLRLPPQVA QHTLRLPPQE GRLRSRFYQL QAIEKEWMEE DGSVSLQVRM PIVDWRRLCK QEPALIEYVI // ID G5ZWQ3_9PROT Unreviewed; 435 AA. AC G5ZWQ3; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 07-JUN-2017, entry version 33. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=HIMB100_00004470 {ECO:0000313|EMBL:EHI49486.1}; OS SAR116 cluster alpha proteobacterium HIMB100. OC Bacteria; Proteobacteria; Alphaproteobacteria; SAR116 cluster. OX NCBI_TaxID=909943 {ECO:0000313|EMBL:EHI49486.1, ECO:0000313|Proteomes:UP000004261}; RN [1] {ECO:0000313|EMBL:EHI49486.1, ECO:0000313|Proteomes:UP000004261} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=strain HIMB100 {ECO:0000313|Proteomes:UP000004261}; RX PubMed=22675578; DOI=10.4056/sigs.1854551; RA Grote J., Bayindirli C., Bergauer K., Carpintero de Moraes P., RA Chen H., D'Ambrosio L., Edwards B., Fernandez-Gomez B., Hamisi M., RA Logares R., Nguyen D., Rii Y.M., Saeck E., Schutte C., Widner B., RA Church M.J., Steward G.F., Karl D.M., Delong E.F., Eppley J.M., RA Schuster S.C., Kyrpides N.C., Rappe M.S.; RT "Draft genome sequence of strain HIMB100, a cultured representative of RT the SAR116 clade of marine Alphaproteobacteria."; RL Stand. Genomic Sci. 5:269-278(2011). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EHI49486.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFXB01000004; EHI49486.1; -; Genomic_DNA. DR RefSeq; WP_009604033.1; NZ_AFXB01000004.1. DR EnsemblBacteria; EHI49486; EHI49486; HIMB100_00004470. DR PATRIC; fig|909943.3.peg.456; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000004261; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000004261}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000004261}. FT DOMAIN 201 372 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 160 187 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 435 AA; 47735 MW; B1B1751C7CA8C235 CRC64; MGLQTAFIVQ PELKQASQSG STRTPQTKLD EAAGLAEAIQ LDVVHKEIIT LSKPRSGTYL GPGVVDRLAG LAEYHDHPLF IINTSLSPVQ HRNLETALKC KVIDRTALIL EIFGARASTH AGRLQVELAA LSFQKSRLVR SWTHLERQRG GGGFLGGPGE RQIELDRRML TDQVKQIKKE LSDVERTRGL QRRNRDRSET PTIALVGYTN AGKSTLFNRL TGADVLSKDM LFATLDPTMR GMHLPSGRQI VLADTVGFIS ALPTELVEAF KSTLEEVVQA DLILHVHDMS SELCAEEALD VATVLDDIGF DEQARDDRIL HIFNKADAAV EDVELPFITT GASGRALTCS ALTGTGVDDV LAQIDRFFAK SDSLCEFTLN PDYGAASAWL HQHARIINSH YDDAGQHIVK ASISQANKAR FKKQWPMASI HETGL // ID G6EJ00_9SPHN Unreviewed; 446 AA. AC G6EJ00; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 07-JUN-2017, entry version 37. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:EHJ58759.1}; GN ORFNames=NSU_4321 {ECO:0000313|EMBL:EHJ58759.1}; OS Novosphingobium pentaromativorans US6-1. OC Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales; OC Sphingomonadaceae; Novosphingobium. OX NCBI_TaxID=1088721 {ECO:0000313|EMBL:EHJ58759.1, ECO:0000313|Proteomes:UP000004030}; RN [1] {ECO:0000313|EMBL:EHJ58759.1, ECO:0000313|Proteomes:UP000004030} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=US6-1 {ECO:0000313|EMBL:EHJ58759.1, RC ECO:0000313|Proteomes:UP000004030}; RX PubMed=22275104; DOI=10.1128/JB.06476-11; RA Luo Y.R., Kang S.G., Kim S.J., Kim M.R., Li N., Lee J.H., Kwon K.K.; RT "Genome sequence of benzo(a)pyrene-degrading bacterium Novosphingobium RT pentaromativorans US6-1."; RL J. Bacteriol. 194:907-907(2012). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EHJ58759.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGFM01000065; EHJ58759.1; -; Genomic_DNA. DR RefSeq; WP_007015229.1; NZ_CP009291.1. DR EnsemblBacteria; EHJ58759; EHJ58759; NSU_4321. DR KEGG; npn:JI59_03565; -. DR PATRIC; fig|1088721.3.peg.4258; -. DR KO; K03665; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000004030; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000004030}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000004030}. FT DOMAIN 206 390 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 446 AA; 49007 MW; 1EE37EA0E5D8672E CRC64; MNDELKGEVT RGARALVVYP QMRGKGDLDP EARLEEAKGL ALAIGLVIAD AIAIPIREPR PGTLFGEGQI QNIATACELN EAELIIVDGS LSAIQQRNLE EKFKRKVIDR TGLILEIFGE RAATAEGRLQ VELAHLDYQA GRLVRSWTHL ERQRGGFGFL GGPGETQIEA DRRMIRDRMA KIRRELEQVR RTRGLHRDRR EKAPWPIVAL VGYTNAGKST LFNRLTGAEV MAQNLLFATL DPTMRAIRLP GVEKAILSDT VGFISDLPTQ LVAAFRATLE EVTAADLILH VRDIANPDTD AQKRQVLDVL GDLGVLGSEV DDEAEEGAEP GIPIIELWNK WDLLGPEHAE KLREAIAHRE DEAIVPISAV MGEGCEHLME VVGHALTADS KVYSFLLPAA DGQRIAFLHA RGEVISEEDA GEGADGPLLR LQVRLAAREL GRFQAL // ID G6EZA2_9PROT Unreviewed; 430 AA. AC G6EZA2; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 07-JUN-2017, entry version 31. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=CIN_07720 {ECO:0000313|EMBL:EHD14840.1}; OS Commensalibacter intestini A911. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales; OC Acetobacteraceae. OX NCBI_TaxID=1088868 {ECO:0000313|EMBL:EHD14840.1, ECO:0000313|Proteomes:UP000005939}; RN [1] {ECO:0000313|EMBL:EHD14840.1, ECO:0000313|Proteomes:UP000005939} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=A911 {ECO:0000313|EMBL:EHD14840.1, RC ECO:0000313|Proteomes:UP000005939}; RA Lee W.-J., Kim E.-K.; RT "Genome Sequence of Commensalibacter intestini A911, isolated from RT Drosophila gut."; RL Submitted (OCT-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EHD14840.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGFR01000003; EHD14840.1; -; Genomic_DNA. DR RefSeq; WP_008853762.1; NZ_AGFR01000003.1. DR EnsemblBacteria; EHD14840; EHD14840; CIN_07720. DR PATRIC; fig|1088868.3.peg.774; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000005939; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000005939}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000005939}. FT DOMAIN 207 376 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 430 AA; 48812 MW; 51901364C8DC0312 CRC64; MTDFDSAHQT TRAAVIVPWD ISNRQSNNRN SQSRLEEAIG LASSIRLEIS HTEIINLRSY RSATLIGQGH IESLKDSIQS NEIDIAIFDT RLSPIQQRNL EKALECKVID RTALILDIFG ERAQTKEGTL QVELAHLQYQ RSRLVRSWTH LERQRGGFGF MGGPGETQIE ADRRLIDERI IRLKKDLEQV RRTRGLHRKA RQKVPFPIVA LIGYTNAGKS TLFNNLTGAD VHAQDQLFAT LDPTMRKLQL PSGKTIILSD TVGFISDLPT ELIAAFRATL EETAEADIIL HVRDISHPET TEQRQDVFSV LDTMVKDQIL EADWRKNTIE VLNKIDLIEN IALIDKPKDF IGISALTSEN LPSLIQMIDD RLAKMMEEIT FVIPVSDGAA LSWLYNHGEI LQRNDDENHM TILVRLSPAN KARFEQLYSY // ID G6FTM8_9CYAN Unreviewed; 604 AA. AC G6FTM8; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 07-JUN-2017, entry version 33. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=FJSC11DRAFT_2225 {ECO:0000313|EMBL:EHC13961.1}; OS Fischerella sp. JSC-11. OC Bacteria; Cyanobacteria; Nostocales; Hapalosiphonaceae; Fischerella. OX NCBI_TaxID=741277 {ECO:0000313|EMBL:EHC13961.1, ECO:0000313|Proteomes:UP000004344}; RN [1] {ECO:0000313|EMBL:EHC13961.1, ECO:0000313|Proteomes:UP000004344} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=JSC-11 {ECO:0000313|EMBL:EHC13961.1, RC ECO:0000313|Proteomes:UP000004344}; RG US DOE Joint Genome Institute (JGI-PGF); RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S., RA Peters L., Land M.L., Hauser L., Sarkisova S., Bryant D.A., Brown I., RA Woyke T.J.; RT "The draft genome of Fischerella sp. JSC-11."; RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EHC13961.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGIZ01000006; EHC13961.1; -; Genomic_DNA. DR RefSeq; WP_009456810.1; NZ_AGIZ01000006.1. DR EnsemblBacteria; EHC13961; EHC13961; FJSC11DRAFT_2225. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000004344; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000004344}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000004344}. FT DOMAIN 431 601 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 390 427 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 604 AA; 66816 MW; 0F02CF2A3E7F2833 CRC64; MTSKQYCKIE RVGFGGPVHW SKTLIETIFG NLQGLKSSQL KQLQRLYHQR IPSDRITTPE FAQRLAAIST EINQPVCTYL NRRGQVIRVG VGTPRQTQIP PLELPRYGAE RLSGIRCIAT HLKSEPPNEA ALTSMALQRL DALVVINITG TGFQKRGGGA TGYVKEAYVA HLTSQESRAL ITSPSLKVAN GNVPSPSWNV SPPMSLDALA KQDLIDLVEG LEEDFRREFV AQEVDTDHDR AVIVGVMTDD LSSQQFHDIV AELGRLVDTA GGEVLQTLWQ KRSRIHPQTV VGEGKVQEIA LTAQTLGANL VVFDRDLSPS QVRNLETQIG VRVVDRTEVI LDIFAQRAQS RAGKLQVELA QLEYMLPRLS GRGQAMSRLG GGIGTRGPGE TKLETERRAI SRRISRLQQE VNQLQAHRER LRQRRQNREI PSVALVGYTN AGKSTLLNAL TNAEVYTADQ LFATLDPTTR RLVVPHAATN EPQEILITDT VGFIHELPAS LMDAFRATLE EVTEADALIH LVDLSHPAWL SHIRSVREIL AQMPVTPGPA LVVFNKIDQV SSETLAQARE EFPLAVFISA SKRLGLETLR QRLGQLVQYA TSSR // ID G6XLV9_9PROT Unreviewed; 435 AA. AC G6XLV9; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 07-JUN-2017, entry version 33. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=GMO_23590 {ECO:0000313|EMBL:EHH67364.1}; OS Gluconobacter morbifer G707. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales; OC Acetobacteraceae; Gluconobacter. OX NCBI_TaxID=1088869 {ECO:0000313|EMBL:EHH67364.1, ECO:0000313|Proteomes:UP000004949}; RN [1] {ECO:0000313|EMBL:EHH67364.1, ECO:0000313|Proteomes:UP000004949} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=G707 {ECO:0000313|EMBL:EHH67364.1, RC ECO:0000313|Proteomes:UP000004949}; RA Lee W.-J., Kim E.-K.; RT "Genome sequence of Gluconobacter morbifer G707, isolated from RT Drosophila gut."; RL Submitted (OCT-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EHH67364.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGQV01000010; EHH67364.1; -; Genomic_DNA. DR RefSeq; WP_008852501.1; NZ_AGQV01000010.1. DR EnsemblBacteria; EHH67364; EHH67364; GMO_23590. DR PATRIC; fig|1088869.3.peg.2353; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000004949; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000004949}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000004949}. FT DOMAIN 207 376 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 435 AA; 47885 MW; BDF6C5FFC87A7B42 CRC64; MSGFETQKPA TRAAVILPWE KSGPQEEIRA ADARLEEAVG LAASIGLVIV RKAAILLRAR RPSTLLGSGQ VEQLAEAVKL DGVDVVIIDA RLSPGQQRNL EKALGCKVVD RTGLILDIFG ARAATREGVL QVELAHLEYQ RSRLVRLWTH LERQRGGFGF LGGPGETQME ADRRMLAERI GKIKKELEQV RRTRGLHRDA RKRVPFPVVA LVGYTNAGKS TLFNALTGAS VQAENQLFAT LDPTMRALRL PSGRNVILSD TVGFISELPT ELVAAFRATL EEVSQADVIL HVRDVAHPDS AAQRADVLHV LDSMVRDGML DAQWPERTIE VLNKADLVGG VQAIPKRENA VAISAITGEG IPDLFEALDQ YLTRSMQDVR VRLSVTDGAA LAWLYDHGEV VERLDHDEGM DVTVRLFPQD RERFEIVYPG RLSAE // ID G6Y9N3_9RHIZ Unreviewed; 463 AA. AC G6Y9N3; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 05-JUL-2017, entry version 37. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=MEA186_13277 {ECO:0000313|EMBL:EHH11542.1}; OS Mesorhizobium amorphae CCNWGS0123. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Phyllobacteriaceae; Mesorhizobium. OX NCBI_TaxID=1082933 {ECO:0000313|EMBL:EHH11542.1, ECO:0000313|Proteomes:UP000002949}; RN [1] {ECO:0000313|EMBL:EHH11542.1, ECO:0000313|Proteomes:UP000002949} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CCNWGS0123 {ECO:0000313|EMBL:EHH11542.1, RC ECO:0000313|Proteomes:UP000002949}; RX PubMed=22247533; DOI=10.1128/JB.06475-11; RA Hao X., Lin Y., Johnstone L., Baltrus D.A., Miller S.J., Wei G., RA Rensing C.; RT "Draft Genome Sequence of Plant Growth-Promoting Rhizobium RT Mesorhizobium amorphae, Isolated from Zinc-Lead Mine Tailings."; RL J. Bacteriol. 194:736-737(2012). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGSN01000104; EHH11542.1; -; Genomic_DNA. DR RefSeq; WP_006202171.1; NZ_CP015318.1. DR EnsemblBacteria; EHH11542; EHH11542; MEA186_13277. DR GeneID; 32100208; -. DR KEGG; mamo:A6B35_19415; -. DR PATRIC; fig|1082933.3.peg.2573; -. DR KO; K03665; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000002949; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000002949}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}. FT DOMAIN 231 404 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 463 AA; 50937 MW; B876A95506DA21DD CRC64; MAREKDADRS VRGKLAHQPG TEAKGPTRAV VIVPVLTRHQ RSDDESNRPR LTRSAEARHD EAVGLARAIN LDLIHTAVAT VNDPRPATLL GSGKVEEFAE IVKEGHAEVV IVDHPLTPVQ QRNLEKELNA KVLDRTGLIL EIFGERARTK EGTLQVELAH LNYQKGRLVR SWTHLERQRG GAGFLGGPGE TQIESDRRIL QDKIIKLKHE LETVRRTRDL HRAKRKKVPF PVVAIVGYTN AGKSTLFNKL TGAGVLAEDM LFATLDPTLR RVRLPHGTPI ILSDTVGFIS DLPTHLVAAF RATLEEVVEA DLVIHLRDIS DPDTAAQAED VERILADLGV DAGDTKRVIE VWNKIDLLDE GNRARLLADG NDGRKAPPIA ISAVTGEGLD ALKALIETRM AGELEALTVT IEPAQFGLVD WLYRNGDVVS RTDNEDGSAT ISLKATHSAR QEIESRLHRK NNA // ID G7CIC3_MYCT3 Unreviewed; 478 AA. AC G7CIC3; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 07-JUN-2017, entry version 34. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=KEK_16563 {ECO:0000313|EMBL:EHI12530.1}; OS Mycobacterium thermoresistibile (strain ATCC 19527 / DSM 44167 / CIP OS 105390 / JCM 6362 / NCTC 10409 / 316). OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae; OC Mycobacterium. OX NCBI_TaxID=1078020 {ECO:0000313|EMBL:EHI12530.1, ECO:0000313|Proteomes:UP000004915}; RN [1] {ECO:0000313|EMBL:EHI12530.1, ECO:0000313|Proteomes:UP000004915} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 19527 / DSM 44167 / CIP 105390 / JCM 6362 / NCTC 10409 / RC 316 {ECO:0000313|Proteomes:UP000004915}; RG Tuberculosis Structural Genomics Consortium; RA Ioerger T.R.; RL Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EHI12530.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGVE01000046; EHI12530.1; -; Genomic_DNA. DR RefSeq; WP_003926794.1; NZ_AGVE01000046.1. DR EnsemblBacteria; EHI12530; EHI12530; KEK_16563. DR PATRIC; fig|1078020.3.peg.3261; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000004915; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 2. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000004915}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000004915}. FT DOMAIN 255 424 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 214 248 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 478 AA; 51995 MW; B812B6E169FFDEF5 CRC64; MTYPETPETP ETVRTAEAPS VGELELQDRA ALRRVAGLST ELTDVSEVEY RQLRLERVVL VGVWTEGTIA DAEASLAELA RLAETAGSQV LEGVIQRRDK PDPATYIGSG KARELRDIVV ATGADTVICD GELSPAQLTA LEKVVQVKVV DRTALILDIF AQHATSREGK AQVSLAQMEY MLPRLRGWGE SMSRQAGGRA GGSGGGVGLR GPGETKIETD RRRIRERMAR LRREIKEMKK VRDTKRHRRL ASAIPSIAIV GYTNAGKSSL LNALTDAGVL VEDALFATLE PTTRRGRFDD GRPFVLTDTV GFVRHLPTQL VEAFRSTLEE VIHADLLVHV VDGADANPLA QIDAVREVLR DVHADHDAPP APELLVVNKI DAASDLTLTQ LRRALPDAVF VSAHTGEGLD RLRQRMSELV APTETAVDVT IPYDRGDLVA RVHSDGRVDA TEHRADGTRI KARVPVALAA SLRDFATV // ID G7GVR6_9ACTN Unreviewed; 498 AA. AC G7GVR6; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 10-MAY-2017, entry version 33. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:GAB07691.1}; GN ORFNames=GOAMR_71_00440 {ECO:0000313|EMBL:GAB07691.1}; OS Gordonia amarae NBRC 15530. OC Bacteria; Actinobacteria; Corynebacteriales; Gordoniaceae; Gordonia. OX NCBI_TaxID=1075090 {ECO:0000313|EMBL:GAB07691.1, ECO:0000313|Proteomes:UP000006023}; RN [1] {ECO:0000313|EMBL:GAB07691.1, ECO:0000313|Proteomes:UP000006023} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NBRC 15530 {ECO:0000313|EMBL:GAB07691.1, RC ECO:0000313|Proteomes:UP000006023}; RA Takarada H., Hosoyama A., Tsuchikane K., Katsumata H., Yamazaki S., RA Fujita N.; RT "Whole genome shotgun sequence of Gordonia amarae NBRC 15530."; RL Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:GAB07691.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BAED01000071; GAB07691.1; -; Genomic_DNA. DR EnsemblBacteria; GAB07691; GAB07691; GOAMR_71_00440. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000006023; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000006023}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000006023}. FT DOMAIN 275 444 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 234 271 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 498 AA; 54041 MW; A7EA24EA6E3D0C3D CRC64; MTEFASQTSA PDLDEPDFDP DDFGPAIDDA PVSAFRMTPP TTGEQQLSDR ASLQRVAGLS TELEDVTEVE YRQLRLERVV LVGVWTEGTA AQAKASMVEL AALAETAGSQ VLDGLIQRRS TPDAATYIGS GKADELRQVV LSTGADTVIC DGELTPAQLT ALEKVVKVKV IDRTALILDI FAQHATSREG KAQVSLAQME YMLPRLRGWG ESMSRQAGGR AGSNGGVGLR GPGETKIETD RRRIRERMAK LRREIREMKT ARTTKRAARQ RSSIPKITVA GYTNAGKSSL VNAMTGSGVL VQDALFATLD PTTRRATLAD GREVVFTDTV GFVRHLPTQL VEAFRSTLEE VVDADLLLHV VDGSDPFPTE QIAAVRRVIN EIVAEEGVAP PPELLVVNKI DAIDENRRTE LRGILDGAMF VSAHTGEGLP ELFDRIRAEV ARNDVEVTIA VPFSRGDVVS RIHRDGEVLS TDHDEQGTIM RVRVPAAMAG ELAELRVS // ID G7H0F6_9ACTN Unreviewed; 489 AA. AC G7H0F6; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 10-MAY-2017, entry version 34. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:GAB09331.1}; GN ORFNames=GOARA_036_00630 {ECO:0000313|EMBL:GAB09331.1}; OS Gordonia araii NBRC 100433. OC Bacteria; Actinobacteria; Corynebacteriales; Gordoniaceae; Gordonia. OX NCBI_TaxID=1073574 {ECO:0000313|EMBL:GAB09331.1, ECO:0000313|Proteomes:UP000035088}; RN [1] {ECO:0000313|EMBL:GAB09331.1, ECO:0000313|Proteomes:UP000035088} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NBRC 100433 {ECO:0000313|EMBL:GAB09331.1, RC ECO:0000313|Proteomes:UP000035088}; RA Yoshida Y., Hosoyama A., Tsuchikane K., Katsumata H., Yamazaki S., RA Fujita N.; RT "Whole genome shotgun sequence of Gordonia araii NBRC 100433."; RL Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:GAB09331.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BAEE01000036; GAB09331.1; -; Genomic_DNA. DR EnsemblBacteria; GAB09331; GAB09331; GOARA_036_00630. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000035088; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000035088}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000035088}. FT DOMAIN 262 433 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 221 248 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 489 AA; 52478 MW; 64E5B0B0D93E8DFD CRC64; MTDHELTVAP DAVEDPGFAP LAPAAEPTTG ELQLDDRASL QRVAGLSTEL ADITEVEYRQ LRLERVVLVG VWTSGTAAQA HANMAELAAL AETAGSQVLD AVIQRRSSPD AATYIGSGKA AELRDIVVST GADTVIADGE LTPAQLTALE KVVKVKVIDR TALILDIFAQ HATSREGKAQ VALAQMEYML PRLRGWGESM SRQAGGRAGS NGGVGLRGPG ETKIETDRRR IRERMAKLRR EIRGMKTART VKRLDRRRSG VPTITVVGYT NAGKSSLVNA MTGSGVLVQN ALFATLDPTT RRARLDDGRE VVFTDTVGFV RHLPTQLVEA FRSTLEEVAD ADLLIHVVDG SETFPLDQVA AVRTVLGEVM TESAASAAPP PELLVVNKVD AMDELARAEL AAALPGAVFV SARTGEGLDE LFERIRSEVG RHDVEMYVTV PFDRGDLVSR IHADGEVQSA EHHESGTSMR VRVPAALAGE LEEFARSAK // ID G7I5C6_MEDTR Unreviewed; 545 AA. AC G7I5C6; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 30-AUG-2017, entry version 38. DE SubName: Full=GTP-binding protein HflX {ECO:0000313|EMBL:AES59578.1}; GN OrderedLocusNames=MTR_1g022980 {ECO:0000313|EMBL:AES59578.1}; OS Medicago truncatula (Barrel medic) (Medicago tribuloides). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae; OC Pentapetalae; rosids; fabids; Fabales; Fabaceae; Papilionoideae; OC Trifolieae; Medicago. OX NCBI_TaxID=3880 {ECO:0000313|EMBL:AES59578.1, ECO:0000313|Proteomes:UP000002051}; RN [1] {ECO:0000313|EMBL:AES59578.1, ECO:0000313|EnsemblPlants:AES59578, ECO:0000313|Proteomes:UP000002051} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=A17 {ECO:0000313|EMBL:AES59578.1}, and RC cv. Jemalong A17 {ECO:0000313|EnsemblPlants:AES59578, RC ECO:0000313|Proteomes:UP000002051}; RX PubMed=22089132; DOI=10.1038/nature10625; RA Young N.D., Debelle F., Oldroyd G.E.D., Geurts R., Cannon S.B., RA Udvardi M.K., Benedito V.A., Mayer K.F.X., Gouzy J., Schoof H., RA Van de Peer Y., Proost S., Cook D.R., Meyers B.C., Spannagl M., RA Cheung F., De Mita S., Krishnakumar V., Gundlach H., Zhou S., RA Mudge J., Bharti A.K., Murray J.D., Naoumkina M.A., Rosen B., RA Silverstein K.A.T., Tang H., Rombauts S., Zhao P.X., Zhou P., RA Barbe V., Bardou P., Bechner M., Bellec A., Berger A., Berges H., RA Bidwell S., Bisseling T., Choisne N., Couloux A., Denny R., RA Deshpande S., Dai X., Doyle J.J., Dudez A.-M., Farmer A.D., RA Fouteau S., Franken C., Gibelin C., Gish J., Goldstein S., RA Gonzalez A.J., Green P.J., Hallab A., Hartog M., Hua A., RA Humphray S.J., Jeong D.-H., Jing Y., Jocker A., Kenton S.M., RA Kim D.-J., Klee K., Lai H., Lang C., Lin S., Macmil S.L., RA Magdelenat G., Matthews L., McCorrison J., Monaghan E.L., Mun J.-H., RA Najar F.Z., Nicholson C., Noirot C., O'Bleness M., Paule C.R., RA Poulain J., Prion F., Qin B., Qu C., Retzel E.F., Riddle C., RA Sallet E., Samain S., Samson N., Sanders I., Saurat O., Scarpelli C., RA Schiex T., Segurens B., Severin A.J., Sherrier D.J., Shi R., Sims S., RA Singer S.R., Sinharoy S., Sterck L., Viollet A., Wang B.-B., Wang K., RA Wang M., Wang X., Warfsmann J., Weissenbach J., White D.D., RA White J.D., Wiley G.B., Wincker P., Xing Y., Yang L., Yao Z., Ying F., RA Zhai J., Zhou L., Zuber A., Denarie J., Dixon R.A., May G.D., RA Schwartz D.C., Rogers J., Quetier F., Town C.D., Roe B.A.; RT "The Medicago genome provides insight into the evolution of rhizobial RT symbioses."; RL Nature 480:520-524(2011). RN [2] {ECO:0000313|EMBL:AES59578.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=A17; RX PubMed=24767513; DOI=10.1186/1471-2164-15-312; RA Tang H., Krishnakumar V., Bidwell S., Rosen B., Chan A., Zhou S., RA Gentzbittel L., Childs K.L., Yandell M., Gundlach H., Mayer K.F., RA Schwartz D.C., Town C.D.; RT "An improved genome release (version Mt4.0) for the model legume RT Medicago truncatula."; RL BMC Genomics 15:312-312(2014). RN [3] {ECO:0000313|EnsemblPlants:AES59578} RP IDENTIFICATION. RC STRAIN=cv. Jemalong A17 {ECO:0000313|EnsemblPlants:AES59578}; RG EnsemblPlants; RL Submitted (APR-2015) to UniProtKB. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CM001217; AES59578.1; -; Genomic_DNA. DR RefSeq; XP_003589327.1; XM_003589279.2. DR EnsemblPlants; AES59578; AES59578; MTR_1g022980. DR GeneID; 11414548; -. DR Gramene; AES59578; AES59578; MTR_1g022980. DR KEGG; mtr:MTR_1g022980; -. DR KO; K03665; -. DR OMA; VILEIFH; -. DR OrthoDB; EOG093609UJ; -. DR Proteomes; UP000002051; Chromosome 1. DR GO; GO:0009507; C:chloroplast; IEA:EnsemblPlants. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000002051}; KW Reference proteome {ECO:0000313|Proteomes:UP000002051}. FT DOMAIN 320 486 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 545 AA; 60866 MW; 9E5A4BC601A74587 CRC64; MMRCACVNGG SVILQPSSSS STIRFQFQQQ QRYLNLVRSH SLSSFSLNVT PHNTEQLQLS SSFSNDAVLL PIQEQEQQQS SPPTPDEDKS TTKLKKKKKD KNDDDNSSNI DNRFKLRNGR EVFEEKAYLV GVERKGEVSD SFGIEDSLSE LEQLADTAGL LVVASTYQKL ASPNPRTYIG SGKVSEIKSA INALDVETVI FDDELSAGQL RNLEKVFGGD VRVCDRTALI LDIFNQRAAT HEASLQVALA QMEYQLPRLT KMWTHLERQS GGQVKGMGEK QIEVDKRILR NQIGVLKKEL ESVRKHRKQY RNRRLSVPVP VVSLVGYTNA GKSTLLNQLT GADVLAEDKL FATLDPTTRR VQMKNGKEFL LTDTVGFIQK LPTTLVAAFR ATLEEISESS LLVHVIDISH PLADQQINAV DKVLSELDVS SIPTLMVWNK IDRASDPQKI RLEAGKRDDV VCISALSGDG IQEFCNAVQD KLKDSMVWVE ALLPFENGDL LSTIHQVGMV EKTEYTEQGT YIKAHVPLRF ARLLTPMRQL CVPRP // ID G7KCX1_MEDTR Unreviewed; 555 AA. AC G7KCX1; A0A0C3XTA7; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 01-OCT-2014, sequence version 2. DT 07-JUN-2017, entry version 32. DE SubName: Full=GTP-binding protein HflX {ECO:0000313|EMBL:AET00246.2}; GN OrderedLocusNames=MTR_5g089970 {ECO:0000313|EMBL:AET00246.2}; OS Medicago truncatula (Barrel medic) (Medicago tribuloides). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae; OC Pentapetalae; rosids; fabids; Fabales; Fabaceae; Papilionoideae; OC Trifolieae; Medicago. OX NCBI_TaxID=3880 {ECO:0000313|EMBL:AET00246.2, ECO:0000313|Proteomes:UP000002051}; RN [1] {ECO:0000313|EMBL:AET00246.2, ECO:0000313|EnsemblPlants:AET00246, ECO:0000313|Proteomes:UP000002051} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=A17 {ECO:0000313|EMBL:AET00246.2}, and RC cv. Jemalong A17 {ECO:0000313|EnsemblPlants:AET00246, RC ECO:0000313|Proteomes:UP000002051}; RX PubMed=22089132; DOI=10.1038/nature10625; RA Young N.D., Debelle F., Oldroyd G.E.D., Geurts R., Cannon S.B., RA Udvardi M.K., Benedito V.A., Mayer K.F.X., Gouzy J., Schoof H., RA Van de Peer Y., Proost S., Cook D.R., Meyers B.C., Spannagl M., RA Cheung F., De Mita S., Krishnakumar V., Gundlach H., Zhou S., RA Mudge J., Bharti A.K., Murray J.D., Naoumkina M.A., Rosen B., RA Silverstein K.A.T., Tang H., Rombauts S., Zhao P.X., Zhou P., RA Barbe V., Bardou P., Bechner M., Bellec A., Berger A., Berges H., RA Bidwell S., Bisseling T., Choisne N., Couloux A., Denny R., RA Deshpande S., Dai X., Doyle J.J., Dudez A.-M., Farmer A.D., RA Fouteau S., Franken C., Gibelin C., Gish J., Goldstein S., RA Gonzalez A.J., Green P.J., Hallab A., Hartog M., Hua A., RA Humphray S.J., Jeong D.-H., Jing Y., Jocker A., Kenton S.M., RA Kim D.-J., Klee K., Lai H., Lang C., Lin S., Macmil S.L., RA Magdelenat G., Matthews L., McCorrison J., Monaghan E.L., Mun J.-H., RA Najar F.Z., Nicholson C., Noirot C., O'Bleness M., Paule C.R., RA Poulain J., Prion F., Qin B., Qu C., Retzel E.F., Riddle C., RA Sallet E., Samain S., Samson N., Sanders I., Saurat O., Scarpelli C., RA Schiex T., Segurens B., Severin A.J., Sherrier D.J., Shi R., Sims S., RA Singer S.R., Sinharoy S., Sterck L., Viollet A., Wang B.-B., Wang K., RA Wang M., Wang X., Warfsmann J., Weissenbach J., White D.D., RA White J.D., Wiley G.B., Wincker P., Xing Y., Yang L., Yao Z., Ying F., RA Zhai J., Zhou L., Zuber A., Denarie J., Dixon R.A., May G.D., RA Schwartz D.C., Rogers J., Quetier F., Town C.D., Roe B.A.; RT "The Medicago genome provides insight into the evolution of rhizobial RT symbioses."; RL Nature 480:520-524(2011). RN [2] {ECO:0000313|EMBL:AET00246.2} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=A17; RX PubMed=24767513; DOI=10.1186/1471-2164-15-312; RA Tang H., Krishnakumar V., Bidwell S., Rosen B., Chan A., Zhou S., RA Gentzbittel L., Childs K.L., Yandell M., Gundlach H., Mayer K.F., RA Schwartz D.C., Town C.D.; RT "An improved genome release (version Mt4.0) for the model legume RT Medicago truncatula."; RL BMC Genomics 15:312-312(2014). RN [3] {ECO:0000313|EnsemblPlants:AET00246} RP IDENTIFICATION. RC STRAIN=cv. Jemalong A17 {ECO:0000313|EnsemblPlants:AET00246}; RG EnsemblPlants; RL Submitted (APR-2015) to UniProtKB. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CM001221; AET00246.2; -; Genomic_DNA. DR RefSeq; XP_003617287.2; XM_003617239.2. DR EnsemblPlants; AET00246; AET00246; MTR_5g089970. DR GeneID; 11437034; -. DR Gramene; AET00246; AET00246; MTR_5g089970. DR KEGG; mtr:MTR_5g089970; -. DR OrthoDB; EOG09360975; -. DR Proteomes; UP000002051; Chromosome 5. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR CDD; cd01878; HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 2. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000002051}; KW Reference proteome {ECO:0000313|Proteomes:UP000002051}. FT DOMAIN 277 523 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 555 AA; 61470 MW; 2B0680753DBAA11F CRC64; MLRNLSATLE STKRKILTSS KCRIYPPPSP YSTAPVDDAP PKLLVVQPRL RSEKLLQAKL NEALCLANSL EDQRDGYFHT DFFDLPLPPH VIVQNPSLKG HKARADTYFG PGTVDTIKCH LNAVESKGEV DAVFVNAILS GIQIRNMERA WNKPVVDRVG LIIEIFNAHA FTKEAKLQAE LAALSYKKSR LVRVLGPNGR LTFGGSGEAE VVSARGRGSG GQGFMSGAGE TELQLQRRRL LDRRNYLLTQ IEEVRRTRAV QRAGRKRQGG SSAQRLATIA VVGYTNAGKS TLVSNLTDSD LYSDCRLFAT VDPRLRSAVL PSGRKVLFSD TVGFISDLPV KLVEAFHATL EEVVEADLLV HVVDSTAPNL EEHRTTVFQV LQQIGVSQEK LQNMIEVWNK IDAEEEFTDV DENVDEHLNE DEEADETSSI DGEEDVNIET LTEEKEDYSD GWLYEEDTVL NEGDFCLPSS AADQQIESSN KDNSVENAGA MLPSSPHVKT SAITGVGLQE LMELIDEKLS SQDEKLKGAQ VVERNLFDRK WRPSHTQDSS IVVEN // ID G7LW28_9GAMM Unreviewed; 426 AA. AC G7LW28; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 30-AUG-2017, entry version 36. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=BrE312_0568 {ECO:0000313|EMBL:EHD20013.1}; OS Brenneria sp. EniD312. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; OC Pectobacteriaceae; Brenneria. OX NCBI_TaxID=598467 {ECO:0000313|EMBL:EHD20013.1, ECO:0000313|Proteomes:UP000002759}; RN [1] {ECO:0000313|EMBL:EHD20013.1, ECO:0000313|Proteomes:UP000002759} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=EniD312 {ECO:0000313|EMBL:EHD20013.1, RC ECO:0000313|Proteomes:UP000002759}; RG US DOE Joint Genome Institute; RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S., RA Peters L., Mikhailova N., Monk A.C., Detter J.C., Han C., Tapia R., RA Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., RA Balakrishnan V., Glasner J., Perna N., Woyke T.; RT "Complete sequence of Brenneria sp. EniD312."; RL Submitted (JUL-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CM001230; EHD20013.1; -; Genomic_DNA. DR RefSeq; WP_009111322.1; NZ_CM001230.1. DR EnsemblBacteria; EHD20013; EHD20013; BrE312_0568. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000002759; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000002759}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000002759}. FT DOMAIN 198 365 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 426 AA; 48146 MW; D03AD871D8E12817 CRC64; MFDRYEAGER AILVHIYFSQ DKDTEDLLEF ESLVSSAGIE SLQVITGSRK APHPKYFVGE GKAEEIALAV KETDAFVVLF DHALTPAQER NLERLCECRV IDRTGLILDI FAQRARTHEG KLQVELAQLR HLATRLVRGW THLERQKGGI GLRGPGETQL ETDRRLLRNR ISQILSRLER VEKQREQGRR ARVRADVPTV SLVGYTNAGK STLFNKITSA GVYAADQLFA TLDPTLRRIE VDDVGDTVLA DTVGFIRQLP HDLVAAFKAT LQETRQASLL LHVVDAADPR LDENIDAVDT VLAEIEADEI PALLVMNKID MLEDFVPRID RNEENLPVRV WLSAQSGEGI PLLFQALTER LSGEIAQYSL SLPPQAGRLR SRFYQLQAIE KEWIEEDGHI GLAIRMPIAD WRRLCKQEQE LTDYVV // ID G7M8W3_9CLOT Unreviewed; 596 AA. AC G7M8W3; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 07-JUN-2017, entry version 31. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=CDLVIII_4957 {ECO:0000313|EMBL:EHJ01448.1}; OS Clostridium sp. DL-VIII. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=641107 {ECO:0000313|EMBL:EHJ01448.1, ECO:0000313|Proteomes:UP000005106}; RN [1] {ECO:0000313|EMBL:EHJ01448.1, ECO:0000313|Proteomes:UP000005106} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DL-VIII {ECO:0000313|EMBL:EHJ01448.1}; RX PubMed=23929491; RA Taghavi S., Izquierdo J.A., van der Lelie D.; RT "Complete Genome Sequence of Clostridium sp. Strain DL-VIII, a Novel RT Solventogenic Clostridium Species Isolated from Anaerobic Sludge."; RL Genome Announc. 1:e00605-13(2013). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CM001240; EHJ01448.1; -; Genomic_DNA. DR RefSeq; WP_009172088.1; NZ_CM001240.1. DR EnsemblBacteria; EHJ01448; EHJ01448; CDLVIII_4957. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000005106; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000005106}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000005106}. FT DOMAIN 364 541 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 596 AA; 67053 MW; AF0AE1707387C764 CRC64; MIYGNIEGIR KSILDELESI YSIRNLKDEV CNIEILNIIS KISSLIEREV SIGINRKGNV TSVAIGDSTS VEIPLIDIEE KRLAGVRVIH THPNGYCNLS ALDLTALLKL KLDAIISVAV IDGNIVDFSL GMLALYNNKL ETEEKSNLSL EEILSINILD RIRFIENLIK TNDVIEETEE KAILVGSDTK ESLEELSELT EACNIPVLKT VFQSRNKVDA AYFIGRGKVL EIASMRQVER ANVIIFDDEL SGSQVRNLEA AIGAKVIDRT TLILEIFATR AKTKEAKIQV ELAQLKYRLG RLQGLGTILS RTGGGIGTRG PGEKKLETDR RHIMETIYDL KDELKKIKKT RDVQREKRNK ENIPKVSLVG YTNAGKSTLR NALCDLAAKK ENKTKEKVFE ANMLFATLDT TTRAITLSKK GVITLTDTVG FVRKLPHDLV EAFKSTLEEV IFSDLLCHVI DASSDSAIDQ YRVVNEVLSE LGAINKETIL VLNKIDMATE EQITALKEII ENHEVIEISA KEKINLEELL NLIEEKLPYN YRKVEYLIPY EKSDVSSYLH RNGRVLEEEY KDNGTYMVVE VDDEVYNKTV EHVVKE // ID G7Q723_9DELT Unreviewed; 579 AA. AC G7Q723; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 10-MAY-2017, entry version 33. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=DFW101_2502 {ECO:0000313|EMBL:EHJ48506.1}; OS Desulfovibrio sp. FW1012B. OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfovibrionales; OC Desulfovibrionaceae; Desulfovibrio. OX NCBI_TaxID=644968 {ECO:0000313|EMBL:EHJ48506.1, ECO:0000313|Proteomes:UP000004662}; RN [1] {ECO:0000313|Proteomes:UP000004662} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=FW1012B {ECO:0000313|Proteomes:UP000004662}; RX PubMed=25767232; RA Ramsay B.D., Hwang C., Woo H.L., Carroll S.L., Lucas S., Han J., RA Lapidus A.L., Cheng J.F., Goodwin L.A., Pitluck S., Peters L., RA Chertkov O., Held B., Detter J.C., Han C.S., Tapia R., Land M.L., RA Hauser L.J., Kyrpides N.C., Ivanova N.N., Mikhailova N., Pagani I., RA Woyke T., Arkin A.P., Dehal P., Chivian D., Criddle C.S., Wu W., RA Chakraborty R., Hazen T.C., Fields M.W.; RT "High-Quality Draft Genome Sequence of Desulfovibrio carbinoliphilus RT FW-101-2B, an Organic Acid-Oxidizing Sulfate-Reducing Bacterium RT Isolated from Uranium(VI)-Contaminated Groundwater."; RL Genome Announc. 3:0-0(2015). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CM001368; EHJ48506.1; -; Genomic_DNA. DR ProteinModelPortal; G7Q723; -. DR STRING; 644968.DFW101_2502; -. DR EnsemblBacteria; EHJ48506; EHJ48506; DFW101_2502. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000004662; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000004662}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000004662}. FT DOMAIN 392 557 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 358 385 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 579 AA; 62490 MW; B490BCCEB87E6945 CRC64; MSTPARGTAI AVKVEGNTLG LKPSQLKALE RLGTRRYPSV GGYTLDQARE LCAIAFGIGR QVGLLIDRKG RPTMILVGSQ KGILIPELDR ARLGSARLRG VRLLHVHLAG EGLSEEDLTD MLFLRLDSVA ALTMDNLAQP VTLQAAHLLP PGAGDAPYDV LPPRPYDRVE EDMNALATAL EDELAREGEK LAAPGTSPSG REKAVLVSVS SAPRTAQEAS LDELAALADT AGLDVAESVV QRVASINPKF ILGKGKLADI EVAALRAGAS LLVFDGELSP SQIRNLTEVT QLRVIDRTQL ILDIFAQHAA TRSGKLQVEM AQLKYLQPRL VRQDRAMSRL MGGIGGRGPG ETKLEVDRRR IRERIGRIKD ELKELRKRRA AARAGRARAG LPVVSLVGYT NAGKSTLLNT LTGSAVLAEN RLFATLDPTS RRLRFPSDRE IILTDTVGFI RELPKELKEA FRATLEELEA ADLLVAVADA SHPEVDGQVA AVADILQEME LGDIPRLLVL NKWDAVPEDL RGPLKNAFPD ALTLSARTRD GLSTLTDAIL DRVRPGFGVR DFGPRPVVPD ETDLPAGTP // ID G7UR17_PSEUP Unreviewed; 452 AA. AC G7UR17; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 07-JUN-2017, entry version 39. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=DSC_12225 {ECO:0000313|EMBL:AER57089.1}; OS Pseudoxanthomonas spadix (strain BD-a59). OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales; OC Xanthomonadaceae; Pseudoxanthomonas. OX NCBI_TaxID=1045855 {ECO:0000313|EMBL:AER57089.1, ECO:0000313|Proteomes:UP000005870}; RN [1] {ECO:0000313|EMBL:AER57089.1, ECO:0000313|Proteomes:UP000005870} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BD-a59 {ECO:0000313|EMBL:AER57089.1, RC ECO:0000313|Proteomes:UP000005870}; RX PubMed=22207748; DOI=10.1128/JB.06436-11; RA Lee S.H., Jin H.M., Lee H.J., Kim J.M., Jeon C.O.; RT "Complete Genome Sequence of the BTEX-Degrading Bacterium RT Pseudoxanthomonas spadix BD-a59."; RL J. Bacteriol. 194:544-544(2012). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP003093; AER57089.1; -; Genomic_DNA. DR RefSeq; WP_014161262.1; NC_016147.2. DR STRING; 1045855.DSC_12225; -. DR EnsemblBacteria; AER57089; AER57089; DSC_12225. DR KEGG; psd:DSC_12225; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000005870; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000005870}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000005870}. FT DOMAIN 203 381 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 162 196 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 452 AA; 49268 MW; 8469FA52E6B2F3FE CRC64; MFERSRKGEH ALLIQPVRGG AAAVTGDEDA AEEFTELARS AGASIAALVT ARTDKPSPST FIGSGKLDEV KAAADATGAD LILVNHALTP GQERNLEKAL ERRVLDRTGL ILDIFAQRAR SHEGKLQVEL AQLRHMATRL VRGWTHLERQ RGGSIGLRGP GETQLETDRR LLQKRVDQLQ KRLEKVEVQH TQMRRARVRS ELPRVALVGY TNAGKSTLFN ALTGAQAYAA DQLFATLDPT VRRVNLAGGH VVLADTVGFV RDLPHELVAA FRSTLSEARE ADLLLHVVDA ADPLHAERIA QVDLVLTEIG AGDIPQLLVF NKIDRIEGAQ PRHDAPEGDL DGDTEPGTLG LARERVWISA RDGVGLDLLQ EALARRLGLQ RICGEVVLPP TAGRLRARLH ALEAVRSEGH DEAGWRLTLD MARTDAEKLL SQPGGDALRV LLPAVEVEQW EA // ID G7W963_DESOD Unreviewed; 543 AA. AC G7W963; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 07-JUN-2017, entry version 35. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Desor_3200 {ECO:0000313|EMBL:AET68704.1}; OS Desulfosporosinus orientis (strain ATCC 19365 / DSM 765 / NCIMB 8382 / OS VKM B-1628) (Desulfotomaculum orientis). OC Bacteria; Firmicutes; Clostridia; Clostridiales; Peptococcaceae; OC Desulfosporosinus. OX NCBI_TaxID=768706 {ECO:0000313|EMBL:AET68704.1, ECO:0000313|Proteomes:UP000006346}; RN [1] {ECO:0000313|Proteomes:UP000006346} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 19365 / DSM 765 / NCIMB 8382 / VKM B-1628 RC {ECO:0000313|Proteomes:UP000006346}; RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S., RA Peters L., Ovchinnikova G., Teshima H., Detter J.C., Han C., Tapia R., RA Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Pester M., RA Spring S., Ollivier B., Rattei T., Klenk H.-P., Wagner M., Loy A., RA Woyke T.; RT "Complete sequence of Desulfosporosinus orientis DSM 765."; RL Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:AET68704.1, ECO:0000313|Proteomes:UP000006346} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 19365 / DSM 765 / NCIMB 8382 / VKM B-1628 RC {ECO:0000313|Proteomes:UP000006346}; RX PubMed=23105050; DOI=10.1128/JB.01392-12; RA Pester M., Brambilla E., Alazard D., Rattei T., Weinmaier T., Han J., RA Lucas S., Lapidus A., Cheng J.F., Goodwin L., Pitluck S., Peters L., RA Ovchinnikova G., Teshima H., Detter J.C., Han C.S., Tapia R., RA Land M.L., Hauser L., Kyrpides N.C., Ivanova N.N., Pagani I., RA Huntmann M., Wei C.L., Davenport K.W., Daligault H., Chain P.S., RA Chen A., Mavromatis K., Markowitz V., Szeto E., Mikhailova N., RA Pati A., Wagner M., Woyke T., Ollivier B., Klenk H.P., Spring S., RA Loy A.; RT "Complete genome sequences of Desulfosporosinus orientis DSM765T, RT Desulfosporosinus youngiae DSM17734T, Desulfosporosinus meridiei RT DSM13257T, and Desulfosporosinus acidiphilus DSM22704T."; RL J. Bacteriol. 194:6300-6301(2012). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP003108; AET68704.1; -; Genomic_DNA. DR STRING; 768706.Desor_3200; -. DR EnsemblBacteria; AET68704; AET68704; Desor_3200. DR KEGG; dor:Desor_3200; -. DR PATRIC; fig|768706.3.peg.3227; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR KO; K03665; -. DR OMA; EREVIIT; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000006346; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000006346}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000006346}. FT DOMAIN 370 543 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 329 363 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 543 AA; 61170 MW; 110068667C37FC09 CRC64; MTMDISGDLS GIRASQLQEL KALEDIKTEP SQLINPGILR ELIQLTRLWN REIAVYLSRS GRLLAAAVGR HAQVTLPQIK RRSQGKHLRC IHTHPSGNFQ LSSLDYSALT SLELESMAAV GALEGKLTGI QMAFLREEGP PYTLELSPQD WHHFDYQDCL GSLSSFRPAK SKKVTPKNAR ERAFLIALQD SELDTYEDLL ELRELARTAG VDVVGELVQL RRYGQSRSYF GRGKLEELLH RLQESEANVL ICDDELSPTQ MRTLEMETGL KVLDRTGLIL DIFAQRARSR EGKLQVELAQ LKHLLPYLTG QGQALSRLGG GVGTRGPGET KLELDRRRMR DRINHLEKEL KQVLQHRDVQ RRQRTRSGLP IIALVGYTNT GKTTFMKLAM EQAGSRSDIP MGENKLFATL DPIVRGIKID SSLEVLLSDT VGFIRKLPTQ LLRAFIATLE EVQQADALIH VIDASHRQAL EHAETVRDVL DQLGCLDKPA ITLLNKIDKI KPEDEPELED LEKYFPYPVK ISLTRGDSLK PVWEILSSLL KHE // ID G7WLN3_METH6 Unreviewed; 443 AA. AC G7WLN3; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 07-JUN-2017, entry version 42. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Mhar_0965 {ECO:0000313|EMBL:AET64336.1}; OS Methanosaeta harundinacea (strain 6Ac). OC Archaea; Euryarchaeota; Methanomicrobia; Methanosarcinales; OC Methanosaetaceae; Methanosaeta. OX NCBI_TaxID=1110509 {ECO:0000313|EMBL:AET64336.1, ECO:0000313|Proteomes:UP000005877}; RN [1] {ECO:0000313|EMBL:AET64336.1, ECO:0000313|Proteomes:UP000005877} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=6Ac {ECO:0000313|EMBL:AET64336.1, RC ECO:0000313|Proteomes:UP000005877}; RX PubMed=22590603; DOI=10.1371/journal.pone.0036756; RA Zhu J., Zheng H., Ai G., Zhang G., Liu D., Liu X., Dong X.; RT "The genome characteristics and predicted function of methyl-group RT oxidation pathway in the obligate aceticlastic methanogens, RT Methanosaeta spp."; RL PLoS ONE 7:E36756-E36756(2012). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP003117; AET64336.1; -; Genomic_DNA. DR RefSeq; WP_014586521.1; NC_017527.1. DR STRING; 1110509.Mhar_0965; -. DR EnsemblBacteria; AET64336; AET64336; Mhar_0965. DR GeneID; 12510134; -. DR KEGG; mhi:Mhar_0965; -. DR PATRIC; fig|1110509.7.peg.1080; -. DR eggNOG; arCOG00353; Archaea. DR eggNOG; COG2262; LUCA. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG093Z07D6; -. DR Proteomes; UP000005877; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000005877}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000005877}. FT DOMAIN 188 357 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 443 AA; 49433 MW; 4F2AC0DC91A536BA CRC64; MRREKTAVLL FREDPREDLR PEEVTELRGL AEAAGYTVLA EVFQRRGRDR RFQLGRGKVV EAASLGPDKL IFNEPLSPGQ IFNIGKEFEI PPMDRFNLIL EIFASRASTR EAKLQVELAR LSYEAPFVRT IESLKKLSER PGYRGSGSYD VSMYRDIKGR MAKIRAELRA VEETGVRRRE RRRKLGFDLV ALAGYTNAGK STLFNRLAEE AVAAKDQPFT TLSPTTRAVA ARDRRFLLTD TVGFIDDLPL FLIKAFRSTL AEIVEADLVL LVVDLSDPPE VLRERVASCH GALWDCGCYA PLVSVLNKVD LITPEEAEER CRLLEDLAPT PVLVSAREGL GLEALLDAIL EKLPPLEEFL VRLPASEAGM GQLSRLYEVA EPLEVRYGEE VEVLLRGRRE IVAKALRGAE RPEADQDMDD RSGAATAPEA RPPKPGDPPP DGE // ID G7Z6T6_AZOL4 Unreviewed; 409 AA. AC G7Z6T6; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 07-JUN-2017, entry version 41. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=AZOLI_1350 {ECO:0000313|EMBL:CBS86659.1}; OS Azospirillum lipoferum (strain 4B). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales; OC Rhodospirillaceae; Azospirillum. OX NCBI_TaxID=862719 {ECO:0000313|EMBL:CBS86659.1, ECO:0000313|Proteomes:UP000005667}; RN [1] {ECO:0000313|Proteomes:UP000005667} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=4B {ECO:0000313|Proteomes:UP000005667}; RX PubMed=22216014; DOI=10.1371/journal.pgen.1002430; RA Wisniewski-Dye F., Borziak K., Khalsa-Moyers G., Alexandre G., RA Sukharnikov L.O., Wuichet K., Hurst G.B., McDonald W.H., RA Robertson J.S., Barbe V., Calteau A., Rouy Z., Mangenot S., RA Prigent-Combaret C., Normand P., Boyer M., Siguier P., Dessaux Y., RA Elmerich C., Condemine G., Krishnen G., Kennedy I., Paterson A.H., RA Gonzalez V., Mavingui P., Zhulin I.B.; RT "Azospirillum genomes reveal transition of bacteria from aquatic to RT terrestrial environments."; RL PLoS Genet. 7:E1002430-E1002430(2011). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; FQ311868; CBS86659.1; -; Genomic_DNA. DR STRING; 862719.AZOLI_1350; -. DR EnsemblBacteria; CBS86659; CBS86659; AZOLI_1350. DR KEGG; ali:AZOLI_1350; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR KO; K03665; -. DR OMA; FNNHAHV; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000005667; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000005667}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000005667}. FT DOMAIN 180 351 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 409 AA; 45231 MW; 5EA3665E8D312E93 CRC64; MRPPESRLEE AIGLAQAIQL DVIHAECAKV NRPQPSTLLG SGTVEHLAEV VEENEATLVI LDHALSPVQQ RNLERALKAK VIDRTGLILE IFGARARTRE GMLQVELASL TYQKSRLVRS WTHLERQRGG FGFLGGPGES QLELDRRLIG DRIIKIKKEL EEVRRTRGLH RKARAKVPYP VVALVGYTNA GKSTLFNRLA NADVFAQNLL FATLDPTMRQ VTLPSGRKVI LSDTVGFISD LPHGLVAAFR ATLEEVDAAD IILHVRDIAH IDSDAQKADV HEVLSDMGID PETDDRVIEV LNKIDALDGE SRAAILAQTG RNPRAVAVSA LSGEGIDDLD RLLDQRMNVN RQVVDLSVEL GDGAALAWLY AKGEVLERRD DEERAHLHVS LDPADLARFE KRFQPQSQA // ID G7ZHM5_AZOL4 Unreviewed; 448 AA. AC G7ZHM5; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 07-JUN-2017, entry version 39. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=AZOLI_p50433 {ECO:0000313|EMBL:CBS91419.1}; OS Azospirillum lipoferum (strain 4B). OG Plasmid AZO_p5 {ECO:0000313|EMBL:CBS91419.1, OG ECO:0000313|Proteomes:UP000005667}. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales; OC Rhodospirillaceae; Azospirillum. OX NCBI_TaxID=862719 {ECO:0000313|EMBL:CBS91419.1, ECO:0000313|Proteomes:UP000005667}; RN [1] {ECO:0000313|Proteomes:UP000005667} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=4B {ECO:0000313|Proteomes:UP000005667}; RX PubMed=22216014; DOI=10.1371/journal.pgen.1002430; RA Wisniewski-Dye F., Borziak K., Khalsa-Moyers G., Alexandre G., RA Sukharnikov L.O., Wuichet K., Hurst G.B., McDonald W.H., RA Robertson J.S., Barbe V., Calteau A., Rouy Z., Mangenot S., RA Prigent-Combaret C., Normand P., Boyer M., Siguier P., Dessaux Y., RA Elmerich C., Condemine G., Krishnen G., Kennedy I., Paterson A.H., RA Gonzalez V., Mavingui P., Zhulin I.B.; RT "Azospirillum genomes reveal transition of bacteria from aquatic to RT terrestrial environments."; RL PLoS Genet. 7:E1002430-E1002430(2011). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; FQ311873; CBS91419.1; -; Genomic_DNA. DR RefSeq; WP_014250240.1; NC_016624.1. DR EnsemblBacteria; CBS91419; CBS91419; AZOLI_p50433. DR KEGG; ali:AZOLI_p50433; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000005667; Plasmid AZO_p5. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000005667}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Plasmid {ECO:0000313|EMBL:CBS91419.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000005667}. FT DOMAIN 219 397 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 448 AA; 48575 MW; 1D9442EF0E9A05A5 CRC64; MGTNPNTDTN TIETPRSSLG RALVLHPVLR GTETDRSPEA SLEEAVGLAA AIELEVAQAA VVKVNQPRPA TLLGGGAIEQ YAKLLDDARE AGEDIDLVIV DHALTPVQQR NLEKAFGTKV IDRTGLILEI FGARARTHEG QLQVELASLT YQKSRLVRSW THLERQRGGF GFLGGPGESQ LEIDRRLIGN RIVKIKRELD DVRRTRGLHR KARAKVPYPV VALVGYTNAG KSTLFNRMAG ADVFAKNLLF ATLDPTMRQV VLPSGRKVIL SDTVGFISDL PTHLVAAFRA TLEEVQSADI ILHVRDIAHP DTEAQKADVE AILTDLGIDP ERDPRVVEVS NKIDLLDGAE LDAVLARAGR SGNTCAVSAA TGDRLDTLFR ILDDRMTAGR ELVELDVEHG DGATLAWLYA HGEVIGRRDD DSHAHLQVAI EPAVLARIAP LAQARAAA // ID G8AQ33_AZOBR Unreviewed; 419 AA. AC G8AQ33; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 07-JUN-2017, entry version 38. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=AZOBR_p110020 {ECO:0000313|EMBL:CCC99544.1}; OS Azospirillum brasilense Sp245. OG Plasmid AZOBR_p1 {ECO:0000313|EMBL:CCC99544.1, OG ECO:0000313|Proteomes:UP000007319}. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales; OC Rhodospirillaceae; Azospirillum. OX NCBI_TaxID=1064539 {ECO:0000313|EMBL:CCC99544.1, ECO:0000313|Proteomes:UP000007319}; RN [1] {ECO:0000313|EMBL:CCC99544.1, ECO:0000313|Proteomes:UP000007319} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Sp245 {ECO:0000313|EMBL:CCC99544.1, RC ECO:0000313|Proteomes:UP000007319}; RX PubMed=22216014; DOI=10.1371/journal.pgen.1002430; RA Wisniewski-Dye F., Borziak K., Khalsa-Moyers G., Alexandre G., RA Sukharnikov L.O., Wuichet K., Hurst G.B., McDonald W.H., RA Robertson J.S., Barbe V., Calteau A., Rouy Z., Mangenot S., RA Prigent-Combaret C., Normand P., Boyer M., Siguier P., Dessaux Y., RA Elmerich C., Condemine G., Krishnen G., Kennedy I., Paterson A.H., RA Gonzalez V., Mavingui P., Zhulin I.B.; RT "Azospirillum genomes reveal transition of bacteria from aquatic to RT terrestrial environments."; RL PLoS Genet. 7:E1002430-E1002430(2011). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; HE577328; CCC99544.1; -; Genomic_DNA. DR EnsemblBacteria; CCC99544; CCC99544; AZOBR_p110020. DR KEGG; abs:AZOBR_p110020; -. DR PATRIC; fig|192.7.peg.2979; -. DR KO; K03665; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000007319; Plasmid AZOBR_p1. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000007319}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Plasmid {ECO:0000313|EMBL:CCC99544.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000007319}. FT DOMAIN 193 364 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 419 AA; 46261 MW; 3B14AA893C761A3B CRC64; MVHPVLRSEA DGVLRHPESC LDEAVGLARA IDLEVVHAEC ARVNRPQPSI LLGSGTVEHF AQIVEETEAS LVILDHALSP VQQRNLEKAL KVKVIDRTGL ILEIFGARAR TREGMLQVEL AALTYQKSRL VRSWTHLERQ RGGFGFLGGP GESQLEMDRR LIGDRIVKIK KELEEVRRTR GLHRKARAKV PYPVVALVGY TNAGKSTLFN RLANADVFAK DLLFATLDPT MRQVTLPSGR KVILSDTVGF ISDLPHGLVA AFRATLEEVD AADIILHVRD VSHQDSEPQK ADVHEVMSDM GIDPDADDRV IEVLNKIDAL DDESREAILA QTARNPRAVA VSALSGAGIA DLDRLLDQRM NAHRHVVDLS VELGDGAALA WLYAKGEVLE RRDDEVQAHI QVAIDPADLA RFEKRFVHG // ID G8AQG2_AZOBR Unreviewed; 468 AA. AC G8AQG2; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 07-JUN-2017, entry version 38. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=AZOBR_p110149 {ECO:0000313|EMBL:CCC99673.1}; OS Azospirillum brasilense Sp245. OG Plasmid AZOBR_p1 {ECO:0000313|EMBL:CCC99673.1, OG ECO:0000313|Proteomes:UP000007319}. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales; OC Rhodospirillaceae; Azospirillum. OX NCBI_TaxID=1064539 {ECO:0000313|EMBL:CCC99673.1, ECO:0000313|Proteomes:UP000007319}; RN [1] {ECO:0000313|EMBL:CCC99673.1, ECO:0000313|Proteomes:UP000007319} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Sp245 {ECO:0000313|EMBL:CCC99673.1, RC ECO:0000313|Proteomes:UP000007319}; RX PubMed=22216014; DOI=10.1371/journal.pgen.1002430; RA Wisniewski-Dye F., Borziak K., Khalsa-Moyers G., Alexandre G., RA Sukharnikov L.O., Wuichet K., Hurst G.B., McDonald W.H., RA Robertson J.S., Barbe V., Calteau A., Rouy Z., Mangenot S., RA Prigent-Combaret C., Normand P., Boyer M., Siguier P., Dessaux Y., RA Elmerich C., Condemine G., Krishnen G., Kennedy I., Paterson A.H., RA Gonzalez V., Mavingui P., Zhulin I.B.; RT "Azospirillum genomes reveal transition of bacteria from aquatic to RT terrestrial environments."; RL PLoS Genet. 7:E1002430-E1002430(2011). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; HE577328; CCC99673.1; -; Genomic_DNA. DR RefSeq; WP_014197179.1; NC_016594.1. DR EnsemblBacteria; CCC99673; CCC99673; AZOBR_p110149. DR KEGG; abs:AZOBR_p110149; -. DR PATRIC; fig|192.7.peg.3088; -. DR KO; K03665; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000007319; Plasmid AZOBR_p1. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000007319}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Plasmid {ECO:0000313|EMBL:CCC99673.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000007319}. FT DOMAIN 233 410 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 468 AA; 50958 MW; F19C1490C30E3F05 CRC64; MPDSDDRPSP RSAASVSRSV QGNDPDRAGP PSAGRALVIL PVLSTHPDDG NAAARQPDAR LSEAIALAQA IRLEVPHAEV IRVARPDPAT LFGRGTADRI GGMVEAFHAD LVVIDHPLSP VQQRNLERRC MAKVIDRTGL ILEIFGERAH TREGQLQVEL AALTYQRSRL VRSWTHLERQ RGGFGFLGGP GESQLELDRR LIAERISRLK SDLEEVRRTR KLHRSARQRG GTPLVALVGY TNAGKSTLFN RLSGAGVTAE DMLFATLDPT VRRIALSSGK TMALSDTVGF VSELPTQLVA AFRATLEEVQ AADLILHVRD VSHPDTAAQK ADVDSVLADL GIDAANDPRV VEVLNKTDQM PATARGALHM RLANQRMMEG EERAVAVSAL TGEGLDDLLD LLDRRVSAER QVLELSVNLS DGRALAWLYE HGQVLDRRDE DGQAHVHVAL APADAARFES RFVGQDSR // ID G8M3B6_CLOCD Unreviewed; 608 AA. AC G8M3B6; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 07-JUN-2017, entry version 34. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Clocl_4000 {ECO:0000313|EMBL:AEV70436.1}; OS Clostridium clariflavum (strain DSM 19732 / NBRC 101661 / EBR45). OC Bacteria; Firmicutes; Clostridia; Clostridiales; Ruminococcaceae; OC Ruminiclostridium. OX NCBI_TaxID=720554 {ECO:0000313|EMBL:AEV70436.1, ECO:0000313|Proteomes:UP000005435}; RN [1] {ECO:0000313|Proteomes:UP000005435} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 19732 / NBRC 101661 / EBR45 RC {ECO:0000313|Proteomes:UP000005435}; RG US DOE Joint Genome Institute; RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S., RA Peters L., Teshima H., Detter J.C., Han C., Tapia R., Land M., RA Hauser L., Kyrpides N., Ivanova N., Pagani I., Kitzmiller T., Lynd L., RA Izquierdo J., Woyke T.; RT "Complete sequence of Clostridium clariflavum DSM 19732."; RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP003065; AEV70436.1; -; Genomic_DNA. DR STRING; 720554.Clocl_4000; -. DR EnsemblBacteria; AEV70436; AEV70436; Clocl_4000. DR KEGG; ccl:Clocl_4000; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR KO; K03665; -. DR OMA; EREVIIT; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000005435; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000005435}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000005435}. FT DOMAIN 385 550 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 608 AA; 67644 MW; 32C294B2C3CD0920 CRC64; MGNIYINGNL DSLKKSVIGE LEALLNIQTD GNDFIPPELT EAISNISSRI NREISVFLDR KGNIVDISVG DSSTVALPEV KGRRDKSRLS GIRCIHTHPN GVGMVSLVDI NSMLNLRLDA MAAVGVSNGN ITEIFVAIPV RSERNEFDKY HVYGPYKIHD KKINGLWNVI EETDRAAGTI LHENKTDVER TIIVGLETST GKIINGKSEG ERSLDELEEL VRTAGGQVVK KVLQKRSERD SAYYIGKGKL EELSLIRQAL DADMIVFDDE LSGAQLRNIE EVVGIKVIDR TTLILDIFAQ RARSREGKLQ VELAQLKYRV SRLIGLGNQL SRLGGGIGTR GPGEKKLEVD RRHIRRRISY LEDELSKVEK RRNFMRKTRD KDSLPVIALV GYTNAGKSTL MNALCKSDVF AEDKLFATLD PTARGLKLPN GRDAILVDTV GFIRKLPHEL VEAFKSTLEE AVYGDILIHV VDITNEESIE QIEVVNNILN SLGALNKPVV MALNKVDLLT QRQRPPVLNP LGSVVEISAV TLEGIDVLLK AVADALGFEE EEMELLIPYH EGWAISYVHE NGKILEKIYD EKGVYIRVSM LKSKSNYIKA FECPCSIK // ID G8M3Q6_9BURK Unreviewed; 422 AA. AC G8M3Q6; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 07-JUN-2017, entry version 36. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:AET89378.1}; GN ORFNames=BYI23_A015400 {ECO:0000313|EMBL:AET89378.1}; OS Burkholderia sp. YI23. OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Burkholderia. OX NCBI_TaxID=1097668 {ECO:0000313|EMBL:AET89378.1, ECO:0000313|Proteomes:UP000006801}; RN [1] {ECO:0000313|EMBL:AET89378.1, ECO:0000313|Proteomes:UP000006801} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=YI23 {ECO:0000313|EMBL:AET89378.1, RC ECO:0000313|Proteomes:UP000006801}; RX PubMed=22275096; DOI=10.1128/JB.06479-11; RA Lim J.S., Choi B.S., Choi A.Y., Kim K.D., Kim D.I., Choi I.Y., RA Ka J.O.; RT "Complete Genome Sequence of the Fenitrothion-Degrading Burkholderia RT sp. Strain YI23."; RL J. Bacteriol. 194:896-896(2012). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP003087; AET89378.1; -; Genomic_DNA. DR RefSeq; WP_014191603.1; NC_016589.1. DR STRING; 1097668.BYI23_A015400; -. DR EnsemblBacteria; AET89378; AET89378; BYI23_A015400. DR KEGG; byi:BYI23_A015400; -. DR PATRIC; fig|1097668.3.peg.1693; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR KO; K03665; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000006801; Chromosome 1. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000006801}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}. FT DOMAIN 191 362 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 157 184 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 422 AA; 46315 MW; 4503F39B8DD34473 CRC64; MINAALVGID FGKIDFEASL EELSLLAQSA GAHPAVTLTG RRQSPDAKMF IGSGKVEELR LQCEASDVEL VIFNHALAPA QQRNLEVALN RRVVDRTSLI LDIFAQRARS HEGKLQVELA QLQYLSTRLI RAWTHLERQK GGIGLRGPGE TQLETDRRLI GERIKALKSR LEKLRRQHGT QRRQRVRNRT MSVSLVGYTN AGKSTLFNAL TKAQAYAADQ LFATLDTTSR RVFLGEEAGH VVVSDTVGFI RELPHQLVAA FRATLEETIH ADVLLHVVDA SSAVRLDQID QVNEVLRGIG ADGIRQILVF NKIDAVPELA ARGEAVERDE YGNISRVFLS ARTGQGLDAL RAAIAEIATA EAEETDAGLP SVLAEFPVPQ EASEATQSTQ AGSNDIHGTN AQPEDHRQDA ERDDHKVPEH GH // ID G8NTP1_GRAMM Unreviewed; 485 AA. AC G8NTP1; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 07-JUN-2017, entry version 36. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=AciX8_2035 {ECO:0000313|EMBL:AEU36365.1}; OS Granulicella mallensis (strain ATCC BAA-1857 / DSM 23137 / MP5ACTX8). OC Bacteria; Acidobacteria; Acidobacteriales; Acidobacteriaceae; OC Granulicella. OX NCBI_TaxID=682795 {ECO:0000313|EMBL:AEU36365.1, ECO:0000313|Proteomes:UP000007113}; RN [1] {ECO:0000313|EMBL:AEU36365.1, ECO:0000313|Proteomes:UP000007113} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-1857 / DSM 23137 / MP5ACTX8 RC {ECO:0000313|Proteomes:UP000007113}; RG US DOE Joint Genome Institute; RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L., RA Pitluck S., Peters L., Lu M., Detter J.C., Han C., Tapia R., Land M., RA Hauser L., Kyrpides N., Ivanova N., Mikhailova N., Pagani I., RA Rawat S., Mannisto M., Haggblom M., Woyke T.; RT "Complete sequence of Granulicella mallensis MP5ACTX8."; RL Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP003130; AEU36365.1; -; Genomic_DNA. DR RefSeq; WP_014265243.1; NC_016631.1. DR ProteinModelPortal; G8NTP1; -. DR STRING; 682795.AciX8_2035; -. DR EnsemblBacteria; AEU36365; AEU36365; AciX8_2035. DR KEGG; gma:AciX8_2035; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000007113; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000007113}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000007113}. FT DOMAIN 262 422 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 221 255 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 485 AA; 52907 MW; 8AD50A9CC41F26CF CRC64; MSSKYSPSIK DSRLVAAQEQ ALLRARQQAT REQAVLVAIE FTADRRRLSP AAQQARAAAA ILNRSALGEE PEIDASSGPP KPADLDFDAS LAEFQELARS AGATIAAVLI QRRPHPDPAT LVGGGKLDEI VATVAATGAS LVLFDHDLTP SQARNVEARL PCTVIDRTQL ILDIFARHAR TREGMLQVEL AQLEYQLPRL AGKGKSMSQL GGGIGTRGPG ETQLETDRRR INLRLDRIKQ QLEAVRRIRR QQRGRREAVP VPTVALVGYT NAGKSTLFNS LTGAEVLASE RMFATLDPKL RQLTLPSRRK VLLSDTVGFL RNLPHALVTS FRATLEEVER AELLLHVRDA ASPTLDEQRS QVEAVLSELN VGEKQTLQVL NKTDLLPPET PFAPGTIPVS GLTGAGLDDL LHAIDAALTS DPLIEVRFRI PQSEGRILSA LERGATLSGQ RFDGNLVYLT ALGPATLLRR YRQYQLREEE ALSEG // ID G8PEX5_PEDCP Unreviewed; 421 AA. AC G8PEX5; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 07-JUN-2017, entry version 37. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:AEV95654.1}; GN OrderedLocusNames=PECL_1430 {ECO:0000313|EMBL:AEV95654.1}; OS Pediococcus claussenii (strain ATCC BAA-344 / DSM 14800 / JCM 18046 / OS KCTC 3811 / P06). OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; OC Pediococcus. OX NCBI_TaxID=701521 {ECO:0000313|EMBL:AEV95654.1, ECO:0000313|Proteomes:UP000005444}; RN [1] {ECO:0000313|Proteomes:UP000005444} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-344 / DSM 14800 / JCM 18046 / KCTC 3811 / P06 RC {ECO:0000313|Proteomes:UP000005444}; RA Pittet V., Abegunde T., Marfleet T., Haakensen M., Morrow K., RA Jayaprakash T., Schroeder K., Trost B., Byrns S., Bergsveinson J., RA Kusalik A., Ziola B.; RT "Genome and plasmid sequences for the beer-spoilage organism RT Pediococcus claussenii ATCC BAA-344T."; RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP003137; AEV95654.1; -; Genomic_DNA. DR RefSeq; WP_014215848.1; NC_016605.1. DR STRING; 701521.PECL_1430; -. DR EnsemblBacteria; AEV95654; AEV95654; PECL_1430. DR KEGG; pce:PECL_1430; -. DR PATRIC; fig|701521.8.peg.1334; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR KO; K03665; -. DR OMA; FNNHAHV; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000005444; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000005444}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000005444}. FT DOMAIN 200 330 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 421 AA; 47262 MW; 65D3765E143FAE26 CRC64; MEEIEKVIIA GLELPGSNLE YQMDELASLV IANNMEVVDR ILQKLDRPNS ATYFGSGKLE EITNLATAQK ADTVVVSEEL SPSQLSNLEK ETGLHFLDRT GLILEIFANR AHSREAKLQV ELAKLEYQLP RLRTSSSQRL DQQTAGNAGG GYTNRGAGET KLELNRRTIR NKIAHINKEL KEISTSSEVQ RKQRDKKDIP SVALVGYTNT GKSTTMNGLV RMFGRSDEKQ VFEKNMLFAT LDTSVRKLSF PDRKEIVLSD TVGFVSHLPH HLIQAFRSTL AEAAQADLLV QVVDLSDPHY REMMTTTEET LREIGVTDVP MVYAFNKADL AGVTYPTLDG TQLTYSARQV QSLEMLTSLI KKQLFKNYVE ATFLIPFSEG QVVDFLNGNA NVKNTEYTEN GTKITAELKQ QDYQRLENYL L // ID G8PHY6_PSEUV Unreviewed; 491 AA. AC G8PHY6; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 07-JUN-2017, entry version 35. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=PSE_3270 {ECO:0000313|EMBL:AEV37778.1}; OS Pseudovibrio sp. (strain FO-BEG1). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae; Pseudovibrio. OX NCBI_TaxID=911045 {ECO:0000313|EMBL:AEV37778.1, ECO:0000313|Proteomes:UP000005634}; RN [1] {ECO:0000313|Proteomes:UP000005634} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=FO-BEG1 {ECO:0000313|Proteomes:UP000005634}; RA Bondarev V., Richter M., Piel J., Schwedt A., Schulz-Vogt H.N.; RT "The genus Pseudovibrio contains metabolically versatile and RT symbiotically interacting bacteria."; RL Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP003147; AEV37778.1; -; Genomic_DNA. DR RefSeq; WP_014285814.1; NC_016642.1. DR STRING; 911045.PSE_3270; -. DR EnsemblBacteria; AEV37778; AEV37778; PSE_3270. DR KEGG; psf:PSE_3270; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000005634; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000005634}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000005634}. FT DOMAIN 238 409 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 491 AA; 54924 MW; 2B6211D3C751E791 CRC64; MKPQSKKEAG LNRKQRDANV EAGEDEVTRG TRSLVIVPII SSRALARGKG APERPFGAER SPQARLEEAV GLAAAIELEI VSSGLVRLAN VKPGSLFGSG KVEEIRGQIE IEEIELVVVD HPLTPIQQRN LERDWNTKVI DRTGLILEIF GERAQTKEGR LQVELAHLTW QKSRLVRSWT HLERQRGGLG FVGGPGETQI EADRRIIQDR ITLLKGQLEQ VQRTRKLHRK QRKKVPHPVI AFVGYTNAGK STLFNRMTNA EVFAKDLLFA TLDPTLRRLK LPHGREVILS DTVGFISELP HNLVAAFRAT LEEVIQADIV LHVRDIAHED TKAQSLDVNE TLEMLGLKVS ESDRVIEVYN KIDKLDEAHR EKLLESNSVD EGPISVSAIS GDGIPDLLAR IEARLAEQLD TVTMVLPHSD GQGHAWLYQH CEILSRDDVE DGIRLAVRVP DAHRSRVRER FAKYFVTGLE LPDEPVSEED DDTDDSGYSP I // ID G8QI65_DECSP Unreviewed; 395 AA. AC G8QI65; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 07-JUN-2017, entry version 39. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Dsui_3136 {ECO:0000313|EMBL:AEV27468.1}; OS Dechlorosoma suillum (strain ATCC BAA-33 / DSM 13638 / PS) (Azospira OS oryzae). OC Bacteria; Proteobacteria; Betaproteobacteria; Rhodocyclales; OC Rhodocyclaceae; Azospira. OX NCBI_TaxID=640081 {ECO:0000313|EMBL:AEV27468.1, ECO:0000313|Proteomes:UP000005633}; RN [1] {ECO:0000313|EMBL:AEV27468.1, ECO:0000313|Proteomes:UP000005633} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-33 / DSM 13638 / PS RC {ECO:0000313|Proteomes:UP000005633}; RX PubMed=22535943; DOI=10.1128/JB.00124-12; RA Byrne-Bailey K.G., Coates J.D.; RT "Complete genome sequence of the anaerobic perchlorate-reducing RT bacterium Azospira suillum strain PS."; RL J. Bacteriol. 194:2767-2768(2012). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP003153; AEV27468.1; -; Genomic_DNA. DR RefSeq; WP_014238148.1; NC_016616.1. DR STRING; 640081.Dsui_3136; -. DR EnsemblBacteria; AEV27468; AEV27468; Dsui_3136. DR KEGG; dsu:Dsui_3136; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000005633; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000005633}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000005633}. FT DOMAIN 205 371 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 171 198 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 395 AA; 42976 MW; 42FBA01DCF64F3C0 CRC64; MFDRPSAGDP RVPGSERALL IQVDFGQPNI EDSQEELHLL ASSAGAEVVD VLVAKRGAPD AATYVGKGKV QEIGAVAAAH DATLVIFNHE LSPAQERNLE RALQCRVIDR TSLILDIFAL RASSSEGKLQ VELAQLEHLA TRLVRGWTHL ERQRGGIGMR GPGEKQLETD RRLLGVRVKS LKERLAKLSR QRNVQRRARS RRDVLNVSLV GYTNAGKSTL FNAMTKAGVY AADQLFATLD TTSRKLWLPE VGSVVMSDTV GFIRDLPHAL VEAFKATLEA TAQADLLLHV VDSASHAREE QIAEVNKVLH EIGADQVPQI LVWNKADLTG LPAAVERDEY GKLHRVRLSA RTGEGLDLLR QALTEFARDN SLSMTTAASA DDAAAASAND AVQDV // ID G8QVE2_SPHPG Unreviewed; 450 AA. AC G8QVE2; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 07-JUN-2017, entry version 37. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=SpiGrapes_2699 {ECO:0000313|EMBL:AEV30457.1}; OS Sphaerochaeta pleomorpha (strain ATCC BAA-1885 / DSM 22778 / Grapes). OC Bacteria; Spirochaetes; Spirochaetales; Spirochaetaceae; OC Sphaerochaeta. OX NCBI_TaxID=158190 {ECO:0000313|EMBL:AEV30457.1, ECO:0000313|Proteomes:UP000005632}; RN [1] {ECO:0000313|EMBL:AEV30457.1, ECO:0000313|Proteomes:UP000005632} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-1885 / DSM 22778 / Grapes RC {ECO:0000313|Proteomes:UP000005632}; RG US DOE Joint Genome Institute; RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S., RA Peters L., Ovchinnikova G., Munk A.C., Detter J.C., Han C., Tapia R., RA Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., RA Ritalahtilisa K., Loeffler F., Woyke T.; RT "Complete sequence of Spirochaeta sp. grapes."; RL Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP003155; AEV30457.1; -; Genomic_DNA. DR RefSeq; WP_014271297.1; NC_016633.1. DR STRING; 158190.SpiGrapes_2699; -. DR EnsemblBacteria; AEV30457; AEV30457; SpiGrapes_2699. DR KEGG; sgp:SpiGrapes_2699; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000005632; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000005632}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000005632}. FT DOMAIN 220 386 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 450 AA; 50748 MW; 217BD45A9B0DF8EC CRC64; METDHFEQKE ENSSKGKRIH DIGEDKQKAL LMVIMENNEE KAHAQVRGEE LSSLVETMGP SVISTTYIPL REANSATLIG SGKVQEIKAL IDQQSPDLII FDHSLNPRVQ RNLEKEFDCC VIDRDEVILQ IFADRAATKE SVLQVELARL EYSLPRLSRR WANLSQQRGG VKGSKGEGET QLELDHRQIK DKIVLLKTQL KKVQQQRTIQ RNQRMNGNVP MGAIVGYTNS GKSSLLNALS NAGVLVENKL FATLDPTTRM VKLPGGEEIL LSDTVGFVSD LPHNLVDSFK STLEEAKYAD FLIIVCDASH PDMINCYKTT VKVLEELGCT DKPAIVMINK MDAIYDQFAV SRMKSLYSPT VETSVKNNQG IEELLKQIGE TIHELCPTTH YRIPDNRYDL IAHIRRTGQV ETLDYTDNGI EVGARIQKRF QGPLEGFRMF TEEEEEPSEE // ID G8R050_OWEHD Unreviewed; 401 AA. AC G8R050; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 07-JUN-2017, entry version 36. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Oweho_2754 {ECO:0000313|EMBL:AEV33716.1}; OS Owenweeksia hongkongensis (strain DSM 17368 / CIP 108786 / JCM 12287 / OS NRRL B-23963 / UST20020801). OC Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales; OC Cryomorphaceae; Owenweeksia. OX NCBI_TaxID=926562 {ECO:0000313|EMBL:AEV33716.1, ECO:0000313|Proteomes:UP000005631}; RN [1] {ECO:0000313|EMBL:AEV33716.1, ECO:0000313|Proteomes:UP000005631} RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 17368 / JCM 12287 / NRRL B-23963 RC {ECO:0000313|Proteomes:UP000005631}; RX PubMed=23450211; DOI=10.4056/sigs.3296896; RA Riedel T., Held B., Nolan M., Lucas S., Lapidus A., Tice H., RA Del Rio T.G., Cheng J.F., Han C., Tapia R., Goodwin L.A., Pitluck S., RA Liolios K., Mavromatis K., Pagani I., Ivanova N., Mikhailova N., RA Pati A., Chen A., Palaniappan K., Rohde M., Tindall B.J., Detter J.C., RA Goker M., Woyke T., Bristow J., Eisen J.A., Markowitz V., RA Hugenholtz P., Klenk H.P., Kyrpides N.C.; RT "Genome sequence of the orange-pigmented seawater bacterium RT Owenweeksia hongkongensis type strain (UST20020801(T))."; RL Stand. Genomic Sci. 7:120-130(2012). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP003156; AEV33716.1; -; Genomic_DNA. DR RefSeq; WP_014203065.1; NC_016599.1. DR STRING; 926562.Oweho_2754; -. DR EnsemblBacteria; AEV33716; AEV33716; Oweho_2754. DR KEGG; oho:Oweho_2754; -. DR PATRIC; fig|926562.3.peg.2771; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000005631; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000005631}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000005631}. FT DOMAIN 204 390 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 401 AA; 46032 MW; FF2BFE75A706948B CRC64; MIESKKKNLS TEPEKAVLIG VITQFQPEEK LGEYMDELEF LADTAGAICV KRFWQKLDKP NPKTLLGSGK IEEIASFVKS ENIDIAIFDD ELSPSQLKNI EKIFECKVLD RTNLILDIFA SRAVTSYART QVELAQYQYL LPRLTNMWTH LSKQKGGIGM KGPGEREIET DRRIIRDKIS LLKDKLKKID KQMAIQRGNR GSLIRVALVG YTNVGKSTLM NLLSKSEVFA ENKLFATLDT TVRKVVLENL PFLLTDTVGF IRKLPTQLVE SFKSTLDEVR ESDVLIHVVD ISHPNFEEHI ETVNNTIKDI DPNIADKTVM MVFNKIDQYS YEVKDEDDLS PATKANYTLD DWKRTWFGKS DKNVVFISAT ERENIEDLKH RIYEVVAELH AIRFPFNNFL Y // ID G8RKS9_MYCRN Unreviewed; 471 AA. AC G8RKS9; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 07-JUN-2017, entry version 36. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=MycrhN_5588 {ECO:0000313|EMBL:AEV76056.1}; OS Mycobacterium rhodesiae (strain NBB3). OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae; OC Mycobacterium. OX NCBI_TaxID=710685 {ECO:0000313|EMBL:AEV76056.1, ECO:0000313|Proteomes:UP000005442}; RN [1] {ECO:0000313|EMBL:AEV76056.1, ECO:0000313|Proteomes:UP000005442} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NBB3 {ECO:0000313|EMBL:AEV76056.1, RC ECO:0000313|Proteomes:UP000005442}; RG US DOE Joint Genome Institute; RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S., RA Peters L., Mikhailova N., Gu W., Detter J.C., Han C., Tapia R., RA Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Mattes T., RA Holmes A., Rutledge P., Paulsen I., Coleman N., Woyke T.; RT "Complete sequence of Mycobacterium rhodesiae NBB3."; RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP003169; AEV76056.1; -; Genomic_DNA. DR STRING; 710685.MycrhN_5588; -. DR EnsemblBacteria; AEV76056; AEV76056; MycrhN_5588. DR KEGG; mrh:MycrhN_5588; -. DR PATRIC; fig|710685.3.peg.5614; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000005442; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000005442}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}. FT DOMAIN 248 417 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 207 241 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 471 AA; 50763 MW; F390480457771F28 CRC64; MTHPEFPVNE KPSAGELALE DRAALRRVAG LSTELSDISE VEYRQLRLER VVLVGVWTEG SAADVDASMA ELAALAETAG SEVLDGLIQR RDKPDPATYI GSGKAAELRE VVLATGADTV ICDGELSPAQ LTALEKAVKV KVIDRTALIL DIFAQHATSR EGKAQVTLAQ MEYMLPRLRG WGESMSRQAG GRAGGAGGGV GTRGPGETKI ETDRRRIRER MSKLRREIKD MKKIRDTQRS RRLASDAASI AIVGYTNAGK SSLLNALTGA GVLVENALFA TLEPTTRRGE FEDGRAFVLT DTVGFVRHLP TQLVEAFRST LEEVVDADLL VHVVDGSDVN PLAQIRAVRT VVNEVIVDHQ HKPAPELVVV NKIDAADDLA LAQLRRALPD AVFVSAHTGE GLQRLQQRMA ELVAPTDTAV DVTIPYDRGD LVNKVHADGR VDATEHTADG TRIKARVPVS LAATLGEFAT F // ID G8SGZ3_ACTS5 Unreviewed; 471 AA. AC G8SGZ3; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 05-JUL-2017, entry version 39. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:AEV88033.1}; GN OrderedLocusNames=ACPL_7153 {ECO:0000313|EMBL:AEV88033.1}; OS Actinoplanes sp. (strain ATCC 31044 / CBS 674.73 / SE50/110). OC Bacteria; Actinobacteria; Micromonosporales; Micromonosporaceae; OC Actinoplanes. OX NCBI_TaxID=134676 {ECO:0000313|EMBL:AEV88033.1, ECO:0000313|Proteomes:UP000005440}; RN [1] {ECO:0000313|Proteomes:UP000005440} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 31044 / CBS 674.73 / SE50/110 RC {ECO:0000313|Proteomes:UP000005440}; RA Schwientek P., Szczepanowski R., Kalinowski J., Klein A., Selber K., RA Wehmeier U.F., Stoye J., Puehler A.; RT "The complete genome sequence of the acarbose producer Actinoplanes RT sp. SE50/110."; RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP003170; AEV88033.1; -; Genomic_DNA. DR RefSeq; WP_014694097.1; NZ_LT827010.1. DR STRING; 134676.ACPL_7153; -. DR EnsemblBacteria; AEV88033; AEV88033; ACPL_7153. DR KEGG; ase:ACPL_7153; -. DR PATRIC; fig|134676.3.peg.7064; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000005440; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 2. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000005440}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000005440}. FT DOMAIN 253 418 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 212 246 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 471 AA; 51522 MW; C3C7391FF50AE502 CRC64; MRNTYQAPVL DEPDLTTGDL ELEERHSLRR VAGLSTELTD ITEVEYRQLR LERVVLVGVW TEGSVEDADN SLTELAQLAE TAGSQVLEGL IQRRRQPDAA TFIGRGKVDE LRDAVVASGA DTVICDGELS PSQLRNLEQQ IKVKVVDRTA LILDIFAQHA KSKEGKAQVE LAQLQYLLPR LRGWGESLSR QGGGAGGGGS GGGGVGTRGP GETKLETDRR RINQRIAKLR REIKAMRTAR DTKRSRRQAS GTPAVAIAGY TNAGKSSLLN RLTEAGVLVE NALFATLDPT TRRTSAEDGR VYTLSDTVGF VRHLPHQIVE AFRSTLEEVA DADLVVHVVD GSHPDPEGQV SAVREVLGEV GADRIPELLV INKMDAADEE TVLRLKRAWP DAVFVSARSG SGISELRAAI AERLPRPPVD MRILLPYSRA DLVARVHRTG QVLQSRHLDD GTELRVLVDE RLAADLEEFR C // ID G8T8X9_NIAKG Unreviewed; 394 AA. AC G8T8X9; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 07-JUN-2017, entry version 35. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Niako_6111 {ECO:0000313|EMBL:AEW02336.1}; OS Niastella koreensis (strain DSM 17620 / KACC 11465 / GR20-10). OC Bacteria; Bacteroidetes; Chitinophagia; Chitinophagales; OC Chitinophagaceae; Niastella. OX NCBI_TaxID=700598 {ECO:0000313|EMBL:AEW02336.1, ECO:0000313|Proteomes:UP000005438}; RN [1] {ECO:0000313|EMBL:AEW02336.1, ECO:0000313|Proteomes:UP000005438} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 17620 / KACC 11465 / GR20-10 RC {ECO:0000313|Proteomes:UP000005438}; RG US DOE Joint Genome Institute (JGI-PGF); RA Lucas S., Han J., Lapidus A., Bruce D., Goodwin L., Pitluck S., RA Peters L., Kyrpides N., Mavromatis K., Ivanova N., Mikhailova N., RA Davenport K., Saunders E., Detter J.C., Tapia R., Han C., Land M., RA Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T., Wu D., RA Tindall B., Pomrenke H., Brambilla E., Klenk H.-P., Eisen J.A.; RT "The complete genome of Niastella koreensis GR20-10."; RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP003178; AEW02336.1; -; Genomic_DNA. DR RefSeq; WP_014222246.1; NC_016609.1. DR STRING; 700598.Niako_6111; -. DR EnsemblBacteria; AEW02336; AEW02336; Niako_6111. DR KEGG; nko:Niako_6111; -. DR PATRIC; fig|700598.3.peg.6261; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000005438; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000005438}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Hydrolase {ECO:0000313|EMBL:AEW02336.1}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000005438}. FT DOMAIN 202 384 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 394 AA; 45496 MW; 2DFD2DD48D40F58F CRC64; MLDKKNIIQN EEKAVLVGLV HKLQTEEQVT EYLDELAFLA ETAGAKAVKR FVQKLPHPDS RTFVGKGKLE EIKNYIEGRD INIVIFDDEL SGSQIQNIEN VLEVKTIDRS DLILDIFARR AKTAQAKTQV ELAQYQYLMP RLRGMWKHLE RLGGGIGTRG PGETEIETDR RIVREKIALL RKRLSEIDKQ SATQRKDRGE FIRVALVGYT NVGKSTIMNL LSKSDVFAEN KLFATLDTTT RKVVFETTPF LLSDTVGFIR KLPHHLVESF KSTLDEVREA DILLHVADTS HPQYEDQIGV VNKTLQELNV IDKPTITIFN KMDQYEKNTF DPWLEEEVRT EILVDLKERW ENQLQGNCVF ISATERRNID ELRSTILNKV KELYRIRYPY KTGF // ID G8UPL4_TANFA Unreviewed; 411 AA. AC G8UPL4; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 30-AUG-2017, entry version 36. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:AEW19833.1}; GN OrderedLocusNames=BFO_1905 {ECO:0000313|EMBL:AEW19833.1}; OS Tannerella forsythia (strain ATCC 43037 / JCM 10827 / FDC 338) OS (Bacteroides forsythus). OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Tannerellaceae; OC Tannerella. OX NCBI_TaxID=203275 {ECO:0000313|EMBL:AEW19833.1, ECO:0000313|Proteomes:UP000005436}; RN [1] {ECO:0000313|Proteomes:UP000005436} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43037 / JCM 10827 / FDC 338 RC {ECO:0000313|Proteomes:UP000005436}; RA Dewhirst F., Tanner A., Izard J., Brinkac L., Durkin A.S., RA Hostetler J., Shetty J., Torralba M., Gill S., Nelson K.; RT "Complete sequence of Tannerella forsythia ATCC 43037."; RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP003191; AEW19833.1; -; Genomic_DNA. DR RefSeq; WP_014225237.1; NC_016610.1. DR STRING; 203275.BFO_1905; -. DR EnsemblBacteria; AEW19833; AEW19833; BFO_1905. DR KEGG; tfo:BFO_1905; -. DR PATRIC; fig|203275.8.peg.1727; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000005436; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000005436}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000005436}. FT DOMAIN 202 386 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 170 197 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 411 AA; 47521 MW; 494D06377E2AEC24 CRC64; MKEFIITREQ TEKAVLVGLV TPDQDERRVK EYLDELDFLA DTAGVRPVKR FIQKLDMPHS VTFVGSGKLQ QIKEYVIEHE IGIVVFDDEL SAKQLRNIEK ALQVRILDRT NLILDIFAKR AQTAHAKTQV ELAQYRYMLP RLTRLWTHLE RQRGGVGMRG PGETQLETDK RIILDKISRL KRELAEIDKQ KSSQRKNRGK MVRVALVGYT NVGKSTLMNL LSKSEVFAEN KLFATLDTTV RKVIIENLPF LLSDTVGFIR KLPVELVESF KSTLDEVREA DLLLHMVDVS HPMFEEQIEV VDRTLAEIGC ESKPVIMIFN KVDAFSFVPK EEDDLTPRQR ENLSLSELKE TWMNKRSGNT VFISARGRTN IDALKAVLYE RVKAIHITRF PYNDFLFQHY ETDEEEMHSE A // ID G8XBJ8_FLACA Unreviewed; 406 AA. AC G8XBJ8; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 21-MAR-2012, sequence version 2. DT 07-JUN-2017, entry version 35. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=FCOL_13090 {ECO:0000313|EMBL:AEW87413.2}; OS Flavobacterium columnare (strain ATCC 49512 / CIP 103533 / TG 44/87). OC Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales; OC Flavobacteriaceae; Flavobacterium. OX NCBI_TaxID=1041826 {ECO:0000313|EMBL:AEW87413.2, ECO:0000313|Proteomes:UP000005638}; RN [1] {ECO:0000313|Proteomes:UP000005638} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 49512 / CIP 103533 / TG 44/87 RC {ECO:0000313|Proteomes:UP000005638}; RA Tekedar H.C., Karsi A., Gillaspy A.F., Dyer D., Benton N.R., RA Zaitshik J., Vamenta S., Banes M.M., Gulsoy N., Aboko-Cole M., RA Waldbieser G.C., Lawrence M.L.; RT "Complete genome sequence of Flavobacterium columnare ATCC 49512."; RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP003222; AEW87413.2; -; Genomic_DNA. DR RefSeq; WP_014166667.1; NC_016510.2. DR STRING; 1041826.FCOL_13090; -. DR EnsemblBacteria; AEW87413; AEW87413; FCOL_13090. DR KEGG; fco:FCOL_13090; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000005638; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000005638}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000005638}. FT DOMAIN 200 386 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 406 AA; 47065 MW; A1F22EA3ED9CCD31 CRC64; MLEKEKHIFE KTVIVGIVTQ SQNEDKLNEY LDELEFLTFT AGGEVVKRFT QKMDKPNPKT FVGTGKLEQI NLYIKENDIK TVIFDDELSP AQQKNITREL DCKVLDRTNL ILDIFAQRAE TSYARTQVEL AQCQYLLPRL TGMWTHLERQ RGGIGMRGPG ETEIETDRRI VRDRIALLKE KIKTIDKQMA IQRSNRGAMV RVALVGYTNV GKSTLMNAVG KSEVFVENKL FATLDTTVRK VVIKNLPFLL SDTVGFIRKL PTQLVESFKS TLDEVREADL LLHIVDISHP EFEDHIESVN QILQDIKSSD KPTIMVFNKI DSYQHLTIAE DDLITEKTTK HYTLEDWKNT WMNRLGENHA LFISATEKHN FEEFREKIYE AVRQIHITRF PYNNFLYPDY KEADGE // ID G9EJW5_9GAMM Unreviewed; 418 AA. AC G9EJW5; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 30-AUG-2017, entry version 35. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=LDG_5482 {ECO:0000313|EMBL:EHL32525.1}; OS Legionella drancourtii LLAP12. OC Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales; OC Legionellaceae; Legionella. OX NCBI_TaxID=658187 {ECO:0000313|EMBL:EHL32525.1, ECO:0000313|Proteomes:UP000002770}; RN [1] {ECO:0000313|EMBL:EHL32525.1, ECO:0000313|Proteomes:UP000002770} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=LLAP12 {ECO:0000313|EMBL:EHL32525.1, RC ECO:0000313|Proteomes:UP000002770}; RX PubMed=22047552; DOI=10.1186/1471-2164-12-542; RA Gimenez G., Bertelli C., Moliner C., Robert C., Raoult D., RA Fournier P.E., Greub G.; RT "Insight into cross-talk between intra-amoebal pathogens."; RL BMC Genomics 12:542-542(2011). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JH413798; EHL32525.1; -; Genomic_DNA. DR RefSeq; WP_006869462.1; NZ_JH413798.1. DR ProteinModelPortal; G9EJW5; -. DR STRING; 658187.LDG_5482; -. DR EnsemblBacteria; EHL32525; EHL32525; LDG_5482. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000002770; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000002770}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000002770}. FT DOMAIN 198 363 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 418 AA; 47036 MW; 6F1BF1ED9B72AA85 CRC64; MFERPQGGER ALLVQLALPG VDAEKALQEF EELARSANAE VLDCVLGTRA TPEAKYYVGK GKAEEIAQLV KALDAELVLV NHELSPSQER NLERLLECRV VDRSGLILDI FAQRARTFEG KLQVELAQLQ HLSTRLIRGW THLERQKGGI GLRGPGETQL ETDRRLLRER IKYINRRLEK VRCSRDQNRQ ARRKAAMPTV SLVGYTNAGK STLFNALTGE RIYVANQLFA TLDPTMRQLS LPGASGVILA DTVGFIRDLP HHLVEAFRAT LEETQQADLL LHVIDISDPH WRDTVFSVQQ VLDELGVNDI PVIQVFNKID LQEGWEAKID YNQEWCKVWI SAAANIGLDL LKEAISTQLH GAVLIEDVVL KPVQAKLRAQ LYQLGAILHE SLSDEGDWLL KIRITRAQKQ RLFASASK // ID G9PD26_9ACTO Unreviewed; 525 AA. AC G9PD26; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 07-JUN-2017, entry version 37. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=HMPREF0045_00305 {ECO:0000313|EMBL:EHM89640.1}; OS Actinomyces graevenitzii C83. OC Bacteria; Actinobacteria; Actinomycetales; Actinomycetaceae; OC Actinomyces. OX NCBI_TaxID=435830 {ECO:0000313|EMBL:EHM89640.1, ECO:0000313|Proteomes:UP000003822}; RN [1] {ECO:0000313|EMBL:EHM89640.1, ECO:0000313|Proteomes:UP000003822} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C83 {ECO:0000313|EMBL:EHM89640.1, RC ECO:0000313|Proteomes:UP000003822}; RG The Broad Institute Genome Sequencing Platform; RG The Broad Institute Genome Sequencing Center for Infectious Disease; RA Earl A., Ward D., Feldgarden M., Gevers D., Sibley C.D., Field T.R., RA Grinwis M., Eshaghurshan C.S., Surette M.G., Young S.K., Zeng Q., RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L., RA Arachchi H.M., Berlin A., Brown A., Chapman S.B., Chen Z., Dunbar C., RA Freedman E., Gearin G., Goldberg J., Griggs A., Gujja S., Heiman D., RA Howarth C., Larson L., Lui A., MacDonald P.J.P., Montmayeur A., RA Murphy C., Neiman D., Pearson M., Priest M., Roberts A., Saif S., RA Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., Wortman J., RA Nusbaum C., Birren B.; RT "The Genome Sequence of Actinomyces graevenitzii C83."; RL Submitted (OCT-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EHM89640.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACRN01000001; EHM89640.1; -; Genomic_DNA. DR RefSeq; WP_005984845.1; NZ_JH470338.1. DR EnsemblBacteria; EHM89640; EHM89640; HMPREF0045_00305. DR PATRIC; fig|435830.3.peg.295; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000003822; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 2. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000003822}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000003822}. FT DOMAIN 290 456 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 525 AA; 56414 MW; C4C7EC4A48DE578D CRC64; MTKTNNFSAG NPLVSSEAAP SRDSSAQARD IIDRVLSRSG TALASTAAQH ERGEKNDAGA LERAERAALT RVAGLSTELE DVSEVEYRQI RLEKVVLIGI YSTNAQEAEY SLRELAALAE TAGSQVLDAL LQRRDTPDPA TYLGSGKAKE LAQIVADTGA DTVIADGDLA PSQRRALEDV VKVKVVDRTA LILDIFAQHA KSREGKAQVE LAQLEYLLPR LRGWGESMSR QAGGRVAAGQ GIGSRGPGET KIELDRRRIR DRMAKLRREI KAMAPARETK RGSRQRGAIA SVAIAGYTNA GKSSLLNAIT GAQIMVQDAL FATLDPTVRR ASTPDGRVYT LTDTVGFVRN LPHELIEAFR STLEEVAQAD LILHVVDAAH PDPVGQISAV RQVLADIDGV ENIPELVVFN KADLADPVDL VGLRTREPNS VVVSAYTGKG IEQLVERIAQ LLPRPEVMVD LILPYSRGDL LARVHEDGDI EILEYVETGT HLRARVHPGL ASALKQAALA GSGTRGADRG GVEPN // ID G9PYM1_9BACT Unreviewed; 385 AA. AC G9PYM1; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 07-JUN-2017, entry version 36. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=HMPREF1006_00733 {ECO:0000313|EMBL:EHL64448.1}; OS Synergistes sp. 3_1_syn1. OC Bacteria; Synergistetes; Synergistia; Synergistales; Synergistaceae; OC Synergistes. OX NCBI_TaxID=457415 {ECO:0000313|EMBL:EHL64448.1, ECO:0000313|Proteomes:UP000003380}; RN [1] {ECO:0000313|EMBL:EHL64448.1, ECO:0000313|Proteomes:UP000003380} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=3_1_syn1 {ECO:0000313|EMBL:EHL64448.1, RC ECO:0000313|Proteomes:UP000003380}; RG The Broad Institute Genome Sequencing Platform; RA Earl A., Ward D., Feldgarden M., Gevers D., Daigneault M., Strauss J., RA Allen-Vercoe E., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., RA Haas B., Abouelleil A., Alvarado L., Arachchi H.M., Berlin A., RA Brown A., Chapman S.B., Chen Z., Dunbar C., Freedman E., Gearin G., RA Goldberg J., Griggs A., Gujja S., Heiman D., Howarth C., Larson L., RA Lui A., MacDonald P.J.P., Montmayeur A., Murphy C., Neiman D., RA Pearson M., Priest M., Roberts A., Saif S., Shea T., Shenoy N., RA Sisk P., Stolte C., Sykes S., Wortman J., Nusbaum C., Birren B.; RT "The Genome Sequence of Synergistes sp. 3_1_syn1."; RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EHL64448.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACUH01000059; EHL64448.1; -; Genomic_DNA. DR RefSeq; WP_008712634.1; NZ_JH414697.1. DR EnsemblBacteria; EHL64448; EHL64448; HMPREF1006_00733. DR PATRIC; fig|457415.3.peg.2517; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000003380; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR Gene3D; 3.20.20.10; -; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR029066; PLP-binding_barrel. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000003380}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000003380}. FT DOMAIN 206 376 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 172 199 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 385 AA; 42560 MW; 16CC8A8EB5E979B4 CRC64; MSRQKRTSID LSLKPPKAVI AAVDCGSADD TEQSLDELVM LLENIGVPVA ARVVQKRNIP DPAHFIGAGK ALEIKEYALP NEVTHLVVDD FLSPTQKSNL QKVTGLQVWD RAFVIMKIFE SRAHTAEAKL QVELAQYRYE IPSLKGLGHQ MSRTGGGIGT RGPGETEFER HRRKLDRRMK SIEQRLDDVR KRREERRDRR RRDGVPVAAL VGYTNSGKST LLQALSKDAG IVAKDQLFST LDTVVRKIGY RGGEGHFLLS DTVGFIRKLP PALVAAFRAT LEEAANADLL LLVLDSADKE PIETLGIVLD TLNDLKADHL PRIVVLNKID KSGEAADFIA VELRARGERV VCTCALDGRG FDELLGEIKK IFESEVALTG IKDIL // ID G9RW81_9FIRM Unreviewed; 413 AA. AC G9RW81; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 07-JUN-2017, entry version 32. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=HMPREF1032_00532 {ECO:0000313|EMBL:EHL67136.1}; OS Subdoligranulum sp. 4_3_54A2FAA. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Ruminococcaceae; OC Subdoligranulum. OX NCBI_TaxID=665956 {ECO:0000313|EMBL:EHL67136.1, ECO:0000313|Proteomes:UP000003855}; RN [1] {ECO:0000313|EMBL:EHL67136.1, ECO:0000313|Proteomes:UP000003855} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=4_3_54A2FAA {ECO:0000313|EMBL:EHL67136.1, RC ECO:0000313|Proteomes:UP000003855}; RG The Broad Institute Genome Sequencing Platform; RA Earl A., Ward D., Feldgarden M., Gevers D., Daigneault M., Strauss J., RA Allen-Vercoe E., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., RA Haas B., Abouelleil A., Alvarado L., Arachchi H.M., Berlin A., RA Brown A., Chapman S.B., Chen Z., Dunbar C., Freedman E., Gearin G., RA Goldberg J., Griggs A., Gujja S., Heiman D., Howarth C., Larson L., RA Lui A., MacDonald P.J.P., Montmayeur A., Murphy C., Neiman D., RA Pearson M., Priest M., Roberts A., Saif S., Shea T., Shenoy N., RA Sisk P., Stolte C., Sykes S., Wortman J., Nusbaum C., Birren B.; RT "The Genome Sequence of Subdoligranulum sp. 4_3_54A2FAA."; RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EHL67136.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACWW01000077; EHL67136.1; -; Genomic_DNA. DR RefSeq; WP_009324906.1; NZ_JH414706.1. DR EnsemblBacteria; EHL67136; EHL67136; HMPREF1032_00532. DR PATRIC; fig|665956.3.peg.3129; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000003855; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000003855}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000003855}. FT DOMAIN 200 360 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 166 193 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 413 AA; 44680 MW; 71EDF70E789796A7 CRC64; MTEEPIKVVL FAADCGGYDI ERSMEELAAL AQANGMEAVA EVVQKRETPE AATFLGEGRL AEGRMLCINL GAECAVFDAE LSGSQIRNLE ELLEVQVIDR TMLILEIFAS RAVTNEGKLQ TELATLQYRL PRLAGLGASL SRQGGGGGGG AGARRGAGES KLEYDRRHVR RRIDALRERL EELERRRAET RKSREKSGVP VVALVGYTNV GKSSLLNRLC GAQVLEADML FATLDPTARR LTLPSGLACV AVDTVGFVSR LPHNLVQAFK STLEEAAFAD VILKVCDASD PEAAAQLAVT DDVLGELGCG DIPQIVVYNK CDRVENAALF DTSAMRTSAV TGEGLDALLA RLDAALAGRV RRIAVLLPYD KLGEATPMRE NGTVLTEEYR PEGVYLEGIV KTMDLHRFTP YLV // ID G9WJ18_9LACT Unreviewed; 437 AA. AC G9WJ18; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 07-JUN-2017, entry version 36. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=OKIT_0345 {ECO:0000313|EMBL:EHN58467.1}; OS Oenococcus kitaharae DSM 17330. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Leuconostocaceae; OC Oenococcus. OX NCBI_TaxID=1045004 {ECO:0000313|EMBL:EHN58467.1, ECO:0000313|Proteomes:UP000004959}; RN [1] {ECO:0000313|EMBL:EHN58467.1, ECO:0000313|Proteomes:UP000004959} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 17330 {ECO:0000313|EMBL:EHN58467.1}; RX PubMed=22235313; DOI=10.1371/journal.pone.0029626; RA Borneman A.R., McCarthy J.M., Chambers P.J., Bartowsky E.J.; RT "Functional divergence in the genus oenococcus as predicted by genome RT sequencing of the newly-described species, Oenococcus kitaharae."; RL PLoS ONE 7:E29626-E29626(2012). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EHN58467.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFVZ01000001; EHN58467.1; -; Genomic_DNA. DR RefSeq; WP_007744756.1; NZ_KE386622.1. DR EnsemblBacteria; EHN58467; EHN58467; OKIT_0345. DR PATRIC; fig|1045004.4.peg.344; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000004959; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000004959}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000004959}. FT DOMAIN 211 383 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 170 197 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 437 AA; 48464 MW; DBB4901AA0FE6ACC CRC64; MAEQLFNTEQ AKERVILVAL ENQKNSASFA YTIEEFKNLA AANNLNVVDV LTQKYDRPNA STYFGKGKVT ELKELVAARE AELVISNDDL TATQIRNLKK KIGGGTRVVD RTALILDIFA SRAKSKLAKL QIRLAQKQYQ LPRLHTALAN ELDQQGGAGG GSFTSRGSGE TKLELNRRTI EDQITQIKAE LKTLLSASTV QRSQRDHSGL KTVALVGYTN AGKSTWMNRM IEKYSESKED IDDKKVFEKD MLFATLDATV RAIRLPNKRR FLLSDTVGFV SNLPHNLIAS FQSTLDEAVH ADLLVQIVDV SDPHYRDMMA TTKSTLAAIG AEQIPMVTVF NKADKAGVTY PERSGEDLIA SALDDNSLDA FIKLLDEKLF ADFKTVELMI PFDQGAVVNQ ILNGNNVLEQ DFTAQGTRLR VELPAAQIET YQAFVQK // ID G9YNY6_9FIRM Unreviewed; 430 AA. AC G9YNY6; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 07-JUN-2017, entry version 35. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=HMPREF0372_01214 {ECO:0000313|EMBL:EHM53019.1}; OS Flavonifractor plautii ATCC 29863. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Flavonifractor. OX NCBI_TaxID=411475 {ECO:0000313|EMBL:EHM53019.1, ECO:0000313|Proteomes:UP000004459}; RN [1] {ECO:0000313|EMBL:EHM53019.1, ECO:0000313|Proteomes:UP000004459} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29863 {ECO:0000313|EMBL:EHM53019.1, RC ECO:0000313|Proteomes:UP000004459}; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Hou S., Chen J., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Zhang X., Suruliraj S., Warren W., Chinwalla A., RA Mardis E.R., Wilson R.K.; RL Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EHM53019.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGCK01000086; EHM53019.1; -; Genomic_DNA. DR RefSeq; WP_007489592.1; NZ_JH417693.1. DR EnsemblBacteria; EHM53019; EHM53019; HMPREF0372_01214. DR PATRIC; fig|411475.3.peg.1052; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000004459; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000004459}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000004459}. FT DOMAIN 205 366 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 164 198 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 430 AA; 47751 MW; 924826CEA7A714C7 CRC64; MTENETKQAK NRAVLVGLNA HCLSAEENAD DTSMEELADL LETAGGVCVG TVFQNKDAPD PRTFIGEGKA AEVKELVGAM GADMVVVDNP LSPSQQRVLS EELGVQVLDR AALILDIFAQ RARTREGRLQ VELAQYQYLL PRLLGMWTHL ERQEGAIGTR GPGETQLETD RRHIRRKIQK LREELEQVRR VRATQRTRRE KNEVPVVAIV GYTNAGKSTL LNRLTGADIP ANNRLFDTLD TTTRTLEISD TCTVLLSDTV GFIRKLPHHL VEAFKATLEE LSYADLLLHV IDASNPLWRE QAAVVEQLIV ELGAEQTPRI DVFNKCDRFT GDILPHGADI VSISAKTGQG LDELLKKIGG RLDTGACRVV LRLPYDQGGV VDMLHRQAKV ERVDYGEAIE VEAVCTPVQL GRLKDYIVSG WTPPKEPWED // ID G9ZKA1_9LACO Unreviewed; 428 AA. AC G9ZKA1; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 07-JUN-2017, entry version 35. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=HMPREF9103_00149 {ECO:0000313|EMBL:EHM01248.1}; OS Lactobacillus parafarraginis F0439. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; OC Lactobacillus. OX NCBI_TaxID=797515 {ECO:0000313|EMBL:EHM01248.1, ECO:0000313|Proteomes:UP000004625}; RN [1] {ECO:0000313|EMBL:EHM01248.1, ECO:0000313|Proteomes:UP000004625} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=F0439 {ECO:0000313|EMBL:EHM01248.1, RC ECO:0000313|Proteomes:UP000004625}; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Hou S., Chen J., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Zhang X., Suruliraj S., Warren W., Chinwalla A., RA Mardis E.R., Wilson R.K.; RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EHM01248.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGEY01000010; EHM01248.1; -; Genomic_DNA. DR RefSeq; WP_008210419.1; NZ_JH414908.1. DR EnsemblBacteria; EHM01248; EHM01248; HMPREF9103_00149. DR PATRIC; fig|797515.3.peg.134; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000004625; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000004625}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000004625}. FT DOMAIN 204 372 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 428 AA; 47653 MW; 93CBD251B1D7B26E CRC64; MDLTQTLTPV VTIGLNQHPN SFNYSMTELN NLAEANNMKV VETLVQKLDR PDPATYFGKG KIEELGQVVI DDGVDTIVAN DELSPSQIRN IEKATKARII DRTGLILEIF ANRAQSREAK LQVELAKLKY QLPRLHTSAS QRLDQQTGTS SGAGGATNRG AGESQYEMNR RTLEKRITHV NHELKEADKA DQIKRQQRDK SETPTVALVG YTNAGKSTIM NGMINLLGEN EDKQVLVKNM LFATLDTSVR KLALPDQKKF LLSDTVGFVS QLPHQLVQAF KSTLAEAANA DLLIQVVDYS DPHRDMMIKT TEDTLKEIGI DNIPMVVALN KADKMETPYP TREGDNLIMA ATDKKSLVEL TAIIKEKVFK NFKTLQLMIP FDKGDVVSYL NDNATVLKTD YDANGTLITA ELNEVDAKRF SRYVQPVD // ID G9ZVR4_9PROT Unreviewed; 434 AA. AC G9ZVR4; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 07-JUN-2017, entry version 32. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=HMPREF9946_00630 {ECO:0000313|EMBL:EHM02940.1}; OS Acetobacteraceae bacterium AT-5844. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales; OC Acetobacteraceae; unclassified Acetobacteraceae. OX NCBI_TaxID=1054213 {ECO:0000313|EMBL:EHM02940.1, ECO:0000313|Proteomes:UP000003292}; RN [1] {ECO:0000313|EMBL:EHM02940.1, ECO:0000313|Proteomes:UP000003292} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=AT-5844 {ECO:0000313|Proteomes:UP000003292}; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Hou S., Chen J., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Zhang X., Suruliraj S., Warren W., Chinwalla A., RA Mardis E.R., Wilson R.K.; RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EHM02940.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGEZ01000022; EHM02940.1; -; Genomic_DNA. DR RefSeq; WP_007435024.1; NZ_JH599929.1. DR EnsemblBacteria; EHM02940; EHM02940; HMPREF9946_00630. DR PATRIC; fig|1054213.3.peg.595; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000003292; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000003292}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000003292}. FT DOMAIN 211 383 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 434 AA; 46953 MW; 9607153C1C20B89E CRC64; MLAAVLLPHE RPARLTGTDA GVLAFPDQRS ISRAAEARLA EAVGLAASIG LTIVHSAAFP LRTRRPSTLL GEGQVEAAKL EIEEHQVGVV VVDAALTPVQ QRNLERAWGC KVIDRTGLIL EIFGERARTR EGTLQVELAH LEYQRTRLVR SWTHLERQRG GFGFLGGPGE SQIEIDRRLI GERIVKLKKE LEQVRRTRGL HRAARTRVPF PVVALVGYTN AGKSTLFNAL TGAGVYAQDQ LFATLDPTMR AIKLPSGRTV ILSDTVGFIS DLPTQLIEAF RATLEEVAAA DIILHVRDVA HPDTASQRSD VMEVLEEMAS GPNPTLDENW QGRTIEVLNK ADLLGGIAVV PGTDAAAIAV SALTGEGLDA LRAALDARLA AGMETVEYAL PPADGARIAW LYQHGEVLSR ADGDDSIQLV VRLAPADRAR FEQS // ID GTPB6_HUMAN Reviewed; 516 AA. AC O43824; Q53F77; Q5HYX8; DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot. DT 05-OCT-2010, sequence version 3. DT 30-AUG-2017, entry version 131. DE RecName: Full=Putative GTP-binding protein 6; DE AltName: Full=Pseudoautosomal GTP-binding protein-like; GN Name=GTPBP6; Synonyms=PGPL; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15772651; DOI=10.1038/nature03440; RA Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., RA Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., RA Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., RA Jones M.C., Hurles M.E., Andrews T.D., Scott C.E., Searle S., RA Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., RA Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., RA Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., RA Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., RA Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., RA Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., RA Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., RA Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., RA Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., RA Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., RA Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., RA Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., RA Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., RA Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., RA Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., RA Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., RA Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., RA Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., RA Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., RA Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., RA Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., RA Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., RA Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., RA de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., RA Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., RA Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., RA Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., RA Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., RA McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., RA Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., RA Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., RA Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., RA Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., RA Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., RA Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., RA Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., RA Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., RA Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., RA Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., RA Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., RA Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., RA Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., RA Williams G., Williams L., Williamson A., Williamson H., Wilming L., RA Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., RA Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., RA Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., RA Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., RA Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., RA Gibbs R.A., Beck S., Rogers J., Bentley D.R.; RT "The DNA sequence of the human X chromosome."; RL Nature 434:325-337(2005). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 9-516. RA Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.; RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 100-516. RC TISSUE=Muscle; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 114-516. RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., RA Phelan M., Farmer A.; RT "Cloning of human full-length CDSs in BD Creator(TM) system donor RT vector."; RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases. RN [5] RP PARTIAL NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY. RX PubMed=9466997; DOI=10.1093/hmg/7.3.407; RA Gianfrancesco F., Esposito T., Montanini L., Ciccodicola A., Mumm S., RA Mazzarella R., Rao E., Giglio S., Rappold G., Forabosco A.; RT "A novel pseudoautosomal gene encoding a putative GTP-binding protein RT resides in the vicinity of the Xp/Yp telomere."; RL Hum. Mol. Genet. 7:407-414(1998). CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000255|PROSITE-ProRule:PRU01042}; CC -!- TISSUE SPECIFICITY: Ubiquitously expressed. CC {ECO:0000269|PubMed:9466997}. CC -!- MISCELLANEOUS: The gene coding for this protein is located in the CC pseudoautosomal region 1 (PAR1) of X and Y chromosomes. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000255|PROSITE- CC ProRule:PRU01042}. CC -!- SEQUENCE CAUTION: CC Sequence=AAH14636.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305}; CC Sequence=AAP36024.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305}; CC Sequence=BAD97132.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305}; CC Sequence=CAA74749.2; Type=Miscellaneous discrepancy; Note=Has an upstream in-frame stop codon because of a region of poor sequence quality.; Evidence={ECO:0000305}; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AC126759; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BX000483; CAI41972.1; -; Genomic_DNA. DR EMBL; AK223412; BAD97132.1; ALT_INIT; mRNA. DR EMBL; BC014636; AAH14636.1; ALT_INIT; mRNA. DR EMBL; BT007360; AAP36024.1; ALT_INIT; mRNA. DR EMBL; Y14391; CAA74749.2; ALT_SEQ; mRNA. DR CCDS; CCDS75943.1; -. DR RefSeq; NP_036359.3; NM_012227.3. DR UniGene; Hs.437145; -. DR ProteinModelPortal; O43824; -. DR SMR; O43824; -. DR BioGrid; 113858; 16. DR IntAct; O43824; 2. DR STRING; 9606.ENSP00000316598; -. DR iPTMnet; O43824; -. DR PhosphoSitePlus; O43824; -. DR BioMuta; GTPBP6; -. DR EPD; O43824; -. DR MaxQB; O43824; -. DR PaxDb; O43824; -. DR PeptideAtlas; O43824; -. DR PRIDE; O43824; -. DR DNASU; 8225; -. DR GeneID; 8225; -. DR KEGG; hsa:8225; -. DR CTD; 8225; -. DR GeneCards; GTPBP6; -. DR HGNC; HGNC:30189; GTPBP6. DR HPA; HPA035467; -. DR HPA; HPA055418; -. DR MIM; 300124; gene. DR neXtProt; NX_O43824; -. DR eggNOG; KOG0410; Eukaryota. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR HOVERGEN; HBG052970; -. DR InParanoid; O43824; -. DR PhylomeDB; O43824; -. DR ChiTaRS; GTPBP6; human. DR GeneWiki; GTPBP6; -. DR GenomeRNAi; 8225; -. DR PRO; PR:O43824; -. DR Proteomes; UP000005640; Unplaced. DR CleanEx; HS_GTPBP6; -. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0005525; F:GTP binding; TAS:ProtInc. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0043022; F:ribosome binding; IBA:GO_Central. DR CDD; cd01878; HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 2: Evidence at transcript level; KW Complete proteome; GTP-binding; Magnesium; Metal-binding; KW Nucleotide-binding; Reference proteome. FT CHAIN 1 516 Putative GTP-binding protein 6. FT /FTId=PRO_0000304798. FT DOMAIN 295 459 Hflx-type G. {ECO:0000255|PROSITE- FT ProRule:PRU01042}. FT NP_BIND 301 308 GTP. {ECO:0000255|PROSITE- FT ProRule:PRU01042}. FT NP_BIND 327 331 GTP. {ECO:0000255|PROSITE- FT ProRule:PRU01042}. FT NP_BIND 349 352 GTP. {ECO:0000255|PROSITE- FT ProRule:PRU01042}. FT NP_BIND 418 421 GTP. {ECO:0000255|PROSITE- FT ProRule:PRU01042}. FT NP_BIND 437 439 GTP. {ECO:0000255|PROSITE- FT ProRule:PRU01042}. FT METAL 308 308 Magnesium. {ECO:0000255|PROSITE- FT ProRule:PRU01042}. FT METAL 329 329 Magnesium. {ECO:0000255|PROSITE- FT ProRule:PRU01042}. FT CONFLICT 171 171 V -> I (in Ref. 2; BAD97132). FT {ECO:0000305}. SQ SEQUENCE 516 AA; 56883 MW; AA81CEA655F579C7 CRC64; MWALRAAVRP GLRLSRVGRG RSAPRAAAPS CPARALAAVG RRSPGNLEGP WGGGRGLRAD GGRSRTGDDE EEPEDADENA EEELLRGEPL LPAGTQRVCL VHPDVKWGPG KSQMTRAEWQ VAEATALVHT LDGWSVVQTM VVSTKTPDRK LIFGKGNFEH LTEKIRGSPD VTCVFLNVER MAAPTKKELE AAWGVEVFDR FTVVLHIFRC NARTKEARLQ VALAEMPLHR SNLKRDVAHL YRGVGSRYIM GSGESFMQLQ QRLLREKEAK IRKALDRLRK KRHLLRRQRT RREFPVISVV GYTNCGKTTL IKALTGDAAI QPRDQLFATL DVTAHAGTLP SRMTVLYVDT IGFLSQLPHG LIESFSATLE DVAHSDLILH VRDVSHPEAE LQKCSVLSTL RGLQLPAPLL DSMVEVHNKV DLVPGYSPTE PNVVPVSALR GHGLQELKAE LDAAVLKATG RQILTLRVRL AGAQLSWLYK EATVQEVDVI PEDGAADVRV IISNSAYGKF RKLFPG // ID GTPB6_MOUSE Reviewed; 514 AA. AC Q3U6U5; Q3TX13; Q3UMM2; DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot. DT 11-OCT-2005, sequence version 1. DT 30-AUG-2017, entry version 88. DE RecName: Full=Putative GTP-binding protein 6; GN Name=Gtpbp6; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; TISSUE=Bone marrow, and Lung; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [2] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Brown adipose tissue; RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001; RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R., RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.; RT "A tissue-specific atlas of mouse protein phosphorylation and RT expression."; RL Cell 143:1174-1189(2010). CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000255|PROSITE-ProRule:PRU01042}; CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000255|PROSITE- CC ProRule:PRU01042}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AK144812; BAE26076.1; -; mRNA. DR EMBL; AK152225; BAE31052.1; -; mRNA. DR EMBL; AK152972; BAE31629.1; -; mRNA. DR EMBL; AK159462; BAE35103.1; -; mRNA. DR CCDS; CCDS51604.1; -. DR RefSeq; NP_660129.2; NM_145147.5. DR UniGene; Mm.86267; -. DR ProteinModelPortal; Q3U6U5; -. DR SMR; Q3U6U5; -. DR STRING; 10090.ENSMUSP00000076458; -. DR iPTMnet; Q3U6U5; -. DR PhosphoSitePlus; Q3U6U5; -. DR MaxQB; Q3U6U5; -. DR PaxDb; Q3U6U5; -. DR PeptideAtlas; Q3U6U5; -. DR PRIDE; Q3U6U5; -. DR GeneID; 107999; -. DR KEGG; mmu:107999; -. DR UCSC; uc008ypr.2; mouse. DR CTD; 8225; -. DR MGI; MGI:1306825; Gtpbp6. DR eggNOG; KOG0410; Eukaryota. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR HOVERGEN; HBG052970; -. DR InParanoid; Q3U6U5; -. DR TreeFam; TF315022; -. DR PRO; PR:Q3U6U5; -. DR Proteomes; UP000000589; Unplaced. DR CleanEx; MM_GTPBP6; -. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0043022; F:ribosome binding; IBA:GO_Central. DR CDD; cd01878; HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 1: Evidence at protein level; KW Complete proteome; GTP-binding; Magnesium; Metal-binding; KW Nucleotide-binding; Reference proteome. FT CHAIN 1 514 Putative GTP-binding protein 6. FT /FTId=PRO_0000304799. FT DOMAIN 285 449 Hflx-type G. {ECO:0000255|PROSITE- FT ProRule:PRU01042}. FT METAL 298 298 Magnesium. {ECO:0000255|PROSITE- FT ProRule:PRU01042}. FT METAL 319 319 Magnesium. {ECO:0000255|PROSITE- FT ProRule:PRU01042}. FT CONFLICT 350 350 N -> S (in Ref. 1; BAE26076/BAE35103). FT {ECO:0000305}. FT CONFLICT 501 501 R -> G (in Ref. 1; BAE35103). FT {ECO:0000305}. SQ SEQUENCE 514 AA; 56475 MW; 95774C6439C0B3E6 CRC64; MLFLRAAVLP GFWLPRVRRV QLVRSPAVTL PSPVRTVHAG SRVWGSAWAG GGPVRGGGEE DPREDEEEEE DELLRAPPLL PLDTQRVCVL HPDVKRPAGK KPRSTAEWQV AEAAALVRAL PGWSVASTLV VPSAAPGSRL VFGKGNFQDV TEKIKGCQDI TSVFLNVERM APPTKKELES AWGLRVFDRF TLVLHIFRCN ARTREARMQL ALAEIPLLRS SVNTDSGQQD QQGWGSRYIM GSGESPTELR ARALRDRELR LRRVLERLRD KRRLMRKERV RREFPVVSVV GYTNCGKTTL IQALTGEAAL QPRDQPFATL DVTVHAGLLP SRLRILYVDT IGFLSQLPHN LIHAFSATLE DVAYSDVLVH VTDVSHPDAE LQKATVLSTL RGLHLPPALL ESALEVHSKV DLVPGYTPPC SGALAVSAIS GRGLDELKAA LEASVLRATG RQVLTLCVRL GGPQLGWLYK EAVVQQVQEL PEGDAAHVTV VITQAAYGRF RKLFPIDAPS ALPH // ID H0DIP7_9STAP Unreviewed; 417 AA. AC H0DIP7; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 07-JUN-2017, entry version 33. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:EHM68839.1}; GN ORFNames=SEVCU012_0729 {ECO:0000313|EMBL:EHM68839.1}; OS Staphylococcus pettenkoferi VCU012. OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae; OC Staphylococcus. OX NCBI_TaxID=904314 {ECO:0000313|EMBL:EHM68839.1, ECO:0000313|Proteomes:UP000008944}; RN [1] {ECO:0000313|EMBL:EHM68839.1, ECO:0000313|Proteomes:UP000008944} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=VCU012 {ECO:0000313|EMBL:EHM68839.1, RC ECO:0000313|Proteomes:UP000008944}; RA Jones M., Archer G., Boundy S., Durkin A.S., Kim M., Mishra P., RA Singh I., Peterson S.; RL Submitted (OCT-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EHM68839.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGUA01000080; EHM68839.1; -; Genomic_DNA. DR EnsemblBacteria; EHM68839; EHM68839; SEVCU012_0729. DR PATRIC; fig|904314.5.peg.1522; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000008944; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000008944}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000008944}. FT DOMAIN 212 373 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 417 AA; 47802 MW; 3110649660448F7C CRC64; MKEVYELSRS HTKTTAKPKE KAILIGVNEN SEKQFDFDST MHELNALSKT CQLDVEMSFT QNRENIDHKY YVGKGKLDEI KAYVEHNDID VAVTNDELTT AQSKTLNGNL NIKIIDRTQL ILEIFALRAR SKEGKLQVEL AQLDYLLPRL QGHGRSLSRL GGGIGTRGPG ETKLEMDRRH IRTRMNEIKH QLQTVVDHRE RYRNQREQNK VYQVALVGYT NAGKSSWFNA LTDAETYEQD KLFATLDPKT RQLQINDGFN MIISDTVGFI QKLPTTLIAA FKSTLEEAKG ADLLLHVVDG SHKEYRTQFD TVNRILNDLD MEGIPQAVIF NKKDLCDQAI PSAAEPSVFV SARNEQDIEK VKTLLYEQVQ ETLDYYEEHV DSSDAKRLYY LKQHTLVTEL TFNENTNQYD IKGYAKD // ID H0E2T0_9ACTN Unreviewed; 447 AA. AC H0E2T0; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 07-JUN-2017, entry version 35. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=PAI11_10950 {ECO:0000313|EMBL:EHN12008.1}; OS Patulibacter medicamentivorans. OC Bacteria; Actinobacteria; Thermoleophilia; Solirubrobacterales; OC Patulibacteraceae; Patulibacter. OX NCBI_TaxID=1097667 {ECO:0000313|EMBL:EHN12008.1, ECO:0000313|Proteomes:UP000005143}; RN [1] {ECO:0000313|EMBL:EHN12008.1, ECO:0000313|Proteomes:UP000005143} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=I11 {ECO:0000313|EMBL:EHN12008.1, RC ECO:0000313|Proteomes:UP000005143}; RX PubMed=23212173; DOI=10.1007/s10532-012-9610-5; RA Almeida B., Kjeldal H., Lolas I., Knudsen A.D., Carvalho G., RA Nielsen K.L., Barreto Crespo M.T., Stensballe A., Nielsen J.L.; RT "Quantitative proteomic analysis of ibuprofen-degrading Patulibacter RT sp. strain I11."; RL Biodegradation 24:615-630(2013). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EHN12008.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGUD01000051; EHN12008.1; -; Genomic_DNA. DR RefSeq; WP_007571811.1; NZ_AGUD01000051.1. DR EnsemblBacteria; EHN12008; EHN12008; PAI11_10950. DR PATRIC; fig|1097667.3.peg.1093; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000005143; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000005143}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000005143}. FT DOMAIN 213 387 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 178 205 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 447 AA; 48986 MW; 29B2D1F373AF1A20 CRC64; MTKRQRGQSQ TTHPHDLDQQ RAAADQRALV VGVLPEGDDL VELRELLRTA EVEVVDQMVQ HRDEPHPNTY VGEGKLEEIK ARAAELDATL VVTDDELSPR QERNLEGKLG IPVLDRTALI LDIFAVHAHS AEGKLQVELA QLQYNLARMR GLWSHLDRLG VGGVGTRGPG ETQIETDRRL ARDRITKLRR RLEDVKGTRA VMRAERARSS HVPNVALVGY TNAGKSTLLN ALTGSEVGVQ DRLFHTLDPT TRTLRWNGRT YLLTDTVGFI RKLPHHLVEA FGATLEETVI ADLLLHVVDA SQSDEQITSV MTAVNGVLTE IGALDGGVGV GGGIAPVVVL NKCDLIDDAR REELAVRFPD AVQVAAAAGE GLGQLAGRME REFESTLRPV ELLVPYPAGS TLAELHELAG DLEQEHRADG VLVRARLPRQ LVARYDEFRV HPAGAEA // ID H0HWE5_9RHIZ Unreviewed; 463 AA. AC H0HWE5; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 07-JUN-2017, entry version 33. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=MAXJ12_22526 {ECO:0000313|EMBL:EHK54988.1}; OS Mesorhizobium alhagi CCNWXJ12-2. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Phyllobacteriaceae; Mesorhizobium. OX NCBI_TaxID=1107882 {ECO:0000313|EMBL:EHK54988.1, ECO:0000313|Proteomes:UP000003250}; RN [1] {ECO:0000313|EMBL:EHK54988.1, ECO:0000313|Proteomes:UP000003250} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CCNWXJ12-2 {ECO:0000313|EMBL:EHK54988.1, RC ECO:0000313|Proteomes:UP000003250}; RX PubMed=22328758; DOI=10.1128/JB.06635-11; RA Zhou M., Chen W., Chen H., Wei G.; RT "Draft Genome Sequence of Mesorhizobium alhagi CCNWXJ12-2T, a Novel RT Salt-Resistant Species Isolated from the Desert of Northwestern RT China."; RL J. Bacteriol. 194:1261-1262(2012). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AHAM01000184; EHK54988.1; -; Genomic_DNA. DR RefSeq; WP_008838102.1; NZ_AHAM01000184.1. DR EnsemblBacteria; EHK54988; EHK54988; MAXJ12_22526. DR PATRIC; fig|1107882.3.peg.4398; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000003250; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000003250}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000003250}. FT DOMAIN 231 404 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 190 224 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 463 AA; 50593 MW; D9C2A64EEB36759F CRC64; MAQNGRAGDG ARKGRGGEAN AGRGELTRAV VIVPLLSRSP RTDEDTGRPR LNRSPEARLD EAVGLAQAID LDIVHKAIVT LNDPRPSTLF GSGKVEEIAQ VIKDGHAELL IVDHPLTPVQ QRNLEKATEA KVLDRTGLIL EIFGERARTK EGTLQVDLAH LNYQKGRLVR SWTHLERQRG GAGFLGGPGE TQIESDRRAL QEKITKLKRE LETVRRTRDL HRAKRKKVPF PVVAIVGYTN AGKSTLFNRL TGAGVLAEDM LFATLDPTLR RVRLPHGTPV ILSDTVGFIS DLPTHLIAAF RATLEEVVEA DLIIHLRDIS DPDTAAQAED VERILVDLGV DASDEKRIIE VWNKIDRLDE GNRERLLAEG AGGKASPPVA ISAITGEGID KLAAIIEERL SGELEPVTVT LAADQLGLTD WLYRNGDVVA RTDNEDGSVS ISMKATAAAR EEIENRLRRN NKG // ID H0PXF9_9RHOO Unreviewed; 385 AA. AC H0PXF9; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 30-AUG-2017, entry version 38. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:BAL23151.1}; GN ORFNames=AZKH_0812 {ECO:0000313|EMBL:BAL23151.1}; OS Azoarcus sp. KH32C. OC Bacteria; Proteobacteria; Betaproteobacteria; Rhodocyclales; OC Zoogloeaceae; Azoarcus. OX NCBI_TaxID=748247 {ECO:0000313|EMBL:BAL23151.1, ECO:0000313|Proteomes:UP000007106}; RN [1] {ECO:0000313|EMBL:BAL23151.1, ECO:0000313|Proteomes:UP000007106} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=KH32C {ECO:0000313|EMBL:BAL23151.1, RC ECO:0000313|Proteomes:UP000007106}; RA Nishizawa T., Tago T., Oshima K., Hattori M., Ishii S., Otsuka S., RA Senoo K.; RT "Complete genome sequence of Azoarcus sp. KH32C."; RL Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AP012304; BAL23151.1; -; Genomic_DNA. DR RefSeq; WP_015434459.1; NC_020516.1. DR EnsemblBacteria; BAL23151; BAL23151; AZKH_0812. DR KEGG; aza:AZKH_0812; -. DR PATRIC; fig|748247.4.peg.817; -. DR KO; K03665; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000007106; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000007106}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000007106}. FT DOMAIN 198 364 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 385 AA; 42020 MW; 61E0F52A9AB93812 CRC64; MFERPDSGER AVLVQLDLNQ GALDERLSEL KLLTLSAGAS VEAVVGGRRA RPDPALFAGR GKVQEIAETL RANEADFVIF NHALSPGQQR NLERELKCRV VDRTALILDI FAQRARSHEG KLQVELAQLE HLATRLVRGW THLERQKGGI GLRGPGETQL ETDRRLLGKR VKVLKERLTQ IEKQRRVRRR GREGHSVLSV SLVGYTNAGK STLFNALTKA GAYAADQLFA TLDTTSRRLY VGEGANVVLS DTVGFIRDLP HALVAAFHAT LEETANADLL LHVVDSASED REAQIEAVNG VLGEIGAGDV PYIMVMNKID LTQVEPGVQR DEYGKIVRVF LSARTGEGLG LLRDALAEVA RAATATPEGS DRSAADPTGY DPIQM // ID H0Q695_9RHOO Unreviewed; 437 AA. AC H0Q695; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 30-AUG-2017, entry version 37. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=AZKH_p0625 {ECO:0000313|EMBL:BAL27508.1}; OS Azoarcus sp. KH32C. OG Plasmid pAZKH {ECO:0000313|EMBL:BAL27508.1, OG ECO:0000313|Proteomes:UP000007106}. OC Bacteria; Proteobacteria; Betaproteobacteria; Rhodocyclales; OC Zoogloeaceae; Azoarcus. OX NCBI_TaxID=748247 {ECO:0000313|EMBL:BAL27508.1, ECO:0000313|Proteomes:UP000007106}; RN [1] {ECO:0000313|EMBL:BAL27508.1, ECO:0000313|Proteomes:UP000007106} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=KH32C {ECO:0000313|EMBL:BAL27508.1, RC ECO:0000313|Proteomes:UP000007106}; RA Nishizawa T., Tago T., Oshima K., Hattori M., Ishii S., Otsuka S., RA Senoo K.; RT "Complete genome sequence of Azoarcus sp. KH32C."; RL Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AP012305; BAL27508.1; -; Genomic_DNA. DR RefSeq; WP_015452279.1; NC_020548.1. DR EnsemblBacteria; BAL27508; BAL27508; AZKH_p0625. DR KEGG; aza:AZKH_p0625; -. DR PATRIC; fig|748247.4.peg.5205; -. DR KO; K03665; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000007106; Plasmid pAZKH. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000007106}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Plasmid {ECO:0000313|EMBL:BAL27508.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000007106}. FT DOMAIN 211 381 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 176 203 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 437 AA; 48727 MW; 206C05DE70E82878 CRC64; MQSEVQGKPT YAVVAAVQLP NVSDVEFEAS LTELRELAKT LGLTVVHTFI QKRSGFDTSA YLGTGKRQEI HEFVNGANGT AHEIDMILVD HEISPSQARN LELAVGCEVM DRTMVILEIF HRNARSRAAR AQVEIARLGY MAPRLREAAK LAGPQGRQRS GTGGRGAGES HTELDRRKVR DRIAELQEDI DAMEVERKTQ RARRQGRQSL AGVALVGYTN AGKSTLMRAL TGSEVLVANK LFATLDTTVR VLYPESVPRV LVSDTVGFIK NLPHGLVASF KSTLDEALDA SLLLHVIDAS DPGFERQLHV TDHVLEEIGA DVLPRLRVFN KIDHVGDAEA QAEREAALRA QYPDCVVMSA RRPEDVAKLR QRIVAFFQQD LIAAELFLPW SAQQWRKEIY ANCEVLEERA EDEGAFFHVR GERDTVESLR EQFEQVR // ID H0QI82_ARTGO Unreviewed; 525 AA. AC H0QI82; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 07-JUN-2017, entry version 34. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:GAB12533.1}; GN ORFNames=ARGLB_016_00450 {ECO:0000313|EMBL:GAB12533.1}; OS Arthrobacter globiformis NBRC 12137. OC Bacteria; Actinobacteria; Micrococcales; Micrococcaceae; Arthrobacter. OX NCBI_TaxID=1077972 {ECO:0000313|EMBL:GAB12533.1, ECO:0000313|Proteomes:UP000003828}; RN [1] {ECO:0000313|EMBL:GAB12533.1, ECO:0000313|Proteomes:UP000003828} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NBRC 12137 {ECO:0000313|EMBL:GAB12533.1, RC ECO:0000313|Proteomes:UP000003828}; RA Miyazawa S., Hosoyama A., Tsuchikane K., Katsumata H., Yamazaki S., RA Fujita N.; RT "Whole genome shotgun sequence of Arthrobacter globiformis NBRC RT 12137."; RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:GAB12533.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BAEG01000016; GAB12533.1; -; Genomic_DNA. DR RefSeq; WP_003798745.1; NZ_BAEG01000016.1. DR EnsemblBacteria; GAB12533; GAB12533; ARGLB_016_00450. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000003828; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 2. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000003828}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000003828}. FT DOMAIN 304 469 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 525 AA; 56664 MW; A3E61F4A34FC329A CRC64; MTNQQNSGSE PAAQDMSPEE IQAVIDRILA KDVPARNASA AGGGSADSKG VLGKAQAISQ LAEEHSTFDG DQQDLEERRA LRRTAGLSTE LEDVTEVEYR QLRLERVVLA GLWSEGTLAD AENSLRELAA LAETAGSEVL DGLVQRRAKP DPGTFLGAGK ALELKDVVMS TGADTVVVDA ELAPSQRRGL EDIVKVKVID RTALILDIFA QHAKSREGKA QVELAQLEYL LPRLRGWGES MSRQAGGQVG GAGAGMGSRG PGETKIELDR RRIRTRMAKL RREIAAMKPA RETKRANRRR NEVPSVAIAG YTNAGKSSLL NRLTDAGVLV ENALFATLDP TVRKAETSDG VGYTLADTVG FVRSLPTQLV EAFRSTLEEV ADADLILHVV DVSHPDPEGQ IAAVRSVFAE VDARKVPEII VLNKADAADP FVVERLKQRE PRHVVVSART GEGIAELLKA ISESIPRPNV KMQLLVPYHR GDLISKLHDS DAEILSLDHE EGGTRAVVMV REGLAAELES FSTDD // ID H0QYQ5_9ACTN Unreviewed; 529 AA. AC H0QYQ5; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 07-JUN-2017, entry version 35. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:GAB17956.1}; GN ORFNames=GOEFS_042_00470 {ECO:0000313|EMBL:GAB17956.1}; OS Gordonia effusa NBRC 100432. OC Bacteria; Actinobacteria; Corynebacteriales; Gordoniaceae; Gordonia. OX NCBI_TaxID=1077974 {ECO:0000313|EMBL:GAB17956.1, ECO:0000313|Proteomes:UP000035034}; RN [1] {ECO:0000313|EMBL:GAB17956.1, ECO:0000313|Proteomes:UP000035034} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NBRC 100432 {ECO:0000313|EMBL:GAB17956.1, RC ECO:0000313|Proteomes:UP000035034}; RA Yoshida I., Takarada H., Hosoyama A., Tsuchikane K., Katsumata H., RA Yamazaki S., Fujita N.; RT "Whole genome shotgun sequence of Gordonia effusa NBRC 100432."; RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:GAB17956.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BAEH01000042; GAB17956.1; -; Genomic_DNA. DR RefSeq; WP_007317293.1; NZ_BAEH01000042.1. DR EnsemblBacteria; GAB17956; GAB17956; GOEFS_042_00470. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000035034; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000035034}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000035034}. FT DOMAIN 295 474 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 529 AA; 56869 MW; 45AC24843618AA0C CRC64; MTDTNISDPI IDGDTWPARS APDAGDTWPA RSAPDAGDTW PARSAPDAGD TWPARSANIP TTGDLQLDDR ASLQRVAGLS TELTDVTEVE YRQLRLEKVV LVGVWTHGTQ AQAHAAMAEL AALAETAGSQ VLDALIQRRS KPDSATYIGS GKAGELREVV LATEADTVIC DGELTPAQLT ALEKVVKVKV IDRTALILDI FAQHATSREG KAQVSLAQME YMLPRLRGWG ESMSRQAGGR AGSNGGVGLR GPGETKIETD RRRIRERMAK MRREIRLMKT ARVVKRAARQ RNSVPALTVV GYTNAGKSSL VNAMTGSGVL VQDALFATLD PTTRRAKLDD GRVVVFTDTV GFVRHLPTQL VEAFRSTLEE AADADVLLHV VDGADDYPLD QITAVRQVLK EIVSESSGQP NTGADGAALP PELLVVNKVD AMTELQITQL RAALPDAVFI SARTGEGIPE LFDRVRSALG RNDVELFVSV PFSRGDLVSR IHAEGEVFSA DHDSAGTRMR VRVPAALAGE LRELVVLAQ // ID H0TNT0_9BRAD Unreviewed; 461 AA. AC H0TNT0; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 07-JUN-2017, entry version 34. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=BRAS3843_2590008 {ECO:0000313|EMBL:CCE08118.1}; OS Bradyrhizobium sp. STM 3843. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Bradyrhizobiaceae; Bradyrhizobium. OX NCBI_TaxID=551947 {ECO:0000313|EMBL:CCE08118.1, ECO:0000313|Proteomes:UP000002686}; RN [1] {ECO:0000313|EMBL:CCE08118.1, ECO:0000313|Proteomes:UP000002686} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=STM3843 {ECO:0000313|Proteomes:UP000002686}; RA Mornico D., Miche L., Bena G., Nouwen N., Vermeglio A., Vallenet D., RA Smith A.A.T., Giraud E., Medigue C., Moulin L.; RT "Comparative Genomics of Aeschynomene Symbionts: Insights into the RT Ecological Lifestyle of Nod-Independent Photosynthetic RT Bradyrhizobia."; RL Genes (Basel) 3:35-61(2012). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:CCE08118.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CAFK01000178; CCE08118.1; -; Genomic_DNA. DR RefSeq; WP_008970631.1; NZ_CAFK01000178.1. DR EnsemblBacteria; CCE08118; CCE08118; BRAS3843_2590008. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000002686; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000002686}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000002686}. FT DOMAIN 228 402 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 187 214 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 461 AA; 50868 MW; 4D41ADA9A61BDFC6 CRC64; MEPRDRDRGA DHPKSADVQN TGRVIVIGPY LRARHGAVQP GASDARDFEA RLDEATGLAR AIDLTVAEAL IATIGQIRPA TYLGKGKVDE IAGLIAGQLP GHGIELVVMD CALSPIQQRN LEKAWNTKVL DRTGLILEIF GRRAKTKEGS LQVELAHLNY QRSRLVRSWT HLERQRGGFG FMGGPGETQI EADRRLISER ISRLENELKK VQATRRLHRA GRQRVPYRVV ALVGYTNAGK STLFNRLTRA DVQAADMLFA TLDPTLRAIS LPHGGKAMLS DTVGFISNLP TQLVAAFRAT LEEVLEADVI LHVRDISHED AEAQQQDVEM VLSQLGIDPE ASDNIIEVWN KVDCLDDAHR ENLENIAARR PPERPCLLVS AATGEGVDTL LQAIEDRLAA ARTTLDLSID AADGAGISWL HRNAEVLNKE LHDGRYEMTV RVDPSKRDIV VDRYHAVPRV A // ID H0UL07_9BACT Unreviewed; 373 AA. AC H0UL07; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 07-JUN-2017, entry version 34. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=JonanDRAFT_0994 {ECO:0000313|EMBL:EHM13366.1}; OS Jonquetella anthropi DSM 22815. OC Bacteria; Synergistetes; Synergistia; Synergistales; Synergistaceae; OC Jonquetella. OX NCBI_TaxID=885272 {ECO:0000313|EMBL:EHM13366.1, ECO:0000313|Proteomes:UP000003806}; RN [1] {ECO:0000313|EMBL:EHM13366.1, ECO:0000313|Proteomes:UP000003806} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 22815 {ECO:0000313|EMBL:EHM13366.1, RC ECO:0000313|Proteomes:UP000003806}; RG US DOE Joint Genome Institute (JGI-PGF); RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., RA Tice H., Bruce D., Goodwin L., Pitluck S., Peters L., Mikhailova N., RA Held B., Kyrpides N., Mavromatis K., Ivanova N., Markowitz V., RA Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Gronow S., Wellnitz S., RA Brambilla E., Klenk H.-P., Eisen J.A.; RT "The Noncontiguous Finished genome of Jonquetella anthropi DSM RT 22815."; RL Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CM001376; EHM13366.1; -; Genomic_DNA. DR RefSeq; WP_008523019.1; NZ_CM001376.1. DR EnsemblBacteria; EHM13366; EHM13366; JonanDRAFT_0994. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000003806; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000003806}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000003806}. FT DOMAIN 202 372 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 373 AA; 40572 MW; A6D77C62B796FC48 CRC64; MPPDFKDSPQ RRRALVFGLE LPGSDQLTLE LEELRLLLAN LGVEAVQTVV QKRLQPDPAT CLGSGRAAEL RGAIAGLEAD LAVSNEPLSP RQMHELRALW GCDVWDRPLV ITKIFQGRAS SAEAKLQIDL ARCRYELPHL RGLGEQMSRT GGGIGTRGPG ETEFERHRRK LERRERDLSR QLGRVQAARG GQRKRRARSG MTTVAFVGYT NCGKTTLVAS LSGDRALHGE DKLFATLDTA IRRVRLPSGR LILAGDTVGF IRRLPPELVA SFRATLEEVA EAGVLAVVMD VCDPHPEDTF GVICKILADL GASDRIGVLV LNKIDRVPEG DAAKAVLALS KHGFPVCCTS ALTGRGLDEL LTALDGLTER RGE // ID H0X4L1_OTOGA Unreviewed; 448 AA. AC H0X4L1; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 30-AUG-2017, entry version 27. DE SubName: Full=GTP binding protein 6 (putative) {ECO:0000313|Ensembl:ENSOGAP00000010144}; GN Name=GTPBP6 {ECO:0000313|Ensembl:ENSOGAP00000010144}; OS Otolemur garnettii (Small-eared galago) (Garnett's greater bushbaby). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Strepsirrhini; OC Lorisiformes; Galagidae; Otolemur. OX NCBI_TaxID=30611 {ECO:0000313|Ensembl:ENSOGAP00000010144, ECO:0000313|Proteomes:UP000005225}; RN [1] {ECO:0000313|Ensembl:ENSOGAP00000010144} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RG The Broad Institute Genome Sequencing Platform; RA Di Palma F., Johnson J., Lander E.S., Lindblad-Toh K., Jaffe D.B., RA Gnerre S., MacCallum I., Przybylski D., Ribeiro F.J., Burton J.N., RA Walker B.J., Sharpe T., Hall G.; RT "Version 3 of the genome sequence of Otolemur garnettii (Bushbaby)."; RL Submitted (MAR-2011) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Ensembl:ENSOGAP00000010144} RP IDENTIFICATION. RG Ensembl; RL Submitted (JAN-2012) to UniProtKB. CC -!- CAUTION: The sequence shown here is derived from an Ensembl CC automatic analysis pipeline and should be considered as CC preliminary data. {ECO:0000313|Ensembl:ENSOGAP00000010144}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AAQR03098135; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR STRING; 30611.ENSOGAP00000010144; -. DR Ensembl; ENSOGAT00000011329; ENSOGAP00000010144; ENSOGAG00000011327. DR eggNOG; KOG0410; Eukaryota. DR eggNOG; COG2262; LUCA. DR GeneTree; ENSGT00390000001397; -. DR InParanoid; H0X4L1; -. DR OMA; MDTVGFM; -. DR OrthoDB; EOG091G0852; -. DR TreeFam; TF315022; -. DR Proteomes; UP000005225; Unassembled WGS sequence. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR CDD; cd01878; HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 4: Predicted; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000005225}; KW Reference proteome {ECO:0000313|Proteomes:UP000005225}. FT DOMAIN 228 392 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 190 217 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 448 AA; 49987 MW; D3C8D4FB0C0E3230 CRC64; EEPEDADEEE EEEEELLRRD PLLPAGTQRV FLVHPDVKWG PGKPQMTTAT WQVAEATALV HTLDGWSVVQ TMVMSTKTPT KKLIFGKGNF EQLTETIRGC PEITSVFLNV ERMAAPTKKE LEAAWGLEVF DRFTIVLHIF RCHARTREAR LQVALAEIPL LRSNLRNNIA HQDHQGGGSR YIMGSGESFM QVQQRVLREK EAKIRRALER LRGKRRLLCR QRTRREFPVV SVVGYTNCGK TTLIKALTGD VAVQPRDQLF ATLDITAHAG SLPSHMTVLY MDTIGFLSEL PHGLIESFSA TLEDVAHSDL ILHVRDVSHP ETERQKASVL SSLRSLNLPG PLLDTMVEVH NKVDLVPGYS PTEPHAVAIS ALLGSGLQQL KADLEDAVLR ATGRQLLTLR VHLAGAQLSW LHREATVQQV AVIPEEGVAE VQVIIISKSA YGKFRKLF // ID H0Y2S1_HUMAN Unreviewed; 516 AA. AC H0Y2S1; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 29-OCT-2014, sequence version 2. DT 05-JUL-2017, entry version 46. DE SubName: Full=Putative GTP-binding protein 6 {ECO:0000313|Ensembl:ENSP00000316598}; GN Name=GTPBP6 {ECO:0000313|Ensembl:ENSP00000316598}; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606 {ECO:0000313|Ensembl:ENSP00000316598, ECO:0000313|Proteomes:UP000005640}; RN [1] {ECO:0000313|Proteomes:UP000005640} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15772651; DOI=10.1038/nature03440; RA Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., RA Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., RA Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., RA Jones M.C., Hurles M.E., Andrews T.D., Scott C.E., Searle S., RA Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., RA Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., RA Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., RA Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., RA Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., RA Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., RA Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., RA Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., RA Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., RA Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., RA Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., RA Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., RA Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., RA Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., RA Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., RA Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., RA Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., RA Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., RA Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., RA Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., RA Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., RA Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., RA Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., RA de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., RA Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., RA Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., RA Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., RA Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., RA McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., RA Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., RA Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., RA Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., RA Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., RA Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., RA Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., RA Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., RA Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., RA Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., RA Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., RA Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., RA Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., RA Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., RA Williams G., Williams L., Williamson A., Williamson H., Wilming L., RA Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., RA Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., RA Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., RA Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., RA Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., RA Gibbs R.A., Beck S., Rogers J., Bentley D.R.; RT "The DNA sequence of the human X chromosome."; RL Nature 434:325-337(2005). RN [2] {ECO:0000313|Ensembl:ENSP00000316598} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15815621; DOI=10.1038/nature03466; RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., RA Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., RA Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., RA Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J., RA Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., RA Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., RA Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., RA Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., RA Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., RA Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., RA Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., RA Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., RA Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., RA Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., RA Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., RA Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., RA Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., RA Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., RA McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., RA Waterston R.H., Wilson R.K.; RT "Generation and annotation of the DNA sequences of human chromosomes 2 RT and 4."; RL Nature 434:724-731(2005). RN [3] {ECO:0000313|Ensembl:ENSP00000316598} RP IDENTIFICATION. RG Ensembl; RL Submitted (JAN-2012) to UniProtKB. CC -!- CAUTION: The sequence shown here is derived from an Ensembl CC automatic analysis pipeline and should be considered as CC preliminary data. {ECO:0000313|Ensembl:ENSP00000316598}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BX000483; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; FO681518; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR RefSeq; NP_036359.3; NM_012227.3. DR UniGene; Hs.437145; -. DR ProteinModelPortal; H0Y2S1; -. DR PaxDb; H0Y2S1; -. DR PeptideAtlas; H0Y2S1; -. DR PRIDE; H0Y2S1; -. DR Ensembl; ENST00000326153; ENSP00000316598; ENSG00000178605. DR GeneID; 8225; -. DR KEGG; hsa:8225; -. DR UCSC; uc033doq.2; human. DR CTD; 8225; -. DR HGNC; HGNC:30189; GTPBP6. DR OpenTargets; ENSG00000178605; -. DR eggNOG; KOG0410; Eukaryota. DR eggNOG; COG2262; LUCA. DR GeneTree; ENSGT00390000001397; -. DR OMA; MDTVGFM; -. DR OrthoDB; EOG091G0852; -. DR TreeFam; TF315022; -. DR ChiTaRS; GTPBP6; human. DR GenomeRNAi; 8225; -. DR Proteomes; UP000005640; Chromosome X. DR Bgee; ENSG00000178605; -. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR CDD; cd01878; HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 1: Evidence at protein level; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000005640}; KW Proteomics identification {ECO:0000213|EPD:H0Y2S1, KW ECO:0000213|MaxQB:H0Y2S1, ECO:0000213|PeptideAtlas:H0Y2S1}; KW Reference proteome {ECO:0000313|Proteomes:UP000005640}. FT DOMAIN 295 459 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 257 288 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 516 AA; 56897 MW; 0BCF19A88FB5A984 CRC64; MWALRAAVRP GLRLSRVGRG RSAPRAAAPS CPARALAAVG RRSPGNLEGP WGGGRGLRAD GGRSRTGDDE EEPEDADENA EEELLRGEPL LPAGTQRVCL VHPDVKWGPG KSQMTRAEWQ VAEATALVHT LDGWSVVQTM VVSTKTPDRK LIFGKGNFEH LTEKIRGSPD ITCVFLNVER MAAPTKKELE AAWGVEVFDR FTVVLHIFRC NARTKEARLQ VALAEMPLHR SNLKRDVAHL YRGVGSRYIM GSGESFMQLQ QRLLREKEAK IRKALDRLRK KRHLLRRQRT RREFPVISVV GYTNCGKTTL IKALTGDAAI QPRDQLFATL DVTAHAGTLP SRMTVLYVDT IGFLSQLPHG LIESFSATLE DVAHSDLILH VRDVSHPEAE LQKCSVLSTL RGLQLPAPLL DSMVEVHNKV DLVPGYSPTE PNVVPVSALR GHGLQELKAE LDAAVLKATG RQILTLRVRL AGAQLSWLYK EATVQEVDVI PEDGAADVRV IISNSAYGKF RKLFPG // ID H0ZK59_TAEGU Unreviewed; 450 AA. AC H0ZK59; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 10-MAY-2017, entry version 29. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSTGUP00000010979}; GN Name=GTPBP6 {ECO:0000313|Ensembl:ENSTGUP00000010979}; OS Taeniopygia guttata (Zebra finch) (Poephila guttata). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda; OC Coelurosauria; Aves; Neognathae; Passeriformes; Passeroidea; OC Estrildidae; Estrildinae; Taeniopygia. OX NCBI_TaxID=59729 {ECO:0000313|Ensembl:ENSTGUP00000010979, ECO:0000313|Proteomes:UP000007754}; RN [1] {ECO:0000313|Ensembl:ENSTGUP00000010979, ECO:0000313|Proteomes:UP000007754} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=20360741; DOI=10.1038/nature08819; RA Warren W.C., Clayton D.F., Ellegren H., Arnold A.P., Hillier L.W., RA Kunstner A., Searle S., White S., Vilella A.J., Fairley S., Heger A., RA Kong L., Ponting C.P., Jarvis E.D., Mello C.V., Minx P., Lovell P., RA Velho T.A., Ferris M., Balakrishnan C.N., Sinha S., Blatti C., RA London S.E., Li Y., Lin Y.C., George J., Sweedler J., Southey B., RA Gunaratne P., Watson M., Nam K., Backstrom N., Smeds L., Nabholz B., RA Itoh Y., Whitney O., Pfenning A.R., Howard J., Volker M., RA Skinner B.M., Griffin D.K., Ye L., McLaren W.M., Flicek P., RA Quesada V., Velasco G., Lopez-Otin C., Puente X.S., Olender T., RA Lancet D., Smit A.F., Hubley R., Konkel M.K., Walker J.A., RA Batzer M.A., Gu W., Pollock D.D., Chen L., Cheng Z., Eichler E.E., RA Stapley J., Slate J., Ekblom R., Birkhead T., Burke T., Burt D., RA Scharff C., Adam I., Richard H., Sultan M., Soldatov A., Lehrach H., RA Edwards S.V., Yang S.P., Li X., Graves T., Fulton L., Nelson J., RA Chinwalla A., Hou S., Mardis E.R., Wilson R.K.; RT "The genome of a songbird."; RL Nature 464:757-762(2010). RN [2] {ECO:0000313|Ensembl:ENSTGUP00000010979} RP IDENTIFICATION. RG Ensembl; RL Submitted (JAN-2012) to UniProtKB. CC -!- CAUTION: The sequence shown here is derived from an Ensembl CC automatic analysis pipeline and should be considered as CC preliminary data. {ECO:0000313|Ensembl:ENSTGUP00000010979}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABQF01013079; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR STRING; 59729.ENSTGUP00000010979; -. DR Ensembl; ENSTGUT00000011094; ENSTGUP00000010979; ENSTGUG00000010642. DR eggNOG; KOG0410; Eukaryota. DR eggNOG; COG2262; LUCA. DR GeneTree; ENSGT00390000001397; -. DR InParanoid; H0ZK59; -. DR OMA; MDTVGFM; -. DR OrthoDB; EOG091G0852; -. DR TreeFam; TF315022; -. DR Proteomes; UP000007754; Chromosome 1. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR CDD; cd01878; HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 4: Predicted; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000007754}; KW Reference proteome {ECO:0000313|Proteomes:UP000007754}. FT DOMAIN 223 387 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 185 219 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 450 AA; 50266 MW; 7EB172AD8FEA6B9E CRC64; EDDEAALEAL LGPSPLAPGP SAQRVAIVNP AVKWGPQKSP LTTAELQIAE AVALVDTLQN WTVLDKIIIP TKNPNKKFVF GKGNFQVLTE KIKKLPHVTA VFLNVERISS LTKKELEGAW GVPVFDRYTV VLHIFRCNAR TKEAKLQIAL AEIPLLRSNL KNELSQRDQQ RGGSRYIMGS GETFLETQNR VLKERELKIR NALEKLRRKR ALLRAQRRKC EFPMVSVMGY TNSGKTTLIK ALTGEAGLQP RDQLFATLDI TAHAGYLPSH MAVIYVDTIG FLTDLPHNLV ESFSATLEEV AYSDLIVHVR DITHPETILQ KATVLSVLRN LNLPSHLLDS MVEVHNKVDL TERYKPTEEN ALAVSALHGY GLEELKQEIE KKILTATGKK ILTVNINLEG PQLSWLYKEA TVQEVEVMPE DGKARVKVII GSSAFGRYKN LFPNSEIFIS // ID H1BIY2_9FIRM Unreviewed; 414 AA. AC H1BIY2; DT 21-MAR-2012, integrated into UniProtKB/TrEMBL. DT 21-MAR-2012, sequence version 1. DT 07-JUN-2017, entry version 33. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=HMPREF0984_00339 {ECO:0000313|EMBL:EHO86099.1}; OS Eubacterium sp. 3_1_31. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Eubacteriaceae; OC Eubacterium. OX NCBI_TaxID=457402 {ECO:0000313|EMBL:EHO86099.1, ECO:0000313|Proteomes:UP000004469}; RN [1] {ECO:0000313|EMBL:EHO86099.1, ECO:0000313|Proteomes:UP000004469} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=3_1_31 {ECO:0000313|EMBL:EHO86099.1, RC ECO:0000313|Proteomes:UP000004469}; RG The Broad Institute Genome Sequencing Platform; RA Earl A., Ward D., Feldgarden M., Gevers D., Daigneault M., Strauss J., RA Allen-Vercoe E., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., RA Haas B., Abouelleil A., Alvarado L., Arachchi H.M., Berlin A., RA Chapman S.B., Gearin G., Goldberg J., Griggs A., Gujja S., Hansen M., RA Heiman D., Howarth C., Larimer J., Lui A., MacDonald P.J.P., RA McCowen C., Montmayeur A., Murphy C., Neiman D., Pearson M., RA Priest M., Roberts A., Saif S., Shea T., Sisk P., Stolte C., Sykes S., RA Wortman J., Nusbaum C., Birren B.; RT "The Genome Sequence of Eubacterium sp. 3_1_31."; RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EHO86099.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACTL01000005; EHO86099.1; -; Genomic_DNA. DR RefSeq; WP_008687342.1; NZ_JH594448.1. DR EnsemblBacteria; EHO86099; EHO86099; HMPREF0984_00339. DR PATRIC; fig|457402.3.peg.337; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000004469; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000004469}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000004469}. FT DOMAIN 189 357 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 148 182 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 414 AA; 47442 MW; 1BBBBB76F1496543 CRC64; MEDIIVVFAD IDTPQEENEE FIELIKACDM NIVTCFKQPL KAINFRTFIG KGKCLEIQTY LTSTKVDTII FNQELSPLQI RNLEEIFQIP VLDRTDLILA IFEKRAVTPV ARLQIESAQL KKLLPRLIGA NTQLGRQSAS GKNKGAGEKQ LELDRRRIKA RIHEVDRELK KVEAQRHTQR RARQRSRLPL VALVGYTNAG KSTIMNQLLR CSAHKEEKQV VEKDMLFATL DTSIRCIAQP HGHSFLLSDT VGFVNRLPHE LIEAFHSTLE EVKYADMLLQ VVDASDEEKA KHMAVTMETL REIGAGDLPM LTVFNKCDKT EYPYPHSKGH ELYISAKAKN NMDALLSALN KQLFAQEHHV KLQLPYEQTA IYAALMKQAC ILEREDQEEG MYLDALLNEE LYQKYQQYII QLYA // ID H1DAV4_9FUSO Unreviewed; 545 AA. AC H1DAV4; DT 21-MAR-2012, integrated into UniProtKB/TrEMBL. DT 21-MAR-2012, sequence version 1. DT 07-JUN-2017, entry version 33. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=HMPREF9466_02587 {ECO:0000313|EMBL:EHO17751.1}; OS Fusobacterium necrophorum subsp. funduliforme 1_1_36S. OC Bacteria; Fusobacteria; Fusobacteriales; Fusobacteriaceae; OC Fusobacterium. OX NCBI_TaxID=742814 {ECO:0000313|EMBL:EHO17751.1, ECO:0000313|Proteomes:UP000003092}; RN [1] {ECO:0000313|EMBL:EHO17751.1, ECO:0000313|Proteomes:UP000003092} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=1_1_36S {ECO:0000313|EMBL:EHO17751.1, RC ECO:0000313|Proteomes:UP000003092}; RG The Broad Institute Genome Sequencing Platform; RA Earl A., Ward D., Feldgarden M., Gevers D., Strauss J., Ambrose C., RA Allen-Vercoe E., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., RA Haas B., Abouelleil A., Alvarado L., Arachchi H.M., Berlin A., RA Brown A., Chapman S.B., Chen Z., Dunbar C., Freedman E., Gearin G., RA Goldberg J., Griggs A., Gujja S., Heiman D., Howarth C., Larson L., RA Lui A., MacDonald P.J.P., Montmayeur A., Murphy C., Neiman D., RA Pearson M., Priest M., Roberts A., Saif S., Shea T., Shenoy N., RA Sisk P., Stolte C., Sykes S., Wortman J., Nusbaum C., Birren B.; RT "The Genome Sequence of Fusobacterium necrophorum 1_1_36S."; RL Submitted (OCT-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EHO17751.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADLZ01000025; EHO17751.1; -; Genomic_DNA. DR EnsemblBacteria; EHO17751; EHO17751; HMPREF9466_02587. DR PATRIC; fig|742814.3.peg.2735; -. DR Proteomes; UP000003092; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000003092}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000003092}. FT DOMAIN 364 540 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 323 357 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 545 AA; 61415 MW; B66310C79CCDF18D CRC64; MIYGNIEGIK DFTLQQLEKL YEIKLNKGQL ISEEIAMFLS DISTKLNKEI NLCIDRNGNI TEISIGDSST VTLPFIPVYE KKLSGKRIVH THPNGNPKLS SVDISALLKL KLDAILAIGC TEETMTGAGL ALCCLEGESL HYEEHLYSSI QELEAFPFLE TVQKVETDLR RRNIVEDDKE YAILVGIDSK ASLEELEELA HACNIEVLGQ FFQNRSKADK VLFLGAGKAK ELSLFRQIKR ANLIIADEEL SGLQVKNLEE VTGCKVIDRT TLILEIFARR ARSREAKIQV ELAQLKYRSN RLIGYGVTMS RLGGGVGSKG PGEKKLEIDR RRIRENISFL KKELENIKKT RSLQREKREH SNIPKLSLVG YTNVGKSTLR NLLAANYTPN SHGKEGVFAE NMLFATLDTT TRTILLDDNT LLSLTDTVGF IRKLPHDLIE AFKSTLEEVI FSDLILHVVD ASSEEALSQM EAVHQVLSEL NCQDKKNILV LNKCDMATPE QIQIIREQYP DITAVEISAK EHKNIELLLE EIKKNYRKIQ KHAVI // ID H1FZX9_9GAMM Unreviewed; 427 AA. AC H1FZX9; DT 21-MAR-2012, integrated into UniProtKB/TrEMBL. DT 21-MAR-2012, sequence version 1. DT 30-AUG-2017, entry version 33. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=ECTPHS_00405 {ECO:0000313|EMBL:EHQ51116.1}; OS Ectothiorhodospira sp. PHS-1. OC Bacteria; Proteobacteria; Gammaproteobacteria; Chromatiales; OC Ectothiorhodospiraceae; Ectothiorhodospira. OX NCBI_TaxID=519989 {ECO:0000313|EMBL:EHQ51116.1, ECO:0000313|Proteomes:UP000005314}; RN [1] {ECO:0000313|EMBL:EHQ51116.1, ECO:0000313|Proteomes:UP000005314} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=PHS-1 {ECO:0000313|EMBL:EHQ51116.1, RC ECO:0000313|Proteomes:UP000005314}; RA Saltikov C.W., Zargar K., Conrad A., Bernick D., Lowe T.M., Stolc V., RA Hoeft S., Oremland R.S., Stolz J.; RT "ArxA, a new clade of arsenite oxidase within the DMSO family of RT molybdenum oxidoreductases."; RL Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EHQ51116.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGBG01000001; EHQ51116.1; -; Genomic_DNA. DR RefSeq; WP_008930683.1; NZ_AGBG01000001.1. DR EnsemblBacteria; EHQ51116; EHQ51116; ECTPHS_00405. DR PATRIC; fig|519989.5.peg.83; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000005314; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000005314}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000005314}. FT DOMAIN 198 365 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 164 191 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 427 AA; 47649 MW; 361605C9C475EE58 CRC64; MFERPRSGER AILVHVDLPA QDGDDDCSEF MELARSAGAD PLALATGTRK APDPRYFIGS GKAEEVRDLV AAHGAELVIF DHALSPSQER NLERLFQCRV LDRSGLILDI FAQRARSHEG KLQVELAQLR HMSTRLVRGW THLERQKGGI GLRGPGETQL ETDRRLLGVR IKQIQKRLEK VEQQREQGRQ SRRRAEIPTV SLVGYTNAGK STLFNRLTQA GVYAADQLFA TLDPTLRRVD LPSQQRVILA DTVGFVRHLP HDLVAAFRAT LTETREAALL LHVVDAHAAE RDIYLRQVDE VLEEIGARDV PQVLVFNKID LIPGAEPRIE PGTVGTPTRA WVSAQTGAGV DDLLQWLGDY FAESIVQGWL ALPPQAGRER AGLYALEAVE AEEVSETGEL RLKVRLPRRR LEELFRGGGF TPKLMDD // ID H1HMK3_9BACT Unreviewed; 415 AA. AC H1HMK3; DT 21-MAR-2012, integrated into UniProtKB/TrEMBL. DT 21-MAR-2012, sequence version 1. DT 07-JUN-2017, entry version 32. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=HMPREF9944_01397 {ECO:0000313|EMBL:EHO70190.1}; OS Prevotella maculosa OT 289. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Prevotellaceae; OC Prevotella. OX NCBI_TaxID=999422 {ECO:0000313|EMBL:EHO70190.1, ECO:0000313|Proteomes:UP000003167}; RN [1] {ECO:0000313|EMBL:EHO70190.1, ECO:0000313|Proteomes:UP000003167} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=OT 289 {ECO:0000313|EMBL:EHO70190.1, RC ECO:0000313|Proteomes:UP000003167}; RG The Broad Institute Genome Sequencing Platform; RA Earl A., Ward D., Feldgarden M., Gevers D., Izard J., Blanton J.M., RA Mathney J., Tanner A.C., Dewhirst F.E., Young S.K., Zeng Q., RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L., RA Arachchi H.M., Berlin A., Chapman S.B., Gearin G., Goldberg J., RA Griggs A., Gujja S., Hansen M., Heiman D., Howarth C., Larimer J., RA Lui A., MacDonald P.J.P., McCowen C., Montmayeur A., Murphy C., RA Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T., RA Sisk P., Stolte C., Sykes S., Wortman J., Nusbaum C., Birren B.; RT "The Genome Sequence of Prevotella maculosa OT 289."; RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EHO70190.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGEK01000027; EHO70190.1; -; Genomic_DNA. DR RefSeq; WP_008565358.1; NZ_JH594503.1. DR EnsemblBacteria; EHO70190; EHO70190; HMPREF9944_01397. DR PATRIC; fig|999422.3.peg.1451; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000003167; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000003167}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000003167}. FT DOMAIN 216 400 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 415 AA; 47488 MW; 745719B09067BCB3 CRC64; MKEFVISEVK AETAVLVGLI TDGQNEAKTK EYLDELEFLA DTAGAVTVRR FTQKVNGPSA VTYVGKGKLE EIKQYIEDCA ENEEPIGMVI FDDELSAKQI RNIENELKVK ILDRTSLILD IFAMRAQTAN AKTQVELAQY RYMLPRLQRL WTHLERQGGG SGSGGGKGSV GLRGPGETQL EMDRRIILQR ITLLKQRLLE IDKQKTTQRK NRGRLIRVSL VGYTNVGKST IMNLLSKSEV FAENKLFATL DTTVRKVVIE NLPFLLADTV GFIRKLPTDL VDSFKSTLDE VREADLLLHV VDLSHPDFEE QIQVVERTLA DLGCNEKPSM IVFNKIDNYR WTEKDEDDLT PETRENITLE DLKKTWMARL DESCMFISAK EKLNVEAFRE TLYKKVRELH VQKYPYNDFL YPEVE // ID H1HS84_9FIRM Unreviewed; 424 AA. AC H1HS84; DT 21-MAR-2012, integrated into UniProtKB/TrEMBL. DT 21-MAR-2012, sequence version 1. DT 07-JUN-2017, entry version 35. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=HMPREF9623_00566 {ECO:0000313|EMBL:EHO17712.1}; OS Stomatobaculum longum. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Lachnospiraceae; OC Stomatobaculum. OX NCBI_TaxID=796942 {ECO:0000313|EMBL:EHO17712.1, ECO:0000313|Proteomes:UP000018466}; RN [1] {ECO:0000313|EMBL:EHO17712.1, ECO:0000313|Proteomes:UP000018466} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ACC2 {ECO:0000313|EMBL:EHO17712.1, RC ECO:0000313|Proteomes:UP000018466}; RG The Broad Institute Genome Sequencing Platform; RA Earl A., Ward D., Feldgarden M., Gevers D., Sizova M., Hazen A., RA Epstein S., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B., RA Abouelleil A., Alvarado L., Arachchi H.M., Berlin A., Brown A., RA Chapman S.B., Chen Z., Dunbar C., Freedman E., Gearin G., Goldberg J., RA Griggs A., Gujja S., Heiman D., Howarth C., Larson L., Lui A., RA MacDonald P.J.P., Montmayeur A., Murphy C., Neiman D., Pearson M., RA Priest M., Roberts A., Saif S., Shea T., Shenoy N., Sisk P., RA Stolte C., Sykes S., Wortman J., Nusbaum C., Birren B.; RT "The Genome Sequence of Lachnospiraceae bacterium ACC2."; RL Submitted (OCT-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EHO17712.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGEL01000004; EHO17712.1; -; Genomic_DNA. DR RefSeq; WP_009532399.1; NZ_JH590861.1. DR EnsemblBacteria; EHO17712; EHO17712; HMPREF9623_00566. DR PATRIC; fig|796942.3.peg.568; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000018466; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000018466}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000018466}. FT DOMAIN 202 367 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 424 AA; 46620 MW; 27C6DFCEB30056A2 CRC64; MAELIVTEEA KERVVLIGIQ QRERDGSEES LTELGELLKT AGAEPVGRLL QPREAPDSGT YFGKGKVEEL RELLLSLEAD AVAADDELSP AQMKNLSEAL GVKVMDRTMI ILDIFAQHAV TAEGKLQVEL AQLHYTQAHL LGMHSSLSRL GGGVGTRGPG EQKLELDRRA IRARISFLRE KLGELKRHRE VSRAQREKSG SYIVALVGYT NAGKSTLLNR LTDAGILAEN KLFATLDPTT RKLSLPGGEE VLVTDTVGFI RKLPHQLIEA FHSTLEEARY ADLILHVVDA SSPEADTQMA VVYETLRELK ALEDHSIIAV YNKTDLPGTE TLPKDIHAAA SVRISAATGE GIAALKELIS AEKKKSRRAF EALFPYAAAG RIQSIRRQGK LLTERYEPEG IYVRAEVPAA LYEQLMQEQQ SQSN // ID H1LFL9_9LACO Unreviewed; 425 AA. AC H1LFL9; DT 21-MAR-2012, integrated into UniProtKB/TrEMBL. DT 21-MAR-2012, sequence version 1. DT 07-JUN-2017, entry version 35. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=HMPREF9104_01395 {ECO:0000313|EMBL:EHO51688.1}; OS Lactobacillus kisonensis F0435. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; OC Lactobacillus. OX NCBI_TaxID=797516 {ECO:0000313|EMBL:EHO51688.1, ECO:0000313|Proteomes:UP000005025}; RN [1] {ECO:0000313|EMBL:EHO51688.1, ECO:0000313|Proteomes:UP000005025} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=F0435 {ECO:0000313|EMBL:EHO51688.1, RC ECO:0000313|Proteomes:UP000005025}; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Hou S., Chen J., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Zhang X., Suruliraj S., Warren W., Chinwalla A., RA Mardis E.R., Wilson R.K.; RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EHO51688.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGRJ01000132; EHO51688.1; -; Genomic_DNA. DR RefSeq; WP_008856570.1; NZ_JH591035.1. DR EnsemblBacteria; EHO51688; EHO51688; HMPREF9104_01395. DR PATRIC; fig|797516.3.peg.1246; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000005025; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000005025}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}. FT DOMAIN 204 372 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 425 AA; 47145 MW; D30B0B23EAB1061D CRC64; MDVTDALTPV VTIGLNRNSS SFDYSMTELN NLVEANNMTV AETLVQKLDK PDPATYFGKG KIEELKQVVI DDGVATIVAN DELSPSQIRN IEKATNARII DRTGLILEIF ANRAQSREAK LQVELAKLKY QLPRLHTSAS QRLDQQTGTA SGAGGATNRG AGESQYELNR RTLEKRITHV NQELKEASKA DQTKRKQRDQ SDIPTVALVG YTNAGKSTVM NGLIKLLGED EDKQVLVKNM LFATLDTSIR RLTLPDQKTF LLSDTVGFVS QLPHQLVQAF KSTLSEAANA DLLIQVVDGS DPHRDLMMKT TEDTLNEIGV TNMPMIVALN KADKQDIAYP TREGDNLIMS AMDDASLTTL IDMIKEKVFK NYQTISLLIP FSKGEVVSYL NDNTNILKTE YKDDGTLITS ELNETDAKRL EKYRV // ID H1Q3K9_9BACT Unreviewed; 415 AA. AC H1Q3K9; DT 21-MAR-2012, integrated into UniProtKB/TrEMBL. DT 21-MAR-2012, sequence version 1. DT 07-JUN-2017, entry version 35. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=HMPREF9140_01497 {ECO:0000313|EMBL:EHO68715.1}; OS Prevotella micans F0438. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Prevotellaceae; OC Prevotella. OX NCBI_TaxID=883158 {ECO:0000313|EMBL:EHO68715.1, ECO:0000313|Proteomes:UP000016023}; RN [1] {ECO:0000313|EMBL:EHO68715.1, ECO:0000313|Proteomes:UP000016023} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=F0438 {ECO:0000313|EMBL:EHO68715.1, RC ECO:0000313|Proteomes:UP000016023}; RG The Broad Institute Genome Sequencing Platform; RA Earl A., Ward D., Feldgarden M., Gevers D., Izard J., Baranova O.V., RA Blanton J.M., Wade W.G., Dewhirst F.E., Young S.K., Zeng Q., RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L., RA Arachchi H.M., Berlin A., Chapman S.B., Gearin G., Goldberg J., RA Griggs A., Gujja S., Hansen M., Heiman D., Howarth C., Larimer J., RA Lui A., MacDonald P.J.P., McCowen C., Montmayeur A., Murphy C., RA Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T., RA Sisk P., Stolte C., Sykes S., Wortman J., Nusbaum C., Birren B.; RT "The Genome Sequence of Prevotella micans F0438."; RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EHO68715.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGWK01000041; EHO68715.1; -; Genomic_DNA. DR RefSeq; WP_006952973.1; NZ_JH594522.1. DR EnsemblBacteria; EHO68715; EHO68715; HMPREF9140_01497. DR PATRIC; fig|883158.3.peg.1494; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000016023; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000016023}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000016023}. FT DOMAIN 216 400 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 415 AA; 47486 MW; 389512469FFFD6F2 CRC64; MKEFVISEVK AETAVLVGLI TQEQNEAKTK EYLDELEFLA DTAGAVTVKR FTQRVGGPSA VTYVGKGKLE EIKNFIKLKE DEEEPIGMVI FDDELSAKQL RNIENELGIK ILDRTSLILD IFAMRAQTAN AKTQVELAQY RYMLPRLQRL WTHLERQGGG SGSGGGKGSV GLRGPGETQL EMDRRIILQR MSLLKQRLVE IDKQKITQRK NRGRLIRVAL VGYTNVGKST IMNLLAKSEV FAENKLFATL DTTVRKVVVE NLPFLLADTV GFIRKLPTDL VDSFKSTLDE VREADLLLHI VDISHPDFEE QIQVVNQTLT DLDSSEKPMM IVFNKIDNYH WLEKEPDDLT PPTKENTSLN ELKKTWMARE ADNCLFISAK QRENIEEFRS TLYKKVRELH VQKYPYNDFL YDIEQ // ID H1S2X4_9BURK Unreviewed; 419 AA. AC H1S2X4; DT 21-MAR-2012, integrated into UniProtKB/TrEMBL. DT 21-MAR-2012, sequence version 1. DT 07-JUN-2017, entry version 31. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=OR16_10399 {ECO:0000313|EMBL:EHP43189.1}; OS Cupriavidus basilensis OR16. OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Cupriavidus. OX NCBI_TaxID=1127483 {ECO:0000313|EMBL:EHP43189.1, ECO:0000313|Proteomes:UP000005808}; RN [1] {ECO:0000313|EMBL:EHP43189.1, ECO:0000313|Proteomes:UP000005808} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=OR16 {ECO:0000313|EMBL:EHP43189.1, RC ECO:0000313|Proteomes:UP000005808}; RX PubMed=22461549; DOI=10.1128/JB.06752-11; RA Cserhati M., Kriszt B., Szoboszlay S., Toth A., Szabo I., Tancsics A., RA Nagy I., Horvath B., Nagy I., Kukolya J.; RT "De Novo Genome Project of Cupriavidus basilensis OR16."; RL J. Bacteriol. 194:2109-2110(2012). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EHP43189.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AHJE01000022; EHP43189.1; -; Genomic_DNA. DR RefSeq; WP_006157759.1; NZ_AHJE01000022.1. DR EnsemblBacteria; EHP43189; EHP43189; OR16_10399. DR PATRIC; fig|1127483.3.peg.2082; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000005808; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000005808}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000005808}. FT DOMAIN 202 372 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 161 195 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 419 AA; 46428 MW; 2FBB93100F7FBD41 CRC64; MQSRATSNSE SSRAILVGVD FGKHDFQESL SELALLTSTA GSTPVHTLTG RRSRPDPALF IGSGKAEELK EAADALDADV VVFNHSLSPA QQRNLERFLQ RHVIDRTGLI LDIFGQRAQS HVGKVQVELA QVQYQASRLV RAWSHLERQK GGIGMRGGPG ERQLELDRRL LDERAKRLKA DLTRLQRQHS TQRRARARND TLSISLVGYT NAGKSTLFNA LTKARAYAAD QLFATLDTTS RRLYLEGVGN VVLSDTVGFI RDLPTQLVAA FRATLEETVH ADLLLHVVDA SSPVRHEQVE QVNRVLAEIN ADDIPQIVVM NKIDASPELL EQGPRVERNE QGVPTRVFVS ARDGIGLDAL REALVEVARW LAERPPERPP LDPRLAGAQP YQDEDLDSDL DDDFDGDATR VDPEEPDTQ // ID H1X4S1_WEICO Unreviewed; 427 AA. AC H1X4S1; DT 21-MAR-2012, integrated into UniProtKB/TrEMBL. DT 21-MAR-2012, sequence version 1. DT 10-MAY-2017, entry version 34. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:CCF29574.1}; GN ORFNames=WEISSC39_00205 {ECO:0000313|EMBL:CCF29574.1}; OS Weissella confusa LBAE C39-2. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Leuconostocaceae; OC Weissella. OX NCBI_TaxID=1127131 {ECO:0000313|EMBL:CCF29574.1, ECO:0000313|Proteomes:UP000004839}; RN [1] {ECO:0000313|EMBL:CCF29574.1, ECO:0000313|Proteomes:UP000004839} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=LBAE C39-2 {ECO:0000313|EMBL:CCF29574.1, RC ECO:0000313|Proteomes:UP000004839}; RA Amari M., Laguerre S., Gabriel V., Moulis C., Loux V., Klopp C., RA Robert H., Gabriel B., Vuillemin M., Morel S., Remaud-Simeon M., RA Fontagne-Faucher C.; RT "Genome sequence of Weissella confusa LBAE C39-2 isolated from a wheat RT sourdough."; RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:CCF29574.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CAGH01000001; CCF29574.1; -; Genomic_DNA. DR EnsemblBacteria; CCF29574; CCF29574; WEISSC39_00205. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000004839; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000004839}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}. FT DOMAIN 204 373 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 427 AA; 47472 MW; 66BA607BFE818ED1 CRC64; MIENDLHPIR KVVLAGLDKQ NAEFDYEMIE LANLAEANYM EVVGTVTQKL ERPNAATYFG KGKVEELKEA VEYYEADMVV TNDELSPSQI RNLESGTGAG IMDRTALILD IFASRAKTRV AKLQVAIAQL QYQLPRLRTS MNVRLDQQTG GGGGSFTSRG AGETKLEMNR RHIEHQISLL RAELKDVEAD DQTRRARRDK QSIKNVALVG YTNAGKSTFM NGLVRQFGEN QEKTVFQADM LFATLETSVR KLNLPDNQSF LLSDTVGFVS KLPHGLVAAF RATLAEAAQA DLLLQVVDYA DENYKEMMST TARTLKEIGV GDIPMITIYN KADKIEGLSF PDREGDTLTL SAQDDASLDL LVNVIREHIF ADHQEVKVLI PFDQGQLVNE LNEEASVHSI DYVEAGTMMD VTLTPVQAAR FAKYIVD // ID H1XUJ1_9BACT Unreviewed; 424 AA. AC H1XUJ1; DT 21-MAR-2012, integrated into UniProtKB/TrEMBL. DT 21-MAR-2012, sequence version 1. DT 07-JUN-2017, entry version 34. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=Calab_0853 {ECO:0000313|EMBL:EHO40490.1}; OS Caldithrix abyssi DSM 13497. OC Bacteria; Calditrichaeota; Calditrichae; Calditrichales; OC Calditrichaceae; Caldithrix. OX NCBI_TaxID=880073 {ECO:0000313|EMBL:EHO40490.1, ECO:0000313|Proteomes:UP000004671}; RN [1] {ECO:0000313|EMBL:EHO40490.1, ECO:0000313|Proteomes:UP000004671} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 13497 {ECO:0000313|EMBL:EHO40490.1, RC ECO:0000313|Proteomes:UP000004671}; RG US DOE Joint Genome Institute (JGI-PGF); RA Lucas S., Han J., Lapidus A., Bruce D., Goodwin L., Pitluck S., RA Peters L., Kyrpides N., Mavromatis K., Ivanova N., Mikhailova N., RA Chertkov O., Detter J.C., Tapia R., Han C., Land M., Hauser L., RA Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Spring S., RA Brambilla E., Klenk H.-P., Eisen J.A.; RT "The permanent draft genome of Caldithrix abyssi DSM 13497."; RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CM001402; EHO40490.1; -; Genomic_DNA. DR RefSeq; WP_006927487.1; NZ_CP018099.1. DR EnsemblBacteria; EHO40490; EHO40490; Calab_0853. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000004671; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000004671}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000004671}. FT DOMAIN 202 368 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 424 AA; 48811 MW; 6393D200858967FF CRC64; MEKIIRTDKQ PERCVLVGVI QRGQSRWEVE DHLSELAALA RTSGADIIDT FIQERPSPDP AYFIGKGKIE EIAEYVSFND IDLLIFDDEL SPAQVRNIEN LTGIKVIDRT ALILDIFALH ARTNMAKVQV ELAQLNYYLP RLTRQWQHLS RQVGGIGTKG PGETQLETDR RLVRQRISHL KEKLEKIAHQ NEVQRQQRQE LFRAALIGYT NAGKSTLMNA LTNARVLIED QLFATLDTTV RRLALNPTTT ILLSDTVGFI RKLPHHLVAS FQTTLAEAIE ADLLIHVVDV THPHFEAQVK TVNQILDELH LNEKKRLLVF NKVDRLKNHH LIDQLRLLHP EALFISAARH IGLQHLRNRL LNLAEERYEI EQIRLNYQRG AAEHLIYPLA KILEKSSDEQ YLYLTIKYDK ANKSKINQIT AKYR // ID H1YGS0_9SPHI Unreviewed; 394 AA. AC H1YGS0; DT 21-MAR-2012, integrated into UniProtKB/TrEMBL. DT 21-MAR-2012, sequence version 1. DT 07-JUN-2017, entry version 35. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=Mucpa_2214 {ECO:0000313|EMBL:EHQ26349.1}; OS Mucilaginibacter paludis DSM 18603. OC Bacteria; Bacteroidetes; Sphingobacteriia; Sphingobacteriales; OC Sphingobacteriaceae; Mucilaginibacter. OX NCBI_TaxID=714943 {ECO:0000313|EMBL:EHQ26349.1, ECO:0000313|Proteomes:UP000002774}; RN [1] {ECO:0000313|EMBL:EHQ26349.1, ECO:0000313|Proteomes:UP000002774} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 18603 {ECO:0000313|EMBL:EHQ26349.1, RC ECO:0000313|Proteomes:UP000002774}; RG US DOE Joint Genome Institute (JGI-PGF); RA Lucas S., Han J., Lapidus A., Bruce D., Goodwin L., Pitluck S., RA Peters L., Kyrpides N., Mavromatis K., Ivanova N., Mikhailova N., RA Held B., Detter J.C., Tapia R., Han C., Land M., Hauser L., RA Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Tindall B., RA Brambilla E., Klenk H.-P., Eisen J.A.; RT "The permanent draft genome of Mucilaginibacter paludis DSM 18603."; RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CM001403; EHQ26349.1; -; Genomic_DNA. DR RefSeq; WP_008506411.1; NZ_CM001403.1. DR ProteinModelPortal; H1YGS0; -. DR STRING; 714943.Mucpa_2214; -. DR EnsemblBacteria; EHQ26349; EHQ26349; Mucpa_2214. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000002774; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000002774}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000002774}. FT DOMAIN 203 383 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 394 AA; 45086 MW; 2CBC208A94CC05BB CRC64; MKQKFYDTAV KQEKAILVGV ITPNETAEQG KEYLDELEFL VETAGGKTVK TFTQKMLRPE RSTFVGTGKL EEIKAYVDAE EIDIVVFDDG LSPSQLRNIE NELQVKILDR NNLILDIFAA RAQTSQARTQ VELAQLQYLL PRLTRLWTHL ERQKGGIGMR GPGESQIETD RRIILNKISL LKERLKLIDR QNETQRKNRG QLIRVALVGY TNVGKSTIMN MISKSEVFAE NKLFATLDTT VRKVVIDNLP FLLSDTVGFI RKLPHHLVEC FKSTLDEVRE ADILLHVVDV SHPNFEDQIK TVNETLKELG AIDKPVITVF NKIDAYKPIP VDPSEPEIKL TLNDFKQSWM AKNNSPAIFI SALNKENIDE FRSIVYERAK AIHTERYPYD NLLY // ID H1Z3W7_9EURY Unreviewed; 415 AA. AC H1Z3W7; DT 21-MAR-2012, integrated into UniProtKB/TrEMBL. DT 21-MAR-2012, sequence version 1. DT 07-JUN-2017, entry version 34. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=Metlim_2547 {ECO:0000313|EMBL:EHQ36589.1}; OS Methanoplanus limicola DSM 2279. OC Archaea; Euryarchaeota; Methanomicrobia; Methanomicrobiales; OC Methanomicrobiaceae; Methanoplanus. OX NCBI_TaxID=937775 {ECO:0000313|EMBL:EHQ36589.1, ECO:0000313|Proteomes:UP000005741}; RN [1] {ECO:0000313|EMBL:EHQ36589.1, ECO:0000313|Proteomes:UP000005741} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 2279 {ECO:0000313|EMBL:EHQ36589.1, RC ECO:0000313|Proteomes:UP000005741}; RG US DOE Joint Genome Institute (JGI-PGF); RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., RA Tice H., Bruce D., Goodwin L., Pitluck S., Peters L., Mikhailova N., RA Lu M., Kyrpides N., Mavromatis K., Ivanova N., Markowitz V., RA Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Wirth R., RA Brambilla E.-M., Klenk H.-P., Eisen J.A.; RT "The Improved High-Quality Draft genome of Methanoplanus limicola DSM RT 2279."; RL Submitted (OCT-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CM001436; EHQ36589.1; -; Genomic_DNA. DR RefSeq; WP_004079009.1; NZ_CM001436.1. DR EnsemblBacteria; EHQ36589; EHQ36589; Metlim_2547. DR PATRIC; fig|937775.9.peg.2871; -. DR OrthoDB; POG093Z07D6; -. DR Proteomes; UP000005741; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000005741}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000005741}. FT DOMAIN 190 359 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 415 AA; 47095 MW; 4D17324E5F08214D CRC64; MKRIIVAQRN YPNSDTAANS RKLAELKELS HAAGYMVVGT FVQSKKPDRN YQIGRGKVDE LAEFVESLGA EKVIFNNQLS VTQIYNISET CRCEVMDRLQ LILEIFAARA TTKRAKLQVE LAKLRYELPK VKSIVSMQKK DEKQGFMGLG SYENSHEQDI RKRITRIRAE LQQGSGSESQ RIFRHERGFS LVALAGYTNA GKSTLFQSLV KEETIIKNML FTTLSPTTRS LTVNSRKMLL TDTVGFIEDL PHWMVDAFRS TLDEIFLADV ILLVVDMSDP MDIIRQKLAV SHDIFRERTE GAVIVTALNK ADLLPDEELQ EKLEVISSLT PAPVMISAKS GEGLNELKQR LYEKLPEWEH CRISIPVSEE SISMVSWLYD ESVVHTIEYG DSIIMEIEAR DEIIQKIKPF ALSSE // ID H1ZE68_MYROD Unreviewed; 411 AA. AC H1ZE68; DT 21-MAR-2012, integrated into UniProtKB/TrEMBL. DT 21-MAR-2012, sequence version 1. DT 07-JUN-2017, entry version 34. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=Myrod_1784 {ECO:0000313|EMBL:EHQ42617.1}; OS Myroides odoratus DSM 2801. OC Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales; OC Flavobacteriaceae; Myroides. OX NCBI_TaxID=929704 {ECO:0000313|EMBL:EHQ42617.1, ECO:0000313|Proteomes:UP000005785}; RN [1] {ECO:0000313|EMBL:EHQ42617.1, ECO:0000313|Proteomes:UP000005785} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 2801 {ECO:0000313|EMBL:EHQ42617.1, RC ECO:0000313|Proteomes:UP000005785}; RG US DOE Joint Genome Institute (JGI-PGF); RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., RA Tice H., Bruce D., Goodwin L., Pitluck S., Peters L., Mikhailova N., RA Lu M., Kyrpides N., Mavromatis K., Ivanova N., Markowitz V., RA Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Tindall B., Schuetze A., RA Brambilla E., Klenk H.-P., Eisen J.A.; RT "The draft genome of Myroides odoratus DSM 2801."; RL Submitted (OCT-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CM001437; EHQ42617.1; -; Genomic_DNA. DR RefSeq; WP_002988789.1; NZ_CM001437.1. DR ProteinModelPortal; H1ZE68; -. DR EnsemblBacteria; EHQ42617; EHQ42617; Myrod_1784. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000005785; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000005785}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Hydrolase {ECO:0000313|EMBL:EHQ42617.1}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000005785}. FT DOMAIN 200 386 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 411 AA; 47679 MW; E7D840600847333F CRC64; MIEREEINFE RSVIVGIINR DQDEAKLNEY LDELEFLTIT AGGEVHKRFS QKLDQPNAKT FLGTGKMEEI KSYIVEHDIH TVIFDDELSP GQQKNITRIL DCKVLDRTNL ILDIFAQRAQ TSYARTQVEL AQFQYLLPRL SGMWTHLERQ RGGIGMRGPG ETEIETDRRI VRDRITLLRE KLKVIDKQMA SQRSNRGAMV RVALVGYTNV GKSTLMNAIG KSEVFVENKL FATLDTTVRK IVIGNLPFLL SDTVGFIRKL PTQLVESFKS TLDEVREADL LLHVVDISHH DFEDHIASVN DILKDIKSDD KPTIMVFNKI DAYHPEVIAE DDLMTERTSR HYSIEEWKKT WMNKVGVDNA IFISATNKEN FEEFRKKVYE TVRQIHITRF PYNNFLYPDF DHLIENEEDK I // ID H2BSJ7_9FLAO Unreviewed; 406 AA. AC H2BSJ7; DT 21-MAR-2012, integrated into UniProtKB/TrEMBL. DT 21-MAR-2012, sequence version 1. DT 07-JUN-2017, entry version 33. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=Gilli_1902 {ECO:0000313|EMBL:EHQ02544.1}; OS Gillisia limnaea DSM 15749. OC Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales; OC Flavobacteriaceae; Gillisia. OX NCBI_TaxID=865937 {ECO:0000313|EMBL:EHQ02544.1, ECO:0000313|Proteomes:UP000003844}; RN [1] {ECO:0000313|Proteomes:UP000003844} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 15749 {ECO:0000313|Proteomes:UP000003844}; RX PubMed=23450183; DOI=10.4056/sigs.3216895; RA Riedel T., Held B., Nolan M., Lucas S., Lapidus A., Tice H., RA Del Rio T.G., Cheng J.F., Han C., Tapia R., Goodwin L.A., Pitluck S., RA Liolios K., Mavromatis K., Pagani I., Ivanova N., Mikhailova N., RA Pati A., Chen A., Palaniappan K., Land M., Rohde M., Tindall B.J., RA Detter J.C., Goker M., Bristow J., Eisen J.A., Markowitz V., RA Hugenholtz P., Kyrpides N.C., Klenk H.P., Woyke T.; RT "Genome sequence of the Antarctic rhodopsins-containing flavobacterium RT Gillisia limnaea type strain (R-8282(T))."; RL Stand. Genomic Sci. 7:107-119(2012). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JH594606; EHQ02544.1; -; Genomic_DNA. DR RefSeq; WP_006988854.1; NZ_JH594606.1. DR ProteinModelPortal; H2BSJ7; -. DR EnsemblBacteria; EHQ02544; EHQ02544; Gilli_1902. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000003844; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000003844}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Hydrolase {ECO:0000313|EMBL:EHQ02544.1}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000003844}. FT DOMAIN 200 385 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 406 AA; 47017 MW; 182DAE702E96129A CRC64; MIEKTDLNYE KVVLIGIVTR EQDEDKLNEY LDELEFLTYT AGGEVLKRFT QKMEKPDPKT FMGSGKILEV KAFIDEHDVG TAIFDDELSP AQQKNIEKVL NVKILDRTNL ILDIFAQRAQ TSYARKQVEL AQYQYLLPRL AGMWTHLERQ RGGIGMRGPG ETEIETDRRI VRDKISLLKK KIETIDKQME VQRGNRGQLV RVALVGYTNV GKSTLMNLIS KSEVFAENKL FATLDTTVRK VVIRNLPFLL TDTVGFIRKL PTQLIESFKS TLDEVREADL LLHIVDISHP NFEEHIASVN QTLADIKSAN KPTIMVFNKI DAYTAEKIEE DDLITEKSKE HYSLEEWQQT WMNKLGDNVI FISALNKENI EDFKRKVYET VRQIHVTRFP YNNLLYPEYD TYGEEE // ID H2CG95_9LEPT Unreviewed; 588 AA. AC H2CG95; DT 21-MAR-2012, integrated into UniProtKB/TrEMBL. DT 21-MAR-2012, sequence version 1. DT 07-JUN-2017, entry version 33. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=Lepil_1081 {ECO:0000313|EMBL:EHQ05776.1}; OS Leptonema illini DSM 21528. OC Bacteria; Spirochaetes; Leptospirales; Leptospiraceae; Leptonema. OX NCBI_TaxID=929563 {ECO:0000313|EMBL:EHQ05776.1, ECO:0000313|Proteomes:UP000005737}; RN [1] {ECO:0000313|EMBL:EHQ05776.1, ECO:0000313|Proteomes:UP000005737} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 21528 {ECO:0000313|EMBL:EHQ05776.1, RC ECO:0000313|Proteomes:UP000005737}; RG US DOE Joint Genome Institute (JGI-PGF); RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., RA Tice H., Bruce D., Goodwin L., Pitluck S., Peters L., Mikhailova N., RA Held B., Kyrpides N., Mavromatis K., Ivanova N., Markowitz V., RA Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Gronow S., Wellnitz S., RA Brambilla E.-M., Klenk H.-P., Eisen J.A.; RT "The Improved High-Quality Draft genome of Leptonema illini DSM RT 21528."; RL Submitted (OCT-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JH597773; EHQ05776.1; -; Genomic_DNA. DR RefSeq; WP_002770730.1; NZ_JH597773.1. DR EnsemblBacteria; EHQ05776; EHQ05776; Lepil_1081. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000005737; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000005737}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000005737}. FT DOMAIN 389 555 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 355 382 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 588 AA; 66643 MW; B9EF8AB9D71E5FD4 CRC64; MPALRILEEE GALINLTGSL NGLKPAQLDR LRRLFRRRFP AEQLMTGEFA RELSELSHDI SRQIGVLADR RGRIDHVMVG DDRRIFIPEL ERGGAARLRE LRLIHTHLKK EPLSEEDLFD LTLLRLDTVT AITVDQRGLP EFFYTARLSP SAKTGYELFE PVRPGQEQEA FDILIEQIER EFRQSRDKTR KASGGPRAYL VGLYTPEMRR KRMPDESMDE LEELCRTAGV NPVRRFVQNR QKADPATVVG SGKIRDLSVA AVQDEIDLMI FDRELAPSQA IRISRETSLK IIDRTQLILD IFAQNARSRD GKLQVELAQL RYLKGRLSET DDNMSRLTGG IGARGPGETK LEIGRRRVEE KIGRLEKELK SLKGRRELLR SRRNRSGVPV CSIVGYTNAG KSTLLNALTR SEVIAENRLF ATLDPTTRRL RFPEERELIL SDTVGFIYDL PPELERAFEA TLEELGDSDL LLHCIDAADP LREQKIRDVE SILLHLGLDE IPVLRVYNKI DRMGEEQKGE LMVAAPVDSV FVSAQKGLGF EDLLLIMERR LFDHGTEVAA VAKKEGRAKK AAVQETVKSA TKEDEARG // ID H2FZ00_OCESG Unreviewed; 428 AA. AC H2FZ00; DT 21-MAR-2012, integrated into UniProtKB/TrEMBL. DT 21-MAR-2012, sequence version 1. DT 30-AUG-2017, entry version 38. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=GU3_05420 {ECO:0000313|EMBL:AEY00841.1}; OS Oceanimonas sp. (strain GK1). OC Bacteria; Proteobacteria; Gammaproteobacteria; Aeromonadales; OC Aeromonadaceae; Oceanimonas. OX NCBI_TaxID=511062 {ECO:0000313|EMBL:AEY00841.1, ECO:0000313|Proteomes:UP000007742}; RN [1] {ECO:0000313|EMBL:AEY00841.1, ECO:0000313|Proteomes:UP000007742} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=GK1 {ECO:0000313|EMBL:AEY00841.1, RC ECO:0000313|Proteomes:UP000007742}; RX PubMed=22461556; DOI=10.1128/JB.00023-12; RA Parsa Yeganeh L., Azarbaijani R., Sarikhan S., Mousavi H., RA Ramezani M., Amoozegar M.A., Shahzadeh Fazeli A., Salekdeh G.H.; RT "Complete genome sequence of Oceanimonas sp. GK1, a halotolerant RT bacterium from Gavkhouni Wetland in Iran."; RL J. Bacteriol. 194:2123-2124(2012). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP003171; AEY00841.1; -; Genomic_DNA. DR RefSeq; WP_014291568.1; NC_016745.1. DR STRING; 511062.GU3_05420; -. DR EnsemblBacteria; AEY00841; AEY00841; GU3_05420. DR KEGG; oce:GU3_05420; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000007742; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000007742}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000007742}. FT DOMAIN 198 365 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 428 AA; 48424 MW; 282FF85E8DE0A4B4 CRC64; MFERYQGGES AILVHINFTD DSEREDLEEL QLLADSAGVT TCAVVTSSRA APQSKFFIGT GKVEELASLV QMHQADVVIF NHSLSPAQER NLEREVKCRV LDRTGLILDI FAQRARTHEG KLQVELAQLR HLSTRLVRGW THLERQKGGI GLRGPGETQL ETDRRLLRER IKYIQKRLEK VSRQREQGRR ARQRNEIPTL SLVGYTNAGK STLFNRLTES DVYAADQLFA TLDPTLRKIE LPDAGLAILA DTVGFIRHLP HDLVAAFKAT LQETRDADLL LHVVDCADEQ MRDNIDEVNS VLEQIEADEI PVLMVFNKID KLDPPEPRIE RDDQGRPRAV WVSAQQGLGI DGLLKALNEL LAGTLVEHRL TLPPSASRLR SRLYALNGIV TESFGDQGEY VVEIRLQQAD WHRLLKQEGE QLERFISD // ID H2IS59_RAHAC Unreviewed; 434 AA. AC H2IS59; DT 21-MAR-2012, integrated into UniProtKB/TrEMBL. DT 21-MAR-2012, sequence version 1. DT 30-AUG-2017, entry version 38. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Rahaq2_0456 {ECO:0000313|EMBL:AEX50390.1}; OS Rahnella aquatilis (strain ATCC 33071 / DSM 4594 / JCM 1683 / NBRC OS 105701 / NCIMB 13365 / CIP 78.65). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; OC Yersiniaceae; Rahnella. OX NCBI_TaxID=745277 {ECO:0000313|EMBL:AEX50390.1, ECO:0000313|Proteomes:UP000009010}; RN [1] {ECO:0000313|Proteomes:UP000009010} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33071 / DSM 4594 / JCM 1683 / NBRC 105701 / NCIMB 13365 / RC CIP 78.65 {ECO:0000313|Proteomes:UP000009010}; RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S., RA Peters L., Ovchinnikova G., Held B., Detter J.C., Han C., Tapia R., RA Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Sobecky P., RA Martinez R., Woyke T.; RT "Complete sequence of chromosome of Rahnella aquatilis CIP 78.65."; RL Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP003244; AEX50390.1; -; Genomic_DNA. DR RefSeq; WP_014333660.1; NZ_JMPO01000135.1. DR STRING; 745277.Rahaq2_0456; -. DR EnsemblBacteria; AEX50390; AEX50390; Rahaq2_0456. DR KEGG; raq:Rahaq2_0456; -. DR PATRIC; fig|745277.3.peg.432; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000009010; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000009010}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000009010}. FT DOMAIN 198 365 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 434 AA; 48654 MW; 4CEA9A6663EA9DDE CRC64; MFDRYEAGEQ AVLVHIYFSQ DKDTEDLSEF ESLVSSAGVE ALQVVTGSRK APHPKYFVGE GKAQEIADAV KATGASVILF DHALSPGQER NLEALCECRV VDRTGLILDI FAQRARTHEG KLQVELAQLR HIATRLVRGW THLERQGGGI GARGPGETQL ETDRRLLRDR ITLILSRLEK VAKQREQGRR SRVRADIPTV SLVGYTNAGK STLFNRITQA DVYVANQLFA TLDPTLRRIM VADVGETVLA DTVGFIRHLP HDLVAAFKAT LQETRQASLL LHVIDAADIR VQENIDAVNT VLAEIEADEI PALLVMNKID MLDDFVPRID RNEENLPVRV WLSAVTGEGI PLLFQALTER LSGEIAQHEL CLPPEAGRLR SRFYQLQAIE KEWIEEDGSI GLMVRMPIVD WRRLCKQEQE LESYVRNQSL SDLA // ID H2J813_MARPK Unreviewed; 403 AA. AC H2J813; DT 21-MAR-2012, integrated into UniProtKB/TrEMBL. DT 21-MAR-2012, sequence version 1. DT 07-JUN-2017, entry version 36. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Marpi_1092 {ECO:0000313|EMBL:AEX85504.1}; OS Marinitoga piezophila (strain DSM 14283 / JCM 11233 / KA3). OC Bacteria; Thermotogae; Petrotogales; Petrotogaceae; Marinitoga. OX NCBI_TaxID=443254 {ECO:0000313|EMBL:AEX85504.1, ECO:0000313|Proteomes:UP000007161}; RN [1] {ECO:0000313|Proteomes:UP000007161} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 14283 / JCM 11233 / KA3 RC {ECO:0000313|Proteomes:UP000007161}; RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S., RA Peters L., Mikhailova N., Teshima H., Detter J.C., Han C., Tapia R., RA Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Jebbar M., RA Vannier P., Oger P., Cario A., Bartlett D., Noll K.M., Woyke T.; RT "Complete sequence of chromosome of Marinitoga piezophila KA3."; RL Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP003257; AEX85504.1; -; Genomic_DNA. DR RefSeq; WP_014296576.1; NC_016751.1. DR STRING; 443254.Marpi_1092; -. DR EnsemblBacteria; AEX85504; AEX85504; Marpi_1092. DR KEGG; mpz:Marpi_1092; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000007161; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000007161}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000007161}. FT DOMAIN 189 355 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 157 184 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 403 AA; 46274 MW; C7D5B25A67D7F79C CRC64; MRIKKGVLVL INSKNLREDV EEIIELSKNI NIEIVEYIHQ NLNKPDPLTF IGKGKFEDLK ELIAFVDAEV LVINSELSPR QYIHISKELN IEVYDRTDVI LKIFSEHAET QESKLQIKLA TLKHILPRIY GLGSEMSRTG GGIGTRGPGE QEKEYKKRTI KNEISKIQNK LKKIKSQREL TRKNKKDIIK VSIVGYASAG KSTLLKELSH ENKIKISEKM FSTLSPKSRR VMLPSGLFVI LSDTVGFIRN LPHELIEAFK STLEEIKYSD LIIHLVDISS QNIEERISTA YDVLENIKAL DIPRILVFNK IDKINDEQLS ILKNIYKNAI FISCKTGENI ENLKKAIQDK LIEEEIIKTF EIEEEYKNVQ NWFKKRGKIG IEEIAFNNTD IKLKIYARNG GAL // ID H2K0S7_STRHJ Unreviewed; 496 AA. AC H2K0S7; DT 21-MAR-2012, integrated into UniProtKB/TrEMBL. DT 21-MAR-2012, sequence version 1. DT 07-JUN-2017, entry version 38. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=SHJG_6894 {ECO:0000313|EMBL:AEY92161.1}; OS Streptomyces hygroscopicus subsp. jinggangensis (strain 5008). OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae; OC Streptomyces. OX NCBI_TaxID=1133850 {ECO:0000313|EMBL:AEY92161.1, ECO:0000313|Proteomes:UP000007170}; RN [1] {ECO:0000313|Proteomes:UP000007170} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=5008 {ECO:0000313|Proteomes:UP000007170}; RA Wu H., Bai L.; RT "Genomic analysis of Streptomyces hygroscopicus subsp. jinggangensis RT 5008."; RL Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP003275; AEY92161.1; -; Genomic_DNA. DR RefSeq; WP_014675448.1; NC_017765.1. DR STRING; 1133850.SHJG_6894; -. DR EnsemblBacteria; AEY92161; AEY92161; SHJG_6894. DR KEGG; shy:SHJG_6894; -. DR PATRIC; fig|1133850.20.peg.7500; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000007170; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000007170}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}. FT DOMAIN 274 439 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 496 AA; 54169 MW; 773EC3D8C214D8BC CRC64; MTSSSSPSQD AKRLAHAYPE GLRADALMEE DVAWSYEIDG DRDGDQFDRS ERAALRRVVG LSTELEDVTE VEYRQLRLER VVLVGVWTTG TAQDADNSLA ELAALAETAG ALVLDGVIQR RDKPDAATYI GSGKAAELRD IVIETGADTV ICDGELSPGQ LIQLEDVVKV KVIDRTALIL DIFAQHAKSR EGKAQVALAQ MQYMLPRLRG WGQSLSRQMG GGRGGLATRG PGETKIETDR RRIREKMAKM RREIADMKTG REIKRQERRR NKVPSVAIAG YTNAGKSSLL NRLTGAGVLV ENALFATLDP TVRRAETPSG RLYTLADTVG FVRHLPHHLV EAFRSTMEEV GDSDLILHVV DGSHPNPEEQ LAAVREVIRD VGAIDVPEIV VVNKADAADP LVLQRLLRVE KRSIAVSART GQGIEELLGL IDNELPRPSV EIEALVPYTH GKLVARAHTE GEVISEEHTA EGTLLKVRVH EELAADLAPY VPVSAA // ID H2TU47_TAKRU Unreviewed; 375 AA. AC H2TU47; DT 21-MAR-2012, integrated into UniProtKB/TrEMBL. DT 21-MAR-2012, sequence version 1. DT 30-AUG-2017, entry version 23. DE SubName: Full=GTP binding protein 6 (putative) {ECO:0000313|Ensembl:ENSTRUP00000028205}; OS Takifugu rubripes (Japanese pufferfish) (Fugu rubripes). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata; OC Eupercaria; Tetraodontiformes; Tetradontoidea; Tetraodontidae; OC Takifugu. OX NCBI_TaxID=31033 {ECO:0000313|Ensembl:ENSTRUP00000028205, ECO:0000313|Proteomes:UP000005226}; RN [1] {ECO:0000313|Ensembl:ENSTRUP00000028205} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=21551351; RA Kai W., Kikuchi K., Tohari S., Chew A.K., Tay A., Fujiwara A., RA Hosoya S., Suetake H., Naruse K., Brenner S., Suzuki Y., Venkatesh B.; RT "Integration of the genetic map and genome assembly of fugu RT facilitates insights into distinct features of genome evolution in RT teleosts and mammals."; RL Genome Biol. Evol. 3:424-442(2011). RN [2] {ECO:0000313|Ensembl:ENSTRUP00000028205} RP IDENTIFICATION. RG Ensembl; RL Submitted (FEB-2012) to UniProtKB. CC -!- CAUTION: The sequence shown here is derived from an Ensembl CC automatic analysis pipeline and should be considered as CC preliminary data. {ECO:0000313|Ensembl:ENSTRUP00000028205}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR Ensembl; ENSTRUT00000028317; ENSTRUP00000028205; ENSTRUG00000011175. DR eggNOG; KOG0410; Eukaryota. DR eggNOG; COG2262; LUCA. DR GeneTree; ENSGT00390000001397; -. DR Proteomes; UP000005226; Unplaced. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR CDD; cd01878; HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000005226}; KW Reference proteome {ECO:0000313|Proteomes:UP000005226}. FT DOMAIN 142 306 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 375 AA; 41987 MW; 35C742C0965B9138 CRC64; FQSLTEKIRQ TAGITAVFVN VERLSPLSVK ELKEAWGVNV FDRYSVVLHI FRCNAQTKEA KLQISLAEIP LLSNGRSRLR NDVANLDQQG GRSKYIGGSG ETLLEVQQRL LRERELKIRS ALEKLRRKRH LLRSQRKHKE FPVVSVLGYT NCGKTTLIKS LTGDSGLQPK NQLFATLDVT VHAGQLPNHM TVLYVDTIGF LSQLPHQLID SFSATLEDIK HSDLLVHVRD ISHPETVNQK VNVLNVLKNL QIPERLLGSM IEVHNKIDLI DNYQFMDPHV LPISALDGRG LDELKMAVEA EIIASTGKHI LDLRVDLSSP QLSWLYKEAT VQDVEVDAND GSAIVKVVIS TAAYGRYKKL FSDFHSSDKC SSALA // ID H2TU48_TAKRU Unreviewed; 464 AA. AC H2TU48; DT 21-MAR-2012, integrated into UniProtKB/TrEMBL. DT 21-MAR-2012, sequence version 1. DT 30-AUG-2017, entry version 27. DE SubName: Full=GTP binding protein 6 (putative) {ECO:0000313|Ensembl:ENSTRUP00000028206}; OS Takifugu rubripes (Japanese pufferfish) (Fugu rubripes). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata; OC Eupercaria; Tetraodontiformes; Tetradontoidea; Tetraodontidae; OC Takifugu. OX NCBI_TaxID=31033 {ECO:0000313|Ensembl:ENSTRUP00000028206, ECO:0000313|Proteomes:UP000005226}; RN [1] {ECO:0000313|Ensembl:ENSTRUP00000028206} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=21551351; RA Kai W., Kikuchi K., Tohari S., Chew A.K., Tay A., Fujiwara A., RA Hosoya S., Suetake H., Naruse K., Brenner S., Suzuki Y., Venkatesh B.; RT "Integration of the genetic map and genome assembly of fugu RT facilitates insights into distinct features of genome evolution in RT teleosts and mammals."; RL Genome Biol. Evol. 3:424-442(2011). RN [2] {ECO:0000313|Ensembl:ENSTRUP00000028206} RP IDENTIFICATION. RG Ensembl; RL Submitted (FEB-2012) to UniProtKB. CC -!- CAUTION: The sequence shown here is derived from an Ensembl CC automatic analysis pipeline and should be considered as CC preliminary data. {ECO:0000313|Ensembl:ENSTRUP00000028206}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR STRING; 31033.ENSTRUP00000028206; -. DR Ensembl; ENSTRUT00000028318; ENSTRUP00000028206; ENSTRUG00000011175. DR eggNOG; KOG0410; Eukaryota. DR eggNOG; COG2262; LUCA. DR GeneTree; ENSGT00390000001397; -. DR InParanoid; H2TU48; -. DR OMA; MDTVGFM; -. DR OrthoDB; EOG091G0852; -. DR TreeFam; TF315022; -. DR Proteomes; UP000005226; Unplaced. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR GO; GO:0043022; F:ribosome binding; IBA:GO_Central. DR CDD; cd01878; HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000005226}; KW Reference proteome {ECO:0000313|Proteomes:UP000005226}. FT DOMAIN 234 398 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 464 AA; 52207 MW; 491B1E4415DDF872 CRC64; EEEEEEDFID DSEVEELFQQ QDIAEVGQGQ HRLFIVHPDV KWGSRKQHLT TAELMLAEAV GLVNTLDNWT VVDSIILSTK TPEKKRIFGK GNFQSLTEKI RQTAGITAVF VNVERLSPLS VKELKEAWGV NVFDRYSVVL HIFRCNAQTK EAKLQISLAE IPLLSNGRSR LRNDVANLDQ QGGRSKYIGG SGETLLEVQQ RLLRERELKI RSALEKLRRK RHLLRSQRKH KEFPVVSVLG YTNCGKTTLI KSLTGDSGLQ PKNQLFATLD VTVHAGQLPN HMTVLYVDTI GFLSQLPHQL IDSFSATLED IKHSDLLVHV RDISHPETVN QKVNVLNVLK NLQIPERLLG SMIEVHNKID LIDNYQFMDP HVLPISALDG RGLDELKMAV EAEIIASTGK HILDLRVDLS SPQLSWLYKE ATVQDVEVDA NDGSAIVKVV ISTAAYGRYK KLFSGKINDT CLPH // ID H2TU49_TAKRU Unreviewed; 446 AA. AC H2TU49; DT 21-MAR-2012, integrated into UniProtKB/TrEMBL. DT 21-MAR-2012, sequence version 1. DT 30-AUG-2017, entry version 21. DE SubName: Full=GTP binding protein 6 (putative) {ECO:0000313|Ensembl:ENSTRUP00000028207}; OS Takifugu rubripes (Japanese pufferfish) (Fugu rubripes). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata; OC Eupercaria; Tetraodontiformes; Tetradontoidea; Tetraodontidae; OC Takifugu. OX NCBI_TaxID=31033 {ECO:0000313|Ensembl:ENSTRUP00000028207, ECO:0000313|Proteomes:UP000005226}; RN [1] {ECO:0000313|Ensembl:ENSTRUP00000028207} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=21551351; RA Kai W., Kikuchi K., Tohari S., Chew A.K., Tay A., Fujiwara A., RA Hosoya S., Suetake H., Naruse K., Brenner S., Suzuki Y., Venkatesh B.; RT "Integration of the genetic map and genome assembly of fugu RT facilitates insights into distinct features of genome evolution in RT teleosts and mammals."; RL Genome Biol. Evol. 3:424-442(2011). RN [2] {ECO:0000313|Ensembl:ENSTRUP00000028207} RP IDENTIFICATION. RG Ensembl; RL Submitted (FEB-2012) to UniProtKB. CC -!- CAUTION: The sequence shown here is derived from an Ensembl CC automatic analysis pipeline and should be considered as CC preliminary data. {ECO:0000313|Ensembl:ENSTRUP00000028207}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR Ensembl; ENSTRUT00000028319; ENSTRUP00000028207; ENSTRUG00000011175. DR eggNOG; KOG0410; Eukaryota. DR eggNOG; COG2262; LUCA. DR GeneTree; ENSGT00390000001397; -. DR Proteomes; UP000005226; Unplaced. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR CDD; cd01878; HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000005226}; KW Reference proteome {ECO:0000313|Proteomes:UP000005226}. FT DOMAIN 224 388 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 446 AA; 50090 MW; 6AD7C52137817868 CRC64; DSEVEELFQQ QDIAEVGQGQ HRLFIVHPDV KWGSRKQHLT TAELMLAEAV GLVNTLDNWT VVDSIILSTK TPEKKRIFGK GNFQSLTEKI RQTAGITAVF VNVERLSPLS VKELKEAWGV NVFDRYSVVL HIFRCNAQTK EAKLQISLAE IPLLSNGRSR LRNDVANLDQ QGGRSKYIGG SGETLLEVQQ RLLRERELKI RSALEKLRRK RHLLRSQRKH KEFPVVSVLG YTNCGKTTLI KSLTGDSGLQ PKNQLFATLD VTVHAGQLPN HMTVLYVDTI GFLSQLPHQL IDSFSATLED IKHSDLLVHV RDISHPETVN QKVNVLNVLK NLQIPERLLG SMIEVHNKID LIDNYQFMDP HVLPISALDG RGLDELKMAV EAEIIASTGK HILDLRVDLS SPQLSWLYKE ATVQDVEVDA NDGSAIVKVV ISTAAYGRYK KLFSVK // ID H2VIB4_CAEJA Unreviewed; 1525 AA. AC H2VIB4; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 09-JAN-2013, sequence version 2. DT 10-MAY-2017, entry version 26. DE SubName: Full=Uncharacterized protein {ECO:0000313|EnsemblMetazoa:CJA00975}; OS Caenorhabditis japonica. OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida; OC Rhabditoidea; Rhabditidae; Peloderinae; Caenorhabditis. OX NCBI_TaxID=281687 {ECO:0000313|EnsemblMetazoa:CJA00975}; RN [1] {ECO:0000313|EnsemblMetazoa:CJA00975} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DF5081 {ECO:0000313|EnsemblMetazoa:CJA00975}; RG Caenorhabditis japonica Sequencing Consortium; RA Wilson R.K.; RL Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EnsemblMetazoa:CJA00975} RP IDENTIFICATION. RC STRAIN=DF5081 {ECO:0000313|EnsemblMetazoa:CJA00975}; RG EnsemblMetazoa; RL Submitted (NOV-2012) to UniProtKB. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR STRING; 281687.CJA00975; -. DR EnsemblMetazoa; CJA00975; CJA00975; WBGene00120179. DR eggNOG; KOG0017; Eukaryota. DR eggNOG; KOG0410; Eukaryota. DR eggNOG; COG2262; LUCA. DR eggNOG; COG2801; LUCA. DR InParanoid; H2VIB4; -. DR OrthoDB; EOG091G0852; -. DR Proteomes; UP000005237; Unassembled WGS sequence. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro. DR GO; GO:0015074; P:DNA integration; IEA:InterPro. DR CDD; cd01878; HflX; 1. DR Gene3D; 3.30.420.10; -; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR001584; Integrase_cat-core. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR012337; RNaseH-like_dom. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR Pfam; PF00665; rve; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF53098; SSF53098; 1. DR PROSITE; PS51705; G_HFLX; 1. DR PROSITE; PS50994; INTEGRASE; 1. PE 4: Predicted; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000005237}; KW Reference proteome {ECO:0000313|Proteomes:UP000005237}. FT DOMAIN 331 487 Integrase catalytic. FT {ECO:0000259|PROSITE:PS50994}. FT DOMAIN 1295 1461 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 1246 1281 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 1525 AA; 171906 MW; 3E2CDCE87D0F1791 CRC64; MKTLRGPLDK LLMKDAEWRW TKVEAESFQK LKDVLSSDLN LTHYMPKIPI VVAADACDYG IGAVISHRFA DGTEKPIAHA ARSLNSAEKN YSQIEKEGLG LIFAVKRFHK YLFGRKFLLR TDHKPLLSIF GSKKGIPVHS QNRLVRWSTI LLAYDFDIEY VKTDEFGQAD ALSRMIQKTP LENEDIVIAQ VEEDVKEVLY AAVRKLPIRV KDIQEETGKS NTLKEVINCV SRNSWPKKPE GKLKQFFDIR SVLSVVQNCL MFKERVVIPE ALQKATLRQL HEGHPGIVRM KQLARSFVYW PRMDSDIEKL VAACTTCQIH GKTTRKVPLE PWTTPDRVWQ RIHIDYAGPD NGQYYLVVVD AKSKWAEVAI VKSISSVSTV RTLKSIFSTH GYPETLVSDN GTQFVSREFA SMCEEYGIEH IRSPAFHPQS NGQAERFVDT LKRGLKKLKG EGSVDTEIMS KFLLYYRSTP SNALGGLTPA EVHLGRRLRT RMSLMIPKLK LNTGSQKSSL MKDQFDKHHG TRPKHFSVNE SVYAKVFERN AWSWKPATVV QRQGRVVYMV RLNDGRERVV HANQLKLRVE QTDECKDELW TTTMFDIFEV PLPQETSTPM SVTTPTFATP SREQQQQGHQ SHAQARMPSS AQFSQRSQQH QSPGVVPVRR GNRVLVTVVI LLTTQQCIYI RTAFRNSAPK SSSRSSPSRR RSDEKRRQKD KKEDREDSMH RDREKRHDES NASKKPPPKP ASSSSQHHQN HHHHDFKSDR DSTTSSSSRA TVNGNADVAK RDAEKRDAEK RRKEKESRKP SDAGSQRERE REKEKMRNIQ KLQSQQPYHP DDSRNARKER SIGGSDQKTE RKRKADETIK NEFKIPKKTS SAPPPPPSRA TYGSQLQSGP LTRESLPSSS TGKSEKSTAL SKVEKAVPGP AKKELSSGDT SPDRTRFLTS RYHIARLCSM LVNADKQYDA FQKGLQNKKN QQVEEHLEAL SDIEEDEFSE TSPSPPAAPT TAVSTNPKSR SFAPHKGYAK NANKSPSSEE SSGAEDGKEG DTEHETDSED DEDVPGASRR GESDSPGSPA ADAQKNKTGP EMPTTSSKFA TERWSVLVVH PKVRWGSGSA SVLKQADRQL EEAVALVDNL PNMIAVDSLI MPVDYNTKRK AIWAAGNLEK LVAQKETARA TALMINVDVL SPSQQEELFR IFEVPIFDRY NVVLATFKEF ARTDEARLQI ALAEIPYIKH RIHAISSRRI HSRPEILHIE QQYAEVEGDL NEILRKREQD LRKELKEATR KSSEQNISSK NSSDAVVAVV GYTNAGKTSL VKRLTGAETL TPKDQLFATL DTTRHVAKLP SGRSAVFTDT IGFLSDLPMH LISAFEATLA HVKLADVIVH LRDVSNADWK AQEEDVVATL KSIGVSEKIL NERMITVDNK IDKEGAASAT ETDNTTRISC QTGDGMRDLI QLITEKVSLA TKCKTIRMRL DVRSPVIEWL YRNEFVVVEP IADGNTLIFD VVMNESEIGQ FRKKFAYLKK KKSSS // ID H3AXX3_LATCH Unreviewed; 552 AA. AC H3AXX3; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 30-AUG-2017, entry version 33. DE SubName: Full=GTP binding protein 6 (putative) {ECO:0000313|Ensembl:ENSLACP00000014494}; GN Name=GTPBP6 {ECO:0000313|Ensembl:ENSLACP00000014494}; OS Latimeria chalumnae (West Indian ocean coelacanth). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Coelacanthiformes; Coelacanthidae; Latimeria. OX NCBI_TaxID=7897 {ECO:0000313|Ensembl:ENSLACP00000014494, ECO:0000313|Proteomes:UP000008672}; RN [1] {ECO:0000313|Ensembl:ENSLACP00000014494} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Wild caught {ECO:0000313|Ensembl:ENSLACP00000014494}; RX PubMed=9215903; RA Zardoya R., Meyer A.; RT "The complete DNA sequence of the mitochondrial genome of a 'living RT fossil,' the coelacanth (Latimeria chalumnae)."; RL Genetics 146:995-1010(1997). RN [2] {ECO:0000313|Ensembl:ENSLACP00000014494} RP IDENTIFICATION. RG Ensembl; RL Submitted (FEB-2012) to UniProtKB. CC -!- CAUTION: The sequence shown here is derived from an Ensembl CC automatic analysis pipeline and should be considered as CC preliminary data. {ECO:0000313|Ensembl:ENSLACP00000014494}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFYH01098047; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR RefSeq; XP_005999040.1; XM_005998978.2. DR STRING; 7897.ENSLACP00000014494; -. DR Ensembl; ENSLACT00000014594; ENSLACP00000014494; ENSLACG00000012754. DR GeneID; 102346725; -. DR KEGG; lcm:102346725; -. DR CTD; 8225; -. DR eggNOG; KOG0410; Eukaryota. DR eggNOG; COG2262; LUCA. DR GeneTree; ENSGT00390000001397; -. DR InParanoid; H3AXX3; -. DR OMA; MDTVGFM; -. DR OrthoDB; EOG091G0852; -. DR TreeFam; TF315022; -. DR Proteomes; UP000008672; Unassembled WGS sequence. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR CDD; cd01878; HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008672}; KW Reference proteome {ECO:0000313|Proteomes:UP000008672}. FT DOMAIN 331 495 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 552 AA; 61469 MW; BD30BD03D014D10D CRC64; MLLRIGWRSW FCRWSCSGNL AVNVDRKARF ARSVSFLHSA GSEAAAAAFA VPTPRGPARA WLSPHRGAGV GAVAFSSTSV RLRKRKGGKA AGDSSEEEEE DLDVDDEVDL GDQEVEELFE QRSPGVPEGG QRVFIVHPDV KWGAQKQHLT TGDLQMAEAV ALVNTLPNWR VVDKIILSTK TPDKRRIFGK GNFQTLTEKI RGLPQITAVF MNVERLSALT QKELQESWGV KVFDRYTVVL HIFRCNARTK EAKLQIALAE IPLLKSHLKS ESSHLDQQGG GSRYIMGSGE TFMEVQQRLL KERELKIKNA LVKLRKKRHL LRSQRKQREF PIISVMGYTN CGKTTLIKAL TGDVGLQPRD QLFATLDITA HAGFLPSHMT ILYVDTIGFL SQLPHNLIES FSATLEDVAH SDLIVHVRDI SHPETINQKL NVLTVLKNLH LPSHLLDSII EVHNKIDLLN GYQPTEPSVV PVSALHGSGL EELKNRIEEA VLKATGKLTL TIKIDLSGQQ LSWLYKEATV QEVDVLPDDG AANVKVIISK SAHGRYKKLF QQ // ID H3C218_TETNG Unreviewed; 431 AA. AC H3C218; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 30-AUG-2017, entry version 24. DE SubName: Full=GTP binding protein 6 (putative) {ECO:0000313|Ensembl:ENSTNIP00000002286}; OS Tetraodon nigroviridis (Spotted green pufferfish) (Chelonodon OS nigroviridis). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata; OC Eupercaria; Tetraodontiformes; Tetradontoidea; Tetraodontidae; OC Tetraodon. OX NCBI_TaxID=99883 {ECO:0000313|Ensembl:ENSTNIP00000002286, ECO:0000313|Proteomes:UP000007303}; RN [1] {ECO:0000313|Ensembl:ENSTNIP00000002286} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15496914; DOI=10.1038/nature03025; RA Jaillon O., Aury J.-M., Brunet F., Petit J.-L., Stange-Thomann N., RA Mauceli E., Bouneau L., Fischer C., Ozouf-Costaz C., Bernot A., RA Nicaud S., Jaffe D., Fisher S., Lutfalla G., Dossat C., Segurens B., RA Dasilva C., Salanoubat M., Levy M., Boudet N., Castellano S., RA Anthouard V., Jubin C., Castelli V., Katinka M., Vacherie B., RA Biemont C., Skalli Z., Cattolico L., Poulain J., De Berardinis V., RA Cruaud C., Duprat S., Brottier P., Coutanceau J.-P., Gouzy J., RA Parra G., Lardier G., Chapple C., McKernan K.J., McEwan P., Bosak S., RA Kellis M., Volff J.-N., Guigo R., Zody M.C., Mesirov J., RA Lindblad-Toh K., Birren B., Nusbaum C., Kahn D., Robinson-Rechavi M., RA Laudet V., Schachter V., Quetier F., Saurin W., Scarpelli C., RA Wincker P., Lander E.S., Weissenbach J., Roest Crollius H.; RT "Genome duplication in the teleost fish Tetraodon nigroviridis reveals RT the early vertebrate proto-karyotype."; RL Nature 431:946-957(2004). RN [2] {ECO:0000313|Ensembl:ENSTNIP00000002286} RP IDENTIFICATION. RG Ensembl; RL Submitted (FEB-2012) to UniProtKB. CC -!- CAUTION: The sequence shown here is derived from an Ensembl CC automatic analysis pipeline and should be considered as CC preliminary data. {ECO:0000313|Ensembl:ENSTNIP00000002286}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR Ensembl; ENSTNIT00000003887; ENSTNIP00000002286; ENSTNIG00000010659. DR eggNOG; KOG0410; Eukaryota. DR eggNOG; COG2262; LUCA. DR GeneTree; ENSGT00390000001397; -. DR Proteomes; UP000007303; Unassembled WGS sequence. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR CDD; cd01878; HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000007303}; KW Reference proteome {ECO:0000313|Proteomes:UP000007303}. FT DOMAIN 202 366 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 431 AA; 47966 MW; CB98199014B75CCA CRC64; QRLVIVHPDV KWGSRKQHLT TAELMLAEAV GLVNTLDNWT VVDTVVLSTK TPEKKRIFGK GNFQSLTEKI RQTAGITAVF VNVEHLSPLS ERELEEAWGV KVLDRYSVVL HIFRCNARTK EAKLQISLAE IPLLRRSRLK NEIANLDQQG GRSKYIGGSG ETLLEVQQRL LKEREMKIRT ALEKLRRKRH LLRAQRKQQE FPMVSVLGYT NSGKTTLIKS LTGDSGLQPK NQLFATLDVT VHAGQLPNHM TVLYVDTIGF LSQLPHRLID SFSATLEDIK HSDLLLHVRD VSHPETLNQK ANVLNVLKNL QIPDRLIGSM IEVHNKIDLV DSYQFTDPRA LPVSALGGRG LDRLKEAVEA EIVAATGKHT LALPVDLSSP QLSWLYKEAA VQDLEVNADD GSAVVKVVIS AAAYGRYKKL FSVSAPPATS S // ID H3CZ89_TETNG Unreviewed; 444 AA. AC H3CZ89; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 30-AUG-2017, entry version 26. DE SubName: Full=GTP binding protein 6 (putative) {ECO:0000313|Ensembl:ENSTNIP00000013574}; OS Tetraodon nigroviridis (Spotted green pufferfish) (Chelonodon OS nigroviridis). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata; OC Eupercaria; Tetraodontiformes; Tetradontoidea; Tetraodontidae; OC Tetraodon. OX NCBI_TaxID=99883 {ECO:0000313|Ensembl:ENSTNIP00000013574, ECO:0000313|Proteomes:UP000007303}; RN [1] {ECO:0000313|Ensembl:ENSTNIP00000013574} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15496914; DOI=10.1038/nature03025; RA Jaillon O., Aury J.-M., Brunet F., Petit J.-L., Stange-Thomann N., RA Mauceli E., Bouneau L., Fischer C., Ozouf-Costaz C., Bernot A., RA Nicaud S., Jaffe D., Fisher S., Lutfalla G., Dossat C., Segurens B., RA Dasilva C., Salanoubat M., Levy M., Boudet N., Castellano S., RA Anthouard V., Jubin C., Castelli V., Katinka M., Vacherie B., RA Biemont C., Skalli Z., Cattolico L., Poulain J., De Berardinis V., RA Cruaud C., Duprat S., Brottier P., Coutanceau J.-P., Gouzy J., RA Parra G., Lardier G., Chapple C., McKernan K.J., McEwan P., Bosak S., RA Kellis M., Volff J.-N., Guigo R., Zody M.C., Mesirov J., RA Lindblad-Toh K., Birren B., Nusbaum C., Kahn D., Robinson-Rechavi M., RA Laudet V., Schachter V., Quetier F., Saurin W., Scarpelli C., RA Wincker P., Lander E.S., Weissenbach J., Roest Crollius H.; RT "Genome duplication in the teleost fish Tetraodon nigroviridis reveals RT the early vertebrate proto-karyotype."; RL Nature 431:946-957(2004). RN [2] {ECO:0000313|Ensembl:ENSTNIP00000013574} RP IDENTIFICATION. RG Ensembl; RL Submitted (FEB-2012) to UniProtKB. CC -!- CAUTION: The sequence shown here is derived from an Ensembl CC automatic analysis pipeline and should be considered as CC preliminary data. {ECO:0000313|Ensembl:ENSTNIP00000013574}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR STRING; 99883.ENSTNIP00000013574; -. DR Ensembl; ENSTNIT00000013768; ENSTNIP00000013574; ENSTNIG00000010659. DR eggNOG; KOG0410; Eukaryota. DR eggNOG; COG2262; LUCA. DR GeneTree; ENSGT00390000001397; -. DR InParanoid; H3CZ89; -. DR OMA; MDTVGFM; -. DR OrthoDB; EOG091G0852; -. DR TreeFam; TF315022; -. DR Proteomes; UP000007303; Unassembled WGS sequence. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR CDD; cd01878; HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000007303}; KW Reference proteome {ECO:0000313|Proteomes:UP000007303}. FT DOMAIN 222 386 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 444 AA; 49370 MW; 3641BC664C40C9BE CRC64; DSEVEELFQQ RGAAGVGQGQ QRLVIVHPDV KWGSRKQHLT TAELMLAEAV GLVNTLDNWT VVDTVVLSTK TPEKKRIFGK GNFQSLTEKI RQTAGITAVF VNVEHLSPLS ERELEEAWGV KVLDRYSVVL HIFRCNARTK EAKLQISLAE IPLLRRSRLK NEIANLDQQG GRSKYIGGSG ETLLEVQQRL LKEREMKIRT ALEKLRRKRH LLRAQRKQQE FPMVSVLGYT NSGKTTLIKS LTGDSGLQPK NQLFATLDVT VHAGQLPNHM TVLYVDTIGF LSQLPHRLID SFSATLEDIK HSDLLLHVRD VSHPETLNQK ANVLNVLKNL QIPDRLIGSM IEVHNKIDLV DSYQFTDPRA LPVSALGGRG LDRLKEAVEA EIVAATGKHT LALPVDLSSP QLSWLYKEAA VQDLEVNADD GSAVVKVVIS AAAYGRYKKL FSGG // ID H3KFT3_9BURK Unreviewed; 396 AA. AC H3KFT3; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 07-JUN-2017, entry version 34. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=HMPREF9440_01602 {ECO:0000313|EMBL:EHY31022.1}; OS Sutterella parvirubra YIT 11816. OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Sutterellaceae; Sutterella. OX NCBI_TaxID=762967 {ECO:0000313|EMBL:EHY31022.1, ECO:0000313|Proteomes:UP000004956}; RN [1] {ECO:0000313|EMBL:EHY31022.1, ECO:0000313|Proteomes:UP000004956} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=YIT 11816 {ECO:0000313|EMBL:EHY31022.1, RC ECO:0000313|Proteomes:UP000004956}; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Hou S., Chen J., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Zhang X., Suruliraj S., Warren W., Chinwalla A., RA Mardis E.R., Wilson R.K.; RL Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EHY31022.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFBQ01000242; EHY31022.1; -; Genomic_DNA. DR RefSeq; WP_008542638.1; NZ_JH604985.1. DR EnsemblBacteria; EHY31022; EHY31022; HMPREF9440_01602. DR PATRIC; fig|762967.3.peg.1257; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000004956; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000004956}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000004956}. FT DOMAIN 194 359 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 396 AA; 44612 MW; 8CE0B389E52A4D8B CRC64; MKASRAFLVC VTIGRVRYAD SAEELRLLVT SDGLEPCGLL EARREKPDPA TFLGSGKIEE LGELAREAKA DVVVFDTALS AAQQRNIERA IELPVLDRTT LILEIFRARA KSREGRLQVE LARLEHLSTR LVRGWTHLER QRGGLGKTGG PGEKQIELDR RMIGVRVKQL REQLKKLARQ RGTQRRARTR GDTLTVSLVG YTNAGKSTLF NRLTRAKSYA ADQLFATLDT TARRFWVNDE ETVVASDTVG FIRGLPHQLV EAFKSTLDET VHADLLLHVV DAASPVREEQ IREVNLVLEE IEADDVPVII VYNKIDRTTH EPEIVRHPDG TPKAVFVSAL TGAGMDLLRE AVAEFSGRWR EEHPNEPREP EPWEEELEAE RRMTPEEELK ALEALL // ID H3NEX9_9LACT Unreviewed; 415 AA. AC H3NEX9; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 07-JUN-2017, entry version 32. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=HMPREF9703_01110 {ECO:0000313|EMBL:EHR32994.1}; OS Dolosigranulum pigrum ATCC 51524. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Carnobacteriaceae; OC Dolosigranulum. OX NCBI_TaxID=883103 {ECO:0000313|EMBL:EHR32994.1, ECO:0000313|Proteomes:UP000003599}; RN [1] {ECO:0000313|EMBL:EHR32994.1, ECO:0000313|Proteomes:UP000003599} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51524 {ECO:0000313|EMBL:EHR32994.1, RC ECO:0000313|Proteomes:UP000003599}; RG The Broad Institute Genome Sequencing Platform; RA Earl A., Ward D., Feldgarden M., Gevers D., Huys G., Young S.K., RA Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., RA Alvarado L., Arachchi H.M., Berlin A., Chapman S.B., Gearin G., RA Goldberg J., Griggs A., Gujja S., Hansen M., Heiman D., Howarth C., RA Larimer J., Lui A., MacDonald P.J.P., McCowen C., Montmayeur A., RA Murphy C., Neiman D., Pearson M., Priest M., Roberts A., Saif S., RA Shea T., Sisk P., Stolte C., Sykes S., Wortman J., Nusbaum C., RA Birren B.; RT "The Genome Sequence of Dolosigranulum pigrum ATCC 51524."; RL Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EHR32994.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGEF01000009; EHR32994.1; -; Genomic_DNA. DR RefSeq; WP_004636281.1; NZ_JH601103.1. DR EnsemblBacteria; EHR32994; EHR32994; HMPREF9703_01110. DR PATRIC; fig|883103.3.peg.1081; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000003599; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000003599}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000003599}. FT DOMAIN 199 361 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 415 AA; 46814 MW; 70A73412738AC9DA CRC64; MKKKQQYEQV ILVGVQTKES DDQFRESLNE LQALVENAGG EVVGELTQKR DQIDTKTFIG SGKLIELSHL TDELAASTVV FNQQLSPSHT RNIQEVVDAK VIDRTQVILD IFALRARSKE GQLQVQLAQL EYMLPRLVGQ GENMSRLGAG IGTRGPGESK LETDRRHITA QMTDIRRELQ KITDHRQRNR QHRSESGVIQ IGLIGYTNAG KSTVLNALTD AGTYEADALF ATLDPLTREL ELPSGAQATM TDTVGFIQDL PTTLIEAFKS TIEEARGADM LLHVIDAAQP NIQTRERTVR ELLEQLEMDD IPVLYVYNKA DMIEDVNFTA ESYPSVVISA RREEDANYIL REIEAFLQEE FVYYEAQIEP SRGDILARLR QETIMTEQAF NEEARQYDVA GYTKPEGYWD TQLNG // ID H3NHT3_9LACT Unreviewed; 410 AA. AC H3NHT3; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 07-JUN-2017, entry version 34. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=HMPREF9708_00361 {ECO:0000313|EMBL:EHR37732.1}; OS Facklamia languida CCUG 37842. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Aerococcaceae; OC Facklamia. OX NCBI_TaxID=883113 {ECO:0000313|EMBL:EHR37732.1, ECO:0000313|Proteomes:UP000006190}; RN [1] {ECO:0000313|EMBL:EHR37732.1, ECO:0000313|Proteomes:UP000006190} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CCUG 37842 {ECO:0000313|EMBL:EHR37732.1, RC ECO:0000313|Proteomes:UP000006190}; RG The Broad Institute Genome Sequencing Platform; RA Earl A., Ward D., Feldgarden M., Gevers D., Huys G., Young S.K., RA Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., RA Alvarado L., Arachchi H.M., Berlin A., Chapman S.B., Gearin G., RA Goldberg J., Griggs A., Gujja S., Hansen M., Heiman D., Howarth C., RA Larimer J., Lui A., MacDonald P.J.P., McCowen C., Montmayeur A., RA Murphy C., Neiman D., Pearson M., Priest M., Roberts A., Saif S., RA Shea T., Sisk P., Stolte C., Sykes S., Wortman J., Nusbaum C., RA Birren B.; RT "The Genome Sequence of Facklamia languida CCUG 37842."; RL Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EHR37732.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGEG01000003; EHR37732.1; -; Genomic_DNA. DR RefSeq; WP_006308307.1; NZ_JH601133.1. DR EnsemblBacteria; EHR37732; EHR37732; HMPREF9708_00361. DR PATRIC; fig|883113.3.peg.365; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000006190; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000006190}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000006190}. FT DOMAIN 201 362 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 410 AA; 47189 MW; E227D28A7E4770C9 CRC64; MIEVDAGVER VMIVGVQTDR YEEDQFEEMM QEMVDLAQTA QGKVVCQVRQ KLPHLDHRYA VGPGKLEEIK LALDHHRIDL VIFFNPLSPS MNRSIETVLQ VRVIDRVQLI LDIFALRAKS MEGQLQVSLA QYEYLLPRIT GQGKMLSRLG GGIGTRGPGE TQLESDRRHI RSQITHIKRS LDDVANHRER TRSKRQRSRE FNIGLVGYTN AGKSTIMHQL TGTDTYVQDQ LFATLDPLTR QFSINGHPVF TLTDTVGFIE ELPTELIEAF KSTLEEIRYL DLLLHVVDAS NPAHTMHEET VLRILRDLEV DHLPILTVYN KSDCLNQPFN PTISPNVLIS AKNDQDMERL KEAIWRMCLE EAEEYSVRIR PEDADRIAIY QQRTLVTSLE FNEEENYYQV SGFRKLFIVD // ID H3NNL8_9FIRM Unreviewed; 421 AA. AC H3NNL8; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 07-JUN-2017, entry version 34. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=HMPREF9709_00929 {ECO:0000313|EMBL:EHR33993.1}; OS Helcococcus kunzii ATCC 51366. OC Bacteria; Firmicutes; Tissierellia; Tissierellales; Peptoniphilaceae; OC Helcococcus. OX NCBI_TaxID=883114 {ECO:0000313|EMBL:EHR33993.1, ECO:0000313|Proteomes:UP000004191}; RN [1] {ECO:0000313|EMBL:EHR33993.1, ECO:0000313|Proteomes:UP000004191} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51366 {ECO:0000313|EMBL:EHR33993.1, RC ECO:0000313|Proteomes:UP000004191}; RG The Broad Institute Genome Sequencing Platform; RA Earl A., Ward D., Feldgarden M., Gevers D., Huys G., Young S.K., RA Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., RA Alvarado L., Arachchi H.M., Berlin A., Chapman S.B., Gearin G., RA Goldberg J., Griggs A., Gujja S., Hansen M., Heiman D., Howarth C., RA Larimer J., Lui A., MacDonald P.J.P., McCowen C., Montmayeur A., RA Murphy C., Neiman D., Pearson M., Priest M., Roberts A., Saif S., RA Shea T., Sisk P., Stolte C., Sykes S., Wortman J., Nusbaum C., RA Birren B.; RT "The Genome Sequence of Helcococcus kunzii ATCC 51366."; RL Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EHR33993.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGEI01000021; EHR33993.1; -; Genomic_DNA. DR RefSeq; WP_005398375.1; NZ_JH601088.1. DR EnsemblBacteria; EHR33993; EHR33993; HMPREF9709_00929. DR PATRIC; fig|883114.3.peg.919; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000004191; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000004191}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000004191}. FT DOMAIN 197 365 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 421 AA; 48311 MW; 1087656FB1B9E90F CRC64; MDKEKIITVH LNNKGKYTEN QINAKIEEMK ELVRSSDSEF VASVVQNVKE INSKYYIGSG KAEEIKEMAE NLEVDTIIFD NELTGSQIKN LEDIIGKKIL DRTGLILDIF ATRAKTKEAK LQVKLAQLEY MLPRLVGYRN YLSREGAGVG TRGPGEQKLE TDRRAIQREI SSIKSKLTDI ERIRNVERSK RINSEIPIVS LIGYSNVGKS TILNSIGDMS SNNTKNVFAD NMLFATLDTS ARKVKLPNDR DIIITDTVGF VTDLPTKLVE SFKSTLEEIN YSDLLLIVVD ASNEDYEMQI DATKSVLKDM GIIGKDILYV FNKMDLNPDF VYYGGIDKEI YISARKEEDL DKLLNKIQEI LFKDFKIYRS FVPYTDLDII RDKVYIQYKD REKFTETGVE TYLYLNNSEL EKYRKYIIDG E // ID H3NVI6_9GAMM Unreviewed; 420 AA. AC H3NVI6; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 30-AUG-2017, entry version 32. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=OMB55_00000960 {ECO:0000313|EMBL:EHQ56391.1}; OS gamma proteobacterium HIMB55. OC Bacteria; Proteobacteria; Gammaproteobacteria; Cellvibrionales; OC Halieaceae. OX NCBI_TaxID=745014 {ECO:0000313|EMBL:EHQ56391.1, ECO:0000313|Proteomes:UP000003408}; RN [1] {ECO:0000313|EMBL:EHQ56391.1, ECO:0000313|Proteomes:UP000003408} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=HIMB55 {ECO:0000313|EMBL:EHQ56391.1, RC ECO:0000313|Proteomes:UP000003408}; RX PubMed=22493201; DOI=10.1128/JB.00171-12; RA Huggett M.J., Rappe M.S.; RT "Genome Sequence of Strain HIMB55, a Novel Marine Gammaproteobacterium RT of the OM60/NOR5 Clade."; RL J. Bacteriol. 194:2393-2394(2012). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EHQ56391.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGIF02000001; EHQ56391.1; -; Genomic_DNA. DR RefSeq; WP_009469914.1; NZ_AGIF02000001.1. DR EnsemblBacteria; EHQ56391; EHQ56391; OMB55_00000960. DR PATRIC; fig|745014.4.peg.94; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000003408; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000003408}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Hydrolase {ECO:0000313|EMBL:EHQ56391.1}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000003408}. FT DOMAIN 199 365 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 420 AA; 46178 MW; 7ACFC9F453209B73 CRC64; MFFELHSGGE RAVLVQIAID GSANEPDLGE FIELVRSAGG EPAAVVRGSR RSPTAKYFVG EGKLEEIAEE VASAEAELVV FNHALSPSQE RNLEAYLKCR VIARTGLILD IFAQRARTHE GKLQVELAQL KHISTRLIRG WTHLERQKGG IGLRGPGETQ LETDRRLLRA RVSAIESRLD KVRQQRAQNR RARQRAEVPL VSLVGYTNAG KSTLFNTWSE SGVYAADQLF ATLDPTLARV EIEGLGGVII ADTVGFIADL PHTLVEAFRA TLEETLNASL LIHVIDVAAD DREFLKSEVE SVLDEIGAGD IPQLIVYNKI DLLEREPRIT RDSDGRPDTV SVSAKTGAGL DLLRDAIGER LAGQFFTGFV ELSPMQGKLR AALYELGAIQ SEEWLDNGSS SVSLHLPDSD WTRLKQQHGF // ID H3SBP0_9BACL Unreviewed; 427 AA. AC H3SBP0; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 07-JUN-2017, entry version 33. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=PDENDC454_04631 {ECO:0000313|EMBL:EHQ63404.1}; OS Paenibacillus dendritiformis C454. OC Bacteria; Firmicutes; Bacilli; Bacillales; Paenibacillaceae; OC Paenibacillus. OX NCBI_TaxID=1131935 {ECO:0000313|EMBL:EHQ63404.1, ECO:0000313|Proteomes:UP000003900}; RN [1] {ECO:0000313|EMBL:EHQ63404.1, ECO:0000313|Proteomes:UP000003900} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C454 {ECO:0000313|EMBL:EHQ63404.1, RC ECO:0000313|Proteomes:UP000003900}; RX PubMed=22461558; DOI=10.1128/JB.00158-12; RA Sirota-Madi A., Olender T., Helman Y., Brainis I., Finkelshtein A., RA Roth D., Hagai E., Leshkowitz D., Brodsky L., Galatenko V., RA Nikolaev V., Gutnick D.L., Lancet D., Ben-Jacob E.; RT "Genome Sequence of the Pattern-Forming Social Bacterium Paenibacillus RT dendritiformis C454 Chiral Morphotype."; RL J. Bacteriol. 194:2127-2128(2012). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EHQ63404.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AHKH01000008; EHQ63404.1; -; Genomic_DNA. DR RefSeq; WP_006675440.1; NZ_AHKH01000008.1. DR EnsemblBacteria; EHQ63404; EHQ63404; PDENDC454_04631. DR PATRIC; fig|1131935.3.peg.919; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000003900; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000003900}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000003900}. FT DOMAIN 208 372 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 427 AA; 48195 MW; 4FA57B27D7F6CD89 CRC64; MRRTFYETSS DIQDRAVLVT LITDEVRRSR LRPEDSLQEL VQLAETAGVA VLSVMMQQRE NADSKWFIGK GKVAELGAVI AELDATTAIF DQELSGAQVR NLEEALDVKI IDRTQLILDI FAQRAKTREG IIQVELAQLS YLLPRLSGHG RNLSRLGGGI GTRGPGETKL ETDRRHIRRR ISDLKRQLQE VVRHRGVYRE RRKKSGAIQV ALVGYTNAGK STLLRQLTEA DVYVENQLFA TLDPTSRQWE LPNGKSTILT DTVGFIQHLP HELVASFRAT LEEVNEADLI LHVVDASSLM REEQMRVVDD ILQQLGAGAK PQIVLYNKKD MCIEEQRHML PLDESHFLIS AYDEADLEQV RLAVQQHLSG RTVTYRLPGA RGDLIALAHR IGEVLEQEAD GEDVRLTVRL DRAEAELHSY KLEPYLS // ID H3SHM6_9BACL Unreviewed; 424 AA. AC H3SHM6; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 07-JUN-2017, entry version 32. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=PDENDC454_15217 {ECO:0000313|EMBL:EHQ61418.1}; OS Paenibacillus dendritiformis C454. OC Bacteria; Firmicutes; Bacilli; Bacillales; Paenibacillaceae; OC Paenibacillus. OX NCBI_TaxID=1131935 {ECO:0000313|EMBL:EHQ61418.1, ECO:0000313|Proteomes:UP000003900}; RN [1] {ECO:0000313|EMBL:EHQ61418.1, ECO:0000313|Proteomes:UP000003900} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C454 {ECO:0000313|EMBL:EHQ61418.1, RC ECO:0000313|Proteomes:UP000003900}; RX PubMed=22461558; DOI=10.1128/JB.00158-12; RA Sirota-Madi A., Olender T., Helman Y., Brainis I., Finkelshtein A., RA Roth D., Hagai E., Leshkowitz D., Brodsky L., Galatenko V., RA Nikolaev V., Gutnick D.L., Lancet D., Ben-Jacob E.; RT "Genome Sequence of the Pattern-Forming Social Bacterium Paenibacillus RT dendritiformis C454 Chiral Morphotype."; RL J. Bacteriol. 194:2127-2128(2012). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EHQ61418.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AHKH01000038; EHQ61418.1; -; Genomic_DNA. DR RefSeq; WP_006677537.1; NZ_AHKH01000038.1. DR EnsemblBacteria; EHQ61418; EHQ61418; PDENDC454_15217. DR PATRIC; fig|1131935.3.peg.3162; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000003900; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000003900}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000003900}. FT DOMAIN 201 369 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 160 187 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 424 AA; 47981 MW; F7C562ED91D584DE CRC64; MEQLTIQPQK AVLAGVNLNH QTDFDYSMEE LANLAAACGV EVVGVVTQNL SKVNTTHYIG TGKLQDVTIM LNQHEADMVI FNDELSPSQL RNLEKDLDCK VVDRTLLILD IFGERAKTKE AQLQVEVAEL QYMLPRLVGL RESLGRQSGG VGTKNRGAGE KKLELDRRRI EERITALNKE LEILVAHRQT QRKKRKKTEL PVVSLVGYTN AGKSTVMNTL VELFTDSKDK FVFEKDMLFA TLDTSVRSID LEDNKTFLLT DTVGFVSKLP HHLVKAFRST LEEVKEADLL VHVVDFSNPE YEQHIRITNE TLKAIGIEGI PMIYAYNKID LKEGAIPESQ DSIIYMAAKR KQGIDELLAA IRAHVFKDYV KCEMLIPYDQ GQHVSYLNEH ANVLATEYEE LGTKLTLECR QSDYQKFAQY VCEA // ID H3ZKP3_THELN Unreviewed; 424 AA. AC H3ZKP3; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 07-JUN-2017, entry version 36. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=OCC_08305 {ECO:0000313|EMBL:EHR79475.1}; OS Thermococcus litoralis (strain ATCC 51850 / DSM 5473 / JCM 8560 / OS NS-C). OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae; OC Thermococcus. OX NCBI_TaxID=523849 {ECO:0000313|EMBL:EHR79475.1, ECO:0000313|Proteomes:UP000015502}; RN [1] {ECO:0000313|EMBL:EHR79475.1, ECO:0000313|Proteomes:UP000015502} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51850 / DSM 5473 / JCM 8560 / NS-C RC {ECO:0000313|Proteomes:UP000015502}; RX PubMed=22493191; DOI=10.1128/JB.00123-12; RA Gardner A.F., Kumar S., Perler F.B.; RT "Genome sequence of the model hyperthermophilic archaeon Thermococcus RT litoralis NS-C."; RL J. Bacteriol. 194:2375-2376(2012). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP006670; EHR79475.1; -; Genomic_DNA. DR RefSeq; WP_004066779.1; NC_022084.1. DR EnsemblBacteria; EHR79475; EHR79475; OCC_08305. DR GeneID; 16550758; -. DR KEGG; tlt:OCC_08305; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG093Z07D6; -. DR Proteomes; UP000015502; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000015502}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}. FT DOMAIN 186 362 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 424 AA; 48665 MW; 1A00D116D7A9F326 CRC64; MRAIGVIRHS PNRRVNKEEF EELLRSAGYE ILAIVEQTRE EHPKYNIGPG KLQEVKELIK ELNPDRIIFA NPLTPSQSFN ITKELKIDVI DKWQLVLEIF EKRAHSKEAK LQVELANLQY ELPLVKEAIR RIKLGDRAGF KGMGEYQTQQ YLKHIRYRMG KIRKELEKVK ADREVKRKRR EEVGFILVAL AGYTNAGKST LLNALADENI EAKTQMFTTL DTTTRRFTIN GKRALITDTV GFIDDLPPFI VEAFHSTLEE IVRADIVLLV LDSSEPWREI KRKFLASIEV LKELKALDKP ILVVLNKKDL TSEEELSDKK KAIEELISRK GITVSGIASI SAKERDLKEL YTALEEVMFT LPKYRLFEIL VKEREKVPKV IALINSIGEI LDVKYGETTR ISAYIQVGMI KSLTKMGVEL KHPS // ID H4F8M9_9RHIZ Unreviewed; 444 AA. AC H4F8M9; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 07-JUN-2017, entry version 31. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=PDO_2258 {ECO:0000313|EMBL:EHS50873.1}; OS Rhizobium sp. PDO1-076. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium. OX NCBI_TaxID=1125979 {ECO:0000313|EMBL:EHS50873.1, ECO:0000313|Proteomes:UP000017669}; RN [1] {ECO:0000313|EMBL:EHS50873.1, ECO:0000313|Proteomes:UP000017669} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=PDO-076 {ECO:0000313|EMBL:EHS50873.1, RC ECO:0000313|Proteomes:UP000017669}; RX PubMed=22493196; DOI=10.1128/JB.00198-12; RA Brown S.D., Klingeman D.M., Lu T.Y., Johnson C.M., Utturkar S.M., RA Land M.L., Schadt C.W., Doktycz M.J., Pelletier D.A.; RT "Draft Genome Sequence of Rhizobium sp. Strain PDO1-076, a Bacterium RT Isolated from Populus deltoides."; RL J. Bacteriol. 194:2383-2384(2012). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EHS50873.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AHZC01000321; EHS50873.1; -; Genomic_DNA. DR RefSeq; WP_007604045.1; NZ_AHZC01000321.1. DR EnsemblBacteria; EHS50873; EHS50873; PDO_2258. DR PATRIC; fig|1125979.3.peg.3130; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000017669; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000017669}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000017669}. FT DOMAIN 206 378 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 165 199 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 444 AA; 49373 MW; F632EAABBC19DAB7 CRC64; MRAVVLVPVL KHGRQPVLPE GPPPAPSRSN EARLEEAMGL ARAIDLTIAA GMIVPVNQPR PATLLGSGKI EEVTAMLDER DAGLVIVDHP LTPVQQRNLE KEWNAKVIDR TGLILEIFGR RASTKEGTLQ VELAHLNYQK GRLVRSWTHL ERQRGGAGFM GGPGETQIEA DRRMLQDRIV KLEKELEQVV RTRQLHRAKR RKVPHPIVAL VGYTNAGKST LFNRITGAGV LAEDMLFATL DPTLRRMKLP HGRTVILSDT VGFISNLPTH LVAAFRATLE EVLEADLILH VRDMADPDNG AQSADVLRIL DDLGIDEKER SERIIEIWNK IDRLDPETHD AIMQKAKGRE NVMSVSAITG EGVDRLLDVI SQRLSGVLTE ATITIPADKH ALISWAYENA VVTGREDHED GSVSLDVRLT ERQADEMERK LGSGQKPDKE DWER // ID H4GJK6_9LACO Unreviewed; 425 AA. AC H4GJK6; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 07-JUN-2017, entry version 33. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=PS3_6496 {ECO:0000313|EMBL:EHS86516.1}; OS Lactobacillus gastricus PS3. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; OC Lactobacillus. OX NCBI_TaxID=1144300 {ECO:0000313|EMBL:EHS86516.1, ECO:0000313|Proteomes:UP000004567}; RN [1] {ECO:0000313|EMBL:EHS86516.1, ECO:0000313|Proteomes:UP000004567} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=PS3 {ECO:0000313|EMBL:EHS86516.1, RC ECO:0000313|Proteomes:UP000004567}; RX PubMed=23846278; RA Martin V., Cardenas N., Jimenez E., Maldonado A., Rodriguez J.M., RA Fernandez L.; RT "Genome Sequence of Lactobacillus gastricus PS3, a Strain Isolated RT from Human Milk."; RL Genome Announc. 1:E00489-13(2013). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EHS86516.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AICN01000042; EHS86516.1; -; Genomic_DNA. DR RefSeq; WP_007122239.1; NZ_AICN01000042.1. DR EnsemblBacteria; EHS86516; EHS86516; PS3_6496. DR PATRIC; fig|1144300.3.peg.980; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000004567; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000004567}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000004567}. FT DOMAIN 202 371 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 425 AA; 47824 MW; A1B43A35AE473428 CRC64; METTKPNLDQ IIIIGLDTGQ SNFDYTMNEL VELAKANNMQ VLDRLDQALD RPNAATYFGK GKVEELANLT AALKATTIVA NDELSPSQIK NLTDATKTRV IDRTALILEI FAQRAQSREA KIQVEIAQLQ YRLPRLRTAN NITLDQQSGG GAGMSNRGAG ETQMEMDRRV IQRHISHLRN ELKEIQKSED TKRSQRDKSA IPTAALVGYT NAGKSTIMNQ LVERYGVSVD KQVFEKDMLF ATLDTSVRQL TLKDQKRFLL SDTVGFVSKL PTQLVEAFKS TLAEAANADL LIQVIDYSDP HYEEMIKTTE STLHQIGIED IPMVYVFNKA DRTAVEYPVM EGEDRIVISA KDAASIDLLE QIIRQHLFKD YQTATLLVPF AEGNVVSYLN EHTNILETTY EEAGTRLKVE LSSEDLHRFE NYLTE // ID H5TC32_9ALTE Unreviewed; 427 AA. AC H5TC32; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 30-AUG-2017, entry version 33. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=GPUN_1743 {ECO:0000313|EMBL:GAB55859.1}; OS Glaciecola punicea ACAM 611. OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales; OC Alteromonadaceae; Glaciecola. OX NCBI_TaxID=1121923 {ECO:0000313|EMBL:GAB55859.1, ECO:0000313|Proteomes:UP000053586}; RN [1] {ECO:0000313|EMBL:GAB55859.1, ECO:0000313|Proteomes:UP000053586} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ACAM 611 {ECO:0000313|EMBL:GAB55859.1, RC ECO:0000313|Proteomes:UP000053586}; RX PubMed=22628500; DOI=10.1128/JB.00463-12; RA Qin Q.-L., Xie B.-B., Shu Y.-L., Rong J.-C., Zhao D.-L., Zhang X.-Y., RA Chen X.-L., Zhou B.-C., Zhanga Y.-Z.; RT "Genome sequence of proteorhodopsin-containing sea ice bacterium RT Glaciecola punicea ACAM 611T."; RL J. Bacteriol. 194:3267-3267(2012). RN [2] {ECO:0000313|EMBL:GAB55859.1, ECO:0000313|Proteomes:UP000053586} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ACAM 611 {ECO:0000313|EMBL:GAB55859.1, RC ECO:0000313|Proteomes:UP000053586}; RX PubMed=25009843; RA Qin Q.-L., Xie B.-B., Yu Y., Shu Y.-L., Rong J.-C., Zhang Y.-J., RA Zhao D.-L., Chen X.-L., Zhang X.-Y., Chen B., Zhou B.-C., Zhang Y.-Z.; RT "Comparative genomics of the marine bacterial genus Glaciecola reveals RT the high degree of genomic diversity and genomic characteristic for RT cold adaptation."; RL Environ. Microbiol. 16:1642-1653(2014). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:GAB55859.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BAET01000018; GAB55859.1; -; Genomic_DNA. DR RefSeq; WP_006005395.1; NZ_BAET01000018.1. DR EnsemblBacteria; GAB55859; GAB55859; GPUN_1743. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000053586; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000053586}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000053586}. FT DOMAIN 198 365 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 427 AA; 47990 MW; AED1EAE99A3F8067 CRC64; MFDRYEGGEQ AVLVHIDFSD EQNKEDIDEL QLLVSSAGVN NVGIVTASRK APHAKFFVGT GKAQEIADTV AALCADLVIF NHALSPSQER NLEKLCLCRV LDRTSLILDI FAQRARTHEG KLQVELAQLR HISTRLIRGW THLERQKGGI GLRGPGETQL ETDRRLLRGR LKTILKRLDK VQKQREQGRR SRKRAEIPTV SLVGYTNAGK STLFNTITDA GVYAADQLFA TLDPTLRKIE LQEVGQAILA DTVGFIRHLP HDLVAAFKAT LQETQEATLL LHVVDYADEQ YAENMGQVND VLKEIEADEV PQLIICNKID RLDGVVPKID RDDEGRPTRV WVSAQNGTGI DLLKQALTEC LRQEMVNYTL AVPAGDGKIR GMLYELNCIN EQEYSDTGDW IVSITMMASD WHRMDKKVDN RLSHYII // ID H5TYP4_9ACTN Unreviewed; 523 AA. AC H5TYP4; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 12-APR-2017, entry version 29. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:GAB38602.1}; GN ORFNames=GOSPT_046_00680 {ECO:0000313|EMBL:GAB38602.1}; OS Gordonia sputi NBRC 100414. OC Bacteria; Actinobacteria; Corynebacteriales; Gordoniaceae; Gordonia. OX NCBI_TaxID=1089453 {ECO:0000313|EMBL:GAB38602.1, ECO:0000313|Proteomes:UP000005845}; RN [1] {ECO:0000313|EMBL:GAB38602.1, ECO:0000313|Proteomes:UP000005845} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NBRC 100414 {ECO:0000313|EMBL:GAB38602.1, RC ECO:0000313|Proteomes:UP000005845}; RA Yoshida I., Hosoyama A., Tsuchikane K., Katsumata H., Yamazaki S., RA Fujita N.; RT "Whole genome shotgun sequence of Gordonia sputi NBRC 100414."; RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:GAB38602.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BAFC01000046; GAB38602.1; -; Genomic_DNA. DR EnsemblBacteria; GAB38602; GAB38602; GOSPT_046_00680. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000005845; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000005845}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000005845}. FT DOMAIN 290 470 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 249 276 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 523 AA; 56326 MW; 78765174182F87AB CRC64; MTETSPQVHD LHDTRPVDAN APAIDLSRDL IDPDDLVDPA DFGDHDDSRD RAHTPTTGEL ALSDRASLQR VAGLSTELTD VTEVEYRQLR LERVVLVGVW TEGTAAAAKA NMEELAALAE TAGSVVLEAV IQRRSSPDPA TFIGSGKAQE LRDVVADTGA DTVICDGELT PAQLTALEKV VKVKVIDRTA LILDIFAQHA SSREGKAQVA LAQMEYMLPR LRGWGESMSR QAGGRAGSNG GVGLRGPGET KIETDRRRIR ERMAKLRREI REMRTARTTK RSARLRGAVP RIAVAGYTNA GKSSLVNAMT GSGVLVQDAL FATLDPTTRR ATLEDGRELV FTDTVGFVRH LPTQLVEAFR STLEEVVDAD LVLHVVDGSD PFPAEQITAV RRVINDVVAE EGVAPPPELL VINKIDAIDA SRLTELRGML GAGGSTHGPN SAGVVYVSAR TGEGLPELFE AVREFVGRDD VELTVDIPFT RGDLVSRIHR EGEVLATDHS TEGTRMRVRV PSALAGELAS LAQ // ID H5UNU2_9MICO Unreviewed; 493 AA. AC H5UNU2; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 07-JUN-2017, entry version 32. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:GAB47400.1}; GN ORFNames=MOPEL_009_00910 {ECO:0000313|EMBL:GAB47400.1}; OS Mobilicoccus pelagius NBRC 104925. OC Bacteria; Actinobacteria; Micrococcales; Dermatophilaceae; OC Mobilicoccus. OX NCBI_TaxID=1089455 {ECO:0000313|EMBL:GAB47400.1, ECO:0000313|Proteomes:UP000004367}; RN [1] {ECO:0000313|EMBL:GAB47400.1, ECO:0000313|Proteomes:UP000004367} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NBRC 104925 {ECO:0000313|EMBL:GAB47400.1, RC ECO:0000313|Proteomes:UP000004367}; RA Yoshida Y., Hosoyama A., Tsuchikane K., Katsumata H., Yamazaki S., RA Fujita N.; RT "Whole genome shotgun sequence of Mobilicoccus pelagius NBRC 104925."; RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:GAB47400.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BAFE01000009; GAB47400.1; -; Genomic_DNA. DR RefSeq; WP_009481298.1; NZ_BAFE01000009.1. DR EnsemblBacteria; GAB47400; GAB47400; MOPEL_009_00910. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000004367; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 2. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000004367}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000004367}. FT DOMAIN 271 439 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 230 257 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 493 AA; 54309 MW; 395E45ADD73C5519 CRC64; MTNHTERTSA DILSGRASAL SDSDDWHLAD PDFTSYDGDQ FEREERAAMR RVQGLSTELE DVTEVEYRQL RLERVVLVGV WSEGTLEEAE NSLRELAALA ETAGSTVLAG VVQRRYRPDP ATYVGSGKAE ELRDIVVAEG ADTVVADSQL APNQRRALED VVKVKVIDRT ALILDIFAQH AKSKEGKAQV ELAQLQYLLP RLRGWGESMS RQAGGQVSGG AGMGSRGPGE TKIELDRRRI NQRMAKLRRE IKEMKTVRDT KRSGRRANHV PAVAIAGYTN AGKSSLLNRI TGAGALVENA LFATLDPTIR RAETPDGREF TIADTVGFVR SLPHELVEAF RSTLEEVADA DLLLHVVDGS HPDPEGQITA VRQVLADVWD DPNDQPKEVV VVNKADIADP EVVDRILRHE KYSIAVSARS GAGIEELRAL IADELPHQDV ELTLLVPYGR GDVVNTLHSV ADVLSEEHLP EGTRLHVRVF SHQAETFREF VPQ // ID H5UZB7_ATLHE Unreviewed; 426 AA. AC H5UZB7; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 30-AUG-2017, entry version 34. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:GAB51075.1}; GN ORFNames=EH105704_02_01040 {ECO:0000313|EMBL:GAB51075.1}; OS Atlantibacter hermannii NBRC 105704. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; OC Enterobacteriaceae; Atlantibacter. OX NCBI_TaxID=1115512 {ECO:0000313|EMBL:GAB51075.1, ECO:0000313|Proteomes:UP000010297}; RN [1] {ECO:0000313|EMBL:GAB51075.1, ECO:0000313|Proteomes:UP000010297} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NBRC 105704 {ECO:0000313|EMBL:GAB51075.1, RC ECO:0000313|Proteomes:UP000010297}; RA Yoshida I., Hosoyama A., Tsuchikane K., Katsumata H., Yamazaki S., RA Fujita N.; RT "Whole genome shotgun sequence of Escherichia hermannii NBRC 105704."; RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:GAB51075.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BAFF01000002; GAB51075.1; -; Genomic_DNA. DR RefSeq; WP_002434123.1; NZ_BAFF01000002.1. DR EnsemblBacteria; GAB51075; GAB51075; EH105704_02_01040. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000010297; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000010297}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000010297}. FT DOMAIN 198 365 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 426 AA; 47986 MW; 4271F5409AE480D6 CRC64; MFDRYDAGEQ AVLVHIYFSQ DKDMEDLQEF DSLVSSAGVE ALQVITGSRK APHPKYFVGE GKAVEIADAV KATGASVVLF DHALTPAQER NLERLCECRV IDRTGLILDI FAQRARTHEG KLQVELAQLR HLATRLVRGW THLERQKGGI GLRGPGETQL ETDRRLLRNR ITLILSRLEK VEKQREQGRR SRSKADIPTV SLVGYTNAGK STLFNQITEA QVYAADQLFA TLDPTLRRID VADVGETVLA DTVGFIRHLP HDLVAAFKAT LQETRQATLL LHVVDAADVR MQENIDAVNT VLEEIEADEI PTLLVMNKID ALDGFQPRID RDDENKPIRV WLSAQTGDGV PLLFQALTER LSGEIAQHTL RLPPEAGRLR SRFYQLQAIE KEWMEEDGSV GMDVRMPIVD WRRLCKQEPT LVDYVV // ID H5WIF1_9BURK Unreviewed; 407 AA. AC H5WIF1; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 12-APR-2017, entry version 28. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=BurJ1DRAFT_2950 {ECO:0000313|EMBL:EHR71771.1}; OS Burkholderiales bacterium JOSHI_001. OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales. OX NCBI_TaxID=864051 {ECO:0000313|EMBL:EHR71771.1, ECO:0000313|Proteomes:UP000004674}; RN [1] {ECO:0000313|EMBL:EHR71771.1, ECO:0000313|Proteomes:UP000004674} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=JOSHI_001 {ECO:0000313|EMBL:EHR71771.1, RC ECO:0000313|Proteomes:UP000004674}; RG US DOE Joint Genome Institute; RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S., RA Peters L., Mikhailova N., Zeytun A., Lu M., Detter J.C., Han C., RA Tapia R., Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., RA Smith J., Lewis G., Woyke T.; RT "Noncontiguous Finished sequence of Burkholderiales bacterium RT JOSHI_001."; RL Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CM001438; EHR71771.1; -; Genomic_DNA. DR EnsemblBacteria; EHR71771; EHR71771; BurJ1DRAFT_2950. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000004674; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000004674}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000004674}. FT DOMAIN 211 383 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 407 AA; 44431 MW; DDFC2DCEAB91EB17 CRC64; MSRKPDEAAD DADATAGAPP RAVLVGVDFG PGSPFDPTLD ELALLAESAG DVPVARVIAR RKAPDPALFV GSGKADEIKE LVLVHQAHGV VFDQALSPAQ QRNLERHLGV PVADRTALIL EIFARRAQSH EGKLQVELAR LQYLSTRLVR RWSHLERQRG GVGHRGGPGE AQIELDRRMI GERIKSLKAR LVKVQRQRGT QRKARERSGT FRVSLVGYTN AGKSTLFNAL VKARAYAADQ LFATLDTTTR SLYLEELGGS VSLSDTVGFI RDLPHRLVEA FKATLQEAVD ADLLLHVVDA SSPLLHEQRD EVERVLFEIG AQDIPQLLVF NKLDQIDPPP RDSLDWVERG PGQPVPRVYV SALRGQGLDT LRAVIARAAR GEPLIPGKPV PIDAQPTDVH ALEVPGP // ID H5X0U6_9PSEU Unreviewed; 487 AA. AC H5X0U6; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 07-JUN-2017, entry version 34. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=SacmaDRAFT_3733 {ECO:0000313|EMBL:EHR51946.1}; OS Saccharomonospora marina XMU15. OC Bacteria; Actinobacteria; Pseudonocardiales; Pseudonocardiaceae; OC Saccharomonospora. OX NCBI_TaxID=882083 {ECO:0000313|EMBL:EHR51946.1, ECO:0000313|Proteomes:UP000004926}; RN [1] {ECO:0000313|EMBL:EHR51946.1, ECO:0000313|Proteomes:UP000004926} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=XMU15 {ECO:0000313|EMBL:EHR51946.1}; RX PubMed=22768369; DOI=10.4056/sigs.2655905; RA Klenk H.P., Lu M., Lucas S., Lapidus A., Copeland A., Pitluck S., RA Goodwin L.A., Han C., Tapia R., Brambilla E.M., Potter G., Land M., RA Ivanova N., Rohde M., Goker M., Detter J.C., Li W.J., Kyrpides N.C., RA Woyke T.; RT "Genome sequence of the ocean sediment bacterium Saccharomonospora RT marina type strain (XMU15(T))."; RL Stand. Genomic Sci. 6:265-275(2012). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CM001439; EHR51946.1; -; Genomic_DNA. DR RefSeq; WP_009155328.1; NZ_CM001439.1. DR EnsemblBacteria; EHR51946; EHR51946; SacmaDRAFT_3733. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000004926; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 2. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000004926}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000004926}. FT DOMAIN 260 429 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 487 AA; 52304 MW; 445A7BE10913C5F3 CRC64; MTEPTHTSLG RLEEFDGLDT VADVSTGELE LEERASLRRV AGLSTELADI TEVEYRKLRL ERVVLVGVWT EGTAAQSQAS LAELARLAET AGSQVLEGLV QRRSRPDPAT YIGSGKVREL ADVVVATGAD TVICDGELSP GQLRQLEAKL KVKVIDRTAL ILDIFAQHAR SREGKAQVEL AQLQYLIPRL RGWGESLSRQ AGGRAGGANG GVGLRGPGET KLETDRRRIS KRVAKLRREI AAMDTIRATK RGRRLANEVP GVALVGYTNA GKSSLLNAMT GAGVLVEDAL FATLDPTTRR AMTPDGKAYT ITDTVGFVRH LPHQLVDAFR STLEEAADAD VLVHVVDGSA PAPEEQVGAV REVLGEIARH RGEPLPPELL VINKADAADE VTLTRLRHLM PDAVVVSANT GQGINVLVEE IAGRLPRPEA VVEVVVPYTR GELVARAHAD GEVLAEEHTP EGTRLRARVR PDLAAALEDY ITDGSAV // ID H5Y1J6_9FIRM Unreviewed; 419 AA. AC H5Y1J6; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 07-JUN-2017, entry version 32. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=DesyoDRAFT_0416 {ECO:0000313|EMBL:EHQ87609.1}; OS Desulfosporosinus youngiae DSM 17734. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Peptococcaceae; OC Desulfosporosinus. OX NCBI_TaxID=768710 {ECO:0000313|EMBL:EHQ87609.1, ECO:0000313|Proteomes:UP000005104}; RN [1] {ECO:0000313|EMBL:EHQ87609.1, ECO:0000313|Proteomes:UP000005104} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 17734 {ECO:0000313|EMBL:EHQ87609.1, RC ECO:0000313|Proteomes:UP000005104}; RG US DOE Joint Genome Institute (JGI-PGF); RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S., RA Peters L., Ovchinnikova G., Lu M., Land M.L., Hauser L., Pester M., RA Spring S., Ollivier B., Rattei T., Klenk H.-P., Wagner M., Loy A., RA Woyke T.J.; RT "The Noncontiguous Finished genome of Desulfosporosinus youngiae DSM RT 17734."; RL Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CM001441; EHQ87609.1; -; Genomic_DNA. DR RefSeq; WP_007778778.1; NZ_CM001441.1. DR EnsemblBacteria; EHQ87609; EHQ87609; DesyoDRAFT_0416. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000005104; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000005104}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000005104}. FT DOMAIN 197 365 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 156 190 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 419 AA; 47414 MW; 8942ABE1514FF96F CRC64; MRQKQKAILV GVNLNNQQDF TNSMKELSNL AEACEIEVVG EKSQNLNSVI KAYYIGKGKL QEVLALIQEK KADMVIFNDE LSPSQIRNLE ATLKCKVIDR TVLILDIFAQ RARTREAQLQ VEVAKLQYML PRLIGSGESL GRQGGGAGLK NRGSGETKLE LDRRKIEERI SSLNKELEIL VAQRQNQRKR RKKKEIPVIA LVGYTNTGKS TIMNVMLDLF NPTSEKQVFE KNMLFATLET SVRSIELPDN KTFLLTDTVG FISKLPHHLV KAFRSTLEEV AEADLLIHVV DYSNPFYKEQ IEVTKETLKE LGADNIPVIY AYNKTDLAEV EIPKGAEDNV YLSAKRKTGI DDLVGAIREK AFAHYVCCEM LIPYDKGKVV SYFNDNATIK STVYESNGVL ISMECKEADY ERYHQYCLV // ID H5Y4A1_9FIRM Unreviewed; 538 AA. AC H5Y4A1; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 07-JUN-2017, entry version 31. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=DesyoDRAFT_2881 {ECO:0000313|EMBL:EHQ89929.1}; OS Desulfosporosinus youngiae DSM 17734. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Peptococcaceae; OC Desulfosporosinus. OX NCBI_TaxID=768710 {ECO:0000313|EMBL:EHQ89929.1, ECO:0000313|Proteomes:UP000005104}; RN [1] {ECO:0000313|EMBL:EHQ89929.1, ECO:0000313|Proteomes:UP000005104} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 17734 {ECO:0000313|EMBL:EHQ89929.1, RC ECO:0000313|Proteomes:UP000005104}; RG US DOE Joint Genome Institute (JGI-PGF); RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S., RA Peters L., Ovchinnikova G., Lu M., Land M.L., Hauser L., Pester M., RA Spring S., Ollivier B., Rattei T., Klenk H.-P., Wagner M., Loy A., RA Woyke T.J.; RT "The Noncontiguous Finished genome of Desulfosporosinus youngiae DSM RT 17734."; RL Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CM001441; EHQ89929.1; -; Genomic_DNA. DR EnsemblBacteria; EHQ89929; EHQ89929; DesyoDRAFT_2881. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000005104; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000005104}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000005104}. FT DOMAIN 369 538 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 328 362 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 538 AA; 59990 MW; D0459DA8EC56619D CRC64; MIMDISGDLS GIRASQLQEL KNLSDLKTER SELIHPEILK ELIRLTQLWN REIAVYLSRS GTLLAAAVGR HAAVTLPPIK GRALGKHLRC IHTHPNGNYR LSPLDHSALA SLQLESMTSL GVGEGKLTGI QIAYRAGEGE PLIVNLSPQN WIEFDYTESL ACLSRSIPER PKTKTAQGKE QAFLIALVDN EQETNDDLLE LRELARTAGV DVVGQLVQLR RYGQSRSYFG SGKLEELVHR LQETDADVLI CDDELSPTQL RTLETETGLK VLDRTGLILD IFAQRAQSRE GKLQVELAQL KHLLPYLTGQ GQALSRLGGG VGTRGPGETK LELDRRRMRD RINQLEKELK LVLKHRDVQR RQRTRSGLPM VALVGYTNTG KTTFMKKAME QTGGRSDLPA GENKLFATLD PLVRGIRIDP SLEILLSDTV GFIRKLPTQL LRAFIATLEE VRQADVLIHV IDASHPQAFQ HAETVQEVLN QLECADKPML TLLNKVDKIR NEDDLNELAG YLPYPVKISL KRGDTLKPVW KILGSLLS // ID H6L5F3_SAPGL Unreviewed; 403 AA. AC H6L5F3; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 07-JUN-2017, entry version 33. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:AFC25169.1}; GN OrderedLocusNames=SGRA_2441 {ECO:0000313|EMBL:AFC25169.1}; OS Saprospira grandis (strain Lewin). OC Bacteria; Bacteroidetes; Saprospiria; Saprospirales; Saprospiraceae; OC Saprospira. OX NCBI_TaxID=984262 {ECO:0000313|EMBL:AFC25169.1, ECO:0000313|Proteomes:UP000007519}; RN [1] {ECO:0000313|EMBL:AFC25169.1, ECO:0000313|Proteomes:UP000007519} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Lewin {ECO:0000313|EMBL:AFC25169.1, RC ECO:0000313|Proteomes:UP000007519}; RX PubMed=22675601; DOI=10.4056/sigs.2445005; RA Saw J., Yuryev A., Kanbe M., Hou S., Young A., Aizawa S., Alam M.; RT "Complete genome sequencing and analysis of Saprospira grandis str. RT Lewin, a predatory marine bacterium."; RL Stand. Genomic Sci. 6:84-93(2012). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002831; AFC25169.1; -; Genomic_DNA. DR RefSeq; WP_015692782.1; NC_016940.1. DR EnsemblBacteria; AFC25169; AFC25169; SGRA_2441. DR KEGG; sgn:SGRA_2441; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000007519; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000007519}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000007519}. FT DOMAIN 209 391 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 403 AA; 46769 MW; 51FED4604E936D8D CRC64; MSEKWNLGEK NFQPKLGIEK AVLVAVILPD QPEELVHEHL DELEFLAETA GAKTVKRFTQ RLDHPDRRTF VRKGKMEEIR DYVEDKEINL VIFDDDLTGK QTSFLEEEIK CKIVDRSSLI LDIFASNAQT AQAKAQVELA QMQYLLPRLR GLWTHLERQR GGIGMRGPGE KEIETDRRIV RDRISLLKKK LAKIDLQAST QRKSRQGMIR AALVGYTNVG KSTLMNRLGK SEVLVENKLF ATLDTTVRKV VVGNMPFLLS DTVGFIRKLP HHLVESFKST LDEVRESDLL IHVVDISHPQ YRDHIQVVEQ TLKELGAGSI PCLYVFNKMD RYRSEVFDDF LTAEEREQLE SELRKQWQEK TQNKATFMAV TEEEGIEEFR ESLAQHIGEL YIERYPHKKN FWY // ID H6LEH7_ACEWD Unreviewed; 604 AA. AC H6LEH7; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 07-JUN-2017, entry version 37. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Awo_c12960 {ECO:0000313|EMBL:AFA48080.1}; OS Acetobacterium woodii (strain ATCC 29683 / DSM 1030 / JCM 2381 / KCTC OS 1655 / WB1). OC Bacteria; Firmicutes; Clostridia; Clostridiales; Eubacteriaceae; OC Acetobacterium. OX NCBI_TaxID=931626 {ECO:0000313|EMBL:AFA48080.1, ECO:0000313|Proteomes:UP000007177}; RN [1] {ECO:0000313|Proteomes:UP000007177} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29683 / DSM 1030 / JCM 2381 / KCTC 1655 / WB1 RC {ECO:0000313|Proteomes:UP000007177}; RA Poehlein A., Schmidt S., Kaster A.-K., Goenrich M., Vollmers J., RA Thuermer A., Gottschalk G., Thauer R.K., Daniel R., Mueller V.; RT "Complete genome sequence of Acetobacterium woodii."; RL Submitted (JUL-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002987; AFA48080.1; -; Genomic_DNA. DR RefSeq; WP_014355683.1; NC_016894.1. DR STRING; 931626.Awo_c12960; -. DR EnsemblBacteria; AFA48080; AFA48080; Awo_c12960. DR KEGG; awo:Awo_c12960; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR KO; K03665; -. DR OMA; EREVIIT; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000007177; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000007177}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000007177}. FT DOMAIN 378 547 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 337 364 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 604 AA; 68077 MW; ACA377885A15EB2F CRC64; MADNTKNGVR QSYIKELEDL VGYEMENQVL LDENILEIMK RLTLATKREI LICTNEKNRI QWVNIGDAST VNIGNAEMEY HVKTLNKYRV IHTHPGGNPR LSAEDFSAAK KQSLQCIIAI GVDEKIPLGY SIGVPIIEAE TMEYGQGLFK TLKELNNFPL EHYILLANRF IKNDPHNKFD AEDEEERALL IGLDLPGNKG VELVDSMEEL RQLVKTAGGT VLEQVCQARS QIDSTFYVGK GKLQELIKVI QNNDINLIVA NDELNSRQIA NIEAATGTKT VDRTTIILDI FARHAKTKEG KLQVELAQQK YRMSHLKGLG IVMSRTGGGI GTRGPGEKKL ETDRRHIRKQ LDELEARIER INRSNQINAL QRQKNKVKTI GLIGYTNSGK STLFNQLTQS EVITKDGLFI TLDSTLRKVD PEQGDYLVSD TVGFIDKLPH DLIKAFKTTL MEVETADLLL HVVDLSNHNY EAQISVVNQV LADIGAGHKK VMMIYNKIDK LPQTERAALL LKNQTAKETQ ALYISAKETL GMASLFETVN WLLIGEKRQI KLLIPYDDNK SLALLHELKV VQEIDYQAAG NMVTIDMTDE FPTHLFEQYQ VNED // ID H6MZ09_GORPV Unreviewed; 503 AA. AC H6MZ09; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 07-JUN-2017, entry version 36. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=GPOL_c21110 {ECO:0000313|EMBL:AFA73150.1}; OS Gordonia polyisoprenivorans (strain DSM 44266 / VH2). OC Bacteria; Actinobacteria; Corynebacteriales; Gordoniaceae; Gordonia. OX NCBI_TaxID=1112204 {ECO:0000313|EMBL:AFA73150.1, ECO:0000313|Proteomes:UP000009154}; RN [1] {ECO:0000313|EMBL:AFA73150.1, ECO:0000313|Proteomes:UP000009154} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 44266 / VH2 {ECO:0000313|Proteomes:UP000009154}; RX PubMed=22327575; DOI=10.1128/AEM.07969-11; RA Hiessl S., Schuldes J., Thurmer A., Halbsguth T., Broker D., RA Angelov A., Liebl W., Daniel R., Steinbuchel A.; RT "Involvement of two latex-clearing proteins during rubber degradation RT and insights into the subsequent degradation pathway revealed by the RT genome sequence of Gordonia polyisoprenivorans strain VH2."; RL Appl. Environ. Microbiol. 78:2874-2887(2012). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP003119; AFA73150.1; -; Genomic_DNA. DR RefSeq; WP_014359824.1; NC_016906.1. DR STRING; 1112204.GPOL_c21110; -. DR EnsemblBacteria; AFA73150; AFA73150; GPOL_c21110. DR KEGG; gpo:GPOL_c21110; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000009154; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000009154}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000009154}. FT DOMAIN 278 447 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 237 264 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 503 AA; 54403 MW; 0ECCF5886D9B50A9 CRC64; MSNTTHTAYP IPTPDLAEDT GIAEDTGVTD DQGITGSYRT DEPTTGELQL SERASLQRVA GLSTELTDIT EVEYRQLRLE RVVLVGVWTE GTSAQARAAM TELAALAETA GSAVLDAVIQ RRNAPDPGTY IGSGKAEELR EIVLATGADT VICDGELTPG QLTALEKVVK VKVIDRTALI LDIFAQHATS REGKAQVSLA QMEYMMPRLR GWGESMSRQA GGRAGSNGGV GLRGPGETKI ETDRRRIRER MAKLRREIRD MKKARVTKRS ARSRSAVPSL TVAGYTNAGK SSLVNAMTGS GMLVQDALFA TLDPTTRRAT LDDGREVVFT DTVGFVRHLP TQLVEAFRST LEEVVDADLL LHVVDGSDEF PAEQIAAVRR VINEVVAEEG VSAPPELLVI NKIDAIDHTR MTELRAMAPD AVFVSARTGE GLPALFDRVR EFVGRTDVEL TLAVPYTRGD LISRIHEEGE VLASDHTADG TRMTVRVPQA FAGQLADLVV TRS // ID H6ND45_9BACL Unreviewed; 443 AA. AC H6ND45; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 07-JUN-2017, entry version 36. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=PM3016_3151 {ECO:0000313|EMBL:AFC30006.1}; OS Paenibacillus mucilaginosus 3016. OC Bacteria; Firmicutes; Bacilli; Bacillales; Paenibacillaceae; OC Paenibacillus. OX NCBI_TaxID=1116391 {ECO:0000313|EMBL:AFC30006.1, ECO:0000313|Proteomes:UP000007523}; RN [1] {ECO:0000313|EMBL:AFC30006.1, ECO:0000313|Proteomes:UP000007523} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=3016 {ECO:0000313|EMBL:AFC30006.1}; RX PubMed=22535950; DOI=10.1128/JB.00323-12; RA Ma M., Wang Z., Li L., Jiang X., Guan D., Cao F., Chen H., Wang X., RA Shen D., Du B., Li J.; RT "Complete Genome Sequence of Paenibacillus mucilaginosus 3016, a RT Bacterium Functional as Microbial Fertilizer."; RL J. Bacteriol. 194:2777-2778(2012). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP003235; AFC30006.1; -; Genomic_DNA. DR RefSeq; WP_013916629.1; NC_016935.1. DR ProteinModelPortal; H6ND45; -. DR EnsemblBacteria; AFC30006; AFC30006; PM3016_3151. DR KEGG; pmq:PM3016_3151; -. DR KO; K03665; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000007523; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000007523}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000007523}. FT DOMAIN 209 373 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 168 195 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 443 AA; 49623 MW; F88EA5317012887C CRC64; MRQTTHEVTT ELDDRAILVS LVTQEQKRQD AYDPEYSLAE LIALAETAQV EVLGTLTQNK EYADSKWFIG KGKAEELKEM LQENGANTAI FDQELSGAQV RNLETYLDVK IIDRTQLILD IFAQRARTRE GIIQVELAQL SYLLPRLSGH GKNLSRLGGG IGTRGPGETK LETDRRHIRD RIAELKRQLA ETVRHRTLHR ERRKKSGVFQ VALVGYTNAG KSTLLRQLTA ADVYVENQLF ATLDPTSRQL KLPSGVEIVL TDTVGFIQNL PHDLVAAFRA TLEEANEADL ILHVVDSSTE MMPIQMRVVD QVLEELGAHG KDRVTVFNKV DLLSPSQADM LTTEGEFLRV SAFHEADLKR LVDTLEAHLA GDSKTYRIPA DKGDMISLVY RVGEVLENGV DGDDMLMTVR VNSKEYDKIG YMLAAYDQSQ HAQGDRGENT EHV // ID H6R371_NOCCG Unreviewed; 507 AA. AC H6R371; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 07-JUN-2017, entry version 37. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=NOCYR_3707 {ECO:0000313|EMBL:CCF64470.1}; OS Nocardia cyriacigeorgica (strain GUH-2). OC Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae; Nocardia. OX NCBI_TaxID=1127134 {ECO:0000313|EMBL:CCF64470.1, ECO:0000313|Proteomes:UP000008190}; RN [1] {ECO:0000313|EMBL:CCF64470.1, ECO:0000313|Proteomes:UP000008190} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=GUH-2 {ECO:0000313|EMBL:CCF64470.1, RC ECO:0000313|Proteomes:UP000008190}; RX PubMed=22461543; DOI=10.1128/JB.00161-12; RA Zoropogui A., Pujic P., Normand P., Barbe V., Beaman B., Beaman L., RA Boiron P., Colinon C., Deredjian A., Graindorge A., Mangenot S., RA Nazaret S., Neto M., Petit S., Roche D., Vallenet D., RA Rodriguez-Nava V., Richard Y., Cournoyer B., Blaha D.; RT "Genome Sequence of the Human- and Animal-Pathogenic Strain Nocardia RT cyriacigeorgica GUH-2."; RL J. Bacteriol. 194:2098-2099(2012). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; FO082843; CCF64470.1; -; Genomic_DNA. DR STRING; 1127134.NOCYR_3707; -. DR EnsemblBacteria; CCF64470; CCF64470; NOCYR_3707. DR KEGG; ncy:NOCYR_3707; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000008190; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000008190}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000008190}. FT DOMAIN 274 443 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 233 267 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 507 AA; 54337 MW; F5DB41E3F385CF84 CRC64; MTNGSDLFDG ADDVDGAEFD DTDVTPVAPS RRGGWAPEPT TGELQLEDRS ALRRVAGLST ELTDITEVEY RQLRLERVVL VGVWTEGSAA RAEASMAELA ALAETAGSEV LEALIQRRDR PDPATYIGSG KAEELRSVVL GSGADTVICD GELTPAQLTA LEKVVKVKVI DRTALILDIF AQHATSREGK AQVALAQMEY MLPRLRGWGE SMSRQAGGRA GSNGGVGLRG PGETKIETDR RRIRERMAKL RREIREMKTA RDTMRSRRTS SGIPSVAIVG YTNAGKSSLM NALTGSGVLV QDALFATLDP TTRRAELDDG REVVFTDTVG FVRHLPTQLV EAFRSTLEEV TGADLLLHVV DGSDALPSEQ IKAVREVVTD VIRESGTPAP PELLVVNKID AIDPVELTRL RALLPGAVFV SAHKGTGIDE LRDRLAEVLG GLDVEISVLL PYTRGDLLAR IHADGRIESS SHEEAGTRVH ARVPHALAAA LSEYAHAGTA VADGPAS // ID H6RVP7_BLASD Unreviewed; 487 AA. AC H6RVP7; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 07-JUN-2017, entry version 34. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:CCG04527.1}; GN OrderedLocusNames=BLASA_3670 {ECO:0000313|EMBL:CCG04527.1}; OS Blastococcus saxobsidens (strain DD2). OC Bacteria; Actinobacteria; Geodermatophilales; Geodermatophilaceae; OC Blastococcus. OX NCBI_TaxID=1146883 {ECO:0000313|EMBL:CCG04527.1, ECO:0000313|Proteomes:UP000007517}; RN [1] {ECO:0000313|Proteomes:UP000007517} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DD2 {ECO:0000313|Proteomes:UP000007517}; RA Genoscope.; RT "Complete genome sequence of Blastococcus saxobsidens strain DD2."; RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; FO117623; CCG04527.1; -; Genomic_DNA. DR RefSeq; WP_014377403.1; NC_016943.1. DR EnsemblBacteria; CCG04527; CCG04527; BLASA_3670. DR KEGG; bsd:BLASA_3670; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000007517; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000007517}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000007517}. FT DOMAIN 266 430 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 487 AA; 52325 MW; C0F90C735821FA13 CRC64; MTTAPDALPF DEQTELDTRR AAAAQRDETD ETTGSYAREA RGALRRVAGL STELADVTEV EYRQLRLERV VLVGVWTEGT QADADRSLAE LAALAETAGS QVLEAVSQRR DKPDAATYVG SGKANEIRDV VAATGADTVI CDGELTPGQL NQLEKILKVK VVDRTALILD IFAQHASSRE GKAQVELAQM QYMLPRLRGW GESLSRQAGG RVAGGGGIGT RGPGETKIET DRRRIRARVS KLRREIAGMA TARATQRSSR DRHAVPSVAI AGYTNAGKSS LLNQLTGAGV LVENALFATL DPTVRRAQSP DGREYTLTDT VGFVRHLPHQ LVDAFRSTLE EVAAADLLVH VVDGSDPDPL GQIDAVRIVL SEIDAAAVPE LIVVNKVDAM TEEDILTLRQ ALPGAVWVSA RTGAGMETLR RMIAERLPHP DVEVDVLVPY ERGDLVARVH RDGEVLAEQH EGAGTRLTAR VDGALAAVLE EFAVPVG // ID H6SSG0_PARPM Unreviewed; 438 AA. AC H6SSG0; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 07-JUN-2017, entry version 34. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=RSPPHO_01213 {ECO:0000313|EMBL:CCG07839.1}; OS Pararhodospirillum photometricum DSM 122. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales; OC Rhodospirillaceae; Pararhodospirillum. OX NCBI_TaxID=1150469 {ECO:0000313|EMBL:CCG07839.1, ECO:0000313|Proteomes:UP000033220}; RN [1] {ECO:0000313|EMBL:CCG07839.1, ECO:0000313|Proteomes:UP000033220} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM122 {ECO:0000313|Proteomes:UP000033220}; RA Duquesne K., Sturgis J.; RT "Shotgun genome sequence of Phaeospirillum photometricum DSM 122."; RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; HE663493; CCG07839.1; -; Genomic_DNA. DR RefSeq; WP_014414478.1; NC_017059.1. DR EnsemblBacteria; CCG07839; CCG07839; RSPPHO_01213. DR KEGG; rpm:RSPPHO_01213; -. DR PATRIC; fig|1150469.3.peg.1372; -. DR KO; K03665; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000033220; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000033220}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000033220}. FT DOMAIN 208 376 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 438 AA; 48661 MW; D7D4694746271ADE CRC64; MTTFEYEGPP PPTRAAVLHP SLRKGPAKAR SPQDCLEEAK GLATAITLDV VLAEVVPLTR RVPATCLGGG AVERIKEEVE RESIALVVVD TQLTPIQQRN LEREWACKVI DRTGLILEIF GERARTAEGK LQVELAHLTY QRSRLVRSWT HLERQRGGSG FLGGPGETQI ELDRRLIDDR IVRLKRELEE VRRTRGLHRE ARKRVPYPVV ALVGYTNAGK STLFNQLTAG GVLAKDMLFA TLDPTMRALD LPSGRKVILS DTVGFVSDLP HELVAAFRAT LEEVQAADVI VHVRDIAGLD TEAQKADVED VLRGMDLEER QPLEALNKAD CLDPEERARL EEDLAPDSDQ VMLSALTGEG LDRLLARIDA RLALARLVLE VRLPLEDGAT LAWLYRKGEV LERRDDEDHC VLTVRLDPAD VGRLPPAYRP PSPPDTLF // ID H7EH15_9SPIO Unreviewed; 425 AA. AC H7EH15; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 07-JUN-2017, entry version 31. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=TresaDRAFT_2784 {ECO:0000313|EMBL:EIC03133.1}; OS Treponema saccharophilum DSM 2985. OC Bacteria; Spirochaetes; Spirochaetales; Spirochaetaceae; Treponema. OX NCBI_TaxID=907348 {ECO:0000313|EMBL:EIC03133.1, ECO:0000313|Proteomes:UP000003571}; RN [1] {ECO:0000313|EMBL:EIC03133.1, ECO:0000313|Proteomes:UP000003571} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 2985 {ECO:0000313|EMBL:EIC03133.1, RC ECO:0000313|Proteomes:UP000003571}; RG US DOE Joint Genome Institute (JGI-PGF); RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., RA Tice H., Bruce D., Goodwin L., Pitluck S., Peters L., Kyrpides N., RA Mavromatis K., Ivanova N., Markowitz V., Cheng J.-F., Hugenholtz P., RA Woyke T., Wu D., Gronow S., Wellnitz S., Brambilla E., Klenk H.-P., RA Eisen J.A.; RT "The draft genome of Treponema saccharophilum DSM 2985."; RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EIC03133.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGRW01000022; EIC03133.1; -; Genomic_DNA. DR RefSeq; WP_002701776.1; NZ_AGRW01000022.1. DR ProteinModelPortal; H7EH15; -. DR EnsemblBacteria; EIC03133; EIC03133; TresaDRAFT_2784. DR PATRIC; fig|907348.3.peg.76; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000003571; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000003571}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Hydrolase {ECO:0000313|EMBL:EIC03133.1}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000003571}. FT DOMAIN 196 368 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 425 AA; 46986 MW; 9EE28AE3B9281D19 CRC64; MIYLQEEESR KTTALLIGAP GDDLSELKGL VDTLGMETLR AVTLTRMDIT PAYGMGKGKA EELSALAEEI GADVIIFDFD LDPRKQRNWE KLSKKPSFDR QEVILRIFAQ RAQTKEAVLQ VELARLEHSL PRLAHSYGDM ARQRGGNFGS KGSGETQLEL DTRAIREKIR LVKKELSAVV RDRETQRKRR EKVPVPTCAL AGYTNAGKSS LLNALTGADA FVEDKLFATL DPTTRKLQLA NGANILLTDT VGFISNLPHG LVNAFKSTLE EAERANLIII VIDASDPDAE SQYRTVVEVL KEIGAENSPR IIALNKIDRI EEMDEAERIL VLSRLEKLFP ENVKISAKNR TGFAELSEKI CDALMGTGGK YVIPVEQQHI LSVARKTGIV ESEEWLDDGI HATIRAGTSE SGKKLSAMLG QYKAE // ID H7F1T5_9LIST Unreviewed; 417 AA. AC H7F1T5; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 07-JUN-2017, entry version 34. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=KKC_00185 {ECO:0000313|EMBL:EIA21639.1}; OS Listeria fleischmannii subsp. coloradonensis. OC Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria. OX NCBI_TaxID=1081736 {ECO:0000313|EMBL:EIA21639.1, ECO:0000313|Proteomes:UP000004950}; RN [1] {ECO:0000313|EMBL:EIA21639.1, ECO:0000313|Proteomes:UP000004950} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=TTU M1-001 {ECO:0000313|EMBL:EIA21639.1, RC ECO:0000313|Proteomes:UP000004950}; RX PubMed=23524352; DOI=10.1099/ijs.0.048587-0; RA den Bakker H.C., Manuel C.S., Fortes E.D., Wiedmann M., RA Nightingale K.K.; RT "Genome sequencing identifies Listeria fleischmannii subsp. RT coloradonensis subsp. nov., isolated from a ranch."; RL Int. J. Syst. Evol. Microbiol. 63:3257-3268(2013). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EIA21639.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGUG01000001; EIA21639.1; -; Genomic_DNA. DR RefSeq; WP_007542810.1; NZ_AGUG01000001.1. DR EnsemblBacteria; EIA21639; EIA21639; KKC_00185. DR PATRIC; fig|1081736.4.peg.36; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000004950; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000004950}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000004950}. FT DOMAIN 194 363 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 417 AA; 47510 MW; 6A89FD9EC841C48B CRC64; MNKKVILVGV SGSDKNFEYT MVELANLAEA NHYEIKDVVK QNIDRINKAT YVGKGKVEEL KQIGEMLQVD AFVINDELTA SQIRNLEEEL EKEIIDRTAL ILAIFAERAK TREAKLQVEI ARLKYELPRL SNSDEVFDQQ SGKTGLANRG SGEKKIESDR RIIKNQIRHL TSELEEIVQE RETRRRKRKK NEIPVVSLVG YTNAGKSTTM NGLVNQFSKS AHKQVFEKDM LFATLETSVR EIILPDNKQF LLTDTVGFVS KLPTHLVKAF RSTLEEAKEA DLLLHVVDYS DENYKAMIET TEATLLAVGV KDVPVLYIYN KADQVSGAEY PVLQEEGLIY SAKDEASLAM LTEEITKKIF TGYKETSYLI PFDRGDIISH LNEHARVLFQ DYTEEGTKLR VEVSPADYER FQSFQLK // ID H7F3R8_9LIST Unreviewed; 405 AA. AC H7F3R8; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 07-JUN-2017, entry version 31. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=KKC_04164 {ECO:0000313|EMBL:EIA20927.1}; OS Listeria fleischmannii subsp. coloradonensis. OC Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria. OX NCBI_TaxID=1081736 {ECO:0000313|EMBL:EIA20927.1, ECO:0000313|Proteomes:UP000004950}; RN [1] {ECO:0000313|EMBL:EIA20927.1, ECO:0000313|Proteomes:UP000004950} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=TTU M1-001 {ECO:0000313|EMBL:EIA20927.1, RC ECO:0000313|Proteomes:UP000004950}; RX PubMed=23524352; DOI=10.1099/ijs.0.048587-0; RA den Bakker H.C., Manuel C.S., Fortes E.D., Wiedmann M., RA Nightingale K.K.; RT "Genome sequencing identifies Listeria fleischmannii subsp. RT coloradonensis subsp. nov., isolated from a ranch."; RL Int. J. Syst. Evol. Microbiol. 63:3257-3268(2013). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EIA20927.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGUG01000027; EIA20927.1; -; Genomic_DNA. DR RefSeq; WP_007544262.1; NZ_AGUG01000027.1. DR EnsemblBacteria; EIA20927; EIA20927; KKC_04164. DR PATRIC; fig|1081736.4.peg.801; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000004950; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000004950}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000004950}. FT DOMAIN 196 319 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 169 192 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 405 AA; 46297 MW; FDA232F399BC4E14 CRC64; MEKEQVIVVG VLLKDADEVA FHYSMEELGR LVDTANGEVI NQMVQKMERV RKESYIGRGK LEELKNLVLE TKADTVVFNS ELTPSQIRNI EAEVDAKIID RTSLILDIFA MRAKSREGKL QVAYAQYEYL LPRLSGQGSS LSKLGGGIGT RGPGETKLEM DRRLLRLKMH QIKEELTQVE KHRERIREKR KQNGVFRFGL IGYTNAGKST IFNQLTKAET LEEDQLFATL DPTTRKMKLV NGFEVLLTDT VGFIQDLPTS LVAAFKSTLE ESADMDMLLH VVDSSNADYM KHIKTVKDIL QALQISDIPV LTLYNKKDKQ HPTFVATEAN NMEISALHMN FPNEMRERLL EEVKKIWIPY FLTVKASEGT KIAFLKRATY ISKMDFDEIN ETYQIRGYFS GKERL // ID H7FNR2_9FLAO Unreviewed; 419 AA. AC H7FNR2; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 07-JUN-2017, entry version 28. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=HJ01_00733 {ECO:0000313|EMBL:EIA10051.1}; OS Flavobacterium frigoris PS1. OC Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales; OC Flavobacteriaceae; Flavobacterium. OX NCBI_TaxID=1086011 {ECO:0000313|EMBL:EIA10051.1, ECO:0000313|Proteomes:UP000005566}; RN [1] {ECO:0000313|EMBL:EIA10051.1, ECO:0000313|Proteomes:UP000005566} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=PS1 {ECO:0000313|EMBL:EIA10051.1, RC ECO:0000313|Proteomes:UP000005566}; RA Raymond J., Kim H.J.; RT "Flavobacterium frigoris PS1, a freeze-tolerant bacterium from RT Antarctic sea ice."; RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EIA10051.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AHKF01000010; EIA10051.1; -; Genomic_DNA. DR RefSeq; WP_007136910.1; NZ_AHKF01000010.1. DR EnsemblBacteria; EIA10051; EIA10051; HJ01_00733. DR PATRIC; fig|1086011.3.peg.721; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000005566; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000005566}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000005566}. FT DOMAIN 201 387 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 419 AA; 48383 MW; DB7CF8800E673B13 CRC64; MLEKETINFE KTAIVGIVTQ NQSEEKLKEY LDELEFLTYT AGGEVVKRFS QKMERPNPKT FVGTGKIEEI HHFVKENDIS TLVFDDELSP SQQKNISKII TECKILDRTH LILDIFAQRA ETSYARTQVE LAQCQYLLPR LSGMWTHLER QKGGIGMRGP GETEIETDRR IVRDRIALLK EKIKAIDKQM GTQRGNRGAM VRVALVGYTN VGKSTLMNAV GKSDVFVENK LFATLDTTVR KVVIKNLPFL LSDTVGFIRK LPTQLVDSFK STLDEVREAD LLLHVVDISH PEFEDHIASV NQTLLDIKAN DKPVIMVFNK IDAYKPLTID DDDLMTEKTP RHFTLEEWKS TWMSRVGEQN ALFISATNKE NFEEFRERVY EAVRHIHITR FPYNKFLYPD YKDAVEKEDK EDKEEEETE // ID H8E2C4_9MICO Unreviewed; 507 AA. AC H8E2C4; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 07-JUN-2017, entry version 29. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=OR221_1002 {ECO:0000313|EMBL:EIC09294.1}; OS Microbacterium laevaniformans OR221. OC Bacteria; Actinobacteria; Micrococcales; Microbacteriaceae; OC Microbacterium. OX NCBI_TaxID=1160710 {ECO:0000313|EMBL:EIC09294.1, ECO:0000313|Proteomes:UP000004547}; RN [1] {ECO:0000313|EMBL:EIC09294.1, ECO:0000313|Proteomes:UP000004547} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=OR221 {ECO:0000313|EMBL:EIC09294.1, RC ECO:0000313|Proteomes:UP000004547}; RX PubMed=22628508; DOI=10.1128/JB.00474-12; RA Brown S.D., Palumbo A.V., Panikov N., Ariyawansa T., Klingeman D.M., RA Johnson C.M., Land M.L., Utturkar S.M., Epstein S.S.; RT "Draft Genome Sequence for Microbacterium laevaniformans Strain OR221, RT a Bacterium Tolerant to Metals, Nitrate, and Low pH."; RL J. Bacteriol. 194:3279-3280(2012). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EIC09294.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AJGR01000114; EIC09294.1; -; Genomic_DNA. DR RefSeq; WP_005048878.1; NZ_AJGR01000114.1. DR EnsemblBacteria; EIC09294; EIC09294; OR221_1002. DR PATRIC; fig|1160710.3.peg.546; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000004547; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000004547}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000004547}. FT DOMAIN 289 454 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 507 AA; 54679 MW; 4CCEE2E1643EE301 CRC64; MTHTTETTDA HGEDTPLDPV DRVLARAEGR SSANVFGAAQ ALQDAATVAY GDTDGDQWDR EERAALRRVP GLSTELEDVT EVEYRQLRLE NVVLVGVYPQ GSQEDAENSL RELAALAETA GAVVLDGVLQ RRPHPDPATY IGRGKAAELR DLVAAVGADT VIADTELAPS QRRALEDVVK VKVIDRTTVI LDIFSQHAKS REGKAQVELA QLEYLLPRLR GWGESMSRQA GGQVGAGGAG MGSRGPGETK IELDRRRIRT KMAQLRRQLR DFAPAREAKR SERKRNTIPS VAIAGYTNAG KSSLLNRLTS AGVLVENALF ATLDATVRRA QAADGRVYTL TDTVGFVRNL PHQLVEAFRS TLEEVGDADV LVHVVDGSHP DPAAQLATVR DVMGDVGARS TREIVVFNKA DLVDDDARLV LRGLEPSALF VSSRTGEGID QLRTVIEDAL PLPAVEVRAL VPYERGDLIN AVHESGHIVS TAHEEGGTAV HAHVSERLAA ELAPYAL // ID H8FXP5_PHAMO Unreviewed; 451 AA. AC H8FXP5; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 12-APR-2017, entry version 30. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=PHAMO_580039 {ECO:0000313|EMBL:CCG43133.1}; OS Phaeospirillum molischianum DSM 120. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales; OC Rhodospirillaceae; Phaeospirillum. OX NCBI_TaxID=1150626 {ECO:0000313|EMBL:CCG43133.1, ECO:0000313|Proteomes:UP000004169}; RN [1] {ECO:0000313|EMBL:CCG43133.1, ECO:0000313|Proteomes:UP000004169} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM120 {ECO:0000313|Proteomes:UP000004169}; RX PubMed=22689244; DOI=10.1128/JB.00605-12; RA Duquesne K., Prima V., Ji B., Rouy Z., Medigue C., Talla E., RA Sturgis J.N.; RT "Draft Genome Sequence of the Purple Photosynthetic Bacterium RT Phaeospirillum molischianum DSM120, a Particularly Versatile RT Bacterium."; RL J. Bacteriol. 194:3559-3560(2012). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:CCG43133.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CAHP01000054; CCG43133.1; -; Genomic_DNA. DR EnsemblBacteria; CCG43133; CCG43133; PHAMO_580039. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000004169; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000004169}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000004169}. FT DOMAIN 221 392 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 451 AA; 49741 MW; 91242B22F7A332AE CRC64; MVSRPPESSV LSSRQRALVV HPARKAERRG EGAADSLPVT AVRLPEARLA EAIGLAQAID LDIVLAEAVP VPRPRPATLL GKGAVERLAD AIADAEITLA VIDSPLTPVQ QRNLEKAWGC KVIDRTGLIL EIFGARARTR EGTLQVELAA LSYQRSRLVR SWTHLERQRG GFGFLGGPGE TQIEADRRMI GDRIVKLERE LDDVKRTRDL HRKARRRVPY PIVALVGYTN AGKSTLFNTI TRAEVMAKDM LFATLDPTMR TLDLPSGRKV ILSDTVGFIS DLPHELVAAF RATLEEVLEA DVVVHVRDIS HPDSEAQAAD VEAVLRELGL EEMVDNGLVE GLNKIDLLDA ERREEVFNQA QRHSARLPFS AVTGEGVPAL LAELDRRLGQ GRAMIDVSLS LTDGASIAWL YRHGEVVARR DDQSHAYLRV KLEAADVRRF QQRQASARPL S // ID H8GLS5_METAL Unreviewed; 422 AA. AC H8GLS5; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 07-JUN-2017, entry version 32. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=Metal_2921 {ECO:0000313|EMBL:EIC30602.1}; OS Methylomicrobium album BG8. OC Bacteria; Proteobacteria; Gammaproteobacteria; Methylococcales; OC Methylococcaceae; Methylomicrobium. OX NCBI_TaxID=686340 {ECO:0000313|EMBL:EIC30602.1, ECO:0000313|Proteomes:UP000005090}; RN [1] {ECO:0000313|EMBL:EIC30602.1, ECO:0000313|Proteomes:UP000005090} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BG8 {ECO:0000313|EMBL:EIC30602.1, RC ECO:0000313|Proteomes:UP000005090}; RX PubMed=23580712; RA Kits K.D., Kalyuzhnaya M.G., Klotz M.G., Jetten M.S., RA Op den Camp H.J., Vuilleumier S., Bringel F., Dispirito A.A., RA Murrell J.C., Bruce D., Cheng J.F., Copeland A., Goodwin L., RA Hauser L., Lajus A., Land M.L., Lapidus A., Lucas S., Medigue C., RA Pitluck S., Woyke T., Zeytun A., Stein L.Y.; RT "Genome Sequence of the Obligate Gammaproteobacterial Methanotroph RT Methylomicrobium album Strain BG8."; RL Genome Announc. 1:E0017013-E0017013(2013). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CM001475; EIC30602.1; -; Genomic_DNA. DR RefSeq; WP_005373294.1; NZ_CM001475.1. DR ProteinModelPortal; H8GLS5; -. DR EnsemblBacteria; EIC30602; EIC30602; Metal_2921. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000005090; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000005090}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000005090}. FT DOMAIN 196 363 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 162 189 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 422 AA; 47122 MW; EC1D21415AD34119 CRC64; MFDRPDSGER AVLVHLILHS GQEDLLELKE LARSAGAEPV HTVTGSRKNP DPKYFVGSGK VDEIKQAIAD HVADIVLFNH PLTPSQERNL ESALGVRVVD RNGLILDIFA QRAQTFEGKL QVELAQLKHL STRLVRGWTH LERQKGGIGL RGPGETQLET DRRLIGDRIK QIQSRLEKVE KQRHQSRGKR RKAEIPTVSL VGYTNAGKST LFNRLTGANI YAADQLFATL DPTLRNCRLP NNSAIVLADT VGFIRHLPHE LVAAFKSTLQ EASEADLLLH VIDAHAEDRD ETITQVNQVL KEIGADKIRQ LEIYNKIDLL DGGRPRIDRD ETGRPVRVWL SATTGEGADL SLQALAEIFS VHKIRMRCHL RPEQGDIRAK IYAYADVFAE KIGDDGHFEM VIEIDPKHSG VLEKIPSEVI SP // ID H8GV72_DEIGI Unreviewed; 569 AA. AC H8GV72; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 05-JUL-2017, entry version 37. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:AFD26746.1}; GN OrderedLocusNames=DGo_CA2820 {ECO:0000313|EMBL:AFD26746.1}; OS Deinococcus gobiensis (strain DSM 21396 / JCM 16679 / CGMCC 1.7299 / OS I-0). OC Bacteria; Deinococcus-Thermus; Deinococci; Deinococcales; OC Deinococcaceae; Deinococcus. OX NCBI_TaxID=745776 {ECO:0000313|EMBL:AFD26746.1, ECO:0000313|Proteomes:UP000007575}; RN [1] {ECO:0000313|EMBL:AFD26746.1, ECO:0000313|Proteomes:UP000007575} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 21396 / JCM 16679 / CGMCC 1.7299 / I-0 RC {ECO:0000313|Proteomes:UP000007575}; RX PubMed=22470573; DOI=10.1371/journal.pone.0034458; RA Yuan M., Chen M., Zhang W., Lu W., Wang J., Yang M., Zhao P., Tang R., RA Li X., Hao Y., Zhou Z., Zhan Y., Yu H., Teng C., Yan Y., Ping S., RA Wang Y., Lin M.; RT "Genome sequence and transcriptome analysis of the radioresistant RT bacterium Deinococcus gobiensis: insights into the extreme RT environmental adaptations."; RL PLoS ONE 7:E34458-E34458(2012). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002191; AFD26746.1; -; Genomic_DNA. DR EnsemblBacteria; AFD26746; AFD26746; DGo_CA2820. DR KEGG; dgo:DGo_CA2820; -. DR PATRIC; fig|745776.4.peg.2897; -. DR KO; K03665; -. DR OMA; EREVIIT; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000007575; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000007575}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000007575}. FT DOMAIN 382 550 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 341 368 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 569 AA; 62082 MW; 992271B8B93CAF3D CRC64; MHGNLSGLRP AQLKSLGNLY RRRIEPGRVG SPELARNLAE LSNDVRREVS VLIDRRGRVI SVSVADAKAA ELPEVRQGEN RLAGFHLLHA HPRGGALSKG DLSTLFLKRL DAVSAIEVRN EGQPGLVHTA HLTPPGTVGE EEDWRILPPV PAFQIDEFDL GAQVSALEEE IARAASTREA KKDRERALLV QIDQGEFDAE ERLEELGELA RTAGAEVVYK ELIYRRNLKP GTLVGAGKLE ELTGRAYHLD ADLLIFGQEL GPAQAREIEA ATGLKVIDRT QLILDIFALH AQGVESRLQV ELAQLRYMKP RLLGAGAALS RIGGGGGSAG GGAIGTRGPG ETKLELDRRR INDRLAFLEK QLEGVAQRRE ERRKSRERND VPVVSIVGYT NAGKSTLLNA FTHAAEEPRR VLAENKLFAT LRPTSRQGYL EGIGPVVLTD TVGFIRDLPK DLTRAFRSTL EEIGDADVLL HVVDAAGPGA DTRLDAVNRI LEELGFVDMP TVVALNKADA ADPETLARER ERTEGIPVSA LRNIGLADLK EALADAIGQV QRQELARQEE VRALAAEWH // ID H8KXB3_SOLCM Unreviewed; 396 AA. AC H8KXB3; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 07-JUN-2017, entry version 38. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Solca_3437 {ECO:0000313|EMBL:AFD08442.1}; OS Solitalea canadensis (strain ATCC 29591 / DSM 3403 / NBRC 15130 / OS NCIMB 12057 / USAM 9D) (Flexibacter canadensis). OC Bacteria; Bacteroidetes; Sphingobacteriia; Sphingobacteriales; OC Sphingobacteriaceae; Solitalea. OX NCBI_TaxID=929556 {ECO:0000313|EMBL:AFD08442.1, ECO:0000313|Proteomes:UP000007590}; RN [1] {ECO:0000313|Proteomes:UP000007590} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29591 / DSM 3403 / NBRC 15130 / NCIMB 12057 / USAM 9D RC {ECO:0000313|Proteomes:UP000007590}; RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., RA Tice H., Bruce D., Goodwin L., Pitluck S., Peters L., Ovchinnikova G., RA Lu M., Kyrpides N., Mavromatis K., Ivanova N., Brettin T., RA Detter J.C., Han C., Larimer F., Land M., Hauser L., Markowitz V., RA Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Spring S., Schroeder M., RA Kopitz M., Brambilla E., Klenk H.-P., Eisen J.A.; RT "The complete genome of Solitalea canadensis DSM 3403."; RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP003349; AFD08442.1; -; Genomic_DNA. DR RefSeq; WP_014681665.1; NC_017770.1. DR EnsemblBacteria; AFD08442; AFD08442; Solca_3437. DR KEGG; scn:Solca_3437; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000007590; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000007590}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000007590}. FT DOMAIN 202 376 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 396 AA; 45419 MW; 0D6BE54B3E9B5FEE CRC64; MGNYSTARKQ ERAVLVGVVT PDETELQERE YLDELAFLAE TAGAETIKIF MQKLQRPDSK TFVGSGKLEE IIEYVQAEEA DMVIFDDELS PSQLRNLGRE FKEIKILDRS NLILDIFANR AQTAQAKTQV ELAQYQYLLP RLTRMWTHLE RQRGGIGMRG PGESQIETDR RIILDKIALL KERLEKIDKQ NATQRKNRGE LVRVALVGYT NVGKSTIMNM LSKSEVFAEN KLFATLDTTV RKMVINNLPF LLSDTVGFIR KLPHHLVECF KSTLAEVREA DILIHVADIS HPNFEDHIIT VNETLKELGA RDKEMITVFN KIDAYKGEGD TTLSLEDFKS TWMAKHNSPA IFISAKDRLN IDSLRKEIYE RAKAIHLSRF PYDGLLYNMD YVEETE // ID H8L4F4_FRAAD Unreviewed; 438 AA. AC H8L4F4; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 07-JUN-2017, entry version 35. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Fraau_1169 {ECO:0000313|EMBL:AFC85628.1}; OS Frateuria aurantia (strain ATCC 33424 / DSM 6220 / NBRC 3245 / NCIMB OS 13370) (Acetobacter aurantius). OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales; OC Rhodanobacteraceae; Frateuria. OX NCBI_TaxID=767434 {ECO:0000313|EMBL:AFC85628.1, ECO:0000313|Proteomes:UP000005234}; RN [1] {ECO:0000313|Proteomes:UP000005234} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33424 / DSM 6220 / NBRC 3245 / NCIMB 13370 RC {ECO:0000313|Proteomes:UP000005234}; RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., RA Tice H., Bruce D., Goodwin L., Pitluck S., Peters L., Ovchinnikova G., RA Teshima H., Kyrpides N., Mavromatis K., Ivanova N., Brettin T., RA Detter J.C., Han C., Larimer F., Land M., Hauser L., Markowitz V., RA Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Brambilla E., RA Klenk H.-P., Eisen J.A.; RT "The complete genome of Frateuria aurantia DSM 6220."; RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP003350; AFC85628.1; -; Genomic_DNA. DR EnsemblBacteria; AFC85628; AFC85628; Fraau_1169. DR KEGG; fau:Fraau_1169; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000005234; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000005234}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000005234}. FT DOMAIN 190 356 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 438 AA; 47963 MW; 653260AC8F866DCD CRC64; MLVLPHGGSV SGNPVRRADE FAELAASAGA QVLARVAARV ADPNPRYYIG TGKAEEVREA AAAVDANVIL VDHILSPVQE RNLEKLLDLR VVDRAGLILD IFAQRARSHE GKLEVELAQL KHLATRLVRG WTHLDSQRGG AIGNRGPGET QLETDRRLLG ERVKLLTRRL EKVQTQRTQQ RRARLRNTVP RVALVGYTNA GKSTLFNAIT QGDVYAADQL FATLDPTVRQ LEGLTCGPAV LADTVGFVRD LPHDLVAAFR ATLAEARDAD LLLHVSDAAD DEREHLQQVV DEVLEEIGAG DVPQLRVMNK VDLTEGLPRL DRDAEGKVHR VWLSAASGQG LDLLRDALGE LLAGHDRIRA TVCLPLAFGR LHARLWAQGL ITAERVEDDG WYLDLQTPRQ VLVQLASHLG GAEAVWLREV AGPEPEPADD EYEVLPLT // ID H8MQR1_CORCM Unreviewed; 551 AA. AC H8MQR1; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 07-JUN-2017, entry version 36. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:AFE09049.1}; GN OrderedLocusNames=COCOR_01246 {ECO:0000313|EMBL:AFE09049.1}; OS Corallococcus coralloides (strain ATCC 25202 / DSM 2259 / NBRC 100086 OS / M2) (Myxococcus coralloides). OC Bacteria; Proteobacteria; Deltaproteobacteria; Myxococcales; OC Cystobacterineae; Myxococcaceae; Corallococcus. OX NCBI_TaxID=1144275 {ECO:0000313|EMBL:AFE09049.1, ECO:0000313|Proteomes:UP000007587}; RN [1] {ECO:0000313|Proteomes:UP000007587} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 25202 / DSM 2259 / NBRC 100086 / M2 RC {ECO:0000313|Proteomes:UP000007587}; RA Huntley S., Zhang Y., Treuner-Lange A., Sensen C.W., RA Sogaard-Andersen L.; RT "Genome sequence of the fruiting myxobacterium Corallococcus RT coralloides DSM 2259."; RL Submitted (MAR-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP003389; AFE09049.1; -; Genomic_DNA. DR EnsemblBacteria; AFE09049; AFE09049; COCOR_01246. DR KEGG; ccx:COCOR_01246; -. DR KO; K03665; -. DR OMA; EREVIIT; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000007587; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000007587}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000007587}. FT DOMAIN 379 543 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 338 365 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 551 AA; 61071 MW; 5AC007A6251C9AB3 CRC64; MKEIYGNTLG LKTSEQQRLR NTFRRRVDPR EIVSAELARH LTELSHELNR QVGVLINRKG DIEHVVVGNA HKLELPDIGR ARAGQIRLRG LRLVHTHLKS EPLTKDDLTD LALLRLDCVA AVGVGNEGLP GILHWAYLVP ENGSGEFWHV STLPSVHGEQ PDLLATLDAL EEEFNRNAAA RTVSGKERAI LVAVCLDGNR ARAESSLAEL KELARTAGVE VVDSVLQMKR EADPRYLIGR GKLEDLNLRS MQSMVDLLIF DKDLTPSQGR HIGDATSLKI LDRTQLILDI FAQRAQTAEG KLQVELAQLK YRLPRLVQGD DSLSRLMGGG VGGRGPGETK LEIDRRRVRE RITNLERRID VISRERSVRR AQRNRREVPV ISIVGYTNAG KSTLLNAITN AEVLAEDKLF ATLDPTSRRL RFPQEREVII TDTVGFIRDL PKDLVAAFRA TLEELYDASL LLHVVDASDP ARDDQVEAVE KILASLGLME KPRLMVWNKA DQLSADEVES LLRSRGGVAI SAVKREGLAT LLAKADTTLF AEGASESIGV V // ID H8MWD9_CORCM Unreviewed; 491 AA. AC H8MWD9; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 07-JUN-2017, entry version 34. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX1 {ECO:0000313|EMBL:AFE09050.1}; GN Synonyms=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=COCOR_07884 {ECO:0000313|EMBL:AFE09050.1}; OS Corallococcus coralloides (strain ATCC 25202 / DSM 2259 / NBRC 100086 OS / M2) (Myxococcus coralloides). OC Bacteria; Proteobacteria; Deltaproteobacteria; Myxococcales; OC Cystobacterineae; Myxococcaceae; Corallococcus. OX NCBI_TaxID=1144275 {ECO:0000313|EMBL:AFE09050.1, ECO:0000313|Proteomes:UP000007587}; RN [1] {ECO:0000313|Proteomes:UP000007587} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 25202 / DSM 2259 / NBRC 100086 / M2 RC {ECO:0000313|Proteomes:UP000007587}; RA Huntley S., Zhang Y., Treuner-Lange A., Sensen C.W., RA Sogaard-Andersen L.; RT "Genome sequence of the fruiting myxobacterium Corallococcus RT coralloides DSM 2259."; RL Submitted (MAR-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP003389; AFE09050.1; -; Genomic_DNA. DR RefSeq; WP_014400661.1; NC_017030.1. DR EnsemblBacteria; AFE09050; AFE09050; COCOR_07884. DR KEGG; ccx:COCOR_07884; -. DR KO; K03665; -. DR OMA; VILEIFH; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000007587; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 2. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000007587}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000007587}. FT DOMAIN 272 437 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 491 AA; 53273 MW; 5BEFC6F8AE8A0A7D CRC64; MAKTLPERPR AVLVGVQLPG VTDEAHAADL AELKRLVHTL GFDAVATVSQ RRQRLATGTV LGSGKLKELS ALTGGSGVIP SGAQGKTSKA REKWEAEADA EPEGPDAPVA PGDADLDGSG SEPPDEDDDA FPDTDADPES DADAEATAIE PGPRPTVVVV DHELSPSQLR NLERATGVQV LDRAGVIVDI FHRHARSHEA RMQVEIARLN YLAPRLREAP GGRERQQGRG SGDSAIELDR RKIRDRLAEL REGLAAIQKD QDQRRYARRD QLRVALVGYT NAGKSSLMRA LTGSTVLVAD QLFATLDTTV RAMQPETRPR ILVSDTVGFI QKLPHDLVAS FRSTLDEALE ASLLLYVVDA SDPTWAAQLE VTRTVLREIG ADVVPGKLVF NKVDRLDAAA QEALRAQHPE ALLVSAHRPD DVAGLRREII AFFEASMVEA DLVIPYARQA RIGEVYEHTT VVSQAYDETG SRLRVRGLPG AIARLTRSFQ E // ID H8XNE1_FLAIG Unreviewed; 407 AA. AC H8XNE1; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 07-JUN-2017, entry version 32. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:CCG52058.1}; GN OrderedLocusNames=KQS_00225 {ECO:0000313|EMBL:CCG52058.1}; OS Flavobacterium indicum (strain DSM 17447 / CIP 109464 / GPTSA100-9). OC Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales; OC Flavobacteriaceae; Flavobacterium. OX NCBI_TaxID=1094466 {ECO:0000313|EMBL:CCG52058.1, ECO:0000313|Proteomes:UP000007599}; RN [1] {ECO:0000313|Proteomes:UP000007599} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 17447 / CIP 109464 / GPTSA100-9 RC {ECO:0000313|Proteomes:UP000007599}; RA Barbier P., Houel A., Loux V., Poulain J., Bernardet J.-F., RA Touchon M., Duchaud E.; RT "Complete genome sequence of Flavobacterium indicum GPTSA100-9T, RT isolated from warm spring water."; RL Submitted (MAR-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; HE774682; CCG52058.1; -; Genomic_DNA. DR RefSeq; WP_014387202.1; NC_017025.1. DR EnsemblBacteria; CCG52058; CCG52058; KQS_00225. DR KEGG; fin:KQS_00225; -. DR PATRIC; fig|1094466.5.peg.45; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000007599; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000007599}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Hydrolase {ECO:0000313|EMBL:CCG52058.1}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000007599}. FT DOMAIN 200 386 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 407 AA; 47137 MW; B78568E45FEBC001 CRC64; MLEKETHNFE KTVIVGIVTQ LQDEDKLNEY LDELEFLTYT AGGEVVKRFT QKMDKPNPKT FVGSGKLEEI NYYIKDNEVK TVIFDDELTP AQQKNITREL DCKVLDRTNL ILDIFAQRAE TSYARTQVEL AQCQYLLPRL TGMWTHLERQ RGGIGMRGPG ETEIETDRRI VRDRIALLKE KIKTIDKQMA IQRSNRGAMV RVALVGYTNV GKSTLMNAVG KSEVFVENKL FATLDTTVRK TVIKNLPFLL SDTVGFIRKL PTQLVESFKS TLDEVREADL LLHVVDISHP DFEDHIESVN QILQDIKSAD KPTIMVFNKI DAYSYDKIDE TDITIEKTTK NFSLEDWKKT WMSKLGDKNT LFISATEKAN FEEFREKVYE AVREIHITRF PYNKFLYPDY KEAIENE // ID H8Z844_9GAMM Unreviewed; 438 AA. AC H8Z844; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 07-JUN-2017, entry version 31. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=Thi970DRAFT_03591 {ECO:0000313|EMBL:EIC19979.1}; OS Thiorhodovibrio sp. 970. OC Bacteria; Proteobacteria; Gammaproteobacteria; Chromatiales; OC Chromatiaceae; Thiorhodovibrio. OX NCBI_TaxID=631362 {ECO:0000313|EMBL:EIC19979.1, ECO:0000313|Proteomes:UP000002964}; RN [1] {ECO:0000313|Proteomes:UP000002964} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=970 {ECO:0000313|Proteomes:UP000002964}; RG US DOE Joint Genome Institute (JGI-PGF); RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S., RA Peters L., Land M.L., Hauser L., Vogl K., Liu Z., Overmann J., RA Frigaard N.-U., Bryant D.A., Woyke T.J.; RL Submitted (JUN-2011) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:EIC19979.1, ECO:0000313|Proteomes:UP000002964} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=970 {ECO:0000313|EMBL:EIC19979.1, RC ECO:0000313|Proteomes:UP000002964}; RG US DOE Joint Genome Institute; RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S., RA Peters L., Ovchinnikova G., Zhang X., Detter J.C., Han C., Tapia R., RA Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Vogl K., RA Liu Z., Overmann J., Frigaard N.-U., Bryant D., Woyke T.; RL Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JH603170; EIC19979.1; -; Genomic_DNA. DR RefSeq; WP_009150382.1; NZ_JH603170.1. DR EnsemblBacteria; EIC19979; EIC19979; Thi970DRAFT_03591. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000002964; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000002964}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000002964}. FT DOMAIN 198 365 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 164 191 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 438 AA; 48480 MW; D45B96AFD308241D CRC64; MFERPDAGER ALLVQLAIGR KLDAEETTEF RLLVEAAGAL EVGLVTGTRD APDPRFFVGQ GKAAELAEQV AATDAELVIF DHALSPAQER NLERRLSCRV VDRNGLILDI FARRARSFEG KLQVELAQLR HLSTRLVRGW THLERQKGGI GLRGPGETQL ETDRRLLGQR IVALNKRLER IETQRAQGRQ ARDRAEIATV SLVGYTNAGK STLFNRLTAA GVFQADQLFA TLDPTLRRLE LPNAPAVVVA DTVGFISQLP HELVAAFRAT LQETRSAALL LHVIDAAGNE RERCERDVEQ VLMEIGTEGI ARLRVMNKID QLADQGPRVD RDAAGQVTTV WLSARTGDGV ELLIDALAER FRGQVENCQL ELNPSEGALR AWLYRHGQIL AEEARADGGW TMAVMIDRER LRRELKRHGR LLDARAPAAG TTLEAACQ // ID H9H018_HORSE Unreviewed; 110 AA. AC H9H018; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 30-AUG-2017, entry version 16. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSECAP00000022759}; OS Equus caballus (Horse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Perissodactyla; Equidae; Equus. OX NCBI_TaxID=9796 {ECO:0000313|Ensembl:ENSECAP00000022759, ECO:0000313|Proteomes:UP000002281}; RN [1] {ECO:0000313|Ensembl:ENSECAP00000022759, ECO:0000313|Proteomes:UP000002281} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Thoroughbred {ECO:0000313|Ensembl:ENSECAP00000022759, RC ECO:0000313|Proteomes:UP000002281}; RX PubMed=19892987; DOI=10.1126/science.1178158; RG Broad Institute Genome Sequencing Platform; RG Broad Institute Whole Genome Assembly Team; RA Wade C.M., Giulotto E., Sigurdsson S., Zoli M., Gnerre S., Imsland F., RA Lear T.L., Adelson D.L., Bailey E., Bellone R.R., Bloecker H., RA Distl O., Edgar R.C., Garber M., Leeb T., Mauceli E., MacLeod J.N., RA Penedo M.C.T., Raison J.M., Sharpe T., Vogel J., Andersson L., RA Antczak D.F., Biagi T., Binns M.M., Chowdhary B.P., Coleman S.J., RA Della Valle G., Fryc S., Guerin G., Hasegawa T., Hill E.W., Jurka J., RA Kiialainen A., Lindgren G., Liu J., Magnani E., Mickelson J.R., RA Murray J., Nergadze S.G., Onofrio R., Pedroni S., Piras M.F., RA Raudsepp T., Rocchi M., Roeed K.H., Ryder O.A., Searle S., Skow L., RA Swinburne J.E., Syvaenen A.C., Tozaki T., Valberg S.J., Vaudin M., RA White J.R., Zody M.C., Lander E.S., Lindblad-Toh K.; RT "Genome sequence, comparative analysis, and population genetics of the RT domestic horse."; RL Science 326:865-867(2009). RN [2] {ECO:0000313|Ensembl:ENSECAP00000022759} RP IDENTIFICATION. RC STRAIN=Thoroughbred {ECO:0000313|Ensembl:ENSECAP00000022759}; RG Ensembl; RL Submitted (MAR-2012) to UniProtKB. CC -!- CAUTION: The sequence shown here is derived from an Ensembl CC automatic analysis pipeline and should be considered as CC preliminary data. {ECO:0000313|Ensembl:ENSECAP00000022759}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR STRING; 9796.ENSECAP00000022759; -. DR PaxDb; H9H018; -. DR Ensembl; ENSECAT00000029002; ENSECAP00000022759; ENSECAG00000026952. DR eggNOG; KOG0410; Eukaryota. DR eggNOG; COG2262; LUCA. DR GeneTree; ENSGT00390000001397; -. DR OrthoDB; EOG091G0852; -. DR Proteomes; UP000002281; Unplaced. DR Bgee; ENSECAG00000026952; -. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR GO; GO:0043022; F:ribosome binding; IBA:GO_Central. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF13167; GTP-bdg_N; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000002281}; KW Reference proteome {ECO:0000313|Proteomes:UP000002281}. FT DOMAIN 4 92 GTP-bdg_N. {ECO:0000259|Pfam:PF13167}. SQ SEQUENCE 110 AA; 12382 MW; 2DD2193336786571 CRC64; AEWQVAEARA LVHTLDNWSV VETMVVPTRT PDKKLVFGKG NLEQLTERIR GSPEVTAVFL NVERMSAPTQ KELEAAWGVP VFDRITVVLH IFRCNARTTE ARLQLALAEL // ID H9ULU2_SPIAZ Unreviewed; 447 AA. AC H9ULU2; DT 13-JUN-2012, integrated into UniProtKB/TrEMBL. DT 13-JUN-2012, sequence version 1. DT 07-JUN-2017, entry version 37. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Spiaf_2454 {ECO:0000313|EMBL:AFG38485.1}; OS Spirochaeta africana (strain ATCC 700263 / DSM 8902 / Z-7692). OC Bacteria; Spirochaetes; Spirochaetales; Spirochaetaceae; Spirochaeta. OX NCBI_TaxID=889378 {ECO:0000313|EMBL:AFG38485.1, ECO:0000313|Proteomes:UP000007383}; RN [1] {ECO:0000313|Proteomes:UP000007383} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 700263 / DSM 8902 / Z-7692 RC {ECO:0000313|Proteomes:UP000007383}; RX PubMed=23991249; DOI=10.4056/sigs.3607108; RA Liolos K., Abt B., Scheuner C., Teshima H., Held B., Lapidus A., RA Nolan M., Lucas S., Deshpande S., Cheng J.F., Tapia R., Goodwin L.A., RA Pitluck S., Pagani I., Ivanova N., Mavromatis K., Mikhailova N., RA Huntemann M., Pati A., Chen A., Palaniappan K., Land M., Rohde M., RA Tindall B.J., Detter J.C., Goker M., Bristow J., Eisen J.A., RA Markowitz V., Hugenholtz P., Woyke T., Klenk H.P., Kyrpides N.C.; RT "Complete genome sequence of the halophilic bacterium Spirochaeta RT africana type strain (Z-7692(T)) from the alkaline Lake Magadi in the RT East African Rift."; RL Stand. Genomic Sci. 8:165-176(2013). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP003282; AFG38485.1; -; Genomic_DNA. DR EnsemblBacteria; AFG38485; AFG38485; Spiaf_2454. DR KEGG; sfc:Spiaf_2454; -. DR PATRIC; fig|889378.3.peg.2431; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000007383; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000007383}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000007383}. FT DOMAIN 227 391 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 193 220 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 447 AA; 49918 MW; 4A3A29765F5FA13F CRC64; MTISFGLGTG PAFPAPLSLL YFPQMIEFTE REPDGAILVG TTNPHRSLHE TEDLLNELSE LCSNIDLEPR ASIIAPLSRP QPRFFVGSGK VDEILQLAEE YDCSCIVFDE ELSPSQQRNL ERHTKLAVID RREVILEIFK QRATTQEAVL QVQLASLEYS LPRLTRAWTH LSRQRGGAKG TRGEGEKQLE VDRRLVQRRI TAVKRELAQV EEHRATMRKK RESIPMPTGA LVGYTNAGKS TLLEYLSGAE LGSENKLFAT LDPTTKRIEL ADAGPVLLTD TVGFVRNLPH ELVDAFHSTL EETLHASFIV HVVDAAAPNA REQYEAVNAV LRELGAEQYP TIVALNKADL AAPDQLFHPR TPGPVVEISA KTGAGIERLT ATIERLLEHT MNRTRFRFPV ERSDLPALLH RSGRVLSERY EDDAILVEAL VPPRIHGKLQ EYVQKKG // ID HFLX_ACIC5 Reviewed; 432 AA. AC C1F407; DT 21-SEP-2011, integrated into UniProtKB/Swiss-Prot. DT 26-MAY-2009, sequence version 1. DT 07-JUN-2017, entry version 51. DE RecName: Full=GTPase HflX {ECO:0000255|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000255|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000255|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=ACP_1034; OS Acidobacterium capsulatum (strain ATCC 51196 / DSM 11244 / JCM 7670 / OS NBRC 15755 / NCIMB 13165 / 161). OC Bacteria; Acidobacteria; Acidobacteriales; Acidobacteriaceae; OC Acidobacterium. OX NCBI_TaxID=240015; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51196 / DSM 11244 / JCM 7670 / NBRC 15755 / NCIMB 13165 / RC 161; RX PubMed=19201974; DOI=10.1128/AEM.02294-08; RA Ward N.L., Challacombe J.F., Janssen P.H., Henrissat B., RA Coutinho P.M., Wu M., Xie G., Haft D.H., Sait M., Badger J., RA Barabote R.D., Bradley B., Brettin T.S., Brinkac L.M., Bruce D., RA Creasy T., Daugherty S.C., Davidsen T.M., DeBoy R.T., Detter J.C., RA Dodson R.J., Durkin A.S., Ganapathy A., Gwinn-Giglio M., Han C.S., RA Khouri H., Kiss H., Kothari S.P., Madupu R., Nelson K.E., Nelson W.C., RA Paulsen I., Penn K., Ren Q., Rosovitz M.J., Selengut J.D., RA Shrivastava S., Sullivan S.A., Tapia R., Thompson L.S., Watkins K.L., RA Yang Q., Yu C., Zafar N., Zhou L., Kuske C.R.; RT "Three genomes from the phylum Acidobacteria provide insight into the RT lifestyles of these microorganisms in soils."; RL Appl. Environ. Microbiol. 75:2046-2056(2009). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000255|HAMAP-Rule:MF_00900}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00900}; CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000255|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000255|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000255|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001472; ACO32170.1; -; Genomic_DNA. DR RefSeq; WP_015896193.1; NC_012483.1. DR ProteinModelPortal; C1F407; -. DR SMR; C1F407; -. DR STRING; 240015.ACP_1034; -. DR EnsemblBacteria; ACO32170; ACO32170; ACP_1034. DR KEGG; aca:ACP_1034; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000002207; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; GTP-binding; Magnesium; Metal-binding; KW Nucleotide-binding; Reference proteome. FT CHAIN 1 432 GTPase HflX. FT /FTId=PRO_0000412652. FT DOMAIN 210 375 Hflx-type G. {ECO:0000255|HAMAP- FT Rule:MF_00900}. FT NP_BIND 216 223 GTP. {ECO:0000255|HAMAP-Rule:MF_00900}. FT NP_BIND 241 245 GTP. {ECO:0000255|HAMAP-Rule:MF_00900}. FT NP_BIND 263 266 GTP. {ECO:0000255|HAMAP-Rule:MF_00900}. FT NP_BIND 329 332 GTP. {ECO:0000255|HAMAP-Rule:MF_00900}. FT NP_BIND 353 355 GTP. {ECO:0000255|HAMAP-Rule:MF_00900}. FT METAL 223 223 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_00900}. FT METAL 243 243 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_00900}. SQ SEQUENCE 432 AA; 47075 MW; 29830161CD68DF28 CRC64; MARRAASADL DSLDLDSLGD QEPGAAEKGG SDDAFESGVA EFRELVLSAG AEIAAEVQQR RGRADAATLI GSGKVEEVRA VAESSHADVI VFGQNLTPTQ LRNLENALPG RVIDRTQLIL DIFARHARTR EGMLQVELAQ LEYMLPRLTG RGREMSRLGG GIGTRGPGET QLETDRRRIQ RRISTLKGEL ESVRRIRSQQ RQRREAVPVP TVALVGYTNA GKSTLFNALT GAGVLASSRM FATLDPKLRA IVLPSRRKVL LSDTVGFIRD LPPTLISSFR ATLEEVQKAE VLLHVQDCSS ATREEHRAEV KHVLAELGAG DKPQIEVLNK VDLLSPEEQE GLRSGHGRPM AISARTGMGL EDLLERIDEA LQADPMVEAR LRVPQSEGEV IAAIEAGGVI RNREFEGNLV FLKVSAPASL IGRFRRFATL PK // ID HFLX_AKKM8 Reviewed; 437 AA. AC B2UPE7; DT 21-SEP-2011, integrated into UniProtKB/Swiss-Prot. DT 01-JUL-2008, sequence version 1. DT 07-JUN-2017, entry version 56. DE RecName: Full=GTPase HflX {ECO:0000255|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000255|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000255|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Amuc_0587; OS Akkermansia muciniphila (strain ATCC BAA-835 / Muc). OC Bacteria; Verrucomicrobia; Verrucomicrobiae; Verrucomicrobiales; OC Akkermansiaceae; Akkermansia. OX NCBI_TaxID=349741; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-835 / Muc; RX PubMed=21390229; DOI=10.1371/journal.pone.0016876; RA van Passel M.W., Kant R., Zoetendal E.G., Plugge C.M., Derrien M., RA Malfatti S.A., Chain P.S., Woyke T., Palva A., de Vos W.M., Smidt H.; RT "The genome of Akkermansia muciniphila, a dedicated intestinal mucin RT degrader, and its use in exploring intestinal metagenomes."; RL PLoS ONE 6:E16876-E16876(2011). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000255|HAMAP-Rule:MF_00900}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00900}; CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000255|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000255|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000255|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001071; ACD04424.1; -; Genomic_DNA. DR RefSeq; WP_012419639.1; NC_010655.1. DR ProteinModelPortal; B2UPE7; -. DR SMR; B2UPE7; -. DR STRING; 349741.Amuc_0587; -. DR EnsemblBacteria; ACD04424; ACD04424; Amuc_0587. DR KEGG; amu:Amuc_0587; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000001031; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; GTP-binding; Magnesium; Metal-binding; KW Nucleotide-binding; Reference proteome. FT CHAIN 1 437 GTPase HflX. FT /FTId=PRO_0000412653. FT DOMAIN 212 382 Hflx-type G. {ECO:0000255|HAMAP- FT Rule:MF_00900}. FT NP_BIND 218 225 GTP. {ECO:0000255|HAMAP-Rule:MF_00900}. FT NP_BIND 243 247 GTP. {ECO:0000255|HAMAP-Rule:MF_00900}. FT NP_BIND 265 268 GTP. {ECO:0000255|HAMAP-Rule:MF_00900}. FT NP_BIND 331 334 GTP. {ECO:0000255|HAMAP-Rule:MF_00900}. FT NP_BIND 360 362 GTP. {ECO:0000255|HAMAP-Rule:MF_00900}. FT METAL 225 225 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_00900}. FT METAL 245 245 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_00900}. SQ SEQUENCE 437 AA; 48734 MW; 6B41523F102F479A CRC64; MFEIREKPEM VERAMLVSVY FDPSEAGEKQ AMLDELEDLV SNLGIGIAGK HLIKSRDMHA KFLCGTGKAQ EVKQLALDCR ADCVVFDNML SPSQQREWER LVDECVIDRE EVILDIFARR ARTREATLQV ELARMQYSLP RMARMWNHLD RQGGGSGGGK GGGGAARGEG EKQIEVDRRL ARARIEAIQR ELVLVTRQRA TQRKERERQA VATAAIVGYT NAGKSSLLSL VSGSEVMARD MLFATLDTTT RKIELPHGQP LLLTDTVGFI RNLPHRLVEA FKSTLEEAVL ADFLIQVVDA SDPEAVRHYE TTLEVLNELG AGDKPMIVVL NKVDLVPEER RGALETLLAP HFSGRVVPMS VKEGNGEGDL LNACVEMLES RVRRARFLIP YTRSDLVAAM HSEGKVFSTE YVEEGTLLEA VLPVAFYNKL ESFLADR // ID HFLX_BACPE Reviewed; 423 AA. AC D3FTV4; DT 21-SEP-2011, integrated into UniProtKB/Swiss-Prot. DT 23-MAR-2010, sequence version 1. DT 07-JUN-2017, entry version 53. DE RecName: Full=GTPase HflX {ECO:0000255|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000255|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000255|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=BpOF4_19480; OS Bacillus pseudofirmus (strain OF4). OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus. OX NCBI_TaxID=398511; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=OF4; RX PubMed=21951522; DOI=10.1111/j.1462-2920.2011.02591.x; RA Janto B., Ahmed A., Ito M., Liu J., Hicks D.B., Pagni S., RA Fackelmayer O.J., Smith T.A., Earl J., Elbourne L.D., Hassan K., RA Paulsen I.T., Kolsto A.B., Tourasse N.J., Ehrlich G.D., Boissy R., RA Ivey D.M., Li G., Xue Y., Ma Y., Hu F.Z., Krulwich T.A.; RT "Genome of alkaliphilic Bacillus pseudofirmus OF4 reveals adaptations RT that support the ability to grow in an external pH range from 7.5 to RT 11.4."; RL Environ. Microbiol. 13:3289-3309(2011). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000255|HAMAP-Rule:MF_00900}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00900}; CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000255|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000255|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000255|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001878; ADC51935.1; -; Genomic_DNA. DR RefSeq; WP_012959297.1; NC_013791.2. DR ProteinModelPortal; D3FTV4; -. DR SMR; D3FTV4; -. DR STRING; 398511.BpOF4_19480; -. DR EnsemblBacteria; ADC51935; ADC51935; BpOF4_19480. DR KEGG; bpf:BpOF4_19480; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000001544; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; GTP-binding; Magnesium; Metal-binding; KW Nucleotide-binding; Reference proteome. FT CHAIN 1 423 GTPase HflX. FT /FTId=PRO_0000412654. FT DOMAIN 201 363 Hflx-type G. {ECO:0000255|HAMAP- FT Rule:MF_00900}. FT NP_BIND 207 214 GTP. {ECO:0000255|HAMAP-Rule:MF_00900}. FT NP_BIND 232 236 GTP. {ECO:0000255|HAMAP-Rule:MF_00900}. FT NP_BIND 254 257 GTP. {ECO:0000255|HAMAP-Rule:MF_00900}. FT NP_BIND 320 323 GTP. {ECO:0000255|HAMAP-Rule:MF_00900}. FT NP_BIND 341 343 GTP. {ECO:0000255|HAMAP-Rule:MF_00900}. FT METAL 214 214 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_00900}. FT METAL 234 234 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_00900}. SQ SEQUENCE 423 AA; 47943 MW; FD2BDDCE48FDD701 CRC64; MQDIKQRDIE HVILVGCQVN REDEEFEQSI AELESLAKTA KGKVVGTITQ KREKVESSTY VGKGKVQELV HLIEETEADL VIFNDELQAS QMRNLHAECG IAVIDRTQLI LDIFASRAKS REGKLQVELA QLKYLLPRLS GQGLALSRQG GGIGTRGPGE TQLETDRRHI RRRMNEIERQ LEAVVNHRVR YREKRKKNAA IQLALVGYTN AGKSTLLNRL TKADTLEEDQ LFATLDPTTR QLHLPSGFSV LMSDTVGFIQ DLPTTLVASF RSTLEELKEA DLLLHVVDCS HPDYEQHERT VIKLIEELEA HSIPQLLIYN KADQKTDVFI PTHTKDSIIM SAYNEEDLLA LKVKIEQALK GMMMPYRSII KADEGHILAA ARQETMIHTQ QFDESREAYV IEGHALENTS IYSQLKERLL KES // ID HFLX_BACSU Reviewed; 420 AA. AC P94478; Q796I0; DT 20-JAN-2009, integrated into UniProtKB/Swiss-Prot. DT 26-MAY-2009, sequence version 2. DT 07-JUN-2017, entry version 107. DE RecName: Full=GTPase HflX {ECO:0000255|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000255|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000255|HAMAP-Rule:MF_00900}; Synonyms=ynbA; GN OrderedLocusNames=BSU17430; OS Bacillus subtilis (strain 168). OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus. OX NCBI_TaxID=224308; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RA Borchert S., Klein C., Piksa B., Hammelmann M., Entian K.-D.; RT "Sequencing of a 26 kb region of the Bacillus subtilis genome RT downstream of spoVJ."; RL Submitted (AUG-1996) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=168; RX PubMed=9384377; DOI=10.1038/36786; RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., RA Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., RA Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., RA Brouillet S., Bruschi C.V., Caldwell B., Capuano V., Carter N.M., RA Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., RA Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., RA Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., RA Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., RA Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., RA Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., RA Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., RA Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., RA Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., RA Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., RA Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., RA Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., RA Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., RA Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., RA Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., RA Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., RA Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., RA Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., RA Yoshikawa H., Danchin A.; RT "The complete genome sequence of the Gram-positive bacterium Bacillus RT subtilis."; RL Nature 390:249-256(1997). RN [3] RP SEQUENCE REVISION TO 114; 181 AND C-TERMINUS. RX PubMed=19383706; DOI=10.1099/mic.0.027839-0; RA Barbe V., Cruveiller S., Kunst F., Lenoble P., Meurice G., RA Sekowska A., Vallenet D., Wang T., Moszer I., Medigue C., Danchin A.; RT "From a consortium sequence to a unified sequence: the Bacillus RT subtilis 168 reference genome a decade later."; RL Microbiology 155:1758-1775(2009). RN [4] RP DISRUPTION PHENOTYPE. RC STRAIN=CRK6000; RX PubMed=12427945; RA Morimoto T., Loh P.C., Hirai T., Asai K., Kobayashi K., Moriya S., RA Ogasawara N.; RT "Six GTP-binding proteins of the Era/Obg family are essential for cell RT growth in Bacillus subtilis."; RL Microbiology 148:3539-3552(2002). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000255|HAMAP-Rule:MF_00900}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00900}; CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000255|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000255|HAMAP- CC Rule:MF_00900}. CC -!- DISRUPTION PHENOTYPE: No visible phenotype. CC {ECO:0000269|PubMed:12427945}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000255|HAMAP- CC Rule:MF_00900}. CC -!- SEQUENCE CAUTION: CC Sequence=AAB41077.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305}; CC Sequence=AAB41077.1; Type=Frameshift; Positions=330; Evidence={ECO:0000305}; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U66480; AAB41077.1; ALT_FRAME; Genomic_DNA. DR EMBL; AL009126; CAB13627.2; -; Genomic_DNA. DR PIR; B69888; B69888. DR RefSeq; NP_389625.2; NC_000964.3. DR RefSeq; WP_003245432.1; NZ_JNCM01000035.1. DR ProteinModelPortal; P94478; -. DR STRING; 224308.Bsubs1_010100009591; -. DR PaxDb; P94478; -. DR PRIDE; P94478; -. DR EnsemblBacteria; CAB13627; CAB13627; BSU17430. DR GeneID; 938169; -. DR KEGG; bsu:BSU17430; -. DR PATRIC; fig|224308.179.peg.1891; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR InParanoid; P94478; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR PhylomeDB; P94478; -. DR BioCyc; BSUB:BSU17430-MONOMER; -. DR Proteomes; UP000001570; Chromosome. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0043022; F:ribosome binding; IBA:GO_Central. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; GTP-binding; Magnesium; Metal-binding; KW Nucleotide-binding; Reference proteome. FT CHAIN 1 420 GTPase HflX. FT /FTId=PRO_0000360644. FT DOMAIN 201 363 Hflx-type G. {ECO:0000255|HAMAP- FT Rule:MF_00900}. FT NP_BIND 207 214 GTP. {ECO:0000255|HAMAP-Rule:MF_00900}. FT NP_BIND 232 236 GTP. {ECO:0000255|HAMAP-Rule:MF_00900}. FT NP_BIND 254 257 GTP. {ECO:0000255|HAMAP-Rule:MF_00900}. FT NP_BIND 320 323 GTP. {ECO:0000255|HAMAP-Rule:MF_00900}. FT NP_BIND 341 343 GTP. {ECO:0000255|HAMAP-Rule:MF_00900}. FT METAL 214 214 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_00900}. FT METAL 234 234 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_00900}. FT CONFLICT 114 114 F -> L (in Ref. 1; AAB41077). FT {ECO:0000305}. FT CONFLICT 181 181 L -> V (in Ref. 1; AAB41077). FT {ECO:0000305}. SQ SEQUENCE 420 AA; 47638 MW; A197FA648E9C1949 CRC64; MNEQETIQEK AILVGCQLPH ITDEHFENSM EELASLTKTA DGKVLTSVTQ KRNRADAATY IGKGKVEELK ALVEELEADL LIFNDELSPS QLKSLATAIE VKMIDRTQLI LDIFAKRART REGKLQIELA QLQYALPRLT GQGINLSRQG GGIGARGPGE TKLETDRRHI RNRIHEINTQ LSTVIRHRSR YRERRKKNGV LQIALVGYTN AGKSTWFNRL TSADSYEEDL LFATLDPMTR KMVLPSGYSV LLSDTVGFIQ DLPTTLIAAF RSTLEEVKEA DLILHLIDSS NEDYAGHEKT VLRLLEELEA DDIPMLTAYN KRDQKLPDFI PTAGRDHIMV SAKFEDDAAA FKEAIQRYLR QELLTSFEAH VPASEGKLLS RIKSETMVDR FYFNEENEQY DISGYVQEEQ SIIGELKKYM // ID HFLX_CALS4 Reviewed; 428 AA. AC Q8RAS5; DT 21-SEP-2011, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2002, sequence version 1. DT 07-JUN-2017, entry version 81. DE RecName: Full=GTPase HflX {ECO:0000255|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000255|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000255|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=TTE1127; OS Caldanaerobacter subterraneus subsp. tengcongensis (strain DSM 15242 / OS JCM 11007 / NBRC 100824 / MB4) (Thermoanaerobacter tengcongensis). OC Bacteria; Firmicutes; Clostridia; Thermoanaerobacterales; OC Thermoanaerobacteraceae; Caldanaerobacter. OX NCBI_TaxID=273068; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 15242 / JCM 11007 / NBRC 100824 / MB4; RX PubMed=11997336; DOI=10.1101/gr.219302; RA Bao Q., Tian Y., Li W., Xu Z., Xuan Z., Hu S., Dong W., Yang J., RA Chen Y., Xue Y., Xu Y., Lai X., Huang L., Dong X., Ma Y., Ling L., RA Tan H., Chen R., Wang J., Yu J., Yang H.; RT "A complete sequence of the T. tengcongensis genome."; RL Genome Res. 12:689-700(2002). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000255|HAMAP-Rule:MF_00900}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00900}; CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000255|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000255|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000255|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE008691; AAM24362.1; -; Genomic_DNA. DR ProteinModelPortal; Q8RAS5; -. DR SMR; Q8RAS5; -. DR STRING; 273068.TTE1127; -. DR PRIDE; Q8RAS5; -. DR EnsemblBacteria; AAM24362; AAM24362; TTE1127. DR KEGG; tte:TTE1127; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000000555; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; GTP-binding; Magnesium; Metal-binding; KW Nucleotide-binding; Reference proteome. FT CHAIN 1 428 GTPase HflX. FT /FTId=PRO_0000412663. FT DOMAIN 214 374 Hflx-type G. {ECO:0000255|HAMAP- FT Rule:MF_00900}. FT NP_BIND 220 227 GTP. {ECO:0000255|HAMAP-Rule:MF_00900}. FT NP_BIND 245 249 GTP. {ECO:0000255|HAMAP-Rule:MF_00900}. FT NP_BIND 267 270 GTP. {ECO:0000255|HAMAP-Rule:MF_00900}. FT NP_BIND 333 336 GTP. {ECO:0000255|HAMAP-Rule:MF_00900}. FT NP_BIND 352 354 GTP. {ECO:0000255|HAMAP-Rule:MF_00900}. FT METAL 227 227 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_00900}. FT METAL 247 247 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_00900}. SQ SEQUENCE 428 AA; 48467 MW; 9343788413CFDCA4 CRC64; MQKIEYIIIT KLWVGDCMEE LARDKERAIL VAIISSPEDE ETLNELKELA VTAGAEVIGI LTQKKKGINK AHYIGKGKLE ELKMFVENQQ ADLVIVNDEL TGTQIKNLED ALGVKIVDRT NLILDIFAKR ARSKEGMLQV ELAQLKYRLP RLVGLGGQLS RLGGGIGTRG PGETKLEVDR RHIRNRIKAI EEKLEELEKH RNLQRQRRKK NQIPVVAIVG YTNAGKSTLL NALTGADAYV EDKLFATLDP TARKLVLPSG REVILTDTVG FIRKLPHDLV EAFKSTLEEV KYADLLLHVI DVTSPDMDEK IKVVEKVLSD LGAIETPRIN VYNKIDLLEI VPSGNNRDIY ISAKNKIGLD RLLEAIEREL FKETEVVSFL FPYEKTREYN YLKERGKVIE EDFDEKGISV KAEVTCEIKE RLRNFIIS // ID HFLX_CARHZ Reviewed; 414 AA. AC Q3AFV0; DT 21-SEP-2011, integrated into UniProtKB/Swiss-Prot. DT 22-NOV-2005, sequence version 1. DT 05-JUL-2017, entry version 87. DE RecName: Full=GTPase HflX {ECO:0000255|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000255|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000255|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=CHY_0112; OS Carboxydothermus hydrogenoformans (strain ATCC BAA-161 / DSM 6008 / OS Z-2901). OC Bacteria; Firmicutes; Clostridia; Thermoanaerobacterales; OC Thermoanaerobacteraceae; Carboxydothermus. OX NCBI_TaxID=246194; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-161 / DSM 6008 / Z-2901; RX PubMed=16311624; DOI=10.1371/journal.pgen.0010065; RA Wu M., Ren Q., Durkin A.S., Daugherty S.C., Brinkac L.M., Dodson R.J., RA Madupu R., Sullivan S.A., Kolonay J.F., Nelson W.C., Tallon L.J., RA Jones K.M., Ulrich L.E., Gonzalez J.M., Zhulin I.B., Robb F.T., RA Eisen J.A.; RT "Life in hot carbon monoxide: the complete genome sequence of RT Carboxydothermus hydrogenoformans Z-2901."; RL PLoS Genet. 1:563-574(2005). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000255|HAMAP-Rule:MF_00900}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00900}; CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000255|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000255|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000255|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000141; ABB14230.1; -; Genomic_DNA. DR ProteinModelPortal; Q3AFV0; -. DR SMR; Q3AFV0; -. DR STRING; 246194.CHY_0112; -. DR EnsemblBacteria; ABB14230; ABB14230; CHY_0112. DR KEGG; chy:CHY_0112; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000002706; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; GTP-binding; Magnesium; Metal-binding; KW Nucleotide-binding; Reference proteome. FT CHAIN 1 414 GTPase HflX. FT /FTId=PRO_0000412655. FT DOMAIN 191 351 Hflx-type G. {ECO:0000255|HAMAP- FT Rule:MF_00900}. FT NP_BIND 197 204 GTP. {ECO:0000255|HAMAP-Rule:MF_00900}. FT NP_BIND 222 226 GTP. {ECO:0000255|HAMAP-Rule:MF_00900}. FT NP_BIND 244 247 GTP. {ECO:0000255|HAMAP-Rule:MF_00900}. FT NP_BIND 309 312 GTP. {ECO:0000255|HAMAP-Rule:MF_00900}. FT NP_BIND 329 331 GTP. {ECO:0000255|HAMAP-Rule:MF_00900}. FT METAL 204 204 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_00900}. FT METAL 224 224 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_00900}. SQ SEQUENCE 414 AA; 46383 MW; F664C4364143CDA6 CRC64; MEKALVAFLV ENLKKFPYQK EEFLALLKTR GIEAVDIISQ RLEHPVPATY FGYGKVQEIG ELLKKHNLNL LAVGGDLTPT QAKNLEEILE VTVVDRTQII LEIFAEHAHT HEGKIQVELA RLMYNLPRIT GLGRVLSRLG GGIGTRGPGE TKLEVLRRTI RKRIAELRRE LKEIEQNRKV KRSRRLEAGV PIVALVGYTN AGKSTLLNAL TGAGVLAEDK LFATLDPTVR KLTLPGGQKL LLIDTVGFIE NMPPLIKEAF KSTLEVVHEA ELILHVVDGA NPYREEQEAV VEKILTEMKV RVPVITVYNK VDLLPEPVLF LGKRAVAISA RTGYNMELLL KLIEENLFWQ EVTVKAVLPF AQAFKIGDLK ENLKLINLEY LPEGIEVTVA GPRERIARYL GREKLEESNG EKPV // ID HFLX_CLOSW Reviewed; 423 AA. AC D9R4W7; DT 21-SEP-2011, integrated into UniProtKB/Swiss-Prot. DT 05-OCT-2010, sequence version 1. DT 07-JUN-2017, entry version 49. DE RecName: Full=GTPase HflX {ECO:0000255|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000255|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000255|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Closa_2505; OS Clostridium saccharolyticum (strain ATCC 35040 / DSM 2544 / NRCC 2533 OS / WM1). OC Bacteria; Firmicutes; Clostridia; Clostridiales; Lachnospiraceae. OX NCBI_TaxID=610130; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 35040 / DSM 2544 / NRCC 2533 / WM1; RG US DOE Joint Genome Institute; RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L., RA Pitluck S., Chertkov O., Detter J.C., Han C., Tapia R., Land M., RA Hauser L., Chang Y.-J., Jeffries C., Kyrpides N., Ivanova N., RA Mikhailova N., Mouttaki H., Lin L., Zhou J., Hemme C.L., Woyke T.; RT "Complete sequence of Clostridium saccharolyticum WM1."; RL Submitted (JUL-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000255|HAMAP-Rule:MF_00900}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00900}; CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000255|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000255|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000255|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002109; ADL05074.1; -; Genomic_DNA. DR RefSeq; WP_013273160.1; NC_014376.1. DR ProteinModelPortal; D9R4W7; -. DR STRING; 610130.Closa_2505; -. DR EnsemblBacteria; ADL05074; ADL05074; Closa_2505. DR KEGG; csh:Closa_2505; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000001662; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; GTP-binding; Magnesium; Metal-binding; KW Nucleotide-binding; Reference proteome. FT CHAIN 1 423 GTPase HflX. FT /FTId=PRO_0000412656. FT DOMAIN 202 366 Hflx-type G. {ECO:0000255|HAMAP- FT Rule:MF_00900}. FT NP_BIND 208 215 GTP. {ECO:0000255|HAMAP-Rule:MF_00900}. FT NP_BIND 233 237 GTP. {ECO:0000255|HAMAP-Rule:MF_00900}. FT NP_BIND 255 258 GTP. {ECO:0000255|HAMAP-Rule:MF_00900}. FT NP_BIND 321 324 GTP. {ECO:0000255|HAMAP-Rule:MF_00900}. FT NP_BIND 344 346 GTP. {ECO:0000255|HAMAP-Rule:MF_00900}. FT METAL 215 215 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_00900}. FT METAL 235 235 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_00900}. SQ SEQUENCE 423 AA; 47413 MW; 60D92596229A2EF3 CRC64; MTELIELKEI EERVILVAVS TGDEEDAKGS LDELEELVKT AGAVAVDKVI QNRERIHPGT YLGKGKIEEI KDRIWELDAT GIVCDDELSP AQLRNLEGAL DTKVMDRTMV ILDIFASRAV TREGKIQVEL AQLRYRSARL VGLRSSLSRL GGGIGTRGPG EKKLEMDRRL IHDRIGMLKA ELEDVKRHRE VVRQQRDKNH VPAAAIVGYT NAGKSTLLNR LTDAGILAED KLFATLDPTT RNLSLPGGQQ ILLTDTVGFI RKLPHHLIEA FKSTLEEAKY SDIILHVVDC SNPQMDMQMY VVYETLRELG ICDKIMITVF NKIDAADAGV ILRDVSSDHQ VRISAKTGEG LDELINLLET ILRNQKVYLE RIYSYKEAGK IQLIRKYGQL LKEEYQEDGI FVNAYVPSEL FASLADNADA FNE // ID HFLX_ECOLI Reviewed; 426 AA. AC P25519; Q2M6D2; DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1994, sequence version 3. DT 30-AUG-2017, entry version 137. DE RecName: Full=GTPase HflX {ECO:0000255|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000255|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000255|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=b4173, JW4131; OS Escherichia coli (strain K12). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=83333; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=8248183; DOI=10.1073/pnas.90.22.10866; RA Noble J.A., Innis M.A., Koonin E.V., Rudd K.E., Banuett F., RA Herskowitz I.; RT "The Escherichia coli hflA locus encodes a putative GTP-binding RT protein and two membrane proteins, one of which contains a protease- RT like domain."; RL Proc. Natl. Acad. Sci. U.S.A. 90:10866-10870(1993). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 / MG1655 / ATCC 47076; RX PubMed=7610040; DOI=10.1093/nar/23.12.2105; RA Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L., RA Blattner F.R.; RT "Analysis of the Escherichia coli genome VI: DNA sequence of the RT region from 92.8 through 100 minutes."; RL Nucleic Acids Res. 23:2105-2119(1995). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 / MG1655 / ATCC 47076; RX PubMed=9278503; DOI=10.1126/science.277.5331.1453; RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., RA Mau B., Shao Y.; RT "The complete genome sequence of Escherichia coli K-12."; RL Science 277:1453-1462(1997). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911; RX PubMed=16738553; DOI=10.1038/msb4100049; RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.; RT "Highly accurate genome sequences of Escherichia coli K-12 strains RT MG1655 and W3110."; RL Mol. Syst. Biol. 2:E1-E5(2006). RN [5] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-56. RX PubMed=2020545; DOI=10.1093/nar/19.5.1063; RA Kajitani M., Ishihama A.; RT "Identification and sequence determination of the host factor gene for RT bacteriophage Q beta."; RL Nucleic Acids Res. 19:1063-1066(1991). RN [6] RP PRELIMINARY FUNCTION. RX PubMed=3040675; DOI=10.1128/jb.169.9.4076-4085.1987; RA Banuett F., Herskowitz I.; RT "Identification of polypeptides encoded by an Escherichia coli locus RT (hflA) that governs the lysis-lysogeny decision of bacteriophage RT lambda."; RL J. Bacteriol. 169:4076-4085(1987). RN [7] RP FUNCTION, ENZYME REGULATION, SUBUNIT, INTERACTION WITH 50S SUBUNIT, RP AND DOMAIN. RX PubMed=19109926; DOI=10.1016/j.bbrc.2008.12.072; RA Jain N., Dhimole N., Khan A.R., De D., Tomar S.K., Sajish M., RA Dutta D., Parrack P., Prakash B.; RT "E. coli HflX interacts with 50S ribosomal subunits in presence of RT nucleotides."; RL Biochem. Biophys. Res. Commun. 379:201-205(2009). RN [8] RP FUNCTION, AND ENZYME REGULATION. RX PubMed=19824612; DOI=10.1021/bi901074h; RA Shields M.J., Fischer J.J., Wieden H.J.; RT "Toward understanding the function of the universally conserved GTPase RT HflX from Escherichia coli: a kinetic approach."; RL Biochemistry 48:10793-10802(2009). RN [9] RP FUNCTION AS A GTPASE, ENZYME REGULATION, SUBUNIT, SUBCELLULAR RP LOCATION, AND DISRUPTION PHENOTYPE. RC STRAIN=K12; RX PubMed=19181811; DOI=10.1128/JB.01353-08; RA Dutta D., Bandyopadhyay K., Datta A.B., Sardesai A.A., Parrack P.; RT "Properties of HflX, an enigmatic protein from Escherichia coli."; RL J. Bacteriol. 191:2307-2314(2009). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. In vitro, also exhibits ATPase activity. CC {ECO:0000255|HAMAP-Rule:MF_00900, ECO:0000269|PubMed:19109926, CC ECO:0000269|PubMed:19181811, ECO:0000269|PubMed:19824612}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00900}; CC -!- ENZYME REGULATION: Intrinsic GTPase activity is very slow and can CC be stimulated by the presence of 50S ribosomal subunits or 70S CC ribosomes. GTPase activity is inhibited by ATP. CC {ECO:0000269|PubMed:19109926, ECO:0000269|PubMed:19181811, CC ECO:0000269|PubMed:19824612}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. This CC interaction occurs in the presence of GTP, GDP, ATP or ADP, but CC not in their absence. {ECO:0000255|HAMAP-Rule:MF_00900, CC ECO:0000269|PubMed:19109926, ECO:0000269|PubMed:19181811}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00900, CC ECO:0000269|PubMed:19181811}. Note=May associate with membranes. CC -!- DOMAIN: Full-length protein is required for specific association CC with the 50S ribosomal subunit. {ECO:0000269|PubMed:19109926}. CC -!- DISRUPTION PHENOTYPE: Disruption does not affect lambda lysogeny CC or the transposition frequency of transposable elements. CC {ECO:0000269|PubMed:19181811}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000255|HAMAP- CC Rule:MF_00900}. CC -!- SEQUENCE CAUTION: CC Sequence=BAA00645.1; Type=Frameshift; Positions=18; Evidence={ECO:0000305}; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U00005; AAC43398.1; -; Unassigned_DNA. DR EMBL; U14003; AAA97069.1; -; Genomic_DNA. DR EMBL; U00096; AAC77130.1; -; Genomic_DNA. DR EMBL; AP009048; BAE78174.1; -; Genomic_DNA. DR EMBL; D00743; BAA00645.1; ALT_FRAME; Genomic_DNA. DR PIR; S56398; S56398. DR RefSeq; NP_418594.1; NC_000913.3. DR RefSeq; WP_000460362.1; NZ_LN832404.1. DR PDB; 5ADY; EM; 4.50 A; 6=1-426. DR PDBsum; 5ADY; -. DR ProteinModelPortal; P25519; -. DR SMR; P25519; -. DR BioGrid; 4261252; 360. DR DIP; DIP-9895N; -. DR IntAct; P25519; 1. DR STRING; 316385.ECDH10B_4368; -. DR PaxDb; P25519; -. DR PRIDE; P25519; -. DR EnsemblBacteria; AAC77130; AAC77130; b4173. DR EnsemblBacteria; BAE78174; BAE78174; BAE78174. DR GeneID; 948688; -. DR KEGG; ecj:JW4131; -. DR KEGG; eco:b4173; -. DR PATRIC; fig|1411691.4.peg.2528; -. DR EchoBASE; EB0432; -. DR EcoGene; EG10437; hflX. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR InParanoid; P25519; -. DR KO; K03665; -. DR PhylomeDB; P25519; -. DR BioCyc; EcoCyc:EG10437-MONOMER; -. DR BioCyc; MetaCyc:EG10437-MONOMER; -. DR PRO; PR:P25519; -. DR Proteomes; UP000000318; Chromosome. DR Proteomes; UP000000625; Chromosome. DR GO; GO:0005737; C:cytoplasm; IDA:EcoliWiki. DR GO; GO:0005829; C:cytosol; IDA:EcoCyc. DR GO; GO:0005524; F:ATP binding; IDA:EcoliWiki. DR GO; GO:0016887; F:ATPase activity; IDA:EcoCyc. DR GO; GO:0005525; F:GTP binding; IDA:EcoCyc. DR GO; GO:0003924; F:GTPase activity; IDA:EcoCyc. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0043023; F:ribosomal large subunit binding; IDA:EcoCyc. DR GO; GO:0043022; F:ribosome binding; IDA:EcoCyc. DR GO; GO:0019843; F:rRNA binding; IDA:EcoCyc. DR GO; GO:0036289; P:peptidyl-serine autophosphorylation; IDA:EcoCyc. DR GO; GO:0072344; P:rescue of stalled ribosome; IDA:EcoCyc. DR GO; GO:0009408; P:response to heat; IMP:EcoCyc. DR GO; GO:0032790; P:ribosome disassembly; IDA:EcoCyc. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 1: Evidence at protein level; KW 3D-structure; ATP-binding; Complete proteome; Cytoplasm; GTP-binding; KW Magnesium; Metal-binding; Nucleotide-binding; Reference proteome. FT CHAIN 1 426 GTPase HflX. FT /FTId=PRO_0000122463. FT DOMAIN 198 365 Hflx-type G. {ECO:0000255|HAMAP- FT Rule:MF_00900}. FT NP_BIND 204 211 GTP. {ECO:0000255|HAMAP-Rule:MF_00900}. FT NP_BIND 229 233 GTP. {ECO:0000255|HAMAP-Rule:MF_00900}. FT NP_BIND 251 254 GTP. {ECO:0000255|HAMAP-Rule:MF_00900}. FT NP_BIND 317 320 GTP. {ECO:0000255|HAMAP-Rule:MF_00900}. FT NP_BIND 343 345 GTP. {ECO:0000255|HAMAP-Rule:MF_00900}. FT METAL 211 211 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_00900}. FT METAL 231 231 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_00900}. FT CONFLICT 53 53 H -> R (in Ref. 5; BAA00645). FT {ECO:0000305}. FT CONFLICT 56 56 Y -> S (in Ref. 5; BAA00645). FT {ECO:0000305}. SQ SEQUENCE 426 AA; 48327 MW; 8D0A5BE92EE32591 CRC64; MFDRYDAGEQ AVLVHIYFTQ DKDMEDLQEF ESLVSSAGVE ALQVITGSRK APHPKYFVGE GKAVEIAEAV KATGASVVLF DHALSPAQER NLERLCECRV IDRTGLILDI FAQRARTHEG KLQVELAQLR HLATRLVRGW THLERQKGGI GLRGPGETQL ETDRRLLRNR IVQIQSRLER VEKQREQGRQ SRIKADVPTV SLVGYTNAGK STLFNRITEA RVYAADQLFA TLDPTLRRID VADVGETVLA DTVGFIRHLP HDLVAAFKAT LQETRQATLL LHVIDAADVR VQENIEAVNT VLEEIDAHEI PTLLVMNKID MLEDFEPRID RDEENKPNRV WLSAQTGAGI PQLFQALTER LSGEVAQHTL RLPPQEGRLR SRFYQLQAIE KEWMEEDGSV SLQVRMPIVD WRRLCKQEPA LIDYLI // ID HFLX_FLAPJ Reviewed; 413 AA. AC A6H294; DT 21-SEP-2011, integrated into UniProtKB/Swiss-Prot. DT 24-JUL-2007, sequence version 1. DT 07-JUN-2017, entry version 63. DE RecName: Full=GTPase HflX {ECO:0000255|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000255|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000255|HAMAP-Rule:MF_00900}; OrderedLocusNames=FP2414; OS Flavobacterium psychrophilum (strain JIP02/86 / ATCC 49511). OC Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales; OC Flavobacteriaceae; Flavobacterium. OX NCBI_TaxID=402612; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=JIP02/86 / ATCC 49511; RX PubMed=17592475; DOI=10.1038/nbt1313; RA Duchaud E., Boussaha M., Loux V., Bernardet J.-F., Michel C., RA Kerouault B., Mondot S., Nicolas P., Bossy R., Caron C., Bessieres P., RA Gibrat J.-F., Claverol S., Dumetz F., Le Henaff M., Benmansour A.; RT "Complete genome sequence of the fish pathogen Flavobacterium RT psychrophilum."; RL Nat. Biotechnol. 25:763-769(2007). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000255|HAMAP-Rule:MF_00900}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00900}; CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000255|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000255|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000255|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AM398681; CAL44468.1; -; Genomic_DNA. DR RefSeq; WP_011964502.1; NC_009613.3. DR RefSeq; YP_001297269.1; NC_009613.3. DR ProteinModelPortal; A6H294; -. DR STRING; 402612.FP2414; -. DR EnsemblBacteria; CAL44468; CAL44468; FP2414. DR GeneID; 5299510; -. DR KEGG; fps:FP2414; -. DR PATRIC; fig|402612.5.peg.2470; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000006394; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; GTP-binding; Magnesium; Metal-binding; KW Nucleotide-binding; Reference proteome. FT CHAIN 1 413 GTPase HflX. FT /FTId=PRO_0000412657. FT DOMAIN 200 386 Hflx-type G. {ECO:0000255|HAMAP- FT Rule:MF_00900}. FT NP_BIND 206 213 GTP. {ECO:0000255|HAMAP-Rule:MF_00900}. FT NP_BIND 231 235 GTP. {ECO:0000255|HAMAP-Rule:MF_00900}. FT NP_BIND 252 255 GTP. {ECO:0000255|HAMAP-Rule:MF_00900}. FT NP_BIND 318 321 GTP. {ECO:0000255|HAMAP-Rule:MF_00900}. FT NP_BIND 364 366 GTP. {ECO:0000255|HAMAP-Rule:MF_00900}. FT METAL 213 213 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_00900}. FT METAL 233 233 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_00900}. SQ SEQUENCE 413 AA; 47692 MW; 1F43C3801251A3AC CRC64; MLEKETINFE KTIIVGIVTQ NQSEEKLKEY LDELEFLTFT AGGEVVKRFS QKMERPNPKT FLGTGKIEEI NLYVLENGIS TIVFDDELTP SQQKNISKII DCKILDRTHL ILDIFAQRAE TSYARTQVEL AQCIYLLPRL SGMWTHLERQ KGGIGMRGPG ETEIETDRRI VRDRIALLKE KIKIIDKQQA TQRGNRGAMV RVALVGYTNV GKSTLMNAVG KSDVFVENKL FATLDTTVRK VVIKNLPFLL SDTVGFIRKL PTQLVDSFKS TLDEVREADL LLHVVDISHQ DFEDHIDAVN KILLDIKSAD KPTIMVFNKI DAYKHLTIDA DDLMTERTSK HYTLQEWKNT WMNKVGEQNA LFISATNKEN FEEFRKKVYE TVREIHITRF PYNKFLYPDY EDAIDKEEEQ DQD // ID HFLX_GLUDA Reviewed; 450 AA. AC A9H253; B5ZEJ7; DT 21-SEP-2011, integrated into UniProtKB/Swiss-Prot. DT 21-SEP-2011, sequence version 2. DT 30-AUG-2017, entry version 66. DE RecName: Full=GTPase HflX {ECO:0000255|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000255|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000255|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=GDI0162, Gdia_2232; OS Gluconacetobacter diazotrophicus (strain ATCC 49037 / DSM 5601 / OS PAl5). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales; OC Acetobacteraceae; Gluconacetobacter. OX NCBI_TaxID=272568; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 49037 / DSM 5601 / PAl5; RX PubMed=19775431; DOI=10.1186/1471-2164-10-450; RA Bertalan M., Albano R., de Padua V., Rouws L., Rojas C., Hemerly A., RA Teixeira K., Schwab S., Araujo J., Oliveira A., Franca L., RA Magalhaes V., Alqueres S., Cardoso A., Almeida W., Loureiro M.M., RA Nogueira E., Cidade D., Oliveira D., Simao T., Macedo J., Valadao A., RA Dreschsel M., Freitas F., Vidal M., Guedes H., Rodrigues E., RA Meneses C., Brioso P., Pozzer L., Figueiredo D., Montano H., RA Junior J., de Souza Filho G., Martin Quintana Flores V., Ferreira B., RA Branco A., Gonzalez P., Guillobel H., Lemos M., Seibel L., Macedo J., RA Alves-Ferreira M., Sachetto-Martins G., Coelho A., Santos E., RA Amaral G., Neves A., Pacheco A.B., Carvalho D., Lery L., Bisch P., RA Rossle S.C., Urmenyi T., Rael Pereira A., Silva R., Rondinelli E., RA von Kruger W., Martins O., Baldani J.I., Ferreira P.C.; RT "Complete genome sequence of the sugarcane nitrogen-fixing endophyte RT Gluconacetobacter diazotrophicus Pal5."; RL BMC Genomics 10:450-450(2009). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 49037 / DSM 5601 / PAl5; RX PubMed=21304715; DOI=10.4056/sigs.972221; RA Giongo A., Tyler H.L., Zipperer U.N., Triplett E.W.; RT "Two genome sequences of the same bacterial strain, Gluconacetobacter RT diazotrophicus PAl 5, suggest a new standard in genome sequence RT submission."; RL Stand. Genomic Sci. 2:309-317(2010). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000255|HAMAP-Rule:MF_00900}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00900}; CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000255|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000255|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000255|HAMAP- CC Rule:MF_00900}. CC -!- SEQUENCE CAUTION: CC Sequence=CAP54105.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305}; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AM889285; CAP54105.1; ALT_INIT; Genomic_DNA. DR EMBL; CP001189; ACI51987.1; -; Genomic_DNA. DR RefSeq; WP_012222401.1; NC_010125.1. DR STRING; 272568.GDI_0162; -. DR EnsemblBacteria; ACI51987; ACI51987; Gdia_2232. DR EnsemblBacteria; CAP54105; CAP54105; GDI0162. DR KEGG; gdi:GDI0162; -. DR KEGG; gdj:Gdia_2232; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000000736; Chromosome. DR Proteomes; UP000001176; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; GTP-binding; Magnesium; Metal-binding; KW Nucleotide-binding; Reference proteome. FT CHAIN 1 450 GTPase HflX. FT /FTId=PRO_0000412658. FT DOMAIN 230 395 Hflx-type G. {ECO:0000255|HAMAP- FT Rule:MF_00900}. FT NP_BIND 236 243 GTP. {ECO:0000255|HAMAP-Rule:MF_00900}. FT NP_BIND 261 265 GTP. {ECO:0000255|HAMAP-Rule:MF_00900}. FT NP_BIND 283 286 GTP. {ECO:0000255|HAMAP-Rule:MF_00900}. FT NP_BIND 349 352 GTP. {ECO:0000255|HAMAP-Rule:MF_00900}. FT NP_BIND 373 375 GTP. {ECO:0000255|HAMAP-Rule:MF_00900}. FT METAL 243 243 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_00900}. FT METAL 263 263 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_00900}. FT CONFLICT 103 105 PEP -> AEA (in Ref. 2; ACI51987). FT {ECO:0000305}. FT CONFLICT 177 177 S -> T (in Ref. 2; ACI51987). FT {ECO:0000305}. FT CONFLICT 341 341 A -> T (in Ref. 2; ACI51987). FT {ECO:0000305}. FT CONFLICT 376 378 APG -> TPA (in Ref. 2; ACI51987). FT {ECO:0000305}. SQ SEQUENCE 450 AA; 48648 MW; 36A8F244A9E7C74C CRC64; METKPPIPLA VLVGIQTPDV DDIAHEASLA ELGRLVKTLG YAVVGTVSQK REGTGAALLL GSGKLAELAA LTGGTGVVTS MAPPPKSKAR QRFEGAAEGA APPEPDPDAA RRPEFVIVDH ELSPSQIRNL ERATGAQVLD RTGVIVEIFH RHANTREARL QVEMARLKYV APRLRESSGG GGRQQGPGAG ESTLALDRRK IRDRLAELKT QLDAVQRDGD QRRSARRDQL RVALVGYTNA GKSSLMRALT GSQVLVEDKL FATLDTTVRI LQPETRPRIL VSDTVGFIKQ LPHDLVASFR STLAEALEAS LLLFVVDASD PTYESQLEVT RGVLREIGAD AVPSRLVLNK MDRLDPAARA ALRDKHPDAI MLSAHAPGDV SALRDTLIAF FEAEMVEDTL VLPYAKQGLI GEIYESARVL SEDHDETGRV LKVRALPAAI TRLKRSLAAR // ID HFLX_HYPBU Reviewed; 375 AA. AC A2BLW4; DT 21-SEP-2011, integrated into UniProtKB/Swiss-Prot. DT 20-FEB-2007, sequence version 1. DT 07-JUN-2017, entry version 71. DE RecName: Full=GTPase HflX {ECO:0000255|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000255|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000255|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Hbut_1138; OS Hyperthermus butylicus (strain DSM 5456 / JCM 9403 / PLM1-5). OC Archaea; Crenarchaeota; Thermoprotei; Desulfurococcales; OC Pyrodictiaceae; Hyperthermus. OX NCBI_TaxID=415426; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 5456 / JCM 9403 / PLM1-5; RX PubMed=17350933; DOI=10.1155/2007/745987; RA Bruegger K., Chen L., Stark M., Zibat A., Redder P., Ruepp A., RA Awayez M., She Q., Garrett R.A., Klenk H.-P.; RT "The genome of Hyperthermus butylicus: a sulfur-reducing, peptide RT fermenting, neutrophilic Crenarchaeote growing up to 108 degrees C."; RL Archaea 2:127-135(2007). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000255|HAMAP-Rule:MF_00900}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00900}; CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000255|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000255|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000255|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000493; ABM80975.1; -; Genomic_DNA. DR RefSeq; WP_011822293.1; NC_008818.1. DR ProteinModelPortal; A2BLW4; -. DR SMR; A2BLW4; -. DR STRING; 415426.Hbut_1138; -. DR EnsemblBacteria; ABM80975; ABM80975; Hbut_1138. DR GeneID; 4782129; -. DR KEGG; hbu:Hbut_1138; -. DR eggNOG; arCOG00353; Archaea. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; FNNHAHV; -. DR OrthoDB; POG093Z07D6; -. DR BioCyc; HBUT415426:GC56-1138-MONOMER; -. DR Proteomes; UP000002593; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; GTP-binding; Magnesium; Metal-binding; KW Nucleotide-binding; Reference proteome. FT CHAIN 1 375 GTPase HflX. FT /FTId=PRO_0000412665. FT DOMAIN 194 371 Hflx-type G. {ECO:0000255|HAMAP- FT Rule:MF_00900}. FT NP_BIND 200 207 GTP. {ECO:0000255|HAMAP-Rule:MF_00900}. FT NP_BIND 225 229 GTP. {ECO:0000255|HAMAP-Rule:MF_00900}. FT NP_BIND 246 249 GTP. {ECO:0000255|HAMAP-Rule:MF_00900}. FT NP_BIND 314 317 GTP. {ECO:0000255|HAMAP-Rule:MF_00900}. FT NP_BIND 349 351 GTP. {ECO:0000255|HAMAP-Rule:MF_00900}. FT METAL 207 207 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_00900}. FT METAL 227 227 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_00900}. SQ SEQUENCE 375 AA; 41777 MW; EC6F3E05E26A011D CRC64; MAKVAVWKPS ILVLPRGLAR WEVREAYVLA ETAGYRVVDV LYYRRVSSSK LLSDAKLEEL AEKAKSLVGN EYARIIVYDN LKPREYFRIV KATGVNTIDR TMLILEIFSL HAGSREAKLQ IELARLRHEL PLVREAIRLS KLKELPGFLG PGGYAIDAYY RYMVSRIAKI KRELRELRRR HEIERSKRRS AGLPHIAIVG YASAGKTSLF NAITGLQKPV GPEYFTTITP KRRAISFNGL RTVFIDTVGF IMRIPPEIIE AFHSTLEEAA TADVILYVVD VSEPDTVIAE KLDEGLQTLR RIGVIDKPLI IAANKIDLVP QEDIERLTRL LEGAASTLYP ALEAVIPVSA KTGAGVAKLL CRIATLLAGT KGSTC // ID HFLX_MAGMM Reviewed; 432 AA. AC A0L4B2; DT 21-SEP-2011, integrated into UniProtKB/Swiss-Prot. DT 12-DEC-2006, sequence version 1. DT 07-JUN-2017, entry version 67. DE RecName: Full=GTPase HflX {ECO:0000255|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000255|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000255|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Mmc1_0278; OS Magnetococcus marinus (strain ATCC BAA-1437 / JCM 17883 / MC-1). OC Bacteria; Proteobacteria; Alphaproteobacteria; Magnetococcales; OC Magnetococcaceae; Magnetococcus. OX NCBI_TaxID=156889; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-1437 / JCM 17883 / MC-1; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., RA Pitluck S., Kiss H., Goodwin L.A., Brettin T., Bruce D., Han C., RA Tapia R., Gilna P., Schmutz J., Larimer F., Land M., Hauser L., RA Kyrpides N., Mikhailova N., Richardson P.; RT "Complete sequence of Magnetococcus sp. MC-1."; RL Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000255|HAMAP-Rule:MF_00900}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00900}; CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000255|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000255|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000255|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000471; ABK42805.1; -; Genomic_DNA. DR RefSeq; WP_011711977.1; NC_008576.1. DR ProteinModelPortal; A0L4B2; -. DR SMR; A0L4B2; -. DR STRING; 156889.Mmc1_0278; -. DR EnsemblBacteria; ABK42805; ABK42805; Mmc1_0278. DR KEGG; mgm:Mmc1_0278; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; FNNHAHV; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000002586; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; GTP-binding; Magnesium; Metal-binding; KW Nucleotide-binding; Reference proteome. FT CHAIN 1 432 GTPase HflX. FT /FTId=PRO_0000412661. FT DOMAIN 202 367 Hflx-type G. {ECO:0000255|HAMAP- FT Rule:MF_00900}. FT NP_BIND 208 215 GTP. {ECO:0000255|HAMAP-Rule:MF_00900}. FT NP_BIND 233 237 GTP. {ECO:0000255|HAMAP-Rule:MF_00900}. FT NP_BIND 255 258 GTP. {ECO:0000255|HAMAP-Rule:MF_00900}. FT NP_BIND 321 324 GTP. {ECO:0000255|HAMAP-Rule:MF_00900}. FT NP_BIND 345 347 GTP. {ECO:0000255|HAMAP-Rule:MF_00900}. FT METAL 215 215 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_00900}. FT METAL 235 235 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_00900}. SQ SEQUENCE 432 AA; 48556 MW; 1716F6945E85F9A2 CRC64; MLETHQAPDR AILLQALEPK VTRDACQRLL DELVHLSTTA GLEVHATQLL SLQKAVPATY FGSGQVEELA RRIEEDEIDV AVVNHALTPI QQRNLEKKLN AKVVDRTGLI LEIFAARART REGIMQVELA SLMYQQSRLV RSWTHLERQR GGVGLRGGPG ERQIEVDRRL IRERIHKLKK QLEEVERTRA LQRQPRQDIP LFTVALVGYT NAGKSTLFNL LTRAGVLAED KLFATLDPTM RAVDLPDGGR ILLSDTVGFI RQLPHQLVAA FKATLEEVMS ADMLLHVVDL SDPEWERYVE SVNGVLQELE VQHTRTLTVY NKIDRLESRG ILERELARGD TIGVSAQTGE GVEPLLSELR RAVGRAMLRY EVILPVSDGR WLAKFHAEAS VVEVREGEDF TTLIVELAPA VLGRLQGEVE REGVEVQFRP VD // ID HFLX_METJA Reviewed; 402 AA. AC Q58526; DT 14-NOV-2003, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 07-JUN-2017, entry version 102. DE RecName: Full=GTPase HflX {ECO:0000255|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000255|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000255|HAMAP-Rule:MF_00900}; OrderedLocusNames=MJ1126; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000255|HAMAP-Rule:MF_00900}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00900}; CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000255|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000255|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000255|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99128.1; -; Genomic_DNA. DR PIR; E64440; E64440. DR ProteinModelPortal; Q58526; -. DR STRING; 243232.MJ_1126; -. DR EnsemblBacteria; AAB99128; AAB99128; MJ_1126. DR KEGG; mja:MJ_1126; -. DR eggNOG; arCOG00353; Archaea. DR eggNOG; COG2262; LUCA. DR InParanoid; Q58526; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG093Z07D6; -. DR PhylomeDB; Q58526; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0043022; F:ribosome binding; IBA:GO_Central. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; GTP-binding; Magnesium; Metal-binding; KW Nucleotide-binding; Reference proteome. FT CHAIN 1 402 GTPase HflX. FT /FTId=PRO_0000205444. FT DOMAIN 181 350 Hflx-type G. {ECO:0000255|HAMAP- FT Rule:MF_00900}. FT NP_BIND 187 194 GTP. {ECO:0000255|HAMAP-Rule:MF_00900}. FT NP_BIND 212 216 GTP. {ECO:0000255|HAMAP-Rule:MF_00900}. FT NP_BIND 233 236 GTP. {ECO:0000255|HAMAP-Rule:MF_00900}. FT NP_BIND 300 303 GTP. {ECO:0000255|HAMAP-Rule:MF_00900}. FT NP_BIND 328 330 GTP. {ECO:0000255|HAMAP-Rule:MF_00900}. FT METAL 194 194 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_00900}. FT METAL 214 214 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_00900}. SQ SEQUENCE 402 AA; 46482 MW; 4DA94B9D200B77AF CRC64; MLILRKDSKF DRKSIEELKE LAEVLYNPVK TIVQIRKADP KYQIGSGLVE RIAENIKEEN IEIVIVGNIL TPSQKYNLAK KFKVEVIDKI ELVLRIFYKH ARTKEAQLQV RLAELQYELP RAREKVRLAK MGEQPGFGGY GDYEVEKYYQ KVKREIATIK RKLEKLREHR RVARKGRAKF DTVGLIGYTN AGKTSLLNAL TGENKESKNQ VFTTLTTTTR AIKGIKRKIL VTDTVGFIDD LPPFMIEAFL STIEESADSD LILIVVDASD DIEEIKRKLK VNHEILSKIN CKAPIITVFN KVDKITKEKK RKILEELDRY IVNPIFVSAK YDINMDLLKE MIIEHLNLSI GTIETDNPRL ISYLYENTEI IEDILEDNKH IITFRAKERD VNRILKLHKS AV // ID HFLX_NITMS Reviewed; 371 AA. AC A9A623; DT 21-SEP-2011, integrated into UniProtKB/Swiss-Prot. DT 15-JAN-2008, sequence version 1. DT 07-JUN-2017, entry version 64. DE RecName: Full=GTPase HflX {ECO:0000255|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000255|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000255|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Nmar_1605; OS Nitrosopumilus maritimus (strain SCM1). OC Archaea; Thaumarchaeota; Nitrosopumilales; Nitrosopumilaceae; OC Nitrosopumilus. OX NCBI_TaxID=436308; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SCM1; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., RA Dalin E., Tice H., Pitluck S., Chain P., Malfatti S., Shin M., RA Vergez L., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., RA Lykidis A., Stahl D., Richardson P.; RT "Complete sequence of Nitrosopumilus maritimus SCM1."; RL Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000255|HAMAP-Rule:MF_00900}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00900}; CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000255|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000255|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000255|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000866; ABX13501.1; -; Genomic_DNA. DR ProteinModelPortal; A9A623; -. DR STRING; 436308.Nmar_1605; -. DR EnsemblBacteria; ABX13501; ABX13501; Nmar_1605. DR KEGG; nmr:Nmar_1605; -. DR eggNOG; arCOG00353; Archaea. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR Proteomes; UP000000792; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; GTP-binding; Magnesium; Metal-binding; KW Nucleotide-binding; Reference proteome. FT CHAIN 1 371 GTPase HflX. FT /FTId=PRO_0000412666. FT DOMAIN 184 355 Hflx-type G. {ECO:0000255|HAMAP- FT Rule:MF_00900}. FT NP_BIND 190 197 GTP. {ECO:0000255|HAMAP-Rule:MF_00900}. FT NP_BIND 215 219 GTP. {ECO:0000255|HAMAP-Rule:MF_00900}. FT NP_BIND 236 239 GTP. {ECO:0000255|HAMAP-Rule:MF_00900}. FT NP_BIND 304 307 GTP. {ECO:0000255|HAMAP-Rule:MF_00900}. FT NP_BIND 333 335 GTP. {ECO:0000255|HAMAP-Rule:MF_00900}. FT METAL 197 197 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_00900}. FT METAL 217 217 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_00900}. SQ SEQUENCE 371 AA; 42035 MW; 6C9508383DD22C5D CRC64; MKSAILITYD KEDVINEAKG LCDAAGFQVV HTIKQKFLKR PKYGISGGIL ERLEEISEKI RPDVIVFDEV LKPSQNYNLA AALHREILDR EALILEIFES RASSAESKLQ VKLAQLRYEM ARAKEKVRLS SMGEQPGFMG IGKFEVDVYY NDIKHRMNTV RSKLEKAGKQ RELHRQGRKR MGFKTISLAG YTSAGKTTLF NMMTGETRDQ SSELFTTLST TTRRVSINQE PFLISDTVGF ISKLPAYMID AFKSTLEELG HTDIIIVVID IGDSIFELKK KFSSCMRTLS ELGVEKDRMV YALNKSDLLE HSEIEEKIET LNLVDNKKWI PVSAKTGKNV KQLKELIGDI LESHNSHKFG KKIGVEETFG N // ID HFLX_SULSO Reviewed; 356 AA. AC Q980M3; DT 21-SEP-2011, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2001, sequence version 1. DT 07-JUN-2017, entry version 112. DE RecName: Full=GTPase HflX {ECO:0000255|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000255|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000255|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=SSO0269; OS Sulfolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / OS P2). OC Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae; OC Sulfolobus. OX NCBI_TaxID=273057; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2; RX PubMed=11427726; DOI=10.1073/pnas.141222098; RA She Q., Singh R.K., Confalonieri F., Zivanovic Y., Allard G., RA Awayez M.J., Chan-Weiher C.C.-Y., Clausen I.G., Curtis B.A., RA De Moors A., Erauso G., Fletcher C., Gordon P.M.K., RA Heikamp-de Jong I., Jeffries A.C., Kozera C.J., Medina N., Peng X., RA Thi-Ngoc H.P., Redder P., Schenk M.E., Theriault C., Tolstrup N., RA Charlebois R.L., Doolittle W.F., Duguet M., Gaasterland T., RA Garrett R.A., Ragan M.A., Sensen C.W., Van der Oost J.; RT "The complete genome of the crenarchaeon Sulfolobus solfataricus P2."; RL Proc. Natl. Acad. Sci. U.S.A. 98:7835-7840(2001). RN [2] RP FUNCTION, ENZYME REGULATION, SUBUNIT, AND INTERACTION WITH 50S RP SUBUNIT. RC STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2; RX PubMed=21478358; DOI=10.1128/JB.01552-10; RA Blombach F., Launay H., Zorraquino V., Swarts D.C., Cabrita L.D., RA Benelli D., Christodoulou J., Londei P., van der Oost J.; RT "An HflX-Type GTPase from Sulfolobus solfataricus binds to the 50S RT ribosomal subunit in all nucleotide-bound states."; RL J. Bacteriol. 193:2861-2867(2011). RN [3] RP X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) OF WILD-TYPE IN COMPLEX WITH RP GDP AND OF MUTANTS PRO-235 AND SER-235, BIOPHYSICOCHEMICAL PROPERTIES, RP AND MUTAGENESIS OF ASN-189; THR-193; THR-213; GLY-235 AND PHE-236. RX PubMed=20400571; DOI=10.1093/jb/mvq039; RA Huang B., Wu H., Hao N., Blombach F., van der Oost J., Li X., RA Zhang X.C., Rao Z.; RT "Functional study on GTP hydrolysis by the GTP-binding protein from RT Sulfolobus solfataricus, a member of the HflX family."; RL J. Biochem. 148:103-113(2010). RN [4] RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) IN COMPLEX WITH GDP, FUNCTION RP AS A GTPASE, ENZYME REGULATION, AND SUBUNIT. RX PubMed=19787775; DOI=10.1002/prot.22599; RA Wu H., Sun L., Blombach F., Brouns S.J., Snijders A.P., Lorenzen K., RA van den Heuvel R.H., Heck A.J., Fu S., Li X., Zhang X.C., Rao Z., RA van der Oost J.; RT "Structure of the ribosome associating GTPase HflX."; RL Proteins 78:705-713(2010). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. Specific for GTP. {ECO:0000255|HAMAP-Rule:MF_00900, CC ECO:0000269|PubMed:19787775, ECO:0000269|PubMed:21478358}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00900}; CC -!- ENZYME REGULATION: GTPase activity is stimulated by the presence CC of 50S ribosomal subunits. Hydrolysis is probably regulated by the CC HflX N-terminal domain. {ECO:0000269|PubMed:19787775, CC ECO:0000269|PubMed:21478358}. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=5.3 uM for GTP {ECO:0000269|PubMed:20400571}; CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. Does CC not associate with 70S ribosomes. {ECO:0000255|HAMAP- CC Rule:MF_00900, ECO:0000269|PubMed:19787775, CC ECO:0000269|PubMed:20400571, ECO:0000269|PubMed:21478358}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000255|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000255|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE006641; AAK40607.1; -; Genomic_DNA. DR PIR; H90168; H90168. DR RefSeq; WP_009990543.1; NC_002754.1. DR PDB; 2QTF; X-ray; 2.00 A; A=1-356. DR PDB; 2QTH; X-ray; 2.00 A; A=1-356. DR PDB; 3KXI; X-ray; 2.65 A; A=1-356. DR PDB; 3KXK; X-ray; 2.35 A; A/B=1-356. DR PDB; 3KXL; X-ray; 2.50 A; A/B=1-356. DR PDBsum; 2QTF; -. DR PDBsum; 2QTH; -. DR PDBsum; 3KXI; -. DR PDBsum; 3KXK; -. DR PDBsum; 3KXL; -. DR ProteinModelPortal; Q980M3; -. DR SMR; Q980M3; -. DR STRING; 273057.SSO0269; -. DR EnsemblBacteria; AAK40607; AAK40607; SSO0269. DR GeneID; 27426564; -. DR KEGG; sso:SSO0269; -. DR PATRIC; fig|273057.12.peg.263; -. DR eggNOG; arCOG00353; Archaea. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR InParanoid; Q980M3; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG093Z07D6; -. DR BRENDA; 3.6.5.3; 6163. DR EvolutionaryTrace; Q980M3; -. DR Proteomes; UP000001974; Chromosome. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0043022; F:ribosome binding; IBA:GO_Central. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Cytoplasm; GTP-binding; Magnesium; KW Metal-binding; Nucleotide-binding; Reference proteome. FT CHAIN 1 356 GTPase HflX. FT /FTId=PRO_0000412528. FT DOMAIN 180 356 Hflx-type G. {ECO:0000255|HAMAP- FT Rule:MF_00900}. FT NP_BIND 186 193 GTP. {ECO:0000255|HAMAP-Rule:MF_00900, FT ECO:0000305|PubMed:19787775, FT ECO:0000305|PubMed:20400571}. FT NP_BIND 211 215 GTP. {ECO:0000255|HAMAP-Rule:MF_00900}. FT NP_BIND 232 235 GTP. {ECO:0000255|HAMAP-Rule:MF_00900}. FT NP_BIND 300 303 GTP. {ECO:0000255|HAMAP-Rule:MF_00900, FT ECO:0000305|PubMed:19787775, FT ECO:0000305|PubMed:20400571}. FT NP_BIND 334 336 GTP. {ECO:0000255|HAMAP-Rule:MF_00900, FT ECO:0000305|PubMed:19787775, FT ECO:0000305|PubMed:20400571}. FT METAL 193 193 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_00900}. FT METAL 213 213 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_00900}. FT MUTAGEN 189 189 N->P: Loss of GTPase activity. FT {ECO:0000269|PubMed:20400571}. FT MUTAGEN 193 193 T->N: Loss of GTPase activity. FT {ECO:0000269|PubMed:20400571}. FT MUTAGEN 213 213 T->V: Decrease in GTPase activity. FT {ECO:0000269|PubMed:20400571}. FT MUTAGEN 235 235 G->P: Loss of GTPase activity. FT {ECO:0000269|PubMed:20400571}. FT MUTAGEN 235 235 G->S: Decrease in GTPase activity. FT {ECO:0000269|PubMed:20400571}. FT MUTAGEN 236 236 F->P: Increase in KM for GTP and in FT GTPase activity. FT {ECO:0000269|PubMed:20400571}. FT STRAND 2 7 {ECO:0000244|PDB:2QTF}. FT TURN 10 12 {ECO:0000244|PDB:2QTF}. FT HELIX 13 22 {ECO:0000244|PDB:2QTF}. FT STRAND 25 31 {ECO:0000244|PDB:2QTF}. FT TURN 39 41 {ECO:0000244|PDB:2QTF}. FT HELIX 45 52 {ECO:0000244|PDB:2QTF}. FT STRAND 59 64 {ECO:0000244|PDB:2QTF}. FT HELIX 68 78 {ECO:0000244|PDB:2QTF}. FT STRAND 82 84 {ECO:0000244|PDB:2QTF}. FT HELIX 86 97 {ECO:0000244|PDB:2QTF}. FT HELIX 101 121 {ECO:0000244|PDB:2QTF}. FT HELIX 145 164 {ECO:0000244|PDB:2QTF}. FT STRAND 181 185 {ECO:0000244|PDB:2QTF}. FT TURN 188 191 {ECO:0000244|PDB:3KXK}. FT HELIX 192 200 {ECO:0000244|PDB:2QTF}. FT STRAND 218 223 {ECO:0000244|PDB:2QTF}. FT STRAND 226 232 {ECO:0000244|PDB:2QTF}. FT HELIX 242 244 {ECO:0000244|PDB:2QTF}. FT HELIX 245 253 {ECO:0000244|PDB:2QTF}. FT HELIX 254 257 {ECO:0000244|PDB:2QTF}. FT STRAND 258 266 {ECO:0000244|PDB:2QTF}. FT HELIX 271 288 {ECO:0000244|PDB:2QTF}. FT STRAND 295 300 {ECO:0000244|PDB:2QTF}. FT HELIX 302 304 {ECO:0000244|PDB:2QTF}. FT HELIX 309 323 {ECO:0000244|PDB:2QTF}. FT STRAND 327 332 {ECO:0000244|PDB:2QTF}. FT TURN 335 338 {ECO:0000244|PDB:2QTF}. FT HELIX 341 355 {ECO:0000244|PDB:2QTF}. SQ SEQUENCE 356 AA; 40538 MW; 602D4DBBE3BEAB1C CRC64; MKTAALFVSK EFEEEAIALV EGANYKVTSI YKLPKSPNVK FYIQYDKLQQ IKNDEEISTL IIFEQLKPRH FINIRRELKG KEVLDKILLL LEIFALHAGS KEAKMQIELA RLKYELPIIK ETYTKSKIGE QQGPLGAGTY GVESTIKFYK RRINKLMKEL ESIKIFKEKS IESNKRNNIP SIGIVGYTNS GKTSLFNSLT GLTQKVDTKL FTTMSPKRYA IPINNRKIML VDTVGFIRGI PPQIVDAFFV TLSEAKYSDA LILVIDSTFS ENLLIETLQS SFEILREIGV SGKPILVTLN KIDKINGDLY KKLDLVEKLS KELYSPIFDV IPISALKRTN LELLRDKIYQ LATQLS // ID HFLX_THEKO Reviewed; 442 AA. AC Q5JGB4; DT 21-SEP-2011, integrated into UniProtKB/Swiss-Prot. DT 15-FEB-2005, sequence version 1. DT 07-JUN-2017, entry version 89. DE RecName: Full=GTPase HflX {ECO:0000255|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000255|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000255|HAMAP-Rule:MF_00900}; OrderedLocusNames=TK1976; OS Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1) OS (Pyrococcus kodakaraensis (strain KOD1)). OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae; OC Thermococcus. OX NCBI_TaxID=69014; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-918 / JCM 12380 / KOD1; RX PubMed=15710748; DOI=10.1101/gr.3003105; RA Fukui T., Atomi H., Kanai T., Matsumi R., Fujiwara S., Imanaka T.; RT "Complete genome sequence of the hyperthermophilic archaeon RT Thermococcus kodakaraensis KOD1 and comparison with Pyrococcus RT genomes."; RL Genome Res. 15:352-363(2005). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000255|HAMAP-Rule:MF_00900}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00900}; CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000255|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000255|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000255|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AP006878; BAD86165.1; -; Genomic_DNA. DR RefSeq; WP_011250926.1; NC_006624.1. DR ProteinModelPortal; Q5JGB4; -. DR SMR; Q5JGB4; -. DR STRING; 69014.TK1976; -. DR EnsemblBacteria; BAD86165; BAD86165; TK1976. DR GeneID; 3235683; -. DR KEGG; tko:TK1976; -. DR PATRIC; fig|69014.16.peg.1931; -. DR eggNOG; arCOG00353; Archaea. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR InParanoid; Q5JGB4; -. DR KO; K03665; -. DR OMA; FNNHAHV; -. DR OrthoDB; POG093Z07D6; -. DR Proteomes; UP000000536; Chromosome. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0043022; F:ribosome binding; IBA:GO_Central. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; GTP-binding; Magnesium; Metal-binding; KW Nucleotide-binding; Reference proteome. FT CHAIN 1 442 GTPase HflX. FT /FTId=PRO_0000412667. FT DOMAIN 186 362 Hflx-type G. {ECO:0000255|HAMAP- FT Rule:MF_00900}. FT NP_BIND 192 199 GTP. {ECO:0000255|HAMAP-Rule:MF_00900}. FT NP_BIND 217 221 GTP. {ECO:0000255|HAMAP-Rule:MF_00900}. FT NP_BIND 238 241 GTP. {ECO:0000255|HAMAP-Rule:MF_00900}. FT NP_BIND 306 309 GTP. {ECO:0000255|HAMAP-Rule:MF_00900}. FT NP_BIND 341 343 GTP. {ECO:0000255|HAMAP-Rule:MF_00900}. FT METAL 199 199 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_00900}. FT METAL 219 219 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_00900}. SQ SEQUENCE 442 AA; 50606 MW; EEC96347DDC0D6DC CRC64; MRAIGVIRNS RRERLSRAEF EELLRSAGYE VLAIVEQNRE EHPRYNIGPG KLEELKELVK ELKPDKVIFA NRLTPSQAYN LWKELRIEIM DRWQLVLEIF EKRAHSKEAK LQVELASLQY EIPLVKEAIR RIRLGDRAGF KGMGEYQTQQ YLKHIRYRMG KIRDELERVK ADREVKRKKR ENAGFVLVAL AGYTNAGKST LLNALADENV EAKNQMFTTL DTTTRRFRLG TKRILATDTV GFIDGLPPFI VEAFHSTLEE IVKADIVLLV LDSSEPWGEI RRKFLASLQV LRELKALEKP IIVALNKIDL IEEADAEEKV RLIWELARER GISLEDVVKI SAREGRLEEL MDALNRVVLK LPKYGAFRII VKEPEKVPAV MALINSVGEV LSVEYGEKTR IDAYVQTGMV GEIKKMGAEI ERLNHSGEGE ELEQDEGYSD GG // ID HFLX_THEPD Reviewed; 424 AA. AC A1RY30; DT 21-SEP-2011, integrated into UniProtKB/Swiss-Prot. DT 06-FEB-2007, sequence version 1. DT 07-JUN-2017, entry version 68. DE RecName: Full=GTPase HflX {ECO:0000255|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000255|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000255|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Tpen_0708; OS Thermofilum pendens (strain DSM 2475 / Hrk 5). OC Archaea; Crenarchaeota; Thermoprotei; Thermoproteales; Thermofilaceae; OC Thermofilum. OX NCBI_TaxID=368408; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 2475 / Hrk 5; RX PubMed=18263724; DOI=10.1128/JB.01949-07; RA Anderson I., Rodriguez J., Susanti D., Porat I., Reich C., RA Ulrich L.E., Elkins J.G., Mavromatis K., Lykidis A., Kim E., RA Thompson L.S., Nolan M., Land M., Copeland A., Lapidus A., Lucas S., RA Detter C., Zhulin I.B., Olsen G.J., Whitman W., Mukhopadhyay B., RA Bristow J., Kyrpides N.; RT "Genome sequence of Thermofilum pendens reveals an exceptional loss of RT biosynthetic pathways without genome reduction."; RL J. Bacteriol. 190:2957-2965(2008). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000255|HAMAP-Rule:MF_00900}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00900}; CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000255|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000255|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000255|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000505; ABL78110.1; -; Genomic_DNA. DR RefSeq; WP_011752375.1; NC_008698.1. DR ProteinModelPortal; A1RY30; -. DR SMR; A1RY30; -. DR STRING; 368408.Tpen_0708; -. DR EnsemblBacteria; ABL78110; ABL78110; Tpen_0708. DR GeneID; 4601589; -. DR KEGG; tpe:Tpen_0708; -. DR eggNOG; arCOG00353; Archaea. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG093Z07D6; -. DR Proteomes; UP000000641; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; GTP-binding; Magnesium; Metal-binding; KW Nucleotide-binding; Reference proteome. FT CHAIN 1 424 GTPase HflX. FT /FTId=PRO_0000412668. FT DOMAIN 194 364 Hflx-type G. {ECO:0000255|HAMAP- FT Rule:MF_00900}. FT NP_BIND 200 207 GTP. {ECO:0000255|HAMAP-Rule:MF_00900}. FT NP_BIND 225 229 GTP. {ECO:0000255|HAMAP-Rule:MF_00900}. FT NP_BIND 246 249 GTP. {ECO:0000255|HAMAP-Rule:MF_00900}. FT NP_BIND 314 317 GTP. {ECO:0000255|HAMAP-Rule:MF_00900}. FT NP_BIND 342 344 GTP. {ECO:0000255|HAMAP-Rule:MF_00900}. FT METAL 207 207 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_00900}. FT METAL 227 227 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_00900}. SQ SEQUENCE 424 AA; 47211 MW; 9C82C7436C6093D6 CRC64; MSVDGRQAVI VVARLSGKGD LALLDELRKL VEAAGYAVAG ELLQKSRYED PKYNIGRGKV LELKRLVEEK KPLKVVFLND LKPNQAYNLS KETGVEVIDR YELILEIFAK RAGSRESKLQ IELAKLKREL SFAKEYINLA KRGELHGFLG GGKYAVDAYY AYVSMRISKI EEELRKIRKM KEERIARRVE AGLYTVALTG YTGAGKTTLF NVLTGENGYI DGKPFATLST LSRRTYFHGF PVLVTDTIGF IDDLPDALVD AFYTTLRETL AADVILLVLD VSDTPAEIRR KLTASMEVLL NLGVPPTRIL LVGNKIDKVS SAELEERERL LEDSGLRYTL ISAARRIGIH ELTQAVVEML PEKVSATLAL TREALAEDLR ELLDRCRVRE VVQGSDGKLL VVVEGRRDIV ARLQARAGMG LVDG // ID HFLX_TREDE Reviewed; 391 AA. AC Q73J26; DT 21-SEP-2011, integrated into UniProtKB/Swiss-Prot. DT 05-JUL-2004, sequence version 1. DT 07-JUN-2017, entry version 88. DE RecName: Full=GTPase HflX {ECO:0000255|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000255|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000255|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=TDE_2750; OS Treponema denticola (strain ATCC 35405 / CIP 103919 / DSM 14222). OC Bacteria; Spirochaetes; Spirochaetales; Spirochaetaceae; Treponema. OX NCBI_TaxID=243275; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 35405 / CIP 103919 / DSM 14222; RX PubMed=15064399; DOI=10.1073/pnas.0307639101; RA Seshadri R., Myers G.S.A., Tettelin H., Eisen J.A., Heidelberg J.F., RA Dodson R.J., Davidsen T.M., DeBoy R.T., Fouts D.E., Haft D.H., RA Selengut J., Ren Q., Brinkac L.M., Madupu R., Kolonay J.F., RA Durkin S.A., Daugherty S.C., Shetty J., Shvartsbeyn A., RA Gebregeorgis E., Geer K., Tsegaye G., Malek J.A., Ayodeji B., RA Shatsman S., McLeod M.P., Smajs D., Howell J.K., Pal S., Amin A., RA Vashisth P., McNeill T.Z., Xiang Q., Sodergren E., Baca E., RA Weinstock G.M., Norris S.J., Fraser C.M., Paulsen I.T.; RT "Comparison of the genome of the oral pathogen Treponema denticola RT with other spirochete genomes."; RL Proc. Natl. Acad. Sci. U.S.A. 101:5646-5651(2004). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000255|HAMAP-Rule:MF_00900}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00900}; CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000255|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000255|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000255|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE017226; AAS13267.1; -; Genomic_DNA. DR RefSeq; NP_973348.1; NC_002967.9. DR RefSeq; WP_002667011.1; NC_002967.9. DR ProteinModelPortal; Q73J26; -. DR STRING; 243275.TDE2750; -. DR EnsemblBacteria; AAS13267; AAS13267; TDE_2750. DR GeneID; 2740717; -. DR KEGG; tde:TDE2750; -. DR PATRIC; fig|243275.7.peg.2596; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000008212; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; GTP-binding; Magnesium; Metal-binding; KW Nucleotide-binding; Reference proteome. FT CHAIN 1 391 GTPase HflX. FT /FTId=PRO_0000412664. FT DOMAIN 222 391 Hflx-type G. {ECO:0000255|HAMAP- FT Rule:MF_00900}. FT NP_BIND 228 235 GTP. {ECO:0000255|HAMAP-Rule:MF_00900}. FT NP_BIND 253 257 GTP. {ECO:0000255|HAMAP-Rule:MF_00900}. FT NP_BIND 278 281 GTP. {ECO:0000255|HAMAP-Rule:MF_00900}. FT NP_BIND 344 347 GTP. {ECO:0000255|HAMAP-Rule:MF_00900}. FT NP_BIND 369 371 GTP. {ECO:0000255|HAMAP-Rule:MF_00900}. FT METAL 235 235 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_00900}. FT METAL 255 255 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_00900}. SQ SEQUENCE 391 AA; 43571 MW; 7B2955ECA7FED328 CRC64; MYITDNETKK ALLIFTDIFS GPASNSHISR STLQEKSAKA LKEIEEKELK SLVETIFLKP LSSLRFRIAK ENPATLVGSG QLEKIAQAIE EEGADLVVFN SAVSPRIQRN LEAALNTCVI DRSEVIIQIF ADRAQTREAV LQAELARLEY SMPRLTRRWT SLAQQRGGAK GTRGASRGAG EKKLELDRRR LKTEITKLKK EVERVRLQRS EQRKTRLNGD KKIGAIVGYT NAGKSSLLKK LSGAEVFTED KLFATLDAET RKVFLQTGEK NIQILLTDTV GFVSNLPHQL IDAFRSTLEE AALADFLIIV CDAAHPAMPE CLEVTKKVLD ELSCSDKPSI IAINKMDDIF DEAQLLNLKE RYPEAVEISV TTGQGLEGLK KKITDIIIFD K // ID I0A1F8_FERFK Unreviewed; 342 AA. AC I0A1F8; DT 13-JUN-2012, integrated into UniProtKB/TrEMBL. DT 13-JUN-2012, sequence version 1. DT 07-JUN-2017, entry version 25. DE SubName: Full=GTPase {ECO:0000313|EMBL:AFH42815.1}; GN OrderedLocusNames=FFONT_0827 {ECO:0000313|EMBL:AFH42815.1}; OS Fervidicoccus fontis (strain DSM 19380 / JCM 18336 / VKM B-2539 / OS Kam940). OC Archaea; Crenarchaeota; Thermoprotei; Fervidicoccales; OC Fervidicoccaceae; Fervidicoccus. OX NCBI_TaxID=1163730 {ECO:0000313|EMBL:AFH42815.1, ECO:0000313|Proteomes:UP000007391}; RN [1] {ECO:0000313|Proteomes:UP000007391} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 19380 / VKM B-2539 / Kam940 RC {ECO:0000313|Proteomes:UP000007391}; RA Lebedinsky A.V., Mardanov A.V., Gumerov V.M., Beletsky A.V., RA Kublanov I.V., Perevalova A.A., Bonch-Osmolovskaya E.A., Ravin N.V., RA Skryabin K.G.; RT "Fervidicoccus fontis complete genome analysis confirms its distinct RT phylogenetic position and predicts its environmental function."; RL Submitted (MAR-2012) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP003423; AFH42815.1; -; Genomic_DNA. DR EnsemblBacteria; AFH42815; AFH42815; FFONT_0827. DR KEGG; ffo:FFONT_0827; -. DR KO; K03665; -. DR OMA; FNNHAHV; -. DR OrthoDB; POG093Z07D6; -. DR BioCyc; FFON1163730:GLD9-842-MONOMER; -. DR Proteomes; UP000007391; Chromosome. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 4: Predicted; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000007391}; KW Reference proteome {ECO:0000313|Proteomes:UP000007391}. FT DOMAIN 166 259 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 132 159 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 342 AA; 38646 MW; 8624BCE20AFEE9AB CRC64; MKTLSVLIGL DIQESVTIRK NSGRYLISDY KLREIVEKKE KVKAEVILIE PELPPRDKIN IIKATKADVI DRTLLLLEVF ESNAGSKEAK LQISLARSGH MLPLVREVLN NSKRGELPGF LAGGTYAIDK YYRQLRRQVA KTRRELEEIR IRRDILRERR RVSGLPLIAI IGYANAGKTT LFNLLTGSNK ETSNKPFTTI SPKVSLSNLG FLVIDTVGFV MNVPPEIIEA FYSTLEEIRE ADVLLLLLDS TEDLFLIEER VKQASVTLSN IESLYKPIVV ALNKVEKTGR DDIEEKRAKL YQTCKSVFPM FVGLAKVSAK KGLGIDEMVN VIWKALNRKQ AY // ID I0ANL5_IGNAJ Unreviewed; 420 AA. AC I0ANL5; DT 13-JUN-2012, integrated into UniProtKB/TrEMBL. DT 13-JUN-2012, sequence version 1. DT 07-JUN-2017, entry version 35. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:AFH50572.1}; GN OrderedLocusNames=IALB_2869 {ECO:0000313|EMBL:AFH50572.1}; OS Ignavibacterium album (strain DSM 19864 / JCM 16511 / NBRC 101810 / OS Mat9-16). OC Bacteria; Ignavibacteriae; Ignavibacteria; Ignavibacteriales; OC Ignavibacteriaceae; Ignavibacterium. OX NCBI_TaxID=945713 {ECO:0000313|EMBL:AFH50572.1, ECO:0000313|Proteomes:UP000007394}; RN [1] {ECO:0000313|EMBL:AFH50572.1, ECO:0000313|Proteomes:UP000007394} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 19864 / JCM 16511 / NBRC 101810 / Mat9-16 RC {ECO:0000313|Proteomes:UP000007394}; RX PubMed=22661972; DOI=10.3389/fmicb.2012.00185; RA Liu Z., Frigaard N.-U., Vogl K., Iino T., Ohkuma M., Overmann J., RA Bryant D.A.; RT "Complete genome of Ignavibacterium album, a metabolically versatile, RT flagellated, facultative anaerobe from the phylum Chlorobi."; RL Front. Microbiol. 3:185-185(2012). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP003418; AFH50572.1; -; Genomic_DNA. DR RefSeq; WP_014561711.1; NC_017464.1. DR EnsemblBacteria; AFH50572; AFH50572; IALB_2869. DR KEGG; ial:IALB_2869; -. DR PATRIC; fig|945713.3.peg.2888; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000007394; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000007394}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000007394}. FT DOMAIN 200 366 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 17 44 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 420 AA; 47688 MW; CD8ED02DA26DFE28 CRC64; MIEVTKKTVE RAMLIALDTK EFSKETVEEH IEELEELAAT AGAETIFKII QTKRGIDPAF YIGKGKAEEL AQLIELNEIN IVIFDDDLTP VQVRNLEKLF NRKVIDRSGL ILDIFASRAK TKEAKTQVEL AQLQYMLPRL TRAWTHLSKQ YGGIGTKGPG ETQIETDRRL IRTRISLLKN KLEKIEAHRM TQSSGRKGFL RIAIAGYTNA GKSTLFNLLT EANVFAENKL FATLDSTTRS LDIDDTHKIL ISDTVGFIRK LPAHLIASFK STLNEVRDAD IILHVIDISH PYFEDHIKVV DETLKEFGSA EKRVIKVFNK VDIVSDKSLI DFVKNVYKES VIISASRGIN ISSLKTMLKN ILNENIVEEK IELPLTATKK ASQIHEFAEV LKTEYDDNKI QIIYRTSRQN SEKIKKIIAY // ID I0GJC3_CALEA Unreviewed; 421 AA. AC I0GJC3; DT 13-JUN-2012, integrated into UniProtKB/TrEMBL. DT 13-JUN-2012, sequence version 1. DT 07-JUN-2017, entry version 35. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:BAL80860.1}; GN OrderedLocusNames=CSE_07340 {ECO:0000313|EMBL:BAL80860.1}; OS Caldisericum exile (strain DSM 21853 / NBRC 104410 / AZM16c01). OC Bacteria; Caldiserica; Caldisericia; Caldisericales; Caldisericaceae; OC Caldisericum. OX NCBI_TaxID=511051 {ECO:0000313|EMBL:BAL80860.1, ECO:0000313|Proteomes:UP000004793}; RN [1] {ECO:0000313|EMBL:BAL80860.1, ECO:0000313|Proteomes:UP000004793} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 21853 / NBRC 104410 / AZM16c01 RC {ECO:0000313|Proteomes:UP000004793}; RA Narita-Yamada S., Kawakoshi A., Nakamura S., Sasagawa M., Fukada J., RA Sekine M., Kato Y., Fukai R., Sasaki K., Hanamaki A., Narita H., RA Konno Y., Mori K., Yamazaki S., Suzuki K., Fujita N.; RT "Whole genome sequence of Caldisericum exile AZM16c01."; RL Submitted (JAN-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AP012051; BAL80860.1; -; Genomic_DNA. DR RefSeq; WP_014453263.1; NC_017096.1. DR EnsemblBacteria; BAL80860; BAL80860; CSE_07340. DR KEGG; cex:CSE_07340; -. DR PATRIC; fig|511051.3.peg.720; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000004793; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000004793}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000004793}. FT DOMAIN 198 363 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 421 AA; 48483 MW; F1C90A9DC6599FD5 CRC64; MEKIDRKAIL VHIISKENKE LREEYLEEFR LLVETLSYEI VAETTYSLRE PRYSTFLGTG KIEELKKLAQ LTDAKIVFID TTLTFLQLRN LSKELGVPVV DRPHLILMIF SMRARTTEAK LQVELSQLKM RLPEIVHEDV DLDQQTGSEM GLKGPGERKT ELKRRYIAKR IQILEKKLEE IKKHRVEIRK RRTKSSIPII SIVGYTNAGK STLLNTLTQS EAYVEDKLFA TLDSLSRVGE IKQNISAIFV DTIGFIRDLP PQLIYAFHST LEEILDSWII IHLVDASDPL FRDKMEVVLC TLKDLGASNI PIITVFNKID KIGEEPLKYL QSIYKDAIFI SAKESIGIDQ LKERLANMLS ELIVRVKIVL PYKDAHLLDE IYTVANVISR KDTEENIILY VEGYYSNLGK FKNYFSSQRT A // ID I0GP69_SELRL Unreviewed; 599 AA. AC I0GP69; DT 13-JUN-2012, integrated into UniProtKB/TrEMBL. DT 13-JUN-2012, sequence version 1. DT 07-JUN-2017, entry version 37. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:BAL82556.1}; GN OrderedLocusNames=SELR_08480 {ECO:0000313|EMBL:BAL82556.1}; OS Selenomonas ruminantium subsp. lactilytica (strain NBRC 103574 / OS TAM6421). OC Bacteria; Firmicutes; Negativicutes; Selenomonadales; OC Selenomonadaceae; Selenomonas. OX NCBI_TaxID=927704 {ECO:0000313|EMBL:BAL82556.1, ECO:0000313|Proteomes:UP000007887}; RN [1] {ECO:0000313|EMBL:BAL82556.1, ECO:0000313|Proteomes:UP000007887} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NBRC 103574 / TAM6421 {ECO:0000313|Proteomes:UP000007887}; RA Oguchi A., Ankai A., Kaneko J., Yamada-Narita S., Fukui S., RA Takahashi M., Onodera T., Kojima S., Fushimi T., Abe N., Kamio Y., RA Yamazaki S., Fujita N.; RT "Whole genome sequence of Selenomonas ruminantium subsp. lactilytica RT TAM6421."; RL Submitted (OCT-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AP012292; BAL82556.1; -; Genomic_DNA. DR RefSeq; WP_014423995.1; NC_017068.1. DR EnsemblBacteria; BAL82556; BAL82556; SELR_08480. DR GeneID; 31522126; -. DR KEGG; sri:SELR_08480; -. DR PATRIC; fig|927704.6.peg.871; -. DR KO; K03665; -. DR OMA; EREVIIT; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000007887; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000007887}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000007887}. FT DOMAIN 379 544 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 599 AA; 66855 MW; 474CEC8FC068C972 CRC64; MQVNGDLANI KTYVLEKLKA LYELKVPIGQ ISTRELNEEM LAITEDTDRE VAVYLNRQGK VVQVSLGDTA TVDLPEFKQK TRSDLRLSGI RCIHTHPSGD VRLSSPDLSS LRRLRFDCMA AIGRKDGKII GCLAFFAGEM SEDGTQLLTQ YGPAEDKVLA QINLNMLVTV VNKKLAAQST KSTEDEVERA ILAGVERPGS SWPIEESMAE LERLADTAGA KVVATFTQRK EKPDAAFFLG KGKVNELAME IQNLEATLLI LDDELTPSQQ HNLERMLGVK VIDRTALILD IFAQRANSRE GKLQVELAQL RYNLPRLSGQ GLALSRLGGG IGTRGPGETK LEVDRRRIYS KIHDIEELID GMKKSRTLHR KRRKESQIPL VALVGYTNAG KSTLLNKLTG SEVFAEDKLF ATLDPTTRHL ELPEKQEILL TDTVGFIQKL PHTLVKAFRA TLEEVQEADL LLHVVDCSNE NLEAQIEAVV AVLQELEADN KPVLYVFNKA DQLDNPHIRE QLLHGRDGVF ISAMTGENLD ALQRRIEGFF QESQVRMTLL IPYAEGAAVT RLHQLNAVVE TSYEETGTKV EVRLPLSEKD NFVQYELKE // ID I0HGH8_ACTM4 Unreviewed; 462 AA. AC I0HGH8; DT 13-JUN-2012, integrated into UniProtKB/TrEMBL. DT 13-JUN-2012, sequence version 1. DT 07-JUN-2017, entry version 38. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=AMIS_68950 {ECO:0000313|EMBL:BAL92115.1}; OS Actinoplanes missouriensis (strain ATCC 14538 / DSM 43046 / CBS 188.64 OS / JCM 3121 / NCIMB 12654 / NBRC 102363 / 431). OC Bacteria; Actinobacteria; Micromonosporales; Micromonosporaceae; OC Actinoplanes. OX NCBI_TaxID=512565 {ECO:0000313|EMBL:BAL92115.1, ECO:0000313|Proteomes:UP000007882}; RN [1] {ECO:0000313|EMBL:BAL92115.1, ECO:0000313|Proteomes:UP000007882} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 14538 / DSM 43046 / CBS 188.64 / JCM 3121 / NCIMB 12654 / RC NBRC 102363 / 431 {ECO:0000313|Proteomes:UP000007882}; RA Ohnishi Y., Ishikawa J., Sekine M., Hosoyama A., Harada T., Narita H., RA Hata T., Konno Y., Tutikane K., Fujita N., Horinouchi S., Hayakawa M.; RT "Complete genome sequence of Actinoplanes missouriensis 431 (= NBRC RT 102363)."; RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AP012319; BAL92115.1; -; Genomic_DNA. DR EnsemblBacteria; BAL92115; BAL92115; AMIS_68950. DR KEGG; ams:AMIS_68950; -. DR PATRIC; fig|512565.3.peg.6896; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000007882; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 2. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000007882}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000007882}. FT DOMAIN 244 409 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 203 237 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 462 AA; 50253 MW; 7A8BC0D1E5092CF1 CRC64; MLDEPDLTTG ELELEERHSL RRVAGLSTEL TDITEVEYRQ LRLERVVLVG VWTEGSVADA ENSLTELAAL AETAGSQVLE GLIQRRKQPD AATFIGRGKV DELRDVVLST GADTVICDGE LSPSQLRNLE QQVKIKVVDR TALILDIFAQ HAKSREGKAQ VELAQLQYLL PRLRGWGDSL SRQGGGAGGG SGGGGVGTRG PGETKLETDR RRINTRIAKL RREIKAMKTV RETKRSRRSA SGVPAVAIAG YTNAGKSSLL NRLTQAGVLV EDALFATLDP TTRRTAAEDG RVFTLSDTVG FVRHLPHQIV EAFRSTLEEV AQADLVVHVV DGAHPDPEGQ VSAVREVLGE VGADRIPELL AVNKVDAADE ETILRLKRTW PDAVFVSARS GAGIDELHAA IAERLPRPAV DMMVLVPYDR GDLVARVHRS GQVLQSRHLD DGTELRVRVS EEIAAELEAF RL // ID I0HSV2_RUBGI Unreviewed; 389 AA. AC I0HSV2; DT 13-JUN-2012, integrated into UniProtKB/TrEMBL. DT 13-JUN-2012, sequence version 1. DT 07-JUN-2017, entry version 36. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:BAL96089.1}; GN OrderedLocusNames=RGE_27500 {ECO:0000313|EMBL:BAL96089.1}; OS Rubrivivax gelatinosus (strain NBRC 100245 / IL144). OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Rubrivivax. OX NCBI_TaxID=983917 {ECO:0000313|EMBL:BAL96089.1, ECO:0000313|Proteomes:UP000007883}; RN [1] {ECO:0000313|EMBL:BAL96089.1, ECO:0000313|Proteomes:UP000007883} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NBRC 100245 / IL144 {ECO:0000313|Proteomes:UP000007883}; RX PubMed=22689232; DOI=10.1128/JB.00511-12; RA Nagashima S., Kamimura A., Shimizu T., Nakamura-isaki S., Aono E., RA Sakamoto K., Ichikawa N., Nakazawa H., Sekine M., Yamazaki S., RA Fujita N., Shimada K., Hanada S., Nagashima K.V.P.; RT "Complete genome sequence of phototrophic betaproteobacterium RT Rubrivivax gelatinosus IL144."; RL J. Bacteriol. 194:3541-3542(2012). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AP012320; BAL96089.1; -; Genomic_DNA. DR RefSeq; WP_014428951.1; NC_017075.1. DR EnsemblBacteria; BAL96089; BAL96089; RGE_27500. DR KEGG; rge:RGE_27500; -. DR PATRIC; fig|983917.3.peg.2678; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000007883; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000007883}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000007883}. FT DOMAIN 207 381 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 389 AA; 42312 MW; 03921F20CDBDD95B CRC64; MTSAAPQTLS QEGGPTRAVL VGVDLGGDSH FDPTLDELAL LAESAGDVAV ARVTARRKAP DAALFVGSGK ADEIRAMVGA TQAHGVIFDQ TLSPAQQRNL ERHLGVPVAD RTSLILDIFA ARAQSHEGKL QVELARLQYV ATRLVRRWSH LERQRGGIGT RGGPGEAQIE LDRRMIGERI KSVKARLEKV KQQRGTQRRA RERRGTFRVS LVGYTNAGKS TLFNALVKAR TYAADQLFAT LDTTTRSLWL GEAGASVSLS DTVGFIRDLP HKLVEAFEAT LREAADADLL LHVVDAASPA LLEQQAEVER VLEEIGAAGV PQILVFNKCD LLEESRLPRQ PRDEVEVHPG MRRARVFVSA RDGQGLDVLR QVIAEAARPA PEAQTITNE // ID I0I415_CALAS Unreviewed; 475 AA. AC I0I415; DT 13-JUN-2012, integrated into UniProtKB/TrEMBL. DT 13-JUN-2012, sequence version 1. DT 07-JUN-2017, entry version 35. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:BAM00003.1}; GN OrderedLocusNames=CLDAP_19630 {ECO:0000313|EMBL:BAM00003.1}; OS Caldilinea aerophila (strain DSM 14535 / JCM 11387 / NBRC 104270 / OS STL-6-O1). OC Bacteria; Chloroflexi; Caldilineae; Caldilineales; Caldilineaceae; OC Caldilinea. OX NCBI_TaxID=926550 {ECO:0000313|EMBL:BAM00003.1, ECO:0000313|Proteomes:UP000007880}; RN [1] {ECO:0000313|EMBL:BAM00003.1, ECO:0000313|Proteomes:UP000007880} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 14535 / JCM 11387 / NBRC 104270 / STL-6-O1 RC {ECO:0000313|Proteomes:UP000007880}; RA Oguchi A., Hosoyama A., Sekine M., Fukai R., Kato Y., Nakamura S., RA Hanada S., Yamazaki S., Fujita N.; RT "Complete genome sequence of Caldilinea aerophila DSM 14535 (= NBRC RT 102666)."; RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AP012337; BAM00003.1; -; Genomic_DNA. DR RefSeq; WP_014433238.1; NC_017079.1. DR EnsemblBacteria; BAM00003; BAM00003; CLDAP_19630. DR KEGG; cap:CLDAP_19630; -. DR PATRIC; fig|926550.5.peg.2173; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000007880; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000007880}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000007880}. FT DOMAIN 241 412 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 200 237 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 475 AA; 52298 MW; 4D295457F4AB0E6C CRC64; MSSFDSSHSQ NPLSSDNRGR DRIVRDETGL VVTAPPEERA ILVGVELQNH PSLLSLEDSL NELALLAKTA GVRVVGRLTQ RLAAPNPATL IGVGKLEELR AAVAELGANM VIFDEELSPR QQRELEKALG EEIKVIDRTA LILDIFARHA RTREGAVQVE LAQYEYRLPR LTRAWTHLAR QAGGRAGGAT GGVGVRGPGE TQLEVDRREI NRRIAFLKQE LAEIRKHREQ YRSQRRQSAL PLIALVGYTN AGKSTLLNAI ADADVVAEDQ LFATLDPTTR RVRLPSDRLV LFSDTVGFIQ KLPLTLVAAF RSTLEEVNEA DLLVHVVDIS HPNMEEQIAA VEEILEDLGA ADKPIVMALN KIDRLDPSNP EHARRIEQAL ADNPNAVPIS ALNGQGLDRL LQAIDDALSH RMIAIDVVIP YSRGDLVALM HEHGMVESET HEEQGTHIVG RLPVELIGRL APYWTPKQAV DKNPA // ID I0IFS6_PHYMF Unreviewed; 437 AA. AC I0IFS6; DT 13-JUN-2012, integrated into UniProtKB/TrEMBL. DT 13-JUN-2012, sequence version 1. DT 07-JUN-2017, entry version 34. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:BAM04114.1}; GN OrderedLocusNames=PSMK_19550 {ECO:0000313|EMBL:BAM04114.1}; OS Phycisphaera mikurensis (strain NBRC 102666 / KCTC 22515 / OS FYK2301M01). OC Bacteria; Planctomycetes; Phycisphaerae; Phycisphaerales; OC Phycisphaeraceae; Phycisphaera. OX NCBI_TaxID=1142394 {ECO:0000313|EMBL:BAM04114.1, ECO:0000313|Proteomes:UP000007881}; RN [1] {ECO:0000313|EMBL:BAM04114.1, ECO:0000313|Proteomes:UP000007881} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NBRC 102666 / KCTC 22515 / FYK2301M01 RC {ECO:0000313|Proteomes:UP000007881}; RA Ankai A., Hosoyama A., Terui Y., Sekine M., Fukai R., Kato Y., RA Nakamura S., Yamada-Narita S., Kawakoshi A., Fukunaga Y., Yamazaki S., RA Fujita N.; RT "Complete genome sequence of Phycisphaera mikurensis NBRC 102666."; RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AP012338; BAM04114.1; -; Genomic_DNA. DR RefSeq; WP_014437332.1; NC_017080.1. DR EnsemblBacteria; BAM04114; BAM04114; PSMK_19550. DR KEGG; phm:PSMK_19550; -. DR PATRIC; fig|1142394.8.peg.2014; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000007881; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000007881}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000007881}. FT DOMAIN 198 364 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 437 AA; 47822 MW; 8B859D92EE2FACB4 CRC64; MESERAVLVA ALLPDFNGNP HDPLDELRSL AGTAGALPVA EILQKKGKPE PATFIGRGKV QEVAEAIRLH EAQVVIFEND LTPRQIANLE ERVEAKVVDR SELILDIFAS RATTHEARLQ VELAQLQYTF PRLRAMWSHL ERISGGAPTG IGTRGPGEQQ LEVDRRIVRK KLGLLRSQIA EIQGRKERAV AARNLDHFSV GLVGYTNAGK STLFNSLTAA GTYADDKLFA TLSTKTREWK LGGGDAVMLS DTVGFVRNLP HHLVASFKAT LEEAVHAHLL LLVVDVSDPH CLDHLKTVRH VLDDVGAGER PFLLVLNKID AMAHNADLLV LESEHPDAIR VSAKSGDNLA ALTEAVRDAL HGQVQEMVLT VDQADGKAIT FLENRTEVLG RDYADTTVDF RVRIGGNQLD RLRAMDTTAR LPGEAEAPPW RASRTPA // ID I0IQJ9_LEPFC Unreviewed; 529 AA. AC I0IQJ9; DT 13-JUN-2012, integrated into UniProtKB/TrEMBL. DT 13-JUN-2012, sequence version 1. DT 07-JUN-2017, entry version 36. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=LFE_1870 {ECO:0000313|EMBL:BAM07548.1}; OS Leptospirillum ferrooxidans (strain C2-3). OC Bacteria; Nitrospirae; Nitrospirales; Nitrospiraceae; Leptospirillum. OX NCBI_TaxID=1162668 {ECO:0000313|EMBL:BAM07548.1, ECO:0000313|Proteomes:UP000007382}; RN [1] {ECO:0000313|Proteomes:UP000007382} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C2-3 {ECO:0000313|Proteomes:UP000007382}; RA Fujimura R., Sato Y., Nishizawa T., Nanba K., Oshima K., Hattori M., RA Kamijo T., Ohta H.; RT "The complete genome sequence of the pioneer microbe on fresh volcanic RT deposit, Leptospirillum ferrooxidans strain C2-3."; RL Submitted (MAR-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AP012342; BAM07548.1; -; Genomic_DNA. DR EnsemblBacteria; BAM07548; BAM07548; LFE_1870. DR KEGG; lfc:LFE_1870; -. DR PATRIC; fig|1162668.3.peg.2225; -. DR KO; K03665; -. DR OMA; EREVIIT; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000007382; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000007382}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000007382}. FT DOMAIN 350 515 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 309 336 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 529 AA; 59043 MW; 9B38AF108BBB568F CRC64; MWVTTELAGV MGEISFEIGR QVGVFISREG AVLDVIVGGP KELYIESLPP SRGGDHLLRG IRLVHTHLRT EPINQDDLND LALLRLDAQI VLHIDESAPR IRRFSQALIN PDKKGETPWL VNESVPFSAE RLEVADTVLE IEEALSESKG SSRHQTSGQE RAILVSASKE SLLFQKDGME ELRELAESAG VQVLGEEIQK LRTVHPSTLL SADRLKVLII HALQVGATII IFEQNLTPAQ VKNIAALTDL KIIDRTQLIL DIFARRAHSS DGKLQVEVAQ LKYLLPRLEQ RSTALSRLTG GIGGRGPGET RLEEDRRRVR DRITSLTEKL SKLGDERRQR KERRQENGLP IVSLVGYTNV GKSTLLNQLT GSEVLTENKL FATLDPTSRR LRFPREREII LTDTVGFIRN LPADLKRAFL STFDELKDAH LLIHVADGSH PSIEAQIKQV DSLLTEMEIG EKPKLLVINK ADLLDDEKKE SLSLLFPEAI LISATHPDTL RGLLGQMEER LFFKRLSDPP DHVAMAPVP // ID I0JMV2_HALH3 Unreviewed; 411 AA. AC I0JMV2; DT 13-JUN-2012, integrated into UniProtKB/TrEMBL. DT 13-JUN-2012, sequence version 1. DT 07-JUN-2017, entry version 40. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:CCG45472.1}; GN OrderedLocusNames=HBHAL_3125 {ECO:0000313|EMBL:CCG45472.1}; OS Halobacillus halophilus (strain ATCC 35676 / DSM 2266 / JCM 20832 / OS NBRC 102448/ NCIMB 2269) (Sporosarcina halophila). OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Halobacillus. OX NCBI_TaxID=866895 {ECO:0000313|EMBL:CCG45472.1, ECO:0000313|Proteomes:UP000007397}; RN [1] {ECO:0000313|EMBL:CCG45472.1, ECO:0000313|Proteomes:UP000007397} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 35676 / DSM 2266 / JCM 20832 / NBRC 102448/ NCIMB 2269 RC {ECO:0000313|Proteomes:UP000007397}; RX PubMed=22583374; DOI=10.1111/j.1462-2920.2012.02770.x; RA Saum S.H., Pfeiffer F., Palm P., Rampp M., Schuster S.C., Muller V., RA Oesterhelt D.; RT "Chloride and organic osmolytes: a hybrid strategy to cope with RT elevated salinities by the moderately halophilic, chloride-dependent RT bacterium Halobacillus halophilus."; RL Environ. Microbiol. 15:1619-1633(2013). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; HE717023; CCG45472.1; -; Genomic_DNA. DR RefSeq; WP_014643364.1; NC_017668.1. DR EnsemblBacteria; CCG45472; CCG45472; HBHAL_3125. DR KEGG; hhd:HBHAL_3125; -. DR PATRIC; fig|866895.3.peg.2145; -. DR KO; K03665; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000007397; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000007397}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000007397}. FT DOMAIN 197 358 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 411 AA; 47198 MW; 8B7F8C6A5C1F07C2 CRC64; MQGKERVILV ARKDPNEEEK RFNSSLEELQ SLTETADGDI CRVITQKRDR VHPATYLGEG KLEEIKAAAL ETDAELIIFN DELTPGQLRN ISDKVERRVL DRSQLILDIF ASRARTKEGK LQVELAQLQY LLPRLAGQGT ELSRLGGGIG TRGPGETKLE TDRRHIRRRI DDIKKRLNAV VKQREQYRQR RKENRAFQIA IVGYTNAGKS TFFNRVTESD SYEENLLFAT LDPLTRQMSL PSGFQALISD TVGFIQDLPT TLIAAFRSTL EEVTEADFIL HMVDASHPDH LQQEKTVLRL LDELGAGQLP MLTVYNKKDL LREDFIPETH PSLTVSVHDR IDLKRILDKI EVVLKEEWHE YDVFIPASEG KRLQQFKKFS MITSMDFYED KEGYALHGFI HPDHPLKHQI L // ID I0KDJ8_9BACT Unreviewed; 428 AA. AC I0KDJ8; DT 13-JUN-2012, integrated into UniProtKB/TrEMBL. DT 13-JUN-2012, sequence version 1. DT 07-JUN-2017, entry version 38. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=FAES_4201 {ECO:0000313|EMBL:CCH02201.1}; OS Fibrella aestuarina BUZ 2. OC Bacteria; Bacteroidetes; Cytophagia; Cytophagales; Cytophagaceae; OC Fibrella. OX NCBI_TaxID=1166018 {ECO:0000313|EMBL:CCH02201.1, ECO:0000313|Proteomes:UP000011058}; RN [1] {ECO:0000313|EMBL:CCH02201.1, ECO:0000313|Proteomes:UP000011058} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BUZ 2 {ECO:0000313|EMBL:CCH02201.1}; RX PubMed=22689241; DOI=10.1128/JB.00550-12; RA Filippini M., Qi W., Blom J., Goesmann A., Smits T.H., Bagheri H.C.; RT "Genome Sequence of Fibrella aestuarina BUZ 2T, a Filamentous Marine RT Bacterium."; RL J. Bacteriol. 194:3555-3555(2012). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; HE796683; CCH02201.1; -; Genomic_DNA. DR RefSeq; WP_015333300.1; NC_020054.1. DR ProteinModelPortal; I0KDJ8; -. DR EnsemblBacteria; CCH02201; CCH02201; FAES_4201. DR KEGG; fae:FAES_4201; -. DR PATRIC; fig|1166018.3.peg.1156; -. DR KO; K03665; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000011058; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000011058}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000011058}. FT DOMAIN 200 392 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 161 198 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 428 AA; 48789 MW; 2E7C343C934E8E19 CRC64; MIETHKQPET AVLVAVSTQK QTASQTQEYL DELAFLAETS GIVTKKTFTQ KLERPDVRTF VGKGKLEEIQ TYVMAEPVDT IIFDDDLTPA QVRNLEAEFK DIKVLDRSLL ILNIFSMRAQ TAQSRVQVEL AQYQYIFPRL TRMWTHLSRQ KGGAGMRGPG EKELETDRRI VKDRIAFLKE KLEKIDKQSQ TRRKERDRLV RVALVGYTNV GKSTLMRTVA KTDVFAENKL FATVDSTVRK VTLGNIPFLL TDTVGFIRKL PTMLIESFKS TLDEVREADI LLHVVDISHP SFEEHIDVVH KTLIELGVAD KPVVLVFNKM DAFVPKEEWA PEFDAETEGE VPADERRQTA LTYLKRMNLA KQAEHVVFVS AQTGENLSEL RELLYEMVKE RHFQIYPNWL NVPLLETATL GGDGARPSAE EVTPKLEN // ID I0KYT2_9ACTN Unreviewed; 484 AA. AC I0KYT2; DT 13-JUN-2012, integrated into UniProtKB/TrEMBL. DT 13-JUN-2012, sequence version 1. DT 07-JUN-2017, entry version 35. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=MILUP08_41646 {ECO:0000313|EMBL:CCH16729.1}; OS Micromonospora lupini str. Lupac 08. OC Bacteria; Actinobacteria; Micromonosporales; Micromonosporaceae; OC Micromonospora. OX NCBI_TaxID=1150864 {ECO:0000313|EMBL:CCH16729.1, ECO:0000313|Proteomes:UP000003448}; RN [1] {ECO:0000313|Proteomes:UP000003448} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Lupac 08 {ECO:0000313|Proteomes:UP000003448}; RX PubMed=22815450; DOI=10.1128/JB.00628-12; RA Alonso-Vega P., Normand P., Bacigalupe R., Pujic P., Lajus A., RA Vallenet D., Carro L., Coll P., Trujillo M.E.; RT "Genome Sequence of Micromonospora lupini Lupac 08, Isolated from Root RT Nodules of Lupinus angustifolius."; RL J. Bacteriol. 194:4135-4135(2012). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:CCH16729.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CAIE01000016; CCH16729.1; -; Genomic_DNA. DR RefSeq; WP_007456835.1; NZ_HF570108.1. DR EnsemblBacteria; CCH16729; CCH16729; MILUP08_41646. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000003448; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000003448}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000003448}. FT DOMAIN 255 420 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 484 AA; 52924 MW; 721C60D709463B42 CRC64; MRDQESFVPV EDEFDDVTTG EMELSERQSL RRVPGLSTEL SDVTEVEYRQ LRLERVVLVG VWTEGTVTDA ENSLTELAAL AETAGSQVLE GLIQRRTRPD PATYIGRGKV DDLGAVVLST GADTVICDGE LSPSQLRNLE QRTKVKVVDR TALILDIFAQ HAKSKEGKAQ VELAQLQYLL PRLRGWGETL SRQTGGSGRG GGAGGGVGVR GPGETKLETD RRRIRHRISR LRREIKSMRT VRVTKRARRT RNSVPAVAIA GYTNAGKSSL LNRLTGAGVL VENALFATLD PTTRKATTSD GRLYTLSDTV GFVRHLPHQI VEAFRSTLEE VAEADLVVHV VDGTHPDPEE QVRAVHEVLA EVGADRLPEL LVVNKTDAAD EDRLLRLKRL WPEAIFVSAY SGRGIDALRA AIEERLPQPA VEVRAVLPYD RGDLVSRVHR TGEVLSTSHL PEGTLLHVRV SAALAAELAP FDVAREGQAV GSRP // ID I0L7N6_9ACTN Unreviewed; 383 AA. AC I0L7N6; DT 13-JUN-2012, integrated into UniProtKB/TrEMBL. DT 13-JUN-2012, sequence version 1. DT 07-JUN-2017, entry version 33. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=MILUP08_44711 {ECO:0000313|EMBL:CCH19833.1}; OS Micromonospora lupini str. Lupac 08. OC Bacteria; Actinobacteria; Micromonosporales; Micromonosporaceae; OC Micromonospora. OX NCBI_TaxID=1150864 {ECO:0000313|EMBL:CCH19833.1, ECO:0000313|Proteomes:UP000003448}; RN [1] {ECO:0000313|EMBL:CCH19833.1, ECO:0000313|Proteomes:UP000003448} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Lupac 08 {ECO:0000313|EMBL:CCH19833.1, RC ECO:0000313|Proteomes:UP000003448}; RX PubMed=22815450; DOI=10.1128/JB.00628-12; RA Alonso-Vega P., Normand P., Bacigalupe R., Pujic P., Lajus A., RA Vallenet D., Carro L., Coll P., Trujillo M.E.; RT "Genome Sequence of Micromonospora lupini Lupac 08, Isolated from Root RT Nodules of Lupinus angustifolius."; RL J. Bacteriol. 194:4135-4135(2012). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CAIE01000036; CCH19833.1; -; Genomic_DNA. DR RefSeq; WP_007462302.1; NZ_HF570108.1. DR EnsemblBacteria; CCH19833; CCH19833; MILUP08_44711. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000003448; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000003448}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000003448}. FT DOMAIN 220 383 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 179 213 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 383 AA; 41277 MW; 08EEA51E21F35BB3 CRC64; MAGSWLLGPD AGAQGERPTA VLMAVRGDDG AADSGTGSLT SLTELRRLAD TDGLTVADEV VQSRSHPDPA TYVGSGKVDE LAALAERAHA DLVIADGELT PGQVRNLEER IGVRVVDRTA LILDIFAEHA RTSEGRVQVE LAQIAYQLPR LRGGGRTMSR VGGGRTAGGA GMGVRGPGEM RLETQRRTLR QRATRLRRNA SELARRRERT RSRRARNQVP SVSITGYTNA GKSALLNRLT GADAQVEDVL FATLDPTVRR ISTGELTYTL TDTVGFVRHL PHQLVDAFRS TLEEVTRSDL ALHVVDASAP DALDQITTVH GVLHEIGARD VPELLVLNKI DVAPSEWVDA LCRVHPDAVA VSARTGAGID HLRAELARRV RHQ // ID I0QTJ6_9GAMM Unreviewed; 452 AA. AC I0QTJ6; DT 13-JUN-2012, integrated into UniProtKB/TrEMBL. DT 13-JUN-2012, sequence version 1. DT 30-AUG-2017, entry version 33. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=SPM24T3_10666 {ECO:0000313|EMBL:EIC84619.1}; OS Serratia sp. M24T3. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; OC Yersiniaceae; Serratia. OX NCBI_TaxID=932213 {ECO:0000313|EMBL:EIC84619.1, ECO:0000313|Proteomes:UP000011072}; RN [1] {ECO:0000313|EMBL:EIC84619.1, ECO:0000313|Proteomes:UP000011072} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=M24T3 {ECO:0000313|EMBL:EIC84619.1, RC ECO:0000313|Proteomes:UP000011072}; RX PubMed=22740681; DOI=10.1128/JB.00670-12; RA Proenca D.N., Espirito Santo C., Grass G., Morais P.V.; RT "Draft Genome Sequence of Serratia sp. Strain M24T3, Isolated from RT Pinewood Disease Nematode Bursaphelenchus xylophilus."; RL J. Bacteriol. 194:3764-3764(2012). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EIC84619.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AJHJ01000010; EIC84619.1; -; Genomic_DNA. DR RefSeq; WP_009636740.1; NZ_AJHJ01000010.1. DR EnsemblBacteria; EIC84619; EIC84619; SPM24T3_10666. DR PATRIC; fig|932213.3.peg.2160; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000011072; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000011072}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000011072}. FT DOMAIN 198 365 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 452 AA; 50876 MW; BB0C9E6629E36386 CRC64; MFDRYEAGEQ AVLVHIYFSQ DKVTEDLSEF ESLVSSAGVE ALQVITGSRK APHPKYFVGE GKAQEIADAV KATGASVILF DHALSPGQER NLEALCECRV VDRTGLILDI FAQRARTHEG KLQVELAQLR HIATRLVRGW THLERQGGGI GARGPGETQL ETDRRLLRDR ITLILSRLER VSKQREQGRR SRMRADIPTV SLVGYTNAGK STLFNRITEA DVYVADQLFA TLDPTLRRIM VADVGETVMA DTVGFIRHLP HDLVAAFKAT LQETRQASLL LHVIDAADIR VEENIDAVNT VLAEIEADDI PALLVMNKID MLDDFVPRID RNEENLPIRV WLSAVTGEGI PLLFQALTER LSGEIAQVEL CLPPDAGRLR SRFYQLQAIE KEWIEEDGSI GLMVRMPIVD WRRLCKQEPA MGEYVRNGFP VDFEEKNHWD NLTDIEPEEH QS // ID I0R303_9MICO Unreviewed; 477 AA. AC I0R303; DT 13-JUN-2012, integrated into UniProtKB/TrEMBL. DT 13-JUN-2012, sequence version 1. DT 07-JUN-2017, entry version 34. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=IMCC13023_07180 {ECO:0000313|EMBL:EIC92239.1}; OS Candidatus Aquiluna sp. IMCC13023. OC Bacteria; Actinobacteria; Micrococcales; Microbacteriaceae; OC Luna cluster; Luna-1 subcluster; Candidatus Aquiluna. OX NCBI_TaxID=1081644 {ECO:0000313|EMBL:EIC92239.1, ECO:0000313|Proteomes:UP000054510}; RN [1] {ECO:0000313|Proteomes:UP000054510} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=IMCC13023 {ECO:0000313|Proteomes:UP000054510}; RX PubMed=22689238; DOI=10.1128/JB.00586-12; RA Kang I., Lee K., Yang S.J., Choi A., Kang D., Lee Y.K., Cho J.C.; RT "Genome sequence of "Candidatus Aquiluna" sp. strain IMCC13023, a RT marine member of the Actinobacteria isolated from an arctic fjord."; RL J. Bacteriol. 194:3550-3551(2012). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EIC92239.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AJKR01000002; EIC92239.1; -; Genomic_DNA. DR RefSeq; WP_007541366.1; NZ_AJKR01000002.1. DR EnsemblBacteria; EIC92239; EIC92239; IMCC13023_07180. DR PATRIC; fig|1081644.3.peg.725; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000054510; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 2. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000054510}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000054510}. FT DOMAIN 257 422 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 477 AA; 52057 MW; DE8C1858ACD1BC2A CRC64; MEPESTIDRI LRRGSLAPAS EYDGDQLELE ERASLRRVPG LSTELEDISE VEYRQLRLEK VVLIGVWGTG TVTRAENSLR ELAALAETAG AEVLDGLLQR RAKPDPASYF GKGKAEELRE LVKEVGADTV IADAELAPSQ RRTLEDIVKV KVVDRTAIIL DIFAQHAKSK EGKAQVELAQ LEYLLPRLRG WGESMSRQAG GQAAGGVGIG SRGPGETKIE LDRRRINTKM AKLRREIALM KSARDTKRLK REKARVPQVA IAGYTNAGKS SLLNRLTKAG VLVENALFAT LDPTIRRHET PDGRSYTLAD TVGFVRSLPH QLVEAFRSTL EEIAGADLIV HVVDATDPDP LGQIQTVRLV VAEVDASAIE ELIVFNKADL VSEEEHIRLR GLCPGAFLVS SRTGLGIAEL EAAIASSLPR PEVLFDGLIP YDRGDLVSRI HVAGKVQSIE YVEGGTKVKA LVREDLAAEL ASLTRRP // ID I0RZN3_MYCXE Unreviewed; 483 AA. AC I0RZN3; DT 13-JUN-2012, integrated into UniProtKB/TrEMBL. DT 13-JUN-2012, sequence version 1. DT 07-JUN-2017, entry version 33. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=MXEN_03139 {ECO:0000313|EMBL:EID16586.1}; OS Mycobacterium xenopi RIVM700367. OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae; OC Mycobacterium. OX NCBI_TaxID=1150591 {ECO:0000313|EMBL:EID16586.1, ECO:0000313|Proteomes:UP000003584}; RN [1] {ECO:0000313|EMBL:EID16586.1, ECO:0000313|Proteomes:UP000003584} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=RIVM700367 {ECO:0000313|EMBL:EID16586.1, RC ECO:0000313|Proteomes:UP000003584}; RX PubMed=22628510; DOI=10.1128/JB.00482-12; RA Abdallah A.M., Rashid M., Adroub S.A., Elabdalaoui H., Ali S., RA van Soolingen D., Bitter W., Pain A.; RT "Complete Genome Sequence of Mycobacterium xenopi Type Strain RT RIVM700367."; RL J. Bacteriol. 194:3282-3283(2012). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EID16586.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AJFI01000022; EID16586.1; -; Genomic_DNA. DR RefSeq; WP_003919336.1; NZ_AJFI01000022.1. DR EnsemblBacteria; EID16586; EID16586; MXEN_03139. DR PATRIC; fig|1150591.3.peg.627; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000003584; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000003584}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000003584}. FT DOMAIN 250 419 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 216 243 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 483 AA; 51957 MW; 7CDE4F56170591E3 CRC64; MTYPESPDQV LPEPSAGELA LDDRSALRRV AGLSTELADI SEVEYRQLRL ERVVLVGVWT EGSAADAEAS LAELAALAET AGSLVLEGLI QRRSKPDPST YIGSGKAQEL REVVLATGAD TVICDGELSP AQLTALEKAV KVKVIDRTAL ILDIFAQHAT SREGKAQVSL AQMEYMLPRL RGWGESMSRQ AGGRAGGSTG GVGLRGPGET KIETDRRRIR ERMARLRRDI KGMKRVRDTQ RRRRLASDVP SIAIVGYTNA GKSSLLNALT GAGVLVEDAL FATLEPTTRR GQFDDGRSFV ISDTVGFVRH LPTQLVEAFR STLEEVVDAD LLVHVVDGSD VNPLAQISAV RHVLCEVIAD HHGDPAPELL VVNKVDAAGD LALAKLRRAL PGAVFVSTRT GEGIDILRKR MAELTELSKP TDTAVDVVIP YHRGDLVSRV HTDGRVQEAE HHAHGTRIKA RVPVALAASL REFAAAGSQA TTS // ID I0TE09_9BACT Unreviewed; 416 AA. AC I0TE09; DT 13-JUN-2012, integrated into UniProtKB/TrEMBL. DT 13-JUN-2012, sequence version 1. DT 07-JUN-2017, entry version 30. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:EID33862.1}; GN ORFNames=HMPREF9969_1727 {ECO:0000313|EMBL:EID33862.1}; OS Prevotella sp. oral taxon 306 str. F0472. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Prevotellaceae; OC Prevotella. OX NCBI_TaxID=1095752 {ECO:0000313|EMBL:EID33862.1, ECO:0000313|Proteomes:UP000004421}; RN [1] {ECO:0000313|EMBL:EID33862.1, ECO:0000313|Proteomes:UP000004421} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=F0472 {ECO:0000313|EMBL:EID33862.1, RC ECO:0000313|Proteomes:UP000004421}; RA Durkin A.S., McCorrison J., Torralba M., Gillis M., Methe B., RA Sutton G., Nelson K.E.; RL Submitted (MAR-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EID33862.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AJIN01000025; EID33862.1; -; Genomic_DNA. DR RefSeq; WP_009434549.1; NZ_AJIN01000025.1. DR EnsemblBacteria; EID33862; EID33862; HMPREF9969_1727. DR PATRIC; fig|1095752.3.peg.833; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000004421; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000004421}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000004421}. FT DOMAIN 216 400 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 416 AA; 47687 MW; EF08687123CEB2A8 CRC64; MKEFIISEVK TETAILVGLI TKEQDEAKTK EYLDELEFLA DTAGAVTVKR FTQRVNGPSA VTYVGKGKLE EIKEYIKQKE DDDEPIGMVI FDDELSAKQM RNIEQELGVK ILDRTSLILD IFAMRAQTAN AKTQVELAQY RYMLPRLQRL WTHLERQGGG SGSGGGKGSV GLRGPGETQL EMDRRIILQR MSLLKQRLAE IDKQKTTQRK NRGRLIRVAL VGYTNVGKST TMNLLAKSEV FAENKLFATL DTTVRKVVVE NLPFLLADTV GFIRKLPTDL VDSFKSTLDE VREADLLLHV VDISHPDFEE QIQVVNQTLT ELGCADKPSM IIFNKIDNYH WIEKEEDDLT PATKENITLE ELKKTWMAKE QEQCLFISAK NKENIDEFRD VLYKKVRELH VQKYPYNDFL YNIEEE // ID I0WJW9_9FLAO Unreviewed; 407 AA. AC I0WJW9; DT 13-JUN-2012, integrated into UniProtKB/TrEMBL. DT 13-JUN-2012, sequence version 1. DT 07-JUN-2017, entry version 32. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=W5A_01640 {ECO:0000313|EMBL:EID76685.1}; OS Imtechella halotolerans K1. OC Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales; OC Flavobacteriaceae; Imtechella. OX NCBI_TaxID=946077 {ECO:0000313|EMBL:EID76685.1, ECO:0000313|Proteomes:UP000005938}; RN [1] {ECO:0000313|EMBL:EID76685.1, ECO:0000313|Proteomes:UP000005938} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K1 {ECO:0000313|EMBL:EID76685.1, RC ECO:0000313|Proteomes:UP000005938}; RX PubMed=22740661; DOI=10.1128/JB.00506-12; RA Kumar S., Vikram S., Subramanian S., Raghava G.P., Pinnaka A.K.; RT "Genome Sequence of the Halotolerant Bacterium Imtechella halotolerans RT K1T."; RL J. Bacteriol. 194:3731-3731(2012). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EID76685.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AJJU01000002; EID76685.1; -; Genomic_DNA. DR RefSeq; WP_008236715.1; NZ_AJJU01000002.1. DR EnsemblBacteria; EID76685; EID76685; W5A_01640. DR PATRIC; fig|946077.3.peg.337; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000005938; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000005938}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000005938}. FT DOMAIN 200 385 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 407 AA; 47259 MW; E51D7B0F44473CC1 CRC64; MLEKQQIEYE KVVLIGVITQ QQDESKSREY LDELEFLTYT AGGEVIQRFT QKIDVPNPKT FIGTGKMEEV EIFVNEHEVG TVIFDDELSP AQQKNIERIL KCKILDRTSL ILDIFAQRAQ TSYARTQVEL AQYQYLLPRL TGLWTHLERQ RGGIGMRGPG ETEIETDRRI VRDRIALLKK KLETIDKQMA TQRSNRGALV RVALVGYTNV GKSTLMNVIA KSEVFAENKL FATLDTTVRK VVIGNLPFLL SDTVGFIRKL PTQLVESFKS TLDEVREADL LLHVVDISHP NFEEHIHSVN QILTEIKSAD KPTIMVFNKI DAYEHLAIDE DDLITEKTAK YFTLEEWKQT WMNRMGDHVL FISALNRDNL EEFRQRVYQE VRRIHVTRFP YNNFLYPEFI EEGNEEE // ID I0XC74_9SPIO Unreviewed; 413 AA. AC I0XC74; DT 13-JUN-2012, integrated into UniProtKB/TrEMBL. DT 13-JUN-2012, sequence version 1. DT 07-JUN-2017, entry version 32. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=MSI_01960 {ECO:0000313|EMBL:EID86240.1}; OS Treponema sp. JC4. OC Bacteria; Spirochaetes; Spirochaetales; Spirochaetaceae; Treponema. OX NCBI_TaxID=1124982 {ECO:0000313|EMBL:EID86240.1, ECO:0000313|Proteomes:UP000002967}; RN [1] {ECO:0000313|EMBL:EID86240.1, ECO:0000313|Proteomes:UP000002967} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=JC4 {ECO:0000313|EMBL:EID86240.1, RC ECO:0000313|Proteomes:UP000002967}; RX PubMed=22815447; DOI=10.1128/JB.00754-12; RA Rosewarne C.P., Cheung J.L., Smith W.J., Evans P.N., Tomkins N.W., RA Denman S.E., O Cuiv P., Morrison M.; RT "Draft genome sequence of Treponema sp. strain JC4, a novel spirochete RT isolated from the bovine rumen."; RL J. Bacteriol. 194:4130-4130(2012). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EID86240.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AJGU01000001; EID86240.1; -; Genomic_DNA. DR RefSeq; WP_009102729.1; NZ_AJGU01000001.1. DR EnsemblBacteria; EID86240; EID86240; MSI_01960. DR PATRIC; fig|1124982.3.peg.196; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000002967; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000002967}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000002967}. FT DOMAIN 194 361 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 162 189 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 413 AA; 46194 MW; 8E835C697B3F0BFE CRC64; MVEVEKEQNK VPRALLVGEP GNDLQELKGL VQTLGLDIIQ RLTLNRMEVQ PQYGIGTGKA QEINELAHKI EADCIIFDFN IEPRKQRNWE ELTGLSVFDR QEVIIRIFAS RAQSKEATLQ VELARLQYSL PRLAHLRNDF ARQRGGAFGA KGSGETQLEL DQRRIREKIA QIKHDLAEVE LNRQTQRKQR GKQPSCALVG YTNAGKSSLL NALTGSDAFV ENKLFATLDP LTKKLPLNDS AGVLITDTVG FISNLPHHLI DAFKSTLEEA ATADLLLLVL DASDPNAESQ YETVCDVLDE IGANENPRIL LLNKIDKCDD ETKQLEKLRL KFPEALCISA KEEIGFVDLK DKIYNMLYGE ICNYVIPVSQ VLLINELRKS GCIQTEEWLD DGVHISARAV GRLLALASPF IVE // ID I0XST9_9LEPT Unreviewed; 541 AA. AC I0XST9; DT 13-JUN-2012, integrated into UniProtKB/TrEMBL. DT 13-JUN-2012, sequence version 1. DT 07-JUN-2017, entry version 35. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:EIE01947.1}; GN ORFNames=LEP1GSC185_0902 {ECO:0000313|EMBL:EIE01947.1}; OS Leptospira licerasiae serovar Varillal str. VAR 010. OC Bacteria; Spirochaetes; Leptospirales; Leptospiraceae; Leptospira. OX NCBI_TaxID=1049972 {ECO:0000313|EMBL:EIE01947.1, ECO:0000313|Proteomes:UP000004889}; RN [1] {ECO:0000313|EMBL:EIE01947.1, ECO:0000313|Proteomes:UP000004889} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=VAR 010 {ECO:0000313|EMBL:EIE01947.1}; RX PubMed=23145189; DOI=10.1371/journal.pntd.0001853; RA Ricaldi J.N., Fouts D.E., Selengut J.D., Harkins D.M., Patra K.P., RA Moreno A., Lehmann J.S., Purushe J., Sanka R., Torres M., RA Webster N.J., Vinetz J.M., Matthias M.A.; RT "Whole Genome Analysis of Leptospira licerasiae Provides Insight into RT Leptospiral Evolution and Pathogenicity."; RL PLoS Negl. Trop. Dis. 6:E1853-E1853(2012). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EIE01947.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AHOO02000005; EIE01947.1; -; Genomic_DNA. DR RefSeq; WP_008590039.1; NZ_AHOO02000005.1. DR EnsemblBacteria; EIE01947; EIE01947; LEP1GSC185_0902. DR PATRIC; fig|1049972.3.peg.219; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000004889; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000004889}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000004889}. FT DOMAIN 350 516 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 309 343 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 541 AA; 61579 MW; 4C147DB60E580860 CRC64; MIITPEVSRT LTELSFEISR QIGILIDRNG YVTHVIVGSD SSIDIPWLDR IRTSEARLRG LRLVHSHLKE ESLNQEDLTD LALLRLDYIT AVTMDEKGLP KSYYSAHVNP EDEEGEPWTV LPKKVPGQLE EGILDEILDI ESRMTRYRKN LKGAQKENRA FLVGVYPENN RVRPPAQSIE ELKELCRTAG VHVVDSFIQR KNRLDPSTVL GKGKLEEIVL KAIQKQVELL VFDLELTPSQ AKKISDYADL KVLDRTQLIL DIFARNATSR DGKLQVELAQ LKYLKGRLSE LDDNMSRLTG GIGGRGPGET KLEIGKRRVE ERISRLEQEL KSLKKRREIA RRRRKKNEIP VCGIVGYTNA GKSTLLNAMT NSSVLSEDKL FATLDPTSRR IRFPEEREII ISDTVGFIHD LPPELSNAFK ATLEELGDSD LLVHVVDVSN PEFRQQMEAV ETILEDLNLS DIPRILVFNK IDGLPEEARN ELLREADLDT IYVSATKGFG LNTLLNRIEE RIYSQAEAKL SSSKLWEEDE DWEEETEKTY V // ID I0YSA3_COCSC Unreviewed; 422 AA. AC I0YSA3; DT 13-JUN-2012, integrated into UniProtKB/TrEMBL. DT 13-JUN-2012, sequence version 1. DT 07-JUN-2017, entry version 19. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EIE21272.1}; DE Flags: Fragment; GN ORFNames=COCSUDRAFT_17737 {ECO:0000313|EMBL:EIE21272.1}; OS Coccomyxa subellipsoidea (strain C-169) (Green microalga). OC Eukaryota; Viridiplantae; Chlorophyta; Trebouxiophyceae; OC Trebouxiophyceae incertae sedis; Coccomyxaceae; Coccomyxa. OX NCBI_TaxID=574566 {ECO:0000313|EMBL:EIE21272.1, ECO:0000313|Proteomes:UP000007264}; RN [1] {ECO:0000313|EMBL:EIE21272.1, ECO:0000313|Proteomes:UP000007264} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C-169 {ECO:0000313|EMBL:EIE21272.1, RC ECO:0000313|Proteomes:UP000007264}; RX PubMed=22630137; DOI=10.1186/gb-2012-13-5-r39; RA Blanc G., Agarkova I., Grimwood J., Kuo A., Brueggeman A., Dunigan D., RA Gurnon J., Ladunga I., Lindquist E., Lucas S., Pangilinan J., RA Proschold T., Salamov A., Schmutz J., Weeks D., Yamada T., RA Claverie J.M., Grigoriev I., Van Etten J., Lomsadze A., Borodovsky M.; RT "The genome of the polar eukaryotic microalga coccomyxa subellipsoidea RT reveals traits of cold adaptation."; RL Genome Biol. 13:R39-R39(2012). CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EIE21272.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGSI01000013; EIE21272.1; -; Genomic_DNA. DR RefSeq; XP_005645816.1; XM_005645759.1. DR GeneID; 17039254; -. DR KEGG; csl:COCSUDRAFT_17737; -. DR KO; K03665; -. DR Proteomes; UP000007264; Unassembled WGS sequence. DR GO; GO:0003824; F:catalytic activity; IEA:InterPro. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR CDD; cd01878; HflX; 1. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000007264}; KW Reference proteome {ECO:0000313|Proteomes:UP000007264}. FT DOMAIN 199 374 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT NON_TER 1 1 {ECO:0000313|EMBL:EIE21272.1}. SQ SEQUENCE 422 AA; 46312 MW; A70736DD84D37A36 CRC64; ERALLVGVGA ANTGRRQGIQ YSLQDSLEEL AGLAEAAGLK VVGTLTQHID PDAQTYLGPG KVEEMLQAVA SRGANTVIFD GELSPRQLRN LSRKCSQQTR VCDRTALILD IFKQRAFTKE GQLQVEYAAT EYQLPRLTRM WTHLERQSGA GKMKGMGEKQ IDVDRRLLRS RLAILRGRLE EVQQCREQYR RSRAELAVPL IALVGYTNAG KSCLMNALTS AAVLSEDALF ATLDTTVRKI ILPSGLQARP QRHHSSSCLL DTVGFIQKLP PQLVAAFRAT LDDIKAASVI LHVVDCSHPL AAAQGEAVLK VLKEIGATEV PIITVWNKMD LVRDPEMVAT VAGGRQSVVC VSAHTGQGVD ELLNVIEEQL KASMEFVHLL IPFSKASSLW DVLLWRANAS YCIGNIIHGS VCFHLQHRPC IV // ID I0YW40_COCSC Unreviewed; 706 AA. AC I0YW40; DT 13-JUN-2012, integrated into UniProtKB/TrEMBL. DT 13-JUN-2012, sequence version 1. DT 07-JUN-2017, entry version 18. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EIE22609.1}; GN ORFNames=COCSUDRAFT_63755 {ECO:0000313|EMBL:EIE22609.1}; OS Coccomyxa subellipsoidea (strain C-169) (Green microalga). OC Eukaryota; Viridiplantae; Chlorophyta; Trebouxiophyceae; OC Trebouxiophyceae incertae sedis; Coccomyxaceae; Coccomyxa. OX NCBI_TaxID=574566 {ECO:0000313|EMBL:EIE22609.1, ECO:0000313|Proteomes:UP000007264}; RN [1] {ECO:0000313|EMBL:EIE22609.1, ECO:0000313|Proteomes:UP000007264} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C-169 {ECO:0000313|EMBL:EIE22609.1, RC ECO:0000313|Proteomes:UP000007264}; RX PubMed=22630137; DOI=10.1186/gb-2012-13-5-r39; RA Blanc G., Agarkova I., Grimwood J., Kuo A., Brueggeman A., Dunigan D., RA Gurnon J., Ladunga I., Lindquist E., Lucas S., Pangilinan J., RA Proschold T., Salamov A., Schmutz J., Weeks D., Yamada T., RA Claverie J.M., Grigoriev I., Van Etten J., Lomsadze A., Borodovsky M.; RT "The genome of the polar eukaryotic microalga coccomyxa subellipsoidea RT reveals traits of cold adaptation."; RL Genome Biol. 13:R39-R39(2012). CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EIE22609.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGSI01000009; EIE22609.1; -; Genomic_DNA. DR RefSeq; XP_005647153.1; XM_005647096.1. DR GeneID; 17040596; -. DR KEGG; csl:COCSUDRAFT_63755; -. DR Proteomes; UP000007264; Unassembled WGS sequence. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR CDD; cd01878; HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 4: Predicted; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000007264}; KW Reference proteome {ECO:0000313|Proteomes:UP000007264}. FT DOMAIN 237 308 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 196 223 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 706 AA; 74823 MW; 02FA49ED074506B2 CRC64; MGLVYSRAAD LITLRGFASD PCRSCVMVHP RAQPPPYVQE AMRLAESYAG AHCKSIAVGP SRGSPPTSAA FFGSGAVESL KGQLAALDPH TVFVNCMLSG VQQRNLEAAW QRPVTDRVGL IIKIFAQRAR TREARLQVEM ASLDYKVSRL VRSVDAATGQ RAGFGEGGLT EVVSARERGR SGGTSGGLGG SAGGGETELQ LQRRRIRARI KALKRQLAEV RQTRVTQRAG RLRAGKPVCA VVGYTNAGKS SLVSALSGDD VGVQDRLFET LDPTMRQVML PSGRGAILSD TVGFISDLPP SLIKAFQASN LTLYNIRILC PVLATLEEVV EADLLLHVMD GSSEQMLQQR DAVLAVLRRL GVSEMRLQKS LIEVVNKSDI FPGTASQSPD DTDLSAPDVA EPDLAAPDLA EPDLEASKLD TPSSSCGAPE EAGEVEGPWL HGGEVPSAKG SADTQALSDG SVEKQDSGAD ASCSGQQEAG SLSKKTSSGE TADRELGMQR EKSRGGFCGR GVEKEGTCRE TDGHSAALDW ARGRAGRQPS VVVTSAVTGD GLDDLLLEMD KKVSLKFAMR ELSEGAIRMG PRVLTENIVG PVVPGAEQEL KLIVHVEHEV RRGFWQRIHL SHSSFAATGS ISWRQGVCLK RPGELDLARQ AGENSSPSRA PASTEGSMRR DSRAAVYEDA GSSPTSHKAD PQGVGSQGTS TGDNAV // ID I1AR37_9RHOB Unreviewed; 417 AA. AC I1AR37; DT 13-JUN-2012, integrated into UniProtKB/TrEMBL. DT 13-JUN-2012, sequence version 1. DT 07-JUN-2017, entry version 29. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=C357_21182 {ECO:0000313|EMBL:EIE48958.1}; OS Citreicella sp. 357. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae; Citreicella. OX NCBI_TaxID=766499 {ECO:0000313|EMBL:EIE48958.1, ECO:0000313|Proteomes:UP000003110}; RN [1] {ECO:0000313|EMBL:EIE48958.1, ECO:0000313|Proteomes:UP000003110} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=357 {ECO:0000313|EMBL:EIE48958.1, RC ECO:0000313|Proteomes:UP000003110}; RX PubMed=22965089; DOI=10.1128/JB.01261-12; RA Suarez-Suarez L.Y., Brunet-Galmes I., Pina-Villalonga J.M., RA Christie-Oleza J.A., Pena A., Bennasar A., Armengaud J., Nogales B., RA Bosch R.; RT "Draft Genome Sequence of Citreicella aestuarii Strain 357, a Member RT of the Roseobacter Clade Isolated without Xenobiotic Pressure from a RT Petroleum-Polluted Beach."; RL J. Bacteriol. 194:5464-5465(2012). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EIE48958.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AJKJ01000158; EIE48958.1; -; Genomic_DNA. DR EnsemblBacteria; EIE48958; EIE48958; C357_21182. DR PATRIC; fig|766499.3.peg.4157; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000003110; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000003110}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000003110}. FT DOMAIN 197 366 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 417 AA; 46450 MW; 4969E381C8A3440D CRC64; MTRAWVLHPD IRFERDRRDA DMALEEAVAL AAALPNLDVA GATVVPLRDP HPGTLFGSGK IEELRARIEA EEIELVLVDG PVSPVQQRNL EKAWKVKLLD RTGLILEIFS DRAATREGVL QVEMAALSYQ RTRLVRAWTH LERQRGGLGF VGGPGETQIE ADRRAIDEQL VRLRRQLDRV VKTRELHRKA RAKVPYPIVA LVGYTNAGKS TLFNRLTGAD VMAKDMLFAT LDPTMRAVRL PTGIDVILSD TVGFISDLPT ELVAAFRATL EEVIAADIIL HVRDISHPNT AEQARDVDQI LTSLGVNEDV PLLEVWNKTD RLDPESHDAM QARADRDEGV FAASALTGAG LDTLLRAVTD RLQGDSIEED LRLGFDDGKR RSWLFGKGLV LDERQDDDGS LLRVRWSATD RARFQTL // ID I1DUT4_9GAMM Unreviewed; 431 AA. AC I1DUT4; DT 13-JUN-2012, integrated into UniProtKB/TrEMBL. DT 13-JUN-2012, sequence version 1. DT 30-AUG-2017, entry version 34. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:GAB57812.1}; GN ORFNames=RNAN_0782 {ECO:0000313|EMBL:GAB57812.1}; OS Rheinheimera nanhaiensis E407-8. OC Bacteria; Proteobacteria; Gammaproteobacteria; Chromatiales; OC Chromatiaceae; Rheinheimera. OX NCBI_TaxID=562729 {ECO:0000313|EMBL:GAB57812.1, ECO:0000313|Proteomes:UP000004374}; RN [1] {ECO:0000313|EMBL:GAB57812.1, ECO:0000313|Proteomes:UP000004374} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=E407-8 {ECO:0000313|EMBL:GAB57812.1, RC ECO:0000313|Proteomes:UP000004374}; RX PubMed=23209246; DOI=10.1128/JB.01922-12; RA Zhang X.-Y., Zhang Y.-J., Qin Q.-L., Xie B.-B., Chen X.-L., RA Zhou B.-C., Zhang Y.-Z.; RT "Genome Sequence of the Protease-Producing Bacterium Rheinheimera RT nanhaiensis E407-8T, Isolated from Deep-Sea Sediment of the South RT China Sea."; RL J. Bacteriol. 194:7001-7002(2012). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:GAB57812.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BAFK01000003; GAB57812.1; -; Genomic_DNA. DR RefSeq; WP_008218910.1; NZ_BAFK01000003.1. DR EnsemblBacteria; GAB57812; GAB57812; RNAN_0782. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000004374; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000004374}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000004374}. FT DOMAIN 198 364 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 157 191 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 431 AA; 47442 MW; 4ACB2FC9D7DE09C9 CRC64; MSELNAVSEQ AILVHVNFSQ QHTSEDLGEL KLLVSSAGVQ AIDVVTTSRS APDAKFFVGS GKAQDIANLI ADTGATLVIF NHALSPAQTR NLERLCLARV IDRTTLILDI FAQRARTFEG KLQVELAQLK HLSSRLVRGW DSLDRQKGGI GLRGPGETQL ETDRRLLRER VKALQARLAK LQTQRQQGRR ARQRAEVPVV SVVGYTNAGK STLFNRLTKA DVYAADQLFA TLDPTLRKLP LKGVGDIILA DTVGFIRHLP HDLVAAFKST LQETRDADLQ LHVVDVADAR KGDNMQQVAK VLADIDADQL PQLLVFNKID LLGQPARIEY NDAGQPVAVY LSAMTGAGLD LLAQAMAQLL SERYIDIALA LPPAQASWRS RCHQQDCVVQ EQYTEDGTCH LQLRLSAAQW QRMVKQSQGV LENYIVSAPV I // ID I1GNS0_BRADI Unreviewed; 591 AA. AC I1GNS0; DT 13-JUN-2012, integrated into UniProtKB/TrEMBL. DT 13-JUN-2012, sequence version 1. DT 07-JUN-2017, entry version 28. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:KQK13414.1, ECO:0000313|EnsemblPlants:BRADI1G10007.1}; GN Name=LOC100827021 {ECO:0000313|EnsemblPlants:BRADI1G10007.1}; GN ORFNames=BRADI_1g10007 {ECO:0000313|EMBL:KQK13414.1}; OS Brachypodium distachyon (Purple false brome) (Trachynia distachya). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; BOP clade; OC Pooideae; Brachypodieae; Brachypodium. OX NCBI_TaxID=15368 {ECO:0000313|EnsemblPlants:BRADI1G10007.1, ECO:0000313|Proteomes:UP000008810}; RN [1] {ECO:0000313|EMBL:KQK13414.1, ECO:0000313|EnsemblPlants:BRADI1G10007.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Bd21 {ECO:0000313|EMBL:KQK13414.1, RC ECO:0000313|EnsemblPlants:BRADI1G10007.1}; RX PubMed=20148030; DOI=10.1038/nature08747; RG International Brachypodium Initiative; RT "Genome sequencing and analysis of the model grass Brachypodium RT distachyon."; RL Nature 463:763-768(2010). RN [2] {ECO:0000313|EnsemblPlants:BRADI1G10007.1} RP IDENTIFICATION. RC STRAIN=cv. Bd21 {ECO:0000313|EnsemblPlants:BRADI1G10007.1}; RG EnsemblPlants; RL Submitted (NOV-2012) to UniProtKB. RN [3] {ECO:0000313|EMBL:KQK13414.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=Bd21 {ECO:0000313|EMBL:KQK13414.1}; RG The International Brachypodium Initiative; RA Lucas S., Harmon-Smith M., Lail K., Tice H., Grimwood J., Bruce D., RA Barry K., Lindquist E., Wang M., Pitluck S., Vogel J.P., Garvin D.F., RA Mockler T.C., Jenkins J., Schmutz J., Rokhsar D., Bevan M.W.; RT "WGS assembly of Brachypodium distachyon."; RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CM000880; KQK13414.1; -; Genomic_DNA. DR RefSeq; XP_003560327.1; XM_003560279.3. DR RefSeq; XP_010230570.1; XM_010232268.2. DR RefSeq; XP_010230574.1; XM_010232272.2. DR STRING; 15368.BRADI1G10007.1; -. DR EnsemblPlants; BRADI1G10007.1; BRADI1G10007.1; BRADI1G10007. DR GeneID; 100827021; -. DR Gramene; BRADI1G10007.1; BRADI1G10007.1; BRADI1G10007. DR KEGG; bdi:100827021; -. DR eggNOG; KOG0410; Eukaryota. DR eggNOG; COG2262; LUCA. DR InParanoid; I1GNS0; -. DR OMA; NGPEAIS; -. DR OrthoDB; EOG09360975; -. DR Proteomes; UP000008810; Chromosome 1. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR GO; GO:0043022; F:ribosome binding; IBA:GO_Central. DR CDD; cd01878; HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 2. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008810}; KW Reference proteome {ECO:0000313|Proteomes:UP000008810}. FT DOMAIN 300 563 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 591 AA; 64818 MW; 3F8415DAC8B4657D CRC64; MFRAAISRLG AHLHRHPSPA SPPVRALSTG RGKRSSPTAA PPEPEDEGLM RGLFVLSRDP EHPPRLLVVQ PRLRPSTLLD SKLAEALNLA SSLQEARDGF DRADESAAKD GPPHLVVQNP ASRGRNHADT YFGPGTVDNI KCYLRALDAE EELDAVFVNT LLSGIQQRNL EVAWVKPVLD RVGLIIEIFN AHAETKEAKL QSELAALMYM KTRLVRVRGP GGRLTFGTSG EAEVVSARGR GSGGRGFMSG AGETELQLQR RRIQDRRISL LTQIEDVRRT RAIQRSSRKR HGGSFGQELV TIAVVGYTNA GKSTLVSALS EADLYSDDRL FATVDPRLRS VILPSGRKAL LSDTVGFISD LPVQLVEAFH ATLEEVAEAD MLVHVLDSSA PNLDEHRSTV LQVLQQIGVS EDKINNMIEV WNKIDLVDNN ALTDGIEDEI FLTEGEEEED LFSEDDVPSE QSSFDSLDDT VDSESLSEEN SENGDDKMAS DKSFDEPIDM KAMNSELLTT ECFREPNGPK AVTTSGCTLT QSVSTCHVKT SAVTGTGLQE LLQLIDTKLN EQQQTVVQRS YGPFDRKWRP CSLDGKKAAE Q // ID I1IKQ2_BRADI Unreviewed; 560 AA. AC I1IKQ2; DT 13-JUN-2012, integrated into UniProtKB/TrEMBL. DT 13-JUN-2012, sequence version 1. DT 30-AUG-2017, entry version 34. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:KQJ88003.1, ECO:0000313|EnsemblPlants:BRADI4G14850.1}; GN Name=LOC100827192 {ECO:0000313|EnsemblPlants:BRADI4G14850.1}; GN ORFNames=BRADI_4g14850 {ECO:0000313|EMBL:KQJ88003.1}; OS Brachypodium distachyon (Purple false brome) (Trachynia distachya). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; BOP clade; OC Pooideae; Brachypodieae; Brachypodium. OX NCBI_TaxID=15368 {ECO:0000313|EnsemblPlants:BRADI4G14850.1, ECO:0000313|Proteomes:UP000008810}; RN [1] {ECO:0000313|EMBL:KQJ88003.1, ECO:0000313|EnsemblPlants:BRADI4G14850.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Bd21 {ECO:0000313|EMBL:KQJ88003.1, RC ECO:0000313|EnsemblPlants:BRADI4G14850.1}; RX PubMed=20148030; DOI=10.1038/nature08747; RG International Brachypodium Initiative; RT "Genome sequencing and analysis of the model grass Brachypodium RT distachyon."; RL Nature 463:763-768(2010). RN [2] {ECO:0000313|EnsemblPlants:BRADI4G14850.1} RP IDENTIFICATION. RC STRAIN=cv. Bd21 {ECO:0000313|EnsemblPlants:BRADI4G14850.1}; RG EnsemblPlants; RL Submitted (NOV-2012) to UniProtKB. RN [3] {ECO:0000313|EMBL:KQJ88003.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=Bd21 {ECO:0000313|EMBL:KQJ88003.1}; RG The International Brachypodium Initiative; RA Lucas S., Harmon-Smith M., Lail K., Tice H., Grimwood J., Bruce D., RA Barry K., Lindquist E., Wang M., Pitluck S., Vogel J.P., Garvin D.F., RA Mockler T.C., Jenkins J., Schmutz J., Rokhsar D., Bevan M.W.; RT "WGS assembly of Brachypodium distachyon."; RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CM000883; KQJ88003.1; -; Genomic_DNA. DR RefSeq; XP_003575913.2; XM_003575865.2. DR STRING; 15368.BRADI4G14850.1; -. DR EnsemblPlants; BRADI4G14850.1; BRADI4G14850.1; BRADI4G14850. DR GeneID; 100827192; -. DR Gramene; BRADI4G14850.1; BRADI4G14850.1; BRADI4G14850. DR KEGG; bdi:100827192; -. DR eggNOG; KOG0410; Eukaryota. DR eggNOG; COG2262; LUCA. DR InParanoid; I1IKQ2; -. DR KO; K03665; -. DR OMA; VILEIFH; -. DR OrthoDB; EOG093609UJ; -. DR Proteomes; UP000008810; Chromosome 4. DR ExpressionAtlas; I1IKQ2; baseline. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR GO; GO:0043022; F:ribosome binding; IBA:GO_Central. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000008810}; KW Reference proteome {ECO:0000313|Proteomes:UP000008810}. FT DOMAIN 336 501 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 302 329 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 560 AA; 61760 MW; D65560CFFE94797B CRC64; MRAACYSSFV AAASLPLTST SSAASDPRRL SLSRSSLRCS PLRRGGGGVA RALDERLLEA AAAAPAPAEV EVEDESGVTE VEDGGQWEGE GAEEGVGSSE AEGEQGQRKS KRQQQQQQQE EAAAAERDRF KLINGKEIFQ EKTYLVGVEC KRAGGYDFSI EESLKELEQL ADTAGLMVVG STYQKLSNPN PRTYIGSGKV GEIRTAIQAL DVETVIFDDE LSAGQLRNLE KSFGGSVRVC DRTALILDIF NQRAATHEAD LQVTLAQMEY QLPRLTKMWT HLERQSGGQV KGMGEKQIEV DKRILRTQIS TLRKELESVR KHRKLYRNRR QSVPIPVVSL VGYTNAGKST LLNRLTGADV LAEDKLFATL DPTTRRVLMK SGTEFLLTDT VGFIQKLPTM LVAAFRATLE EISESSIIVH LVDISHPLAQ QQIDAVDKVL KELDIESIPK LVVWNKIDNT DDPLRVKEEA EKQGTICISA MNGDGLEEFC YAIQTKLKDS MVPIEAFVPY DKGELLNDIH KVGMVEKMEY MENGTFVKAH VPLPLARLLT PLRQQVAAAL // ID I1IKQ3_BRADI Unreviewed; 436 AA. AC I1IKQ3; DT 13-JUN-2012, integrated into UniProtKB/TrEMBL. DT 13-JUN-2012, sequence version 1. DT 05-JUL-2017, entry version 23. DE SubName: Full=Uncharacterized protein {ECO:0000313|EnsemblPlants:BRADI4G14850.2}; GN Name=LOC100827192 {ECO:0000313|EnsemblPlants:BRADI4G14850.2}; OS Brachypodium distachyon (Purple false brome) (Trachynia distachya). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; BOP clade; OC Pooideae; Brachypodieae; Brachypodium. OX NCBI_TaxID=15368 {ECO:0000313|EnsemblPlants:BRADI4G14850.2, ECO:0000313|Proteomes:UP000008810}; RN [1] {ECO:0000313|EnsemblPlants:BRADI4G14850.2} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Bd21 {ECO:0000313|EnsemblPlants:BRADI4G14850.2}; RX PubMed=20148030; DOI=10.1038/nature08747; RG International Brachypodium Initiative; RT "Genome sequencing and analysis of the model grass Brachypodium RT distachyon."; RL Nature 463:763-768(2010). RN [2] {ECO:0000313|EnsemblPlants:BRADI4G14850.2} RP IDENTIFICATION. RC STRAIN=cv. Bd21 {ECO:0000313|EnsemblPlants:BRADI4G14850.2}; RG EnsemblPlants; RL Submitted (NOV-2012) to UniProtKB. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EnsemblPlants; BRADI4G14850.2; BRADI4G14850.2; BRADI4G14850. DR Gramene; BRADI4G14850.2; BRADI4G14850.2; BRADI4G14850. DR eggNOG; KOG0410; Eukaryota. DR eggNOG; COG2262; LUCA. DR Proteomes; UP000008810; Chromosome 4. DR ExpressionAtlas; I1IKQ3; baseline. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000008810}; KW Reference proteome {ECO:0000313|Proteomes:UP000008810}. FT DOMAIN 336 436 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 302 329 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 436 AA; 47946 MW; 39A96BD2AFC6A154 CRC64; MRAACYSSFV AAASLPLTST SSAASDPRRL SLSRSSLRCS PLRRGGGGVA RALDERLLEA AAAAPAPAEV EVEDESGVTE VEDGGQWEGE GAEEGVGSSE AEGEQGQRKS KRQQQQQQQE EAAAAERDRF KLINGKEIFQ EKTYLVGVEC KRAGGYDFSI EESLKELEQL ADTAGLMVVG STYQKLSNPN PRTYIGSGKV GEIRTAIQAL DVETVIFDDE LSAGQLRNLE KSFGGSVRVC DRTALILDIF NQRAATHEAD LQVTLAQMEY QLPRLTKMWT HLERQSGGQV KGMGEKQIEV DKRILRTQIS TLRKELESVR KHRKLYRNRR QSVPIPVVSL VGYTNAGKST LLNRLTGADV LAEDKLFATL DPTTRRVLMK SGTEFLLTDT VGFIQKLPTM LVAAFRATLE EISESSIIVH LVDIRCETDV HNILVM // ID I1MXZ3_SOYBN Unreviewed; 529 AA. AC I1MXZ3; DT 13-JUN-2012, integrated into UniProtKB/TrEMBL. DT 09-JAN-2013, sequence version 2. DT 30-AUG-2017, entry version 36. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:KRH05872.1, ECO:0000313|EnsemblPlants:GLYMA17G37250.1}; GN Name=LOC100803039 {ECO:0000313|EnsemblPlants:GLYMA17G37250.1}; GN ORFNames=GLYMA_17G253900 {ECO:0000313|EMBL:KRH05872.1}; OS Glycine max (Soybean) (Glycine hispida). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae; OC Pentapetalae; rosids; fabids; Fabales; Fabaceae; Papilionoideae; OC Phaseoleae; Glycine; Soja. OX NCBI_TaxID=3847 {ECO:0000313|EnsemblPlants:GLYMA17G37250.1, ECO:0000313|Proteomes:UP000008827}; RN [1] {ECO:0000313|EnsemblPlants:GLYMA17G37250.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Williams 82 {ECO:0000313|EnsemblPlants:GLYMA17G37250.1}; RX PubMed=16247559; DOI=10.1007/s11103-005-8882-0; RA Saski C., Lee S.-B., Daniell H., Wood T.C., Tomkins J., Kim H.-G., RA Jansen R.K.; RT "Complete chloroplast genome sequence of Glycine max and comparative RT analyses with other legume genomes."; RL Plant Mol. Biol. 59:309-322(2005). RN [2] {ECO:0000313|EMBL:KRH05872.1} RP NUCLEOTIDE SEQUENCE. RC TISSUE=Callus {ECO:0000313|EMBL:KRH05872.1}; RX PubMed=20075913; DOI=10.1038/nature08670; RA Schmutz J., Cannon S.B., Schlueter J., Ma J., Mitros T., Nelson W., RA Hyten D.L., Song Q., Thelen J.J., Cheng J., Xu D., Hellsten U., RA May G.D., Yu Y., Sakurai T., Umezawa T., Bhattacharyya M.K., RA Sandhu D., Valliyodan B., Lindquist E., Peto M., Grant D., Shu S., RA Goodstein D., Barry K., Futrell-Griggs M., Abernathy B., Du J., RA Tian Z., Zhu L., Gill N., Joshi T., Libault M., Sethuraman A., RA Zhang X.-C., Shinozaki K., Nguyen H.T., Wing R.A., Cregan P., RA Specht J., Grimwood J., Rokhsar D., Stacey G., Shoemaker R.C., RA Jackson S.A.; RT "Genome sequence of the palaeopolyploid soybean."; RL Nature 463:178-183(2010). RN [3] {ECO:0000313|EnsemblPlants:GLYMA17G37250.1} RP IDENTIFICATION. RC STRAIN=Williams 82 {ECO:0000313|EnsemblPlants:GLYMA17G37250.1}; RG EnsemblPlants; RL Submitted (MAY-2013) to the EMBL/GenBank/DDBJ databases. RN [4] {ECO:0000313|EMBL:KRH05872.1} RP NUCLEOTIDE SEQUENCE. RC TISSUE=Callus {ECO:0000313|EMBL:KRH05872.1}; RA Hoefler B.C., Straight P.D.; RL Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CM000850; KRH05872.1; -; Genomic_DNA. DR RefSeq; XP_003550400.1; XM_003550352.3. DR UniGene; Gma.6966; -. DR STRING; 3847.GLYMA17G37250.1; -. DR EnsemblPlants; GLYMA17G37250.1; GLYMA17G37250.1; GLYMA17G37250. DR GeneID; 100803039; -. DR Gramene; GLYMA17G37250.1; GLYMA17G37250.1; GLYMA17G37250. DR KEGG; gmx:100803039; -. DR eggNOG; KOG0410; Eukaryota. DR eggNOG; COG2262; LUCA. DR InParanoid; I1MXZ3; -. DR KO; K03665; -. DR OMA; VILEIFH; -. DR OrthoDB; EOG093609UJ; -. DR Proteomes; UP000008827; Chromosome 17. DR GO; GO:0009507; C:chloroplast; IEA:EnsemblPlants. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR GO; GO:0043022; F:ribosome binding; IBA:GO_Central. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000008827}; KW Reference proteome {ECO:0000313|Proteomes:UP000008827}. FT DOMAIN 304 470 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 529 AA; 59098 MW; 94F0BDC5E9154B2E CRC64; MSGTGTFFYG SVIQPLIRYH YLSPPIPIRP LCCISPLITS IHSNDAVSPQ NGTLRFQTEH QQHSEEPLPV PSLSAAEENK ATTKLRKKKE DDVVSDNRFK LRNGREVFEE KAYLVGVERK NDVQDFGIEE SLSELSQLVD TAGLLVVGST YQKLTSPNPR TYIGSGKVSE IKSAIHALGV ETVIFDDELS AGQLRNLEKI FGGDVRVCDR TALILDIFNQ RAATHEASLQ VSLAQMEYQL PRLTKMWTHL ERQAGGKVKG MGEKQIEVDK RILRNQIGIL KKELESVRKH RKQYRNRRFS VPVAVVSLVG YTNAGKSTLL NQLTGADVLA EDKLFATLDP TTRRVQMKNG KEFLLTDTVG FIQKLPTTLV AAFRATLEEI SESSLLVHVV DISHPLAEQQ INAVDKVLSE LDVSSIPKLI VWNKVDKVGD PQKLRLEAEK RDDVVCISAL SGNGLQEFCN AVQDKLKDSM VWVEALVPFE NGDLLSTIHQ VGMVEKTEYT EQGTYIKAHV PLRFARMLTP MRQLCVSQP // ID I1R1C1_ORYGL Unreviewed; 558 AA. AC I1R1C1; DT 13-JUN-2012, integrated into UniProtKB/TrEMBL. DT 13-JUN-2012, sequence version 1. DT 30-AUG-2017, entry version 27. DE SubName: Full=Uncharacterized protein {ECO:0000313|EnsemblPlants:ORGLA11G0156300.1}; OS Oryza glaberrima (African rice). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; BOP clade; OC Oryzoideae; Oryzeae; Oryzinae; Oryza. OX NCBI_TaxID=4538 {ECO:0000313|EnsemblPlants:ORGLA11G0156300.1, ECO:0000313|Proteomes:UP000007306}; RN [1] {ECO:0000313|EnsemblPlants:ORGLA11G0156300.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=IRGC 96717 {ECO:0000313|EnsemblPlants:ORGLA11G0156300.1}; RA Wing R.A., Yu Y., Rounsley S., Reddy-Marri P., Goicoechea J.L., RA Sisneros N., Lee S., Song X., Angelova A., Kudrna D.P., de Baynast K., RA Zuccolo A.; RT "The complete genome of Oryza glaberrima."; RL Submitted (JUN-2010) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EnsemblPlants:ORGLA11G0156300.1} RP IDENTIFICATION. RG EnsemblPlants; RL Submitted (JUN-2015) to UniProtKB. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR STRING; 4538.ORGLA11G0156300.1; -. DR EnsemblPlants; ORGLA11G0156300.1; ORGLA11G0156300.1; ORGLA11G0156300. DR Gramene; ORGLA11G0156300.1; ORGLA11G0156300.1; ORGLA11G0156300. DR eggNOG; KOG0410; Eukaryota. DR eggNOG; COG2262; LUCA. DR OMA; VILEIFH; -. DR OrthoDB; EOG093609UJ; -. DR Proteomes; UP000007306; Unassembled WGS sequence. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000007306}; KW Reference proteome {ECO:0000313|Proteomes:UP000007306}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1 24 {ECO:0000256|SAM:SignalP}. FT CHAIN 25 558 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5003652012. FT DOMAIN 334 499 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 300 327 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 558 AA; 61254 MW; 05FE13E783D11E85 CRC64; MRAACFFTAA AAAAASLPLP STSASASACC QRRPASLRCS RPRRSFGVAR ALDERLVEAA PPAPPAETEV EEPGVADGGG EGEGEGEVEE AAPSGEEEEE EEQPARAPVR SRRRQEEEEE AAPGHDRFKL INGKEIFQEK AYLVGVECKR SGGSMFSIEE SLEELEQLAD TAGLMVVGST YQKLSTPNPR TYIGSGKVAE IKSAIHAHDV ETVIFDDELS PGQLRNLEKS FGGGVRVCDR TALILDIFNQ RAATHEAALQ VTLAQMEYQL PRLTKMWSHL ERQSGGQVKG MGEKQIEVDK RILRTQISAL RKELESVRKH RKLYRNRRQS VPIPVVSLVG YTNAGKSTLL NRLTGADVLA EDKLFATLDP TTRRVLMKNG TEFLLTDTVG FIQKLPTMLV AAFRATLEEI SESSVIVHLV DISHPLAQQQ IDAVDKVLKE LDIESIPKLV VWNKIDNTDD TLRVKEEAEK QGIICISAIN GDGLEEFCNA IQAKLKDSLV PIEAFVPYDK GELLSDIHKV GMVEKTEYME NGTFVKAHVP LPLARLLTPL RQQVAAVS // ID I1XL26_METNJ Unreviewed; 381 AA. AC I1XL26; DT 11-JUL-2012, integrated into UniProtKB/TrEMBL. DT 11-JUL-2012, sequence version 1. DT 07-JUN-2017, entry version 35. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Q7A_2285 {ECO:0000313|EMBL:AFI85095.1}; OS Methylophaga nitratireducenticrescens (strain ATCC BAA-2433 / DSM OS 25689 / JAM1). OC Bacteria; Proteobacteria; Gammaproteobacteria; Thiotrichales; OC Piscirickettsiaceae; Methylophaga. OX NCBI_TaxID=754476 {ECO:0000313|EMBL:AFI85095.1, ECO:0000313|Proteomes:UP000009144}; RN [1] {ECO:0000313|EMBL:AFI85095.1, ECO:0000313|Proteomes:UP000009144} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=JAM1 {ECO:0000313|EMBL:AFI85095.1, RC ECO:0000313|Proteomes:UP000009144}; RX PubMed=22815445; DOI=10.1128/JB.00726-12; RA Villeneuve C., Martineau C., Mauffrey F., Villemur R.; RT "Complete genome sequences of Methylophaga sp. strain JAM1 and RT Methylophaga sp. strain JAM7."; RL J. Bacteriol. 194:4126-4127(2012). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP003390; AFI85095.1; -; Genomic_DNA. DR RefSeq; WP_014707463.1; NC_017857.2. DR EnsemblBacteria; AFI85095; AFI85095; Q7A_2285. DR KEGG; mej:Q7A_2285; -. DR PATRIC; fig|754476.3.peg.2258; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000009144; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000009144}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000009144}. FT DOMAIN 207 374 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 173 200 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 381 AA; 43244 MW; 1FFF13FBD9944A91 CRC64; MFDRPDSNAA FEENSEQESV VLVHLDFNDR GFDEKQQEFL ELVNSTGTNI SAVVHGKRQR PDSKYFAGSG KVEEIAELVA ANDAAVVIFN HELSPSQERN LEQRLKCRVL GRTGLILDIF ARRARSHEGK LQVELAQLQH LSTRLVRGWT HLERQKGGIG LRGPGETQLE TDRRLLGQRI KSLKKRLDKV RSQRDQGRRS RQRSGIPVVS LVGYTNVGKS TLFNRMTASD VYADDRLFAT LDPTLRRLRL ADTEPLIIAD TVGFIRQLPH DLVESFSSTL EETRDASLLL HVVDAAALDR DELMKHVDDV LQQIGADELP QLIIYNKIDR LENVQPKIER DQQGKIRRIW LSAQIGEGLD LLRMALQEYF PEQLSAIESV N // ID I1YKW5_METFJ Unreviewed; 382 AA. AC I1YKW5; DT 11-JUL-2012, integrated into UniProtKB/TrEMBL. DT 11-JUL-2012, sequence version 1. DT 07-JUN-2017, entry version 36. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Q7C_2433 {ECO:0000313|EMBL:AFJ03558.1}; OS Methylophaga frappieri (strain ATCC BAA-2434 / DSM 25690 / JAM7). OC Bacteria; Proteobacteria; Gammaproteobacteria; Thiotrichales; OC Piscirickettsiaceae; Methylophaga. OX NCBI_TaxID=754477 {ECO:0000313|EMBL:AFJ03558.1, ECO:0000313|Proteomes:UP000009145}; RN [1] {ECO:0000313|EMBL:AFJ03558.1, ECO:0000313|Proteomes:UP000009145} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=JAM7 {ECO:0000313|EMBL:AFJ03558.1, RC ECO:0000313|Proteomes:UP000009145}; RX PubMed=22815445; DOI=10.1128/JB.00726-12; RA Villeneuve C., Martineau C., Mauffrey F., Villemur R.; RT "Complete genome sequences of Methylophaga sp. strain JAM1 and RT Methylophaga sp. strain JAM7."; RL J. Bacteriol. 194:4126-4127(2012). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP003380; AFJ03558.1; -; Genomic_DNA. DR RefSeq; WP_014704976.1; NC_017856.1. DR EnsemblBacteria; AFJ03558; AFJ03558; Q7C_2433. DR KEGG; mec:Q7C_2433; -. DR PATRIC; fig|754477.3.peg.2391; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000009145; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000009145}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000009145}. FT DOMAIN 207 374 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 382 AA; 42987 MW; 218751487ECD6DC0 CRC64; MFDRPDSKAA LSEDSQQDSV ILVHLNFNDP AFDETQEEFF ELVNSTGAKI AGVIAGKRYR PDAKYFAGSG KVDEIGEFVE QHHASLVIFN HELSPSQERN LEQRLKCRVL GRTGLILDIF ARRARSHEGK LQVELAQLQH LSTRLVRGWT HLERQKGGIG LRGPGETQLE TDRRLLGGRI KSLKKRLDKV RSQREQGRRS RQRSGIPVIS LVGYTNVGKS SLFNKMTAAG VYADDRLFAT LDPTLRRMQL VDTEPLILAD TVGFIRQLPH DLVESFSSTL EETRDANLLL HVVDAVAPDR DELMAQVDSV LEQIGAQGVP QLTIYNKIDK ANDLQPRIER DQQGQIQRVW LSAQTGEGLE LLRLALQERF PADMPYAQPV NP // ID I1YSS5_PREI7 Unreviewed; 420 AA. AC I1YSS5; DT 11-JUL-2012, integrated into UniProtKB/TrEMBL. DT 11-JUL-2012, sequence version 1. DT 07-JUN-2017, entry version 38. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:AFJ08164.1}; GN OrderedLocusNames=PIN17_A1888 {ECO:0000313|EMBL:AFJ08164.1}; OS Prevotella intermedia (strain 17). OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Prevotellaceae; OC Prevotella. OX NCBI_TaxID=246198 {ECO:0000313|EMBL:AFJ08164.1, ECO:0000313|Proteomes:UP000010099}; RN [1] {ECO:0000313|EMBL:AFJ08164.1, ECO:0000313|Proteomes:UP000010099} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=17 {ECO:0000313|EMBL:AFJ08164.1, RC ECO:0000313|Proteomes:UP000010099}; RA Heidelberg J., Mongodin E., Moffat K., Khouri H., Brinkac L., RA Durkin A.S., Duncan M., Nelson K.E.; RL Submitted (APR-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP003503; AFJ08164.1; -; Genomic_DNA. DR RefSeq; WP_014710357.1; NC_017861.1. DR EnsemblBacteria; AFJ08164; AFJ08164; PIN17_A1888. DR KEGG; pit:PIN17_A1888; -. DR PATRIC; fig|246198.10.peg.2320; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000010099; Chromosome II. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000010099}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000010099}. FT DOMAIN 216 400 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 420 AA; 48110 MW; 9B10E585EE19C947 CRC64; MKEFVISEVK AETAILVGLI TQEQDEAKTK EYLDELEFLA DTAGAVTVKR FTQRVGGPNM TSYVGKGKLA EIKEYIKAKE DEDEPIGMVI FDDELSAKQL RNIENELQVK ILDRTSLILD IFAMRAQTAN AKTQVELAQY RYMLPRLQRL WTHLERQGGG SGSGGGKGSV GLRGPGETQL EMDRRIILQR MTLLKQRLVE IDKQKITQRK NRGRLIRVAL VGYTNVGKST IMNMLAKSEV FAENKLFATL DTTVRKVVLQ NLPFLLADTV GFIRKLPTDL VDSFKSTLDE VREADLLLHV VDISHPDFEE QIQVVTETLK DLECAEKPSM IIFNKIDNYT WEEKEEDDLT PMSKENVSLE ELKRTWMAKL NDDCLFISAK EKENIDEFRD ILYKKVKELH VQKYPYNDFL YNTDVEEGVQ // ID I2BDM5_SHIBC Unreviewed; 426 AA. AC I2BDM5; K6W1E5; DT 11-JUL-2012, integrated into UniProtKB/TrEMBL. DT 11-JUL-2012, sequence version 1. DT 30-AUG-2017, entry version 40. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:AFJ48629.1}; GN OrderedLocusNames=EBL_c35740 {ECO:0000313|EMBL:AFJ48629.1}; OS Shimwellia blattae (strain ATCC 29907 / DSM 4481 / JCM 1650 / NBRC OS 105725 / CDC 9005-74) (Escherichia blattae). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; OC Enterobacteriaceae; Shimwellia. OX NCBI_TaxID=630626 {ECO:0000313|EMBL:AFJ48629.1, ECO:0000313|Proteomes:UP000001955}; RN [1] {ECO:0000313|Proteomes:UP000001955} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29907 / DSM 4481 / JCM 1650 / NBRC 105725 / CDC 9005-74 RC {ECO:0000313|Proteomes:UP000001955}; RA Daniel R.; RT "The complete genome sequence of the B12 producing Escherichia blattae RT strain DSM4481 isolated from a cockroach."; RL Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001560; AFJ48629.1; -; Genomic_DNA. DR RefSeq; WP_002441609.1; NZ_BAHA01000013.1. DR EnsemblBacteria; AFJ48629; AFJ48629; EBL_c35740. DR KEGG; ebt:EBL_c35740; -. DR PATRIC; fig|630626.3.peg.3492; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000001955; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000001955}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000001955}. FT DOMAIN 198 365 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 426 AA; 47948 MW; CFC960C0A9CDCF5C CRC64; MFDRYEAGEQ AVLVHIYFTQ DKDLEDIQEF ESLVSSAGVD AMQVITGTRK APHPKYFVGE GKALEIADAV KATGASVVLF DHALSPAQER NLEQVCQCRV IDRTGLILDI FAQRARTHEG KLQVELAQLR HLATRLVRGW THLERQKGGI GLRGPGETQL ETDRRLLRGR ISQILSRLEK VEKQREQGRR SRTKADIPTI SLVGYTNAGK STLFNRITEA QVYAADRLFA TLDPTLRRID VADVGEAVLA DTVGFIRQLP HDLVAAFKAT LQETRQATLL LHVIDAADVR VQENIEAVDE VLEEIDAHEI PTLLVMNKID ALDGFTPRID RDEENVPVRV WLSAQTGEGI PLLFQALTER LAGELAQHTL CLPPQAGRLR SRFYQLQAIE KEWMEEDGSV GLQIRMPVVD WRRLCKQEPE LTDYIV // ID I2EVC5_EMTOG Unreviewed; 416 AA. AC I2EVC5; DT 11-JUL-2012, integrated into UniProtKB/TrEMBL. DT 11-JUL-2012, sequence version 1. DT 07-JUN-2017, entry version 34. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Emtol_2492 {ECO:0000313|EMBL:AFK03628.1}; OS Emticicia oligotrophica (strain DSM 17448 / GPTSA100-15). OC Bacteria; Bacteroidetes; Cytophagia; Cytophagales; Cytophagaceae; OC Emticicia. OX NCBI_TaxID=929562 {ECO:0000313|EMBL:AFK03628.1, ECO:0000313|Proteomes:UP000002875}; RN [1] {ECO:0000313|EMBL:AFK03628.1, ECO:0000313|Proteomes:UP000002875} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 17448 / GPTSA100-15 {ECO:0000313|Proteomes:UP000002875}; RG US DOE Joint Genome Institute (JGI-PGF); RA Lucas S., Han J., Lapidus A., Bruce D., Goodwin L., Pitluck S., RA Peters L., Kyrpides N., Mavromatis K., Ivanova N., Ovchinnikova G., RA Teshima H., Detter J.C., Tapia R., Han C., Land M., Hauser L., RA Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Tindall B., RA Pomrenke H., Brambilla E., Klenk H.-P., Eisen J.A.; RT "The complete genome of chromosome of Emticicia oligotrophica DSM RT 17448."; RL Submitted (JUL-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002961; AFK03628.1; -; Genomic_DNA. DR EnsemblBacteria; AFK03628; AFK03628; Emtol_2492. DR KEGG; eol:Emtol_2492; -. DR PATRIC; fig|929562.3.peg.2198; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000002875; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000002875}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000002875}. FT DOMAIN 205 393 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 166 193 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 416 AA; 48141 MW; 0B02DAD40C3E900D CRC64; MLKSPIFSTA KQQESAILVG LITQKQNAEQ TKEYLDELEF LATTAGVITK RVFTQRLERP DSRTFVGKGK LEEIKVWLIE NPVDSIIFDD DLTAPQVRNL EMMFQDIKIL DRSLLILNIF SQRAQTDQAK RQVELAQYQY LLPRLTRMWT HLSRQKGGIG MRGPGEKELE TDKRIVKDRI AFLKDKLEKI DKQSFTRRKE RSRLVRVALV GYTNVGKSTL MRRLAKTEVF AENKLFATID STVRKVVLGN IPFLLTDTVG FIRKLPTQLI ESFKSTLDEI READILIHVV DISHPSFEEQ IEVVNVTLAE IGASEKSMIL VFNKLDLFKP ESEDNLDEHL TTIDENLLQK NLDRLKNSYL KKNTENVVFI SAEHKENLAD LRDVLIQKIQ EKHFLIYPNW DPTQNPLYDW QGVVQE // ID I2F3N3_9BACT Unreviewed; 400 AA. AC I2F3N3; DT 11-JUL-2012, integrated into UniProtKB/TrEMBL. DT 11-JUL-2012, sequence version 1. DT 07-JUN-2017, entry version 39. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE Flags: Precursor; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=Theba_0822 {ECO:0000313|EMBL:AFK06536.1}; OS Mesotoga prima MesG1.Ag.4.2. OC Bacteria; Thermotogae; Kosmotogales; Kosmotogaceae; Mesotoga. OX NCBI_TaxID=660470 {ECO:0000313|EMBL:AFK06536.1, ECO:0000313|Proteomes:UP000002881}; RN [1] {ECO:0000313|EMBL:AFK06536.1, ECO:0000313|Proteomes:UP000002881} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MesG1.Ag.4.2 {ECO:0000313|EMBL:AFK06536.1}; RX PubMed=22798451; RA Zhaxybayeva O., Swithers K.S., Foght J., Green A.G., Bruce D., RA Detter C., Han S., Teshima H., Han J., Woyke T., Pitluck S., Nolan M., RA Ivanova N., Pati A., Land M.L., Dlutek M., Doolittle W.F., Noll K.M., RA Nesbo C.L.; RT "Genome Sequence of the Mesophilic Thermotogales Bacterium Mesotoga RT prima MesG1.Ag.4.2 Reveals the Largest Thermotogales Genome To Date."; RL Genome Biol. Evol. 4:700-708(2012). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP003532; AFK06536.1; -; Genomic_DNA. DR RefSeq; WP_014730581.1; NC_017934.1. DR ProteinModelPortal; I2F3N3; -. DR STRING; 660470.ThebaDRAFT_0030; -. DR EnsemblBacteria; AFK06536; AFK06536; Theba_0822. DR KEGG; mpg:Theba_0822; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR KO; K03665; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000002881; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000002881}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000002881}. FT DOMAIN 177 342 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 136 170 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 400 AA; 45388 MW; E6BF9A88EB356FF0 CRC64; MKTEILGELQ ELARTAGYYV TESVVQNLDY PDPRHYLGKG KVDFAKRMIE AFGVSLAITR HELSPSQAMN LERLLGIHVI DRTQLILEIF AEHATTKEGK LEVELASLKY QLPRLKGFGR MLSQTGAGIG TRGPGEKKLE IDRRQAQDRI SRLRKEIEEL AKRREISRKK RQSSSVPLVS FVGYTNVGKS SLVSEISSED LIIEDKLFAT LDTRVRKAKL PAGMQLLVSD TVGFIRELPH ELMESFKSTL DEVKYSDILV VVSDASDMAI KDKYSVVDRT LREIGAGEIR RIHVLNKIDL CTNERLAELE GSFPDSVMVS ALRSYNIEGI LNEITRKLFG EKSRRTLRLT PAEFSNFMRF RNSVEVLSES FDRELIEIVY LSSDEINERL ISSICEEGRK // ID I2GCP0_9BACT Unreviewed; 416 AA. AC I2GCP0; DT 11-JUL-2012, integrated into UniProtKB/TrEMBL. DT 11-JUL-2012, sequence version 1. DT 07-JUN-2017, entry version 30. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=BN8_00606 {ECO:0000313|EMBL:CCH51664.1}; OS Fibrisoma limi BUZ 3. OC Bacteria; Bacteroidetes; Cytophagia; Cytophagales; Cytophagaceae; OC Fibrisoma. OX NCBI_TaxID=1185876 {ECO:0000313|EMBL:CCH51664.1, ECO:0000313|Proteomes:UP000009309}; RN [1] {ECO:0000313|EMBL:CCH51664.1, ECO:0000313|Proteomes:UP000009309} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BUZ 3T {ECO:0000313|Proteomes:UP000009309}; RA Filippini M., Qi W., Jaenicke S., Goesmann A., Smits T.H., RA Bagheri H.C.; RT "Genome Sequence of the Filamentous Bacterium Fibrisoma limi BUZ 3T."; RL J. Bacteriol. 194:4445-4445(2012). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:CCH51664.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CAIT01000004; CCH51664.1; -; Genomic_DNA. DR RefSeq; WP_009280250.1; NZ_CAIT01000004.1. DR EnsemblBacteria; CCH51664; CCH51664; BN8_00606. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000009309; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 2. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 2. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000009309}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000009309}. FT DOMAIN 200 392 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 168 198 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 416 AA; 47405 MW; FDBA57F4D2E734F9 CRC64; MIDTHKNPET AVLVALVTQK QTADQTKEYL DELAFLAETS GIRTVKTFVQ KLERPDTRTF VGKGKLEEIQ TYITDNPVDT IIFDDDLTPA QVRNLEGEFK EIKVLDRSLL ILNIFSMRAQ TAQARVQVEL AQYQYLYPRL TRMWTHLSRQ KGGVGMRGPG ESELETDRRI VKDRIAFLKE KLEKIDKQSQ TRRKERDRLA RVALVGYTNV GKSTLMRTLA KAEVFAENKL FATVDSTVRK VVLGNIPFLL TDTVGFIRKL PTTLIESFKS TLDEVREADI LLHVVDVSHP SFEEHIEVVS STLSDIGAAD KPTILVFNKI DQFEPKEDSA YELVQEQEGE VPVAVRKQTA LQYLKKTYLT QKAEHVVFIS AQNRENIDEL RDLIYNLVKE KHFTIYPNWV NVPLSESAEY GDGLAG // ID I2JJ01_9GAMM Unreviewed; 438 AA. AC I2JJ01; DT 11-JUL-2012, integrated into UniProtKB/TrEMBL. DT 11-JUL-2012, sequence version 1. DT 30-AUG-2017, entry version 34. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=DOK_11444 {ECO:0000313|EMBL:EIF42953.1}; OS gamma proteobacterium BDW918. OC Bacteria; Proteobacteria; Gammaproteobacteria; Cellvibrionales; OC Spongiibacteraceae. OX NCBI_TaxID=1168065 {ECO:0000313|EMBL:EIF42953.1, ECO:0000313|Proteomes:UP000003473}; RN [1] {ECO:0000313|EMBL:EIF42953.1, ECO:0000313|Proteomes:UP000003473} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BDW918 {ECO:0000313|EMBL:EIF42953.1, RC ECO:0000313|Proteomes:UP000003473}; RX PubMed=22740675; DOI=10.1128/JB.00678-12; RA Kim S.M., Cho S.J., Lee S.B.; RT "Genome Sequence of the Unclassified Marine Gammaproteobacterium RT BDW918."; RL J. Bacteriol. 194:3753-3754(2012). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EIF42953.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AJMK01000043; EIF42953.1; -; Genomic_DNA. DR RefSeq; WP_008250583.1; NZ_JH650806.1. DR EnsemblBacteria; EIF42953; EIF42953; DOK_11444. DR PATRIC; fig|1168065.3.peg.2397; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000003473; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000003473}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000003473}. FT DOMAIN 199 365 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 165 192 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 438 AA; 49281 MW; 6CD13E175662D5E7 CRC64; MLFERPNSGE RAILVHLDFH SEDEREDSNE FVQLVTSAGG DPVAFITGSR KRPDARLFVG TGKLEEIREA LIANEGELVL FNHSLSPSQE RNIERELQCR VLDRTGLILD IFAQRAHTHE GKLQVELAQL QHMSTRLVRG WTHLERQKGG IGLRGPGESQ LETDRRLLRA RITAIQSRLQ KVRRQREQAR RARRRAEIPA LSLVGYTNAG KSTLFNVLTT SSVYAADQLF ATLDPTVRRI TVDDVGPVIL ADTVGFIRHL PHKLVEAFRA TLEEAVIADL LIHVVDCADP ERQDNMKQVM NVLAEIGAAD IPILEVYNKT DLIGSEPRIE RDEAGQPVRV WLSARDDRGL DLFYQALSEL LGNEICETSI TLTAAQGRLR ARLFSFDAVL DEEMNDDGSQ RLKVRLPEAD WQRLLAGESI TEASLDSSRP VSMREEFC // ID I2N7H4_9ACTN Unreviewed; 496 AA. AC I2N7H4; DT 11-JUL-2012, integrated into UniProtKB/TrEMBL. DT 11-JUL-2012, sequence version 1. DT 07-JUN-2017, entry version 34. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=STSU_07968 {ECO:0000313|EMBL:EIF92971.1}; OS Streptomyces tsukubensis NRRL18488. OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae; OC Streptomyces. OX NCBI_TaxID=1114943 {ECO:0000313|EMBL:EIF92971.1, ECO:0000313|Proteomes:UP000005940}; RN [1] {ECO:0000313|EMBL:EIF92971.1, ECO:0000313|Proteomes:UP000005940} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NRRL18488 {ECO:0000313|EMBL:EIF92971.1, RC ECO:0000313|Proteomes:UP000005940}; RX PubMed=22740677; DOI=10.1128/JB.00692-12; RA Barreiro C., Prieto C., Sola-Landa A., Solera E., Martinez-Castro M., RA Perez-Redondo R., Garcia-Estrada C., Aparicio J.F., RA Fernandez-Martinez L.T., Santos-Aberturas J., Salehi-Najafabadi Z., RA Rodriguez-Garcia A., Tauch A., Martin J.F.; RT "Draft Genome of Streptomyces tsukubaensis NRRL 18488, the Producer of RT the Clinically Important Immunosuppressant Tacrolimus (FK506)."; RL J. Bacteriol. 194:3756-3757(2012). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EIF92971.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AJSZ01000230; EIF92971.1; -; Genomic_DNA. DR RefSeq; WP_006346161.1; NZ_AJSZ01000230.1. DR EnsemblBacteria; EIF92971; EIF92971; STSU_07968. DR PATRIC; fig|1114943.5.peg.1619; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000005940; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 2. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000005940}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000005940}. FT DOMAIN 275 440 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 496 AA; 53877 MW; F6E75B718C6CF0CD CRC64; MTSSSSPSQD QRNSAQTRTE SLRADALMEE DVAWSHGIDG ERDGEQFDRS DRAALRRVAG LSTELEDVTE VEYRQLRLER VVLVGVWTSG TVRDAENSLA ELAALAETAG ALVLDGVIQR RDKPDPATYI GSGKALELRD IVLESGADTV VCDGELSPGQ LIHLEDVVKV KVVDRTALIL DIFAQHAKSR EGKAQVALAQ MQYMLPRLRG WGQSLSRQMG GGGGGGMATR GPGETKIETD RRRIREKMAK MRREIAEMKT GREIKRQERR RNKVPSVAIA GYTNAGKSSL LNRLTGAGVL VENALFATLD PTVRRAETPG GRLYTLADTV GFVRHLPHHL VEAFRSTMEE VADADLILHV VDGSHPVPEE QLAAVREVIR DVGAVGIPEI VVINKADAAD PVVLQRLLRI ERRAIAVSAR SGAGIEELLG LIDLELPRPE VQVEALVPYT EGGLVSRVHA DGEILSEEHT SEGTLLKARV HEELASALAP YALVGS // ID I3BVZ8_THINJ Unreviewed; 426 AA. AC I3BVZ8; DT 11-JUL-2012, integrated into UniProtKB/TrEMBL. DT 11-JUL-2012, sequence version 1. DT 07-JUN-2017, entry version 33. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=Thini_3015 {ECO:0000313|EMBL:EIJ35541.1}; OS Thiothrix nivea (strain ATCC 35100 / DSM 5205 / JP2). OC Bacteria; Proteobacteria; Gammaproteobacteria; Thiotrichales; OC Thiotrichaceae; Thiothrix. OX NCBI_TaxID=870187 {ECO:0000313|EMBL:EIJ35541.1, ECO:0000313|Proteomes:UP000005317}; RN [1] {ECO:0000313|Proteomes:UP000005317} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 35100 / DSM 5205 / JP2 RC {ECO:0000313|Proteomes:UP000005317}; RX PubMed=22675589; DOI=10.4056/sigs.2344929; RA Lapidus A., Nolan M., Lucas S., Glavina Del Rio T., Tice H., RA Cheng J.F., Tapia R., Han C., Goodwin L., Pitluck S., Liolios K., RA Pagani I., Ivanova N., Huntemann M., Mavromatis K., Mikhailova N., RA Pati A., Chen A., Palaniappan K., Land M., Brambilla E.M., Rohde M., RA Abt B., Verbarg S., Goker M., Bristow J., Eisen J.A., Markowitz V., RA Hugenholtz P., Kyrpides N.C., Klenk H.P., Woyke T.; RT "Genome sequence of the filamentous, gliding Thiothrix nivea neotype RT strain (JP2(T))."; RL Stand. Genomic Sci. 5:398-406(2011). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JH651384; EIJ35541.1; -; Genomic_DNA. DR RefSeq; WP_002709441.1; NZ_JH651384.1. DR EnsemblBacteria; EIJ35541; EIJ35541; Thini_3015. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000005317; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000005317}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000005317}. FT DOMAIN 200 366 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 166 193 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 426 AA; 47955 MW; 13AF68B3A3ECF0B4 CRC64; MELFERPGGG ERAVLVQISF NAAKSPQDEK EFVELAYSAG AQLVGFVAGS RQSPDPRYFI GEGKAEEIRL LLNAKDANLA IFDHSLSPAQ ERNLEKRLQC RVLDRTGLIL DIFAQRARSH EGKLQVELAQ LKHLSTRLVR GWTHLERQKG GIGLRGPGET QLETDRRLIG ERIKQINKRL EKVQNQREQG RQARKKAEIP TVSLVGYTNA GKSTLFNALT EAEVYAADQL FATLDPTLRK VQLPNQQETI LADTVGFIRH LPHDLVAAFR STLQETIDAD LLLHVIDSHD EQLELYREQV NKVIAEIGAE NVPQIEVMNK IDLGGQTPHV EEGNGITPTR IYVSAQKQSG LDILLEYLGN YFAGQMFRGE LNIPPLHARL RARLYADKAI QQESITDEGN FRLKVAIDQR RLNQYLHEEG LLLTDL // ID I3C4A7_9FLAO Unreviewed; 404 AA. AC I3C4A7; DT 11-JUL-2012, integrated into UniProtKB/TrEMBL. DT 11-JUL-2012, sequence version 1. DT 07-JUN-2017, entry version 33. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=JoomaDRAFT_1435 {ECO:0000313|EMBL:EIJ38450.1}; OS Joostella marina DSM 19592. OC Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales; OC Flavobacteriaceae; Joostella. OX NCBI_TaxID=926559 {ECO:0000313|EMBL:EIJ38450.1, ECO:0000313|Proteomes:UP000004690}; RN [1] {ECO:0000313|EMBL:EIJ38450.1, ECO:0000313|Proteomes:UP000004690} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 19592 {ECO:0000313|EMBL:EIJ38450.1, RC ECO:0000313|Proteomes:UP000004690}; RG US DOE Joint Genome Institute (JGI-PGF); RA Lucas S., Copeland A., Lapidus A., Bruce D., Goodwin L., Pitluck S., RA Peters L., Chertkov O., Ovchinnikova G., Kyrpides N., Mavromatis K., RA Detter J.C., Han C., Land M., Hauser L., Markowitz V., Cheng J.-F., RA Hugenholtz P., Woyke T., Wu D., Tindall B., Brambilla E., Klenk H.-P., RA Eisen J.A.; RT "Improved High-Quality Draft genome of Joostella marina DSM 19592."; RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JH651379; EIJ38450.1; -; Genomic_DNA. DR RefSeq; WP_008611642.1; NZ_JH651379.1. DR ProteinModelPortal; I3C4A7; -. DR EnsemblBacteria; EIJ38450; EIJ38450; JoomaDRAFT_1435. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000004690; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000004690}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000004690}. FT DOMAIN 200 386 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 168 195 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 404 AA; 46717 MW; 320ECF9FCBFBC1D1 CRC64; MLEKKTIDYE KVVLIGIINQ EQDEEKSREY LDELEFLAYT AGGEVATRFT QKVDIPNPKT FIGTGKMEQI REYVSENDIG TVIFDDELTP AQQKNIEKIL KAKILDRTSL ILDIFAQRAQ TSYARTQVEL AQYQYLLPRL TGLWTHLERQ RGGIGMRGPG ETEIETDRRI VRDRIALLKK KLEKIDKQME TQRGNRGALV RVALIGYTNV GKSTLMNVIS KSDVFAENKL FATLDTTVRK VVIGNLPFLL SDTVGFIRKL PTQLVESFKS TLDEVREADL LLHVVDISHP NFEEHIASVN QILDEIKSAD KPTIMVFNKI DNYEHETIDE DDLVTEKTTK HFTLKEWEQT WMSRLDSKDV LFISALNKEN LEEFRKKVYD SVREIHVTRF PYNSFLYPEY EEGL // ID I3CDS0_9GAMM Unreviewed; 434 AA. AC I3CDS0; DT 11-JUL-2012, integrated into UniProtKB/TrEMBL. DT 11-JUL-2012, sequence version 1. DT 07-JUN-2017, entry version 32. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=BegalDRAFT_0853 {ECO:0000313|EMBL:EIJ41763.1}; OS Beggiatoa alba B18LD. OC Bacteria; Proteobacteria; Gammaproteobacteria; Thiotrichales; OC Thiotrichaceae; Beggiatoa. OX NCBI_TaxID=395493 {ECO:0000313|EMBL:EIJ41763.1, ECO:0000313|Proteomes:UP000005744}; RN [1] {ECO:0000313|EMBL:EIJ41763.1, ECO:0000313|Proteomes:UP000005744} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=B18LD {ECO:0000313|EMBL:EIJ41763.1, RC ECO:0000313|Proteomes:UP000005744}; RG US DOE Joint Genome Institute; RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S., RA Peters L., Mikhailova N., Held B., Detter J.C., Han C., Tapia R., RA Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Samuel K., RA Teske A., Mueller J., Woyke T.; RT "Improved High-Quality Draft sequence of Beggiatoa alba B18lD."; RL Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JH600070; EIJ41763.1; -; Genomic_DNA. DR RefSeq; WP_002683999.1; NZ_JH600070.1. DR EnsemblBacteria; EIJ41763; EIJ41763; BegalDRAFT_0853. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000005744; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000005744}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000005744}. FT DOMAIN 198 365 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 434 AA; 48845 MW; 92E3B4B434AC8A73 CRC64; MFERPRTGER ALLVHITIHQ FTEQASLEEF TELVRSAGAL PILSITGTRP MPDPALFVGS GKLQEILDAI QSNDIEIVLF NHTLSPVQER NLERELKCRV LDRTGVILDI FAQRARSFEG KLQVELAQLQ HLSTRLIRGW THLERQKGGI GLRGPGETQL ELDRRLIAGR IKNINKRLEK VSQQREISRR ARQRAEIPVV SLVGYTNAGK STLFNRLTNA EVYAADQLFA TLDATLRRID LPDKTPLILA DTVGFIQQLP HDLVAAFRAT LDETRLANIL LHVVDASDPE RQNRINQVNQ VLTEIEAQQV SQILIYNKVD KLGDEQPHIE RDETGRICKI WLSAVTGAGI DLLHLALSEQ LHETSIQQWV QVSANNGQLR ARLYQLSTVL AEEYSENGDS LLKIQLLPKN LTQLLESEKD LQIVEKLAGL PKAS // ID I3D7R4_9PAST Unreviewed; 457 AA. AC I3D7R4; DT 11-JUL-2012, integrated into UniProtKB/TrEMBL. DT 11-JUL-2012, sequence version 1. DT 30-AUG-2017, entry version 32. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:EIJ67757.1}; GN ORFNames=HMPREF1052_0475 {ECO:0000313|EMBL:EIJ67757.1}; OS Pasteurella bettyae CCUG 2042. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Pasteurella. OX NCBI_TaxID=1095749 {ECO:0000313|EMBL:EIJ67757.1, ECO:0000313|Proteomes:UP000006457}; RN [1] {ECO:0000313|EMBL:EIJ67757.1, ECO:0000313|Proteomes:UP000006457} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CCUG 2042 {ECO:0000313|EMBL:EIJ67757.1, RC ECO:0000313|Proteomes:UP000006457}; RA Harkins D.M., Madupu R., Durkin A.S., Torralba M., Methe B., RA Sutton G.G., Nelson K.E.; RL Submitted (MAR-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EIJ67757.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AJSX01000041; EIJ67757.1; -; Genomic_DNA. DR RefSeq; WP_005761502.1; NZ_AJSX01000041.1. DR EnsemblBacteria; EIJ67757; EIJ67757; HMPREF1052_0475. DR PATRIC; fig|1095749.3.peg.1776; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000006457; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000006457}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000006457}. FT DOMAIN 217 384 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 183 210 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 457 AA; 51203 MW; 387DCBC9D3F921FE CRC64; MDKEIYIHQS AVNSTALSSG TKLSAQSDNA IVVHVFFSQD KNLEDLEEFQ QLTSSANVHI LKTITTARST PQAKYFVGLG KAEEIADAVK SYGANVVLVN HILTPAQTRN LEMLCNCRVV DRTGVILDIF AQRARSHEGK LQVELAQLKH LATRLIRRKT GLDQQKGAVG LRGPGETQLE TDRRLIKVRI AQLQSRLTKV EKQRNQNRQT RQKADIPTVS LVGYTNAGKS TLFNQITQAG VYAADQLFAT LDPTLRRLQI QDVGTTILAD TVGFIRDLPH DLISAFKSTL QETTEASLLL HVIDSADARK LENITAVNQV LEEIKANQVP TLLVYNKIDN LENVTPHIVY DENQIPVAVY LSAFTGDGID LLINAIRQRL TDEILYLNLT LQPQEGKIRH QLYQLNCIRD EKISDKGEFL LEIQVDKVEW LKLVKTFAHL NQFTPQGILD EMNIGKL // ID I3DBU8_HAEPH Unreviewed; 360 AA. AC I3DBU8; DT 11-JUL-2012, integrated into UniProtKB/TrEMBL. DT 11-JUL-2012, sequence version 1. DT 07-JUN-2017, entry version 33. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:EIJ69191.1}; GN ORFNames=HMPREF1050_0955 {ECO:0000313|EMBL:EIJ69191.1}; OS Haemophilus parahaemolyticus HK385. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=1095744 {ECO:0000313|EMBL:EIJ69191.1, ECO:0000313|Proteomes:UP000003016}; RN [1] {ECO:0000313|EMBL:EIJ69191.1, ECO:0000313|Proteomes:UP000003016} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=HK385 {ECO:0000313|EMBL:EIJ69191.1, RC ECO:0000313|Proteomes:UP000003016}; RA Harkins D.M., Madupu R., Durkin A.S., Torralba M., Methe B., RA Sutton G.G., Nelson K.E.; RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EIJ69191.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AJSW01000043; EIJ69191.1; -; Genomic_DNA. DR EnsemblBacteria; EIJ69191; EIJ69191; HMPREF1050_0955. DR PATRIC; fig|1095744.4.peg.1437; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000003016; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000003016}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}. FT DOMAIN 127 294 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 93 120 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 360 AA; 40496 MW; 260428F7B51F1B6A CRC64; MGATLVLVNH ELSPSQTRNL QSLCNCRVVD RTGLILDIFA QRARSHEGKL QVELAQLKHL ASRLVRRLGN QDQQKGGAVG LRGPGETQLE TDRRLIKVRI QQLQNRLAKV SKQREQNRKT RQKADIPTIS LVGYTNAGKS SLFNAITQAD VYAADQLFAT LDPTLRRMQI QDVGTTILAD TVGFIRFLPH DLVSAFKSTL QETVEASLLL HVIDVADERK NENIQAVNQV LEEIGAADIP TLLVYNKVDK LDGIQPFVER DDESKVTAVY LSAQSGEGID LLFEAIHEQL RNELVKETLL LSPTAGNLYT LFKQQKGIKA EHFNEFGDRI INIEIDKVQW NKWAKQYPEL IECIELAKWG // ID I3DZK2_BACMT Unreviewed; 419 AA. AC I3DZK2; DT 11-JUL-2012, integrated into UniProtKB/TrEMBL. DT 11-JUL-2012, sequence version 1. DT 07-JUN-2017, entry version 35. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:AIE59742.1}; GN ORFNames=BMMGA3_06570 {ECO:0000313|EMBL:AIE59742.1}; OS Bacillus methanolicus MGA3. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus. OX NCBI_TaxID=796606 {ECO:0000313|EMBL:AIE59742.1, ECO:0000313|Proteomes:UP000027602}; RN [1] {ECO:0000313|EMBL:AIE59742.1, ECO:0000313|Proteomes:UP000027602} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MGA3 {ECO:0000313|EMBL:AIE59742.1, RC ECO:0000313|Proteomes:UP000027602}; RX PubMed=25758049; RA Irla M., Neshat A., Brautaset T., Ruckert C., Kalinowski J., RA Wendisch V.F.; RT "Transcriptome analysis of thermophilic methylotrophic Bacillus RT methanolicus MGA3 using RNA-sequencing provides detailed insights into RT its previously uncharted transcriptional landscape."; RL BMC Genomics 16:73-73(2015). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP007739; AIE59742.1; -; Genomic_DNA. DR RefSeq; WP_003349188.1; NZ_CP007739.1. DR PRIDE; I3DZK2; -. DR EnsemblBacteria; AIE59742; AIE59742; BMMGA3_06570. DR KEGG; bmet:BMMGA3_06570; -. DR KO; K03665; -. DR Proteomes; UP000027602; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000027602}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000027602}. FT DOMAIN 200 362 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 419 AA; 47949 MW; FE6C5930D2A29D19 CRC64; MEQHTDLEKA ILVGCQTSEE DDVRFQYSME ELAALTKTAK GNVLVSVVQK RERIHPSTYI GKGKVDELKA LVEELEADVV IVNDELSPSQ IRNLSRHLNV RIIDRTQLIL DIFAQRARSK EGKLQVELAQ LQYLLPRLSG KGTELSRLGG GIGTRGPGET KLESDRRHIR RRIDDIKTQL KGIVQHRERY RERRKKNRAF QIALVGYTNA GKSTLFNRLT EADSYEENQL FATLDPMTRK LILPSGFTVL VTDTVGFIQE LPTTLIAAFR STLEEVKEAD LLLHVVDMSN PDYFQHEKTV NELLEDLEIH QIPQITVYNK KDIQHPDFVP TAKTETVIIS AFNKEDRDML KKKIEEAMIG MMNYYHVILP STEGKLLSQL KNETILRELS FDEEKQSYIC KGYAFKDHQI SGILKENSV // ID I3I5P7_9GAMM Unreviewed; 442 AA. AC I3I5P7; DT 11-JUL-2012, integrated into UniProtKB/TrEMBL. DT 11-JUL-2012, sequence version 1. DT 30-AUG-2017, entry version 33. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=O59_003780 {ECO:0000313|EMBL:EIK43382.1}; OS Cellvibrio sp. BR. OC Bacteria; Proteobacteria; Gammaproteobacteria; Cellvibrionales; OC Cellvibrionaceae; Cellvibrio. OX NCBI_TaxID=1134474 {ECO:0000313|EMBL:EIK43382.1, ECO:0000313|Proteomes:UP000003395}; RN [1] {ECO:0000313|EMBL:EIK43382.1, ECO:0000313|Proteomes:UP000003395} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BR {ECO:0000313|EMBL:EIK43382.1, RC ECO:0000313|Proteomes:UP000003395}; RA Peng Y.Y., Li N.Z., Xia T., Qiu R.R.; RL Submitted (MAY-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EIK43382.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AICM01000009; EIK43382.1; -; Genomic_DNA. DR RefSeq; WP_007645039.1; NZ_JH668205.1. DR EnsemblBacteria; EIK43382; EIK43382; O59_003780. DR PATRIC; fig|1134474.3.peg.3602; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000003395; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000003395}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000003395}. FT DOMAIN 199 366 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 442 AA; 49004 MW; 84772518FCFD6597 CRC64; MFFDRPESGE LAVLVHLNLS HGQDAEDPRE FEELVLSAGG DPVAFLTGSR IVPTAKFLIS TGKLQELQQL VVDNGAELVI FNHTLTPSQE RNLERELQCR VLDRTGLILD IFAQRARTFE GKLQVELAQL RHSATRLIRG WTHLERQKGG IGLRGPGETQ LETDRRLLRN RIGQIEQRLE KVRSQREQGR RSRQRAAIPT VSLVGYTNAG KSTLFNRITG ADVYAENKLF ATLDPTMRRI ELSDVGAVVL ADTVGFISHL PHRLVEAFKA TLEEASNSTL LLHVIDSAAE ERLRNIEQVE LVLEEIEAAD LPQLRVYNKV DLLADTGPHI DRDETGKPIA VWLSAQTGAG CELLNQAISE VLGKELVSGC LVVPPTQGRL RAMLYAQQAV VSENHRADGA SLLQVRIPKD DLLRILSAAN IAFESLLWDE SGTLPDMPVA QE // ID I3II02_9BACT Unreviewed; 436 AA. AC I3II02; DT 11-JUL-2012, integrated into UniProtKB/TrEMBL. DT 11-JUL-2012, sequence version 1. DT 07-JUN-2017, entry version 32. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=KSU1_B0490 {ECO:0000313|EMBL:GAB61347.1}; OS Candidatus Jettenia caeni. OC Bacteria; Planctomycetes; Planctomycetia; Candidatus Brocadiales; OC Candidatus Brocadiaceae; Candidatus Jettenia. OX NCBI_TaxID=247490 {ECO:0000313|EMBL:GAB61347.1, ECO:0000313|Proteomes:UP000002985}; RN [1] {ECO:0000313|EMBL:GAB61347.1, ECO:0000313|Proteomes:UP000002985} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=22673575; DOI=10.1016/j.febslet.2012.04.041; RA Hira D., Toh H., Migita C.T., Okubo H., Nishiyama T., Hattori M., RA Furukawa K., Fujii T.; RT "Anammox organism KSU-1 expresses a NirK-type copper-containing RT nitrite reductase instead of a NirS-type with cytochrome cd1."; RL FEBS Lett. 586:1658-1663(2012). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:GAB61347.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BAFH01000002; GAB61347.1; -; Genomic_DNA. DR RefSeq; WP_007220469.1; NZ_BAFH01000002.1. DR EnsemblBacteria; GAB61347; GAB61347; KSU1_B0490. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000002985; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000002985}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000002985}. FT DOMAIN 200 366 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 436 AA; 49248 MW; 1A58BD3CACF4EE0E CRC64; MKLKETAFTV RAERAILFRA MLNRNRGEAP LEELQRLAET AGARVVYTAI QNRISIDPVY YLGKGKALEL ADAAKELDAD VLICDDDLTP AQVRNLEKVI GKKVIDRSEL ILDIFATRAK TFQAKLQVEL AQLEYTKPRL KRMWTHLSRI EGGIGTRGPG EKQLEVDKRI ISRKIQYLKK KLYEVEKRQE RLVSSRKEFF TISIVGYTNA GKSTLMNALT DVDTLVEDKL FATLDTKTGM CRLENGKKIL ISDTVGFIQK LPHHLISSFK ATLEEARHAD LLLHVVDISS PVVQEQIDAV NAVLKELGCD NKPVIMVFNK VDTITNESIV PLLRNRYGDC VMISAKTQRG IEDLKRRIEG ELEQNFVEIE LSCSPGNGKL IAYLHEHAHI INSQFHEQGV TFKLLVENRL IHKLRMMDSD IQIQGTSLSD GADTDI // ID I3JK50_ORENI Unreviewed; 525 AA. AC I3JK50; DT 11-JUL-2012, integrated into UniProtKB/TrEMBL. DT 11-JUL-2012, sequence version 1. DT 30-AUG-2017, entry version 34. DE SubName: Full=GTP binding protein 6 (putative) {ECO:0000313|Ensembl:ENSONIP00000009244}; GN Name=gtpbp6 {ECO:0000313|Ensembl:ENSONIP00000009244}; OS Oreochromis niloticus (Nile tilapia) (Tilapia nilotica). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata; OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids; OC Pseudocrenilabrinae; Oreochromini; Oreochromis. OX NCBI_TaxID=8128 {ECO:0000313|Ensembl:ENSONIP00000009244, ECO:0000313|Proteomes:UP000005207}; RN [1] {ECO:0000313|Ensembl:ENSONIP00000009244} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RG Broad Institute Genome Assembly Team; RG Broad Institute Sequencing Platform; RA Di Palma F., Johnson J., Lander E.S., Lindblad-Toh K.; RT "The Genome Sequence of Oreochromis niloticus (Nile Tilapia)."; RL Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Ensembl:ENSONIP00000009244} RP IDENTIFICATION. RG Ensembl; RL Submitted (MAY-2012) to UniProtKB. RN [3] {ECO:0000313|Proteomes:UP000005207} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=25186727; DOI=10.1038/nature13726; RA Brawand D., Wagner C.E., Li Y.I., Malinsky M., Keller I., Fan S., RA Simakov O., Ng A.Y., Lim Z.W., Bezault E., Turner-Maier J., RA Johnson J., Alcazar R., Noh H.J., Russell P., Aken B., Alfoldi J., RA Amemiya C., Azzouzi N., Baroiller J.F., Barloy-Hubler F., Berlin A., RA Bloomquist R., Carleton K.L., Conte M.A., D'Cotta H., Eshel O., RA Gaffney L., Galibert F., Gante H.F., Gnerre S., Greuter L., Guyon R., RA Haddad N.S., Haerty W., Harris R.M., Hofmann H.A., Hourlier T., RA Hulata G., Jaffe D.B., Lara M., Lee A.P., MacCallum I., Mwaiko S., RA Nikaido M., Nishihara H., Ozouf-Costaz C., Penman D.J., Przybylski D., RA Rakotomanga M., Renn S.C., Ribeiro F.J., Ron M., Salzburger W., RA Sanchez-Pulido L., Santos M.E., Searle S., Sharpe T., Swofford R., RA Tan F.J., Williams L., Young S., Yin S., Okada N., Kocher T.D., RA Miska E.A., Lander E.S., Venkatesh B., Fernald R.D., Meyer A., RA Ponting C.P., Streelman J.T., Lindblad-Toh K., Seehausen O., RA Di Palma F.; RT "The genomic substrate for adaptive radiation in African cichlid RT fish."; RL Nature 513:375-381(2014). CC -!- CAUTION: The sequence shown here is derived from an Ensembl CC automatic analysis pipeline and should be considered as CC preliminary data. {ECO:0000313|Ensembl:ENSONIP00000009244}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AERX01028549; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR STRING; 8128.ENSONIP00000009244; -. DR Ensembl; ENSONIT00000009249; ENSONIP00000009244; ENSONIG00000007330. DR eggNOG; KOG0410; Eukaryota. DR eggNOG; COG2262; LUCA. DR GeneTree; ENSGT00390000001397; -. DR InParanoid; I3JK50; -. DR OMA; MDTVGFM; -. DR OrthoDB; EOG091G0852; -. DR TreeFam; TF315022; -. DR Proteomes; UP000005207; Unplaced. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR CDD; cd01878; HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000005207}; KW Reference proteome {ECO:0000313|Proteomes:UP000005207}. FT DOMAIN 300 464 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 525 AA; 58952 MW; 08CFCDAD63EB671A CRC64; MPVLQRSCTK SCQIGARATC RLLHTPHRTH AVNTCQQQRG ATILQTRAFG LSAFRLKSTD DLSSSNGFNE EGEDEDFLED SEVEELFQQQ IPAGIGEGQH RVFIIHPDVK WGSRKQHLTT AELMMAEAEG LVNTLENWTV VDKMILSTKT PEKKRIFGKG NFQTLTERIR QTAGITAVFV NVERLSPLSE REFEEVWGVK VFDRYSVVLH IFRCNARTKE AKLQISLAEI PLLRSRLKNE MANLDQQGGG SRYIGGSGET LYEIQQRLLK EREIKIRLAL EKLRKKRHLL RSQRKHREFP VVSVLGYTNC GKTTLIKALT GDTGLQPRNQ LFATLDVTVH AGQLPSHMTV LYVDTIGFLS QLPHQLIDSF SATLEDIKHS DLLIHVRDIS HPETANQKVN VLNVLKNLQI PDRLMNSMIE VHNKTDLITN YESAEPAALP ISALEGRGLE QLKEAVEEEI LKATGKQILD LTVNLSSPQL SWLYKEATVQ DVQVNADEGS AVVKVIIGTA AHGRYKKLFG SRVSS // ID I3TD63_THEC1 Unreviewed; 354 AA. AC I3TD63; DT 05-SEP-2012, integrated into UniProtKB/TrEMBL. DT 05-SEP-2012, sequence version 1. DT 05-JUL-2017, entry version 33. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=TCELL_0276 {ECO:0000313|EMBL:AFK50701.1}; OS Thermogladius cellulolyticus (strain 1633). OC Archaea; Crenarchaeota; Thermoprotei; Desulfurococcales; OC Desulfurococcaceae; Thermogladius. OX NCBI_TaxID=1184251 {ECO:0000313|EMBL:AFK50701.1, ECO:0000313|Proteomes:UP000005270}; RN [1] {ECO:0000313|EMBL:AFK50701.1, ECO:0000313|Proteomes:UP000005270} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=1633 {ECO:0000313|EMBL:AFK50701.1, RC ECO:0000313|Proteomes:UP000005270}; RX PubMed=22843584; DOI=10.1128/JB.00894-12; RA Mardanov A.V., Kochetkova T.V., Beletsky A.V., RA Bonch-Osmolovskaya E.A., Ravin N.V., Skryabin K.G.; RT "Complete genome sequence of the hyperthermophilic cellulolytic RT Crenarchaeon 'Thermogladius cellulolyticus' 1633."; RL J. Bacteriol. 194:4446-4447(2012). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP003531; AFK50701.1; -; Genomic_DNA. DR EnsemblBacteria; AFK50701; AFK50701; TCELL_0276. DR KEGG; thg:TCELL_0276; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG093Z07D6; -. DR Proteomes; UP000005270; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000005270}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000005270}. FT DOMAIN 182 354 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 354 AA; 39985 MW; 78BD8D1348239531 CRC64; MKTGKVAVFI PSKYRDFVDE ELSLVKTVYG VVDQVHFVKR PNPRTYIQQD KLKELAENPP DKLVVMDILR PSQVTNILRE VKTEVVDRVL LILEVFAQHA GSREALLQIE LARIKHMLPL VRDFIRKSKL GELAGYLGPG RYGYEKYYTF LRRREGRIRR EIEEIRRVRE VRRERRVREG VPHVAIAGYT CAGKTTLFNA LTGKNMPVGP EPFTTLSPKT AKLDIDGVHM VVTDTVGFIR DLPPEITEAF YATLEEVTAA DLIVLVVDSS KPLKRVISEV DSSLKIFNDI GVHGKPIIIA LNKIDLINVN GVEELVRELS KSAVNATRIV PISAEKRINL DALKREIVGV FKGT // ID I3TL99_TISMK Unreviewed; 455 AA. AC I3TL99; DT 05-SEP-2012, integrated into UniProtKB/TrEMBL. DT 05-SEP-2012, sequence version 1. DT 05-JUL-2017, entry version 36. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:AFK53537.1}; GN OrderedLocusNames=TMO_1698 {ECO:0000313|EMBL:AFK53537.1}; OS Tistrella mobilis (strain KA081020-065). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales; OC Rhodospirillaceae; Tistrella. OX NCBI_TaxID=1110502 {ECO:0000313|EMBL:AFK53537.1, ECO:0000313|Proteomes:UP000005258}; RN [1] {ECO:0000313|EMBL:AFK53537.1, ECO:0000313|Proteomes:UP000005258} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=KA081020-065 {ECO:0000313|EMBL:AFK53537.1, RC ECO:0000313|Proteomes:UP000005258}; RX PubMed=22458477; DOI=10.1021/ja301735a; RA Xu Y., Kersten R.D., Nam S.J., Lu L., Al-Suwailem A.M., Zheng H., RA Fenical W., Dorrestein P.C., Moore B.S., Qian P.Y.; RT "Bacterial biosynthesis and maturation of the didemnin anti-cancer RT agents."; RL J. Am. Chem. Soc. 134:8625-8632(2012). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP003236; AFK53537.1; -; Genomic_DNA. DR EnsemblBacteria; AFK53537; AFK53537; TMO_1698. DR KEGG; tmo:TMO_1698; -. DR PATRIC; fig|1110502.3.peg.1748; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000005258; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000005258}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000005258}. FT DOMAIN 222 393 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 455 AA; 50375 MW; C8DEC6A0D93EE058 CRC64; MSDDKIIIRP DGDLPARALV LQPDVKEQRR GAPAPVEDDP EAVRSMRARL DEGMALTGAL GLDVAEGLVV PVARMRPSTL LGSGKVDEIK AKLEAAPVDL VVMNRPLTPI QQRNLEKAWN VKVIDRIWLI LEIFADRART REGRLQVELA RLGYQRSRLV RSWTHLERQR GGRGFLAGPG ETQIETDRRI IDDKMARLKL QLAEVVRTRE LHRKKRREVP YPVVALVGYT NAGKSTLFNR VTGASVMAKD MLFATLDPTM RALDLPSGRR VILSDTVGFV SELPTGLIAA FRATLEEVRE AALIIHVRDI ADPDTGAQRR DVLHVLGELG MGHRLADDVL EFRNKLDMLE GEARERVLNE AARAEDAVAG SALSGEGLDR LFAAIDARLA IGDELAHFDV PHADGQALAW LYEHGEVAER ADDEAVAHVA VRLKPQDLSR FHARWPHLSA PVSPT // ID I3UCQ8_ADVKW Unreviewed; 362 AA. AC I3UCQ8; DT 05-SEP-2012, integrated into UniProtKB/TrEMBL. DT 05-SEP-2012, sequence version 1. DT 07-JUN-2017, entry version 35. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=TKWG_13420 {ECO:0000313|EMBL:AFK62796.1}; OS Advenella kashmirensis (strain DSM 17095 / LMG 22695 / WT001) OS (Tetrathiobacter kashmirensis). OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Alcaligenaceae. OX NCBI_TaxID=1036672 {ECO:0000313|EMBL:AFK62796.1, ECO:0000313|Proteomes:UP000005267}; RN [1] {ECO:0000313|EMBL:AFK62796.1, ECO:0000313|Proteomes:UP000005267} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 17095 / LMG 22695 / WT001 RC {ECO:0000313|Proteomes:UP000005267}; RX PubMed=21914874; DOI=10.1128/JB.05781-11; RA Ghosh W., George A., Agarwal A., Raj P., Alam M., Pyne P., RA Das Gupta S.K.; RT "Whole-genome shotgun sequencing of the sulfur-oxidizing RT chemoautotroph Tetrathiobacter kashmirensis."; RL J. Bacteriol. 193:5553-5554(2011). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP003555; AFK62796.1; -; Genomic_DNA. DR RefSeq; WP_014750887.1; NC_017964.1. DR EnsemblBacteria; AFK62796; AFK62796; TKWG_13420. DR KEGG; aka:TKWG_13420; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000005267; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000005267}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000005267}. FT DOMAIN 190 356 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 362 AA; 40182 MW; 8BE93DDFD504EC09 CRC64; MRVLIISVDS GDLDHPAHAE EFQMLAEGAG ADIAGTLTVK RDKPDAAYYI GKGKLEEAVA MAEAEDVELI LFDQPLSPAQ QRNLERAFER RVVDRVALIL DIFALRAKSH EGKLQVELAQ LQHLVTRLTR MWTHLERQRG GIGMRGPGES QLEMDRRMIG SKVKVLRERL ARVERQRKTQ RRSRVRSNTL SVSLVGYTNA GKSTLFNALT RADAYAADQL FATLDTTTRK IWIEGAGNVV ISDTVGFIRD LPTTLIAAFK ATLEETVHAD LLLHVVDAAS PQRDEQIAEV DKVLEEIGAN EIPCILIYNK IDQAGYEPQV ERNEKGEPAR IFVSALQRTG LDGLRGAIAE FRPSIGNEVA IL // ID I3VVY0_THESW Unreviewed; 412 AA. AC I3VVY0; DT 05-SEP-2012, integrated into UniProtKB/TrEMBL. DT 05-SEP-2012, sequence version 1. DT 07-JUN-2017, entry version 34. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Tsac_1669 {ECO:0000313|EMBL:AFK86675.1}; OS Thermoanaerobacterium saccharolyticum (strain DSM 8691 / JW/SL-YS485). OC Bacteria; Firmicutes; Clostridia; Thermoanaerobacterales; OC Thermoanaerobacterales Family III. Incertae Sedis; OC Thermoanaerobacterium. OX NCBI_TaxID=1094508 {ECO:0000313|EMBL:AFK86675.1, ECO:0000313|Proteomes:UP000006178}; RN [1] {ECO:0000313|Proteomes:UP000006178} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 8691 / JW/SL-YS485 {ECO:0000313|Proteomes:UP000006178}; RA Brown S.D., Land M.L., Herring C.D.; RT "Thermoanaerobacterium saccharolyticum JW/SL-YS485."; RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP003184; AFK86675.1; -; Genomic_DNA. DR EnsemblBacteria; AFK86675; AFK86675; Tsac_1669. DR KEGG; tsh:Tsac_1669; -. DR PATRIC; fig|1094508.3.peg.1691; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000006178; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000006178}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000006178}. FT DOMAIN 198 358 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 164 191 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 412 AA; 46630 MW; B6DB5617FDB591F7 CRC64; MDNKINDSKE KAVLVGVLID DDDRESIEEL EELANTAGAE VVGVMTQSRT NIDRTSYIGK GKLMELKEFI ENNDVDVIIV NDELTGIQIK NIEDVTNVKV IDRTGLILDI FAKRAKSAEG MLQVELAQLK YRLPRLQGIG NDLSRLGGGI GTRGPGETKL ETDRRHIKER IRAIEGKIDD LRRHRELLRE RRRKNEIPVV AIIGYTNAGK STLMNVLTNS SVYAEDKLFA TLDPTARKLV LPSGREIVLI DTVGFIRKLP HDLVEAFKST LEELKYADVL LHVIDISAKD VMHKIGVVES VLKDLDVIDK PKINVYNKSD LLDKIPENKG DNVYISAKER IGIDELLETI DRFTYSDLSV LDFYFAYANN DEYLFLKKNS KILKEEYDEK GIKIRAQVSA MEKNVLRDFI IS // ID I3WGU9_BIFBI Unreviewed; 523 AA. AC I3WGU9; DT 05-SEP-2012, integrated into UniProtKB/TrEMBL. DT 05-SEP-2012, sequence version 1. DT 07-JUN-2017, entry version 34. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:AFL04112.1}; GN ORFNames=BBB_0518 {ECO:0000313|EMBL:AFL04112.1}; OS Bifidobacterium bifidum BGN4. OC Bacteria; Actinobacteria; Bifidobacteriales; Bifidobacteriaceae; OC Bifidobacterium. OX NCBI_TaxID=484020 {ECO:0000313|EMBL:AFL04112.1, ECO:0000313|Proteomes:UP000006173}; RN [1] {ECO:0000313|EMBL:AFL04112.1, ECO:0000313|Proteomes:UP000006173} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BGN4 {ECO:0000313|EMBL:AFL04112.1}; RX PubMed=22887663; DOI=10.1128/JB.00988-12; RA Yu D.S., Jeong H., Lee D.H., Kwon S.K., Song J.Y., Kim B.K., RA Park M.S., Ji G.E., Oh T.K., Kim J.F.; RT "Complete Genome Sequence of the Probiotic Bacterium Bifidobacterium RT bifidum Strain BGN4."; RL J. Bacteriol. 194:4757-4758(2012). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001361; AFL04112.1; -; Genomic_DNA. DR EnsemblBacteria; AFL04112; AFL04112; BBB_0518. DR KEGG; bbf:BBB_0518; -. DR PATRIC; fig|484020.3.peg.515; -. DR KO; K03665; -. DR Proteomes; UP000006173; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000006173}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000006173}. FT DOMAIN 286 452 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 523 AA; 56869 MW; E4E40E577F9298EE CRC64; MPLSQQNTVD ANQAGQPGEQ EEPVLTGVLA DQSDVLLDEN GDGHVGQRDA EEWEERESRN QLKHVAGLGE LQDVTEVEYR KVRLERVVLV GVWSSMTTTA AQAEESLREL AALAETAGAV VCDGLLQHRY KPDSATYVGS GKARELADIV AVNEADTIIV DDDLPPSQRR ALEDATKVKV VDRTAVILDI FAQHATSREG KAQVELAQLE YMLPRLRGWG GSLSRQAGGR AAGADAGIGS RGPGETKIEM DRRVIRSRIA RLRRQIAQMA PAREVKRGSR RRYGLPTIAV VGYTNAGKSS LTNRLTGSAE LVENALFATL DTAVRRARAK DGRLYAYVDT VGFVRNLPTQ LIEAFKSTLE EVAEADIILH VVDGSHPDPF SQIDAVNDVL ADIEGGEEIP RVVVFNKIDR IDAATRERLA ALEPEASLVS AATGEGLDDL LRRIESMLPV PGVHVSALLP YDAGSLLSRV REYGNVDSVD YRADGIWIEA DVDRRLAAQI VDRAIDETDG DGSDHIDAEH DVD // ID I3Y661_THIV6 Unreviewed; 451 AA. AC I3Y661; DT 05-SEP-2012, integrated into UniProtKB/TrEMBL. DT 05-SEP-2012, sequence version 1. DT 07-JUN-2017, entry version 36. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Thivi_0410 {ECO:0000313|EMBL:AFL72479.1}; OS Thiocystis violascens (strain ATCC 17096 / DSM 198 / 6111) (Chromatium OS violascens). OC Bacteria; Proteobacteria; Gammaproteobacteria; Chromatiales; OC Chromatiaceae; Thiocystis. OX NCBI_TaxID=765911 {ECO:0000313|EMBL:AFL72479.1, ECO:0000313|Proteomes:UP000006062}; RN [1] {ECO:0000313|EMBL:AFL72479.1, ECO:0000313|Proteomes:UP000006062} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 17096 / DSM 198 / 6111 RC {ECO:0000313|Proteomes:UP000006062}; RG US DOE Joint Genome Institute; RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S., RA Peters L., Ovchinnikova G., Teshima H., Detter J.C., Han C., Tapia R., RA Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Vogl K., RA Liu Z., Frigaard N.-U., Bryant D., Woyke T.; RT "Complete sequence of Thiocystis violascens DSM 198."; RL Submitted (JUN-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP003154; AFL72479.1; -; Genomic_DNA. DR EnsemblBacteria; AFL72479; AFL72479; Thivi_0410. DR KEGG; tvi:Thivi_0410; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000006062; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000006062}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000006062}. FT DOMAIN 219 386 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 451 AA; 49299 MW; 485C1B572BE82298 CRC64; MKATTHVSAG HGTPAPSGGS LVFERPKLGE RAVLVHLDIG STVLPDEREE FALLATAAGA EVVGTLGGSR AVPDPRLFVG TGKAEELKSM VAALDADLAI FNHPLSPAQE RNLERLLQCR VVDRSGLILD IFAQRARSFE GKLQVELAQL KHLSTRLVRG WTHLERQKGG IGLRGPGETQ LETDRRLLSK RVDTLDRRLE RIEVQRAQGR KARARAELPV ISLVGYTNAG KSTLFNQLTA AGVFEADQLF ATLDPTLRRL ALPSGGRVLV ADTVGFVSHL PHELVAAFRS TLEEARNANL LLHVVDAAAI QRARQIDDVE HVLADIGCDE LPRLEVFNKI DLLDDALPRT ERDANGMPTR VWLSARTGAG IEALLMALGE LTGGSQTRKR FRLEPGDGKL RAWLFEHARV LSDQPVETGG WTIEFVVGSA QLDRLLATDD ALRRRLHALS R // ID I3YVH7_AEQSU Unreviewed; 404 AA. AC I3YVH7; DT 05-SEP-2012, integrated into UniProtKB/TrEMBL. DT 05-SEP-2012, sequence version 1. DT 07-JUN-2017, entry version 35. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Aeqsu_1506 {ECO:0000313|EMBL:AFL80995.1}; OS Aequorivita sublithincola (strain DSM 14238 / LMG 21431 / ACAM 643 / OS 9-3). OC Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales; OC Flavobacteriaceae; Aequorivita. OX NCBI_TaxID=746697 {ECO:0000313|EMBL:AFL80995.1, ECO:0000313|Proteomes:UP000006049}; RN [1] {ECO:0000313|EMBL:AFL80995.1, ECO:0000313|Proteomes:UP000006049} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 14238 / LMG 21431 / ACAM 643 / 9-3 RC {ECO:0000313|Proteomes:UP000006049}; RG US DOE Joint Genome Institute (JGI-PGF); RA Lucas S., Copeland A., Lapidus A., Goodwin L., Pitluck S., Peters L., RA Munk A.C.C., Kyrpides N., Mavromatis K., Pagani I., Ivanova N., RA Ovchinnikova G., Zeytun A., Detter J.C., Han C., Land M., Hauser L., RA Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Tindall B., RA Faehnrich R., Brambilla E., Klenk H.-P., Eisen J.A.; RT "The complete genome of Aequorivita sublithincola DSM 14238."; RL Submitted (JUN-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP003280; AFL80995.1; -; Genomic_DNA. DR RefSeq; WP_014782252.1; NC_018013.1. DR ProteinModelPortal; I3YVH7; -. DR EnsemblBacteria; AFL80995; AFL80995; Aeqsu_1506. DR KEGG; asl:Aeqsu_1506; -. DR PATRIC; fig|746697.3.peg.1529; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000006049; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000006049}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Hydrolase {ECO:0000313|EMBL:AFL80995.1}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000006049}. FT DOMAIN 200 385 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 404 AA; 46404 MW; 1F059AD28099359B CRC64; MIEKTDISYE KTVLIGLITQ YQDEVKAEEY LDELEFLAYT AGGEVLKRFV QKMEKPNPKT FIGTGKLQDV KNFVEENDVG VVIFDDELSP AQQKNIQKEL DCKVLDRTNL ILDIFAQRAQ TSNASTQVEL AQYQYLLPRL AGMWTHLERQ RGGIGMRGPG ETEIETDRRI VRDRIALLKD KLKKIDRQMG VQRGNRGALV RVALVGYTNV GKSTLMNVIS KSDVFAENKL FATLDTTVRK VVIGNLPFLL TDTVGFIRKL PTQLVESFKS TLDEVREADL LLHVVDISHP SFEHHIDSVD KILEEIGSAD KPTIMVFNKI DAYEAEEIEE DDLMTEKTKA HYTLEEWKQT WMAKLNGDAI FISALNKENF SEFRKLVYEK VKEIHTTRFP YNSFLYEDYV EEED // ID I3Z2T4_BELBD Unreviewed; 419 AA. AC I3Z2T4; DT 05-SEP-2012, integrated into UniProtKB/TrEMBL. DT 05-SEP-2012, sequence version 1. DT 07-JUN-2017, entry version 36. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Belba_0906 {ECO:0000313|EMBL:AFL83552.1}; OS Belliella baltica (strain DSM 15883 / CIP 108006 / LMG 21964 / BA134). OC Bacteria; Bacteroidetes; Cytophagia; Cytophagales; Cyclobacteriaceae; OC Belliella. OX NCBI_TaxID=866536 {ECO:0000313|EMBL:AFL83552.1, ECO:0000313|Proteomes:UP000006050}; RN [1] {ECO:0000313|Proteomes:UP000006050} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 15883 / CIP 108006 / LMG 21964 / BA134 RC {ECO:0000313|Proteomes:UP000006050}; RA Lucas S., Copeland A., Lapidus A., Goodwin L., Pitluck S., Peters L., RA Mikhailova N., Davenport K., Kyrpides N., Mavromatis K., Pagani I., RA Ivanova N., Ovchinnikova G., Zeytun A., Detter J.C., Han C., Land M., RA Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T., Wu D., RA Tindall B., Pomrenke H., Brambilla E., Klenk H.-P., Eisen J.A.; RT "The complete genome of Belliella baltica DSM 15883."; RL Submitted (JUN-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP003281; AFL83552.1; -; Genomic_DNA. DR RefSeq; WP_014771560.1; NC_018010.1. DR EnsemblBacteria; AFL83552; AFL83552; Belba_0906. DR KEGG; bbd:Belba_0906; -. DR PATRIC; fig|866536.3.peg.930; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000006050; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000006050}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000006050}. FT DOMAIN 210 399 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 419 AA; 48282 MW; F9FE36E01900EFB0 CRC64; MTKYSKKLQK LHETAPKVDT AVLVALIKQG QSDRQIHDFL DELAFLTETL GAKTVYRFTQ RLEKPDVKSF VGTGKLEEIR TYIEHFEVDM VIFDDDLSPS QMRNLENELK VKVYDRSLLI LDIFLKRAQT AQAKTQVELA RFQYLLPRLT NMWTHLERQR GGTTTRGGSG EKEIETDKRD IRGRITLLKE KLKEVEKQGI TQRKSRKGIV RVSLVGYTNV GKSTLMNLIT KTDILAENKL FATVDSTVRK VVLENIPFLL SDTVGFIRKL PTHLIESFKS TLDEIREADL LIHVVDISHP GFEDHIAVVN ETLNEIGARD KPMLLVFNKI DLVAQMPSEE EQMNMTEIEL EESNFLDFEK LSEAYKKKTG ISPVFMAAES GQNVEEFREV LVREVKKEHK KMYPHYLEDE KIDMTGFEE // ID I3ZCZ7_TERRK Unreviewed; 514 AA. AC I3ZCZ7; DT 05-SEP-2012, integrated into UniProtKB/TrEMBL. DT 05-SEP-2012, sequence version 1. DT 07-JUN-2017, entry version 34. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Terro_0783 {ECO:0000313|EMBL:AFL87115.1}; OS Terriglobus roseus (strain DSM 18391 / NRRL B-41598 / KBS 63). OC Bacteria; Acidobacteria; Acidobacteriales; Acidobacteriaceae; OC Terriglobus. OX NCBI_TaxID=926566 {ECO:0000313|EMBL:AFL87115.1, ECO:0000313|Proteomes:UP000006056}; RN [1] {ECO:0000313|EMBL:AFL87115.1, ECO:0000313|Proteomes:UP000006056} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 18391 / NRRL B-41598 / KBS 63 RC {ECO:0000313|Proteomes:UP000006056}; RG US DOE Joint Genome Institute (JGI-PGF); RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., RA Tice H., Bruce D., Goodwin L., Pitluck S., Peters L., Mikhailova N., RA Munk A.C.C., Kyrpides N., Mavromatis K., Ivanova N., Brettin T., RA Detter J.C., Han C., Larimer F., Land M., Hauser L., Markowitz V., RA Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Brambilla E., RA Klenk H.-P., Eisen J.A.; RT "Complete genome of Terriglobus roseus DSM 18391."; RL Submitted (JUN-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP003379; AFL87115.1; -; Genomic_DNA. DR RefSeq; WP_014784684.1; NC_018014.1. DR EnsemblBacteria; AFL87115; AFL87115; Terro_0783. DR KEGG; trs:Terro_0783; -. DR PATRIC; fig|926566.3.peg.775; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000006056; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000006056}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000006056}. FT DOMAIN 266 432 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 225 259 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 514 AA; 56234 MW; AEE85011B60E0B33 CRC64; MSTKQRTART GLSGQRPTAS RLEVAAAAAV TSSKDGYVTE KERELAVLVS VEITGERRRL TAAAAQARAA AAIHDGDDDA DEPEAVAELD FDAALEEFQE LARSAGAEVV ATVVQRRGKP DPAMLIGPGK VEELAAVVAS SGANLVLFDH DLTPSQLRNL DRELPVRVID RTQLILDIFA RHARTREGHL QVELAQLEYQ LPRLAGKGKA MSQLGGGIGT RGPGETKLET DRRRIRARID RLKEQLDTVR RNRRQQRQRR EAVPVPTVAL VGYTNAGKST LFNALTDAGV LESARMFATL DPKLRHLALP SRRKVLLSDT VGFIRNLPHA LVTSFRATLE EVERAELLLH VRDAASPNID EQKMQVERVL AELDVSKTPT LQVLNKTDLL PADKLAELKD FPEANTIAVS AHTGDGLQAL IAAIEERIGG AGAVDPTATA SFRIPQREGR AIAALEAGCF IENKRFEGNL VYFTAHGPAS LLQRYRRYIE LAHGELPQTS PVEARPRRRT RQIA // ID I3ZZC8_ORNRL Unreviewed; 401 AA. AC I3ZZC8; DT 05-SEP-2012, integrated into UniProtKB/TrEMBL. DT 05-SEP-2012, sequence version 1. DT 07-JUN-2017, entry version 36. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Ornrh_0867 {ECO:0000313|EMBL:AFL97062.1}; OS Ornithobacterium rhinotracheale (strain ATCC 51463 / DSM 15997 / CCUG OS 23171 / CIP 104009 / LMG 9086). OC Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales; OC Flavobacteriaceae; Ornithobacterium. OX NCBI_TaxID=867902 {ECO:0000313|EMBL:AFL97062.1, ECO:0000313|Proteomes:UP000006051}; RN [1] {ECO:0000313|EMBL:AFL97062.1, ECO:0000313|Proteomes:UP000006051} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51463 / DSM 15997 / CCUG 23171 / LMG 9086 RC {ECO:0000313|Proteomes:UP000006051}; RG US DOE Joint Genome Institute (JGI-PGF); RA Lucas S., Copeland A., Lapidus A., Goodwin L., Pitluck S., Peters L., RA Mikhailova N., Teshima H., Kyrpides N., Mavromatis K., Pagani I., RA Ivanova N., Ovchinnikova G., Zeytun A., Detter J.C., Han C., Land M., RA Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T., Wu D., RA Lang E., Kopitz M., Brambilla E., Klenk H.-P., Eisen J.A.; RT "The complete genome of Ornithobacterium rhinotracheale DSM 15997."; RL Submitted (JUN-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP003283; AFL97062.1; -; Genomic_DNA. DR RefSeq; WP_014790663.1; NC_018016.1. DR EnsemblBacteria; AFL97062; AFL97062; Ornrh_0867. DR KEGG; orh:Ornrh_0867; -. DR PATRIC; fig|867902.3.peg.849; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000006051; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000006051}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000006051}. FT DOMAIN 200 384 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 401 AA; 46715 MW; C51C2D17CAC31CD5 CRC64; MLEKKEARYE RVILVGVITQ NQTEEKLSEY MDELAFLAYT AGAETIARFT QKLQQPDSKY FVGSGKLNEI KEFVEENDID TVIFDDELSP SQLKNIERVL DRKIIDRTNL ILDIFAQRAE TSYARTQVEL AQYEYILPRL TRMWTHLERQ RGGIGLRGPG ETQIQTDRRI IRDRISLLKK KLETIDRQMA TQRKNRGSLI RVALVGYTNV GKSTLMNLIS KSNVFAEDKL FATLDTTVRK VVIGNLPFLL SDTVGFIRKL PTQLVESFKS TLDEVREADL ILHVVDISHE SFEDQIRSVN EILKEIDVVD KPTIMVFNKI DNFSFVPKAE DDLSEPTREN ISLDEWERMW IAKSEFPTLF ISAKKKKNIA AFKKTLYEEV KKIHTQRYPY NNFLFQYYDE E // ID I4AHV7_BERLS Unreviewed; 416 AA. AC I4AHV7; DT 05-SEP-2012, integrated into UniProtKB/TrEMBL. DT 05-SEP-2012, sequence version 1. DT 07-JUN-2017, entry version 36. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Fleli_1104 {ECO:0000313|EMBL:AFM03542.1}; OS Bernardetia litoralis (strain ATCC 23117 / DSM 6794 / NBRC 15988 / OS NCIMB 1366 / Sio-4) (Flexibacter litoralis). OC Bacteria; Bacteroidetes; Cytophagia; Cytophagales; Bernardetiaceae; OC Bernardetia. OX NCBI_TaxID=880071 {ECO:0000313|EMBL:AFM03542.1, ECO:0000313|Proteomes:UP000006054}; RN [1] {ECO:0000313|Proteomes:UP000006054} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 23117 / DSM 6794 / NBRC 15988 / NCIMB 1366 / Sio-4 RC {ECO:0000313|Proteomes:UP000006054}; RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., RA Tice H., Bruce D., Goodwin L., Pitluck S., Peters L., Ovchinnikova G., RA Lu M., Kyrpides N., Mavromatis K., Ivanova N., Brettin T., RA Detter J.C., Han C., Larimer F., Land M., Hauser L., Markowitz V., RA Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Spring S., Lang E., RA Kopitz M., Brambilla E., Klenk H.-P., Eisen J.A.; RT "The complete genome of Flexibacter litoralis DSM 6794."; RL Submitted (JUN-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP003345; AFM03542.1; -; Genomic_DNA. DR RefSeq; WP_014796999.1; NC_018018.1. DR EnsemblBacteria; AFM03542; AFM03542; Fleli_1104. DR KEGG; fli:Fleli_1104; -. DR PATRIC; fig|880071.3.peg.1075; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000006054; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000006054}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Hydrolase {ECO:0000313|EMBL:AFM03542.1}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000006054}. FT DOMAIN 201 382 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 416 AA; 48025 MW; BA2177F5A305B908 CRC64; MLETSTIKPE TAVLVGIVNQ TQNSQKSQEY LDELEFLAET LGITCVKRFT QQLDTPDTTT FVRKGKIEEI QEYMASKEID TVIFDDELSP RHVRNIGKEF ENKQVFDRST LILEIFKHRA QTSQASTQVE LARYQYLLPR LTNMWTHLSR QRGGVGQRGA GEKEIETDRR IVRDRITLLK ERLKKIEKQD ETRRKQRHKV VRVSLVGYTN VGKSTLMRIL TGSDVFAENK LFATVDSTVR KVFWEGIPFL LSDTVGFIRK LPTMLIESFK STLKEIVEAD VLIHVVDISH PAFEEHIKVV QETLKELGAA DKPTLLVFNK IDAYTNDVQV GQNYLVCPPT LEELKESYLG VDKKHTVFVS AAKQENLEEL KDKLIELIAS RHFQIYPNYV RPNHYAEAKD YNKEDYGIIE DNQEEE // ID I4BAT5_TURPD Unreviewed; 385 AA. AC I4BAT5; DT 05-SEP-2012, integrated into UniProtKB/TrEMBL. DT 05-SEP-2012, sequence version 1. DT 07-JUN-2017, entry version 34. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Turpa_3758 {ECO:0000313|EMBL:AFM14392.1}; OS Turneriella parva (strain ATCC BAA-1111 / DSM 21527 / NCTC 11395 / H) OS (Leptospira parva). OC Bacteria; Spirochaetes; Leptospirales; Leptospiraceae; Turneriella. OX NCBI_TaxID=869212 {ECO:0000313|EMBL:AFM14392.1, ECO:0000313|Proteomes:UP000006048}; RN [1] {ECO:0000313|EMBL:AFM14392.1, ECO:0000313|Proteomes:UP000006048} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-1111 / DSM 21527 / NCTC 11395 / H RC {ECO:0000313|Proteomes:UP000006048}; RG US DOE Joint Genome Institute (JGI-PGF); RA Lucas S., Han J., Lapidus A., Bruce D., Goodwin L., Pitluck S., RA Peters L., Kyrpides N., Mavromatis K., Ivanova N., Mikhailova N., RA Chertkov O., Detter J.C., Tapia R., Han C., Land M., Hauser L., RA Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Gronow S., RA Wellnitz S., Brambilla E., Klenk H.-P., Eisen J.A.; RT "The complete chromosome of genome of Turneriella parva DSM 21527."; RL Submitted (JUN-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002959; AFM14392.1; -; Genomic_DNA. DR RefSeq; WP_014804869.1; NC_018020.1. DR EnsemblBacteria; AFM14392; AFM14392; Turpa_3758. DR KEGG; tpx:Turpa_3758; -. DR PATRIC; fig|869212.3.peg.3786; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000006048; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000006048}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000006048}. FT DOMAIN 212 383 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 385 AA; 43321 MW; 9445CC3B527399E2 CRC64; MDASSLYQKK LVSKEQYRAL CVGQYGSSYF PDKRSQEESL RELLMLAETA GVKTLHELFF NHDDIHPAMF FSSGQIERIR RVCTDLDLNL LFVDAQLKPN QLRNLEEELK IRVLGRIEVI LDIFAMRAKT REALLQVELA QLLYILPRLK GLGGVLSRQG ATGAPGIGTR GPGETMLETD RRYIRRRIQK IRSDLKDVER HRSTARQGRG LATFALVGYT NAGKSSILNA LSSSSQKVFA EDKLFATLDT FSRKIYLGEQ NFRPFYAVVT DTVGFIRNLP ASLIAAFQST LGEIKHADWV IEVHDASSVQ LEDEMEVVRG ELDRLGVADK PRLLYFNKDD LVFADTRAEL TEKYPNAIWG NALSREGVAA LRQRLAESAA NVHVA // ID I4BWC6_ACEMN Unreviewed; 379 AA. AC I4BWC6; DT 05-SEP-2012, integrated into UniProtKB/TrEMBL. DT 05-SEP-2012, sequence version 1. DT 07-JUN-2017, entry version 36. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Anamo_0957 {ECO:0000313|EMBL:AFM21583.1}; OS Acetomicrobium mobile (strain ATCC BAA-54 / DSM 13181 / NGA) OS (Acetomicrobium mobile). OC Bacteria; Synergistetes; Synergistia; Synergistales; Synergistaceae; OC Acetomicrobium. OX NCBI_TaxID=891968 {ECO:0000313|EMBL:AFM21583.1, ECO:0000313|Proteomes:UP000006061}; RN [1] {ECO:0000313|Proteomes:UP000006061} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC BAA-54 / DSM 13181 / NGA RC {ECO:0000313|Proteomes:UP000006061}; RX PubMed=23961311; DOI=10.4056/sigs.3547050; RA Mavromatis K., Stackebrandt E., Held B., Lapidus A., Nolan M., RA Lucas S., Hammon N., Deshpande S., Cheng J.F., Tapia R., Goodwin L.A., RA Pitluck S., Liolios K., Pagani I., Ivanova N., Mikhailova N., RA Huntemann M., Pati A., Chen A., Palaniappan K., Land M., Rohde M., RA Spring S., Goker M., Woyke T., Detter J.C., Bristow J., Eisen J.A., RA Markowitz V., Hugenholtz P., Klenk H.P., Kyrpides N.C.; RT "Complete genome sequence of the moderate thermophile Anaerobaculum RT mobile type strain (NGA(T))."; RL Stand. Genomic Sci. 8:47-57(2013). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP003198; AFM21583.1; -; Genomic_DNA. DR RefSeq; WP_014806816.1; NC_018024.1. DR EnsemblBacteria; AFM21583; AFM21583; Anamo_0957. DR KEGG; amo:Anamo_0957; -. DR PATRIC; fig|891968.3.peg.937; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000006061; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000006061}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000006061}. FT DOMAIN 197 369 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 156 197 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 379 AA; 42272 MW; 82BBB42AD3D052DC CRC64; MVNEERKAVI VCLERQGAND DIDLLAEELA LLLSNLDIRV VGRIDQRRAS PDPATFIGKG KLYEVKALME SLGATLVVCN DSLLPTQLHN MRSILKAEVW DRSFVIMKIF EARAHSAEAK LQVELALCKY EIPLLKGLGW QMSQTGGGIG TRGPGETEFE RHRRKLERKV VALQRKLEQV RRRRLNLRKR RKKTETQTVA IVGYTNSGKS TLLRALSHDE DIYCADKLFA TLDPKVRKVS LPSGKLVLFA DTVGFIRKLP VELVAAFRAT LEEVNEAALL LIVIDPLDKD PVESLRVVEE TLSQIGAASI SRLIAVNKID MLDNKEKLEA ILERLAIHSG CDIIPISALK KINMPLLLKK VDETLRQGDF SSSLTGALN // ID I4CCL5_DESTA Unreviewed; 602 AA. AC I4CCL5; DT 05-SEP-2012, integrated into UniProtKB/TrEMBL. DT 05-SEP-2012, sequence version 1. DT 07-JUN-2017, entry version 36. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Desti_4685 {ECO:0000313|EMBL:AFM27306.1}; OS Desulfomonile tiedjei (strain ATCC 49306 / DSM 6799 / DCB-1). OC Bacteria; Proteobacteria; Deltaproteobacteria; Syntrophobacterales; OC Syntrophaceae; Desulfomonile. OX NCBI_TaxID=706587 {ECO:0000313|EMBL:AFM27306.1, ECO:0000313|Proteomes:UP000006055}; RN [1] {ECO:0000313|Proteomes:UP000006055} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 49306 / DSM 6799 / DCB-1 RC {ECO:0000313|Proteomes:UP000006055}; RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., RA Tice H., Bruce D., Goodwin L., Pitluck S., Peters L., Ovchinnikova G., RA Zeytun A., Lu M., Kyrpides N., Mavromatis K., Ivanova N., Brettin T., RA Detter J.C., Han C., Larimer F., Land M., Hauser L., Markowitz V., RA Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Spring S., Schroeder M., RA Brambilla E., Klenk H.-P., Eisen J.A.; RT "Complete sequence of chromosome of Desulfomonile tiedjei DSM 6799."; RL Submitted (JUN-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP003360; AFM27306.1; -; Genomic_DNA. DR RefSeq; WP_014812414.1; NC_018025.1. DR EnsemblBacteria; AFM27306; AFM27306; Desti_4685. DR KEGG; dti:Desti_4685; -. DR PATRIC; fig|706587.4.peg.5302; -. DR KO; K03665; -. DR OMA; EREVIIT; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000006055; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000006055}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Hydrolase {ECO:0000313|EMBL:AFM27306.1}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000006055}. FT DOMAIN 418 538 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 602 AA; 67346 MW; EC808A4A7B5FC799 CRC64; MGRARAISLR IVDTILKDGT EERSFNAMRE TRAKAGKESG LHAVYGLTRG LKHSQKIRLE KLALRRIPAN RVITQEMARH LTEISSEIRR QIGILVDRQG NIYRVLVGDA RSILIPRLTG WRVGVGRLRG LRLIHTHLKD EHLTEEDLTD LALLRLDLVA SVGVDSQGLP TVIHIAHLLP DNPMKQIWQL LDPTPPSLLD LDFSAFIRSL EDEISRSIST RSVKATQDRA YLIGRTVGKD WEIEESLDEL NELAKSCGVE VVGTSIQKRN TVDPHFLVGK GKLREVVIDA LQKGADLLVF DAELSPSQVR SIGDFTELKV IDRSQLILDI FAQRAKSREG KIQVELAQLK YALPRLAEKD DALSRLTGGI GGRGPGETRL EIDRRRIRSR IDFLERQIGQ LGKRRALRRQ LRNRREVPII SIVGYTNAGK STLLNNLTKS DILTEDKLFA TLDPTSRRLR FPRETEVIIT DTVGFLKDLP ETLVAAFSAT LDELADADLL IHVIDCSNEA FEAQMQAVEK LLEQLGLNLI PLIRVFNKQD LMNPEMVRNI SASYNGIGIS ANDSKSFPPL IRRMEDEILT ALSNRMNDAP QQSSGTVTGV TA // ID I4D7N9_DESAJ Unreviewed; 536 AA. AC I4D7N9; DT 05-SEP-2012, integrated into UniProtKB/TrEMBL. DT 05-SEP-2012, sequence version 1. DT 07-JUN-2017, entry version 35. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Desaci_2902 {ECO:0000313|EMBL:AFM41813.1}; OS Desulfosporosinus acidiphilus (strain DSM 22704 / JCM 16185 / SJ4). OC Bacteria; Firmicutes; Clostridia; Clostridiales; Peptococcaceae; OC Desulfosporosinus. OX NCBI_TaxID=646529 {ECO:0000313|EMBL:AFM41813.1, ECO:0000313|Proteomes:UP000002892}; RN [1] {ECO:0000313|EMBL:AFM41813.1, ECO:0000313|Proteomes:UP000002892} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 22704 / JCM 16185 / SJ4 RC {ECO:0000313|Proteomes:UP000002892}; RX PubMed=23105050; DOI=10.1128/JB.01392-12; RA Pester M., Brambilla E., Alazard D., Rattei T., Weinmaier T., Han J., RA Lucas S., Lapidus A., Cheng J.F., Goodwin L., Pitluck S., Peters L., RA Ovchinnikova G., Teshima H., Detter J.C., Han C.S., Tapia R., RA Land M.L., Hauser L., Kyrpides N.C., Ivanova N.N., Pagani I., RA Huntmann M., Wei C.L., Davenport K.W., Daligault H., Chain P.S., RA Chen A., Mavromatis K., Markowitz V., Szeto E., Mikhailova N., RA Pati A., Wagner M., Woyke T., Ollivier B., Klenk H.P., Spring S., RA Loy A.; RT "Complete genome sequences of Desulfosporosinus orientis DSM765T, RT Desulfosporosinus youngiae DSM17734T, Desulfosporosinus meridiei RT DSM13257T, and Desulfosporosinus acidiphilus DSM22704T."; RL J. Bacteriol. 194:6300-6301(2012). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP003639; AFM41813.1; -; Genomic_DNA. DR RefSeq; WP_014827806.1; NC_018068.1. DR EnsemblBacteria; AFM41813; AFM41813; Desaci_2902. DR KEGG; dai:Desaci_2902; -. DR KO; K03665; -. DR OMA; EREVIIT; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000002892; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000002892}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000002892}. FT DOMAIN 367 536 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 536 AA; 60079 MW; D59BD036045362B8 CRC64; MEISGDLSGI KASQLRDLKK LSEYQTGRDD LIHPEILSGL IRLTQLWNRE ICIYLSRSGL LIASAVGKHA TVTLLPLKGR SQSKHLRCLH THPNGVPRLS SLDFSALTSL KLESMTAIGV LRGELTGFQL AYLTSDGSPY VVDLKPDNWN KFNYFESQQE HYHNHNSQIK LESKPDKERA FLLALQDGEQ EVSENLEELA ELADTAGVEV VGQLVQPRRS SQSRSFIGSG KLEELVHRIQ ETRADVLISD DELSPSQLRT LEMETGLKIL DRTGLILDIF AQRAHSREGK LQVELAQLKH LLPYLTGQGQ TLSRLGGGIG SRGPGETKLE LDRRRMRQRI NLLDKELKLV LQHREIQRRQ RAKSGLPMIA LVGYTNAGKT TFMKNAMEQA GFRSDIPSGE NKLFATLDPI VRRIKLTPSL EILLSDTVGF IRKLPTQLLK AFLATLEEVQ QADILIHVLD VSHPQALQQA ETVHEILGQL ECHDKPVITL LNKVDKVHDD EEISRIAQLL PYSIPLSLKR GDSLAPIWNV LESLLE // ID I4ECB7_9CHLR Unreviewed; 463 AA. AC I4ECB7; DT 05-SEP-2012, integrated into UniProtKB/TrEMBL. DT 05-SEP-2012, sequence version 1. DT 12-APR-2017, entry version 31. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=ynbA {ECO:0000313|EMBL:CCF82329.1}; GN Synonyms=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=NITHO_1020009 {ECO:0000313|EMBL:CCF82329.1}; OS Nitrolancea hollandica Lb. OC Bacteria; Chloroflexi; Sphaerobacteridae; Sphaerobacterales; OC Sphaerobacterineae; Sphaerobacteraceae; Nitrolancea. OX NCBI_TaxID=1129897 {ECO:0000313|EMBL:CCF82329.1, ECO:0000313|Proteomes:UP000004221}; RN [1] {ECO:0000313|EMBL:CCF82329.1, ECO:0000313|Proteomes:UP000004221} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=none {ECO:0000313|Proteomes:UP000004221}; RX PubMed=22763649; DOI=10.1038/ismej.2012.70; RA Sorokin D.Y., Lucker S., Vejmelkova D., Kostrikina N.A., RA Kleerebezem R., Rijpstra W.I., Damste J.S., Le Paslier D., Muyzer G., RA Wagner M., van Loosdrecht M.C., Daims H.; RT "Nitrification expanded: discovery, physiology and genomics of a RT nitrite-oxidizing bacterium from the phylum Chloroflexi."; RL ISME J. 6:2245-2256(2012). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:CCF82329.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CAGS01000005; CCF82329.1; -; Genomic_DNA. DR EnsemblBacteria; CCF82329; CCF82329; NITHO_1020009. DR Proteomes; UP000004221; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000004221}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000004221}. FT DOMAIN 232 401 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 191 218 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 463 AA; 51728 MW; E9B92DF883BF2376 CRC64; MKVRTPWYDS CIANVHDIDP YAEERLTTIA QTHETNSPAE RALLVAVDWR HDDWDIASSL EELAQLAETA GLDVVGSITQ ALPHPNHAHY VGSGKLNEIK ELRESLRYDV VLVDDELPPA QLRNLEEALE VKVIDRTALI LDIFARRAQT HEGRLQVELA QLEYRLPRLT RMWTHLSRQA VGGVGLRGPG ETQLEADRRQ ARQRIAFIKQ QLDEVHRHRQ LYRERRQKEN IPIVALVGYT NAGKSTLLNT LAGASVLAED KLFATLDPTT RRIELPGGHH VLVTDTVGFI NKLPTLLIAA FRATLEEILE AAVLVHVLDV THPKSAEQAE TVRQVIEELG ADDRPVITAL NKIDRLNGAL TPDQLAAELG LSPDYVPISA QTGNGLDLLL SRVEEVLASE SRLVDVQVMV PYGEAGLVDL FHRKGQVRSE EFTETGAVLS GRIPQHMLPR FEPFRQTRAA RAR // ID I4ERQ7_9ACTN Unreviewed; 387 AA. AC I4ERQ7; DT 05-SEP-2012, integrated into UniProtKB/TrEMBL. DT 05-SEP-2012, sequence version 1. DT 07-JUN-2017, entry version 37. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=MODMU_0613 {ECO:0000313|EMBL:CCH86070.1}; OS Modestobacter marinus. OC Bacteria; Actinobacteria; Geodermatophilales; Geodermatophilaceae; OC Modestobacter. OX NCBI_TaxID=477641 {ECO:0000313|Proteomes:UP000006461}; RN [1] {ECO:0000313|EMBL:CCH86070.1, ECO:0000313|Proteomes:UP000006461} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BC501 {ECO:0000313|EMBL:CCH86070.1, RC ECO:0000313|Proteomes:UP000006461}; RX PubMed=22887672; DOI=10.1128/JB.01029-12; RA Normand P., Gury J., Pujic P., Chouaia B., Crotti E., Brusetti L., RA Daffonchio D., Vacherie B., Barbe V., Medigue C., Calteau A., RA Ghodhbane-Gtari F., Essoussi I., Nouioui I., Abbassi-Ghozzi I., RA Gtari M.; RT "Genome sequence of radiation-resistant Modestobacter marinus strain RT BC501, a representative Actinobacterium that thrives on calcareous RT stone surfaces."; RL J. Bacteriol. 194:4773-4774(2012). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; FO203431; CCH86070.1; -; Genomic_DNA. DR RefSeq; WP_014738680.1; NC_017955.1. DR EnsemblBacteria; CCH86070; CCH86070; MODMU_0613. DR KEGG; mmar:MODMU_0613; -. DR PATRIC; fig|477641.3.peg.584; -. DR KO; K03665; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000006461; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000006461}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000006461}. FT DOMAIN 223 387 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 387 AA; 41318 MW; 9C7439538452620A CRC64; MPGPWLVRSG GTALLSADDP AAGQDDGARA VLLGLEASGE AAGGLDELER LAETDGVAVV GRLTQARDEP DPATYLGSGK VAELAGLVRE RQAGMVIADG ELSPAQVRNL EERLAARVVD RTALILDIFG QHARSSEGRA QVELAQLAYQ LPRLRGQGTE LSRVGGGRVA GGAGIGVRGP GEQRLETERR HLRRRMALLR RQVAETGRRR ARTRSRRRHN QVPSVAITGY TNAGKSALLN RLTGADALVQ DALFATLDPT VRQTRSPGGR RYTLTDTVGF VRHLPHQLVD AFRSTLEEVV EADLVLHVVD ASAPDAMDQV TTVRGVLYEI GARDHTELLA LNKVDVAPPE WLAALRSAYP DAVAVSALTG EGIEDLRAAI DRALPPG // ID I4F222_9ACTN Unreviewed; 499 AA. AC I4F222; DT 05-SEP-2012, integrated into UniProtKB/TrEMBL. DT 05-SEP-2012, sequence version 1. DT 07-JUN-2017, entry version 35. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=MODMU_4289 {ECO:0000313|EMBL:CCH89685.1}; OS Modestobacter marinus. OC Bacteria; Actinobacteria; Geodermatophilales; Geodermatophilaceae; OC Modestobacter. OX NCBI_TaxID=477641 {ECO:0000313|Proteomes:UP000006461}; RN [1] {ECO:0000313|EMBL:CCH89685.1, ECO:0000313|Proteomes:UP000006461} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BC501 {ECO:0000313|EMBL:CCH89685.1, RC ECO:0000313|Proteomes:UP000006461}; RX PubMed=22887672; DOI=10.1128/JB.01029-12; RA Normand P., Gury J., Pujic P., Chouaia B., Crotti E., Brusetti L., RA Daffonchio D., Vacherie B., Barbe V., Medigue C., Calteau A., RA Ghodhbane-Gtari F., Essoussi I., Nouioui I., Abbassi-Ghozzi I., RA Gtari M.; RT "Genome sequence of radiation-resistant Modestobacter marinus strain RT BC501, a representative Actinobacterium that thrives on calcareous RT stone surfaces."; RL J. Bacteriol. 194:4773-4774(2012). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; FO203431; CCH89685.1; -; Genomic_DNA. DR RefSeq; WP_014742251.1; NC_017955.1. DR EnsemblBacteria; CCH89685; CCH89685; MODMU_4289. DR KEGG; mmar:MODMU_4289; -. DR PATRIC; fig|477641.3.peg.4011; -. DR KO; K03665; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000006461; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000006461}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000006461}. FT DOMAIN 276 440 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 499 AA; 53351 MW; 7A314C7FC597680C CRC64; MTTAQNRAIL DEAEARVDKA ARARAQDPTP APTTPWDAPD DSTGSYVKEE RGALRRVAGL STELTDVTEV EYRQLRLERV VLVGVWTEGT AVDAHRSLAE LAALAETAGS QVLDALVQRR DKPDPATYVG SGKAAELRDV VAATGADTVI CDGELAPGQL NQLEKILKVK VVDRTALILD IFAQHATSRE GKAQVELAQM QYMLPRLRGW GESLSRQAGG RVAGGGGIGT RGPGETKIET DRRRIRARVS KLRKEIAGMA TARTTQRNSR DRNATPSVAI AGYTNAGKSS LLNQLTDAGV LVQDALFATL DPTVRRAQTP DGREFTVTDT VGFVRHLPHQ LVDAFRSTLE EVAAADLLVH VVDGSDPDPL GQIDAVRVVL NEIDAAAVPE LIVVNKVDAM TEDDVLALRQ ALPGAAWVSA RTGEGIEALR DVIAARLPHP DVDVEVLVPY DRGDLVARVH RDGEVIEERH GATGTLLTAR VAPALAAVLE DYAAPVAGI // ID I4N4Q9_9PSED Unreviewed; 433 AA. AC I4N4Q9; DT 05-SEP-2012, integrated into UniProtKB/TrEMBL. DT 05-SEP-2012, sequence version 1. DT 30-AUG-2017, entry version 33. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=PMM47T1_10997 {ECO:0000313|EMBL:EIK96449.1}; OS Pseudomonas sp. M47T1. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=1179778 {ECO:0000313|EMBL:EIK96449.1, ECO:0000313|Proteomes:UP000004339}; RN [1] {ECO:0000313|EMBL:EIK96449.1, ECO:0000313|Proteomes:UP000004339} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=M47T1 {ECO:0000313|EMBL:EIK96449.1, RC ECO:0000313|Proteomes:UP000004339}; RX PubMed=22887683; DOI=10.1128/JB.01116-12; RA Proenca D.N., Espirito Santo C., Grass G., Morais P.V.; RT "Draft Genome Sequence of Pseudomonas sp. Strain M47T1, Carried by RT Bursaphelenchus xylophilus Isolated from Pinus pinaster."; RL J. Bacteriol. 194:4789-4790(2012). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EIK96449.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AJWX01000008; EIK96449.1; -; Genomic_DNA. DR RefSeq; WP_008368556.1; NZ_AJWX01000008.1. DR EnsemblBacteria; EIK96449; EIK96449; PMM47T1_10997. DR PATRIC; fig|1179778.3.peg.2203; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000004339; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000004339}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000004339}. FT DOMAIN 199 366 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 165 192 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 433 AA; 48823 MW; 8D1C012ACC603011 CRC64; MFFERHGGGE RAILVHLDGQ DPEAREDPQE FQELAVSAGA ETVAFVNVAR HQPTAKYLIG SGKVEELRDR VKAEQVDLVI FNHTLTPSQE RNLERAFECR VLDRTGLILD IFAQRARTHE GKLQVELAQL EHMSTRLVRG WTHLERQKGG IGLRGPGETQ LETDRRLLRV RLRQIKARLE KVRSQREQAR RGRRRADIPS VSLVGYTNAG KSTLFNAVTS SEVYAADQLF ATLDPTLRRL QLDDLGPVIL ADTVGFIRHL PHKLVEAFRA TLEESSNSDL LLHVIDAHEP ERLQQIEQVM AVLTEIGAHG LPILEVYNKI DLLEGVEPQI QRDAEGKPQR VWVSARDGRG LELVKQAVAE LLGEDLFVGT LRLPQQLGRL RAQFFEMGVV QSEAHDEDGS SLLAVRVPRT ELNRLVSRAG MEPLEFIEQH TLQ // ID I4VPB6_9GAMM Unreviewed; 432 AA. AC I4VPB6; DT 05-SEP-2012, integrated into UniProtKB/TrEMBL. DT 05-SEP-2012, sequence version 1. DT 07-JUN-2017, entry version 32. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=UU9_10442 {ECO:0000313|EMBL:EIL89057.1}; OS Rhodanobacter fulvus Jip2. OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales; OC Rhodanobacteraceae; Rhodanobacter. OX NCBI_TaxID=1163408 {ECO:0000313|EMBL:EIL89057.1, ECO:0000313|Proteomes:UP000004210}; RN [1] {ECO:0000313|EMBL:EIL89057.1, ECO:0000313|Proteomes:UP000004210} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Jip2T {ECO:0000313|Proteomes:UP000004210}; RX PubMed=22843592; DOI=10.1128/JB.00871-12; RA Kostka J.E., Green S.J., Rishishwar L., Prakash O., Katz L.S., RA Marino-Ramirez L., Jordan I.K., Munk C., Ivanova N., Mikhailova N., RA Watson D.B., Brown S.D., Palumbo A.V., Brooks S.C.; RT "Genome sequences for six rhodanobacter strains, isolated from soils RT and the terrestrial subsurface, with variable denitrification RT capabilities."; RL J. Bacteriol. 194:4461-4462(2012). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EIL89057.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AJXU01000042; EIL89057.1; -; Genomic_DNA. DR RefSeq; WP_007081725.1; NZ_AJXU01000042.1. DR EnsemblBacteria; EIL89057; EIL89057; UU9_10442. DR PATRIC; fig|1163408.3.peg.2141; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000004210; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000004210}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000004210}. FT DOMAIN 200 366 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 432 AA; 47124 MW; 62A217440CC4AF1F CRC64; MFDRQKKGDR AVLVMPHSRG EGDSARRAEE FAELVKSAGA EVLTAIAARI DVPNPRFYIG SGKADEVAEA VAALEADLVL VDHELTPVQE RNLEKQLKVR VVDRAGLILD IFAQRARSHE GKLEVELAQL KHIATRLVRG WTHLDAQRGG AIGNRGPGET QLETDRRLLN ERVKILGKRL EKVQTQRTQQ RRARLRNTVP RVALVGYTNA GKSTLFNALT TGEVYAADQL FATLDPTVRK IDGLSCGPAV LADTVGFIRE LPHDLVAAFR ATLAEAREAD LLLHVSDAAD DEREPLHRVV NKVLQEIDAG DLPQLQVMNK IDLAGLEPRI DRDGDGRPYR VWLSAATGAG VELLHQALGE LLGGDRVQSS LHLPLTAGRL HARLKASGAI AEETVDEHGW RLRIDAPRSV LAPLGADATE AGMLRDLLAP AS // ID I4VPL0_9GAMM Unreviewed; 421 AA. AC I4VPL0; DT 05-SEP-2012, integrated into UniProtKB/TrEMBL. DT 05-SEP-2012, sequence version 1. DT 07-JUN-2017, entry version 31. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=UU5_16067 {ECO:0000313|EMBL:EIL89151.1}; OS Rhodanobacter sp. 115. OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales; OC Rhodanobacteraceae; Rhodanobacter. OX NCBI_TaxID=1162282 {ECO:0000313|EMBL:EIL89151.1, ECO:0000313|Proteomes:UP000004557}; RN [1] {ECO:0000313|EMBL:EIL89151.1, ECO:0000313|Proteomes:UP000004557} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=115 {ECO:0000313|EMBL:EIL89151.1, RC ECO:0000313|Proteomes:UP000004557}; RX PubMed=22843592; DOI=10.1128/JB.00871-12; RA Kostka J.E., Green S.J., Rishishwar L., Prakash O., Katz L.S., RA Marino-Ramirez L., Jordan I.K., Munk C., Ivanova N., Mikhailova N., RA Watson D.B., Brown S.D., Palumbo A.V., Brooks S.C.; RT "Genome sequences for six rhodanobacter strains, isolated from soils RT and the terrestrial subsurface, with variable denitrification RT capabilities."; RL J. Bacteriol. 194:4461-4462(2012). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EIL89151.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AJXS01000383; EIL89151.1; -; Genomic_DNA. DR EnsemblBacteria; EIL89151; EIL89151; UU5_16067. DR PATRIC; fig|1162282.3.peg.3030; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000004557; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000004557}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000004557}. FT DOMAIN 159 354 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 421 AA; 45792 MW; F75233A35462D96A CRC64; MLGNLAARVD VPNPRYYIGS GKADEVAEMA RALEADLILV DHLLSPVQER NLEKHLGVRV VDRAGLILDI FAQRARSHEG KLEVELAQLK HLATRLVRGW THLDAQRGGA IGNRGPGETQ LETDRRLLGE RVKMLTKRLE KVQTQRGQQR RARLRNTVPR IALVGYTNAG KSTLFNALTT GGVYAADQLF ATLDPTVRKL DDLDCGPAVL ADTVGFVRDL PHDLVAAFRG TLAEARDADL LLHVSDAADE ERDRMHRVVD QVLEEIGAGD LPQLRIMNKI DMIHADIPAD EDQEASIHGR IPQESVASAV AGAVQPRIDR DGEGRPRTVW LSAGTGQGLD LLRQALGELL GGDRMQSKLH LPLSAGRLHA KLKAAGVIAG EVVDEHGWQL RIDAPRSVIA SLAGGRDADA SSLRDLLGTI E // ID I4VW34_9GAMM Unreviewed; 433 AA. AC I4VW34; DT 05-SEP-2012, integrated into UniProtKB/TrEMBL. DT 05-SEP-2012, sequence version 1. DT 30-AUG-2017, entry version 34. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=UU7_13003 {ECO:0000313|EMBL:EIL91425.1}; OS Rhodanobacter spathiphylli B39. OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales; OC Rhodanobacteraceae; Rhodanobacter. OX NCBI_TaxID=1163407 {ECO:0000313|EMBL:EIL91425.1, ECO:0000313|Proteomes:UP000003226}; RN [1] {ECO:0000313|EMBL:EIL91425.1, ECO:0000313|Proteomes:UP000003226} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=B39 {ECO:0000313|EMBL:EIL91425.1, RC ECO:0000313|Proteomes:UP000003226}; RX PubMed=22843592; DOI=10.1128/JB.00871-12; RA Kostka J.E., Green S.J., Rishishwar L., Prakash O., Katz L.S., RA Marino-Ramirez L., Jordan I.K., Munk C., Ivanova N., Mikhailova N., RA Watson D.B., Brown S.D., Palumbo A.V., Brooks S.C.; RT "Genome sequences for six rhodanobacter strains, isolated from soils RT and the terrestrial subsurface, with variable denitrification RT capabilities."; RL J. Bacteriol. 194:4461-4462(2012). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EIL91425.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AJXT01000043; EIL91425.1; -; Genomic_DNA. DR RefSeq; WP_007809005.1; NZ_AJXT01000043.1. DR EnsemblBacteria; EIL91425; EIL91425; UU7_13003. DR PATRIC; fig|1163407.3.peg.2616; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000003226; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000003226}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}. FT DOMAIN 200 366 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 166 193 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 433 AA; 47174 MW; A42CBC5018BB2668 CRC64; MFDRQKKGDR AVLVLPHSRG EGDTARRAEE FAELVKSAGA EVLAVISARV EDPNPRYYIG SGKANEVAEA ARALDADLVL VDHLLTPVQE RNLEKHLGVR VVDRAGLILD IFAQRARSHE GKLEVELAQL KHLATRLVRG WTHLDAQRGG AIGNRGPGET QLETDRRLLG ERVKQLTKRL EKVQVQRGQQ RRARMRNTVP RVALVGYTNA GKSTLFNALT TGDVFAADLL FATLDPTVRK LEDLSCGPAV IADTVGFIRE LPHDLVAAFR ATLAEARDAD LLLHVSDAAD EERERLHRVV DNVLEEIDAG DVPQLRVMNK IDLAGAEPRI ERDASGKPVR VWLSAATGVG LDLLRQALGE LLGGERVRSP LHLPLSAGRL HARLKAAGAI SGESIDEHGW QLHIDAPRSV IAPLGGGDPV EAKLLQELLA VAE // ID I4Z0L3_9RHIZ Unreviewed; 464 AA. AC I4Z0L3; DT 05-SEP-2012, integrated into UniProtKB/TrEMBL. DT 05-SEP-2012, sequence version 1. DT 07-JUN-2017, entry version 30. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=MicloDRAFT_00022380 {ECO:0000313|EMBL:EIM29755.1}; OS Microvirga lotononidis. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Methylobacteriaceae; Microvirga. OX NCBI_TaxID=864069 {ECO:0000313|EMBL:EIM29755.1, ECO:0000313|Proteomes:UP000003947}; RN [1] {ECO:0000313|EMBL:EIM29755.1, ECO:0000313|Proteomes:UP000003947} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=WSM3557 {ECO:0000313|EMBL:EIM29755.1, RC ECO:0000313|Proteomes:UP000003947}; RG US DOE Joint Genome Institute; RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S., RA Peters L., Zhang X., Detter J.C., Han C., Tapia R., Land M., RA Hauser L., Kyrpides N., Ivanova N., Pagani I., Brau L., Yates R., RA O'Hara G., Rui T., Howieson J., Reeve W., Woyke T.; RT "Improved High-Quality Draft sequence of Microvirga sp. WSM3557."; RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JH660641; EIM29755.1; -; Genomic_DNA. DR RefSeq; WP_009491221.1; NZ_JH660641.1. DR EnsemblBacteria; EIM29755; EIM29755; MicloDRAFT_00022380. DR PATRIC; fig|864069.3.peg.2437; -. DR Proteomes; UP000003947; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000003947}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000003947}. FT DOMAIN 231 405 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 464 AA; 51393 MW; 2FBE89A8A7BEBBC0 CRC64; MTEPRSPGEE RLAQLAEPEK EVAAGTRTLV IGPYRTRRRR GAVETDGQGA NPRPPEARLD EITGLALAID LTIIQSLIAP LASPRPATFI GSGKVEELAG LIRAEDIGLV VMDCALSPVQ QRNLEKAWGA KVIDRTGLIL EIFGRRARTR EGTLQVELAH LSYQKGRLVR SWTHLERQRG GFGFLGGPGE TQIEADRRLI QERMNRIERD LESVVKTRSL HRTSRRRVPY PIIALVGYTN AGKSTLFNRM TQADVLAENM LFATLDPTSR AIELPHGEKA ILSDTVGFIS DLPTMLVAAF RATLEDVVEA DVLLHVRDVS HGETEAQAGD VAVVLRELGI DPDDTRRVVE VWNKADLLSA DDRERLSTAS HRTGEERRPI LISALTGDGI SELLATIEHH LSLGRPTYEV DVAPEDGQGL AWLHENTEIL DRTTRENGHT ILQIRLVAGK EPRFLNRFPD ARVL // ID I4Z5P7_9BURK Unreviewed; 401 AA. AC I4Z5P7; DT 05-SEP-2012, integrated into UniProtKB/TrEMBL. DT 05-SEP-2012, sequence version 1. DT 07-JUN-2017, entry version 30. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=LepocDRAFT_00002710 {ECO:0000313|EMBL:EIM31539.1}; OS Leptothrix ochracea L12. OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Leptothrix. OX NCBI_TaxID=735332 {ECO:0000313|EMBL:EIM31539.1, ECO:0000313|Proteomes:UP000053899}; RN [1] {ECO:0000313|EMBL:EIM31539.1, ECO:0000313|Proteomes:UP000053899} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=L12 {ECO:0000313|EMBL:EIM31539.1, RC ECO:0000313|Proteomes:UP000053899}; RG US DOE Joint Genome Institute; RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S., RA Peters L., Zeytun A., Detter J.C., Han C., Tapia R., Land M., RA Hauser L., Kyrpides N., Ivanova N., Pagani I., Stepanauskas R., RA Masland D., Poulton N., Emerson D., Fleming E., Woyke T.; RT "Improved High-Quality Draft sequence of Leptothrix ochracea L12."; RL Submitted (APR-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JH660678; EIM31539.1; -; Genomic_DNA. DR RefSeq; WP_009453399.1; NZ_JH660678.1. DR EnsemblBacteria; EIM31539; EIM31539; LepocDRAFT_00002710. DR Proteomes; UP000053899; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000053899}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000053899}. FT DOMAIN 203 377 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 401 AA; 44240 MW; 7F5D090FF9486837 CRC64; MTAPVVSAAD LPRALLVGVD FGGKAFFDPS LDELALLAES AGDLPVAKLT AKRRSVDAAL FVGSGKADEI KALVQLHAAQ CVIFDQPLGP AQQRNLEKHL GVEVLDRTML ILEIFAARAR SHEGKLQVEL AKLQYLSTRL VRRWSHLERQ RGGVGLRGGP GETQIELDRR MIAERIKAVK ERLVKVKRQR GTQRKARERS GVLRVSLVGY TNAGKSTLFN ALVKAHVYAA DQLFATLDTT TRQLYLEEAR ARVSLSDTVG FIRDLPHALV NAFQATLQEA MEADVLLHVV DAASPTWFEQ VREVQRVLAD IGAAEVPQIL VFNKQDLMDE SLQPRTDEDF FELEPGRSVP RLFVSAMTGY GLPRLRQAIA DCREAEGDGL INGDAFTTQP YSESDDQPVI P // ID I4ZA24_9BACT Unreviewed; 416 AA. AC I4ZA24; DT 05-SEP-2012, integrated into UniProtKB/TrEMBL. DT 05-SEP-2012, sequence version 1. DT 07-JUN-2017, entry version 30. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=PrebiDRAFT_1357 {ECO:0000313|EMBL:EIM33066.1}; OS Prevotella bivia DSM 20514. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Prevotellaceae; OC Prevotella. OX NCBI_TaxID=868129 {ECO:0000313|EMBL:EIM33066.1, ECO:0000313|Proteomes:UP000002786}; RN [1] {ECO:0000313|EMBL:EIM33066.1, ECO:0000313|Proteomes:UP000002786} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 20514 {ECO:0000313|EMBL:EIM33066.1, RC ECO:0000313|Proteomes:UP000002786}; RG US DOE Joint Genome Institute (JGI-PGF); RA Lucas S., Copeland A., Lapidus A., Bruce D., Goodwin L., Pitluck S., RA Peters L., Mikhailova N., Munk A.C.C., Kyrpides N., Mavromatis K., RA Detter J.C., Han C., Land M., Hauser L., Markowitz V., Cheng J.-F., RA Hugenholtz P., Woyke T., Wu D., Gronow S., Wellnitz S., Brambilla E., RA Klenk H.-P., Eisen J.A.; RT "Improved High-Quality Draft genome of Prevotella bivia DSM 20514."; RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JH660660; EIM33066.1; -; Genomic_DNA. DR RefSeq; WP_004338561.1; NZ_JH660660.1. DR ProteinModelPortal; I4ZA24; -. DR EnsemblBacteria; EIM33066; EIM33066; PrebiDRAFT_1357. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000002786; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000002786}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000002786}. FT DOMAIN 216 400 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 416 AA; 47461 MW; 0728A46EC0CDAB0B CRC64; MKEFVISEVK TESAVLVGLI TQNQDEAKTK EYLDELEFLA DTAGAVTVKR FTQRVNGPSA VTYVGKGKLE EIRDYIKQKE DEEDPVGMVI FDDELSAKQM RNIEQMLAVK ILDRTSLILD IFAMRAQTAN AKTQVELAQY RYMLPRLQRL WTHLERQGGG SGSGGGKGSV GLRGPGETQL EMDRRIILNR MSLLKERLAE IDKQKSTQRK NRGRMIRVAL VGYTNVGKST TMNLLAKSEV FAENKLFATL DTTVRKVVVD NLPFLLADTV GFIRKLPTDL VDSFKSTLDE VREADLLLHV VDISHPDFEE QIEVVNKTLA DLGCADKPSM LIFNKIDNYT WVEKDEDDLT PPTKENITLD ELKRTWMAKA DGNCLFISAR EKENIDEFRE TLYKMVRELH VQKYPYNDFL YTIEEE // ID I5AW12_EUBCE Unreviewed; 411 AA. AC I5AW12; DT 05-SEP-2012, integrated into UniProtKB/TrEMBL. DT 05-SEP-2012, sequence version 1. DT 07-JUN-2017, entry version 34. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=EubceDRAFT1_2233 {ECO:0000313|EMBL:EIM57985.1}; OS [Eubacterium] cellulosolvens 6. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Eubacteriaceae; OC Eubacterium. OX NCBI_TaxID=633697 {ECO:0000313|EMBL:EIM57985.1, ECO:0000313|Proteomes:UP000005753}; RN [1] {ECO:0000313|EMBL:EIM57985.1, ECO:0000313|Proteomes:UP000005753} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=6 {ECO:0000313|EMBL:EIM57985.1, RC ECO:0000313|Proteomes:UP000005753}; RG US DOE Joint Genome Institute (JGI-PGF); RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L., RA Pitluck S., Land M.L., Hauser L., Chang Y.-J., Anderson I.J., RA Johnson E., Mulhopadhyay B., Kyrpides N., Woyke T.J.; RL Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:EIM57985.1, ECO:0000313|Proteomes:UP000005753} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=6 {ECO:0000313|EMBL:EIM57985.1, RC ECO:0000313|Proteomes:UP000005753}; RG US DOE Joint Genome Institute; RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S., RA Peters L., Mikhailova N., Gu W., Detter J.C., Han C., Tapia R., RA Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Johnson E., RA Mukhopadhyay B., Anderson I., Woyke T.; RT "Improved High-Quality Draft sequence of Eubacterium cellulosolvens RT 6."; RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CM001487; EIM57985.1; -; Genomic_DNA. DR RefSeq; WP_004604110.1; NZ_CM001487.1. DR ProteinModelPortal; I5AW12; -. DR STRING; 633697.EubceDRAFT_1809; -. DR EnsemblBacteria; EIM57985; EIM57985; EubceDRAFT1_2233. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000005753; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000005753}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000005753}. FT DOMAIN 199 363 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 411 AA; 45606 MW; 7EC705F2CE886E38 CRC64; MYENEQKVER MILAAVCCGE ENDTRASLRE LAALAETAGA CVVGTAIQNR DYPDPGTYMG SGKIEEIREM VIMLDADGVI CDDELSPAQM NNLENALDCR VADRTLLILD IFAGRAQTSE GKIQVELAQL KYRQAHLVGM RNYLSRLGGG IGTRGPGEKK LEIDRRLIAD RIGALGRELK EVRKHREVLR AARKKGNIRQ VAIVGYTNAG KSTLLNTMTN AGVLEEDALF ATLDPTTRIL DLPGGSQVLL TDTVGFIDKL PHALIDAFRS TLEEAAYADY IIHVADASNP RVEQQMEVVY ETLHELGADD KKIVTLFNKQ DKTDGSVRLH DHRADYVLSV SAKEGTGLED LRNVLEKIIL EEQIFVERVF PYTEAGKLAL IRQNGTLMEE EYREDGIAVK AYVPRDIYGK I // ID I5B2J0_9DELT Unreviewed; 538 AA. AC I5B2J0; DT 05-SEP-2012, integrated into UniProtKB/TrEMBL. DT 05-SEP-2012, sequence version 1. DT 07-JUN-2017, entry version 29. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=DespoDRAFT_01787 {ECO:0000313|EMBL:EIM63703.1}; OS Desulfobacter postgatei 2ac9. OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfobacterales; OC Desulfobacteraceae; Desulfobacter. OX NCBI_TaxID=879212 {ECO:0000313|EMBL:EIM63703.1, ECO:0000313|Proteomes:UP000005778}; RN [1] {ECO:0000313|EMBL:EIM63703.1, ECO:0000313|Proteomes:UP000005778} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=2ac9 {ECO:0000313|EMBL:EIM63703.1, RC ECO:0000313|Proteomes:UP000005778}; RG US DOE Joint Genome Institute (JGI-PGF); RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S., RA Peters L., Land M.L., Hauser L., Orellana R., Lovley D., Woyke T.J.; RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:EIM63703.1, ECO:0000313|Proteomes:UP000005778} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=2ac9 {ECO:0000313|EMBL:EIM63703.1, RC ECO:0000313|Proteomes:UP000005778}; RG US DOE Joint Genome Institute; RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S., RA Peters L., Ovchinnikova G., Held B., Detter J.C., Han C., Tapia R., RA Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Orellana R., RA Lovley D., Woyke T.; RT "Improved High-Quality Draft sequence of Desulfobacter postgatei RT 2ac9."; RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CM001488; EIM63703.1; -; Genomic_DNA. DR RefSeq; WP_004072942.1; NZ_CM001488.1. DR EnsemblBacteria; EIM63703; EIM63703; DespoDRAFT_01787. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000005778; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000005778}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000005778}. FT DOMAIN 378 538 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 337 371 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 538 AA; 60500 MW; 1DA4A7742F6E2999 CRC64; MKRIVYGNLD GLNKAQINRI ENLYNIKSPP EYILSPEAAI EIVDISRDIR RQVGLLLDRN GKVICVIAGE PQRIVIPVTP DYRPGPGRLK GLRCVHTHLS HEALTQDDLT DLALLRLDYI TAICLNADGT PGPVYSAHIL PDPEADPYRI LPATSLDHLD TDCQAQILEL ESELSRHNRL YSGETGQENA FLINAATEGI SSAHISMDEL KELCKTSRIK VVGSAIQQRK KIDPKFVVGK GKLSELIIKA IQNYATLLVF DQELSPSQIR SITDFVEMKV IDRTQLILDI FAKQAKSSEG KYQVELAQLE YMLPRLITKN TAMSRLTGGI GGRGPGETKL EVNRRRARER ITRLKKEIEK IRKQRKQQKA RRKRKDLPVI SIVGYTNAGK STLLNTLTQS SIIAANRLFA TLDPSSRRLR FPRDKEVIIT DTVGFIQNLP KELLEAFHAT LEELEQADVI LHVIDISNPR YMQQKETVDQ LLKSLNLNKI PTLYVFNKMD QADLSNFDSP WLLNQGILVS ALEKASLAPL VEKLEAMV // ID I5C4Y6_9RHIZ Unreviewed; 457 AA. AC I5C4Y6; DT 05-SEP-2012, integrated into UniProtKB/TrEMBL. DT 05-SEP-2012, sequence version 1. DT 07-JUN-2017, entry version 32. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=A33O_04336 {ECO:0000313|EMBL:EIM76888.1}; OS Nitratireductor aquibiodomus RA22. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Phyllobacteriaceae; Nitratireductor. OX NCBI_TaxID=1189611 {ECO:0000313|EMBL:EIM76888.1, ECO:0000313|Proteomes:UP000004622}; RN [1] {ECO:0000313|EMBL:EIM76888.1, ECO:0000313|Proteomes:UP000004622} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=RA22 {ECO:0000313|EMBL:EIM76888.1, RC ECO:0000313|Proteomes:UP000004622}; RX PubMed=23105054; DOI=10.1128/JB.01510-12; RA Singh A., Jangir P.K., Kumari C., Sharma R.; RT "Genome Sequence of Nitratireductor aquibiodomus Strain RA22."; RL J. Bacteriol. 194:6307-6307(2012). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EIM76888.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AJXZ01000007; EIM76888.1; -; Genomic_DNA. DR EnsemblBacteria; EIM76888; EIM76888; A33O_04336. DR PATRIC; fig|1189611.3.peg.891; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000004622; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000004622}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000004622}. FT DOMAIN 226 397 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 185 219 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 457 AA; 50504 MW; 63ED39EAC0916D2A CRC64; MADTRKPAEA ARGDDRLTLE PDPTRAAVIS PVLTSERRAA ESSAASSRAA EARHEEAIGL TEAIDLDVAF AEIVSVSTPR PATLLGTGKL EEIAARVEEE AVEVVIIDHP LTPVQQRNLE KALKAKVLDR TGLILEIFGR RARTKEGRLQ VDLAHLEYQR GRLVRSWTHL ERQRGGGGFM GGPGETQIEA DRRQLQERIM RLKKDLEQVR RTRDLHRAKR RKVPFPIIAI VGYTNAGKST LFNRLTGASV MAEDMLFATL DPTLRRVQLP HGTTIILSDT VGFISDLPTH LVAAFRATLE EVIEADLIVH LRDISDPDTA AQAMDVEAIL GDLGVDAADR KRVLEVWNKI DSLDPERRRA LLEGTRASDA PLAISAITGE GISDLLALIE ERISGQIVMT SIELSPDRMS LLDWIYRNGE VVERSNNDDG SISLKVRMTE TARQDVQEQL SGNKTSR // ID I5C5R7_9BACT Unreviewed; 421 AA. AC I5C5R7; DT 05-SEP-2012, integrated into UniProtKB/TrEMBL. DT 05-SEP-2012, sequence version 1. DT 07-JUN-2017, entry version 32. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=A3SI_07759 {ECO:0000313|EMBL:EIM77169.1}; OS Nitritalea halalkaliphila LW7. OC Bacteria; Bacteroidetes; Cytophagia; Cytophagales; Cyclobacteriaceae; OC Nitritalea. OX NCBI_TaxID=1189621 {ECO:0000313|EMBL:EIM77169.1, ECO:0000313|Proteomes:UP000005551}; RN [1] {ECO:0000313|EMBL:EIM77169.1, ECO:0000313|Proteomes:UP000005551} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=LW7 {ECO:0000313|EMBL:EIM77169.1, RC ECO:0000313|Proteomes:UP000005551}; RA Jangir P.K., Singh A., Shivaji S., Sharma R.; RT "Genome sequence of Nitritalea halalkaliphila LW7."; RL Submitted (MAY-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EIM77169.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AJYA01000016; EIM77169.1; -; Genomic_DNA. DR RefSeq; WP_009054448.1; NZ_AJYA01000016.1. DR EnsemblBacteria; EIM77169; EIM77169; A3SI_07759. DR PATRIC; fig|1189621.3.peg.1620; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000005551; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000005551}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000005551}. FT DOMAIN 210 399 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 421 AA; 48878 MW; 24658726214EAD59 CRC64; MSKYTRKLKK LYDTAPRQET AVLVAIIRQQ QSERQVQEYL EELAFLTETL GAKTVYQFTQ RMENPDVRTF VGSGKLEEIR AYVEHFQVDM VIFDDDLTPS QLRNLENELK VKVYDRSLLI LDIFLNRAQT AQAKTQVELA RFQYILPRLT RMWTHLERQR GGTTTRGGSG EKEIETDKRD IRSKISLLKA KLKEIEKQGV TQRKGRKGIV RVSLVGYTNV GKSTLMNLIT KTDILAENKL FATVDATVRK VVLEQIPFLL SDTVGFIRKL PTHLIESFKS TLDEIREADL LVHVVDIAHP GFEDHIAVVE QTLREIGAGD KPILLVFNKI DLISPMPTEE EMQEMSPVEL EERQFLDLQG LEELYEKKTG IQPVFMAAEH ATHVEQFRER LLEEVRKQHK RMYPHYLEDE TIDFSEWEDM E // ID I6SYF9_ENTHA Unreviewed; 403 AA. AC I6SYF9; DT 03-OCT-2012, integrated into UniProtKB/TrEMBL. DT 03-OCT-2012, sequence version 1. DT 07-JUN-2017, entry version 34. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=EHR_07840 {ECO:0000313|EMBL:AFM70502.1}; OS Enterococcus hirae (strain ATCC 9790 / DSM 20160 / JCM 8729 / LMG 6399 OS / NBRC 3181 / NCIMB 6459 / NCDO 1258). OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Enterococcaceae; OC Enterococcus. OX NCBI_TaxID=768486 {ECO:0000313|EMBL:AFM70502.1, ECO:0000313|Proteomes:UP000002895}; RN [1] {ECO:0000313|EMBL:AFM70502.1, ECO:0000313|Proteomes:UP000002895} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 9790 / DSM 20160 / JCM 8729 / LMG 6399 / NBRC 3181 / NCIMB RC 6459 / NCDO 1258 {ECO:0000313|Proteomes:UP000002895}; RX PubMed=22933757; DOI=10.1128/JB.01075-12; RA Gaechter T., Wunderlin C., Schmidheini T., Solioz M.; RT "Genome sequence of Enterococcus hirae (Streptococcus faecalis) ATCC RT 9790, a model organism for the study of ion transport, bioenergetics, RT and copper homeostasis."; RL J. Bacteriol. 194:5126-5127(2012). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP003504; AFM70502.1; -; Genomic_DNA. DR RefSeq; WP_014834488.1; NC_018081.1. DR EnsemblBacteria; AFM70502; AFM70502; EHR_07840. DR KEGG; ehr:EHR_07840; -. DR PATRIC; fig|768486.3.peg.1496; -. DR KO; K03665; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000002895; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000002895}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000002895}. FT DOMAIN 190 352 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 403 AA; 45281 MW; 8B5CC7BC447C9F5C CRC64; MIIVGVETEQ NQRYFTESMA ELSKLTNTAS GEVVFTLTQK RPQVDRQTII GKGKLQELIQ QADAHEADLI IFNHEMPPRQ SQLVSEAVGI PIIDRVQLIL DIFAMRARSK EGKLQVELAQ LEYLLPRLAG QGKSLSRLGG GIGTRGPGET KLETDRRHIR NKILGVKREL KAVEAHRARN RQKRQSSEIF QIGLIGYTNA GKSTILNLLT QADTYSKDQL FATLDPLTKK WRFAEGFEIT VTDTVGFIQD LPTQLIDAFH STLEESQSMD LLLHVVDASS PDRILQEQTV LQLMAELKME EMPVLTVYNK ADQIEPALFT PSLFPNVLIS AQSADGKEKL VQAIKQQLLE LMVPYTLFVP SQDGQTLSAL RRQTLVLKEH FVEEKNGYEV KGFAKSTSKW LNS // ID I6XYY3_PSEPQ Unreviewed; 464 AA. AC I6XYY3; DT 03-OCT-2012, integrated into UniProtKB/TrEMBL. DT 03-OCT-2012, sequence version 1. DT 07-JUN-2017, entry version 35. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:AFN46527.1}; GN OrderedLocusNames=HMPREF9154_1379 {ECO:0000313|EMBL:AFN46527.1}; OS Pseudopropionibacterium propionicum (strain F0230a) (Propionibacterium OS propionicum). OC Bacteria; Actinobacteria; Propionibacteriales; Propionibacteriaceae; OC Pseudopropionibacterium. OX NCBI_TaxID=767029 {ECO:0000313|EMBL:AFN46527.1, ECO:0000313|Proteomes:UP000003118}; RN [1] {ECO:0000313|Proteomes:UP000003118} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=F0230a {ECO:0000313|Proteomes:UP000003118}; RA Durkin A.S., Radune D., Hostetler J., Torralba M., Gillis M., RA Methe B., Sutton G., Nelson K.E.; RT "The complete genome of chromosome of Propionibacterium propionicum RT F0230a."; RL Submitted (JUL-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002734; AFN46527.1; -; Genomic_DNA. DR RefSeq; WP_014846425.1; NC_018142.1. DR EnsemblBacteria; AFN46527; AFN46527; HMPREF9154_1379. DR KEGG; ppc:HMPREF9154_1379; -. DR PATRIC; fig|767029.3.peg.1344; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000003118; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 2. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000003118}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000003118}. FT DOMAIN 246 411 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 464 AA; 50777 MW; E2A2C3337C50ECAD CRC64; MSTSLHAQPN HDGDQSELAE RHSLRRVVGM RTELEDISEV EYRQLRLERV VLVSVWTSGT QEDADNAMAE LKLLAETAGS EVLEALVQRR SQPDPATYIG RGKVEEVADV VRATGADTVI CDGELQPAQL RNLEDRIKVK VVDRTALILD IFASHAKSAE GKAQVELAQL QYLKQRLRGW GGNLSRQAGG RAAGGAGIGG RGPGETKLET DRRRIHHRIA QLRRRLREMD VTREGKRAER RRNRVPSVAI VGYTNAGKSS LLNRLTGAGV LVEDALFATL DPTTRRTETR DGRVFTLTDT VGFVRHLPHD LVEAFRSTLE ESTTADLLLH VVDASDPDPE GQIAAVRQVL AEIGASDVPE LLVCNKADRA DATTLLALRA GHPGCVVVSA RTGHGLEELA DAVEARLPNP EVWVETLIPY SRGDLMDRIH RTGTIETLEH TGEGTKVRAR VHPGLAEELG EYGV // ID I6ZY69_MELRP Unreviewed; 421 AA. AC I6ZY69; DT 03-OCT-2012, integrated into UniProtKB/TrEMBL. DT 03-OCT-2012, sequence version 1. DT 07-JUN-2017, entry version 35. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=MROS_0716 {ECO:0000313|EMBL:AFN73958.1}; OS Melioribacter roseus (strain JCM 17771 / P3M-2). OC Bacteria; Ignavibacteriae; Ignavibacteria; Ignavibacteriales; OC Melioribacteraceae; Melioribacter. OX NCBI_TaxID=1191523 {ECO:0000313|EMBL:AFN73958.1, ECO:0000313|Proteomes:UP000009011}; RN [1] {ECO:0000313|EMBL:AFN73958.1, ECO:0000313|Proteomes:UP000009011} RP NUCLEOTIDE SEQUENCE. RC STRAIN=P3M {ECO:0000313|Proteomes:UP000009011}; RX PubMed=23301019; DOI=10.1371/journal.pone.0053047; RA Kadnikov V.V., Mardanov A.V., Podosokorskaya O.A., Gavrilov S.N., RA Kublanov I.V., Beletsky A.V., Bonch-Osmolovskaya E.A., Ravin N.V.; RT "Genomic analysis of Melioribacter roseus, facultatively anaerobic RT organotrophic bacterium representing a novel deep lineage within RT Bacteriodetes/Chlorobi group."; RL PLoS ONE 8:E53047-E53047(2013). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP003557; AFN73958.1; -; Genomic_DNA. DR RefSeq; WP_014855394.1; NC_018178.1. DR EnsemblBacteria; AFN73958; AFN73958; MROS_0716. DR KEGG; mro:MROS_0716; -. DR PATRIC; fig|1191523.3.peg.749; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000009011; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000009011}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000009011}. FT DOMAIN 200 366 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 421 AA; 47938 MW; 47686275C27106DC CRC64; MIDLKNTPRE RAILIALPVG GFTKEQVEEH LDELELLAST AGAETVFKIL QDRIKPDPAY FIGKGKAEEI AQLIELNDIQ IVIFDNDLNP TQVRNLEKLF NRKILDRSGL ILDIFALHAK TREAKTQVEL AQLEYMLPRL TRAWTHLSKQ YGGIGTKGPG ETQIETDRRL IRTRISKLKE NLRKIESQQI VKSSARKKLI NATLVGYTNA GKSTLLNLLT NASVLAEDKL FATLDSTTRI FNLEKNKQIL LSDTVGFIRK LPAHLVASFK STLNVVSDAD VILHVIDASH DYFEDHIKTV DDTLRQLHCD KKLQIKIFNK IDALKEKDII NYISANYPGS YLVSAQRGIG IQKLKSALID IYEQNFVEGE LRISHTQPKK ISMVYEIAEV LDTRYEDEFV LLKYRTSKIN ENHIKKLIQH N // ID I7CLH0_NATSJ Unreviewed; 464 AA. AC I7CLH0; DT 03-OCT-2012, integrated into UniProtKB/TrEMBL. DT 03-OCT-2012, sequence version 1. DT 07-JUN-2017, entry version 34. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=NJ7G_3396 {ECO:0000313|EMBL:AFO58614.1}; OS Natrinema sp. (strain J7-2). OC Archaea; Euryarchaeota; Halobacteria; Natrialbales; Natrialbaceae; OC Natrinema. OX NCBI_TaxID=406552 {ECO:0000313|EMBL:AFO58614.1, ECO:0000313|Proteomes:UP000006507}; RN [1] {ECO:0000313|EMBL:AFO58614.1, ECO:0000313|Proteomes:UP000006507} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=J7-2 {ECO:0000313|EMBL:AFO58614.1, RC ECO:0000313|Proteomes:UP000006507}; RX PubMed=22911826; DOI=10.1371/journal.pone.0041621; RA Feng J., Liu B., Zhang Z., Ren Y., Li Y., Gan F., Huang Y., Chen X., RA Shen P., Wang L., Tang B., Tang X.F.; RT "The complete genome sequence of Natrinema sp. J7-2, a haloarchaeon RT capable of growth on synthetic media without amino acid supplements."; RL PLoS ONE 7:E41621-E41621(2012). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP003412; AFO58614.1; -; Genomic_DNA. DR EnsemblBacteria; AFO58614; AFO58614; NJ7G_3396. DR KEGG; nat:NJ7G_3396; -. DR PATRIC; fig|406552.5.peg.2978; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG093Z07D6; -. DR Proteomes; UP000006507; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000006507}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000006507}. FT DOMAIN 216 399 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 132 159 {ECO:0000256|SAM:Coils}. FT COILED 182 212 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 464 AA; 51766 MW; 330E37401E42D638 CRC64; MSASDGSRKR RAAALERARP TTPGRHETTR MNTIIAKRVD SGTADTSEIR DLARAAGYTV VGEVTQSRRA DPALQIGEGK AEELAALAAE TDATTVVFDN RLGPYQTYNL GQLLPEGVEV IDRFTLILEI FGQRAQTRKA QLQVELAELR YELPRAEAKT SLAKREEHPG FMGLGEYDES RERDIKAQIS RIKDELERIE QTEQQRRERR RDSGFDLVAL AGYTNAGKST LLRQLATDLE VAENEELHPD LDPTAESQDK LFTTLGTTTR RAAIDRRDML VTDTVGFISD LPHWLVESFK STLDSVYRAD LVLLVVDVSE SIDSIHEKLV TSHDTLYERN EAPIVTVLNK IDQVSDEELT DKREALSSLA PNPVTVSAKE GLNVDGLLER IDRELPDWEE ERLMLPMTDD TMSVVSWLHD NANVDDVTYG DEDVIVSFEA RPAVISQARS RASELRTTAA ESAS // ID I7EWL5_PHAIB Unreviewed; 423 AA. AC I7EWL5; DT 03-OCT-2012, integrated into UniProtKB/TrEMBL. DT 03-OCT-2012, sequence version 1. DT 07-JUN-2017, entry version 36. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:AFO91197.1}; GN OrderedLocusNames=PGA1_c14860 {ECO:0000313|EMBL:AFO91197.1}; OS Phaeobacter inhibens (strain ATCC 700781 / DSM 17395 / CIP 105210 / OS JCM 21319 / NBRC 16654 / NCIMB 13546 / BS107). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae; Phaeobacter. OX NCBI_TaxID=391619 {ECO:0000313|EMBL:AFO91197.1, ECO:0000313|Proteomes:UP000002914}; RN [1] {ECO:0000313|EMBL:AFO91197.1, ECO:0000313|Proteomes:UP000002914} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 17395 {ECO:0000313|EMBL:AFO91197.1, RC ECO:0000313|Proteomes:UP000002914}; RX PubMed=22717884; DOI=10.1038/ismej.2012.62; RA Thole S., Kalhoefer D., Voget S., Berger M., Engelhardt T., RA Liesegang H., Wollherr A., Kjelleberg S., Daniel R., Simon M., RA Thomas T., Brinkhoff T.; RT "Phaeobacter gallaeciensis genomes from globally opposite locations RT reveal high similarity of adaptation to surface life."; RL ISME J. 6:2229-2244(2012). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002976; AFO91197.1; -; Genomic_DNA. DR RefSeq; WP_014879946.1; NC_018290.1. DR ProteinModelPortal; I7EWL5; -. DR STRING; 391619.RGBS107_14551; -. DR EnsemblBacteria; AFO91197; AFO91197; PGA1_c14860. DR KEGG; pga:PGA1_c14860; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR KO; K03665; -. DR OMA; FNNHAHV; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000002914; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000002914}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000002914}. FT DOMAIN 203 372 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 423 AA; 47356 MW; CCE3110C7F27C987 CRC64; MEHDRTPTRA WVVHPDIKSD RDRRDPVSAL AEGVSLAEAL PDIEVIGSAV VRLPKAHAGM LFGSGKIDEL KAQFHDEEVE LVLIDGPVSP VQQRNLEKAW KVKILDRTGL ILEIFSDRAR TREGVLQVEM AALSYQRTRL VRAWTHLERQ RGGLGFVGGP GETQIEADRR AIDEQLVRLR RQLDKVVKTR TLHRAARAKI PYPIVALVGY TNAGKSTLFN RLTGAEVMAK DMLFATLDPT MRRVQLPDGP EIILSDTVGF ISDLPTELVA AFRATLEEVL AADVVVHVRD ISHDETQNQA ADVESILASL GVDDSRARLE VWNKLDLLDD EQAEARRQRA EREDGIHAIS AISGEGLEDL LADITSQLRL IRHEDEITLT FAQGKQRAWL FEQDVVQSET QTEIGFELTV LWTETQKNRF AAL // ID I7L797_9LACO Unreviewed; 426 AA. AC I7L797; DT 03-OCT-2012, integrated into UniProtKB/TrEMBL. DT 03-OCT-2012, sequence version 1. DT 07-JUN-2017, entry version 32. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=BN55_05130 {ECO:0000313|EMBL:CCI82482.1}; OS Lactobacillus hominis DSM 23910 = CRBIP 24.179. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; OC Lactobacillus. OX NCBI_TaxID=1423758 {ECO:0000313|EMBL:CCI82482.1, ECO:0000313|Proteomes:UP000009320}; RN [1] {ECO:0000313|EMBL:CCI82482.1, ECO:0000313|Proteomes:UP000009320} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CRBIP 24.179T {ECO:0000313|Proteomes:UP000009320}; RA Cousin S., Ma L., Bizet C., Loux V., Bouchier C., Clermont D., RA Creno S.; RT "Draft Genome Sequence of Lactobacillus hominis Strain CRBIP 24.179T, RT isolated from human intestine."; RL Submitted (JUN-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:CCI82482.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CAKE01000025; CCI82482.1; -; Genomic_DNA. DR RefSeq; WP_008471581.1; NZ_CAKE01000025.1. DR EnsemblBacteria; CCI82482; CCI82482; BN55_05130. DR PATRIC; fig|1423758.3.peg.1523; -. DR Proteomes; UP000009320; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000009320}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000009320}. SQ SEQUENCE 426 AA; 47858 MW; E8509A77457C358D CRC64; MIETKSKQIK AFIAGVNLKD PNFDYYMTEL RELARANNME VVGQASQNAE NIVAGTYFGV GKINQIKAMA QGLKAKALVI NDELTPTQIR NLESMTKLKV VDRTELILEI FSNRAKTKQA KLQVQLARLQ YELPRLHPSE NSLDQQRGSG GASGGFANRG SGETKLELNR RTIGKQISAI KKELKEISKQ EDVKSARRNN SRLPQVALVG YTNAGKSTTL NELLKVFSED SDKKQVFEKN MLFATLDTSV RRIDLPDDRS FILSDTVGFI SKLPHNLIES FKATLQEAKQ ADLLVNVVDS SDPNMVQMTK TTQKVLQEIG ITNVPMITAY NKADLTERQF PQIEGNDILY SAKDKDSIKE LARLISKKIF SNYEKVNLLI PLSAGKELSY MHEYGKVTKE DYEDDGIHIT AQLSPSDLIR YKKYQV // ID I7LBK0_9CORY Unreviewed; 512 AA. AC I7LBK0; DT 03-OCT-2012, integrated into UniProtKB/TrEMBL. DT 03-OCT-2012, sequence version 1. DT 07-JUN-2017, entry version 34. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:CCI83169.1}; GN ORFNames=BN46_0421 {ECO:0000313|EMBL:CCI83169.1}, GN HMPREF9719_00056 {ECO:0000313|EMBL:EJZ83017.1}; OS Turicella otitidis ATCC 51513. OC Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae; OC Turicella. OX NCBI_TaxID=883169 {ECO:0000313|EMBL:CCI83169.1, ECO:0000313|Proteomes:UP000011016}; RN [1] {ECO:0000313|EMBL:CCI83169.1, ECO:0000313|Proteomes:UP000011016} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51513 {ECO:0000313|EMBL:CCI83169.1, RC ECO:0000313|Proteomes:UP000011016}; RX PubMed=23045487; DOI=10.1128/JB.01412-12; RA Brinkrolf K., Schneider J., Knecht M., Ruckert C., Tauch A.; RT "Draft Genome Sequence of Turicella otitidis ATCC 51513, Isolated from RT Middle Ear Fluid from a Child with Otitis Media."; RL J. Bacteriol. 194:5968-5969(2012). RN [2] {ECO:0000313|EMBL:EJZ83017.1, ECO:0000313|Proteomes:UP000006078} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51513 {ECO:0000313|EMBL:EJZ83017.1, RC ECO:0000313|Proteomes:UP000006078}; RG The Broad Institute Genome Sequencing Platform; RA Earl A., Ward D., Feldgarden M., Gevers D., Huys G., Walker B., RA Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B., RA Abouelleil A., Alvarado L., Arachchi H.M., Berlin A.M., Chapman S.B., RA Goldberg J., Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., RA Larimer J., McCowen C., Montmayeur A., Murphy C., Neiman D., RA Pearson M., Priest M., Roberts A., Saif S., Shea T., Sisk P., RA Sykes S., Wortman J., Nusbaum C., Birren B.; RT "The Genome Sequence of Turicella otitidis ATCC 51513."; RL Submitted (AUG-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:CCI83169.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CAJZ01000058; CCI83169.1; -; Genomic_DNA. DR EMBL; AHAE01000003; EJZ83017.1; -; Genomic_DNA. DR RefSeq; WP_004599946.1; NZ_JH815192.1. DR EnsemblBacteria; CCI83169; CCI83169; BN46_0421. DR EnsemblBacteria; EJZ83017; EJZ83017; HMPREF9719_00056. DR PATRIC; fig|883169.3.peg.54; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000006078; Unassembled WGS sequence. DR Proteomes; UP000011016; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000006078}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000006078}. FT DOMAIN 257 426 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 216 243 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 512 AA; 54591 MW; CB9E65DB28D69967 CRC64; MARTDFGAAG ASPRGSEPTT GELDLESRNA LRHIGRGTEI TRTEQQDVYE VEYRKLRLEK VVLVGVWGDA TADEIDASMQ ELAALAETAG SEVLEILYQR RDRPDPGTYV GSGKVAELAD VVAATGADTV IADGELSPGQ LVSLEEKLNA KVIDRTMLIL DIFAQHASSK EGKAQVSLAQ LEYLFNRARG WGGNLSRQAG GRAGSNGGVG LRGPGETKIE TDRRRIRAEM ARLRKELAHM KTSREVKRAK RGGSLVPQVA VAGYTNAGKS SLINALTGAG VLVEDALFAT LDPTTRHAKL ADGRSVTFTD TVGFVRHLPT QLVESFKSSL EELLEADVMV HVVDGAAAMP LAQIEAVRSI VAEVAEDAGQ PAPPEILVVN KIDAADPVTL AELRHQLREC HFVSAATGEG IDELESAIEL FLNSLETRVR LLVPYTRGDV VSRVHRLGSV LGEDYMPDGT AIEALVPSRL ASELAEFARE NDLELTLGGA EDSAGADREE DGLGSSGEAA AS // ID I7LCU2_9LACO Unreviewed; 428 AA. AC I7LCU2; DT 03-OCT-2012, integrated into UniProtKB/TrEMBL. DT 03-OCT-2012, sequence version 1. DT 07-JUN-2017, entry version 31. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=BN53_08770 {ECO:0000313|EMBL:CCI84293.1}; OS Lactobacillus pasteurii DSM 23907 = CRBIP 24.76. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; OC Lactobacillus. OX NCBI_TaxID=1423790 {ECO:0000313|EMBL:CCI84293.1, ECO:0000313|Proteomes:UP000009311}; RN [1] {ECO:0000313|EMBL:CCI84293.1, ECO:0000313|Proteomes:UP000009311} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CRBIP 24.76T {ECO:0000313|Proteomes:UP000009311}; RA Cousin S., Bouchier C., Loux V., Ma L., Creno S., Bizet C., RA Clermont D.; RT "Draft Genome Sequence of Lactobacillus pasteurii CRBIP 24.76T."; RL Submitted (JUN-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:CCI84293.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CAKD01000001; CCI84293.1; -; Genomic_DNA. DR RefSeq; WP_009558836.1; NZ_CAKD01000001.1. DR EnsemblBacteria; CCI84293; CCI84293; BN53_08770. DR PATRIC; fig|1423790.3.peg.1410; -. DR Proteomes; UP000009311; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000009311}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000009311}. SQ SEQUENCE 428 AA; 47746 MW; AD740348F96B27FE CRC64; MIDNKPKAIK AFIAGVNLDD PNFDYYMNEL ANLVEANNME VVGQARQNLQ TIVAGTYFGV GKINEIKNMA HGLKAKVLVL NDELTPVQIR NLEKLTKLRV IDRTELILEI FASRARTKQA KLQVQLARLQ YELPRLHPSE NNLDQQRGSG GSSSGGFANR GAGESKLELN RRTIGKQISA IKKELKAVAG QEEIKASRRN QSLLPKVALV GYTNAGKSTT MNGLLKAFSD LDDDKQVFVK NMLFATLDTS VRRIDIGNNF SFILSDTVGF ISKLPHNLVE SFKATLQEAR DADLLVNVVD SSDPNMLQMI RTTQQVLEEI GAGNIPMITA YNKADLTDRS YPQIEGKDIL YSANDKKSIK MLADLISKQV FNNYEKFKLK LPLTDGKTLA YLHEHAHVIE ENYQDDGIYL VAQIAPSDQA NFQKFILN // ID I7LHQ8_9CLOT Unreviewed; 601 AA. AC I7LHQ8; DT 03-OCT-2012, integrated into UniProtKB/TrEMBL. DT 03-OCT-2012, sequence version 1. DT 07-JUN-2017, entry version 30. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=CAAU_2137 {ECO:0000313|EMBL:CCJ34221.1}; OS Caloramator australicus RC3. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Caloramator. OX NCBI_TaxID=857293 {ECO:0000313|EMBL:CCJ34221.1, ECO:0000313|Proteomes:UP000007652}; RN [1] {ECO:0000313|EMBL:CCJ34221.1, ECO:0000313|Proteomes:UP000007652} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=RC3 {ECO:0000313|EMBL:CCJ34221.1, RC ECO:0000313|Proteomes:UP000007652}; RX PubMed=21421756; DOI=10.1128/JB.00193-11; RA Ogg C.D., Patel B.K.C.; RT "Draft genome sequence of Caloramator australicus strain RC3T, a RT thermoanaerobe from the Great Artesian Basin of Australia."; RL J. Bacteriol. 193:2664-2665(2011). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:CCJ34221.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CAKP01000113; CCJ34221.1; -; Genomic_DNA. DR RefSeq; WP_008909477.1; NZ_CAKP01000113.1. DR EnsemblBacteria; CCJ34221; CCJ34221; CAAU_2137. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000007652; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000007652}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000007652}. FT DOMAIN 376 547 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 335 369 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 601 AA; 67329 MW; 94FB125BA0A0E03A CRC64; MIRGNLEGVK KSYINELEAL FEIDLDKNLI ISKDILNVLS RISWELKREI SIYINRRGKI VDIAIGDSET VNLEEIFEKR KEGGLSGIRC IHTHPSGQGE LSVVDITALV SLRFDMMVAV GVNEGKPIDF SIGLISVIDG MLSKRADILG PYEAGIIESI DALKLIREVE EKLEERVFIL EEKAKEKVIL VAAGNDDLYT VEESLEELKE LAETAGAEVV FKLYQKKSKI DPATYIGSGK AREISLLRQS LMADAVIFDD QLSPAQIRNL EEILGCKVID RTALILDIFA QRAKSKEGKL QVELAQLKYR LPRLTGFGAM LSRTGGGIGT RGPGEKKLEI DKRHIMRRIN DLEKELEAVR NTRQVQREKR LSNEIPVVSI VGYTNAGKST LRNKLCEIAG VDKEKVFEAN MLFATLDTTT RLVNLPNGKD VLISDTVGFI RKLPHELVEA FKSTLEEIIY SDLILHVVDA SNKNAEAQIK VVNSVLEEIG AGDKRKILVL NKMDIADCES LEILRGKFKD VVEISAVEGT NLDVLLKVIQ DNVYKDMIRA KLLIPYSDTK VVSYLHQNNC IEKEEYTEEG ILVCINTTKD VYGRIKEFEV E // ID I7LQV7_9LACT Unreviewed; 417 AA. AC I7LQV7; DT 03-OCT-2012, integrated into UniProtKB/TrEMBL. DT 03-OCT-2012, sequence version 1. DT 07-JUN-2017, entry version 33. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=BN193_10500 {ECO:0000313|EMBL:CCK20638.1}; OS Lactococcus raffinolactis 4877. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Lactococcus. OX NCBI_TaxID=1215915 {ECO:0000313|EMBL:CCK20638.1, ECO:0000313|Proteomes:UP000009323}; RN [1] {ECO:0000313|EMBL:CCK20638.1, ECO:0000313|Proteomes:UP000009323} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=4877 {ECO:0000313|EMBL:CCK20638.1, RC ECO:0000313|Proteomes:UP000009323}; RA Meslier V., Lechatelier E., Loux V., Renault P.; RT "Genome sequence of Lactococcus raffinolactis 4877."; RL Submitted (JUL-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:CCK20638.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CALL01000110; CCK20638.1; -; Genomic_DNA. DR RefSeq; WP_003140233.1; NZ_HE999982.1. DR EnsemblBacteria; CCK20638; CCK20638; BN193_10500. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000009323; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000009323}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000009323}. FT DOMAIN 201 361 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 167 197 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 417 AA; 46821 MW; BDE9A703A2E7BACB CRC64; MIKTEKMQEK VVLVGVETFD NNQTFEASMT ELASLAATAG AVVTTVFTQK KERLDGKYLV GIGKLQEIKD NLEADEADMV IFNEKLTPRQ NVNLEGFLGV KVIDRMQLIL DIFALRARSH VGMLQVELAQ LKYLLPRLSG SKGLELSRQA GGIGSRGAGE SQLETDRRHI RHRLEIIEAQ LKKAEKVQEN SRQKRNQSSI FKLGLIGYTN AGKSSVFNDL TQKIQYEQDE LFATLDATTK DFSLQDEFTV TLTDTVGFIQ DLPTELVQAF KSTLEESKNV DLLLHVIDAS DSNHKIHEDV VESIMKDLEM SDIAVLTIYN KLDLADDFAP TILPNVQIST KSEVGVQQLR QAIIAKIKEL FVPFELTLPY EAAYRLPMLR KIALIDTVVA EDETETYHVS GSISEREKWR LVEDGLC // ID I7Z986_9GAMM Unreviewed; 423 AA. AC I7Z986; DT 03-OCT-2012, integrated into UniProtKB/TrEMBL. DT 03-OCT-2012, sequence version 1. DT 07-JUN-2017, entry version 31. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=WQQ_46670 {ECO:0000313|EMBL:EIT68232.1}; OS Hydrocarboniphaga effusa AP103. OC Bacteria; Proteobacteria; Gammaproteobacteria; Nevskiales; OC Sinobacteraceae; Hydrocarboniphaga. OX NCBI_TaxID=1172194 {ECO:0000313|EMBL:EIT68232.1, ECO:0000313|Proteomes:UP000003704}; RN [1] {ECO:0000313|EMBL:EIT68232.1, ECO:0000313|Proteomes:UP000003704} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=AP103 {ECO:0000313|EMBL:EIT68232.1, RC ECO:0000313|Proteomes:UP000003704}; RX PubMed=22933753; DOI=10.1128/JB.01017-12; RA Chang H.K., Zylstra G.J., Chae J.C.; RT "Genome Sequence of n-Alkane-Degrading Hydrocarboniphaga effusa Strain RT AP103T (ATCC BAA-332T)."; RL J. Bacteriol. 194:5120-5120(2012). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EIT68232.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AKGD01000004; EIT68232.1; -; Genomic_DNA. DR EnsemblBacteria; EIT68232; EIT68232; WQQ_46670. DR PATRIC; fig|1172194.4.peg.4527; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000003704; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000003704}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000003704}. FT DOMAIN 184 351 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 423 AA; 47039 MW; 60AE9661354A7BCB CRC64; MASAASSDYE SDRREFEDLA RSAGADVLLL IGGSRQRPDA GLYIGSGKAD EVAAAVAAGG AELAIFNHDL SPSQERNLEK ILRCRVLDRA GLILDIFARR ARSHEGKLQV ELAQLRHLRT RLVRGWTHLE RQKGGIGMRG PGETQLETDR RLIDDKIVTL RRHLEEVRAR RAQNRNSRKR NEVPSVSLVG YTNAGKSSLF NAMTGDDTYA SSKLFATLDT TVRRLDLPEG EPAVLADTVG FIRDLPHDLI AAFRATLEES RESDLLLHVT DASDPERMAR IEQVNAVLHE IGADEVPRLQ VFNKIDLRED ETARIERDDS GLAVRVYVSA QTGAGLDLLK AAIVERIRPG LPEFLILVPP HAARLRAQLF ELRAVRREQI EEDGSVHLTV SLAYERLRGL CVAAGLEPPP EPRMLEEWES SNR // ID I8RG56_9FIRM Unreviewed; 599 AA. AC I8RG56; DT 03-OCT-2012, integrated into UniProtKB/TrEMBL. DT 03-OCT-2012, sequence version 1. DT 07-JUN-2017, entry version 32. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=FB4_3398 {ECO:0000313|EMBL:EIW18578.1}; OS Pelosinus fermentans B4. OC Bacteria; Firmicutes; Negativicutes; Selenomonadales; Sporomusaceae; OC Pelosinus. OX NCBI_TaxID=1149862 {ECO:0000313|EMBL:EIW18578.1, ECO:0000313|Proteomes:UP000004324}; RN [1] {ECO:0000313|EMBL:EIW18578.1, ECO:0000313|Proteomes:UP000004324} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=B4 {ECO:0000313|EMBL:EIW18578.1}; RX PubMed=22933770; DOI=10.1128/JB.01174-12; RA Brown S.D., Podar M., Klingeman D.M., Johnson C.M., Yang Z.K., RA Utturkar S.M., Land M.L., Mosher J.J., Hurt R.A.Jr., Phelps T.J., RA Palumbo A.V., Arkin A.P., Hazen T.C., Elias D.A.; RT "Draft Genome Sequences for Two Metal-Reducing Pelosinus fermentans RT Strains Isolated from a Cr(VI)-Contaminated Site and for Type Strain RT R7."; RL J. Bacteriol. 194:5147-5148(2012). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EIW18578.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AKVJ01000025; EIW18578.1; -; Genomic_DNA. DR RefSeq; WP_007934294.1; NZ_AKVJ01000025.1. DR EnsemblBacteria; EIW18578; EIW18578; FB4_3398. DR PATRIC; fig|1149862.3.peg.2363; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000004324; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000004324}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000004324}. FT DOMAIN 376 541 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 599 AA; 67302 MW; DB45048D0916D00D CRC64; MTTIYGDVNG IRKSIINRLE ELYEFTIPFG QVITNELAQK LIDLTDDLNR ELVVYITRKG QVTCVAVGDV YTVILPEVDG RRSVNRLSGI RCIHTHPSGE TELSGVDIAS LKEMRFDLMA ALGRKDEMIQ ASFGIITNIE NDQFNTQMIG PLSIDEFIEL DITYLTAQIE RQLDLNTKTS AIAEPERALL VGVERQGKWR ITDSLKELAQ LAETAGAEVL GMTWQKRDRP DSALFIGRGK VQEISLLRQE KNVNLIIFDD ELSPAQQRNL EKALGIKVLD RTALILDIFA QRARSHEGKL QVELAQLRYN LPRLGGQGLV LSRLGGGIGT RGPGETKLEV DRRRIRERVS DITKQIEYIK KQRNLHRKRR ETTRIPTIAL VGYTNAGKST LLNLLTASEV LAEDKLFATL DPTTRNITLT NGQQALITDT VGFIQKLPHQ LIAAFRATLE EVVQADILLH VVDVSHPQYQ EQSHAVFQVL HELNVDIKQL ITIFNKADKV EDSNSVSALL KTENSVMISA LHGHGIEGLL LLIENAIKQK TIEMHLLIPY DESNVIAKLY DISNVHSTEY REDGIYVSIS LSPDQTNYFN RYAIGVEQE // ID I8UJ26_9BACI Unreviewed; 410 AA. AC I8UJ26; DT 03-OCT-2012, integrated into UniProtKB/TrEMBL. DT 03-OCT-2012, sequence version 1. DT 07-JUN-2017, entry version 32. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=A374_04929 {ECO:0000313|EMBL:EIT86890.1}; OS Fictibacillus macauensis ZFHKF-1. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Fictibacillus. OX NCBI_TaxID=1196324 {ECO:0000313|EMBL:EIT86890.1, ECO:0000313|Proteomes:UP000004080}; RN [1] {ECO:0000313|EMBL:EIT86890.1, ECO:0000313|Proteomes:UP000004080} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ZFHKF-1 {ECO:0000313|EMBL:EIT86890.1, RC ECO:0000313|Proteomes:UP000004080}; RX PubMed=22887677; DOI=10.1128/JB.01049-12; RA Cai L., Zhang T.; RT "Genome of Bacillus macauensis ZFHKF-1, a Long-Chain-Forming RT Bacterium."; RL J. Bacteriol. 194:4780-4780(2012). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EIT86890.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AKKV01000020; EIT86890.1; -; Genomic_DNA. DR EnsemblBacteria; EIT86890; EIT86890; A374_04929. DR PATRIC; fig|1196324.3.peg.1001; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000004080; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000004080}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000004080}. FT DOMAIN 202 361 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 410 AA; 46564 MW; 43003AC5ADF0F097 CRC64; MEEIIHVPNE KAILVGCQLP RQSDERFFYS MEELQSLIKT ANGTAVVTVT QKRERYDAST FIGKGKIEEI KALQEELEAD IIVFNDELTP AQNRNLSRFF DVLVIDRTQL ILDIFATRAQ SREGKLQVEL AQLQYLLPRL SGMGVSLSRL GAGIGTRGPG ETKLEKDRRH IRSRITEIKH QLQDIVHHRD RYRERRKENQ SIQVALVGYT NAGKSTLFNG LTEADSYEEN LLFATLDPLT RKMKLPSGFQ VLVSDTVGFI QDLPTSLIAA FRSTLEEAKE ADLLLHVVDG SALDREQHEQ TVHSILKELK ASHLPMVTLY NKRDKGTGPF VPPEAFAISA INEQDIKKVK QLLEEKLKEQ LHYYHIYVSA SDGRKLALLR SHTLLTYQQF DEESGSYECK GYAPSSMKLH // ID I9BQT1_9RALS Unreviewed; 427 AA. AC I9BQT1; DT 03-OCT-2012, integrated into UniProtKB/TrEMBL. DT 03-OCT-2012, sequence version 1. DT 07-JUN-2017, entry version 29. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=MW7_3466 {ECO:0000313|EMBL:EIZ02131.1}; OS Ralstonia sp. PBA. OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Ralstonia. OX NCBI_TaxID=795666 {ECO:0000313|EMBL:EIZ02131.1, ECO:0000313|Proteomes:UP000004277}; RN [1] {ECO:0000313|EMBL:EIZ02131.1, ECO:0000313|Proteomes:UP000004277} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=PBA {ECO:0000313|EMBL:EIZ02131.1, RC ECO:0000313|Proteomes:UP000004277}; RA Gan H.M., Yahya A.; RT "Draft Genome of Ralstonia sp. PBA."; RL Submitted (MAY-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EIZ02131.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AKCV01000043; EIZ02131.1; -; Genomic_DNA. DR EnsemblBacteria; EIZ02131; EIZ02131; MW7_3466. DR PATRIC; fig|795666.3.peg.3441; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000004277; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000004277}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000004277}. FT DOMAIN 223 393 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 189 216 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 427 AA; 47137 MW; 4F77ED3158E4497E CRC64; MCAADAGTPP PFPTLPDPIP RLQSQSTSQT EPIRAILVGV DFGKHDFQES LNELALLATT AGSLPVYTLT GKRQRPDPAL YIGSGKAEEL RTAADAYDAE IIIFNHALSP AQQRNLERFT GRYVLDRTGL ILDIFGQRAQ SHVGKVQVEL AQVQYRASRL VRAWSHLERQ KGGIGMRGGP GERQIELDRR MLDERAKRLK SDLTRLQRQH DTQRRARTRN EAFNVSLVGY TNAGKSTLFN SLTKARAYAA DQLFATLDTT SRRLYLEGLG NVVLSDTVGF IRDLPTQLVA AFRATLEETV HADLLLHVVD GSSPVRHEQI QQVNRVLEEI DALGIPQIVV INKIDAAPEL LVQGPHLERD ETGFPARVFV SAREGLGLEL LRDAIVKAAT RLREEAAAGR PPAEPDPRFM QQSPLSNHAI PAIPGED // ID I9DRP6_9ALTE Unreviewed; 430 AA. AC I9DRP6; DT 03-OCT-2012, integrated into UniProtKB/TrEMBL. DT 03-OCT-2012, sequence version 1. DT 30-AUG-2017, entry version 33. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=AGRI_08015 {ECO:0000313|EMBL:EIW88715.1}; OS Alishewanella agri BL06. OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales; OC Alteromonadaceae; Alishewanella. OX NCBI_TaxID=1195246 {ECO:0000313|EMBL:EIW88715.1, ECO:0000313|Proteomes:UP000035062}; RN [1] {ECO:0000313|EMBL:EIW88715.1, ECO:0000313|Proteomes:UP000035062} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BL06 {ECO:0000313|EMBL:EIW88715.1, RC ECO:0000313|Proteomes:UP000035062}; RX PubMed=22933763; DOI=10.1128/JB.01129-12; RA Kim J., Jung J., Sung J.S., Chun J., Park W.; RT "Genome Sequence of Pectin-Degrading Alishewanella agri, Isolated from RT Landfill Soil."; RL J. Bacteriol. 194:5135-5136(2012). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EIW88715.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AKKU01000015; EIW88715.1; -; Genomic_DNA. DR RefSeq; WP_008984469.1; NZ_AKKU01000015.1. DR EnsemblBacteria; EIW88715; EIW88715; AGRI_08015. DR PATRIC; fig|1195246.3.peg.1574; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000035062; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000035062}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000035062}. FT DOMAIN 197 363 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 430 AA; 48141 MW; 795538D286E70D6D CRC64; MFDLAEPAEQ AVLVHVNFPQ EHSTEDLQEL RMLVASAGVV VLGELSCSRQ APDAKLFIGS GKAAELAALV ADTGATVVIF NNELSPSQTR NLERLCQARV IDRTSLILDI FAQRARTYEG KLQVELAQLQ HLASRLIRGF DNERQKGGIG LRGPGETRLE TDRRLLRDRV KALKIRLDKL GRQREQGRRA RQRSEQPVLS IVGYTNAGKS TLFNRLTTAE VYAADQLFAT LDPTLRRIEL PQFGEAILAD TVGFIRHLPH DLVAAFKSTL QETRDADLQL HVIDAADARR AENMRQVQLV LTEIDAAEVP QLLVYNKIDQ LAQSPRIDYN EQGLPEAVWL SAKTGAGLDL LQQAVIQLLS QQHLQLVLRL PPRLSQIRAQ LFALQAVQHE QYQEDGSCEL SLKITAANWA RLLKQCEQPL ENYIVRPPVF // ID I9S806_9BACE Unreviewed; 421 AA. AC I9S806; DT 03-OCT-2012, integrated into UniProtKB/TrEMBL. DT 03-OCT-2012, sequence version 1. DT 07-JUN-2017, entry version 31. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=HMPREF1068_01025 {ECO:0000313|EMBL:EIY51478.1}; OS Bacteroides nordii CL02T12C05. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae; OC Bacteroides. OX NCBI_TaxID=997884 {ECO:0000313|EMBL:EIY51478.1, ECO:0000313|Proteomes:UP000003089}; RN [1] {ECO:0000313|EMBL:EIY51478.1, ECO:0000313|Proteomes:UP000003089} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CL02T12C05 {ECO:0000313|EMBL:EIY51478.1, RC ECO:0000313|Proteomes:UP000003089}; RG The Broad Institute Genome Sequencing Platform; RA Earl A., Ward D., Feldgarden M., Gevers D., Zitomersky N.L., RA Coyne M.J., Comstock L.E., Young S.K., Zeng Q., Gargeya S., RA Fitzgerald M., Haas B., Abouelleil A., Alvarado L., Arachchi H.M., RA Berlin A., Chapman S.B., Gearin G., Goldberg J., Griggs A., Gujja S., RA Hansen M., Heiman D., Howarth C., Larimer J., Lui A., RA MacDonald P.J.P., McCowen C., Montmayeur A., Murphy C., Neiman D., RA Pearson M., Priest M., Roberts A., Saif S., Shea T., Sisk P., RA Stolte C., Sykes S., Wortman J., Nusbaum C., Birren B.; RT "The Genome Sequence of Bacteroides nordii CL02T12C05."; RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EIY51478.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGXS01000015; EIY51478.1; -; Genomic_DNA. DR RefSeq; WP_007483990.1; NZ_JH724314.1. DR EnsemblBacteria; EIY51478; EIY51478; HMPREF1068_01025. DR PATRIC; fig|997884.3.peg.1039; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000003089; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000003089}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000003089}. FT DOMAIN 217 401 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 421 AA; 48041 MW; E9FAE51199CAB343 CRC64; MKEFVISEAQ VETAVLVGLI TQTQDERKTK EYLDELEFLA ETAGAEVVKK FTQKLPTANS VTYVGKGKLE EIKEYILNEE ENEREVGMVI FDDELSAKQI RNIEAELKIK ILDRTSLILD IFAMRAQTAN AKTQVELAQY KYMLPRLQRL WTHLERQGGG SGSGSGKGGS VGLRGPGETQ LEMDRRIILN RMSLLKERLA EIDKQKSTQR KNRGRMIRVA LVGYTNVGKS TIMNLLAKSE VFAENKLFAT LDTTVRKVII ENLPFLLSDT VGFIRKLPTD LVDSFKSTLD EVREADLLLH VVDISHPGFE EQIEVVNKTL ADIGGAGKPM ILIFNKIDAY TYIEKAVDDL TPKTKENLTL EELMKTWMAK VEDNCLFISA RERINIEELK SVVYKRVKEL HVQKYPYNDF LYQTYEEEEE E // ID I9WJ81_9SPHN Unreviewed; 447 AA. AC I9WJ81; DT 03-OCT-2012, integrated into UniProtKB/TrEMBL. DT 03-OCT-2012, sequence version 1. DT 05-JUL-2017, entry version 33. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=WSK_1134 {ECO:0000313|EMBL:EIZ80341.1}; OS Novosphingobium sp. Rr 2-17. OC Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales; OC Sphingomonadaceae; Novosphingobium. OX NCBI_TaxID=555793 {ECO:0000313|EMBL:EIZ80341.1, ECO:0000313|Proteomes:UP000004732}; RN [1] {ECO:0000313|EMBL:EIZ80341.1, ECO:0000313|Proteomes:UP000004732} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=RR2-17 {ECO:0000313|Proteomes:UP000004732}; RX PubMed=22933764; DOI=10.1128/JB.01159-12; RA Gan H.M., Chew T.H., Hudson A.O., Savka M.A.; RT "Genome Sequence of Novosphingobium sp. Strain Rr 2-17, a Nopaline RT Crown Gall-Associated Bacterium Isolated from Vitis vinifera L. RT Grapevine."; RL J. Bacteriol. 194:5137-5138(2012). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EIZ80341.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AKFJ01000014; EIZ80341.1; -; Genomic_DNA. DR EnsemblBacteria; EIZ80341; EIZ80341; WSK_1134. DR PATRIC; fig|555793.3.peg.1137; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000004732; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000004732}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000004732}. FT DOMAIN 206 391 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 447 AA; 49083 MW; 964FA95F1F6A407C CRC64; MNDEPTGEVT HGARAFVVYP QMRGRGNLDP ASRLEEAKGL ALAIGLVVAD AITIPIREPR AGTLFGEGQI ENIAIGCTQN DAELVIVDGA LTAIQQRNLE EKLKRKVIDR TGLILEIFGE RAATAEGRLQ VELAHLDYQA GRLVRSWTHL ERQRGGFGFL GGPGETQIEA DRRLIRDRMA KIRRELEQVR RTRGLHRERR EKAPWPVIAL VGYTNAGKST LFNRLTGASV MAQDLLFATL DPTMRAIRLP GVEKGILSDT VGFISDLPTQ LVAAFRATLE EVTAADVILH VRDIANADTD VQKRQVLDVL ADLGVVPGEA DLKKTTETAS EPLIPIIEVW NKWDLLEPDH AHELRQAAAR SEQTIVPLSA LTGEGCDNLL EVVGHKLTLE AKLCTFLIPA ADGQRLAFLH ARGDVVDEEN AGEGADGPLL RLHVRMTERE LGRFQAL // ID J0D3T7_9BIFI Unreviewed; 542 AA. AC J0D3T7; DT 03-OCT-2012, integrated into UniProtKB/TrEMBL. DT 03-OCT-2012, sequence version 1. DT 07-JUN-2017, entry version 32. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=HMPREF9156_01090 {ECO:0000313|EMBL:EJD64595.1}; OS Scardovia wiggsiae F0424. OC Bacteria; Actinobacteria; Bifidobacteriales; Bifidobacteriaceae; OC Scardovia. OX NCBI_TaxID=857290 {ECO:0000313|EMBL:EJD64595.1, ECO:0000313|Proteomes:UP000006415}; RN [1] {ECO:0000313|EMBL:EJD64595.1, ECO:0000313|Proteomes:UP000006415} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=F0424 {ECO:0000313|EMBL:EJD64595.1, RC ECO:0000313|Proteomes:UP000006415}; RG The Broad Institute Genome Sequencing Platform; RA Earl A., Ward D., Feldgarden M., Gevers D., Izard J., Ganesan A., RA Baranova O.V., Blanton J.M., Tanner A.C., Mathney J., Dewhirst F.E., RA Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B., RA Abouelleil A., Alvarado L., Arachchi H.M., Berlin A., Chapman S.B., RA Gearin G., Goldberg J., Griggs A., Gujja S., Hansen M., Heiman D., RA Howarth C., Larimer J., Lui A., MacDonald P.J.P., McCowen C., RA Montmayeur A., Murphy C., Neiman D., Pearson M., Priest M., RA Roberts A., Saif S., Shea T., Sisk P., Stolte C., Sykes S., RA Wortman J., Nusbaum C., Birren B.; RT "The Genome Sequence of Scardovia wiggsiae F0424."; RL Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EJD64595.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGZS01000006; EJD64595.1; -; Genomic_DNA. DR RefSeq; WP_007148153.1; NZ_JH719940.1. DR EnsemblBacteria; EJD64595; EJD64595; HMPREF9156_01090. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000006415; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000006415}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000006415}. FT DOMAIN 296 462 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 542 AA; 58616 MW; F5E714AABE3CB587 CRC64; MTENRNRQLN KSKASYKSTR KAGRRNTDLG SVLDSQSEIL LNSAHAGSRS NGAIARQQDD EGWKEREGRN ELKRVTGLGE LEDVTEVEYR RIRLERVVLV GVWSSRETTQ AQAEESLREL AALARTAGAQ VMEGVLQHRF KPDPATYVGK GKANEIAAIV AATDSDTIIV DADLPPSQRR ALEDVAKVKV VDRTAVILDI FAQHATSREG KAQVELAQLE YMLPRLRGWG AALSRQAGGQ SAGANGGIGS RGPGETQIEL DRRVIRTRMA RLRRQIARMA PARDIKRGSR RRNSLPTVAV VGYTNAGKSS LINRLTRSHE LVENALFATL DTAVRHSEAA NGRRFMYVDT VGFVRQLPTQ LIEAFKSTLE EAAGASVIIH VVDASHPNPF SQIDAVNDVL QDIPGIEGTP ALIVFNKIDC IDEAALQRLK NLVPDAFFIS ALTEEGIDAL RKAVESRLPQ PGVHVDAVIP YTRGDLVSRA RQFGSVGQVE YGDTGIHLTA DVDSRLAAHI VASAEVAASA NGASHDTAGI SSADHSVSGF AG // ID J0QSI5_9RHIZ Unreviewed; 456 AA. AC J0QSI5; DT 03-OCT-2012, integrated into UniProtKB/TrEMBL. DT 03-OCT-2012, sequence version 1. DT 07-JUN-2017, entry version 33. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=ME5_01382 {ECO:0000313|EMBL:EJF88831.1}; OS Bartonella tamiae Th239. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Bartonellaceae; Bartonella. OX NCBI_TaxID=1094558 {ECO:0000313|EMBL:EJF88831.1, ECO:0000313|Proteomes:UP000008952}; RN [1] {ECO:0000313|EMBL:EJF88831.1, ECO:0000313|Proteomes:UP000008952} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Th239 {ECO:0000313|EMBL:EJF88831.1, RC ECO:0000313|Proteomes:UP000008952}; RG The Broad Institute Genome Sequencing Platform; RG The Broad Institute Genome Sequencing Center for Infectious Disease; RA Feldgarden M., Kirby J., Kosoy M., Birtles R., Probert W.S., RA Chiaraviglio L., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., RA Haas B., Abouelleil A., Alvarado L., Arachchi H.M., Berlin A., RA Chapman S.B., Gearin G., Goldberg J., Griggs A., Gujja S., Hansen M., RA Heiman D., Howarth C., Larimer J., Lui A., MacDonald P.J.P., RA McCowen C., Montmayeur A., Murphy C., Neiman D., Pearson M., RA Priest M., Roberts A., Saif S., Shea T., Sisk P., Stolte C., Sykes S., RA Wortman J., Nusbaum C., Birren B.; RT "The Genome Sequence of Bartonella tamiae Th239."; RL Submitted (MAR-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EJF88831.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AIMB01000008; EJF88831.1; -; Genomic_DNA. DR RefSeq; WP_008039705.1; NZ_JH725147.1. DR EnsemblBacteria; EJF88831; EJF88831; ME5_01382. DR PATRIC; fig|1094558.3.peg.1484; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000008952; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000008952}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000008952}. FT DOMAIN 218 390 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 177 204 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 456 AA; 51800 MW; 7978FD3540D570F3 CRC64; MTKEIERADK LISRETAATR AIVIIPLLRE RVSEDRRNIR SVQSKIDEAI GLAQAIRLDV VEHHKVTMNT LRPATLLGPG KVEEFSRIIE DKEIDLAIID RGLTPVQQRN LEKFWNCKVI DRTALILEIF GDRAATKEGV LQVELAHLNY QKGRLVRSWT HLERQRGGGG FLGGPGETQI ESDRRQLQDK IVRIKRELDT VVKTRALHRA KRKKTSHPVI ALVGYTNAGK STLFNQLTGA NVLAKDMLFA TLDPTLRRIT LPHGQLVILS DTVGFISNLP THLIAAFRAT LEEVIEADLI LHVRDMSDPD HYIHAQDVRD ILKSLGVDID DHNHIFEIWN KTDLLDDISR ETLKETARNA ANYAFLVSAL KGEGLLELEK AIERQISGEM IQHNIRLKAE DFALLDWIYK NVGNIERHNE DDGSIVLKFV ITQEIDKRLN NLLETHGYQT KNTDKL // ID J0UET8_9BURK Unreviewed; 392 AA. AC J0UET8; DT 03-OCT-2012, integrated into UniProtKB/TrEMBL. DT 03-OCT-2012, sequence version 1. DT 07-JUN-2017, entry version 32. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=PMI14_00444 {ECO:0000313|EMBL:EJE54637.1}; OS Acidovorax sp. CF316. OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Comamonadaceae; Acidovorax. OX NCBI_TaxID=1144317 {ECO:0000313|EMBL:EJE54637.1, ECO:0000313|Proteomes:UP000004811}; RN [1] {ECO:0000313|EMBL:EJE54637.1, ECO:0000313|Proteomes:UP000004811} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CF316 {ECO:0000313|EMBL:EJE54637.1, RC ECO:0000313|Proteomes:UP000004811}; RX PubMed=23045501; DOI=10.1128/JB.01243-12; RA Brown S.D., Utturkar S.M., Klingeman D.M., Johnson C.M., Martin S.L., RA Land M.L., Lu T.Y., Schadt C.W., Doktycz M.J., Pelletier D.A.; RT "Twenty-one genome sequences from Pseudomonas species and 19 genome RT sequences from diverse bacteria isolated from the rhizosphere and RT endosphere of Populus deltoides."; RL J. Bacteriol. 194:5991-5993(2012). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EJE54637.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AKJX01000016; EJE54637.1; -; Genomic_DNA. DR RefSeq; WP_007848872.1; NZ_AKJX01000016.1. DR EnsemblBacteria; EJE54637; EJE54637; PMI14_00444. DR PATRIC; fig|1144317.3.peg.409; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000004811; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000004811}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000004811}. FT DOMAIN 203 376 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 392 AA; 43145 MW; DF9404A82397AC7E CRC64; MSAPASSDAG GGASVLLVGV DFGLPHFDGE LEELGLLAQT AGLNPVARLT CKRKAPDAAL FVGSGKADEI RTLAQMHGAV EVLFDQSLSP AQQRNLERHL ELPVSDRTFL ILEIFAQRAR SHEGKLQVEL ARLQYLSTRL VRRWSHLERQ TGGIGARGGP GEKQIELDRR MIGEAIKRTR ERLSKVKRQR STQRRQRDRR DTFTISLVGY TNAGKSTLFN ALVKARAYAA DQLFATLDTT TRQLYLGDAG RSVSLSDTVG FIRDLPHGLV DAFQATLQEA VDADLLLHVV DASNPHFPEQ MDQVQRVLHE IGAADIPQLL VFNKLDALDA EQQPALLEDQ YEVEGQMVPR LFVSARSGQG LDNLRRVLSA RVLEAREDMT PADAAPLPAH EG // ID J0V1C4_STREE Unreviewed; 175 AA. AC J0V1C4; DT 03-OCT-2012, integrated into UniProtKB/TrEMBL. DT 03-OCT-2012, sequence version 1. DT 07-JUN-2017, entry version 16. DE SubName: Full=GTP-binding protein {ECO:0000313|EMBL:EJG45041.1}; GN ORFNames=AMCSP13_000797 {ECO:0000313|EMBL:EJG45041.1}; OS Streptococcus pneumoniae 2070335. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=914141 {ECO:0000313|EMBL:EJG45041.1, ECO:0000313|Proteomes:UP000002642}; RN [1] {ECO:0000313|EMBL:EJG45041.1, ECO:0000313|Proteomes:UP000002642} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=2070335 {ECO:0000313|EMBL:EJG45041.1, RC ECO:0000313|Proteomes:UP000002642}; RA Piet J.R., van Schaik B.D.C., Brouwer M.C., Jakobs M.E., RA Zwinderman A.H., van Kampen A.H.C., Bass F., van der Ende A., RA van de Beek D.; RT "Pneumococcal Genome sequencing reveals virulence genes associated RT with mortality in patients with community-acquired pneumococcal RT meningitis."; RL Submitted (JUN-2012) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EJG45041.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ALBB01000005; EJG45041.1; -; Genomic_DNA. DR EnsemblBacteria; EJG45041; EJG45041; AMCSP13_000797. DR PATRIC; fig|914141.3.peg.793; -. DR BioCyc; SPNE914141:G12BK-204-MONOMER; -. DR Proteomes; UP000002642; Unassembled WGS sequence. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. PE 4: Predicted; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000002642}. FT DOMAIN 1 86 GTP-bdg_N. {ECO:0000259|Pfam:PF13167}. FT DOMAIN 88 164 GTP-bdg_M. {ECO:0000259|Pfam:PF16360}. FT COILED 131 165 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 175 AA; 19702 MW; 5FEB018854B13403 CRC64; MEELASLAKT AGAVVVDSYR QKREKYDSKT FVGSGKLEEI ALMVDAEEIT TVIVNNRLTP RQNVNLEEVL GVKVIDRMQL ILDIFAMRAR SHEGKLQVHL AQLKYLLPRL VGQGIMLSRQ AGGIGSRGPG ESQLELNRRS VRNQITDIER QLKVVEKNRA TVRENVWSLA LLRLV // ID J1FKR7_9BACT Unreviewed; 340 AA. AC J1FKR7; DT 03-OCT-2012, integrated into UniProtKB/TrEMBL. DT 03-OCT-2012, sequence version 1. DT 07-JUN-2017, entry version 23. DE SubName: Full=GTP-binding protein HflX {ECO:0000313|EMBL:EJF10931.1}; DE Flags: Fragment; GN ORFNames=O71_06262 {ECO:0000313|EMBL:EJF10931.1}; OS Pontibacter sp. BAB1700. OC Bacteria; Bacteroidetes; Cytophagia; Cytophagales; Hymenobacteraceae; OC Pontibacter. OX NCBI_TaxID=1144253 {ECO:0000313|EMBL:EJF10931.1, ECO:0000313|Proteomes:UP000003746}; RN [1] {ECO:0000313|EMBL:EJF10931.1, ECO:0000313|Proteomes:UP000003746} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BAB1700 {ECO:0000313|EMBL:EJF10931.1, RC ECO:0000313|Proteomes:UP000003746}; RX PubMed=23105068; DOI=10.1128/JB.01550-12; RA Joshi M.N., Sharma A.C., Pandya R.V., Patel R.P., Saiyed Z.M., RA Saxena A.K., Bagatharia S.B.; RT "Draft Genome Sequence of Pontibacter sp. nov. BAB1700, a RT Halotolerant, Industrially Important Bacterium."; RL J. Bacteriol. 194:6329-6330(2012). CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EJF10931.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AKIS01000039; EJF10931.1; -; Genomic_DNA. DR RefSeq; WP_007654105.1; NZ_AKIS01000039.1. DR EnsemblBacteria; EJF10931; EJF10931; O71_06262. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000003746; Unassembled WGS sequence. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000003746}; KW Reference proteome {ECO:0000313|Proteomes:UP000003746}. FT DOMAIN 204 340 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT NON_TER 340 340 {ECO:0000313|EMBL:EJF10931.1}. SQ SEQUENCE 340 AA; 38744 MW; A8EF90792E55B003 CRC64; MGKQKYYETA KPQETAVLVA VPGYKQTDEQ TNEYLDELAF LTETAGAVAM KRFVQKLDKP DTRTFVGSGK LEEIQAYVKE HNIDMVIFDD DLSPSQVRNI ERELQVKIVD RSLLILDIFA LRAKTAQAHT QVELAQYQYL LPRLTNLWTH LSKQKGGIGM KGPGETEIET DRRIVRDKIS LLRDRLEKFE KQNFEQRKSR AGMVRVALVG YTNVGKSTLM NLLSKSDVFA ENKLFATVDA TVRKVVLDNI PFLLSDTVGF IRKLPTKLIE AFKSTLDEIR EADLLVHVVD VSHPSFEDHI AVVNDTLLDI KSADKPVLLV FNKIDQYLEQ REQEMQEESG // ID J1H2Q0_9ACTO Unreviewed; 539 AA. AC J1H2Q0; DT 03-OCT-2012, integrated into UniProtKB/TrEMBL. DT 03-OCT-2012, sequence version 1. DT 07-JUN-2017, entry version 30. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:EJF39533.1}; GN ORFNames=HMPREF1318_0064 {ECO:0000313|EMBL:EJF39533.1}; OS Actinomyces massiliensis F0489. OC Bacteria; Actinobacteria; Actinomycetales; Actinomycetaceae; OC Actinomyces. OX NCBI_TaxID=1125718 {ECO:0000313|EMBL:EJF39533.1, ECO:0000313|Proteomes:UP000002941}; RN [1] {ECO:0000313|EMBL:EJF39533.1, ECO:0000313|Proteomes:UP000002941} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=F0489 {ECO:0000313|EMBL:EJF39533.1, RC ECO:0000313|Proteomes:UP000002941}; RA Harkins D.M., Madupu R., Durkin A.S., Torralba M., Methe B., RA Sutton G.G., Nelson K.E.; RL Submitted (MAY-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EJF39533.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AKFT01000177; EJF39533.1; -; Genomic_DNA. DR RefSeq; WP_008732780.1; NZ_AKFT01000177.1. DR EnsemblBacteria; EJF39533; EJF39533; HMPREF1318_0064. DR PATRIC; fig|1125718.3.peg.2232; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000002941; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 2. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000002941}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000002941}. FT DOMAIN 308 474 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 539 AA; 57303 MW; 2955AEF31D0547A5 CRC64; MNESRTPDTA ASAGPDDLYT GADGVDRADD AAPTAEDVVA RILSRAGTAL ASTASGHAQR ESDDDGLLER EARAGTRRIA SLTTELEDVS EVEYRRIRLE RVVLVGLDLP RAADPAASVL DAAQDAETSL SELAALSETA GSQVLDALIQ KRDHPDPATY LGSGKARELA EMVAAVGADT VIVDGELAPS QRRALEDVVG VKVVDRTALI LDIFAQHAKS REGKAQVELA QLEYLLPRLR GWGESMSRQA GGRVVGGQGI GSRGPGETKI ELDRRRIRHR MAKLRREIRA MAPSREVKRG SRRRGPIPAV AIAGYTNAGK SSLMNRLTDA GLMVQDALFA TLDPTVRRAE TADGRVYTLT DTVGFVRNLP HELIEAFRST LEEVAGADLV LHIVDAAHPD PVGQVAAVRA VLADIPGALD VPELIVLNKI DLTDAVTRAA LRTRLPGAIE ISARTGEGIE DLRARIDAML PRPSVPVDVV VPYSRGDLVS RVHTDGEIDV VEYVETGTRI VGRADAALAA ELRTAALPDA AADSAPSSP // ID J1H539_9CLOT Unreviewed; 422 AA. AC J1H539; DT 03-OCT-2012, integrated into UniProtKB/TrEMBL. DT 03-OCT-2012, sequence version 1. DT 07-JUN-2017, entry version 30. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:EJF40363.1}; GN ORFNames=HMPREF1141_0105 {ECO:0000313|EMBL:EJF40363.1}; OS Clostridium sp. MSTE9. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=1105031 {ECO:0000313|EMBL:EJF40363.1, ECO:0000313|Proteomes:UP000004073}; RN [1] {ECO:0000313|EMBL:EJF40363.1, ECO:0000313|Proteomes:UP000004073} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MSTE9 {ECO:0000313|EMBL:EJF40363.1, RC ECO:0000313|Proteomes:UP000004073}; RA Harkins D.M., Madupu R., Durkin A.S., Torralba M., Methe B., RA Sutton G.G., Nelson K.E.; RL Submitted (MAY-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EJF40363.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AKFU01000034; EJF40363.1; -; Genomic_DNA. DR RefSeq; WP_009063358.1; NZ_AKFU01000034.1. DR EnsemblBacteria; EJF40363; EJF40363; HMPREF1141_0105. DR PATRIC; fig|1105031.3.peg.1837; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000004073; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000004073}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000004073}. FT DOMAIN 200 362 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 159 196 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 422 AA; 46598 MW; FAB54B0AD7AB2BC3 CRC64; MELFENEVRP ERALLVAVDT GEYDVEASMA ELYELTRSAG AEPFGSMVQK RPSPDSATCV GSGMAEDIAD YCTRYEIDLL IFDCELSPTQ IRNLDELTKV RVIDRTMLIL DIFAARAKSK EGKLQVELAQ LRYLLPRLSG KGIAMSRLGG GIGTRGPGET KLETDRRHIR RRIEGLKEQL EEVEKHREQI NRRRQKDGVI TVALVGYTNA GKSTLMNYLT QAGVLAKDQL FATLDPTARA LKLPSGVTVM LIDTVGFVRR LPHHLVNAFR STLEQAALAD LILNVCDASS PEAQTHLEVT RALLAELGWK DRPVIPVLNK CDLVPELGAV PMIGNAVRIS AVTGAGIDEL LETVERNLPV RTVQVEALLP FAESGLAARV RKDGALQEEE FTEHGLRIVA RVGPELLEQL SRYLVDSDKP ED // ID J1SAV9_9ACTN Unreviewed; 495 AA. AC J1SAV9; DT 03-OCT-2012, integrated into UniProtKB/TrEMBL. DT 03-OCT-2012, sequence version 1. DT 30-AUG-2017, entry version 36. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=SU9_05561 {ECO:0000313|EMBL:EJJ08047.1}; OS Streptomyces auratus AGR0001. OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae; OC Streptomyces. OX NCBI_TaxID=1160718 {ECO:0000313|EMBL:EJJ08047.1, ECO:0000313|Proteomes:UP000009036}; RN [1] {ECO:0000313|EMBL:EJJ08047.1, ECO:0000313|Proteomes:UP000009036} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=AGR0001 {ECO:0000313|EMBL:EJJ08047.1, RC ECO:0000313|Proteomes:UP000009036}; RX PubMed=22965094; DOI=10.1128/JB.01155-12; RA Han X., Li M., Ding Z., Zhao J., Ji K., Wen M., Lu T.; RT "Genome Sequence of Streptomyces auratus Strain AGR0001, a RT Phoslactomycin-Producing Actinomycete."; RL J. Bacteriol. 194:5472-5473(2012). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EJJ08047.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AJGV01000045; EJJ08047.1; -; Genomic_DNA. DR RefSeq; WP_006602691.1; NZ_JH725387.1. DR EnsemblBacteria; EJJ08047; EJJ08047; SU9_05561. DR PATRIC; fig|1160718.3.peg.1140; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000009036; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 2. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000009036}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000009036}. FT DOMAIN 275 440 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 495 AA; 54045 MW; 2F1910A99387872E CRC64; MTSSSSLPQD RQRLSESLRA HALMEEDVAW SHEIDGERDG EQYDRSARAA LRRVAGLSTE LEDVTEVEYR QLRLERVVLV GVWTTGTVQE AENSLAELAA LAETAGALVL DGVIQRRDKP DPATYIGSGK ALELRDIVLE SGADTVVCDG ELSPGQLIHL EDVVKVKVVD RTALILDIFA QHAKSREGKA QVSLAQMQYM LPRLRGWGQS LSRQMGGGGS GSAGGGMATR GPGETKIETD RRRIREKMAK MRREIAEMKT GRDIKRQERR RHKVPSVAIA GYTNAGKSSL LNRLTGAGVL VENALFATLD PTVRRAETPS GRLYTLADTV GFVRHLPHHL VEAFRSTMEE VGDSDLILHV VDGSHPVPEE QLAAVREVIR EVGATDVPEI VVVNKADAAD PLVLQRLLRQ EKHALAVSAR TGQGMAELLE LLDEELPRPR VEIEVLVPYT QGALVSRAHS EGEVISEEHT ADGTVLKARV HEELAAAFEP FVAAA // ID J1SNN7_9RHIZ Unreviewed; 441 AA. AC J1SNN7; DT 03-OCT-2012, integrated into UniProtKB/TrEMBL. DT 03-OCT-2012, sequence version 1. DT 07-JUN-2017, entry version 33. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=PMI11_04942 {ECO:0000313|EMBL:EJJ26843.1}; OS Rhizobium sp. CF142. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium. OX NCBI_TaxID=1144314 {ECO:0000313|EMBL:EJJ26843.1, ECO:0000313|Proteomes:UP000009023}; RN [1] {ECO:0000313|EMBL:EJJ26843.1, ECO:0000313|Proteomes:UP000009023} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CF142 {ECO:0000313|EMBL:EJJ26843.1, RC ECO:0000313|Proteomes:UP000009023}; RX PubMed=23045501; DOI=10.1128/JB.01243-12; RA Brown S.D., Utturkar S.M., Klingeman D.M., Johnson C.M., Martin S.L., RA Land M.L., Lu T.Y., Schadt C.W., Doktycz M.J., Pelletier D.A.; RT "Twenty-one genome sequences from Pseudomonas species and 19 genome RT sequences from diverse bacteria isolated from the rhizosphere and RT endosphere of Populus deltoides."; RL J. Bacteriol. 194:5991-5993(2012). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EJJ26843.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AJWE01000104; EJJ26843.1; -; Genomic_DNA. DR RefSeq; WP_007822483.1; NZ_AJWE01000104.1. DR EnsemblBacteria; EJJ26843; EJJ26843; PMI11_04942. DR PATRIC; fig|1144314.3.peg.4966; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000009023; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000009023}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000009023}. FT DOMAIN 203 375 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 162 196 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 441 AA; 49016 MW; 70E2BBF38F659303 CRC64; MRATVVVPVL KSRSRGGQTE STSTRTPESR LDEATGLAQA IDLDVVNASI VSVSDPRPAT LLGTGKIEEI KHLLDERDSG LVIVDHPLTP VQQRNLEKEW NAKVIDRTGL ILEIFGRRAS TKEGTLQVDL AHLNYQKGRL VRSWTHLERQ RGGGGFMGGP GETQIEADRR LLQDRIIKLE RELEQVVRTR QLHRAKRRKV PHPIVALVGY TNAGKSTLFN RITGAGVLAE DMLFATLDPT LRRMKLPHGR TVILSDTVGF ISDLPTHLVA AFRATLEEVL EADLVLHVRD MSDVDNQAQS ADVLRILNDL GIDEAEGERR ILEVWNKIDR LEPEAHDAMV QKSSGMKNVI AVSAISGEGV DRLMDEISRR LSGVMTETTV TLPVDKLALL PWLYDHAVVG SREDNEDGSV TLDLRLSETE ATELERRIGN GPKPAKEDWE R // ID J2L9U7_9BURK Unreviewed; 359 AA. AC J2L9U7; DT 03-OCT-2012, integrated into UniProtKB/TrEMBL. DT 03-OCT-2012, sequence version 1. DT 07-JUN-2017, entry version 31. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=PMI15_03293 {ECO:0000313|EMBL:EJL81963.1}; OS Polaromonas sp. CF318. OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Comamonadaceae; Polaromonas. OX NCBI_TaxID=1144318 {ECO:0000313|EMBL:EJL81963.1, ECO:0000313|Proteomes:UP000007275}; RN [1] {ECO:0000313|EMBL:EJL81963.1, ECO:0000313|Proteomes:UP000007275} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CF318 {ECO:0000313|EMBL:EJL81963.1, RC ECO:0000313|Proteomes:UP000007275}; RX PubMed=23045501; DOI=10.1128/JB.01243-12; RA Brown S.D., Utturkar S.M., Klingeman D.M., Johnson C.M., Martin S.L., RA Land M.L., Lu T.Y., Schadt C.W., Doktycz M.J., Pelletier D.A.; RT "Twenty-one genome sequences from Pseudomonas species and 19 genome RT sequences from diverse bacteria isolated from the rhizosphere and RT endosphere of Populus deltoides."; RL J. Bacteriol. 194:5991-5993(2012). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EJL81963.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AKIV01000082; EJL81963.1; -; Genomic_DNA. DR EnsemblBacteria; EJL81963; EJL81963; PMI15_03293. DR PATRIC; fig|1144318.3.peg.3182; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000007275; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000007275}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000007275}. FT DOMAIN 168 347 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 359 AA; 39704 MW; 0A819753A48337F9 CRC64; MLAQTAGLQP VARVTCKRRA PDAALFIGSG KADEIKLLAL DTGATEVLFD QSLSPAQQRN LERHLDMPVN DRTLLILEIF AQRARSHEGK LQVELARLQY MSTRLVRRWS HLERQTGGAG VRGGPGEKQI ELDKRMIGDA IKRTKERLAK VKKQRQTQRK QRERRNSFTI SLVGYTNAGK STLFNALVKA RAYAADQLFA TLDTTTRQLY LGDAGRSVSL SDTVGFIRDL PHGLIDAFAA TLQEAADADL LLHVVDGANP DYLEQIEQVQ RVLSEIGAAD VPQILVFNKL DAIEKDNMPL QLQDMFELRD AFEGSSRSAE RVFVSARTGE GLPLLRALLA GYAAHPPAEE IPLATEDLV // ID J2LFA5_9SPHN Unreviewed; 444 AA. AC J2LFA5; DT 03-OCT-2012, integrated into UniProtKB/TrEMBL. DT 03-OCT-2012, sequence version 1. DT 07-JUN-2017, entry version 32. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=PMI04_00573 {ECO:0000313|EMBL:EJK86156.1}; OS Sphingobium sp. AP49. OC Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales; OC Sphingomonadaceae; Sphingobium. OX NCBI_TaxID=1144307 {ECO:0000313|EMBL:EJK86156.1, ECO:0000313|Proteomes:UP000006480}; RN [1] {ECO:0000313|EMBL:EJK86156.1, ECO:0000313|Proteomes:UP000006480} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=AP49 {ECO:0000313|EMBL:EJK86156.1, RC ECO:0000313|Proteomes:UP000006480}; RX PubMed=23045501; DOI=10.1128/JB.01243-12; RA Brown S.D., Utturkar S.M., Klingeman D.M., Johnson C.M., Martin S.L., RA Land M.L., Lu T.Y., Schadt C.W., Doktycz M.J., Pelletier D.A.; RT "Twenty-one genome sequences from Pseudomonas species and 19 genome RT sequences from diverse bacteria isolated from the rhizosphere and RT endosphere of Populus deltoides."; RL J. Bacteriol. 194:5991-5993(2012). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EJK86156.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AJVL01000009; EJK86156.1; -; Genomic_DNA. DR RefSeq; WP_007705497.1; NZ_AJVL01000009.1. DR EnsemblBacteria; EJK86156; EJK86156; PMI04_00573. DR PATRIC; fig|1144307.3.peg.537; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000006480; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000006480}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000006480}. FT DOMAIN 209 390 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 444 AA; 48629 MW; DCBBAEEBF2084D90 CRC64; MAIFNRDSDD EVARGARAVV VHAETHNADR RDSDARLEEA RGLALAIGID VRSAQSFRVR DRKPATLFGS GQVDQIATLV TQEEAELVIV DNALTPVQQS NLEKGTGAKV IDRTGLILEI FGERAATNEG RLQVELAHLD YQAGRLVRSW THLERQRGGF GFLGGPGETQ IEADRRMIRD RMAKIRRELD QVTKTRGLHR ARRQRAPWPV IALVGYTNAG KSTLFNRLTG AEVMAEDLLF ATLDPTMRQI VLPGLDKAIL SDTVGFVSDL PTQLIAAFRA TLEEVLSADI IVHVRDIAHP DTDAQRDDVL DVLSELGVAG EGALERADTD SDPPPIIEAW NKLDLLDQEA VALAREAASR RDDVVIISAL TGDGVDGLQR AISERLTQGA TVHNLRLPIA DGAGLAWLHE HGEVLASHPG DAEMRVEVRL SDSALARFLK RDRI // ID J2LXQ7_KLEPN Unreviewed; 426 AA. AC J2LXQ7; DT 03-OCT-2012, integrated into UniProtKB/TrEMBL. DT 03-OCT-2012, sequence version 1. DT 30-AUG-2017, entry version 34. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=UUU_01640 {ECO:0000313|EMBL:EJK92866.1}; OS Klebsiella pneumoniae subsp. pneumoniae DSM 30104. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; OC Enterobacteriaceae; Klebsiella. OX NCBI_TaxID=1162296 {ECO:0000313|EMBL:EJK92866.1, ECO:0000313|Proteomes:UP000036622}; RN [1] {ECO:0000313|Proteomes:UP000036622} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 30104 {ECO:0000313|Proteomes:UP000036622}; RA Lee J.H., Song M.K.; RT "Genome sequencing of Klebsiella pneumonia JC2877."; RL Submitted (JUL-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EJK92866.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AJJI01000001; EJK92866.1; -; Genomic_DNA. DR RefSeq; WP_004146725.1; NZ_AJJI01000001.1. DR ProteinModelPortal; J2LXQ7; -. DR EnsemblBacteria; EJK92866; EJK92866; UUU_01640. DR PATRIC; fig|1162296.3.peg.188; -. DR Proteomes; UP000036622; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000036622}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000036622}. FT DOMAIN 198 365 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 426 AA; 48070 MW; 7E24BDE9CE348D9F CRC64; MFDRYDAGEQ AVLVHIYFSQ DKDMEDLQEF ETLASSAGVE AMQVITGSRK APHPKYFVGE GKAVEIAEAV KATGASVVLF DHALSPAQER NLERLCECRV IDRTGLILDI FAQRARTHEG KLQVELAQLR HMATRLVRGW THLERQKGGI GLRGPGETQL ETDRRLLRNR IMQILSRLEK VEKQREQGRR SRAKADIPTV SLVGYTNAGK STLFNQITAA EVYAANQLFA TLDPTLRRID VPDVGETVLA DTVGFIRHLP HDLVAAFKAT LQETRQATLL LHVIDAADVR VQENIDAVNT VLAEIEADEI PALLVMNKID MLDDFEPRID RDDENKPIRV WLSAQTGVGV PLLFQALTER LSGEVAQHTL RLPPKEGRLR SRFYQLQAIE KEWMEDDGSV SLQVRMPIVD WRRLCKQEPT LVDYVV // ID J2PI00_9SPHN Unreviewed; 470 AA. AC J2PI00; DT 03-OCT-2012, integrated into UniProtKB/TrEMBL. DT 03-OCT-2012, sequence version 1. DT 05-JUL-2017, entry version 33. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=PMI02_02920 {ECO:0000313|EMBL:EJL26942.1}; OS Novosphingobium sp. AP12. OC Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales; OC Sphingomonadaceae; Novosphingobium. OX NCBI_TaxID=1144305 {ECO:0000313|EMBL:EJL26942.1, ECO:0000313|Proteomes:UP000007515}; RN [1] {ECO:0000313|EMBL:EJL26942.1, ECO:0000313|Proteomes:UP000007515} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=AP12 {ECO:0000313|EMBL:EJL26942.1, RC ECO:0000313|Proteomes:UP000007515}; RX PubMed=23045501; DOI=10.1128/JB.01243-12; RA Brown S.D., Utturkar S.M., Klingeman D.M., Johnson C.M., Martin S.L., RA Land M.L., Lu T.Y., Schadt C.W., Doktycz M.J., Pelletier D.A.; RT "Twenty-one genome sequences from Pseudomonas species and 19 genome RT sequences from diverse bacteria isolated from the rhizosphere and RT endosphere of Populus deltoides."; RL J. Bacteriol. 194:5991-5993(2012). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EJL26942.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AKKE01000086; EJL26942.1; -; Genomic_DNA. DR EnsemblBacteria; EJL26942; EJL26942; PMI02_02920. DR PATRIC; fig|1144305.3.peg.2811; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000007515; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000007515}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000007515}. FT DOMAIN 210 414 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 470 AA; 52071 MW; 1F10890497F3E8C6 CRC64; MNDELKGEVT RGARALVVYP QMRGPRGQMA DLDTEARLEE ARGLALAIGL EVAEAIAIVI REPRAATLFG EGQIQNISVA CELNEAELVI VDGSLTAIQQ RNLEEKLKRK VIDRTGLILE IFGERAATAE GRLQVELAHL DYQAGRLVRS WTHLERQRGG FGFLGGPGET QIEADRRLIR DRMAKIRREL EQVRRTRGLH RGRREKAPWP IVALVGYTNA GKSTLFNRLT GAEVMAEDLL FATLDPTMRA IRLPGMEKAI LSDTVGFISD LPTQLVAAFR ATLEEVTAAD VIVHVRDIAN PDTEAQKRQV LDVLADLGVL HPQPDARTLR NTAREERAAG WAQEEKDEKA DGEPQIPIIE VWNKWDLLDP EQAHSLREAM THREGEIIVP VSALTGEGCE ELLTVASRTL TLDSKVYSFV IPAADGQRLA FLHARGEIVA EEDAGEGDEG PQLRLQVRLS ARELGRFMSL // ID J2UWZ9_9RHIZ Unreviewed; 471 AA. AC J2UWZ9; DT 03-OCT-2012, integrated into UniProtKB/TrEMBL. DT 03-OCT-2012, sequence version 1. DT 07-JUN-2017, entry version 32. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=PMI41_04936 {ECO:0000313|EMBL:EJM97806.1}; OS Phyllobacterium sp. YR531. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Phyllobacteriaceae; Phyllobacterium. OX NCBI_TaxID=1144343 {ECO:0000313|EMBL:EJM97806.1, ECO:0000313|Proteomes:UP000007283}; RN [1] {ECO:0000313|EMBL:EJM97806.1, ECO:0000313|Proteomes:UP000007283} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=YR531 {ECO:0000313|EMBL:EJM97806.1, RC ECO:0000313|Proteomes:UP000007283}; RX PubMed=23045501; DOI=10.1128/JB.01243-12; RA Brown S.D., Utturkar S.M., Klingeman D.M., Johnson C.M., Martin S.L., RA Land M.L., Lu T.Y., Schadt C.W., Doktycz M.J., Pelletier D.A.; RT "Twenty-one genome sequences from Pseudomonas species and 19 genome RT sequences from diverse bacteria isolated from the rhizosphere and RT endosphere of Populus deltoides."; RL J. Bacteriol. 194:5991-5993(2012). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EJM97806.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AKIZ01000041; EJM97806.1; -; Genomic_DNA. DR RefSeq; WP_008129220.1; NZ_AKIZ01000041.1. DR EnsemblBacteria; EJM97806; EJM97806; PMI41_04936. DR PATRIC; fig|1144343.3.peg.5008; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000007283; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000007283}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000007283}. FT DOMAIN 237 411 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 196 223 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 471 AA; 52162 MW; A4CDA6B9C41E71BB CRC64; MTKETTRNAN NKGGIAEDGD TAREATRALV IVPVLPHRFA DGGKQDDPKA PVYYREFQRS EEARLEEAKG LARAIDLDIV HSDIVQVSAP RPATLLGSGK VDMIAEIIEE THAELVIVDH ALTPVQQRNL EKAWNAKVLD RTGLILEIFG RRAQTKEGTL QVELAHLTYQ KGRLVRSWTH LERQRGGGGF LGGPGETQIE SDRRALQEKI LRIKRELETV VRTRALHRSK RRKVPHPIVA LVGYTNAGKS TLFNRMTGAG VVAEDMLFAT LDPTLRRIRL EHGEMVILSD TVGFISNLPT HLVAAFRATL EEVVEADLIL HIRDISDPDT AAQAEDVHGI MADLGIERGD TKRIIEVWNK IDLLDEPGRE TAQRLSAAAT GNEHPVPVSA ITGEGVDFLL SEIENRIAGK LAHVKLTLKP EQMGLIDWIY QHSSNVKRKD QEDGSVVLTM DMTATSNAIL QDKMLGKKRA N // ID J2V2G4_9BURK Unreviewed; 374 AA. AC J2V2G4; DT 03-OCT-2012, integrated into UniProtKB/TrEMBL. DT 03-OCT-2012, sequence version 1. DT 07-JUN-2017, entry version 33. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=PMI40_03682 {ECO:0000313|EMBL:EJM99796.1}; OS Herbaspirillum sp. YR522. OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Oxalobacteraceae; Herbaspirillum. OX NCBI_TaxID=1144342 {ECO:0000313|EMBL:EJM99796.1, ECO:0000313|Proteomes:UP000007507}; RN [1] {ECO:0000313|EMBL:EJM99796.1, ECO:0000313|Proteomes:UP000007507} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=YR522 {ECO:0000313|EMBL:EJM99796.1, RC ECO:0000313|Proteomes:UP000007507}; RX PubMed=23045501; DOI=10.1128/JB.01243-12; RA Brown S.D., Utturkar S.M., Klingeman D.M., Johnson C.M., Martin S.L., RA Land M.L., Lu T.Y., Schadt C.W., Doktycz M.J., Pelletier D.A.; RT "Twenty-one genome sequences from Pseudomonas species and 19 genome RT sequences from diverse bacteria isolated from the rhizosphere and RT endosphere of Populus deltoides."; RL J. Bacteriol. 194:5991-5993(2012). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EJM99796.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AKJA01000120; EJM99796.1; -; Genomic_DNA. DR RefSeq; WP_008117848.1; NZ_AKJA01000120.1. DR EnsemblBacteria; EJM99796; EJM99796; PMI40_03682. DR PATRIC; fig|1144342.3.peg.3412; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000007507; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000007507}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000007507}. FT DOMAIN 190 356 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 156 183 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 374 AA; 40595 MW; 53420466EFC7120D CRC64; MRAGLVGLDF GKGDFAASLD ELFLLAKSAG AEPVMTITGR RASPDAALFV GSGKAQEVAD AVADLQLELV IFNHALSPAQ QRNLERVLKV RVLDRTSLIL DIFAQRAKSH VGKVQVELAQ LQHLATRLIR GWTHLERQKG GIGLRGPGET QLETDRRLLG ERVKALRAVL AKLRKQHATQ RRARGRNDTF SVSLVGYTNA GKSTIFNAVA KAGVYAANQL FATLDTTSRR VYLGDAGHAV VSDTVGFIRE LPHQLVEAFR ATLEETIHAD LLLHVVDAAS PVRMEQIEQV NLVLKEIGAD HVPQILVWNK IDAAGLEPAI EHDEYGNIQR VFVSAKSGAG LDLLREAVAA SLKAAMEARG RSQSLPVDSE DVRA // ID J3DHR3_9BURK Unreviewed; 375 AA. AC J3DHR3; DT 03-OCT-2012, integrated into UniProtKB/TrEMBL. DT 03-OCT-2012, sequence version 1. DT 07-JUN-2017, entry version 32. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=PMI16_01145 {ECO:0000313|EMBL:EJL92206.1}; OS Herbaspirillum sp. CF444. OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Oxalobacteraceae; Herbaspirillum. OX NCBI_TaxID=1144319 {ECO:0000313|EMBL:EJL92206.1, ECO:0000313|Proteomes:UP000007296}; RN [1] {ECO:0000313|EMBL:EJL92206.1, ECO:0000313|Proteomes:UP000007296} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CF444 {ECO:0000313|EMBL:EJL92206.1, RC ECO:0000313|Proteomes:UP000007296}; RX PubMed=23045501; DOI=10.1128/JB.01243-12; RA Brown S.D., Utturkar S.M., Klingeman D.M., Johnson C.M., Martin S.L., RA Land M.L., Lu T.Y., Schadt C.W., Doktycz M.J., Pelletier D.A.; RT "Twenty-one genome sequences from Pseudomonas species and 19 genome RT sequences from diverse bacteria isolated from the rhizosphere and RT endosphere of Populus deltoides."; RL J. Bacteriol. 194:5991-5993(2012). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EJL92206.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AKJW01000021; EJL92206.1; -; Genomic_DNA. DR RefSeq; WP_007877288.1; NZ_AKJW01000021.1. DR EnsemblBacteria; EJL92206; EJL92206; PMI16_01145. DR PATRIC; fig|1144319.3.peg.1157; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000007296; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000007296}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000007296}. FT DOMAIN 190 356 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 375 AA; 41022 MW; 6A996DB383342CDC CRC64; MRAALVGLDF GKSDFAASLD ELFLLAKSAG AEPVTTITGK RASPDAALFV GSGKAQEVAD AVADLQLDIV IFNHALSPAQ QRNLERVLKT RVLDRTSLIL DIFAQRAKSH EGKVQVELAQ LQHLATRLIR GWTHLERQKG GIGLRGPGET QLETDRRLLG DRVKALRGQL AKLHRQHATQ RRARGRNDTF SVSLVGYTNA GKSTVFNAMA KAGVYAANQL FATLDTTSRR VYLGEVGHVV ISDTVGFIRE LPHQLVAAFR ATLEETIHAD LLLHVVDAAS PVRMEQIEQV NLVLKEIGAD HIPQILVWNK IDAAELEPAV EHDEYGRIHR VFISAKTGAG LDLLRQAIAD SLRSSIEARR GAQSQVVDSQ DVHAH // ID J3JCP3_9LACO Unreviewed; 451 AA. AC J3JCP3; DT 03-OCT-2012, integrated into UniProtKB/TrEMBL. DT 03-OCT-2012, sequence version 1. DT 07-JUN-2017, entry version 28. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=A11Y_20873 {ECO:0000313|EMBL:EJN56779.1}; OS Lactobacillus coryniformis subsp. coryniformis CECT 5711. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; OC Lactobacillus. OX NCBI_TaxID=1185325 {ECO:0000313|EMBL:EJN56779.1, ECO:0000313|Proteomes:UP000007271}; RN [1] {ECO:0000313|EMBL:EJN56779.1, ECO:0000313|Proteomes:UP000007271} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CECT5711 {ECO:0000313|Proteomes:UP000007271}; RA Rodriguez J.M.; RT "Complete Genome Sequence of Lactobacillus coryniformis CECT5711."; RL Submitted (MAY-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EJN56779.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AKFP01000001; EJN56779.1; -; Genomic_DNA. DR EnsemblBacteria; EJN56779; EJN56779; A11Y_20873. DR PATRIC; fig|1185325.3.peg.49; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000007271; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000007271}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000007271}. FT DOMAIN 224 396 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 451 AA; 50782 MW; DB86966687C45CF7 CRC64; MYDDQQETYF PIIDHNSSHY TYGGNMQEIE LTKVLIGGVS QNQAYFESDM AELAELVKAN QMTVVGDIRQ NLERAVAATY FGSGKLEEIR QLAEENDAQV LVVNDELSPS QIRNLEHELK MTLLDRTGLI LAIFANRAQS REAKMQVQIA RLQYELPRLR VGEQANLMQQ GGGPGFANRG SGETKLEMNQ RTIKNKISQL RHELKTMEVA QQTKRAQRER SAIPTVALVG YTNAGKSTTM NGLLRRFNAD AENAKTVFER DMLFATLDTS VREITLPDNK KFLLSDTVGF INKLPTQLVK AFRSTLAEAA AADLLVQVID FSDPNYQEMI KVTEKTLHTM GIDDIPMIYA YNKADRKTDT AFPLQTGEHD LVYSATDQAS LELLTQMITK ELFADLTKVA FMIPFADGKW VDYLNEHANI LEQDYTASGT QITAEVSPED RQRLAKYIIE V // ID J3N9C7_ORYBR Unreviewed; 384 AA. AC J3N9C7; DT 03-OCT-2012, integrated into UniProtKB/TrEMBL. DT 03-OCT-2012, sequence version 1. DT 30-AUG-2017, entry version 27. DE SubName: Full=Uncharacterized protein {ECO:0000313|EnsemblPlants:OB11G24130.1}; OS Oryza brachyantha. OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; BOP clade; OC Oryzoideae; Oryzeae; Oryzinae; Oryza. OX NCBI_TaxID=4533 {ECO:0000313|EnsemblPlants:OB11G24130.1}; RN [1] {ECO:0000313|EnsemblPlants:OB11G24130.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=IRGC 101232 {ECO:0000313|EnsemblPlants:OB11G24130.1}; RX PubMed=23481403; RA Chen J., Huang Q., Gao D., Wang J., Lang Y., Liu T., Li B., Bai Z., RA Luis Goicoechea J., Liang C., Chen C., Zhang W., Sun S., Liao Y., RA Zhang X., Yang L., Song C., Wang M., Shi J., Liu G., Liu J., Zhou H., RA Zhou W., Yu Q., An N., Chen Y., Cai Q., Wang B., Liu B., Min J., RA Huang Y., Wu H., Li Z., Zhang Y., Yin Y., Song W., Jiang J., RA Jackson S.A., Wing R.A., Wang J., Chen M.; RT "Whole-genome sequencing of Oryza brachyantha reveals mechanisms RT underlying Oryza genome evolution."; RL Nat. Commun. 4:1595-1595(2013). RN [2] {ECO:0000313|EnsemblPlants:OB11G24130.1} RP IDENTIFICATION. RG EnsemblPlants; RL Submitted (APR-2013) to UniProtKB. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR STRING; 4533.OB11G24130.1; -. DR EnsemblPlants; OB11G24130.1; OB11G24130.1; OB11G24130. DR Gramene; OB11G24130.1; OB11G24130.1; OB11G24130. DR eggNOG; KOG0410; Eukaryota. DR eggNOG; COG2262; LUCA. DR OMA; VILEIFH; -. DR OrthoDB; EOG093609UJ; -. DR Proteomes; UP000006038; Chromosome 11. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000006038}; KW Reference proteome {ECO:0000313|Proteomes:UP000006038}. FT DOMAIN 160 325 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 126 153 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 384 AA; 42828 MW; 1A67774E24C107E0 CRC64; MVVGSTYQKL STPNPRTYIG SGKVAEIKSA IHSLDVETVI FDDELSPGQL RNLEKSFGGG VRVCDRTALI LDIFNQRAAT HEAALQVTLA QMEYQLPRLT KMWTHLERQS GGQVKGMGEK QIEVDKRILR TQISALKKEL ESVRKHRKLY RNRRQSVPIP VVSLVGYTNA GKSTLLNRLT GADVLAEDKL FATLDPTTRR VLMKNGTEFL LTDTVGFIQK LPTMLVAAFR ATLEEISESS VIVHLVDISH PLAQEQIDAV DKVLKELDIE SIPKLVVWNK IDNTDDTLRV KEEAEKQGII WISAINGDGL EDFCNAIQAK LKDSLVPIEA FVPYDKGELL SDIHKVGMVE KTEYMENGTF VKAHVPLPLA RLLTPLRQQV VAAL // ID J4K855_9FIRM Unreviewed; 415 AA. AC J4K855; DT 31-OCT-2012, integrated into UniProtKB/TrEMBL. DT 31-OCT-2012, sequence version 1. DT 07-JUN-2017, entry version 29. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:EJP20431.1}; GN ORFNames=HMPREF1140_0635 {ECO:0000313|EMBL:EJP20431.1}; OS Lachnoanaerobaculum sp. ICM7. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Lachnospiraceae; OC Lachnoanaerobaculum. OX NCBI_TaxID=936594 {ECO:0000313|EMBL:EJP20431.1, ECO:0000313|Proteomes:UP000006599}; RN [1] {ECO:0000313|EMBL:EJP20431.1, ECO:0000313|Proteomes:UP000006599} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ICM7 {ECO:0000313|EMBL:EJP20431.1, RC ECO:0000313|Proteomes:UP000006599}; RA Durkin A.S., McCorrison J., Torralba M., Gillis M., Methe B., RA Sutton G., Nelson K.E.; RL Submitted (JUL-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EJP20431.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ALJL01000023; EJP20431.1; -; Genomic_DNA. DR RefSeq; WP_009663239.1; NZ_ALJL01000023.1. DR EnsemblBacteria; EJP20431; EJP20431; HMPREF1140_0635. DR PATRIC; fig|936594.3.peg.1419; -. DR Proteomes; UP000006599; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000006599}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000006599}. FT DOMAIN 199 364 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 165 195 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 415 AA; 46362 MW; 1A02DF854431D5AD CRC64; MSTYETKEIV EKVVLLGVDV GDDTKESMKE LAELVDTAGA TVLDSIIQSR ERMHPGTYIG KGKIEEVKDR VIELGATGVV CDDELTPAQL RNLEDLLDTK VMDRTMVILD IFAKRATTSE GKIQVELAQL KFSSARLVGL RSSLSRLGGG IGTRGPGEKK LEMDRRLIHE RISQLKAELK KVENHRDLIR KSRDENLAFN VAIVGYTNAG KSTLLNKLTD ANILAEDKLF ATLDPTTRKL KLGSGQEILV TDTVGFIRKL PHHLIEAFKS TLEEAKYANL LIHMVDASNE EASSQMLVVY DTLRSLDVVD KDIITVFNKT DLMEENMELP RDFHADKVLK MSAKTGEGIE DLKKTVEDIL QKQRVYLEHV FPYKDAGKIA IVRKFGEILS EEYIDEGISI KAYIPAEIFG KVIST // ID J4KBG3_9FIRM Unreviewed; 427 AA. AC J4KBG3; DT 31-OCT-2012, integrated into UniProtKB/TrEMBL. DT 31-OCT-2012, sequence version 1. DT 07-JUN-2017, entry version 32. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:EJP26221.1}; GN ORFNames=HMPREF1142_0842 {ECO:0000313|EMBL:EJP26221.1}; OS Peptostreptococcaceae bacterium AS15. OC Bacteria; Firmicutes; Clostridia; Clostridiales; OC Peptostreptococcaceae. OX NCBI_TaxID=936556 {ECO:0000313|EMBL:EJP26221.1, ECO:0000313|Proteomes:UP000006605}; RN [1] {ECO:0000313|EMBL:EJP26221.1, ECO:0000313|Proteomes:UP000006605} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=AS15 {ECO:0000313|EMBL:EJP26221.1, RC ECO:0000313|Proteomes:UP000006605}; RA Durkin A.S., McCorrison J., Torralba M., Gillis M., Methe B., RA Sutton G., Nelson K.E.; RL Submitted (JUL-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EJP26221.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ALJM01000003; EJP26221.1; -; Genomic_DNA. DR RefSeq; WP_009079933.1; NZ_ALJM01000003.1. DR EnsemblBacteria; EJP26221; EJP26221; HMPREF1142_0842. DR PATRIC; fig|936556.4.peg.140; -. DR Proteomes; UP000006605; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000006605}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000006605}. FT DOMAIN 202 372 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 427 AA; 48829 MW; E2B671D164B6B032 CRC64; MENKIEKVIL VGLNITSTVK RQGDIDIYDS MKELEELAEA ANTMILGTVI QNKDSYDVAY YIGKGKAQEL AEMAKNMEAD TIIFNEELSG VQIKNLEEVT NVKVIDRATL ILDIFASRAL SKEGKLQVEL AQQKYRSSRL IGLGSQMSRL GGGIGTRGPG EKQLEIDKRH IRQRIIDIQR ELKEITKNRQ TQRSSRMKSN MPLVALVGYT NSGKSTILNE IIKTHKDYDK SKEVDAKDML FATLDVQLRK ATLPSNSDFL VTDTVGFVSS IPHDLIDAFK ATLEEVKYAD LLLHVVDLSN DKHKLQMDTT NKVLSEIGVE NKKMLYVFNK ADKVDYDTKV YVDDPFVIIS ATKRYNLDKF YEMIEDCLNK SKKKVKMLIP FAKSEIISKL HEKYNFEEYY DETGTIITVN LEDEDYNRYK EYVTEEF // ID J4V6K4_9GAMM Unreviewed; 431 AA. AC J4V6K4; DT 31-OCT-2012, integrated into UniProtKB/TrEMBL. DT 31-OCT-2012, sequence version 1. DT 30-AUG-2017, entry version 29. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:EJP74037.1}; GN ORFNames=NT02SARS_0607 {ECO:0000313|EMBL:EJP74037.1}; OS SAR86 cluster bacterium SAR86B. OC Bacteria; Proteobacteria; Gammaproteobacteria; SAR86 cluster. OX NCBI_TaxID=1123867 {ECO:0000313|EMBL:EJP74037.1, ECO:0000313|Proteomes:UP000010116}; RN [1] {ECO:0000313|EMBL:EJP74037.1, ECO:0000313|Proteomes:UP000010116} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=22170421; DOI=10.1038/ismej.2011.189; RA Dupont C.L., Rusch D.B., Yooseph S., Lombardo M.J., Richter R.A., RA Valas R., Novotny M., Yee-Greenbaum J., Selengut J.D., Haft D.H., RA Halpern A.L., Lasken R.S., Nealson K., Friedman R., Venter J.C.; RT "Genomic insights to SAR86, an abundant and uncultivated marine RT bacterial lineage."; RL ISME J. 6:1186-1199(2012). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JH611164; EJP74037.1; -; Genomic_DNA. DR Proteomes; UP000010116; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000010116}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000010116}. FT DOMAIN 202 365 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 431 AA; 48148 MW; BBA95C1084BC8F5A CRC64; MITEQKLPES ALLIFLDVYS LKNKNNLDNP YKEFFTLVQS AGLEVIGSIM GKQNLPSTSA FINSGKILEI KSLVKELKPD LVIINHALSA SQARNLEKIF KVRVIDKTEL ILDIFAARAS SHIGKLQVEL AQLNHLSTRL IRGWTHLERQ KGGIGLRGPG ETQLETDRRL IGQRIKTLKS KLNKAYKQRQ INTYARKKGR SKIVSLVGYT NAGKTSLFNL LTNSDQHAAD QLFATLDSVT RKNHDPKLGS ILFSDTVGFI SDLPTELIAS FKATLDELLS ADLLLHVIDI ADEDYKEKEY EVNKILKSIG IKEIPILRVM NKCDMKEIEN PSLNNASDIC WISVKDQTGI VELRRSIDGI LSGGIYEGWI SIESRLGKVR SDLYNMGCIK EEKSSSNGTI LAFVNIGQDQ LNRLLDNEGV SIESNDKIEL N // ID J4VNM3_9PORP Unreviewed; 112 AA. AC J4VNM3; DT 31-OCT-2012, integrated into UniProtKB/TrEMBL. DT 31-OCT-2012, sequence version 1. DT 07-SEP-2016, entry version 14. DE SubName: Full=GTP-binding GTPase N-terminal domain protein {ECO:0000313|EMBL:EJU16521.1}; DE Flags: Fragment; GN ORFNames=HMPREF1323_0157 {ECO:0000313|EMBL:EJU16521.1}; OS Porphyromonas sp. oral taxon 279 str. F0450. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; OC Porphyromonadaceae; Porphyromonas. OX NCBI_TaxID=1125723 {ECO:0000313|EMBL:EJU16521.1, ECO:0000313|Proteomes:UP000004156}; RN [1] {ECO:0000313|EMBL:EJU16521.1, ECO:0000313|Proteomes:UP000004156} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=F0450 {ECO:0000313|EMBL:EJU16521.1, RC ECO:0000313|Proteomes:UP000004156}; RA Durkin A.S., McCorrison J., Torralba M., Gillis M., Methe B., RA Sutton G., Nelson K.E.; RL Submitted (JUL-2012) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EJU16521.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ALKJ01000021; EJU16521.1; -; Genomic_DNA. DR EnsemblBacteria; EJU16521; EJU16521; HMPREF1323_0157. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000004156; Unassembled WGS sequence. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF13167; GTP-bdg_N; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000004156}; KW Reference proteome {ECO:0000313|Proteomes:UP000004156}. FT DOMAIN 31 112 GTP-bdg_N. {ECO:0000259|Pfam:PF13167}. FT NON_TER 112 112 {ECO:0000313|EMBL:EJU16521.1}. SQ SEQUENCE 112 AA; 12905 MW; 13218C389CA173B4 CRC64; MREFIITEAK SEEAVLVGLI TKNQNEEQAR EYLDELDFLS STAGVRAVRR FTQRLDQPHS VTFVGKGKLE EIRLFVEENE IGIVIFDDEL SPKQLRNIEQ ALKVKILDRT SL // ID J5HF48_9PAST Unreviewed; 464 AA. AC J5HF48; DT 31-OCT-2012, integrated into UniProtKB/TrEMBL. DT 31-OCT-2012, sequence version 1. DT 30-AUG-2017, entry version 34. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:EJP28380.1}; GN ORFNames=HMPREF1128_2001 {ECO:0000313|EMBL:EJP28380.1}; OS Haemophilus sputorum HK 2154. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=1078483 {ECO:0000313|EMBL:EJP28380.1, ECO:0000313|Proteomes:UP000006974}; RN [1] {ECO:0000313|EMBL:EJP28380.1, ECO:0000313|Proteomes:UP000006974} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=HK2154 {ECO:0000313|Proteomes:UP000006974}; RA Durkin A.S., McCorrison J., Torralba M., Gillis M., Methe B., RA Sutton G., Nelson K.E.; RL Submitted (JUL-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EJP28380.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ALJP01000012; EJP28380.1; -; Genomic_DNA. DR RefSeq; WP_007525834.1; NZ_ALJP01000012.1. DR EnsemblBacteria; EJP28380; EJP28380; HMPREF1128_2001. DR PATRIC; fig|1078483.3.peg.1412; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000006974; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000006974}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000006974}. FT DOMAIN 231 398 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 197 224 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 464 AA; 52220 MW; 0100FA3D50934396 CRC64; MIISSISTQT TLPSEDENSS LGFLFPENSE KTHPTQLEEK DRAILVHLFL SPEKDIENLT EFQTLAHSAG VEVLATLTTS RSTPHAKYFV GTGKAEEIQQ AVEALSANLV LVNHELSPSQ TRNLSALCGC RVVDRTGLIL DIFAQRARSY EGKLQVELAQ LKHLSTRLVR RLGKQDQQKG GAVGLRGPGE TQLETDRRLI KVRIQQLQRR LEKVNQQRHQ NRKTRQKADI PTVSLVGYTN AGKSTLFNTL TQADVYAADQ LFATLDPTLR RLQLPEVGTT IFADTVGFIR NLPHDLVSAF KSTLQETCEA TLLLHVIDAA DARKLENISA VNQVLDEIRA NEVPILQVYN KIDALPAVSP FIERDENGKP IAVYLSAQSG LGVDLLHQAI CERLRNTLVT KQLLLPPTSG QIYAQFYQHH CIKQERFNEF GDRLLTIEVD EIQWQKWLKQ YPELTEYLEF AQWA // ID J5KY80_PASMD Unreviewed; 41 AA. AC J5KY80; DT 31-OCT-2012, integrated into UniProtKB/TrEMBL. DT 31-OCT-2012, sequence version 1. DT 20-JAN-2016, entry version 9. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EJS89794.1}; DE Flags: Fragment; GN ORFNames=AAUPMC_09613 {ECO:0000313|EMBL:EJS89794.1}; OS Pasteurella multocida subsp. multocida str. Anand1_cattle. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Pasteurella. OX NCBI_TaxID=1032867 {ECO:0000313|EMBL:EJS89794.1, ECO:0000313|Proteomes:UP000002749}; RN [1] {ECO:0000313|EMBL:EJS89794.1, ECO:0000313|Proteomes:UP000002749} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Anand1_cattle {ECO:0000313|EMBL:EJS89794.1, RC ECO:0000313|Proteomes:UP000002749}; RA Ahir V.B., Roy A., Jhala M.K., Mathakiya R.A., Bhanderi B.B., RA Bhatt V.D., Jakhesara S.J., Koringa P.G., Joshi C.G.; RL Submitted (JUL-2012) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EJS89794.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ALBY01001429; EJS89794.1; -; Genomic_DNA. DR EnsemblBacteria; EJS89794; EJS89794; AAUPMC_09613. DR Proteomes; UP000002749; Unassembled WGS sequence. DR InterPro; IPR025121; GTPase_HflX_N. DR Pfam; PF13167; GTP-bdg_N; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000002749}; KW Reference proteome {ECO:0000313|Proteomes:UP000002749}. FT DOMAIN 1 41 GTP-bdg_N. {ECO:0000259|Pfam:PF13167}. FT NON_TER 41 41 {ECO:0000313|EMBL:EJS89794.1}. SQ SEQUENCE 41 AA; 4382 MW; 74A88B961CDECFA5 CRC64; MGQGKAEEIA EAVQNTQADV VLVNHALTPA QTRNLESLCQ C // ID J5XYL8_9ACTN Unreviewed; 437 AA. AC J5XYL8; DT 31-OCT-2012, integrated into UniProtKB/TrEMBL. DT 31-OCT-2012, sequence version 1. DT 07-JUN-2017, entry version 30. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:EJU32782.1}; GN ORFNames=HMPREF1155_0972 {ECO:0000313|EMBL:EJU32782.1}; OS Slackia sp. CM382. OC Bacteria; Actinobacteria; Coriobacteriia; Eggerthellales; OC Eggerthellaceae; Slackia. OX NCBI_TaxID=1111137 {ECO:0000313|EMBL:EJU32782.1, ECO:0000313|Proteomes:UP000004399}; RN [1] {ECO:0000313|EMBL:EJU32782.1, ECO:0000313|Proteomes:UP000004399} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CM382 {ECO:0000313|EMBL:EJU32782.1, RC ECO:0000313|Proteomes:UP000004399}; RA Durkin A.S., McCorrison J., Torralba M., Gillis M., Methe B., RA Sutton G., Nelson K.E.; RL Submitted (JUL-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EJU32782.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ALNO01000016; EJU32782.1; -; Genomic_DNA. DR RefSeq; WP_009078351.1; NZ_ALNO01000016.1. DR EnsemblBacteria; EJU32782; EJU32782; HMPREF1155_0972. DR PATRIC; fig|1111137.3.peg.1256; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000004399; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000004399}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000004399}. FT DOMAIN 215 380 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 437 AA; 47502 MW; 089C43C8BB6B3D6C CRC64; MSFGISDQAA SMEQAERAVL VGIERKGDPD AAMRLASTLS ELERLSETAG ASVVATTSQR LVSPNPRTFV GTGKAEEIAS LCLAHAADVV IFDEELTPAQ QGNLEKIMPQ NVKVIDRTAL ILDIFALHAT SKEGRLQVRL AQNQYLLPRL RGMWAHLASN RMGGGVGSRF GEGESQLEVD RRLVRKRITT IRRELDHLAS VRAVQRRSRR LSGVFRIAEA GYTNAGKSSL INALTGADVL SYDKLFATLD STTRRLSLPE GRDATITDTV GFIQKLPTNL IEAFRSTLDE ISEADLILHV VDASSPRRDA QAKAVVETLG LIGAQDIPCM VVCNKVDLLG GEERAELIRQ HSDACLVSAR TGEGMDALRA AIVERIAAYE VPVVLSVPFD RGDAVSRVHS ECTVLEESYD ERGTTVVARI PSGLLEAYAP FIVRDDD // ID J6HFA5_9FIRM Unreviewed; 429 AA. AC J6HFA5; DT 31-OCT-2012, integrated into UniProtKB/TrEMBL. DT 31-OCT-2012, sequence version 1. DT 07-JUN-2017, entry version 31. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:EJU21433.1}; GN ORFNames=HMPREF1143_0297 {ECO:0000313|EMBL:EJU21433.1}; OS Peptoanaerobacter stomatis. OC Bacteria; Firmicutes; Clostridia; Clostridiales; OC Peptostreptococcaceae; Peptoanaerobacter. OX NCBI_TaxID=796937 {ECO:0000313|EMBL:EJU21433.1, ECO:0000313|Proteomes:UP000005244}; RN [1] {ECO:0000313|EMBL:EJU21433.1, ECO:0000313|Proteomes:UP000005244} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=OBRC8 {ECO:0000313|EMBL:EJU21433.1, RC ECO:0000313|Proteomes:UP000005244}; RA Durkin A.S., McCorrison J., Torralba M., Gillis M., Methe B., RA Sutton G., Nelson K.E.; RL Submitted (JUL-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EJU21433.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ALNK01000027; EJU21433.1; -; Genomic_DNA. DR RefSeq; WP_009531281.1; NZ_ALNK01000027.1. DR EnsemblBacteria; EJU21433; EJU21433; HMPREF1143_0297. DR PATRIC; fig|796941.3.peg.1585; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000005244; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000005244}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000005244}. FT DOMAIN 204 374 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 429 AA; 48941 MW; 85B5697FAC0D5AAD CRC64; MSDTKNIEKV ILVGLNITTN IKKQTDIDIY DSMKELEELA QAAGTKILGT TVQNKETYDA AYYIGKGKAE ELAELAENME ADTIIFNEEL SGVQIKNLEE ITKAKVIDRT TLILDIFASR ALSKEGKLQV ELAQQKYRSA RLIGLGSQLS RLGGGIGTRG PGEKKLEIDK RHIKQRIIDI QKELKEISKN RQTQRSSRAK SNLPLVALVG YTNSGKSTIL NEIIKTHKDY DKEKEVYVQD MLFATLDVQL RKATLPSNSD YLITDTVGFV SQIPHDLIEA FKATLEEVKY ADLLLHVVDL SNDKYKLQMD TTNKVLSEIG VDNKKVLYVF NKADKVNYEA NISVNEPFIM ISATKRYNID KFYEMIEQML SKSKKKVELL IPYSNSDIIN KLHDKYNFEE IYEENGTRLK VSLEEEEYGR YKNFITQEF // ID J6J8E9_9RHOB Unreviewed; 465 AA. AC J6J8E9; DT 31-OCT-2012, integrated into UniProtKB/TrEMBL. DT 31-OCT-2012, sequence version 1. DT 07-JUN-2017, entry version 30. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=A33M_2258 {ECO:0000313|EMBL:EJW12135.1}; OS Rhodovulum sp. PH10. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae; Rhodovulum. OX NCBI_TaxID=1187851 {ECO:0000313|EMBL:EJW12135.1, ECO:0000313|Proteomes:UP000002930}; RN [1] {ECO:0000313|EMBL:EJW12135.1, ECO:0000313|Proteomes:UP000002930} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=PH10 {ECO:0000313|EMBL:EJW12135.1, RC ECO:0000313|Proteomes:UP000002930}; RX PubMed=23105089; DOI=10.1128/JB.01695-12; RA Khatri I., Nupur, Korpole S., Subramanian S., Pinnaka A.K.; RT "Draft Genome Sequence of Rhodovulum sp. Strain PH10, a Phototrophic RT Alphaproteobacterium Isolated from a Soil Sample of Mangrove of RT Namkhana, India."; RL J. Bacteriol. 194:6363-6363(2012). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EJW12135.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AKZI01000036; EJW12135.1; -; Genomic_DNA. DR RefSeq; WP_008385170.1; NZ_AKZI01000036.1. DR EnsemblBacteria; EJW12135; EJW12135; A33M_2258. DR PATRIC; fig|1187851.3.peg.1501; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000002930; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000002930}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000002930}. FT DOMAIN 229 402 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 465 AA; 51044 MW; 5C49452CB1B4A4FF CRC64; MEPRRQDRSA DRPSPPTGSA TARCVVLGPY LRNPEPRSAG ATAPGHEADT RSPEARLDEA TGLARAIDLD VVESGIVLLG AVRPSTYLGK GKVEEIAGLV KSTEASLVVM DCALSPVQQR NLEKAWNAKV VDRTGLILEI FGRRAATREG TLQVELAHLT YQKSRLVRSW THLERQRGGF GFLGGPGETQ LETDRRIIQD RIRRIEHDLD TVKRTRALHR TSRKRVPYPI VALVGYTNAG KSTLFNRLTR SGVLATDMLF ATLDPTLRAV DLPDGPRVIL SDTVGFVSDL PTMLVAAFRA TLEEVIEADL ILHVRDVSHG DTQAQSKDVD TVLAELGIPP EDPRLLEVWN KIDNVSAEER ERLENLASRR PPEKRPQLVS ATTGQGLDAL IRDISERVAK TRVPLTVTLD AADGAGFGWL HRHGDVLETS TSEDGVTTVQ LRVHPSREGQ VRAKFGDRVQ GTETP // ID J7IZA3_DESMD Unreviewed; 536 AA. AC J7IZA3; DT 31-OCT-2012, integrated into UniProtKB/TrEMBL. DT 31-OCT-2012, sequence version 1. DT 07-JUN-2017, entry version 30. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Desmer_2465 {ECO:0000313|EMBL:AFQ44383.1}; OS Desulfosporosinus meridiei (strain ATCC BAA-275 / DSM 13257 / NCIMB OS 13706 / S10). OC Bacteria; Firmicutes; Clostridia; Clostridiales; Peptococcaceae; OC Desulfosporosinus. OX NCBI_TaxID=768704 {ECO:0000313|EMBL:AFQ44383.1, ECO:0000313|Proteomes:UP000005262}; RN [1] {ECO:0000313|EMBL:AFQ44383.1, ECO:0000313|Proteomes:UP000005262} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-275 / DSM 13257 / NCIMB 13706 / S10 RC {ECO:0000313|Proteomes:UP000005262}; RX PubMed=23105050; DOI=10.1128/JB.01392-12; RA Pester M., Brambilla E., Alazard D., Rattei T., Weinmaier T., Han J., RA Lucas S., Lapidus A., Cheng J.F., Goodwin L., Pitluck S., Peters L., RA Ovchinnikova G., Teshima H., Detter J.C., Han C.S., Tapia R., RA Land M.L., Hauser L., Kyrpides N.C., Ivanova N.N., Pagani I., RA Huntmann M., Wei C.L., Davenport K.W., Daligault H., Chain P.S., RA Chen A., Mavromatis K., Markowitz V., Szeto E., Mikhailova N., RA Pati A., Wagner M., Woyke T., Ollivier B., Klenk H.P., Spring S., RA Loy A.; RT "Complete genome sequences of Desulfosporosinus orientis DSM765T, RT Desulfosporosinus youngiae DSM17734T, Desulfosporosinus meridiei RT DSM13257T, and Desulfosporosinus acidiphilus DSM22704T."; RL J. Bacteriol. 194:6300-6301(2012). RN [2] {ECO:0000313|Proteomes:UP000005262} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-275 / DSM 13257 / NCIMB 13706 / S10 RC {ECO:0000313|Proteomes:UP000005262}; RA Huntemann M., Wei C.-L., Han J., Detter J.C., Han C., Davenport K., RA Daligault H., Erkkila T., Gu W., Munk A.C.C., Teshima H., Xu Y., RA Chain P., Tapia R., Chen A., Krypides N., Mavromatis K., Markowitz V., RA Szeto E., Ivanova N., Mikhailova N., Ovchinnikova G., Pagani I., RA Pati A., Goodwin L., Peters L., Pitluck S., Woyke T., Pester M., RA Spring S., Ollivier B., Rattei T., Klenk H.-P., Wagner M., Loy A.; RT "Finished genome of Desulfosporosinus meridiei DSM 13257."; RL Submitted (AUG-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP003629; AFQ44383.1; -; Genomic_DNA. DR EnsemblBacteria; AFQ44383; AFQ44383; Desmer_2465. DR KEGG; dmi:Desmer_2465; -. DR KO; K03665; -. DR OMA; EREVIIT; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000005262; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000005262}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000005262}. FT DOMAIN 368 536 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 327 361 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 536 AA; 59762 MW; 8173C4F389610A88 CRC64; MMDISGDLSG IRASQIQELK NLSGIKTERS ELIHPEILNE LIRLTELWNR EIAVYLARNG NLLASAVGRH ATVTLPPVKG RSLGKHLRCI HTHPNGNHKL SSLDYSALES LGLESMVSIG VFQGSLTGIE IAFRMEEQSP YIVNLTPQKW TEFDYYASLS DLSKSKGKTK NESGQAGKER AFLIALEDSE SETNEDLLEL RELARTAGVD VVGQLVQLRR YGQTRSYFGS GKLEELIHRL QETDANVLIC DDELSPTQLR TLEAETGLKV LDRTGLILDI FAQRAQSREG KLQVELAQLK HLLPHLTGQG LALSRLGAGV GSRGPGETKL ELDRRRMRDR INQLEKELKL VLQQRDVLRR QRTRSGLPLI ALVGYTNAGK TTFMTKAMEQ AGSRSDLPVG ENKLFATLDP IVRSIRIDSS LEILLSDTVG FIRKLPTQLL RAFMATLEEV KQADVLIHIV DASHPQAVHH AETVHEVLSQ LESADKPMIT LLNKIDQVYE EDLSQLTSYL PYPIKISLKQ GDSLKPVWKV LSSLLN // ID J7L902_NOCAA Unreviewed; 453 AA. AC J7L902; DT 31-OCT-2012, integrated into UniProtKB/TrEMBL. DT 31-OCT-2012, sequence version 1. DT 07-JUN-2017, entry version 33. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:AFR06952.1}; GN OrderedLocusNames=B005_3586 {ECO:0000313|EMBL:AFR06952.1}; OS Nocardiopsis alba (strain ATCC BAA-2165 / BE74). OC Bacteria; Actinobacteria; Streptosporangiales; Nocardiopsaceae; OC Nocardiopsis. OX NCBI_TaxID=1205910 {ECO:0000313|EMBL:AFR06952.1, ECO:0000313|Proteomes:UP000003779}; RN [1] {ECO:0000313|Proteomes:UP000003779} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-2165 / BE74 {ECO:0000313|Proteomes:UP000003779}; RA Qiao J., Chen L., Li Y., Wang J., Zhang W., Chen S.; RT "Whole-genome sequence of Nocardiopsis alba strain ATCC BAA-2165 RT associated with honeybees."; RL Submitted (AUG-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP003788; AFR06952.1; -; Genomic_DNA. DR EnsemblBacteria; AFR06952; AFR06952; B005_3586. DR KEGG; nal:B005_3586; -. DR PATRIC; fig|1205910.3.peg.3393; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000003779; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 2. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000003779}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000003779}. FT DOMAIN 232 397 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 191 218 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 453 AA; 48991 MW; 3A32AC50514DC119 CRC64; MELAERHALR RVQGLSTELT DVTEVENRSL RLERVVLIGV WTRGTQADAD NSLTELAALA ETAGALVLEG LTQRRAKPDP ATYIGKGKAA ELRDAVAATG ADTVICDGEL TPGQLIQLED VVKVKVIDRT ALILDIFAQH ARSSEGKAQV ELAQLSYLLP RLRGWGHTLS RQAGGAGGGG NGGVGLRGPG ETKIETDRRR INDKIAKLRR QLSHMRTARD VKRDVRRTRQ VPSVALAGYT NAGKSSLLNR LTGAGVLVEN ALFATLDPTV RQARTPDGRG FTLSDTVGFV RHLPHQLVEA FRSTLEEVSD ADLILHVVDG SHPDPEQQLS AVREVFADID AGDVRELIVV NKVDAADPDT LKTLRTRHPD LVEVSARTGE GIPELVTALA EALPEIAQEV RALVPYSRGD LIARAHEEGR IIGEEHTGEG TELHAFVPAP LAARLEEYAL TRV // ID J7QL26_METSZ Unreviewed; 443 AA. AC J7QL26; DT 31-OCT-2012, integrated into UniProtKB/TrEMBL. DT 31-OCT-2012, sequence version 1. DT 07-JUN-2017, entry version 34. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=BN69_0227 {ECO:0000313|EMBL:CCJ05678.1}; OS Methylocystis sp. (strain SC2). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Methylocystaceae; Methylocystis. OX NCBI_TaxID=187303 {ECO:0000313|EMBL:CCJ05678.1, ECO:0000313|Proteomes:UP000005263}; RN [1] {ECO:0000313|EMBL:CCJ05678.1, ECO:0000313|Proteomes:UP000005263} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SC2 {ECO:0000313|EMBL:CCJ05678.1, RC ECO:0000313|Proteomes:UP000005263}; RX PubMed=23045511; DOI=10.1128/JB.01446-12; RA Dam B., Dam S., Kube M., Reinhardt R., Liesack W.; RT "Complete Genome Sequence of Methylocystis sp. Strain SC2, an Aerobic RT Methanotroph with High-Affinity Methane Oxidation Potential."; RL J. Bacteriol. 194:6008-6009(2012). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; HE956757; CCJ05678.1; -; Genomic_DNA. DR RefSeq; WP_014889712.1; NC_018485.1. DR EnsemblBacteria; CCJ05678; CCJ05678; BN69_0227. DR KEGG; msc:BN69_0227; -. DR PATRIC; fig|187303.17.peg.253; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000005263; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000005263}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000005263}. FT DOMAIN 203 377 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 443 AA; 48753 MW; D6B0BA64D4FE2F05 CRC64; MTPNGAGARA LVIGPYLAQG AALSRDTAAR LMEAVGLAEA IDLDVVGQVP VSLNEVRPAT YLGKGKVEEI GELVKSKDAA LVSMDCQLSP VQQRNLERAW DAKVIDRTGL ILEIFGERAR TKEGALQVEL AHLAYQKSRL VRSWTHLERQ RGGFGFLGGP GETQIETDRR LIEERMRRIE HDLDKVKRTR ALHRKTRRDI PYPVVALVGY TNAGKSTLFN RLTKAEVLAQ DMLFATLDPT LRQIKLPHGA RILLSDTVGF ISDLPTMLVS AFRATLEEVT LADVVLHVRD VAHEDWEAQA KDVEAILSEL GLTGEAEGRV LEVWNKIDAL DPERLSALQH AVSGIEPQRR PTLVSALTGQ GLDELLARIE SALAAGRVRF EMDLDVADGE GLAWLHAHTE VLEREALPEG GVHLVVRIDP ERSEGLARRF PQAEIIREAG AGR // ID J7U4G3_MORMO Unreviewed; 426 AA. AC J7U4G3; DT 31-OCT-2012, integrated into UniProtKB/TrEMBL. DT 31-OCT-2012, sequence version 1. DT 30-AUG-2017, entry version 40. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=MU9_214 {ECO:0000313|EMBL:AGG29260.1}; OS Morganella morganii subsp. morganii KT. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; OC Morganellaceae; Morganella. OX NCBI_TaxID=1124991 {ECO:0000313|EMBL:AGG29260.1, ECO:0000313|Proteomes:UP000011834}; RN [1] {ECO:0000313|EMBL:AGG29260.1, ECO:0000313|Proteomes:UP000011834} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=KT {ECO:0000313|EMBL:AGG29260.1}; RX PubMed=23282187; RA Chen Y.T., Peng H.L., Shia W.C., Hsu F.R., Ken C.F., Tsao Y.M., RA Chen C.H., Liu C.E., Hsieh M.F., Chen H.C., Tang C.Y., Ku T.H.; RT "Whole-genome sequencing and identification of Morganella morganii KT RT pathogenicity-related genes."; RL BMC Genomics 13:S4-S4(2012). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP004345; AGG29260.1; -; Genomic_DNA. DR RefSeq; WP_004234480.1; NC_020418.1. DR EnsemblBacteria; AGG29260; AGG29260; MU9_214. DR GeneID; 14669425; -. DR KEGG; mmk:MU9_214; -. DR KO; K03665; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000011834; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000011834}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000011834}. FT DOMAIN 198 365 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 426 AA; 48023 MW; 96009AFE9F62340D CRC64; MFDRYEGGER AVLVHIFFSQ DKNTDDLSEF ESLVTSAGVT PVQIVTGSRS APHPKYFAGE GKAEEIADAV TESEADVVLF NHALSPAQER NLERLCQCRV VDRTGVILDI FAQRARTHEG KLQVELAQLR HLSTRLVRGW THLERQKGGI GLRGPGETQL ESDRRMLRDK IKQISGRLEK VERQRGQGRQ ARSKADIPTV SLVGYTNAGK SSLFNHITDA KVYAADQLFA TLDPTLRRID VDDVGTVVLA DTVGFIRHLP HDLVAAFKAT LQETREATLL LHVVDAADNR VDENIHAVNA VLEEIDAHEI PVLIVMNKID MLDDFEPRID RNEDNLPVRV WLSAQTGAGI PLLFRALTER LSGEIAHLEL CLPPSEGRLR SRFYQLQAIE REWLDDDGRI CLEIRLPIVD WRRLCKQEQQ LADYVI // ID J8VTX6_9SPHN Unreviewed; 464 AA. AC J8VTX6; DT 31-OCT-2012, integrated into UniProtKB/TrEMBL. DT 31-OCT-2012, sequence version 1. DT 05-JUL-2017, entry version 30. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=LH128_05345 {ECO:0000313|EMBL:EJU14105.1}; OS Sphingomonas sp. LH128. OC Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales; OC Sphingomonadaceae; Sphingomonas. OX NCBI_TaxID=473781 {ECO:0000313|EMBL:EJU14105.1, ECO:0000313|Proteomes:UP000004402}; RN [1] {ECO:0000313|EMBL:EJU14105.1, ECO:0000313|Proteomes:UP000004402} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=LH128 {ECO:0000313|EMBL:EJU14105.1, RC ECO:0000313|Proteomes:UP000004402}; RX PubMed=24657861; DOI=10.1128/AEM.00306-14; RA Fida T.T., Breugelmans P., Lavigne R., van der Meer J.R., De Mot R., RA Vaysse P.J., Springael D.; RT "Identification of opsA, a Gene Involved in Solute Stress Mitigation RT and Survival in Soil, in the Polycyclic Aromatic Hydrocarbon-Degrading RT Bacterium Novosphingobium sp. Strain LH128."; RL Appl. Environ. Microbiol. 80:3350-3361(2014). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EJU14105.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ALVC01000054; EJU14105.1; -; Genomic_DNA. DR PATRIC; fig|473781.5.peg.1059; -. DR Proteomes; UP000004402; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000004402}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000004402}. FT DOMAIN 210 408 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 464 AA; 51755 MW; 3C8FCC68DE603BFD CRC64; MNDELKGEVT RGARALVVYP QMRGPRGERN DLDPEARLEE ARGLALAIGL EVVEAMAIVI REARPGTLFG EGQIQNISTA CTLNEAELII VDGSLSAIQQ RNLEEKLKRK VIDRTGLILE IFGERAATAE GRLQVELAHL DYQAGRLVRS WTHLERQRGG FGFLGGPGET QIEADRRMIR DRMAKIRREL EQVRRTRGLH RDRREKAPWP VVALVGYTNA GKSTLFNRLT GASVMAENLL FATLDPTMRA IRMPGLEKAI LSDTVGFISD LPTELIAAFR ATLEEVTAAD VILHVRDIAN PDTEAQKRQV LDVLADLGVI QPPLDDRKAR QAPALDWSDD EPDDEPEPQV PIIEVWNKWD LLDPDQAHEL REVAMHREGE VIVPVSALTG EGCDALLDIA SRNLTRDSRI YSFVLPVADG QRFAFLHARG EVVSEEDAGE GEQGPQMRLE VRLSEREFGR FKAL // ID J9F1E9_WUCBA Unreviewed; 445 AA. AC J9F1E9; DT 31-OCT-2012, integrated into UniProtKB/TrEMBL. DT 31-OCT-2012, sequence version 1. DT 07-JUN-2017, entry version 18. DE SubName: Full=GTP-binding protein HflX {ECO:0000313|EMBL:EJW88323.1}; GN ORFNames=WUBG_00767 {ECO:0000313|EMBL:EJW88323.1}; OS Wuchereria bancrofti. OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Spirurida; OC Filarioidea; Onchocercidae; Wuchereria. OX NCBI_TaxID=6293 {ECO:0000313|EMBL:EJW88323.1, ECO:0000313|Proteomes:UP000004810}; RN [1] {ECO:0000313|Proteomes:UP000004810} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NA {ECO:0000313|Proteomes:UP000004810}; RA Nutman T.B., Fink D.L., Russ C., Young S., Zeng Q., Koehrsen M., RA Alvarado L., Berlin A., Chapman S.B., Chen Z., Freedman E., RA Gellesch M., Goldberg J., Griggs A., Gujja S., Heilman E.R., RA Heiman D., Hepburn T., Howarth C., Jen D., Larson L., Lewis B., RA Mehta T., Park D., Pearson M., Roberts A., Saif S., Shea T., RA Shenoy N., Sisk P., Stolte C., Sykes S., Walk T., White J., RA Yandava C., Haas B., Henn M.R., Nusbaum C., Birren B.; RT "The Genome Sequence of Wuchereria bancrofti."; RL Submitted (AUG-2012) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EJW88323.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADBV01000146; EJW88323.1; -; Genomic_DNA. DR InParanoid; J9F1E9; -. DR Proteomes; UP000004810; Unassembled WGS sequence. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR CDD; cd01878; HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000004810}; KW Reference proteome {ECO:0000313|Proteomes:UP000004810}. FT DOMAIN 221 384 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 445 AA; 50615 MW; 2AE5ADAE05AA5CD4 CRC64; MNDEFNIISK SYGIQSIAPG VQRILLIHPR LRRGRFFDLN PARAKLQLEE AVALVNTLPN FKVMETTAVS TDRSTKKKRL WGSGRIQRII ALKEKISATA LMIDVDILSP KQQAELTSIF RTPIYDRYNI VLLIFKIFAK TKEAKLQIQL AEIPYIRQRL LSMYELHVDP SLLHLDTSEK SKTERLEVLR YREQHLRKCL KAAVEEKVNL RIGEAQKNIR TVVAVVGYTN AGKSSLIKRL TGRNLYVEDR LFATLDTSLH VFRLPSGLPI LFADTIGFIS NLPTQLLASF QATLNHVANA DLLLHVEDVS NPDYLTQRNV VMKTLSALKV RNELLKSVIR VGNKIDKLCR LPPNEPNTYF VSCADGRGFV ELLAAVDKRV LTISGVTIRR LKLRPHSEAF SYLCKYSFLV GQPIPSEDNN YLLCNVVMDD NEFSKFRANF SFSKI // ID J9HCG0_9BACL Unreviewed; 426 AA. AC J9HCG0; DT 31-OCT-2012, integrated into UniProtKB/TrEMBL. DT 31-OCT-2012, sequence version 1. DT 07-JUN-2017, entry version 31. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=URH17368_2304 {ECO:0000313|EMBL:EJY55149.1}; OS Alicyclobacillus hesperidum URH17-3-68. OC Bacteria; Firmicutes; Bacilli; Bacillales; Alicyclobacillaceae; OC Alicyclobacillus. OX NCBI_TaxID=1200346 {ECO:0000313|EMBL:EJY55149.1, ECO:0000313|Proteomes:UP000035011}; RN [1] {ECO:0000313|EMBL:EJY55149.1, ECO:0000313|Proteomes:UP000035011} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=URH17-3-68 {ECO:0000313|EMBL:EJY55149.1, RC ECO:0000313|Proteomes:UP000035011}; RX PubMed=23105079; DOI=10.1128/JB.01612-12; RA Wang P., Li L., Chen X., Jiang N., Liu G., Chen L., Xu J., Song H., RA Chen Z., Ma Y.; RT "Draft Genome Sequence of Alicyclobacillus hesperidum Strain URH17-3- RT 68."; RL J. Bacteriol. 194:6348-6348(2012). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EJY55149.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AKZN01000049; EJY55149.1; -; Genomic_DNA. DR EnsemblBacteria; EJY55149; EJY55149; URH17368_2304. DR PATRIC; fig|1200346.3.peg.2361; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000035011; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000035011}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000035011}. FT DOMAIN 197 363 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 164 191 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 426 AA; 47450 MW; 9727A88F75590EBA CRC64; MTEQRDRVIL VMCQTGRESE DRFSYRKDEL KGLCEAAGAL VIGVVTQKRP AADPRTLVGE GKVFELVDLV ERGEATLVVA DRELSPAQVR NLERYLPCRV IDRTQLILDI FARRAVTREG RVQVEMAQLS YLLPRLTGRG AEMSRLGGGI GTRGPGETKL ELDRRRIRTR LAGLRRELEA IARQRATARD KRLREVPTVA LVGYTNAGKT TLQARWVADK GGGGAITGEN RLFDTLDPAA RQVRTRLGHP YVVIDTVGFV ENLPHHLVEA FRSTLEEARH ADVIVVVVDA GHAPSAHLAT TRRVLADLGA LDKPIITFFN KVDTVAEPPG PDVGALVSLY GSARHGDLDE LYHAVERQLE LDEVHVTIHA REDDTEWQSL LRGGRIEHAE TTASGEWRMT AVTSRKQAHL WQQMQRDGSE HDNRHP // ID J9HMD5_9ACTN Unreviewed; 483 AA. AC J9HMD5; DT 31-OCT-2012, integrated into UniProtKB/TrEMBL. DT 31-OCT-2012, sequence version 1. DT 07-JUN-2017, entry version 30. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=A27L6_004500000020 {ECO:0000313|EMBL:EJX36434.1}; OS actinobacterium SCGC AAA027-L06. OC Bacteria; Actinobacteria. OX NCBI_TaxID=913338 {ECO:0000313|EMBL:EJX36434.1, ECO:0000313|Proteomes:UP000006343}; RN [1] {ECO:0000313|EMBL:EJX36434.1, ECO:0000313|Proteomes:UP000006343} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SCGC AAA027-L06 {ECO:0000313|EMBL:EJX36434.1, RC ECO:0000313|Proteomes:UP000006343}; RG US DOE Joint Genome Institute (JGI-PGF); RA Han J., Cheng J.-F., Goodwin L., Pitluck S., Peters L., Huntemann M., RA Wei C.-L., Han J., Chen A., Kyrpides N., Mavrommatis K., Markowitz V., RA Szeto E., Pagani I., Pati A., Garcia S.L., McMahon T., Srivastava A., RA Grossart H.-P., Martinez M., Stepanauskas R., Sczyrba A., Warnecke F., RA Woyke T.J.; RT "The standard draft genome of actinobacterium SCGC AAA027-L06."; RL Submitted (AUG-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EJX36434.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AJWB01000036; EJX36434.1; -; Genomic_DNA. DR EnsemblBacteria; EJX36434; EJX36434; A27L6_004500000020. DR PATRIC; fig|913338.3.peg.350; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000006343; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000006343}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000006343}. FT DOMAIN 267 432 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 233 260 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 483 AA; 52904 MW; D37BAD0BB12AC9B2 CRC64; MSESKFGSDD GLEIDIDTLI RENAQAVADY ELQDSDESNN QDLQDRQALR RVNGLSTELQ DVSDAEYRQL RLEKVVLVGV WTEGTSKDAD NSLKELAALA ETAGSQVMDA LIQRRDKPDP ATFIGSGKVT EVRQAVVATG ADTVICDGEL SPAQLRTLEQ KVKVKVVDRT ALILDIFAQH AKSREGKAQV ELAQMSYMLP RLRGWGESLS RQSGGTGGIG GRGPGETKIE TDRRRINDKM SKLRREIKEM KISRDIKRNE RRKNNIPSVA IAGYTNAGKS SLLNRLTGVD VLVENALFAT LDPTVRKTQS HDGRVYTFVD TVGFVRHLPH QLVEAFKSTL EEVSQSDLIV HVVDGSHPDP MEQIRAVRQV INEIGGGEIL EIIAINKADI AAPEVLMELL RTESNAYAIS ARTGYGVPTL VKAIESALPK PNVEINAVIP FSRGDLVSAV HETGEIISEE YLPEGTKIHA MVGGALARKI ELL // ID J9IW57_9SPIT Unreviewed; 730 AA. AC J9IW57; DT 31-OCT-2012, integrated into UniProtKB/TrEMBL. DT 31-OCT-2012, sequence version 1. DT 30-AUG-2017, entry version 18. DE SubName: Full=Small GTP-binding protein domain containing protein {ECO:0000313|EMBL:EJY76820.1}; GN ORFNames=OXYTRI_01662 {ECO:0000313|EMBL:EJY76820.1}; OS Oxytricha trifallax. OC Eukaryota; Alveolata; Ciliophora; Intramacronucleata; Spirotrichea; OC Stichotrichia; Sporadotrichida; Oxytrichidae; Oxytrichinae; Oxytricha. OX NCBI_TaxID=1172189 {ECO:0000313|EMBL:EJY76820.1, ECO:0000313|Proteomes:UP000006077}; RN [1] {ECO:0000313|EMBL:EJY76820.1, ECO:0000313|Proteomes:UP000006077} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SB310 {ECO:0000313|Proteomes:UP000006077}; RX PubMed=23382650; DOI=10.1371/journal.pbio.1001473; RA Swart E.C., Bracht J.R., Magrini V., Minx P., Chen X., Zhou Y., RA Khurana J.S., Goldman A.D., Nowacki M., Schotanus K., Jung S., RA Fulton R.S., Ly A., McGrath S., Haub K., Wiggins J.L., Storton D., RA Matese J.C., Parsons L., Chang W.J., Bowen M.S., Stover N.A., RA Jones T.A., Eddy S.R., Herrick G.A., Doak T.G., Wilson R.K., RA Mardis E.R., Landweber L.F.; RT "The Oxytricha trifallax Macronuclear Genome: A Complex Eukaryotic RT Genome with 16,000 Tiny Chromosomes."; RL PLoS Biol. 11:E1001473-E1001473(2013). CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EJY76820.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AMCR01011079; EJY76820.1; -; Genomic_DNA. DR EnsemblProtists; EJY76820; EJY76820; OXYTRI_01662. DR Proteomes; UP000006077; Unassembled WGS sequence. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR CDD; cd01878; HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000006077}; KW Reference proteome {ECO:0000313|Proteomes:UP000006077}. FT DOMAIN 461 638 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 730 AA; 83908 MW; 39419C5E6752F684 CRC64; MGQKRTFSQL QSEDSMDDQS VHCLTLHPIT WPNRGPKIEL YLAEEAIGLV KSLNWTVATG LNYDEDHEES QHEQDNDQQK LKKQLDMDDN HQNNKQQEEA SENSDLSDGG TSKKVNKTDR SKLIKAYKEK QKLDAGADDY EKYFEDSEVK KIRGGSGKRS VRVSHAKNAK NVKTEGIRNG DFIYAPNELK GVYHNGGLIL EFDEEGNEDT VFDEWKNPAL RESIAISSIV KLRKIHSGTY FQKGKLNELG YFLKENPDIN VVYINSTLTG LQQKKLEKRF NDIVQSRDDK LRNYYLRSAL KEKFNPTDVE SDTSQMSELE QNNQDKNQNR NIRVIDRFGI ILQIFAQRAK TRTAQLQIEL AWLSYAKTML VRGGAPTFGQ LGNIFSGNMM RRDIAEMEIK SAKGRKSGAS GTMGGEGETQ LEIERRRLGD REAKILKELG DLDKKTQNEK LKKERSHNTL PLIGLIGYTN AGKTALMNLV TGSKLESQDL LFQTLNTTNK RFRFENGQNA LMLDTIGFIT NLPHGLIESF KSTLEEIHFA DILVHVRDIS HPYSNYQRDT VLRVLKEIGV DEETLRTKYV EVWNKIDLLK NQQEFMQQLI HEQEQAMPEY PVIMMSCKEG TNKALLMQEL TNMSSKLMGK KLTKLTYKYD MHDKVQRWLL ENASINSFDN DNIDYDYENG NITVRVNIDD VIYQQYLKKF ETEKFQDFKE NKSTPLKGIK SGRLTPPPGW // ID J9R761_RIEAN Unreviewed; 406 AA. AC J9R761; DT 28-NOV-2012, integrated into UniProtKB/TrEMBL. DT 28-NOV-2012, sequence version 1. DT 07-JUN-2017, entry version 31. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=B739_0598 {ECO:0000313|EMBL:AFR35202.1}; OS Riemerella anatipestifer RA-CH-1. OC Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales; OC Flavobacteriaceae; Riemerella. OX NCBI_TaxID=1228997 {ECO:0000313|EMBL:AFR35202.1, ECO:0000313|Proteomes:UP000006276}; RN [1] {ECO:0000313|EMBL:AFR35202.1, ECO:0000313|Proteomes:UP000006276} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=RA-CH-1 {ECO:0000313|EMBL:AFR35202.1, RC ECO:0000313|Proteomes:UP000006276}; RA Chun C.A., Shu W.M., Kang Z.D., Jia W.X.; RT "Riemerella anatipestifer vaccine strains."; RL Submitted (SEP-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP003787; AFR35202.1; -; Genomic_DNA. DR RefSeq; WP_004916260.1; NC_018609.1. DR ProteinModelPortal; J9R761; -. DR EnsemblBacteria; AFR35202; AFR35202; B739_0598. DR GeneID; 29730984; -. DR KEGG; rag:B739_0598; -. DR PATRIC; fig|1228997.3.peg.595; -. DR KO; K03665; -. DR Proteomes; UP000006276; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000006276}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000006276}. FT DOMAIN 200 384 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 406 AA; 47392 MW; 5F6D625981337229 CRC64; MLEKKEHLYE KAVLVGLITK DQDEDKLTEY LDELEFLAYT AGATVEKRFT QKLSQPDSRT FVGKGKMEEI RDFVKENEVG TVIFDDELSP SQLKNLEREM EVKILDRTNL ILDIFAQRAQ TSYARTQVEL AQYEYLLPRL TRMWTHLERQ RGGIGMRGPG ETEIETDRRI IRDRISLLKE KLKTIDKQMA TQRNNRGKMV RVALVGYTNV GKSTLMNVIS KSEVFAENKL FATLDTTVRK VVIGNLPFLL TDTVGFIRKL PTQLVESFKS TLDEVREADL LVHVVDISHE SFEDHIESVN QILQEIDAHR KPAIMIFNKI DDFSYEKKDE DDLTPATKKN ISLDEWRKTW MAKSKFPTVF ISALTKENFP EMKKLIYDEV HRIHISRFPY NDFLFQYYDN DAEIEE // ID J9SHW0_9ACTN Unreviewed; 482 AA. AC J9SHW0; DT 28-NOV-2012, integrated into UniProtKB/TrEMBL. DT 28-NOV-2012, sequence version 1. DT 07-JUN-2017, entry version 34. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=KTR9_2131 {ECO:0000313|EMBL:AFR48768.1}; OS Gordonia sp. KTR9. OC Bacteria; Actinobacteria; Corynebacteriales; Gordoniaceae; Gordonia. OX NCBI_TaxID=337191 {ECO:0000313|EMBL:AFR48768.1, ECO:0000313|Proteomes:UP000003281}; RN [1] {ECO:0000313|EMBL:AFR48768.1, ECO:0000313|Proteomes:UP000003281} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=KTR9 {ECO:0000313|EMBL:AFR48768.1, RC ECO:0000313|Proteomes:UP000003281}; RX PubMed=22923396; DOI=10.1128/AEM.02120-12; RA Chen H.P., Zhu S.H., Casabon I., Hallam S.J., Crocker F.H., Mohn W.W., RA Indest K.J., Eltis L.D.; RT "Genomic and transcriptomic studies of an RDX (hexahydro-1,3,5- RT trinitro-1,3,5-triazine)-degrading actinobacterium."; RL Appl. Environ. Microbiol. 78:7798-7800(2012). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002907; AFR48768.1; -; Genomic_DNA. DR EnsemblBacteria; AFR48768; AFR48768; KTR9_2131. DR KEGG; gor:KTR9_2131; -. DR PATRIC; fig|337191.3.peg.2427; -. DR KO; K03665; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000003281; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR002792; TRAM_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. DR PROSITE; PS50926; TRAM; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000003281}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}. FT DOMAIN 259 429 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT DOMAIN 422 482 TRAM. {ECO:0000259|PROSITE:PS50926}. FT COILED 218 245 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 482 AA; 51441 MW; 72A3C9AC67FDDBB4 CRC64; MTAADLGVRD TADPTGAGPA GADPTTGELQ LSERASLQRV AGLSTELTDV TEVEYRQLRL ERVVLVGVWT EGSAAAAKAN MAELAALAET AGSQILDAVI QRRSKPDPAT YIGSGKAEEL REIVLATGAD TVVCDGELTP AQLNALEKVV KVKVIDRTAL ILDIFAQHAT SREGKAQVSL AQMEYMLPRL RGWGESMSRQ AGGRAGSNGG VGLRGPGETK IETDRRRIRE RMAKLRREIR GMKKARTTKR AARKSGSIPT ITVAGYTNAG KSSLVNAMTG AGVLVQDALF ATLDPTTRRA TLDDGRAVVF TDTVGFVRHL PTQLVEAFRS TLEEVVDADL LLHVVDGADA FPMAQISAVR QVINDIVAEE GVTAPPELLV INKIDAIDGN RLTELRGALG SDAVFISART GEGLPELFGR VREFVGREDV EMTIEVPFDR GDVVSRVHSE GEVISSEHTE AGTTMKVRVP AAFAGEIADL RV // ID J9W5P8_LACBU Unreviewed; 428 AA. AC J9W5P8; DT 28-NOV-2012, integrated into UniProtKB/TrEMBL. DT 28-NOV-2012, sequence version 1. DT 07-JUN-2017, entry version 32. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=LBUCD034_1913 {ECO:0000313|EMBL:AFS00902.1}; OS Lactobacillus buchneri CD034. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; OC Lactobacillus. OX NCBI_TaxID=1071400 {ECO:0000313|EMBL:AFS00902.1, ECO:0000313|Proteomes:UP000007332}; RN [1] {ECO:0000313|EMBL:AFS00902.1, ECO:0000313|Proteomes:UP000007332} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CD034 {ECO:0000313|EMBL:AFS00902.1}; RX PubMed=22465289; DOI=10.1016/j.jbiotec.2012.03.007; RA Heinl S., Wibberg D., Eikmeyer F., Szczepanowski R., Blom J., RA Linke B., Goesmann A., Grabherr R., Schwab H., Puhler A., Schluter A.; RT "Insights into the completely annotated genome of Lactobacillus RT buchneri CD034, a strain isolated from stable grass silage."; RL J. Biotechnol. 161:153-166(2012). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP003043; AFS00902.1; -; Genomic_DNA. DR RefSeq; WP_014940415.1; NC_018610.1. DR EnsemblBacteria; AFS00902; AFS00902; LBUCD034_1913. DR KEGG; lbn:LBUCD034_1913; -. DR PATRIC; fig|1071400.3.peg.1830; -. DR KO; K03665; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000007332; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000007332}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000007332}. FT DOMAIN 204 372 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 428 AA; 48047 MW; 0973625ACE7131BD CRC64; MDLQVTLTPV VTIGLNRNTS SFEYSMTELN NLAEANNMKV VETLVQKLDR PDPATYFGKG KIEELTQVVI DDGVDTIVVN DELSPSQIRN IEKNTHSRII DRTGLILEIF ANRAQSREAK LQVELAKLKY QLPRLHTSAS QRLDQQTGTS SGAGGATNRG AGESQYELNR RTLEKRITHV NQELKETAKA DQTKRKQRDR SEMPTVALVG YTNAGKSTVM NGMINLYGEN EDKQVMVKNM LFATLDTSVR KLTLPDQKRF LLSDTVGFVS QLPHQLVQAF KSTLSEAANA DLLIQVVDYS DPHRELMMKT TEDTLSEIGV NGVPMIVALN KADKMEVAFP SREGDNLIMS AMDEKSLQEL TTMIKEKIFK NYHRLTLLIP FSDGDVVSYL NENTNIETTD YRDDGTVITA ELNDVDAKRF EKYLLTTE // ID J9Z8C8_LEPFM Unreviewed; 521 AA. AC J9Z8C8; DT 28-NOV-2012, integrated into UniProtKB/TrEMBL. DT 28-NOV-2012, sequence version 1. DT 07-JUN-2017, entry version 34. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=LFML04_0461 {ECO:0000313|EMBL:AFS52699.1}; OS Leptospirillum ferriphilum (strain ML-04). OC Bacteria; Nitrospirae; Nitrospirales; Nitrospiraceae; Leptospirillum. OX NCBI_TaxID=1048260 {ECO:0000313|EMBL:AFS52699.1, ECO:0000313|Proteomes:UP000006177}; RN [1] {ECO:0000313|EMBL:AFS52699.1, ECO:0000313|Proteomes:UP000006177} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ML-04 {ECO:0000313|EMBL:AFS52699.1, RC ECO:0000313|Proteomes:UP000006177}; RX PubMed=22203551; DOI=10.1007/s12275-011-1099-9; RA Mi S., Song J., Lin J., Che Y., Zheng H., Lin J.; RT "Complete genome of Leptospirillum ferriphilum ML-04 provides insight RT into its physiology and environmental adaptation."; RL J. Microbiol. 49:890-901(2011). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002919; AFS52699.1; -; Genomic_DNA. DR RefSeq; WP_014960219.1; NC_018649.1. DR EnsemblBacteria; AFS52699; AFS52699; LFML04_0461. DR KEGG; lfi:LFML04_0461; -. DR PATRIC; fig|1048260.3.peg.495; -. DR KO; K03665; -. DR OMA; EREVIIT; -. DR Proteomes; UP000006177; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000006177}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000006177}. FT DOMAIN 343 508 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 521 AA; 59391 MW; CAD5ED9999811453 CRC64; MNQMAEISHE TGRQIGILLS REGTVEDVLV GTPQDIYIEK LPASRGGDHL LRGLSLVHTH IKGEPLSQDD LNDLALLRLD AQIVVHMKPR LPQVDSFSLA TLDPDPKAPL PWTLEANLRV TPRNLEGHER IRSIEEEMRR VRTSSRHHLS ERERAILVSA SPDSVASQEE NVQELEELAL SAGVDVLGKE IQRIASYHPS TLLSRNRLKS LIIHALHVQA SLIIFEQNLS PVQVKTIADM TELKVIDRTQ LILDIFARRA HSSDGKLQVE LAQLRYLLPR LEKRSTALSR LTGGIGGRGP GETRLEEDRR RVRDRISHLS EKLDRVALER QNRKERRKER DVPIVSLVGY TNVGKSTLLN QLTGSSVLTE NRMFATLDPT TRRLRFPRER EIILTDTVGF IRNLPGDLRR AFLATFDELK DAHLLLHVAD AFHPKMEEQI QRVEELLKEM EIDRIPRILI LNKTDCLSPA ERDILSVRFP DAFQVAALDK TTLLPLLEEM ERRLFSRFLH DDPDRVLATR K // ID K0B075_CLOA9 Unreviewed; 430 AA. AC K0B075; DT 28-NOV-2012, integrated into UniProtKB/TrEMBL. DT 28-NOV-2012, sequence version 1. DT 07-JUN-2017, entry version 34. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Curi_c10370 {ECO:0000313|EMBL:AFS78051.1}; OS Clostridium acidurici (strain ATCC 7906 / CIP 104303 / DSM 604 / NCIMB OS 10678 / BCRC 14475 / NCCB 46094 / 9a) (Gottschalkia acidurici). OC Bacteria; Firmicutes; Clostridia; Clostridiales; Gottschalkia. OX NCBI_TaxID=1128398 {ECO:0000313|EMBL:AFS78051.1, ECO:0000313|Proteomes:UP000006094}; RN [1] {ECO:0000313|EMBL:AFS78051.1, ECO:0000313|Proteomes:UP000006094} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 7906 / CIP 104303 / DSM 604 / NCIMB 10678 / BCRC 14475 / RC NCCB 46094 / 9a {ECO:0000313|Proteomes:UP000006094}; RX PubMed=23240052; DOI=10.1371/journal.pone.0051662; RA Hartwich K., Poehlein A., Daniel R.; RT "The purine-utilizing bacterium Clostridium acidurici 9a: a genome- RT guided metabolic reconsideration."; RL PLoS ONE 7:E51662-E51662(2012). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP003326; AFS78051.1; -; Genomic_DNA. DR RefSeq; WP_014967188.1; NC_018664.1. DR EnsemblBacteria; AFS78051; AFS78051; Curi_c10370. DR KEGG; cad:Curi_c10370; -. DR PATRIC; fig|1128398.3.peg.1038; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000006094; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000006094}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000006094}. FT DOMAIN 202 373 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 430 AA; 48874 MW; A9C67135E3E0D9AF CRC64; MYEIEDDKLE KIIIVGVDRN KRGEITVESS MDELAELVKA ADGIVEGRVV QNREHIDSAY HIGKGKAEEI AVACEELDID TVVFNDELSG AQIRNLENII ERKIIDRTSL ILDIFAKRAT SKEGKLQVEL AQLKYRLPRL IGFRNYLSRT GGGIGTKGPG EQKLELDRRH ILGRINDIQR QLKELDKVRM VKRKQRRSND IPIVALVGYT NAGKSTLLNS LIRLDEDYKE EKEVFVKDML FATLETNLRK ATLPNGRDFL ITDTVGFVSK LPTHLVEAFK GTLEEVQFAD LLLHVVDITN EDLEIQMVTT MKIIKDLDVI DKPIITVFNK VDEGNIEDIA YKVPEPKIFI SAKTGHNLEL LLKMIEDNLP QSYYNVDLLI PFSKGDLLSY IFDNTKVESQ EHTAEGTLVT VTLDQADYNR CKEYIVDKNE // ID K0C6E9_ALCDB Unreviewed; 455 AA. AC K0C6E9; DT 28-NOV-2012, integrated into UniProtKB/TrEMBL. DT 28-NOV-2012, sequence version 1. DT 07-JUN-2017, entry version 37. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:AFT69059.1}; GN OrderedLocusNames=B5T_00775 {ECO:0000313|EMBL:AFT69059.1}; OS Alcanivorax dieselolei (strain DSM 16502 / CGMCC 1.3690 / B-5). OC Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales; OC Alcanivoracaceae; Alcanivorax. OX NCBI_TaxID=930169 {ECO:0000313|EMBL:AFT69059.1, ECO:0000313|Proteomes:UP000006286}; RN [1] {ECO:0000313|EMBL:AFT69059.1, ECO:0000313|Proteomes:UP000006286} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 16502 / CGMCC 1.3690 / B-5 RC {ECO:0000313|Proteomes:UP000006286}; RX PubMed=23144414; DOI=10.1128/JB.01813-12; RA Lai Q., Li W., Shao Z.; RT "Complete genome sequence of Alcanivorax dieselolei type strain B5."; RL J. Bacteriol. 194:6674-6674(2012). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP003466; AFT69059.1; -; Genomic_DNA. DR RefSeq; WP_014993140.1; NC_018691.1. DR EnsemblBacteria; AFT69059; AFT69059; B5T_00775. DR KEGG; adi:B5T_00775; -. DR PATRIC; fig|930169.3.peg.759; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000006286; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000006286}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Hydrolase {ECO:0000313|EMBL:AFT69059.1}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Protease {ECO:0000313|EMBL:AFT69059.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000006286}. FT DOMAIN 205 371 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 171 198 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 455 AA; 51276 MW; D3977011901A60B5 CRC64; MDLFERTEQV RTGAGERAIL VHMDLPDAFG REDLEEFHHL VVSSGVVPVA ELLGKRDRPD PALFIGSGKS EELAELVRQE EADVVLFNHA LSPAQERNLE RAAKCRVLDR TGLILDIFAQ RARTHEGRLQ VELAQLRHLA SRLVRGWTHL ERQKGGIGLR GPGETQLETD RRLIRDRIRA IEARLEKVRK QREQGRRARD RSETPLISLV GYTNAGKSTL FNALTTGEVY VADQLFATLD PTLRKVRVPG VGPAILADTV GFIRHLPHRL VEAFRATLEE TVNASLLLHI TDCSAEERDD NVASVNEVLE EIGADQVPVL HVYNKVDRFG DTPRLDRDEQ GRPWRVWLSA REQQGFDLLY QAIAERLAEH WVDRWLRLPP EAGRLRARLH EAGEVLAEEA GTDGAMLLRV HLNRVHFERL LREAGLSEKD VLVPAPQVAE GSAHSYNPER SHKAG // ID K0C7A5_CYCSP Unreviewed; 419 AA. AC K0C7A5; DT 28-NOV-2012, integrated into UniProtKB/TrEMBL. DT 28-NOV-2012, sequence version 1. DT 07-JUN-2017, entry version 34. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Q91_1552 {ECO:0000313|EMBL:AFT67587.1}; OS Cycloclasticus sp. (strain P1). OC Bacteria; Proteobacteria; Gammaproteobacteria; Thiotrichales; OC Piscirickettsiaceae; Cycloclasticus. OX NCBI_TaxID=385025 {ECO:0000313|EMBL:AFT67587.1, ECO:0000313|Proteomes:UP000006282}; RN [1] {ECO:0000313|EMBL:AFT67587.1, ECO:0000313|Proteomes:UP000006282} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=P1 {ECO:0000313|EMBL:AFT67587.1, RC ECO:0000313|Proteomes:UP000006282}; RX PubMed=23144416; DOI=10.1128/JB.01837-12; RA Lai Q., Li W., Wang B., Yu Z., Shao Z.; RT "Complete genome sequence of the pyrene-degrading bacterium RT Cycloclasticus sp. strain P1."; RL J. Bacteriol. 194:6677-6677(2012). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP003230; AFT67587.1; -; Genomic_DNA. DR RefSeq; WP_015006357.1; NC_018697.1. DR EnsemblBacteria; AFT67587; AFT67587; Q91_1552. DR KEGG; cyq:Q91_1552; -. DR PATRIC; fig|385025.3.peg.1587; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000006282; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000006282}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Hydrolase {ECO:0000313|EMBL:AFT67587.1}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Protease {ECO:0000313|EMBL:AFT67587.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000006282}. FT DOMAIN 200 367 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 419 AA; 47175 MW; 8C5D779D6102DE3B CRC64; MELFDRPGTG ERALIVHLSI NESFSEDDLS EFEQLVISAN VEPLATVTGS RRSPDARFFV GKGKLDEVKH QLHETCADIV LFNHTLSPSQ QRNLEKELEV RVLDRTNLIL DIFAQRAQSF EGKLQVELAQ LQHLSTRLIR GWTHLERQKG GIGLRGPGET QLETDRRLIG QRIRQIKTRL TKVNKQRDQG RRSRQRADVP TVSLVGYTNA GKSTLFNVLT NSAIYAADQL FATLDPTLRQ VKLPDYGELV LADTVGFIQN LPHELVAAFR STLQETIEAD LLLHVVDASS PNRQEQIHEV NSVLKEIGAD NIPQVMVYNK IDCLPAVDAH VDKDETDSVN AVWLSAMDGD GINLLLETLS TLCHDENTRM SVVLKPEQAK LRAKLFQVAQ ILKEENRDDG CWVIELNISN KYKHLLTTI // ID K0D8W6_ALTMS Unreviewed; 429 AA. AC K0D8W6; DT 28-NOV-2012, integrated into UniProtKB/TrEMBL. DT 28-NOV-2012, sequence version 1. DT 30-AUG-2017, entry version 35. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=AMBLS11_17285 {ECO:0000313|EMBL:AFT80022.1}; OS Alteromonas macleodii (strain Black Sea 11). OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales; OC Alteromonadaceae; Alteromonas. OX NCBI_TaxID=1004785 {ECO:0000313|EMBL:AFT80022.1, ECO:0000313|Proteomes:UP000006295}; RN [1] {ECO:0000313|Proteomes:UP000006295} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Black Sea 11 {ECO:0000313|Proteomes:UP000006295}; RX PubMed=23019517; DOI=10.1038/srep00696; RA Lopez-Perez M., Gonzaga A., Martin-Cuadrado A.B., Onyshchenko O., RA Ghavidel A., Ghai R., Rodriguez-Valera F.; RT "Genomes of surface isolates of Alteromonas macleodii: the life of a RT widespread marine opportunistic copiotroph."; RL Sci. Rep. 2:696-696(2012). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP003845; AFT80022.1; -; Genomic_DNA. DR RefSeq; WP_014999853.1; NC_018692.1. DR EnsemblBacteria; AFT80022; AFT80022; AMBLS11_17285. DR KEGG; amk:AMBLS11_17285; -. DR PATRIC; fig|1004785.3.peg.3612; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR Proteomes; UP000006295; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000006295}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000006295}. FT DOMAIN 198 365 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 164 191 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 429 AA; 48111 MW; 646EFA99217836E4 CRC64; MFDRYEAGEQ AVLVHVNFSD ENSKEDLSEL ELLVSSAGVN AVEVITTSRS APHAKFFVGS GKAEETAAAV KAHDANVVIF NHALSPSQER NLEALCKCRV LDRTGLILDI FAQRARTHEG KLQVELAQLR HISTRLIRGW THLERQKGGI GLRGPGETQL ETDRRLLRGR IKAILRRLEK VQKQREQGRR SRKRAEIPTV SLVGYTNAGK STLFNTITDS HVYAADQLFA TLDPTLRKIE LKDVGPAILA DTVGFIRHLP HDLVAAFKAT LQETQEADLL LHVVDIADAK YRETMDEVND VLEEIEAGEI QQLLICNKID KLDDVQPRIE RNDEGVPTRV WLSAQTGEGT ELLSQALTEC LGKSMVNYTL KIPPAQSRLR GVLYELNCIA SEEYDSQGDW VVDVRMPAAD WNRLEKRLEN GISEYVVRH // ID K0F441_9NOCA Unreviewed; 533 AA. AC K0F441; DT 28-NOV-2012, integrated into UniProtKB/TrEMBL. DT 28-NOV-2012, sequence version 1. DT 07-JUN-2017, entry version 32. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=O3I_029930 {ECO:0000313|EMBL:AFU03935.1}; OS Nocardia brasiliensis ATCC 700358. OC Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae; Nocardia. OX NCBI_TaxID=1133849 {ECO:0000313|EMBL:AFU03935.1, ECO:0000313|Proteomes:UP000006304}; RN [1] {ECO:0000313|EMBL:AFU03935.1, ECO:0000313|Proteomes:UP000006304} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=HUJEG-1 {ECO:0000313|EMBL:AFU03935.1}; RX PubMed=22535940; DOI=10.1128/JB.00210-12; RA Vera-Cabrera L., Ortiz-Lopez R., Elizondo-Gonzalez R., RA Perez-Maya A.A., Ocampo-Candiani J.; RT "Complete genome sequence of Nocardia brasiliensis HUJEG-1."; RL J. Bacteriol. 194:2761-2762(2012). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP003876; AFU03935.1; -; Genomic_DNA. DR EnsemblBacteria; AFU03935; AFU03935; O3I_029930. DR KEGG; nbr:O3I_029930; -. DR KO; K03665; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000006304; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 2. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000006304}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000006304}. FT DOMAIN 296 465 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 255 289 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 533 AA; 57601 MW; D688A07CB13432F7 CRC64; MTKQNTFEFT RAEDFTEGAE DISTSDFDND MTGSEFEDAG DVVAQHAARM KRSGGWTPAE PTVGEMQLDE RSSLRRVAGL STELTDITEV EYRQLRLERV VLVGVWTAGS AAQADASMTE LAALAETAGS EVLEGLIQRR DKPDPATYIG SGKADELRAV VLETGADTVI CDGELTPAQL TALEKVVKVK VIDRTALILD IFAQHATSRE GKAQVALAQM EYMLPRLRGW GESMSRQAGG RAGSNGGVGL RGPGETKIET DRRRIRERMA KLRREIREMK TARDTMRARR NSSGIPSVAI VGYTNAGKSS LMNALTGAGL LVQDALFATL DPTTRRADLD DGREVVFTDT VGFVRHLPTQ LVEAFRSTLE EVTGADLLLH VVDGSDPLPA EQIKAVREVI TDVIKEQGTV APPELLVVNK IDALDQLALT RLRGQLPDAE FVSVHADIGI DTLRDRLAEV LGGLDVEVGV LLPYTRGDLL ARIHADGRII TSTHEEGGTR VRARVPHSLA AALAEYAHAG GADKAETNGH VEI // ID K0I2E1_9BURK Unreviewed; 395 AA. AC K0I2E1; DT 28-NOV-2012, integrated into UniProtKB/TrEMBL. DT 28-NOV-2012, sequence version 1. DT 05-JUL-2017, entry version 35. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=C380_08420 {ECO:0000313|EMBL:AFU45389.1}; OS Acidovorax sp. KKS102. OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Comamonadaceae; Acidovorax. OX NCBI_TaxID=358220 {ECO:0000313|EMBL:AFU45389.1, ECO:0000313|Proteomes:UP000006306}; RN [1] {ECO:0000313|EMBL:AFU45389.1, ECO:0000313|Proteomes:UP000006306} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=KKS102 {ECO:0000313|EMBL:AFU45389.1, RC ECO:0000313|Proteomes:UP000006306}; RX PubMed=23209225; DOI=10.1128/JB.01848-12; RA Ohtsubo Y., Maruyama F., Mitsui H., Nagata Y., Tsuda M.; RT "Complete Genome Sequence of Acidovorax sp. Strain KKS102, a RT Polychlorinated-Biphenyl Degrader."; RL J. Bacteriol. 194:6970-6971(2012). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP003872; AFU45389.1; -; Genomic_DNA. DR EnsemblBacteria; AFU45389; AFU45389; C380_08420. DR KEGG; ack:C380_08420; -. DR PATRIC; fig|358220.3.peg.1709; -. DR KO; K03665; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000006306; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000006306}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}. FT DOMAIN 204 377 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 395 AA; 43642 MW; 248091A900A316B7 CRC64; MALSSASASS STMTPVLLVG VDFGLPHFDA ELEELGLLAQ TAGMQPVARI TCKRKAPDAA LFIGSGKADE IRTLAHMHGA VEVLFDQSLS PAQQRNLERH IELPVNDRTL LILEIFAQRA RSHEGKLQVE LAKLQYVSTR LVRRWSHLER QTGGIGARGG PGEKQIELDR RMIGDAIKRT RERLVKVKRQ RSTQRRQRER RDTFNISLVG YTNAGKSTLF NALVKARAYA ADQLFATLDT TTRQLYLADA ARSVSLSDTV GFIRDLPHGL VDAFQATLQE AVDADLLLHV VDASNSDFPE QMAQVERVLQ EIGASDIPQI LVFNKLDALP EERRPPVLVD QYEVGGQLLP RLFVSARSGE GLDELRRALA ARLMAAQEVL DMTPADTLEL PDALS // ID K0IDU6_NITGG Unreviewed; 376 AA. AC K0IDU6; DT 28-NOV-2012, integrated into UniProtKB/TrEMBL. DT 28-NOV-2012, sequence version 1. DT 07-JUN-2017, entry version 27. DE SubName: Full=Putative GTP-binding protein {ECO:0000313|EMBL:AFU56988.1}; GN OrderedLocusNames=Ngar_c00380 {ECO:0000313|EMBL:AFU56988.1}; OS Nitrososphaera gargensis (strain Ga9.2). OC Archaea; Thaumarchaeota; Nitrososphaeria; Nitrososphaerales; OC Nitrososphaeraceae; Nitrososphaera. OX NCBI_TaxID=1237085 {ECO:0000313|EMBL:AFU56988.1, ECO:0000313|Proteomes:UP000008037}; RN [1] {ECO:0000313|EMBL:AFU56988.1, ECO:0000313|Proteomes:UP000008037} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Ga9.2 {ECO:0000313|Proteomes:UP000008037}; RX PubMed=23057602; DOI=10.1111/j.1462-2920.2012.02893.x; RA Spang A., Poehlein A., Offre P., Zumbragel S., Haider S., Rychlik N., RA Nowka B., Schmeisser C., Lebedeva E.V., Rattei T., Bohm C., Schmid M., RA Galushko A., Hatzenpichler R., Weinmaier T., Daniel R., Schleper C., RA Spieck E., Streit W., Wagner M.; RT "The genome of the ammonia-oxidizing Candidatus Nitrososphaera RT gargensis: insights into metabolic versatility and environmental RT adaptations."; RL Environ. Microbiol. 14:3122-3145(2012). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002408; AFU56988.1; -; Genomic_DNA. DR EnsemblBacteria; AFU56988; AFU56988; Ngar_c00380. DR KEGG; nga:Ngar_c00380; -. DR PATRIC; fig|1237085.11.peg.43; -. DR KO; K03665; -. DR OMA; VILEIFH; -. DR OrthoDB; POG093Z07D6; -. DR Proteomes; UP000008037; Chromosome. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008037}; KW Reference proteome {ECO:0000313|Proteomes:UP000008037}. FT DOMAIN 199 371 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 376 AA; 42883 MW; 0AE3D0B49E9F11D1 CRC64; MLRLITWTGL ERVSTKTILV SYPDSFRLEE GKSLVESADC KIVKIFTQKY LNHSQYGIGA GKAEEIRDFV KGEEEGIQQL VVDEHLTSKQ LYNLSKLVEV QAIDRERLIL NIFYSRATTT EAKLQIELAE IQYEIPRVRE IAKMTSGNER AGKGGMGEYT VDVKFRDLKR RMNFIREKLV EAKKKRDLYH QQRTRTQMPV VSLVGYTGSG KTTLFNLLTK EHRETSSSLF TTLSTTTRVM KFNDEKQGDL LLTDTVGFIS RLPPYMIDAF KSTLEESLAA HLILLLVDAS EDVQNIDIKY SSCWDVLDEL KVDHAKVLVV LTKQDAVDAQ KMQEVMQQLQ LKEPIMIISS KTGYGIRKLK NMMVSKSRPK MVGGQP // ID K0IMM2_NITGG Unreviewed; 377 AA. AC K0IMM2; DT 28-NOV-2012, integrated into UniProtKB/TrEMBL. DT 28-NOV-2012, sequence version 1. DT 07-JUN-2017, entry version 34. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Ngar_c34940 {ECO:0000313|EMBL:AFU60407.1}; OS Nitrososphaera gargensis (strain Ga9.2). OC Archaea; Thaumarchaeota; Nitrososphaeria; Nitrososphaerales; OC Nitrososphaeraceae; Nitrososphaera. OX NCBI_TaxID=1237085 {ECO:0000313|EMBL:AFU60407.1, ECO:0000313|Proteomes:UP000008037}; RN [1] {ECO:0000313|EMBL:AFU60407.1, ECO:0000313|Proteomes:UP000008037} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Ga9.2 {ECO:0000313|Proteomes:UP000008037}; RX PubMed=23057602; DOI=10.1111/j.1462-2920.2012.02893.x; RA Spang A., Poehlein A., Offre P., Zumbragel S., Haider S., Rychlik N., RA Nowka B., Schmeisser C., Lebedeva E.V., Rattei T., Bohm C., Schmid M., RA Galushko A., Hatzenpichler R., Weinmaier T., Daniel R., Schleper C., RA Spieck E., Streit W., Wagner M.; RT "The genome of the ammonia-oxidizing Candidatus Nitrososphaera RT gargensis: insights into metabolic versatility and environmental RT adaptations."; RL Environ. Microbiol. 14:3122-3145(2012). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002408; AFU60407.1; -; Genomic_DNA. DR EnsemblBacteria; AFU60407; AFU60407; Ngar_c34940. DR KEGG; nga:Ngar_c34940; -. DR PATRIC; fig|1237085.11.peg.3496; -. DR KO; K03665; -. DR OMA; FNNHAHV; -. DR OrthoDB; POG093Z07D6; -. DR Proteomes; UP000008037; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000008037}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000008037}. FT DOMAIN 188 359 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 377 AA; 42723 MW; 491D682448E918F8 CRC64; MMAFQRKAIL ITYPVDQAIK EAISLADAAG YEIVDTVTQR QITRSRFGIG RGKAEEVKEL VEELRPDVII FDEVIKPTQM YNLASLCKVE IVDRERLILE IFERRASTTE SQIQIKLAQL RYDMARAREK VRLARAGEQP GFYGLGKYEA DIYFLDIRKR AAVLKKKLEK EETRRQLHRN QRTRAGLPTV SLAGYTSAGK TTLFNKLTGE AKATDKQIFI TLSTFTRAID LHGDKVLLND TVGFISKLPA YMIDAFKSTL DELTYASLVL LVIDISEPIE EVARKYDSSL DVINEFKVPA TKIIHVLNKV DLTTIEDAFD KAGQLGILDT KRVIPVSAKT GYNINQLKNL IRTVLFEMEK GEDAEVKEER VEKEEQG // ID K0J7L0_AMPXN Unreviewed; 406 AA. AC K0J7L0; DT 28-NOV-2012, integrated into UniProtKB/TrEMBL. DT 28-NOV-2012, sequence version 1. DT 07-JUN-2017, entry version 35. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:BAM47553.1}; GN OrderedLocusNames=AXY_14210 {ECO:0000313|EMBL:BAM47553.1}; OS Amphibacillus xylanus (strain ATCC 51415 / DSM 6626 / JCM 7361 / LMG OS 17667 / NBRC 15112 / Ep01). OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Amphibacillus. OX NCBI_TaxID=698758 {ECO:0000313|EMBL:BAM47553.1, ECO:0000313|Proteomes:UP000006294}; RN [1] {ECO:0000313|EMBL:BAM47553.1, ECO:0000313|Proteomes:UP000006294} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51415 / DSM 6626 / JCM 7361 / LMG 17667 / NBRC 15112 / RC Ep01 {ECO:0000313|Proteomes:UP000006294}; RA Nakazawa H., Katano Y., Nakamura S., Sasagawa M., Fukada J., Arai T., RA Sasakura N., Mochizuki D., Hosoyama A., Harada K., Horikawa H., RA Kato Y., Harada T., Sasaki K., Sekiguchi M., Hodoyama M., Nishiko R., RA Narita H., Hanamaki A., Hata C., Konno Y., Niimura Y., Yamazaki S., RA Fujita N.; RT "Whole genome sequence of Amphibacillus xylinus NBRC 15112."; RL Submitted (JAN-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AP012050; BAM47553.1; -; Genomic_DNA. DR RefSeq; WP_015010155.1; NC_018704.1. DR EnsemblBacteria; BAM47553; BAM47553; AXY_14210. DR KEGG; axl:AXY_14210; -. DR PATRIC; fig|698758.3.peg.1417; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000006294; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000006294}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000006294}. FT DOMAIN 195 356 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 161 188 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 406 AA; 46428 MW; 6A6918AED4E12744 CRC64; MAEKILIIAV QRQTDDDLHF HYSMEEIKSL SKTARGEVVD VITQKRNQPH PATYLGKGKI EEIDLIIESE EIDLIIANDE LSASQMRNLQ NRTGVSVIDR SQLILDIFAS RATSNEGKLQ VELAQYQYLL PRLHGQGLAL SRLAGGIGTR GPGETKLESD RRHINRRINE IKRRLQTVVN QREQYRKRRR LNHTFNIAIV GYTNAGKSTL FNRLTDSDSF EEDQLFATLD PMSRKLKLPS GLSAIITDTV GFMQDLPTEL IAAFKSTLEE VSEADLIFHV VDASHPDHDQ QQATVLELLE ELNADHIPML TIYNKRDQIE GDFIPMLKPS IVVSALVESD RQDILVETER LIKKIWRKYQ ITLPADQGKI LQQYKQHSLM ISEVFLEEQQ AYQIEGYLPE DHPLIR // ID K0JW36_SACES Unreviewed; 481 AA. AC K0JW36; DT 28-NOV-2012, integrated into UniProtKB/TrEMBL. DT 28-NOV-2012, sequence version 1. DT 07-JUN-2017, entry version 36. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:CCH29019.1}; GN OrderedLocusNames=BN6_16970 {ECO:0000313|EMBL:CCH29019.1}; OS Saccharothrix espanaensis (strain ATCC 51144 / DSM 44229 / JCM 9112 / OS NBRC 15066 / NRRL 15764). OC Bacteria; Actinobacteria; Pseudonocardiales; Pseudonocardiaceae; OC Saccharothrix. OX NCBI_TaxID=1179773 {ECO:0000313|EMBL:CCH29019.1, ECO:0000313|Proteomes:UP000006281}; RN [1] {ECO:0000313|EMBL:CCH29019.1, ECO:0000313|Proteomes:UP000006281} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51144 / DSM 44229 / JCM 9112 / NBRC 15066 / NRRL 15764 RC {ECO:0000313|Proteomes:UP000006281}; RX PubMed=22958348; DOI=10.1186/1471-2164-13-465; RA Strobel T., Al-Dilaimi A., Blom J., Gessner A., Kalinowski J., RA Luzhetska M., Puhler A., Szczepanowski R., Bechthold A., Ruckert C.; RT "Complete genome sequence of Saccharothrix espanaensis DSM 44229T and RT comparison to the other completely sequenced Pseudonocardiaceae."; RL BMC Genomics 13:465-465(2012). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; HE804045; CCH29019.1; -; Genomic_DNA. DR RefSeq; WP_015099132.1; NC_019673.1. DR EnsemblBacteria; CCH29019; CCH29019; BN6_16970. DR KEGG; sesp:BN6_16970; -. DR PATRIC; fig|1179773.3.peg.1701; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000006281; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000006281}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000006281}. FT DOMAIN 254 423 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 481 AA; 52142 MW; 01E84850A159A938 CRC64; MTENTHNSND WLDHDAELST GELALADRAA LRRVSGLSTE LQDVTEVEYR QLRLERVVLV GVWTEGTAAD SEASLAELAL LAETAGSEVL EGLVQRRDRP DPATYIGSGK VSELRDVVIS TGADTVICDG ELSPGQLRQL EEKLKVKVVD RTALILDIFA QHASSKEGKA QVELAQLQYL LPRLRGWGES LSRQAGGRAG GGNGGVGLRG PGETKLETDR RRIRAKISKL RRQIAGMSVI RDTKRGARIA NAVPNVAIAG YTNAGKSSLL NALTGAGVLV EDALFATLDP TTRRSQTPEG LPYTLTDTVG FVRHLPHQLV EAFRSTLEEV ADADLLVHVV DGSDAMPEKQ VTAVREVISE ISERRDDPMP AELLVVNKVD AVGELGLARL RHLFPTAVLV SAHTGEGIQE LRERIATLIP RPEVVVEAMV PYARGELVAR IHREGEILKE RHTEEGTELS ARVRPDLAGV LEQFAVNGSR A // ID K0NKI1_DESTT Unreviewed; 540 AA. AC K0NKI1; DT 28-NOV-2012, integrated into UniProtKB/TrEMBL. DT 28-NOV-2012, sequence version 1. DT 07-JUN-2017, entry version 36. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:CCK80448.1}; GN OrderedLocusNames=TOL2_C22870 {ECO:0000313|EMBL:CCK80448.1}; OS Desulfobacula toluolica (strain DSM 7467 / Tol2). OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfobacterales; OC Desulfobacteraceae; Desulfobacula. OX NCBI_TaxID=651182 {ECO:0000313|EMBL:CCK80448.1, ECO:0000313|Proteomes:UP000007347}; RN [1] {ECO:0000313|EMBL:CCK80448.1, ECO:0000313|Proteomes:UP000007347} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 7467 / Tol2 {ECO:0000313|Proteomes:UP000007347}; RX PubMed=23088741; DOI=10.1111/j.1462-2920.2012.02885.x; RA Wohlbrand L., Jacob J.H., Kube M., Mussmann M., Jarling R., Beck A., RA Amann R., Wilkes H., Reinhardt R., Rabus R.; RT "Complete genome, catabolic sub-proteomes and key-metabolites of RT Desulfobacula toluolica To12 marine, aromatic compound-degrading, RT sulfate-reducing bacterium."; RL Environ. Microbiol. 15:1334-1355(2013). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; FO203503; CCK80448.1; -; Genomic_DNA. DR RefSeq; WP_014957760.1; NC_018645.1. DR EnsemblBacteria; CCK80448; CCK80448; TOL2_C22870. DR KEGG; dto:TOL2_C22870; -. DR PATRIC; fig|651182.5.peg.2707; -. DR KO; K03665; -. DR OMA; EREVIIT; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000007347; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000007347}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000007347}. FT DOMAIN 378 540 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 337 371 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 540 AA; 61371 MW; BBA77609D2F6EC2D CRC64; MKKKLHGNTS GLRNTQIKKI ETLYNYSTPP EYLADPELAQ FLVDLSHDIR RQIGLLIDRN GKIIYVIVGE PHRVVIPITS GYMAIPGKLK GLRLIHTHLK DEPLTRDDLT DLALLRLDYI TAICITQNGK PGSVYSGHIL PDEDSDPYQV LEPATIKDLN NDCLAQIIAL ESELTRKNSL YRPETGRENA FLINATTLDT KEAYASIEEL KELCKTSHIN VIGTAVQRRK AIDPKFVVGK GKLSSLIIKA IQNYATLLVF DRELSASQIR SITDFVEMKV IDRTQLILDI FAKQAKSREG KFQVELAQME YLLPRLISKN TAMSRLTGGI GGRGPGETKL ELNRRRVREK INQLKKEIAK IRKQRQQQKS RRKRKELPII SIVGYTNAGK STLLNTLTQS RITAANRLFA TLDPSSRRLR FPRDTEVIIT DTVGFIQDLP KELMEAFHAT LDELSDADII LHVIDISNPR YRQQKESVEK ILKNLKLEHI PTLYIFNKTD KISLDDFDDQ WLLNQGFPVC ATQKQSLKLL VEKLESMVKT // ID K0P6L1_9BACT Unreviewed; 407 AA. AC K0P6L1; DT 28-NOV-2012, integrated into UniProtKB/TrEMBL. DT 28-NOV-2012, sequence version 1. DT 07-JUN-2017, entry version 33. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:CCM10468.1}; GN ORFNames=CAHE_0691 {ECO:0000313|EMBL:CCM10468.1}; OS Cardinium endosymbiont cEper1 of Encarsia pergandiella. OC Bacteria; Bacteroidetes; Cytophagia; Cytophagales; Amoebophilaceae; OC Candidatus Cardinium. OX NCBI_TaxID=1231626 {ECO:0000313|EMBL:CCM10468.1, ECO:0000313|Proteomes:UP000003996}; RN [1] {ECO:0000313|EMBL:CCM10468.1, ECO:0000313|Proteomes:UP000003996} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CEper1 {ECO:0000313|EMBL:CCM10468.1}; RX PubMed=23133394; DOI=10.1371/journal.pgen.1003012; RA Penz T., Schmitz-Esser S., Kelly S.E., Cass B.N., Muller A., Woyke T., RA Malfatti S.A., Hunter M.S., Horn M.; RT "Comparative Genomics Suggests an Independent Origin of Cytoplasmic RT Incompatibility in Cardinium hertigii."; RL PLoS Genet. 8:e1003012-e1003012(2012). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; HE983995; CCM10468.1; -; Genomic_DNA. DR RefSeq; WP_014934835.1; NC_018605.1. DR EnsemblBacteria; CCM10468; CCM10468; CAHE_0691. DR KEGG; che:CAHE_0691; -. DR PATRIC; fig|1231626.3.peg.676; -. DR KO; K03665; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000003996; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000003996}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000003996}. FT DOMAIN 209 390 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 407 AA; 45721 MW; 5751456B6D4EF283 CRC64; MYTDRSNPSN LVVNQEAQTA ILIALITFHQ PLAKTESYLT ELAFLAGTSG LKIVKNFMQR LERPNGATFV GKGKVKEIAD FIKSEKIRFA IFDDELTPSQ VRNLERLLSC QILDRSLLIF NIFSMRAQTK QARTQVALAY HQYLLPRLTR MWSHLTNQKG GSAGMRGPGE KELETDKRMI QYKITQLRKK LATIAQQCTT RRKARIDLVR VALVGYTNVG KSTLMKLLSK SDVLTDDKLF ATVDATVRKV VLNQHFFLLT DTVGFIRKLP HTLVECFKST LEEIKEADLL LHIVDGSHDG FQEQIDIVDQ TLTEIGAANL PRILVFNKID MMHQSKKVMV IQAIDAPVAS RTGLYSHAVS GYPSVCISAT KQLHIDLLKE MITKQIEEIQ ATKYIKASSI GSVVDIG // ID K0PWE1_9RHIZ Unreviewed; 444 AA. AC K0PWE1; DT 28-NOV-2012, integrated into UniProtKB/TrEMBL. DT 28-NOV-2012, sequence version 1. DT 07-JUN-2017, entry version 32. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:CCM75592.1}; GN ORFNames=BN77_2749 {ECO:0000313|EMBL:CCM75592.1}; OS Rhizobium mesoamericanum STM3625. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium. OX NCBI_TaxID=1211777 {ECO:0000313|EMBL:CCM75592.1, ECO:0000313|Proteomes:UP000009319}; RN [1] {ECO:0000313|EMBL:CCM75592.1, ECO:0000313|Proteomes:UP000009319} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=STM3625 {ECO:0000313|EMBL:CCM75592.1, RC ECO:0000313|Proteomes:UP000009319}; RA Moulin L., Mornico D., Melkonian R., Klonowska A.; RT "Draft Genome Sequence of Rhizobium mesoamericanum STM3625, a RT Nitrogen-Fixing Symbiont of Mimosa pudica Isolated in French Guiana RT (South America)."; RL Genome Announc. 1:e00066-e00112(2013). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:CCM75592.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CANI01000018; CCM75592.1; -; Genomic_DNA. DR RefSeq; WP_007532488.1; NZ_HF536772.1. DR EnsemblBacteria; CCM75592; CCM75592; BN77_2749. DR GeneID; 31825981; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000009319; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000009319}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000009319}. FT DOMAIN 206 378 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 165 199 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 444 AA; 48896 MW; B00471F2124D3FDA CRC64; MRATVVVPVL KQARAGRGGA DGVPVVTRTP ESRLEEATGL AQAIDLDVVN GAIVTVNDPR PATLMGTGKI EEIKATLDAN DSGLVIVDHP LTPVQQRNLE KEWNAKVIDR TGLILEIFGR RASTKEGTLQ VDLAHLNYQK GRLVRSWTHL ERQRGGGGFM GGPGETQIEA DRRLLQDRIV KLERELEQVV RTRQLHRAKR KKVPHPIVAL VGYTNAGKST LFNRITGAGV LAEDMLFATL DPTLRRMKLP HGRTVILSDT VGFISDLPTH LVAAFRATLE EVLEADLILH VRDMSDVDNQ AQSADVLRIL KDLGIDEEEG DKRIIEVWNK IDRLEPEAHD AIVQKASGAE NVVALSAISG EGIDTLMGEI SRRLSGVLTE ATVRLPVDKL ALLPWLYDHA IVNGREDNED GSITLDVRLS ETEAVELERR LGNGPKAARE DWER // ID K0R4R3_THAOC Unreviewed; 606 AA. AC K0R4R3; DT 28-NOV-2012, integrated into UniProtKB/TrEMBL. DT 28-NOV-2012, sequence version 1. DT 10-MAY-2017, entry version 16. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EJK47620.1}; GN ORFNames=THAOC_33645 {ECO:0000313|EMBL:EJK47620.1}; OS Thalassiosira oceanica (Marine diatom). OC Eukaryota; Stramenopiles; Bacillariophyta; Coscinodiscophyceae; OC Thalassiosirophycidae; Thalassiosirales; Thalassiosiraceae; OC Thalassiosira. OX NCBI_TaxID=159749 {ECO:0000313|EMBL:EJK47620.1, ECO:0000313|Proteomes:UP000007974}; RN [1] {ECO:0000313|EMBL:EJK47620.1, ECO:0000313|Proteomes:UP000007974} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CCMP1005 {ECO:0000313|EMBL:EJK47620.1}; RX PubMed=22835381; DOI=10.1186/gb-2012-13-7-r66; RA Lommer M., Specht M., Roy A.S., Kraemer L., Andreson R., RA Gutowska M.A., Wolf J., Bergner S.V., Schilhabel M.B., RA Klostermeier U.C., Beiko R.G., Rosenstiel P., Hippler M., Laroche J.; RT "Genome and low-iron response of an oceanic diatom adapted to chronic RT iron limitation."; RL Genome Biol. 13:R66-R66(2012). CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EJK47620.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGNL01046785; EJK47620.1; -; Genomic_DNA. DR EnsemblProtists; EJK47620; EJK47620; THAOC_33645. DR Proteomes; UP000007974; Unassembled WGS sequence. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000007974}; KW Reference proteome {ECO:0000313|Proteomes:UP000007974}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1 24 {ECO:0000256|SAM:SignalP}. FT CHAIN 25 606 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5003838869. FT DOMAIN 353 525 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 606 AA; 66918 MW; 6C31B7ADE7AE6DDE CRC64; MTSSSIPALR ILLLCTAIAA FVAAFAPPPS SSRHRTIRTV EGTTPGSISL FDDADQEGAP LAILFEDVES ELDELTRGVD REEERTVSQV ENVALTDEED RILTDQEDRL FQYINNTVRV ESCILVGVED LSLARKARKV TGDDFGSWTL EESMVEMREL IQTAGLALKG EITQRLQEVN PRTYIGSGKV DEAKQLLATI NDELERRGEG ECCTVVFDAE LYPGQQKALE NAFNKKVIDN DFLGSDQEDV VKLPVTYSGH LDIFAQHAKT REGKLQVDLA LHEYRKPRLT RMWTHLERQS GSGGVGLRGP GETQLEVDKR ILRDRILVLK AKIDDVQKQR DLHRRGRKKG GLPVLALVGY TNAGKSTLLN CLTRAGILAE NILFATLDPT TRRVKLPGYK THPEVLLTDT VGFIQKLPTQ LVAAFRATLE EVKEADVLIH IIDVANPTWR KQEESVTSVL NEIGAGSKPI VRVFNKLDLL EPEDAEMLKY EAACAEDFSV GISSKTGEGL GDFVAVVEDA LSGLLVPVEL ELPYSCGDVV NTIHEVGSIE TIDYRENGTY VVGRVPRSLA MKLERYNVAL VGASSKEDSE SEIDWAAIGR GRHTAK // ID K0UEM9_MYCVA Unreviewed; 482 AA. AC K0UEM9; DT 28-NOV-2012, integrated into UniProtKB/TrEMBL. DT 28-NOV-2012, sequence version 1. DT 07-JUN-2017, entry version 34. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=MVAC_25495 {ECO:0000313|EMBL:EJZ05336.1}; OS Mycobacterium vaccae ATCC 25954. OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae; OC Mycobacterium. OX NCBI_TaxID=1194972 {ECO:0000313|EMBL:EJZ05336.1, ECO:0000313|Proteomes:UP000006072}; RN [1] {ECO:0000313|EMBL:EJZ05336.1, ECO:0000313|Proteomes:UP000006072} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 25954 {ECO:0000313|EMBL:EJZ05336.1, RC ECO:0000313|Proteomes:UP000006072}; RX PubMed=23105074; DOI=10.1128/JB.01462-12; RA Ho Y.S., Adroub S.A., Abadi M., Al Alwan B., Alkhateeb R., Gao G., RA Ragab A., Ali S., van Soolingen D., Bitter W., Pain A., Abdallah A.M.; RT "Complete Genome Sequence of Mycobacterium vaccae Type Strain ATCC RT 25954."; RL J. Bacteriol. 194:6339-6340(2012). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EJZ05336.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ALQA01000082; EJZ05336.1; -; Genomic_DNA. DR RefSeq; WP_003933651.1; NZ_JH814704.1. DR EnsemblBacteria; EJZ05336; EJZ05336; MVAC_25495. DR PATRIC; fig|1194972.3.peg.5075; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000006072; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000006072}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}. FT DOMAIN 259 428 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 218 252 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 482 AA; 51952 MW; AD2084F5F0DABB01 CRC64; MLNDIRANLD SPMTHPELPH DNPSVGELAL EDRTALRRVA GLSTELADVT EVEYRQLRLE RVVLVGVWTE GSAADADASL AELRALAETA GSEVLEGLIQ RRDKPDPSTY IGSGKAAELR EIVVATGADT VICDGELSPA QLNALEKVVK VKVIDRTALI LDIFAQHATS REGKAQVSLA QMEYMLPRLR GWGESMSRQA GGRAGGAGGG VGTRGPGETK IETDRRRIRE RMSKLRREIR EMKQVRDTQR GRRVANDVPS VAIVGYTNAG KSSLLNALTG AGVLVENALF ATLEPTTRRG ELPDGREFVL TDTVGFVRHL PTQLVEAFRS TLEEVADADL LVHVVDGSDA NPLAQINAVR QVVNDVVAET DAPAPPELLV VNKIDAADGL TLAQLRRALP GAVFVSAHTG DGLERLQARM AEMIAPRDTV VDVTIPYERG DLVNRVHAEG RVDAVEHTES GTRMKARVPV SLAAGLTGYT TY // ID K0YXH3_9ACTN Unreviewed; 433 AA. AC K0YXH3; DT 28-NOV-2012, integrated into UniProtKB/TrEMBL. DT 28-NOV-2012, sequence version 1. DT 07-JUN-2017, entry version 34. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=HMPREF9451_00598 {ECO:0000313|EMBL:EJZ84289.1}; OS Slackia piriformis YIT 12062. OC Bacteria; Actinobacteria; Coriobacteriia; Eggerthellales; OC Eggerthellaceae; Slackia. OX NCBI_TaxID=742818 {ECO:0000313|EMBL:EJZ84289.1, ECO:0000313|Proteomes:UP000006069}; RN [1] {ECO:0000313|EMBL:EJZ84289.1, ECO:0000313|Proteomes:UP000006069} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=YIT 12062 {ECO:0000313|EMBL:EJZ84289.1, RC ECO:0000313|Proteomes:UP000006069}; RG The Broad Institute Genome Sequencing Platform; RA Earl A., Ward D., Feldgarden M., Gevers D., Morotomi M., Walker B., RA Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B., RA Abouelleil A., Alvarado L., Arachchi H.M., Berlin A.M., Chapman S.B., RA Goldberg J., Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., RA Larimer J., McCowen C., Montmayeur A., Murphy C., Neiman D., RA Pearson M., Priest M., Roberts A., Saif S., Shea T., Sisk P., RA Sykes S., Wortman J., Nusbaum C., Birren B.; RT "The Genome Sequence of Slackia piriformis YIT 12062."; RL Submitted (AUG-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EJZ84289.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADMD01000002; EJZ84289.1; -; Genomic_DNA. DR EnsemblBacteria; EJZ84289; EJZ84289; HMPREF9451_00598. DR PATRIC; fig|742818.3.peg.649; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000006069; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR Gene3D; 3.40.350.10; -; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR029149; Creatin/AminoP/Spt16_NTD. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000006069}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000006069}. FT DOMAIN 213 378 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 433 AA; 47094 MW; 604A787EFB8D8DD2 CRC64; MSFADMSQES FTGDAERAVL VGIDYKDALE SLLESSLAEL ARLTDTAGAV VVATVSQRLD APNPRTFVGS GKAEEIADLC RSFAADVVIF DEELTPSQQS NLEKAMPRDV KVIDRTALIL DIFALHATTK EGRLQVRLAQ NQYLLPRLRG MWAHLASNRM GGGVGSRFGE GESQLEVDRR MVRKRITSIR RELEQVSRMR QTQRSARYAS GVFKVAEAGY TNAGKSSLLN RLSGSDVLSY DKLFATLDST TRKLVLPEGR EVTLTDTVGF IQKLPTTLVE AFKSTLDEIR GADLILHVVD ASSDERDAQM RAVEGTLEQI GAQGISRILV FNKIDLVEPS VRAALSARFP SAVLVSAETG EGADSLIEAI ARAASASEKV MEVLVPYSRG DVVSIAHERC SVLAESYDER GTALTVRVPS DLTALFEGYA LSD // ID K0Z0G1_9ACTO Unreviewed; 512 AA. AC K0Z0G1; DT 28-NOV-2012, integrated into UniProtKB/TrEMBL. DT 28-NOV-2012, sequence version 1. DT 07-JUN-2017, entry version 31. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=HMPREF9241_01504 {ECO:0000313|EMBL:EJZ85504.1}; OS Actinomyces turicensis ACS-279-V-Col4. OC Bacteria; Actinobacteria; Actinomycetales; Actinomycetaceae; OC Actinomyces. OX NCBI_TaxID=883077 {ECO:0000313|EMBL:EJZ85504.1, ECO:0000313|Proteomes:UP000003994}; RN [1] {ECO:0000313|EMBL:EJZ85504.1, ECO:0000313|Proteomes:UP000003994} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ACS-279-V-Col4 {ECO:0000313|EMBL:EJZ85504.1, RC ECO:0000313|Proteomes:UP000003994}; RG The Broad Institute Genome Sequencing Platform; RA Earl A., Ward D., Feldgarden M., Gevers D., Saerens B., RA Vaneechoutte M., Walker B., Young S.K., Zeng Q., Gargeya S., RA Fitzgerald M., Haas B., Abouelleil A., Alvarado L., Arachchi H.M., RA Berlin A., Chapman S.B., Goldberg J., Griggs A., Gujja S., Hansen M., RA Howarth C., Imamovic A., Larimer J., McCowen C., Montmayeur A., RA Murphy C., Neiman D., Pearson M., Priest M., Roberts A., Saif S., RA Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C., Birren B.; RT "The Genome Sequence of Actinomyces turicensis ACS-279-V-COL4."; RL Submitted (JUL-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EJZ85504.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGWQ01000008; EJZ85504.1; -; Genomic_DNA. DR RefSeq; WP_006681703.1; NZ_JH815210.1. DR EnsemblBacteria; EJZ85504; EJZ85504; HMPREF9241_01504. DR PATRIC; fig|883077.3.peg.1518; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000003994; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000003994}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000003994}. FT DOMAIN 277 443 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 512 AA; 55875 MW; 9218032DDA20D68E CRC64; MDNPGFSADD ELAQQRANDV VARILARRGT ALESTAGQDH SADAGDLERE ARAGTRRIQG YANDREEISE VEYRQVRLEK VVLVGLRTTQ TEEEVETSLR ELAALAQTAG SQVLDAVVQK RVKPDPATYL GSGKAKELAG IVRAVEADTV IVDEELAPSQ RRGLEDVVDA KVVDRTALIL DIFAQHAKSR EGKAQVELAQ LEYLLPRLRG WGDSMSRQAG GRVAGGAGIG SRGPGETKIE LDRRRIRTRM AKLREEIRKM EPARRTQRLS RRRGAVPSVA IVGYTNAGKS TLLNQLTGAG VLVEDALFAT LDPTVRRTQT ADGREYTLSD TVGFVRNLPT QLVEAFRSTL EEAGEADLLV HVVDAAHPDP VGQVEAVHQV LGEIEGALGI PEIIVLNKAD LASAEQLALL RTYFPSSVAV SGYTGFGVDE LRHRIEEALP RPRIQIDCVI PYSRGDLVHQ IHEDGEVDHE EYVAEGTRIR ARVDEHLAAL IRDVALPVAT EGAPYTRQDS GE // ID K0Z6N1_9ACTO Unreviewed; 489 AA. AC K0Z6N1; DT 28-NOV-2012, integrated into UniProtKB/TrEMBL. DT 28-NOV-2012, sequence version 1. DT 07-JUN-2017, entry version 34. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=HMPREF9240_00148 {ECO:0000313|EMBL:EJZ87889.1}; OS Actinomyces neuii BVS029A5. OC Bacteria; Actinobacteria; Actinomycetales; Actinomycetaceae; OC Actinomyces. OX NCBI_TaxID=888439 {ECO:0000313|EMBL:EJZ87889.1, ECO:0000313|Proteomes:UP000006075}; RN [1] {ECO:0000313|EMBL:EJZ87889.1, ECO:0000313|Proteomes:UP000006075} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BVS029A5 {ECO:0000313|EMBL:EJZ87889.1, RC ECO:0000313|Proteomes:UP000006075}; RG The Broad Institute Genome Sequencing Platform; RA Earl A., Ward D., Feldgarden M., Gevers D., Saerens B., RA Vaneechoutte M., Walker B., Young S.K., Zeng Q., Gargeya S., RA Fitzgerald M., Haas B., Abouelleil A., Alvarado L., Arachchi H.M., RA Berlin A., Chapman S.B., Goldberg J., Griggs A., Gujja S., Hansen M., RA Howarth C., Imamovic A., Larimer J., McCowen C., Montmayeur A., RA Murphy C., Neiman D., Pearson M., Priest M., Roberts A., Saif S., RA Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C., Birren B.; RT "The Genome Sequence of Actinomyces neuii subsp. anitratus BVS029A5."; RL Submitted (JUL-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EJZ87889.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGWP01000002; EJZ87889.1; -; Genomic_DNA. DR RefSeq; WP_004804823.1; NZ_JH815213.1. DR EnsemblBacteria; EJZ87889; EJZ87889; HMPREF9240_00148. DR PATRIC; fig|888439.3.peg.153; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000006075; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000006075}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000006075}. FT DOMAIN 268 433 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 489 AA; 53183 MW; A898F94D9238E1CD CRC64; MKQDNKDRAE DVVARILART GTALESTEGM DTSADAGAME REERRALRRV SGLNHSEDAI ESVEYQRLAL ERVVLVGIYT ADAAKAEDSL RELAALAQTA GSLVLDGVLQ RREKPDPGTY LGSGKARELR DLVHSVDADT VIVDGELPPS QRRGLEDVVK VKVVDRTALI LDIFAQHAKS REGKAQVELA QLEYMLPRLR GWGKSLSRQA GGRAAAGEGI GSRGPGETKI EMDRRRIRHR MARLRKQIAG MKAARDTKRS GRTRTNTPAA VVVGYTNAGK SSLLNALVGS QIMVADELFA TLDPTVRKAE TPEGRSYTLT DTVGFVSNLP HQLVEAFRST LEEVAQADLL LHVVDAAHPD PEAQIRAVRK VLADIEGAMD IPQLMVLNKA DLASKERIAV LRSKHKNSVV VSARTGQGIA ELKLAIERML PHPDVPIDLV IPFSRGDLVG RAHEEAQIDQ IDYTASGTRL RGMARADLAG LLQDAAVDE // ID K1E401_9MICO Unreviewed; 499 AA. AC K1E401; DT 28-NOV-2012, integrated into UniProtKB/TrEMBL. DT 28-NOV-2012, sequence version 1. DT 07-JUN-2017, entry version 32. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=B277_06263 {ECO:0000313|EMBL:EKA61741.1}; OS Janibacter hoylei PVAS-1. OC Bacteria; Actinobacteria; Micrococcales; Intrasporangiaceae; OC Janibacter. OX NCBI_TaxID=1210046 {ECO:0000313|EMBL:EKA61741.1, ECO:0000313|Proteomes:UP000004474}; RN [1] {ECO:0000313|EMBL:EKA61741.1, ECO:0000313|Proteomes:UP000004474} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=PVAS-1 {ECO:0000313|EMBL:EKA61741.1, RC ECO:0000313|Proteomes:UP000004474}; RX PubMed=23144385; DOI=10.1128/JB.01728-12; RA Pawar S.P., Dhotre D.P., Shetty S.A., Chowdhury S.P., Chaudhari B.L., RA Shouche Y.S.; RT "Genome Sequence of Janibacter hoylei MTCC8307, Isolated from the RT Stratospheric Air."; RL J. Bacteriol. 194:6629-6630(2012). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EKA61741.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ALWX01000022; EKA61741.1; -; Genomic_DNA. DR EnsemblBacteria; EKA61741; EKA61741; B277_06263. DR PATRIC; fig|1210046.3.peg.1211; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000004474; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 2. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000004474}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000004474}. FT DOMAIN 279 444 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 499 AA; 54452 MW; 39AA92CEFD1E3196 CRC64; MTEPLRSAHD GGDDITINPT IDRVLSRRAQ ALADDDGFVD RSDYDGEQLD REERSALRRV QGLSTELEDI TEVEYRQLRL ERVVLAAVWT DGRVEDAENS LRELAALAET AGSEVLAGVL QRRQNPDPGT YLGSGKALEL RDIVVAEGAD TVVCDDELSP SQRRALEDVV KVKVIDRTAL ILDIFAQHAT SREGRAQVEL AQLTYLLPRL RGWGESMSRQ AGGQAAGGQG MGSRGPGETK IELDRRRINS RIAKLKRDIA GMKTHRDTSR SSRRHNGTPS VVIAGYTNAG KSTLLNRLTH AGVLVDNQLF ATLDTTVRRS ETADGREFTL ADTVGFVRHL PEQLVEAFRS TLEEVGDADL LLHVVDGSHP DPEGQISAVR SVLADVDATD VKEVVVINKA DAADPEVVDR ILRNERYSVA VSARTGQGIP ELLDLVAEEL PRPDIDVEVL VPYARGDLVS RLHDEAEILA EEHVAEGTHL RARVHGDLAA ELTPFAAAG // ID K1KJY4_9BURK Unreviewed; 399 AA. AC K1KJY4; DT 28-NOV-2012, integrated into UniProtKB/TrEMBL. DT 28-NOV-2012, sequence version 1. DT 07-JUN-2017, entry version 33. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=HMPREF9465_00343 {ECO:0000313|EMBL:EKB32049.1}; OS Sutterella wadsworthensis 2_1_59BFAA. OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Sutterellaceae; Sutterella. OX NCBI_TaxID=742823 {ECO:0000313|EMBL:EKB32049.1, ECO:0000313|Proteomes:UP000005835}; RN [1] {ECO:0000313|EMBL:EKB32049.1, ECO:0000313|Proteomes:UP000005835} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=2_1_59BFAA {ECO:0000313|EMBL:EKB32049.1, RC ECO:0000313|Proteomes:UP000005835}; RG The Broad Institute Genome Sequencing Platform; RA Earl A., Ward D., Feldgarden M., Gevers D., Daigneault M., Strauss J., RA Allen-Vercoe E., Walker B., Young S.K., Zeng Q., Gargeya S., RA Fitzgerald M., Haas B., Abouelleil A., Alvarado L., Arachchi H.M., RA Berlin A.M., Chapman S.B., Goldberg J., Griggs A., Gujja S., RA Hansen M., Howarth C., Imamovic A., Larimer J., McCowen C., RA Montmayeur A., Murphy C., Neiman D., Pearson M., Priest M., RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., RA Nusbaum C., Birren B.; RT "The Genome Sequence of Sutterella wadsworthensis 2_1_59BFAA."; RL Submitted (MAY-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EKB32049.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADMG01000010; EKB32049.1; -; Genomic_DNA. DR RefSeq; WP_005433514.1; NZ_JH815513.1. DR EnsemblBacteria; EKB32049; EKB32049; HMPREF9465_00343. DR PATRIC; fig|742823.3.peg.340; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000005835; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000005835}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000005835}. FT DOMAIN 194 360 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 399 AA; 44701 MW; 9563AA60C133ADFC CRC64; MKATRAFLVC VVVGRVVYQD SAEELALLVK SDGLEPVGLL DAKRDKPDPA FFIGSGKVDE LGELAHELHA DVVVFDVPLS AAQQRNIERA IELPVLDRTQ LILDIFRARA KSREGRLQVE LAQLEHLSTR LVRGWTHLER QRGGLGKTGG PGEKQIELDR RMIGVRMKQL RDQLKRLARQ RDTQRRSRSR SDTLSVSLVG YTNAGKSTLF NRLTRAKSYA ADQLFATLDT TARRCWISDE ETVVASDTVG FIRGLPHQLV EAFKSTLDET VHADLLLHVV DASSSVREDQ ISEVNAVLEE IKADDVPAIL VYNKIDNTAL EPEIVRHPDG RPKAVFVSAL TGEGLDLLRQ AIGEFAHQWR VDNPNEPRAP EPWEEEVAHD LVALADDNIE DFLVRKKKR // ID K1LTQ4_9LACT Unreviewed; 412 AA. AC K1LTQ4; DT 28-NOV-2012, integrated into UniProtKB/TrEMBL. DT 28-NOV-2012, sequence version 1. DT 07-JUN-2017, entry version 33. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=HMPREF9706_01686 {ECO:0000313|EMBL:EKB53428.1}; OS Facklamia hominis CCUG 36813. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Aerococcaceae; OC Facklamia. OX NCBI_TaxID=883111 {ECO:0000313|EMBL:EKB53428.1, ECO:0000313|Proteomes:UP000004465}; RN [1] {ECO:0000313|EMBL:EKB53428.1, ECO:0000313|Proteomes:UP000004465} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CCUG 36813 {ECO:0000313|EMBL:EKB53428.1, RC ECO:0000313|Proteomes:UP000004465}; RG The Broad Institute Genome Sequencing Platform; RA Earl A., Ward D., Feldgarden M., Gevers D., Huys G., Walker B., RA Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B., RA Abouelleil A., Alvarado L., Arachchi H.M., Berlin A.M., Chapman S.B., RA Goldberg J., Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., RA Larimer J., McCowen C., Montmayeur A., Murphy C., Neiman D., RA Pearson M., Priest M., Roberts A., Saif S., Shea T., Sisk P., RA Sykes S., Wortman J., Nusbaum C., Birren B.; RT "The Genome Sequence of Facklamia hominis CCUG 36813."; RL Submitted (JUL-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EKB53428.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGZD01000013; EKB53428.1; -; Genomic_DNA. DR RefSeq; WP_006908994.1; NZ_JH932292.1. DR EnsemblBacteria; EKB53428; EKB53428; HMPREF9706_01686. DR PATRIC; fig|883111.3.peg.1705; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000004465; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000004465}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000004465}. FT DOMAIN 201 362 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 412 AA; 46971 MW; 6D1B8A46AD2F8B72 CRC64; MIEIETGPER VLIVGVETGD YTAEKFDELM QEMQSLTQTA KGQVVQVIRQ KLDHLDHRTA VGTGKLEEIK ACLELEEIDL VIFFNALSPS MNRNLEEALS VRVIDRIQLI LAIFAMRAKS REGKLQVSLA QYEYLLPRMT GSNKHLSRLA GGIGTRGPGE SKLESDRRHI RARINQIKES LKEVTQHRER TRSRRQSGRD FNIGLIGYTN AGKSTLLQAL THQETYIQDQ LFATLDPLTR KLTIKGYPVF TITDTVGFIE ALPTELIEAF KSTLEEIRYM DLLLHVVDAS SPARHMHEES VMNLMKQLDL DHLPMLTVYN KSDQAKSSFQ PILSPHITLS AKNPDDIERL KEAIWDQCIQ HAESYSVQVF PGEADLLALY QQNTLVEAID FDDEKQVYQV RGYRRHLNSQ QN // ID K1LUX6_9LACT Unreviewed; 427 AA. AC K1LUX6; DT 28-NOV-2012, integrated into UniProtKB/TrEMBL. DT 28-NOV-2012, sequence version 1. DT 07-JUN-2017, entry version 33. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=HMPREF9707_01556 {ECO:0000313|EMBL:EKB53803.1}; OS Facklamia ignava CCUG 37419. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Aerococcaceae; OC Facklamia. OX NCBI_TaxID=883112 {ECO:0000313|EMBL:EKB53803.1, ECO:0000313|Proteomes:UP000005147}; RN [1] {ECO:0000313|EMBL:EKB53803.1, ECO:0000313|Proteomes:UP000005147} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CCUG 37419 {ECO:0000313|EMBL:EKB53803.1, RC ECO:0000313|Proteomes:UP000005147}; RG The Broad Institute Genome Sequencing Platform; RA Earl A., Ward D., Feldgarden M., Gevers D., Huys G., Walker B., RA Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B., RA Abouelleil A., Alvarado L., Arachchi H.M., Berlin A.M., Chapman S.B., RA Goldberg J., Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., RA Larimer J., McCowen C., Montmayeur A., Murphy C., Neiman D., RA Pearson M., Priest M., Roberts A., Saif S., Shea T., Sisk P., RA Sykes S., Wortman J., Nusbaum C., Birren B.; RT "The Genome Sequence of Facklamia ignava CCUG 37419."; RL Submitted (JUL-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EKB53803.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGZE01000037; EKB53803.1; -; Genomic_DNA. DR EnsemblBacteria; EKB53803; EKB53803; HMPREF9707_01556. DR PATRIC; fig|883112.3.peg.1554; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000005147; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000005147}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000005147}. FT DOMAIN 216 379 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 427 AA; 49109 MW; 2D77FC329C70305D CRC64; MLYRKLDNSD HRKGIMIENQ IRPERVLIVG IQTEEMSDQK FQMNFDEMLD LTRTAQGNPV AQITQKLDRL HPKSAVGQGK LYEIKALIEV EEIDLVIFLN RLSPSINQYL EKELQIKVID RVQLILDIFA QRARTQAGQL QVKLAQYEYL LPRIVGQGLS LSRLGAGIGT RGPGETKLET DRRVIRKQIS QIKAQLKDLA NHRERARERR LNSHAFNIGL VGYTNAGKST LLNQLTQSGA YVQDQLFATL DPLTRQFSIN SHDLFTITDT VGFIDELPTE LIYAFRSTLE EIRDVDLLIH VVDSSSESRL MHEDTVDSLL KTLNMRNIPM LTVYNKGDLL KTPNQLVSLR QPSLIMSAYQ SQDIEKLKQM IWQEAIEQFK RYEAVVESND GQRLAKLRRT TLVESIDFDE KRQHYIVTGY ERQGDNE // ID K1LZ17_9BACT Unreviewed; 420 AA. AC K1LZ17; DT 28-NOV-2012, integrated into UniProtKB/TrEMBL. DT 28-NOV-2012, sequence version 1. DT 07-JUN-2017, entry version 31. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:EKB49354.1}; GN ORFNames=B879_02014 {ECO:0000313|EMBL:EKB49354.1}; OS Cecembia lonarensis LW9. OC Bacteria; Bacteroidetes; Cytophagia; Cytophagales; Cyclobacteriaceae; OC Cecembia. OX NCBI_TaxID=1225176 {ECO:0000313|EMBL:EKB49354.1, ECO:0000313|Proteomes:UP000004478}; RN [1] {ECO:0000313|EMBL:EKB49354.1, ECO:0000313|Proteomes:UP000004478} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=LW9 {ECO:0000313|EMBL:EKB49354.1, RC ECO:0000313|Proteomes:UP000004478}; RX PubMed=23144386; DOI=10.1128/JB.01729-12; RA Shivaji S., Ara S., Singh A., Pinnaka A.K.; RT "Draft Genome Sequence of Cecembia lonarensis Strain LW9T, Isolated RT from Lonar Lake, a Haloalkaline Lake in India."; RL J. Bacteriol. 194:6631-6631(2012). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EKB49354.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AMGM01000027; EKB49354.1; -; Genomic_DNA. DR RefSeq; WP_009185044.1; NZ_AMGM01000027.1. DR EnsemblBacteria; EKB49354; EKB49354; B879_02014. DR PATRIC; fig|1225176.3.peg.2149; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000004478; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 2. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000004478}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000004478}. FT DOMAIN 210 399 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 420 AA; 48072 MW; E1E9E720A757632D CRC64; MSKYSRKLQK LYDTAPKQET AVLVALIHQG QTEQQVQEYL DELAFLTETL GAKTVYKFTQ RLEKPDVRTF VGSGKLEEIQ AYVTHFEVDM IIFDDDLSPS QMRNLENELK VKVYDRSLLI LDIFLNRAQT AQAKTQVELA RFQYLLPRLT RMWTHLERQR GGTGTRGGAG EKEIETDKRD IRNKITLLKT KLKEIEKQGE TQRKGRKGIV RVALVGYTNV GKSTLMNLIT KTNILAENKL FATVDSTVRK VVLENIPFLL SDTVGFIRKL PTHLIESFKS TLDEIREADL LVHVVDISHP GFEDHIAVVK STLNEIGAGD KPMLLVFNKI DLVPAMPSEE EMHNMSEVEL EEQQYLDFGK LSKAYEKKTG IPPVFMAAEN GTNVEEFRTV LTKEVKKQHL KIYPHYLERE TIDLSQFGEE // ID K1M025_9FLAO Unreviewed; 403 AA. AC K1M025; DT 28-NOV-2012, integrated into UniProtKB/TrEMBL. DT 28-NOV-2012, sequence version 1. DT 07-JUN-2017, entry version 33. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=HMPREF9699_01668 {ECO:0000313|EMBL:EKB55678.1}; OS Bergeyella zoohelcum ATCC 43767. OC Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales; OC Flavobacteriaceae; Bergeyella. OX NCBI_TaxID=883096 {ECO:0000313|EMBL:EKB55678.1, ECO:0000313|Proteomes:UP000006085}; RN [1] {ECO:0000313|EMBL:EKB55678.1, ECO:0000313|Proteomes:UP000006085} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43767 {ECO:0000313|EMBL:EKB55678.1, RC ECO:0000313|Proteomes:UP000006085}; RG The Broad Institute Genome Sequencing Platform; RA Earl A., Ward D., Feldgarden M., Gevers D., Huys G., Walker B., RA Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B., RA Abouelleil A., Alvarado L., Arachchi H.M., Berlin A.M., Chapman S.B., RA Goldberg J., Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., RA Larimer J., McCowen C., Montmayeur A., Murphy C., Neiman D., RA Pearson M., Priest M., Roberts A., Saif S., Shea T., Sisk P., RA Sykes S., Wortman J., Nusbaum C., Birren B.; RT "The Genome Sequence of Bergeyella zoohelcum ATCC 43767."; RL Submitted (JUL-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EKB55678.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGYA01000027; EKB55678.1; -; Genomic_DNA. DR RefSeq; WP_002664051.1; NZ_JH932293.1. DR EnsemblBacteria; EKB55678; EKB55678; HMPREF9699_01668. DR PATRIC; fig|883096.3.peg.1719; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000006085; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000006085}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000006085}. FT DOMAIN 200 384 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 403 AA; 47041 MW; 5B810D2B7ED97C78 CRC64; MLEKKEHIYE KAVLVGLITK EQDEDKLTEY LDELEFLAYT AGATVEKRFT QKMLQPDSKT FVGKGKMEEI RDFVKENEIG TVIFDDELSP SQLKNLEREM EVKILDRTNL ILDIFAQRAQ TSYARTQVEL AQYEYLLPRL TRMWTHLERQ RGGIGMRGPG ETEIETDRRI IRDRISLLKE KLKTIDKQMA TQRNNRGKMV RVALVGYTNV GKSTLMNALS KSEVFAENKL FATLDTTVRK VVIGNLPFLL TDTVGFIRKL PTQLVESFKS TLDEVREADL LIHVVDISHE SFEDHIASVN QILQEIDAHR KPIIMIFNKI DDFSYEKKDE DDLTPITKKN ISLDEWKKTW MAKSKFPTVF ISALTKENFP EMKKLIYDEV LKIHISRFPY NDFLFEYYDD EEV // ID K1P0G2_CRAGI Unreviewed; 404 AA. AC K1P0G2; DT 28-NOV-2012, integrated into UniProtKB/TrEMBL. DT 28-NOV-2012, sequence version 1. DT 07-JUN-2017, entry version 19. DE SubName: Full=Putative GTP-binding protein ynbA {ECO:0000313|EMBL:EKC17177.1}; GN ORFNames=CGI_10002082 {ECO:0000313|EMBL:EKC17177.1}; OS Crassostrea gigas (Pacific oyster) (Crassostrea angulata). OC Eukaryota; Metazoa; Lophotrochozoa; Mollusca; Bivalvia; Pteriomorphia; OC Ostreoida; Ostreoidea; Ostreidae; Crassostrea. OX NCBI_TaxID=29159 {ECO:0000313|EMBL:EKC17177.1, ECO:0000313|Proteomes:UP000005408}; RN [1] {ECO:0000313|EMBL:EKC17177.1, ECO:0000313|Proteomes:UP000005408} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=05x7-T-G4-1.051#20 {ECO:0000313|EMBL:EKC17177.1}; RX PubMed=22992520; DOI=10.1038/nature11413; RA Zhang G., Fang X., Guo X., Li L., Luo R., Xu F., Yang P., Zhang L., RA Wang X., Qi H., Xiong Z., Que H., Xie Y., Holland P.W.H., Paps J., RA Zhu Y., Wu F., Chen Y., Wang J., Peng C., Meng J., Yang L., Liu J., RA Wen B., Zhang N., Huang Z., Zhu Q., Feng Y., Mount A., Hedgecock D., RA Xu Z., Liu Y., Domazet-Loso T., Du Y., Sun X., Zhang S., Liu B., RA Cheng P., Jiang X., Li J., Fan D., Wang W., Fu W., Wang T., Wang B., RA Zhang J., Peng Z., Li Y., Li N., Wang J., Chen M., He Y., Tan F., RA Song X., Zheng Q., Huang R., Yang H., Du X., Chen L., Yang M., RA Gaffney P.M., Wang S., Luo L., She Z., Ming Y., Huang W., Zhang S., RA Huang B., Zhang Y., Qu T., Ni P., Miao G., Wang J., Wang Q., RA Steinberg C.E.W., Wang H., Li N., Qian L., Zhang G., Li Y., Yang H., RA Liu X., Wang J., Yin Y., Wang J.; RT "The oyster genome reveals stress adaptation and complexity of shell RT formation."; RL Nature 490:49-54(2012). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JH823193; EKC17177.1; -; Genomic_DNA. DR RefSeq; XP_011421933.1; XM_011423631.1. DR EnsemblMetazoa; EKC17177; EKC17177; CGI_10002082. DR GeneID; 105324532; -. DR KEGG; crg:105324532; -. DR InParanoid; K1P0G2; -. DR OMA; FNNHAHV; -. DR OrthoDB; EOG091G0852; -. DR Proteomes; UP000005408; Unassembled WGS sequence. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000005408}; KW Reference proteome {ECO:0000313|Proteomes:UP000005408}. FT DOMAIN 211 385 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 404 AA; 46528 MW; 1E5A38DB07847CB2 CRC64; MQDLNSENSE KTRACIYDIQ LPEERHGEIV KRVEECESLV KTYGGKVIHK TIQRRHHAAT RTFIGHHKLE SLVALACEEK ANLIILNREL KPGQIYNIEF YLEKNKLQKQ IRIWDRLDLI IAIFSRHAKS SEAKLQLELA KIEHFGPRIY GMGEELSQQS AGIGTRGIGE TNTEIMKRHI AKRKKLLRKK IEKLQSIKKA NRDRRLKMGF KIVSIIGYTN AGKSQLFQSL TNKNNVVVRN ELFATLDTKI AHLFLPNTKP SQTVVLCDTI GFIRDLPTNL IDSFHSTLEE TIKSDLLLHV VDISENDFSA KIKEVEKVLK ILGCDHVPRF FIFNKIDKLS SEDFINSFQA SKMLSGYNYV FVSAKTGENI VQLREKITFW FFGGQVEKSE ENPSPFLREN YENH // ID K2GET0_9BACI Unreviewed; 416 AA. AC K2GET0; DT 28-NOV-2012, integrated into UniProtKB/TrEMBL. DT 28-NOV-2012, sequence version 1. DT 07-JUN-2017, entry version 36. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=MJ3_02152 {ECO:0000313|EMBL:EKE32722.1}; OS Salimicrobium jeotgali. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Salimicrobium. OX NCBI_TaxID=1230341 {ECO:0000313|EMBL:EKE32722.1, ECO:0000313|Proteomes:UP000011746}; RN [1] {ECO:0000313|EMBL:EKE32722.1, ECO:0000313|Proteomes:UP000011746} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MJ3 {ECO:0000313|EMBL:EKE32722.1, RC ECO:0000313|Proteomes:UP000011746}; RX PubMed=23144427; DOI=10.1128/JB.01808-12; RA Lee S.H., Jung J.Y., Jeon C.O.; RT "Draft Genome Sequence of Salimicrobium sp. Strain MJ3, Isolated from RT Myulchi-Jeot, Korean Fermented Seafood."; RL J. Bacteriol. 194:6695-6695(2012). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EKE32722.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AMPQ01000002; EKE32722.1; -; Genomic_DNA. DR RefSeq; WP_008587753.1; NZ_CP011361.2. DR EnsemblBacteria; EKE32722; EKE32722; MJ3_02152. DR KEGG; sje:AAV35_006725; -. DR PATRIC; fig|1230341.3.peg.446; -. DR KO; K03665; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000011746; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000011746}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Hydrolase {ECO:0000313|EMBL:EKE32722.1}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Protease {ECO:0000313|EMBL:EKE32722.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000011746}. FT DOMAIN 195 356 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 416 AA; 47432 MW; CBCE3E00809B7559 CRC64; MDKEKALILA RKDPRKKETF DYSLEELKDL TKTAGGEVVS VLVQQLEKPH KAHYLGDGKL EEAAGVIEEH EIELVIINDE LSPTQLRNIT NRLEVRVIDR SQLILDIFAY RAKTKEGKLQ VELAQLQYLL PRLSGQGVQL SRLGGGIGTR GPGETKLETD RRHIRRRIRD VRTRLDQVVE HRKQYRERRK ENSAFQVAIV GYTNAGKTTF FNKITSADSL QEDKLFATLD PLTRQTQLPS GLEVLMSDTV GFIQHLPTTL IAAFRSTLEE VTEADFILHI VDASASDHDQ HEKTVLSLLE ELGAENLPRL TVYNKQDKVE GPFTPMEKPS VQTSFKDDRG VGDALSAIEE VLSENWDPYH TYVKAEEGKF LKTLELNTLV YVREFLEERG EYVVRGYIDP LHPLRDKVIP KEHKDE // ID K2HKZ3_9RHOB Unreviewed; 416 AA. AC K2HKZ3; DT 28-NOV-2012, integrated into UniProtKB/TrEMBL. DT 28-NOV-2012, sequence version 1. DT 07-JUN-2017, entry version 30. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=OCGS_2306 {ECO:0000313|EMBL:EKE43574.1}; OS Oceaniovalibus guishaninsula JLT2003. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae; Oceaniovalibus. OX NCBI_TaxID=1231392 {ECO:0000313|EMBL:EKE43574.1, ECO:0000313|Proteomes:UP000006765}; RN [1] {ECO:0000313|EMBL:EKE43574.1, ECO:0000313|Proteomes:UP000006765} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=JLT2003 {ECO:0000313|EMBL:EKE43574.1, RC ECO:0000313|Proteomes:UP000006765}; RX PubMed=23144420; DOI=10.1128/JB.01874-12; RA Tang K., Liu K., Jiao N.; RT "Draft Genome Sequence of Oceaniovalibus guishaninsula JLT2003T."; RL J. Bacteriol. 194:6683-6683(2012). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EKE43574.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AMGO01000052; EKE43574.1; -; Genomic_DNA. DR RefSeq; WP_007427458.1; NZ_AMGO01000052.1. DR EnsemblBacteria; EKE43574; EKE43574; OCGS_2306. DR PATRIC; fig|1231392.3.peg.2318; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000006765; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000006765}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000006765}. FT DOMAIN 196 365 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 416 AA; 45576 MW; 3EC033866A85B613 CRC64; MRALVLHPDI QTDRDRRPAG PALGEALALA AALPDLDVAG GEVVRLPRAH PGHLFGTGKL AELKARIEAD DVGLVLIDGP VSPVQQRNLE KEWSVKVLDR TGLILEIFSD RARTREGVLQ VEMAALSYQR TRLVRAWTHL ERQRGGLGFV GGPGETQIEA DRRAIDDQIV RLRKQLDKVV RTRELHRAAR AKVPYPIVAL VGYTNAGKST LFNRLTGADV MAKDMLFATL DPTMRRIDLP SGAEIILSDT VGFISDLPTQ LVAAFRATLE EVLAADLIVH VRDIAHPETE AQARDVEAIL TELGVDDATP RIEVWNKADL LAEDAASATA AQAARRDDVL ILSALTGAGI DTLTAAITAA LDEARMRKTL VLPHAAGKRR AWLYEQGVVE DERQSEDGNH LTVNWTARQA RRFHDL // ID K2IYA7_9GAMM Unreviewed; 436 AA. AC K2IYA7; DT 28-NOV-2012, integrated into UniProtKB/TrEMBL. DT 28-NOV-2012, sequence version 1. DT 30-AUG-2017, entry version 33. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=B3C1_17972 {ECO:0000313|EMBL:EKE67858.1}; OS Gallaecimonas xiamenensis 3-C-1. OC Bacteria; Proteobacteria; Gammaproteobacteria; Gallaecimonas. OX NCBI_TaxID=745411 {ECO:0000313|EMBL:EKE67858.1, ECO:0000313|Proteomes:UP000006755}; RN [1] {ECO:0000313|EMBL:EKE67858.1, ECO:0000313|Proteomes:UP000006755} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=3-C-1 {ECO:0000313|EMBL:EKE67858.1, RC ECO:0000313|Proteomes:UP000006755}; RX PubMed=23209203; DOI=10.1128/JB.01854-12; RA Lai Q., Wang L., Wang W., Shao Z.; RT "Genome Sequence of Gallaecimonas xiamenensis Type Strain 3-C-1."; RL J. Bacteriol. 194:6937-6937(2012). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EKE67858.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AMRI01000036; EKE67858.1; -; Genomic_DNA. DR RefSeq; WP_008486587.1; NZ_AMRI01000036.1. DR ProteinModelPortal; K2IYA7; -. DR EnsemblBacteria; EKE67858; EKE67858; B3C1_17972. DR PATRIC; fig|745411.4.peg.3533; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000006755; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000006755}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Hydrolase {ECO:0000313|EMBL:EKE67858.1}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Protease {ECO:0000313|EMBL:EKE67858.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000006755}. FT DOMAIN 198 365 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 436 AA; 48832 MW; 0E22D731452EEB0E CRC64; MFDRYEAGEQ AVLVHVDFAA ESDREDLDEL KMLVDSAGVT TLAVVTTRRN APHPKFYIGT GKAEEVAETV QALGAEVVIF NHALSPAQER NLERLFQCRV LDRTTLILDI FAQRARTHEG KLQVELAQLK HLSTRLVRGW THLERQKGGI GLRGPGETQL ETDRRLLRDR ITHIQKRLEK VAKQREQGRR ARSRREVPTL SLVGYTNAGK STLFNALTSA DVYAADQLFA TLDPTLRKVQ LADVGPVILA DTVGFIRHLP HDLVAAFKAT LEETREASLL LHVVDAADER AADNTLQVKH VLKEIEADEV PVLMVYNKLD KLDDVAPRID RSDDGTPVAV WLSAQKHQGL ELLLQALSER VSEEVFCATL CLPPSQGKLR AELFALQAVT EERIDDQGQW LLKVRMPDID WQRLNKQGQG AALRFIVSDP ADKVLQ // ID K2JCZ7_9RHOB Unreviewed; 432 AA. AC K2JCZ7; DT 28-NOV-2012, integrated into UniProtKB/TrEMBL. DT 28-NOV-2012, sequence version 1. DT 07-JUN-2017, entry version 31. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=B30_06461 {ECO:0000313|EMBL:EKE72602.1}; OS Celeribacter baekdonensis B30. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae; Celeribacter. OX NCBI_TaxID=1208323 {ECO:0000313|EMBL:EKE72602.1, ECO:0000313|Proteomes:UP000006762}; RN [1] {ECO:0000313|EMBL:EKE72602.1, ECO:0000313|Proteomes:UP000006762} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=B30 {ECO:0000313|EMBL:EKE72602.1, RC ECO:0000313|Proteomes:UP000006762}; RA Wang W.; RT "Celeribacter baekdonensis B30 Genome Sequencing."; RL Submitted (SEP-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EKE72602.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AMRK01000003; EKE72602.1; -; Genomic_DNA. DR EnsemblBacteria; EKE72602; EKE72602; B30_06461. DR PATRIC; fig|1208323.3.peg.1332; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000006762; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000006762}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000006762}. FT DOMAIN 207 381 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 432 AA; 48649 MW; 990F30E4A73BE113 CRC64; MSELHEHEVL KTRAWVIHPD ITSDRNRRDP VAGLEEAVAL ADALPELEVV GSEIVRLPKM QPGQLFGSGK IAELKERLNA AEVDLVLIDG RVSPVQQRNL EKEWKVKLLD RTGLILEIFS DRARTREGVL QVEMAALTYQ RTRLVRAWTH LERQRGGLGF VGGPGETQIE ADRRAIDDHL LRLKRQLEKV VKTRELHRAA RAKVPFPIVA LVGYTNAGKS TFFNKVTGAD VFVKDMLFAT LDPTMRSVVL EAPQGGTDRE IILSDTVGFI SSLPTQLVAA FRATLEEVLD ADLILHVRDI SHEKSDEQAA DVRKILSDLG IKEDAPMFEV WNKIDLLDDE ARQARLERAQ SEDDKFAISA VTGEGVADLL AAISKYFEEE KISRDLLLPY AQGKQRAWLF AEGVVEQETA TEEGYQMTVL WTPRQEKQFR EM // ID K2JQW3_9PROT Unreviewed; 456 AA. AC K2JQW3; DT 28-NOV-2012, integrated into UniProtKB/TrEMBL. DT 28-NOV-2012, sequence version 1. DT 07-JUN-2017, entry version 31. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=P24_04774 {ECO:0000313|EMBL:EKE77653.1}; OS Oceanibaculum indicum P24. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales; OC Rhodospirillaceae; Oceanibaculum. OX NCBI_TaxID=1207063 {ECO:0000313|EMBL:EKE77653.1, ECO:0000313|Proteomes:UP000006746}; RN [1] {ECO:0000313|EMBL:EKE77653.1, ECO:0000313|Proteomes:UP000006746} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=P24 {ECO:0000313|EMBL:EKE77653.1, RC ECO:0000313|Proteomes:UP000006746}; RX PubMed=23209207; DOI=10.1128/JB.01859-12; RA Lai Q., Shao Z.; RT "Genome Sequence of Oceanibaculum indicum Type Strain P24."; RL J. Bacteriol. 194:6942-6942(2012). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EKE77653.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AMRL01000004; EKE77653.1; -; Genomic_DNA. DR EnsemblBacteria; EKE77653; EKE77653; P24_04774. DR PATRIC; fig|1207063.3.peg.967; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000006746; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000006746}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000006746}. FT DOMAIN 226 398 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 192 222 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 456 AA; 50292 MW; 2745C81143A56D3D CRC64; MSRTPANGMG DSFHERNQGI ATQASSTRAL ILHLDLLSAA DKSGGAVRAP EARLEEACGL ALAIDLDIVH SEVVRVSRAT PATLMGSGQV ERFADVIDAM EIEVAVIDTA LSPVQQRNLE RSLKCKVIDR TALILEIFGA RARTHEGRLQ VELAALTYQR SRLVRSWTHL ERQRGGAGFM GGPGESQIEL DRRIIDDKIV KLKRQLDEVK RTRELHRSAR RKVPYPIVAL VGYTNAGKST LFNRMTRSAV FAKDLLFATL DPTMRRLSLP SGRQIILSDT VGFISDLPTQ LVAAFRATLE EVLEADIILH VRDVAHPDSA AQRADVEAVL ADLGIAPEES DTPIIEVLNK VDLLPEEDRA QVLNLAARDP DKVAVSALEG SGTDELLTLL DQRLNARREL LRVDVDLSDG ATLAWLYRHG EVLEREDDEK HSHLLVGLDP ADRARFERRQ AGQPLS // ID K2KFW5_9GAMM Unreviewed; 432 AA. AC K2KFW5; DT 28-NOV-2012, integrated into UniProtKB/TrEMBL. DT 28-NOV-2012, sequence version 1. DT 30-AUG-2017, entry version 34. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=A10D4_10741 {ECO:0000313|EMBL:EKE81549.1}; OS Idiomarina xiamenensis 10-D-4. OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales; OC Idiomarinaceae; Idiomarina. OX NCBI_TaxID=740709 {ECO:0000313|EMBL:EKE81549.1, ECO:0000313|Proteomes:UP000014115}; RN [1] {ECO:0000313|EMBL:EKE81549.1, ECO:0000313|Proteomes:UP000014115} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=10-D-4 {ECO:0000313|EMBL:EKE81549.1, RC ECO:0000313|Proteomes:UP000014115}; RX PubMed=23209204; DOI=10.1128/JB.01855-12; RA Lai Q., Wang L., Wang W., Shao Z.; RT "Genome Sequence of Idiomarina xiamenensis Type Strain 10-D-4."; RL J. Bacteriol. 194:6938-6938(2012). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EKE81549.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AMRG01000013; EKE81549.1; -; Genomic_DNA. DR RefSeq; WP_008489485.1; NZ_AMRG01000013.1. DR EnsemblBacteria; EKE81549; EKE81549; A10D4_10741. DR PATRIC; fig|740709.3.peg.2171; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000014115; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000014115}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000014115}. FT DOMAIN 198 365 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 432 AA; 48403 MW; 7739D9E2C5EDABEC CRC64; MFDRYESGEQ AILVHVDLPA EVDREDLSEL KLLVSSAGVE TLGVVTASRA SPSPKFFVGS GKAEEIAEQV KALNANIIIF NHALSPTQER NLEKVCECRV LDRTGLILDI FAQRARTHEG KLQVELAQLR HIATRLVRGW THLERQKGGI GLRGPGETQL ETDRRLIRGR IKNILRRLER VQKQREQGRR ARKRAEVPTV SLVGYTNAGK STLFNRLTAS DVYAADQLFA TLDPTLRRID VDEVGPVILA DTVGFIRHLP HDLVAAFKAT LQETQEADLL LHVVDVADEQ QQENIDQVAE VLAEIEADQV PQLLICNKID KLAEATPRID YDDDGKPQRV WLSAQSGAGT DLISQALQQL LGPSMHDMTL SLPPAMGKLR GVLYQLDAVL EEQLTEQGEL ALHVRIADID WRRLLKQYQE QGKDLEAYID RR // ID K2N270_9RHIZ Unreviewed; 458 AA. AC K2N270; DT 28-NOV-2012, integrated into UniProtKB/TrEMBL. DT 28-NOV-2012, sequence version 1. DT 07-JUN-2017, entry version 32. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=NA2_13240 {ECO:0000313|EMBL:EKF18363.1}; OS Nitratireductor pacificus pht-3B. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Phyllobacteriaceae; Nitratireductor. OX NCBI_TaxID=391937 {ECO:0000313|EMBL:EKF18363.1, ECO:0000313|Proteomes:UP000006786}; RN [1] {ECO:0000313|EMBL:EKF18363.1, ECO:0000313|Proteomes:UP000006786} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=pht-3B {ECO:0000313|Proteomes:UP000006786}; RX PubMed=23209217; DOI=10.1128/JB.01905-12; RA Lai Q., Li G., Shao Z.; RT "Genome Sequence of Nitratireductor pacificus Type Strain pht-3B."; RL J. Bacteriol. 194:6958-6958(2012). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EKF18363.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AMRM01000014; EKF18363.1; -; Genomic_DNA. DR RefSeq; WP_008597485.1; NZ_AMRM01000014.1. DR EnsemblBacteria; EKF18363; EKF18363; NA2_13240. DR PATRIC; fig|391937.3.peg.2718; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000006786; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000006786}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000006786}. FT DOMAIN 226 397 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 185 219 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 458 AA; 49824 MW; AFC98825E3ECA2E1 CRC64; MTQPRKPEGR GQTDDSGTRG AVATRAFVVS PVLAADRRAA ESGTTPARSP EARSEEAVGL AEAIDLQVVS AEIIPVGTPR PATLIGTGKL DDLAARVAEA EIEVVIIDHP LTPVQQRNLE KALNAKVLDR TGLILEIFGR RARTKEGRLQ VELAHLEYQR GRLVRSWTHL ERQRGGGGFM GGPGETQIEA DRRLLQDRIV RLKRELETVR RTRDLHRSKR RKVPFPIVAI VGYTNAGKST LFNRLTGAAV MAEDMLFATL DPTLRRVQLP HGTTIILSDT VGFISDLPTH LVAAFRATLE EVIEADLVIH LRDISDPASS AQAADVEEIL GDLGVDVADK KHVLEVWNKI DNLDAEKRRA LLDGTRGAEA PLAVSAVTGE GIDALLAQVE ARISGVVKAI TISLTPAQMP LLDWVYRNGD VTERSDNDDG SVTMTVRATD AARREISERL GSRPAEEA // ID K2N891_9RHIZ Unreviewed; 436 AA. AC K2N891; DT 28-NOV-2012, integrated into UniProtKB/TrEMBL. DT 28-NOV-2012, sequence version 1. DT 07-JUN-2017, entry version 31. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=NA8A_02660 {ECO:0000313|EMBL:EKF43678.1}; OS Nitratireductor indicus C115. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Phyllobacteriaceae; Nitratireductor. OX NCBI_TaxID=1231190 {ECO:0000313|EMBL:EKF43678.1, ECO:0000313|Proteomes:UP000007374}; RN [1] {ECO:0000313|EMBL:EKF43678.1, ECO:0000313|Proteomes:UP000007374} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C115 {ECO:0000313|EMBL:EKF43678.1, RC ECO:0000313|Proteomes:UP000007374}; RX PubMed=23209238; DOI=10.1128/JB.01917-12; RA Lai Q., Li G., Yu Z., Shao Z.; RT "Genome Sequence of Nitratireductor indicus Type Strain C115."; RL J. Bacteriol. 194:6990-6990(2012). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EKF43678.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AMSI01000002; EKF43678.1; -; Genomic_DNA. DR EnsemblBacteria; EKF43678; EKF43678; NA8A_02660. DR PATRIC; fig|1231190.3.peg.561; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000007374; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000007374}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000007374}. FT DOMAIN 206 377 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 165 199 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 436 AA; 47811 MW; 537101F678366CBC CRC64; MAEPTRAFVV TPILAAERRA AEKGAPIRSA DARSQEAVGL AEAIDLDVIA AEIVAVNQPR PATLLGTGKL DELAARVAEA EAEVVIVDHP LTPVQQRNLE KALNAKVLDR TGLILEIFGR RARTKEGRLQ VDLAHLEYQR GRLVRSWTHL ERQRGGGGFM GGPGETQIEA DRRLLQDKIV RLKRELETVR RTRDLHRSKR RKVPFPIVAI VGYTNAGKST LFNRLTGASV MAEDMLFATL DPTLRRVQLP HGTTVILSDT VGFISDLPTH LVAAFRATLE EVVEADLIIH LRDISDPDSS AQANDVASIL GDLGVDAADK TRVLEVWNKI DNLADEQRHA QLEITHGPDA PIAISAVTGE GIDTLLSTVE QRISGALAPL TLTLSPRQMQ FLDWVYRHGD VVERKDNDDG SITITVRATD MARNEILEKL TGDSKS // ID K2P7S7_9RHIZ Unreviewed; 444 AA. AC K2P7S7; DT 28-NOV-2012, integrated into UniProtKB/TrEMBL. DT 28-NOV-2012, sequence version 1. DT 07-JUN-2017, entry version 32. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=QWE_22001 {ECO:0000313|EMBL:EKF57058.1}; OS Agrobacterium albertimagni AOL15. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Rhizobiaceae; Rhizobium/Agrobacterium group; Agrobacterium. OX NCBI_TaxID=1156935 {ECO:0000313|EMBL:EKF57058.1, ECO:0000313|Proteomes:UP000007123}; RN [1] {ECO:0000313|EMBL:EKF57058.1, ECO:0000313|Proteomes:UP000007123} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=AOL15 {ECO:0000313|EMBL:EKF57058.1, RC ECO:0000313|Proteomes:UP000007123}; RX PubMed=23209236; DOI=10.1128/JB.01912-12; RA Trimble W.L., Phung le T., Meyer F., Gilbert J.A., Silver S.; RT "Draft Genome Sequence of Agrobacterium albertimagni Strain AOL15."; RL J. Bacteriol. 194:6986-6987(2012). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EKF57058.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ALJF01000023; EKF57058.1; -; Genomic_DNA. DR RefSeq; WP_006728385.1; NZ_ALJF01000023.1. DR EnsemblBacteria; EKF57058; EKF57058; QWE_22001. DR PATRIC; fig|1156935.5.peg.4478; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000007123; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000007123}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000007123}. FT DOMAIN 206 378 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 165 199 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 444 AA; 49194 MW; A78C1655983324F0 CRC64; MRALVLVPVL KQAKAQPLPD GAPPAPSRSN EARLEEAIGL ARAIDLTIVQ GLIVQINQPR PATLMGSGKI AEVKALLDEH NAGLVIVDHP LTPVQQRNLE KEWGAKVIDR TGLILEIFGR RASTKEGTLQ VELAHLNYQK GRLVRSWTHL ERQRGGAGFM GGPGETQIEA DRRQLQDKII KLERELEQVV RTRQLHRAKR RKVPHPIVAL VGYTNAGKST LFNRITGAGV LAEDMLFATL DPTLRRMKLP HGRTVIMSDT VGFISDLPTH LVAAFRATLE EVLEADLVLH VRDMSDPDNG AQSADVLRIL DDLGIDEKER AERILEVWNK IDRLDPENHD GLLQKAAGRE NVLPVSAVTG EGVDTLLDVI SQRLSGVLTE ATITIPSDKH AVISWLYENG IVDGREDHED GSVSLDMRLT DRQANELERK LGGLKPPVRE DWER // ID K2Q720_9FLAO Unreviewed; 403 AA. AC K2Q720; DT 28-NOV-2012, integrated into UniProtKB/TrEMBL. DT 28-NOV-2012, sequence version 1. DT 07-JUN-2017, entry version 31. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=I215_00640 {ECO:0000313|EMBL:EKF56676.1}; OS Galbibacter marinus. OC Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales; OC Flavobacteriaceae; Galbibacter. OX NCBI_TaxID=555500 {ECO:0000313|EMBL:EKF56676.1, ECO:0000313|Proteomes:UP000007364}; RN [1] {ECO:0000313|EMBL:EKF56676.1, ECO:0000313|Proteomes:UP000007364} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ck-I2-15 {ECO:0000313|Proteomes:UP000007364}; RX PubMed=23209227; DOI=10.1128/JB.01852-12; RA Lai Q., Li C., Shao Z.; RT "Genome Sequence of Galbibacter marinum Type Strain ck-I2-15."; RL J. Bacteriol. 194:6973-6973(2012). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EKF56676.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AMSG01000001; EKF56676.1; -; Genomic_DNA. DR RefSeq; WP_008990005.1; NZ_AMSG01000001.1. DR EnsemblBacteria; EKF56676; EKF56676; I215_00640. DR PATRIC; fig|555500.3.peg.133; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000007364; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000007364}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000007364}. FT DOMAIN 200 385 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 403 AA; 46754 MW; 148109C33727419C CRC64; MLERKQIDYE KVVLVGIITK EQDEEKSQEY LDELEFLAFT AGGTVEGRFT QKIDLPNPKT FIGSGKMEEI LTFVDENDIG TVIFDDELTP AQQKNIERVL KVKVLDRTSL ILDIFAQRAQ TSYARTQVEL AQYQYLLPRL TGLWTHLERQ RGGIGMRGPG ETEIETDRRI VRDRIALLKK KLTKIDKQME TQRGNRGALV RVALIGYTNV GKSTLMNVIS KSDVFAENKL FATLDTTVRK VVIGNLPFLL TDTVGFIRKL PTQLVESFKS TLDEVREADL LLHVVDISHP TFEDHINSVN QILDEIKSAD KPTIMVFNKI DNYEHLTIEE DDLVTERTTK HFTLEEWKNT WMNRMGDNVL FISALERENL EEFRKRVYEE VRRIHVTRFP YNSFLYPEYN EDL // ID K3ZHX7_SETIT Unreviewed; 557 AA. AC K3ZHX7; DT 28-NOV-2012, integrated into UniProtKB/TrEMBL. DT 28-NOV-2012, sequence version 1. DT 30-AUG-2017, entry version 34. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:KQK95141.1, ECO:0000313|EnsemblPlants:Si026179m}; GN Name=LOC101777129 {ECO:0000313|EnsemblPlants:Si026179m}; GN ORFNames=SETIT_026179mg {ECO:0000313|EMBL:KQK95141.1}; OS Setaria italica (Foxtail millet) (Panicum italicum). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACMAD clade; Panicoideae; Panicodae; Paniceae; Cenchrinae; Setaria. OX NCBI_TaxID=4555 {ECO:0000313|EnsemblPlants:Si026179m}; RN [1] {ECO:0000313|EMBL:KQK95141.1, ECO:0000313|EnsemblPlants:Si026179m, ECO:0000313|Proteomes:UP000004995} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Yugu1 {ECO:0000313|EnsemblPlants:Si026179m, RC ECO:0000313|Proteomes:UP000004995}, and RC Yugu1 {ECO:0000313|EMBL:KQK95141.1}; RX PubMed=22580951; DOI=10.1038/nbt.2196; RA Bennetzen J.L., Schmutz J., Wang H., Percifield R., Hawkins J., RA Pontaroli A.C., Estep M., Feng L., Vaughn J.N., Grimwood J., RA Jenkins J., Barry K., Lindquist E., Hellsten U., Deshpande S., RA Wang X., Wu X., Mitros T., Triplett J., Yang X., Ye C.Y., RA Mauro-Herrera M., Wang L., Li P., Sharma M., Sharma R., Ronald P.C., RA Panaud O., Kellogg E.A., Brutnell T.P., Doust A.N., Tuskan G.A., RA Rokhsar D., Devos K.M.; RT "Reference genome sequence of the model plant Setaria."; RL Nat. Biotechnol. 30:555-561(2012). RN [2] {ECO:0000313|EnsemblPlants:Si026179m} RP IDENTIFICATION. RC STRAIN=Yugu1 {ECO:0000313|EnsemblPlants:Si026179m}; RG EnsemblPlants; RL Submitted (OCT-2012) to UniProtKB. RN [3] {ECO:0000313|EMBL:KQK95141.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=Yugu1 {ECO:0000313|EMBL:KQK95141.1}; RA Cajimat M.N.B., Milazzo M.L., Fulhorst C.F.; RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CM003535; KQK95141.1; -; Genomic_DNA. DR RefSeq; XP_004979600.1; XM_004979543.2. DR STRING; 4555.Si026179m; -. DR EnsemblPlants; Si026179m; Si026179m; Si026179m.g. DR GeneID; 101777129; -. DR Gramene; Si026179m; Si026179m; Si026179m.g. DR KEGG; sita:101777129; -. DR eggNOG; KOG0410; Eukaryota. DR eggNOG; COG2262; LUCA. DR InParanoid; K3ZHX7; -. DR KO; K03665; -. DR OMA; VILEIFH; -. DR OrthoDB; EOG093609UJ; -. DR Proteomes; UP000004995; Chromosome VIII. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000004995}; KW Reference proteome {ECO:0000313|Proteomes:UP000004995}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1 21 {ECO:0000256|SAM:SignalP}. FT CHAIN 22 557 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5010127820. FT DOMAIN 333 498 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 557 AA; 61200 MW; E46551B9D1097707 CRC64; MSAAACLFAA AVSLTLPSTS APAFAGASGR RSRWIPAALR SSPTRRRGPV RALDERLLEA AAAPAAKDTE GEEAGVDVGD GFGDAEGDGV GAQEVVEEEQ RPPARAFVKS RRQRQEEEEA AAGQDRFKLI NGKEIFQEKA YLVGVEFKRT GGNLFGIEES LKELEQLADT AGLVVVGSTY QKLSTPNPRT YIGSGKVSEI RSAIQALDVE TVIFDDELSP GQLRNLEKSF GGSVRVCDRT ALILDIFNQR AATHEAALQV TLAQMEYQLP RLTKMWNHLE RQAGGQVKGM GEKQIEVDKR ILRTQIGALK KELESVRKHR KLYRNRRQSV PIPVVSLVGY TNAGKSTLLN RLTGADVLAE DKLFATLDPT TRRVLMKNGT EFLLTDTVGF IQKLPTMLVA AFRATLEEIS ESSVIVHLVD ISHPLAQQQI DAVDRVLKEL DVESIPKLVV WNKIDNTDEP LRVKEEAENQ GIICISAMNG DGLEEFCNTI QAKLKDSMVP IEAFVPYDKG DLLNDIHKVG MVEKMEYKEN GTFVKAHVPL PLARLLTPLR QQVVAAV // ID K4A7F1_SETIT Unreviewed; 593 AA. AC K4A7F1; DT 28-NOV-2012, integrated into UniProtKB/TrEMBL. DT 28-NOV-2012, sequence version 1. DT 07-JUN-2017, entry version 30. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:KQK87316.1, ECO:0000313|EnsemblPlants:Si034807m}; GN Name=LOC101754455 {ECO:0000313|EnsemblPlants:Si034807m}; GN ORFNames=SETIT_034807mg {ECO:0000313|EMBL:KQK87316.1}; OS Setaria italica (Foxtail millet) (Panicum italicum). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACMAD clade; Panicoideae; Panicodae; Paniceae; Cenchrinae; Setaria. OX NCBI_TaxID=4555 {ECO:0000313|EnsemblPlants:Si034807m}; RN [1] {ECO:0000313|EMBL:KQK87316.1, ECO:0000313|EnsemblPlants:Si034807m, ECO:0000313|Proteomes:UP000004995} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Yugu1 {ECO:0000313|EnsemblPlants:Si034807m, RC ECO:0000313|Proteomes:UP000004995}, and RC Yugu1 {ECO:0000313|EMBL:KQK87316.1}; RX PubMed=22580951; DOI=10.1038/nbt.2196; RA Bennetzen J.L., Schmutz J., Wang H., Percifield R., Hawkins J., RA Pontaroli A.C., Estep M., Feng L., Vaughn J.N., Grimwood J., RA Jenkins J., Barry K., Lindquist E., Hellsten U., Deshpande S., RA Wang X., Wu X., Mitros T., Triplett J., Yang X., Ye C.Y., RA Mauro-Herrera M., Wang L., Li P., Sharma M., Sharma R., Ronald P.C., RA Panaud O., Kellogg E.A., Brutnell T.P., Doust A.N., Tuskan G.A., RA Rokhsar D., Devos K.M.; RT "Reference genome sequence of the model plant Setaria."; RL Nat. Biotechnol. 30:555-561(2012). RN [2] {ECO:0000313|EnsemblPlants:Si034807m} RP IDENTIFICATION. RC STRAIN=Yugu1 {ECO:0000313|EnsemblPlants:Si034807m}; RG EnsemblPlants; RL Submitted (OCT-2012) to UniProtKB. RN [3] {ECO:0000313|EMBL:KQK87316.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=Yugu1 {ECO:0000313|EMBL:KQK87316.1}; RA Cajimat M.N.B., Milazzo M.L., Fulhorst C.F.; RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CM003536; KQK87316.1; -; Genomic_DNA. DR RefSeq; XP_012704243.1; XM_012848789.1. DR RefSeq; XP_012704244.1; XM_012848790.1. DR RefSeq; XP_012704245.1; XM_012848791.1. DR STRING; 4555.Si034807m; -. DR EnsemblPlants; Si034807m; Si034807m; Si034807m.g. DR GeneID; 101754455; -. DR Gramene; Si034807m; Si034807m; Si034807m.g. DR KEGG; sita:101754455; -. DR eggNOG; KOG0410; Eukaryota. DR eggNOG; COG2262; LUCA. DR InParanoid; K4A7F1; -. DR OMA; NGPEAIS; -. DR OrthoDB; EOG09360975; -. DR Proteomes; UP000004995; Chromosome IX. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR CDD; cd01878; HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000004995}; KW Reference proteome {ECO:0000313|Proteomes:UP000004995}. FT DOMAIN 309 565 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 593 AA; 65237 MW; E90903464AC0862B CRC64; MLRSAISRLG ARLRLRLHHD PRTHHPSPVS PHLRALSSRR GKRSSPTASP ADTEDEGPLS GLFVLSRDPE CPPRLLVVQP RLRPGSLLDT KLAEALNLAN SLEEPRDGFY HSEFGAKGAP RHLVVQNPAS RGRSHADTYF GPGTVDNVKC YLRASESEEE DVDAVFVNTI LSGIQQRNLE VAWGKPVLDR VGLIIEIFNA HAETKEAKLQ SELAALMYMK TRLVRVRGPG GALTFGPSGE AEVVSARGRG SGGRGFMSGA GETELQLQRR RIQERRVKLL TQIEHVRRTR AIQRSGRKRH GGSFGQELVT VAVVGYTNAG KSTLVSALSE TDLYSDDRLF ATVDPRLRSV ILPSGRKALL SDTVGFISDL PIQLVEAFHA TLEEVVEADM LVHVLDSSAP NLEEHRSTVL QVLQQIGVSQ EKINNMIEVW NKIDLVDENA ASDGVEDEIF LTEGEEEDDM FSEDGVPSEQ SSLDSLDDGA DSEYLSEEKF EDNNDEVSSK ESSEMKAMNP DLSSKECFGE LCVPDAIGYP LTQQMPSCHV KTSAVTGVGL QELLALIDRK LTEQQNVVQR SYGPFDRKWR PSSSMDGEKA AEQ // ID K4BCZ8_SOLLC Unreviewed; 613 AA. AC K4BCZ8; DT 28-NOV-2012, integrated into UniProtKB/TrEMBL. DT 28-NOV-2012, sequence version 1. DT 07-JUN-2017, entry version 31. DE SubName: Full=Uncharacterized protein {ECO:0000313|EnsemblPlants:Solyc02g092010.2.1}; OS Solanum lycopersicum (Tomato) (Lycopersicon esculentum). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae; OC Pentapetalae; asterids; lamiids; Solanales; Solanaceae; Solanoideae; OC Solaneae; Solanum; Lycopersicon. OX NCBI_TaxID=4081 {ECO:0000313|EnsemblPlants:Solyc02g092010.2.1, ECO:0000313|Proteomes:UP000004994}; RN [1] {ECO:0000313|EnsemblPlants:Solyc02g092010.2.1} RP IDENTIFICATION. RC STRAIN=cv. Heinz 1706 {ECO:0000313|EnsemblPlants:Solyc02g092010.2.1}; RG EnsemblPlants; RL Submitted (JUN-2015) to UniProtKB. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR RefSeq; XP_004231950.1; XM_004231902.3. DR UniGene; Les.11795; -. DR STRING; 4081.Solyc02g092010.2.1; -. DR PaxDb; K4BCZ8; -. DR EnsemblPlants; Solyc02g092010.2.1; Solyc02g092010.2.1; Solyc02g092010.2. DR GeneID; 101245217; -. DR Gramene; Solyc02g092010.2.1; Solyc02g092010.2.1; Solyc02g092010.2. DR KEGG; sly:101245217; -. DR eggNOG; KOG0410; Eukaryota. DR eggNOG; COG2262; LUCA. DR InParanoid; K4BCZ8; -. DR OMA; CNEDEVP; -. DR OrthoDB; EOG09360975; -. DR Proteomes; UP000004994; Chromosome 2. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR GO; GO:0043022; F:ribosome binding; IBA:GO_Central. DR CDD; cd01878; HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000004994}; KW Reference proteome {ECO:0000313|Proteomes:UP000004994}. FT DOMAIN 320 588 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 613 AA; 67890 MW; F71208F7153C8FE8 CRC64; MLRTISNLRS SLTSGICLPQ ALRHFSQFSI SLLPTQTQSI HLLVNPSPST QSSLFHSLSS PCSSLLLQKH QDGSGDDFNT DPKSPPRLFV VQPRFRPDSV LKPKLNEALN LANSLEEQRH GFYDTEFLDK QMPHHLVVQN PASRSIRADT FFGPGTVDTV KCHVNSLDTQ EGIDAIFVNA ILTGIQQRNL ERAWGKPVLD RVGLIIEIFN AHAQTKEAKL QAELAALMYK KSRLVRVRGP GGRYGFGVGG EAEVVSARGR GSGGRGFISG AGETELQLQR RRILERRNQL LSEIKEVRRT RALQRAARKR HGGSDGQEIP TVAVVGYTNA GKSTLVSAVS ESFLYCDDRL FATVDPKLRS VVLPSGRKVL LSDTVGFISE LPIQLVEAFH ATLEEVVEAD LLVHVLDSSA PNLNEQREAV LQVLGQIGVS EQKLQNMIEV WNKIDLREDF VGDGYCNEDE VPSGLEENND VASNKLCEED LLEYDDNEDE DFEQSGKLGE VIDDQQGNYT DELVSGDEQE SWVDYNGSLV GCGSAEVQQN DPSNKWEVVG SENQFGSESA PHVKTSALTG VGLQELLELL DEKLKPQKTI EKDIFDRKWR PPRTEDARIA VEQ // ID K4BVF6_SOLLC Unreviewed; 547 AA. AC K4BVF6; DT 28-NOV-2012, integrated into UniProtKB/TrEMBL. DT 28-NOV-2012, sequence version 1. DT 30-AUG-2017, entry version 37. DE SubName: Full=Uncharacterized protein {ECO:0000313|EnsemblPlants:Solyc04g080770.2.1}; OS Solanum lycopersicum (Tomato) (Lycopersicon esculentum). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae; OC Pentapetalae; asterids; lamiids; Solanales; Solanaceae; Solanoideae; OC Solaneae; Solanum; Lycopersicon. OX NCBI_TaxID=4081 {ECO:0000313|EnsemblPlants:Solyc04g080770.2.1, ECO:0000313|Proteomes:UP000004994}; RN [1] {ECO:0000313|EnsemblPlants:Solyc04g080770.2.1} RP IDENTIFICATION. RC STRAIN=cv. Heinz 1706 {ECO:0000313|EnsemblPlants:Solyc04g080770.2.1}; RG EnsemblPlants; RL Submitted (JUN-2015) to UniProtKB. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR RefSeq; XP_004238264.1; XM_004238216.3. DR UniGene; Les.5265; -. DR STRING; 4081.Solyc04g080770.2.1; -. DR PaxDb; K4BVF6; -. DR EnsemblPlants; Solyc04g080770.2.1; Solyc04g080770.2.1; Solyc04g080770.2. DR GeneID; 101261514; -. DR Gramene; Solyc04g080770.2.1; Solyc04g080770.2.1; Solyc04g080770.2. DR KEGG; sly:101261514; -. DR eggNOG; KOG0410; Eukaryota. DR eggNOG; COG2262; LUCA. DR InParanoid; K4BVF6; -. DR KO; K03665; -. DR OMA; VILEIFH; -. DR OrthoDB; EOG093609UJ; -. DR Proteomes; UP000004994; Chromosome 4. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR GO; GO:0043022; F:ribosome binding; IBA:GO_Central. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000004994}; KW Reference proteome {ECO:0000313|Proteomes:UP000004994}. FT DOMAIN 324 490 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 547 AA; 61321 MW; 56739ED0BE31684C CRC64; MSLCFCSNLK PSILFPESKF RWIQTRTRPV SFTKLIQTKY SYRGCIKAVG EEIGVLSPDD SLSERNPVIE EEPVPETEVN EVENGVASVV AEGKAQTWIS KSENKEKLDE EDENASRFKL RNGKEVFEEK AYLVGVACKG DTEDSFGIEE SLKELAQLAD TAGLLVVDST YQKLSSPNPR TYIGSGKVSE IKSAIRAFDV ETVIFDDELS PGQLRNLEKA FGGDVRVCDR TALILDIFNQ RAATREASLQ VSLAQMEYQL PRLTRMWTHL ERQAGGQVKG MGEKQIEVDK RILRTQIGVL KKELESVRKH RKQYRNRRVS VPVPVVSLVG YTNAGKSTLL NQLTGADVLA EDQLFATLDP TTRRVQMKNG KEFLLTDTVG FIQKLPTTLV AAFRATLEEI AESSILVHVV DISHPLAEQQ IEAVEKVLSE LDTSSIPKLM LWNKVDKAED PEKIKLEAKM RNDVVCVSAL TGEGLDEFCN EIQNRLKDAM VWVEALIPFD KGELLSTIHQ VGMVERTEYS EKGTLVRAHV PLRFARLLTP MRQMCVS // ID K4IKK4_BIFAP Unreviewed; 507 AA. AC K4IKK4; DT 09-JAN-2013, integrated into UniProtKB/TrEMBL. DT 09-JAN-2013, sequence version 1. DT 07-JUN-2017, entry version 35. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=BAST_0522 {ECO:0000313|EMBL:AFU71112.1}; OS Bifidobacterium asteroides (strain PRL2011). OC Bacteria; Actinobacteria; Bifidobacteriales; Bifidobacteriaceae; OC Bifidobacterium. OX NCBI_TaxID=1147128 {ECO:0000313|EMBL:AFU71112.1, ECO:0000313|Proteomes:UP000007006}; RN [1] {ECO:0000313|EMBL:AFU71112.1, ECO:0000313|Proteomes:UP000007006} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=PRL2011 {ECO:0000313|EMBL:AFU71112.1, RC ECO:0000313|Proteomes:UP000007006}; RX PubMed=23028506; DOI=10.1371/journal.pone.0044229; RA Bottacini F., Milani C., Turroni F., Sanchez B., Foroni E., RA Duranti S., Serafini F., Viappiani A., Strati F., Ferrarini A., RA Delledonne M., Henrissat B., Coutinho P., Fitzgerald G.F., RA Margolles A., van Sinderen D., Ventura M.; RT "Bifidobacterium asteroides PRL2011 genome analysis reveals clues for RT colonization of the insect gut."; RL PLoS ONE 7:E44229-E44229(2012). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP003325; AFU71112.1; -; Genomic_DNA. DR EnsemblBacteria; AFU71112; AFU71112; BAST_0522. DR KEGG; bast:BAST_0522; -. DR PATRIC; fig|1147128.3.peg.538; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000007006; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000007006}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000007006}. FT DOMAIN 275 441 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 507 AA; 55387 MW; 4887221168CF1D85 CRC64; MTQEQPTQEH GSAVDDAHQD PLSHKSEVLT GSQGRAGQDQ EWEERSRRNA FRHVEGLGEL QDVTEVEYRK VRLERVVLVG VWSGSRTTVG QAEESLRELA ALARTAGAEV LDGLLQQRVK PDPATYLGSG KARELADIVA RLGADTIITD DDLHPSQRRA LEDVTKVKVV DRTALILDIF AQHATSREGK AQVELAQLEY MLPRLRGWGG SLSRQAGGQA AGQAGGIGSR GPGETKIETD RRVIRRRISR LKRQIAQMAP SRQVKRGSRR RYQLPAVAVV GYTNAGKSSL TNRLTGSEEL VENALFATLD TAVRRTKAAD GRLYVYVDTV GFVRRLPTQL VEAFKSTLEE VGQSDLILHV VDGSHPDPFG QIRAVDAVLA DIPGAESIPR LLVFNKVDLI DKDARQRLAN LEPEAFLVSA KEGQGLESLR KRVEELLPAP AVHVQAILSY TSGSLLEQVR QMGRVESLEY RADGVALSAD VDDRLAAAVL DQAIDQKPLQ ASAGDTP // ID K4ISF4_PSYTT Unreviewed; 410 AA. AC K4ISF4; DT 09-JAN-2013, integrated into UniProtKB/TrEMBL. DT 09-JAN-2013, sequence version 1. DT 07-JUN-2017, entry version 36. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=P700755_001530 {ECO:0000313|EMBL:AFU68415.1}; OS Psychroflexus torquis (strain ATCC 700755 / ACAM 623). OC Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales; OC Flavobacteriaceae; Psychroflexus. OX NCBI_TaxID=313595 {ECO:0000313|EMBL:AFU68415.1, ECO:0000313|Proteomes:UP000008514}; RN [1] {ECO:0000313|EMBL:AFU68415.1, ECO:0000313|Proteomes:UP000008514} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Bowman J., Ferriera S., Johnson J., Kravitz S., Halpern A., RA Remington K., Beeson K., Tran B., Rogers Y.-H., Friedman R., RA Venter J.C.; RL Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:AFU68415.1, ECO:0000313|Proteomes:UP000008514} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700755 / ACAM 623 {ECO:0000313|Proteomes:UP000008514}; RA Feng S., Powell S.M., Bowman J.P.; RT "The complete sequence of Psychroflexus torquis an extreme RT psychrophile from sea-ice that is stimulated by light."; RL Submitted (SEP-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP003879; AFU68415.1; -; Genomic_DNA. DR RefSeq; WP_015024014.1; NC_018721.1. DR ProteinModelPortal; K4ISF4; -. DR STRING; 313595.P700755_07757; -. DR EnsemblBacteria; AFU68415; AFU68415; P700755_001530. DR KEGG; ptq:P700755_001530; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000008514; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000008514}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000008514}. FT DOMAIN 200 385 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 410 AA; 47644 MW; 6AE556D88B06932E CRC64; MLDAQNINYE TTVLIGIVNQ FQNEEKSKEY LDELEFLTYT AGGEVLKRFQ QKLEVPNPKT FIGKGKLEQV RDYVEEHQVG TAIFDDELSP GQQRSIEKIL KCKVVDRTYL IMDIFAQRAK TSNASTQVEL AQYEYLLPRL AGLWTHLERQ QGGIGMRGPG ETEIETDRRI VRDKITLLKK KLKTIDKQMA VQRGNRGSLV RVALVGYTNV GKSTLMNVIS KSEVFAENKL FATLDTTVRK VVIRNLPFLL TDTVGFIRKL PTQLVESFKS TLDEVREADL LLHVVDISHE NFEDHIESVN SILDDINAKD KPCIMVFNKI DNYEPEVIEE DDLMVEKSYQ HYTLEEWKKT WMQREGDNVL FISATEKENI EEFRKKVYET ARKIHIKRFP YNNFLYPEYE AYTGDEEEEM // ID K4KQ26_SIMAS Unreviewed; 437 AA. AC K4KQ26; DT 09-JAN-2013, integrated into UniProtKB/TrEMBL. DT 09-JAN-2013, sequence version 1. DT 07-JUN-2017, entry version 37. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=M5M_15355 {ECO:0000313|EMBL:AFV00204.1}; OS Simiduia agarivorans (strain DSM 21679 / JCM 13881 / BCRC 17597 / OS SA1). OC Bacteria; Proteobacteria; Gammaproteobacteria; Cellvibrionales; OC Cellvibrionaceae; Simiduia. OX NCBI_TaxID=1117647 {ECO:0000313|EMBL:AFV00204.1, ECO:0000313|Proteomes:UP000000466}; RN [1] {ECO:0000313|EMBL:AFV00204.1, ECO:0000313|Proteomes:UP000000466} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 21679 / JCM 13881 / BCRC 17597 / SA1 RC {ECO:0000313|Proteomes:UP000000466}; RX PubMed=23405302; DOI=10.1128/genomeA.00039-12; RA Lin S.Y., Shieh W.Y., Chen J.S., Tang S.L.; RT "Complete genome sequence of Simiduia agarivorans SA1(T), a marine RT bacterium able to degrade a variety of polysaccharides."; RL Genome Announc. 1:E00039-E00039(2013). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP003746; AFV00204.1; -; Genomic_DNA. DR RefSeq; WP_015048356.1; NZ_ATUQ01000010.1. DR EnsemblBacteria; AFV00204; AFV00204; M5M_15355. DR KEGG; saga:M5M_15355; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000000466; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000000466}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000000466}. FT DOMAIN 199 366 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 437 AA; 49155 MW; F055C947BC2D8701 CRC64; MFFERPESGE LAILVHLEFQ LNIETNDPRE FEELALSAGA DPVAFLTGKR PSPDARTFMG SGKLEELRDL VTLHEAKLVI FNHALSPSQE RNLEAELKCR VLDRTGLILD IFAQRARTHE GKLQVELAQL RHMSTRLVRG WTHLERQKGG IGLRGPGETQ LETDRRLLRA RISFIESRLE DVRRSRQQAR RSRSRADIPT VSLVGYTNAG KSTLFNTITD AKVYAQDQLF ATLDPTMRRV ELPDVGAAVL ADTVGFISHL PHKLVEAFRA TLEEAASATL LLHVIDAPSE ERKRNMEEVQ LVLEEIDAHE LPQLKVYNKI DLLDDFGPRI DRDDQGQPVA VWLSAKTGAG VPLLLQAVAE LLGDEIVHQQ VQLPVRWARL RARLYERNAI LSESIADDGA YDLDVRISKV DLLRLLSAEK IPLADSPWKG LDEPPAW // ID K4L8V8_9FIRM Unreviewed; 601 AA. AC K4L8V8; DT 09-JAN-2013, integrated into UniProtKB/TrEMBL. DT 09-JAN-2013, sequence version 1. DT 07-JUN-2017, entry version 34. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=DCF50_p2921 {ECO:0000313|EMBL:AFV06924.1}; OS Dehalobacter sp. CF. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Peptococcaceae; OC Dehalobacter. OX NCBI_TaxID=1131462 {ECO:0000313|EMBL:AFV06924.1, ECO:0000313|Proteomes:UP000000482}; RN [1] {ECO:0000313|EMBL:AFV06924.1, ECO:0000313|Proteomes:UP000000482} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CF {ECO:0000313|EMBL:AFV06924.1}; RX PubMed=23284863; DOI=10.1371/journal.pone.0052038; RA Tang S., Gong Y., Edwards E.A.; RT "Semi-automatic in silico gap closure enabled de novo assembly of two RT dehalobacter genomes from metagenomic data."; RL PLoS ONE 7:E52038-E52038(2012). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP003870; AFV06924.1; -; Genomic_DNA. DR RefSeq; WP_015044953.1; NC_018867.1. DR EnsemblBacteria; AFV06924; AFV06924; DCF50_p2921. DR KEGG; dec:DCF50_p2921; -. DR PATRIC; fig|1131462.4.peg.2952; -. DR KO; K03665; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000000482; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000000482}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000000482}. FT DOMAIN 380 545 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 601 AA; 66853 MW; 9A91EF77A115C99E CRC64; MLQVNGEIES IKNSILEKLN SFYTYQIPRD HLWTQELIEQ LAEISSQVNK EIAVYADRKG RITDVSIGNH STVKLAEVEQ KRSLQRLSGT RCIHTHPKSS GLLSSMDISS LKQLNLDAMI AIGIRNNRAE DLYVGILSPT TIEEVNIFGP LSADIDDFAL LFQNIEDADN ILRKLPAEKA KTSERAILVG LQTRYSRDLY GISEAEVSFA ELEELAKTAG ALIVGHLMQK KEARDSSTII GPGKLEELQQ MIQTRQADLV IFDEELNGTQ QRILEEKLGL KVLSRTGLIL DIFAQHARSR EGILQVELAQ LEYRLPRLTG TGVALSRLGG GIGTRGPGET KLETDRRHIR SRIAHLRERL DDIRRQRGVL RGNRQKNNIP VLSIVGYTNA GKSTLLNALC GSDVLAEDKL FATLDPTTRK LPLNNGSTVL LSDTVGFIRR LPPNLLDAFK STLEEVVLSD QILIVADAAD PQVEDHIWIV DEILAELGAG SKPTLIVLNK VDRLHPDNRI SLWRETRPVV EISALQRSGL EELKQAIEKE LFSDHIRVSL EIPVSDGAAL AWLYANTKVL EVVYDEQVTH VEAELAASLL STVERYRVSA P // ID K4MAM6_9EURY Unreviewed; 419 AA. AC K4MAM6; DT 09-JAN-2013, integrated into UniProtKB/TrEMBL. DT 09-JAN-2013, sequence version 1. DT 07-JUN-2017, entry version 31. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=Mpsy_0951 {ECO:0000313|EMBL:AFV23160.1}; OS Methanolobus psychrophilus R15. OC Archaea; Euryarchaeota; Methanomicrobia; Methanosarcinales; OC Methanosarcinaceae; Methanolobus. OX NCBI_TaxID=1094980 {ECO:0000313|EMBL:AFV23160.1, ECO:0000313|Proteomes:UP000000459}; RN [1] {ECO:0000313|EMBL:AFV23160.1, ECO:0000313|Proteomes:UP000000459} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=R15 {ECO:0000313|EMBL:AFV23160.1, RC ECO:0000313|Proteomes:UP000000459}; RA Chen Z., Yu H., Li L., Hu S., Dong X.; RT "The genome and transcriptome of a newly described psychrophilic RT archaeon, Methanolobus psychrophilus R15, reveal its cold adaptive RT characteristics."; RL Environ. Microbiol. Rep. 4:633-641(2012). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP003083; AFV23160.1; -; Genomic_DNA. DR RefSeq; WP_015052883.1; NC_018876.1. DR EnsemblBacteria; AFV23160; AFV23160; Mpsy_0951. DR GeneID; 13844566; -. DR KEGG; mpy:Mpsy_0951; -. DR PATRIC; fig|1094980.5.peg.887; -. DR KO; K03665; -. DR OrthoDB; POG093Z07D6; -. DR Proteomes; UP000000459; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000000459}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000000459}. FT DOMAIN 191 360 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 157 184 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 419 AA; 47914 MW; B9ACA3D1C76D8AC7 CRC64; MKRAILVKRN DPRSDEHKNE LQMLELKELA HSAGYTVVAE MIQTRHPDSR YQVGRGKVEE LAQVVQGLNA DKIIFHNPLS TMQIYNISET CRREVIDKFQ LILEIFATRA TTPRSKLQVE LARLEYELPR ARTIISILKK EERPGFMGLG GYENSYAQDV KNRINRIRNE LESMERDRDS LRSLRHSKGF SLVALAGYTN AGKSTLFNSL VKEDVQVKDM MFTTLVPTTR SLDVEGRNVL LTDTVGFIED LPHWMVDAFR STLNEIFLAD VVLLVVDSSE PVETIRRKLL ASHETMWEQL QEVEIVTAFN KADMLTKEEL SDRMLALEYL TPNPVAISAK KGFCLDILKA ELRNHLPKWE RIHISLPLSE EGMSMVSWLF QEGVVHNISY GDSIDIDLEA RDAVINKARS FAKEHASFP // ID K4QTU9_9ACTN Unreviewed; 497 AA. AC K4QTU9; DT 09-JAN-2013, integrated into UniProtKB/TrEMBL. DT 09-JAN-2013, sequence version 1. DT 07-JUN-2017, entry version 36. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=BN159_2652 {ECO:0000313|EMBL:CCK27031.1}; OS Streptomyces davawensis JCM 4913. OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae; OC Streptomyces. OX NCBI_TaxID=1214101 {ECO:0000313|EMBL:CCK27031.1, ECO:0000313|Proteomes:UP000008043}; RN [1] {ECO:0000313|EMBL:CCK27031.1, ECO:0000313|Proteomes:UP000008043} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=JCM 4913 {ECO:0000313|EMBL:CCK27031.1, RC ECO:0000313|Proteomes:UP000008043}; RX PubMed=23043000; DOI=10.1128/JB.01592-12; RA Jankowitsch F., Schwarz J., Ruckert C., Gust B., Szczepanowski R., RA Blom J., Pelzer S., Kalinowski J., Mack M.; RT "Genome Sequence of the Bacterium Streptomyces davawensis JCM 4913 and RT Heterologous Production of the Unique Antibiotic Roseoflavin."; RL J. Bacteriol. 194:6818-6827(2012). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; HE971709; CCK27031.1; -; Genomic_DNA. DR RefSeq; WP_015657423.1; NC_020504.1. DR EnsemblBacteria; CCK27031; CCK27031; BN159_2652. DR GeneID; 31224685; -. DR KEGG; sdv:BN159_2652; -. DR PATRIC; fig|1214101.3.peg.2693; -. DR KO; K03665; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000008043; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 2. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000008043}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000008043}. FT DOMAIN 275 440 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 497 AA; 54303 MW; 8C8E3162ABBF4682 CRC64; MTSSSSPSQD SQRLAHNYAE GLRADALMEE DVAWSHDIDG ERDGEQFDRS ERAALRRVAG LSTELEDVTE VEYRQLRLER VVLVGVWTTG TVQDAENSLA ELAALAETAG ALVLDGVIQR RDKPDAATYI GSGKANELRD IVLESGADTV ICDGELSPGQ LIHLEDVVKV KVIDRTALIL DIFAQHAKSR EGKAQVALAQ MQYMLPRLRG WGQSLSRQMG GGKGGGLATR GPGETKIETD RRRIREKMAK MRREIAEMKT GREIKRQERK RNKVPSVAIA GYTNAGKSSL LNRLTGAGVL VENALFATLD PTVRRAETPS GRLYTLADTV GFVRHLPHHL VEAFRSTMEE VGESDLILHV VDGSHPDPEE QLAAVREVIT DVGATRVPEI VVINKADAAD PLTLQRLLRI EKRSIAVSAR TGQGIAELLA LIDNELPRPS VEIEALVPYT LGKLVARAHD EGEVISEEHT PEGTLLKVRV HEELAAELAP YVPTPAV // ID K4ZJM0_PAEAL Unreviewed; 428 AA. AC K4ZJM0; DT 09-JAN-2013, integrated into UniProtKB/TrEMBL. DT 09-JAN-2013, sequence version 1. DT 07-JUN-2017, entry version 29. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:EJW15655.1}; GN ORFNames=PAV_7c00280 {ECO:0000313|EMBL:EJW15655.1}; OS Paenibacillus alvei DSM 29. OC Bacteria; Firmicutes; Bacilli; Bacillales; Paenibacillaceae; OC Paenibacillus. OX NCBI_TaxID=1206781 {ECO:0000313|EMBL:EJW15655.1, ECO:0000313|Proteomes:UP000006321}; RN [1] {ECO:0000313|EMBL:EJW15655.1, ECO:0000313|Proteomes:UP000006321} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 29 {ECO:0000313|EMBL:EJW15655.1, RC ECO:0000313|Proteomes:UP000006321}; RX PubMed=23105091; DOI=10.1128/JB.01698-12; RA Djukic M., Becker D., Poehlein A., Voget S., Daniel R.; RT "Genome Sequence of Paenibacillus alvei DSM 29, a Secondary Invader RT during European Foulbrood Outbreaks."; RL J. Bacteriol. 194:6365-6365(2012). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EJW15655.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AMBZ01000007; EJW15655.1; -; Genomic_DNA. DR RefSeq; WP_005549858.1; NZ_AMBZ01000007.1. DR EnsemblBacteria; EJW15655; EJW15655; PAV_7c00280. DR PATRIC; fig|1206781.3.peg.4709; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000006321; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000006321}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000006321}. FT DOMAIN 208 372 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 428 AA; 48509 MW; 303CFEE858243234 CRC64; MRKEPHHTNQ NIPDRAVLVT LITDDVKRSG VDPQYSLDEL VQLAETAGVE VLTTMTQQRE FRDPRWFIGK GKVQELRGVI DELGATTAIF DQELSGAQVR NLEEALDVKI VDRTQLILDI FAQRAKTREG IIQVELAQLS YLLPRLSGHG KNLSRQGGGI GTRGPGESQL ETDRRHIRGR ISDLKRQLHE VVRSRNLHRE RRKKTGAYQV ALVGYTNAGK STLLRQLTQA DVYVENQLFA TLDPTSRQWE LPSGKEVVLT DTVGFIQNLP HDLVAAFRAT LEEVNEADLI LHVMDASSPM REDHMRVVED ILQQLGAGAK PQIVLYNKKD LCTPEQRQML PHDKSHFIIS AYDEGDLERI RQVVQDQLAG QTITYRIAAD RGDLIALIYR MGEVLQQEID ENDLLLKVRL DRLAAEQHGY KLIDYVVK // ID K4ZLN3_PAEAL Unreviewed; 424 AA. AC K4ZLN3; DT 09-JAN-2013, integrated into UniProtKB/TrEMBL. DT 09-JAN-2013, sequence version 1. DT 07-JUN-2017, entry version 32. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:EJW16680.1}; GN ORFNames=PAV_5c02630 {ECO:0000313|EMBL:EJW16680.1}; OS Paenibacillus alvei DSM 29. OC Bacteria; Firmicutes; Bacilli; Bacillales; Paenibacillaceae; OC Paenibacillus. OX NCBI_TaxID=1206781 {ECO:0000313|EMBL:EJW16680.1, ECO:0000313|Proteomes:UP000006321}; RN [1] {ECO:0000313|EMBL:EJW16680.1, ECO:0000313|Proteomes:UP000006321} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 29 {ECO:0000313|EMBL:EJW16680.1, RC ECO:0000313|Proteomes:UP000006321}; RX PubMed=23105091; DOI=10.1128/JB.01698-12; RA Djukic M., Becker D., Poehlein A., Voget S., Daniel R.; RT "Genome Sequence of Paenibacillus alvei DSM 29, a Secondary Invader RT during European Foulbrood Outbreaks."; RL J. Bacteriol. 194:6365-6365(2012). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EJW16680.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AMBZ01000005; EJW16680.1; -; Genomic_DNA. DR RefSeq; WP_005548768.1; NZ_AMBZ01000005.1. DR EnsemblBacteria; EJW16680; EJW16680; PAV_5c02630. DR PATRIC; fig|1206781.3.peg.3918; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000006321; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000006321}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000006321}. FT DOMAIN 201 369 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 424 AA; 48277 MW; 10088C78E1145110 CRC64; MEQLTIELQK AVLVGVNMNH QPDFDYSMEE LANLAGACDI QIVGRVTQNL SRLHTSHYIG TGKLQEITMM LNQHEANLVI FNDELSPSQL RNLEADLDCK VVDRTLLILD IFGQRAKTRE AQLQVEVAEL QYMLPRLVGL RESLGRQSGG VGTKNRGTGE TKLELDRRRI EERITAMSRE LEALVAHRQI QRKKRKKTEI PVVSLVGYTN AGKSTVMNAL VEKFTGSQEK FVFEKDMLFA TLETSVRNIE LEDNKEFLLT DTVGFVSKLP HHLVKAFRST LEEVREADLL VHVVDFSNSE YEQHIHITNE TLKAIGVEDI PMIYAYNKID LKEGEIPESQ DNSLYISAKG KQGLDELIAA IRGQVFRNYV KCEMLIPYHE GQHVSYLNEH AHVLATEYEE QGTKLVLECK QSDYQKFAQY VQPS // ID K5BBJ7_MYCHD Unreviewed; 472 AA. AC K5BBJ7; DT 09-JAN-2013, integrated into UniProtKB/TrEMBL. DT 09-JAN-2013, sequence version 1. DT 07-JUN-2017, entry version 32. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:EKF24110.1}; GN ORFNames=C731_1870 {ECO:0000313|EMBL:EKF24110.1}; OS Mycobacterium hassiacum (strain DSM 44199 / CIP 105218 / JCM 12690 / OS 3849). OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae; OC Mycobacterium. OX NCBI_TaxID=1122247 {ECO:0000313|EMBL:EKF24110.1, ECO:0000313|Proteomes:UP000006265}; RN [1] {ECO:0000313|EMBL:EKF24110.1, ECO:0000313|Proteomes:UP000006265} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 44199 / CIP 105218 / JCM 12690 / 3849 RC {ECO:0000313|Proteomes:UP000006265}; RX PubMed=23209251; DOI=10.1128/JB.01880-12; RA Tiago I., Maranha A., Mendes V., Alarico S., Moynihan P.J., RA Clarke A.J., Macedo-Ribeiro S., Pereira P.J., Empadinhas N.; RT "Genome sequence of Mycobacterium hassiacum DSM 44199, a rare source RT of heat-stable mycobacterial proteins."; RL J. Bacteriol. 194:7010-7011(2012). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EKF24110.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AMRA01000046; EKF24110.1; -; Genomic_DNA. DR RefSeq; WP_005626836.1; NZ_KB903929.1. DR EnsemblBacteria; EKF24110; EKF24110; C731_1870. DR PATRIC; fig|1122247.3.peg.1800; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000006265; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000006265}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000006265}. FT DOMAIN 249 418 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 208 242 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 472 AA; 51260 MW; 9236996D0D69BC9C CRC64; MTYPEPGSEP TTPSTGELAL EDRSALRRVA GLSTELTDVS EVEYRRLRLE RVVLVGVWTE GSAADAEASL AELARLAETA GSQVLEGLIQ RRDRPDPATY IGSGKAEELR RIVEATGADT VICDGELSPA QLTALEKVVK VKVIDRTALI LDIFAQHASS KEGKAQVELA QLEYMLPRLR GWGESMSRQA GGRAGGSGGG VGLRGPGETK IETDRRRIRE RMAKLRREIK EMRKVRDTQR SRRRESDVAS IAIVGYTNAG KSSLLNALTG AGVLVEDALF ATLEPTTRRG QFGDGRPFVL TDTVGFVRHL PTQLVEAFRS TLEEVVDADL LVHVVDGSDA NPLAQISAVR AVIDEVIRDH RAKPAPELLV VNKIDAADEL TLTQLRRALP DAVFVSARTG EGLDRLQARM AELVPPSDTV VDVTIPYHRG DLVSKVHADG RVDLTEHTPD GTRIKARVPA PLAAALREYA TF // ID K5ZLF0_9PROT Unreviewed; 426 AA. AC K5ZLF0; DT 09-JAN-2013, integrated into UniProtKB/TrEMBL. DT 09-JAN-2013, sequence version 1. DT 07-JUN-2017, entry version 30. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=MXAZACID_06536 {ECO:0000313|EMBL:EKN00196.1}; OS Acidocella sp. MX-AZ02. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales; OC Acetobacteraceae; Acidocella. OX NCBI_TaxID=1214225 {ECO:0000313|EMBL:EKN00196.1, ECO:0000313|Proteomes:UP000006217}; RN [1] {ECO:0000313|EMBL:EKN00196.1, ECO:0000313|Proteomes:UP000006217} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MX-AZ02 {ECO:0000313|EMBL:EKN00196.1, RC ECO:0000313|Proteomes:UP000006217}; RX PubMed=23405365; RA Servin-Garciduenas L.E., Garrett R.A., Amils R., Martinez-Romero E.; RT "Genome Sequence of the Acidophilic Bacterium Acidocella sp. Strain RT MX-AZ02."; RL Genome Announc. 1:E00041-12(2013). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EKN00196.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AMPS01000081; EKN00196.1; -; Genomic_DNA. DR RefSeq; WP_008493406.1; NZ_JH976207.1. DR EnsemblBacteria; EKN00196; EKN00196; MXAZACID_06536. DR PATRIC; fig|1214225.3.peg.1266; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000006217; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000006217}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000006217}. FT DOMAIN 207 375 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 426 AA; 46198 MW; 2CEF10D1CFA33884 CRC64; MQETAPPPSR AAILLPWDRQ AAFAAGQIRS AEARLAEAVG LAASIGLVIV HEQIFQLRSL TPATLLGKGQ VELAATALRG AQVDVAVVDA ALTPVQQRNL EKAFGTKVID RTGLILDIFG ARARTREGSL QVELAHLEYQ RSRLVRSWTH LERQRGGFGF LGGPGETQIE ADRRLIGDRI VKLKAELEEV RRTRGLHRGA RKKVPYPVVA LVGYTNAGKS TLFNALTGAT VMAEDQLFAT LDPTMRGLVL PSGRNIILSD TVGFISELPT ELVAAFRATL EEVAEADLLL HVRDISHPDT EAQARDVRAV LTRMAKEGTL DEGWPSHTLE VLNKADALGG IANVVQGEGI AVSALTGEGL DRLLQTIDAR LAAAEQLVEL QVPVEDGARL AWLYRHGEVV AREDDEHHVT LQVRLSAVDK ARFEAL // ID K6CAA1_BACAZ Unreviewed; 420 AA. AC K6CAA1; DT 09-JAN-2013, integrated into UniProtKB/TrEMBL. DT 09-JAN-2013, sequence version 1. DT 07-JUN-2017, entry version 28. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=BAZO_05919 {ECO:0000313|EMBL:EKN68030.1}; OS Bacillus azotoformans LMG 9581. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus. OX NCBI_TaxID=1131731 {ECO:0000313|EMBL:EKN68030.1, ECO:0000313|Proteomes:UP000006315}; RN [1] {ECO:0000313|EMBL:EKN68030.1, ECO:0000313|Proteomes:UP000006315} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=LMG 9581 {ECO:0000313|EMBL:EKN68030.1, RC ECO:0000313|Proteomes:UP000006315}; RX PubMed=23087684; RA Heylen K., Keltjens J.; RT "Redundancy and modularity in membrane-associated dissimilatory RT nitrate reduction in Bacillus."; RL Front. Microbiol. 3:371-371(2012). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EKN68030.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AJLR01000042; EKN68030.1; -; Genomic_DNA. DR EnsemblBacteria; EKN68030; EKN68030; BAZO_05919. DR PATRIC; fig|1131731.3.peg.1231; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000006315; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000006315}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000006315}. FT DOMAIN 201 362 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 420 AA; 48021 MW; AD67F639E3EE7A1D CRC64; MIENQTQKER ALLVGCQLPN MDDERFLYSL DELASLTNTA KGEVMMSLSQ KRNKVHSATY IGKGKIEEIS ALEKELEIDL IIFNDELSPS QTRNLSEKFE ARVIDRTQLI LDIFASRAKS KEGKLQVELA QYEYLLPRLA GQGLALSRLG GGIGTRGPGE TKLEADRRHI RRRIDEIKGQ LQTIVEHRNR YRERRKKNQV FQISLVGYTN AGKSTIFNRL TEAGSFEENL LFATLDPMTR KFLLPCGLTT LLTDTVGFIE DLPTSLIAAF RSTLEEVKEA DLILHVVDCS NPDYFNHEKT VYRILEDLDV KDIPILTVYN KKDLVTTQFV PSTNDMVFIS AYDQADLNTL QEKIETKIIS QMEFYHLFIP GTEGRLLAQL KSETVLLEQL FNEQKELYEC KGYINPSLAL YQQTKDLHLQ // ID K6DQK8_9BACI Unreviewed; 419 AA. AC K6DQK8; DT 09-JAN-2013, integrated into UniProtKB/TrEMBL. DT 09-JAN-2013, sequence version 1. DT 07-JUN-2017, entry version 31. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=BABA_04229 {ECO:0000313|EMBL:EKN70619.1}; OS Bacillus bataviensis LMG 21833. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus. OX NCBI_TaxID=1117379 {ECO:0000313|EMBL:EKN70619.1, ECO:0000313|Proteomes:UP000006316}; RN [1] {ECO:0000313|EMBL:EKN70619.1, ECO:0000313|Proteomes:UP000006316} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=LMG 21833T {ECO:0000313|Proteomes:UP000006316}; RX PubMed=23087684; RA Heylen K., Keltjens J.; RT "Redundancy and modularity in membrane-associated dissimilatory RT nitrate reduction in Bacillus."; RL Front. Microbiol. 3:371-371(2012). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EKN70619.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AJLS01000036; EKN70619.1; -; Genomic_DNA. DR RefSeq; WP_007083881.1; NZ_AJLS01000036.1. DR EnsemblBacteria; EKN70619; EKN70619; BABA_04229. DR PATRIC; fig|1117379.3.peg.873; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000006316; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000006316}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000006316}. FT DOMAIN 200 362 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 419 AA; 47766 MW; F4285E2DE8EE5C66 CRC64; MEQKETKEKA ILVGCQTNNN DDLRFHYSME ELGSLTETAQ AEVLISVIQK RDRVHPATYI GKGKVEELNA LVDELDADIV IFNDELSPSQ KRNLSSQVNA RIIDRTQLIL DIFAQRARSK EGKLQVELAQ LQYILPRLAG QGIALSRLGA GIGTRGPGET KLESDRRHIR RRIDDIKTQL SVIVQHRDRY RERRKKNKTF QIAIVGYTNA GKSTLFNRLS EAESYEENQL FATLDPMTRK LILPSGFISL ITDTVGFIQD LPTSLIAAFR STLEEVKEAD LLLHVVDMSN PDYFQHEKTV KKLLDDLEVK DIPQLTVYNK KDLQHPDFVP TADTPTAFIS AFDEKDRHAL KEKMERVIIE LMTPFEVQVP STAGKLLSQL KNETILRELT FEEEGQCYRC KGFALKDHQI TGQLQKFNI // ID K6GGP6_9GAMM Unreviewed; 430 AA. AC K6GGP6; DT 09-JAN-2013, integrated into UniProtKB/TrEMBL. DT 09-JAN-2013, sequence version 1. DT 07-JUN-2017, entry version 32. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:EKO36190.1}; GN ORFNames=B273_0491 {ECO:0000313|EMBL:EKO36190.1}; OS SAR86 cluster bacterium SAR86E. OC Bacteria; Proteobacteria; Gammaproteobacteria; SAR86 cluster. OX NCBI_TaxID=1208365 {ECO:0000313|EMBL:EKO36190.1, ECO:0000313|Proteomes:UP000010310}; RN [1] {ECO:0000313|EMBL:EKO36190.1, ECO:0000313|Proteomes:UP000010310} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SAR86E {ECO:0000313|EMBL:EKO36190.1}; RA Dupont C.L., Rusch D.B., Lombardo M.-J., Novotny M., Yee-Greenbaum J., RA Laskin R.; RL Submitted (SEP-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EKO36190.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AMWX01000012; EKO36190.1; -; Genomic_DNA. DR EnsemblBacteria; EKO36190; EKO36190; B273_0491. DR PATRIC; fig|1208365.4.peg.1086; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000010310; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000010310}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000010310}. FT DOMAIN 203 369 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 162 189 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 430 AA; 48512 MW; 99AFA64C519BF916 CRC64; MEKTSQPKDQ RAIIVSIDLL RAHQDHLEQF NSNEFIELAK SSGLKVEHHF FSKQNFVAAS HFLSKGKADE LKYIVESENI KLVVLDCELS PSQERNLEKL LCARVLDRTG LILDIFAARA QSDIGKLQVE LAQLSFLSTR LVRGWSHLER QKGGIGLRGP GETQLETDRR LISNRIKQLK KKLDKQHNQK NLNRYSRKKG NNKLVALVGY TNAGKTSLFN LLTKGGLDAE DKLFATLDTT TRRSNFKFQT FETVLFSDTV GFISNLPTKL VESFKATLDD LASADLLIHV IDAADSNRDI KTKEVDLILD ELGVNSMPQI RALNKIDLIK NKEIWPTNNL HLEIKISSET GEGLEELKNK VSECLFGNLL HGWVQFSPVQ ASVRSKLFDS GCIIEEKLDS SGQHQSLVSI SQSMLEQFEE IDIFKNLKPI // ID K6SY33_9CLOT Unreviewed; 595 AA. AC K6SY33; DT 09-JAN-2013, integrated into UniProtKB/TrEMBL. DT 09-JAN-2013, sequence version 1. DT 07-JUN-2017, entry version 29. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=A370_05078 {ECO:0000313|EMBL:EKQ51208.1}; OS Clostridium sp. Maddingley MBC34-26. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=1196322 {ECO:0000313|EMBL:EKQ51208.1, ECO:0000313|Proteomes:UP000001325}; RN [1] {ECO:0000313|EMBL:EKQ51208.1, ECO:0000313|Proteomes:UP000001325} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Maddingley MBC34-26 {ECO:0000313|Proteomes:UP000001325}; RX PubMed=23405323; RA Rosewarne C.P., Greenfield P., Li D., Tran-Dinh N., Bradbury M.I., RA Midgley D.J., Hendry P.; RT "Draft Genome Sequence of Clostridium sp. Maddingley, Isolated from RT Coal-Seam Gas Formation Water."; RL Genome Announc. 1:E00081-12(2013). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EKQ51208.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ALXI01000164; EKQ51208.1; -; Genomic_DNA. DR PATRIC; fig|1196322.3.peg.4938; -. DR Proteomes; UP000001325; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000001325}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000001325}. FT DOMAIN 364 541 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 595 AA; 67056 MW; 7AB15969612A0A78 CRC64; MIYGNIEGIK KSIIDELESI YSIRTLKDEV CDIEILNIIS RISSFIEREV SVGINRKGNV TSVAIGDSTS VEVPIIDIEE KRLSGIRVIH THPNGYCNLS ALDLTALLKL KLDAIVSVAI LDGKIIDFSL GMLTLYNNKL ETDEKRNLSL EEITSIHILD RIRFIENLIK TNDVIEDTEE KAILVGSDTK ESLEELAELT EACNIPVLKT VFQSRSKVDA AYYIGRGKVL EIASMRQVER ANVIIFDDEL SGSQVRNLEA ALGAKVIDRT TLILEIFATR AKSKESKIQV ELAQLKYRLS RLQGLGTILS RTGGGIGTRG PGEKKLETDR RHIMETIYDL KDELKKIKKT RDVQREKRNK ENIPKVSLVG YTNAGKSTLR NVLCDIAAKK ENKIKEKVFE ANMLFATLDT TTRALTLSKK GIITLTDTVG FVRKLPHDLV EAFKSTLEEV IFSDLLCHVI DASSDTAAEQ YEAVNEVLNE LGVLEKETVL ILNKIDKATE EQMLKIKEII GNKDIIEISA KEKINLEELL GIIEEKLPYN YKKVEYLIPY EKGDIQSFLH RNARILEEEY KDNGTYMVAE VDDEVFNKTQ EYAQV // ID K6VB44_9APIC Unreviewed; 676 AA. AC K6VB44; DT 09-JAN-2013, integrated into UniProtKB/TrEMBL. DT 09-JAN-2013, sequence version 1. DT 07-JUN-2017, entry version 18. DE SubName: Full=GTP binding protein {ECO:0000313|EMBL:GAB66412.1}; GN ORFNames=PCYB_091980 {ECO:0000313|EMBL:GAB66412.1}; OS Plasmodium cynomolgi strain B. OC Eukaryota; Alveolata; Apicomplexa; Aconoidasida; Haemosporida; OC Plasmodiidae; Plasmodium; Plasmodium (Plasmodium). OX NCBI_TaxID=1120755 {ECO:0000313|EMBL:GAB66412.1, ECO:0000313|Proteomes:UP000006319}; RN [1] {ECO:0000313|EMBL:GAB66412.1, ECO:0000313|Proteomes:UP000006319} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=B {ECO:0000313|EMBL:GAB66412.1, RC ECO:0000313|Proteomes:UP000006319}; RX PubMed=22863735; DOI=10.1038/ng.2375; RA Tachibana S., Sullivan S.A., Kawai S., Nakamura S., Kim H.R., Goto N., RA Arisue N., Palacpac N.M.Q., Honma H., Yagi M., Tougan T., Katakai Y., RA Kaneko O., Mita T., Kita K., Yasutomi Y., Sutton P.L., Shakhbatyan R., RA Horii T., Yasunaga T., Barnwell J.W., Escalante A.A., Carlton J.M., RA Tanabe K.; RT "Plasmodium cynomolgi genome sequences provide insight into Plasmodium RT vivax and the monkey malaria clade."; RL Nat. Genet. 44:1051-1055(2012). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; DF157101; GAB66412.1; -; Genomic_DNA. DR RefSeq; XP_004222359.1; XM_004222311.1. DR EnsemblProtists; GAB66412; GAB66412; PCYB_091980. DR GeneID; 14692766; -. DR KEGG; pcy:PCYB_091980; -. DR EuPathDB; PlasmoDB:PCYB_091980; -. DR Proteomes; UP000006319; Chromosome 9. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR SUPFAM; SSF52540; SSF52540; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000006319}; KW Reference proteome {ECO:0000313|Proteomes:UP000006319}. FT DOMAIN 155 211 GTP-bdg_N. {ECO:0000259|Pfam:PF13167}. FT DOMAIN 461 501 G (guanine nucleotide-binding). FT {ECO:0000259|Pfam:PF01926}. SQ SEQUENCE 676 AA; 77241 MW; F9C1ED297CCC7B06 CRC64; MLRWSTTLRT FPRTQKRCFT NRSKKEIIVL HPILKKTKSG SKSFEEIIYD AQEALGLARS AGFKVANGIS MPLGGWTFFK NPSGSKEEGE GDDLANSYHE EDTFRGSLQS NEGTPCGGDA DEGERCLTYE DSGGDARIGA PSEEVPPQGD DLERKIAESI IIKTNRIDNK FYFGKGKLNE LSTYFLKHPT PYVFINTLLS PEQFRNLDML FNSLLRSRHD ELKLRRQKQR GEDCLSVRAS EFSAEDDGCA EDDGYAEDAR GEELAYVEMY NEWMERQAER EDQEDGSVSE GEEQATLGEA EEEGVVFRDD AEDKDVPLYV ELFDRYSIIL QILKSRAKSN LSKLQLELAR ANFIFNTYAE DNKSRMKYIK YIENNVLGKS NFDYEEKYSR QNTFDADRQM GKKKNYDHLG YTSSYIKSSE TYKEYEKRII QNLYAKLKKE LGKCKNNNAL QSSARKHKAL IAVVGYTNVG KTKLINYLTK SNLKARNLFF QTLDNAFKSV TLEAIKNADV LIHVIDVCHP YREQHKKCVI DTLHKIGIPS DFLKYNMIEV WNKVDKLADE ELLNLYKTKP KNVLPISAKV GTNCDVLIKI LQTMINRIKD VQVLTLQFST MEAQERLAYL LKNFKVVPNS ISYSNDGNTT FIKLVENPRN LSKYYERFGK DEKGPSGEDA HKGAAS // ID K6VPN3_9MICO Unreviewed; 526 AA. AC K6VPN3; DT 09-JAN-2013, integrated into UniProtKB/TrEMBL. DT 09-JAN-2013, sequence version 1. DT 07-JUN-2017, entry version 32. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:GAB77335.1}; GN ORFNames=AUCHE_05_02400 {ECO:0000313|EMBL:GAB77335.1}; OS Austwickia chelonae NBRC 105200. OC Bacteria; Actinobacteria; Micrococcales; Dermatophilaceae; Austwickia. OX NCBI_TaxID=1184607 {ECO:0000313|EMBL:GAB77335.1, ECO:0000313|Proteomes:UP000008495}; RN [1] {ECO:0000313|EMBL:GAB77335.1, ECO:0000313|Proteomes:UP000008495} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NBRC 105200 {ECO:0000313|EMBL:GAB77335.1, RC ECO:0000313|Proteomes:UP000008495}; RA Yoshida I., Hosoyama A., Tsuchikane K., Katsumata H., Ando Y., RA Ohji S., Hamada M., Tamura T., Yamazoe A., Yamazaki S., Fujita N.; RT "Whole genome shotgun sequence of Austwickia chelonae NBRC 105200."; RL Submitted (AUG-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:GAB77335.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BAGZ01000005; GAB77335.1; -; Genomic_DNA. DR RefSeq; WP_006502087.1; NZ_BAGZ01000005.1. DR EnsemblBacteria; GAB77335; GAB77335; AUCHE_05_02400. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000008495; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 2. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000008495}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000008495}. FT DOMAIN 266 470 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 526 AA; 57531 MW; 3D54795A01DA17C8 CRC64; MTRPEDIFST RASALADNDD WHRDDPDFVS YDGDQLEREE RAAMRRVGGL STELEDVTEV EYRELRLEKV VLAGVWSAGT VEDAENSLRE LAALAETAGS QVMAGVLQRR QRPDAATFLG SGKAEELRDV VVNEGADTVV CDAELSPSQR RALEDIVKVK VIDRTALILD IFAQHAKSRE GKAQVELAQL QYLLPRLRGW GESMSRQAGG QAAGGMGMGS RGPGETKIEL DRRRINSRMA KLRREIRHMK TTRDVKRGAR RENQVPAVVL AGYTNAGKSS LLNRLTGAGV LVENALFATL DPTVRKAVTP DGRPYTLSDT VGFVRSLPHQ LVEAFRSTLE EVAEADVLLH VVDGSHPDPF AQISAVREVL AEVMSSGAEG ARLGSTEETD ALAKDAWSSD PRDRAARKEG ADVRTGPREI VVVNKADLAD PEILQQLVRR ERDCLVVSAR TGECMDALIA RIATEIPRPH IDLTVLIPYD RGALVHRIHE EADVLSEEHT AEGTRLQVRV LPDLAGELSG FVSGGL // ID K6WKK5_9MICO Unreviewed; 495 AA. AC K6WKK5; DT 09-JAN-2013, integrated into UniProtKB/TrEMBL. DT 09-JAN-2013, sequence version 1. DT 07-JUN-2017, entry version 32. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:GAB94296.1}; GN ORFNames=KILIM_004_00870 {ECO:0000313|EMBL:GAB94296.1}; OS Kineosphaera limosa NBRC 100340. OC Bacteria; Actinobacteria; Micrococcales; Dermatophilaceae; OC Kineosphaera. OX NCBI_TaxID=1184609 {ECO:0000313|EMBL:GAB94296.1, ECO:0000313|Proteomes:UP000008366}; RN [1] {ECO:0000313|EMBL:GAB94296.1, ECO:0000313|Proteomes:UP000008366} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NBRC 100340 {ECO:0000313|EMBL:GAB94296.1, RC ECO:0000313|Proteomes:UP000008366}; RA Yoshida I., Isaki S., Hosoyama A., Tsuchikane K., Katsumata H., RA Ando Y., Ohji S., Hamada M., Tamura T., Yamazoe A., Yamazaki S., RA Fujita N.; RT "Whole genome shotgun sequence of Kineosphaera limosa NBRC 100340."; RL Submitted (AUG-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:GAB94296.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BAHD01000004; GAB94296.1; -; Genomic_DNA. DR RefSeq; WP_006590829.1; NZ_BAHD01000004.1. DR EnsemblBacteria; GAB94296; GAB94296; KILIM_004_00870. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000008366; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 2. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000008366}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000008366}. FT DOMAIN 272 437 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 495 AA; 54241 MW; BDC0E6E85716AFCA CRC64; MTNSHNPRQS SDILDFRASA LADDDNWHER DPDFVAFDGD QLEREERAAM RRVAGLSTEL EDVTEVEYRQ LRLERVVLAG VWCEGSVEDA ENSLRELAAL AETAGSTVLA GVLQRRLRPD PATYLGSGKA EELRDIVADE GADTVVCDSE LAPSQRRALE DVVKVKVIDR TALILDIFAQ HAKSREGKAQ VELAQLQYLL PRLRGWGESM SRQAGGRVAG GEGIGSRGPG ETKIELDRRR INTKIAKLRR EIRGMKKTRD TKRSARHANK VPAVAIAGYT NAGKSSLLNR LTGAGVLVEN ALFATLDPTV RRAQTQDGRD YTLADTVGFV RSLPTQLVEA FRSTLEEVAD SDLLLHVVDG SHPDPEGQIS AVRAVLADVE ATDVPEIIVV NKADAADPEV LDRLRRHEKG AVIVSARTGA GLDELRDIID AALPKPHIPM TLLVPYDRGD IVNRLHTDAE VLAEEHTPDG TRLEVKVSED QVEPLREFEL ADVTG // ID K6WP81_9ACTN Unreviewed; 497 AA. AC K6WP81; DT 09-JAN-2013, integrated into UniProtKB/TrEMBL. DT 09-JAN-2013, sequence version 1. DT 07-JUN-2017, entry version 31. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:GAB88314.1}; GN ORFNames=GORHZ_013_00170 {ECO:0000313|EMBL:GAB88314.1}; OS Gordonia rhizosphera NBRC 16068. OC Bacteria; Actinobacteria; Corynebacteriales; Gordoniaceae; Gordonia. OX NCBI_TaxID=1108045 {ECO:0000313|EMBL:GAB88314.1, ECO:0000313|Proteomes:UP000008363}; RN [1] {ECO:0000313|EMBL:GAB88314.1, ECO:0000313|Proteomes:UP000008363} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NBRC 16068 {ECO:0000313|EMBL:GAB88314.1, RC ECO:0000313|Proteomes:UP000008363}; RA Takarada H., Isaki S., Hosoyama A., Tsuchikane K., Katsumata H., RA Baba S., Ohji S., Yamazaki S., Fujita N.; RT "Whole genome shotgun sequence of Gordonia rhizosphera NBRC 16068."; RL Submitted (AUG-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:GAB88314.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BAHC01000013; GAB88314.1; -; Genomic_DNA. DR RefSeq; WP_006329535.1; NZ_BAHC01000013.1. DR EnsemblBacteria; GAB88314; GAB88314; GORHZ_013_00170. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000008363; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000008363}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000008363}. FT DOMAIN 274 443 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 233 267 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 497 AA; 53781 MW; D56D7BCB43170259 CRC64; MTESAATPFP LSAPDDDDFE SIDSGPDNVR DILHDLTDPT TGELQLSERA SLQRVAGLST ELADITEVEY RQLRLERVVL VGVWTEGSAA QARANMAELA ALAETAGSQV LDALIQRRSR PDSATYIGSG KADELREAVL ATGADTVICD GELTPAQLTA LEKIVKVKVI DRTALILDIF AQHATSREGK AQVSLAQMEY MLPRLRGWGE SMSRQAGGRA GSNGGVGLRG PGETKIETDR RRIRERMAKL RREIREMKKS RTVMRAARER TGIPRLTVVG YTNAGKSSLV NAMTGAGVLV QNALFATLDP TTRRATLDDG RAVVFTDTVG FVRHLPTQLV EAFRSTLEEV VDADLLLHVV DGSDPFPAEQ ISAVRQVIGE VVAEEGAQPP PELLVINKID AIDATRMTEL RGAFGDAAYV SARTGEGLPE LFERIREFIG RSDIEMTIDV PYTRGDLVSR LHEEGEVLSA EHTADGTTMR VRVPAAFAGA LADLEVG // ID K6YAE8_9ALTE Unreviewed; 429 AA. AC K6YAE8; DT 09-JAN-2013, integrated into UniProtKB/TrEMBL. DT 09-JAN-2013, sequence version 1. DT 30-AUG-2017, entry version 31. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=GLIP_0996 {ECO:0000313|EMBL:GAC13638.1}; OS Aliiglaciecola lipolytica E3. OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales; OC Alteromonadaceae; Aliiglaciecola. OX NCBI_TaxID=1127673 {ECO:0000313|EMBL:GAC13638.1, ECO:0000313|Proteomes:UP000006334}; RN [1] {ECO:0000313|EMBL:GAC13638.1, ECO:0000313|Proteomes:UP000006334} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=E3 {ECO:0000313|EMBL:GAC13638.1, RC ECO:0000313|Proteomes:UP000006334}; RX PubMed=25009843; RA Qin Q.-L., Xie B.-B., Yu Y., Shu Y.-L., Rong J.-C., Zhang Y.-J., RA Zhao D.-L., Chen X.-L., Zhang X.-Y., Chen B., Zhou B.-C., Zhang Y.-Z.; RT "Comparative genomics of the marine bacterial genus Glaciecola reveals RT the high degree of genomic diversity and genomic characteristic for RT cold adaptation."; RL Environ. Microbiol. 16:1642-1653(2014). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:GAC13638.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BAEN01000022; GAC13638.1; -; Genomic_DNA. DR RefSeq; WP_008843455.1; NZ_BAEN01000022.1. DR EnsemblBacteria; GAC13638; GAC13638; GLIP_0996. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000006334; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000006334}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000006334}. FT DOMAIN 198 365 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 164 191 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 429 AA; 48520 MW; B4F4E5EEEF525A3E CRC64; MFDRYEAGEQ AVLVHIDFSD DSSKEDLQEL QMLVSSAGVN AVEVITASRQ APHPKYFTGS GKAEEIANAV RTCNADVVIF NHPLSPSQER NLEALCKCRV LDRTGLILDI FAQRARTHEG KLQVELAQLR HISTRLIRGW THLERQKGGI GLRGPGETQL ETDRRLLRVR IKSILRRLEK VQKQREQGRR ARKRAEMPTI SLVGYTNAGK STLFNTITDA GVYAADQLFA TLDPTLRKIQ LQDVGQAILA DTVGFIRHLP HDLVAAFKAT LQETQEADLL LHVVDYSDEQ YMDNIDQVND VLEEIDASEI QQLMICNKID RMEGVEPRID RDEEGVPIRV WISAQQNQGI DLLFNALTEC LSQSIVQFTL RIPPKEGKLR GALFRMNCIS AESYAEDGDW LVDVRMPTSD WNRLEKRSEI DLSSLVVKH // ID K6YQR3_9ALTE Unreviewed; 429 AA. AC K6YQR3; DT 09-JAN-2013, integrated into UniProtKB/TrEMBL. DT 09-JAN-2013, sequence version 1. DT 30-AUG-2017, entry version 32. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=GARC_2011 {ECO:0000313|EMBL:GAC18978.1}; OS Paraglaciecola arctica BSs20135. OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales; OC Alteromonadaceae; Paraglaciecola. OX NCBI_TaxID=493475 {ECO:0000313|EMBL:GAC18978.1, ECO:0000313|Proteomes:UP000006327}; RN [1] {ECO:0000313|EMBL:GAC18978.1, ECO:0000313|Proteomes:UP000006327} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BSs20135 {ECO:0000313|EMBL:GAC18978.1, RC ECO:0000313|Proteomes:UP000006327}; RX PubMed=25009843; RA Qin Q.-L., Xie B.-B., Yu Y., Shu Y.-L., Rong J.-C., Zhang Y.-J., RA Zhao D.-L., Chen X.-L., Zhang X.-Y., Chen B., Zhou B.-C., Zhang Y.-Z.; RT "Comparative genomics of the marine bacterial genus Glaciecola reveals RT the high degree of genomic diversity and genomic characteristic for RT cold adaptation."; RL Environ. Microbiol. 16:1642-1653(2014). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:GAC18978.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BAEO01000027; GAC18978.1; -; Genomic_DNA. DR RefSeq; WP_007619329.1; NZ_BAEO01000027.1. DR EnsemblBacteria; GAC18978; GAC18978; GARC_2011. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000006327; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000006327}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000006327}. FT DOMAIN 198 365 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 164 191 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 429 AA; 48355 MW; 658B273BDB5F2AD8 CRC64; MFDRYEAGEQ AVLVHIDFAD ENSKEDLLEL QLLVSSAGVN AIDVVTGSRQ TPQARYFVGS GKAEEIANAV RALQADVVIF NHSLSPSQER NLEQLCQCRV LDRTGLILDI FSQRARTHEG KLQVELAQLR HISTRLIRGW THLDKQKGGI GLRGPGESQL ETDRRLLAAR VKAIQRRLDK VQKQREQGRR SRVRAEIPTV SLVGYTNAGK STLFNTMTDS AVYAADQLFA TLDPTLRKIQ LQDVGAAILA DTVGFIRHLP HDLIAAFKAT LQETQQANLL LHVVDYSDEQ FRENIGQVNE VLEEIKADEI QQLVVCNKID RMDGVNAKID RDESGMPIRV WISAQQGLGI DLLLNAITEC LSKNMVQHSL LIPPHKSNLR GVFFDMNCIA SEDYAENGDW QVDVRMEQRD WNRLIKRIDV DLESYIVEI // ID K7G329_PELSI Unreviewed; 403 AA. AC K7G329; DT 09-JAN-2013, integrated into UniProtKB/TrEMBL. DT 09-JAN-2013, sequence version 1. DT 30-AUG-2017, entry version 28. DE SubName: Full=GTP binding protein 6 (putative) {ECO:0000313|Ensembl:ENSPSIP00000014690}; GN Name=GTPBP6 {ECO:0000313|Ensembl:ENSPSIP00000014690}; OS Pelodiscus sinensis (Chinese softshell turtle) (Trionyx sinensis). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Archelosauria; Testudines; Cryptodira; Trionychia; Trionychidae; OC Pelodiscus. OX NCBI_TaxID=13735 {ECO:0000313|Ensembl:ENSPSIP00000014690, ECO:0000313|Proteomes:UP000007267}; RN [1] {ECO:0000313|Ensembl:ENSPSIP00000014690} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=17381049; DOI=10.1080/10425170600760091; RA Jung S.-O., Lee Y.-M., Kartavtsev Y., Park I.-S., Kim D.S., Lee J.-S.; RT "The complete mitochondrial genome of the Korean soft-shelled turtle RT Pelodiscus sinensis (Testudines, Trionychidae)."; RL DNA Seq. 17:471-483(2006). RN [2] {ECO:0000313|Proteomes:UP000007267} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Daiwa-1 {ECO:0000313|Proteomes:UP000007267}; RG Soft-shell Turtle Genome Consortium; RL Submitted (OCT-2011) to the EMBL/GenBank/DDBJ databases. RN [3] {ECO:0000313|Ensembl:ENSPSIP00000014690} RP IDENTIFICATION. RG Ensembl; RL Submitted (NOV-2012) to UniProtKB. CC -!- CAUTION: The sequence shown here is derived from an Ensembl CC automatic analysis pipeline and should be considered as CC preliminary data. {ECO:0000313|Ensembl:ENSPSIP00000014690}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGCU01170708; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR STRING; 13735.ENSPSIP00000014690; -. DR Ensembl; ENSPSIT00000014759; ENSPSIP00000014690; ENSPSIG00000013117. DR eggNOG; KOG0410; Eukaryota. DR eggNOG; COG2262; LUCA. DR GeneTree; ENSGT00390000001397; -. DR OMA; MDTVGFM; -. DR OrthoDB; EOG091G0852; -. DR TreeFam; TF315022; -. DR Proteomes; UP000007267; Unassembled WGS sequence. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR CDD; cd01878; HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000007267}; KW Reference proteome {ECO:0000313|Proteomes:UP000007267}. FT DOMAIN 182 346 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 403 AA; 45421 MW; 65AA8E1BF1B82201 CRC64; TKAELQIAEA VALVNTLQNW TVLDKIILST KTPDKKFIFG KGNFQILTEK IKELPHITAV FLNIERLSPL TKKELEDAWG VTVFDRYTVV LHIFRCNART KEAKLQIALA EIPLLRANLK NEMSQLDQQR GGSRYIMGSG ETFMEMQYRL LKEKEFKIRN ALEKLRGKRS VLRTQRRRRE FPVISVMGYT NCGKTTLIKA LTGDEGLQPR DQLFATLDIT AHGGYLPSHL AVIYVDTIGF LSELPHDLVE SFSATLEDVA YSDLIVHVRD ISHPETVLQK ASVLSVLKKL NLPSHLLDSV VEVHNKVDLI ESYQSPEPNA IAVSALLGYG LEELKEEIER TVLKTTGKKI LTIKIKLAGP QLSWLYKEAT VQEVDVMPED GMANVKVIIS NSALGKYKKL FPQ // ID K7J1U3_NASVI Unreviewed; 472 AA. AC K7J1U3; DT 09-JAN-2013, integrated into UniProtKB/TrEMBL. DT 09-JAN-2013, sequence version 1. DT 07-JUN-2017, entry version 24. DE SubName: Full=Uncharacterized protein {ECO:0000313|EnsemblMetazoa:NV15323-PA}; GN Name=LOC100121260 {ECO:0000313|EnsemblMetazoa:NV15323-PA}; OS Nasonia vitripennis (Parasitic wasp). OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; OC Pterygota; Neoptera; Holometabola; Hymenoptera; Apocrita; Terebrantes; OC Chalcidoidea; Pteromalidae; Pteromalinae; Nasonia. OX NCBI_TaxID=7425 {ECO:0000313|EnsemblMetazoa:NV15323-PA, ECO:0000313|Proteomes:UP000002358}; RN [1] {ECO:0000313|EnsemblMetazoa:NV15323-PA} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=AsymCX {ECO:0000313|EnsemblMetazoa:NV15323-PA}; RX PubMed=20075255; DOI=10.1126/science.1178028; RG Nasonia Genome Working Group; RA Werren J.H., Richards S., Desjardins C.A., Niehuis O., Gadau J., RA Colbourne J.K., Werren J.H., Richards S., Desjardins C.A., Niehuis O., RA Gadau J., Colbourne J.K., Beukeboom L.W., Desplan C., Elsik C.G., RA Grimmelikhuijzen C.J., Kitts P., Lynch J.A., Murphy T., Oliveira D.C., RA Smith C.D., van de Zande L., Worley K.C., Zdobnov E.M., Aerts M., RA Albert S., Anaya V.H., Anzola J.M., Barchuk A.R., Behura S.K., RA Bera A.N., Berenbaum M.R., Bertossa R.C., Bitondi M.M., RA Bordenstein S.R., Bork P., Bornberg-Bauer E., Brunain M., RA Cazzamali G., Chaboub L., Chacko J., Chavez D., Childers C.P., RA Choi J.H., Clark M.E., Claudianos C., Clinton R.A., Cree A.G., RA Cristino A.S., Dang P.M., Darby A.C., de Graaf D.C., Devreese B., RA Dinh H.H., Edwards R., Elango N., Elhaik E., Ermolaeva O., Evans J.D., RA Foret S., Fowler G.R., Gerlach D., Gibson J.D., Gilbert D.G., RA Graur D., Grunder S., Hagen D.E., Han Y., Hauser F., Hultmark D., RA Hunter H.C. IV, Hurst G.D., Jhangian S.N., Jiang H., Johnson R.M., RA Jones A.K., Junier T., Kadowaki T., Kamping A., Kapustin Y., RA Kechavarzi B., Kim J., Kim J., Kiryutin B., Koevoets T., Kovar C.L., RA Kriventseva E.V., Kucharski R., Lee H., Lee S.L., Lees K., Lewis L.R., RA Loehlin D.W., Logsdon J.M. Jr., Lopez J.A., Lozado R.J., Maglott D., RA Maleszka R., Mayampurath A., Mazur D.J., McClure M.A., Moore A.D., RA Morgan M.B., Muller J., Munoz-Torres M.C., Muzny D.M., Nazareth L.V., RA Neupert S., Nguyen N.B., Nunes F.M., Oakeshott J.G., Okwuonu G.O., RA Pannebakker B.A., Pejaver V.R., Peng Z., Pratt S.C., Predel R., RA Pu L.L., Ranson H., Raychoudhury R., Rechtsteiner A., Reese J.T., RA Reid J.G., Riddle M., Robertson H.M., Romero-Severson J., RA Rosenberg M., Sackton T.B., Sattelle D.B., Schluns H., Schmitt T., RA Schneider M., Schuler A., Schurko A.M., Shuker D.M., Simoes Z.L., RA Sinha S., Smith Z., Solovyev V., Souvorov A., Springauf A., RA Stafflinger E., Stage D.E., Stanke M., Tanaka Y., Telschow A., RA Trent C., Vattathil S., Verhulst E.C., Viljakainen L., Wanner K.W., RA Waterhouse R.M., Whitfield J.B., Wilkes T.E., Williamson M., RA Willis J.H., Wolschin F., Wyder S., Yamada T., Yi S.V., Zecher C.N., RA Zhang L., Gibbs R.A.; RT "Functional and evolutionary insights from the genomes of three RT parasitoid Nasonia species."; RL Science 327:343-348(2010). RN [2] {ECO:0000313|EnsemblMetazoa:NV15323-PA} RP IDENTIFICATION. RG EnsemblMetazoa; RL Submitted (MAR-2014) to UniProtKB. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR RefSeq; XP_001604860.1; XM_001604810.4. DR RefSeq; XP_003424173.1; XM_003424125.3. DR STRING; 7425.NV15323-PA; -. DR EnsemblMetazoa; NV15323-RA; NV15323-PA; NV15323. DR GeneID; 100121260; -. DR KEGG; nvi:100121260; -. DR eggNOG; KOG0410; Eukaryota. DR eggNOG; COG2262; LUCA. DR InParanoid; K7J1U3; -. DR OMA; MDTVGFM; -. DR PhylomeDB; K7J1U3; -. DR Proteomes; UP000002358; Chromosome 2. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR CDD; cd01878; HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000002358}; KW Reference proteome {ECO:0000313|Proteomes:UP000002358}. FT DOMAIN 254 414 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 472 AA; 53756 MW; 0D2E5BC7C8616CEC CRC64; MNSIFKRLTP LAKSGLLFGK QTVQRKTWFM ASRFRYEDTY FHVDEEKELE NPEYNEISNE YLGAIAKGHR TFVIQPYIKW GKGKKYNTNR DLQLAEAVAL VETLPHWTVV DKMCVPLLTL EREQLFGSGS LENVKTRVKC GRNVTAIFIS TNTLKHVQLL ELEKIFGVPV YDRYSLVIHI FRCHAMSPEA KLQVALAELP YIYKKMSELC GRINLLEKRR LYLQAREAQL RTALKKLKNN RDTIRKKRKN RGFATVAVVG YTNAGKTSLI KALTSDEMLK PRNVLFATLD TTAHEGYLPC NMKVLYIDTI GFIQDVPETL IEPFVATLDD AMIADIIVHV YDASHPDKEA QIDHVRKTLK SLTDGNRPLI EVANKCDLIE AGTLPEETLG ISAKTTSGID VLRHEIEKKV LSETGRSVIK MRVESGSEAA AWLYKEATVV NAEADPKDPQ FLLLDVVVTE NTLHRFRRFL KQ // ID K7KB86_SOYBN Unreviewed; 598 AA. AC K7KB86; DT 09-JAN-2013, integrated into UniProtKB/TrEMBL. DT 09-JAN-2013, sequence version 1. DT 07-JUN-2017, entry version 32. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:KRH73556.1, ECO:0000313|EnsemblPlants:GLYMA02G44930.2}; GN Name=LOC100777376 {ECO:0000313|EnsemblPlants:GLYMA02G44930.2}; GN ORFNames=GLYMA_02G280500 {ECO:0000313|EMBL:KRH73556.1}; OS Glycine max (Soybean) (Glycine hispida). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae; OC Pentapetalae; rosids; fabids; Fabales; Fabaceae; Papilionoideae; OC Phaseoleae; Glycine; Soja. OX NCBI_TaxID=3847 {ECO:0000313|EnsemblPlants:GLYMA02G44930.2, ECO:0000313|Proteomes:UP000008827}; RN [1] {ECO:0000313|EnsemblPlants:GLYMA02G44930.2} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Williams 82 {ECO:0000313|EnsemblPlants:GLYMA02G44930.2}; RX PubMed=16247559; DOI=10.1007/s11103-005-8882-0; RA Saski C., Lee S.-B., Daniell H., Wood T.C., Tomkins J., Kim H.-G., RA Jansen R.K.; RT "Complete chloroplast genome sequence of Glycine max and comparative RT analyses with other legume genomes."; RL Plant Mol. Biol. 59:309-322(2005). RN [2] {ECO:0000313|EMBL:KRH73556.1} RP NUCLEOTIDE SEQUENCE. RC TISSUE=Callus {ECO:0000313|EMBL:KRH73556.1}; RX PubMed=20075913; DOI=10.1038/nature08670; RA Schmutz J., Cannon S.B., Schlueter J., Ma J., Mitros T., Nelson W., RA Hyten D.L., Song Q., Thelen J.J., Cheng J., Xu D., Hellsten U., RA May G.D., Yu Y., Sakurai T., Umezawa T., Bhattacharyya M.K., RA Sandhu D., Valliyodan B., Lindquist E., Peto M., Grant D., Shu S., RA Goodstein D., Barry K., Futrell-Griggs M., Abernathy B., Du J., RA Tian Z., Zhu L., Gill N., Joshi T., Libault M., Sethuraman A., RA Zhang X.-C., Shinozaki K., Nguyen H.T., Wing R.A., Cregan P., RA Specht J., Grimwood J., Rokhsar D., Stacey G., Shoemaker R.C., RA Jackson S.A.; RT "Genome sequence of the palaeopolyploid soybean."; RL Nature 463:178-183(2010). RN [3] {ECO:0000313|EnsemblPlants:GLYMA02G44930.2} RP IDENTIFICATION. RC STRAIN=Williams 82 {ECO:0000313|EnsemblPlants:GLYMA02G44930.2}; RG EnsemblPlants; RL Submitted (MAY-2013) to the EMBL/GenBank/DDBJ databases. RN [4] {ECO:0000313|EMBL:KRH73556.1} RP NUCLEOTIDE SEQUENCE. RC TISSUE=Callus {ECO:0000313|EMBL:KRH73556.1}; RA Hoefler B.C., Straight P.D.; RL Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CM000835; KRH73556.1; -; Genomic_DNA. DR RefSeq; XP_006575630.1; XM_006575567.2. DR STRING; 3847.GLYMA02G44930.2; -. DR EnsemblPlants; GLYMA02G44930.2; GLYMA02G44930.2; GLYMA02G44930. DR GeneID; 100777376; -. DR Gramene; GLYMA02G44930.2; GLYMA02G44930.2; GLYMA02G44930. DR KEGG; gmx:100777376; -. DR eggNOG; KOG0410; Eukaryota. DR eggNOG; KOG4197; Eukaryota. DR eggNOG; COG2262; LUCA. DR InParanoid; K7KB86; -. DR OMA; NGPEAIS; -. DR OrthoDB; EOG09360975; -. DR Proteomes; UP000008827; Chromosome 2. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR GO; GO:0043022; F:ribosome binding; IBA:GO_Central. DR CDD; cd01878; HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 2. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008827}; KW Reference proteome {ECO:0000313|Proteomes:UP000008827}. FT DOMAIN 298 568 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 598 AA; 66419 MW; 66CCA5CD597C613A CRC64; MKDTRVISFG VRKTLPQPLP ANDDGEVQKH REVKMLRSFS PRKFLTSLSC KRLYTSEGEA ARAILPKLLV VQPRVRPEKL LQAKLNEALC LANSLEDQRD GYFHTDFFDK PLPPHVLVQN RLPRADTYFG RGTVDNIKVH IDAAAESKGD VDAVFVNAIL SGIQQRNLEM AWGKPVLDRV GLIIEIFNAH AFTKEAKLQA ELAALSYKKT RLVRIRGPDG RNTFGASGEA EVVSARGRGS GGQGFMSGAG ETELQLQRRR ILERRNYLLS QIEEVRRTRA LQRAGRKRRG GSSGEGLATV AVVGYTNAGK STLVSRLSDS DLYSDCRLFA TVDPRVRSAV LPSGKKVLFS DTVGFISDLP VQLVEAFQAT LEEVVEADLL VHVVDSSAPN LDEHRSTVFQ VLQQIGVSEE KLQNMIEVWN KIDMEEECMD VDEYLDDEDK DGDADENSSF SGEDDVKSEV LPEREKDRAG SISGAENEGI KEVDCEGMEE KEDYSDGWLY DDDLVDEDEF CSPSTVADQQ NESYKKDNSV VKDGSIGQSG PHVKTSAVTG VGLQELLELI DKKLSVQNKK GARVVERSIY DRKWRPSHNQ ESGIAVEQ // ID K7RN85_ACIA4 Unreviewed; 473 AA. AC K7RN85; DT 06-FEB-2013, integrated into UniProtKB/TrEMBL. DT 06-FEB-2013, sequence version 1. DT 07-JUN-2017, entry version 34. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=PACID_15960 {ECO:0000313|EMBL:AFV89409.1}; OS Acidipropionibacterium acidipropionici (strain ATCC 4875 / DSM 20272 / OS JCM 6432 / NBRC 12425 / NCIMB 8070) (Propionibacterium OS acidipropionici). OC Bacteria; Actinobacteria; Propionibacteriales; Propionibacteriaceae; OC Acidipropionibacterium. OX NCBI_TaxID=1171373 {ECO:0000313|EMBL:AFV89409.1, ECO:0000313|Proteomes:UP000000214}; RN [1] {ECO:0000313|EMBL:AFV89409.1, ECO:0000313|Proteomes:UP000000214} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 4875 / DSM 20272 / JCM 6432 / NBRC 12425 / NCIMB 8070 RC {ECO:0000313|Proteomes:UP000000214}; RX PubMed=23083487; DOI=10.1186/1471-2164-13-562; RA Parizzi L.P., Grassi M.C., Llerena L.A., Carazzolle M.F., RA Queiroz V.L., Lunardi I., Zeidler A.F., Teixeira P.J., Mieczkowski P., RA Rincones J., Pereira G.A.; RT "The genome sequence of Propionibacterium acidipropionici provides RT insights into its biotechnological and industrial potential."; RL BMC Genomics 13:562-562(2012). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP003493; AFV89409.1; -; Genomic_DNA. DR RefSeq; WP_015070315.1; NC_019395.1. DR EnsemblBacteria; AFV89409; AFV89409; PACID_15960. DR KEGG; pbo:PACID_15960; -. DR PATRIC; fig|1171373.8.peg.1580; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000000214; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR Gene3D; 1.10.10.10; -; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR011991; WHTH_DNA-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000000214}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000000214}. FT DOMAIN 251 416 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 217 244 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 473 AA; 51557 MW; 7054A7D06F1B6FAB CRC64; MTPSDHDYPD DPVPDYDGDQ FDLDARLSLT RVPGMSTDLS DITEVEYRQL RLERVVLISV WTEGTASDAE NAMTELKLLA ETAGSQVLDA LIQRRPTPDP ATYIGSGKVK ELREVVVATG ADTVICDGEL DAAQLRNLED RVGVKVVDRT ILILDIFAQH ARSVEGRTQV ELAQLQYMKQ RLRGWGTSLS RQTGGRAAGG VGIGGRGPGE TKIETDRRRI NTRISRLRRK LRAMEGTRAE KRADRTRNRI PSVSIVGYTN AGKSSLLNRM TRAGVLVEDA LFATLDPTTR RATTDDGRVY TLTDTVGFVR HLPHHLVEAF ASTLEETARA DLLVHVVDAA DADPQGQVNA VRQVLTGIGA GEIDEILVLN KADLMDPGTE ITLRTAFPGA FIVSAHTGQG VEELVAEIER RLPVPTELVD AVVPYERGDL MDRIHRLGTI TSIEHTATGT HVVAHLHPGL AAEVRSVDGG ARD // ID K7SDM0_GLUOY Unreviewed; 435 AA. AC K7SDM0; DT 06-FEB-2013, integrated into UniProtKB/TrEMBL. DT 06-FEB-2013, sequence version 1. DT 07-JUN-2017, entry version 32. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=B932_1906 {ECO:0000313|EMBL:AFW01474.1}; OS Gluconobacter oxydans H24. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales; OC Acetobacteraceae; Gluconobacter. OX NCBI_TaxID=1224746 {ECO:0000313|EMBL:AFW01474.1, ECO:0000313|Proteomes:UP000000223}; RN [1] {ECO:0000313|EMBL:AFW01474.1, ECO:0000313|Proteomes:UP000000223} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=H24 {ECO:0000313|EMBL:AFW01474.1}; RX PubMed=23472221; RA Ge X., Zhao Y., Hou W., Zhang W., Chen W., Wang J., Zhao N., Lin J., RA Wang W., Chen M., Wang Q., Jiao Y., Yuan Z., Xiong X.; RT "Complete Genome Sequence of the Industrial Strain Gluconobacter RT oxydans H24."; RL Genome Announc. 1:E00003-E00013(2013). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP003926; AFW01474.1; -; Genomic_DNA. DR RefSeq; WP_015073533.1; NC_019396.1. DR EnsemblBacteria; AFW01474; AFW01474; B932_1906. DR GeneID; 29878498; -. DR KEGG; goh:B932_1906; -. DR PATRIC; fig|1224746.3.peg.1876; -. DR KO; K03665; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000000223; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000000223}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000000223}. FT DOMAIN 207 376 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 435 AA; 47876 MW; 2F1566458CA2A7CA CRC64; MSGFDTKKPA TRAAVILPWE KTGPQEDIRA ADARLEEAVG LAASIGLVIV RQAAILLRAR RPATLLGSGQ VEQLAEAVKL DQVDVVIIDA RLSPGQQRNL EKALGCKVMD RTGLILDIFG ARAATREGVL QVELAHLEYQ RSRLVRLWTH LERQRGGFGF LGGPGETQME ADRRMLAERI GKIKKELEQV RRTRGLHRDA RKRVPFPIVA LVGYTNAGKS TLFNALTGAS VHAQDQLFAT LDPTMRALRL PSGRNVILSD TVGFISDLPT ELIAAFRATL EEVSQADVIL HVRDIAHPDS AAQRADVLNV LDGMVRDGML DAQWPERTIE VLNKADLMGG VEAVPKRENA VAISAITGDG IPDLFETLDQ YLTQAMLDIR VQLSLQDGAA LAWLYQHGEV VERLDHENGM DVSVRLFPMD QERFEISYPG RTVAV // ID K7SL95_GLUOY Unreviewed; 449 AA. AC K7SL95; DT 06-FEB-2013, integrated into UniProtKB/TrEMBL. DT 06-FEB-2013, sequence version 1. DT 07-JUN-2017, entry version 32. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=B932_1391 {ECO:0000313|EMBL:AFW00973.1}; OS Gluconobacter oxydans H24. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales; OC Acetobacteraceae; Gluconobacter. OX NCBI_TaxID=1224746 {ECO:0000313|EMBL:AFW00973.1, ECO:0000313|Proteomes:UP000000223}; RN [1] {ECO:0000313|EMBL:AFW00973.1, ECO:0000313|Proteomes:UP000000223} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=H24 {ECO:0000313|EMBL:AFW00973.1}; RX PubMed=23472221; RA Ge X., Zhao Y., Hou W., Zhang W., Chen W., Wang J., Zhao N., Lin J., RA Wang W., Chen M., Wang Q., Jiao Y., Yuan Z., Xiong X.; RT "Complete Genome Sequence of the Industrial Strain Gluconobacter RT oxydans H24."; RL Genome Announc. 1:E00003-E00013(2013). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP003926; AFW00973.1; -; Genomic_DNA. DR EnsemblBacteria; AFW00973; AFW00973; B932_1391. DR KEGG; goh:B932_1391; -. DR PATRIC; fig|1224746.3.peg.1375; -. DR KO; K03665; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000000223; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000000223}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000000223}. FT DOMAIN 230 395 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 449 AA; 49375 MW; 29F3B40E6EC499A2 CRC64; METASPTPLA VLVGIQTPDV DDIAHEASLE ELGRLVKTLG YEVIGSVSQK REGTGAASLL GAGKLEELAD ITGGRGIITP IVKTPMTKAR KRFESAAEAH EPVEDETDDL RRPEFVIVDH ELTPSQIRNL ERATGAQVLD RTGVIVEIFH RHANTREAKL QVEMARLRYV APRLRESSNG GGRQQGPGAG ESNLSLDRRK IRDRLAELKT QLEAVQRDSD HRRSARKDQL RVALVGYTNA GKSSLMRALT GSQVLVQDKL FATLDTTVRT LQPETRPRIL VSDTVGFIKQ LPHDLVASFR STLSEALEAS LLLFVVDASD PTYEAQLEVS RSVLHEIGAD VVPSRLVLNK MDRVDDARRA ELLEKHPDAI PLSAHRPEDV SALRETLIAF FEADMVEDVL VLPYAKQGMI GEIYESARVL SEDHDETGRV LTVRGLPGAI ARLKRSLAT // ID K7WCE9_9NOST Unreviewed; 578 AA. AC K7WCE9; DT 06-FEB-2013, integrated into UniProtKB/TrEMBL. DT 06-FEB-2013, sequence version 1. DT 07-JUN-2017, entry version 31. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:AFW93058.1}; GN ORFNames=ANA_C10251 {ECO:0000313|EMBL:AFW93058.1}; OS Anabaena sp. 90. OC Bacteria; Cyanobacteria; Nostocales; Nostocaceae; Anabaena. OX NCBI_TaxID=46234 {ECO:0000313|EMBL:AFW93058.1, ECO:0000313|Proteomes:UP000010101}; RN [1] {ECO:0000313|EMBL:AFW93058.1, ECO:0000313|Proteomes:UP000010101} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=90 {ECO:0000313|EMBL:AFW93058.1}; RX PubMed=23148582; DOI=10.1186/1471-2164-13-613; RA Wang H., Sivonen K., Rouhiainen L., Fewer D.P., Lyra C., RA Rantala-Ylinen A., Vestola J., Jokela J., Rantasarkka K., Li Z., RA Liu B.; RT "Genome-derived insights into the biology of the hepatotoxic bloom- RT forming cyanobacterium Anabaena sp. strain 90."; RL BMC Genomics 13:613-613(2012). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP003284; AFW93058.1; -; Genomic_DNA. DR RefSeq; WP_015078222.1; NC_019427.1. DR EnsemblBacteria; AFW93058; AFW93058; ANA_C10251. DR KEGG; anb:ANA_C10251; -. DR PATRIC; fig|46234.3.peg.292; -. DR KO; K03665; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000010101; Chromosome chANA01. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000010101}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000010101}. FT DOMAIN 405 575 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 364 391 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 578 AA; 63491 MW; 081A87393897B33B CRC64; METIFGNVQG LKSSQLKQLQ RLYHQRISGD RITTTDFAQR LAAISTEINQ PICTYINRRG QVIRVGVGTP RQTQIPPLEL PRYGAERLSG IRCLSTNLKS EQPSESALTA MALQRLDALV VFNITGGGFT KRGGGSTGYV KEAYLAHLVA NNRQLVVTQS AGISIGDAGT YSHISPPLSL DALADQDFLD LVASLEEEFS REYVAQEVDA DHDRVVIVGV LTENITPQQF QDIIVELTRL VDTAGGVVLQ TLQQKRSRIH PQTVIGEGKV QEVAIAVQTL GANLVVFDRD LSRSQVRNLE AQIGVRVVDR TEVILDIFAQ RAQSGAGKLQ VELAQLGYML PRLTGKGEGM SRLGGGIGTR GPGETKLETE RRAIQKRISR LQHEVNQLQA HRCRLRQRRQ HREVPSVALV GYTNAGKSTL LNALTNSEVY TADQLFATLD PTTRRLIIPH AETGAPQETL MTDTVGFIHE LPASLMDAFR ATLEEVTEAD ALLHLVDLSH PAWLNHIRAV RDILAQMPIT PGPALVAFNK IDQVSSETLA LAREEFPLAV FISASQRLGL ETLRQRLSLL IQYAVGDD // ID K8E2P4_CARML Unreviewed; 420 AA. AC K8E2P4; DT 06-FEB-2013, integrated into UniProtKB/TrEMBL. DT 24-JUL-2013, sequence version 2. DT 07-JUN-2017, entry version 36. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:CCO10362.2}; GN ORFNames=BN424_898 {ECO:0000313|EMBL:CCO10362.2}; OS Carnobacterium maltaromaticum LMA28. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Carnobacteriaceae; OC Carnobacterium. OX NCBI_TaxID=1234679 {ECO:0000313|EMBL:CCO10362.2, ECO:0000313|Proteomes:UP000000212}; RN [1] {ECO:0000313|Proteomes:UP000000212} RP NUCLEOTIDE SEQUENCE. RC STRAIN=LMA28 {ECO:0000313|Proteomes:UP000000212}; RX PubMed=23405327; DOI=10.1128/genomeA.00115-12; RA Cailliez-Grimal C., Chaillou S., Anba-Mondoloni J., Loux V., RA Afzal M.I., Rahman A., Kergourlay G., Champomier-Verges M.C., RA Zagorec M., Dalgaard P., Leisner J.J., Prevost H., RA Revol-Junelles A.M., Borges F.; RT "Complete Chromosome Sequence of Carnobacterium maltaromaticum LMA RT 28."; RL Genome Announc. 1:0-0(2013). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; HE999757; CCO10362.2; -; Genomic_DNA. DR RefSeq; WP_015075769.1; NC_019425.2. DR EnsemblBacteria; CCO10362; CCO10362; BN424_898. DR KEGG; cml:BN424_898; -. DR KO; K03665; -. DR OrthoDB; POG091H0464; -. DR BioCyc; CMAL1234679:G132D-898-MONOMER; -. DR Proteomes; UP000000212; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000000212}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000000212}. FT DOMAIN 195 364 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 154 181 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 420 AA; 47701 MW; 36AC9343A6B795E0 CRC64; MEKNIIIIGV SGNQENFDYS MTELKELAFA NQLKVVGEIR QNLAKAHVAT YVGKGKLTEI INLAVELEVD TIVTNDELTP TQLRNLEAQL ELTVIDRTRL ILAIFAERAQ SKEAKLQVEI AQLNYEMPRL RTDQGTTLDQ QGGGSGLNNR GSGEKQIELD RRTIKNQIKR LNLELESITK EQQTRRHKRQ KNQIPLVSLV GYTNAGKSTT MNQLLQHFHS QEAKTVFEKD MLFATLDTSV REIVLPDRKK FLLSDTVGFV SKLPHQLVKA FRSTLEETKQ ADLLIHVVDY SDPNYQLMMD TTDKTLAEIG ILDIPVILAY NKADLIPEIS YPTYEDNHFI YSARDEKSLS MLVEIIKSTI FKEYTKATFL IPYNQTQYVA YLNEKAAVES EEYLDNGTKI VAEVGPIDLN KLAMFHVDSD // ID K8ESD9_CARML Unreviewed; 415 AA. AC K8ESD9; DT 06-FEB-2013, integrated into UniProtKB/TrEMBL. DT 24-JUL-2013, sequence version 2. DT 07-JUN-2017, entry version 38. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:CCO11481.2}; GN ORFNames=BN424_2040 {ECO:0000313|EMBL:CCO11481.2}; OS Carnobacterium maltaromaticum LMA28. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Carnobacteriaceae; OC Carnobacterium. OX NCBI_TaxID=1234679 {ECO:0000313|EMBL:CCO11481.2, ECO:0000313|Proteomes:UP000000212}; RN [1] {ECO:0000313|Proteomes:UP000000212} RP NUCLEOTIDE SEQUENCE. RC STRAIN=LMA28 {ECO:0000313|Proteomes:UP000000212}; RX PubMed=23405327; DOI=10.1128/genomeA.00115-12; RA Cailliez-Grimal C., Chaillou S., Anba-Mondoloni J., Loux V., RA Afzal M.I., Rahman A., Kergourlay G., Champomier-Verges M.C., RA Zagorec M., Dalgaard P., Leisner J.J., Prevost H., RA Revol-Junelles A.M., Borges F.; RT "Complete Chromosome Sequence of Carnobacterium maltaromaticum LMA RT 28."; RL Genome Announc. 1:0-0(2013). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; HE999757; CCO11481.2; -; Genomic_DNA. DR RefSeq; WP_015076650.1; NC_019425.2. DR EnsemblBacteria; CCO11481; CCO11481; BN424_2040. DR KEGG; cml:BN424_2040; -. DR KO; K03665; -. DR OrthoDB; POG091H0464; -. DR BioCyc; CMAL1234679:G132D-2040-MONOMER; -. DR Proteomes; UP000000212; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000000212}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000000212}. FT DOMAIN 199 360 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 415 AA; 46921 MW; 258F2E81584FC8E6 CRC64; MNTKEARERV IIVGVQTTES DQAFVYSLKE LAQLTETAKG EVVAELTQKR PRMDSKTYLG KGKLQELVRL AEETEADVII FNHGLTPGQT RNIQAEIDLK VIDRVQLILD VFAMRAQSKE GKLQVGLAQL HYLLPRLAGQ GKNLSKLGGG IGTRGPGETK LETDRRHIRD QITDIKRTLK ETEAHRERSR ERRNDGTTFQ IGLMGYTNAG KSTLLNQLTH AETYEQNQLF ATLDPLTRKL VLPTGMNVTL TDTVGFIQDL PTQLIDAFHS TLEETKNVDL LLHVVDAAAE DMLGHEKTVL ELLKELKMDR IPMLTVYNKR DLITGSFLPD LFPSVLISAR NDDDIAELYH KIMEIMKETL VPYQFEIAAD QGGALVKLKK ETLIISEEYN EEKNSYFVKG YAKEQSKWIG ERELE // ID K8GKA5_9CYAN Unreviewed; 563 AA. AC K8GKA5; DT 06-FEB-2013, integrated into UniProtKB/TrEMBL. DT 06-FEB-2013, sequence version 1. DT 07-JUN-2017, entry version 33. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=OsccyDRAFT_2050 {ECO:0000313|EMBL:EKQ69422.1}; OS Oscillatoriales cyanobacterium JSC-12. OC Bacteria; Cyanobacteria; Oscillatoriophycideae; Oscillatoriales; OC unclassified Oscillatoriales. OX NCBI_TaxID=864702 {ECO:0000313|EMBL:EKQ69422.1, ECO:0000313|Proteomes:UP000001332}; RN [1] {ECO:0000313|EMBL:EKQ69422.1, ECO:0000313|Proteomes:UP000001332} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=JSC-12 {ECO:0000313|EMBL:EKQ69422.1, RC ECO:0000313|Proteomes:UP000001332}; RG DOE Joint Genome Institute; RA Brown I., Huntemann M., Wei C.-L., Han J., Detter J.C., Han C., RA Tapia R., Chen A., Kyrpides N., Mavromatis K., Markowitz V., Szeto E., RA Ivanova N., Mikhailova N., Ovchinnikova G., Pagani I., Pati A., RA Goodwin L., Nordberg H.P., Cantor M.N., Hua S.X., Woyke T.; RT "Improved high quality draft of Oscillatoriales sp. JSC-12."; RL Submitted (OCT-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EKQ69422.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AJUB01000010; EKQ69422.1; -; Genomic_DNA. DR RefSeq; WP_009556330.1; NZ_CM001633.1. DR EnsemblBacteria; EKQ69422; EKQ69422; OsccyDRAFT_2050. DR PATRIC; fig|864702.5.peg.2206; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000001332; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000001332}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000001332}. FT DOMAIN 391 561 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 350 384 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 563 AA; 62559 MW; A3756D9FBF5BDEEC CRC64; MHIETVYGHL QGVKPSQFKQ LQRLYQARLP GDRITTAEFA QRVAAISTDL GQPICVYVNR RGQVIRVGVG TLRQTRIPPL ELPRYGVERL SGIRCISTQL KVEPPNESTL TCMAIQRLDA LIILTLSGSG FERRGGGATG YIRETYLAHL IPHPEANWTV SPPLSLDVLT NQDFVSLVEG LEEEFRRDFV ARQVDRDQDR VLLVGLHTDN CTAQAFQDSL AELARLVDTA GGEVLQTMKQ RRNQPHPQTV VGEGKVQEIA RTAQTLGANV VVFDRDLSPA QVRNLEEQIG LRVVDRTEVI LDIFAQRAQS GAGKLQVELA QLEYRLPRLT GRGQSMSRLG GGIGTRGPGE TKLETERRAI QRRISRLQQE VNQLQAHRAR MRQRRQHQEV PSIAVVGYTN AGKSTLLNVL TNAEVYTADQ LFATLDPTTR RLVVPDAMTQ APRSILLTDT VGFIHDLPPS LVDAFRATLE EVTEANALLH VVDLSHPAWH NQIRSVMTIL SQMPIAPGPV LLAFNKIDQV DSNTLALAQE EFPQAVFISA CDRLGLETLR RRLGQLVHYA MSG // ID K8WDP3_PRORE Unreviewed; 426 AA. AC K8WDP3; DT 06-FEB-2013, integrated into UniProtKB/TrEMBL. DT 06-FEB-2013, sequence version 1. DT 30-AUG-2017, entry version 35. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=OOC_03317 {ECO:0000313|EMBL:EKT58684.1}; OS Providencia rettgeri Dmel1. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; OC Morganellaceae; Providencia. OX NCBI_TaxID=1141663 {ECO:0000313|EMBL:EKT58684.1, ECO:0000313|Proteomes:UP000009338}; RN [1] {ECO:0000313|EMBL:EKT58684.1, ECO:0000313|Proteomes:UP000009338} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Dmel1 {ECO:0000313|EMBL:EKT58684.1}; RX PubMed=23145767; DOI=10.1186/1471-2164-13-612; RA Galac M.R., Lazzaro B.P.; RT "Comparative genomics of bacteria in the genus Providencia isolated RT from wild Drosophila melanogaster."; RL BMC Genomics 13:612-612(2012). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EKT58684.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AJSB01000004; EKT58684.1; -; Genomic_DNA. DR RefSeq; WP_004907402.1; NZ_CM001774.1. DR EnsemblBacteria; EKT58684; EKT58684; OOC_03317. DR PATRIC; fig|1141663.3.peg.678; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000009338; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000009338}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000009338}. FT DOMAIN 198 365 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 426 AA; 48156 MW; C3E07FB9E0DEDE90 CRC64; MFDRYEGGEL AVLVHVFFSQ EKDVDNLAEF ESLVTSAGVK PVQIVTGSRK APHPKFFVGE GKAEEIAQAV EESGADVVLF NHTLSPAQER NLERICQCKV VDRTGVILDI FAQRARTHEG KLQVELAQLR HLSTRLVRGW THLERQKGGI GLRGPGETQL ETDRRLLRDK IKQILSRLSR VEKQREQGRQ ARSKADIPTI SLVGYTNAGK SSLFNRMTAA DVYAADQLFA TLDPTLRRID VEDVGVVVLA DTVGFIRHLP HDLVAAFKAT LQETREATLL LHVIDAADNR LDENIHAVES VLEEIEADEI PTLLVMNKVD MLEDFVPRID RDEDNKPVRV WVSAQTGDGI SLLLQALTER LSGEIAHVEL RLPPNEGRLR SRFYQLQSIE REWQEEDGSI GLEVRMPMVD WRRLCKQEQQ LPDYVI // ID K8WLT8_9GAMM Unreviewed; 426 AA. AC K8WLT8; DT 06-FEB-2013, integrated into UniProtKB/TrEMBL. DT 06-FEB-2013, sequence version 1. DT 30-AUG-2017, entry version 30. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=OO7_00580 {ECO:0000313|EMBL:EKT61593.1}; OS Providencia sneebia DSM 19967. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; OC Morganellaceae; Providencia. OX NCBI_TaxID=1141660 {ECO:0000313|EMBL:EKT61593.1, ECO:0000313|Proteomes:UP000010290}; RN [1] {ECO:0000313|EMBL:EKT61593.1, ECO:0000313|Proteomes:UP000010290} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 19967 {ECO:0000313|EMBL:EKT61593.1}; RX PubMed=23145767; DOI=10.1186/1471-2164-13-612; RA Galac M.R., Lazzaro B.P.; RT "Comparative genomics of bacteria in the genus Providencia isolated RT from wild Drosophila melanogaster."; RL BMC Genomics 13:612-612(2012). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EKT61593.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AKKN01000001; EKT61593.1; -; Genomic_DNA. DR RefSeq; WP_008914022.1; NZ_CM001773.1. DR EnsemblBacteria; EKT61593; EKT61593; OO7_00580. DR PATRIC; fig|1141660.3.peg.115; -. DR Proteomes; UP000010290; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000010290}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000010290}. FT DOMAIN 198 365 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 426 AA; 48035 MW; AEC60AD4BF32099B CRC64; MFDRYEGGEL AVLVHVFFSQ EKDTENLAEF ESLVTSAGVK PVQIVTGSRK SPHPKYFVGE GKAEEIAEAV QESGADVVLF NHTLSPAQER NLERLCQCKV VDRTGVILDI FAQRARTHEG KLQVELAQLR HLSTRLVRGW THLERQKGGI GLRGPGETQL ETDRRLLRGK ISQILSRLSR VEKQREQGRQ ARNKADISTV SLVGYTNAGK SSLFNRITDS EVYAADQLFA TLDPTLRRIN VEDVGTVVLA DTVGFIRHLP HDLVAAFKAT LQETREATLL LHVIDAADSR VDENIHAVES VLEEIEANEI PTLLVMNKVD MLEDFIPRID RNEDNKPVRV WVSAQTGEGI PLLLQALTER LSGEIAHLEL CLPPSEGRLR SRFYQLEAIE REWQEEDGSI GLEVRMPIVE WQRLCKQEQQ LLSYVI // ID K8WMB5_9GAMM Unreviewed; 426 AA. AC K8WMB5; DT 06-FEB-2013, integrated into UniProtKB/TrEMBL. DT 06-FEB-2013, sequence version 1. DT 30-AUG-2017, entry version 31. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=OOA_11178 {ECO:0000313|EMBL:EKT61116.1}; OS Providencia burhodogranariea DSM 19968. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; OC Morganellaceae; Providencia. OX NCBI_TaxID=1141662 {ECO:0000313|EMBL:EKT61116.1, ECO:0000313|Proteomes:UP000009336}; RN [1] {ECO:0000313|EMBL:EKT61116.1, ECO:0000313|Proteomes:UP000009336} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 19968 {ECO:0000313|EMBL:EKT61116.1, RC ECO:0000313|Proteomes:UP000009336}; RX PubMed=23145767; DOI=10.1186/1471-2164-13-612; RA Galac M.R., Lazzaro B.P.; RT "Comparative genomics of bacteria in the genus Providencia isolated RT from wild Drosophila melanogaster."; RL BMC Genomics 13:612-612(2012). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EKT61116.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AKKL01000031; EKT61116.1; -; Genomic_DNA. DR RefSeq; WP_008912238.1; NZ_KB233223.1. DR EnsemblBacteria; EKT61116; EKT61116; OOA_11178. DR PATRIC; fig|1141662.3.peg.2262; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000009336; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000009336}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000009336}. FT DOMAIN 198 365 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 426 AA; 48049 MW; 2E0ABC086152C04D CRC64; MFDRYEGGEL AVLVHVFFSQ EKDTENLAEF ESLVTSAGVK PVQIVTGSRK SPHPKYYVGE GKAEEIAEAV QASGADVVLF NHTLTPAQER NLERLCECKV VDRTGVILDI FAQRARTHEG KLQVELAQLR HMSTRLVRGW THLERQKGGI GLRGPGETQL ETDRRLLRVK ISQILSRLSR VEKQREQGRQ ARNKADIPTI SLVGYTNAGK SSLFNRMTAS DVYAADQLFA TLDPTLRRID VDDVGTVVLA DTVGFIRNLP HDLVAAFKAT LQETREATLL LHVIDAADSR LDENIRAVES VLEEIEADEI PTLLVMNKVD MLEEFVPRID RNEDNKPVRV WLSAQTGDGI PLLLQALTER LSGEIAHVEI RLPPNEGRLR SRFYQLNAIE REWLEEDGSI GLEVRMPMVD WCRLCKQEQQ LPSYVI // ID K8Z759_9ENTE Unreviewed; 411 AA. AC K8Z759; DT 06-FEB-2013, integrated into UniProtKB/TrEMBL. DT 06-FEB-2013, sequence version 1. DT 07-JUN-2017, entry version 30. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=C683_1139 {ECO:0000313|EMBL:EKU26864.1}; OS Catellicoccus marimammalium M35/04/3. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Enterococcaceae; OC Catellicoccus. OX NCBI_TaxID=1234409 {ECO:0000313|EMBL:EKU26864.1, ECO:0000313|Proteomes:UP000016057}; RN [1] {ECO:0000313|EMBL:EKU26864.1, ECO:0000313|Proteomes:UP000016057} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=M35/04/3 {ECO:0000313|EMBL:EKU26864.1, RC ECO:0000313|Proteomes:UP000016057}; RX PubMed=23405330; RA Weigand M.R., Ryu H., Bozcek L., Konstantinidis K.T., RA Santo Domingo J.W.; RT "Draft Genome Sequence of Catellicoccus marimammalium, a Novel Species RT Commonly Found in Gull Feces."; RL Genome Announc. 1:E00019-12(2013). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EKU26864.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AMYT01000022; EKU26864.1; -; Genomic_DNA. DR RefSeq; WP_009491940.1; NZ_AMYT01000022.1. DR EnsemblBacteria; EKU26864; EKU26864; C683_1139. DR PATRIC; fig|1234409.3.peg.1091; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000016057; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000016057}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000016057}. FT DOMAIN 199 323 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 411 AA; 47133 MW; 4F362E5342F09CC0 CRC64; MVEKLTKERV LVCGAYTQKE KEHFQSSMEE LKRLVETAQG EVIVENIQHR EDIDQKTVLG KGKIAEIQEQ VIAENIDLVV VNTSLTPRQL ANLEEILPCR VIDRTQLILD IFALRARSKE GKLQVAKAQI DYLLPRLTVM NGHLSKLGGG IGTRGPGETK LETDRRHLHR QQLRIQKELK EVKKHRELAR KNRTQNSGLN IGLVGYTNAG KSTFLNVLTQ AETYEKDELF ATLDPLTRQY RLKEGLKMTF TDTVGFIQDL PTTLVEAFHS TLEETQNMDL LFHIVDASSP ERDEQEKTVL RLLDELGCQS IPVLTIYNKM DQVAGDFVPT QFPHLCLSLK ERGAKEEIET GIIKFLQEIW QPYTYSLPVS EVQKLYALQE FTLVEKMEFS EEETYNITGY GNQKYAYLYE K // ID K9AI81_9MICO Unreviewed; 480 AA. AC K9AI81; DT 06-FEB-2013, integrated into UniProtKB/TrEMBL. DT 06-FEB-2013, sequence version 1. DT 07-JUN-2017, entry version 32. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=C272_10014 {ECO:0000313|EMBL:EKU47038.1}; OS Brevibacterium casei S18. OC Bacteria; Actinobacteria; Micrococcales; Brevibacteriaceae; OC Brevibacterium. OX NCBI_TaxID=1229781 {ECO:0000313|EMBL:EKU47038.1, ECO:0000313|Proteomes:UP000009879}; RN [1] {ECO:0000313|EMBL:EKU47038.1, ECO:0000313|Proteomes:UP000009879} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=S18 {ECO:0000313|EMBL:EKU47038.1, RC ECO:0000313|Proteomes:UP000009879}; RA Sharma R., Singh A., Jangir P.K.; RT "Genome Sequence of Brevibacterium casei S18."; RL Submitted (SEP-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EKU47038.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AMSP01000007; EKU47038.1; -; Genomic_DNA. DR EnsemblBacteria; EKU47038; EKU47038; C272_10014. DR PATRIC; fig|1229781.4.peg.2012; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000009879; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 2. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000009879}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000009879}. FT DOMAIN 255 420 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 480 AA; 52312 MW; D80285FABB42ADF6 CRC64; MLDRVLARGA QALSPKEAAA DEESQFDLAE RAALRRVAGL STELEDVTEV EYRQIRLERV VLAGLWNTTL DEAENSIREL AALAETAGSE VLDAIVQRRD KPDPGTYLGR GKAAELKEIV EAVGADTVII DSELAPSQRR GLEDVIKVKV VDRVALILDI FAQHAKSREG KAQVELAQLE YLLPRLRGWG ESLSRQAGGR VAGGAGIGSR GPGETKIELD RRRIRTRMAK LRRQIAGMAP ARDTKRKNRA RNHVPSVAIV GYTNAGKSSL LNRLTDAEVM VQNALFATLD PTVRQSRTSD GITFTYTDTV GFVRNLPHQL VEAFRSTLEE ASDSDLLLHV VDASHPDPQG QIHAVREVLG DVDTGDIPEL LVFNKVDLAD ETVVTALRAE YPGARFVSAT TGEGIAELVE TIEEKLPSPN IEVSVLIPYE RGDLVSKIYA LGTVDHEEHG PGGTGMHAKV PAELAAELEE FRRPDMVIGE // ID K9AT10_9STAP Unreviewed; 411 AA. AC K9AT10; DT 06-FEB-2013, integrated into UniProtKB/TrEMBL. DT 06-FEB-2013, sequence version 1. DT 07-JUN-2017, entry version 31. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=C273_00915 {ECO:0000313|EMBL:EKU50538.1}; OS Staphylococcus massiliensis S46. OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae; OC Staphylococcus. OX NCBI_TaxID=1229783 {ECO:0000313|EMBL:EKU50538.1, ECO:0000313|Proteomes:UP000009885}; RN [1] {ECO:0000313|EMBL:EKU50538.1, ECO:0000313|Proteomes:UP000009885} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=S46 {ECO:0000313|EMBL:EKU50538.1, RC ECO:0000313|Proteomes:UP000009885}; RX PubMed=23929469; RA Srivastav R., Singh A., Jangir P.K., Kumari C., Muduli S., Sharma R.; RT "Genome Sequence of Staphylococcus massiliensis Strain S46, Isolated RT from the Surface of Healthy Human Skin."; RL Genome Announc. 1:e00553-13(2013). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EKU50538.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AMSQ01000001; EKU50538.1; -; Genomic_DNA. DR RefSeq; WP_009381825.1; NZ_AMSQ01000001.1. DR EnsemblBacteria; EKU50538; EKU50538; C273_00915. DR PATRIC; fig|1229783.3.peg.187; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000009885; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000009885}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000009885}. FT DOMAIN 206 367 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 411 AA; 47031 MW; FC2B214E15A10F9C CRC64; MSQLKPLETK QHKETACLIG VDSEEDQTFD FESTMAELNA LSHTCQLDVR GQITQNRHQF DHKYYVGKGK LQEINEFVTM NDIDVVVVND ELTTAQSKHL NDTLNVKIID RTQLILEIFA LRAKSKEGKL QVEYAQLDYL LPRLQGHGKS LSRLGGGIGT RGPGETKLEM DRRHIRTRMN EIKHQLQTVV NHRERYRNKR IQNEVFHVAL VGYTNAGKSS WFNTLADETT YEKDLLFATL DPKTRRIQIN NGFNLIISDT VGFIQKLPTT LIAAFKSTLE EAKGANLLLH VVDASHDNYK TQYDTVNRLI KDLDMDTIPQ AVIFNKKDLC TGEAPISEHP NVFVSSKDQS DIHHVKDLVF DCIKDTLDYY EETLSSSEAS RLYFLKQNTL VTNLEFNEAD ETYTIQGYKN K // ID K9DGT5_9BURK Unreviewed; 412 AA. AC K9DGT5; DT 06-FEB-2013, integrated into UniProtKB/TrEMBL. DT 06-FEB-2013, sequence version 1. DT 05-JUL-2017, entry version 33. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=HMPREF9710_02123 {ECO:0000313|EMBL:EKU82496.1}; OS Massilia timonae CCUG 45783. OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Oxalobacteraceae; Massilia. OX NCBI_TaxID=883126 {ECO:0000313|EMBL:EKU82496.1, ECO:0000313|Proteomes:UP000009874}; RN [1] {ECO:0000313|EMBL:EKU82496.1, ECO:0000313|Proteomes:UP000009874} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CCUG 45783 {ECO:0000313|EMBL:EKU82496.1, RC ECO:0000313|Proteomes:UP000009874}; RG The Broad Institute Genome Sequencing Platform; RA Earl A., Ward D., Feldgarden M., Gevers D., Huys G., Walker B., RA Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B., RA Abouelleil A., Alvarado L., Arachchi H.M., Berlin A.M., Chapman S.B., RA Goldberg J., Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., RA Larimer J., McCowen C., Montmayeur A., Murphy C., Neiman D., RA Pearson M., Priest M., Roberts A., Saif S., Shea T., Sisk P., RA Sykes S., Wortman J., Nusbaum C., Birren B.; RT "The Genome Sequence of Massilia timonae CCUG 45783."; RL Submitted (SEP-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EKU82496.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGZI01000026; EKU82496.1; -; Genomic_DNA. DR EnsemblBacteria; EKU82496; EKU82496; HMPREF9710_02123. DR PATRIC; fig|883126.3.peg.2153; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000009874; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000009874}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000009874}. FT DOMAIN 199 366 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 412 AA; 44761 MW; 2007C24027C097F9 CRC64; MADAPGTPTL RAALVGIDFG TGDFAASLDE LSLLARSAGA DPITTITAKR SSPDPAHFVG SGKADEIALD AKALGAEIVI FNHALSPAQQ RNLERRLQLR VIDRTSLILD IFAQRAKSHE GKLQVELAQL QHLATRLIRG WTHLERQKGG IGLRGPGETQ LETDRRLIGE RVKMLRARLG KLRKQHETQR RQRGRNKTFS VSLVGYTNAG KSTLFNTLTK AGVYVANQLF ATLDTTSRRM YLGDEVGSVV ISDTVGFVRE LPHQLVAAFR ATLEETIHAD LLLHVVDSAS PTRMEQVEQV NEVLREIGAD HVPQILVWNK IDAAGLEPGV ERDEYDKINR VFISAHSGAG LDLLRSAIAE AAKSAPGPGG YSNPENEEHD EAFGLAEEDA SVDAHPGGLA DNMPTSTHVR PN // ID K9ECA4_9LACT Unreviewed; 418 AA. AC K9ECA4; DT 06-FEB-2013, integrated into UniProtKB/TrEMBL. DT 06-FEB-2013, sequence version 1. DT 07-JUN-2017, entry version 30. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=HMPREF9698_00340 {ECO:0000313|EMBL:EKU94308.1}; OS Alloiococcus otitis ATCC 51267. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Carnobacteriaceae; OC Alloiococcus. OX NCBI_TaxID=883081 {ECO:0000313|EMBL:EKU94308.1, ECO:0000313|Proteomes:UP000009875}; RN [1] {ECO:0000313|EMBL:EKU94308.1, ECO:0000313|Proteomes:UP000009875} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51267 {ECO:0000313|EMBL:EKU94308.1, RC ECO:0000313|Proteomes:UP000009875}; RG The Broad Institute Genome Sequencing Platform; RA Earl A., Ward D., Feldgarden M., Gevers D., Huys G., Walker B., RA Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B., RA Abouelleil A., Alvarado L., Arachchi H.M., Berlin A.M., Chapman S.B., RA Goldberg J., Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., RA Larimer J., McCowen C., Montmayeur A., Murphy C., Neiman D., RA Pearson M., Priest M., Roberts A., Saif S., Shea T., Sisk P., RA Sykes S., Wortman J., Nusbaum C., Birren B.; RT "The Genome Sequence of Alloiococcus otitis ATCC 51267."; RL Submitted (SEP-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EKU94308.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGXA01000004; EKU94308.1; -; Genomic_DNA. DR EnsemblBacteria; EKU94308; EKU94308; HMPREF9698_00340. DR PATRIC; fig|883081.3.peg.343; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000009875; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000009875}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000009875}. FT DOMAIN 198 359 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 418 AA; 47027 MW; 53A1045AA9E7016D CRC64; MSKTGFEDVV IVGVQKEETD YDFHYSLDEL ENLVNNAHGR VVGRISQKRD SLDQKTFVGK GKLKEIKDLV EAKDATCLIF NQELSPSHVR NIQDFINVKV LDRIQVILDI FAMRAQSKAG RLQVELAQLN YLLPRLAGQG ENLSRLGGGI GTRGPGETKL ETDRRHIQKQ ISDIKKELVK LADHRKRSRQ KRQESQIVQI GLIGYTNAGK STLLNKLTGS QSLEKDILFA TLDPITRQLT LPSGLQVTLT DTVGFIKDLP TQLIESFKST LEESRQADIL LHLVDASSPN RVSQEDTVVA LLEDLDMEDI PRLTVYNKKD KLDQAFTPLA FPNLLISALD DQDITYLKSS IENFLMDQIM ATYQVDLPAS RGDIYSALQQ GTIVKKEKFD KTNQSYKIEG YAKKDSYWQS LLEEGVDG // ID K9EJL4_9ACTO Unreviewed; 515 AA. AC K9EJL4; DT 06-FEB-2013, integrated into UniProtKB/TrEMBL. DT 06-FEB-2013, sequence version 1. DT 07-JUN-2017, entry version 29. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=HMPREF9233_00159 {ECO:0000313|EMBL:EKU96071.1}; OS Actinobaculum massiliense ACS-171-V-Col2. OC Bacteria; Actinobacteria; Actinomycetales; Actinomycetaceae; OC Actinobaculum. OX NCBI_TaxID=883066 {ECO:0000313|EMBL:EKU96071.1, ECO:0000313|Proteomes:UP000009888}; RN [1] {ECO:0000313|EMBL:EKU96071.1, ECO:0000313|Proteomes:UP000009888} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ACS-171-V-Col2 {ECO:0000313|Proteomes:UP000009888}; RG The Broad Institute Genome Sequencing Platform; RA Earl A., Ward D., Feldgarden M., Gevers D., Saerens B., RA Vaneechoutte M., Walker B., Young S.K., Zeng Q., Gargeya S., RA Fitzgerald M., Haas B., Abouelleil A., Alvarado L., Arachchi H.M., RA Berlin A., Chapman S.B., Goldberg J., Griggs A., Gujja S., Hansen M., RA Howarth C., Imamovic A., Larimer J., McCowen C., Montmayeur A., RA Murphy C., Neiman D., Pearson M., Priest M., Roberts A., Saif S., RA Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C., Birren B.; RT "The Genome Sequence of Actinobaculum massiliae ACS-171-V-COL2."; RL Submitted (SEP-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EKU96071.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGWL01000001; EKU96071.1; -; Genomic_DNA. DR RefSeq; WP_007000377.1; NZ_JH992955.1. DR EnsemblBacteria; EKU96071; EKU96071; HMPREF9233_00159. DR PATRIC; fig|883066.3.peg.161; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000009888; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000009888}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000009888}. FT DOMAIN 284 450 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 515 AA; 55920 MW; EC0A8F952806545E CRC64; MHTKSNHDSS QASAEASNRG EEADNRTVDI HSRAGTSLQA DPRYGRAWAG DWLDREQRKG LQRVEGIGGN FADDEQVELE YRQVRLERVV LVGVYAQGRT EAEESLRELA ALADTAGSTV VAGVLQRRDI PDNATFLGKG KAHELADLVR AQTADTVIVD SELAPSQRRA LEDVVGVKVI DRTALVLDIF ARHAKSKEGK AQVELAQLEY LLPRLRGWGE SMSRQAGGQV AGGAGIGSRG PGETQLELDR RRIRFRMAKL RRDIKKMKPA RETRRAERQR TGIPSVVIVG YTNAGKSSLL NRLTGAGVLV ENALFATLDP TVRRARTPSD REFTLSDTVG FVRNLPTQLV EAFRSTLEEV GEADVLLHVV DASHADPVGQ VKAVHEVLNG VDGAREAPEL IVLSKIDLAD PVDLAALRTR FPDAVAVSAA TGEGLDELMG KIDELLPQLE SEIEGVIPFS RGDLVSLIYE YGDLLAPVAY RDNGTFVHAR VPKSIAAQFE AASGNSDGHS PERSS // ID K9GN08_9PROT Unreviewed; 433 AA. AC K9GN08; DT 06-FEB-2013, integrated into UniProtKB/TrEMBL. DT 06-FEB-2013, sequence version 1. DT 07-JUN-2017, entry version 32. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=C882_2774 {ECO:0000313|EMBL:EKV26482.1}; OS Caenispirillum salinarum AK4. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales; OC Rhodospirillaceae; Caenispirillum. OX NCBI_TaxID=1238182 {ECO:0000313|EMBL:EKV26482.1, ECO:0000313|Proteomes:UP000009881}; RN [1] {ECO:0000313|EMBL:EKV26482.1, ECO:0000313|Proteomes:UP000009881} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=AK4 {ECO:0000313|EMBL:EKV26482.1, RC ECO:0000313|Proteomes:UP000009881}; RX PubMed=23409257; RA Khatri I., Singh A., Korpole S., Pinnaka A.K., Subramanian S.; RT "Draft Genome Sequence of an Alphaproteobacterium, Caenispirillum RT salinarum AK4(T), Isolated from a Solar Saltern."; RL Genome Announc. 1:E00199-12(2013). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EKV26482.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ANHY01000030; EKV26482.1; -; Genomic_DNA. DR RefSeq; WP_009542765.1; NZ_ANHY01000030.1. DR EnsemblBacteria; EKV26482; EKV26482; C882_2774. DR PATRIC; fig|1238182.3.peg.4325; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000009881; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000009881}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000009881}. FT DOMAIN 209 381 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 175 205 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 433 AA; 48553 MW; AB0A534E97A3BD10 CRC64; MTEPTSTKRD PARCLVVHPA IKQRGTNDDA RDPTERLEEA KGLALAIDLN IVHGEVVTLN KPRPATFLGE GQVERLQSII EDNEVEVVVM DCHLSPVQQR NLERNWKTKV IDRTGLILEI FGERARTREG QLQVELAHLS YQRSRLVRSW THLERQRGGA GFMGGPGETQ IEIDRRLISE RITRLKKELE EVKRTRNLHR EARRRVPYPI VALVGYTNAG KSTLFNRLTK SEVYAQDQLF ATLDPTMRGL VLPSGKQVIL SDTVGFVSDL PHELVAAFHA TLEEVLEADV IVHVRDAHSP DTAAQKADVE HVLRVELNLG EEVDAGLLEA MNKIDLLAPE AHDELVQQAA RDDNMIALSA ITGEGVDRLL ATVDEVLSRS RETIETDVPL SDGATISWLY RKGDVVSRED NEETAHMIVR LDPADAERFR MGK // ID K9P832_CYAGP Unreviewed; 778 AA. AC K9P832; DT 06-MAR-2013, integrated into UniProtKB/TrEMBL. DT 06-MAR-2013, sequence version 1. DT 07-JUN-2017, entry version 35. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Cyagr_1570 {ECO:0000313|EMBL:AFY28729.1}; OS Cyanobium gracile (strain ATCC 27147 / PCC 6307). OC Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Cyanobium. OX NCBI_TaxID=292564 {ECO:0000313|EMBL:AFY28729.1, ECO:0000313|Proteomes:UP000010388}; RN [1] {ECO:0000313|Proteomes:UP000010388} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 27147 / PCC 6307 {ECO:0000313|Proteomes:UP000010388}; RX PubMed=23277585; DOI=10.1073/pnas.1217107110; RA Shih P.M., Wu D., Latifi A., Axen S.D., Fewer D.P., Talla E., RA Calteau A., Cai F., Tandeau de Marsac N., Rippka R., Herdman M., RA Sivonen K., Coursin T., Laurent T., Goodwin L., Nolan M., RA Davenport K.W., Han C.S., Rubin E.M., Eisen J.A., Woyke T., Gugger M., RA Kerfeld C.A.; RT "Improving the coverage of the cyanobacterial phylum using diversity- RT driven genome sequencing."; RL Proc. Natl. Acad. Sci. U.S.A. 110:1053-1058(2013). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP003495; AFY28729.1; -; Genomic_DNA. DR EnsemblBacteria; AFY28729; AFY28729; Cyagr_1570. DR KEGG; cgc:Cyagr_1570; -. DR PATRIC; fig|292564.3.peg.1495; -. DR KO; K03665; -. DR OMA; NPQTLWG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000010388; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0051920; F:peroxiredoxin activity; IEA:InterPro. DR GO; GO:0045454; P:cell redox homeostasis; IEA:InterPro. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR000866; AhpC/TSA. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR019479; Peroxiredoxin_C. DR InterPro; IPR012336; Thioredoxin-like_fold. DR InterPro; IPR013766; Thioredoxin_domain. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF10417; 1-cysPrx_C; 1. DR Pfam; PF00578; AhpC-TSA; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF52833; SSF52833; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. DR PROSITE; PS51352; THIOREDOXIN_2; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000010388}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000010388}. FT DOMAIN 379 550 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT DOMAIN 570 726 Thioredoxin. FT {ECO:0000259|PROSITE:PS51352}. FT COILED 340 374 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 778 AA; 84616 MW; BB3FB6DA3BCB3EEF CRC64; MRQGVLAGRT AGLRPAERRR LEQICHRRHP AEAVADLLTL QRLAAEVRGL ELPLTLVVDG RGLCRLLWVG ELEHAARLLE KLPGPSRRQG HNLRLLTCAG AGRQAQLQPT AQEAVVGMDL APELWLRFGP QPEAGGRWPA AIHTPATSGD RAWQGVLAGD LADLCGQDPA ALVSEEAPAA AAPAPTPEGP ERVLLLVQTS GDRALNERRI AELEGLVRSA GAVPVGRVEQ RRQGPATRNP WGEGKLREAA LEARRVGASL VVADRELTPA QARDMESLLD LPISDRSELI LDIFAQRAAS GAGRLQVELA QLRYRLPRLT GRGLSLSRQG GGIGTRGPGE TQLEKDRRAI ARRIERLQRE VRRLGDHRAR LRQGRRDLPR VALVGYTNAG KSSLLNALTG ASGDQAVLAE DQLFATLDPT TRRIGRGAAG GGPPLLVTDT VGFIRELPPQ LMEAFRSTFE EALDADGLLI VVDLADPAWP EQLATVRTIL DALKATMPRR VIGNQIDRCA SGELERARAL EPGMLFVSAT ADLGLQHLRQ ELQSWTAAAT TDDPAAVPAS AGANFSPMTL QLGDTVPDFT QESQLGPINL YDFAGDSWVV LFSHPADYTP VCTTELGEVS RLRAEWEKRN VKTIALSVDS AESHKGWIGD INETQNTTVD YPILADSDKK VSSLYGMIHP NSLSNLTVRS VFIIDPSKKL RLQITYPAST GRNFDEILRV IDSLQLTDHH QVATPVNWKE GDDCVVVPSI PTDEARAKFP KGVTEIRPYL RMTPQPNK // ID K9PL18_9CYAN Unreviewed; 583 AA. AC K9PL18; DT 06-MAR-2013, integrated into UniProtKB/TrEMBL. DT 06-MAR-2013, sequence version 1. DT 07-JUN-2017, entry version 31. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=Cal7507_3056 {ECO:0000313|EMBL:AFY33469.1}; OS Calothrix sp. PCC 7507. OC Bacteria; Cyanobacteria; Nostocales; Rivulariaceae; Calothrix. OX NCBI_TaxID=99598 {ECO:0000313|EMBL:AFY33469.1, ECO:0000313|Proteomes:UP000010390}; RN [1] {ECO:0000313|EMBL:AFY33469.1, ECO:0000313|Proteomes:UP000010390} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=PCC 7507 {ECO:0000313|EMBL:AFY33469.1, RC ECO:0000313|Proteomes:UP000010390}; RG US DOE Joint Genome Institute; RA Gugger M., Coursin T., Rippka R., Tandeau De Marsac N., Huntemann M., RA Wei C.-L., Han J., Detter J.C., Han C., Tapia R., Teshima H., Chen A., RA Krypides N., Mavromatis K., Markowitz V., Szeto E., Ivanova N., RA Ovchinnikova G., Pagani I., Pati A., Goodwin L., Peters L., RA Pitluck S., Woyke T., Kerfeld C.; RT "Finished genome of Calothrix sp. PCC 7507."; RL Submitted (APR-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP003943; AFY33469.1; -; Genomic_DNA. DR EnsemblBacteria; AFY33469; AFY33469; Cal7507_3056. DR KEGG; calo:Cal7507_3056; -. DR PATRIC; fig|99598.3.peg.3463; -. DR KO; K03665; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000010390; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000010390}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000010390}. FT DOMAIN 408 578 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 367 401 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 583 AA; 64454 MW; 3F02CF2C27F6B498 CRC64; METIFGNLQG LKSSQLKQLQ RLYHQRIPGD TITTSDFSQR LAAISTELNQ PVCAYLNRRG QVIRVGVGTP RQTQIPPLEL PRYGAERLSG IRCIATNLKP EPPNEAALTA MAMQRLDVLV VLNITGTGFT RRGGGAAGYI KEAYLAHLTP QDSRALITSP SLLKVESNNV QSPSWTVSSP LSIDDLALQD FLELVENLEA EFQREFVAQE VDADHDRVLL VGVITDQITP QRFQDTLAEL ARLVDTAGGD VLQTLQQKRS RIHPQTVVGE GKVQEVALTA QTIGANLVVF DRDLSPSQVR NLEAQIGVRV VDRTEVILDI FAQRAQSRAG KLQVELAQLE YMQPRLTGRG RTMSRLGGGI GTRGPGETKL ETERRAIQQR ISRLQKEVNQ LQAHRSRLRQ RRQHQEVPSV ALVGYTNAGK STLLNALTNA EVYTADQLFA TLDPTTRRLV IPNSSTSEPQ EILITDTVGF IHELPPSLMD AFRATLEEVT EADGLLHLVD LSHPAWLSHI RSVREILAQM PITPGPALVA FNKIDQVSSE TLALAREEFP LAVFISASQR LGLETLRQRL AQLIQYAVNS GKY // ID K9PYP4_9CYAN Unreviewed; 566 AA. AC K9PYP4; DT 06-MAR-2013, integrated into UniProtKB/TrEMBL. DT 06-MAR-2013, sequence version 1. DT 07-JUN-2017, entry version 32. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=Lepto7376_1587 {ECO:0000313|EMBL:AFY37924.1}; OS Leptolyngbya sp. PCC 7376. OC Bacteria; Cyanobacteria; Synechococcales; Leptolyngbyaceae; OC Leptolyngbya. OX NCBI_TaxID=111781 {ECO:0000313|EMBL:AFY37924.1, ECO:0000313|Proteomes:UP000010389}; RN [1] {ECO:0000313|EMBL:AFY37924.1, ECO:0000313|Proteomes:UP000010389} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=PCC 7376 {ECO:0000313|Proteomes:UP000010389}; RG US DOE Joint Genome Institute; RA Gugger M., Coursin T., Rippka R., Tandeau De Marsac N., Huntemann M., RA Wei C.-L., Han J., Detter J.C., Han C., Tapia R., Teshima H., Chen A., RA Krypides N., Mavromatis K., Markowitz V., Szeto E., Ivanova N., RA Mikhailova N., Pagani I., Pati A., Goodwin L., Peters L., Pitluck S., RA Woyke T., Kerfeld C.; RT "Finished genome of Leptolyngbya sp. PCC 7376."; RL Submitted (APR-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP003946; AFY37924.1; -; Genomic_DNA. DR RefSeq; WP_015133694.1; NC_019683.1. DR EnsemblBacteria; AFY37924; AFY37924; Lepto7376_1587. DR KEGG; lep:Lepto7376_1587; -. DR PATRIC; fig|111781.3.peg.1814; -. DR KO; K03665; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000010389; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000010389}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Hydrolase {ECO:0000313|EMBL:AFY37924.1}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000010389}. FT DOMAIN 398 566 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 357 394 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 566 AA; 63155 MW; BE93A8492B6562F0 CRC64; MRETPINTSI YGSLKGLKSS QLKQLQRLYQ QSVPSDRLTT PELAQRIAAL STDLNQSVCV YLNRRGKVIR VGVGSPRQTQ IPAIELPRYG AERLSGIRCL AATPKDVPPK ESSLTAMVLQ RLDALVTFTL TQTGTTKRGR GATGYVKNGY VAHLLPQTHP SHEYWEVSDA EPLEAIAEQD FLDLVEGLEE EFRREFTAQK VDQTHDRVIL VGLQTDGIKD QRFTDGLTEL ARLVDTAGGE VLLTMEQRRS HPHPQTLVGS GKVDDIALQI QTLGASLVVF DQDLSPAQSR NLERKFGVKV CDRTEVILDI FAQRAQSRAG KLQVELAQLE YMLPRLTGRG QAMSRLGGGI GTRGPGETKL ETERRTIQNR LSRLQKEVDQ LQAHRSRMRN QRQRQDVPTF SIVGYTNAGK STLINALTNA EVYAADQLFA TLDPTTRRLT LTDDDHQART ILLTDTVGFI HELPPALVDA FRATLEEVTE ADALIHVIDL SHPAWQHQLH SVEKILEEMP IMPAQALLVF NKLDQVPSEA LDTAKTLYPH AIFISAGDRL GFETLRQRLT QMLKHL // ID K9QI54_9NOSO Unreviewed; 571 AA. AC K9QI54; DT 06-MAR-2013, integrated into UniProtKB/TrEMBL. DT 06-MAR-2013, sequence version 1. DT 07-JUN-2017, entry version 32. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=Nos7107_4538 {ECO:0000313|EMBL:AFY45068.1}; OS Nostoc sp. PCC 7107. OC Bacteria; Cyanobacteria; Nostocales; Nostocaceae; Nostoc. OX NCBI_TaxID=317936 {ECO:0000313|EMBL:AFY45068.1, ECO:0000313|Proteomes:UP000010381}; RN [1] {ECO:0000313|EMBL:AFY45068.1, ECO:0000313|Proteomes:UP000010381} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=PCC 7107 {ECO:0000313|EMBL:AFY45068.1, RC ECO:0000313|Proteomes:UP000010381}; RG US DOE Joint Genome Institute; RA Gugger M., Coursin T., Rippka R., Tandeau De Marsac N., Huntemann M., RA Wei C.-L., Han J., Detter J.C., Han C., Tapia R., Davenport K., RA Daligault H., Erkkila T., Gu W., Munk A.C.C., Teshima H., Xu Y., RA Chain P., Chen A., Krypides N., Mavromatis K., Markowitz V., Szeto E., RA Ivanova N., Mikhailova N., Ovchinnikova G., Pagani I., Pati A., RA Goodwin L., Peters L., Pitluck S., Woyke T., Kerfeld C.; RT "Finished genome of Nostoc sp. PCC 7107."; RL Submitted (AUG-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP003548; AFY45068.1; -; Genomic_DNA. DR EnsemblBacteria; AFY45068; AFY45068; Nos7107_4538. DR KEGG; nos:Nos7107_4538; -. DR PATRIC; fig|317936.3.peg.4921; -. DR KO; K03665; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000010381; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000010381}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Hydrolase {ECO:0000313|EMBL:AFY45068.1}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000010381}. FT DOMAIN 398 568 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 357 391 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 571 AA; 63089 MW; 0C5088553FAB6CB3 CRC64; MQGLKSSQLK QLQRLYHQRI PGDRITTPEF SQRLAAISTE INQPVCAYLN RRGQVIRVGV GTPRQTQIPP LELPRYGAER LSGIRCIATH LKSEPPNEVA LTAMAMQRLD ALVMLNITGT GFTRRGGGAT GYVKEAYLAH LVSDTKQLVA AQNSALGTQN SAIYSSISPP MSLDMLAEQD FIDLVEGLEE EFRREFVAQE VDADHDRVLI VAVMTDQLTP QQFHDTIAEL GRLVDTAGGD VLHTVQQKRS RIHPQTVIGE GKVQEVALTA QTLGCNLVVF DRDLSPSQVR NLEAQIGVRV VDRTEVILDI FAQRAQSRAG KLQVELAQLG YMLPRLTGRG RAMSRLGGGI GTRGPGETKL ETERRAIQRR ISRLQQEVDQ LQAHRSRLRQ RRQHQEVPSV ALVGYTNAGK STSLNALTNA EVYTADQLFA TLDPTTRRLV IPHADTNEPQ EILITDTVGF IHELPASLMD AFRATLEEVT EADALLHLVD LSHPAWLSHI RSVREILAAM PVTPGPALVA FNKIDQVDSE TLAIAREEFP LAVFISASER LGLETLRLRL SQLIAYAVEP K // ID K9QWD1_NOSS7 Unreviewed; 590 AA. AC K9QWD1; DT 06-MAR-2013, integrated into UniProtKB/TrEMBL. DT 06-MAR-2013, sequence version 1. DT 07-JUN-2017, entry version 29. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Nos7524_3588 {ECO:0000313|EMBL:AFY49379.1}; OS Nostoc sp. (strain ATCC 29411 / PCC 7524). OC Bacteria; Cyanobacteria; Nostocales; Nostocaceae; Nostoc. OX NCBI_TaxID=28072 {ECO:0000313|EMBL:AFY49379.1, ECO:0000313|Proteomes:UP000010378}; RN [1] {ECO:0000313|Proteomes:UP000010378} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29411 / PCC 7524 {ECO:0000313|Proteomes:UP000010378}; RX PubMed=23277585; DOI=10.1073/pnas.1217107110; RA Shih P.M., Wu D., Latifi A., Axen S.D., Fewer D.P., Talla E., RA Calteau A., Cai F., Tandeau de Marsac N., Rippka R., Herdman M., RA Sivonen K., Coursin T., Laurent T., Goodwin L., Nolan M., RA Davenport K.W., Han C.S., Rubin E.M., Eisen J.A., Woyke T., Gugger M., RA Kerfeld C.A.; RT "Improving the coverage of the cyanobacterial phylum using diversity- RT driven genome sequencing."; RL Proc. Natl. Acad. Sci. U.S.A. 110:1053-1058(2013). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP003552; AFY49379.1; -; Genomic_DNA. DR EnsemblBacteria; AFY49379; AFY49379; Nos7524_3588. DR KEGG; nop:Nos7524_3588; -. DR PATRIC; fig|28072.8.peg.3929; -. DR KO; K03665; -. DR OMA; EREVIIT; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000010378; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000010378}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000010378}. FT DOMAIN 417 590 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 376 410 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 590 AA; 65093 MW; 7D66FC6A5AA1009C CRC64; MRGASLLVET PIETIFGNLQ GLKSSQLKQL QRLYHQRIPG DRITTPEFSQ RLAAISTEIN LPVCAYVNRR GQVIRVGVGT PRQTQIPPME LPRYGAERLS GIRCIATHLK AEPPNEAALT AMAMQRLDAL AVINITGTGF TRRGGGATGY VKEAYLAHLV PQDARALIPS AAFSGSKNVQ SPSWSVSPPL NLDDLAQQDF IDLVEGLEEE FRREFVAQEV DADHDRVLIV GVMTDEMSLQ QFHDTLAELA RLVDTAGGDV LQTVQQKRSR IHPQTVIGEG KVQEVALTAQ TLGCNLVVFD RDLSPAQVRN LEAQIGIRVV DRTEVILDIF AQRAQSGAGK LQVELAQLEY MLPRLTGRGQ AMSRLGGGIG TRGPGETKLE TERRAIQRRI SRLQQEVNQL QAHRSRLRQR RQHREVPSVA LVGYTNAGKS TLLNALTNAE VYTADQLFAT LDPTTRRLVI PGAENGETQE ILITDTVGFI HELPASLMDA FRATLEEVTE ADALLHLVDL SHPAWLSHIR SVREILAQMP ITPGPALVAF NKIDQVDSQT LALAREEFPL AVFISASQRL GLETLRHRLS QLIQYAVDLR // ID K9R6K9_9CYAN Unreviewed; 582 AA. AC K9R6K9; DT 06-MAR-2013, integrated into UniProtKB/TrEMBL. DT 06-MAR-2013, sequence version 1. DT 07-JUN-2017, entry version 33. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=Riv7116_0970 {ECO:0000313|EMBL:AFY53545.1}; OS Rivularia sp. PCC 7116. OC Bacteria; Cyanobacteria; Nostocales; Rivulariaceae; Rivularia. OX NCBI_TaxID=373994 {ECO:0000313|EMBL:AFY53545.1, ECO:0000313|Proteomes:UP000010380}; RN [1] {ECO:0000313|EMBL:AFY53545.1, ECO:0000313|Proteomes:UP000010380} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=PCC 7116 {ECO:0000313|EMBL:AFY53545.1, RC ECO:0000313|Proteomes:UP000010380}; RG US DOE Joint Genome Institute; RA Gugger M., Coursin T., Rippka R., Tandeau De Marsac N., Huntemann M., RA Wei C.-L., Han J., Detter J.C., Han C., Tapia R., Chen A., RA Kyrpides N., Mavromatis K., Markowitz V., Szeto E., Ivanova N., RA Pagani I., Pati A., Goodwin L., Nordberg H.P., Cantor M.N., Hua S.X., RA Woyke T., Kerfeld C.A.; RT "Finished chromosome of genome of Rivularia sp. PCC 7116."; RL Submitted (AUG-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP003549; AFY53545.1; -; Genomic_DNA. DR RefSeq; WP_015117123.1; NC_019678.1. DR EnsemblBacteria; AFY53545; AFY53545; Riv7116_0970. DR KEGG; riv:Riv7116_0970; -. DR PATRIC; fig|373994.3.peg.1025; -. DR KO; K03665; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000010380; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000010380}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000010380}. FT DOMAIN 409 579 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 368 402 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 582 AA; 64564 MW; D193AAC0BF299CE9 CRC64; MPIETIFGNL QGLKHSQQKQ LQRLYHQRIP GDSFTTPEFA QRLAAISSEI NQPVCAYLNR RGQVIRVGVG TPRKTQIPLT ELPRYGAERL SGIRCIATQL KPEYPSDGAL TAMALQRLDA LVVLNITATG FQRRGGGATG YVKEAYLAHL APEDTRTLIA SQNPQLETSD YSSPSWSVSP PMSLDALSKQ DFLDLVEGLE EEFQREFVGK EVDSDRDRVV IVGVVTQKDT PQQFQDTLKE LGRLVDTAGG EVLQMMRQKR SRIHPQTVVG EGKVQEIALS VQTLGANLVV FDRDLSPAQV RNLEAQIGVR VVDRTEVILD IFAQRARSGA GKLQVELAQL EYMLPRLTGR GQAMSRLGGG IGTRGPGETK LETERRAISR RITRLQKEVN QLQAHRERLR QRRQHREIPT IAIVGYTNAG KSTLLNALTN ASVYTADQLF ATLDPTTRRL VVPHAVTNEA QEILVTDTVG FIHELPEALM DAFRATLEEV TEADALVHLV DLSHPAWLSH IRSVRDILAQ MPVTPGPGLV VFNKIDRANS ETLALAREEY PMAVFISAYE RLGLETLRER LAQLIQYATA SG // ID K9S566_9CYAN Unreviewed; 564 AA. AC K9S566; DT 06-MAR-2013, integrated into UniProtKB/TrEMBL. DT 06-MAR-2013, sequence version 1. DT 07-JUN-2017, entry version 32. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=GEI7407_0850 {ECO:0000313|EMBL:AFY65348.1}; OS Geitlerinema sp. PCC 7407. OC Bacteria; Cyanobacteria; Oscillatoriophycideae; Oscillatoriales; OC Coleofasciculaceae; Geitlerinema. OX NCBI_TaxID=1173025 {ECO:0000313|EMBL:AFY65348.1, ECO:0000313|Proteomes:UP000010383}; RN [1] {ECO:0000313|EMBL:AFY65348.1, ECO:0000313|Proteomes:UP000010383} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=PCC 7407 {ECO:0000313|EMBL:AFY65348.1, RC ECO:0000313|Proteomes:UP000010383}; RG US DOE Joint Genome Institute; RA Gugger M., Coursin T., Rippka R., Tandeau De Marsac N., Huntemann M., RA Wei C.-L., Han J., Detter J.C., Han C., Tapia R., Davenport K., RA Daligault H., Erkkila T., Gu W., Munk A.C.C., Teshima H., Xu Y., RA Chain P., Chen A., Krypides N., Mavromatis K., Markowitz V., Szeto E., RA Ivanova N., Mikhailova N., Ovchinnikova G., Pagani I., Pati A., RA Goodwin L., Peters L., Pitluck S., Woyke T., Kerfeld C.; RT "Finished genome of Geitlerinema sp. PCC 7407."; RL Submitted (MAY-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP003591; AFY65348.1; -; Genomic_DNA. DR RefSeq; WP_015170915.1; NC_019703.1. DR EnsemblBacteria; AFY65348; AFY65348; GEI7407_0850. DR KEGG; gei:GEI7407_0850; -. DR PATRIC; fig|1173025.3.peg.959; -. DR KO; K03665; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000010383; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000010383}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Hydrolase {ECO:0000313|EMBL:AFY65348.1}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000010383}. FT DOMAIN 389 559 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 348 385 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 564 AA; 62192 MW; C4F3297C582CDF98 CRC64; MDTIYGNLQG LKSSQIKQIQ RLYHQRLPGD RFTTSDFAQR LAAISTEIGQ PLCVYINRRG QVIRVGVGTP IQTQIPPLEL PRYGAERLCG IRCIATQRDT SPPSTAVLTA MALQRLDALV VLGLSGSGFE RRGGGASGYV REVHLAHLVP HPETTWTVSP PLSLDLLSQQ DFLDLVEGLE AEFEREYVAQ QVDADHDRVL LVGLMTSSVT AARFQDNLAE LVRLVESAGG EVLQITHQRR NQPHPQIVVG EGKVQEITLL AQTVGANLIV FDRDLSPAQI RNLETRIGVR VVDRTEVILD IFAQHAQSRA GKLQVELAQL EYMMPRLTGR GRTMSRLGGG IGTRGPGETK LETERRAIQR RIARLQQEVN QLQAHRARLR QQRQHQEVPS VAIVGYTNAG KSTLLNALTN AEVYTADQLF ATLDPTSRRL IVPDAATHEP RTVILTDTVG FIHELPPSLV DAFRATLEEV TEADALLHVV DLSHDAWQNQ LRSVMKILSE MPVTPGPSLV VFNKIDQVGS DALAIAQEEY PHGVFVSAGA RLGLETLRQR IAQLVQYALA PSQP // ID K9SI50_9CYAN Unreviewed; 588 AA. AC K9SI50; DT 06-MAR-2013, integrated into UniProtKB/TrEMBL. DT 06-MAR-2013, sequence version 1. DT 07-JUN-2017, entry version 34. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=Pse7367_1521 {ECO:0000313|EMBL:AFY69810.1}; OS Pseudanabaena sp. PCC 7367. OC Bacteria; Cyanobacteria; Synechococcales; Pseudanabaenaceae; OC Pseudanabaena. OX NCBI_TaxID=82654 {ECO:0000313|EMBL:AFY69810.1, ECO:0000313|Proteomes:UP000010386}; RN [1] {ECO:0000313|EMBL:AFY69810.1, ECO:0000313|Proteomes:UP000010386} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=PCC 7367 {ECO:0000313|EMBL:AFY69810.1, RC ECO:0000313|Proteomes:UP000010386}; RG US DOE Joint Genome Institute; RA Gugger M., Coursin T., Rippka R., Tandeau De Marsac N., Huntemann M., RA Wei C.-L., Han J., Detter J.C., Han C., Tapia R., Davenport K., RA Daligault H., Erkkila T., Gu W., Munk A.C.C., Teshima H., Xu Y., RA Chain P., Chen A., Krypides N., Mavromatis K., Markowitz V., Szeto E., RA Ivanova N., Mikhailova N., Ovchinnikova G., Pagani I., Pati A., RA Goodwin L., Peters L., Pitluck S., Woyke T., Kerfeld C.; RT "Finished chromosome of genome of Pseudanabaena sp. PCC 7367."; RL Submitted (MAY-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP003592; AFY69810.1; -; Genomic_DNA. DR RefSeq; WP_015164779.1; NC_019701.1. DR EnsemblBacteria; AFY69810; AFY69810; Pse7367_1521. DR KEGG; pseu:Pse7367_1521; -. DR PATRIC; fig|82654.3.peg.1751; -. DR KO; K03665; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000010386; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000010386}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000010386}. FT DOMAIN 418 585 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 384 411 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 588 AA; 65541 MW; 8AD421B1E7AF00F3 CRC64; MSTIYGHTQG LKPSQLKQIQ RLYRRRVPAP TFITPEFAQR LANISAEIKA PLCIFIDRRG HVVRVGVGTL QQTKIPPAEL PRYGDERLSG LRCIGTKLKS APPSTADLSA MAMQRLDAFV ALTLNKSGYV DRGYVAHLVP NTAAEHESTT WTVLPPQSLD AISKQDFLEL VFNLEAEFSR EFTAQAVEIE QDLAIIVGLI SDRHKNRHQN RHQNRQKGKH KYADRSNHSD RADRSDRQEP IDPHTSLLEM QQLVESAGGQ VLDLIAQKRD RPHPQTVIGQ GKVEEIALAA QAQRANLIVF NQELSPAQTR NLERLLGIRV SDRTEVILDI FAQRAQSAAG KLQVELAQLE YRLPRLSGRG QALSRLGGGI GTRGPGETKL ESDRRTIQKR ISHLQRQVNQ LQAQRDRMRQ RRVKQEIPTV AIVGYTNAGK STLLNSLTKS TAYAADQLFA TLDPTTRRLN IAGHEPILLT DTVGFIHELP PPLVDAFRAT LEEVTEADAL LHVVDASHPA WLDQVRSVNQ ILAEMPIAVG PVLLAFNKCD RMEDFGAIQD FIRTENVNAV LISATKRKGF EDLQQGLIKL VSYAVGKF // ID K9SXF3_9SYNE Unreviewed; 559 AA. AC K9SXF3; DT 06-MAR-2013, integrated into UniProtKB/TrEMBL. DT 06-MAR-2013, sequence version 1. DT 07-JUN-2017, entry version 34. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=Syn7502_03448 {ECO:0000313|EMBL:AFY75297.1}; OS Synechococcus sp. PCC 7502. OC Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; OC Synechococcus. OX NCBI_TaxID=1173263 {ECO:0000313|EMBL:AFY75297.1, ECO:0000313|Proteomes:UP000010385}; RN [1] {ECO:0000313|EMBL:AFY75297.1, ECO:0000313|Proteomes:UP000010385} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=PCC 7502 {ECO:0000313|EMBL:AFY75297.1, RC ECO:0000313|Proteomes:UP000010385}; RG US DOE Joint Genome Institute; RA Gugger M., Coursin T., Rippka R., Tandeau De Marsac N., Huntemann M., RA Wei C.-L., Han J., Detter J.C., Han C., Tapia R., Davenport K., RA Daligault H., Erkkila T., Gu W., Munk A.C.C., Teshima H., Xu Y., RA Chain P., Chen A., Krypides N., Mavromatis K., Markowitz V., Szeto E., RA Ivanova N., Mikhailova N., Ovchinnikova G., Pagani I., Pati A., RA Goodwin L., Peters L., Pitluck S., Woyke T., Kerfeld C.; RT "Finished chromosome of genome of Synechococcus sp. PCC 7502."; RL Submitted (MAY-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP003594; AFY75297.1; -; Genomic_DNA. DR RefSeq; WP_015169948.1; NC_019702.1. DR EnsemblBacteria; AFY75297; AFY75297; Syn7502_03448. DR KEGG; synp:Syn7502_03448; -. DR PATRIC; fig|1173263.3.peg.3574; -. DR KO; K03665; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000010385; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000010385}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000010385}. FT DOMAIN 389 558 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 355 382 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 559 AA; 62233 MW; B03BFF33E783F6A8 CRC64; MENIYGDTQG LKPSQIKQLE RLYRQRLPIE SLTTPEFAQR LAGISSDINK PVCVFVNRRG QVIRVGLGTP NHAKIPLMEL PRYGEERLCG LRCIATNLKH EPPSITDLTA MAMQRLDSLI TVTITSKGYV DRAYTAHILP ESIDGESWYV SPPQSLDAVS KQDFLELVSG LEDQFRREYK AQVVEDEQDR VILVGLITSD ASYRSSHKKS TQKPQELLSE LGQLVDSAGG VVLSTILQKR DRPHPQTVLG EGKVQEIALA AQTQGANLIV FDRELSPAQI RNLERLMGIR VSDRTEVILD IFAQRAQSAA GKLQVELAQL QYRLPRLAGR GMALSRLGGG IGTRGPGETK LETDRRVIQK RITQLQHQVD QLQSQRARMR QQRIDQEIPT VAIVGYTNAG KSTLLNALTK STVYAADKLF ATLDPTTRRL HIRDQEHDPN PQTILITDTV GFIHELPPPL VNAFRATLEE VTEADVLIHL VDISHEAWES QLEAVNQILA DMPIAVGATL TVFNKIDAVP DLDEIKAKYP DAIYVSAMQR QGLDQLLQEL ITVVKAEVS // ID K9T7L5_9CYAN Unreviewed; 569 AA. AC K9T7L5; DT 06-MAR-2013, integrated into UniProtKB/TrEMBL. DT 06-MAR-2013, sequence version 1. DT 07-JUN-2017, entry version 36. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=Ple7327_2859 {ECO:0000313|EMBL:AFY78116.1}; OS Pleurocapsa sp. PCC 7327. OC Bacteria; Cyanobacteria; Pleurocapsales; Hyellaceae; Pleurocapsa. OX NCBI_TaxID=118163 {ECO:0000313|EMBL:AFY78116.1, ECO:0000313|Proteomes:UP000010382}; RN [1] {ECO:0000313|EMBL:AFY78116.1, ECO:0000313|Proteomes:UP000010382} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=PCC 7327 {ECO:0000313|EMBL:AFY78116.1, RC ECO:0000313|Proteomes:UP000010382}; RG US DOE Joint Genome Institute; RA Gugger M., Coursin T., Rippka R., Tandeau De Marsac N., Huntemann M., RA Wei C.-L., Han J., Detter J.C., Han C., Tapia R., Chen A., RA Kyrpides N., Mavromatis K., Markowitz V., Szeto E., Ivanova N., RA Pagani I., Pati A., Goodwin L., Nordberg H.P., Cantor M.N., Hua S.X., RA Woyke T., Kerfeld C.A.; RT "Finished genome of Pleurocapsa sp. PCC 7327."; RL Submitted (MAY-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP003590; AFY78116.1; -; Genomic_DNA. DR EnsemblBacteria; AFY78116; AFY78116; Ple7327_2859. DR KEGG; plp:Ple7327_2859; -. DR PATRIC; fig|118163.3.peg.3186; -. DR KO; K03665; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000010382; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000010382}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000010382}. FT DOMAIN 397 567 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 356 393 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 569 AA; 63434 MW; 5229A160331AC43D CRC64; MPIDTIYGNL QGLKPSQIKQ LQRLYHQRLP GDRFTTPEFA QRLAAISTEI DRPVCAYVNR RGQIVRVGIG TPRQTQIPAL ELPRYGAERL CGIRCIATKL KAEPPKEASL TAMVLQRLDA LVVLTLTGTG FERRGGGATG YVKEAFIAHL LPPSDLNPDN RYYWTVSAPM NLDVLARQDF LDLVEGLEAE FQREYVAQQV DADRDRAIVV GLKTEDMSDD EFKTGLAELE RLVDTAGGEV LDTIRQKRPR PDSQTVVGAG KVEEIALKVQ TLGANLVVFD RDLSPAQVRN LETQFGIRVV DRTEVILDIF AQRAQSRAGK LQVELAQLEY MLPRLTGRGR AMSRLGGGIG TRGPGETKLE TERRTIQRRI ARLQQEVNEL QAHRSRLRKQ RQKKEVPSVA IVGYTNAGKS TLINALTNAE VYVADRLFAT LDPTTRRLLV PDPETGESRT ILLTDTVGFI HELPPSLVDA FRATLEEVTE ADALLHVVDL SHRAWHAQLR SVMAILAEMP LTPGPMLIAF NKIDRVDSET LERAKEEFPL AVFISATERF GLETLTEKLG QLVHYAMAQ // ID K9TKU9_9CYAN Unreviewed; 571 AA. AC K9TKU9; DT 06-MAR-2013, integrated into UniProtKB/TrEMBL. DT 06-MAR-2013, sequence version 1. DT 07-JUN-2017, entry version 33. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=Oscil6304_3175 {ECO:0000313|EMBL:AFY82756.1}; OS Oscillatoria acuminata PCC 6304. OC Bacteria; Cyanobacteria; Oscillatoriophycideae; Oscillatoriales; OC Oscillatoriaceae; Oscillatoria. OX NCBI_TaxID=56110 {ECO:0000313|EMBL:AFY82756.1, ECO:0000313|Proteomes:UP000010367}; RN [1] {ECO:0000313|EMBL:AFY82756.1, ECO:0000313|Proteomes:UP000010367} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=PCC 6304 {ECO:0000313|EMBL:AFY82756.1, RC ECO:0000313|Proteomes:UP000010367}; RG US DOE Joint Genome Institute; RA Gugger M., Coursin T., Rippka R., Tandeau De Marsac N., Huntemann M., RA Wei C.-L., Han J., Detter J.C., Han C., Tapia R., Davenport K., RA Daligault H., Erkkila T., Gu W., Munk A.C.C., Teshima H., Xu Y., RA Chain P., Chen A., Krypides N., Mavromatis K., Markowitz V., Szeto E., RA Ivanova N., Mikhailova N., Ovchinnikova G., Pagani I., Pati A., RA Goodwin L., Peters L., Pitluck S., Woyke T., Kerfeld C.; RT "Finished chromosome of genome of Oscillatoria acuminata PCC 6304."; RL Submitted (JUN-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP003607; AFY82756.1; -; Genomic_DNA. DR RefSeq; WP_015149389.1; NC_019693.1. DR EnsemblBacteria; AFY82756; AFY82756; Oscil6304_3175. DR KEGG; oac:Oscil6304_3175; -. DR PATRIC; fig|56110.3.peg.3786; -. DR KO; K03665; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000010367; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000010367}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Hydrolase {ECO:0000313|EMBL:AFY82756.1}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000010367}. FT DOMAIN 399 568 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 358 392 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 571 AA; 62655 MW; 8FE288B3C167849A CRC64; METIYGQLQG LKSSQLKQLN RLYHQKLPVD AITTSEFAQR LAAISTEIND SLCVYINRRG QVIRVGVGSP RQTQIPAMEL PRYGEGRLSG IRCITTQLKG EGPSESSLTA MAIQRLDALV VLNLTGEGFE RRGGGATGYV SQSYLAHLIP QTGMDEGEGD GPIATWTVSP PMSLDALSLQ DFLELVEGLE AEFQREFIAR DVDADHDRAL LVGVMTHNLK DEQFEDGLTE LARLVDTAGG TVLQTMRQKR PRLHPQTVVG KGKVEEIALT AQTLGSNLIV FDRELSPAQV RNLEVQIGVR VVDRTEVILD IFAQRAQSGA GKLQVELAQL EYMLPRLTGR GQAMSRLGGG IGTRGPGETK LETERRAIQR RIARLQQEVN ELQAHRSRMR LRRQHQDVPS VAIVGYTNAG KSTLLNALTN AEIYTADQLF ATLDPTTRRL VIPTVLGSTQ TIVVTDTVGF IHELPPSLMD AFRATLEEVT EADALLHVVD LSHPAWQSQI RSVMKILGEM PVTPGPALVA FNKIDAVDGD TLAIAKEEFP LAVFICASQR LGLETLRQRL AQLIDYAVAP Q // ID K9U528_9CYAN Unreviewed; 593 AA. AC K9U528; DT 06-MAR-2013, integrated into UniProtKB/TrEMBL. DT 06-MAR-2013, sequence version 1. DT 07-JUN-2017, entry version 34. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=Chro_4337 {ECO:0000313|EMBL:AFY89733.1}; OS Chroococcidiopsis thermalis PCC 7203. OC Bacteria; Cyanobacteria; Chroococcidiopsidales; OC Chroococcidiopsidaceae; Chroococcidiopsis. OX NCBI_TaxID=251229 {ECO:0000313|EMBL:AFY89733.1, ECO:0000313|Proteomes:UP000010384}; RN [1] {ECO:0000313|EMBL:AFY89733.1, ECO:0000313|Proteomes:UP000010384} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=PCC 7203 {ECO:0000313|EMBL:AFY89733.1, RC ECO:0000313|Proteomes:UP000010384}; RG US DOE Joint Genome Institute; RA Gugger M., Coursin T., Rippka R., Tandeau De Marsac N., Huntemann M., RA Wei C.-L., Han J., Detter J.C., Han C., Tapia R., Davenport K., RA Daligault H., Erkkila T., Gu W., Munk A.C.C., Teshima H., Xu Y., RA Chain P., Chen A., Krypides N., Mavromatis K., Markowitz V., Szeto E., RA Ivanova N., Mikhailova N., Ovchinnikova G., Pagani I., Pati A., RA Goodwin L., Peters L., Pitluck S., Woyke T., Kerfeld C.; RT "Finished chromosome of genome of Chroococcidiopsis thermalis PCC RT 7203."; RL Submitted (JUN-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP003597; AFY89733.1; -; Genomic_DNA. DR EnsemblBacteria; AFY89733; AFY89733; Chro_4337. DR KEGG; cthe:Chro_4337; -. DR PATRIC; fig|251229.3.peg.5064; -. DR KO; K03665; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000010384; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000010384}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Hydrolase {ECO:0000313|EMBL:AFY89733.1}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000010384}. FT DOMAIN 420 590 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 379 416 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 593 AA; 64881 MW; 5228D059DC28318C CRC64; METIYGNLQG LKSSQLKQLA KLYHQRLPGD RLTTPEFAQR LAAISSDINQ PVCVYINRRG QAIRVGVGTP RQTQIPPLEL PRYGAERLSG IRCIATQLKP EPPNEAALTS MALQRLDALV TLNITSAGFE KRGGGVTGYV KEAYLSHLVP STSIESPLPY GRDSKPAPTD SVRAHSGAPL PTLQTAWSIS PPLSLDSLTK QDFLDLVEGL EAEFGREFVG QQVDTDRDRV LLVGVVTDNA AAREFQDRLA ELGRLVETAG GEVLQVVQQK RPHIHPQTVV GAGKVQEIAL TAQTLGANLI VFDRDLSPAQ VRNLEIQIGI RVVDRTEVIL DIFAQRAQSR AGKLQVELAQ LEYMLPRLTG RGQAMSRLGG GIGTRGPGET KLETERRAIS RRISRLQQEV NQLQAHRSRL RQQRQHQEVP SIALVGYTNA GKSTLLNALT NAEVYTADQL FATLDPTTRR LVITDADTGT PQEIVLTDTV GFIHELPASL MDAFRATLEE VTEADALLHV VDLSHPAWQS QIRAVMGILS EMPVTPGPIL LALNKIDQAD SDTLALAQSE FPQAVFISAE NRLGLETLRQ RLLQLAKYAD ATV // ID K9UH71_9CYAN Unreviewed; 510 AA. AC K9UH71; DT 06-MAR-2013, integrated into UniProtKB/TrEMBL. DT 06-MAR-2013, sequence version 1. DT 07-JUN-2017, entry version 31. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=Cha6605_3460 {ECO:0000313|EMBL:AFY94452.1}; OS Chamaesiphon minutus PCC 6605. OC Bacteria; Cyanobacteria; Synechococcales; Chamaesiphonaceae; OC Chamaesiphon. OX NCBI_TaxID=1173020 {ECO:0000313|EMBL:AFY94452.1, ECO:0000313|Proteomes:UP000010366}; RN [1] {ECO:0000313|EMBL:AFY94452.1, ECO:0000313|Proteomes:UP000010366} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=PCC 6605 {ECO:0000313|EMBL:AFY94452.1, RC ECO:0000313|Proteomes:UP000010366}; RG US DOE Joint Genome Institute; RA Gugger M., Coursin T., Rippka R., Tandeau De Marsac N., Huntemann M., RA Wei C.-L., Han J., Detter J.C., Han C., Tapia R., Chen A., RA Kyrpides N., Mavromatis K., Markowitz V., Szeto E., Ivanova N., RA Pagani I., Pati A., Goodwin L., Nordberg H.P., Cantor M.N., Hua S.X., RA Woyke T., Kerfeld C.A.; RT "Finished chromosome of genome of Chamaesiphon sp. PCC 6605."; RL Submitted (MAY-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP003600; AFY94452.1; -; Genomic_DNA. DR EnsemblBacteria; AFY94452; AFY94452; Cha6605_3460. DR KEGG; cmp:Cha6605_3460; -. DR PATRIC; fig|1173020.3.peg.3972; -. DR KO; K03665; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000010366; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000010366}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000010366}. FT DOMAIN 338 508 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 297 331 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 510 AA; 56316 MW; 3462D76C2413CC2C CRC64; MSVYINRRGQ IIRLGVGTPR QTQIPPLELP RYGAERLSGI RCISTQLKPE IPSESALTSM ALQRLDALVI LNITGSGFQK RGGGATGYIQ DTYLAHLVPH PEINWTISPP LSLDAVSDQD FLDLVDGIES EYARDIANQN VADEIDRVLL VGVKTDYVTT QRFNDGLEEL VRLVETAGGE VLQTVQQKRS KPHPQTVVGE GKIQEIALAA QKIGANLIVF DCNLSPSQGR NLETQIGIRV VDRTEVILDI FAQRAQSGAG KLQVELAQLE YMLPRLTGRG LAMSRQGGGI GTRGPGETKL ETERRTIQKR ISRLQQDVNQ LQAHRSRLRQ QRQHHDVPSV ALVGYTNAGK STLLNTLTNS EVYIADQLFA TLDPTTRRFN VPTSNTGEQR QILLTDTVGF IHELPPPLMD AFRATLEEVT EADALIHLID LSHPAWHSHI RSVMGILSEM PIAPGPSLIV FNKIDRVDGE RLAQAEEEFP NAVFISASER LSLETLRQRV GQLIAYTVPA // ID K9UWT8_9CYAN Unreviewed; 581 AA. AC K9UWT8; DT 06-MAR-2013, integrated into UniProtKB/TrEMBL. DT 06-MAR-2013, sequence version 1. DT 07-JUN-2017, entry version 32. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=Cal6303_0956 {ECO:0000313|EMBL:AFZ00021.1}; OS Calothrix sp. PCC 6303. OC Bacteria; Cyanobacteria; Nostocales; Rivulariaceae; Calothrix. OX NCBI_TaxID=1170562 {ECO:0000313|EMBL:AFZ00021.1, ECO:0000313|Proteomes:UP000010477}; RN [1] {ECO:0000313|EMBL:AFZ00021.1, ECO:0000313|Proteomes:UP000010477} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=PCC 6303 {ECO:0000313|EMBL:AFZ00021.1, RC ECO:0000313|Proteomes:UP000010477}; RA Gugger M., Coursin T., Rippka R., Tandeau De Marsac N., Huntemann M., RA Wei C.-L., Han J., Detter J.C., Han C., Tapia R., Chen A., RA Kyrpides N., Mavromatis K., Markowitz V., Szeto E., Ivanova N., RA Pagani I., Pati A., Goodwin L., Nordberg H.P., Cantor M.N., Hua S.X., RA Woyke T., Kerfeld C.A.; RT "Finished chromosome of genome of Calothrix sp. PCC 6303."; RL Submitted (MAY-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP003610; AFZ00021.1; -; Genomic_DNA. DR EnsemblBacteria; AFZ00021; AFZ00021; Cal6303_0956. DR KEGG; calt:Cal6303_0956; -. DR PATRIC; fig|1170562.3.peg.1046; -. DR KO; K03665; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000010477; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000010477}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000010477}. FT DOMAIN 408 578 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 367 401 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 581 AA; 64319 MW; 0FB837F7CFEDDE75 CRC64; METIFGNLQG LKTSQLKHLQ RLYHQRVPGD RITTSDFSER LAAISTDIKQ PVCAYLNRRG QVIRVGIGTP RQTQIPLSEL PRYGAERLSG IRCISTQLKA ELPSDAALTA MAMQRLDALV VLNITGTGFT KRGGGATGYV KDVYLAHLNA QLSRVLITSG VSITDEGNAL ATPSWQISPP MSLDEISDQD FMDLVEGLEE EFRREYVAQE VDSKSDRVVI VGVVTDGISP QRFQDVIEEL ARLVDTAGGE VLQTILQKRN RIHPQTVVGE GKVQEIALAA QTLGATLVVF DRNLSPSQAR NLENQIGIRV VDRTEVILDI FAQRAQSRAG KLQVELAQLE YIMPRLRGKG EAMSRLGGGI GTRGPGETKL ETERRTIQKR ISRLQQEVNQ LQAHRSRLRQ RRQHEEIPSV ALVGYTNAGK STLLNALTNA EVYTADQLFA TLDPTTRRLV VPDVVENKPQ EILVTDTVGF IHELPDALMD AFRATLEEVT EADALLHLVD LSHPAWLSHI RAVRDILAEM PVTPGPALVI FNKIDEADSD RLAIAREEFP MAVFISAKQR LGLETLRQRI AQLVHYTALN G // ID K9VAQ5_9CYAN Unreviewed; 597 AA. AC K9VAQ5; DT 06-MAR-2013, integrated into UniProtKB/TrEMBL. DT 06-MAR-2013, sequence version 1. DT 07-JUN-2017, entry version 33. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=Osc7112_0305 {ECO:0000313|EMBL:AFZ04926.1}; OS Oscillatoria nigro-viridis PCC 7112. OC Bacteria; Cyanobacteria; Oscillatoriophycideae; Oscillatoriales; OC Oscillatoriaceae; Oscillatoria. OX NCBI_TaxID=179408 {ECO:0000313|EMBL:AFZ04926.1, ECO:0000313|Proteomes:UP000010478}; RN [1] {ECO:0000313|EMBL:AFZ04926.1, ECO:0000313|Proteomes:UP000010478} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=PCC 7112 {ECO:0000313|EMBL:AFZ04926.1, RC ECO:0000313|Proteomes:UP000010478}; RG US DOE Joint Genome Institute; RA Gugger M., Coursin T., Rippka R., Tandeau De Marsac N., Huntemann M., RA Wei C.-L., Han J., Detter J.C., Han C., Tapia R., Davenport K., RA Daligault H., Erkkila T., Gu W., Munk A.C.C., Teshima H., Xu Y., RA Chain P., Chen A., Krypides N., Mavromatis K., Markowitz V., Szeto E., RA Ivanova N., Mikhailova N., Ovchinnikova G., Pagani I., Pati A., RA Goodwin L., Peters L., Pitluck S., Woyke T., Kerfeld C.; RT "Finished chromosome of genome of Oscillatoria sp. PCC 7112."; RL Submitted (MAY-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP003614; AFZ04926.1; -; Genomic_DNA. DR RefSeq; WP_015174261.1; NC_019729.1. DR EnsemblBacteria; AFZ04926; AFZ04926; Osc7112_0305. DR KEGG; oni:Osc7112_0305; -. DR PATRIC; fig|179408.3.peg.380; -. DR KO; K03665; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000010478; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000010478}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000010478}. FT DOMAIN 424 594 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 383 417 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 597 AA; 66100 MW; 108A31B699749184 CRC64; METIYGNLQG LKSSQLKQLE KLYHQRLPGD RITTAEFAQR VAAISTEIDK PICTYINRRG QVIRVGVGTP RQTQIAPLEL PRYGGGRLSG IRCIATHLKP ETPSEAALTA MAIQRLDALV WLTLTGGGFV RRGGGATGYI QETYLAHLIP QGDRPNFEFS VLSAQLEPDS TDEREEPSIQ KSLIQTPHFP WKISEPLNLE ELADQDFLDL VEGLEAEFEA EFVAKQVDAD QDKVLLVGVM TQHMTQLEFE DGLAEITRLV ESAGGQVLQT VRQKRSRPHP QTVVGEGKVQ EISLAAQTIS ANLVVFDRDL APAQIRNLET QIGIRVVDRT EVILDIFAQR ARSSEGKLQV ELAQLEYALP RLTGRGQAMS RQGGGIGTRG PGETKLETER RTIAKRISRL QQEVNQLLAH RFRLRQNRHH HEVPSVAIVG YTNAGKSTLL NLLTNSEVYA ADQLFATLDP TTRRLTIPGT VTREPLSIVL TDTVGFIREL PPALIDAFRA TLEEVTDADA LLHLVDLSHP AWQSQIRSVM NILTDMPVTP GPALVVFNKI DAVDGETLAL AREEFPQAVF ISAAKGLGME TLRDRLAQLI QYALYPR // ID K9VYH2_9CYAN Unreviewed; 575 AA. AC K9VYH2; DT 06-MAR-2013, integrated into UniProtKB/TrEMBL. DT 06-MAR-2013, sequence version 1. DT 07-JUN-2017, entry version 34. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=Cri9333_1648 {ECO:0000313|EMBL:AFZ12537.1}; OS Crinalium epipsammum PCC 9333. OC Bacteria; Cyanobacteria; Oscillatoriophycideae; Oscillatoriales; OC Gomontiellaceae; Crinalium. OX NCBI_TaxID=1173022 {ECO:0000313|EMBL:AFZ12537.1, ECO:0000313|Proteomes:UP000010472}; RN [1] {ECO:0000313|EMBL:AFZ12537.1, ECO:0000313|Proteomes:UP000010472} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=PCC 9333 {ECO:0000313|EMBL:AFZ12537.1, RC ECO:0000313|Proteomes:UP000010472}; RG US DOE Joint Genome Institute; RA Gugger M., Coursin T., Rippka R., Tandeau De Marsac N., Huntemann M., RA Wei C.-L., Han J., Detter J.C., Han C., Tapia R., Davenport K., RA Daligault H., Erkkila T., Gu W., Munk A.C.C., Teshima H., Xu Y., RA Chain P., Chen A., Krypides N., Mavromatis K., Markowitz V., Szeto E., RA Ivanova N., Mikhailova N., Ovchinnikova G., Pagani I., Pati A., RA Goodwin L., Peters L., Pitluck S., Woyke T., Kerfeld C.; RT "Finished chromosome of genome of Crinalium epipsammum PCC 9333."; RL Submitted (JUN-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP003620; AFZ12537.1; -; Genomic_DNA. DR RefSeq; WP_015202658.1; NC_019753.1. DR EnsemblBacteria; AFZ12537; AFZ12537; Cri9333_1648. DR KEGG; cep:Cri9333_1648; -. DR PATRIC; fig|1173022.3.peg.1780; -. DR KO; K03665; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000010472; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000010472}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000010472}. FT DOMAIN 402 572 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 361 398 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 575 AA; 63721 MW; 284F8DA90F5F2C00 CRC64; MNKIEVDEFK VTHIETIYGN LQGLKASHLK QLQKLYHQRL PGDRITTPEF AQRLAAISTD VNQPVCAYIN RRGQVIRLGV GTPRQTQIPP MELPRYGAER LSGIRCIATQ LKSEPPNEAA LTAMALQRLD ALVLLNITGS GFEKRGGGAT GYVKEIYLAH LVPHPEASWT VSPPMSLDVL TDQDLLELVE GLEADFEQKF IAREVEGDRD RVLVVSLKTD DTNTQRYEDG IAEIARLVET AGGEVLQTVK QKRSRPHPQT VVGEGKVQEI ALVAQTIGAN LIVFDRDLSP SQIRNLEIQI GIRVVDRTEV ILDIFAQRAQ SGAGKLQVEL AQLEYMMPRL TGRGQAMSRL GGGIGTRGPG ETKLETERRS IQRRISHLQQ QVNQLQAHRS RLRQQRQHRE VPSLAIVGYT NAGKSTLLNI LTNAEVYTAD QLFATLDPTT RRLKIADAVT GEPRSILLTD TVGFIHELPP SLMDAFRATL EEVTEADALL HVVDLSHPAW HSQVRSVMTI LSEMPITPGP ALIVFNKIDQ AKGEALESAR EEFPQAVFIS ASKHLGLETL RQRVAQLIEY AVSPN // ID K9W0T5_9CYAN Unreviewed; 568 AA. AC K9W0T5; DT 06-MAR-2013, integrated into UniProtKB/TrEMBL. DT 06-MAR-2013, sequence version 1. DT 07-JUN-2017, entry version 37. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=Cri9333_2987 {ECO:0000313|EMBL:AFZ13826.1}; OS Crinalium epipsammum PCC 9333. OC Bacteria; Cyanobacteria; Oscillatoriophycideae; Oscillatoriales; OC Gomontiellaceae; Crinalium. OX NCBI_TaxID=1173022 {ECO:0000313|EMBL:AFZ13826.1, ECO:0000313|Proteomes:UP000010472}; RN [1] {ECO:0000313|EMBL:AFZ13826.1, ECO:0000313|Proteomes:UP000010472} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=PCC 9333 {ECO:0000313|EMBL:AFZ13826.1, RC ECO:0000313|Proteomes:UP000010472}; RG US DOE Joint Genome Institute; RA Gugger M., Coursin T., Rippka R., Tandeau De Marsac N., Huntemann M., RA Wei C.-L., Han J., Detter J.C., Han C., Tapia R., Davenport K., RA Daligault H., Erkkila T., Gu W., Munk A.C.C., Teshima H., Xu Y., RA Chain P., Chen A., Krypides N., Mavromatis K., Markowitz V., Szeto E., RA Ivanova N., Mikhailova N., Ovchinnikova G., Pagani I., Pati A., RA Goodwin L., Peters L., Pitluck S., Woyke T., Kerfeld C.; RT "Finished chromosome of genome of Crinalium epipsammum PCC 9333."; RL Submitted (JUN-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP003620; AFZ13826.1; -; Genomic_DNA. DR RefSeq; WP_015203934.1; NC_019753.1. DR EnsemblBacteria; AFZ13826; AFZ13826; Cri9333_2987. DR KEGG; cep:Cri9333_2987; -. DR PATRIC; fig|1173022.3.peg.3233; -. DR KO; K03665; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000010472; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000010472}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000010472}. FT DOMAIN 392 562 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 351 388 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 568 AA; 63382 MW; AA7DDA85337C8C01 CRC64; METLYGNIQG LKSSHIKQLK QLYEQRISSD RLITPEFAQT IATVSTEIHH PICIYINRRG QIIRVAVGTP SQTQLSAADL PRHSAERLSG IRCIATQTKS EPPDPASLTA MVRQRLDALV VLAISSSGSD RKRGITGDVK ETYLAHLVPD PQTPWIISSP LNIDALSEED FDELIDEWEA EFTGSGHQTL KEFGIESDHD RVLLVGLMTE NMSQHQFEDS LAELARLVDT AGGKVLDTVT QKRSRPHPQT VVGQGKVEEI ANIAHQLRAN LIVFDRDISA SQARNLESTI SIRVVDRTEV ILDIFAQRAQ SQAGKLQVEL AQLEYMLPRL RGRGQEMSRL GGGIGTRGPG ETKLETERRT IQRKINQLQQ EVNQLQAHRT RLREQRQQQE IPVIALAGYT NAGKSTLLNV LTHAEVYTAD QLFATLDPTT RKLVITDPNT QERRSILLTD TVGFIHELPP ALMDAFRATL EEVSEADVLL HLVDLSHPAW ESHIQSVKEI LADLPAMPGQ TLIVFNKVDR VDNETLAEAQ QQYPESVFIS ATKHLELDTL KQRLLQLIDG YVIPSTLS // ID K9WHM4_9CYAN Unreviewed; 597 AA. AC K9WHM4; DT 06-MAR-2013, integrated into UniProtKB/TrEMBL. DT 06-MAR-2013, sequence version 1. DT 07-JUN-2017, entry version 33. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=Mic7113_4215 {ECO:0000313|EMBL:AFZ19915.1}; OS Microcoleus sp. PCC 7113. OC Bacteria; Cyanobacteria; Oscillatoriophycideae; Oscillatoriales; OC Microcoleaceae; Microcoleus. OX NCBI_TaxID=1173027 {ECO:0000313|EMBL:AFZ19915.1, ECO:0000313|Proteomes:UP000010471}; RN [1] {ECO:0000313|EMBL:AFZ19915.1, ECO:0000313|Proteomes:UP000010471} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=PCC 7113 {ECO:0000313|EMBL:AFZ19915.1, RC ECO:0000313|Proteomes:UP000010471}; RG US DOE Joint Genome Institute; RA Gugger M., Coursin T., Rippka R., Tandeau De Marsac N., Huntemann M., RA Wei C.-L., Han J., Detter J.C., Han C., Tapia R., Chen A., RA Kyrpides N., Mavromatis K., Markowitz V., Szeto E., Ivanova N., RA Pagani I., Pati A., Goodwin L., Nordberg H.P., Cantor M.N., Hua S.X., RA Woyke T., Kerfeld C.A.; RT "Finished chromosome of genome of Microcoleus sp. PCC 7113."; RL Submitted (JUN-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP003630; AFZ19915.1; -; Genomic_DNA. DR EnsemblBacteria; AFZ19915; AFZ19915; Mic7113_4215. DR KEGG; mic:Mic7113_4215; -. DR PATRIC; fig|1173027.3.peg.4659; -. DR KO; K03665; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000010471; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000010471}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Hydrolase {ECO:0000313|EMBL:AFZ19915.1}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000010471}. FT DOMAIN 425 595 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 384 418 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 597 AA; 66677 MW; 35B4B6928A26F83D CRC64; MFLYNRNRWI QGPGDWSETP IETIYGNLQG LKSSQLKQLQ RLYQQRFPSD RLTTPEFAQR LAAISTDIKQ PVCTYINRRG QVIRVGVGTP SQTKIPPLEL PRYGAERLSG IRCLATQLKS ETPKEAALTA MVIQRLDALV VLTVTESGFE RRGGGATGYV KETYLAHLLP LIEQGVQNPD DRPLATGVER SWSVSPPLSL DILTQQDFLE LVEGLESEFR REFVAQQVDV DQDRVLIIGL MTDETTKERF EDGLAEIARL VETAGGEVLQ TMRQKRSRPH PQTVVGAGKV QEIALTVQTL GANLVVFDRD LSPAQVRNLE LETGVRVVDR TEVILDIFAQ RAQSRAGKLQ VELAQLEYML PRLTGRGQAM SRLGGGIGTR GPGETKLETE RRSIQRRINR LQQEVNQLQA HRSRLRQRRQ RQEVPTVAVV GYTNAGKSTL LNTLTNAEVY TADQLFATLD PTTRRLPIPN AVTGEPMEIL LTDTVGFIHE LPPPLVDSFR ATLEEVTEAD ALLHLVDLSH PAWQSHIRSV MTILSEMPVT AGPILVAFNK IDRVDSETLT LAQEEFPQGV FVSASERFGL ETLRQKLAQL VHYALNP // ID K9X154_9NOST Unreviewed; 587 AA. AC K9X154; DT 06-MAR-2013, integrated into UniProtKB/TrEMBL. DT 06-MAR-2013, sequence version 1. DT 07-JUN-2017, entry version 32. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=Cylst_4252 {ECO:0000313|EMBL:AFZ26350.1}; OS Cylindrospermum stagnale PCC 7417. OC Bacteria; Cyanobacteria; Nostocales; Nostocaceae; Cylindrospermum. OX NCBI_TaxID=56107 {ECO:0000313|EMBL:AFZ26350.1, ECO:0000313|Proteomes:UP000010475}; RN [1] {ECO:0000313|EMBL:AFZ26350.1, ECO:0000313|Proteomes:UP000010475} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=PCC 7417 {ECO:0000313|EMBL:AFZ26350.1, RC ECO:0000313|Proteomes:UP000010475}; RG US DOE Joint Genome Institute; RA Gugger M., Coursin T., Rippka R., Tandeau De Marsac N., Huntemann M., RA Wei C.-L., Han J., Detter J.C., Han C., Tapia R., Chen A., RA Kyrpides N., Mavromatis K., Markowitz V., Szeto E., Ivanova N., RA Pagani I., Pati A., Goodwin L., Nordberg H.P., Cantor M.N., Hua S.X., RA Woyke T., Kerfeld C.A.; RT "Finished chromosome of genome of Cylindrospermum stagnale PCC 7417."; RL Submitted (JUN-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP003642; AFZ26350.1; -; Genomic_DNA. DR EnsemblBacteria; AFZ26350; AFZ26350; Cylst_4252. DR KEGG; csg:Cylst_4252; -. DR PATRIC; fig|56107.3.peg.4661; -. DR KO; K03665; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000010475; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000010475}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000010475}. FT DOMAIN 414 584 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 373 407 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 587 AA; 64766 MW; 66C0577AA4A09F8B CRC64; METIFGNLQG LKSSQLKQLQ RLYHQRIPGD RITTPDFAQR LAAISTDINQ PVCTYINRRG QVIRVGVGTP RQTQIPPMEL PRYGAERLSG IRCIATHLKP EPPNEAALTA MALQRLDALV VLNITGTGFT RRGGGAAGYV KEVYLAHLVS NTNQLVLNQP SVVGNASPPT PLPNQDTAIS SNISQPLSLD DLAEQDFIDL VEGLEEEFRR EFIAQEVDAD HERVLLIGVL TDGKTAQQFQ DSLSELARLV DTAGGDVLQT VQQKRSRLHP QTVVGEGKVQ EIALTAQTLG ASLVVFDRDL SPTQVRNLEA QIGVRVVDRT EVILDIFAQR AQSRAGKLQV ELAQLEYMMP RLTGRGQTMS RLGGGIGTRG PGETKLETER RAIQKRISRL QQEVNQLQAH RSRLRQRRQH REVPSVALVG YTNAGKSTLL NALTNSEVYT ADQLFATLDP TTRRLIIPHA DTNEPQETLI TDTVGFIHEL PASLMDAFRA TLEEVTEADA LLHLVDLSHP AWLSHIRSVR EILAQMPVTP GPALVAFNKI DQVNSETLAL AKEEFPLAIF ISASQRLGLE TLRLRLSQLI EYAVGCE // ID K9XER1_9CHRO Unreviewed; 577 AA. AC K9XER1; DT 06-MAR-2013, integrated into UniProtKB/TrEMBL. DT 06-MAR-2013, sequence version 1. DT 07-JUN-2017, entry version 31. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=Glo7428_1591 {ECO:0000313|EMBL:AFZ30152.1}; OS Gloeocapsa sp. PCC 7428. OC Bacteria; Cyanobacteria; Oscillatoriophycideae; Chroococcales; OC Chroococcaceae; Gloeocapsa. OX NCBI_TaxID=1173026 {ECO:0000313|EMBL:AFZ30152.1, ECO:0000313|Proteomes:UP000010476}; RN [1] {ECO:0000313|EMBL:AFZ30152.1, ECO:0000313|Proteomes:UP000010476} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=PCC 7428 {ECO:0000313|EMBL:AFZ30152.1, RC ECO:0000313|Proteomes:UP000010476}; RG US DOE Joint Genome Institute; RA Gugger M., Coursin T., Rippka R., Tandeau De Marsac N., Huntemann M., RA Wei C.-L., Han J., Detter J.C., Han C., Tapia R., Davenport K., RA Daligault H., Erkkila T., Gu W., Munk A.C.C., Teshima H., Xu Y., RA Chain P., Chen A., Krypides N., Mavromatis K., Markowitz V., Szeto E., RA Ivanova N., Mikhailova N., Ovchinnikova G., Pagani I., Pati A., RA Goodwin L., Peters L., Pitluck S., Woyke T., Kerfeld C.; RT "Finished chromosome of genome of Gloeocapsa sp. PCC 7428."; RL Submitted (JUN-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP003646; AFZ30152.1; -; Genomic_DNA. DR EnsemblBacteria; AFZ30152; AFZ30152; Glo7428_1591. DR KEGG; glp:Glo7428_1591; -. DR PATRIC; fig|1173026.3.peg.1689; -. DR KO; K03665; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000010476; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000010476}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000010476}. FT DOMAIN 405 574 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 364 401 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 577 AA; 63645 MW; B768C89021F8DC41 CRC64; MPIETIYGNL QGLKSSQIKQ LQRLYQQRLP GDRPTTPEFA QRLAAISTEI NQPVCAYVNR RGQVIRVGVG TPRQTQIPPL ELPRYGAERL SGIRCIATQL KSEPPSEAAL TAMALQRLDV LAVLNITGSG FQRRGGGATG YVKETYLAHL VPSTEETETD TQQTRTSPLA SWSVSQPLSL DVLSNQDFLD LIEGLEAEFR REYVATQVDS DRDRVLIVGV QTDDLTPQAF QDTLDELARL VDTAGGEVLQ TFRQKRSRPH PQTAVGEGKV QEIALTAQTL GANLIVFDRD LSPAQVRNLE TQIGIRVVDR TEVILDIFAQ RARTRAGKLQ VELAQLEYML PRLTGRGQAM SRLGGGIGTR GPGETKLETE RRAIARRIAR LQEEVNQLQA HRSRLRQQRQ HREVPSVAIV GYTNAGKSTL LNALTNAEVY TADQLFATLD PTTRRLVVPD VGGEPQAIVL TDTVGFIHEL PASLMDAFRA TLEEVTEADA LLHVVDLSHP AWQSQIRSVM SILSEMPITP GPMLIALNKV DRVDSDTLAV AQEEFPQAVY ISASDRLGLE TLRQRLGQLV RYAVAPS // ID K9XFQ6_9CHRO Unreviewed; 559 AA. AC K9XFQ6; DT 06-MAR-2013, integrated into UniProtKB/TrEMBL. DT 06-MAR-2013, sequence version 1. DT 07-JUN-2017, entry version 31. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=Glo7428_2963 {ECO:0000313|EMBL:AFZ31455.1}; OS Gloeocapsa sp. PCC 7428. OC Bacteria; Cyanobacteria; Oscillatoriophycideae; Chroococcales; OC Chroococcaceae; Gloeocapsa. OX NCBI_TaxID=1173026 {ECO:0000313|EMBL:AFZ31455.1, ECO:0000313|Proteomes:UP000010476}; RN [1] {ECO:0000313|EMBL:AFZ31455.1, ECO:0000313|Proteomes:UP000010476} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=PCC 7428 {ECO:0000313|EMBL:AFZ31455.1, RC ECO:0000313|Proteomes:UP000010476}; RG US DOE Joint Genome Institute; RA Gugger M., Coursin T., Rippka R., Tandeau De Marsac N., Huntemann M., RA Wei C.-L., Han J., Detter J.C., Han C., Tapia R., Davenport K., RA Daligault H., Erkkila T., Gu W., Munk A.C.C., Teshima H., Xu Y., RA Chain P., Chen A., Krypides N., Mavromatis K., Markowitz V., Szeto E., RA Ivanova N., Mikhailova N., Ovchinnikova G., Pagani I., Pati A., RA Goodwin L., Peters L., Pitluck S., Woyke T., Kerfeld C.; RT "Finished chromosome of genome of Gloeocapsa sp. PCC 7428."; RL Submitted (JUN-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP003646; AFZ31455.1; -; Genomic_DNA. DR RefSeq; WP_015189327.1; NC_019745.1. DR EnsemblBacteria; AFZ31455; AFZ31455; Glo7428_2963. DR KEGG; glp:Glo7428_2963; -. DR PATRIC; fig|1173026.3.peg.3161; -. DR KO; K03665; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000010476; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000010476}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000010476}. FT DOMAIN 382 559 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 341 378 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 559 AA; 62393 MW; A0BE0309C8E03DCF CRC64; MQTIYGNTQG IKSSQIKRLQ ALYEQQQPRD RFITSEFAAS LAAMTTEIHQ PICCYINRRG QVIRIAVGTP SQTQIPPQEL PRRSAERLSK IRCIATQFNS EPPSEAALTT MVRQRLDALI VLSVADRQVK EAFTAHLASD VNIPWVISPP LSLVDLTKQD FDEFVEEWEK EIAQASDGTF LSQEIASDQD RVLLVGVQTD DVAAQRFEDG LAELARLVES AGGIVLDTVR QKRSRPHPQT VVGQGKAEEI ALLAQKLGAN LIVVDRDISP SQARNLEQEI GIRVVDRTEI ILDIFAQRAR SSAGKLQVEL AQLEYMLPRL RGRGREMSRL GGGIGTRGPG ETRLETERRA IQRRIAQLQQ EVNQLQAHRS RIRQQRHQQD IPVMALVGYT NAGKSTLLNV LTNAEVYTAD QLFATLDPTT RKLVITQPNQ ERRSILLTDT VGFIHELPPP LMDAFRATLE EVIEADALLH VVDLSHPAWE SHMTSVQEIL AEMPAIPAKS LIAFNKIDRV DSETLAKAQQ EYPQAVFISA TERLGLETLK QRSLQLSDEL ATITVTQKS // ID K9XZ81_STAC7 Unreviewed; 543 AA. AC K9XZ81; DT 06-MAR-2013, integrated into UniProtKB/TrEMBL. DT 06-MAR-2013, sequence version 1. DT 07-JUN-2017, entry version 36. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Sta7437_3471 {ECO:0000313|EMBL:AFZ36972.1}; OS Stanieria cyanosphaera (strain ATCC 29371 / PCC 7437). OC Bacteria; Cyanobacteria; Pleurocapsales; Dermocarpellaceae; Stanieria. OX NCBI_TaxID=111780 {ECO:0000313|EMBL:AFZ36972.1, ECO:0000313|Proteomes:UP000010473}; RN [1] {ECO:0000313|Proteomes:UP000010473} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29371 / PCC 7437 {ECO:0000313|Proteomes:UP000010473}; RX PubMed=23277585; DOI=10.1073/pnas.1217107110; RA Shih P.M., Wu D., Latifi A., Axen S.D., Fewer D.P., Talla E., RA Calteau A., Cai F., Tandeau de Marsac N., Rippka R., Herdman M., RA Sivonen K., Coursin T., Laurent T., Goodwin L., Nolan M., RA Davenport K.W., Han C.S., Rubin E.M., Eisen J.A., Woyke T., Gugger M., RA Kerfeld C.A.; RT "Improving the coverage of the cyanobacterial phylum using diversity- RT driven genome sequencing."; RL Proc. Natl. Acad. Sci. U.S.A. 110:1053-1058(2013). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP003653; AFZ36972.1; -; Genomic_DNA. DR EnsemblBacteria; AFZ36972; AFZ36972; Sta7437_3471. DR KEGG; scs:Sta7437_3471; -. DR PATRIC; fig|111780.3.peg.3597; -. DR KO; K03665; -. DR OMA; EREVIIT; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000010473; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000010473}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Hydrolase {ECO:0000313|EMBL:AFZ36972.1}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000010473}. FT DOMAIN 364 534 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 323 360 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 543 AA; 60136 MW; C2A2CA840FA94C18 CRC64; MTTVEFAQRL AAISTEINQV VCAYVNRRGQ VIRVGVGTPH QTQIPPLELP RYGAERLCGI RCLATKLKQE PPKEASLTAM VRQRLDALVI LTLTGTGMTR RGGGATGYVK ETYLAHLVPQ SELNLDNQNY WSVSPPLSLD LLSKQDFLSL VEGLETEFER EYLGQEVDAN RDRVVIVGLQ TDRISQEQFE NSLQELTRLV DTAGGEVIYT IQQKRPQSHP QTVVGAGKVE EIALKVQTLG ASLVVFDRDL SPAQVRNLET QFGVRVVDRT EVILDIFAQR AQSRAGKLQV ELAQLEYMLP RLIGRGEAMS RLGGGIGTRG PGETKLETER RGIQKRIARL QQDVNQLQAH RSRLRQQRQK QEIPTVAIAG YTNAGKSTLI NALTSADVYT ADQLFATLDP TTRRLVVPDA VTGEARTILL TDTVGFIEEL PPSLVDAFRA TLEEVIEADA LLHVVDLSHP AWENQIRSVM KILQEMPIAP GPILIAFNKL DQVDSETLAR AREEFPLAVF ISASQRFGLE TLRQKLGELV HYAGDGSRAA KEE // ID K9YEV7_HALP7 Unreviewed; 564 AA. AC K9YEV7; DT 06-MAR-2013, integrated into UniProtKB/TrEMBL. DT 06-MAR-2013, sequence version 1. DT 07-JUN-2017, entry version 30. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=PCC7418_3273 {ECO:0000313|EMBL:AFZ45389.1}; OS Halothece sp. (strain PCC 7418) (Synechococcus sp. (strain PCC 7418)). OC Bacteria; Cyanobacteria; Oscillatoriophycideae; Chroococcales; OC Aphanothecaceae; Halothece cluster; Halothece. OX NCBI_TaxID=65093 {ECO:0000313|EMBL:AFZ45389.1, ECO:0000313|Proteomes:UP000010481}; RN [1] {ECO:0000313|Proteomes:UP000010481} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=PCC 7418 {ECO:0000313|Proteomes:UP000010481}; RX PubMed=23277585; DOI=10.1073/pnas.1217107110; RA Shih P.M., Wu D., Latifi A., Axen S.D., Fewer D.P., Talla E., RA Calteau A., Cai F., Tandeau de Marsac N., Rippka R., Herdman M., RA Sivonen K., Coursin T., Laurent T., Goodwin L., Nolan M., RA Davenport K.W., Han C.S., Rubin E.M., Eisen J.A., Woyke T., Gugger M., RA Kerfeld C.A.; RT "Improving the coverage of the cyanobacterial phylum using diversity- RT driven genome sequencing."; RL Proc. Natl. Acad. Sci. U.S.A. 110:1053-1058(2013). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP003945; AFZ45389.1; -; Genomic_DNA. DR EnsemblBacteria; AFZ45389; AFZ45389; PCC7418_3273. DR KEGG; hao:PCC7418_3273; -. DR PATRIC; fig|65093.3.peg.3452; -. DR KO; K03665; -. DR OMA; EREVIIT; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000010481; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000010481}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Hydrolase {ECO:0000313|EMBL:AFZ45389.1}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000010481}. FT DOMAIN 397 564 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 356 393 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 564 AA; 62684 MW; CF44E88108969E40 CRC64; MSIETIHGNL KGLKSSQLKQ LQRLYHQRQP RDRATTPEFA QRVAAISTDI NQPVSAYINR RGQVIRVGVG SPRETQIPPL ELPRYGAKRL SGIRCVTTAL KSDPPKKPSL TAMVLQRLDV LVTLTLTGQG FQRRGGGATG YVESAYLAHL APESDPNREQ GLYWTVSPPL SLDVVTQQDF LDLVEGLEAE FEREYVAQQV DISHQRVVVV GLMTADLDHQ QFADGLAEVT RLVDTAGGEV LQTITQRRSR PHPQTVIGAG KVQEIAIAVQ TLGASLVAFD QDLTPAQARN LEQEIGVRVI DRTELILDIF AQRARSRAGK LQVELAQLEY LLPRLVGRGE AMSRLGGGIG TRGPGETKLE TERRRIQKRV SRLQQEVNQL QSHRSRMRQQ RQKQEVPTIA VVGYTNAGKS TLLNNLTHAE IYAEDQLFAT LDPTTRRLNV PCQGEMKTIL LTDTVGFIKE LPPALIDAFR ATLEEVSEAD AMLHVVDLSH SAWESQIESV SKILEAMPIM PPESLLVFNK IDQVDSETLS YAKEHFPEAV YISAEKRLGL ETLREKMGEM IINA // ID K9YIY7_CYASC Unreviewed; 558 AA. AC K9YIY7; DT 06-MAR-2013, integrated into UniProtKB/TrEMBL. DT 06-MAR-2013, sequence version 1. DT 07-JUN-2017, entry version 32. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Cyast_0837 {ECO:0000313|EMBL:AFZ46809.1}; OS Cyanobacterium stanieri (strain ATCC 29140 / PCC 7202). OC Bacteria; Cyanobacteria; Oscillatoriophycideae; Chroococcales; OC Cyanobacteriaceae; Cyanobacterium. OX NCBI_TaxID=292563 {ECO:0000313|EMBL:AFZ46809.1, ECO:0000313|Proteomes:UP000010483}; RN [1] {ECO:0000313|Proteomes:UP000010483} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29140 / PCC 7202 {ECO:0000313|Proteomes:UP000010483}; RX PubMed=23277585; DOI=10.1073/pnas.1217107110; RA Shih P.M., Wu D., Latifi A., Axen S.D., Fewer D.P., Talla E., RA Calteau A., Cai F., Tandeau de Marsac N., Rippka R., Herdman M., RA Sivonen K., Coursin T., Laurent T., Goodwin L., Nolan M., RA Davenport K.W., Han C.S., Rubin E.M., Eisen J.A., Woyke T., Gugger M., RA Kerfeld C.A.; RT "Improving the coverage of the cyanobacterial phylum using diversity- RT driven genome sequencing."; RL Proc. Natl. Acad. Sci. U.S.A. 110:1053-1058(2013). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP003940; AFZ46809.1; -; Genomic_DNA. DR EnsemblBacteria; AFZ46809; AFZ46809; Cyast_0837. DR KEGG; csn:Cyast_0837; -. DR PATRIC; fig|292563.3.peg.880; -. DR KO; K03665; -. DR OMA; EREVIIT; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000010483; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000010483}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Hydrolase {ECO:0000313|EMBL:AFZ46809.1}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000010483}. FT DOMAIN 393 558 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 352 389 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 558 AA; 61960 MW; A74D7A04D25CC406 CRC64; MSIAPIYGNL QGIKPNQLKQ LQRLYQQRIR SDRLTSPEFA ERIASISSDL KQPVCVYLNR RGQVIRVGVG TPRQTQIPPL ELPRYGAQRL SGIRCLSTSI KPIPPSEASL TAMARQRLDA LVVFTLTGQG IQRKGGGASG FVKDAYLAHL IPAQDTHNYW EVSPAQDVEA IAEQDFFTLV DSLEEEFSRE FVAQAVEDSQ ERVVLVGLMT DNLSPQKFND SLQELQRLVE SAGGKVLATL EQKRSQPHPQ TLVGAGKVEE IALQVQSMGA NLVAFDRDLS PSQARNLETQ FGVRVVDRTE VILDIFAQRA QSRAGKLQVE LAQLEYMLPR LKGRGRAMSR LGGGIGTRGP GETKLETERR AIQKRITRLQ QEVNQLQSHR ARMRQQRQHQ EIPTVAIVGY TNAGKSTLIN ALTNAQVYTA DQLFATLDPT TRRLTITEQN TGKSSTILLT DTVGFIHELP PSLVDSFRAT LEEVTEADAL LHVVDLSHPA WQSHIESVKN ILADMPLAPA EELIAFNKID QADIEHLELA KEEYSGAVFI SAKERIGFDN LRARLMVS // ID K9Z5S6_CYAAP Unreviewed; 562 AA. AC K9Z5S6; DT 06-MAR-2013, integrated into UniProtKB/TrEMBL. DT 06-MAR-2013, sequence version 1. DT 07-JUN-2017, entry version 35. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Cyan10605_1823 {ECO:0000313|EMBL:AFZ53925.1}; OS Cyanobacterium aponinum (strain PCC 10605). OC Bacteria; Cyanobacteria; Oscillatoriophycideae; Chroococcales; OC Cyanobacteriaceae; Cyanobacterium. OX NCBI_TaxID=755178 {ECO:0000313|EMBL:AFZ53925.1, ECO:0000313|Proteomes:UP000010480}; RN [1] {ECO:0000313|Proteomes:UP000010480} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=PCC 10605 {ECO:0000313|Proteomes:UP000010480}; RX PubMed=23277585; DOI=10.1073/pnas.1217107110; RA Shih P.M., Wu D., Latifi A., Axen S.D., Fewer D.P., Talla E., RA Calteau A., Cai F., Tandeau de Marsac N., Rippka R., Herdman M., RA Sivonen K., Coursin T., Laurent T., Goodwin L., Nolan M., RA Davenport K.W., Han C.S., Rubin E.M., Eisen J.A., Woyke T., Gugger M., RA Kerfeld C.A.; RT "Improving the coverage of the cyanobacterial phylum using diversity- RT driven genome sequencing."; RL Proc. Natl. Acad. Sci. U.S.A. 110:1053-1058(2013). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP003947; AFZ53925.1; -; Genomic_DNA. DR EnsemblBacteria; AFZ53925; AFZ53925; Cyan10605_1823. DR KEGG; can:Cyan10605_1823; -. DR PATRIC; fig|755178.3.peg.1934; -. DR KO; K03665; -. DR OMA; EREVIIT; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000010480; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000010480}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Hydrolase {ECO:0000313|EMBL:AFZ53925.1}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000010480}. FT DOMAIN 393 562 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 352 393 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 562 AA; 62515 MW; 88DAB21F55BA2D74 CRC64; MSIETIYGNL QGLKPSQFKQ LQKLYHQRIS GDRISTVDLA ERIANLSTEL KQPLSVYLNR RGQVIRVGVG TPRQTQIPPL ELPRYGELRL SGIRCLSTSL KPTPPSEASL TAMVRQRLDA LVILTLTGQG IIRKGGGARG FVDKAYLCHL LPLKDTDNYW DVSHPQSLED IVEQDFLDLV NNLEAEFSRE FIAQEVSPQQ ERVLLVGLHT GDREEQKFQD NLQELALLVD SAGGKVLATI EQKRSHPHPQ TLVGAGKVEE IALQVQTLGA NLVVFDRDLS PAQVRNLELQ LGVRVVDRTE VILDIFAQRA QSRAGKLQVE LAQLEYMLPR LTGRGQAMSR LGGGIGTRGP GETKLETERR AIQKRITRLQ QEVNQLQSHR SRLRQQRQAH EITSIAIVGY TNAGKSTLIN TLTNADVYTA DQLFATLDPT TRRLTITDPN TSDTTTLLMT DTVGFIHELP PPLVDSFRAT LEEVTEADAL LHVVDLSHPA WESHIESVKA ILAQMPLAPS VELIALNKID KAKSEHLTIA KEKYPQAVFI SAQQRHGLTT LRDRLLQLVA SN // ID K9Z970_ANACC Unreviewed; 568 AA. AC K9Z970; DT 06-MAR-2013, integrated into UniProtKB/TrEMBL. DT 06-MAR-2013, sequence version 1. DT 07-JUN-2017, entry version 31. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Anacy_0119 {ECO:0000313|EMBL:AFZ55728.1}; OS Anabaena cylindrica (strain ATCC 27899 / PCC 7122). OC Bacteria; Cyanobacteria; Nostocales; Nostocaceae; Anabaena. OX NCBI_TaxID=272123 {ECO:0000313|EMBL:AFZ55728.1, ECO:0000313|Proteomes:UP000010474}; RN [1] {ECO:0000313|Proteomes:UP000010474} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 27899 / PCC 7122 {ECO:0000313|Proteomes:UP000010474}; RX PubMed=23277585; DOI=10.1073/pnas.1217107110; RA Shih P.M., Wu D., Latifi A., Axen S.D., Fewer D.P., Talla E., RA Calteau A., Cai F., Tandeau de Marsac N., Rippka R., Herdman M., RA Sivonen K., Coursin T., Laurent T., Goodwin L., Nolan M., RA Davenport K.W., Han C.S., Rubin E.M., Eisen J.A., Woyke T., Gugger M., RA Kerfeld C.A.; RT "Improving the coverage of the cyanobacterial phylum using diversity- RT driven genome sequencing."; RL Proc. Natl. Acad. Sci. U.S.A. 110:1053-1058(2013). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP003659; AFZ55728.1; -; Genomic_DNA. DR EnsemblBacteria; AFZ55728; AFZ55728; Anacy_0119. DR KEGG; acy:Anacy_0119; -. DR PATRIC; fig|272123.3.peg.127; -. DR KO; K03665; -. DR OMA; EREVIIT; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000010474; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000010474}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000010474}. FT DOMAIN 395 565 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 354 381 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 568 AA; 62422 MW; 91CDAE1FFFA4B7E6 CRC64; MKSSHLKQLQ RLYHQRISGD RITTSEFAQR LAAISTELNQ PVCAYLNRRG QVIRVGVGTP RQTQIPPLEL PRYGAERLSG IRCIATHLKP EPPNESALTA MALQRLDALV VLNITGTGFT KRGGGAAGYV KEAYLAHLVA NSKQLVSTQV GGISIPEAAS YSSISPPLSL DAIAEQDFLD LVESLEEEFR REYIAQEVDA DHDRVVIVGV ATDSTSGQQF QDTIAELVRL VDTAGGDVLQ ILQQKRSRIH PQTVIGEGKV QEVALTAQTL GANLVVFDRD LSPAQIRNLE AQIGVRVIDR TEVILDIFAQ RAQSGAGKLQ VELAQLEYML PRLTGRGKTM SRLGGGIGTR GPGETKLETE RRAIQKRISR LQQEVNQLQA HRCRLRQRRQ HREVPSVAVV GYTNAGKSTL LNALTNAEVY AADQLFATLD PTTRRLIIPN ADTNEPQETL ITDTVGFIHK LPPSLMDAFR ATLEEVTEAD ALLHLVDLSH PAWLSHIRAV REILAQMPIT PGPALVAFNK IDQVSSEALA LAKEEFPLAI FISASQRLGL ENLRYRLSQL IEYAVDDG // ID L0A4A7_DEIPD Unreviewed; 615 AA. AC L0A4A7; DT 06-MAR-2013, integrated into UniProtKB/TrEMBL. DT 06-MAR-2013, sequence version 1. DT 07-JUN-2017, entry version 32. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Deipe_3276 {ECO:0000313|EMBL:AFZ68718.1}; OS Deinococcus peraridilitoris (strain DSM 19664 / LMG 22246 / CIP 109416 OS / KR-200). OC Bacteria; Deinococcus-Thermus; Deinococci; Deinococcales; OC Deinococcaceae; Deinococcus. OX NCBI_TaxID=937777 {ECO:0000313|EMBL:AFZ68718.1, ECO:0000313|Proteomes:UP000010467}; RN [1] {ECO:0000313|Proteomes:UP000010467} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 19664 / LMG 22246 / CIP 109416 / KR-200 RC {ECO:0000313|Proteomes:UP000010467}; RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., RA Tice H., Bruce D., Goodwin L., Pitluck S., Peters L., Mikhailova N., RA Lu M., Kyrpides N., Mavromatis K., Ivanova N., Brettin T., RA Detter J.C., Han C., Larimer F., Land M., Hauser L., Markowitz V., RA Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Pukall R., Steenblock K., RA Brambilla E., Klenk H.-P., Eisen J.A.; RT "Complete sequence of chromosome of Deinococcus peraridilitoris DSM RT 19664."; RL Submitted (MAR-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP003382; AFZ68718.1; -; Genomic_DNA. DR RefSeq; WP_015237016.1; NC_019793.1. DR EnsemblBacteria; AFZ68718; AFZ68718; Deipe_3276. DR KEGG; dpd:Deipe_3276; -. DR KO; K03665; -. DR OMA; EREVIIT; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000010467; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000010467}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000010467}. FT DOMAIN 433 602 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 615 AA; 67345 MW; 2736470095415FA9 CRC64; MAGSVWAKLH QSYGVSALKR VRWRNYFPVR PSLQASSGTQ SFFAGGTTIE KVHGNTSGLK SGQLKQLSNL YRRRLAPGTL TSPELARNLS ELSHELRREV SVLIDRRGRV LSVSVADAKG TELPPVRVGE TRLAGFHLLH THPKGGALSK GDLSTLFLNR LDAVAAIEVR PDGLPGNVHF AHLTPPGTTG EEEDWRVYPP QSAYTVEDFD LGAQVSALEE EIARSRRLRE ARKDRERALL VQIDSGAFDA EERLEELTEL AHTAGAEVVY KELVFRRHLK PGTLVGAGKL EELTSRAYHL DADLLVFGQE LSPAQAREIE EATGLKVLDR TQLILDIFAL HAQGVESRLQ VELAQLRYMK PRLLGQGTRL SRIGASGGSA AGGAIGTRGP GETKLEMDRR RINDRIAFLE KQLTEVAVRR EERRKSRARN DVPVISIVGY TNAGKSTLLN AFTHAAEEPR KVLAENKLFA TLRPTSRQGF IDGVGPVVFT DTVGFIRDLP TDLQRAFRST LEEIGDADVL LHVVDVATPG ADTRHGAVER ILRDLGIQEL PSVVALNKAD AADREVIERE RDRLGGVAVS AAQNTGLDDL KVALHEALRP YVEVPALNLP GLPAD // ID L0AC38_CALLD Unreviewed; 360 AA. AC L0AC38; DT 06-MAR-2013, integrated into UniProtKB/TrEMBL. DT 06-MAR-2013, sequence version 1. DT 07-JUN-2017, entry version 24. DE SubName: Full=GTP-binding protein HflX {ECO:0000313|EMBL:AFZ70999.1}; GN OrderedLocusNames=Calag_1285 {ECO:0000313|EMBL:AFZ70999.1}; OS Caldisphaera lagunensis (strain DSM 15908 / JCM 11604 / IC-154). OC Archaea; Crenarchaeota; Thermoprotei; Acidilobales; Caldisphaeraceae; OC Caldisphaera. OX NCBI_TaxID=1056495 {ECO:0000313|EMBL:AFZ70999.1, ECO:0000313|Proteomes:UP000010469}; RN [1] {ECO:0000313|Proteomes:UP000010469} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 15908 / JCM 11604 / IC-154 RC {ECO:0000313|Proteomes:UP000010469}; RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., RA Tice H., Bruce D., Goodwin L., Pitluck S., Peters L., Mikhailova N., RA Teshima H., Kyrpides N., Mavromatis K., Ivanova N., Brettin T., RA Detter J.C., Han C., Larimer F., Land M., Hauser L., Markowitz V., RA Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Spring S., Schroeder M., RA Brambilla E., Klenk H.-P., Eisen J.A.; RT "Complete genome of Caldisphaera lagunensis DSM 15908."; RL Submitted (MAR-2012) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP003378; AFZ70999.1; -; Genomic_DNA. DR RefSeq; WP_015232896.1; NC_019791.1. DR EnsemblBacteria; AFZ70999; AFZ70999; Calag_1285. DR GeneID; 14212545; -. DR KEGG; clg:Calag_1285; -. DR KO; K03665; -. DR OMA; FNNHAHV; -. DR OrthoDB; POG093Z07D6; -. DR Proteomes; UP000010469; Chromosome. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000010469}; KW Reference proteome {ECO:0000313|Proteomes:UP000010469}. FT DOMAIN 186 358 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 360 AA; 41214 MW; CC449486CD34EDD3 CRC64; MELNKTKNAF LILSSKFYNH FEEALILANT AGYEIVGTKR FRGGKRITDG LIEIVKNNKK ELDFDTVIYY GDIEPSSVFK LEKETKIRVL DRVQLILEIF ALHAGSKEAL LQIEMARIRH DLPIIREYIR RTKLGELPGF LGPGRYGIDT YKKQLTSRLS KIKRDLEDLR ITEQERLKRR KELGMINIPI VGYASAGKTS LFNIITGESK PVGPEYFTTL FPKHKTINYN GLKLAFVDTV GFIRDVPPEV IEAFYSTLEE VTISDIIVFV IDITENENDI KEKILAGTDI LKKLNALNKP IIFALNKIDE IDKIKIYDKI EFVKKTFPND KMVLISAKKN IGIDALLNEI INITKNLNIY // ID L0ADD2_NATGS Unreviewed; 442 AA. AC L0ADD2; DT 06-MAR-2013, integrated into UniProtKB/TrEMBL. DT 06-MAR-2013, sequence version 1. DT 07-JUN-2017, entry version 37. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Natgr_0612 {ECO:0000313|EMBL:AFZ71861.1}; GN ORFNames=C490_01964 {ECO:0000313|EMBL:ELY73069.1}; OS Natronobacterium gregoryi (strain ATCC 43098 / DSM 3393 / CCM 3738 / OS CIP 104747 / JCM 8860 / NBRC 102187 / NCIMB 2189 / SP2). OC Archaea; Euryarchaeota; Halobacteria; Natrialbales; Natrialbaceae; OC Natronobacterium. OX NCBI_TaxID=797304 {ECO:0000313|EMBL:AFZ71861.1, ECO:0000313|Proteomes:UP000010468}; RN [1] {ECO:0000313|Proteomes:UP000010468} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43098 / CCM 3738 / NCIMB 2189 / SP2 RC {ECO:0000313|Proteomes:UP000010468}; RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S., RA Peters L., Mikhailova N., Teshima H., Detter J.C., Han C., Tapia R., RA Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Sproer C., RA Anderson I., Woyke T.; RT "Complete sequence of Natronobacterium gregoryi SP2."; RL Submitted (MAR-2012) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:AFZ71861.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=SP2 {ECO:0000313|EMBL:AFZ71861.1}; RG US DOE Joint Genome Institute; RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S., RA Peters L., Mikhailova N., Teshima H., Detter J.C., Han C., Tapia R., RA Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Sproer C., RA Anderson I., Woyke T.; RT "Complete sequence of Natronobacterium gregoryi SP2."; RL Submitted (MAR-2012) to the EMBL/GenBank/DDBJ databases. RN [3] {ECO:0000313|Proteomes:UP000011613} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SP2 {ECO:0000313|Proteomes:UP000011613}; RA Becker E.A., Seitzer P., Tritt A., Larsen D., Yao A., Wu D., RA Darling A., Eisen J.A., Facciotti M.T.; RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases. RN [4] {ECO:0000313|EMBL:ELY73069.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=SP2 {ECO:0000313|EMBL:ELY73069.1}; RX PubMed=25393412; RA Becker E.A., Seitzer P.M., Tritt A., Larsen D., Krusor M., Yao A.I., RA Wu D., Madern D., Eisen J.A., Darling A.E., Facciotti M.T.; RT "Phylogenetically driven sequencing of extremely halophilic archaea RT reveals strategies for static and dynamic osmo-response."; RL PLoS Genet. 10:E1004784-E1004784(2014). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP003377; AFZ71861.1; -; Genomic_DNA. DR EMBL; AOIC01000019; ELY73069.1; -; Genomic_DNA. DR RefSeq; WP_005576107.1; NZ_AOIC01000019.1. DR EnsemblBacteria; AFZ71861; AFZ71861; Natgr_0612. DR EnsemblBacteria; ELY73069; ELY73069; C490_01964. DR GeneID; 14207776; -. DR KEGG; nge:Natgr_0612; -. DR PATRIC; fig|797304.7.peg.397; -. DR KO; K03665; -. DR OMA; FNNHAHV; -. DR OrthoDB; POG093Z07D6; -. DR Proteomes; UP000010468; Chromosome. DR Proteomes; UP000011613; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000010468}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000010468}. FT DOMAIN 187 382 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 442 AA; 48852 MW; B0DD2EB02A93E2CB CRC64; MSRTDNAPKR TVVAKRSETT PVETDEIETL VRAAGDEVVA AVTQAGHEDA GSYFGRGKVE ELTDTVAETD ARRVVVDDEL TPGQYHTLES AMPDDTAVFD RHRLVLEIFE AGAGSRRAKL QVELAGLRYD LPRLIESADE GMLNEMTERG SPVYDVCDRI DRLERKLASL PEPAEQCRER RREEGFDLVT LAGYTNAGKS TLLHRLADEM ALSEANSSRE TGDASTEKNA TAAVRDRLFE TLETTTRRAT IDGRPLLVTD TVGFVDDLPH DLVESFSATL SEAGAADVVV LVVDTSDPES RFRERLDVSL EVLDPQGVED ERIVPVLNKV DCLSADARAH RLAVAEKRLP SAAADPISVS VLEETNLERL RETVLKRLPT DTAELRVPNC DEAMTLVSRA YDRTTVETVD YDSGVTIECR GPPRVLEELR ARADRIVDKQ RH // ID L0ANV4_NATGS Unreviewed; 433 AA. AC L0ANV4; DT 06-MAR-2013, integrated into UniProtKB/TrEMBL. DT 06-MAR-2013, sequence version 1. DT 07-JUN-2017, entry version 33. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Natgr_3650 {ECO:0000313|EMBL:AFZ74760.1}; OS Natronobacterium gregoryi (strain ATCC 43098 / DSM 3393 / CCM 3738 / OS CIP 104747 / JCM 8860 / NBRC 102187 / NCIMB 2189 / SP2). OC Archaea; Euryarchaeota; Halobacteria; Natrialbales; Natrialbaceae; OC Natronobacterium. OX NCBI_TaxID=797304 {ECO:0000313|EMBL:AFZ74760.1, ECO:0000313|Proteomes:UP000010468}; RN [1] {ECO:0000313|Proteomes:UP000010468} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43098 / CCM 3738 / NCIMB 2189 / SP2 RC {ECO:0000313|Proteomes:UP000010468}; RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S., RA Peters L., Mikhailova N., Teshima H., Detter J.C., Han C., Tapia R., RA Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Sproer C., RA Anderson I., Woyke T.; RT "Complete sequence of Natronobacterium gregoryi SP2."; RL Submitted (MAR-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP003377; AFZ74760.1; -; Genomic_DNA. DR RefSeq; WP_015233893.1; NZ_AOIC01000012.1. DR EnsemblBacteria; AFZ74760; AFZ74760; Natgr_3650. DR GeneID; 14209921; -. DR KEGG; nge:Natgr_3650; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG093Z07D6; -. DR Proteomes; UP000010468; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000010468}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000010468}. FT DOMAIN 186 369 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 102 129 {ECO:0000256|SAM:Coils}. FT COILED 152 182 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 433 AA; 48155 MW; 0FDB01C0A2623A50 CRC64; MRAIIAKRVD SGTPDTSEIR DLAAAAGYTV VGEVTQSRTA DSALQIGEGK ANELATKVAG TDATTVIFDN RLGPYQTYNL GQLLPEGVEV IDRFTLILEI FGQRAQTRKA QLQVELAELR YELPRAEAKT SLAKREEHPG FMGLGEYDES REQDIKNQIS RIRDELERIE QTEQQRRERR RDSGFDLVAL AGYTNAGKST LLRRLAADLD VDENEDLHRD LESTAESQDK LFTTLGTTTR RADIEPRDVL VTDTVGFISD LPHWLVESFK STLDSVYRAD LVLLVVDVSE SVDAIHEKLV TCHDTLYERN EAPIVTVLNK IDAVDDEALA EKREAISSLA PSPVTVSAKE GANVDALLER IDRELPDWEE ERLVLPMTDD TMSLVSWIHD NANVEDVSYG DDDVLVSFEA RPAVISQARS RAGELQTAQL ESA // ID L0DIW4_SINAD Unreviewed; 434 AA. AC L0DIW4; DT 06-MAR-2013, integrated into UniProtKB/TrEMBL. DT 06-MAR-2013, sequence version 1. DT 07-JUN-2017, entry version 33. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Sinac_5048 {ECO:0000313|EMBL:AGA29202.1}; OS Singulisphaera acidiphila (strain ATCC BAA-1392 / DSM 18658 / VKM OS B-2454 / MOB10). OC Bacteria; Planctomycetes; Planctomycetia; Planctomycetales; OC Isosphaeraceae; Singulisphaera. OX NCBI_TaxID=886293 {ECO:0000313|EMBL:AGA29202.1, ECO:0000313|Proteomes:UP000010798}; RN [1] {ECO:0000313|EMBL:AGA29202.1, ECO:0000313|Proteomes:UP000010798} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 18658 {ECO:0000313|EMBL:AGA29202.1}; RG US DOE Joint Genome Institute (JGI-PGF); RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., RA Tice H., Bruce D., Goodwin L., Pitluck S., Peters L., Ovchinnikova G., RA Chertkov O., Kyrpides N., Mavromatis K., Ivanova N., Brettin T., RA Detter J.C., Han C., Larimer F., Land M., Hauser L., Markowitz V., RA Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Tindall B., Pomrenke H., RA Brambilla E., Klenk H.-P., Eisen J.A.; RT "Complete sequence of chromosome of Singulisphaera acidiphila DSM RT 18658."; RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP003364; AGA29202.1; -; Genomic_DNA. DR RefSeq; WP_015248308.1; NZ_JH621480.1. DR EnsemblBacteria; AGA29202; AGA29202; Sinac_5048. DR KEGG; saci:Sinac_5048; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000010798; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000010798}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000010798}. FT DOMAIN 203 369 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 434 AA; 48525 MW; 2B270FA7E203454C CRC64; MGELKSTERL DRREKTILVG VLLSDGEYSQ DDPLDEIRGL AKTAGLVVVG SMLQKRQHVD IATYIGSGKV AELKELVEAH EADLVVFDND LGPAQTRNLE RILGVKVIDR TEVILDIFAT RARTHEAHLQ VELAQLEYAM PRLKRMWTHL SRYKGGIGVR GPGEKQLEED RRLVVHRIQD LKAKLGKVQA RKEREVAGRS DTPSVSLVGY TNAGKSTLMN ALTDAGVFVE DKLFATLDTR TRRWRLNGGG QVLLSDTVGF IRNLPHTLVA SFKATLEEAR QADLLLHVVD ASSPEAEMQI RAVKNVLEEL GLADQPTILV LNKADRVPDR SFLDVLKAHH HDPITISAAQ GDGIDRLEQA VRESLHERSL DAEIETGVEN GRVLAYLAQH AQIINRAYDE DDRVILQCRL PRRCLEFLYE NGANVRENGQ RLYA // ID L0DXW4_THIND Unreviewed; 454 AA. AC L0DXW4; DT 06-MAR-2013, integrated into UniProtKB/TrEMBL. DT 06-MAR-2013, sequence version 1. DT 07-JUN-2017, entry version 36. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX [H] {ECO:0000313|EMBL:AGA34414.1}; GN Synonyms=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=TVNIR_2776 {ECO:0000313|EMBL:AGA34414.1}; OS Thioalkalivibrio nitratireducens (strain DSM 14787 / UNIQEM 213 / OS ALEN2). OC Bacteria; Proteobacteria; Gammaproteobacteria; Chromatiales; OC Ectothiorhodospiraceae; Thioalkalivibrio. OX NCBI_TaxID=1255043 {ECO:0000313|EMBL:AGA34414.1, ECO:0000313|Proteomes:UP000010809}; RN [1] {ECO:0000313|Proteomes:UP000010809} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 14787 / UNIQEM 213 / ALEN2 RC {ECO:0000313|Proteomes:UP000010809}; RA Tikhonova T.V., Pavlov A.R., Beletsky A.V., Mardanov A.V., RA Sorokin D.Y., Ravin N.V., Popov V.O.; RT "Complete sequence of Thioalkalivibrio nitratireducens."; RL Submitted (DEC-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP003989; AGA34414.1; -; Genomic_DNA. DR RefSeq; WP_015259525.1; NC_019902.2. DR EnsemblBacteria; AGA34414; AGA34414; TVNIR_2776. DR KEGG; tni:TVNIR_2776; -. DR PATRIC; fig|1255043.3.peg.2801; -. DR KO; K03665; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000010809; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000010809}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000010809}. FT DOMAIN 199 367 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 165 195 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 454 AA; 49786 MW; F5E3FB7AF0E29682 CRC64; MFERPESGDR ALLVALAVGE PANIEPQIRE FQDLAESAGA EVVGLISGSR RNPDPRFFVG SGKADEIAAA VEATGADLAI FNHPLSPSQE RNLERHLKCR VLDRSGLILD IFAQRARSHE GKLQVELAQL RHMSTRLVRG WTHLERQKGG IGLRGPGETQ LETDRRLLAA RIKHIERRLE KVQRAREQGR QARRRNETPT VALVGYTNAG KSTLFNRLTE AQVYAADQLF ATLDPTLRRL DLAPHQSVIL ADTVGFVRDL PHELIAAFKA TLTETREAAL LLHVIDASDP EREVHVEQVE SVLEEIGAGE VPIWCVYNKI DCVPSADEGG TPARFEAGGD TLWVSAVTGA GVEALQTRLA NHFTETMFRG WVALPAAAGR LRSRLFAERA VEAEQTGADG RMHLRLNVPE RLLRALLREA GLEPDPHRLR VGAAEAPVAE PAEPDLAEAG HPGS // ID L0EE48_THECK Unreviewed; 428 AA. AC L0EE48; DT 06-MAR-2013, integrated into UniProtKB/TrEMBL. DT 06-MAR-2013, sequence version 1. DT 07-JUN-2017, entry version 31. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Theco_1752 {ECO:0000313|EMBL:AGA57884.1}; OS Thermobacillus composti (strain DSM 18247 / JCM 13945 / KWC4). OC Bacteria; Firmicutes; Bacilli; Bacillales; Paenibacillaceae; OC Thermobacillus. OX NCBI_TaxID=717605 {ECO:0000313|EMBL:AGA57884.1, ECO:0000313|Proteomes:UP000010795}; RN [1] {ECO:0000313|Proteomes:UP000010795} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 18247 / JCM 13945 / KWC4 RC {ECO:0000313|Proteomes:UP000010795}; RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S., RA Peters L., Ovchinnikova G., Teshima H., Detter J.C., Han C., Tapia R., RA Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Anderson I., RA Woyke T.; RT "Complete sequence of chromosome of Thermobacillus composti KWC4."; RL Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP003255; AGA57884.1; -; Genomic_DNA. DR RefSeq; WP_015254635.1; NC_019897.1. DR EnsemblBacteria; AGA57884; AGA57884; Theco_1752. DR KEGG; tco:Theco_1752; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000010795; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000010795}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000010795}. FT DOMAIN 207 371 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 166 193 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 428 AA; 47437 MW; AB8793B8F5C985FE CRC64; MTTLHETAAD IRERAILVSL VTDEIKRAGV DPEYSLRELV ALAETAGVEV LTAVTQHREA PDPRFFLGKG KVEELRAVAQ ELGATTAIFD QELSGAQVRN LEEGLDLKII DRTQLILDIF AGRAKTREGI IQVELAQLSY LLPRLAGHGK NLSRLGGGIG TRGPGETKLE TDRRHIRERI ADLKRQLKEV VRHRSVQRER RRKTGVTQVA LVGYTNAGKS TLLRELTNAD VYVENQLFAT LDPTSRAWTL PDGTEVVLTD TVGFIQNLPH ELVAAFRSTL EEAAEADLIL HVVDSSSPYR EEQMAVVDRI LTELGAGDRP RIVLYNKIDL CTNEELHLLR RDGDALLVSA FSASDREAIG RAVQDKLTGE IRSFAIPAAR GDLIALAHRM GEVVEQSVSD DGETMRIAVR LNKREYEVSG YKLQPYAL // ID L0EW17_LIBCB Unreviewed; 447 AA. AC L0EW17; DT 06-MAR-2013, integrated into UniProtKB/TrEMBL. DT 06-MAR-2013, sequence version 1. DT 07-JUN-2017, entry version 30. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=B488_11600 {ECO:0000313|EMBL:AGA65152.1}; OS Liberibacter crescens (strain BT-1). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Rhizobiaceae; Liberibacter. OX NCBI_TaxID=1215343 {ECO:0000313|EMBL:AGA65152.1, ECO:0000313|Proteomes:UP000010799}; RN [1] {ECO:0000313|EMBL:AGA65152.1, ECO:0000313|Proteomes:UP000010799} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BT-1 {ECO:0000313|EMBL:AGA65152.1, RC ECO:0000313|Proteomes:UP000010799}; RX PubMed=23408754; RA Leonard M.T., Fagen J.R., Davis-Richardson A.G., Davis M.J., RA Triplett E.W.; RT "Complete genome sequence of Liberibacter crescens BT-1."; RL Stand. Genomic Sci. 7:271-283(2012). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP003789; AGA65152.1; -; Genomic_DNA. DR EnsemblBacteria; AGA65152; AGA65152; B488_11600. DR KEGG; lcc:B488_11600; -. DR PATRIC; fig|1215343.11.peg.1196; -. DR KO; K03665; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000010799; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000010799}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000010799}. FT DOMAIN 217 388 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 447 AA; 50102 MW; 145D726D79DF1872 CRC64; MVVFLIKKDK ICKDTSRVIV VEVVLKSISS SADDISNISF SESRLHEAVG LAQAIDLQVV RSFVVAVSRP SPATLIRKGK IKEINTIIHD LDVGLIIIDQ SLTPVQQRNL EKIWNIKVID RIGLILEIFG RRALTKEGAL QVELAHLNYQ KGRLVRSWTH LERQRGGTGF LGGPGETQIE ADRRMLQQKI CYLEQQLEKV VRTRQLHRAK RKKVPYPIIA LVGYTNAGKS TLFNRITGSS VFVENMLFST LDPTLRRIIL PHGPVAFLAD TVGFISDLPT HLVAAFRATL EEVRQADVIL HVRDISNRNN AAQARDVYTI LSDLDIDVME DCGRILEVWN KVDCLEPHFR KEIFQEAASQ GAIPVSSITG DGFNVLASEI TRRLSGKTVT ENIVLSVNQL SFLPWIYQHA QVKRRNDMEN GSIHLNISIA HAELIGLEKL LSSHVVD // ID L0F9G4_DESDL Unreviewed; 538 AA. AC L0F9G4; DT 06-MAR-2013, integrated into UniProtKB/TrEMBL. DT 06-MAR-2013, sequence version 1. DT 07-JUN-2017, entry version 32. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Desdi_1857 {ECO:0000313|EMBL:AGA69306.1}; OS Desulfitobacterium dichloroeliminans (strain LMG P-21439 / DCA1). OC Bacteria; Firmicutes; Clostridia; Clostridiales; Peptococcaceae; OC Desulfitobacterium. OX NCBI_TaxID=871963 {ECO:0000313|EMBL:AGA69306.1, ECO:0000313|Proteomes:UP000010797}; RN [1] {ECO:0000313|Proteomes:UP000010797} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=LMG P-21439 / DCA1 {ECO:0000313|Proteomes:UP000010797}; RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S., RA Peters L., Ovchinnikova G., Teshima H., Detter J.C., Han C., Tapia R., RA Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Kruse T., RA de Vos W.M., Boon N., Smidt H., Woyke T.; RT "Complete sequence of Desulfitobacterium dichloroeliminans LMG P- RT 21439."; RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP003344; AGA69306.1; -; Genomic_DNA. DR RefSeq; WP_015262293.1; NC_019903.1. DR EnsemblBacteria; AGA69306; AGA69306; Desdi_1857. DR KEGG; ddl:Desdi_1857; -. DR KO; K03665; -. DR OMA; EREVIIT; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000010797; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000010797}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000010797}. FT DOMAIN 362 534 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 321 348 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 538 AA; 59247 MW; CB084C49BE9F1403 CRC64; MDILGDIAGI RGTQLKDLKE LTLLRTERPG LIHFDLLEGI CKLTSQWNKE IALYINRSGI VIAVAVGQHA TVKLPPLPAR QAGRLRCIHT HPSGNEHLSS MDLSALSSTG LESMSSLGVK NGQITGVEIA FPGDSGHEIL NLTPKEFRSF SYDTSVNDFR SRPASPVLKI SDQEKAFLVA LEDEDPGYEL LSELAELALT AGVEVVGKLL QPKRFGSPVS YLGKGKLQEL TQHLQDSGAN VLICDDELLP VQQRTLEQAT GIKVLDRTTL ILDIFALRAK SREGKLQVEL AQLKHLLPRL SGQGINLSRL GGGVGTRGPG ESKLEMDKRR VRKKINLLEA ELIEIRKVRT TQRRQREKSG IPLIALVGYT NAGKTTLLQK AMEQTRSKGE AIQGEDKLFA TLDPIVRGIK LNQTTHILLS DTVGFIQKLP HQLLHAFLAT LEEVQNADIL IHVLDASHPR ALERADTVHG ILGQLECSNK PRITLLNKTD KISHPSDLNR LAQELSHPIP MSLTQDSTLE PVWNKVLELL SVDKDETN // ID L0FWK1_ECHVK Unreviewed; 421 AA. AC L0FWK1; DT 06-MAR-2013, integrated into UniProtKB/TrEMBL. DT 06-MAR-2013, sequence version 1. DT 07-JUN-2017, entry version 33. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Echvi_1152 {ECO:0000313|EMBL:AGA77423.1}; OS Echinicola vietnamensis (strain DSM 17526 / LMG 23754 / KMM 6221). OC Bacteria; Bacteroidetes; Cytophagia; Cytophagales; Cyclobacteriaceae; OC Echinicola. OX NCBI_TaxID=926556 {ECO:0000313|EMBL:AGA77423.1, ECO:0000313|Proteomes:UP000010796}; RN [1] {ECO:0000313|Proteomes:UP000010796} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 17526 / LMG 23754 / KMM 6221 RC {ECO:0000313|Proteomes:UP000010796}; RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., RA Tice H., Bruce D., Goodwin L., Pitluck S., Peters L., Ovchinnikova G., RA Teshima H., Kyrpides N., Mavromatis K., Ivanova N., Brettin T., RA Detter J.C., Han C., Larimer F., Land M., Hauser L., Markowitz V., RA Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Brambilla E., RA Klenk H.-P., Eisen J.A.; RT "The complete genome of Echinicola vietnamensis DSM 17526."; RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP003346; AGA77423.1; -; Genomic_DNA. DR RefSeq; WP_015264987.1; NC_019904.1. DR EnsemblBacteria; AGA77423; AGA77423; Echvi_1152. DR KEGG; evi:Echvi_1152; -. DR PATRIC; fig|926556.3.peg.1212; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000010796; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 2. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000010796}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000010796}. FT DOMAIN 210 399 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 421 AA; 48262 MW; E041BF7DB7516547 CRC64; MSKYTRKLKK LIDTAPVEET AVLVALIKQN QSEQEVEEHL DELAFLTETL GAKEVYRFTQ RLEKPDVRSF VGSGKLEEIQ AYVKHFEVDM VIFDDDLSPS QMRNLENELK VQVYDRSLLI LDIFLNRAQT AQAKTQVELA RFQYLLPRLT RMWTHLERQR GGTATRGGAG EKEIETDKRI IRNQITLLKE KLRKIEKQGE TQRKGRKGIV RVALVGYTNV GKSTLMNLVT KSDVLAENKL FATVDSTVRK VVLENISFLL SDTVGFIRKL PTHLIESFKS TLMEIKESDL LVHVVDISHP GFEDHIAVVN QTLNELGAGD KPVLLVFNKI DLVPKMPSEE ALMNMSELEV EEANYLDLDR LKNVYTKKMG IEPVFMAAQD GTNIETFRKS LVSQVKKQHK KIYPHYLESE TYDLSQFDDM E // ID L0GZ67_9GAMM Unreviewed; 445 AA. AC L0GZ67; DT 06-MAR-2013, integrated into UniProtKB/TrEMBL. DT 06-MAR-2013, sequence version 1. DT 07-JUN-2017, entry version 31. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=Thimo_2391 {ECO:0000313|EMBL:AGA91127.1}; OS Thioflavicoccus mobilis 8321. OC Bacteria; Proteobacteria; Gammaproteobacteria; Chromatiales; OC Chromatiaceae; Thioflavicoccus. OX NCBI_TaxID=765912 {ECO:0000313|EMBL:AGA91127.1, ECO:0000313|Proteomes:UP000010816}; RN [1] {ECO:0000313|EMBL:AGA91127.1, ECO:0000313|Proteomes:UP000010816} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=8321 {ECO:0000313|EMBL:AGA91127.1, RC ECO:0000313|Proteomes:UP000010816}; RG US DOE Joint Genome Institute; RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S., RA Peters L., Ovchinnikova G., Lu M., Detter J.C., Han C., Tapia R., RA Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Vogl K., RA Liu Z., Imhoff J., Thiel V., Frigaard N.-U., Bryant D., Woyke T.; RT "Complete sequence of chromosome of Thioflavicoccus mobilis 8321."; RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP003051; AGA91127.1; -; Genomic_DNA. DR RefSeq; WP_015281260.1; NC_019940.1. DR EnsemblBacteria; AGA91127; AGA91127; Thimo_2391. DR KEGG; tmb:Thimo_2391; -. DR PATRIC; fig|765912.4.peg.2341; -. DR KO; K03665; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000010816; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR Gene3D; 3.40.50.1220; -; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR029035; DHS-like_NAD/FAD-binding_dom. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000010816}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000010816}. FT DOMAIN 198 365 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 445 AA; 48326 MW; F4AD569F891142CC CRC64; MLERPRSGEQ AVLVNLTIGP SDGEAAAEEL RQLADAAGAV CVGTLGGSRA VPDARLFIGS GKAEELKGLV AAEGADLVIF NHVLSPAQQR NLERELGRRV VDRTGLILDI FAQRARSFEG KLQVELAQLE HLATRLVRGW THLERQKGGI GLRGPGETQL ETDRRLLDKR IAVLKRRLAR IGAQRDQGRR ARRKAELPAV ALVGYTNAGK STLFNRLTGA GVYQADQLFA TLDPTLRRLP LPSGQVVTVA DTVGFVSDLP HELVAAFRAT LEETRSAELL LHVIDAAAAT RDRQIEDVTA VLAEIGAEAV PQLQVMNKID LLEDAMPRVE YDAQGRPARV WLSAGDGVGL DLLMAAIAER CRGADTRRRV RLAPRDGRLR AWLYSHGQVL VDVELPAGGW EIEVRIPALA LERLRHRDPA AASVLDAAPD MADQSVVDWP TMLAG // ID L0IAC0_HALRX Unreviewed; 473 AA. AC L0IAC0; DT 06-MAR-2013, integrated into UniProtKB/TrEMBL. DT 06-MAR-2013, sequence version 1. DT 07-JUN-2017, entry version 32. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Halru_1151 {ECO:0000313|EMBL:AGB15768.1}; OS Halovivax ruber (strain DSM 18193 / JCM 13892 / XH-70). OC Archaea; Euryarchaeota; Halobacteria; Natrialbales; Natrialbaceae; OC Halovivax. OX NCBI_TaxID=797302 {ECO:0000313|EMBL:AGB15768.1, ECO:0000313|Proteomes:UP000010846}; RN [1] {ECO:0000313|Proteomes:UP000010846} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 18193 / JCM 13892 / XH-70 RC {ECO:0000313|Proteomes:UP000010846}; RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S., RA Peters L., Mikhailova N., Davenport K., Detter J.C., Han C., Tapia R., RA Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Sproer C., RA Anderson I., Woyke T.; RT "Complete sequence of Halovivax ruber XH-70."; RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP003050; AGB15768.1; -; Genomic_DNA. DR EnsemblBacteria; AGB15768; AGB15768; Halru_1151. DR KEGG; hru:Halru_1151; -. DR KO; K03665; -. DR OMA; VILEIFH; -. DR OrthoDB; POG093Z07D6; -. DR Proteomes; UP000010846; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000010846}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000010846}. FT DOMAIN 227 412 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 473 AA; 51955 MW; 17946044A07386E9 CRC64; MQRNADRQTA STSEEPTTGS QTDEAATSGS ATGEETTNRD DSGSIAKKGT AIVAARGNQA PVETTEIRQL TEAAGYRVVD EFTQVRPRDP GTNLGDGKVA EIARRAEVTE AMALVVDGEL TPTQTTTLAA RMPDETRVFD RYRLILAIFA EQARHRRAQL QVELARLRYD LPRIKEAADE GLLNRRTERG TPYYDVRDRI DRLERKLEEL PTPAEQFRER RRQEGFDLVT LAGYTNAGKS TLLHRLADDL SVTDASPAHP DETGVAEIED RLFKTLETTT RRATLDERPT LVTDTVGFVQ DLPHWLVQSF SETLSEAASA DVVVLVADGA DPVGEFEAKL DVSLSVLDEQ DVARDDVVVT VNKIDCQSSA DVERRRRIAA ERADSVVTMS ASEGTNFDRL VDAIAARLPS RRETITLPNG DEAMSLLSWL YDHVTVDSVE YTGKTVVITV DGRPSVIAKA LARAEAIAAT AEE // ID L0IC33_HALRX Unreviewed; 433 AA. AC L0IC33; DT 06-MAR-2013, integrated into UniProtKB/TrEMBL. DT 06-MAR-2013, sequence version 1. DT 07-JUN-2017, entry version 34. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Halru_1774 {ECO:0000313|EMBL:AGB16373.1}; OS Halovivax ruber (strain DSM 18193 / JCM 13892 / XH-70). OC Archaea; Euryarchaeota; Halobacteria; Natrialbales; Natrialbaceae; OC Halovivax. OX NCBI_TaxID=797302 {ECO:0000313|EMBL:AGB16373.1, ECO:0000313|Proteomes:UP000010846}; RN [1] {ECO:0000313|Proteomes:UP000010846} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 18193 / JCM 13892 / XH-70 RC {ECO:0000313|Proteomes:UP000010846}; RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S., RA Peters L., Mikhailova N., Davenport K., Detter J.C., Han C., Tapia R., RA Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Sproer C., RA Anderson I., Woyke T.; RT "Complete sequence of Halovivax ruber XH-70."; RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP003050; AGB16373.1; -; Genomic_DNA. DR EnsemblBacteria; AGB16373; AGB16373; Halru_1774. DR KEGG; hru:Halru_1774; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG093Z07D6; -. DR Proteomes; UP000010846; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000010846}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000010846}. FT DOMAIN 186 369 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 102 129 {ECO:0000256|SAM:Coils}. FT COILED 152 182 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 433 AA; 48087 MW; 9C80C1EC2895DF98 CRC64; MRAVIAKRVD SGVPDTSEIT DLAEAAGYTV VGECTQTRTA DAALQLGEGK VGELATLVAE TDATTVIFDN RLGPYQTYNL GQRLPEGAEV IDRFTLILEI FGQRAQTRKA QLQVELAELR YELPRAEAKA SLARRDEHPG FMGLGEYDES REEDIKAQIS RIRDELAQIE QTEEQRRARR RDSGFDLVAL AGYTNAGKST LLRRLASDLD VDENADLHPD LDATAESEDR LFTTLGTTTR RADIEPRDVL VTDTVGFISD LPHWLVESFK STLDSVYRAD LVLLVVDVSE PIDEIHEKLV TSHDTLYERN EAPIVTVFNK IDRVSDEELA EKRRALSGLA PNPVAVSARE GEGVDRLLGR IDAELPDWEH ERLVLPMTDD TMSVVSWIHD NAHVEDVTYG DADVHVSFEA RPEIVARART RAGDLREAAA ESA // ID L0IV74_9MYCO Unreviewed; 470 AA. AC L0IV74; DT 06-MAR-2013, integrated into UniProtKB/TrEMBL. DT 06-MAR-2013, sequence version 1. DT 07-JUN-2017, entry version 35. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=Mycsm_02569 {ECO:0000313|EMBL:AGB22904.1}; OS Mycobacterium sp. JS623. OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae; OC Mycobacterium. OX NCBI_TaxID=212767 {ECO:0000313|EMBL:AGB22904.1, ECO:0000313|Proteomes:UP000010844}; RN [1] {ECO:0000313|Proteomes:UP000010844} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=JS623 {ECO:0000313|Proteomes:UP000010844}; RG US DOE Joint Genome Institute; RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S., RA Peters L., Teshima H., Detter J.C., Han C., Tapia R., Land M., RA Hauser L., Kyrpides N., Ivanova N., Pagani I., Mattes T., Holmes A., RA Rutledge P., Paulsen I., Coleman N., Woyke T.; RT "Complete sequence of chromosome of Mycobacterium smegmatis JS623."; RL Submitted (OCT-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP003078; AGB22904.1; -; Genomic_DNA. DR RefSeq; WP_015306484.1; NC_019966.1. DR EnsemblBacteria; AGB22904; AGB22904; Mycsm_02569. DR KEGG; msa:Mycsm_02569; -. DR PATRIC; fig|710686.3.peg.2589; -. DR KO; K03665; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000010844; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000010844}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}. FT DOMAIN 247 416 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 206 233 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 470 AA; 50567 MW; D119F5F7BAD7A647 CRC64; MTYPDFRPGT PSAGELALED RTALRRVAGL STELADVSEV EYRQLRLERV VLVGVWTEGS AADADASMAE LAALAETAGS EVLEGLVQRR DKPDPSTYIG SGKAQELREV VLATGADTVI CDGELSPAQL TALEKAVKVK VIDRTALILD IFAQHATSRE GKAQVAYAQM EYMLPRLRGW GESMSRQAGG RAGGSGGGVG LRGPGETKIE TDRRRIRERM SKLRREIKDM KTVRDTQRSK RVASDVPSIA IVGYTNAGKS SLLNALTGAG VLVENALFAT LEPTTRRGEF ADGRPFVLTD TVGFVRHLPT QLVEAFRSTL EEVVDANLLV HVVDGSDVNP LAQINAVRQV VNEVVTDHDG KPPPELLVVN KIDAADGLTL AQLRSALPDA VFVSARTGDG LERLQQRMAA VIEPTDTAVD VTIPYDRGDL VNKVHADGRV DATEHTAHGT RIKARVPVPL AASLQEFATF // ID L0JNE1_NATP1 Unreviewed; 433 AA. AC L0JNE1; DT 06-MAR-2013, integrated into UniProtKB/TrEMBL. DT 06-MAR-2013, sequence version 1. DT 07-JUN-2017, entry version 35. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Natpe_2521 {ECO:0000313|EMBL:AGB32333.1}; OS Natrinema pellirubrum (strain DSM 15624 / CIP 106293 / JCM 10476 / OS NCIMB 786 / 157). OC Archaea; Euryarchaeota; Halobacteria; Natrialbales; Natrialbaceae; OC Natrinema. OX NCBI_TaxID=797303 {ECO:0000313|EMBL:AGB32333.1, ECO:0000313|Proteomes:UP000010843}; RN [1] {ECO:0000313|Proteomes:UP000010843} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 15624 / JCM 10476 / NCIMB 786 RC {ECO:0000313|Proteomes:UP000010843}; RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S., RA Peters L., Teshima H., Detter J.C., Han C., Tapia R., Land M., RA Hauser L., Kyrpides N., Ivanova N., Pagani I., Sproer C., Anderson I., RA Woyke T.; RT "Complete sequence of chromosome of Natrinema pellirubrum DSM 15624."; RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP003372; AGB32333.1; -; Genomic_DNA. DR RefSeq; WP_015299077.1; NZ_AOIE01000070.1. DR EnsemblBacteria; AGB32333; AGB32333; Natpe_2521. DR GeneID; 14335684; -. DR KEGG; npe:Natpe_2521; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG093Z07D6; -. DR Proteomes; UP000010843; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000010843}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000010843}. FT DOMAIN 186 369 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 102 129 {ECO:0000256|SAM:Coils}. FT COILED 152 182 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 433 AA; 48558 MW; 22D90DABFB371A28 CRC64; MNTIIAKRVD SGTPDTSEIR DLARAAGYTV VGEVTQSRRA DPALQIGEGK AEELAALVEE TDATTVIFDN RLGPYQTYNL GQLLPEGVEV IDRFTLILEI FGQRAQTRKA QLQVELAELR YELPRAEAKT SLAKREEHPG FMGLGEYDES REQDIKAQIS RIKDELERIE QTEQQRRERR RDSGFDLVAL AGYTNAGKST LLRQLATDLE VEENEDLHRD LDPTAESQDK LFTTLGTTTR RADIDRRDVL VTDTVGFISD LPHWLVESFK STLDSVYRAD LVLLVVDVSE PIDEIHEKLV TSHDTLYERN EAPIVTVLNK IDQVDDAELA EKREALSSLA PNPVTVSAKE GLNVDGLLER IERELPDWEA ERLLLPMTDD TMSVVSWLHD NARVDDVTYG DEDVVVSFEA RPAVISQARS RASELRTTAA ESA // ID L0JUE7_9EURY Unreviewed; 435 AA. AC L0JUE7; DT 06-MAR-2013, integrated into UniProtKB/TrEMBL. DT 06-MAR-2013, sequence version 1. DT 07-JUN-2017, entry version 31. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=Natoc_0504 {ECO:0000313|EMBL:AGB36366.1}; OS Natronococcus occultus SP4. OC Archaea; Euryarchaeota; Halobacteria; Natrialbales; Natrialbaceae; OC Natronococcus. OX NCBI_TaxID=694430 {ECO:0000313|EMBL:AGB36366.1, ECO:0000313|Proteomes:UP000010878}; RN [1] {ECO:0000313|EMBL:AGB36366.1, ECO:0000313|Proteomes:UP000010878} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SP4 {ECO:0000313|EMBL:AGB36366.1, RC ECO:0000313|Proteomes:UP000010878}; RG DOE Joint Genome Institute; RA Eisen J., Huntemann M., Wei C.-L., Han J., Detter J.C., Han C., RA Tapia R., Chen A., Kyrpides N., Mavromatis K., Markowitz V., Szeto E., RA Ivanova N., Mikhailova N., Ovchinnikova G., Pagani I., Pati A., RA Goodwin L., Nordberg H.P., Cantor M.N., Hua S.X., Woyke T., Eisen J., RA Klenk H.-P., Klenk H.-P.; RT "FINISHED of Natronococcus occultus SP4, DSM 3396."; RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP003929; AGB36366.1; -; Genomic_DNA. DR RefSeq; WP_015319822.1; NC_019974.1. DR EnsemblBacteria; AGB36366; AGB36366; Natoc_0504. DR GeneID; 14405532; -. DR KEGG; nou:Natoc_0504; -. DR KO; K03665; -. DR OrthoDB; POG093Z07D6; -. DR Proteomes; UP000010878; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000010878}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000010878}. FT DOMAIN 188 379 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 435 AA; 47762 MW; 12372123B93AC482 CRC64; MSRSAPSQTA RAVVAKRAPN APVETDEIES LARANGDDVV ATVTQVGPND SGTYLGSGKL DELATVVADR EADRVVVDDG LTPDQHHTIE RRMPAETVVV DRYRLVLELF ESQAGTRRAQ LQVELARLQY DLPRVIAAAD EGMLNQQTEK GSRIYDVEER IDRLETKLEE LPDPAEQFRE RRREEGFDLV TLAGYTNAGK STLLHRLADD MSLEDRDEDA PADDGDATAA IEDRLFETLE TTTRRATLDG RPALVTDTVG FVDELPHELV ESFSSTLSEA AAADVVVLVA DASDDLERFR NRLSVSLDVL AAQGVDAERI VPVVNKADAL SDAERRRRYS TASDLVPEDA ATPILASVLA GTNVEDVRDA IRERFPEERA TLTLPNTDAA MSLVSTAHDR TTVESVDYEG ETVELACRGR PDVLERLRGR AEQLE // ID L0JZQ6_9EURY Unreviewed; 433 AA. AC L0JZQ6; DT 06-MAR-2013, integrated into UniProtKB/TrEMBL. DT 06-MAR-2013, sequence version 1. DT 07-JUN-2017, entry version 33. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=Natoc_1526 {ECO:0000313|EMBL:AGB37333.1}; OS Natronococcus occultus SP4. OC Archaea; Euryarchaeota; Halobacteria; Natrialbales; Natrialbaceae; OC Natronococcus. OX NCBI_TaxID=694430 {ECO:0000313|EMBL:AGB37333.1, ECO:0000313|Proteomes:UP000010878}; RN [1] {ECO:0000313|EMBL:AGB37333.1, ECO:0000313|Proteomes:UP000010878} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SP4 {ECO:0000313|EMBL:AGB37333.1, RC ECO:0000313|Proteomes:UP000010878}; RG DOE Joint Genome Institute; RA Eisen J., Huntemann M., Wei C.-L., Han J., Detter J.C., Han C., RA Tapia R., Chen A., Kyrpides N., Mavromatis K., Markowitz V., Szeto E., RA Ivanova N., Mikhailova N., Ovchinnikova G., Pagani I., Pati A., RA Goodwin L., Nordberg H.P., Cantor M.N., Hua S.X., Woyke T., Eisen J., RA Klenk H.-P., Klenk H.-P.; RT "FINISHED of Natronococcus occultus SP4, DSM 3396."; RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP003929; AGB37333.1; -; Genomic_DNA. DR RefSeq; WP_015320783.1; NC_019974.1. DR EnsemblBacteria; AGB37333; AGB37333; Natoc_1526. DR GeneID; 14404610; -. DR KEGG; nou:Natoc_1526; -. DR KO; K03665; -. DR OrthoDB; POG093Z07D6; -. DR Proteomes; UP000010878; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000010878}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Hydrolase {ECO:0000313|EMBL:AGB37333.1}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000010878}. FT DOMAIN 186 369 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 102 129 {ECO:0000256|SAM:Coils}. FT COILED 152 182 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 433 AA; 48569 MW; F52A13DD43ACA6E0 CRC64; MNAIIAKRVD SGTADTTEIR ELAEAAGYTV LGEVTQSRTA DAALQLGEGK AEELAAVAER TDVETVIFDN RLGPYQTYNL GQLLPEGVEV IDRFTLILEI FGQRAQTRKA QLQVELAELR YELPRAEAKT SLAKRDEHPG FMGLGEYDES REQDIKAQIS RIKDELEQIE QTEEHRRERR RDSGFDLVAL AGYTNAGKST LLRQLATDLE IEENEQLHPD LDTTAESQDR LFTTLGTTTR RADIEPRDVL VTDTVGFISD LPHWLVESFK STLDSVYRAD LVLLVVDVSE DVDEIHEKLV TSHDTLYERN EAPIVTVLNK VDQVDEEELE RKKEALSALA PNPVVVSARE GTNVDELLER IDRELPDWEE ERLVLPMTDD TMSVVSWLHD NAHVEDVNYG DDDVLVSFEA RPAVISQARS RASELQTAAA ESA // ID L0KDJ6_HALHC Unreviewed; 559 AA. AC L0KDJ6; DT 06-MAR-2013, integrated into UniProtKB/TrEMBL. DT 06-MAR-2013, sequence version 1. DT 07-JUN-2017, entry version 32. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Halha_2570 {ECO:0000313|EMBL:AGB42444.1}; OS Halobacteroides halobius (strain ATCC 35273 / DSM 5150 / MD-1). OC Bacteria; Firmicutes; Clostridia; Halanaerobiales; Halobacteroidaceae; OC Halobacteroides. OX NCBI_TaxID=748449 {ECO:0000313|EMBL:AGB42444.1, ECO:0000313|Proteomes:UP000010880}; RN [1] {ECO:0000313|Proteomes:UP000010880} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 35273 / DSM 5150 / MD-1 RC {ECO:0000313|Proteomes:UP000010880}; RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., RA Tice H., Bruce D., Goodwin L., Pitluck S., Peters L., Mikhailova N., RA Gu W., Kyrpides N., Mavromatis K., Ivanova N., Brettin T., RA Detter J.C., Han C., Larimer F., Land M., Hauser L., Markowitz V., RA Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Tindall B., Pomrenke H., RA Brambilla E., Klenk H.-P., Eisen J.A.; RT "The complete genome of Halobacteroides halobius DSM 5150."; RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP003359; AGB42444.1; -; Genomic_DNA. DR EnsemblBacteria; AGB42444; AGB42444; Halha_2570. DR KEGG; hhl:Halha_2570; -. DR PATRIC; fig|748449.3.peg.2492; -. DR KO; K03665; -. DR OMA; EREVIIT; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000010880; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000010880}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000010880}. FT DOMAIN 341 506 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 310 337 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 559 AA; 64210 MW; 72499F80DCAFBA64 CRC64; MNNLDKLLEF RLERGKLITQ QLLNKVVDFN EEQINLLLNR KGQVIDYQLG TLQTDLIEGV RRRRSKKRLS GLRILVFHKG KRRIKKELVL KYRLDNLTYF NLNRQYLEII FPEIKQGRLT GIAKQQLGLK EADTFNYVDI VYKLEEELSH VETHQIKQSQ ERAILVGSKE ESLKELKNLT TTAKVEVVTN LTIRDRVVDP AYYIGQGKVS QIKRTLINQQ ANVIIFDDEL TPAQYSNLEE GLGVKVIDRT QLILDIFAQQ AQTKEGQLQV ELAQLKYLLP RLIGQGAKMS RLGGGIGTRG PGETKLEIDR RRIRKRIHRL KKDLKKIRKN RQLQRKNRRH PVISLVGYTN AGKSTVMNLL TKAEVEAKGR LFATLDSTLR QIKLPIGRQV IVSDTVGFIK KLPHDLIAAF KATLEEIKEA NLLLHVVDSS HPNLKERMAV VHDELEDLGV LDKEIITVFN KADLVADNKL DLLQRDYPNS VVISALHGKG KERLLNKISS FIVQGMIKVK LKLSYDKANW LDRIYQEGRV LNRSYDNQGI KLEAQIPNRL AAKLKKYKI // ID L0KY40_METHD Unreviewed; 414 AA. AC L0KY40; DT 06-MAR-2013, integrated into UniProtKB/TrEMBL. DT 06-MAR-2013, sequence version 1. DT 07-JUN-2017, entry version 34. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Metho_0748 {ECO:0000313|EMBL:AGB48998.1}; OS Methanomethylovorans hollandica (strain DSM 15978 / NBRC 107637 / OS DMS1). OC Archaea; Euryarchaeota; Methanomicrobia; Methanosarcinales; OC Methanosarcinaceae; Methanomethylovorans. OX NCBI_TaxID=867904 {ECO:0000313|EMBL:AGB48998.1, ECO:0000313|Proteomes:UP000010866}; RN [1] {ECO:0000313|Proteomes:UP000010866} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 15978 / NBRC 107637 / DMS1 RC {ECO:0000313|Proteomes:UP000010866}; RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., RA Tice H., Bruce D., Goodwin L., Pitluck S., Peters L., Mikhailova N., RA Held B., Kyrpides N., Mavromatis K., Ivanova N., Brettin T., RA Detter J.C., Han C., Larimer F., Land M., Hauser L., Markowitz V., RA Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Spring S., Schroeder M., RA Brambilla E., Klenk H.-P., Eisen J.A.; RT "Complete sequence of chromosome of Methanomethylovorans hollandica RT DSM 15978."; RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP003362; AGB48998.1; -; Genomic_DNA. DR RefSeq; WP_015324166.1; NC_019977.1. DR EnsemblBacteria; AGB48998; AGB48998; Metho_0748. DR GeneID; 14407961; -. DR KEGG; mhz:Metho_0748; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG093Z07D6; -. DR Proteomes; UP000010866; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000010866}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000010866}. FT DOMAIN 191 360 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 414 AA; 46852 MW; B57E734FCD46E69D CRC64; MKKVIVVQRV DPDSDDLKNK RQLAELKDLA FAANYSVTGE VIQSRYPDKK YQLGKGKVQE LALSVKALDA EKVIFCNELS SMQLYNITDT CKCAVIDKFQ LILEIFALRA TTRRAKLQVE LARLEYEIPR AKIIVSHLKK EERPGFMGLG SYEDSYEQDI KGRIARIKGE LSHVQGHNES LRTFRHAHGL SMVALAGYTN AGKSTLFNAL MEEDVDVADM LFTTLSPVAR SMDVMGRKVI LTDTVGFIED LPHWLIDAFR STLDEIFFAD IILLVVDASE PLDIMHDKLL TCHETLWEQV HDASVITVMN KTDLISQEEL NEKMEALGYL VPNPVYISAK TMGGLGDLKQ AIRSKLPVWE RKEISMPFSK HSMSVLSWLF KEGVVHSVKY TDQILVDLEA REEVINKVIS FIDV // ID L0MDB6_SERMA Unreviewed; 426 AA. AC L0MDB6; DT 06-MAR-2013, integrated into UniProtKB/TrEMBL. DT 06-MAR-2013, sequence version 1. DT 30-AUG-2017, entry version 40. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=D781_0335 {ECO:0000313|EMBL:AGB80701.1}; OS Serratia marcescens FGI94. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; OC Yersiniaceae; Serratia. OX NCBI_TaxID=1249634 {ECO:0000313|EMBL:AGB80701.1, ECO:0000313|Proteomes:UP000011001}; RN [1] {ECO:0000313|EMBL:AGB80701.1, ECO:0000313|Proteomes:UP000011001} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=FGI94 {ECO:0000313|EMBL:AGB80701.1, RC ECO:0000313|Proteomes:UP000011001}; RX PubMed=23516234; RA Aylward F.O., Tremmel D.M., Starrett G.J., Bruce D.C., Chain P., RA Chen A., Davenport K.W., Detter C., Han C.S., Han J., Huntemann M., RA Ivanova N.N., Kyrpides N.C., Markowitz V., Mavrommatis K., Nolan M., RA Pagani I., Pati A., Pitluck S., Teshima H., Deshpande S., Goodwin L., RA Woyke T., Currie C.R.; RT "Complete Genome of Serratia sp. Strain FGI 94, a Strain Associated RT with Leaf-Cutter Ant Fungus Gardens."; RL Genome Announc. 1:E0023912-E0023912(2013). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP003942; AGB80701.1; -; Genomic_DNA. DR RefSeq; WP_015344294.1; NC_020064.1. DR EnsemblBacteria; AGB80701; AGB80701; D781_0335. DR GeneID; 32371135; -. DR KEGG; smaf:D781_0335; -. DR PATRIC; fig|1249634.3.peg.300; -. DR KO; K03665; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000011001; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000011001}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}. FT DOMAIN 198 365 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 426 AA; 48118 MW; FD4E681D42EEA6D5 CRC64; MFDRYEAGEQ AVLVHIYFSQ DKDTEDLSEF ESLVSSAGVQ ALQVVTGSRK APHPKYFVGE GKAEEIADAV KASGASVVLF DHALSPAQER NLERLCECRV IDRTGLILDI FAQRARTHEG KLQVELAQLR HIATRLVRGW THLERQKGGI GLRGPGETQL ETDRRLLRDR ISLILRRLER VEKQREQGRR ARTRADVPTV SLVGYTNAGK STLFNRMTSA EVYAADQLFA TLDPTLRRID VADVGDTVLA DTVGFIRHLP HDLVAAFKAT LQETRQASLL LHVIDAADSR VDENIEAVNS VLTEIESDEI PTLLVMNKID MLDDFVPRID RNDENLPIRV WLSAVSGEGI PLLYQALTER LSGEIAHHEL RLPPQAGRLR SRFYQLQAIE KEWNEEDGSI GMVVRMPIVE WRRLCKQEHD LINFIV // ID L0NGD2_9RHIZ Unreviewed; 456 AA. AC L0NGD2; DT 06-MAR-2013, integrated into UniProtKB/TrEMBL. DT 06-MAR-2013, sequence version 1. DT 12-APR-2017, entry version 28. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=NT26_1638 {ECO:0000313|EMBL:CCF19362.1}; OS Rhizobium sp. NT-26. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium. OX NCBI_TaxID=1125847 {ECO:0000313|EMBL:CCF19362.1, ECO:0000313|Proteomes:UP000010792}; RN [1] {ECO:0000313|EMBL:CCF19362.1, ECO:0000313|Proteomes:UP000010792} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NT-26 {ECO:0000313|EMBL:CCF19362.1, RC ECO:0000313|Proteomes:UP000010792}; RX PubMed=23589360; DOI=10.1093/gbe/evt061; RA Andres J., Arsene-Ploetze F., Barbe V., Brochier-Armanet C., RA Cleiss-Arnold J., Coppee J.Y., Dillies M.A., Geist, L, Joublin A., RA Koechler S., Lassalle F., Marchal M., Medigue C., Muller D., Nesme X., RA Plewniak F., Proux C., Ramirez-Bahena M.H., Schenowitz C., RA Sismeiro O., Vallenet D., Santini J.M., Bertin P.N.; RT "Life in an arsenic-containing gold mine: genome and physiology of the RT autotrophic arsenite-oxidizing bacterium rhizobium sp. NT-26."; RL Genome Biol. Evol. 5:934-953(2013). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; FO082820; CCF19362.1; -; Genomic_DNA. DR EnsemblBacteria; CCF19362; CCF19362; NT26_1638. DR Proteomes; UP000010792; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000010792}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000010792}. FT DOMAIN 218 390 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 177 211 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 456 AA; 50686 MW; 997F7B3A3158E759 CRC64; MIPETDRRRD DMRAVVLVPV LKNARASRAA QPEAAPAPQR SEEARLEEAI GLARAIDLEV VQGLIVQVSQ PRPATLMGTG KIGEIKALLD QHDAGLVIVD HPLTPVQQRN LEKEWNAKVI DRTGLILEIF GRRASTKEGT LQVDLAHLNY QKGRLVRSWT HLERQRGGAG FMGGPGETQI EADRRLLQER IVKLERELEQ VVRTRQLHRA KRRKVPHPIV ALVGYTNAGK STLFNRITGA GVLAEDMLFA TLDPTLRRMK LPHGRTVILS DTVGFISDLP THLVAAFRAT LEEVLEADLI LHVRDMSDPD NAAQSADVMR ILSDLGIDEK EREARIIEVW NKIDRLDPEA HDAMAERASG RDNIMAVSAI TGEGVDALLA EIARRLSGVL TETTVAIPAD KLALVSWVYE NAIVDERRDQ EDGSVELDVR LSESQAAALE RRLGNGPRPE KEDWER // ID L0WGX0_9GAMM Unreviewed; 455 AA. AC L0WGX0; DT 06-MAR-2013, integrated into UniProtKB/TrEMBL. DT 06-MAR-2013, sequence version 1. DT 30-AUG-2017, entry version 32. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=A11A3_00580 {ECO:0000313|EMBL:EKF75944.1}; OS Alcanivorax hongdengensis A-11-3. OC Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales; OC Alcanivoracaceae; Alcanivorax. OX NCBI_TaxID=1177179 {ECO:0000313|EMBL:EKF75944.1, ECO:0000313|Proteomes:UP000010164}; RN [1] {ECO:0000313|EMBL:EKF75944.1, ECO:0000313|Proteomes:UP000010164} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=A-11-3 {ECO:0000313|EMBL:EKF75944.1, RC ECO:0000313|Proteomes:UP000010164}; RX PubMed=23209226; DOI=10.1128/JB.01849-12; RA Lai Q., Shao Z.; RT "Genome Sequence of the Alkane-Degrading Bacterium Alcanivorax RT hongdengensis Type Strain A-11-3."; RL J. Bacteriol. 194:6972-6972(2012). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EKF75944.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AMRJ01000001; EKF75944.1; -; Genomic_DNA. DR RefSeq; WP_008927307.1; NZ_AMRJ01000001.1. DR EnsemblBacteria; EKF75944; EKF75944; A11A3_00580. DR PATRIC; fig|1177179.3.peg.115; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000010164; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000010164}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}. FT DOMAIN 205 371 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 455 AA; 50830 MW; D29EF3F725D498B7 CRC64; MDLFDRTEQT RTGAGERAIL VHMELPDAMG REDLDEFHHL VTSSGVVPAV ELTGKRDRPD PALFIGSGKS EELAALVKEH EADVVLFNHA LSPAQERNLE RAVKCRVLDR TGLILDIFAQ RARTHEGRLQ VELAQLRHLS SRLVRGWTHL ERQKGGIGLR GPGETQLETD RRLLRDRIRA IESRLDKVRK QRAQGRRARQ RAETPLISLV GYTNAGKSTL FNAITTGDVY VADQLFATLD PTLRKVKIPG VGPAILADTV GFIRHLPHRL GQAFRATLEE TVNASLLLHV TDCSAEERDA NVEAVNEVLE EIKAEKIPVL HVYNKVDNLD QPPRLERDEH GQPWRVWISA HTGDGFDLLF DAIAERLAVG WVDCWLKLPP AAGRLRARLH EAGEVLEETT ATDGSMLLRV TVNRVHFERL LREQGLKEED LRVAAPTVAE GEAPSYNSER SPKAG // ID L1IDN1_GUITH Unreviewed; 473 AA. AC L1IDN1; DT 06-MAR-2013, integrated into UniProtKB/TrEMBL. DT 06-MAR-2013, sequence version 1. DT 07-JUN-2017, entry version 22. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EKX34019.1, ECO:0000313|EnsemblProtists:EKX34019}; GN ORFNames=GUITHDRAFT_147529 {ECO:0000313|EMBL:EKX34019.1}; OS Guillardia theta CCMP2712. OC Eukaryota; Cryptophyta; Pyrenomonadales; Geminigeraceae; Guillardia. OX NCBI_TaxID=905079 {ECO:0000313|EMBL:EKX34019.1, ECO:0000313|Proteomes:UP000011087}; RN [1] {ECO:0000313|EMBL:EKX34019.1, ECO:0000313|EnsemblProtists:EKX34019, ECO:0000313|Proteomes:UP000011087} RP NUCLEOTIDE SEQUENCE. RC STRAIN=CCMP2712 {ECO:0000313|EMBL:EKX34019.1, RC ECO:0000313|Proteomes:UP000011087}; RX PubMed=23201678; DOI=10.1038/nature11681; RG DOE Joint Genome Institute; RA Curtis B.A., Tanifuji G., Burki F., Gruber A., Irimia M., Maruyama S., RA Arias M.C., Ball S.G., Gile G.H., Hirakawa Y., Hopkins J.F., Kuo A., RA Rensing S.A., Schmutz J., Symeonidi A., Elias M., Eveleigh R.J., RA Herman E.K., Klute M.J., Nakayama T., Obornik M., Reyes-Prieto A., RA Armbrust E.V., Aves S.J., Beiko R.G., Coutinho P., Dacks J.B., RA Durnford D.G., Fast N.M., Green B.R., Grisdale C.J., Hempel F., RA Henrissat B., Hoppner M.P., Ishida K., Kim E., Koreny L., Kroth P.G., RA Liu Y., Malik S.B., Maier U.G., McRose D., Mock T., Neilson J.A., RA Onodera N.T., Poole A.M., Pritham E.J., Richards T.A., Rocap G., RA Roy S.W., Sarai C., Schaack S., Shirato S., Slamovits C.H., RA Spencer D.F., Suzuki S., Worden A.Z., Zauner S., Barry K., Bell C., RA Bharti A.K., Crow J.A., Grimwood J., Kramer R., Lindquist E., RA Lucas S., Salamov A., McFadden G.I., Lane C.E., Keeling P.J., RA Gray M.W., Grigoriev I.V., Archibald J.M.; RT "Algal genomes reveal evolutionary mosaicism and the fate of RT nucleomorphs."; RL Nature 492:59-65(2012). RN [2] {ECO:0000313|EnsemblProtists:EKX34019, ECO:0000313|Proteomes:UP000011087} RP NUCLEOTIDE SEQUENCE. RC STRAIN=CCMP2712 {ECO:0000313|EnsemblProtists:EKX34019, RC ECO:0000313|Proteomes:UP000011087}; RA Kuo A., Curtis B.A., Tanifuji G., Burki F., Gruber A., Irimia M., RA Maruyama S., Arias M.C., Ball S.G., Gile G.H., Hirakawa Y., RA Hopkins J.F., Rensing S.A., Schmutz J., Symeonidi A., Elias M., RA Eveleigh R.J., Herman E.K., Klute M.J., Nakayama T., Obornik M., RA Reyes-Prieto A., Armbrust E.V., Aves S.J., Beiko R.G., Coutinho P., RA Dacks J.B., Durnford D.G., Fast N.M., Green B.R., Grisdale C., RA Hempe F., Henrissat B., Hoppner M.P., Ishida K.-I., Kim E., Koreny L., RA Kroth P.G., Liu Y., Malik S.-B., Maier U.G., McRose D., Mock T., RA Neilson J.A., Onodera N.T., Poole A.M., Pritham E.J., Richards T.A., RA Rocap G., Roy S.W., Sarai C., Schaack S., Shirato S., Slamovits C.H., RA Spencer D.F., Suzuki S., Worden A.Z., Zauner S., Barry K., Bell C., RA Bharti A.K., Crow J.A., Grimwood J., Kramer R., Lindquist E., RA Lucas S., Salamov A., McFadden G.I., Lane C.E., Keeling P.J., RA Gray M.W., Grigoriev I.V., Archibald J.M.; RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases. RN [3] {ECO:0000313|EnsemblProtists:EKX34019} RP IDENTIFICATION. RG EnsemblProtists; RL Submitted (MAR-2016) to UniProtKB. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JH993122; EKX34019.1; -; Genomic_DNA. DR RefSeq; XP_005820999.1; XM_005820942.1. DR EnsemblProtists; EKX34019; EKX34019; GUITHDRAFT_147529. DR GeneID; 17290745; -. DR KEGG; gtt:GUITHDRAFT_147529; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR Proteomes; UP000011087; Unassembled WGS sequence. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 2. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 4: Predicted; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000011087}; KW Reference proteome {ECO:0000313|Proteomes:UP000011087}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1 22 {ECO:0000256|SAM:SignalP}. FT CHAIN 23 473 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5008769928. FT DOMAIN 281 324 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 246 276 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 473 AA; 53004 MW; 9890DE8912673078 CRC64; MPGMISFALL WSMVMSVGHV HAFTLIPGPH CLSKRGRWSD GPKRFSSLNM NLFGSETITT KKGDRAYIVG ADIKRNRYKT LESSWEVDDS LDELQRLCET AGLVVLGREF QSMQNPSPST FIGAGKVEAL AKTVKTLEID VVVFDDELSP AQGRNIQTIL GEDVRVLDRT MLILQIFAQR ARTREAKLQV QAAQMKYMMP RLQYFMTEGA GMEARGGGGG GGKNLKGMGE SQIEADKRLF RKQVGEEEDE AELQNVEKEM EEVKQQREVY RTKRRERDNL PIIAIVGYTN AGKSTMLNKL CGSEEVYADD LLFATLDPTT RKLRVQNIIE ELMLEDTPQE KIESPAWLRI HERVIPECTV ATSAKSGDGL AELLDIVEEA LLQLSVMIEC LLPYSASDLL AEIHKVGTII QEDFQESGTR VVAYVPPSLR NKLGEEEVGK QGRIGQNRTE QGRTREDRTG MDRISKDRTG QDK // ID L1L3Z7_9ACTN Unreviewed; 498 AA. AC L1L3Z7; DT 06-MAR-2013, integrated into UniProtKB/TrEMBL. DT 06-MAR-2013, sequence version 1. DT 07-JUN-2017, entry version 32. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:EKX67308.1}; GN ORFNames=STRIP9103_07309 {ECO:0000313|EMBL:EKX67308.1}; OS Streptomyces ipomoeae 91-03. OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae; OC Streptomyces. OX NCBI_TaxID=698759 {ECO:0000313|EMBL:EKX67308.1, ECO:0000313|Proteomes:UP000010411}; RN [1] {ECO:0000313|EMBL:EKX67308.1, ECO:0000313|Proteomes:UP000010411} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=91-03 {ECO:0000313|EMBL:EKX67308.1, RC ECO:0000313|Proteomes:UP000010411}; RA Huguet-Tapia J.C., Durkin A.S., Pettis G.S., Badger J.H.; RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EKX67308.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AEJC01000158; EKX67308.1; -; Genomic_DNA. DR RefSeq; WP_009307298.1; NZ_AEJC01000158.1. DR EnsemblBacteria; EKX67308; EKX67308; STRIP9103_07309. DR PATRIC; fig|698759.3.peg.2139; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000010411; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000010411}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000010411}. FT DOMAIN 276 441 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 498 AA; 54260 MW; 8CD31C095E084210 CRC64; MTSSSSPSQA AQRAFAQNNT EGLRADALME EDVAWSFEID GERDGDQFDR SDRAALRRVA GLSTELEDVT EVEYRQLRLE RVVLVGVWTS GTVRDAENSL AELAALAETA GALVLDGVIQ RRDKPDAATY IGSGKADELR DIVLETGADT VICDGELSPG QLIHLEDVVK VKVIDRTALI LDIFAQHAKS REGKAQVALA QMQYMLPRLR GWGQSLSRQM GGGKGGGLAT RGPGETKIET DRRRIREKMA KMRREIAEMK TGREIKRQER RRNKVPSVAI AGYTNAGKSS LLNRLTGAGV LVENALFATL DPTVRRAESP SGLLYTLADT VGFVRHLPHH LVEAFRSTME EVGESDLILH VVDGSHPNPE EQLAAVREVI RDVGATDVPE IVVINKADAA DPLVLQRLLR NEKRSIAVSA RTGQGIDELL ALVDSELPRP SVEIEALVPY THGKLVARTH TEGEVISEEH TPEGTLLKAR VHEELAADLA PYVPAATG // ID L1M0N7_PSEPU Unreviewed; 433 AA. AC L1M0N7; DT 06-MAR-2013, integrated into UniProtKB/TrEMBL. DT 06-MAR-2013, sequence version 1. DT 30-AUG-2017, entry version 31. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=CSV86_13360 {ECO:0000313|EMBL:EKX84777.1}; OS Pseudomonas putida CSV86. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=1005395 {ECO:0000313|EMBL:EKX84777.1, ECO:0000313|Proteomes:UP000010448}; RN [1] {ECO:0000313|EMBL:EKX84777.1, ECO:0000313|Proteomes:UP000010448} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CSV86 {ECO:0000313|EMBL:EKX84777.1, RC ECO:0000313|Proteomes:UP000010448}; RX PubMed=23469351; RA Phale P.S., Paliwal V., Raju S.C., Modak A., Purohit H.J.; RT "Genome Sequence of Naphthalene-Degrading Soil Bacterium Pseudomonas RT putida CSV86."; RL Genome Announc. 1:E00234-12(2013). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EKX84777.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AMWJ01000094; EKX84777.1; -; Genomic_DNA. DR RefSeq; WP_009399550.1; NZ_AMWJ01000094.1. DR EnsemblBacteria; EKX84777; EKX84777; CSV86_13360. DR PATRIC; fig|1005395.3.peg.2563; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000010448; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000010448}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000010448}. FT DOMAIN 199 366 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 165 192 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 433 AA; 48597 MW; 3F84D6F772AEF23F CRC64; MFFERHGGGE RAVLVHLEGQ SPEAREDPQE FQELALSAGA DIVALANVAR HQPTAKFLIG SGKVEELRDL VKAEEADLVI FNHTLTPSQE RNLERVFECR VLDRTGLILD IFAQRARTHE GKLQVELAQL EHMSTRLVRG WTHLERQKGG IGLRGPGETQ LETDRRLLRV RLRQIKARLE KVRSQREQAR RGRKRADVPS VSLVGYTNAG KSTLFNALTS SEVYAADQLF ATLDPTLRRL ELGDIGPIVL ADTVGFIRHL PHKLVEAFRA TLEESSNSDL LLHVIDAHEP ERMAQIEQVM AVLGEIGAEG LPILEVYNKL DLLEGIEPHI QRNADGKPER VWVSAREGRG LELVGQAIAE LLGDDLFIGT LRLEQRYARL RAQFFAAGAV QNEEHDEEGS SLLAVRLPRA DFNRLVTREG LEPVEFIEQH TLQ // ID L1MGT7_9CORY Unreviewed; 505 AA. AC L1MGT7; DT 06-MAR-2013, integrated into UniProtKB/TrEMBL. DT 06-MAR-2013, sequence version 1. DT 07-JUN-2017, entry version 32. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=HMPREF9997_01379 {ECO:0000313|EMBL:EKX90164.1}; OS Corynebacterium durum F0235. OC Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae; OC Corynebacterium. OX NCBI_TaxID=1035195 {ECO:0000313|EMBL:EKX90164.1, ECO:0000313|Proteomes:UP000010445}; RN [1] {ECO:0000313|EMBL:EKX90164.1, ECO:0000313|Proteomes:UP000010445} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=F0235 {ECO:0000313|EMBL:EKX90164.1, RC ECO:0000313|Proteomes:UP000010445}; RA Weinstock G., Sodergren E., Lobos E.A., Fulton L., Fulton R., RA Courtney L., Fronick C., O'Laughlin M., Godfrey J., Wilson R.M., RA Miner T., Farmer C., Delehaunty K., Cordes M., Minx P., Tomlinson C., RA Chen J., Wollam A., Pepin K.H., Bhonagiri V., Zhang X., Suruliraj S., RA Warren W., Mitreva M., Mardis E.R., Wilson R.K.; RL Submitted (MAY-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EKX90164.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AMEM01000018; EKX90164.1; -; Genomic_DNA. DR RefSeq; WP_006063608.1; NZ_KB290831.1. DR EnsemblBacteria; EKX90164; EKX90164; HMPREF9997_01379. DR PATRIC; fig|1035195.3.peg.1236; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000010445; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000010445}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000010445}. FT DOMAIN 280 449 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 239 266 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 505 AA; 54712 MW; 8EBF572C31B1677E CRC64; MTNKHHDKLL AAAFADHQDN LSHAEPLETA TSAAPHNSAA PTTGELDLEA RSSLRRLTRG TNIHSTEQSD GYDVEYRKLR LEKVVLVGVW TEGTTAEIDA SMAELAALAE TAGSEVTEML YQKRDRPDPG TYIGSGKVQE LKDIVAATGS DTVICDGELS PGQMIALEKA LDVKVIDRTM LILDIFAQHA KSKEGKAQVS LAQMEYLITR VRGWGGALSR QAGGRAGSNG GVGLRGPGET KIEADRRRLR SEMAKLRKEL TGMKTAREVK RSQRRASTIP QIAIAGYTNA GKSSLINAMT GAGVLVEDAL FATLDPTTRR AELADGRAVV FTDTVGFVRH LPTQLVESFR STLEEVVEAD LVLHVVDGSD PFPLKQIEAV NSVITEIVQE QKVQAPPEII VVNKIDQADP LTLAELRHVL DDVVFVSART GDGIAELEAR VELFLNSLDD HVTVLIPFTH GGVVARIHEL GTVLKEDYTA EGTLIDVRLP HSVATELQDF IVETS // ID L1MRV7_9BACT Unreviewed; 453 AA. AC L1MRV7; DT 06-MAR-2013, integrated into UniProtKB/TrEMBL. DT 06-MAR-2013, sequence version 1. DT 07-JUN-2017, entry version 31. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=HMPREF9999_00260 {ECO:0000313|EMBL:EKX93694.1}; OS Prevotella sp. oral taxon 473 str. F0040. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Prevotellaceae; OC Alloprevotella. OX NCBI_TaxID=1035197 {ECO:0000313|EMBL:EKX93694.1, ECO:0000313|Proteomes:UP000010460}; RN [1] {ECO:0000313|EMBL:EKX93694.1, ECO:0000313|Proteomes:UP000010460} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=F0040 {ECO:0000313|EMBL:EKX93694.1, RC ECO:0000313|Proteomes:UP000010460}; RA Weinstock G., Sodergren E., Lobos E.A., Fulton L., Fulton R., RA Courtney L., Fronick C., O'Laughlin M., Godfrey J., Wilson R.M., RA Miner T., Farmer C., Delehaunty K., Cordes M., Minx P., Tomlinson C., RA Chen J., Wollam A., Pepin K.H., Bhonagiri V., Zhang X., Suruliraj S., RA Warren W., Mitreva M., Mardis E.R., Wilson R.K.; RL Submitted (MAY-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EKX93694.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AMEK01000014; EKX93694.1; -; Genomic_DNA. DR RefSeq; WP_009437920.1; NZ_KB290724.1. DR EnsemblBacteria; EKX93694; EKX93694; HMPREF9999_00260. DR PATRIC; fig|1035197.3.peg.218; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000010460; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 2. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000010460}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000010460}. FT DOMAIN 234 432 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 453 AA; 51307 MW; 7E1493F3B4C001D3 CRC64; MKEFIQTEVK AETAVLVALI TKTQNEHKTQ EYLEELAFLA ETAGAETVHR FTQRMDGPSS VTYVGKGKLE EIRAYIEDCE KAAEEAEEDP LWPADVEKPR PVGMVIFDDE LSAKQLRNIE AVLQVKILDR TSLILDIFAM RAQTANAKTQ VELAQYRYML PRLQRLWTHL ERQGGGSGGA GGGKGGSVGL RGPGETQLEM DRRIILNRMS LLKERLADID RQKTTQRQNR GKMVRVALVG YTNVGKSTLL NLLSKSEVFA ENKLFATLDT TVRKVIVHNL PFLLADTVGF IRKLPTDLVD SFKSTLDETR EADLLVHVVD VSHPDFEEQL QVVNRTLCDL GCADKPQILV FNKMDAYTCT PKDPNDLTPA TKENVTLPEL MQTWMGRTQG TGENMTEQQG TAPLDVIFIS ARERENIEEL RDLFYKRVRE IHVQKYPYND FLFYDYDAEG EMV // ID L1NI19_9BACT Unreviewed; 415 AA. AC L1NI19; DT 06-MAR-2013, integrated into UniProtKB/TrEMBL. DT 06-MAR-2013, sequence version 1. DT 07-JUN-2017, entry version 31. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=HMPREF9151_00632 {ECO:0000313|EMBL:EKY02827.1}; OS Prevotella saccharolytica F0055. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Prevotellaceae; OC Prevotella. OX NCBI_TaxID=1127699 {ECO:0000313|EMBL:EKY02827.1, ECO:0000313|Proteomes:UP000010433}; RN [1] {ECO:0000313|EMBL:EKY02827.1, ECO:0000313|Proteomes:UP000010433} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=F0055 {ECO:0000313|EMBL:EKY02827.1, RC ECO:0000313|Proteomes:UP000010433}; RA Weinstock G., Sodergren E., Lobos E.A., Fulton L., Fulton R., RA Courtney L., Fronick C., O'Laughlin M., Godfrey J., Wilson R.M., RA Miner T., Farmer C., Delehaunty K., Cordes M., Minx P., Tomlinson C., RA Chen J., Wollam A., Pepin K.H., Bhonagiri V., Zhang X., Suruliraj S., RA Warren W., Mitreva M., Mardis E.R., Wilson R.K.; RL Submitted (MAY-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EKY02827.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AMEP01000045; EKY02827.1; -; Genomic_DNA. DR RefSeq; WP_009161801.1; NZ_KB290974.1. DR EnsemblBacteria; EKY02827; EKY02827; HMPREF9151_00632. DR PATRIC; fig|1127699.3.peg.581; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000010433; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000010433}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000010433}. FT DOMAIN 216 400 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 415 AA; 47578 MW; B08D482594C68393 CRC64; MKEFVISEVK AETAILVGLI TQQQNEAKTK EYLDELEFLA DTAGAVTVKR FTQKVNAPSM VTYVGKGKLE EIKQYIKAEE EAEREIGMVI FDDELSAKQM RNIEKELNVK ILDRTSLILD IFAMRAQTAS AKTQVELAQY RYMLPRLQRL WTHLERQGGG SGSGGGKGSV GLRGPGETQL EMDRRIILGR MALLKERLAE IDKQKTTQRK NRGRMIRTAL VGYTNVGKST LMNLLSKSEV FAENKLFATL DTTVRKVVIE NLPFLLADTV GFIRKLPTDL VDSFKSTLDE VREADLLVHV VDISHPDFEE QIQVVENTLK ELDCADKPSM IVFNKIDSYT FVEKDKDDLT PATKENRTLD ELKHTWMARL HDNCIFISAR ERINIDELRD MIYKKVRELH VQKYPYNDFL YEMIE // ID L1NPB4_9NEIS Unreviewed; 386 AA. AC L1NPB4; DT 06-MAR-2013, integrated into UniProtKB/TrEMBL. DT 06-MAR-2013, sequence version 1. DT 07-JUN-2017, entry version 30. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=HMPREF9120_01939 {ECO:0000313|EMBL:EKY05186.1}; OS Neisseria sp. oral taxon 020 str. F0370. OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=1127694 {ECO:0000313|EMBL:EKY05186.1, ECO:0000313|Proteomes:UP000010457}; RN [1] {ECO:0000313|EMBL:EKY05186.1, ECO:0000313|Proteomes:UP000010457} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=F0370 {ECO:0000313|EMBL:EKY05186.1, RC ECO:0000313|Proteomes:UP000010457}; RA Weinstock G., Sodergren E., Lobos E.A., Fulton L., Fulton R., RA Courtney L., Fronick C., O'Laughlin M., Godfrey J., Wilson R.M., RA Miner T., Farmer C., Delehaunty K., Cordes M., Minx P., Tomlinson C., RA Chen J., Wollam A., Pepin K.H., Bhonagiri V., Zhang X., Suruliraj S., RA Warren W., Mitreva M., Mardis E.R., Wilson R.K.; RL Submitted (MAY-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EKY05186.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AMER01000151; EKY05186.1; -; Genomic_DNA. DR RefSeq; WP_009426545.1; NZ_KB291130.1. DR EnsemblBacteria; EKY05186; EKY05186; HMPREF9120_01939. DR PATRIC; fig|1127694.3.peg.1792; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000010457; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000010457}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000010457}. FT DOMAIN 213 382 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 386 AA; 42132 MW; 84D1135A72E7447B CRC64; MSERRPDKTL GKPERIMLVG VMLEADYSGA NETRERAFRA ALDEAEELVR ATGGELVRRE TAKRARAHTA LFVGTGKAEE LAAAVAADNI ELAVFNHELS PTQERNLEKI LQCRVLDRVG LILAIFAQRA QSQEGRLQVE LAQLTHLSGR LVRGYGHLQS QKGGIGLKGP GETQLETDRR LIGQKITALK KRLEAVKRGR ATRRKARQSG SLPTFALAGY TNTGKSSLFN RLTKADVFAK DQLFATLDTT ARRLYLSPEA SVILTDTVGF VRDLPHGLVA AFSATLEETA LADLIIHVID ASRDDHERQT DDVNRVLAEI GAGDIPQLLV YNKTDLLPPD TRPTGILRNA QGRPIAVNIS VKTGAGLDGL RQALIELALS DGLYKP // ID L1P5D6_9FLAO Unreviewed; 403 AA. AC L1P5D6; DT 06-MAR-2013, integrated into UniProtKB/TrEMBL. DT 06-MAR-2013, sequence version 1. DT 07-JUN-2017, entry version 31. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=HMPREF9075_00961 {ECO:0000313|EMBL:EKY10725.1}; OS Capnocytophaga sp. oral taxon 332 str. F0381. OC Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales; OC Flavobacteriaceae; Capnocytophaga. OX NCBI_TaxID=1127692 {ECO:0000313|EMBL:EKY10725.1, ECO:0000313|Proteomes:UP000010419}; RN [1] {ECO:0000313|EMBL:EKY10725.1, ECO:0000313|Proteomes:UP000010419} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=F0381 {ECO:0000313|EMBL:EKY10725.1, RC ECO:0000313|Proteomes:UP000010419}; RA Weinstock G., Sodergren E., Lobos E.A., Fulton L., Fulton R., RA Courtney L., Fronick C., O'Laughlin M., Godfrey J., Wilson R.M., RA Miner T., Farmer C., Delehaunty K., Cordes M., Minx P., Tomlinson C., RA Chen J., Wollam A., Pepin K.H., Bhonagiri V., Zhang X., Suruliraj S., RA Warren W., Mitreva M., Mardis E.R., Wilson R.K.; RL Submitted (MAY-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EKY10725.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AMET01000070; EKY10725.1; -; Genomic_DNA. DR RefSeq; WP_009415691.1; NZ_KB291310.1. DR EnsemblBacteria; EKY10725; EKY10725; HMPREF9075_00961. DR PATRIC; fig|1127692.3.peg.871; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000010419; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000010419}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000010419}. FT DOMAIN 200 385 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 403 AA; 46466 MW; A3F68B30B44EEC68 CRC64; MIEQINLNYE KVVLVGIINQ QQTEEKSKEY LDELEFLTYT AGGEVLKRFT QKLDVPNPKT FIGTGKMEEV QQYVEENEVG TVIFDDELTP AQQKNIEHIL KVKILDRTGL ILDIFAQRAQ TSYSRTQVEL AQYEYLLPRL TGLWTHLERQ RGGIGMRGPG ETEIETDRRI VRDRIALLKK KLSAIDKQMA TQRSNRGALV RVALIGYTNV GKSTLMNVIS KSDVFAENKL FATLDTTVRK VVIENLPFLL SDTVGFIRKL PTQLIESFKS TLDEVREADL LLHVVDISHP NFEDHIHSVN QILAEIESAN KPTIMVFNKI DAYTHEVIAE DDLATQRTAK HFTLEDWKNT WMQKMGRDVL FISALNKENL EEFRKVVYEK VKEIHITRFP YNNFLYDIDE ISS // ID L1QDW3_9CLOT Unreviewed; 598 AA. AC L1QDW3; DT 06-MAR-2013, integrated into UniProtKB/TrEMBL. DT 06-MAR-2013, sequence version 1. DT 07-JUN-2017, entry version 30. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=HMPREF0216_02218 {ECO:0000313|EMBL:EKY26179.1}; OS Clostridium celatum DSM 1785. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=545697 {ECO:0000313|EMBL:EKY26179.1, ECO:0000313|Proteomes:UP000010420}; RN [1] {ECO:0000313|EMBL:EKY26179.1, ECO:0000313|Proteomes:UP000010420} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 1785 {ECO:0000313|EMBL:EKY26179.1, RC ECO:0000313|Proteomes:UP000010420}; RA Weinstock G., Sodergren E., Lobos E.A., Fulton L., Fulton R., RA Courtney L., Fronick C., O'Laughlin M., Godfrey J., Wilson R.M., RA Miner T., Farmer C., Delehaunty K., Cordes M., Minx P., Tomlinson C., RA Chen J., Wollam A., Pepin K.H., Bhonagiri V., Zhang X., Suruliraj S., RA Warren W., Mitreva M., Mardis E.R., Wilson R.K.; RL Submitted (MAY-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EKY26179.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AMEZ01000059; EKY26179.1; -; Genomic_DNA. DR RefSeq; WP_005213972.1; NZ_KB291650.1. DR EnsemblBacteria; EKY26179; EKY26179; HMPREF0216_02218. DR PATRIC; fig|545697.3.peg.2180; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000010420; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000010420}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000010420}. FT DOMAIN 364 541 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 598 AA; 67124 MW; 8B9427E130101DFC CRC64; MIYGNIDGVK KSALEELEAL YKAKCPKDEV CSLNIIETIS RVSAFIEREV SVAIDRRGNI RSIAIGDSTS VEIETLDIRE KKLAGVRIIH THPNGMSNLS ALDISALLKL KLDAIVAIGI YEGKILDCSL GLLTVLDDKL DYEEIQNIAL EDLSKIHILN KINYIDSLIK EKDIIEDEGE KAILVGSDTR ESLEELKELT KACDIPVLES VYQSRSKIDA AFYIGRGKVL EIAQLRQKLR ANVIIFDDEL SGSQVRNLEA AIGAKVIDRT TLILEIFARR AKSREAKIQV ELAQLKYRMS RLQGLGTIMS RTGGGIGTRG PGEKKLETDR RHIKEEIYDL NDELKKIKKI RETQREKRNK ESIPKVSLVG YTNAGKSTLR NALCDVAAQK EVIGKEKVFE ADMLFATLDI TTRAIVLKNK GVITLTDTVG FVRKLPHDLV EAFKSTLEEV IYSDLLCHVV DTSSDTALEQ IKAVEEVLFE LGAKDKDTIL VLNKIDKATE EQIATVKEAT AEYNTIEISA REGINLNELL NLIEENLPYN MKKCEFLIPY DKSDISSFLH RNGRVLEEDY RENGTFMIVE VDDESYNKTK DYIVNIIA // ID L2F514_9GAMM Unreviewed; 449 AA. AC L2F514; DT 06-MAR-2013, integrated into UniProtKB/TrEMBL. DT 06-MAR-2013, sequence version 1. DT 07-JUN-2017, entry version 30. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=MOMA_06036 {ECO:0000313|EMBL:ELA08097.1}; OS Moraxella macacae 0408225. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Moraxellaceae; Moraxella. OX NCBI_TaxID=1230338 {ECO:0000313|EMBL:ELA08097.1, ECO:0000313|Proteomes:UP000023795}; RN [1] {ECO:0000313|EMBL:ELA08097.1, ECO:0000313|Proteomes:UP000023795} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=0408225 {ECO:0000313|EMBL:ELA08097.1, RC ECO:0000313|Proteomes:UP000023795}; RX PubMed=23409273; RA Ladner J.T., Whitehouse C.A., Koroleva G.I., Palacios G.F.; RT "Genome Sequence of Moraxella macacae 0408225, a Novel Bacterial RT Species Isolated from a Cynomolgus Macaque with Epistaxis."; RL Genome Announc. 1:E00188-12(2013). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:ELA08097.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ANIN01000002; ELA08097.1; -; Genomic_DNA. DR RefSeq; WP_009501609.1; NZ_ANIN01000002.1. DR EnsemblBacteria; ELA08097; ELA08097; MOMA_06036. DR PATRIC; fig|1230338.3.peg.1286; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000023795; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000023795}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000023795}. FT DOMAIN 200 365 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 166 193 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 449 AA; 50365 MW; 8665FCBFC844C38C CRC64; MQYFERHQGG ENAILVHLTL THLTDPDDLE EFQLLVESAG AIQQALVTGR RSKPDAKYFV GTGKADEIAQ LVTLHEADIV IFNHSLTPSQ ERNLERLLKC RVLDRTGLIL DIFAQRARTY EGKLQVELAQ LNHLATRLVR GWTHLERQKG GIGLRGPGET QLETDRRLLQ VRVNQLNTKL DKVKQTRAQG RAKRQKSDIP TISLVGYTNA GKSTLFNHLT NETVYAADKL FATLDPTLRH VNWKGLGSVI LVDTVGFVRH LPHELVEAFH ATLEETLEAD LLLHVIDSSR EDMHEQIDAV KSVLSQIKNN VPVLNVFNKI DLTCKPAHIG YSDNHQPNRV YISAQNALGI DKLTTAVQQL IAGDLQNYQL TIAPTLPNSG QLLNHLHDLG VIWQLNYDEQ GNTLVNIRLA NNRLRQLLGQ HKILANDVLA PTDIARLIPP PEPFEIPNI // ID L5KAH2_PTEAL Unreviewed; 431 AA. AC L5KAH2; DT 06-MAR-2013, integrated into UniProtKB/TrEMBL. DT 06-MAR-2013, sequence version 1. DT 07-JUN-2017, entry version 16. DE SubName: Full=Putative GTP-binding protein 6 {ECO:0000313|EMBL:ELK08699.1}; GN ORFNames=PAL_GLEAN10000395 {ECO:0000313|EMBL:ELK08699.1}; OS Pteropus alecto (Black flying fox). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Chiroptera; Megachiroptera; OC Pteropodidae; Pteropodinae; Pteropus. OX NCBI_TaxID=9402 {ECO:0000313|EMBL:ELK08699.1, ECO:0000313|Proteomes:UP000010552}; RN [1] {ECO:0000313|Proteomes:UP000010552} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=23258410; DOI=10.1126/science.1230835; RA Zhang G., Cowled C., Shi Z., Huang Z., Bishop-Lilly K.A., Fang X., RA Wynne J.W., Xiong Z., Baker M.L., Zhao W., Tachedjian M., Zhu Y., RA Zhou P., Jiang X., Ng J., Yang L., Wu L., Xiao J., Feng Y., Chen Y., RA Sun X., Zhang Y., Marsh G.A., Crameri G., Broder C.C., Frey K.G., RA Wang L.F., Wang J.; RT "Comparative analysis of bat genomes provides insight into the RT evolution of flight and immunity."; RL Science 339:456-460(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; KB030869; ELK08699.1; -; Genomic_DNA. DR InParanoid; L5KAH2; -. DR Proteomes; UP000010552; Unassembled WGS sequence. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 4: Predicted; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000010552}; KW Reference proteome {ECO:0000313|Proteomes:UP000010552}. FT DOMAIN 301 431 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 263 290 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 431 AA; 47610 MW; 3080D2311FF781AE CRC64; MWALRAAVRP GVSLSRVVRG RGALRVAPRL PPWPERALTA FGPGDPGDLQ GRGGGGRGPR ADGRRRRAGT EEDEEPEGAE QEEEDVEELL RREPLLPAGT QRVCLVHPEV KWGPAKPLRT RAEWQVAEAK ALVHTLDSWS VVETVVVPTK TPDKKLIFSK GALEHLTEKI RGLAEITAVF LNVERMSAPT KKELEAAWGV QVFDRFTVVL HIFRCNARTR EARLQVALAE LPVLRANLKN DVGRLDGRGG GSRYIMGSGE SFMQVQQRLL KEKEMKIRKA LERLRRKRRL LGTQRRRREL PVVSVVGYTN SGKTTLIKAL TGDAAIQPRD QLFATLDVTA HAGSLPSRMT VIYLDTIGFL SQLPHSLIES FSATLEDVAH SDVILHVRDA SHPESELQSA SVMSALRGLR LPAPLLDGVL EVHNKADLLP G // ID L5N1I4_9BACI Unreviewed; 409 AA. AC L5N1I4; DT 06-MAR-2013, integrated into UniProtKB/TrEMBL. DT 06-MAR-2013, sequence version 1. DT 07-JUN-2017, entry version 31. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=D479_19763 {ECO:0000313|EMBL:ELK44315.1}; OS Halobacillus sp. BAB-2008. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Halobacillus. OX NCBI_TaxID=1246484 {ECO:0000313|EMBL:ELK44315.1, ECO:0000313|Proteomes:UP000010769}; RN [1] {ECO:0000313|EMBL:ELK44315.1, ECO:0000313|Proteomes:UP000010769} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BAB-2008 {ECO:0000313|EMBL:ELK44315.1, RC ECO:0000313|Proteomes:UP000010769}; RX PubMed=23469348; RA Joshi M.N., Pandit A.S., Sharma A., Pandya R.V., Saxena A.K., RA Bagatharia S.B.; RT "Draft Genome Sequence of the Halophilic Bacterium Halobacillus sp. RT Strain BAB-2008."; RL Genome Announc. 1:E00222-12(2013). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:ELK44315.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ANPF01000106; ELK44315.1; -; Genomic_DNA. DR RefSeq; WP_008640368.1; NZ_ANPF01000106.1. DR EnsemblBacteria; ELK44315; ELK44315; D479_19763. DR PATRIC; fig|1246484.3.peg.4004; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000010769; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000010769}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000010769}. FT DOMAIN 195 356 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 409 AA; 46558 MW; AFDFBBA318E3F507 CRC64; MKETAILVAR KDPRADEERF QSSLQELQSL TETAGGEVCK IITQSRDRVH PATYLGQGKL EEIKLEAEAA EAELIIFNDE LSPGQLRNIS DRVERRVIDR SQLILDIFAG RARTKEGKLQ VELAQLQYLL PRLAGQGTAL SRLGGGIGTR GPGETKLETD RRHIQRRIDD IKVRLDTVVR QREQYRKRRK ENRAYQIAIV GYTNAGKSTF FNRVTESQSF EEDLLFATLD PLTRQLNLPS GFRVLLSDTV GFIQDLPTTL IAAFRSTLEE VTEADFVLHM VDASHPDHIQ QEKTVRKLLE ELGASRLPMV TVYNKKDLLT GDFIPPSHPS LTVSVHDPID LKRVLHKVED TWKEDWVEYD VFIPASDGKR LQRFRSSSIV TSMLFKEDQE GYALHGFIDP DHPLKHQIL // ID L7F2V3_9ACTN Unreviewed; 498 AA. AC L7F2V3; DT 06-MAR-2013, integrated into UniProtKB/TrEMBL. DT 06-MAR-2013, sequence version 1. DT 07-JUN-2017, entry version 32. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:ELP65469.1}; GN ORFNames=STRTUCAR8_08039 {ECO:0000313|EMBL:ELP65469.1}; OS Streptomyces turgidiscabies Car8. OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae; OC Streptomyces. OX NCBI_TaxID=698760 {ECO:0000313|EMBL:ELP65469.1, ECO:0000313|Proteomes:UP000010931}; RN [1] {ECO:0000313|EMBL:ELP65469.1, ECO:0000313|Proteomes:UP000010931} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Car8 {ECO:0000313|EMBL:ELP65469.1, RC ECO:0000313|Proteomes:UP000010931}; RX PubMed=21087627; DOI=10.1016/j.plasmid.2010.11.002; RA Huguet-Tapia J.C., Badger J.H., Loria R., Pettis G.S.; RT "Streptomyces turgidiscabies Car8 contains a modular pathogenicity RT island that shares virulence genes with other actinobacterial plant RT pathogens."; RL Plasmid 65:118-124(2011). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:ELP65469.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AEJB01000377; ELP65469.1; -; Genomic_DNA. DR RefSeq; WP_006379462.1; NZ_AEJB01000377.1. DR EnsemblBacteria; ELP65469; ELP65469; STRTUCAR8_08039. DR PATRIC; fig|698760.3.peg.5719; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000010931; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 2. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000010931}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000010931}. FT DOMAIN 275 440 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 498 AA; 54359 MW; 767F5D531E3FE9A0 CRC64; MTSSSSPSQD TERFAHAYPE GLRADALMEE DVAWSHEIDG DRDGDQFDRS ERAALRRVAG LSTELEDVTE VEYRQLRLER VVLVGVWTTG TIRDADNSLA ELAALAETAG ALVLDGVVQR RDKPDAATYI GSGKANELRD IVLETGADTV ICDGELSPGQ LIHLEDVVKV KVIDRTALIL DIFAQHAKSR EGKAQVALAQ MQYMLPRLRG WGQSLSRQMG GGKGGGLATR GPGETKIETD RRRIREKMAK MRREIAEMKT GREIKRQERR RNKVPSVAIA GYTNAGKSSL LNRLTGAGVL VENSLFATLD PTVRRAETPS GRLHTLTDTV GFVRHLPHHL VEAFRSTMEE VGDADLILHV VDGSHPVPEE QLAAVREVIR DVGATGVPEI VVINKADAAD PLTLQRLMRM ETRSIAVSAR TGQGIDELLA LIDNELPRPS VEIEALVPYT HGQLVARAHT DGEVISEEHT AEGTLLKARV HEELAAELAP YVPAAAVL // ID L7LE15_9ACTN Unreviewed; 474 AA. AC L7LE15; DT 06-MAR-2013, integrated into UniProtKB/TrEMBL. DT 06-MAR-2013, sequence version 1. DT 07-JUN-2017, entry version 30. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:GAC58312.1}; GN ORFNames=GOHSU_37_00080 {ECO:0000313|EMBL:GAC58312.1}; OS Gordonia hirsuta DSM 44140 = NBRC 16056. OC Bacteria; Actinobacteria; Corynebacteriales; Gordoniaceae; Gordonia. OX NCBI_TaxID=1121927 {ECO:0000313|EMBL:GAC58312.1, ECO:0000313|Proteomes:UP000053405}; RN [1] {ECO:0000313|EMBL:GAC58312.1, ECO:0000313|Proteomes:UP000053405} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NBRC 16056 {ECO:0000313|EMBL:GAC58312.1, RC ECO:0000313|Proteomes:UP000053405}; RA Isaki-Nakamura S., Hosoyama A., Tsuchikane K., Katsumata H., Baba S., RA Yamazaki S., Fujita N.; RT "Whole genome shotgun sequence of Gordonia hirsuta NBRC 16056."; RL Submitted (DEC-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:GAC58312.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BANT01000037; GAC58312.1; -; Genomic_DNA. DR RefSeq; WP_005942204.1; NZ_BANT01000037.1. DR EnsemblBacteria; GAC58312; GAC58312; GOHSU_37_00080. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000053405; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 2. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000053405}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000053405}. FT DOMAIN 251 420 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 210 237 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 474 AA; 51688 MW; C76B20D4CAA5D305 CRC64; MTELHETTET VSSTTPTTGE LQLDDRTALQ RVAGLSTELT DVTEVEYRRL RLEQVVLVGV WTTGTADEAQ ASMAELAALA ETAGSQVLDA VIQRRPKPDA ATYLGSGKAE ELREIVLATG ADTVICDGEL TPAQLTALER VVKVKVIDRT ALILDIFAQH ATSREGKAQV SLAQMEYMLP RLRGWGESMS RQAGGRAGSN GGVGLRGPGE TKIETDRRRI RERMAKLRKE IRGMKTARTV KRAQRSRGPV PALTVVGYTN AGKSSLVNAM TGSGVLVQDA LFATLDPTTR RARLADGHEV VFTDTVGFVR HLPTQLVEAF RSTLEEAVHA DLLIHVVDGA DAFPDKQISA VRNVLNEVFD DEEIDPPPEL LVINKIDAVD AARMTQLRAE YRDAVFVSAR TGEGIDELFA RITEFVEAGD VEAVLAVPFS RGEVMARLHQ HAHVLETDHT AEGTRVRVRM PKAIAAEYAD LRID // ID L7LIC8_9ACTN Unreviewed; 483 AA. AC L7LIC8; DT 06-MAR-2013, integrated into UniProtKB/TrEMBL. DT 06-MAR-2013, sequence version 1. DT 07-JUN-2017, entry version 30. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:GAC60875.1}; GN ORFNames=GSI01S_13_00580 {ECO:0000313|EMBL:GAC60875.1}; OS Gordonia sihwensis NBRC 108236. OC Bacteria; Actinobacteria; Corynebacteriales; Gordoniaceae; Gordonia. OX NCBI_TaxID=1223544 {ECO:0000313|EMBL:GAC60875.1, ECO:0000313|Proteomes:UP000035083}; RN [1] {ECO:0000313|EMBL:GAC60875.1, ECO:0000313|Proteomes:UP000035083} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NBRC 108236 {ECO:0000313|EMBL:GAC60875.1, RC ECO:0000313|Proteomes:UP000035083}; RA Yoshida I., Hosoyama A., Tsuchikane K., Ando Y., Baba S., Ohji S., RA Hamada M., Tamura T., Yamazoe A., Yamazaki S., Fujita N.; RT "Whole genome shotgun sequence of Gordonia sihwensis NBRC 108236."; RL Submitted (DEC-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:GAC60875.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BANU01000013; GAC60875.1; -; Genomic_DNA. DR EnsemblBacteria; GAC60875; GAC60875; GSI01S_13_00580. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000035083; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 2. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000035083}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000035083}. FT DOMAIN 260 429 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 219 246 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 483 AA; 52044 MW; 19A2110F576B0B45 CRC64; MDESADDRSA EEVPGLSERG RPGEPTVGEL QLDERASLQR VVGLSTELED VTEVEYRRLR LEQVVLVGVW TTGSVAAARA SMAELAALAE TAGSQVLDAL IQRRGKPDPA TYLGSGKAEE LREVVVASGA DTVICDGELT PAQLTALEKV VKVKVIDRTA LILDIFAQHA TSREGKAQVA LAQMEYMLPR LRGWGESMSR QAGGRAGSNG GVGLRGPGET KIETDRRRIR ERMAKLRKEI RGMKTARTVK RAARRRGGVP ALTVVGYTNA GKSSLVNAMT GSGVLVQDAL FATLDPTTRR AQLADGHEVV FTDTVGFVRH LPTQLVEAFR STLEEAVDAD LLVHVVDGSD PFPANQISAV RQVLGEVLAE EDRPAPPEML VVNKIDAVDG VTMTALRAEY PDAQFVSART GEGLDGLFAA ITDFLQRDDV DAVLQVPFAR GEVISRLHQH AHVLDTEHNA EGTRLHVRMP SALAAEYSDL TVA // ID L7VSF8_CLOSH Unreviewed; 597 AA. AC L7VSF8; DT 03-APR-2013, integrated into UniProtKB/TrEMBL. DT 03-APR-2013, sequence version 1. DT 07-JUN-2017, entry version 36. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:AGC69682.1}; GN OrderedLocusNames=Cst_c27390 {ECO:0000313|EMBL:AGC69682.1}; OS Clostridium stercorarium subsp. stercorarium (strain ATCC 35414 / DSM OS 8532 / NCIMB 11754). OC Bacteria; Firmicutes; Clostridia; Clostridiales; Ruminococcaceae; OC Ruminiclostridium. OX NCBI_TaxID=1121335 {ECO:0000313|EMBL:AGC69682.1, ECO:0000313|Proteomes:UP000011220}; RN [1] {ECO:0000313|EMBL:AGC69682.1, ECO:0000313|Proteomes:UP000011220} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 35414 / DSM 8532 / NCIMB 11754 RC {ECO:0000313|Proteomes:UP000011220}; RX PubMed=23516204; DOI=10.1128/genomeA.00073-13; RA Poehlein A., Zverlov V.V., Daniel R., Schwarz W.H., Liebl W.; RT "Complete genome sequence of Clostridium stercorarium subsp. RT stercorarium strain DSM 8532, a thermophilic degrader of plant cell RT wall fibers."; RL Genome Announc. 1:E0007313-E0007313(2013). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP004044; AGC69682.1; -; Genomic_DNA. DR RefSeq; WP_015360358.1; NC_020887.2. DR EnsemblBacteria; AGC69682; AGC69682; Cst_c27390. DR KEGG; csd:Clst_2626; -. DR KEGG; css:Cst_c27390; -. DR PATRIC; fig|1121335.3.peg.2744; -. DR KO; K03665; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000011220; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000011220}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000011220}. FT DOMAIN 378 543 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 344 371 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 597 AA; 66481 MW; 21312A73F583BEB4 CRC64; MQVNGQTEGL KKGILERLQK IYDMKIPKDQ VLTEELTLIL AEISSAINRE ISVLIDRKGN ILDVRVGDSN SAAVYPASVR RSESSLSGVR CVHTHPGGRS ALSELDISTL KQLHLDMMIA LGVSDLKPTD VSCAILTDGM QNVAIYGPFG PFSNRLNEIA EFVYKADKSG KEPAVVQEKR KERALLIGVE TPDTPVIMGV SEASISMKEL VELAKTAGAE VVDTILQKRP SRDPAYLIGK GKLAEIGRIV QEKEIALVIF DEELSGTQLR NIENFTNTKV VDRTGLILDI FGQRAKSREG QVQVELAQLN YLLPRLQGRG ITLSRLGGGI GTRGPGETKL ETDRRHIRRR IDYLKKELER IRNQRQTSRR ERERNKIPVV ALVGYTNAGK STLLNTLCDA DVFAEDKLFA TLDTTTRKLK LEEGMTVLLS DTVGFIRKLP HHLVEAFKST LEEAVLADLL LIVVDASDPF AQDHVRVVNE ILSDLGASSK PSVLVWNKWD LVDKDFHTPF FREKPVEVHV SAITGLGLDE LKKAIKNCLK PETERVTLHI PFSEGWVLPF LYENGMVSSV DYKDNVTIVE AEIDKKYISR INSFIIN // ID L7WD66_NONDD Unreviewed; 403 AA. AC L7WD66; DT 03-APR-2013, integrated into UniProtKB/TrEMBL. DT 03-APR-2013, sequence version 1. DT 07-JUN-2017, entry version 32. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:AGC76813.1}; GN OrderedLocusNames=DDD_1686 {ECO:0000313|EMBL:AGC76813.1}; OS Nonlabens dokdonensis (strain DSM 17205 / KCTC 12402 / DSW-6) OS (Donghaeana dokdonensis). OC Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales; OC Flavobacteriaceae; Nonlabens. OX NCBI_TaxID=592029 {ECO:0000313|EMBL:AGC76813.1, ECO:0000313|Proteomes:UP000011173}; RN [1] {ECO:0000313|EMBL:AGC76813.1, ECO:0000313|Proteomes:UP000011173} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 17205 / KCTC 12402 / DSW-6 RC {ECO:0000313|Proteomes:UP000011173}; RX PubMed=23292138; DOI=10.1093/gbe/evs134; RA Kwon S.K., Kim B.K., Song J.Y., Kwak M.J., Lee C.H., Yoon J.H., RA Oh T.K., Kim J.F.; RT "Genomic makeup of the marine flavobacterium Nonlabens (Donghaeana) RT dokdonensis and identification of a novel class of rhodopsins."; RL Genome Biol. Evol. 5:187-199(2013). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001397; AGC76813.1; -; Genomic_DNA. DR RefSeq; WP_015362310.1; NC_020156.1. DR EnsemblBacteria; AGC76813; AGC76813; DDD_1686. DR KEGG; ndo:DDD_1686; -. DR PATRIC; fig|592029.3.peg.1669; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000011173; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000011173}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000011173}. FT DOMAIN 200 385 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 403 AA; 46619 MW; 7D5EB54C5C640828 CRC64; MLELENHEYE KAILVGVITQ QQNEEKLNEY MDELEFLAYT AGATVHKRFH QKMQKPNPKT FIGKGKMEDV AAYVKANNIG TVIFDDELSP AQQKNIEKIL EAKIIDRTYL ILDIFAQRAQ TSYARTQVEL AQYEYLLPRL VGLWTHLERQ KGGIGMRGPG ETEIETDRRI VRDRITLLKK KLLTIDKQMS TQRGNRGALV RVSLVGYTNV GKSTLMNVVS KSEVFAENKL FATLDTTVRK VVVRNLPFLL TDTVGFIRKL PTQLVESFKS TLDEVRESDL LLHVVDISHE SFEDHIASVN NILGEIDAID KPTIMVFNKI DAYQAQDYDE TDLIEERTSA HYSLEEWKET WMAKMGEDVI FISATEKENM EDFRKKVYDK VREIHVKRFP YNSFLYPDYS EEE // ID L8D540_9GAMM Unreviewed; 429 AA. AC L8D540; DT 03-APR-2013, integrated into UniProtKB/TrEMBL. DT 03-APR-2013, sequence version 1. DT 30-AUG-2017, entry version 29. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=PALB_23730 {ECO:0000313|EMBL:CCQ11476.1}; OS Pseudoalteromonas luteoviolacea B = ATCC 29581. OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales; OC Pseudoalteromonadaceae; Pseudoalteromonas. OX NCBI_TaxID=1268239 {ECO:0000313|EMBL:CCQ11476.1, ECO:0000313|Proteomes:UP000011175}; RN [1] {ECO:0000313|EMBL:CCQ11476.1, ECO:0000313|Proteomes:UP000011175} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=B / ATCC 29581 {ECO:0000313|Proteomes:UP000011175}; RA Cress B.; RL Submitted (DEC-2012) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:CCQ11476.1, ECO:0000313|Proteomes:UP000011175} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=B / ATCC 29581 {ECO:0000313|Proteomes:UP000011175}; RA Cress B.F., Barquera B., Koffas M.A.G.; RT "Draft genome sequence of Pseudoalteromonas luteoviolacea strain B."; RL Submitted (JAN-2013) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:CCQ11476.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CAPN01000047; CCQ11476.1; -; Genomic_DNA. DR ProteinModelPortal; L8D540; -. DR EnsemblBacteria; CCQ11476; CCQ11476; PALB_23730. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000011175; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000011175}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000011175}. FT DOMAIN 198 365 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 429 AA; 48598 MW; 70175E318CE7989D CRC64; MFDRYETGEQ AILVHINFSN ENNREDLNEL EMLVSSAGVN TLAVVQGSRQ APHAKFFVGT GKAEEIAEVV KTHNADVVIF NHQLSPSQER NLERVCQCRV LDRTTLILDI FAQRARTHEG KLQVELAQLR HMSTRLIRGW THLERQKGGI GLRGPGETQL ETDRRLLRER IKSIMKRLEK VSVVREQGRR ARARNDIPSL SLVGYTNAGK SSLFNRITGA DVYAADQLFA TLDPTLRKIE VEDVGPVILA DTVGFIRHLP HDLVAAFKAT LTETREADLQ LHVIDVADVR RAENIKEVQK VLKEIDAHEI PQLEVYNKID LLDEVKPQID RDDEGNPIRV WLSAQSGEGI DLLFQAMTEL ISAKVFHAVL QVPPKLSRLR GALFSLNGVQ SERYDDQGNW VVDVRIPMVD WEKLKKEQQQ NLDSLIVES // ID L8EL50_STRRM Unreviewed; 495 AA. AC L8EL50; DT 03-APR-2013, integrated into UniProtKB/TrEMBL. DT 03-APR-2013, sequence version 1. DT 07-JUN-2017, entry version 29. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=SRIM_26007 {ECO:0000313|EMBL:ELQ80288.1}; OS Streptomyces rimosus subsp. rimosus ATCC 10970. OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae; OC Streptomyces. OX NCBI_TaxID=1265868 {ECO:0000313|EMBL:ELQ80288.1, ECO:0000313|Proteomes:UP000011074}; RN [1] {ECO:0000313|Proteomes:UP000011074} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 10970 {ECO:0000313|Proteomes:UP000011074}; RA Pethick F.E., MacFadyen A.C., Tang Z., Sangal V., Liu T.-T., Chu J., RA Kosec G., Peltkovic H., Guo M., Kirby R., Hoskisson P.A., Herron P.R., RA Hunter I.S.; RT "Draft Genome Sequence of the Oxytetracycline-Producing Bacterium RT Streptomyces rimosus ATCC 10970."; RL Genome Announc.1:E00063-13(2013). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:ELQ80288.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ANSJ01000102; ELQ80288.1; -; Genomic_DNA. DR RefSeq; WP_003983926.1; NZ_ANSJ01000102.1. DR EnsemblBacteria; ELQ80288; ELQ80288; SRIM_26007. DR GeneID; 29533953; -. DR PATRIC; fig|1265868.3.peg.5286; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000011074; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 2. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000011074}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000011074}. FT DOMAIN 275 440 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 495 AA; 54058 MW; DDCC86B5B6C8C749 CRC64; MTSSSSLPQD RQRLSESLRA DALMEEDVAW SYEIDGERDG EQYDRTERAA LRRVAGLSTE LEDVTEVEYR QLRLERVVLV GVWTSGTVQD AENSLAELAA LAETAGALVL DGVVQRRDKP DPATYIGSGK ALELRDIVLE SGADTVVCDG ELSPGQLIHL EDVVKVKVVD RTALILDIFA QHAKSREGKA QVSLAQMQYM LPRLRGWGQS LSRQMGGGGS GSAGGGMATR GPGETKIETD RRRIREKMAK MRREIAEMKT GRDIKRQERR RHKVPSVAIA GYTNAGKSSL LNRLTGAGVL VENALFATLD PTVRRAETPS GRLYTLADTV GFVRHLPHHL VEAFRSTMEE VGDSDLILHV VDGSHPVPEE QLAAVREVIR DVGATDVPEI VVVNKADAAD PLVLQRLLRN EKHAIAVSAR TGQGIDELLA LIDEELPRPQ VEIEALVPYT QGALVSRAHA EGEVISEEHV AEGTVLKARV HEELAAEFQP YVPAA // ID L8FQA4_PSED2 Unreviewed; 217 AA. AC L8FQA4; DT 03-APR-2013, integrated into UniProtKB/TrEMBL. DT 03-APR-2013, sequence version 1. DT 30-AUG-2017, entry version 15. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:ELR02719.1}; DE Flags: Fragment; GN ORFNames=GMDG_08841 {ECO:0000313|EMBL:ELR02719.1}; OS Pseudogymnoascus destructans (strain ATCC MYA-4855 / 20631-21) (Bat OS white-nose syndrome fungus) (Geomyces destructans). OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes; OC Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus. OX NCBI_TaxID=658429 {ECO:0000313|EMBL:ELR02719.1, ECO:0000313|Proteomes:UP000011064}; RN [1] {ECO:0000313|Proteomes:UP000011064} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC MYA-4855 / 20631-21 {ECO:0000313|Proteomes:UP000011064}; RG The Broad Institute Genome Sequencing Platform; RA Cuomo C.A., Blehert D.S., Lorch J.M., Young S.K., Zeng Q., Gargeya S., RA Fitzgerald M., Haas B., Abouelleil A., Alvarado L., Arachchi H.M., RA Berlin A., Brown A., Chapman S.B., Chen Z., Dunbar C., Freedman E., RA Gearin G., Gellesch M., Goldberg J., Griggs A., Gujja S., Heiman D., RA Howarth C., Larson L., Lui A., MacDonald P.J.P., Montmayeur A., RA Murphy C., Neiman D., Pearson M., Priest M., Roberts A., Saif S., RA Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., Wortman J., RA Nusbaum C., Birren B.; RT "The genome sequence of Geomyces destructans 20631-21."; RL Submitted (SEP-2010) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GL574414; ELR02719.1; -; Genomic_DNA. DR RefSeq; XP_012747306.1; XM_012891852.1. DR EnsemblFungi; ELR02719; ELR02719; GMDG_08841. DR GeneID; 24489720; -. DR InParanoid; L8FQA4; -. DR OrthoDB; EOG09370C81; -. DR Proteomes; UP000011064; Unassembled WGS sequence. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000011064}; KW Reference proteome {ECO:0000313|Proteomes:UP000011064}. FT DOMAIN 70 156 GTP-bdg_N. {ECO:0000259|Pfam:PF13167}. FT DOMAIN 159 217 GTP-bdg_M. {ECO:0000259|Pfam:PF16360}. FT NON_TER 1 1 {ECO:0000313|EMBL:ELR02719.1}. FT NON_TER 217 217 {ECO:0000313|EMBL:ELR02719.1}. SQ SEQUENCE 217 AA; 23993 MW; 191062082283873A CRC64; GSAQRPSTSY LSISTTTSDP RVKPEDDGVE KARDLTTKHI DHAVPLIRAV VIHPERSDSG ASESSRQSVE RLEEAVGLAR ALDLDVRAEE IVRIRKVTPA TLFGSGKVEE LAALVRAAEA EAVVIDDALS PVQQRNLEKA WDCKVIDRTG LILEIFGRRA RTKEGRLQVE LARLDYEKSR LVRTWTHLER QRGGTGSTGG PGETQIELDR RLIADRI // ID L8HE75_ACACA Unreviewed; 594 AA. AC L8HE75; DT 03-APR-2013, integrated into UniProtKB/TrEMBL. DT 03-APR-2013, sequence version 1. DT 07-JUN-2017, entry version 17. DE SubName: Full=GTPbinding protein HflX, putative {ECO:0000313|EMBL:ELR23053.1}; GN ORFNames=ACA1_360890 {ECO:0000313|EMBL:ELR23053.1}; OS Acanthamoeba castellanii str. Neff. OC Eukaryota; Amoebozoa; Discosea; Longamoebia; Centramoebida; OC Acanthamoebidae; Acanthamoeba. OX NCBI_TaxID=1257118 {ECO:0000313|EMBL:ELR23053.1, ECO:0000313|Proteomes:UP000011083}; RN [1] {ECO:0000313|EMBL:ELR23053.1, ECO:0000313|Proteomes:UP000011083} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Neff {ECO:0000313|EMBL:ELR23053.1, RC ECO:0000313|Proteomes:UP000011083}; RX PubMed=23375108; DOI=10.1186/gb-2013-14-2-r11; RA Clarke M., Lohan A.J., Liu B., Lagkouvardos I., Roy S., Zafar N., RA Bertelli C., Schilde C., Kianianmomeni A., Burglin T.R., Frech C., RA Turcotte B., Kopec K.O., Synnott J.M., Choo C., Paponov I., RA Finkler A., Soon Heng Tan C., Hutchins A.P., Weinmeier T., Rattei T., RA Chu J.S., Gimenez G., Irimia M., Rigden D.J., Fitzpatrick D.A., RA Lorenzo-Morales J., Bateman A., Chiu C.H., Tang P., Hegemann P., RA Fromm H., Raoult D., Greub G., Miranda-Saavedra D., Chen N., Nash P., RA Ginger M.L., Horn M., Schaap P., Caler L., Loftus B.; RT "Genome of Acanthamoeba castellanii highlights extensive lateral gene RT transfer and early evolution of tyrosine kinase signaling."; RL Genome Biol. 14:R11-R11(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; KB007867; ELR23053.1; -; Genomic_DNA. DR RefSeq; XP_004352530.1; XM_004352478.1. DR EnsemblProtists; ELR23053; ELR23053; ACA1_360890. DR GeneID; 14924023; -. DR KEGG; acan:ACA1_360890; -. DR EuPathDB; AmoebaDB:ACA1_360890; -. DR Proteomes; UP000011083; Unassembled WGS sequence. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000011083}; KW Reference proteome {ECO:0000313|Proteomes:UP000011083}. FT DOMAIN 352 524 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 594 AA; 66861 MW; D5F20DAA7B47D1D5 CRC64; MHMWRRVSSL GVTGAAQCRG SSSTSVLWWR CRRILHSADY AYAADAAGAV PAVPRPQRSV AEAWGSAIDF DWRHGRRASS HPEDEDDDDA AFALASAAKS QSSRRKEEEG DSGRQALDAM QPGRFWSATR PPRVCVVHPY MRNTVYADKR KRRLSLLAER EEEEQVCRGQ DHPDLRLKEA VALVEALEWP VEDSMYLTVN TVNPSHFLGK GKIAELRQAC QAKRADVVVM DTNSLTPAQG QKLAKMLGTR VMDRYRLILE IFAQRAQSEE SRLQVELAGL AYKSVHLKSA MESKHLAQQR GGGAFLSGAG ETNLEIERRH LVVREKKIKA RLEVLQKTRK LHRESRKKQD IPTIAILGYT NAGKSALLNR LCGTSLVSQN QLFASLHTFM RKIELPSGCC ALAADTVGFI SNLPHGLVAP FHSTLEEIGS ADVLLHVRDI TNAETEMQKA NVHKVMKEIG LDTDPDTQHL EVWNKIDLMD DARLDSLVTT QRVLGKRIFP ISARTGAGCD DLLQAIDQRL QALYPERKRV YELLLGENEQ ERLEFLTSHG GRVRTVQPDY QVAGRTRLSV EMRPDVYERY RVRYGELPRP QQHL // ID L8J5C8_9GAMM Unreviewed; 429 AA. AC L8J5C8; DT 03-APR-2013, integrated into UniProtKB/TrEMBL. DT 03-APR-2013, sequence version 1. DT 30-AUG-2017, entry version 30. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=C942_03845 {ECO:0000313|EMBL:ELR63403.1}; OS Photobacterium marinum. OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; OC Vibrionaceae; Photobacterium. OX NCBI_TaxID=1056511 {ECO:0000313|EMBL:ELR63403.1, ECO:0000313|Proteomes:UP000011134}; RN [1] {ECO:0000313|EMBL:ELR63403.1, ECO:0000313|Proteomes:UP000011134} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=AK15 {ECO:0000313|EMBL:ELR63403.1, RC ECO:0000313|Proteomes:UP000011134}; RA Khatri I., Vaidya B., Srinivas T.N.R., Subramanian S., Pinnaka A.; RT "Genome Assembly of Photobacterium sp. AK15."; RL Submitted (DEC-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:ELR63403.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AMZO01000042; ELR63403.1; -; Genomic_DNA. DR RefSeq; WP_007470835.1; NZ_AMZO01000042.1. DR EnsemblBacteria; ELR63403; ELR63403; C942_03845. DR PATRIC; fig|1056511.3.peg.4659; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000011134; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000011134}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000011134}. FT DOMAIN 198 365 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 429 AA; 48733 MW; 703499E88DDC4EB1 CRC64; MFDRYEAGEQ AILVHINFTQ EGEWEDLSEF EMLVSSAGVN TLRVVTGSRK TPHPKYYVGE GKAQEIADAV RAEEAEIVIF NHSLSPAQER NLERICKCRV LDRTGLILDI FAQRARTHEG KLQVELAQLR HISTRLIRGW THLERQKGGI GLRGPGETQL ETDRRLLRDR IKTILRRLEK VSKQREQGRR ARNRAEIPTI SLVGYTNAGK STLFNRVTDA GVYAADQLFA TLDPTLRKID VADVGATILA DTVGFIRHLP HDLVAAFKAT LKETQDATLL LHVVDASDDR FRENIDAVNE VLEEIDASEV PMLVVMNKID NLEDAEPRIE RDEDGIPRRV WVSAMEGLGI DLLFEALTER LSGTMVKHTL RLPPHMIGRY RSKFYQLGCI LREEYESDGS LTIDIRLPMT EWSRLQKRES TSLDDFIVA // ID L8JSG7_9BACT Unreviewed; 384 AA. AC L8JSG7; DT 03-APR-2013, integrated into UniProtKB/TrEMBL. DT 03-APR-2013, sequence version 1. DT 07-JUN-2017, entry version 30. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=C900_02365 {ECO:0000313|EMBL:ELR71780.1}; OS Fulvivirga imtechensis AK7. OC Bacteria; Bacteroidetes; Cytophagia; Cytophagales; Flammeovirgaceae; OC Fulvivirga. OX NCBI_TaxID=1237149 {ECO:0000313|EMBL:ELR71780.1, ECO:0000313|Proteomes:UP000011135}; RN [1] {ECO:0000313|EMBL:ELR71780.1, ECO:0000313|Proteomes:UP000011135} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=AK7 {ECO:0000313|EMBL:ELR71780.1, RC ECO:0000313|Proteomes:UP000011135}; RA Nupur N., Khatri I., Kumar R., Subramanian S., Pinnaka A.; RT "Genome assembly of Fulvivirga imtechensis AK7."; RL Submitted (DEC-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:ELR71780.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AMZN01000033; ELR71780.1; -; Genomic_DNA. DR RefSeq; WP_009579762.1; NZ_AMZN01000033.1. DR EnsemblBacteria; ELR71780; ELR71780; C900_02365. DR PATRIC; fig|1237149.3.peg.2231; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000011135; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000011135}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000011135}. FT DOMAIN 197 369 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 158 192 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 384 AA; 44078 MW; 2A19FBC7386141E7 CRC64; MKEKSNKGVL VAVAKKGEND NVVEEHLDEL AFLALTADIT TEKVFIQKLE QPDTRTFIGK GKLEDVKAYV VAREIDMVIF DDDLSPSQLR NLERELKCQI YDRSLLILDI FLNRAQTAQA KTQVELARYQ YLMPRLTRMW THLERQRGGT GTRGGAGEKE IETDRRNIRN QISVLKKKLE KIEKQNAVQR KSRSNIVRVA LVGYTNVGKS TLMRVLSKSD VKAEDKLFAT VDATVRKVML NHIPFLLSDT VGFIRKLPHH LIESFKSTLA EVREADILLH VVDISHPAYE DHIRVVKETL RDIDATDKPI IYVFNKIDLL EPEEDGEPVE KMHSVHIEQG DEKVFISAEK GINIGGLKEM LFKKIKKRHN QIYPNYLKDE YYSG // ID L8LFS9_9CHRO Unreviewed; 521 AA. AC L8LFS9; DT 03-APR-2013, integrated into UniProtKB/TrEMBL. DT 03-APR-2013, sequence version 1. DT 07-JUN-2017, entry version 29. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=GLO73106DRAFT_00001850 {ECO:0000313|EMBL:ELR96393.1}; OS Gloeocapsa sp. PCC 73106. OC Bacteria; Cyanobacteria; Oscillatoriophycideae; Chroococcales; OC Chroococcaceae; Gloeocapsa. OX NCBI_TaxID=102232 {ECO:0000313|EMBL:ELR96393.1, ECO:0000313|Proteomes:UP000011180}; RN [1] {ECO:0000313|EMBL:ELR96393.1, ECO:0000313|Proteomes:UP000011180} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=PCC 73106 {ECO:0000313|EMBL:ELR96393.1, RC ECO:0000313|Proteomes:UP000011180}; RX PubMed=23277585; DOI=10.1073/pnas.1217107110; RA Shih P.M., Wu D., Latifi A., Axen S.D., Fewer D.P., Talla E., RA Calteau A., Cai F., Tandeau de Marsac N., Rippka R., Herdman M., RA Sivonen K., Coursin T., Laurent T., Goodwin L., Nolan M., RA Davenport K.W., Han C.S., Rubin E.M., Eisen J.A., Woyke T., Gugger M., RA Kerfeld C.A.; RT "Improving the coverage of the cyanobacterial phylum using diversity- RT driven genome sequencing."; RL Proc. Natl. Acad. Sci. U.S.A. 110:1053-1058(2013). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:ELR96393.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ALVY01000227; ELR96393.1; -; Genomic_DNA. DR EnsemblBacteria; ELR96393; ELR96393; GLO73106DRAFT_00001850. DR PATRIC; fig|102232.3.peg.3853; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000011180; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000011180}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000011180}. FT DOMAIN 354 521 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 313 350 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 521 AA; 57485 MW; 6BC9113B38E4DCA0 CRC64; MDFAQRLGAI STEINQPVCA YLNRRGQVIR VGVGTPRQTQ IPAWELPRYG AQRLSGIRCL ATQLKAEPPN QSSLTAMAMQ RLDALATFNL GGAGFELRGG GVTGYVKEAY LAHLVPQLEQ WRVSTSVNLD ALAQQDFLEL VEGLESEFRQ EYVAKQVDGE HERAILVGLM TQNLTEAEYE ASLTELDRLV ASAGGEVLEV IRQKRPRSHP QTVVGVGKVE EIALMTQTLG ANLVVFDRDL SPAQVKNLEE QIGVRVVDRT EVILDIFAQR AQSGAGKLQV ELAQLEYMLP RLSGRGKTMS RLGGGIGTRG PGETKLETER RAIEKRITRL QKEVTQLQAH RSRLRQKRQQ YDLPTVAIMG YTNAGKSTLI NALTNAEVYT ADQLFATLDP TTRRLGVPDT ITGELHALLL TDTVGFINEL PPSLVDAFRA TLEEVTEADA LLHLVDISHG AWLNQLQSVN RIIDDMPLAP RNILVVFNKI DQVSEEILAV ARDEFPQGLF ISASERLGLE ELRQALAQVC S // ID L8M0X3_9CYAN Unreviewed; 573 AA. AC L8M0X3; DT 03-APR-2013, integrated into UniProtKB/TrEMBL. DT 03-APR-2013, sequence version 1. DT 07-JUN-2017, entry version 30. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=Xen7305DRAFT_00032130 {ECO:0000313|EMBL:ELS03489.1}; OS Xenococcus sp. PCC 7305. OC Bacteria; Cyanobacteria; Pleurocapsales; Xenococcaceae; Xenococcus. OX NCBI_TaxID=102125 {ECO:0000313|EMBL:ELS03489.1, ECO:0000313|Proteomes:UP000011203}; RN [1] {ECO:0000313|EMBL:ELS03489.1, ECO:0000313|Proteomes:UP000011203} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=PCC 7305 {ECO:0000313|EMBL:ELS03489.1, RC ECO:0000313|Proteomes:UP000011203}; RX PubMed=23277585; DOI=10.1073/pnas.1217107110; RA Shih P.M., Wu D., Latifi A., Axen S.D., Fewer D.P., Talla E., RA Calteau A., Cai F., Tandeau de Marsac N., Rippka R., Herdman M., RA Sivonen K., Coursin T., Laurent T., Goodwin L., Nolan M., RA Davenport K.W., Han C.S., Rubin E.M., Eisen J.A., Woyke T., Gugger M., RA Kerfeld C.A.; RT "Improving the coverage of the cyanobacterial phylum using diversity- RT driven genome sequencing."; RL Proc. Natl. Acad. Sci. U.S.A. 110:1053-1058(2013). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:ELS03489.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ALVZ01000161; ELS03489.1; -; Genomic_DNA. DR EnsemblBacteria; ELS03489; ELS03489; Xen7305DRAFT_00032130. DR PATRIC; fig|102125.3.peg.2207; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000011203; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000011203}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000011203}. FT DOMAIN 405 573 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 364 401 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 573 AA; 63944 MW; 36449EB637E4DD5B CRC64; MFNRRIESKL IETIYGTYKG LKKNQIKQLK KLYHQKLPVD RLTTADFAQR LAAIATEVGQ PVCTYFNRRG QVIRVGVGTP NETKIPPLEL PRYGAERLCG IRCIATQLDD HPPKESSLTA MIRQRLDALV VLTLTGEGKE RRGGGATGYI RDTYLAHLLP QTDLDLDTQE YWSISEPMSL EFLSSQDFLD LVEGLEAEFE REYVAQEVEE GHDRVILVGL HTDKTTNAEL EESLAELARL VDTAGGVVLQ TISQKRARPH PQTVVGAGKV QEIALRIQTT GANLVVFDRD LSPAQGRNLE SQFGIRVVDR TEVILDIFAQ RAQSRAGKLQ VELAQLEYML PRLVGRGQAM SRLGGGIGTR GPGETKLETE RRSIQKKITH LQRDVNELQA HRSRLRKQRQ KQDIATVAIV GYTNAGKSTL INALTNSDVY AADRLFATLD PTTRRLAIPD PVTGKPCNIL LTDTVGFIQE LPPSLVDAFR ATLEEVTEAD TLLHVVDLSH PSWQNQIRSV MKILQEMPLA VGPMLLVFNK LDQVDSETLA KAQEEYPLAL FIAAKERLGL ATLREKLREL ITN // ID L8N1L4_9CYAN Unreviewed; 496 AA. AC L8N1L4; DT 03-APR-2013, integrated into UniProtKB/TrEMBL. DT 03-APR-2013, sequence version 1. DT 07-JUN-2017, entry version 30. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=Pse7429DRAFT_1330 {ECO:0000313|EMBL:ELS33606.1}; OS Pseudanabaena biceps PCC 7429. OC Bacteria; Cyanobacteria; Synechococcales; Pseudanabaenaceae; OC Pseudanabaena. OX NCBI_TaxID=927668 {ECO:0000313|EMBL:ELS33606.1, ECO:0000313|Proteomes:UP000011201}; RN [1] {ECO:0000313|EMBL:ELS33606.1, ECO:0000313|Proteomes:UP000011201} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=PCC 7429 {ECO:0000313|EMBL:ELS33606.1, RC ECO:0000313|Proteomes:UP000011201}; RX PubMed=23277585; DOI=10.1073/pnas.1217107110; RA Shih P.M., Wu D., Latifi A., Axen S.D., Fewer D.P., Talla E., RA Calteau A., Cai F., Tandeau de Marsac N., Rippka R., Herdman M., RA Sivonen K., Coursin T., Laurent T., Goodwin L., Nolan M., RA Davenport K.W., Han C.S., Rubin E.M., Eisen J.A., Woyke T., Gugger M., RA Kerfeld C.A.; RT "Improving the coverage of the cyanobacterial phylum using diversity- RT driven genome sequencing."; RL Proc. Natl. Acad. Sci. U.S.A. 110:1053-1058(2013). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:ELS33606.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ALWB01000035; ELS33606.1; -; Genomic_DNA. DR EnsemblBacteria; ELS33606; ELS33606; Pse7429DRAFT_1330. DR PATRIC; fig|927668.3.peg.1444; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000011201; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000011201}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000011201}. FT DOMAIN 325 496 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 291 318 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 496 AA; 54990 MW; FE231CADCEEBC964 CRC64; MIRVAIGTPN QTKIPPLELP RYGSDRLSGL RCICATPDVE PPNLNDLTAM LMQRLDALVI LPVNLKGYAE RGYLAHLLPA TEAELPEQQN AWRVSKPMTL EAIAKQDFLE LVEGLEEEFS RNFAGRATDD DRDRVMLVGL MAQKEKSDSM PFAMIELGQL VESAGGTVLD ALWQKRERPH PQTVLGEGKV LELAIAAQTK GANLVVFDRE LTASQTRNLE RVIGLRVSDR TEVILDIFAQ RAQSSEGKLQ VELAQLEYRL PRLAGHGQAL SRLGGGIGTR GPGETKLETD RRTIQKRITF LQQQVNHLQA QRSRIRQKRV DREVPTVAIV GYTNAGKSTL LNAMTRADVY AADKLFATLD PTTRRLNLLG EDEQMHTVLL TDTVGFIHEL PKSLVDAFRA TLEEVSEADV LVHLVDASHS AWEAQLKAVD KILKDMPIAV GPILLVFNKI DAVDDPNAIL EKYPEAIAIS ALKREGFEQM SKSLFKMIEY AIGTLA // ID L8TPR6_9MICC Unreviewed; 503 AA. AC L8TPR6; DT 03-APR-2013, integrated into UniProtKB/TrEMBL. DT 03-APR-2013, sequence version 1. DT 30-AUG-2017, entry version 30. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=G205_16949 {ECO:0000313|EMBL:ELT43676.1}; OS Arthrobacter nitrophenolicus. OC Bacteria; Actinobacteria; Micrococcales; Micrococcaceae; Arthrobacter. OX NCBI_TaxID=683150 {ECO:0000313|EMBL:ELT43676.1, ECO:0000313|Proteomes:UP000011189}; RN [1] {ECO:0000313|EMBL:ELT43676.1, ECO:0000313|Proteomes:UP000011189} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SJCon {ECO:0000313|EMBL:ELT43676.1, RC ECO:0000313|Proteomes:UP000011189}; RA Vikram S., Kumar S., Vaidya B., Pinnaka A.K., Raghava G.P.S.; RT "Draft Genome Sequence of the 2-Chloro-4-Nitrophenol-Degrading RT Bacterium Arthrobacter sp. Strain SJCon."; RL Genome Announc. 1:E00058-13(2013). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:ELT43676.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AOFD01000042; ELT43676.1; -; Genomic_DNA. DR EnsemblBacteria; ELT43676; ELT43676; G205_16949. DR PATRIC; fig|683150.5.peg.3323; -. DR Proteomes; UP000011189; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000011189}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000011189}. FT DOMAIN 282 447 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 503 AA; 54857 MW; EF5FD10F58888EF7 CRC64; MIDRILSKDV PARNLSTPRG EERGNGKPVL GTAQAISRVD EEHTTYDGDQ QDLEERRALR RTAGLSTELE DVTEVEYRQL RLERVVLAGL WSEGTLADAE NSLRELAALA ETAGSEVLDG LVQRRDKPDP GTFLGSGKAQ ELKDIVMSTG ADTVIVDAEL APSQRRGLED IVKVKVIDRT ALILDIFAQH AKSREGKAQV ELAQLEYLLP RLRGWGESMS RQAGGQVGGA AAGMGSRGPG ETKIELDRRR IRTRMAKLRR EIAAMKPARE TKRANRRRNA VPSVAIAGYT NAGKSSLLNR LTDAGVLVEN ALFATLDPTV RKAETADGLG YTLADTVGFV RSLPTQLVEA FRSTLEEVAD ADLILHVVDA SHPDPEGQIA AVRKVFSEVD ARKIPEIIVL NKADAADPFV VERLKQREPR HVVVSARTGQ GIAELLRVIS ESIPRPSVKM ELLIPYNRGD LISKLHDSDA EIISLDHVEA GTRAVVMVRE GLAAELEPFA AND // ID L8XU44_9GAMM Unreviewed; 413 AA. AC L8XU44; DT 03-APR-2013, integrated into UniProtKB/TrEMBL. DT 03-APR-2013, sequence version 1. DT 30-AUG-2017, entry version 33. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=F387_01636 {ECO:0000313|EMBL:ELV07518.1}; OS Wohlfahrtiimonas chitiniclastica SH04. OC Bacteria; Proteobacteria; Gammaproteobacteria; Wohlfahrtiimonas. OX NCBI_TaxID=1261130 {ECO:0000313|EMBL:ELV07518.1, ECO:0000313|Proteomes:UP000011617}; RN [1] {ECO:0000313|EMBL:ELV07518.1, ECO:0000313|Proteomes:UP000011617} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SH04 {ECO:0000313|EMBL:ELV07518.1, RC ECO:0000313|Proteomes:UP000011617}; RX PubMed=23558531; RA Cao X.M., Chen T., Xu L.Z., Yao L.S., Qi J., Zhang X.L., Yan Q.L., RA Deng Y.H., Guo T.Y., Wang J., Hu K.X., Xu B.L.; RT "Complete Genome Sequence of Wohlfahrtiimonas chitiniclastica Strain RT SH04, Isolated from Chrysomya megacephala Collected from Pudong RT International Airport in China."; RL Genome Announc. 1:E0011913-E0011913(2013). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:ELV07518.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AOBV01000010; ELV07518.1; -; Genomic_DNA. DR EnsemblBacteria; ELV07518; ELV07518; F387_01636. DR PATRIC; fig|1261130.3.peg.1666; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000011617; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000011617}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000011617}. FT DOMAIN 185 352 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 413 AA; 46095 MW; 6136410CA5CBF4AC CRC64; MSLQTQDAHA EEIVEFQELV KAADVSELTL IKGKLATPNQ KYFLGLGKVE EVLEAVNALE ANVVIVNHEL SPSQNRNLER FLKVRVVDRT ALILDIFAQR AESFEGKLQV ELAQLTHISS RLVRMWTHLD SLRGGSVGLR GPGESQLEMD KRMIGLRIKQ LKIKLEKVQQ TRAQGQALRN RLGVPVVALV GYTNAGKSSL FNRLTDAGTY VEDKLFATLD PKHRTLFLEN IGDVVLIDTV GFISKLPHEL VTAFHSTLQS AADADLLLEV IDAGDPEREF KSEQVANVLV DIGAEAVPRI QVNNKIDLLE NVEPHVIYND EQQPSAVWIS AEKDLGIQAL KDAIGDYFKD QHVTKNVVLP PSQGRLRAKL FALNAVKNES VNEQGEFVMA LLMHKAEWDR LLKHDVDAQK YLN // ID L8YC93_TUPCH Unreviewed; 820 AA. AC L8YC93; DT 03-APR-2013, integrated into UniProtKB/TrEMBL. DT 03-APR-2013, sequence version 1. DT 10-MAY-2017, entry version 15. DE SubName: Full=Serine/threonine-protein phosphatase 2A regulatory subunit B'' subunit beta {ECO:0000313|EMBL:ELV12580.1}; DE Flags: Fragment; GN ORFNames=TREES_T100013670 {ECO:0000313|EMBL:ELV12580.1}; OS Tupaia chinensis (Chinese tree shrew). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Scandentia; Tupaiidae; Tupaia. OX NCBI_TaxID=246437 {ECO:0000313|EMBL:ELV12580.1, ECO:0000313|Proteomes:UP000011518}; RN [1] {ECO:0000313|Proteomes:UP000011518} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Zhang G., Fan Y., Yao Y., Huang Z.; RT "Genome of the Chinese tree shrew, a rising model animal genetically RT related to primates."; RL Submitted (JUL-2012) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; KB364439; ELV12580.1; -; Genomic_DNA. DR InParanoid; L8YC93; -. DR Proteomes; UP000011518; Unassembled WGS sequence. DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR CDD; cd01878; HflX; 1. DR InterPro; IPR011992; EF-hand-dom_pair. DR InterPro; IPR018247; EF_Hand_1_Ca_BS. DR InterPro; IPR002048; EF_hand_dom. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR Pfam; PF13499; EF-hand_7; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR SUPFAM; SSF47473; SSF47473; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR PROSITE; PS00018; EF_HAND_1; 1. DR PROSITE; PS50222; EF_HAND_2; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 4: Predicted; KW Calcium {ECO:0000256|PROSITE-ProRule:PRU00448}; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000011518}; KW Reference proteome {ECO:0000313|Proteomes:UP000011518}. FT DOMAIN 130 165 EF-hand. {ECO:0000259|PROSITE:PS50222}. FT DOMAIN 512 676 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT CA_BIND 143 154 {ECO:0000256|PROSITE-ProRule:PRU00448}. FT COILED 474 508 {ECO:0000256|SAM:Coils}. FT NON_TER 1 1 {ECO:0000313|EMBL:ELV12580.1}. SQ SEQUENCE 820 AA; 91175 MW; 1AD3F71280D9C7C2 CRC64; PRVPPQVIQR IFYTVNRSWS GRITCAELRR SSFLQNVALL EEEADINQLP EFFSYEHFYV IYCKFWELDT DHDLLIDAQD LARHNDHAIS TKMIDRIFSG AVTRGRRVQK EGKMSYADFV WFLISEEDKK TPTSIEYWFR CMDLDGDGAL SMFELEYFYE EQCRRLDSLA IEALPFQDCL CQMLDLVKPQ SEGKITLHDL KRCKLANVFF DTFFNIEKYL DHEQKEQVSL LRESESDGPE LSDWEKYAAE EYDILVAEEA VGEPWEDGFD AELSPVEQKL SALRSPLAQR SALGDVDLYE FACGEDDLQP LSRCPCDPTE AGLAPCGHGG TGTPMGAGLS GKAREDGRQG RGRDQEWRIP AEWQVAEATA LVHTLAGWSV VQTMVVPTRT PDSKLVFGKG SLEHLTGKIR GSPEITAVFL NVERMAAPTK KELEAAWGVE VFDRFTIVLH IFRCNARTRE ARLQVALAEI PLLRGVLRRR LKEKELKIQR ALERLRAKRR VLRRERARRE LPTIAVVGYT NCGKTTLIRA LTGDPAARPR DQLFATLDVT AHAGSLPSRM TVVYVDTVGF LSQLPHGLVE AFSATLEDVA HSDLILHVRD VSHPEAELQK ASVLGALRGL RLPPTLLDSV LEVHNKVDLL PGYSPPEPGV LAVSALQGCG LQELKARLEE EVLRATGRRV LTLRVRLAGA QLSAVYTPVP AHLLTPSSHS AVYTPVPAQI PTPSSHSAVY TPVPAHLTPS SHGAVYTQYL LTSPPHHPTV LSTPQYLLTP SSHSAVYTPV PAQIPTPSSH GAVYTPVPAQ IPTPSSHGAV YTPVPAHLTV // ID L9PE22_9BURK Unreviewed; 394 AA. AC L9PE22; DT 03-APR-2013, integrated into UniProtKB/TrEMBL. DT 03-APR-2013, sequence version 1. DT 07-JUN-2017, entry version 29. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:ELX09867.1}; GN ORFNames=Jab_2c19510 {ECO:0000313|EMBL:ELX09867.1}; OS Janthinobacterium sp. HH01. OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Oxalobacteraceae; Janthinobacterium. OX NCBI_TaxID=1198452 {ECO:0000313|EMBL:ELX09867.1, ECO:0000313|Proteomes:UP000011616}; RN [1] {ECO:0000313|EMBL:ELX09867.1, ECO:0000313|Proteomes:UP000011616} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=HH01 {ECO:0000313|EMBL:ELX09867.1, RC ECO:0000313|Proteomes:UP000011616}; RX PubMed=23405110; DOI=10.1371/journal.pone.0055045; RA Hornung C., Poehlein A., Haack F.S., Schmidt M., Dierking K., RA Pohlen A., Schulenburg H., Blokesch M., Plener L., Jung K., Bonge A., RA Krohn-Molt I., Utpatel C., Timmermann G., Spieck E., RA Pommerening-Roser A., Bode E., Bode H.B., Daniel R., Schmeisser C., RA Streit W.R.; RT "The Janthinobacterium sp. HH01 Genome Encodes a Homologue of the V. RT cholerae CqsA and L. pneumophila LqsA Autoinducer Synthases."; RL PLoS ONE 8:E55045-E55045(2013). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:ELX09867.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AMWD01000002; ELX09867.1; -; Genomic_DNA. DR RefSeq; WP_008450613.1; NZ_AMWD01000002.1. DR EnsemblBacteria; ELX09867; ELX09867; Jab_2c19510. DR PATRIC; fig|1198452.4.peg.4514; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000011616; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000011616}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000011616}. FT DOMAIN 190 357 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 156 183 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 394 AA; 43394 MW; C6112AAD0E119836 CRC64; MRAALVGIDF GQGDFAASVE ELQLLARSAG AEPVTTITAK RSSPDAAYFV GSGKADEIGL AVLDHRIEIV IFNHALSPAQ QRNLEKRLNI RVLDRTSLIL DIFAQRAASH EGKLQVELAQ LQHLATRLIR GWTHLERQKG GIGLRGPGET QLETDRRLIG ERVKALRARL DKLRKQHETQ RRSRGRSQTF SVSLVGYTNA GKSTLFNAVT KAGVYVADQL FATLDTTSRR VYMGQEVGNV VISDTVGFVR ELPHQLVAAF RATLEETIHA DLLLHVVDAS SPVRMEQIEQ VNLVLKEIGA DHIPQILVWN KIDAAGLEPS VERDEYDKIS RVFLSARTGQ GLDLLRGAIV EWAKNAPGAR LNQAYHVDEE ADEEPAEPEA EPDSSPTLTH VGSH // ID L9U8A8_9GAMM Unreviewed; 436 AA. AC L9U8A8; DT 03-APR-2013, integrated into UniProtKB/TrEMBL. DT 03-APR-2013, sequence version 1. DT 30-AUG-2017, entry version 29. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=HALTITAN_2201 {ECO:0000313|EMBL:ELY21074.1}; OS Halomonas titanicae BH1. OC Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales; OC Halomonadaceae; Halomonas. OX NCBI_TaxID=1204738 {ECO:0000313|EMBL:ELY21074.1, ECO:0000313|Proteomes:UP000011651}; RN [1] {ECO:0000313|EMBL:ELY21074.1, ECO:0000313|Proteomes:UP000011651} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BH1 {ECO:0000313|EMBL:ELY21074.1, RC ECO:0000313|Proteomes:UP000011651}; RX PubMed=23516210; RA Sanchez-Porro C., de la Haba R.R., Cruz-Hernandez N., Gonzalez J.M., RA Reyes-Guirao C., Navarro-Sampedro L., Carballo M., Ventosa A.; RT "Draft Genome of the Marine Gammaproteobacterium Halomonas RT titanicae."; RL Genome Announc. 1:E0008313-E0008313(2013). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:ELY21074.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AOPO01000009; ELY21074.1; -; Genomic_DNA. DR RefSeq; WP_009287759.1; NZ_AOPO01000009.1. DR EnsemblBacteria; ELY21074; ELY21074; HALTITAN_2201. DR PATRIC; fig|1204738.3.peg.3296; -. DR Proteomes; UP000011651; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000011651}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}. FT DOMAIN 199 365 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 436 AA; 49081 MW; 3DAA3A335012751A CRC64; MFFERPDAGE TAVLVHVDFH DEQKREDPGE FLELVRSAGA EPATLLTASR HRPDSRTFIG SGKLEELRAL LAAHEAELVI FNHSLSPSQE RNVEQELKCR VLDRTGLILD IFAQRARTHE GKLQVELAQL EYMSTRLVRG WTHLERQKGG IGLRGPGETQ LETDRRLLRG RIKSIHKRLD KVRSQRDQNR RARARAEIHS VSLVGYTNAG KSTLFNALTN SEVYAADQLF ATLDPTLRRL EIEDVGPVVM ADTVGFIRHL PHKLVEAFQA TLQEASEASL LVHVIDAADP DRELNVEQVE LVLKEIGADD VPVLKVMNKI DKLDSAPRIE RDGHGVPEVV WLSAQQGQGL ELLHEALTER LANDVIGFSL TLTPEQGKLR AGLHELNAVR EEAFDEQGHS VLDVRLPRRD FNQLMAQLGE RANTYLPEAL RETNEW // ID M0QND6_9ACTN Unreviewed; 516 AA. AC M0QND6; DT 03-APR-2013, integrated into UniProtKB/TrEMBL. DT 03-APR-2013, sequence version 1. DT 07-JUN-2017, entry version 31. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:GAC68932.1}; GN ORFNames=GS4_19_01220 {ECO:0000313|EMBL:GAC68932.1}; OS Gordonia soli NBRC 108243. OC Bacteria; Actinobacteria; Corynebacteriales; Gordoniaceae; Gordonia. OX NCBI_TaxID=1223545 {ECO:0000313|EMBL:GAC68932.1, ECO:0000313|Proteomes:UP000011666}; RN [1] {ECO:0000313|EMBL:GAC68932.1, ECO:0000313|Proteomes:UP000011666} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NBRC 108243 {ECO:0000313|EMBL:GAC68932.1, RC ECO:0000313|Proteomes:UP000011666}; RA Isaki-Nakamura S., Hosoyama A., Tsuchikane K., Ando Y., Baba S., RA Ohji S., Hamada M., Tamura T., Yamazoe A., Yamazaki S., Fujita N.; RT "Whole genome shotgun sequence of Gordonia soli NBRC 108243."; RL Submitted (JAN-2013) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:GAC68932.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BANX01000019; GAC68932.1; -; Genomic_DNA. DR RefSeq; WP_007621492.1; NZ_BANX01000019.1. DR EnsemblBacteria; GAC68932; GAC68932; GS4_19_01220. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000011666; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000011666}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000011666}. FT DOMAIN 294 463 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 253 280 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 516 AA; 56059 MW; 91BACCC39422F8FC CRC64; MTEPARFLPE SHPTTDHGRD GDDRPDPRAD EVTPVDIDAD LDDSSDDRRI GRSTAFTIPT TGELQLSERA SLQRVAGLST ELTDVTEVEY RQLRLELVVL VGVWTEGTAA QARASMVELA ALAETAGSQV LDALIQRRSK PDSATYIGSG KADELREVVL ATGADTVICD GELTPAQLTA LEKIVKVKVI DRTALILDIF AQHATSREGK AQVSLAQMEY MLPRLRGWGE SMSRQAGGRA GSNGGVGLRG PGETKIETDR RRIRERMSKL RREIRAMKKS RVVMRSARRQ SSVPALTVAG YTNAGKSSLV NAMTGSGVLV QDALFATLDP TTRRATLDDG REVVFTDTVG FVRHLPTQLV EAFRSTLEEV VDADLVLHVV DGSDEFPLEQ ISAVRRVINE VVADEGAAPP PELLVINKID AVDELRLTEL RGALDGAVFV SAQTGEGLPE LFDRIREFVG RSDVELTLSV PFTRGDVVSR IHREGEVLSA EHDADGTRMH VRVPSAFAGE LSDLVV // ID M0S3G3_MUSAM Unreviewed; 802 AA. AC M0S3G3; DT 03-APR-2013, integrated into UniProtKB/TrEMBL. DT 03-APR-2013, sequence version 1. DT 30-AUG-2017, entry version 29. DE SubName: Full=Uncharacterized protein {ECO:0000313|EnsemblPlants:GSMUA_Achr1P27060_001}; OS Musa acuminata subsp. malaccensis (Wild banana) (Musa malaccensis). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Zingiberales; Musaceae; OC Musa. OX NCBI_TaxID=214687 {ECO:0000313|EnsemblPlants:GSMUA_Achr1P27060_001, ECO:0000313|Proteomes:UP000012960}; RN [1] {ECO:0000313|EnsemblPlants:GSMUA_Achr1P27060_001, ECO:0000313|Proteomes:UP000012960} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Doubled-haploid Pahang [DH-Pahang] RC {ECO:0000313|EnsemblPlants:GSMUA_Achr1P27060_001, RC ECO:0000313|Proteomes:UP000012960}; RX PubMed=22801500; DOI=10.1038/nature11241; RA D Hont A., Denoeud F., Aury J.M., Baurens F.C., Carreel F., RA Garsmeur O., Noel B., Bocs S., Droc G., Rouard M., Da Silva C., RA Jabbari K., Cardi C., Poulain J., Souquet M., Labadie K., Jourda C., RA Lengelle J., Roudier-Goud M., Alberti A., Bernard M., Correa M., RA Ayyampalayam S., Mckain M.R., Leebens-Mack J., Burgess D., RA Freeling M., Mbeguie-A-Mbeguie D., Chabannes M., Wicker T., Panaud O., RA Barbosa J., Hribova E., Heslop-Harrison P., Habas R., Rivallan R., RA Francois P., Poiron C., Kilian A., Burthia D., Jenny C., Bakry F., RA Brown S., Guignon V., Kema G., Dita M., Waalwijk C., Joseph S., RA Dievart A., Jaillon O., Leclercq J., Argout X., Lyons E., Almeida A., RA Jeridi M., Dolezel J., Roux N., Risterucci A.M., Weissenbach J., RA Ruiz M., Glaszmann J.C., Quetier F., Yahiaoui N., Wincker P.; RT "The banana (Musa acuminata) genome and the evolution of RT monocotyledonous plants."; RL Nature 488:213-217(2012). RN [2] {ECO:0000313|EnsemblPlants:GSMUA_Achr1P27060_001} RP IDENTIFICATION. RC STRAIN=subsp. malaccensis RC {ECO:0000313|EnsemblPlants:GSMUA_Achr1P27060_001}; RG EnsemblPlants; RL Submitted (JUN-2013) to UniProtKB. CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|PROSITE- CC ProRule:PRU00108, ECO:0000256|RuleBase:RU000682}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR STRING; 4641.GSMUA_Achr1P27060_001; -. DR EnsemblPlants; GSMUA_Achr1T27060_001; GSMUA_Achr1P27060_001; GSMUA_Achr1G27060_001. DR Gramene; GSMUA_Achr1T27060_001; GSMUA_Achr1P27060_001; GSMUA_Achr1G27060_001. DR OrthoDB; EOG09360975; -. DR Proteomes; UP000012960; Chromosome 1. DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro. DR GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; IEA:InterPro. DR CDD; cd01878; HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR009057; Homeobox-like. DR InterPro; IPR017970; Homeobox_CS. DR InterPro; IPR001356; Homeobox_dom. DR InterPro; IPR003106; Leu_zip_homeo. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF02183; HALZ; 1. DR Pfam; PF00046; Homeobox; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SMART; SM00340; HALZ; 1. DR SMART; SM00389; HOX; 1. DR SUPFAM; SSF46689; SSF46689; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. DR PROSITE; PS00027; HOMEOBOX_1; 1. DR PROSITE; PS50071; HOMEOBOX_2; 1. PE 4: Predicted; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000012960}; KW DNA-binding {ECO:0000256|PROSITE-ProRule:PRU00108, KW ECO:0000256|RuleBase:RU000682}; KW Homeobox {ECO:0000256|PROSITE-ProRule:PRU00108, KW ECO:0000256|RuleBase:RU000682}; KW Nucleus {ECO:0000256|PROSITE-ProRule:PRU00108, KW ECO:0000256|RuleBase:RU000682}; KW Reference proteome {ECO:0000313|Proteomes:UP000012960}. FT DOMAIN 321 449 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT DOMAIN 653 713 Homeobox DNA-binding. FT {ECO:0000259|PROSITE:PS50071}. FT DNA_BIND 655 714 Homeobox. {ECO:0000256|PROSITE- FT ProRule:PRU00108}. FT COILED 712 746 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 802 AA; 88145 MW; 1BF3F365A3375FBB CRC64; MLHLRVITRL RTPLRSLPRI LLTPFSSPPP PSPPFLRPPP PISPPSAPFS TTSSSRRRRG GGDAEADESD GAGVSLFGRD PTHPPKLFVV QPRLRPDSLL HSKLSEALNL ANSLEERRDG VFAEDYGSKE PPPHLVVQNP GARSLRVHSD TYFGRGTVEN VKCELRALVT ENAIDAIFVN AILSGIQQRN LEVSWQKPVL DRIGLIIEIF NAHAETKEAK LQSELAALMY KRTRLVRVRG PGGRMTFGTS GEAEVVSARG RGSGGRGFIS GAGETELQLQ RRRIQERRIH ILSQIEEVRR TRSLQRYARR RHGSSYGQGL ATVAVVGYTN AGKSTLVSAL SESDLYSDDR LFATVDPRVR SVVLPSGKKA LLSDTVGFIS DLPVQLVEAF HATLEEVVEA DLLVHVLDSS SPDLDAQREA VLQVLQQLGV SGEKIKNMIE VWNKIDLLES NGGADECFGE EEIIGEDEEE YPEDDMTCDP SSGKPVDEDD DAMASEFSQE ESLDNADDVA SEFSCGEHMD DNDDYDDGDI ASDVSTEETT KRLQNSRLLL KVESQAWMDM DPHDTFDTDL SLGLGIGPAS TASADDCRRR QRGCCSPCTN LFPDEPSLSL SLSDDASGGG RTMQKAEADR PAQLSSSRSA ASSFSSAADE EENSSGRKKL RLTREQSALL EDRFKEHTTL NPKQKQALAK DLNLRPRQVE VWFQNRRART KLKQTEVDCE FLKKCYEALT NENQRLHKEL QELKALKFAQ PLLHMQLPSA AAPLTMCPSC QRISGGGGDA KDSSKAPKPG HCLNPFSHSA AC // ID M0U991_MUSAM Unreviewed; 343 AA. AC M0U991; DT 03-APR-2013, integrated into UniProtKB/TrEMBL. DT 03-APR-2013, sequence version 1. DT 05-JUL-2017, entry version 19. DE SubName: Full=Uncharacterized protein {ECO:0000313|EnsemblPlants:GSMUA_AchrUn_randomP14820_001}; OS Musa acuminata subsp. malaccensis (Wild banana) (Musa malaccensis). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Zingiberales; Musaceae; OC Musa. OX NCBI_TaxID=214687 {ECO:0000313|EnsemblPlants:GSMUA_AchrUn_randomP14820_001, ECO:0000313|Proteomes:UP000012960}; RN [1] {ECO:0000313|EnsemblPlants:GSMUA_AchrUn_randomP14820_001, ECO:0000313|Proteomes:UP000012960} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Doubled-haploid Pahang [DH-Pahang] RC {ECO:0000313|EnsemblPlants:GSMUA_AchrUn_randomP14820_001, RC ECO:0000313|Proteomes:UP000012960}; RX PubMed=22801500; DOI=10.1038/nature11241; RA D Hont A., Denoeud F., Aury J.M., Baurens F.C., Carreel F., RA Garsmeur O., Noel B., Bocs S., Droc G., Rouard M., Da Silva C., RA Jabbari K., Cardi C., Poulain J., Souquet M., Labadie K., Jourda C., RA Lengelle J., Roudier-Goud M., Alberti A., Bernard M., Correa M., RA Ayyampalayam S., Mckain M.R., Leebens-Mack J., Burgess D., RA Freeling M., Mbeguie-A-Mbeguie D., Chabannes M., Wicker T., Panaud O., RA Barbosa J., Hribova E., Heslop-Harrison P., Habas R., Rivallan R., RA Francois P., Poiron C., Kilian A., Burthia D., Jenny C., Bakry F., RA Brown S., Guignon V., Kema G., Dita M., Waalwijk C., Joseph S., RA Dievart A., Jaillon O., Leclercq J., Argout X., Lyons E., Almeida A., RA Jeridi M., Dolezel J., Roux N., Risterucci A.M., Weissenbach J., RA Ruiz M., Glaszmann J.C., Quetier F., Yahiaoui N., Wincker P.; RT "The banana (Musa acuminata) genome and the evolution of RT monocotyledonous plants."; RL Nature 488:213-217(2012). RN [2] {ECO:0000313|EnsemblPlants:GSMUA_AchrUn_randomP14820_001} RP IDENTIFICATION. RC STRAIN=subsp. malaccensis RC {ECO:0000313|EnsemblPlants:GSMUA_AchrUn_randomP14820_001}; RG EnsemblPlants; RL Submitted (JAN-2017) to UniProtKB. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR STRING; 4641.GSMUA_AchrUn_randomP14820_001; -. DR EnsemblPlants; GSMUA_AchrUn_randomT14820_001; GSMUA_AchrUn_randomP14820_001; GSMUA_AchrUn_randomG14820_001. DR Gramene; GSMUA_AchrUn_randomT14820_001; GSMUA_AchrUn_randomP14820_001; GSMUA_AchrUn_randomG14820_001. DR OrthoDB; EOG093609UJ; -. DR Proteomes; UP000012960; Unplaced. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000012960}; KW Reference proteome {ECO:0000313|Proteomes:UP000012960}. FT DOMAIN 165 254 GTP-bdg_N. {ECO:0000259|Pfam:PF13167}. FT DOMAIN 281 329 GTP-bdg_M. {ECO:0000259|Pfam:PF16360}. SQ SEQUENCE 343 AA; 38258 MW; B73A1EDD420EEE0B CRC64; MSVCFFSTTP HRVTSTAAAS SFSRPVHCQT YPSFHHCGFG HHFRYHVPPI KFLSTPWMSR ARLIGVLKES SEVETDDRQR APASDQEELE EAADGVVANG VVAETSKEGS DLVRKVPVRS KRKIDEEEDG YDRYTLRNGR EVFQEKAYLV GVECKGTEDN TFSIEESLQE LAQLADTAGL SVVGSTYQKL ANPNPRTYIG SGKVAEIKSA IHALDVETVI FDDELSAGQL RNLEKALGGD VRVCDRTALI LDIFNQRAAT HEAALQASIS TQHFDSNILC KVALAQMEYQ LPRLTKMWTH LERQAGGKVK GMGEKQIEVD KRILRTQIST NVFPFLSNFF FLL // ID M0ZWL6_SOLTU Unreviewed; 554 AA. AC M0ZWL6; DT 03-APR-2013, integrated into UniProtKB/TrEMBL. DT 03-APR-2013, sequence version 1. DT 30-AUG-2017, entry version 29. DE SubName: Full=Uncharacterized protein {ECO:0000313|EnsemblPlants:PGSC0003DMT400009607}; OS Solanum tuberosum (Potato). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae; OC Pentapetalae; asterids; lamiids; Solanales; Solanaceae; Solanoideae; OC Solaneae; Solanum. OX NCBI_TaxID=4113 {ECO:0000313|EnsemblPlants:PGSC0003DMT400009607, ECO:0000313|Proteomes:UP000011115}; RN [1] {ECO:0000313|EnsemblPlants:PGSC0003DMT400009607} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. DM1-3 516 R44 RC {ECO:0000313|EnsemblPlants:PGSC0003DMT400009607}; RX PubMed=21743474; DOI=10.1038/nature10158; RG The Potato Genome Sequencing Consortium; RT "Genome sequence and analysis of the tuber crop potato."; RL Nature 475:189-195(2011). RN [2] {ECO:0000313|EnsemblPlants:PGSC0003DMT400009607} RP IDENTIFICATION. RC STRAIN=DM1-3 516 R44 {ECO:0000313|EnsemblPlants:PGSC0003DMT400009607}; RG EnsemblPlants; RL Submitted (JUN-2015) to UniProtKB. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR STRING; 4113.PGSC0003DMT400009607; -. DR EnsemblPlants; PGSC0003DMT400009607; PGSC0003DMT400009607; PGSC0003DMG400003749. DR Gramene; PGSC0003DMT400009607; PGSC0003DMT400009607; PGSC0003DMG400003749. DR eggNOG; KOG0410; Eukaryota. DR eggNOG; COG2262; LUCA. DR InParanoid; M0ZWL6; -. DR OMA; VILEIFH; -. DR OrthoDB; EOG093609UJ; -. DR Proteomes; UP000011115; Unassembled WGS sequence. DR ExpressionAtlas; M0ZWL6; baseline. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000011115}; KW Reference proteome {ECO:0000313|Proteomes:UP000011115}. FT DOMAIN 331 497 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 554 AA; 62034 MW; DBD1576C07E2F780 CRC64; MSLCFCSNLK PSILFPESDF RWVQTRTRPV SFTKLIQTKY SYRGCIKAVG EEIGVLSPDD SLSVRNPVIE EETVPETEVN EVENGVASVV AEEKAQTWIS KSENKEKLDE EDENASRFKL RNGREVFEEK AYLVGVACKG DTEDSFGIEE SLKELAQLAD TAGLLVVDST YQKLSSPNPR TYIGSGKVSE IKSAIRAFDV ETVIFDDELS PGQLRNLEKA FGGDVRVCDR TALILDIFNQ RAATREASLQ ASPLLLSVSL AQMEYQLPRL TRMWTHLERQ AGGQVKGMGE KQIEVDKRIL RTQIGVLKKE LESVRKHRKQ YRNRRVSVPV PVVSLVGYTN AGKSTLLNQL TGADVLAEDR LFATLDPTTR RVQMKNGKEF LLTDTVGFIQ KLPTTLVAAF RATLEEIAES SILVHVADIS HPLAEQQIEA VEKVLSELDT SSIPKLMLWN KVDKAEDPEK IKLEAKTRND VVCVSALTGE GLDEFCNEIQ NRLKDAMVWV EALIPFDKGE LLSTIHQVGM VERTEYTEKG TLVRAHVPLR FARLLTPMRQ MCVS // ID M0ZWL7_SOLTU Unreviewed; 547 AA. AC M0ZWL7; DT 03-APR-2013, integrated into UniProtKB/TrEMBL. DT 03-APR-2013, sequence version 1. DT 05-JUL-2017, entry version 25. DE SubName: Full=Uncharacterized protein {ECO:0000313|EnsemblPlants:PGSC0003DMT400009608}; OS Solanum tuberosum (Potato). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae; OC Pentapetalae; asterids; lamiids; Solanales; Solanaceae; Solanoideae; OC Solaneae; Solanum. OX NCBI_TaxID=4113 {ECO:0000313|EnsemblPlants:PGSC0003DMT400009608, ECO:0000313|Proteomes:UP000011115}; RN [1] {ECO:0000313|EnsemblPlants:PGSC0003DMT400009608} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. DM1-3 516 R44 RC {ECO:0000313|EnsemblPlants:PGSC0003DMT400009608}; RX PubMed=21743474; DOI=10.1038/nature10158; RG The Potato Genome Sequencing Consortium; RT "Genome sequence and analysis of the tuber crop potato."; RL Nature 475:189-195(2011). RN [2] {ECO:0000313|EnsemblPlants:PGSC0003DMT400009608} RP IDENTIFICATION. RC STRAIN=DM1-3 516 R44 {ECO:0000313|EnsemblPlants:PGSC0003DMT400009608}; RG EnsemblPlants; RL Submitted (JUN-2015) to UniProtKB. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR RefSeq; XP_006341977.1; XM_006341915.2. DR EnsemblPlants; PGSC0003DMT400009608; PGSC0003DMT400009608; PGSC0003DMG400003749. DR GeneID; 102603341; -. DR Gramene; PGSC0003DMT400009608; PGSC0003DMT400009608; PGSC0003DMG400003749. DR KEGG; sot:102603341; -. DR eggNOG; KOG0410; Eukaryota. DR eggNOG; COG2262; LUCA. DR KO; K03665; -. DR Proteomes; UP000011115; Unassembled WGS sequence. DR ExpressionAtlas; M0ZWL7; baseline. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000011115}; KW Reference proteome {ECO:0000313|Proteomes:UP000011115}. FT DOMAIN 324 490 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 547 AA; 61352 MW; 46437B095E71F3FE CRC64; MSLCFCSNLK PSILFPESDF RWVQTRTRPV SFTKLIQTKY SYRGCIKAVG EEIGVLSPDD SLSVRNPVIE EETVPETEVN EVENGVASVV AEEKAQTWIS KSENKEKLDE EDENASRFKL RNGREVFEEK AYLVGVACKG DTEDSFGIEE SLKELAQLAD TAGLLVVDST YQKLSSPNPR TYIGSGKVSE IKSAIRAFDV ETVIFDDELS PGQLRNLEKA FGGDVRVCDR TALILDIFNQ RAATREASLQ VSLAQMEYQL PRLTRMWTHL ERQAGGQVKG MGEKQIEVDK RILRTQIGVL KKELESVRKH RKQYRNRRVS VPVPVVSLVG YTNAGKSTLL NQLTGADVLA EDRLFATLDP TTRRVQMKNG KEFLLTDTVG FIQKLPTTLV AAFRATLEEI AESSILVHVA DISHPLAEQQ IEAVEKVLSE LDTSSIPKLM LWNKVDKAED PEKIKLEAKT RNDVVCVSAL TGEGLDEFCN EIQNRLKDAM VWVEALIPFD KGELLSTIHQ VGMVERTEYT EKGTLVRAHV PLRFARLLTP MRQMCVS // ID M1BXJ6_SOLTU Unreviewed; 333 AA. AC M1BXJ6; DT 03-APR-2013, integrated into UniProtKB/TrEMBL. DT 03-APR-2013, sequence version 1. DT 05-JUL-2017, entry version 17. DE SubName: Full=Uncharacterized protein {ECO:0000313|EnsemblPlants:PGSC0003DMT400055207}; OS Solanum tuberosum (Potato). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae; OC Pentapetalae; asterids; lamiids; Solanales; Solanaceae; Solanoideae; OC Solaneae; Solanum. OX NCBI_TaxID=4113 {ECO:0000313|EnsemblPlants:PGSC0003DMT400055207, ECO:0000313|Proteomes:UP000011115}; RN [1] {ECO:0000313|EnsemblPlants:PGSC0003DMT400055207} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. DM1-3 516 R44 RC {ECO:0000313|EnsemblPlants:PGSC0003DMT400055207}; RX PubMed=21743474; DOI=10.1038/nature10158; RG The Potato Genome Sequencing Consortium; RT "Genome sequence and analysis of the tuber crop potato."; RL Nature 475:189-195(2011). RN [2] {ECO:0000313|EnsemblPlants:PGSC0003DMT400055207} RP IDENTIFICATION. RC STRAIN=DM1-3 516 R44 {ECO:0000313|EnsemblPlants:PGSC0003DMT400055207}; RG EnsemblPlants; RL Submitted (JUN-2015) to UniProtKB. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EnsemblPlants; PGSC0003DMT400055207; PGSC0003DMT400055207; PGSC0003DMG400021428. DR Gramene; PGSC0003DMT400055207; PGSC0003DMT400055207; PGSC0003DMG400021428. DR eggNOG; KOG0410; Eukaryota. DR eggNOG; COG2262; LUCA. DR Proteomes; UP000011115; Unassembled WGS sequence. DR ExpressionAtlas; M1BXJ6; baseline. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000011115}; KW Reference proteome {ECO:0000313|Proteomes:UP000011115}. FT DOMAIN 144 210 GTP-bdg_N. {ECO:0000259|Pfam:PF13167}. FT DOMAIN 213 309 GTP-bdg_M. {ECO:0000259|Pfam:PF16360}. SQ SEQUENCE 333 AA; 36858 MW; 03EA76588C401EC4 CRC64; MFRTISHLRS SLTSKICLPQ ALRHFSQFSI SLLPTPTQSI QLPVNPSPST QLSLFHSLSS PCSSLLLQKH QDGSGDDFNT DPKSPPRLFV VQPRFRPDSV LKPKLNEALN LANSLEEQRD GFYDTEFLDK QMPHHLVVQN PASRSIRADT FFGPGTVDTV KCHVNSLDTQ QEGIDAIFVN AILTGIQQRN LERDWGKPVL DRVGLIIEIF NAHAQTKEAK LQAEFAALMY KKSRLVRVRG PGGRYGFGVG GEAEVVSARG RGSGGRGFIS GAGETELQLQ RRRILERKNQ LLSEIKEVRR TRSLQRAARK RHGGSDGQEI PTVAVVGYTN AVG // ID M1BXJ7_SOLTU Unreviewed; 367 AA. AC M1BXJ7; DT 03-APR-2013, integrated into UniProtKB/TrEMBL. DT 03-APR-2013, sequence version 1. DT 05-JUL-2017, entry version 21. DE SubName: Full=Uncharacterized protein {ECO:0000313|EnsemblPlants:PGSC0003DMT400055208}; OS Solanum tuberosum (Potato). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae; OC Pentapetalae; asterids; lamiids; Solanales; Solanaceae; Solanoideae; OC Solaneae; Solanum. OX NCBI_TaxID=4113 {ECO:0000313|EnsemblPlants:PGSC0003DMT400055208, ECO:0000313|Proteomes:UP000011115}; RN [1] {ECO:0000313|EnsemblPlants:PGSC0003DMT400055208} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. DM1-3 516 R44 RC {ECO:0000313|EnsemblPlants:PGSC0003DMT400055208}; RX PubMed=21743474; DOI=10.1038/nature10158; RG The Potato Genome Sequencing Consortium; RT "Genome sequence and analysis of the tuber crop potato."; RL Nature 475:189-195(2011). RN [2] {ECO:0000313|EnsemblPlants:PGSC0003DMT400055208} RP IDENTIFICATION. RC STRAIN=DM1-3 516 R44 {ECO:0000313|EnsemblPlants:PGSC0003DMT400055208}; RG EnsemblPlants; RL Submitted (JUN-2015) to UniProtKB. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EnsemblPlants; PGSC0003DMT400055208; PGSC0003DMT400055208; PGSC0003DMG400021428. DR Gramene; PGSC0003DMT400055208; PGSC0003DMT400055208; PGSC0003DMG400021428. DR eggNOG; KOG0410; Eukaryota. DR eggNOG; COG2262; LUCA. DR Proteomes; UP000011115; Unassembled WGS sequence. DR ExpressionAtlas; M1BXJ7; baseline. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000011115}; KW Reference proteome {ECO:0000313|Proteomes:UP000011115}. FT DOMAIN 321 367 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 367 AA; 40556 MW; 156DA11D296C9505 CRC64; MFRTISHLRS SLTSKICLPQ ALRHFSQFSI SLLPTPTQSI QLPVNPSPST QLSLFHSLSS PCSSLLLQKH QDGSGDDFNT DPKSPPRLFV VQPRFRPDSV LKPKLNEALN LANSLEEQRD GFYDTEFLDK QMPHHLVVQN PASRSIRADT FFGPGTVDTV KCHVNSLDTQ QEGIDAIFVN AILTGIQQRN LERDWGKPVL DRVGLIIEIF NAHAQTKEAK LQAEFAALMY KKSRLVRVRG PGGRYGFGVG GEAEVVSARG RGSGGRGFIS GAGETELQLQ RRRILERKNQ LLSEIKEVRR TRSLQRAARK RHGGSDGQEI PTVAVVGYTN AGKSTLVSAV SESFLYCDDR LFATVDPKLR SVILPSG // ID M1BXJ8_SOLTU Unreviewed; 613 AA. AC M1BXJ8; DT 03-APR-2013, integrated into UniProtKB/TrEMBL. DT 03-APR-2013, sequence version 1. DT 07-JUN-2017, entry version 25. DE SubName: Full=Uncharacterized protein {ECO:0000313|EnsemblPlants:PGSC0003DMT400055209}; OS Solanum tuberosum (Potato). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae; OC Pentapetalae; asterids; lamiids; Solanales; Solanaceae; Solanoideae; OC Solaneae; Solanum. OX NCBI_TaxID=4113 {ECO:0000313|EnsemblPlants:PGSC0003DMT400055209, ECO:0000313|Proteomes:UP000011115}; RN [1] {ECO:0000313|EnsemblPlants:PGSC0003DMT400055209} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. DM1-3 516 R44 RC {ECO:0000313|EnsemblPlants:PGSC0003DMT400055209}; RX PubMed=21743474; DOI=10.1038/nature10158; RG The Potato Genome Sequencing Consortium; RT "Genome sequence and analysis of the tuber crop potato."; RL Nature 475:189-195(2011). RN [2] {ECO:0000313|EnsemblPlants:PGSC0003DMT400055209} RP IDENTIFICATION. RC STRAIN=DM1-3 516 R44 {ECO:0000313|EnsemblPlants:PGSC0003DMT400055209}; RG EnsemblPlants; RL Submitted (JUN-2015) to UniProtKB. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR RefSeq; XP_006363799.1; XM_006363737.2. DR STRING; 4113.PGSC0003DMT400055209; -. DR EnsemblPlants; PGSC0003DMT400055209; PGSC0003DMT400055209; PGSC0003DMG400021428. DR GeneID; 102584148; -. DR Gramene; PGSC0003DMT400055209; PGSC0003DMT400055209; PGSC0003DMG400021428. DR eggNOG; KOG0410; Eukaryota. DR eggNOG; COG2262; LUCA. DR InParanoid; M1BXJ8; -. DR OMA; CNEDEVP; -. DR OrthoDB; EOG09360975; -. DR Proteomes; UP000011115; Unassembled WGS sequence. DR ExpressionAtlas; M1BXJ8; baseline. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR CDD; cd01878; HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000011115}; KW Reference proteome {ECO:0000313|Proteomes:UP000011115}. FT DOMAIN 320 588 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 613 AA; 68051 MW; 004485BEF4A2596B CRC64; MFRTISHLRS SLTSKICLPQ ALRHFSQFSI SLLPTPTQSI QLPVNPSPST QLSLFHSLSS PCSSLLLQKH QDGSGDDFNT DPKSPPRLFV VQPRFRPDSV LKPKLNEALN LANSLEEQRD GFYDTEFLDK QMPHHLVVQN PASRSIRADT FFGPGTVDTV KCHVNSLDTQ EGIDAIFVNA ILTGIQQRNL ERDWGKPVLD RVGLIIEIFN AHAQTKEAKL QAEFAALMYK KSRLVRVRGP GGRYGFGVGG EAEVVSARGR GSGGRGFISG AGETELQLQR RRILERKNQL LSEIKEVRRT RSLQRAARKR HGGSDGQEIP TVAVVGYTNA GKSTLVSAVS ESFLYCDDRL FATVDPKLRS VILPSGRKVL LSDTVGFISE LPIQLVEAFH ATLEEVVEAD LLVHVLDSSA PNLNEQREAV LQVLGQIGVS EQKLQNMIEV WNKIDLREDF VGDGYCNEDE VPSGSEENND VASNKLCEED LLDYDDNEDE DFEQSGKLGE VIDDQQGNYS DELVSGDEQD SWIDCNGSLV GCGSAEVQQN DPSNKWEVVS SENQFGSESA PHVKTSALTG VGLQELLELL DEKLKPQKTI EKDIFDRKWR RPRTEDTRIA VEQ // ID M1E5Z1_9FIRM Unreviewed; 418 AA. AC M1E5Z1; DT 01-MAY-2013, integrated into UniProtKB/TrEMBL. DT 01-MAY-2013, sequence version 1. DT 05-JUL-2017, entry version 34. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=Thena_0937 {ECO:0000313|EMBL:AEE14566.1}; OS Thermodesulfobium narugense DSM 14796. OC Bacteria; Firmicutes; Clostridia; Thermoanaerobacterales; OC Thermodesulfobiaceae; Thermodesulfobium. OX NCBI_TaxID=747365 {ECO:0000313|EMBL:AEE14566.1, ECO:0000313|Proteomes:UP000011765}; RN [1] {ECO:0000313|EMBL:AEE14566.1, ECO:0000313|Proteomes:UP000011765} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 14796 {ECO:0000313|EMBL:AEE14566.1, RC ECO:0000313|Proteomes:UP000011765}; RG US DOE Joint Genome Institute (JGI-PGF); RA Lucas S., Han J., Lapidus A., Bruce D., Goodwin L., Pitluck S., RA Peters L., Kyrpides N., Mavromatis K., Pagani I., Ivanova N., RA Ovchinnikova G., Zhang X., Saunders L., Detter J.C., Tapia R., Han C., RA Land M., Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P., RA Woyke T., Wu D., Spring S., Schroeder M., Brambilla E., Klenk H.-P., RA Eisen J.A.; RT "The complete genome of Thermodesulfobium narugense DSM 14796."; RL Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002690; AEE14566.1; -; Genomic_DNA. DR STRING; 747365.Thena_0937; -. DR EnsemblBacteria; AEE14566; AEE14566; Thena_0937. DR KEGG; tnr:Thena_0937; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR KO; K03665; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000011765; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000011765}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000011765}. FT DOMAIN 196 364 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 162 189 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 418 AA; 47889 MW; BF1B8E159A250DF9 CRC64; MLKSKFKRAL ILETYHSNEN VEYFLDETKA LCLTANFEPV VSILYKLKNK DSTFFIGRGK IEEIKKIILE NEIEAVVIDD EVDPHFFRFL SEFWNVELID KSSLIISIFA KRASTKQGKL QVELARLNYL LSQTSGWGKI LSRLGGGIGT RGPGETKKEI DKRTLSLKIS RLKNEIKLIE KRNKIIKKKR NISNFPNISL VGYTNAGKST LMNVLTNSTV LVRDQLFSTL DTKTAIIKFN DDTKVFLTDT VGFIRKLPHR LIEAFKATLS QISESNFLLH VVDASKPIEI IKQDIKSVNE VLKEINSNDI PSILVFNKID KCTNLTNVHE LAELYKPYCF ISAITGYGID KLLEKIKYFL YPNRIIIKIF LPHEKTKIIN LIKNFSGKIL EKEWSTSGVK IILDIPQDYA DFLNDYII // ID M1FL05_9ALTE Unreviewed; 432 AA. AC M1FL05; DT 01-MAY-2013, integrated into UniProtKB/TrEMBL. DT 01-MAY-2013, sequence version 1. DT 07-JUN-2017, entry version 30. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:AFP31688.1}; GN ORFNames=MRBBS_2752 {ECO:0000313|EMBL:AFP31688.1}; OS Marinobacter sp. BSs20148. OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales; OC Alteromonadaceae; Marinobacter. OX NCBI_TaxID=490759 {ECO:0000313|EMBL:AFP31688.1, ECO:0000313|Proteomes:UP000011757}; RN [1] {ECO:0000313|EMBL:AFP31688.1, ECO:0000313|Proteomes:UP000011757} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BSs20148 {ECO:0000313|EMBL:AFP31688.1}; RX PubMed=23682144; RA Song L., Ren L., Li X., Yu D., Yu Y., Wang X., Liu G.; RT "Complete Genome Sequence of Marinobacter sp. BSs20148."; RL Genome Announc. 1:E00236-13(2013). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP003735; AFP31688.1; -; Genomic_DNA. DR RefSeq; WP_014872036.1; NC_018268.1. DR EnsemblBacteria; AFP31688; AFP31688; MRBBS_2752. DR KEGG; mbs:MRBBS_2752; -. DR PATRIC; fig|490759.3.peg.2732; -. DR KO; K03665; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000011757; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000011757}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000011757}. FT DOMAIN 198 365 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 164 191 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 432 AA; 48344 MW; B5982E46FC40CFAA CRC64; MFERPDVGER AVLVNIDFTA HDGNEDPGEF RELVISAGVE PVDTVTGSRK QPSPRFFVGD GKLEEIRAAV AAAGADVVLF NHSLSPSQER NIERELQCRV LDRTGVILDI FAQRARTHEG KLQVELAQLQ HMSTRLVRGW THLERQKGGI GLRGPGETQL ETDRRLLRER IKSINKRLEK VRRQRDQGRR ARVRADLPTV SLVGYTNAGK STLFNRITSS DVYTADQLFA TLDPTMRRLE LPDIGAVILA DTVGFIRHLP HKLVESFRAT LEETNEAALL LHVIDCHDER RDDNIAQVED VLAEIGADDV PVLQVFNKTD LLDEFVPRVD RNQEGVPVRA WVSAVTGDGL QGLFDAVVER LAQDVVHHFV VLGPADGKFR ALLHEAGSVL SESSRETGET ILEVRLQNRD WHQLLSRAGV REDELVFRAG SE // ID M1LUF6_9PROT Unreviewed; 369 AA. AC M1LUF6; DT 01-MAY-2013, integrated into UniProtKB/TrEMBL. DT 01-MAY-2013, sequence version 1. DT 07-JUN-2017, entry version 36. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=CDSE_0650 {ECO:0000313|EMBL:AGF46939.1}; OS Candidatus Kinetoplastibacterium desouzaii TCC079E. OC Bacteria; Proteobacteria; Betaproteobacteria; Kinetoplastibacterium. OX NCBI_TaxID=1208919 {ECO:0000313|EMBL:AGF46939.1, ECO:0000313|Proteomes:UP000011547}; RN [1] {ECO:0000313|EMBL:AGF46939.1, ECO:0000313|Proteomes:UP000011547} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=TCC079E {ECO:0000313|EMBL:AGF46939.1, RC ECO:0000313|Proteomes:UP000011547}; RX PubMed=23345457; RA Alves J.M., Serrano M.G., Maia da Silva F., Voegtly L.J., RA Matveyev A.V., Teixeira M.M., Camargo E.P., Buck G.A.; RT "Genome evolution and phylogenomic analysis of candidatus RT kinetoplastibacterium, the betaproteobacterial endosymbionts of RT strigomonas and angomonas."; RL Genome Biol. Evol. 5:338-350(2013). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP003803; AGF46939.1; -; Genomic_DNA. DR RefSeq; WP_015396350.1; NC_020294.1. DR EnsemblBacteria; AGF46939; AGF46939; CDSE_0650. DR KEGG; kde:CDSE_0650; -. DR PATRIC; fig|1208919.3.peg.377; -. DR KO; K03665; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000011547; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000011547}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000011547}. FT DOMAIN 192 359 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 369 AA; 41977 MW; CFD14365AF1FE30D CRC64; MKSLIIGVNL NNNIFFNENL KEFFMLAESA GAVVSEYIVV KRDKPDKKYF IGKGKVEEIS TILLTNNSIE VVLFDQPLSP SQQRNLESIW KVRVVDRISL ILDIFALRAK SHEGKLQVEL AQLEYLSTRL TRMWTHLERQ RGGIGMRGPG ESQLEMDRRI INDKVKILKD RIKKLRLRRD SQRSLREKNR AFSVSLVGYT NSGKSTLFNI LAKENTYVAD QLFATLDTTS RNIWINNSIN KNIVLSDTVG FIRDLPHSLI DSFHATLYEA SSADLLLHVV DVFNENYHEQ IANVNSVIKE IGASNIPTIM VYNKIDLSNL QPRVEYDSDG LISSVFLSAA KNAGIDYLRN AIAKISNTVR QNVENFKNI // ID M1LYD5_9PROT Unreviewed; 362 AA. AC M1LYD5; DT 01-MAY-2013, integrated into UniProtKB/TrEMBL. DT 01-MAY-2013, sequence version 1. DT 07-JUN-2017, entry version 31. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=ST1E_0725 {ECO:0000313|EMBL:AGF49091.1}; OS Candidatus Kinetoplastibacterium galatii TCC219. OC Bacteria; Proteobacteria; Betaproteobacteria; Kinetoplastibacterium. OX NCBI_TaxID=1208921 {ECO:0000313|EMBL:AGF49091.1, ECO:0000313|Proteomes:UP000011658}; RN [1] {ECO:0000313|EMBL:AGF49091.1, ECO:0000313|Proteomes:UP000011658} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=TCC219 {ECO:0000313|EMBL:AGF49091.1}; RX PubMed=23345457; RA Alves J.M., Serrano M.G., Maia da Silva F., Voegtly L.J., RA Matveyev A.V., Teixeira M.M., Camargo E.P., Buck G.A.; RT "Genome evolution and phylogenomic analysis of candidatus RT kinetoplastibacterium, the betaproteobacterial endosymbionts of RT strigomonas and angomonas."; RL Genome Biol. Evol. 5:338-350(2013). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP003806; AGF49091.1; -; Genomic_DNA. DR RefSeq; WP_015389575.1; NC_020284.1. DR EnsemblBacteria; AGF49091; AGF49091; ST1E_0725. DR KEGG; kga:ST1E_0725; -. DR PATRIC; fig|1208921.3.peg.375; -. DR KO; K03665; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000011658; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000011658}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000011658}. FT DOMAIN 190 362 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 362 AA; 40630 MW; A19790296A932528 CRC64; MRALVIGVNL NNNNFQYDIE EFNMLAQSAG ADIVHVELFK RDVPDNKFFI GSGKVQEILS LISDLSVEIV LFDHALSPSQ QRNLEKIWGI RVVDRVSLIL DIFALRAKSH EGKLQVELAQ LQHLSTRLTR LWTHLERQRG GIGMRGPGES QLEMDRRIIG SKVKILKERI KKIKSRRFSQ KGLRERNGAF SVSLIGYTNS GKSTIFNVLA KDKVYVANQL FATLDITSRR IWVGNNVNKD IILSDTVGFI RDLPHSIVEA FHATLEETAS ADLLLHVVDS SSKDMYDQIE NVNKVIKEIG ASNIPTVLVY NKIDKSEIAS KILYDNCTGL AAKVFISAVS LDGMDLLRNV ISDASRVMRN NV // ID M1N454_9CLOT Unreviewed; 596 AA. AC M1N454; DT 01-MAY-2013, integrated into UniProtKB/TrEMBL. DT 01-MAY-2013, sequence version 1. DT 07-JUN-2017, entry version 33. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:AGF58227.1}; GN ORFNames=Cspa_c44740 {ECO:0000313|EMBL:AGF58227.1}; OS Clostridium saccharoperbutylacetonicum N1-4(HMT). OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=931276 {ECO:0000313|EMBL:AGF58227.1, ECO:0000313|Proteomes:UP000011728}; RN [1] {ECO:0000313|EMBL:AGF58227.1, ECO:0000313|Proteomes:UP000011728} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=N1-4(HMT) {ECO:0000313|Proteomes:UP000011728}; RA Poehlein A., Daniel R.; RT "Genome sequence of Clostridium saccharoperbutylacetonicum N1- RT 4(HMT)."; RL Submitted (FEB-2013) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP004121; AGF58227.1; -; Genomic_DNA. DR RefSeq; WP_015394538.1; NZ_AOIF01000032.1. DR EnsemblBacteria; AGF58227; AGF58227; Cspa_c44740. DR KEGG; csr:Cspa_c44740; -. DR PATRIC; fig|931276.5.peg.4510; -. DR KO; K03665; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000011728; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000011728}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000011728}. FT DOMAIN 364 541 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 596 AA; 67152 MW; 4666742E02865280 CRC64; MIFGNIEGIK KSIIDELESI YSIRNLKDEV CNEEILYIIS RSSSLIEREV SVGINRKGNV TSVAIGDSTS VEVPLIDIEE KRLSGIRVIH THPNGYCNLS ALDLTALLKL KLDAIVSVAI VDGKIIDFSL GMLSLFNNKL EAEEKSNLSL EEIKTIHILD KIRFIENLIK TNDVIEDTEE KAILVGSDTK ESLEELEELT EACNIPVLKT VFQSRNKIDA AFFIGRGKVL EIASMRQVER ANVIIFDDEL SGSQVRNLEA ALGAKVIDRT TLILEIFATR AKTKEAKIQV ELAQLKYRMS RLQGLGTVLS RTGGGIGTRG PGEKKLETDR RHIMETVYNL KDELKKIKKT RDIQREKRNK ENIPKVSLVG YTNAGKSTLR NALCDLAAKK ENVTKDKVFE ANMLFATLDT TTRAITLSKK GVVTLTDTVG FVRKLPHELV EAFKSTLEEV IYSDLLCHVI DVASDSALDQ YKAVNEVLNE LGAIDKETIF VLNKIDKASE EQIKAIKEEI GEGEIIEISA REKINLEELL NLIEEKVPYN YRKIEYLIPY DKSDVQSYLH RNARVLEEEY KENGTFMIAE VDDEVYNKTV EYMTKE // ID M1NT81_9CORY Unreviewed; 517 AA. AC M1NT81; DT 01-MAY-2013, integrated into UniProtKB/TrEMBL. DT 01-MAY-2013, sequence version 1. DT 07-JUN-2017, entry version 33. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=A605_08400 {ECO:0000313|EMBL:AGF72682.1}; OS Corynebacterium halotolerans YIM 70093 = DSM 44683. OC Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae; OC Corynebacterium. OX NCBI_TaxID=1121362 {ECO:0000313|EMBL:AGF72682.1, ECO:0000313|Proteomes:UP000011723}; RN [1] {ECO:0000313|EMBL:AGF72682.1, ECO:0000313|Proteomes:UP000011723} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=YIM 70093 {ECO:0000313|EMBL:AGF72682.1}; RX PubMed=23408721; RA Ruckert C., Albersmeier A., Al-Dilaimi A., Niehaus K., RA Szczepanowski R., Kalinowski J.; RT "Genome sequence of the halotolerant bacterium Corynebacterium RT halotolerans type strain YIM 70093(T) (= DSM 44683(T))."; RL Stand. Genomic Sci. 7:284-293(2012). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP003697; AGF72682.1; -; Genomic_DNA. DR RefSeq; WP_015401101.1; NZ_JIAJ01000001.1. DR EnsemblBacteria; AGF72682; AGF72682; A605_08400. DR KEGG; chn:A605_08400; -. DR PATRIC; fig|1121362.3.peg.1696; -. DR KO; K03665; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000011723; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000011723}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000011723}. FT DOMAIN 285 456 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 244 271 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 517 AA; 56563 MW; 5CFC460ECC82CA6F CRC64; MTNSHDTDRN NRPADSSHDE LLARAFRDNR PQPRPQEDPG EDQSGLLAPT VGELDLAERN AFRRVTRETT IRSEDITEVE YRKLRLEQVI LVGVWTEGTT AEIEANMAEL AALAETAGAE VLEMLYQKRD KPDPGTYIGS GKVDQLRDII AATGADTVVC DGELAPGQLV ALENALNTKV IDRTMLILDI FAQHAKSKEG KAQVSLAQME YLITRVRGWG GNLSRQAGGR AGSNGGVGLR GPGETKIEAD RRRLRADMAK LRRELAGMKT SREIKRHRRQ SSTTPQIAIA GYTNAGKSSL INAMTGAGVL VEDALFATLD PTTRRATLAD GRAVVFTDTV GFVRHLPTQL VEAFKSTLEE VLAADLMLHV VDGSDPFPLR QIEAVNKVVY DIVRETGEEA PPEIIVVNKI DAADPLVLAE LRHVLDRDDV VFVSAKTGEG VPELEARIEL FLNSLDAHVT VLIPFTRGDL VSRIHESGTV RSEEYTSEGT LIDVRLPRSL AGELTEFIVE PETGSRN // ID M1PKJ7_DESSD Unreviewed; 545 AA. AC M1PKJ7; DT 01-MAY-2013, integrated into UniProtKB/TrEMBL. DT 01-MAY-2013, sequence version 1. DT 07-JUN-2017, entry version 33. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=UWK_03514 {ECO:0000313|EMBL:AGF80030.1}; OS Desulfocapsa sulfexigens (strain DSM 10523 / SB164P1). OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfobacterales; OC Desulfobulbaceae; Desulfocapsa. OX NCBI_TaxID=1167006 {ECO:0000313|EMBL:AGF80030.1, ECO:0000313|Proteomes:UP000011721}; RN [1] {ECO:0000313|Proteomes:UP000011721} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 10523 / SB164P1 {ECO:0000313|Proteomes:UP000011721}; RX DOI=10.4056/sigs.3777412; RA Finster K.W., Kjeldsen K.U., Kube M., Reinhardt R., Mussmann M., RA Amann R., Schreiber L.; RT "Complete genome sequence of Desulfocapsa sulfexigens, a marine RT deltaproteobacterium specialized in disproportionating inorganic RT sulfur compounds."; RL Stand. Genomic Sci. 8:0-0(2013). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP003985; AGF80030.1; -; Genomic_DNA. DR RefSeq; WP_015405712.1; NC_020304.1. DR EnsemblBacteria; AGF80030; AGF80030; UWK_03514. DR KEGG; dsf:UWK_03514; -. DR PATRIC; fig|1167006.5.peg.3778; -. DR KO; K03665; -. DR OMA; EREVIIT; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000011721; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000011721}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000011721}. FT DOMAIN 379 479 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 338 365 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 545 AA; 61705 MW; A204F73FC9B3F41F CRC64; MAIALVSGNT SGLKTNQLKQ LERLGGKRSG RDDIIGPEMA RSLCQLSFEL NRQIGLLLQR SGKVEAVVVG DFKGIMIPQL SHIRSRGRLK GLRLVHTHLA REDISDEDLM DLLFLRLDML SVIKVASDGL PERLYSVHLL PDSREGKNWA FLPPVHPANQ KDSFEEFIHA LEGEFTRKTS SEEVESGQDR AILVSVSNLS KIRAEESMRE LSELSRSDNV VVLERVLQQR RKINPRFILG KGKLADIMIQ ALQLNANLLI FDQELNPSQI RSITDYTELR VIDRTQLILD IFAHRALSRE GKLQVEMAQL KYMLPRLSSR DDALSRLTGG IGARGPGETK LEIDRRRIND RLARLAKELK TVSRERYRRR SRRRKKDLPV LSLVGYTNAG KSTLLNTLTQ SNIVAEDKLF ATLDPTSRRL RFPRDMEVVI TDTVGFIRQL PAELLQAFKA TLEELEEADL LVHVIDLSNP CFREQMKVVD DLLQELDLNT IPCLKLFNKA DQVENDEMLL ADVAREGVVV SALQIETLTP FLEKAQGMMG KILQD // ID M1VMM0_CYAM1 Unreviewed; 578 AA. AC M1VMM0; DT 01-MAY-2013, integrated into UniProtKB/TrEMBL. DT 01-MAY-2013, sequence version 1. DT 05-JUL-2017, entry version 27. DE SubName: Full=GTP binding protein HflX {ECO:0000313|EMBL:BAM83323.1}; GN ORFNames=CYME_CMT373C {ECO:0000313|EMBL:BAM83323.1}; OS Cyanidioschyzon merolae (strain 10D) (Red alga). OC Eukaryota; Rhodophyta; Bangiophyceae; Cyanidiales; Cyanidiaceae; OC Cyanidioschyzon. OX NCBI_TaxID=280699 {ECO:0000313|EMBL:BAM83323.1, ECO:0000313|Proteomes:UP000007014}; RN [1] {ECO:0000313|EMBL:BAM83323.1, ECO:0000313|Proteomes:UP000007014} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=10D {ECO:0000313|EMBL:BAM83323.1, RC ECO:0000313|Proteomes:UP000007014}; RX PubMed=15071595; DOI=10.1038/nature02398; RA Matsuzaki M., Misumi O., Shin-i T., Maruyama S., Takahara M., RA Miyagishima S., Mori T., Nishida K., Yagisawa F., Nishida K., RA Yoshida Y., Nishimura Y., Nakao S., Kobayashi T., Momoyama Y., RA Higashiyama T., Minoda A., Sano M., Nomoto H., Oishi K., Hayashi H., RA Ohta F., Nishizaka S., Haga S., Miura S., Morishita T., Kabeya Y., RA Terasawa K., Suzuki Y., Ishii Y., Asakawa S., Takano H., Ohta N., RA Kuroiwa H., Tanaka K., Shimizu N., Sugano S., Sato N., Nozaki H., RA Ogasawara N., Kohara Y., Kuroiwa T.; RT "Genome sequence of the ultrasmall unicellular red alga RT Cyanidioschyzon merolae 10D."; RL Nature 428:653-657(2004). RN [2] {ECO:0000313|EMBL:BAM83323.1, ECO:0000313|Proteomes:UP000007014} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=10D {ECO:0000313|EMBL:BAM83323.1, RC ECO:0000313|Proteomes:UP000007014}; RX PubMed=17623057; DOI=10.1186/1741-7007-5-28; RA Nozaki H., Takano H., Misumi O., Terasawa K., Matsuzaki M., RA Maruyama S., Nishida K., Yagisawa F., Yoshida Y., Fujiwara T., RA Takio S., Tamura K., Chung S.J., Nakamura S., Kuroiwa H., Tanaka K., RA Sato N., Kuroiwa T.; RT "A 100%-complete sequence reveals unusually simple genomic features in RT the hot-spring red alga Cyanidioschyzon merolae."; RL BMC Biol. 5:28-28(2007). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AP006502; BAM83323.1; -; Genomic_DNA. DR RefSeq; XP_005539359.1; XM_005539302.1. DR STRING; 45157.CMT373CT; -. DR EnsemblPlants; CMT373CT; CMT373CT; CMT373C. DR GeneID; 16998132; -. DR Gramene; CMT373CT; CMT373CT; CMT373C. DR KEGG; cme:CYME_CMT373C; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR Proteomes; UP000007014; Chromosome 20. DR GO; GO:0009507; C:chloroplast; IEA:EnsemblPlants. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000007014}; KW Reference proteome {ECO:0000313|Proteomes:UP000007014}. FT DOMAIN 283 457 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 249 276 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 578 AA; 64582 MW; 8090F06B765FABDE CRC64; MFIGTWLWRG GVTGTSYRCS LEPRGHCYAW APRLPGPRQR AASLAPAIWC CQQNEEQYAE RRMEPAWRAR LRYVPPTRCF LVGAELKSAR LGGAASTRIT LEQSLDELAE LCSTAGMEVM GRTVQKLTEF QSRTLIGSGK VLQVRAMMQS VGATACVFDE QLSPSQQRAL EEAFGGERSG IQVLDRTAVI LDIFAQHAMS REGALQIELA LLQYRLPRLT RMWQHLERQS GGLGVAFRGP GETQIEVDRR IIAQRIARLR RELEGIRQQR QQRRRQRAAQ HLPSLVLTGY TSSGKSTLLN ALTHARVFAD PMLFCTLDPT TRRAEIPGLN VAPEVLITDS VGFIQKLPTE LIAAFRATLE VVVDADIILH VIDRSSPSWR AQAAVVEDTL SELGVLRSKP RIVIWNKMDL IEHATSVRHQ AAILSRQDPP VVPLSALTGE GLDDLMECIS DTLRDMYIPV ECLIPYTEAA LASEALSHGL CDHQDYTPHG IYLSIRVPRR LANQLQKYKI PDAFERSVST GADTDFVRYR GKLRGAGGIL CPGDSETEGH HGDLAERSRE GPYDDSDWRR LARGRHRL // ID M1WKX4_DESPC Unreviewed; 511 AA. AC M1WKX4; DT 01-MAY-2013, integrated into UniProtKB/TrEMBL. DT 01-MAY-2013, sequence version 1. DT 07-JUN-2017, entry version 31. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=BN4_20289 {ECO:0000313|EMBL:CCH50351.1}; OS Desulfovibrio piezophilus (strain DSM 21447 / JCM 15486 / C1TLV30). OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfovibrionales; OC Desulfovibrionaceae; Desulfovibrio. OX NCBI_TaxID=1322246 {ECO:0000313|EMBL:CCH50351.1, ECO:0000313|Proteomes:UP000011724}; RN [1] {ECO:0000313|EMBL:CCH50351.1, ECO:0000313|Proteomes:UP000011724} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 10523 / SB164P1 {ECO:0000313|Proteomes:UP000011724}; RX PubMed=23383081; DOI=10.1371/journal.pone.0055130; RA Pradel N., Ji B., Gimenez G., Talla E., Lenoble P., Garel M., RA Tamburini C., Fourquet P., Lebrun R., Bertin P., Denis Y., RA Pophillat M., Barbe V., Ollivier B., Dolla A.; RT "The First Genomic and Proteomic Characterization of a Deep-Sea RT Sulfate Reducer: Insights into the Piezophilic Lifestyle of RT Desulfovibrio piezophilus."; RL PLoS ONE 8:e55130-e55130(2013). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; FO203427; CCH50351.1; -; Genomic_DNA. DR RefSeq; WP_015416393.1; NC_020409.1. DR EnsemblBacteria; CCH50351; CCH50351; BN4_20289. DR KEGG; dpi:BN4_20289; -. DR PATRIC; fig|879567.3.peg.3373; -. DR KO; K03665; -. DR OMA; EREVIIT; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000011724; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000011724}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000011724}. FT DOMAIN 349 511 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 308 342 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 511 AA; 57444 MW; D9E35A0EDF69EA24 CRC64; MNGNYTNEQA RELAELTTDI GRQLGLIVDR QGKVVLVLVG DNRSIYIPEL PRTRMASGRL RGLRLLHTHL GEETLSQEDL MDMVFLRLDS VTAINVVEGF PETAQAAHLL PPNPDEKSYE IFSPVRWDRM ELDLGQIVEA LEDEFSRQLD ARDIGTEENR VLLVSVDKTS RPVQELSLEE LAELADTAGL KAAGTMIQRV RKQNPKFIMG KGKLAELEVK ALQANASVII FDQELSPTQI RNLAEITERK ILDRTQLILD IFAQHATSAS GKLQVEMAQL KYTLPRLVGK NRAMSRLMGG IGGRGPGETK LEIDRRRANE RLTRLKNELK QVRKRRTQTR ERRAKAGLPI VSLVGYTNAG KSTLLNTLTQ SKVLAEDKLF ATLDPTSRRI RFPQEREVVL TDTVGFIRRL PPDLKEAFRA TLEELESADL LVLVCDASHP EVEEQVEAVR AILREMDLDE IPAILVLNKW DQLDEDSRET MQNVFPEGIP AVAVDRPTLE PVVNAILERL G // ID M1X4M8_9NOST Unreviewed; 529 AA. AC M1X4M8; DT 01-MAY-2013, integrated into UniProtKB/TrEMBL. DT 01-MAY-2013, sequence version 1. DT 05-JUL-2017, entry version 30. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=RINTHH_2660 {ECO:0000313|EMBL:CCH66421.1}; OS Richelia intracellularis HH01. OC Bacteria; Cyanobacteria; Nostocales; Nostocaceae; Richelia. OX NCBI_TaxID=1165094 {ECO:0000313|EMBL:CCH66421.1, ECO:0000313|Proteomes:UP000053051}; RN [1] {ECO:0000313|EMBL:CCH66421.1, ECO:0000313|Proteomes:UP000053051} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=HH01 {ECO:0000313|EMBL:CCH66421.1, RC ECO:0000313|Proteomes:UP000053051}; RA Hilton J.; RL Submitted (MAY-2012) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Proteomes:UP000053051} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=HH01 {ECO:0000313|Proteomes:UP000053051}; RA Hilton J.A., Foster R.A., Tripp H.J., Carter B.J., Zehr J.P., RA Villareal T.A.; RT "Diatom-associated endosymboitic cyanobacterium lacks core nitrogen RT metabolism enzymes."; RL Submitted (JAN-2016) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:CCH66421.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CAIY01000012; CCH66421.1; -; Genomic_DNA. DR EnsemblBacteria; CCH66421; CCH66421; RINTHH_2660. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000053051; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000053051}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000053051}. FT DOMAIN 356 529 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 315 349 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 529 AA; 58353 MW; DE91A904F5F553CD CRC64; MCVYLNRRGQ VIRVGVGSLK QTQIPLQELP RYGAGRLSGI RCITTHMKSE FPNDIVINVM ALQRLDVLVV LSLTKSGFTR RGGGATGYVK ETYLAHLIPQ DAHALITSSY SLQAGTSNIP YPNWSLSPAM SLDVMGKQDF ISLVEGLEAE FRREFTAQEV NNNERVIIVG VMTGRISNHS FEDTLAELAR LVDTAGGYVL HTMWQKRSLI HPQTVVGEGK VNEIALTAQT LGANLVVFDR DLSPAQVRNL EARIGLRVVD RTEIILDIFA QRAQSGAGKL QVELAQLEYI LPRLAGRGEA MSRLGGGIGT RGPGETKLET ERRAIKRRIA RLQGEVNQLQ AHRARLRQRR QHHEVPSVAL VGYTNSGKST LLNTLTNAET YTADQLFATL DPTTRRLSVP HPDRIQTQEI LITDTVGFIH ELPPSLMDAF RATLEEVTEA EALLHLVDLS HPAWLSHIRA VRDILAQMPI TPGPALVAFN KIDCVDSSTL IQAQEEFPLA VFISASEHLG LETLSQGLGQ LVNYALMPR // ID M1Y3C5_NATM8 Unreviewed; 435 AA. AC M1Y3C5; DT 01-MAY-2013, integrated into UniProtKB/TrEMBL. DT 01-MAY-2013, sequence version 1. DT 07-JUN-2017, entry version 31. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:CCQ37013.1}; GN OrderedLocusNames=Nmlp_2863 {ECO:0000313|EMBL:CCQ37013.1}; OS Natronomonas moolapensis (strain DSM 18674 / JCM 14361 / 8.8.11). OC Archaea; Euryarchaeota; Halobacteria; Halobacteriales; Haloarculaceae; OC Natronomonas. OX NCBI_TaxID=268739 {ECO:0000313|EMBL:CCQ37013.1, ECO:0000313|Proteomes:UP000011867}; RN [1] {ECO:0000313|EMBL:CCQ37013.1, ECO:0000313|Proteomes:UP000011867} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 18674 / JCM 14361 / 8.8.11 RC {ECO:0000313|Proteomes:UP000011867}; RX PubMed=23516216; DOI=10.1128/genomeA.00095-13; RA Dyall-Smith M.L., Pfeiffer F., Oberwinkler T., Klee K., Rampp M., RA Palm P., Gross K., Schuster S.C., Oesterhelt D.; RT "Genome of the haloarchaeon Natronomonas moolapensis, a neutrophilic RT member of a previously haloalkaliphilic genus."; RL Genome Announc. 1:e0009513-e0009513(2013). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; HF582854; CCQ37013.1; -; Genomic_DNA. DR RefSeq; WP_015409777.1; NC_020388.1. DR EnsemblBacteria; CCQ37013; CCQ37013; Nmlp_2863. DR GeneID; 14652775; -. DR KEGG; nmo:Nmlp_2863; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG093Z07D6; -. DR Proteomes; UP000011867; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000011867}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000011867}. FT DOMAIN 191 374 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 107 134 {ECO:0000256|SAM:Coils}. FT COILED 157 187 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 435 AA; 48543 MW; C5E0B65E77732E09 CRC64; MTGTNGRAVV AKRVDDGHPD TEEIRDLARA AGYTVVGEVT QARTEDPALC LGEGKVAELA ALVAETDATT VVFDNRLGPY QTYNLGNELP EGIEVIDRFK LILDIFGQRA RTKKAQLQVE LAELRYELPR AEAKASLAKR DERPGFMGLG EYDESRERDI KAQISRIDDE LDRIERTEAH RREQRRESGF DLVALAGYTN AGKSTLLRRL ASDLDIDENE GLHPDLDATA ESENRLFTTL GTTTRRAEFD RRDVLVTDTV GFISDLPHWL VESFRSTLSE VYRADLVLLV VDASDPIEEI REKLVTCHDT LYERNEAPIV TVLNKADLVD DGELAEKRDA LSALAEDPVV VSAKAGANVD DLRARIDEEL PAWRRERLVV PMTEETMSLV SWVHDHAHVE SVDYADDVTV EFEARPAIIE KARSKAGELP TPALE // ID M1YXY9_NITG3 Unreviewed; 428 AA. AC M1YXY9; DT 01-MAY-2013, integrated into UniProtKB/TrEMBL. DT 01-MAY-2013, sequence version 1. DT 07-JUN-2017, entry version 30. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:CCQ90357.1}; GN ORFNames=NITGR_280073 {ECO:0000313|EMBL:CCQ90357.1}; OS Nitrospina gracilis (strain 3/211). OC Bacteria; Nitrospinae/Tectomicrobia group; Nitrospinae; Nitrospinia; OC Nitrospinales; Nitrospinaceae; Nitrospina. OX NCBI_TaxID=1266370 {ECO:0000313|EMBL:CCQ90357.1, ECO:0000313|Proteomes:UP000011704}; RN [1] {ECO:0000313|EMBL:CCQ90357.1, ECO:0000313|Proteomes:UP000011704} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=3/211 {ECO:0000313|EMBL:CCQ90357.1, RC ECO:0000313|Proteomes:UP000011704}; RX PubMed=23439773; DOI=10.3389/fmicb.2013.00027; RA Luecker S., Nowka B., Rattei T., Spieck E., and Daims H.; RT "The genome of Nitrospina gracilis illuminates the metabolism and RT evolution of the major marine nitrite oxidizer."; RL Front. Microbiol. 4:27-27(2013). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:CCQ90357.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CAQJ01000031; CCQ90357.1; -; Genomic_DNA. DR RefSeq; WP_005007742.1; NZ_HG422173.1. DR EnsemblBacteria; CCQ90357; CCQ90357; NITGR_280073. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000011704; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000011704}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000011704}. FT DOMAIN 206 372 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 428 AA; 49114 MW; F08BE830045973D7 CRC64; MKPVYFDTQK VNNHQPRAIL VGVETNQGTG PPVGDSLDEL SGLATTAHYD PVAHLTQRLS TIHPKTYLGS GKVEELHQAV KHHDAEIVIF DENLSPAQTR NLENLLKCNV VDRSWIILEI FSDHARTSEA KTQVELARLK YSLPRLTRMW GHLSRQRGGI GMRDVGETQI QLDRRMIRDQ ISKLTKKLNR IHKEKQTQRK SRQTTYQVAL VGYTNVGKST LMNCLTGADT LVENKLFATL DATVRKVKKN FPYPILLADT VGLIDKLPHD LVASFKSTLD EVRNADLLVH VIDISHPHYR RQMATAESVL NELGMHDTPT VNVFNKIDRI ENQQDVEEMR RLYPDAVFVS CRKELGLDDL RRAIVHHYEA RLVPYQVELD YTRSDLIPEI RKHALVVDER YHDETMTLDL RIWPHHKARL MELLNGYA // ID M1Z4S5_9FIRM Unreviewed; 430 AA. AC M1Z4S5; DT 01-MAY-2013, integrated into UniProtKB/TrEMBL. DT 01-MAY-2013, sequence version 1. DT 10-MAY-2017, entry version 29. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:CCQ92548.1}; GN ORFNames=CUESP1_1960 {ECO:0000313|EMBL:SHD77319.1}, GN CULT_1000013 {ECO:0000313|EMBL:CCQ92548.1}; OS [Clostridium] ultunense Esp. OC Bacteria; Firmicutes; Tissierellia. OX NCBI_TaxID=1288971 {ECO:0000313|EMBL:CCQ92548.1, ECO:0000313|Proteomes:UP000011752}; RN [1] {ECO:0000313|EMBL:CCQ92548.1, ECO:0000313|Proteomes:UP000011752} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Esp {ECO:0000313|EMBL:CCQ92548.1, RC ECO:0000313|Proteomes:UP000011752}; RX PubMed=23538905; DOI=10.1128/genomeA.00107-13; RA Manzoor S., Muller B., Niazi A., Bongcam-Rudloff E., Schnurer A.; RT "Draft Genome Sequence of Clostridium ultunense Strain Esp, a RT Syntrophic Acetate-Oxidizing Bacterium."; RL Genome Announc. 1:e0010713-e0010713(2013). RN [2] {ECO:0000313|EMBL:SHD77319.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=Clostridium ultunense strain Esp {ECO:0000313|EMBL:SHD77319.1}; RA Jaros S., Januszkiewicz K., Wedrychowicz H.; RL Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CARA01000003; CCQ92548.1; -; Genomic_DNA. DR EMBL; LT669839; SHD77319.1; -; Genomic_DNA. DR EnsemblBacteria; CCQ92548; CCQ92548; CULT_1000013. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000011752; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000011752}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000011752}. FT DOMAIN 200 373 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 159 193 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 430 AA; 49201 MW; 815EE0A1D846D9D4 CRC64; MVETNIKKER TLIAGVELAT DIIDIDNSMD ELKELVKAAG GVVIARVTQR KDRIDPAYFI GRGKALEIKN YCQELEINTV VFNDELSGAQ LRNLEKVIDK KIVDRTNLIL DIFANRATSK EGKLQVKLAQ LKYRLPRLVG FRDYLSREGG GIGTRGPGEQ KLETDRRHIL REINQIEKAL KEAEKTRNIK RKRRKDSNLP IVALVGYTNA GKSTLLNHII RMSEEYDESK KVFVYDMLFA TLDTSLRRGQ LPNGQYFLIT DTVGFVSKLP THLIDAFKGT LEEVRFADLI LHVVDASNED LDIQVQTTVD ILKDLEVLDK PIITVFNKMD KVGVNHLLYD SRYVNKKIFI SSKNGTDLDG LLQLIQDNLP IKYKGVVLLI PYDNQSLVNY FLENYKVNYI EYKEDGTEIG LNINLNDYEK YSTYIVRTFK // ID M2Q3S7_9FIRM Unreviewed; 398 AA. AC M2Q3S7; DT 01-MAY-2013, integrated into UniProtKB/TrEMBL. DT 01-MAY-2013, sequence version 1. DT 07-JUN-2017, entry version 29. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=HMPREF9943_00307 {ECO:0000313|EMBL:EMD17520.1}; OS Eggerthia catenaformis OT 569 = DSM 20559. OC Bacteria; Firmicutes; Erysipelotrichia; Erysipelotrichales; OC Erysipelotrichaceae; Eggerthia. OX NCBI_TaxID=999415 {ECO:0000313|EMBL:EMD17520.1, ECO:0000313|Proteomes:UP000011758}; RN [1] {ECO:0000313|EMBL:EMD17520.1, ECO:0000313|Proteomes:UP000011758} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=OT 569 {ECO:0000313|EMBL:EMD17520.1, RC ECO:0000313|Proteomes:UP000011758}; RG The Broad Institute Genome Sequencing Platform; RA Earl A., Ward D., Feldgarden M., Gevers D., Izard J., Blanton J.M., RA Mathney J., Dewhirst F.E., Young S.K., Zeng Q., Gargeya S., RA Fitzgerald M., Haas B., Abouelleil A., Alvarado L., Arachchi H.M., RA Berlin A., Chapman S.B., Gearin G., Goldberg J., Griggs A., Gujja S., RA Hansen M., Heiman D., Howarth C., Larimer J., Lui A., RA MacDonald P.J.P., McCowen C., Montmayeur A., Murphy C., Neiman D., RA Pearson M., Priest M., Roberts A., Saif S., Shea T., Sisk P., RA Stolte C., Sykes S., Wortman J., Nusbaum C., Birren B.; RT "The Genome Sequence of Lactobacillus catenaformis F0143."; RL Submitted (FEB-2013) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EMD17520.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGEJ01000005; EMD17520.1; -; Genomic_DNA. DR RefSeq; WP_004801409.1; NZ_KB446646.1. DR EnsemblBacteria; EMD17520; EMD17520; HMPREF9943_00307. DR PATRIC; fig|999415.3.peg.307; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000011758; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000011758}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000011758}. FT DOMAIN 185 345 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 398 AA; 46353 MW; BCD221DD2711131A CRC64; MKAILAAVNN RNEDFNILLE ELKGLCKACN IEYTHIMIQN TIPSKAYYLG KGKAYELKEW INDEEIVIFN DELSGLQMRN LRALLDIEVT DRTDLILRIF ASRAHTKEAR LQVEIARLNY ELPRLSGMHQ GIYSQQGGMG FRGAGETQLE LDRRKIHNRI AGCKKELAIL KKERQIQRKQ RKYKDIIALT GYTNSGKSSL MNLYTHKKVE AKDMLFATLQ TSSRKVRIKN RDLIMSDTVG FISHLPTHLI QAFLSTLEEV KEASLILMII DRSSPYVNKH IEVTLDTLNK LGVKDIPILY VYNKEDLESQ DFFVPKEPYV FISVKNKTHM NELEDMIITL LTKDYQRVTL DIPYTNGGLY NELSHKYQII KQEFKDRSIS IVLELDQEDY FKYRQYRI // ID M2SGJ2_9SPHN Unreviewed; 414 AA. AC M2SGJ2; DT 01-MAY-2013, integrated into UniProtKB/TrEMBL. DT 01-MAY-2013, sequence version 1. DT 07-JUN-2017, entry version 29. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=C725_0420 {ECO:0000313|EMBL:EMD84490.1}; OS Pacificimonas flava. OC Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales; OC Sphingomonadaceae; Pacificimonas. OX NCBI_TaxID=1234595 {ECO:0000313|EMBL:EMD84490.1, ECO:0000313|Proteomes:UP000011717}; RN [1] {ECO:0000313|EMBL:EMD84490.1, ECO:0000313|Proteomes:UP000011717} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=JLT2015 {ECO:0000313|EMBL:EMD84490.1, RC ECO:0000313|Proteomes:UP000011717}; RX PubMed=23661488; RA Tang K., Liu K., Li S., Jiao N.; RT "Draft Genome Sequence of Strain JLT2015T, Belonging to the Family RT Sphingomonadaceae of the Alphaproteobacteria."; RL Genome Announc. 1:E00226-13(2013). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EMD84490.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AMRV01000001; EMD84490.1; -; Genomic_DNA. DR EnsemblBacteria; EMD84490; EMD84490; C725_0420. DR PATRIC; fig|1234595.3.peg.419; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000011717; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000011717}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000011717}. FT DOMAIN 190 357 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 156 183 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 414 AA; 45466 MW; 83C56D62A5A03712 CRC64; MLPDLSRSEN SRDPEARLEE AVALSAAISL DVADKDIVRV RAPRPATLFG SGQVEMLTAR AEASDAELIV VDGALSPLQQ RNLEKETGRK VIDRTGLILE IFGERAATHE GRLQVELAHL EYQASRLVRS WTHLERQRGG FGFLGGPGET QIETDRRLIR DRMAKIRREL EQVTRTRTLH RERRQKAPYP IVALVGYTNA GKSTLFNRLT GATVMAKDLL FATLDPTMRS ISIPGFDKVI MSDTVGFVSD LPTQLVAAFR ATLEEVLEAD LIVHVRDVAH PDTDAQAADV MRTLADLGVE PGGDVPILDV LNKIDLLPPD RRDALAGRPD TVAVSALTGE GVEHFLNVLS ARLSPDETVY TFDISAGDGA RLAWLERHGR VLGRRMENDH VHVEVALSAL DHGRFLSLRP GGDG // ID M2WE92_9MICC Unreviewed; 579 AA. AC M2WE92; DT 01-MAY-2013, integrated into UniProtKB/TrEMBL. DT 01-MAY-2013, sequence version 1. DT 07-JUN-2017, entry version 30. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=C884_02449 {ECO:0000313|EMBL:EME36842.1}; OS Kocuria palustris PEL. OC Bacteria; Actinobacteria; Micrococcales; Micrococcaceae; Kocuria. OX NCBI_TaxID=1236550 {ECO:0000313|EMBL:EME36842.1, ECO:0000313|Proteomes:UP000009877}; RN [1] {ECO:0000313|EMBL:EME36842.1, ECO:0000313|Proteomes:UP000009877} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=PEL {ECO:0000313|EMBL:EME36842.1, RC ECO:0000313|Proteomes:UP000009877}; RX PubMed=24504000; RA Sharma G., Khatri I., Subramanian S.; RT "Draft Genome Sequence of Kocuria palustris PEL."; RL Genome Announc. 2:e01261-13(2014). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EME36842.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ANHZ02000008; EME36842.1; -; Genomic_DNA. DR RefSeq; WP_006214509.1; NZ_ANHZ02000008.1. DR EnsemblBacteria; EME36842; EME36842; C884_02449. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000009877; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000009877}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000009877}. FT DOMAIN 322 487 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 579 AA; 62524 MW; EE7D33D0953B4E04 CRC64; MTHIPDSGAE PTGTTPTDQQ LEDVVARVLS RAQQRRDRDD RSAPDDSGSE AGTSQEAAEG APAGGGRRDV LSGRARELAD RSVHTDVDGA QMELSERQSL RRVANLSTEL EDITEVEYRE LRLEKVVLAG LWTTGPASEA ENSLRELAAL AETAGSEVLD GIIQRRTNPD PATYLGSGKA LELKDIVAAT GADTVVVDEE LAPSQRRALE DVVKVKVIDR TGLILDIFAQ HAKSKEGKAQ VELAQLEYML PRLRGWGESL SRQAGGRAAG GEGIGSRGPG ETKIEMDRRR IRARMAKLRR EIAAMKPSRE AKRLNRRRNS VPSVAIAGYT NAGKSSLLNR LTDAGVLVEN ALFATLDPTV RKAETPDGIG YTLSDTVGFV RSLPTQLVEA FRSTLEEVAD SDVIVHVVDA SHPDPEGQIR AVHEVLADID ALDLPEIIAL NKADAADPFV VQRMRNTHRD VVVVSARTGE GIDELKQRIS EAIPRPDHVL DLLVPFTDGD IVSRLHGWDA EILRTEYLGE GTHLLVKVRE DLAGELQRYV WQDAQQFGQG VPGDGTYAAA SDAADAGSAE QAASGAEAR // ID M2XLT4_GALSU Unreviewed; 453 AA. AC M2XLT4; DT 01-MAY-2013, integrated into UniProtKB/TrEMBL. DT 01-MAY-2013, sequence version 1. DT 07-JUN-2017, entry version 22. DE SubName: Full=GTP-binding protein HflX {ECO:0000313|EMBL:EME31152.1}; GN ORFNames=Gasu_16470 {ECO:0000313|EMBL:EME31152.1}; OS Galdieria sulphuraria (Red alga). OC Eukaryota; Rhodophyta; Bangiophyceae; Cyanidiales; Cyanidiaceae; OC Galdieria. OX NCBI_TaxID=130081 {ECO:0000313|EMBL:EME31152.1, ECO:0000313|Proteomes:UP000030680}; RN [1] {ECO:0000313|Proteomes:UP000030680} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=074W {ECO:0000313|Proteomes:UP000030680}; RX PubMed=23471408; DOI=10.1126/science.1231707; RA Schonknecht G., Chen W.H., Ternes C.M., Barbier G.G., Shrestha R.P., RA Stanke M., Brautigam A., Baker B.J., Banfield J.F., Garavito R.M., RA Carr K., Wilkerson C., Rensing S.A., Gagneul D., Dickenson N.E., RA Oesterhelt C., Lercher M.J., Weber A.P.; RT "Gene transfer from bacteria and archaea facilitated evolution of an RT extremophilic eukaryote."; RL Science 339:1207-1210(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; KB454494; EME31152.1; -; Genomic_DNA. DR RefSeq; XP_005707672.1; XM_005707615.1. DR EnsemblPlants; EME31152; EME31152; Gasu_16470. DR GeneID; 17089824; -. DR Gramene; EME31152; EME31152; Gasu_16470. DR KEGG; gsl:Gasu_16470; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR Proteomes; UP000030680; Unassembled WGS sequence. DR GO; GO:0009507; C:chloroplast; IEA:EnsemblPlants. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000030680}; KW Reference proteome {ECO:0000313|Proteomes:UP000030680}. FT DOMAIN 179 349 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 453 AA; 50639 MW; D86A5562C2503C61 CRC64; MSELQELCHT AGLEVLATTY QRLETPNPVT FVGSGKVSEI RSLLVCYECN TVVFDCELSP SQQKNLERKL AKDKQVVNVL DRTALILDIF AQHAKTREGK LQVELALNQY RLPRLTRLWT HLERQSGAGG VGLRGPGETQ IESDRRLLSS RISQLKGELE DVRSHRARQR KKRRQFEVPV VSLVGYTNAG KSTLLNALTN AGVLVQDSLF ATLDPTTRRC RLPGLHVHPD ILMTDTVGFI QKLPTTLVAA FRATLEEIAA ADILLHVVDI SSPSSESQQK AVMEVLREIG AAEKSMITVW NKIDRFQGNT GSIRLKAAQI DKHVAVSAAT GEGLQDLVYI LGETLSSLLV PIEALIPYNR CDLLPRIHQY SILDVEDYRP DGIYILGRST DNVALLLAEY RVTEDQESLY FVPVHSNDKN NIDMRQLEDE KEWKRLAKGR HHQGASGNTT YSL // ID M3BJH1_STRMB Unreviewed; 498 AA. AC M3BJH1; DT 01-MAY-2013, integrated into UniProtKB/TrEMBL. DT 01-MAY-2013, sequence version 1. DT 07-JUN-2017, entry version 30. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=H340_14826 {ECO:0000313|EMBL:EME99734.1}; OS Streptomyces mobaraensis NBRC 13819 = DSM 40847. OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae; OC Streptomyces. OX NCBI_TaxID=1223523 {ECO:0000313|EMBL:EME99734.1, ECO:0000313|Proteomes:UP000011740}; RN [1] {ECO:0000313|EMBL:EME99734.1, ECO:0000313|Proteomes:UP000011740} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 40847 {ECO:0000313|EMBL:EME99734.1, RC ECO:0000313|Proteomes:UP000011740}; RX PubMed=23558536; RA Yang H., He T., Wu W., Zhu W., Lu B., Sun W.; RT "Whole-Genome Shotgun Assembly and Analysis of the Genome of RT Streptomyces mobaraensis DSM 40847, a Strain for Industrial Production RT of Microbial Transglutaminase."; RL Genome Announc. 1:E0014313-E0014313(2013). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EME99734.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AORZ01000041; EME99734.1; -; Genomic_DNA. DR RefSeq; WP_004945346.1; NZ_AORZ01000041.1. DR EnsemblBacteria; EME99734; EME99734; H340_14826. DR PATRIC; fig|1223523.3.peg.3036; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000011740; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 2. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000011740}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000011740}. FT DOMAIN 278 443 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 498 AA; 54450 MW; F5287A90C7F370E0 CRC64; MTSTSSLPQD RQDRQSLPES LRADALMEED VAWSHEIDGE RDGDQYDRSE RAALRRVAGL STELEDVTEV EYRQLRLERV VLVGVWTSGT VRDAENSLAE LAALAETAGA QVLDGVIQRR DKPDPATYIG SGKAQELRDI VLESGADTVV CDGELSPGQL IHLEDVVKVK VVDRTALILD IFAQHAKSRE GKAQVSLAQM QYMLPRLRGW GQSLSRQMGG GGSGSSGGGM ATRGPGETKI ETDRRRIREK MARMRREIAE MKTGRDLKRQ ERRRNKVPSV AIAGYTNAGK SSLLNRLTGA GVLVENSLFA TLDPTVRKAE TPGGRLYTLA DTVGFVRHLP HHLVEAFRST MEEVGDSDLI LHVVDGSHPA PEEQLAAVRE VIRDVGALDV PEIVVVNKAD AADPLVLQRL LRVERNAIAV SARTGEGIDE LLALIDEQLP RPAIEVEALV PYTRGALTAR IHSEGEILSE EHTPEGTLVK ARVHEELAAE LRPFVQAA // ID M3EHL0_9LEPT Unreviewed; 557 AA. AC M3EHL0; DT 01-MAY-2013, integrated into UniProtKB/TrEMBL. DT 01-MAY-2013, sequence version 1. DT 30-AUG-2017, entry version 30. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:EMF80528.1}; GN ORFNames=LEP1GSC188_3733 {ECO:0000313|EMBL:EMF80528.1}; OS Leptospira weilii serovar Topaz str. LT2116. OC Bacteria; Spirochaetes; Leptospirales; Leptospiraceae; Leptospira. OX NCBI_TaxID=1088540 {ECO:0000313|EMBL:EMF80528.1, ECO:0000313|Proteomes:UP000011770}; RN [1] {ECO:0000313|EMBL:EMF80528.1, ECO:0000313|Proteomes:UP000011770} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=LT2116 {ECO:0000313|EMBL:EMF80528.1, RC ECO:0000313|Proteomes:UP000011770}; RA Harkins D.M., Durkin A.S., Brinkac L.M., Haft D.H., Selengut J.D., RA Sanka R., DePew J., Purushe J., Tulsiani S.M., Graham G.C., RA Burns M.-A., Dohnt M.F., Smythe L.D., McKay D.B., Craig S.B., RA Vinetz J.M., Sutton G.G., Nierman W.C., Fouts D.E.; RL Submitted (JAN-2013) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EMF80528.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AHOR02000048; EMF80528.1; -; Genomic_DNA. DR RefSeq; WP_004507895.1; NZ_AHOR02000048.1. DR EnsemblBacteria; EMF80528; EMF80528; LEP1GSC188_3733. DR GeneID; 29807941; -. DR Proteomes; UP000011770; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000011770}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}. FT DOMAIN 350 547 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 316 343 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 557 AA; 63262 MW; E3C0751A376D7D87 CRC64; MVISQDFART LCELSLEIGK QIGILIDRSG YVTHVLVGSD NSIEIPFLDR LRTSEARLRG LRLVHTHLKG EPLNQEDLTD LALLRLDYMT AIVMDSSGNP NGYYSAHLNP ESENELWSVL PKKYPGQLTE GILLEEILEI ESRLSRSKKN LKDAQKENRA FLVGVYPERN VGRHPSLSME ELKELCRTAE VHVVDTFIQR KNRLDPSTVL GKGKLEEIIL KAIQKHVELL VFDLELTPSQ AKKISDIADI KVIDRTQLIL DIFARNAKSK DGKLQVELAQ LKYLKGRLTE LDDNMSRLTG GIGGRGPGET KLEIGKRRVE ERITRLEVEL KSLRKRREIN RRQRKRNELP AVGIVGYTNA GKSTFLNALT NSEVLSENKL FATLDPTTRR IRFPEEREII ISDTVGFIHD LPPELSNAFK ATLEELGDSD LLVHVVDVSN PDYKLQMEAV EKILEELEFS HIPMIQVFNK IDNLEKFKTW KTENDSNGYK VFSHPSVNHD PGLEAIADLK EELGIDVHSD TVLVSAYQGW GLKTFLDLLE ERIYNLSRSN YSIAEKL // ID M3GT27_LEPBO Unreviewed; 493 AA. AC M3GT27; DT 01-MAY-2013, integrated into UniProtKB/TrEMBL. DT 01-MAY-2013, sequence version 1. DT 07-JUN-2017, entry version 30. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:EMF97978.1}; GN ORFNames=LEP1GSC123_1842 {ECO:0000313|EMBL:EMF97978.1}; OS Leptospira borgpetersenii str. 200701203. OC Bacteria; Spirochaetes; Leptospirales; Leptospiraceae; Leptospira. OX NCBI_TaxID=1193007 {ECO:0000313|EMBL:EMF97978.1, ECO:0000313|Proteomes:UP000011783}; RN [1] {ECO:0000313|EMBL:EMF97978.1, ECO:0000313|Proteomes:UP000011783} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=200701203 {ECO:0000313|EMBL:EMF97978.1, RC ECO:0000313|Proteomes:UP000011783}; RA Harkins D.M., Durkin A.S., Brinkac L.M., Haft D.H., Selengut J.D., RA Sanka R., DePew J., Purushe J., Picardeau M., Werts C., Goarant C., RA Vinetz J.M., Sutton G.G., Nierman W.C., Fouts D.E.; RL Submitted (JAN-2013) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EMF97978.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AKWO02000103; EMF97978.1; -; Genomic_DNA. DR EnsemblBacteria; EMF97978; EMF97978; LEP1GSC123_1842. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000011783; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 2. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000011783}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000011783}. FT DOMAIN 286 483 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 252 279 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 493 AA; 55934 MW; F22654259A1F7C2E CRC64; MVHTHLKGES LNQEDLTDLA LLRLDYITAV VMDTSGNPNG YYSAHLNPES DDLWSVLPKK YPGQLTEGIL EEILEIESRL SRSKKNLKDA QKENRAFLVG VYPERSVGRH PSLSMEELKE LCRTAEVHVV DTFIQRKNRL DPSTVLGKGK LEEIILKAIQ KHVELLVFDL ELTPSQAKKI SDIADIKVID RTQLILDIFA RNAKSRDGKL QVELAQLKYL KGRLTELDDN MSRLTGGIGG RGPGETKLEI GKRRVEERIT RLEVELKSLK KRREINRRQR KRNELPAVGI VGYTNAGKST FLNALTNSEV LSENKLFATL DPTTRRIRFP EEREIIISDT VGFIHDLPPE LSNAFKATLE ELGDSDLLVH VVDVSNPDYK LQMEAVEKIL EELELSHIPM IQVFNKIDNF EKFKTWKTES DSNGYKTFSH PSINHGPGLE AIADLKEELG IDVHSDTVLV SAYQGWGLKA FLDLLEEKIY NLPRLNYPIA EKL // ID M3VFR5_9ACTN Unreviewed; 469 AA. AC M3VFR5; DT 01-MAY-2013, integrated into UniProtKB/TrEMBL. DT 01-MAY-2013, sequence version 1. DT 07-JUN-2017, entry version 30. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:GAC80314.1}; GN ORFNames=GM1_016_00750 {ECO:0000313|EMBL:GAC80314.1}; OS Gordonia malaquae NBRC 108250. OC Bacteria; Actinobacteria; Corynebacteriales; Gordoniaceae; Gordonia. OX NCBI_TaxID=1223542 {ECO:0000313|EMBL:GAC80314.1, ECO:0000313|Proteomes:UP000035009}; RN [1] {ECO:0000313|EMBL:GAC80314.1, ECO:0000313|Proteomes:UP000035009} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NBRC 108250 {ECO:0000313|EMBL:GAC80314.1, RC ECO:0000313|Proteomes:UP000035009}; RA Yoshida I., Hosoyama A., Tsuchikane K., Ando Y., Baba S., Ohji S., RA Hamada M., Tamura T., Yamazoe A., Yamazaki S., Fujita N.; RT "Whole genome shotgun sequence of Gordonia malaquae NBRC 108250."; RL Submitted (FEB-2013) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:GAC80314.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BAOP01000016; GAC80314.1; -; Genomic_DNA. DR RefSeq; WP_008379268.1; NZ_BAOP01000016.1. DR EnsemblBacteria; GAC80314; GAC80314; GM1_016_00750. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000035009; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000035009}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000035009}. FT DOMAIN 247 416 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 206 233 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 469 AA; 51143 MW; 63903FFC835F9C95 CRC64; MTETHIDTPE HPTTGELALD DRASLQRVVG LSTELDDVTE VEYRQLRLER VVLVGVWTSG TLAQAEASLA ELAALAETAG SEVLEALFQR RSKPDPATYL GSGKAQEVRE VVLATGADTV VCDGELTPAQ LTALEKVVKV KVIDRTALIL DIFAQHATSR EGKAQVSLAQ MEYMLPRLRG WGESMSRQAG GRAGSNGGVG LRGPGETKIE TDRRRIRERM AKLRKEIRGM KTARTVKRAA RRRGTVPALT VVGYTNAGKS SLVNAMTGAG VLVQDALFAT LDPTTRRAEL ADGHEVVFTD TVGFVRHLPT QLVEAFRSTL EEAVDADLLI HVVDGADPFP DLQISTVRQV LREVLEEEKL PPPPEMLVIN KIDAIDDVRM TTLRAEFPDA VFVSARTGEG LPGLFDRITA FVQRDDVEAD LQVPFARGEV ISRLHQYAHV LSTEHNADGT RLHVRMPSAL AGEFADLIV // ID M3WD23_FELCA Unreviewed; 518 AA. AC M3WD23; DT 01-MAY-2013, integrated into UniProtKB/TrEMBL. DT 01-MAY-2013, sequence version 1. DT 30-AUG-2017, entry version 29. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSFCAP00000009571}; GN Name=LOC101098289 {ECO:0000313|Ensembl:ENSFCAP00000009571}; OS Felis catus (Cat) (Felis silvestris catus). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Carnivora; Feliformia; Felidae; OC Felinae; Felis. OX NCBI_TaxID=9685 {ECO:0000313|Ensembl:ENSFCAP00000009571, ECO:0000313|Proteomes:UP000011712}; RN [1] {ECO:0000313|Ensembl:ENSFCAP00000009571, ECO:0000313|Proteomes:UP000011712} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000009571, RC ECO:0000313|Proteomes:UP000011712}; RX PubMed=17975172; DOI=10.1101/gr.6380007; RA Pontius J.U., Mullikin J.C., Smith D.R., Lindblad-Toh K., Gnerre S., RA Clamp M., Chang J., Stephens R., Neelam B., Volfovsky N., RA Schaffer A.A., Agarwala R., Narfstrom K., Murphy W.J., Giger U., RA Roca A.L., Antunes A., Menotti-Raymond M., Yuhki N., RA Pecon-Slattery J., Johnson W.E., Bourque G., Tesler G., O'Brien S.J.; RT "Initial sequence and comparative analysis of the cat genome."; RL Genome Res. 17:1675-1689(2007). RN [2] {ECO:0000313|Ensembl:ENSFCAP00000009571} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000009571}; RA Hillier L.W., Warren W., Obrien S., Wilson R.K.; RT "Sequence assembly of the Felis catus genome version 6.2."; RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases. RN [3] {ECO:0000313|Ensembl:ENSFCAP00000009571} RP IDENTIFICATION. RC STRAIN=breed Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000009571}; RG Ensembl; RL Submitted (MAR-2013) to UniProtKB. CC -!- CAUTION: The sequence shown here is derived from an Ensembl CC automatic analysis pipeline and should be considered as CC preliminary data. {ECO:0000313|Ensembl:ENSFCAP00000009571}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AANG02064347; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AANG02064348; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR STRING; 9685.ENSFCAP00000009571; -. DR Ensembl; ENSFCAT00000010312; ENSFCAP00000009571; ENSFCAG00000010310. DR eggNOG; KOG0410; Eukaryota. DR eggNOG; COG2262; LUCA. DR GeneTree; ENSGT00390000001397; -. DR InParanoid; M3WD23; -. DR OMA; MDTVGFM; -. DR OrthoDB; EOG091G0852; -. DR Proteomes; UP000011712; Chromosome X. DR Bgee; ENSFCAG00000010310; -. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR GO; GO:0043022; F:ribosome binding; IBA:GO_Central. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000011712}; KW Reference proteome {ECO:0000313|Proteomes:UP000011712}. FT DOMAIN 297 461 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 518 AA; 57206 MW; C07025989B9CCB51 CRC64; LWGSSQASRT KSPVPLRSRI GTGHRAPRPA PPLLFCPERA LATFGPGGLK GRGGRGRGPP ADGPRSRTGE VEEPEDAEDE EEKEEELLRR DPLLPVGTQC VCLVHPEVKW GPGKPQPTRA DRQVAEAESL VHTLDRWSVV ERMVVPARTP DGKVAFGRGT LRHLTEKIRA LPENTSVFLN VERMAPPTKK ELEAAWGVQV FDRFTVVLSI FRCNARTKEA RLQVALAELP LLRSHLSSTT RLDGRGGGSR YIMGSGESLM QVQRHLLKDK ELKIKALDRL RDKRHLLGRQ RRRREFPVVS MVGYTNCGKT TLIKALMGDN TIRPQDRLFA TLDVTAHAGW LPSRVAVIYM DTISFLSQLP HSLIESFSAT LEDVAHSDLV VHVRDVSRPE TELQKASVPA ALRGLRLPAS LLDSVLEVHN KVDLVPGYSP AGSQAVAMSA LLGHRLPELR ARLEDAVLRA TGRQVLTLRV RLAGAQLSWL YQEATVQDVD VIPDAGAANV RVVISSSAYS KFRKLFLE // ID M3WIJ1_FELCA Unreviewed; 407 AA. AC M3WIJ1; DT 01-MAY-2013, integrated into UniProtKB/TrEMBL. DT 01-MAY-2013, sequence version 1. DT 30-AUG-2017, entry version 29. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSFCAP00000012301}; OS Felis catus (Cat) (Felis silvestris catus). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Carnivora; Feliformia; Felidae; OC Felinae; Felis. OX NCBI_TaxID=9685 {ECO:0000313|Ensembl:ENSFCAP00000012301, ECO:0000313|Proteomes:UP000011712}; RN [1] {ECO:0000313|Ensembl:ENSFCAP00000012301, ECO:0000313|Proteomes:UP000011712} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000012301, RC ECO:0000313|Proteomes:UP000011712}; RX PubMed=17975172; DOI=10.1101/gr.6380007; RA Pontius J.U., Mullikin J.C., Smith D.R., Lindblad-Toh K., Gnerre S., RA Clamp M., Chang J., Stephens R., Neelam B., Volfovsky N., RA Schaffer A.A., Agarwala R., Narfstrom K., Murphy W.J., Giger U., RA Roca A.L., Antunes A., Menotti-Raymond M., Yuhki N., RA Pecon-Slattery J., Johnson W.E., Bourque G., Tesler G., O'Brien S.J.; RT "Initial sequence and comparative analysis of the cat genome."; RL Genome Res. 17:1675-1689(2007). RN [2] {ECO:0000313|Ensembl:ENSFCAP00000012301} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000012301}; RA Hillier L.W., Warren W., Obrien S., Wilson R.K.; RT "Sequence assembly of the Felis catus genome version 6.2."; RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases. RN [3] {ECO:0000313|Ensembl:ENSFCAP00000012301} RP IDENTIFICATION. RC STRAIN=breed Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000012301}; RG Ensembl; RL Submitted (MAR-2013) to UniProtKB. CC -!- CAUTION: The sequence shown here is derived from an Ensembl CC automatic analysis pipeline and should be considered as CC preliminary data. {ECO:0000313|Ensembl:ENSFCAP00000012301}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AANG02019667; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR STRING; 9685.ENSFCAP00000012301; -. DR Ensembl; ENSFCAT00000013268; ENSFCAP00000012301; ENSFCAG00000013263. DR eggNOG; KOG0410; Eukaryota. DR eggNOG; COG2262; LUCA. DR GeneTree; ENSGT00390000001397; -. DR InParanoid; M3WIJ1; -. DR OMA; CNARTEE; -. DR OrthoDB; EOG091G0852; -. DR Proteomes; UP000011712; Chromosome X. DR Bgee; ENSFCAG00000013263; -. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR GO; GO:0043022; F:ribosome binding; IBA:GO_Central. DR CDD; cd01878; HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000011712}; KW Reference proteome {ECO:0000313|Proteomes:UP000011712}. FT DOMAIN 182 346 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 407 AA; 44907 MW; B9F118B5A1782F01 CRC64; LPEADRQVAE AESLVHTLDR WSVVERMVVP ARTPDGKVAF GRGTLRHLTE KIRALPEITA VFLNVERMAP PTKKELEAAW GVQVFDRFTV VLSIFRCNAR TKEARLQVAL AELPLLRAHL SSTARLDGRG GGSRYIMGSG ESPVQVQRRL LKDKELNIRK ALDRLREKRR LLGRQRRRRE FPVVSMVGYT NCGKTTLIKA LTGDDAVRPQ DRLFATLDVT AHAGWLPSRV AVIYMDTVGF LSQLPHSLIE SFSATLEDVA HSDLVVHVRD VSHPETELQK ATVLAALRGL RLPAPLLDSV LEVHNKVDLV PGYSPSGSQA VAVSALLGHG LPELRARLED AVLRATGRQV LTLRVRLAGA QLSWLHQEAT VLDVDVIPEA GAADVRVVIS SSAYSKFRKL FPESASQ // ID M3XR21_MUSPF Unreviewed; 466 AA. AC M3XR21; DT 01-MAY-2013, integrated into UniProtKB/TrEMBL. DT 01-MAY-2013, sequence version 1. DT 30-AUG-2017, entry version 22. DE SubName: Full=GTP binding protein 6 (putative) {ECO:0000313|Ensembl:ENSMPUP00000001521}; GN Name=GTPBP6 {ECO:0000313|Ensembl:ENSMPUP00000001521}; OS Mustela putorius furo (European domestic ferret) (Mustela furo). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Carnivora; Caniformia; Mustelidae; OC Mustelinae; Mustela. OX NCBI_TaxID=9669 {ECO:0000313|Ensembl:ENSMPUP00000001521, ECO:0000313|Proteomes:UP000000715}; RN [1] {ECO:0000313|Ensembl:ENSMPUP00000001521} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ID#1420 {ECO:0000313|Ensembl:ENSMPUP00000001521}; RA Di Palma F., Alfoldi J., Johnson J., Jaffe D., Berlin A., Gnerre S., RA Grabherr M., Hall G., Lara M., MacCallum I., Mauceli E., RA Przyblyski D., Ribeiro F., Russell P., Sharpe T., Turner-Maier J., RA Walker B.J., Young S., Birren B., Lindblad-Toh K.; RL Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Ensembl:ENSMPUP00000001521} RP IDENTIFICATION. RG Ensembl; RL Submitted (MAR-2013) to UniProtKB. CC -!- CAUTION: The sequence shown here is derived from an Ensembl CC automatic analysis pipeline and should be considered as CC preliminary data. {ECO:0000313|Ensembl:ENSMPUP00000001521}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AEYP01069594; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AEYP01069595; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AEYP01069596; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR STRING; 9669.ENSMPUP00000001521; -. DR Ensembl; ENSMPUT00000001553; ENSMPUP00000001521; ENSMPUG00000001536. DR eggNOG; KOG0410; Eukaryota. DR eggNOG; COG2262; LUCA. DR GeneTree; ENSGT00390000001397; -. DR InParanoid; M3XR21; -. DR OMA; MDTVGFM; -. DR OrthoDB; EOG091G0852; -. DR Proteomes; UP000000715; Unassembled WGS sequence. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR CDD; cd01878; HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 4: Predicted; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000000715}; KW Reference proteome {ECO:0000313|Proteomes:UP000000715}. FT DOMAIN 245 409 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 207 234 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 466 AA; 51876 MW; C4E052E1CC77BD06 CRC64; MFRGPSGAPC KMRCVLGHGR AWRPPVCCHV PGCRVRRTRP CVLLASSSAS RRLWLEQHRC VVEHMAEWQV AEAEALVHTL DGWSVVESMV VPSKTPDGKL TFGKGTLEHL TERVRGSPEI TAVFLNVERL ATPTKKELEA RWGVPVFDRF TVVLHIFRCN ARTKEARLQV ALAELPLLRS RLKSSTARPD AQGWGSRYIM GSGESFVQVQ QRLLKEKEMK IRKALERLRQ KRRLLGTRRR RQEFPVIAVV GYTNCGKTTL IKALTGDDAV QPRDQLFATL DVTAHAGWLP SRMAVIYMDT IGFLSQLPHS LIESFSATLE DVAHSDLIVH VRDVTHPETE LQKASVLSSL RGLRLPAPLL DSMLEVHNKT DLVPGYSPVE PQAVAVSALR GHGLPELKAR LEDAVLRATG RQVLTLRVRL AGAQLSWLHQ EATVQAVDVI PEAGVADVTV VISKSAYGKF RKLFPE // ID M4ANG5_XIPMA Unreviewed; 368 AA. AC M4ANG5; DT 01-MAY-2013, integrated into UniProtKB/TrEMBL. DT 01-MAY-2013, sequence version 1. DT 30-AUG-2017, entry version 21. DE SubName: Full=GTP binding protein 6 (putative) {ECO:0000313|Ensembl:ENSXMAP00000016010}; OS Xiphophorus maculatus (Southern platyfish) (Platypoecilus maculatus). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata; OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; OC Poeciliinae; Xiphophorus. OX NCBI_TaxID=8083 {ECO:0000313|Ensembl:ENSXMAP00000016010, ECO:0000313|Proteomes:UP000002852}; RN [1] {ECO:0000313|Ensembl:ENSXMAP00000016010} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=JP 163 A {ECO:0000313|Ensembl:ENSXMAP00000016010}; RA Walter R., Schartl M., Warren W.; RL Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Ensembl:ENSXMAP00000016010} RP IDENTIFICATION. RC STRAIN=JP 163 A {ECO:0000313|Ensembl:ENSXMAP00000016010}; RG Ensembl; RL Submitted (MAR-2013) to UniProtKB. CC -!- CAUTION: The sequence shown here is derived from an Ensembl CC automatic analysis pipeline and should be considered as CC preliminary data. {ECO:0000313|Ensembl:ENSXMAP00000016010}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGAJ01016885; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR STRING; 8083.ENSXMAP00000016010; -. DR Ensembl; ENSXMAT00000016034; ENSXMAP00000016010; ENSXMAG00000015980. DR eggNOG; KOG0410; Eukaryota. DR eggNOG; COG2262; LUCA. DR GeneTree; ENSGT00390000001397; -. DR InParanoid; M4ANG5; -. DR OMA; IMHILRE; -. DR OrthoDB; EOG091G0852; -. DR Proteomes; UP000002852; Unassembled WGS sequence. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000002852}; KW Reference proteome {ECO:0000313|Proteomes:UP000002852}. FT DOMAIN 274 354 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 368 AA; 41277 MW; 0F1E937D2B9B0C3B CRC64; MLLPASHRGQ PPVLPSSRSL ALSASSLKNW KDLGSSSPTE EEEDEDGDLL EETEVEELFQ QHVPAGIGQG QHRVFIVHPD VKWGSRKQYL TTAELMMAEA EGLVNTLDNW TVVDKIILST KTPEKKKIFG KGNFQLLTEK IRQTPGVTAV FVNVDRLYSV SEQREFEEAW GVKVFDRYSV VLHIFRCNAR TKEAKLQISL AEIPLLSRSR LKNDMADLDQ QGGGARYIGG SGETVYEVQQ RLLKERETRI RSALERLRKK RHLLRSQRKH REFPTVSVLG YTNCGKTTLI KALTGDSGLQ PRNQLFATLD VTVHAGQLPS HMTVLYVDTI GFLSQLPHQL IDSFSATLED IVHSVGRPVS SSTPTYNC // ID M4DN72_BRARP Unreviewed; 561 AA. AC M4DN72; DT 01-MAY-2013, integrated into UniProtKB/TrEMBL. DT 01-MAY-2013, sequence version 1. DT 05-JUL-2017, entry version 22. DE SubName: Full=Uncharacterized protein {ECO:0000313|EnsemblPlants:Bra017959.1-P}; OS Brassica rapa subsp. pekinensis (Chinese cabbage) (Brassica OS pekinensis). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae; OC Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Brassiceae; OC Brassica. OX NCBI_TaxID=51351 {ECO:0000313|EnsemblPlants:Bra017959.1-P, ECO:0000313|Proteomes:UP000011750}; RN [1] {ECO:0000313|EnsemblPlants:Bra017959.1-P, ECO:0000313|Proteomes:UP000011750} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Chiifu-401-42 {ECO:0000313|EnsemblPlants:Bra017959.1-P, RC ECO:0000313|Proteomes:UP000011750}; RX PubMed=21873998; DOI=10.1038/ng.919; RG Brassica rapa Genome Sequencing Project Consortium; RA Wang X., Wang H., Wang J., Sun R., Wu J., Liu S., Bai Y., Mun J.H., RA Bancroft I., Cheng F., Huang S., Li X., Hua W., Wang J., Wang X., RA Freeling M., Pires J.C., Paterson A.H., Chalhoub B., Wang B., RA Hayward A., Sharpe A.G., Park B.S., Weisshaar B., Liu B., Li B., RA Liu B., Tong C., Song C., Duran C., Peng C., Geng C., Koh C., Lin C., RA Edwards D., Mu D., Shen D., Soumpourou E., Li F., Fraser F., RA Conant G., Lassalle G., King G.J., Bonnema G., Tang H., Wang H., RA Belcram H., Zhou H., Hirakawa H., Abe H., Guo H., Wang H., Jin H., RA Parkin I.A., Batley J., Kim J.S., Just J., Li J., Xu J., Deng J., RA Kim J.A., Li J., Yu J., Meng J., Wang J., Min J., Poulain J., Wang J., RA Hatakeyama K., Wu K., Wang L., Fang L., Trick M., Links M.G., Zhao M., RA Jin M., Ramchiary N., Drou N., Berkman P.J., Cai Q., Huang Q., Li R., RA Tabata S., Cheng S., Zhang S., Zhang S., Huang S., Sato S., Sun S., RA Kwon S.J., Choi S.R., Lee T.H., Fan W., Zhao X., Tan X., Xu X., RA Wang Y., Qiu Y., Yin Y., Li Y., Du Y., Liao Y., Lim Y., Narusaka Y., RA Wang Y., Wang Z., Li Z., Wang Z., Xiong Z., Zhang Z.; RT "The genome of the mesopolyploid crop species Brassica rapa."; RL Nat. Genet. 43:1035-1039(2011). RN [2] {ECO:0000313|EnsemblPlants:Bra017959.1-P} RP IDENTIFICATION. RC STRAIN=cv. Chiifu-401-42 {ECO:0000313|EnsemblPlants:Bra017959.1-P}; RG EnsemblPlants; RL Submitted (JUL-2014) to UniProtKB. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR STRING; 3711.Bra017959.1-P; -. DR PRIDE; M4DN72; -. DR EnsemblPlants; Bra017959.1; Bra017959.1-P; Bra017959. DR Gramene; Bra017959.1; Bra017959.1-P; Bra017959. DR InParanoid; M4DN72; -. DR OrthoDB; EOG09360975; -. DR Proteomes; UP000011750; Chromosome A06. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR CDD; cd01878; HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 2. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000011750}; KW Reference proteome {ECO:0000313|Proteomes:UP000011750}. FT DOMAIN 283 528 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 561 AA; 62794 MW; 61D9F181AC5FD101 CRC64; MLRTLSLARD HLRSKAQISS SPFSPPSTIR ALSSPFSSKR HAPKATEEEA PAALKESVLL YPKDPSSTPK LFLVQPRLTP PKFLQAKLNE ALCLANSLEE QRYGYFESDF FDKELPSHVV VQNPIARSSK PREEVDAVFI NAILSAIQQR NLERIWGKPV LDRVGLIIEI FNAHAHTKEA KLQAELAALM YKKSRLVRVR GTDGRQTFGQ FGEAEVVSAR GRAASKGTGF VGGAGETELQ LQRRRIADRR LRLLSQIKEA QRTRLLQRAA RKRQSGLAGK SLATIAVVGY TNAGKSTLTS ALTRTALYCN ERLFATLDPT LKNAILPSGR KVLFSDTVGF ISDLPIQLVE AFQSTLEEVV EADLLLHVVD STAPNIEEHR STVFHVLNQI GVPEEKLKNM IEVWNKIDYE EEEEEEEDMH YLDDGKGEGE EEEEEAELSE DSIVEETSEA SSEATVDEDQ IQNQEDDSDE WLLSEDENVS DSELWKVPEE AKVDAAQKSG PDVRVSALTG VGLKELMYLI DEKLSGEDEK RKSETIVERN DFQSRKWRPS FKDDEEFAAG Q // ID M4DV58_BRARP Unreviewed; 545 AA. AC M4DV58; DT 01-MAY-2013, integrated into UniProtKB/TrEMBL. DT 01-MAY-2013, sequence version 1. DT 05-JUL-2017, entry version 23. DE SubName: Full=Uncharacterized protein {ECO:0000313|EnsemblPlants:Bra020401.1-P}; OS Brassica rapa subsp. pekinensis (Chinese cabbage) (Brassica OS pekinensis). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae; OC Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Brassiceae; OC Brassica. OX NCBI_TaxID=51351 {ECO:0000313|EnsemblPlants:Bra020401.1-P, ECO:0000313|Proteomes:UP000011750}; RN [1] {ECO:0000313|EnsemblPlants:Bra020401.1-P, ECO:0000313|Proteomes:UP000011750} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Chiifu-401-42 {ECO:0000313|EnsemblPlants:Bra020401.1-P, RC ECO:0000313|Proteomes:UP000011750}; RX PubMed=21873998; DOI=10.1038/ng.919; RG Brassica rapa Genome Sequencing Project Consortium; RA Wang X., Wang H., Wang J., Sun R., Wu J., Liu S., Bai Y., Mun J.H., RA Bancroft I., Cheng F., Huang S., Li X., Hua W., Wang J., Wang X., RA Freeling M., Pires J.C., Paterson A.H., Chalhoub B., Wang B., RA Hayward A., Sharpe A.G., Park B.S., Weisshaar B., Liu B., Li B., RA Liu B., Tong C., Song C., Duran C., Peng C., Geng C., Koh C., Lin C., RA Edwards D., Mu D., Shen D., Soumpourou E., Li F., Fraser F., RA Conant G., Lassalle G., King G.J., Bonnema G., Tang H., Wang H., RA Belcram H., Zhou H., Hirakawa H., Abe H., Guo H., Wang H., Jin H., RA Parkin I.A., Batley J., Kim J.S., Just J., Li J., Xu J., Deng J., RA Kim J.A., Li J., Yu J., Meng J., Wang J., Min J., Poulain J., Wang J., RA Hatakeyama K., Wu K., Wang L., Fang L., Trick M., Links M.G., Zhao M., RA Jin M., Ramchiary N., Drou N., Berkman P.J., Cai Q., Huang Q., Li R., RA Tabata S., Cheng S., Zhang S., Zhang S., Huang S., Sato S., Sun S., RA Kwon S.J., Choi S.R., Lee T.H., Fan W., Zhao X., Tan X., Xu X., RA Wang Y., Qiu Y., Yin Y., Li Y., Du Y., Liao Y., Lim Y., Narusaka Y., RA Wang Y., Wang Z., Li Z., Wang Z., Xiong Z., Zhang Z.; RT "The genome of the mesopolyploid crop species Brassica rapa."; RL Nat. Genet. 43:1035-1039(2011). RN [2] {ECO:0000313|EnsemblPlants:Bra020401.1-P} RP IDENTIFICATION. RC STRAIN=cv. Chiifu-401-42 {ECO:0000313|EnsemblPlants:Bra020401.1-P}; RG EnsemblPlants; RL Submitted (APR-2015) to UniProtKB. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR STRING; 3711.Bra020401.1-P; -. DR EnsemblPlants; Bra020401.1; Bra020401.1-P; Bra020401. DR Gramene; Bra020401.1; Bra020401.1-P; Bra020401. DR InParanoid; M4DV58; -. DR OrthoDB; EOG093609UJ; -. DR Proteomes; UP000011750; Chromosome A02. DR GO; GO:0009507; C:chloroplast; IEA:EnsemblPlants. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000011750}; KW Reference proteome {ECO:0000313|Proteomes:UP000011750}. FT DOMAIN 311 477 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 545 AA; 61206 MW; A913B9D412CE8113 CRC64; MSSFLFPSSS PIPKPHWRGN SIPRPNRPIT LSLLHGNSYS WRLSCKLSLD FEESVEEDEI PQFLDFSAEE EEEPSLEKET VSAPTTTLMQ RKKKKGDEES LEDRFKLRNG KEVFEEKAYL VGVERKGDGE CLFDIEESLE ELEQLADTAG LMVVGSTYQK LASPNPRTYI GSGKVSEIKS AINALDVETV IFDDELSPGQ LRNLEKAFGG DVRVCDRTAL ILDIFNQRAA THEAALQVAL AQMEYQLPRL TRMWTHLERQ SGGQVKGMGE KQIEVDKRIL RTQIGVLKKE LESVRKHRKQ YRSRRVAIPV PVVSLVGYTN AGKSTLLNQL TGANVLAENR LFATLDPTTR RVQMHNGKEF LLTDTVGFIQ KLPTTLVAAF RATLEEISES SLLVHVVDIS HPLANQQIEA VEKVMSELDV SSIPKLVVWN KVDRVDDPHK IKLEAEEHGD VICISALTGE GLDKFCNAVH EKLKDSMVWV EALLPFDKGD LLSTIHKVGM VKETEYTENG TLVRAHVPLR FAQLLKPMRH LVKEASYAKK GEIES // ID M4NGC4_9GAMM Unreviewed; 433 AA. AC M4NGC4; DT 29-MAY-2013, integrated into UniProtKB/TrEMBL. DT 29-MAY-2013, sequence version 1. DT 30-AUG-2017, entry version 32. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=R2APBS1_1561 {ECO:0000313|EMBL:AGG88703.1}; OS Rhodanobacter denitrificans. OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales; OC Rhodanobacteraceae; Rhodanobacter. OX NCBI_TaxID=666685 {ECO:0000313|EMBL:AGG88703.1, ECO:0000313|Proteomes:UP000011859}; RN [1] {ECO:0000313|EMBL:AGG88703.1, ECO:0000313|Proteomes:UP000011859} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=2APBS1 {ECO:0000313|EMBL:AGG88703.1, RC ECO:0000313|Proteomes:UP000011859}; RG US DOE Joint Genome Institute; RA Huntemann M., Wei C.-L., Han J., Detter J.C., Han C., Tapia R., RA Munk A.C.C., Chen A., Krypides N., Mavromatis K., Markowitz V., RA Szeto E., Ivanova N., Mikhailova N., Ovchinnikova G., Pagani I., RA Pati A., Goodwin L., Peters L., Pitluck S., Woyke T., Prakash O., RA Elkins J., Brown S., Palumbo A., Hemme C., Zhou J., Watson D., RA Jardine P., Kostka J., Green S.; RT "Complete genome of Rhodanobacter sp. 2APBS1."; RL Submitted (APR-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP003470; AGG88703.1; -; Genomic_DNA. DR RefSeq; WP_015447479.1; NC_020541.1. DR EnsemblBacteria; AGG88703; AGG88703; R2APBS1_1561. DR KEGG; rhd:R2APBS1_1561; -. DR KO; K03665; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000011859; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000011859}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}. FT DOMAIN 200 366 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 433 AA; 47140 MW; A44179027CDC7167 CRC64; MFDRQKKGDR AVLVLPHSRG EGDAARRAEE FAELVKSAGA EVLGVISARV EDPNPRYYIG TGKADEVAEA ARALEADLVL VDHVLTPVQE RNLEKHLGIR VVDRAGLILD IFAQRARSHE GKLEVELAQL KHLATRLVRG WTHLDTQRGG AIGNRGPGET QLETDRRLLG ERVKMLTRRL EKVQTQRGQQ RRARLRNTVP RVALVGYTNA GKSTLFNALT TGDVYAANLL FATLDPTVRK LEGLSCGPAV LADTVGFIRE LPHDLVAAFR ATLAEARDAD LLLHVSDAAD EERDRLHHVV DKVLEEIDAG DVPQLQVMNK IDLAGAEPRI ERDGTGKPVR VWLSAATGAG LDLLRQALGE LLGGERVQSA LQLPLSAGRL HARLKAAGAI SGETVDEHGW QLHIDAPRSV IAPLSGGDPT ETRLLRQLLA VAE // ID M4R6X4_BIBTR Unreviewed; 451 AA. AC M4R6X4; DT 29-MAY-2013, integrated into UniProtKB/TrEMBL. DT 29-MAY-2013, sequence version 1. DT 07-JUN-2017, entry version 31. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=WQG_2180 {ECO:0000313|EMBL:AGH37504.1}; OS Bibersteinia trehalosi USDA-ARS-USMARC-192. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Bibersteinia. OX NCBI_TaxID=1171377 {ECO:0000313|EMBL:AGH37504.1, ECO:0000313|Proteomes:UP000011846}; RN [1] {ECO:0000313|EMBL:AGH37504.1, ECO:0000313|Proteomes:UP000011846} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=192 {ECO:0000313|Proteomes:UP000011846}; RA Harhay G.P., Koren S., Phillippy A., McVey D.S., Kuszak J., RA Clawson M., Harhay D.M., Heaton M., Chitko-Mckown C., Smith T.P.L.; RT "Annotation of the Bibersteinia trehalsoi USDA-ARS-USMARC-192 complete RT genome."; RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP003745; AGH37504.1; -; Genomic_DNA. DR EnsemblBacteria; AGH37504; AGH37504; WQG_2180. DR KEGG; bto:WQG_2180; -. DR PATRIC; fig|1171377.3.peg.218; -. DR KO; K03665; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000011846; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000011846}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000011846}. FT DOMAIN 217 384 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 183 210 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 451 AA; 50820 MW; 0F5F4ED0779959F0 CRC64; MNQQEPNSVD EFGSVLLETP WLAKSKERAI LVHLYLAQNK DVENLHEFQT LAEGAGVEIA TVLTTSRSAP HIKYYVGQGK AQEIADAVKY FNADVVLVNH QLSPAQTRNL QTLCDCRVVD RTGLILDIFA QRARSFEGKL QVELAQLRHL STRLVRRLGN QDQQKGGAVG LRGPGETQLE TDRRLIKVRI QQLQNRLQKV AKQRDQNRKT RQKADIPTVS LVGYTNAGKS TLFNAITHAG VYAADQLFAT LDPTLRRIQI QDVGTAILAD TVGFIRFLPH DLVSAFKSTL QETTEATLLL HVIDGADERR EENIDAVNAV LDEINALEIP SLLVYNKVDK LEEVLPHIEY ADDGTPIAVY LSAQSGQGID LLFQAMQARL KSELVREKLL LPPTSGQIYA EFYQRNCILN EYFNEFGDRL LEIEVDKVQW QKWLKQYPEL LELVALAEWG E // ID M4RE75_9BIFI Unreviewed; 515 AA. AC M4RE75; DT 29-MAY-2013, integrated into UniProtKB/TrEMBL. DT 29-MAY-2013, sequence version 1. DT 07-JUN-2017, entry version 34. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=D805_0596 {ECO:0000313|EMBL:AGH40863.1}; OS Bifidobacterium thermophilum RBL67. OC Bacteria; Actinobacteria; Bifidobacteriales; Bifidobacteriaceae; OC Bifidobacterium. OX NCBI_TaxID=1254439 {ECO:0000313|EMBL:AGH40863.1, ECO:0000313|Proteomes:UP000011835}; RN [1] {ECO:0000313|EMBL:AGH40863.1, ECO:0000313|Proteomes:UP000011835} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=RBL67 {ECO:0000313|EMBL:AGH40863.1}; RX PubMed=23640377; RA Jans C., Lacroix C., Follador R., Stevens M.J.; RT "Complete Genome Sequence of the Probiotic Bifidobacterium RT thermophilum Strain RBL67."; RL Genome Announc. 1:E00191-13(2013). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP004346; AGH40863.1; -; Genomic_DNA. DR EnsemblBacteria; AGH40863; AGH40863; D805_0596. DR KEGG; btp:D805_0596; -. DR PATRIC; fig|1254439.12.peg.599; -. DR KO; K03665; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000011835; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000011835}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000011835}. FT DOMAIN 294 461 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 515 AA; 55743 MW; BFFAA008A0F0FA8B CRC64; MTPQQAGHQG AAEHASDGTL NQSEQSGQSA PAQDEDVLSE HSEVLLDDAA AHPYAHEDQE WREREARNEL KRVAGLGELQ DVTEVEYRKV RLERVVLVGV WSSAKTTQAQ AEESLRELAA LAETAGAQVC DGLLQHRLRP DSATYVGSGK AKEIAGVVAR DEADTIIVDD DLPPSQRRAL EDATKVKVVD RTAVILDIFA QHATSREGKA QVELAQLQYM LPRLRGWGGS LSRQAGGRAA GADAGIGSRG PGETKIEMDR RVIRNRIAKL RKQIAHMAPA RDVKRGSRRR FGLPTVAVVG YTNAGKSSLT NRLTGSRELV ENALFATLDT AVRRASAKDG RQYAYVDTVG FVRRLPTQLV EAFKSTLEEV ADADVIVHVV DASHPDPFAQ IDAVNAILAD INGTESIPRI LVFNKIDRAD QATRERLAAL APEAHLVSAF TGEGIDALRE AVEALLPVPD VHVSALLPYT AGSLVSKIRE YGQMDSIEYR GDGMMIEAQV DSQLAAQVVD AAVDE // ID M4RG55_9ALTE Unreviewed; 261 AA. AC M4RG55; DT 29-MAY-2013, integrated into UniProtKB/TrEMBL. DT 29-MAY-2013, sequence version 1. DT 07-JUN-2017, entry version 22. DE SubName: Full=HSR1-like GTP-binding protein {ECO:0000313|EMBL:AGH42500.1}; GN ORFNames=C427_0390 {ECO:0000313|EMBL:AGH42500.1}; OS Paraglaciecola psychrophila 170. OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales; OC Alteromonadaceae; Paraglaciecola. OX NCBI_TaxID=1129794 {ECO:0000313|EMBL:AGH42500.1, ECO:0000313|Proteomes:UP000011864}; RN [1] {ECO:0000313|EMBL:AGH42500.1, ECO:0000313|Proteomes:UP000011864} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=170 {ECO:0000313|EMBL:AGH42500.1}; RX PubMed=23640379; RA Yin J., Chen J., Liu G., Yu Y., Song L., Wang X., Qu X.; RT "Complete Genome Sequence of Glaciecola psychrophila Strain 170T."; RL Genome Announc. 1:E00199-13(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP003837; AGH42500.1; -; Genomic_DNA. DR EnsemblBacteria; AGH42500; AGH42500; C427_0390. DR KEGG; gps:C427_0390; -. DR PATRIC; fig|1129794.4.peg.386; -. DR KO; K03665; -. DR BioCyc; GPSY1129794:G136Q-396-MONOMER; -. DR Proteomes; UP000011864; Chromosome. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR CDD; cd01878; HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 4: Predicted; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000011864}; KW Reference proteome {ECO:0000313|Proteomes:UP000011864}. FT DOMAIN 198 261 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 157 191 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 261 AA; 29250 MW; 7E7FCB9552787E61 CRC64; MFDRYEAGEQ AVLVHVDFAD ENSKEDLLEL QLLVSSAGVN AIDVVTCSRQ SPQARYFVGS GKAEEIANAV RAQQADVVIF NHSLSPSQER NLEQLCQCRV LDRTGLILDI FAQRARTHEG KLQVELAQLR HMSTRLVRGW THLDKQKGGI GLRGPGESQL ETDRRLLRAR LKAIQRRLDK VQKQREQGRR SRIRAEIPTV SLVGYTNAGK STLFNSMTES AVYVADQLFA TLDPTLRKIQ LQNVGSAILA DTVGFIRHLP H // ID M4S0J6_9SPHN Unreviewed; 432 AA. AC M4S0J6; DT 29-MAY-2013, integrated into UniProtKB/TrEMBL. DT 29-MAY-2013, sequence version 1. DT 07-JUN-2017, entry version 31. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=G432_01180 {ECO:0000313|EMBL:AGH47964.1}; OS Sphingomonas sp. MM-1. OC Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales; OC Sphingomonadaceae; Sphingomonas. OX NCBI_TaxID=745310 {ECO:0000313|EMBL:AGH47964.1, ECO:0000313|Proteomes:UP000011816}; RN [1] {ECO:0000313|EMBL:AGH47964.1, ECO:0000313|Proteomes:UP000011816} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MM-1 {ECO:0000313|EMBL:AGH47964.1}; RX PubMed=23682148; RA Tabata M., Ohtsubo Y., Ohhata S., Tsuda M., Nagata Y.; RT "Complete Genome Sequence of the gamma-Hexachlorocyclohexane-Degrading RT Bacterium Sphingomonas sp. Strain MM-1."; RL Genome Announc. 1:E00247-13(2013). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP004036; AGH47964.1; -; Genomic_DNA. DR RefSeq; WP_015456981.1; NC_020561.1. DR EnsemblBacteria; AGH47964; AGH47964; G432_01180. DR KEGG; sphm:G432_01180; -. DR PATRIC; fig|745310.14.peg.242; -. DR KO; K03665; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000011816; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000011816}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000011816}. FT DOMAIN 209 381 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 432 AA; 46791 MW; B9A5FC087B0CABAC CRC64; MSVFNRADDD GLSRGAKAIV ALPDRGSGSG RDTDARLAEA AGLAAAIGVD VVEKLAFRLR DPKPATLFGS GQVDAIATAA RMAEAELVIV DGALSPIQQR NLEKALDTKV IDRTGLILEI FGERAATAEG RLQVELAHLD YQAGRLVRSW THLERQRGGF GFLGGPGETQ IEADRRLIRD RMAKLRRELE NVTRTRGLHR ARRQRAPWPV IALVGYTNAG KSTLFNRMTG ATVMAENLLF ATLDPTMRQI SLPGIDKAIL SDTVGFVSDL PTQLVAAFRA TLEEVTAADL IIHVRDISHP DSEPQARDVE AVLAEIGIVG GEGGTPIFEA WNKIDALPPE EADRVLAEAA RRDDVVAISA FTGEGVDALQ RAVAERLTHG SRRYSLRVDP ADGGAIAWLH AHGEVLSQEM DGDRLAIEVK LSEADWARYQ AR // ID M4U2E1_9GAMM Unreviewed; 430 AA. AC M4U2E1; DT 29-MAY-2013, integrated into UniProtKB/TrEMBL. DT 29-MAY-2013, sequence version 1. DT 30-AUG-2017, entry version 32. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=PCNPT3_02210 {ECO:0000313|EMBL:AGH80384.1}; OS Psychromonas sp. CNPT3. OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales; OC Psychromonadaceae; Psychromonas. OX NCBI_TaxID=314282 {ECO:0000313|EMBL:AGH80384.1, ECO:0000313|Proteomes:UP000010320}; RN [1] {ECO:0000313|EMBL:AGH80384.1, ECO:0000313|Proteomes:UP000010320} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CNPT3 {ECO:0000313|EMBL:AGH80384.1, RC ECO:0000313|Proteomes:UP000010320}; RA Lauro F.M., Chastain R.A., Stratton T.K., Ferriera S., Johnson J., RA Yayanos A.A., Bartlett D.H.; RT "The complete genome sequence of the deep-sea bacterium Psychromonas RT CNPT2."; RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP004404; AGH80384.1; -; Genomic_DNA. DR RefSeq; WP_015464265.1; NC_020802.1. DR ProteinModelPortal; M4U2E1; -. DR STRING; 314282.PCNPT3_03306; -. DR EnsemblBacteria; AGH80384; AGH80384; PCNPT3_02210. DR KEGG; psy:PCNPT3_02210; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR KO; K03665; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000010320; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000010320}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000010320}. FT DOMAIN 198 365 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 430 AA; 47587 MW; 84226C3CFAD144DF CRC64; MFDRYKAGER ALLVHMTFSD DAKKEDLDEL KLLVSSAGVA SIGVITGPRK TPHPRYFVGT GKAQEIADGV RTLGANVVIF NHSLSPAQQR NLEALCECLV LDRTALILDI FAQRARTYEG KLQIELAQLK HMSTRLIRGW THLERQKGGV GMRGPGETQL ESDRRLLSER ITAIKGRLAK VAKQRDQGRR ARVRGEIATV SLVGYTNAGK STLFNHMTGA DVYAADQLFA TLDPTLRQIK VQDVGNCILA DTVGFVRHLP HDLVAAFKAT LQETREATLL LHIVDCSDEN YRDNIDAVQL VLNDIDAGDV PQLTIMNKID ALDDLKPHID LDDEGKPIRV WLSAKTGEGS DLLLSALSSL LSGQIRELHL CIPPEQGKLR AQLYQINCIV NESYAENGDC LVDIRINNVD LSRLRKQFLG VLDACIKANK // ID M4U855_9GAMM Unreviewed; 449 AA. AC M4U855; DT 29-MAY-2013, integrated into UniProtKB/TrEMBL. DT 29-MAY-2013, sequence version 1. DT 07-JUN-2017, entry version 32. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=PCNPT3_12365 {ECO:0000313|EMBL:AGH82409.1}; OS Psychromonas sp. CNPT3. OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales; OC Psychromonadaceae; Psychromonas. OX NCBI_TaxID=314282 {ECO:0000313|EMBL:AGH82409.1, ECO:0000313|Proteomes:UP000010320}; RN [1] {ECO:0000313|EMBL:AGH82409.1, ECO:0000313|Proteomes:UP000010320} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CNPT3 {ECO:0000313|EMBL:AGH82409.1, RC ECO:0000313|Proteomes:UP000010320}; RA Lauro F.M., Chastain R.A., Stratton T.K., Ferriera S., Johnson J., RA Yayanos A.A., Bartlett D.H.; RT "The complete genome sequence of the deep-sea bacterium Psychromonas RT CNPT2."; RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP004404; AGH82409.1; -; Genomic_DNA. DR RefSeq; WP_015466288.1; NC_020802.1. DR ProteinModelPortal; M4U855; -. DR STRING; 314282.PCNPT3_00481; -. DR EnsemblBacteria; AGH82409; AGH82409; PCNPT3_12365. DR KEGG; psy:PCNPT3_12365; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR KO; K03665; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000010320; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000010320}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000010320}. FT DOMAIN 226 391 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 449 AA; 50450 MW; A0D8A679C0AE5869 CRC64; MSITTADHSV TRALLISIRT PDLTQLDVDE SLSELGRLVT TLGFVVVGKQ TQRQQSTKLL SVLGSGKLEE LATMTNDEEL PLQDEAQVNF NQEQVSDLLA ESETQEMANV VVFDCELSPN QLRSVELALG VEVYDRTRVI IEIFSKHART RTAKLQVEIA RLNYLTPRIR DENSGDRERQ KGSWIGESAF EINRRRIRDK IASLKRELIK LQGEMQGRRS GRVEQQCVAL VGYTNAGKSS LMRALTDSEV LVEDKLFATL DTTVRTLQPP TQPRILISDT VGFIKKLPHD LVASFHSTLE EAKDAALLLY VVDASDVNFK SQLAVVDHVL GELNVDLSNK ILLLNKVDCI SEERQLELLN EYPDALQIST RDKADVAMVH QEIQTFLEKK MCAACFNIPY TASGIMGEIH SKMQVIDEQY HEDGMRLTVK ASPVALERLH KMLQTSFNK // ID M4V7C4_9DELT Unreviewed; 420 AA. AC M4V7C4; DT 29-MAY-2013, integrated into UniProtKB/TrEMBL. DT 29-MAY-2013, sequence version 1. DT 07-JUN-2017, entry version 31. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=A11Q_1081 {ECO:0000313|EMBL:AGH95297.1}; OS Bdellovibrio exovorus JSS. OC Bacteria; Proteobacteria; Deltaproteobacteria; Bdellovibrionales; OC Bdellovibrionaceae; Bdellovibrio. OX NCBI_TaxID=1184267 {ECO:0000313|EMBL:AGH95297.1, ECO:0000313|Proteomes:UP000012040}; RN [1] {ECO:0000313|EMBL:AGH95297.1, ECO:0000313|Proteomes:UP000012040} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=JSS {ECO:0000313|EMBL:AGH95297.1}; RX PubMed=23190728; DOI=10.1038/ismej.2012.149; RA Pasternak Z., Pietrokovski S., Rotem O., Gophna U., RA Lurie-Weinberger M.N., Jurkevitch E.; RT "By their genes ye shall know them: genomic signatures of predatory RT bacteria."; RL ISME J. 7:756-769(2013). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP003537; AGH95297.1; -; Genomic_DNA. DR RefSeq; WP_015469787.1; NC_020813.1. DR EnsemblBacteria; AGH95297; AGH95297; A11Q_1081. DR KEGG; bex:A11Q_1081; -. DR PATRIC; fig|1184267.3.peg.1094; -. DR KO; K03665; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000012040; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000012040}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000012040}. FT DOMAIN 203 366 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 162 196 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 420 AA; 47293 MW; 11C8ACF2AD4CC8B7 CRC64; MNQVRINEKD KVIVVGVGLK SDPITEIKEN LCELEELVGA AGGEVIGSTV QVLPQWNPST LIGSGKVQEI KEMVAESNAQ LVIVDHQLSG IQTRNLQEQI GCKILDRSQL ILDIFAQRAR TYEGKLQVEL AQLLDQMPRM IGAWHDSLSR LGGGIGTRGP GETALENDRR RAKEKVALIK KKLEEVSQQR AQHRQSRKRN EVPSFALIGY TNSGKSSLLN RLTGSQVLAK NMVFATLDPT TRKVFLDEGP PAVVTDTVGF IRKLPPQLIE AFKATLEESA EADILLHVVD LSSPNMERQI EVVEDLIKEF KWEDKKIIHI FNKVDIAPVE RQFRVKHFPR VFVSALTGQG FEQLKKIMAD TINEMQSQVE LYFDRVNEYR LYDLGREAKI LRKEAATEGT ICVAMMTPTL LNKWKDFLVK // ID M4VF19_9DELT Unreviewed; 468 AA. AC M4VF19; DT 29-MAY-2013, integrated into UniProtKB/TrEMBL. DT 29-MAY-2013, sequence version 1. DT 07-JUN-2017, entry version 32. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=A11Q_2425 {ECO:0000313|EMBL:AGH96641.1}; OS Bdellovibrio exovorus JSS. OC Bacteria; Proteobacteria; Deltaproteobacteria; Bdellovibrionales; OC Bdellovibrionaceae; Bdellovibrio. OX NCBI_TaxID=1184267 {ECO:0000313|EMBL:AGH96641.1, ECO:0000313|Proteomes:UP000012040}; RN [1] {ECO:0000313|EMBL:AGH96641.1, ECO:0000313|Proteomes:UP000012040} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=JSS {ECO:0000313|EMBL:AGH96641.1}; RX PubMed=23190728; DOI=10.1038/ismej.2012.149; RA Pasternak Z., Pietrokovski S., Rotem O., Gophna U., RA Lurie-Weinberger M.N., Jurkevitch E.; RT "By their genes ye shall know them: genomic signatures of predatory RT bacteria."; RL ISME J. 7:756-769(2013). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP003537; AGH96641.1; -; Genomic_DNA. DR RefSeq; WP_015471131.1; NC_020813.1. DR EnsemblBacteria; AGH96641; AGH96641; A11Q_2425. DR KEGG; bex:A11Q_2425; -. DR PATRIC; fig|1184267.3.peg.2454; -. DR KO; K03665; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000012040; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 2. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000012040}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000012040}. FT DOMAIN 248 413 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 209 236 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 468 AA; 51658 MW; B3F26EE427309A30 CRC64; MSIENKIKNA VLVGIQLPKV SSAELEASLQ ELTRLVTTLG YNVVGQVTQK RNSDRSAAVL GDGKLKELAE WTGGTGKIAA MVEHKLSKAA QKWQDEKNAL AEENENPEND SENEESGILS EEQKNSAQIV IVDTELSPSQ LRNLESATGV TVLDRTGVII EIFSRHARTR AARLQVEIAR LTYVAPRLRE TGGGEDRGGG GVGGKGAGES SLELDKRKIR DRIKELKTEL ASIGNEHQVR RARREQEISV ALVGYTNAGK SSLMRAMTGS EVLVADKLFA TLDTTIRQLY PETRPKVLMS DTVGFIKKLP HDLVASFKST LDEALHASLL LFVVDSSDPS FRSQLEVTQS VLAEVGATEV PSLLVLNKKD RLTAEQMKSL RAEYPEAVMI STRDKDDLKM MRDKIMGYFE SHMIDETLFI PYTVQGVIGE IRAKMRVLSE SYDEKGVSLT VRATEESLSQ LKKKFKIK // ID M4XM21_9PSED Unreviewed; 433 AA. AC M4XM21; DT 29-MAY-2013, integrated into UniProtKB/TrEMBL. DT 29-MAY-2013, sequence version 1. DT 30-AUG-2017, entry version 36. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=H681_22140 {ECO:0000313|EMBL:AGI26295.1}; OS Pseudomonas sp. ATCC 13867. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=1294143 {ECO:0000313|EMBL:AGI26295.1, ECO:0000313|Proteomes:UP000012082}; RN [1] {ECO:0000313|EMBL:AGI26295.1, ECO:0000313|Proteomes:UP000012082} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 13867 {ECO:0000313|EMBL:AGI26295.1, RC ECO:0000313|Proteomes:UP000012082}; RX PubMed=23723394; RA Ainala S.K., Somasundar A., Park S.; RT "Complete Genome Sequence of Pseudomonas denitrificans ATCC 13867."; RL Genome Announc. 1:E00257-13(2013). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP004143; AGI26295.1; -; Genomic_DNA. DR RefSeq; WP_015479144.1; NC_020829.1. DR EnsemblBacteria; AGI26295; AGI26295; H681_22140. DR GeneID; 32562793; -. DR KEGG; pdr:H681_22140; -. DR PATRIC; fig|1294143.3.peg.4494; -. DR KO; K03665; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000012082; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000012082}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}. FT DOMAIN 199 366 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 165 192 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 433 AA; 48934 MW; 5228EEE16D947061 CRC64; MFFERPGGGE RAILVHLEGQ DPEAREDPQE FQELARSAGA ESVAFISISR HQPSAKYLIG SGKVDELHDL VHAEKVELII FNHTLTPSQE RNLERALECR VLDRTGLILD IFAQRARTHE GKLQVELAQL EHMSTRLVRG WTHLERQKGG IGLRGPGETQ LETDRRLLRG RIRQIKSRLE KVRSQREQAR RGRRRAEIPS VSLVGYTNAG KSTLFNALTT SEVYAANQLF ATLDPTLRRL ELDDVGPIVL ADTVGFIRHL PHKLVEAFRA TLEESSNADL LLHVIDSHEP ERDAQIEQVL AVLQEIGANE LPILEVYNKI DLLPDMRPMI QRDELGKPVR VWVSARESRG LELVEQAVAE LLGEDMFVGT LCLPQRLGRL RAQFFELGAV QSEGHDEQGC AVLQVRLPRV ELNRLVSREG WQPAEFIAQH TLQ // ID M5A3H3_9ACTN Unreviewed; 457 AA. AC M5A3H3; DT 29-MAY-2013, integrated into UniProtKB/TrEMBL. DT 29-MAY-2013, sequence version 1. DT 07-JUN-2017, entry version 34. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=YM304_27000 {ECO:0000313|EMBL:BAN03014.1}; OS Ilumatobacter coccineus YM16-304. OC Bacteria; Actinobacteria; Acidimicrobiia; Acidimicrobiales; OC Acidimicrobiaceae; Ilumatobacter. OX NCBI_TaxID=1313172 {ECO:0000313|EMBL:BAN03014.1, ECO:0000313|Proteomes:UP000011863}; RN [1] {ECO:0000313|EMBL:BAN03014.1, ECO:0000313|Proteomes:UP000011863} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=YM16-304 {ECO:0000313|EMBL:BAN03014.1}; RX PubMed=23524358; DOI=10.1099/ijs.0.047316-0; RA Matsumoto A., Kasai H., Matsuo Y., Shizuri Y., Ichikawa N., Fujita N., RA Omura S., Takahashi Y.; RT "Ilumatobacter nonamiense sp. nov. and Ilumatobacter coccineum sp. RT nov., isolated from seashore sand."; RL Int. J. Syst. Evol. Microbiol. 63:3404-3408(2013). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AP012057; BAN03014.1; -; Genomic_DNA. DR RefSeq; WP_015442261.1; NC_020520.1. DR EnsemblBacteria; BAN03014; BAN03014; YM304_27000. DR KEGG; aym:YM304_27000; -. DR PATRIC; fig|467094.3.peg.2748; -. DR KO; K03665; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000011863; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000011863}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000011863}. FT DOMAIN 214 378 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 457 AA; 49646 MW; 09BD63C40A641F56 CRC64; MSTPYEEALA GTLIDRTIRE KIVLVAVALP GDDEEMVEAS LDELALLVDT AGADEVARVI QKRDAPDHTW YIGKGKVDEL KELCLALDVD TVVFDNELAP SQQYNLEKLL GRTALDRTAV ILDIFGQNAH TMEGKAQVEL ALLRYRLPRL RRGKNAKMSQ QRGGVGARFG GGETKMEVDR RRIMRRINKL EKDLSALAET RALQRQGRRR SGLASVAIVG YTNAGKSTLL NQLTQSGVLT EDRLFATLDP TTRRLALPGG EPVLLTDTVG FISRLPHGLV ESFKGTLEVA ALADYLVHVV DVTAPDPEGQ IAAVHEVLRE IEASAVPELL VFNKADADPI AAKELVESHP GSVALSARTG EGADVFLRTI GDRLRSLSVV YELVVPYDRG DVLASIHREG EVVSVGDGET EWTIRARLSD ASAGRLDEFV VGDDAPADDR ASADTDRSDA EPSEETL // ID M5E7M2_9GAMM Unreviewed; 437 AA. AC M5E7M2; DT 29-MAY-2013, integrated into UniProtKB/TrEMBL. DT 29-MAY-2013, sequence version 1. DT 07-JUN-2017, entry version 33. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=TOL_3024 {ECO:0000313|EMBL:CCU73420.1}; OS Thalassolituus oleivorans MIL-1. OC Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales; OC Thalassolituus. OX NCBI_TaxID=1298593 {ECO:0000313|EMBL:CCU73420.1, ECO:0000313|Proteomes:UP000011866}; RN [1] {ECO:0000313|EMBL:CCU73420.1, ECO:0000313|Proteomes:UP000011866} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MIL-1 {ECO:0000313|EMBL:CCU73420.1}; RX PubMed=23599290; DOI=10.1128/genomeA.00141-13; RA Golyshin P.N., Werner J., Chernikova T.N., Tran H., Ferrer M., RA Yakimov M.M., Teeling H., Golyshina O.V.; RT "Genome Sequence of Thalassolituus oleivorans MIL-1 (DSM 14913T)."; RL Genome Announc. 1:1-3(2013). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; HF680312; CCU73420.1; -; Genomic_DNA. DR RefSeq; WP_015488130.1; NC_020888.1. DR EnsemblBacteria; CCU73420; CCU73420; TOL_3024. DR KEGG; tol:TOL_3024; -. DR PATRIC; fig|1298593.3.peg.2923; -. DR KO; K03665; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000011866; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000011866}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000011866}. FT DOMAIN 200 368 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 437 AA; 49263 MW; 3B33D50367157935 CRC64; MFFDRPDNGG ETAVLVHVNF PEGANREDLN EFRELVISAG ADPVGLVTTK RPTPDAKTFV GRGKVEEIAE VVRLHGSELV IFNHSLSPSQ ERNLERALQC RVLDRTGLIL DIFAQRARTH EGKLQVELAQ LQYQSTRLIR GWTHLERQKG GIGMRGPGET QLETDRRLLR ERVKSINSRL EKVRAQRDQG RRSRKRSDVP TIAIVGYTNA GKSTLFNALT SSEVYAADQM FATLDPTIRR FQVGDVGEVV LADTVGFIRH LPHKLVESFR ATLQEAAEAT LLMHVIDCAA EERDGNIRQV ELVLGEIEAD EVPQLRVYNK IDLLEHGGEA RIDRDDMGVP VAVWLSAQKR LGFDLLNQAM GELLGEDVFD QEISLRPAEA KLRAILYEFG AIRNEAFADN GDIILNVRMQ RHDFKRALAR AEIAEQRFIK PVQEAWH // ID M5EQ50_9RHIZ Unreviewed; 464 AA. AC M5EQ50; DT 29-MAY-2013, integrated into UniProtKB/TrEMBL. DT 29-MAY-2013, sequence version 1. DT 07-JUN-2017, entry version 29. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:CCV06854.1}; GN ORFNames=MESS2_410017 {ECO:0000313|EMBL:CCV06854.1}; OS Mesorhizobium metallidurans STM 2683. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Phyllobacteriaceae; Mesorhizobium. OX NCBI_TaxID=1297569 {ECO:0000313|EMBL:CCV06854.1, ECO:0000313|Proteomes:UP000012062}; RN [1] {ECO:0000313|EMBL:CCV06854.1, ECO:0000313|Proteomes:UP000012062} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=STM 2683 {ECO:0000313|EMBL:CCV06854.1, RC ECO:0000313|Proteomes:UP000012062}; RA Genoscope - CEA; RL Submitted (FEB-2013) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:CCV06854.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CAUM01000108; CCV06854.1; -; Genomic_DNA. DR RefSeq; WP_008875751.1; NZ_CAUM01000108.1. DR EnsemblBacteria; CCV06854; CCV06854; MESS2_410017. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000012062; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000012062}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000012062}. FT DOMAIN 232 405 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 464 AA; 50808 MW; 2E1CCA4065F4D87D CRC64; MAREKDADHS VRGKKSSHQP GTEAKGPTRA VVIVPVLTRQ PRGDDETNRP RLTRSAEARH DEAVGLASAI DLDPIHTAVV TVNDPRPATL LGSGKVAEFA EIVKEGHAEL VIVDHPLTPV QQRNLEKELN AKVLDRTGLI LEIFGERART KEGTLQVELA HLNYQKGRLV RSWTHLERQR GGAGFLGGPG ETQIESDRRV LQDKIIKLKH ELETVRRTRD LHRAKRKKVP FPVVAIVGYT NAGKSTLFNR LTGAGVLAED MLFATLDPTL RRVRLPHGTP VILSDTVGFI SDLPTHLIAA FRATLEEVVE ADLVIHLRDI SDPDTAAQAE DVERILADLG VDADDTKRVI EVWNKIDRLD EGNQVRLLAD GADGKKAPPI AISAVTGEGI DALKAIIETR VSGELATLTI TLTPAQLGLV DWLYRNGDIV SRADNEDGSV TVSLKATQSA REEIESRLHR KNNG // ID M5J6Q6_9LACO Unreviewed; 418 AA. AC M5J6Q6; DT 29-MAY-2013, integrated into UniProtKB/TrEMBL. DT 29-MAY-2013, sequence version 1. DT 07-JUN-2017, entry version 30. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=D271_00658 {ECO:0000313|EMBL:EKW99600.1}; OS Lactobacillus saerimneri 30a. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; OC Lactobacillus. OX NCBI_TaxID=1227363 {ECO:0000313|EMBL:EKW99600.1, ECO:0000313|Proteomes:UP000011912}; RN [1] {ECO:0000313|EMBL:EKW99600.1, ECO:0000313|Proteomes:UP000011912} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=30a {ECO:0000313|EMBL:EKW99600.1, RC ECO:0000313|Proteomes:UP000011912}; RX PubMed=23405290; RA Romano A., Trip H., Campbell-Sills H., Bouchez O., Sherman D., RA Lolkema J.S., Lucas P.M.; RT "Genome Sequence of Lactobacillus saerimneri 30a (Formerly RT Lactobacillus sp. Strain 30a), a Reference Lactic Acid Bacterium RT Strain Producing Biogenic Amines."; RL Genome Announc. 1:E00097-12(2013). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EKW99600.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ANAG01000003; EKW99600.1; -; Genomic_DNA. DR RefSeq; WP_009551172.1; NZ_ANAG01000003.1. DR EnsemblBacteria; EKW99600; EKW99600; D271_00658. DR PATRIC; fig|1227363.6.peg.125; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000011912; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000011912}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000011912}. FT DOMAIN 197 365 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 156 183 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 418 AA; 45962 MW; C62D1CEAE652E99A CRC64; MTAVIIGGIE NQTENFTYTM EELQALAEAD NLEVVASVHQ KLERPVAATY FGAGKVTEIF QAGQVHAADA LIVNDELSPT QIRNLEQDTG LTVIDRTALI LDIFASRART KEAKLQVEIA KLQYQLPRLR TSAAEKLDQQ TAGNAGGGFT NRGAGETKLE LNRRVIEKQI SQLRKKLKDV QKDQVTQSKQ RRASGLPQVA LVGYTNAGKS TTMNGLLQLT GQEEDKQVFV KNMLFATLDT SVRKVHFADN KEFLLSDTVG FVSKLPHNLV AAFESTLAEA RNADLLVQVI DASDPHAREM IATTEETLAS IGIDDIPMIY AYNKADLANT RYPLVTGDAI TYSARDSQSL QVLADVIRQK IFTGYQTLTF LIPFAEGQLV QQLNEEAQII KTDYLATGTQ ITAEVSPQLA AQLQDYVQ // ID M5QZX3_9PSED Unreviewed; 433 AA. AC M5QZX3; DT 29-MAY-2013, integrated into UniProtKB/TrEMBL. DT 29-MAY-2013, sequence version 1. DT 30-AUG-2017, entry version 30. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=B195_03133 {ECO:0000313|EMBL:EMI08562.1}; OS Pseudomonas sp. Lz4W. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=1206777 {ECO:0000313|EMBL:EMI08562.1, ECO:0000313|Proteomes:UP000011925}; RN [1] {ECO:0000313|EMBL:EMI08562.1, ECO:0000313|Proteomes:UP000011925} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Lz4W {ECO:0000313|EMBL:EMI08562.1, RC ECO:0000313|Proteomes:UP000011925}; RX PubMed=23788547; RA Pandiyan A., Ray M.K.; RT "Draft Genome Sequence of the Antarctic Psychrophilic Bacterium RT Pseudomonas syringae Strain Lz4W."; RL Genome Announc. 1:E00377-13(2013). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EMI08562.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AOGS01000005; EMI08562.1; -; Genomic_DNA. DR RefSeq; WP_003439028.1; NZ_AOGS01000005.1. DR EnsemblBacteria; EMI08562; EMI08562; B195_03133. DR GeneID; 29351028; -. DR PATRIC; fig|1206777.3.peg.630; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000011925; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000011925}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000011925}. FT DOMAIN 199 366 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 433 AA; 48908 MW; 67850DC2B9C99C41 CRC64; MFFERHGGGE RAILVHLEGQ DPEAREDPQE FQELAVSAGA ETVAFFNVPR HRPSAKYLIG SGKVEELRDL VKAEKVDIVI FNHVLTPSQE RNLERVFECR VLDRTGLILD IFAQRARTHE GKLQVELAQL DHMSTRLVRG WTHLERQGGG IGMRGPGETQ LETDRRLLRV RISQIKARLK KVRSQREQSR RGRQRADIPT VSLVGYTNAG KSTLFNAVTG SDVFAADQLF ATLDPTLRRL DLADLGPIVL ADTVGFIRHL PHKLVEAFRS TLEESSNSDL LLHVIDAHEP ERMAQIEQVM VVLGEIGAQD LPILEVYNKI DLLEGVEPQI QRDADGKPQR VWLSAREGVG LELLEQAIAE LLGNDLFVGT LRLPQRFARL RAQFFELGVV QKEQHDEEGA CLLDVRLPRS ELNRLVSREG MQPLEFIEQH TLQ // ID M5R9Z5_9PLAN Unreviewed; 462 AA. AC M5R9Z5; DT 29-MAY-2013, integrated into UniProtKB/TrEMBL. DT 29-MAY-2013, sequence version 1. DT 07-JUN-2017, entry version 29. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=RMSM_06782 {ECO:0000313|EMBL:EMI16303.1}; OS Rhodopirellula maiorica SM1. OC Bacteria; Planctomycetes; Planctomycetia; Planctomycetales; OC Planctomycetaceae; Rhodopirellula. OX NCBI_TaxID=1265738 {ECO:0000313|EMBL:EMI16303.1, ECO:0000313|Proteomes:UP000011991}; RN [1] {ECO:0000313|EMBL:EMI16303.1, ECO:0000313|Proteomes:UP000011991} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SM1 {ECO:0000313|EMBL:EMI16303.1, RC ECO:0000313|Proteomes:UP000011991}; RX PubMed=23273849; RA Wegner C.E., Richter-Heitmann T., Klindworth A., Klockow C., RA Richter M., Achstetter T., Glockner F.O., Harder J.; RT "Expression of sulfatases in Rhodopirellula baltica and the diversity RT of sulfatases in the genus Rhodopirellula."; RL Mar. Genomics 0:0-0(2012). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EMI16303.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ANOG01000971; EMI16303.1; -; Genomic_DNA. DR RefSeq; WP_008707051.1; NZ_ANOG01000971.1. DR EnsemblBacteria; EMI16303; EMI16303; RMSM_06782. DR PATRIC; fig|1265738.3.peg.6777; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000011991; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000011991}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000011991}. FT DOMAIN 201 367 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 162 196 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 462 AA; 51405 MW; 1F8D949C1977E864 CRC64; MREQHQLRDD SPERSILARL ILPEQVVEAD PLEELYGLAT TAGTEVVDEL MQRLTRPNHG TFLGKGKVEE LRLMVERHDA DVVIFDNDLN PAQVRNLEKA IDAKVIDRTE LILDIFAAGA RTYEARLAIE LAQLEYSLPR LKRMWTHLSR QAMGVGMRGP GEKQLEVDRR LAQKRIHDLK EELSKVERRR EQQVQARKEA PTVSLVGYTN AGKSTLMNAL TAADVHAADK LFATLDTRTR RWQLPGWGTV LLSDTVGFIR DLPHSLVASF KSTLEETRQA DLLLHVADAS SPTVFEQISA VYRVLEELEI EEKDTLLVLN KIDAIKSSAV LNRVLDRYPN AIPVSAKSNT GLVPLIEAVG EALGREFFDL EVDVAPSDGK LLAYLAAKGE VLSRKYGEEM VTIHVRVPAG AMGPVHRDAV AIRYMDERLG KTNDNQSAED EKSSISIDLP SVPLSDSSSE VA // ID M5TTI4_9PLAN Unreviewed; 468 AA. AC M5TTI4; DT 29-MAY-2013, integrated into UniProtKB/TrEMBL. DT 29-MAY-2013, sequence version 1. DT 07-JUN-2017, entry version 28. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=RRSWK_00709 {ECO:0000313|EMBL:EMI47053.1}; OS Rhodopirellula sp. SWK7. OC Bacteria; Planctomycetes; Planctomycetia; Planctomycetales; OC Planctomycetaceae; Rhodopirellula. OX NCBI_TaxID=595460 {ECO:0000313|EMBL:EMI47053.1, ECO:0000313|Proteomes:UP000012028}; RN [1] {ECO:0000313|EMBL:EMI47053.1, ECO:0000313|Proteomes:UP000012028} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SWK7 {ECO:0000313|EMBL:EMI47053.1, RC ECO:0000313|Proteomes:UP000012028}; RX PubMed=23273849; RA Wegner C.E., Richter-Heitmann T., Klindworth A., Klockow C., RA Richter M., Achstetter T., Glockner F.O., Harder J.; RT "Expression of sulfatases in Rhodopirellula baltica and the diversity RT of sulfatases in the genus Rhodopirellula."; RL Mar. Genomics 0:0-0(2012). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EMI47053.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ANOQ01000012; EMI47053.1; -; Genomic_DNA. DR EnsemblBacteria; EMI47053; EMI47053; RRSWK_00709. DR PATRIC; fig|595460.3.peg.782; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000012028; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000012028}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000012028}. FT DOMAIN 207 373 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 168 195 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 468 AA; 51963 MW; CA64C6173C9DD660 CRC64; MSHQHKSSDL ISLVDDGPER SILARLILPG SVVEDDPLEE LHGLATTAGT EVVDELTQRR GTPDHSTYLG KGKVEELRLM VERHEAHVIF FDNDLSPAQV RNLEKATNAK VIDRTELILD IFAAGARTHE SRLAVELAQL EYSLPRLKRM WTHLSRQSMG VGMRGPGEKQ LEVDRRLAQK RIHDLKMELE KVESRRERQV AGRDELPTIS LVGYTNAGKS TLMNALTEAG VLAQDKLFAT LETRTRRWHL PNWGHVLLSD TVGFIRDLPH SLVASFKSTL EETRQADLLM HVADASSPNV FEQITAVFQV LEELAIQEKD TLLILNKIDS IQSPRILNRV LDRYPHAIPV SAKTGKGLIP LCEAVGEALS REFLDVEVDV SHHDGKLLAY LSAKGKVESR QFHDSHVTVR VRMPAAAMGE VNRSAMRITP THLKLADELA KPGVEAVSDT ESAQADAHDA DTPSSEVA // ID M5UBH7_9PLAN Unreviewed; 491 AA. AC M5UBH7; DT 29-MAY-2013, integrated into UniProtKB/TrEMBL. DT 29-MAY-2013, sequence version 1. DT 07-JUN-2017, entry version 28. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=RSSM_05208 {ECO:0000313|EMBL:EMI53358.1}; OS Rhodopirellula sallentina SM41. OC Bacteria; Planctomycetes; Planctomycetia; Planctomycetales; OC Planctomycetaceae; Rhodopirellula. OX NCBI_TaxID=1263870 {ECO:0000313|EMBL:EMI53358.1, ECO:0000313|Proteomes:UP000011885}; RN [1] {ECO:0000313|EMBL:EMI53358.1, ECO:0000313|Proteomes:UP000011885} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SM41 {ECO:0000313|EMBL:EMI53358.1, RC ECO:0000313|Proteomes:UP000011885}; RX PubMed=23273849; RA Wegner C.E., Richter-Heitmann T., Klindworth A., Klockow C., RA Richter M., Achstetter T., Glockner F.O., Harder J.; RT "Expression of sulfatases in Rhodopirellula baltica and the diversity RT of sulfatases in the genus Rhodopirellula."; RL Mar. Genomics 0:0-0(2012). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EMI53358.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ANOH01000361; EMI53358.1; -; Genomic_DNA. DR EnsemblBacteria; EMI53358; EMI53358; RSSM_05208. DR PATRIC; fig|1263870.3.peg.5511; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000011885; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000011885}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000011885}. FT DOMAIN 207 373 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 168 202 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 491 AA; 54690 MW; CCA468B5373EDF73 CRC64; MSHQHKSSDL ISLVDDGPER SILARLILPG SVVEDDPLEE LHGLATTAGT EVVDELTQRR GTPDHSTYLG KGKVEELRLM VERHDAHVIF FDNDLSPAQV RNLEKATNAK VIDRTELILD IFAAGARTHE SRLAVELAQL EYSLPRLKRM WTHLSRQSMG VGMRGPGEKQ LEVDRRLAQK RIHDLKVELE RVEARRERQV ASRDELPTIS LVGYTNAGKS TLMNALTEAE VLAQDKLFAT LETRTRRWHL PNWGHVLLSD TVGFIRDLPH SLVASFKSTL EETRQADLLM HVADASSPNV FEQITAVYQV LEDLGIQEKD TLLILNKIDS IRSPRVLNRV LDRYPHAIPV SAKTGKGLVP LCEAVGEALS REFLDVEVDV SHQDGKLLAY LSAKGKVESR EFHDSHVTVR VRMPAAAMGE VKRSAMRITP TRLTLADELG KTNGQPQSND ASSASEPDAD RSREPERQTG VAENDNQQNV DVRDSPSSEV A // ID M5XFM9_PRUPE Unreviewed; 552 AA. AC M5XFM9; DT 29-MAY-2013, integrated into UniProtKB/TrEMBL. DT 29-MAY-2013, sequence version 1. DT 07-JUN-2017, entry version 27. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EMJ24271.1}; GN ORFNames=PRUPE_ppa003744mg {ECO:0000313|EMBL:EMJ24271.1}; OS Prunus persica (Peach) (Amygdalus persica). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae; OC Pentapetalae; rosids; fabids; Rosales; Rosaceae; Maloideae; OC Amygdaleae; Prunus. OX NCBI_TaxID=3760 {ECO:0000313|EMBL:EMJ24271.1, ECO:0000313|Proteomes:UP000006882}; RN [1] {ECO:0000313|Proteomes:UP000006882} RP NUCLEOTIDE SEQUENCE. RC STRAIN=cv. Nemared {ECO:0000313|Proteomes:UP000006882}; RX PubMed=23525075; DOI=10.1038/ng.2586; RA Verde I., Abbott A.G., Scalabrin S., Jung S., Shu S., Marroni F., RA Zhebentyayeva T., Dettori M.T., Grimwood J., Cattonaro F., Zuccolo A., RA Rossini L., Jenkins J., Vendramin E., Meisel L.A., Decroocq V., RA Sosinski B., Prochnik S., Mitros T., Policriti A., Cipriani G., RA Dondini L., Ficklin S., Goodstein D.M., Xuan P., Del Fabbro C., RA Aramini V., Copetti D., Gonzalez S., Horner D.S., Falchi R., Lucas S., RA Mica E., Maldonado J., Lazzari B., Bielenberg D., Pirona R., RA Miculan M., Barakat A., Testolin R., Stella A., Tartarini S., RA Tonutti P., Arus P., Orellana A., Wells C., Main D., Vizzotto G., RA Silva H., Salamini F., Schmutz J., Morgante M., Rokhsar D.S.; RT "The high-quality draft genome of peach (Prunus persica) identifies RT unique patterns of genetic diversity, domestication and genome RT evolution."; RL Nat. Genet. 45:487-494(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; KB638913; EMJ24271.1; -; Genomic_DNA. DR RefSeq; XP_007223072.1; XM_007223010.1. DR EnsemblPlants; EMJ24271; EMJ24271; PRUPE_ppa003744mg. DR GeneID; 18789218; -. DR Gramene; EMJ24271; EMJ24271; PRUPE_ppa003744mg. DR KEGG; pper:PRUPE_ppa003744mg; -. DR KO; K03665; -. DR OMA; VILEIFH; -. DR OrthoDB; EOG093609UJ; -. DR Proteomes; UP000006882; Unassembled WGS sequence. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000006882}; KW Reference proteome {ECO:0000313|Proteomes:UP000006882}. FT DOMAIN 329 495 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 552 AA; 61305 MW; 2A16D70A460F7023 CRC64; MSACFSCSLI RSSPLIQDPY LSWPLAKLVR PISSLRLRKY SSASPRIVVR AIEQGLGVVS TDDVSLLQDP PLIDVDTIEF VNEEVHGVID GVADTKSEDE ALTPSTRVKK KKEVEDSSES RFKLRNGREI FEEKAYVVGV EHKRSNTEVL FGVEESLKEL TQLADTAGLM VVGSTYQKLV SPNSRTYIGS GKVAEIKSAI NALGVETVIF DDELSAGQLR NLEKAFGGEV RVCDRTALIL DIFNQRAATH EAALQVALAQ MEYQLPRLTK MWTHLERQAG GKVKGMGEKQ IEVDKRILRT QIGVLKKELE SVRKHRKQYR NQRLSVPVPV VSLVGYTNAG KSTLLNQLTG ANVMAEDRLF ATLDPTTRRV QTKNGKEFLL TDTVGFIQKL PTTVVAAFRA TLEEISESSL LVHVVDISHP LAEQQINAVD KVLSELDVSS IPRLMVWNKV DKVSNPESIK LEAEKRDDVV CISALSGEGV NEFCNAVQEK LKDSMVWVEA LIPFEKGELL STIHKVGMVE RTEHTDKGTL IKAHVPLRYA RLLTPLRQLC IS // ID M6RIY0_LEPIR Unreviewed; 516 AA. AC M6RIY0; DT 29-MAY-2013, integrated into UniProtKB/TrEMBL. DT 29-MAY-2013, sequence version 1. DT 30-AUG-2017, entry version 30. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:EMO05751.1}; GN ORFNames=LEP1GSC116_2833 {ECO:0000313|EMBL:EMO05751.1}; OS Leptospira interrogans serovar Icterohaemorrhagiae str. Verdun HP. OC Bacteria; Spirochaetes; Leptospirales; Leptospiraceae; Leptospira. OX NCBI_TaxID=1049910 {ECO:0000313|EMBL:EMO05751.1, ECO:0000313|Proteomes:UP000012092}; RN [1] {ECO:0000313|EMBL:EMO05751.1, ECO:0000313|Proteomes:UP000012092} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Verdun HP {ECO:0000313|EMBL:EMO05751.1, RC ECO:0000313|Proteomes:UP000012092}; RA Harkins D.M., Durkin A.S., Brinkac L.M., Haft D.H., Selengut J.D., RA Sanka R., DePew J., Purushe J., Picardeau M., Werts C., Goarant C., RA Vinetz J.M., Sutton G.G., Nierman W.C., Fouts D.E.; RL Submitted (JAN-2013) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EMO05751.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AHNZ02000376; EMO05751.1; -; Genomic_DNA. DR EnsemblBacteria; EMO05751; EMO05751; LEP1GSC116_2833. DR Proteomes; UP000012092; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000012092}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}. FT DOMAIN 313 505 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 279 306 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 516 AA; 58750 MW; 9949439C7FDB87FB CRC64; MGSDNSIEIP FLDRLRISEA RLRGLRLVHT HLKGEPLNQE DLTDLALLRL DYFTAIVMDH FGNPNGYYSA HLNPESEDEL WTVLPKQYPG QLTEGILEEI LEIESRLSRS KKNLKDAQKE NRAFLVGVYP ERNVGRHPSL SMEELKELCK TAEVHVVDTF IQRKNRLDPS TVLGKGKLEE IILKAIQKHV ELLVFDLELT PSQAKKISDI ADIKVIDRTQ LILDIFARNA KSRDGKLQVE LAQLKYLKGR LTELDDNMSR LTGGIGGRGP GETKLEIGKR RVEERITRLE VELKSLKKRR EINRRQRKKN ELPAVGIVGY TNAGKSTFLN ALTNSEVLSE NKLFATLDPT TRRIRFPEER EIIISDTVGF IHDLPPELSN AFKATLEELG DSDLLVHVVD VSNPDYKLQM EAVEKILEEL ELSHIPMIQV FNKIDRLEKF KIWVIENGYK KSSSVDHGPG LEAITDLKEE LGIDTFSDSI LVSAFQGWGL KTFLDLLEDR IYNLSRSNYS NTSSVY // ID M6T6G2_LEPIR Unreviewed; 522 AA. AC M6T6G2; DT 29-MAY-2013, integrated into UniProtKB/TrEMBL. DT 29-MAY-2013, sequence version 1. DT 07-JUN-2017, entry version 29. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:EMO26191.1}; GN ORFNames=LEP1GSC170_4424 {ECO:0000313|EMBL:EMO26191.1}; OS Leptospira interrogans serovar Bataviae str. HAI135. OC Bacteria; Spirochaetes; Leptospirales; Leptospiraceae; Leptospira. OX NCBI_TaxID=1085538 {ECO:0000313|EMBL:EMO26191.1, ECO:0000313|Proteomes:UP000012139}; RN [1] {ECO:0000313|EMBL:EMO26191.1, ECO:0000313|Proteomes:UP000012139} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=HAI135 {ECO:0000313|EMBL:EMO26191.1, RC ECO:0000313|Proteomes:UP000012139}; RA Harkins D.M., Durkin A.S., Brinkac L.M., Haft D.H., Selengut J.D., RA Sanka R., DePew J., Purushe J., Matthias M.A., Vinetz J.M., RA Sutton G.G., Nierman W.C., Fouts D.E.; RL Submitted (JAN-2013) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EMO26191.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AHOI02000519; EMO26191.1; -; Genomic_DNA. DR EnsemblBacteria; EMO26191; EMO26191; LEP1GSC170_4424. DR Proteomes; UP000012139; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 2. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 2. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000012139}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000012139}. FT DOMAIN 314 511 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 280 307 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 522 AA; 59316 MW; 1DA6E4272AD31B81 CRC64; MVGSDNSIEI PFLDRLRTSE ARLRGLRLVH THLKGESLNQ EDLTDLALLR LDYFTAIVMD PSGNPNGYYS AHLNPESEDE LWTVLPKQYP GQLTEGILEE ILEIESRLSR SKKNLKDAQK ENRAFLVGVY PERNVGRHPS LSMEELKELC KTAEVHVVDT FIQRKNRLDP STVLGKGKLE EIILKAIQKH VELLVFDLEL TPSQAKKISD IADIKVIDRT QLILDIFARN AKSRDGKLQV ELAQLKYLKG RLTELDDNMS RLTGGIGGRG PGETKLEIGK RRVEERITRL EVELKSLKKR REINRRQRKK NELPAVGIVG YTNAGKSTFL NALTNSEVLS ENKLFATLDP TTRRIRFPEE REIIISDTVG FIHDLPPELS NAFKATLEEL RDSDLLVHVV DISNPDYKLQ MEAVEKILEE LELSHIPLIQ VFNKIDRLEK FKIWAIENNS NGYKKSSFPS VNHGPGLEAI SDFKEDLGMD HLSDSVLVSA FQGWGLKTFL DLLEERIYSL SRSNDSNVSS IY // ID M7MHL2_9FLAO Unreviewed; 403 AA. AC M7MHL2; DT 29-MAY-2013, integrated into UniProtKB/TrEMBL. DT 29-MAY-2013, sequence version 1. DT 07-JUN-2017, entry version 29. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=D778_01627 {ECO:0000313|EMBL:EMQ95737.1}; OS Xanthomarina gelatinilytica. OC Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales; OC Flavobacteriaceae; Xanthomarina. OX NCBI_TaxID=1137281 {ECO:0000313|EMBL:EMQ95737.1, ECO:0000313|Proteomes:UP000012024}; RN [1] {ECO:0000313|EMBL:EMQ95737.1, ECO:0000313|Proteomes:UP000012024} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=AK20 {ECO:0000313|EMBL:EMQ95737.1, RC ECO:0000313|Proteomes:UP000012024}; RA Kumar R., Khatri I., Vaidya B., Subramanian S., Pinnaka A.; RT "Genome assembly of Formosa sp. AK20."; RL Submitted (DEC-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EMQ95737.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ANLA01000004; EMQ95737.1; -; Genomic_DNA. DR RefSeq; WP_007646902.1; NZ_ANLA01000004.1. DR EnsemblBacteria; EMQ95737; EMQ95737; D778_01627. DR PATRIC; fig|1137281.3.peg.226; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000012024; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000012024}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000012024}. FT DOMAIN 200 385 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 403 AA; 46366 MW; 6859D89AF3A29D44 CRC64; MIEKKDIALE RAVLIGVVTK EQDEAKSKEY LDELEFLTYT AGGEVVKRFT QKMDMPNPKT FIGTGKIEDV RVFISENDIG TAIFDDELSA AQERNISKIL GCKVLDRTNL ILDIFAQRAQ TSYARTQVEL AQCEYLLPRL KGMWTHLERQ KGGIGMRGPG ETEIETDRRI VRDKIALLKD KIKTIDKQMA VQRGNRGKMV RVALVGYTNV GKSTLMNVIS KSDVFAENKL FATLDTTVRK VVIQNLPFLL SDTVGFIRKL PTQLVESFKS TLDEVREADL LLHIVDISHP NFEHHIESVN KILGEIDSSD KPTIMVFNKI DAYKPEPFDE TDLETERTEA NYTLQEWKKT WMNRVGNNAL FISALNKENM DDFKKRVYDE VREIHVTRFP YNHFLYPDYN EEE // ID M7MRA2_9MICC Unreviewed; 558 AA. AC M7MRA2; DT 29-MAY-2013, integrated into UniProtKB/TrEMBL. DT 29-MAY-2013, sequence version 1. DT 07-JUN-2017, entry version 31. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=ADIAG_03265 {ECO:0000313|EMBL:EMQ97470.1}; OS Paeniglutamicibacter gangotriensis Lz1y. OC Bacteria; Actinobacteria; Micrococcales; Micrococcaceae; OC Paeniglutamicibacter. OX NCBI_TaxID=1276920 {ECO:0000313|EMBL:EMQ97470.1, ECO:0000313|Proteomes:UP000012015}; RN [1] {ECO:0000313|EMBL:EMQ97470.1, ECO:0000313|Proteomes:UP000012015} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Lz1y {ECO:0000313|EMBL:EMQ97470.1, RC ECO:0000313|Proteomes:UP000012015}; RX PubMed=23766407; RA Shivaji S., Ara S., Bandi S., Singh A., Kumar Pinnaka A.; RT "Draft Genome Sequence of Arthrobacter gangotriensis Strain Lz1yT, RT Isolated from a Penguin Rookery Soil Sample Collected in Antarctica, RT near the Indian Station Dakshin Gangotri."; RL Genome Announc. 1:e00347-13(2013). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EMQ97470.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AOCK01000010; EMQ97470.1; -; Genomic_DNA. DR EnsemblBacteria; EMQ97470; EMQ97470; ADIAG_03265. DR PATRIC; fig|1276920.7.peg.3270; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000012015; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000012015}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000012015}. FT DOMAIN 337 502 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 558 AA; 60643 MW; 0D7B1C9B443ED546 CRC64; MQTPHEHPEQ HNPSTPKGAS DGAGHYSGIQ QAKGNMTNPQ PSGPQDNDLD EAQLQAAIER ILASDAAAAN QASHFGAPED EKILTGRAQA LDKSTREHSS FDGDQEELAA RRALRRSASL STELDDVTEV ENRQLRLERV VLAGIWNEGT AEDAENSLRE LAALAETAGS EVLDGMVQRR AKPDANTYLG SGKAQELREV VAATGADTVI IDTELAPSQR RALEDVVQVK VIDRTALILD IFAQHAKSHE GRAQVELAQL EYLLPRLRGW GESMSRQAGG RVGTAGGGIG SRGPGETKIE LDRRRIRDRM AKLRKEIKGM LPAREAKRAN RKRNSVPSVA IAGYTNAGKS SLLNRLTNAG ALVENALFAT LDPTVRQTET EDGLTYTLAD TVGFVKSLPT QLVEAFRSTL EEVADADLIL HVVDAAHPDP EGQIQAVREV LNDVDARRIP ELIVLNKADV ADPFVVERLR QHEPNHVIVS ARTGEGIGEL LEKISAAIPR PDVQLELMIP YDRGDVVNRL HGAEAEILAV EHTETGTRMM VKVRKSMAAE VEQFSIHG // ID M7N6J4_9BACT Unreviewed; 400 AA. AC M7N6J4; DT 29-MAY-2013, integrated into UniProtKB/TrEMBL. DT 29-MAY-2013, sequence version 1. DT 07-JUN-2017, entry version 29. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:EMR02841.1}; GN ORFNames=ADICEAN_02049 {ECO:0000313|EMBL:EMR02841.1}; OS Cesiribacter andamanensis AMV16. OC Bacteria; Bacteroidetes; Cytophagia; Cytophagales; Flammeovirgaceae; OC Cesiribacter. OX NCBI_TaxID=1279009 {ECO:0000313|EMBL:EMR02841.1, ECO:0000313|Proteomes:UP000011910}; RN [1] {ECO:0000313|EMBL:EMR02841.1, ECO:0000313|Proteomes:UP000011910} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=AMV16 {ECO:0000313|EMBL:EMR02841.1, RC ECO:0000313|Proteomes:UP000011910}; RX PubMed=23682146; RA Shivaji S., Ara S., Begum Z., Srinivas T.N., Singh A., RA Kumar Pinnaka A.; RT "Draft Genome Sequence of Cesiribacter andamanensis Strain AMV16T, RT Isolated from a Soil Sample from a Mud Volcano in the Andaman Islands, RT India."; RL Genome Announc. 1:E00240-13(2013). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EMR02841.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AODQ01000044; EMR02841.1; -; Genomic_DNA. DR RefSeq; WP_009195444.1; NZ_AODQ01000044.1. DR EnsemblBacteria; EMR02841; EMR02841; ADICEAN_02049. DR PATRIC; fig|1279009.4.peg.2078; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000011910; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000011910}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000011910}. FT DOMAIN 202 375 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 170 197 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 400 AA; 45664 MW; 30ED2AD2ED0F550F CRC64; MIEPISTAPK IETAVLVALV TPKQSSQQAK EYLEELAFLA ETSGVQTLKT FTQRLERPDI RSFVGKGKLE EVKAYVQEHE VDIVIFDDEL TPSQVRNLEG ELKCKILDRS LLILNIFSVR AKTAQAKAQV ELAQYQFILP RLTRMWTHLT KQKGGVGMRG PGERELETDR RIVRDRIAFL REKLDKIERQ SETQRKQRHK MVRVALVGYT NVGKSTLMQL LSKSDVFAEN KLFATVDSTV RKVVLEGIPF LLTDTVGFIR KLPHTLVECF KSTLDEIREA DILLHVVDIS HGASHEQIEV VNSTLAEIGA GDKPMIMVYN KVDALPEEER QELLEAGVPE PSEQPIADRV FISALNRENI DSLRRKLSEQ VEKRHFQIFP NYLKPQVYDG QWSYDGEEEE // ID M7NXU4_9GAMM Unreviewed; 381 AA. AC M7NXU4; DT 29-MAY-2013, integrated into UniProtKB/TrEMBL. DT 29-MAY-2013, sequence version 1. DT 07-JUN-2017, entry version 29. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=MPL1_04170 {ECO:0000313|EMBL:EMR13618.1}; OS Methylophaga lonarensis MPL. OC Bacteria; Proteobacteria; Gammaproteobacteria; Thiotrichales; OC Piscirickettsiaceae; Methylophaga. OX NCBI_TaxID=1286106 {ECO:0000313|EMBL:EMR13618.1, ECO:0000313|Proteomes:UP000012019}; RN [1] {ECO:0000313|EMBL:EMR13618.1, ECO:0000313|Proteomes:UP000012019} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MPL {ECO:0000313|EMBL:EMR13618.1, RC ECO:0000313|Proteomes:UP000012019}; RX PubMed=23661481; RA Shetty S.A., Marathe N.P., Munot H., Antony C.P., Dhotre D.P., RA Murrell J.C., Shouche Y.S.; RT "Draft Genome Sequence of Methylophaga lonarensis MPLT, a RT Haloalkaliphilic (Non-Methane-Utilizing) Methylotroph."; RL Genome Announc. 1:E00202-13(2013). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EMR13618.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; APHR01000018; EMR13618.1; -; Genomic_DNA. DR RefSeq; WP_009725856.1; NZ_APHR01000018.1. DR EnsemblBacteria; EMR13618; EMR13618; MPL1_04170. DR PATRIC; fig|1286106.3.peg.835; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000012019; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000012019}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000012019}. FT DOMAIN 207 374 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 166 200 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 381 AA; 42999 MW; AB52D5383C2A6D6A CRC64; MFERPNSDAA FHEKSDREAV VLVHLDFNDS DYDETRQEFI ELVNGTGARI AAVTSGKRQR PDPRYFAGTG KVDEIAEQVL ASNAALVIFN HELSPSQERN LEQKLQCRVL GRTGLILDIF ARRARSHEGK LQVELAQLQH LSTRLVRGWT HLERQKGGIG LRGPGETQLE TDRRLLAQRI KSLKKRLDKV RSQREQGRRS RQRGGVPVVS LVGYTNMGKS TLFNRMTSAE VYADNRLFAT LDPTLRRLRL AGTEPLVLAD TVGFIRDLPH DLVESFSSTL EETRDAALLL HVVDAASSER ESLISHVDEV LSQIGADEVP QVIIYNKIDR LEGVSAKLER NQDGQIHRIW LSAHTGEGLE YLRQALQEYF PEHELQQASS D // ID M7NZI3_9BACL Unreviewed; 425 AA. AC M7NZI3; DT 29-MAY-2013, integrated into UniProtKB/TrEMBL. DT 29-MAY-2013, sequence version 1. DT 07-JUN-2017, entry version 30. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:EMR07085.1}; GN ORFNames=C772_00730 {ECO:0000313|EMBL:EMR07085.1}; OS Bhargavaea cecembensis DSE10. OC Bacteria; Firmicutes; Bacilli; Bacillales; Planococcaceae; Bhargavaea. OX NCBI_TaxID=1235279 {ECO:0000313|EMBL:EMR07085.1, ECO:0000313|Proteomes:UP000011919}; RN [1] {ECO:0000313|EMBL:EMR07085.1, ECO:0000313|Proteomes:UP000011919} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSE10 {ECO:0000313|EMBL:EMR07085.1, RC ECO:0000313|Proteomes:UP000011919}; RX PubMed=23766406; RA Shivaji S., Ara S., Begum Z., Ruth M., Singh A., Kumar Pinnaka A.; RT "Draft Genome Sequence of Bhargavaea cecembensis Strain DSE10T, RT Isolated from a Deep-Sea Sediment Sample Collected at a Depth of 5,904 RT m from the Chagos-Laccadive Ridge System in the Indian Ocean."; RL Genome Announc. 1:e00346-13(2013). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EMR07085.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AOFT01000003; EMR07085.1; -; Genomic_DNA. DR RefSeq; WP_008297515.1; NZ_AOFT01000003.1. DR EnsemblBacteria; EMR07085; EMR07085; C772_00730. DR PATRIC; fig|1235279.3.peg.745; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000011919; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000011919}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000011919}. FT DOMAIN 200 368 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 159 193 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 425 AA; 47880 MW; 3CD1FE7374DACD74 CRC64; MEETLERAVL VGVHLDDDEQ FNYSMEELAN LAEACGVEVS GIVTQNLERP NPSHYIGSGK VKEILMFHDE TDSNLVIFND ELSPSQIRNL ETELDTKVID RTMLILDIFA RRAKTREAQL QVELAQLQYM LPRLVGLRAS LSRQAGSTGG GVATRGPGET KLELDRRRIE DQIARLRREL DSVKSHRETQ RKRRVKRDVP VVSLVGYTNA GKSTIMNSML AGIGDGAGRH VLERDMLFAT LDTSVRNIHL QDNREFLLTD TVGFVGKLPH HLVKAFRSTL EEAADADLLL HVVDVSHPEH RYMMDVTEDT LADIGIEGIP EVHVYNKSDL AGLEHPRKQG NSIWISAKDA GDIRTLTEMI AAKIFGDYVR VRLLIPFDRG DVVSYLNEHA DVKDTEYTEA GTLMDVEIRE ADRNRFREFL APSEE // ID M7TCR7_9EURY Unreviewed; 427 AA. AC M7TCR7; DT 29-MAY-2013, integrated into UniProtKB/TrEMBL. DT 29-MAY-2013, sequence version 1. DT 07-JUN-2017, entry version 28. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=MBGDN05_00868 {ECO:0000313|EMBL:EMR74427.1}; OS Thermoplasmatales archaeon SCGC AB-539-N05. OC Archaea; Euryarchaeota; Thermoplasmata; Thermoplasmatales. OX NCBI_TaxID=1198116 {ECO:0000313|EMBL:EMR74427.1, ECO:0000313|Proteomes:UP000053781}; RN [1] {ECO:0000313|EMBL:EMR74427.1, ECO:0000313|Proteomes:UP000053781} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SCGC AB-539-N05 {ECO:0000313|EMBL:EMR74427.1}; RX PubMed=23535597; DOI=10.1038/nature12033; RA Lloyd K.G., Schreiber L., Petersen D.G., Kjeldsen K.U., Lever M.A., RA Steen A.D., Stepanauskas R., Richter M., Kleindienst S., Lenk S., RA Schramm A., Jorgensen B.B.; RT "Predominant archaea in marine sediments degrade detrital proteins."; RL Nature 496:215-218(2013). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EMR74427.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ALXL01000004; EMR74427.1; -; Genomic_DNA. DR EnsemblBacteria; EMR74427; EMR74427; MBGDN05_00868. DR PATRIC; fig|1198116.5.peg.20; -. DR Proteomes; UP000053781; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000053781}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Hydrolase {ECO:0000313|EMBL:EMR74427.1}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000053781}. FT DOMAIN 189 362 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 427 AA; 48839 MW; C3E9F96EB2177F75 CRC64; MTGNQNNAIV VSLNSDVSEI IELANSLDYN VVETFFQHLE KPDVKSYVGS GKVDEIKEFV KDAEKDIVLV IVDGELKPSQ WFTLEKKLNV EVYDRVRLIL AIFAERADRK EARLQVKLAQ LQYERPFVRE LIHRARSGEH PGLMAGGEYQ VDDYYEMIKK QVKKIKEELE GMRNSREIRR RHRHIGGFYL VSLAGYTNAG KSSLLNLLSD EKVKVEGKLF STLSTTTRRI KNKNIPVLIT DTVGFIKNLP ALIIDAFHST LEEIEVADVV LLIADVSEEK ELVANKLKTS LDELVEINVN SSIVVVLNKT DLISTDELFS RTEYLKNRGL LEDKEVVTIS SKNRENVNEL LSVIYKSLPQ LVSFKIKLPV NEDTQSFISW IYERAFVSDI FYDEFVTLSI ACNPKMHEKI VFKCKNLKGF VVDRLVF // ID M7Y1S6_9BACT Unreviewed; 421 AA. AC M7Y1S6; DT 29-MAY-2013, integrated into UniProtKB/TrEMBL. DT 29-MAY-2013, sequence version 1. DT 07-JUN-2017, entry version 29. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=C943_03379 {ECO:0000313|EMBL:EMS34692.1}; OS Mariniradius saccharolyticus AK6. OC Bacteria; Bacteroidetes; Cytophagia; Cytophagales; Cyclobacteriaceae; OC Mariniradius. OX NCBI_TaxID=1239962 {ECO:0000313|EMBL:EMS34692.1, ECO:0000313|Proteomes:UP000010953}; RN [1] {ECO:0000313|EMBL:EMS34692.1, ECO:0000313|Proteomes:UP000010953} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=AK6 {ECO:0000313|EMBL:EMS34692.1, RC ECO:0000313|Proteomes:UP000010953}; RA Vaidya B., Khatri I., Tanuku N.R.S., Subramanian S., Pinnaka A.; RT "Genome assembly of Mariniradius saccharolyticus AK6."; RL Submitted (JAN-2013) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EMS34692.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AMZY02000005; EMS34692.1; -; Genomic_DNA. DR RefSeq; WP_008624297.1; NZ_AMZY02000005.1. DR EnsemblBacteria; EMS34692; EMS34692; C943_03379. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000010953; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 2. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000010953}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000010953}. FT DOMAIN 210 399 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 421 AA; 48219 MW; 54DEE4B2AC706777 CRC64; MSKLSRKLQK LYDTAPLQET AVLVALIRQG QTEQQANEYL DELAFLTETL GAKTVYKFTQ RLERPDVRTF VGSGKLEEIQ SYVEHFAVDM VIFDDDLSPS QMRNLENELK VKVYDRSLLI LDIFLKRAQT AQAKTQVELA RFQYLLPRLT RMWTHLERQR GGTGTRGGAG EKEIETDKRD IRNKIALLKT KLKEIEKQGL TQRKSRKGIV RVALVGYTNV GKSTLMNLIT KSDILAENKL FATVDSTVRK VVLENIPFLL SDTVGFIRKL PTHLIESFKS TLDEIREADL LIHVVDISHP NFEDHISVVN ETLNEIGAGD KPIFLVFNKM DLVPPKPSEE EMMHMTEHEL QEKRYLDFEQ LATAYGKKTG IAPIFMSAHN GGNVELFRQG LIKEVKKQHL KIYPHYLENE VVDFSAFENL D // ID M7YFH2_TRIUA Unreviewed; 365 AA. AC M7YFH2; DT 29-MAY-2013, integrated into UniProtKB/TrEMBL. DT 29-MAY-2013, sequence version 1. DT 30-AUG-2017, entry version 27. DE SubName: Full=GTP-binding protein hflX {ECO:0000313|EMBL:EMS49063.1, ECO:0000313|EnsemblPlants:TRIUR3_05480-P1}; GN ORFNames=TRIUR3_05480 {ECO:0000313|EMBL:EMS49063.1}; OS Triticum urartu (Red wild einkorn) (Crithodium urartu). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; BOP clade; OC Pooideae; Triticodae; Triticeae; Triticinae; Triticum. OX NCBI_TaxID=4572 {ECO:0000313|EMBL:EMS49063.1}; RN [1] {ECO:0000313|EMBL:EMS49063.1, ECO:0000313|EnsemblPlants:TRIUR3_05480-P1, ECO:0000313|Proteomes:UP000015106} RP NUCLEOTIDE SEQUENCE. RC STRAIN=cv. G1812 {ECO:0000313|EnsemblPlants:TRIUR3_05480-P1}; RX PubMed=23535596; DOI=10.1038/nature11997; RA Ling H.Q., Zhao S., Liu D., Wang J., Sun H., Zhang C., Fan H., Li D., RA Dong L., Tao Y., Gao C., Wu H., Li Y., Cui Y., Guo X., Zheng S., RA Wang B., Yu K., Liang Q., Yang W., Lou X., Chen J., Feng M., Jian J., RA Zhang X., Luo G., Jiang Y., Liu J., Wang Z., Sha Y., Zhang B., Wu H., RA Tang D., Shen Q., Xue P., Zou S., Wang X., Liu X., Wang F., Yang Y., RA An X., Dong Z., Zhang K., Zhang X., Luo M.C., Dvorak J., Tong Y., RA Wang J., Yang H., Li Z., Wang D., Zhang A., Wang J.; RT "Draft genome of the wheat A-genome progenitor Triticum urartu."; RL Nature 496:87-90(2013). RN [2] {ECO:0000313|EnsemblPlants:TRIUR3_05480-P1} RP IDENTIFICATION. RG EnsemblPlants; RL Submitted (JUN-2015) to UniProtKB. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; KD247328; EMS49063.1; -; Genomic_DNA. DR EnsemblPlants; TRIUR3_05480-T1; TRIUR3_05480-P1; TRIUR3_05480. DR Gramene; TRIUR3_05480-T1; TRIUR3_05480-P1; TRIUR3_05480. DR OrthoDB; EOG093609UJ; -. DR Proteomes; UP000015106; Unassembled WGS sequence. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000015106}; KW Reference proteome {ECO:0000313|Proteomes:UP000015106}. FT DOMAIN 222 365 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 188 215 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 365 AA; 40273 MW; C15B7CC52B2C9BF3 CRC64; MRSLSAAEED TATRPRSRFS EWQQRKAGGM LSLSHLVGAA EEDRRATAHA RGGGEEDGRE EGGRGPAGGG RLSSPNPRTY IGSGKVAEIR SAVQALDIET IIFDDELSAG QLRNLEKSFG GGVRVCDRTA LILDIFNQRA ATHEAALQVT LAQMEYQLPR LTKLWTHLER QSGGQVKGMG EKQIEVDKRI LRTQISTLRK ELESVRKHRK LYRNRRRSVP IPVVSLVGYT NAGKSTLLNR LTGADVLAED KLFATLDPTT RRVLMKSGTE FLLTDTVGFI QKLPTMLVAA FRATLEEISE SSIIVHLADI SHPLAQQQIG AVDKVLKELD IDSVPKLVVW NKIRIMFDAL VLSILAPRSI IKPAQ // ID M8E454_9BACL Unreviewed; 442 AA. AC M8E454; DT 29-MAY-2013, integrated into UniProtKB/TrEMBL. DT 29-MAY-2013, sequence version 1. DT 07-JUN-2017, entry version 28. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=I532_00630 {ECO:0000313|EMBL:EMT54066.1}; OS Brevibacillus borstelensis AK1. OC Bacteria; Firmicutes; Bacilli; Bacillales; Paenibacillaceae; OC Brevibacillus. OX NCBI_TaxID=1300222 {ECO:0000313|EMBL:EMT54066.1, ECO:0000313|Proteomes:UP000012081}; RN [1] {ECO:0000313|EMBL:EMT54066.1, ECO:0000313|Proteomes:UP000012081} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=AK1 {ECO:0000313|EMBL:EMT54066.1, RC ECO:0000313|Proteomes:UP000012081}; RA Rajan I., PoliReddy D., Sugumar T., Rathinam K., Alqarawi S., RA Khalil A.B., Sivakumar N.; RT "Assembly of a new bacterial strain Brevibacillus borstelensis AK1."; RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EMT54066.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; APBN01000001; EMT54066.1; -; Genomic_DNA. DR RefSeq; WP_003385742.1; NZ_APBN01000001.1. DR EnsemblBacteria; EMT54066; EMT54066; I532_00630. DR PATRIC; fig|1300222.3.peg.134; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000012081; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000012081}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000012081}. FT DOMAIN 213 375 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 172 206 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 442 AA; 50502 MW; 9D8A7A039BE67D62 CRC64; MWYDRGKKGR DSLEGGIKTK ETAILVGCFL DNRDMERSRL SMEELHELAR TADVEVLDVI TQNRERIDNA WYLGSGKIQE IAHRAEELDV DVIIFNDELS PSQTRNLDTA FDCKVIDRTQ LILDIFAGRA HSREGKIQVE LAQYNYLLPR LAGQGKQLSR LGGGIGTRGP GETKLESDRR HIRRRISELK QQLSELVRTR QLHRERRKKN NVFQIALVGY TNAGKSTLLN QLTSAETLQE DKLFATLDPT TRQLTLPSGL EVLLTDTVGF IQDLPTSLVA AFRSTLEGVK EADLILHVVD AHHPDLEIHM EVVYRILREL KADDIPQLVV YNKADLIMEG TYLPKVEDSI LISAIRAEDR AELLKRIEAY VYSSFDRYTL IVPAERGDIL SLLHREGVEM EQEFDEADSS YRISVRVNRD HPIYGRIAPF LLEKPETEEE SW // ID M9L828_PAEPP Unreviewed; 399 AA. AC M9L828; DT 29-MAY-2013, integrated into UniProtKB/TrEMBL. DT 29-MAY-2013, sequence version 1. DT 10-MAY-2017, entry version 29. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=PPOP_0582 {ECO:0000313|EMBL:GAC41232.1}; OS Paenibacillus popilliae ATCC 14706. OC Bacteria; Firmicutes; Bacilli; Bacillales; Paenibacillaceae; OC Paenibacillus. OX NCBI_TaxID=1212764 {ECO:0000313|EMBL:GAC41232.1, ECO:0000313|Proteomes:UP000029453}; RN [1] {ECO:0000313|EMBL:GAC41232.1, ECO:0000313|Proteomes:UP000029453} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 14706 {ECO:0000313|EMBL:GAC41232.1, RC ECO:0000313|Proteomes:UP000029453}; RA Iiyama K., Mori K., Mon H., Chieda Y., Lee J.M., Kusakabe T., RA Tashiro K., Asano S., Yasunaga-Aoki C., Shimizu S.; RT "Draft Genome Sequence of Paenibacillus popilliae ATCC 14706T."; RL Submitted (OCT-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:GAC41232.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BALG01000025; GAC41232.1; -; Genomic_DNA. DR EnsemblBacteria; GAC41232; GAC41232; PPOP_0582. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000029453; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000029453}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000029453}. FT DOMAIN 174 342 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 133 160 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 399 AA; 45173 MW; 6F98C795C26079DC CRC64; MEELANLAAA CGAEVVGVVT QNLNKVNTSH YIGTGKLQEV TIMLNQHEAN IVIFNDELSP SQLRNLEKDL DCKVVDRTLL ILDIFGERAK TKEAQLQVEV AELQYMLPRL VGLRESLGRQ SGGVGTKNKG TGEKKLELDR RRIEERITAL NKELEALVAH RQTQRKRRKK TELPVVSLVG YTNAGKSTVM NTLVEQFTDS KDKFVFEQDM LFATLDTSVR SIELEDNKAF LLTDTVGFVS KLPHHLVKAF RSTLEEVKEA DLLVHVVDFS NPEYEQQIRI TNETLKAIGI EEIPMIYAYN KIDLKEGVIP ESQNSSIYMA AKRKQGIDEL LAAIRAHVFK DYVTCEMLIP YDQGQHVSYL NEHANVLATA YEELGTKLTL ECRQSDYQKF TQYVYEAQA // ID M9R8H8_9RHOB Unreviewed; 430 AA. AC M9R8H8; DT 26-JUN-2013, integrated into UniProtKB/TrEMBL. DT 26-JUN-2013, sequence version 1. DT 07-JUN-2017, entry version 31. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:AGI68103.1}; GN ORFNames=OAN307_c24980 {ECO:0000313|EMBL:AGI68103.1}; OS Octadecabacter antarcticus 307. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae; Octadecabacter. OX NCBI_TaxID=391626 {ECO:0000313|EMBL:AGI68103.1, ECO:0000313|Proteomes:UP000005307}; RN [1] {ECO:0000313|EMBL:AGI68103.1, ECO:0000313|Proteomes:UP000005307} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=307 {ECO:0000313|EMBL:AGI68103.1}; RX PubMed=23671678; RA Vollmers J., Voget S., Dietrich S., Gollnow K., Smits M., Meyer K., RA Brinkhoff T., Simon M., Daniel R.; RT "Poles Apart: Arctic and Antarctic Octadecabacter strains Share High RT Genome Plasticity and a New Type of Xanthorhodopsin."; RL PLoS ONE 8:E63422-E63422(2013). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP003740; AGI68103.1; -; Genomic_DNA. DR RefSeq; WP_015500120.1; NC_020911.1. DR ProteinModelPortal; M9R8H8; -. DR STRING; 391626.OA307_3968; -. DR EnsemblBacteria; AGI68103; AGI68103; OAN307_c24980. DR KEGG; oat:OAN307_c24980; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR KO; K03665; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000005307; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000005307}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000005307}. FT DOMAIN 203 372 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 430 AA; 47593 MW; 744E59615B1EBA32 CRC64; MGEERSATRA YVLHPEIKSD NARRHAKSAL EEGVALAHAL PELEVAGSQV VSLPKMHPGM LFGKGKIQEI KGWLEDAEAG LVLIDGHVSP VQQRNLEKEW GVKLLDRTGL ILEIFSDRAR TREGVLQVEM AALSYQRTRL VRAWTHLERQ RGGLGFVGGP GETQVEADRR AIDLQLNNLK KQLSKVVKTR ELHRKARAKV PFPIVALVGY TNAGKSTLFN RLTGASVFVE DMLFATLDPT MRKVDLPNGD AIIMSDTVGF ISDLPTQLVA SFRATLEEVL EADVILHVRD ISHPQSADQK KAVLDTLRQL DVNPDVPMIE VLNKIDLLAP EDADYLQALH KDGENVFGTS AVTGQGLDTL LDQITEKLKG TTRALTLTLD WSHGGAQSWL QRENVIETTA QTDTGWTIDV RWSPMQAAKF EKQFPEAFAP // ID M9X1M7_MANHA Unreviewed; 461 AA. AC M9X1M7; DT 26-JUN-2013, integrated into UniProtKB/TrEMBL. DT 26-JUN-2013, sequence version 1. DT 07-JUN-2017, entry version 31. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:AGK00744.1}; GN ORFNames=MHH_c02410 {ECO:0000313|EMBL:AGK00744.1}; OS Mannheimia haemolytica M42548. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Mannheimia. OX NCBI_TaxID=1316932 {ECO:0000313|EMBL:AGK00744.1, ECO:0000313|Proteomes:UP000012987}; RN [1] {ECO:0000313|EMBL:AGK00744.1, ECO:0000313|Proteomes:UP000012987} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=M42548 {ECO:0000313|EMBL:AGK00744.1, RC ECO:0000313|Proteomes:UP000012987}; RX PubMed=23723408; RA Eidam C., Poehlein A., Brenner Michael G., Kadlec K., Liesegang H., RA Brzuszkiewicz E., Daniel R., Sweeney M.T., Murray R.W., Watts J.L., RA Schwarz S.; RT "Complete Genome Sequence of Mannheimia haemolytica Strain 42548 from RT a Case of Bovine Respiratory Disease."; RL Genome Announc. 1:E00318-13(2013). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP005383; AGK00744.1; -; Genomic_DNA. DR RefSeq; WP_006253648.1; NC_021082.1. DR EnsemblBacteria; AGK00744; AGK00744; MHH_c02410. DR GeneID; 15340864; -. DR KEGG; mhx:MHH_c02410; -. DR PATRIC; fig|1316932.3.peg.237; -. DR KO; K03665; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000012987; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000012987}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000012987}. FT DOMAIN 228 395 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 194 221 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 461 AA; 51208 MW; E289BC847E8AC7BE CRC64; MLNESLPNSE ENSAFGFALS EASQTTEAAS PTDPENQDKA ILVHLYLGQH KDVENLLEFK TLAESAGVEV LATLTTSRQS SHIKYYVGQG KAEGIAEAVE RLGATVVLVN HQLSPAQTRN LQSLCGCRVV DRTGLILDIF AQRARSHEGK LQVELAQLRH LSTRLVRRVT NQDQQKGGAV GLRGPGETQL ETDRRLIKVR IQQLLNRLEK VSKQRNQNRK TRQKADIPTV SLVGYTNAGK STLFNAITQA GVYAADQLFA TLDPTLRRIQ VQDVGTTILA DTVGFIRFLP HDLVSAFKST LQETTEATLL LHVIDGSDER KNENIDAVNQ VLDEIGALDI PTLLVFNKID KLEGVEPHIE RNADGTPVAV YLSAQENSGI ELLFQAIQER LRSNLVCENL LLPVTAGAIY AQFKAENCIK TEHFNEFGER IISIEINEVQ WNKWVKQFPD LAEYIELAKW G // ID N0AXI0_9BACI Unreviewed; 419 AA. AC N0AXI0; DT 26-JUN-2013, integrated into UniProtKB/TrEMBL. DT 26-JUN-2013, sequence version 1. DT 07-JUN-2017, entry version 27. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=B1NLA3E_06910 {ECO:0000313|EMBL:AGK53146.1}; OS Bacillus sp. 1NLA3E. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus. OX NCBI_TaxID=666686 {ECO:0000313|EMBL:AGK53146.1, ECO:0000313|Proteomes:UP000013300}; RN [1] {ECO:0000313|EMBL:AGK53146.1, ECO:0000313|Proteomes:UP000013300} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=1NLA3E {ECO:0000313|EMBL:AGK53146.1}; RX PubMed=23833140; RA Venkatramanan R., Prakash O., Woyke T., Chain P., Goodwin L.A., RA Watson D., Brooks S., Kostka J.E., Green S.J.; RT "Genome sequences for three denitrifying bacterial strains isolated RT from a uranium- and nitrate-contaminated subsurface environment."; RL Genome Announc. 1:e00449-13(2013). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP005586; AGK53146.1; -; Genomic_DNA. DR RefSeq; WP_015593206.1; NC_021171.1. DR EnsemblBacteria; AGK53146; AGK53146; B1NLA3E_06910. DR KEGG; baci:B1NLA3E_06910; -. DR KO; K03665; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000013300; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000013300}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000013300}. FT DOMAIN 200 362 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 419 AA; 47935 MW; F243A3873F76B79B CRC64; MERQADLEKV ILVGCQTARV DDLHFQYSME ELASLTDTAK GEVMISVSQK RDRVHPATYI GKGKIEELKA LEDELEPDLI IFNDELSSTQ IRNLSRELDA RVIDRTQLIL DIFATRARSK EGKLQVEYAQ LQYMLPRLVG QGTSMSRLGA GIGTRGPGET KLESDRRHIR RRIDDIKSQL TVIVGHRDRY RERRKKNKAF QIAIVGYTNA GKSTLFNRLT EADTLEENQL FATLDPTTRK MILPSGFTTL TTDTVGFLQD LPTTLIAAFR STLEEVNEAD LLLHVVDCSN PDYFQHEKTV QHLLEELENQ HLPQLTVYNK KDMMQPDFVP VAKTETITIS AFEEEDRQKL KQKVEEMVLG LMESYHVHVP STEGKLLAQL KNETILRELV FDEENQKYNC KGYSFPDQKI SGQLKNFSI // ID N0BB31_9RHIZ Unreviewed; 467 AA. AC N0BB31; DT 26-JUN-2013, integrated into UniProtKB/TrEMBL. DT 26-JUN-2013, sequence version 1. DT 10-MAY-2017, entry version 28. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=HYPDE_30333 {ECO:0000313|EMBL:AGK57741.1}; OS Hyphomicrobium denitrificans 1NES1. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Hyphomicrobiaceae; Hyphomicrobium. OX NCBI_TaxID=670307 {ECO:0000313|EMBL:AGK57741.1, ECO:0000313|Proteomes:UP000005952}; RN [1] {ECO:0000313|EMBL:AGK57741.1, ECO:0000313|Proteomes:UP000005952} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=1NES1 {ECO:0000313|EMBL:AGK57741.1, RC ECO:0000313|Proteomes:UP000005952}; RX PubMed=23833140; RA Venkatramanan R., Prakash O., Woyke T., Chain P., Goodwin L.A., RA Watson D., Brooks S., Kostka J.E., Green S.J.; RT "Genome sequences for three denitrifying bacterial strains isolated RT from a uranium- and nitrate-contaminated subsurface environment."; RL Genome Announc. 1:e00449-13(2013). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP005587; AGK57741.1; -; Genomic_DNA. DR EnsemblBacteria; AGK57741; AGK57741; HYPDE_30333. DR KEGG; hdt:HYPDE_30333; -. DR KO; K03665; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000005952; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000005952}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000005952}. FT DOMAIN 234 407 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 467 AA; 51648 MW; 7373B4651D0CFF10 CRC64; MTPHSENDDG ERASGRKRRR ASKETRQPRT RTLVLVPALK RPARSGEAAK GTREIHTPEN RLSEAVGLAN AIELDIIDSA IVPMSEPRPS TLLGSGKVDE LGQRVRDLDI GLVVVDHALT PVQQRNLEKA WNTKVVDRTG LILEIFGARA RTREGVLQVE LAHLSYQKGR LVRAWTHLER QRGGGGFLGG PGEAQIELDR RMLQDRIDAI KRDLADVVRT RDLHRKGRRK VPYPIVAVVG YTNAGKSTLF NKITGAGVVA MDQVFATLDP TMREVKLPSA RRIILSDTVG FISDLPTMLV AAFRATLEEV VEADLILHVR DIAHEETEAQ ARDVEKVLGE LGIDTIQADG HILEVWNKID LVSHDRRGEL QHEALRNECP PVLVSAATGE GIVPLLDAID RRLSVADEIL DVIIPGSQGA LLNWLHETCD VLAREARKDG SIELRLRIPS EKKERVVGQL RKAGLKV // ID N0E1H0_9MICO Unreviewed; 495 AA. AC N0E1H0; DT 26-JUN-2013, integrated into UniProtKB/TrEMBL. DT 26-JUN-2013, sequence version 1. DT 07-JUN-2017, entry version 29. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=BN10_680039 {ECO:0000313|EMBL:CCH70813.1}; OS Tetrasphaera elongata Lp2. OC Bacteria; Actinobacteria; Micrococcales; Intrasporangiaceae; OC Tetrasphaera. OX NCBI_TaxID=1193181 {ECO:0000313|EMBL:CCH70813.1, ECO:0000313|Proteomes:UP000013167}; RN [1] {ECO:0000313|EMBL:CCH70813.1, ECO:0000313|Proteomes:UP000013167} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Lp2 {ECO:0000313|EMBL:CCH70813.1, RC ECO:0000313|Proteomes:UP000013167}; RX PubMed=23178666; DOI=10.1038/ismej.2012.136; RA Kristiansen R., Nguyen H.T.T., Saunders A.M., Nielsen J.L., Wimmer R., RA Le V.Q., McIlroy S.J., Petrovski S., Seviour R.J., Calteau A., RA Nielsen K.L., Nielsen P.H.; RT "A metabolic model for members of the genus Tetrasphaera involved in RT enhanced biological phosphorus removal."; RL ISME J. 7:543-554(2013). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:CCH70813.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CAIZ01000139; CCH70813.1; -; Genomic_DNA. DR RefSeq; WP_010850656.1; NZ_HF570956.1. DR EnsemblBacteria; CCH70813; CCH70813; BN10_680039. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000013167; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 2. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000013167}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000013167}. FT DOMAIN 276 441 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 495 AA; 54559 MW; C4C63C0E902E4328 CRC64; MTERNSSTGS LFTQRAEALT DDRFDEARFL TDEETADSRD DGDQLDREER AALRRVRGLS TELEDITEVE YRQLRLERVV LASVWSEGTL EDAENSMREL AALAETAGSE VLDGLIQRRS HPDNATYLGK GKAQELRDIV IAEGADTVIC DTELAPSQRR ALEDVVKVKV IDRTALILDI FAQHAKSKEG KAQVELAQMQ YLLPRLRGWG ESMSRQAGGQ VGGAGQGMGS RGPGETKIEL DRRRINTRMA KLRREIKEMK TVRDTKRGSR QAREIPSVAI AGYTNAGKSS LLNRLTGAGV LVQNQLFATL DPTVRRAETP DGREYTLADT VGFVRQLPTQ LVEAFRSTLE EVGDADLLLH VVDGSHPDPE GQISAVRSVL ADVDAADVKE VIVVNKADIA DPEVIDRILR HEKHAIAVSA HTGQGMEALR QLIADEIPRP DILVDVLVPY SRGDLVSRVH DEADLLTEEH VADGTRITAR AKADLAADLE RYAVR // ID N1MFZ2_9SPHN Unreviewed; 444 AA. AC N1MFZ2; DT 26-JUN-2013, integrated into UniProtKB/TrEMBL. DT 26-JUN-2013, sequence version 1. DT 07-JUN-2017, entry version 29. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=EBBID32_2160 {ECO:0000313|EMBL:CCW15886.1}; OS Sphingobium japonicum BiD32. OC Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales; OC Sphingomonadaceae; Sphingobium. OX NCBI_TaxID=1301087 {ECO:0000313|EMBL:CCW15886.1, ECO:0000313|Proteomes:UP000013201}; RN [1] {ECO:0000313|EMBL:CCW15886.1, ECO:0000313|Proteomes:UP000013201} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BiD32 {ECO:0000313|EMBL:CCW15886.1, RC ECO:0000313|Proteomes:UP000013201}; RA Le V.; RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:CCW15886.1, ECO:0000313|Proteomes:UP000013201} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BiD32 {ECO:0000313|EMBL:CCW15886.1, RC ECO:0000313|Proteomes:UP000013201}; RA Nielsen J.L., Zhou N.A., Kjeldal H.; RT "Bisphenol A degrading Sphingobium sp. strain BiD32."; RL Submitted (APR-2013) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:CCW15886.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CAVK010000012; CCW15886.1; -; Genomic_DNA. DR RefSeq; WP_006949170.1; NZ_CAVK010000012.1. DR EnsemblBacteria; CCW15886; CCW15886; EBBID32_2160. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000013201; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0016810; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds; IEA:InterPro. DR CDD; cd01878; HflX; 1. DR Gene3D; 2.30.40.10; -; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR011059; Metal-dep_hydrolase_composite. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 2. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000013201}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000013201}. FT DOMAIN 209 390 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 444 AA; 48188 MW; D87E2C22EC4D4052 CRC64; MAIFNRDSDD EVARGARAVV VHAETHGLER RDSDARLEEA RGLALAIGID VRAGQAFRVR DRKPATLFGS GQVDQIATLV VQEEAELVIV DNALSPVQQS NLEKAVGAKV IDRTGLILEI FGERAATNEG RLQVELAHLD YQAGRLVRSW THLERQRGGF GFLGGPGETQ IEADRRMIRD RMAKIRKELE QVTRTRGLHR ARRQRAPWPV IALVGYTNAG KSTLFNRLTG ADVMAEDLLF ATLDPTMRQI ALPGLDKAIL SDTVGFVSDL PTQLIAAFRA TLEEVLSADL IVHVRDIAHP DSDAQRDDVL DVLSELGVAG EGALDRAEGE PAAPPIIEAW NKLDLLDPEA EALARETASR RDDVVILSAL TGEGVPDLQR AISAKMTAGA KVYGLRIAAA DGAALAWLHE HGEVLTSDAQ GEETRVEVRL SDAAFARFGK RGQG // ID N1V549_9MICC Unreviewed; 516 AA. AC N1V549; DT 26-JUN-2013, integrated into UniProtKB/TrEMBL. DT 26-JUN-2013, sequence version 1. DT 07-JUN-2017, entry version 29. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=D477_005781 {ECO:0000313|EMBL:EMY35144.1}; OS Arthrobacter crystallopoietes BAB-32. OC Bacteria; Actinobacteria; Micrococcales; Micrococcaceae; Arthrobacter. OX NCBI_TaxID=1246476 {ECO:0000313|EMBL:EMY35144.1, ECO:0000313|Proteomes:UP000010729}; RN [1] {ECO:0000313|EMBL:EMY35144.1, ECO:0000313|Proteomes:UP000010729} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BAB-32 {ECO:0000313|EMBL:EMY35144.1, RC ECO:0000313|Proteomes:UP000010729}; RX PubMed=23833141; RA Joshi M.N., Pandit A.S., Sharma A., Pandya R.V., Desai S.M., RA Saxena A.K., Bagatharia S.B.; RT "Draft Genome Sequence of Arthrobacter crystallopoietes Strain BAB-32, RT Revealing Genes for Bioremediation."; RL Genome Announc. 1:e00452-13(2013). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EMY35144.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ANPE02000084; EMY35144.1; -; Genomic_DNA. DR RefSeq; WP_005267926.1; NZ_ANPE02000084.1. DR EnsemblBacteria; EMY35144; EMY35144; D477_005781. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000010729; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 2. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000010729}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000010729}. FT DOMAIN 295 460 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 516 AA; 56180 MW; 784494594A3970CD CRC64; MTNNSAGQPA EEPKLTPEEI QAVIDRILAK DTAARSKTGS GVRGKAQAIS TLDEEHSEYD GEQQDLEERR ALRRVAGLST ELEDVTEVEY RQLRLERVVL AGLWTEGTAE DAENSLRELA ALAETAGSEV LDGVVQRRLK PDPGTFLGSG KAQELRDIVM STGADTVIVD SELSPSQRRG LEDIVKVKVI DRTALILDIF AQHAKSREGK AQVELAQLEY LLPRLRGWGE SMSRQAGGRV GAAGGGIGSR GPGETKIELD RRRIRTRMAK LRREITGMKP ARETKRANRK RHAVPSVAIV GYTNAGKSSL LNRLTNAGVL VENALFATLD PTVRKAETAD GLGYTLADTV GFVRSLPTQL VEAFRSTLEE AADADLLLHV VDASHPDPEG QIAAVREVLA EVDARKIPEI VVLNKADAAD PFTIERLRRR EPRHVVVSAR TGQGIPELLQ AISGGIPRPT VKLELLIPYD RGDVVSRLHS PDAEILAMHH GEEGTELEVM VREGLAAELD AFVRRG // ID N1ZS09_9CLOT Unreviewed; 424 AA. AC N1ZS09; DT 26-JUN-2013, integrated into UniProtKB/TrEMBL. DT 26-JUN-2013, sequence version 1. DT 07-JUN-2017, entry version 28. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=C820_00564 {ECO:0000313|EMBL:EMZ15124.1}; OS Clostridium sp. ASF356. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=97138 {ECO:0000313|EMBL:EMZ15124.1, ECO:0000313|Proteomes:UP000012445}; RN [1] {ECO:0000313|EMBL:EMZ15124.1, ECO:0000313|Proteomes:UP000012445} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ASF356 {ECO:0000313|EMBL:EMZ15124.1, RC ECO:0000313|Proteomes:UP000012445}; RX PubMed=24723722; RA Wannemuehler M.J., Overstreet A.M., Ward D.V., Phillips G.J.; RT "Draft genome sequences of the altered schaedler flora, a defined RT bacterial community from gnotobiotic mice."; RL Genome Announc. 2:e00287-14(2014). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EMZ15124.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AQFQ01000007; EMZ15124.1; -; Genomic_DNA. DR RefSeq; WP_004034251.1; NZ_KB822565.1. DR EnsemblBacteria; EMZ15124; EMZ15124; C820_00564. DR PATRIC; fig|97138.3.peg.570; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000012445; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000012445}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000012445}. FT DOMAIN 207 371 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 166 203 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 424 AA; 47703 MW; 5BC700FE77D49C2E CRC64; MAKQTQLHIS EQTKERVILV AVDLENNTTM DTEACLNELE ELVKTAGAVT VATVVQKRER IHSGHYIGKG KIEEIKMMIQ TYDASGIVCD DELSPAQMKN LEQMLQTKIM DRTMVILDIF ASRAMSKEGK IQVELAQLKY RLSRLAGIGA SMSRLGGGIG TRGPGETKLE TNRRHIKDRI GELNQELNQI QTHRQLLRNQ RNKKGTPLLS LVGYTNAGKS TLINTLTDAG VLAEDKLFAT LDTTTRKVKL PNGTEILLTD TVGFIQKLPH HLIQAFRATL EELNFADILI HVVDASNENR QEQMNIVYQT LKGLHCETTP VITVYNKIDK NVQTPLPIDN IARDKVAISA KTKQGLDSML EKIETLLKSF RIAMKVFLPY TEGSLLNMIH GKCEIVVEQH RAEGVYLEIY AQQEMENRLQ KYKI // ID N2ACI1_9FIRM Unreviewed; 428 AA. AC N2ACI1; DT 26-JUN-2013, integrated into UniProtKB/TrEMBL. DT 26-JUN-2013, sequence version 1. DT 07-JUN-2017, entry version 26. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=C823_04217 {ECO:0000313|EMBL:EMZ22129.1}; OS Eubacterium plexicaudatum ASF492. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Eubacteriaceae; OC Eubacterium. OX NCBI_TaxID=1235802 {ECO:0000313|EMBL:EMZ22129.1, ECO:0000313|Proteomes:UP000012589}; RN [1] {ECO:0000313|EMBL:EMZ22129.1, ECO:0000313|Proteomes:UP000012589} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ASF492 {ECO:0000313|EMBL:EMZ22129.1, RC ECO:0000313|Proteomes:UP000012589}; RX PubMed=24723722; RA Wannemuehler M.J., Overstreet A.M., Ward D.V., Phillips G.J.; RT "Draft genome sequences of the altered schaedler flora, a defined RT bacterial community from gnotobiotic mice."; RL Genome Announc. 2:e00287-14(2014). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EMZ22129.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AQFT01000124; EMZ22129.1; -; Genomic_DNA. DR RefSeq; WP_004066646.1; NZ_KB822502.1. DR EnsemblBacteria; EMZ22129; EMZ22129; C823_04217. DR PATRIC; fig|1235802.3.peg.4481; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000012589; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000012589}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000012589}. FT DOMAIN 203 374 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 162 196 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 428 AA; 48478 MW; 8FBB69B007978BBB CRC64; METKNIQYER ALLAGVNTGT DEQEFARSME ELKSLAKACY MEPVAIVTQN LEHGNKALYV GTGKVREIKE AALAYDADVA VFDDALTPAQ LSNLQKELDM PVLDRTTLIL DIFAIRAGTR EAKLQVESAR LKYLLPRLVG MHEALTRQGG ASGSMSSRGA GEKKLELDRR KIEKRIAQLN RELKEVSAER EVQRKKRQAA RIPLVAMVGY TNAGKSTIMN ALVDRYVKDD DKKVLEKDML FATLDTTVRQ ICTGNNQDFL LSDTVGFIHK LPHSLIKAFH ATLEEVRNAD LLLQVVNVSD PHYKEQMHTT EELLAELHAA GLPMITVYNQ ADRCMDAVEY PKRSGMDKVF ICAKETSSLE LLVRMILERV YEDYVCAEFL IPYTDGVVLS YFMEQAQVIE SAYEEDGTRV RVRCHRADRE KYKKYLQN // ID N2AHV1_9CLOT Unreviewed; 415 AA. AC N2AHV1; DT 26-JUN-2013, integrated into UniProtKB/TrEMBL. DT 26-JUN-2013, sequence version 1. DT 07-JUN-2017, entry version 28. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=C824_02925 {ECO:0000313|EMBL:EMZ26023.1}; OS Clostridium sp. ASF502. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=97139 {ECO:0000313|EMBL:EMZ26023.1, ECO:0000313|Proteomes:UP000012582}; RN [1] {ECO:0000313|EMBL:EMZ26023.1, ECO:0000313|Proteomes:UP000012582} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ASF502 {ECO:0000313|EMBL:EMZ26023.1, RC ECO:0000313|Proteomes:UP000012582}; RX PubMed=24723722; RA Wannemuehler M.J., Overstreet A.M., Ward D.V., Phillips G.J.; RT "Draft genome sequences of the altered schaedler flora, a defined RT bacterial community from gnotobiotic mice."; RL Genome Announc. 2:e00287-14(2014). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EMZ26023.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AQFU01000049; EMZ26023.1; -; Genomic_DNA. DR RefSeq; WP_004080451.1; NZ_KB822466.1. DR EnsemblBacteria; EMZ26023; EMZ26023; C824_02925. DR PATRIC; fig|97139.3.peg.3177; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000012582; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000012582}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000012582}. FT DOMAIN 201 365 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 160 197 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 415 AA; 46757 MW; 461624561054D6E4 CRC64; MELYDLKQEE ERFILVGIQL NDSEPAEESL DELEELARTA GAAAAGRLIQ SREAMHPLTY IGKGKIEELK DLIWEQDASG IICDDELSAV QLNNLQQELE CKVIDRTLLI LDIFAAHAVS GEGKIQVELA QLRYRAARLT GLGRSLSRLG GGIGTRGPGE KKLEMDRRLI RERISHLKRE LKEVEQHRER IRTQRKKSCM KVAALVGYTS AGKSSIENAL TQAGILEDAM LFSTLDTTTR ALELEGKQKI LLTDTVGFIR KLPHHLIEAF KSTLEEARHA DIIIHVVDVS NPQMDTQMHV VYETLRQLGV EGKPVVTLFN KQDLISGQEN FRDFQADYTV DGSAKTGQGM EELKAVLLEI IRREQVYVER LYPFQEAGKI QVIRKNGQLL QEEYLPDGIA VKAYVPKEIY LSGRI // ID N2ALT0_9LACO Unreviewed; 425 AA. AC N2ALT0; DT 26-JUN-2013, integrated into UniProtKB/TrEMBL. DT 26-JUN-2013, sequence version 1. DT 07-JUN-2017, entry version 27. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=C821_00535 {ECO:0000313|EMBL:EMZ25439.1}; OS Lactobacillus sp. ASF360. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; OC Lactobacillus. OX NCBI_TaxID=97137 {ECO:0000313|EMBL:EMZ25439.1, ECO:0000313|Proteomes:UP000012594}; RN [1] {ECO:0000313|EMBL:EMZ25439.1, ECO:0000313|Proteomes:UP000012594} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ASF360 {ECO:0000313|EMBL:EMZ25439.1, RC ECO:0000313|Proteomes:UP000012594}; RX PubMed=24723722; RA Wannemuehler M.J., Overstreet A.M., Ward D.V., Phillips G.J.; RT "Draft genome sequences of the altered schaedler flora, a defined RT bacterial community from gnotobiotic mice."; RL Genome Announc. 2:e00287-14(2014). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EMZ25439.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AQFR01000024; EMZ25439.1; -; Genomic_DNA. DR RefSeq; WP_004040432.1; NZ_KB822413.1. DR EnsemblBacteria; EMZ25439; EMZ25439; C821_00535. DR PATRIC; fig|97137.3.peg.493; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000012594; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000012594}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000012594}. FT DOMAIN 199 368 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 425 AA; 47463 MW; A03C111280FBFABF CRC64; MIDNRPKTTK AFIAGVNLND PNFDYYMTEL ADLTEANNME VVGRAEQKAE NIVAGTYFGV GKINQIKSMA QGLKAKVLVL NDELSPVQIR NLEKMTKLRV IDRTELILEI FASRARTKQA KLQVALARLQ YELPRLHPSE NNLDQQRGGG MSNRGAGETK LELNRRTIGK QISAIKKELK AVASQEEIKA SRRNQSRIPK VALVGYTNAG KSTTMNGLLK AFDHEGSDKQ VFVKNMLFAT LDTSVRKIDI DNNKGFILSD TVGFISKLPH NLVESFKATL QEARDADLLV NVVDSSDPNM IQMVRTTQKV LNEIGAGNIP MITAYNKADR TDRNYPQIEG DDILYSATDE KSIRMLSDLI TKRIFAGYGE FELLLPLSDG KELAFLHEHA QVNKEEFKDD GVHVSANIAP SDQARFKKFM LTENA // ID N2BTJ9_9ACTN Unreviewed; 435 AA. AC N2BTJ9; DT 26-JUN-2013, integrated into UniProtKB/TrEMBL. DT 26-JUN-2013, sequence version 1. DT 07-JUN-2017, entry version 28. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=HMPREF1091_00842 {ECO:0000313|EMBL:EMZ41868.1}; OS Atopobium minutum 10063974. OC Bacteria; Actinobacteria; Coriobacteriia; Coriobacteriales; OC Atopobiaceae; Atopobium. OX NCBI_TaxID=997872 {ECO:0000313|EMBL:EMZ41868.1, ECO:0000313|Proteomes:UP000012651}; RN [1] {ECO:0000313|EMBL:EMZ41868.1, ECO:0000313|Proteomes:UP000012651} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=10063974 {ECO:0000313|EMBL:EMZ41868.1, RC ECO:0000313|Proteomes:UP000012651}; RG The Broad Institute Genome Sequencing Platform; RA Earl A., Ward D., Feldgarden M., Gevers D., Lambert T., Marvaud J.-C., RA Courvalin P., Walker B., Young S.K., Zeng Q., Gargeya S., RA Fitzgerald M., Haas B., Abouelleil A., Alvarado L., Arachchi H.M., RA Berlin A.M., Chapman S.B., Dewar J., Goldberg J., Griggs A., Gujja S., RA Hansen M., Howarth C., Imamovic A., Larimer J., McCowan C., Murphy C., RA Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T., RA Sisk P., Sykes S., Wortman J., Nusbaum C., Birren B.; RT "The Genome Sequence of Atopobium minutum 10063974."; RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EMZ41868.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGXC01000002; EMZ41868.1; -; Genomic_DNA. DR RefSeq; WP_002563617.1; NZ_KB822533.1. DR EnsemblBacteria; EMZ41868; EMZ41868; HMPREF1091_00842. DR PATRIC; fig|997872.3.peg.845; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000012651; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000012651}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000012651}. FT DOMAIN 213 378 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 435 AA; 48188 MW; 3AC2B0CB84ADCAE1 CRC64; MAKPQRFKPL STAPVAERAI LVGVDFGKGE WSIDESLSEL ERLAQTDGAK VVGRLTQRLD HPVSKTFIGS GKAQELVSMV KRLEADVVIF DDELSPSQQS NLEKIIGEPT KVIDRTALIL DIFGVHAKTR EGRLQVQLAQ LQYLYPRLRG MWSHLVGEQT RGGIGSRFGQ GESQLEVDRR LVRKRIGMLK EALAHLDVRR ATQSKARWES GVWRVALVGY TNAGKSTLLN ALTGAEVYAQ DELFATLDPT TRSLDLSEGR KITLTDTVGF IQKLPTTLVE SFNSTLAEVK AADLIVKVAD ASDVHLIKQL QAVDEVLQQI DAQDIPYIVA LNKCDLISPE LKRTLRFTFP KAEFVSAAQK TNLDGLLYRI AKEASAGNSV ITVRIPYDKG ILLKMIHEQA QVIREEYTEQ GLLATVSVAT RMEQTLTPYK IVANS // ID N2JAQ5_9PSED Unreviewed; 434 AA. AC N2JAQ5; DT 26-JUN-2013, integrated into UniProtKB/TrEMBL. DT 26-JUN-2013, sequence version 1. DT 30-AUG-2017, entry version 28. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=HMPREF1487_06744 {ECO:0000313|EMBL:ENA33011.1}; OS Pseudomonas sp. HPB0071. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=1203578 {ECO:0000313|EMBL:ENA33011.1, ECO:0000313|Proteomes:UP000017050}; RN [1] {ECO:0000313|EMBL:ENA33011.1, ECO:0000313|Proteomes:UP000017050} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=HPB0071 {ECO:0000313|EMBL:ENA33011.1, RC ECO:0000313|Proteomes:UP000017050}; RG The Broad Institute Genome Sequencing Platform; RA Earl A., Ward D., Feldgarden M., Gevers D., Schmidt T., Dover J., RA Dai D., Walker B., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., RA Haas B., Abouelleil A., Alvarado L., Arachchi H.M., Berlin A.M., RA Chapman S.B., Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M., RA Howarth C., Imamovic A., Larimer J., McCowan C., Murphy C., Neiman D., RA Pearson M., Priest M., Roberts A., Saif S., Shea T., Sisk P., RA Sykes S., Wortman J., Nusbaum C., Birren B.; RT "The Genome Sequence of Pseudomonas sp. HPB0071."; RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:ENA33011.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AQFP01000009; ENA33011.1; -; Genomic_DNA. DR RefSeq; WP_010796922.1; NZ_KI517367.1. DR EnsemblBacteria; ENA33011; ENA33011; HMPREF1487_06744. DR PATRIC; fig|1203578.3.peg.2449; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000017050; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000017050}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000017050}. FT DOMAIN 199 367 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 165 192 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 434 AA; 49165 MW; 4128EF01C3947B0E CRC64; MFFERPGGGE RAILVHLEGQ DPESREDPQE FQELAHSAGA DTVAMVTVSR HQPSARFLIG TGKVDELHDL VKADEAELVI FNHTLTPSQE RNLERALECR VLDRTGLILD IFAQRARTHE GKLQVELAQL EHMSTRLVRG WTHLERQKGG IGLRGPGETQ LETDRRLLRV RIRQIKQRLE KVRSQREQAR RGRRRAEVPA VSLVGYTNAG KSTLFNTLTS SEVYAANQLF ATLDPTLRRL ELADLGPVVL ADTVGFIRHL PHKLVEAFRA TLEESSNADL LLHVIDSHEE DRMLQIEQVN VVLEEIGANE IPMLEVYNKI DLLENVEPHI QRDEETGRPI RVWASARENR GLELIRQAVA ELLGDDLFVG KLRLPQAMGR LRALLFSQGA VQEESHDEEG YTVLSVRLPR AELNRLVSRE GFKPDDFVAQ HTLQ // ID N4W8Q6_9BACI Unreviewed; 422 AA. AC N4W8Q6; DT 26-JUN-2013, integrated into UniProtKB/TrEMBL. DT 26-JUN-2013, sequence version 1. DT 07-JUN-2017, entry version 31. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=J416_09269 {ECO:0000313|EMBL:ENH96678.1}; OS Gracilibacillus halophilus YIM-C55.5. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; OC Gracilibacillus. OX NCBI_TaxID=1308866 {ECO:0000313|EMBL:ENH96678.1, ECO:0000313|Proteomes:UP000012283}; RN [1] {ECO:0000313|EMBL:ENH96678.1, ECO:0000313|Proteomes:UP000012283} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=YIM-C55.5 {ECO:0000313|EMBL:ENH96678.1, RC ECO:0000313|Proteomes:UP000012283}; RA Sugumar T., Polireddy D.R., Antony A., Madhava Y.R., Sivakumar N.; RT "Draft genome sequence of Gracibacillus halophilus YIM-C55.5, a RT moderately halophilic and thermophilic organism from the Xiaochaidamu RT salt lake."; RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:ENH96678.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; APML01000033; ENH96678.1; -; Genomic_DNA. DR RefSeq; WP_003468906.1; NZ_APML01000033.1. DR EnsemblBacteria; ENH96678; ENH96678; J416_09269. DR PATRIC; fig|1308866.3.peg.1874; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000012283; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000012283}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Hydrolase {ECO:0000313|EMBL:ENH96678.1}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Protease {ECO:0000313|EMBL:ENH96678.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000012283}. FT DOMAIN 196 358 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 162 189 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 422 AA; 48390 MW; 9F65CB0C78086717 CRC64; MVIENVLLIA VQTEDMNQER FHYSLNELRA LARTVGAEVA DVITQNRKKP HQAYYVGEGK LDEIYEQVTK HAIDIVIANQ ELSGGQLRNL QDTLGVRVID RSQLILDIFA KRARTKEGKL QVELAQYAYM LPRLHGQGEA LSRLGGGIGT RGPGETKLET DRRHIQNRMD DIKKRLKTVA NQREQYRGNR RKQQAFQIAI VGYTNAGKST LFNGLTKSDS LYEDKLFATL DPLTRKVHLP SGLEVIVTDT VGFIQDLPTP LIAAFRSTLE EVNEADLIVH VIDANAPNIE DHQQTVQDLL EELDADKIPL LTLYNKRDLV TEQHFIPEQH PYLLISANDP SDINEVKHKI EAMMKEQWKP YSCFIPEEES YRLRDFQTAA LVTEEEYNAI KQGYQLTVYA NHQHPIMKLV KEYYERDDRR NS // ID N6WWW2_9ALTE Unreviewed; 434 AA. AC N6WWW2; DT 26-JUN-2013, integrated into UniProtKB/TrEMBL. DT 26-JUN-2013, sequence version 1. DT 30-AUG-2017, entry version 28. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=J057_17970 {ECO:0000313|EMBL:ENO13308.1}; OS Marinobacter nanhaiticus D15-8W. OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales; OC Alteromonadaceae; Marinobacter. OX NCBI_TaxID=626887 {ECO:0000313|EMBL:ENO13308.1, ECO:0000313|Proteomes:UP000013165}; RN [1] {ECO:0000313|EMBL:ENO13308.1, ECO:0000313|Proteomes:UP000013165} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=D15-8W {ECO:0000313|EMBL:ENO13308.1, RC ECO:0000313|Proteomes:UP000013165}; RX PubMed=23723401; RA Cui Z., Gao W., Li Q., Xu G., Zheng L.; RT "Genome Sequence of the Polycyclic Aromatic Hydrocarbon-Degrading RT Bacterium Strain Marinobacter nanhaiticus D15-8WT."; RL Genome Announc. 1:E00301-13(2013). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:ENO13308.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; APLQ01000014; ENO13308.1; -; Genomic_DNA. DR RefSeq; WP_004581533.1; NZ_KB822693.1. DR EnsemblBacteria; ENO13308; ENO13308; J057_17970. DR PATRIC; fig|626887.3.peg.3594; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000013165; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000013165}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000013165}. FT DOMAIN 198 365 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 434 AA; 48833 MW; 72E08978AFA6F694 CRC64; MFERPDVGER AVIVHIDFSS HNESEDLGEF VELVRSAGVE AVDEVTGSRN QPSSRLFVGE GKLEEIRAAV QVNEADVVLF NHSLSPSQER NLERELKCRV LDRTGVILDI FAQRARTHEG KLQVELAQLE HMSTRLIRGW THLERQKGGI GLRGPGETQL ETDRRLLRGR IKAIHRRLDK VRRQRDQGRR ARKRADIPTV SLVGYTNAGK STLFNHITTA SVYAADQLFA TLDPTLRRLD LPDIGPVVMA DTVGFIRHLP HKLVEAFRAT LEETTEASLL LHVIDCADER RDENIEQVED VLLEIGAHEV PVLQVYNKID LLEDFQPRVD RNEDGLPVRV WVSAMTGAGI QMLFDAVVER LAEDVLQLSV LLGPHDGKLR ALLHEAGSVI DEAYLDNGDA QVEVRLQSRD WHQLLSKAGM RADQVRYAEN AGLK // ID N6WZT9_9RHOO Unreviewed; 453 AA. AC N6WZT9; DT 26-JUN-2013, integrated into UniProtKB/TrEMBL. DT 26-JUN-2013, sequence version 1. DT 30-AUG-2017, entry version 29. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=B447_20730 {ECO:0000313|EMBL:ENO74871.1}; OS Thauera sp. 27. OC Bacteria; Proteobacteria; Betaproteobacteria; Rhodocyclales; OC Zoogloeaceae; Thauera. OX NCBI_TaxID=305700 {ECO:0000313|EMBL:ENO74871.1, ECO:0000313|Proteomes:UP000013140}; RN [1] {ECO:0000313|EMBL:ENO74871.1, ECO:0000313|Proteomes:UP000013140} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=27 {ECO:0000313|EMBL:ENO74871.1, RC ECO:0000313|Proteomes:UP000013140}; RA Liu B., Shapleigh J.P., Frostegard A.H.; RT "Draft Genome Sequences of 6 Strains from Genus Thauera."; RL Submitted (SEP-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:ENO74871.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AMXB01000067; ENO74871.1; -; Genomic_DNA. DR RefSeq; WP_002945707.1; NZ_AMXB01000067.1. DR EnsemblBacteria; ENO74871; ENO74871; B447_20730. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000013140; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000013140}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000013140}. FT DOMAIN 221 391 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 186 213 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 453 AA; 49959 MW; 009BC2BC312425CB CRC64; MQKDLADEPR NAIVASVQRP NVSDAEFEAS LAELRELAKT LGYRVVQTFT QKRAGFDTTG YLGVGKRQEV RDFVAAQSGL EAAPLATVPR TGPIEALLVD HEISPSQARN LELETGCEVM DRTMVILEIF HRNARSRAAK AQVEIARLGY MAPRLREAAK LAGPQGRQRS GVGGRGAGES HTELDRRKIR DRIAELQLEI VAMEAERKTQ RARRQGRQSL ANVALVGYTN AGKSTLMRAL TGSEVLVANK LFATLDTTVR TLYPESVPRV LVSDTVGFIK NLPHGLVASF KSTLDEALDA ALLLHVIDAS DPGFERQLEV TDTVLAEISA DEVPRIRVFN KIDHVGDADA QAECEAALRT KYPGCIVMSA RRPEEVAALR RTIVAFFQQH LVETELLLPW SAQQLRKEIY ANCEVLEERA EDEGAFFRLR GEPEAVERLR GQCVKCGQGD RPG // ID N6XDE3_9ACTO Unreviewed; 553 AA. AC N6XDE3; DT 26-JUN-2013, integrated into UniProtKB/TrEMBL. DT 26-JUN-2013, sequence version 1. DT 07-JUN-2017, entry version 28. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:ENO19228.1}; GN ORFNames=HMPREF9004_0147 {ECO:0000313|EMBL:ENO19228.1}; OS Actinomyces cardiffensis F0333. OC Bacteria; Actinobacteria; Actinomycetales; Actinomycetaceae; OC Actinomyces. OX NCBI_TaxID=888050 {ECO:0000313|EMBL:ENO19228.1, ECO:0000313|Proteomes:UP000013015}; RN [1] {ECO:0000313|EMBL:ENO19228.1, ECO:0000313|Proteomes:UP000013015} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=F0333 {ECO:0000313|EMBL:ENO19228.1, RC ECO:0000313|Proteomes:UP000013015}; RA Aqrawi P., Ayvaz T., Bess C., Blankenburg K., Coyle M., Deng J., RA Forbes L., Fowler G., Francisco L., Fu Q., Gibbs R., Gross S., RA Gubbala S., Hale W., Hemphill L., Highlander S., Hirani K., RA Jackson L., Jakkamsetti A., Javaid M., Jayaseelan J.C., Jiang H., RA Joshi V., Korchina V., Kovar C., Lara F., Lee S., Liu Y., Mata R., RA Mathew T., Munidasa M., Muzny D., Nazareth L., Ngo R., Nguyen L., RA Nguyen N., Okwuonu G., Ongeri F., Palculict T., Patil S., RA Petrosino J., Pham C., Pham P., Pu L.-L., Qin X., Qu J., Reid J., RA Ross M., Ruth R., Saada N., San Lucas F., Santibanez J., Shang Y., RA Simmons D., Song X.-Z., Tang L.-Y., Thornton R., Warren J., RA Weissenberger G., Wilczek-Boney K., Worley K., Youmans B., Zhang J., RA Zhang L., Zhao Z., Zhou C., Zhu D., Zhu Y.; RT "Reference genome for the Human Microbiome Project."; RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:ENO19228.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AQHZ01000001; ENO19228.1; -; Genomic_DNA. DR EnsemblBacteria; ENO19228; ENO19228; HMPREF9004_0147. DR PATRIC; fig|888050.3.peg.146; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000013015; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000013015}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000013015}. FT DOMAIN 279 445 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 553 AA; 60481 MW; BF61272D7001EAE5 CRC64; MDKPLEEREL NDSLDEERAQ SIVARILARR GTALESTEGQ DHSWDAGMLE REARAGTRRI QSQRNDREDI SEVEYRQIRL ERVVLVGLRT TQSEEEVDTS LRELAALAET AGSQVLDAVV QKRVKPDPAT YLGSGKAKEL ADIVRSVEAD TVIVDEELTP SQRRGLEDVI DAKVVDRTAL ILDIFAQHAK SREGKAQVEL AQLEYLLPRL RGWGESMSRQ AGGRVAAGAG IGSRGPGETK IELDRRRIRT RMAKLREEIR KMEPARRTQR LSRRRGAVPS VAILGYTNAG KSTLLNQLTD AGVLVEDALF ATLDPTVRRT ETVDGRAYTL TDTVGFVRNL PTQLVEAFRS TLEEVGEADL LVHVVDAAHP DPVGQVEAVR LVLADIEGAS SIPEIIVLNK ADLASPEHLA LVRTYFPEAV VVSANTGLGI DVLRHRIEEA LPRPSLLIDC VIPYSRGDLV HTIHEEGEVE REEYVSEGTR VIARVNERLG AHIKEAGIVL IGVGGDSFAG AGSLEQALSI GAGSLEGTMP DKREGFEGAV PKRMESPKGS LDD // ID N6XV75_9RHOO Unreviewed; 381 AA. AC N6XV75; DT 26-JUN-2013, integrated into UniProtKB/TrEMBL. DT 26-JUN-2013, sequence version 1. DT 30-AUG-2017, entry version 29. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=C666_14915 {ECO:0000313|EMBL:ENO85661.1}; OS Thauera linaloolentis 47Lol = DSM 12138. OC Bacteria; Proteobacteria; Betaproteobacteria; Rhodocyclales; OC Zoogloeaceae; Thauera. OX NCBI_TaxID=1123367 {ECO:0000313|EMBL:ENO85661.1, ECO:0000313|Proteomes:UP000013232}; RN [1] {ECO:0000313|EMBL:ENO85661.1, ECO:0000313|Proteomes:UP000013232} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=47Lol / DSM 12138 {ECO:0000313|Proteomes:UP000013232}; RA Liu B., Shapleigh J.P., Frostegard A.H.; RT "Draft Genome Sequences of 6 Strains from Genus Thauera."; RL Submitted (SEP-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:ENO85661.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AMXE01000070; ENO85661.1; -; Genomic_DNA. DR RefSeq; WP_004342185.1; NZ_JHYR01000008.1. DR EnsemblBacteria; ENO85661; ENO85661; C666_14915. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000013232; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000013232}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000013232}. FT DOMAIN 198 363 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 381 AA; 41898 MW; 58A2D36E13EC7942 CRC64; MFERPASGER AVLVQLDLGQ GLIEERLSEL RLLVLSAGAS IEAAVQGKRQ APDPKLFAGS GKVQEIGEAL RVHEADIVIF NHALSPGQQR NLERELQCMV IDRTALILDI FAQRARSHEG KLQVELAQLE HLSTRLVRGW THLERQKGGI GLRGPGEKQL ETDRRLLGNR VKMLKSRLAQ IEKQRKVRRR ARERRDVLSV SLVGYTNAGK STLFNALTKA GAYAADQLFA TLDTTARRLY VGGASVVLSD TVGFIRDLPH ALVAAFRATL EETVQADLLL HVVDSASEDR DAQIGAVNEV LAEIGAADVP QAMVWNKIDL TRAEAAVERD DCGNIRRVFL SARTGEGLDL LREALAEVAQ QTFHEDADRE SGTVEAFPIQ S // ID N6XXD5_9RHOO Unreviewed; 381 AA. AC N6XXD5; DT 26-JUN-2013, integrated into UniProtKB/TrEMBL. DT 26-JUN-2013, sequence version 1. DT 30-AUG-2017, entry version 29. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=C664_19541 {ECO:0000313|EMBL:ENO74578.1}; OS Thauera sp. 63. OC Bacteria; Proteobacteria; Betaproteobacteria; Rhodocyclales; OC Zoogloeaceae; Thauera. OX NCBI_TaxID=497321 {ECO:0000313|EMBL:ENO74578.1, ECO:0000313|Proteomes:UP000013007}; RN [1] {ECO:0000313|EMBL:ENO74578.1, ECO:0000313|Proteomes:UP000013007} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=63 {ECO:0000313|EMBL:ENO74578.1, RC ECO:0000313|Proteomes:UP000013007}; RA Liu B., Shapleigh J.P., Frostegard A.H.; RT "Draft Genome Sequences of 6 Strains from Genus Thauera."; RL Submitted (SEP-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:ENO74578.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AMXC01000054; ENO74578.1; -; Genomic_DNA. DR RefSeq; WP_004292990.1; NZ_AMXC01000054.1. DR EnsemblBacteria; ENO74578; ENO74578; C664_19541. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000013007; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000013007}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000013007}. FT DOMAIN 198 363 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 381 AA; 41768 MW; 8858F9574F20C002 CRC64; MFERPASGER AVLVQLDLGQ GAIEERLSEL KLLVLSAGAS VEAVVQGKRA APDPKLFAGS GKVQEIGEAM RAHEADIVIF NHALSPAQQR NLERELACMV IDRTALILDI FAQRARSHEG KLQVELAQLE HLSTRLVRGW THLERQKGGI GLRGPGEKQL ETDRRLLGNR VKMLKSRLAQ IEKQRKVRRR ARERRDVLSV SLVGYTNAGK STLFNALTKA GAYAADQLFA TLDTTSRRLY VGGASVVLSD TVGFIRDLPH ALVAAFRATL EETVQADLLL HVVDSASEDR DAQIDAVNEV LAEIGAAEVP QILVWNKIDL TRAEPAVERS DCGNIRRVFL SARTGEGLDL LREALAEVAQ QTFHEDAGRE SGTVDELPSQ S // ID N6Y0R9_9RHOO Unreviewed; 381 AA. AC N6Y0R9; DT 26-JUN-2013, integrated into UniProtKB/TrEMBL. DT 26-JUN-2013, sequence version 1. DT 30-AUG-2017, entry version 28. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=B447_18798 {ECO:0000313|EMBL:ENO76012.1}; OS Thauera sp. 27. OC Bacteria; Proteobacteria; Betaproteobacteria; Rhodocyclales; OC Zoogloeaceae; Thauera. OX NCBI_TaxID=305700 {ECO:0000313|EMBL:ENO76012.1, ECO:0000313|Proteomes:UP000013140}; RN [1] {ECO:0000313|EMBL:ENO76012.1, ECO:0000313|Proteomes:UP000013140} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=27 {ECO:0000313|EMBL:ENO76012.1, RC ECO:0000313|Proteomes:UP000013140}; RA Liu B., Shapleigh J.P., Frostegard A.H.; RT "Draft Genome Sequences of 6 Strains from Genus Thauera."; RL Submitted (SEP-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:ENO76012.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AMXB01000045; ENO76012.1; -; Genomic_DNA. DR RefSeq; WP_002944219.1; NZ_AMXB01000045.1. DR EnsemblBacteria; ENO76012; ENO76012; B447_18798. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000013140; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000013140}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000013140}. FT DOMAIN 198 363 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 381 AA; 41452 MW; 3968F4A5C58CEAFB CRC64; MFERPASGER AILVQLDLGQ GAIEERLSEL KLLVGSAGAS VEGVVQGRRA SPDSKLFAGS GKVQEIAEAL RANAGDIVVF NHALSPAQQR NLERELQCMV IDRTALILDI FAQRARSHEG KLQVELAQLE HLATRLVRGW THLERQKGGI GLRGPGEKQL ETDRRLLGNR VKMLKTRLAL IEKQRKVRRR ARERRDVLSV SLVGYTNAGK STLFNALTKA GAYAADQLFA TLDTTSRRLY VGGANVVLSD TVGFIRDLPH ALVAAFQATL EETAQADLLL HVVDSASEDR DAQIEAVNQV LAEIGAAEVP QILVWNKIDL TRAAAAVERG DCDKLRRIFL SARTGEGLDL LRDALAEVAS QTFGDDAGRA TGAADERSEQ S // ID N8S6S0_ACIGI Unreviewed; 443 AA. AC N8S6S0; DT 26-JUN-2013, integrated into UniProtKB/TrEMBL. DT 26-JUN-2013, sequence version 1. DT 30-AUG-2017, entry version 30. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=F981_03199 {ECO:0000313|EMBL:ENU58891.1}; OS Acinetobacter guillouiae CIP 63.46. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Moraxellaceae; Acinetobacter. OX NCBI_TaxID=1217655 {ECO:0000313|EMBL:ENU58891.1, ECO:0000313|Proteomes:UP000013121}; RN [1] {ECO:0000313|EMBL:ENU58891.1, ECO:0000313|Proteomes:UP000013121} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CIP 63.46 {ECO:0000313|EMBL:ENU58891.1, RC ECO:0000313|Proteomes:UP000013121}; RG The Broad Institute Genome Sequencing Platform; RG The Broad Institute Genome Sequencing Center for Infectious Disease; RA Cerqueira G., Feldgarden M., Courvalin P., Perichon B., RA Grillot-Courvalin C., Clermont D., Rocha E., Yoon E.-J., Nemec A., RA Walker B., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B., RA Abouelleil A., Alvarado L., Arachchi H.M., Berlin A.M., Chapman S.B., RA Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M., Howarth C., RA Imamovic A., Larimer J., McCowan C., Murphy C., Neiman D., Pearson M., RA Priest M., Roberts A., Saif S., Shea T., Sisk P., Sykes S., RA Wortman J., Nusbaum C., Birren B.; RT "The Genome Sequence of Acinetobacter guillouiae CIP 63.46."; RL Submitted (FEB-2013) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:ENU58891.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; APOS01000030; ENU58891.1; -; Genomic_DNA. DR RefSeq; WP_004722930.1; NZ_KB849283.1. DR EnsemblBacteria; ENU58891; ENU58891; F981_03199. DR PATRIC; fig|1217655.3.peg.3129; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000013121; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000013121}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000013121}. FT DOMAIN 199 364 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 443 AA; 49933 MW; 9522AC3C76A7C47A CRC64; MEYFDQNQGG EKTILVSVNV QILEDLDAEE FRLLAKSAGA DILEHLSVQR IKPDPKFFIG SGKAEEIAEQ VEADEVELVI FDQALSPAQE RNLERILKCR VIDRTGLILD IFAQRARTHE GKLQVELAQL DHLSSRLVRS RSNLDSQKGG IGLRGPGETL LETDRRLLRI RMEQLKDRLE KVRKTRIQGR AARQKANIPT VSLVGYTNAG KSTLFNILAN SDVYAADQLF ATLDPTLRRL DWDGIGTLVL ADTVGFVRNL AHSLVESFKA TLEETLEASL LLHIIDSSSP DVMEQIDAVE TVLNEIGADV PILRVYNKID QSGEEAKIVY AKPHQPERVY VSAHTQQGLD LLRKAVHECL MGQIQRFELQ LKPAYGKLKN QLYDLNVIES EHYDDEGNLQ LVVAMAPQKL EQLINQAHLP LVEILGNKAE QFKRPLEEFE IKR // ID N8ZT76_9GAMM Unreviewed; 443 AA. AC N8ZT76; DT 26-JUN-2013, integrated into UniProtKB/TrEMBL. DT 26-JUN-2013, sequence version 1. DT 30-AUG-2017, entry version 30. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=F960_00919 {ECO:0000313|EMBL:ENV34948.1}; OS Acinetobacter gerneri DSM 14967 = CIP 107464. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Moraxellaceae; Acinetobacter. OX NCBI_TaxID=1120926 {ECO:0000313|EMBL:ENV34948.1, ECO:0000313|Proteomes:UP000013117}; RN [1] {ECO:0000313|EMBL:ENV34948.1, ECO:0000313|Proteomes:UP000013117} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CIP 107464 {ECO:0000313|EMBL:ENV34948.1, RC ECO:0000313|Proteomes:UP000013117}; RG The Broad Institute Genome Sequencing Platform; RG The Broad Institute Genome Sequencing Center for Infectious Disease; RA Cerqueira G., Feldgarden M., Courvalin P., Perichon B., RA Grillot-Courvalin C., Clermont D., Rocha E., Yoon E.-J., Nemec A., RA Walker B., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B., RA Abouelleil A., Alvarado L., Arachchi H.M., Berlin A.M., Chapman S.B., RA Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M., Howarth C., RA Imamovic A., Larimer J., McCowan C., Murphy C., Neiman D., Pearson M., RA Priest M., Roberts A., Saif S., Shea T., Sisk P., Sykes S., RA Wortman J., Nusbaum C., Birren B.; RT "The Genome Sequence of Acinetobacter gerneri CIP 107464."; RL Submitted (FEB-2013) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:ENV34948.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; APPN01000051; ENV34948.1; -; Genomic_DNA. DR RefSeq; WP_004857426.1; NZ_KB849537.1. DR EnsemblBacteria; ENV34948; ENV34948; F960_00919. DR PATRIC; fig|1120926.3.peg.879; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000013117; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000013117}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000013117}. FT DOMAIN 199 364 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 443 AA; 49480 MW; 7C34245C916DDBB1 CRC64; MEYFDRHQGG ERAILVSVSV QLLDDLDAEE FSLLAKSAGA EILEHIHASR IKPDPKLFVG SGKAEELAEL VKSLEAELAI FDHSLSPAQE RNLERILQCR VVDRTGLILD IFAQRARTHE GKLQVELAQL EHLSSRLVRG WTHLERQKGG IGLRGPGESQ LETDRRLLRI RMGQLKDKLE KVRQTRVQGR AARQKASVPT VSLVGYTNAG KSTLFNILAD SEVYAANQLF ATLDPTLRRL NWDGIGALVL ADTVGFVRNL PHSLVESFKA TLEETLEATL LLHVIDSSSP DMLEQIDAVE SVLKEIGADV PVLRIYNKID QSGDEAKIIY AKPHLPDRVY VSAHTGQGLD LLKQAVQECL MGQIQTFDVV LKPSYGKLRT QLYALNVIQS ENYDDEGNLH LSVSMAPHKL EQLIKQAHLP IDQILGDKAK QFHRPLEEFE IKS // ID N9GU86_ACIHA Unreviewed; 445 AA. AC N9GU86; DT 26-JUN-2013, integrated into UniProtKB/TrEMBL. DT 26-JUN-2013, sequence version 1. DT 07-JUN-2017, entry version 26. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=F927_00465 {ECO:0000313|EMBL:ENW20584.1}; OS Acinetobacter haemolyticus CIP 64.3. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Moraxellaceae; Acinetobacter. OX NCBI_TaxID=1217659 {ECO:0000313|EMBL:ENW20584.1, ECO:0000313|Proteomes:UP000017667}; RN [1] {ECO:0000313|EMBL:ENW20584.1, ECO:0000313|Proteomes:UP000017667} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CIP 64.3 {ECO:0000313|EMBL:ENW20584.1, RC ECO:0000313|Proteomes:UP000017667}; RG The Broad Institute Genome Sequencing Platform; RG The Broad Institute Genome Sequencing Center for Infectious Disease; RA Cerqueira G., Feldgarden M., Courvalin P., Perichon B., RA Grillot-Courvalin C., Clermont D., Rocha E., Yoon E.-J., Nemec A., RA Walker B., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B., RA Abouelleil A., Alvarado L., Arachchi H.M., Berlin A.M., Chapman S.B., RA Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M., Howarth C., RA Imamovic A., Larimer J., McCowan C., Murphy C., Neiman D., Pearson M., RA Priest M., Roberts A., Saif S., Shea T., Sisk P., Sykes S., RA Wortman J., Nusbaum C., Birren B.; RT "The Genome Sequence of Acinetobacter haemolyticus CIP 64.3."; RL Submitted (FEB-2013) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:ENW20584.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; APQQ01000009; ENW20584.1; -; Genomic_DNA. DR RefSeq; WP_005086735.1; NZ_KB849812.1. DR EnsemblBacteria; ENW20584; ENW20584; F927_00465. DR PATRIC; fig|1217659.3.peg.455; -. DR Proteomes; UP000017667; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000017667}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000017667}. FT DOMAIN 200 365 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 445 AA; 49786 MW; F167FDF56300222F CRC64; MENFEQRQHG ERAILVNVSV QLLDDLDAEE FRLLAQSAGA EILEHVSVQR QKPDPKFFIG SGKVEEIAEL VRALDAELVI FDHSLSPAQE RNLEKVLKCR VIDRTGLILD IFALRARTHE GKLQVELAQL KHLSTRLIRG FTGNLEQQKG GIGLRGPGES QLETDRRLIR VRITQLKDKL IKVQQTRLQG RAARQKAAIP TISLVGYTNA GKSTLFNILA KSDVYAADQL FATLDPTLRR LEWDGIGTVV LADTVGFVRN LQHDLVESFK ATLEETLEAT LLLHVVDSSS PNMPEQIEAV ESVLKEIGAD APILHVYNKI DLSGDTAKIT YKAPELPDRV YLSAHSGQGL DLLSQAVQQC LMGQLQQFDL VLKPAYGKLR TQLYTLNVIQ SEHYDDEGDL HLSVCIAPHK LEQLIKQAHL PLDEIVGAKS FLFHRVLEEF ESKQE // ID N9U631_9GAMM Unreviewed; 428 AA. AC N9U631; DT 26-JUN-2013, integrated into UniProtKB/TrEMBL. DT 26-JUN-2013, sequence version 1. DT 30-AUG-2017, entry version 30. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=G114_00610 {ECO:0000313|EMBL:ENY73900.1}; OS Aeromonas diversa CDC 2478-85. OC Bacteria; Proteobacteria; Gammaproteobacteria; Aeromonadales; OC Aeromonadaceae; Aeromonas. OX NCBI_TaxID=1268237 {ECO:0000313|EMBL:ENY73900.1, ECO:0000313|Proteomes:UP000023775}; RN [1] {ECO:0000313|EMBL:ENY73900.1, ECO:0000313|Proteomes:UP000023775} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=2478-85 {ECO:0000313|EMBL:ENY73900.1, RC ECO:0000313|Proteomes:UP000023775}; RX PubMed=23792745; DOI=10.1128/genomeA.00330-13; RA Farfan M., Spataro N., Sanglas A., Albarral V., Loren J.G., Bosch E., RA Fuste M.C.; RT "Draft Genome Sequence of the Aeromonas diversa Type Strain."; RL Genome Announc. 1:S69-S82(2013). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:ENY73900.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; APVG01000001; ENY73900.1; -; Genomic_DNA. DR RefSeq; WP_005345796.1; NZ_CDCE01000020.1. DR EnsemblBacteria; ENY73900; ENY73900; G114_00610. DR PATRIC; fig|1268237.3.peg.120; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000023775; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000023775}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}. FT DOMAIN 198 365 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 428 AA; 48309 MW; 4B62735C07CC70D5 CRC64; MFDRYEGGEQ AVLVHVNFSD EGEREDLEEL RMLVSSAGVN TLAVVTTSRG APSSKYFVGS GKAEEIAEQV RLLGADVVIF NHALTPAQER NLERLIECRV VDRTGLILDI FAQRARTHEG KLQVELAQLR HLSTRLVRGW THLERQKGGI GLRGPGETQL ETDRRLLRER IKYILRRLDK VAKQREQGRR ARNRNEVPTV SLVGYTNAGK STLFNQLTAA SVYAADQLFA TLDPTLRRLD VKDVGDVILA DTVGFIRHLP HDLVAAFKAT LQETREADLL LHVVDCADEQ MQENIASVHS VLAEIEADDR PQLMICNKID KLADRPCALE RDEEGRPMRV WLSAQSGEGC DLLYQALTEL LSGAMVHHLL RLPPSQARLR SIFYRLKGIE QESFNEEGDC LLEVRLPAAD WNRLLKQEGD MLQRFISH // ID N9UP53_9SPHN Unreviewed; 446 AA. AC N9UP53; DT 26-JUN-2013, integrated into UniProtKB/TrEMBL. DT 26-JUN-2013, sequence version 1. DT 07-JUN-2017, entry version 31. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=EBMC1_16684 {ECO:0000313|EMBL:ENY80124.1}; OS Sphingopyxis sp. MC1. OC Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales; OC Sphingomonadaceae; Sphingopyxis. OX NCBI_TaxID=1174684 {ECO:0000313|EMBL:ENY80124.1, ECO:0000313|Proteomes:UP000013072}; RN [1] {ECO:0000313|EMBL:ENY80124.1, ECO:0000313|Proteomes:UP000013072} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC1 {ECO:0000313|EMBL:ENY80124.1, RC ECO:0000313|Proteomes:UP000013072}; RA Lolas I.B., Kjeldal H., Almeida B., Le-Quy V., Gough H.L., RA Nielsen J.L.; RT "Differential expression analysis of membrane associated proteins from RT triclosan-degrading sphingopyxis."; RL Submitted (FEB-2013) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:ENY80124.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AOUN01000022; ENY80124.1; -; Genomic_DNA. DR RefSeq; WP_003051688.1; NZ_AOUN01000022.1. DR EnsemblBacteria; ENY80124; ENY80124; EBMC1_16684. DR PATRIC; fig|1174684.3.peg.3374; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000013072; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000013072}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}. FT DOMAIN 206 386 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 172 199 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 446 AA; 48979 MW; 0BE0F4B0869868F9 CRC64; MSDSAEEVTR GAPALLVVPE WHGQRLSRDL DARVEEVKGL AVAIGLKVVA AHPLRLRQTR AATLIGVGQI EAIKPAIAAH DVQLVIVDAA LTAIQQRNLE TAFGTKVIDR TGLILEIFGE RAATAEGRLQ VELAHLDYQA GRLVRSWTHL ERQRGGFGFL GGPGETQIEA DRRMIRNRMA RIRRQLDDAR RTRQLQRAKR QRAPWPVVAL VGYTNAGKST LFNRLTGSDV MAEDMLFATL DPTMREIRLP GIDKAILSDT VGFVSDLPTE LVAAFRATLE EVTTADLIVH VRDIVHPDSD AQYDDVKAIL DSLGVNGPQD GEGEDAADPI PQIEIWNKID TAAPDRRAEI VEIAARRSDV AVISAFTGEG VEAARTLMAA RLTEGHEIQQ IFLGFDEGEA LAWLHARGEV LDNRAEGEGH VLTVRLDPAD QARFRRLWPA KGLPKP // ID N9Y1Y5_9CLOT Unreviewed; 598 AA. AC N9Y1Y5; DT 26-JUN-2013, integrated into UniProtKB/TrEMBL. DT 26-JUN-2013, sequence version 1. DT 07-JUN-2017, entry version 27. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=HMPREF1092_01394 {ECO:0000313|EMBL:ENZ02159.1}; OS Clostridium colicanis 209318. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=999411 {ECO:0000313|EMBL:ENZ02159.1, ECO:0000313|Proteomes:UP000013097}; RN [1] {ECO:0000313|EMBL:ENZ02159.1, ECO:0000313|Proteomes:UP000013097} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=209318 {ECO:0000313|EMBL:ENZ02159.1, RC ECO:0000313|Proteomes:UP000013097}; RG The Broad Institute Genome Sequencing Platform; RA Earl A., Ward D., Feldgarden M., Gevers D., Courvalin P., Lambert T., RA Walker B., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B., RA Abouelleil A., Alvarado L., Arachchi H.M., Berlin A.M., Chapman S.B., RA Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M., Howarth C., RA Imamovic A., Larimer J., McCowan C., Murphy C., Neiman D., Pearson M., RA Priest M., Roberts A., Saif S., Shea T., Sisk P., Sykes S., RA Wortman J., Nusbaum C., Birren B.; RT "The Genome Sequence of Clostridium colicanis 209318."; RL Submitted (JAN-2013) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:ENZ02159.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGYT01000008; ENZ02159.1; -; Genomic_DNA. DR RefSeq; WP_002597895.1; NZ_KB850956.1. DR EnsemblBacteria; ENZ02159; ENZ02159; HMPREF1092_01394. DR PATRIC; fig|999411.4.peg.1370; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000013097; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000013097}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000013097}. FT DOMAIN 364 541 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 598 AA; 67383 MW; 2C8A0D9F25F16748 CRC64; MIHGNVDGVR NSILNELDLL YGIKTQKTEF CSTEIINTIV KLSTQIEREI SVAIDRRGKV TSIAIGDSTS VELPILDINE KRLSGVRVIH THPNGYSNLS ALDLTALLKL KLDAIAAIGI YEGKIIDFSI ANLTVYNNNL VYEEKNNISL DGLFSINILD KIKYAESLIK ENDVEEDLEE KAILVGSDTK ESLEELVELT KACEIPVLKT VFQGRNKIDP AFYIGRGKVL EIANLRQTER ANLIIFDDEL SGAQVRNLEN AIGAKVIDRT TLILEIFARR AKSKEAKIQV ELAQLKYRKS RLMGLGTVLS RTGGGIGTRG PGEKKLETDK RHINETIYDL NSELKKIKKT REVQREKRNK ENIPKVSLVG YTNAGKSTLR NALCKVAALK DNRTKEEVFE ADMLFATLDI TTRAIILKNK GLITLTDTVG FVRKLPHDLV EAFKSTLEEV IYADLLCHVV DSSSEDAIEQ VKAVEEVLRE LDSLDKETIL VLNKVDKASE EQLEEIKKEF SNYNIVEISA KQEVNLDLLI EKIEEKLPYS LKKVEVVIPY NRGDVVSLLH RNARILKEDY VNEGTLMEVE VDEEIYNKTK EYIIKELN // ID O33230_MYCTU Unreviewed; 495 AA. AC O33230; F2GPJ8; I6Y1K1; DT 01-JAN-1998, integrated into UniProtKB/TrEMBL. DT 01-JAN-1998, sequence version 1. DT 05-JUL-2017, entry version 116. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:CCP45523.1}; GN OrderedLocusNames=Rv2725c {ECO:0000313|EMBL:CCP45523.1}; OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv). OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae; OC Mycobacterium; Mycobacterium tuberculosis complex. OX NCBI_TaxID=83332 {ECO:0000313|EMBL:CCP45523.1, ECO:0000313|Proteomes:UP000001584}; RN [1] {ECO:0000313|EMBL:CCP45523.1, ECO:0000313|Proteomes:UP000001584} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 25618 / H37Rv {ECO:0000313|Proteomes:UP000001584}; RX PubMed=9634230; DOI=10.1038/31159; RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C., Harris D., RA Gordon S.V., Eiglmeier K., Gas S., Barry C.E.III., Tekaia F., RA Badcock K., Basham D., Brown D., Chillingworth T., Connor R., RA Davies R., Devlin K., Feltwell T., Gentles S., Hamlin N., Holroyd S., RA Hornsby T., Jagels K., Krogh A., McLean J., Moule S., Murphy L., RA Oliver K., Osborne J., Quail M.A., Rajandream M.A., Rogers J., RA Rutter S., Seeger K., Skelton J., Squares R., Squares S., RA Sulston J.E., Taylor K., Whitehead S., Barrell B.G.; RT "Deciphering the biology of Mycobacterium tuberculosis from the RT complete genome sequence."; RL Nature 393:537-544(1998). RN [2] {ECO:0000213|PubMed:21969609} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21969609; DOI=10.1074/mcp.M111.011445; RA Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., RA Yadav A.K., Shrivastava P., Marimuthu A., Anand S., Sundaram H., RA Kingsbury R., Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., RA Katoch K., Katoch V.M., Kumar P., Chaerkady R., Ramachandran S., RA Dash D., Pandey A.; RT "Proteogenomic analysis of Mycobacterium tuberculosis by high RT resolution mass spectrometry."; RL Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AL123456; CCP45523.1; -; Genomic_DNA. DR RefSeq; NP_217241.1; NC_000962.3. DR RefSeq; WP_003413984.1; NZ_KK339370.1. DR ProteinModelPortal; O33230; -. DR SMR; O33230; -. DR STRING; 83332.Rv2725c; -. DR PaxDb; O33230; -. DR PRIDE; O33230; -. DR EnsemblBacteria; CCP45523; CCP45523; Rv2725c. DR GeneID; 888241; -. DR KEGG; mtu:Rv2725c; -. DR KEGG; mtv:RVBD_2725c; -. DR PATRIC; fig|83332.111.peg.3030; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR PhylomeDB; O33230; -. DR Proteomes; UP000001584; Chromosome. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0005886; C:plasma membrane; IDA:MTBBASE. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0043022; F:ribosome binding; IBA:GO_Central. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 1: Evidence at protein level; KW Complete proteome {ECO:0000313|Proteomes:UP000001584}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000001584}. FT DOMAIN 271 440 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 495 AA; 53328 MW; F82BA93092945121 CRC64; MPANSDARPA ATCHHRVLAM TYPDPPQTGL SDFTPSLGEL ALEDRSALRR VAGLSTELAD VSEVEYRQLR LERVVLVGVW TEGSAADNRA SLAELAALAE TAGSQVLEGL IQRRDKPDPS TYIGSGKAAE LREVIVATGA DTVICDGELS PAQLTALEKA VQVKVIDRTA LILDIFAQHA TSREGKAQVS LAQMEYMLPR LRGWGESMSR QAGGRAGGSG GGVGLRGPGE TKIETDRRRI RERMAKLRRD IRAMKQVRDT QRSRRRHSDV PSIAIVGYTN AGKSSLLNAL TGAGVLVQDA LFATLEPTTR RAEFGDGRPV VLTDTVGFVR HLPTQLVEAF RSTLEEVVHA DLLVHVVDGS DGHPLAQIDA VRQVISEVIA DHDGDPPPEL LVVNKVDVAS DLMLAKLRHG LPGAVFVSAR TGDGIDALRR RMAELVVPAD TAVDVVIPYD RGDLVARVHA DGRIQQAEHK PEGTRIKARV PEALAATLRE FAPRA // ID O67743_AQUAE Unreviewed; 370 AA. AC O67743; DT 01-AUG-1998, integrated into UniProtKB/TrEMBL. DT 01-AUG-1998, sequence version 1. DT 07-JUN-2017, entry version 117. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:AAC07703.1}; GN OrderedLocusNames=aq_1908 {ECO:0000313|EMBL:AAC07703.1}; OS Aquifex aeolicus (strain VF5). OC Bacteria; Aquificae; Aquificales; Aquificaceae; Aquifex. OX NCBI_TaxID=224324 {ECO:0000313|EMBL:AAC07703.1, ECO:0000313|Proteomes:UP000000798}; RN [1] {ECO:0000313|EMBL:AAC07703.1, ECO:0000313|Proteomes:UP000000798} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=VF5 {ECO:0000313|EMBL:AAC07703.1, RC ECO:0000313|Proteomes:UP000000798}; RX PubMed=9537320; DOI=10.1038/32831; RA Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L., RA Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R., RA Feldman R.A., Short J.M., Olson G.J., Swanson R.V.; RT "The complete genome of the hyperthermophilic bacterium Aquifex RT aeolicus."; RL Nature 392:353-358(1998). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000657; AAC07703.1; -; Genomic_DNA. DR PIR; C70464; C70464. DR RefSeq; NP_214311.1; NC_000918.1. DR RefSeq; WP_010881247.1; NC_000918.1. DR ProteinModelPortal; O67743; -. DR STRING; 224324.aq_1908; -. DR EnsemblBacteria; AAC07703; AAC07703; aq_1908. DR GeneID; 1193548; -. DR KEGG; aae:aq_1908; -. DR PATRIC; fig|224324.8.peg.1477; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR InParanoid; O67743; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000000798; Chromosome. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0043022; F:ribosome binding; IBA:GO_Central. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000000798}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000000798}. FT DOMAIN 197 367 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 159 193 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 370 AA; 42100 MW; EBD137F19AB1D215 CRC64; MRAVLVGVWG RDISKEFSKE SIKELKGLVE AVGGKTLGYI LQKRNFPDQK YYIGQGKAQE IREIVRGTKA DTVVFDDFLT PAQISNLEKV INAKVLDRTD LVLEIFSRRA KTKEAKLQVE LAKLMHELPR LHGKGKALSR LGGGLGTRGP GEQETEVRKR LIKKRIHRIK KELEEIKKRR REQRKRRERS EKGERIVRVA IVGYTNAGKS TLMNALTKKD TYVANMLFAT LDTKTSARVI YPDFKLLFTD TVGFIRKLPP ELIESFKATL EEVQEADIIL HVVDVSDEGW LDYVSTVNEV LKELGAEEKP IIYALNKADK LVETENEMNH LPHPAFIEGD AVLISAEKRW GLGKLLDKIV EVAKREEVYI // ID O69972_STRCO Unreviewed; 497 AA. AC O69972; DT 01-AUG-1998, integrated into UniProtKB/TrEMBL. DT 01-AUG-1998, sequence version 1. DT 07-JUN-2017, entry version 109. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=SCO5796 {ECO:0000313|EMBL:CAA18333.1}; OS Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145). OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae; OC Streptomyces; Streptomyces albidoflavus group. OX NCBI_TaxID=100226 {ECO:0000313|Proteomes:UP000001973}; RN [1] {ECO:0000313|EMBL:CAA18333.1, ECO:0000313|Proteomes:UP000001973} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-471 / A3(2) / M145 RC {ECO:0000313|Proteomes:UP000001973}; RX PubMed=12000953; DOI=10.1038/417141a; RA Bentley S.D., Chater K.F., Cerdeno-Tarraga A.M., Challis G.L., RA Thomson N.R., James K.D., Harris D.E., Quail M.A., Kieser H., RA Harper D., Bateman A., Brown S., Chandra G., Chen C.W., Collins M., RA Cronin A., Fraser A., Goble A., Hidalgo J., Hornsby T., Howarth S., RA Huang C.H., Kieser T., Larke L., Murphy L., Oliver K., O'Neil S., RA Rabbinowitsch E., Rajandream M.A., Rutherford K., Rutter S., RA Seeger K., Saunders D., Sharp S., Squares R., Squares S., Taylor K., RA Warren T., Wietzorrek A., Woodward J., Barrell B.G., Parkhill J., RA Hopwood D.A.; RT "Complete genome sequence of the model actinomycete Streptomyces RT coelicolor A3(2)."; RL Nature 417:141-147(2002). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AL939125; CAA18333.1; -; Genomic_DNA. DR PIR; T35116; T35116. DR RefSeq; NP_629920.1; NC_003888.3. DR RefSeq; WP_011030461.1; NC_003888.3. DR ProteinModelPortal; O69972; -. DR STRING; 100226.SCO5796; -. DR EnsemblBacteria; CAA18333; CAA18333; CAA18333. DR GeneID; 1101238; -. DR KEGG; sco:SCO5796; -. DR PATRIC; fig|100226.15.peg.5887; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR InParanoid; O69972; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR PhylomeDB; O69972; -. DR Proteomes; UP000001973; Chromosome. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0043022; F:ribosome binding; IBA:GO_Central. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 2. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000001973}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000001973}. FT DOMAIN 275 440 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 497 AA; 54507 MW; FB3646D4D6E54028 CRC64; MTSSSSPSQD TKRLAQTYPE GLRADALMEE DVAWNRGNDS QWDGEQFDRS DRAALRRVAG LSTELEDVTE VEYRQLRLER VVLVGVWTSG TVQDAENSLA ELAALAETAG ALVLDGVVQR RDKPDAATYI GSGKAEELRD VVLHTGADTV ICDGELSPGQ LIHLEDVVKV KVIDRTALIL DIFAQHAKSR EGKAQVALAQ MQYMLPRLRG WGQSLSRQMG GGKGGGLATR GPGETKIETD RRRIREKMAK MRREIAEMKT GREIKRQERK RHKVPSVAIA GYTNAGKSSL LNRLTGAGVL VENALFATLD PTVRRAETPS GRLYTLADTV GFVRHLPHHL VEAFRSTMEE VGDSDLILHV VDGSHPVPEE QLAAVREVIR DVGATDVPEI VVINKADMAD PLVLQRLLRI EKRAIAVSAR TGQNIDQLLA LIDNELPRPS VEIEALVPYT HGKLVARAHD EGEVISEEHT PEGTLLKVRV HEELAAELAP YVPAPLA // ID O84383_CHLTR Unreviewed; 447 AA. AC O84383; DT 01-NOV-1998, integrated into UniProtKB/TrEMBL. DT 01-NOV-1998, sequence version 1. DT 05-JUL-2017, entry version 97. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:AAC67975.1}; GN OrderedLocusNames=CT_379 {ECO:0000313|EMBL:AAC67975.1}; OS Chlamydia trachomatis (strain D/UW-3/Cx). OC Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae; OC Chlamydia/Chlamydophila group; Chlamydia. OX NCBI_TaxID=272561 {ECO:0000313|EMBL:AAC67975.1, ECO:0000313|Proteomes:UP000000431}; RN [1] {ECO:0000313|EMBL:AAC67975.1, ECO:0000313|Proteomes:UP000000431} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=D/UW-3/Cx {ECO:0000313|Proteomes:UP000000431}; RX PubMed=9784136; DOI=10.1126/science.282.5389.754; RA Stephens R.S., Kalman S., Lammel C.J., Fan J., Marathe R., Aravind L., RA Mitchell W.P., Olinger L., Tatusov R.L., Zhao Q., Koonin E.V., RA Davis R.W.; RT "Genome sequence of an obligate intracellular pathogen of humans: RT Chlamydia trachomatis."; RL Science 282:754-759(1998). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE001273; AAC67975.1; -; Genomic_DNA. DR PIR; G71521; G71521. DR RefSeq; NP_219888.1; NC_000117.1. DR RefSeq; WP_010725178.1; NC_000117.1. DR ProteinModelPortal; O84383; -. DR EnsemblBacteria; AAC67975; AAC67975; CT_379. DR GeneID; 884738; -. DR KEGG; ctr:CT_379; -. DR PATRIC; fig|272561.5.peg.408; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR InParanoid; O84383; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR Proteomes; UP000000431; Chromosome. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0043022; F:ribosome binding; IBA:GO_Central. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000000431}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000000431}. FT DOMAIN 227 393 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 193 223 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 447 AA; 50913 MW; AA1D9C02CECC037C CRC64; MKKDNRDGKK EWQSAIGWRF LLPREEQDPA QALAVCCYTN RAEQDRVPEY VEELISLANS CDLSVLETCT WLLRAPSSSF YLNEGKLEEI ERILEEFPTI GTLLIDEEIS PSQQRNLEKR LRVVVLDRTE LILEIFASRA LTAEAGLQVE LAQARYLLPR LKRMWGHLSR QKSGGSGGGF VKGEGEKQIE LDRRIVRERI HKLSRDLKNV ERQREERRKA KKRNQIPTFA LIGYTNSGKS TLLNLLTSAD TYVENKLFAT LDPKTRRCVL PCGQRVLLTD TVGFIRKLPH TLVAAFKSTL EAALQEDILL HVVDASHPLA LEYVETTKAI LQELGITQPQ VITVLNKMDK VADGVTASRL RLMSPNPVCV SAKTGEGIRE LLRSMEDMVQ EEYPQATLHL PYKEYGLFTE LCDAGLVISH YYENDLLIVK AFLPNNLQKR YSEYIVE // ID P73965_SYNY3 Unreviewed; 534 AA. AC P73965; DT 01-FEB-1997, integrated into UniProtKB/TrEMBL. DT 01-FEB-1997, sequence version 1. DT 05-JUL-2017, entry version 110. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:BAA18033.1}; OS Synechocystis sp. (strain PCC 6803 / Kazusa). OC Bacteria; Cyanobacteria; Synechococcales; Merismopediaceae; OC Synechocystis. OX NCBI_TaxID=1111708 {ECO:0000313|EMBL:BAA18033.1, ECO:0000313|Proteomes:UP000001425}; RN [1] {ECO:0000313|EMBL:BAA18033.1, ECO:0000313|Proteomes:UP000001425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=PCC 6803 / Kazusa {ECO:0000313|Proteomes:UP000001425}; RX PubMed=8905231; DOI=10.1093/dnares/3.3.109; RA Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y., RA Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., RA Hosouchi T., Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., RA Shimpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., RA Tabata S.; RT "Sequence analysis of the genome of the unicellular cyanobacterium RT Synechocystis sp. strain PCC6803. II. Sequence determination of the RT entire genome and assignment of potential protein-coding regions."; RL DNA Res. 3:109-136(1996). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BA000022; BAA18033.1; -; Genomic_DNA. DR PIR; S75472; S75472. DR ProteinModelPortal; P73965; -. DR IntAct; P73965; 1. DR STRING; 1148.SYNGTS_1457; -. DR EnsemblBacteria; BAA18033; BAA18033; BAA18033. DR KEGG; syn:slr1521; -. DR HOGENOM; HOG000260368; -. DR InParanoid; P73965; -. DR KO; K03665; -. DR OMA; EREVIIT; -. DR PhylomeDB; P73965; -. DR Proteomes; UP000001425; Chromosome. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0043022; F:ribosome binding; IBA:GO_Central. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000001425}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000001425}. FT DOMAIN 362 532 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 321 358 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 534 AA; 58540 MW; 1467FB826E377FB8 CRC64; MELAQRLGAI SQEIKQPVSV YVNRRGQIIR VGVGTPRQTQ IPPLELPRYG EKRLSGIRCL TTDLKGEAPR ESSLIAMALQ RLDALVVLSV TGQGFAKRGG GVTGYIDTGY LAHLLPQSSD DMGDRVADWV VSPAVALEDL AEEAILDLVE SLEAEFEREF IARQVEAGQE RVLVMGLKTS ELDDQSFAEG LTELERLVDS AGAQVLQVMQ QNRSKPHPQT VVGEGKVEEL ALAVQTTGAN LVVFDRDLSA AQVRNLEQRC GVRVIDRTEL ILDIFAQRAQ SRAGKLQVEL AQLEYLLPKL VGRGQGMSRL GGGIGTRGPG ETKLETERRT IQSRIAKLQK QVNELQSHRS RLRNQRQQQA VPTVAIVGYT NAGKSTLLNA LTQADIYAAD QLFATLDPTT RRLSLLDPEN QTYHPILLTD TVGFIHKLPD ALVDAFRATL EEVTEADLLL QVVDLSDRAW RRQIASVANI LAEMPLATAP MVMVFNKIDQ VPSEALAAAQ ADYPEAIFLA AAQGIGLETL KKRLLEQILT DLTD // ID Q029X1_SOLUE Unreviewed; 394 AA. AC Q029X1; DT 14-NOV-2006, integrated into UniProtKB/TrEMBL. DT 14-NOV-2006, sequence version 1. DT 07-JUN-2017, entry version 70. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Acid_1161 {ECO:0000313|EMBL:ABJ82155.1}; OS Solibacter usitatus (strain Ellin6076). OC Bacteria; Acidobacteria; Solibacteres; Solibacterales; OC Solibacteraceae; Candidatus Solibacter. OX NCBI_TaxID=234267 {ECO:0000313|EMBL:ABJ82155.1, ECO:0000313|Proteomes:UP000000671}; RN [1] {ECO:0000313|Proteomes:UP000000671} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Ellin6076 {ECO:0000313|Proteomes:UP000000671}; RX PubMed=19201974; DOI=10.1128/AEM.02294-08; RA Ward N.L., Challacombe J.F., Janssen P.H., Henrissat B., RA Coutinho P.M., Wu M., Xie G., Haft D.H., Sait M., Badger J., RA Barabote R.D., Bradley B., Brettin T.S., Brinkac L.M., Bruce D., RA Creasy T., Daugherty S.C., Davidsen T.M., DeBoy R.T., Detter J.C., RA Dodson R.J., Durkin A.S., Ganapathy A., Gwinn-Giglio M., Han C.S., RA Khouri H., Kiss H., Kothari S.P., Madupu R., Nelson K.E., Nelson W.C., RA Paulsen I., Penn K., Ren Q., Rosovitz M.J., Selengut J.D., RA Shrivastava S., Sullivan S.A., Tapia R., Thompson L.S., Watkins K.L., RA Yang Q., Yu C., Zafar N., Zhou L., Kuske C.R.; RT "Three genomes from the phylum Acidobacteria provide insight into the RT lifestyles of these microorganisms in soils."; RL Appl. Environ. Microbiol. 75:2046-2056(2009). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000473; ABJ82155.1; -; Genomic_DNA. DR ProteinModelPortal; Q029X1; -. DR STRING; 234267.Acid_1161; -. DR EnsemblBacteria; ABJ82155; ABJ82155; Acid_1161. DR KEGG; sus:Acid_1161; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000000671; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000000671}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000000671}. FT DOMAIN 153 341 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 394 AA; 42691 MW; 972704746FB12083 CRC64; MQTRPAPEAA TLIGQGKVEE LAASVLSTEA DVVIFDQDLS PTQQRNLEKA LATKVIDRTQ LILDIFASRA RTREGRLQVE LAQLNYLLPR LAGRGVQMSR LGGGIGTRGP GETQLETDRR RIAKRIKKVE DELEGVRAGR ALHRRRRSAV PLATLALAGY TNAGKSTLFN RLTRASVLAD SKMFATLDPT VRPLVLPSRR RVLMSDTVGF IRNLPTTLVK AFRATLEEVN EAALILHVVD ASSPTAPEHT AHVLKVLAEI GAHEVPQILV LNKVDLLAAG DADAASLQRR LLAGLGAAHG EDDPDPSVFS GKMRAVAISA TSGAGIDTLM AAIDEVLPLD PVVRATLDLD SGDGATLALL HEFGRVIETR YHDDRVEVEV DLPESLERRL RSRQ // ID Q036W5_LACP3 Unreviewed; 431 AA. AC Q036W5; DT 14-NOV-2006, integrated into UniProtKB/TrEMBL. DT 14-NOV-2006, sequence version 1. DT 07-JUN-2017, entry version 78. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=LSEI_1999 {ECO:0000313|EMBL:ABJ70757.1}; OS Lactobacillus paracasei (strain ATCC 334 / BCRC 17002 / CIP 107868 / OS KCTC 3260 / NRRL B-441). OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; OC Lactobacillus. OX NCBI_TaxID=321967 {ECO:0000313|EMBL:ABJ70757.1, ECO:0000313|Proteomes:UP000001651}; RN [1] {ECO:0000313|EMBL:ABJ70757.1, ECO:0000313|Proteomes:UP000001651} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 334 / BCRC 17002 / CIP 107868 / KCTC 3260 / NRRL B-441 RC {ECO:0000313|Proteomes:UP000001651}; RX PubMed=17030793; DOI=10.1073/pnas.0607117103; RA Makarova K., Slesarev A., Wolf Y., Sorokin A., Mirkin B., Koonin E., RA Pavlov A., Pavlova N., Karamychev V., Polouchine N., Shakhova V., RA Grigoriev I., Lou Y., Rohksar D., Lucas S., Huang K., Goodstein D.M., RA Hawkins T., Plengvidhya V., Welker D., Hughes J., Goh Y., Benson A., RA Baldwin K., Lee J.H., Diaz-Muniz I., Dosti B., Smeianov V., RA Wechter W., Barabote R., Lorca G., Altermann E., Barrangou R., RA Ganesan B., Xie Y., Rawsthorne H., Tamir D., Parker C., Breidt F., RA Broadbent J., Hutkins R., O'Sullivan D., Steele J., Unlu G., Saier M., RA Klaenhammer T., Richardson P., Kozyavkin S., Weimer B., Mills D.; RT "Comparative genomics of the lactic acid bacteria."; RL Proc. Natl. Acad. Sci. U.S.A. 103:15611-15616(2006). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000423; ABJ70757.1; -; Genomic_DNA. DR RefSeq; WP_011674707.1; NC_008526.1. DR RefSeq; YP_807199.1; NC_008526.1. DR ProteinModelPortal; Q036W5; -. DR EnsemblBacteria; ABJ70757; ABJ70757; LSEI_1999. DR GeneID; 4420546; -. DR KEGG; lca:LSEI_1999; -. DR PATRIC; fig|321967.11.peg.1962; -. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR Proteomes; UP000001651; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000001651}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Hydrolase {ECO:0000313|EMBL:ABJ70757.1}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000001651}. FT DOMAIN 204 374 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 431 AA; 48187 MW; B3A1E9B2FCFF5B6E CRC64; MTEQLSNEPQ SENVLITGIS RQQPDFDYTM TELGELAKAD NYTVVGEVRQ SLDRAAAATY FGSGKVDEIR ELADVKNATT IIINDELSPS QLHNLEKQTK LHVIDRTQLI LDIFADRARS KAAKTQVEIA QLQYALPRLH PSANRLDQQV GGGAGFATRG SGETQLELDR RVLNKRISHL RRELKDASVG DQVRRARREG NDIPVVALVG YTNAGKSTTM NGLLNLFADR PEDKQVFEKD MLFATLDTSV RQLTLPDNRK FLLSDTVGFV SKLPHNLIDS FKATLAEAAN ADLLIQVVDY SDENYPEMMA ITEKTLKEVG IENIPMIEAY NKADLREGTR YPEVTGQRIV YSARDKNSLE ALTRLIKADI FGQDEEHTYL IPFDQGQLVS YLNQETVVKA TDYREDGTLI TAVVNPVQKG KLARFAVKEE V // ID Q03H31_PEDPA Unreviewed; 420 AA. AC Q03H31; DT 14-NOV-2006, integrated into UniProtKB/TrEMBL. DT 14-NOV-2006, sequence version 1. DT 07-JUN-2017, entry version 73. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=PEPE_0395 {ECO:0000313|EMBL:ABJ67491.1}; OS Pediococcus pentosaceus (strain ATCC 25745 / CCUG 21536 / LMG 10740 / OS 183-1w). OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; OC Pediococcus. OX NCBI_TaxID=278197 {ECO:0000313|EMBL:ABJ67491.1, ECO:0000313|Proteomes:UP000000773}; RN [1] {ECO:0000313|EMBL:ABJ67491.1, ECO:0000313|Proteomes:UP000000773} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 25745 / CCUG 21536 / LMG 10740 / 183-1w RC {ECO:0000313|Proteomes:UP000000773}; RX PubMed=17030793; DOI=10.1073/pnas.0607117103; RA Makarova K., Slesarev A., Wolf Y., Sorokin A., Mirkin B., Koonin E., RA Pavlov A., Pavlova N., Karamychev V., Polouchine N., Shakhova V., RA Grigoriev I., Lou Y., Rohksar D., Lucas S., Huang K., Goodstein D.M., RA Hawkins T., Plengvidhya V., Welker D., Hughes J., Goh Y., Benson A., RA Baldwin K., Lee J.H., Diaz-Muniz I., Dosti B., Smeianov V., RA Wechter W., Barabote R., Lorca G., Altermann E., Barrangou R., RA Ganesan B., Xie Y., Rawsthorne H., Tamir D., Parker C., Breidt F., RA Broadbent J., Hutkins R., O'Sullivan D., Steele J., Unlu G., Saier M., RA Klaenhammer T., Richardson P., Kozyavkin S., Weimer B., Mills D.; RT "Comparative genomics of the lactic acid bacteria."; RL Proc. Natl. Acad. Sci. U.S.A. 103:15611-15616(2006). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000422; ABJ67491.1; -; Genomic_DNA. DR RefSeq; WP_011673053.1; NC_008525.1. DR ProteinModelPortal; Q03H31; -. DR STRING; 278197.PEPE_0395; -. DR EnsemblBacteria; ABJ67491; ABJ67491; PEPE_0395. DR KEGG; ppe:PEPE_0395; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; FNNHAHV; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000000773; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000000773}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000000773}. FT DOMAIN 198 362 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 420 AA; 47455 MW; 46771AFF525636C7 CRC64; MNEKILIAGL ELPNMNLDYA MDELRSLAMA NNMDVVDQVT QKLERPNAAT YFGKGKVEDL VQIATALEVD TIVLNDELSP SQLTNLEKET NLHFIDRTGL ILEIFANRAH SREAKLQVEL AKLQYQLPRL RTSSTQRLDQ QTAGNTGGGF TNRGSGETKL ELNRRTIRNK INHINKELKE MTTSSDIQRK QRDKKDIPSV ALVGYTNTGK STTMNGLVRM YGRNEDKQVF EKDMLFATLD TSVRKLTFPD QKELVLSDTV GFVSHLPHQL VKAFRSTLAE AAKADLLVQI VDISDPHYRE MMQTTEDTLN EIGVTDIPMI YAFNKADLAG VSYPTLDGNE LTYSAKQLQS LEMVTALIKK QVFKNYVEAK FLIPFNEGQV VDFLNGNADV KKTDYTEEGT EITAELKEKD YQRLARYVIQ // ID Q03PN5_LACBA Unreviewed; 425 AA. AC Q03PN5; DT 14-NOV-2006, integrated into UniProtKB/TrEMBL. DT 14-NOV-2006, sequence version 1. DT 07-JUN-2017, entry version 77. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=LVIS_1771 {ECO:0000313|EMBL:ABJ64837.1}; OS Lactobacillus brevis (strain ATCC 367 / JCM 1170). OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; OC Lactobacillus. OX NCBI_TaxID=387344 {ECO:0000313|EMBL:ABJ64837.1, ECO:0000313|Proteomes:UP000001652}; RN [1] {ECO:0000313|EMBL:ABJ64837.1, ECO:0000313|Proteomes:UP000001652} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 367 / JCM 1170 {ECO:0000313|Proteomes:UP000001652}; RX PubMed=17030793; DOI=10.1073/pnas.0607117103; RA Makarova K., Slesarev A., Wolf Y., Sorokin A., Mirkin B., Koonin E., RA Pavlov A., Pavlova N., Karamychev V., Polouchine N., Shakhova V., RA Grigoriev I., Lou Y., Rohksar D., Lucas S., Huang K., Goodstein D.M., RA Hawkins T., Plengvidhya V., Welker D., Hughes J., Goh Y., Benson A., RA Baldwin K., Lee J.H., Diaz-Muniz I., Dosti B., Smeianov V., RA Wechter W., Barabote R., Lorca G., Altermann E., Barrangou R., RA Ganesan B., Xie Y., Rawsthorne H., Tamir D., Parker C., Breidt F., RA Broadbent J., Hutkins R., O'Sullivan D., Steele J., Unlu G., Saier M., RA Klaenhammer T., Richardson P., Kozyavkin S., Weimer B., Mills D.; RT "Comparative genomics of the lactic acid bacteria."; RL Proc. Natl. Acad. Sci. U.S.A. 103:15611-15616(2006). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000416; ABJ64837.1; -; Genomic_DNA. DR RefSeq; WP_011668388.1; NC_008497.1. DR ProteinModelPortal; Q03PN5; -. DR STRING; 387344.LVIS_1771; -. DR EnsemblBacteria; ABJ64837; ABJ64837; LVIS_1771. DR GeneID; 4412883; -. DR KEGG; lbr:LVIS_1771; -. DR PATRIC; fig|387344.15.peg.1680; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; FNNHAHV; -. DR Proteomes; UP000001652; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000001652}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000001652}. FT DOMAIN 202 370 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 425 AA; 46715 MW; 2DD046CF16AC1E9C CRC64; MEETPRTPVI TIGLNAGQAT FDYAMAELKN LVEANHMTVV EEVQQALSRP QPGTYFGTGK VEELATIVAD DGVDTVVVND ELTPSQIRNL EKVTKARIID RTGLILEIFA NRAQSREAKL QVQLAKLQYQ LPRLHTSASQ RLDQQTGSGG GGGFTNRGSG ESQTEISRRT LQRAITHVNH ELKEINQAAA TQRQQRERNQ LPSVALVGYT NAGKSTLMNA LVREFGKSDE KQVFVKNMLF ATLDTSVRQL TFPDQKKLLL SDTVGFVSQL PTQLVKAFRS TLAEAANADL LVQVVDYADP NKEAMMATTE QTLHDIGVTD VPMVTVFNKA DLTEATYPSR AGDQLILSAQ DPASIALLVQ TLKEKVFHNY VTADFLIPFA DGDVVAYLND HANVLSTGYE ATGTALKVEL QDTDFNRFKQ YVVTP // ID Q03V38_LEUMM Unreviewed; 433 AA. AC Q03V38; DT 14-NOV-2006, integrated into UniProtKB/TrEMBL. DT 14-NOV-2006, sequence version 1. DT 07-JUN-2017, entry version 77. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=LEUM_1857 {ECO:0000313|EMBL:ABJ62934.1}; OS Leuconostoc mesenteroides subsp. mesenteroides (strain ATCC 8293 / OS NCDO 523). OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Leuconostocaceae; OC Leuconostoc. OX NCBI_TaxID=203120 {ECO:0000313|EMBL:ABJ62934.1, ECO:0000313|Proteomes:UP000000362}; RN [1] {ECO:0000313|EMBL:ABJ62934.1, ECO:0000313|Proteomes:UP000000362} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 8293 / NCDO 523 {ECO:0000313|Proteomes:UP000000362}; RX PubMed=17030793; DOI=10.1073/pnas.0607117103; RA Makarova K., Slesarev A., Wolf Y., Sorokin A., Mirkin B., Koonin E., RA Pavlov A., Pavlova N., Karamychev V., Polouchine N., Shakhova V., RA Grigoriev I., Lou Y., Rohksar D., Lucas S., Huang K., Goodstein D.M., RA Hawkins T., Plengvidhya V., Welker D., Hughes J., Goh Y., Benson A., RA Baldwin K., Lee J.H., Diaz-Muniz I., Dosti B., Smeianov V., RA Wechter W., Barabote R., Lorca G., Altermann E., Barrangou R., RA Ganesan B., Xie Y., Rawsthorne H., Tamir D., Parker C., Breidt F., RA Broadbent J., Hutkins R., O'Sullivan D., Steele J., Unlu G., Saier M., RA Klaenhammer T., Richardson P., Kozyavkin S., Weimer B., Mills D.; RT "Comparative genomics of the lactic acid bacteria."; RL Proc. Natl. Acad. Sci. U.S.A. 103:15611-15616(2006). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000414; ABJ62934.1; -; Genomic_DNA. DR RefSeq; WP_010280121.1; NC_008531.1. DR ProteinModelPortal; Q03V38; -. DR STRING; 203120.LEUM_1857; -. DR EnsemblBacteria; ABJ62934; ABJ62934; LEUM_1857. DR GeneID; 29577450; -. DR KEGG; lme:LEUM_1857; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000000362; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000000362}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000000362}. FT DOMAIN 200 373 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 433 AA; 48553 MW; ED9836388E1BA175 CRC64; MQENPRKVFL VGLTTNQGNL DYELEELANL AKANNLEPVE TFTQKLERPN PSTYFGKGKV EELGEAVKTY DVDMIVVNDE LTPSQIRNLE KTTDATVVDR TGLILEIFAQ RAQTKVAKLQ VQLARLQYQL PRLRKSMSIS LDQQTGTGGA GFTSRGSGET KLEQSRQRIT SQMVHVRQEL ADLDKSENTR SMQRHANNLP NVALVGYTNA GKSTLMNRLL MRFGVGADND DSKQVFEKDM LFATLNTTVR QLTLPDKRQF LLSDTVGFVS KLPHNLVAAF KSTLQEAANA DLILHVVDVS DEHYKAMMET TEKTLTEIGV TGKPVITVYN KADRTELHYP DISGDNVITL SALDTNSQDA LIDLIVKHIF NDSEVVTLHI PFDKGNVVAQ LAAKHKFIEE QYDETGSWLT IELSEVERNL FQQYITKEKS MNS // ID Q04HC4_OENOB Unreviewed; 437 AA. AC Q04HC4; DT 14-NOV-2006, integrated into UniProtKB/TrEMBL. DT 14-NOV-2006, sequence version 1. DT 07-JUN-2017, entry version 70. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=OEOE_0155 {ECO:0000313|EMBL:ABJ56148.1}; OS Oenococcus oeni (strain ATCC BAA-331 / PSU-1). OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Leuconostocaceae; OC Oenococcus. OX NCBI_TaxID=203123 {ECO:0000313|EMBL:ABJ56148.1, ECO:0000313|Proteomes:UP000000774}; RN [1] {ECO:0000313|EMBL:ABJ56148.1, ECO:0000313|Proteomes:UP000000774} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-331 / PSU-1 {ECO:0000313|Proteomes:UP000000774}; RX PubMed=17030793; DOI=10.1073/pnas.0607117103; RA Makarova K., Slesarev A., Wolf Y., Sorokin A., Mirkin B., Koonin E., RA Pavlov A., Pavlova N., Karamychev V., Polouchine N., Shakhova V., RA Grigoriev I., Lou Y., Rohksar D., Lucas S., Huang K., Goodstein D.M., RA Hawkins T., Plengvidhya V., Welker D., Hughes J., Goh Y., Benson A., RA Baldwin K., Lee J.H., Diaz-Muniz I., Dosti B., Smeianov V., RA Wechter W., Barabote R., Lorca G., Altermann E., Barrangou R., RA Ganesan B., Xie Y., Rawsthorne H., Tamir D., Parker C., Breidt F., RA Broadbent J., Hutkins R., O'Sullivan D., Steele J., Unlu G., Saier M., RA Klaenhammer T., Richardson P., Kozyavkin S., Weimer B., Mills D.; RT "Comparative genomics of the lactic acid bacteria."; RL Proc. Natl. Acad. Sci. U.S.A. 103:15611-15616(2006). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000411; ABJ56148.1; -; Genomic_DNA. DR RefSeq; WP_002818070.1; NC_008528.1. DR ProteinModelPortal; Q04HC4; -. DR STRING; 203123.OEOE_0155; -. DR EnsemblBacteria; ABJ56148; ABJ56148; OEOE_0155. DR GeneID; 4415830; -. DR KEGG; ooe:OEOE_0155; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; FNNHAHV; -. DR Proteomes; UP000000774; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000000774}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000000774}. FT DOMAIN 211 383 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 170 197 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 437 AA; 49306 MW; 81EEB10D72E35645 CRC64; MAAQLFDTKK TKERVILTAI ENQKNSQNFD YAIEEFKNLA VADNLEVVDV LTQKYDRPNA ATYFGKGKVE ELKELVNAKE ARLVISNDDL TATQIRNLEK MIASDVRVVD RTGLILDIFA ARAKTKIAKL QVRLAQKQYQ LPRLHTSLAN ELDQQAGAGG ASFTSRGSGE TKLELNRRTI EEQISQIKTE LKSLLSSSTV QRKRRDNSGL KRVALVGYTN AGKSTWMNRI VERYSQIGND SEEKKVFEKD MLFATLDSTV RSIRLPNKRQ FLLSDTVGFI SNLPHNLVAS FQSTLEEASN SDLLVQIVDV SDPHYRDMLT TTSKTLRQIG AEQIPMVTIF NKADKAKLSY PERSGEDLIA SALDKKSLEA FIDLLNKKLF ADLKKVELLI PFDQGSVLSE LIENNQVLHQ EYNDKGTKIV LELSEAKIKQ YQRFVNI // ID Q07XW8_SHEFN Unreviewed; 435 AA. AC Q07XW8; DT 31-OCT-2006, integrated into UniProtKB/TrEMBL. DT 31-OCT-2006, sequence version 1. DT 30-AUG-2017, entry version 75. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Sfri_3310 {ECO:0000313|EMBL:ABI73146.1}; OS Shewanella frigidimarina (strain NCIMB 400). OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales; OC Shewanellaceae; Shewanella. OX NCBI_TaxID=318167 {ECO:0000313|EMBL:ABI73146.1, ECO:0000313|Proteomes:UP000000684}; RN [1] {ECO:0000313|EMBL:ABI73146.1, ECO:0000313|Proteomes:UP000000684} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NCIMB 400 {ECO:0000313|EMBL:ABI73146.1, RC ECO:0000313|Proteomes:UP000000684}; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., RA Pitluck S., Fredrickson J.K., Kolker E., McCuel L.A., DiChristina T., RA Nealson K.H., Newman D., Tiedje J.M., Zhou J., Romine M.F., RA Culley D.E., Serres M., Chertkov O., Brettin T., Bruce D., Han C., RA Tapia R., Gilna P., Schmutz J., Larimer F., Land M., Hauser L., RA Kyrpides N., Mikhailova N., Richardson P.; RT "Complete sequence of Shewanella frigidimarina NCIMB 400."; RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000447; ABI73146.1; -; Genomic_DNA. DR RefSeq; WP_011638749.1; NC_008345.1. DR ProteinModelPortal; Q07XW8; -. DR STRING; 318167.Sfri_3310; -. DR EnsemblBacteria; ABI73146; ABI73146; Sfri_3310. DR KEGG; sfr:Sfri_3310; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000000684; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000000684}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000000684}. FT DOMAIN 198 364 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 164 191 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 435 AA; 49033 MW; 92ADC8CEEC1EC215 CRC64; MFDRYEAGET AVLVHIDFSD EERREDLIEL QLLVESAGAR SVGVITGSRR SPDRKFFIGS GKAEELAAMV AATEANVVIF NHALSPAQER NLEVVCQCRV LDRTTLILDI FAQRARTHEG KMQVELAQLR HMSTRLIRGW THLERQKGGI GMRGPGETQL ETDRRLLRGR IKNINRRLDK VDKQREQSRR ARKRSDLATV SLVGYTNAGK STLFNALTSS DVYAADQLFA TLDPTLRKLS LPDGAVILAD TVGFIRHLPH DLVAAFKATL QETRQAEILL HVVDCADDNM TENFDQVQKV LEEIDADEIT QLIVCNKIDL LEDFAPRIDY DEDGKPERVW VSAQKRIGFD LLLKAITELI GEVICELTLK IPASAGHYLG QFYRLDAIQQ KEYDDLGNCI LSVRLSDANW RRLAKQSQGE LEAFIFEPSE VDVTC // ID Q08T47_STIAD Unreviewed; 567 AA. AC Q08T47; DT 31-OCT-2006, integrated into UniProtKB/TrEMBL. DT 31-OCT-2006, sequence version 1. DT 30-AUG-2017, entry version 66. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:ADO69914.1}; GN OrderedLocusNames=STAUR_2110 {ECO:0000313|EMBL:ADO69914.1}; GN ORFNames=STIAU_2244 {ECO:0000313|EMBL:EAU63676.1}; OS Stigmatella aurantiaca (strain DW4/3-1). OC Bacteria; Proteobacteria; Deltaproteobacteria; Myxococcales; OC Cystobacterineae; Archangiaceae; Stigmatella. OX NCBI_TaxID=378806 {ECO:0000313|EMBL:EAU63676.1, ECO:0000313|Proteomes:UP000032702}; RN [1] {ECO:0000313|EMBL:EAU63676.1, ECO:0000313|Proteomes:UP000032702} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DW4/3-1 {ECO:0000313|EMBL:EAU63676.1, RC ECO:0000313|Proteomes:UP000032702}; RA Nierman W.C.; RL Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:ADO69914.1, ECO:0000313|Proteomes:UP000001351} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DW4/3-1 {ECO:0000313|EMBL:ADO69914.1, RC ECO:0000313|Proteomes:UP000001351}; RX PubMed=21037205; DOI=10.1093/molbev/msq292; RA Huntley S., Hamann N., Wegener-Feldbrugge S., Treuner-Lange A., RA Kube M., Reinhardt R., Klages S., Muller R., Ronning C.M., RA Nierman W.C., Sogaard-Andersen L.; RT "Comparative genomic analysis of fruiting body formation in RT Myxococcales."; RL Mol. Biol. Evol. 28:1083-1097(2011). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002271; ADO69914.1; -; Genomic_DNA. DR EMBL; AAMD01000152; EAU63676.1; -; Genomic_DNA. DR RefSeq; WP_002617481.1; NZ_AAMD01000152.1. DR STRING; 378806.STAUR_2110; -. DR EnsemblBacteria; ADO69914; ADO69914; STAUR_2110. DR EnsemblBacteria; EAU63676; EAU63676; STIAU_2244. DR KEGG; sur:STAUR_2110; -. DR PATRIC; fig|378806.16.peg.2556; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR KO; K03665; -. DR OMA; EREVIIT; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000001351; Chromosome. DR Proteomes; UP000032702; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000001351}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000001351}. FT DOMAIN 395 559 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 354 381 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 567 AA; 62551 MW; 70692762B1D803C7 CRC64; MSGEDGRGRP PTREIESLKE IYGNTLGLKA NEQSRLRNTY RRRVAPNEII SPELARHLTE LSSETNRQVG VLINRKGEIE YVVVGNAHKL ELPDIGRARA GQIRLRGLRL VHTHLKSEPL TKDDLTDLAL LRLDMVAAVG VGHEGLPGVL HYAHLVPENG TGEFWQVATL PSVHHGQPDL VDTLEALEEE FNRKAAARAV GGREKAILVA VCLDGNRARA EASLAELKEL ARTAGVEVLD SVLQVRREAD PRYLIGRGKL EDLNLRSMQS MVDVLIFDKD LTPSQGRHIG EATSLKVLDR TQLILDIFAQ RAQSAEGKLQ VELAQLKYRL PRLVQSDDSL SRLAGGIGGR GPGETKLEID RRRVRERITH LEKRIDAVSR ERSVRRAQRN RRELPVISIV GYTNAGKSTL LNAITNADVL AENKLFATLD PTSRRLRFPQ EREVIITDTV GFIRDLPKDL VAAFRATLEE LYDASLLLHV VDAADPARDE QIEAVETILG SLGLMEKPRL MVWNKADLLP AEDVQALLRS RGGVAISAAT REGLASLLAK ADTTLFAEGA SEMLGAL // ID Q093K7_STIAD Unreviewed; 459 AA. AC Q093K7; DT 31-OCT-2006, integrated into UniProtKB/TrEMBL. DT 31-OCT-2006, sequence version 1. DT 30-AUG-2017, entry version 66. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=STAUR_4927 {ECO:0000313|EMBL:ADO72705.1}; GN ORFNames=STIAU_0094 {ECO:0000313|EMBL:EAU66948.1}; OS Stigmatella aurantiaca (strain DW4/3-1). OC Bacteria; Proteobacteria; Deltaproteobacteria; Myxococcales; OC Cystobacterineae; Archangiaceae; Stigmatella. OX NCBI_TaxID=378806 {ECO:0000313|EMBL:EAU66948.1, ECO:0000313|Proteomes:UP000032702}; RN [1] {ECO:0000313|EMBL:EAU66948.1, ECO:0000313|Proteomes:UP000032702} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DW4/3-1 {ECO:0000313|EMBL:EAU66948.1, RC ECO:0000313|Proteomes:UP000032702}; RA Nierman W.C.; RL Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:ADO72705.1, ECO:0000313|Proteomes:UP000001351} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DW4/3-1 {ECO:0000313|EMBL:ADO72705.1, RC ECO:0000313|Proteomes:UP000001351}; RX PubMed=21037205; DOI=10.1093/molbev/msq292; RA Huntley S., Hamann N., Wegener-Feldbrugge S., Treuner-Lange A., RA Kube M., Reinhardt R., Klages S., Muller R., Ronning C.M., RA Nierman W.C., Sogaard-Andersen L.; RT "Comparative genomic analysis of fruiting body formation in RT Myxococcales."; RL Mol. Biol. Evol. 28:1083-1097(2011). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002271; ADO72705.1; -; Genomic_DNA. DR EMBL; AAMD01000044; EAU66948.1; -; Genomic_DNA. DR RefSeq; WP_002613550.1; NZ_AAMD01000044.1. DR STRING; 378806.STAUR_4927; -. DR EnsemblBacteria; ADO72705; ADO72705; STAUR_4927. DR EnsemblBacteria; EAU66948; EAU66948; STIAU_0094. DR KEGG; sur:STAUR_4927; -. DR PATRIC; fig|378806.16.peg.6112; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR KO; K03665; -. DR OMA; VILEIFH; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000001351; Chromosome. DR Proteomes; UP000032702; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 2. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000001351}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000001351}. FT DOMAIN 240 405 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 459 AA; 50450 MW; F104B37E8A3FD1AB CRC64; MSQSSSARPP AVLVGVQLPN VSDTEHAADL AELGRLVHTL GYEVVATVTQ RRDGVAAGTV LGTGKLKELA QLTGGPGTVP SGAQARKSKA RERWESEDEE PPEDVPMAAL ADEADDTQAV SRPRVVVVDH ELSPSQLSNL ERATGAQVLD RTGVIVDIFH RHARSREARM QVEIARLNYL APRMRESTGS RERQQGRGSG DSAVELDRRK IRDRLAELRE GLAAIQQDQE QRRYARRDQL RVALVGYTNA GKSSLMRALT GSEVLVADQL FATLDTTVRA LQPETRPRVL VSDTVGFIQK LPHDLVASFR STLDEALEAS LLLYVVDASD PTWEAQLEVT REVLRDIGAQ SVPGKLLFNK ADRLSAEARE ALLQRHPEAI VLSAHSPEDV AALRQSVLEF FERSMTEAEL VIPYARQGRI GEVYEHARVL SEVFDENGRR LKIRALPAAI AKLTHAFGT // ID Q0AB59_ALKEH Unreviewed; 421 AA. AC Q0AB59; DT 17-OCT-2006, integrated into UniProtKB/TrEMBL. DT 17-OCT-2006, sequence version 1. DT 30-AUG-2017, entry version 76. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Mlg_0574 {ECO:0000313|EMBL:ABI55928.1}; OS Alkalilimnicola ehrlichii (strain ATCC BAA-1101 / DSM 17681 / MLHE-1). OC Bacteria; Proteobacteria; Gammaproteobacteria; Chromatiales; OC Ectothiorhodospiraceae; Alkalilimnicola. OX NCBI_TaxID=187272 {ECO:0000313|EMBL:ABI55928.1, ECO:0000313|Proteomes:UP000001962}; RN [1] {ECO:0000313|Proteomes:UP000001962} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-1101 / DSM 17681 / MLHE-1 RC {ECO:0000313|Proteomes:UP000001962}; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., RA Pitluck S., Sims D., Brettin T., Bruce D., Han C., Tapia R., Gilna P., RA Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., RA Mikhailova N., Oremland R.S., Hoeft S.E., Switzer-Blum J., Kulp T., RA King G., Tabita R., Witte B., Santini J.M., Basu P., Hollibaugh J.T., RA Xie G., Stolz J.F., Richardson P.; RT "Complete sequence of Alkalilimnicola ehrilichei MLHE-1."; RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000453; ABI55928.1; -; Genomic_DNA. DR ProteinModelPortal; Q0AB59; -. DR STRING; 187272.Mlg_0574; -. DR EnsemblBacteria; ABI55928; ABI55928; Mlg_0574. DR KEGG; aeh:Mlg_0574; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000001962; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000001962}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Hydrolase {ECO:0000313|EMBL:ABI55928.1}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000001962}. FT DOMAIN 186 352 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 152 179 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 421 AA; 46947 MW; D131E8152D48234E CRC64; MLIHLDLDGD PRDTLDEFQA LAESAGAEVV DAVRHRRHSP DPRFFLGRGK VEELAARIPA EGIDLVLIDH AISPAQERNL ERAFRCRVLD RTGLILDIFA QRARSHEGKL QVELAQLRHI ASRLVRGWSH LERQKGGIGL RGPGETQLEM DRRMLGTRIK QLERKLEKVR RQRAQGRQAR RRQEFPVVSL VGYTNAGKST LFNALTGSGL YADDRLFATL DTTLRRLELP DGQPVILADT VGFISDLPHG LVAAFRSTLE EVGESDLLLH VVDAADPDRR EHARQVQQVL ADIGASEVPV LTVYNKADLC QHPVGILRDD REAPEAVWVS AAAGRGLDEL EEAVAECLGG GRVRGRVRLP AHQGRLRARF YQLGQVLDER VEEDGVIDLL VDLPRRELDR LRSNEGLTAP LETETALHDP S // ID Q0AHG0_NITEC Unreviewed; 377 AA. AC Q0AHG0; DT 17-OCT-2006, integrated into UniProtKB/TrEMBL. DT 17-OCT-2006, sequence version 1. DT 07-JUN-2017, entry version 83. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Neut_0962 {ECO:0000313|EMBL:ABI59222.1}; OS Nitrosomonas eutropha (strain C91). OC Bacteria; Proteobacteria; Betaproteobacteria; Nitrosomonadales; OC Nitrosomonadaceae; Nitrosomonas. OX NCBI_TaxID=335283 {ECO:0000313|EMBL:ABI59222.1, ECO:0000313|Proteomes:UP000001966}; RN [1] {ECO:0000313|EMBL:ABI59222.1, ECO:0000313|Proteomes:UP000001966} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C91 {ECO:0000313|EMBL:ABI59222.1, RC ECO:0000313|Proteomes:UP000001966}; RX PubMed=17991028; DOI=10.1111/j.1462-2920.2007.01409.x; RA Stein L.Y., Arp D.J., Berube P.M., Chain P.S., Hauser L., Jetten M.S., RA Klotz M.G., Larimer F.W., Norton J.M., Op den Camp H.J.M., Shin M., RA Wei X.; RT "Whole-genome analysis of the ammonia-oxidizing bacterium, RT Nitrosomonas eutropha C91: implications for niche adaptation."; RL Environ. Microbiol. 9:2993-3007(2007). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000450; ABI59222.1; -; Genomic_DNA. DR RefSeq; WP_011634046.1; NC_008344.1. DR ProteinModelPortal; Q0AHG0; -. DR STRING; 335283.Neut_0962; -. DR EnsemblBacteria; ABI59222; ABI59222; Neut_0962. DR KEGG; net:Neut_0962; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; FNNHAHV; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000001966; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000001966}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Hydrolase {ECO:0000313|EMBL:ABI59222.1}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000001966}. FT DOMAIN 199 371 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 165 192 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 377 AA; 42271 MW; 722F948C0403D9E7 CRC64; MNHDIGTAAD NTAILVDINF GKNDKESLDE LKELAYSDQL SIVAVVEGTR KQPDPATFIG KGKVEEISQI VVQTQAAMVI FNHELSPIQQ RNLSTALACR IIDRTSLILD IFAQRAKSHE GKLQVELAQL EYLSTRLVRG WTHLERQKGG IGLRGPGETQ LETDRRLLAK RVKFLKEKLA KLKQQRDVQR RARKRSEIMS VSIVGYTNAG KSTLFNRLVR SDAYAADKLF ATLDTTTRRL FLPERGLIVI SDTVGFIRDL PHTLVAAFRA TLEETIQADL LLHVVDVSSS NRDVQISEVN KLLQEIGADT IPQILILNKI DLIEQGSSEN YMRDEYGRIA RIHLSARTGA GFGYLYEALV EAFDQNLNKL SSIQQHP // ID Q0APP6_MARMM Unreviewed; 450 AA. AC Q0APP6; DT 17-OCT-2006, integrated into UniProtKB/TrEMBL. DT 17-OCT-2006, sequence version 1. DT 07-JUN-2017, entry version 81. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Mmar10_1449 {ECO:0000313|EMBL:ABI65741.1}; OS Maricaulis maris (strain MCS10). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Hyphomonadaceae; Maricaulis. OX NCBI_TaxID=394221 {ECO:0000313|EMBL:ABI65741.1, ECO:0000313|Proteomes:UP000001964}; RN [1] {ECO:0000313|EMBL:ABI65741.1, ECO:0000313|Proteomes:UP000001964} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MCS10 {ECO:0000313|EMBL:ABI65741.1, RC ECO:0000313|Proteomes:UP000001964}; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., RA Pitluck S., Saunders E., Brettin T., Bruce D., Han C., Tapia R., RA Gilna P., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., RA Mikhailova N., Viollier P., Stephens C., Richardson P.; RT "Complete sequence of Maricaulis maris MCS10."; RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000449; ABI65741.1; -; Genomic_DNA. DR RefSeq; WP_011643388.1; NC_008347.1. DR ProteinModelPortal; Q0APP6; -. DR STRING; 394221.Mmar10_1449; -. DR EnsemblBacteria; ABI65741; ABI65741; Mmar10_1449. DR KEGG; mmr:Mmar10_1449; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000001964; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000001964}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Hydrolase {ECO:0000313|EMBL:ABI65741.1}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000001964}. FT DOMAIN 201 378 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 160 194 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 450 AA; 49584 MW; 0749457F861CD0A2 CRC64; MIEREAPVSR ALVIHPASRA ELGRAEARLE EAYGLAEALD LEVGAAFILQ TRKIDSGRYF GRGKLDELGA MIGELEANVA VIDTNLSPIQ QRNLENAWNV KVIDRTGLIL EIFGQRARTK EGVLQVELAR LAYERSRLVR TWTHLERQRG GRGFLAGPGE TQIETDRRLL NEKMAKLRRQ LDEVRRTRAL HRSQRQDVPF PTVALVGYTN AGKSTLFNKL TGAGVFAQDM PFATLDPTVR AVDLPGGTRI LLSDTVGFIT DLPTELIAAF RATLEEVREA DLLVHIIDAS DPDREGRIQD VESVLDAIEA GPAHDQAMLE AWNKSDRLDD ESTEDLAITI QMANLKAGKP VKLAVSAVTG QGVDSLIDAI ERTLSSENER LQIIVPPQDA RALAWLHAHG DVLDSEIDPA TGATTIQVRL HPVEAGRFRS QFPDLAIPQG IGEVEDEDDF // ID Q0AVN5_SYNWW Unreviewed; 375 AA. AC Q0AVN5; DT 17-OCT-2006, integrated into UniProtKB/TrEMBL. DT 17-OCT-2006, sequence version 1. DT 07-JUN-2017, entry version 75. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Swol_1922 {ECO:0000313|EMBL:ABI69219.1}; OS Syntrophomonas wolfei subsp. wolfei (strain DSM 2245B / Goettingen). OC Bacteria; Firmicutes; Clostridia; Clostridiales; Syntrophomonadaceae; OC Syntrophomonas. OX NCBI_TaxID=335541 {ECO:0000313|EMBL:ABI69219.1, ECO:0000313|Proteomes:UP000001968}; RN [1] {ECO:0000313|Proteomes:UP000001968} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 2245B / Goettingen {ECO:0000313|Proteomes:UP000001968}; RX PubMed=21966920; DOI=10.1111/j.1462-2920.2010.02237.x; RA Sieber J.R., Sims D.R., Han C., Kim E., Lykidis A., Lapidus A.L., RA McDonnald E., Rohlin L., Culley D.E., Gunsalus R., McInerney M.J.; RT "The genome of Syntrophomonas wolfei: new insights into syntrophic RT metabolism and biohydrogen production."; RL Environ. Microbiol. 12:2289-2301(2010). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000448; ABI69219.1; -; Genomic_DNA. DR RefSeq; WP_011641312.1; NC_008346.1. DR ProteinModelPortal; Q0AVN5; -. DR STRING; 335541.Swol_1922; -. DR EnsemblBacteria; ABI69219; ABI69219; Swol_1922. DR KEGG; swo:Swol_1922; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000001968; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000001968}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000001968}. FT DOMAIN 208 375 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 167 204 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 375 AA; 41692 MW; 1B68157A54AE0A02 CRC64; MNKQGAESLS KRTTWEKAIL VAVKTGATKE AEFNSSLQEL AGLAEAAGAK VVATLTQARD KPHAATYIGK GKLQELEHLL AEKEPELLIF DSELSPTQLR KLEDKLQIKI VDRTLLILDI FGQRARSREG LLQVELASLE YRLPRLTGIG KEMSRLGAGI GTRGAGEQKL ELDRRHIRSR IREIKRQMEK LEKTRELHKK QRHRAGYQVI SLVGYTNAGK SSLFNALCQV AHSSGQPQVE ANRRLFQTLD TTTRKIKLDS HYEVLITDTV GFIQNLPHHL VAAFRSTLEE AVAADLLLHV VDLADPAYLD KIKVVEGVLE ELGAEKERIM PVFNKVDLLA GISPIQAPPN YVSARTGQGI EELLGQIKNR LEAIS // ID Q0BT30_GRABC Unreviewed; 460 AA. AC Q0BT30; DT 17-OCT-2006, integrated into UniProtKB/TrEMBL. DT 17-OCT-2006, sequence version 1. DT 07-JUN-2017, entry version 76. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=GbCGDNIH1_1124 {ECO:0000313|EMBL:ABI62022.1}; OS Granulibacter bethesdensis (strain ATCC BAA-1260 / CGDNIH1). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales; OC Acetobacteraceae; Granulibacter. OX NCBI_TaxID=391165 {ECO:0000313|EMBL:ABI62022.1, ECO:0000313|Proteomes:UP000001963}; RN [1] {ECO:0000313|EMBL:ABI62022.1, ECO:0000313|Proteomes:UP000001963} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-1260 / CGDNIH1 {ECO:0000313|Proteomes:UP000001963}; RX PubMed=17827295; DOI=10.1128/JB.00793-07; RA Greenberg D.E., Porcella S.F., Zelazny A.M., Virtaneva K., RA Sturdevant D.E., Kupko J.J. III, Barbian K.D., Babar A., Dorward D.W., RA Holland S.M.; RT "Genome sequence analysis of the emerging human pathogenic acetic acid RT bacterium Granulibacter bethesdensis."; RL J. Bacteriol. 189:8727-8736(2007). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000394; ABI62022.1; -; Genomic_DNA. DR RefSeq; WP_011631831.1; NC_008343.1. DR ProteinModelPortal; Q0BT30; -. DR STRING; 391165.GbCGDNIH1_1124; -. DR EnsemblBacteria; ABI62022; ABI62022; GbCGDNIH1_1124. DR GeneID; 31475828; -. DR KEGG; gbe:GbCGDNIH1_1124; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000001963; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000001963}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000001963}. FT DOMAIN 223 392 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 460 AA; 50017 MW; 3DDE69EA16541F87 CRC64; MAIQDFSSTD HSANSVSSGP ARAAVILPWE KPERGDKVER LDAGRAAEAR LAEAVGLAAS IGLVVVHSGV LPLRARRPST LLGEGQVQLT GQALAGQNIT VVIVDAALTP VQQRNLERAW NTKVIDRTGL ILDIFGERAA TREGTLQVEL AHLEYQRSRL VRSWTHLERQ RGGFGFLGGP GETQIEADRR LITDRIVKLK RELEQVRRTR GLHRTARQRV PFPVVALVGY TNAGKSTLFN AMTGSTVLAK DQLFATLDPT MRGLRLRSGR RVILSDTVGF ISELPTELIA AFRATLEEVA EADVILHVRD VSHPDTAAQR HDVQLVLDGM VRDHDLDADW RGRMIEVLNK ADLLGGVEHV SVAPGSVAVS AITGAGLDEL QAVIDARIAA GLTIAHYSVP AADGAAMAWL HEHGEVLDRQ DDAENGMIAV TVRLRPADQA RFERLHKARP VVDKQDASSQ // ID Q0C0N9_HYPNA Unreviewed; 442 AA. AC Q0C0N9; DT 17-OCT-2006, integrated into UniProtKB/TrEMBL. DT 17-OCT-2006, sequence version 1. DT 07-JUN-2017, entry version 82. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=HNE_2005 {ECO:0000313|EMBL:ABI77825.1}; OS Hyphomonas neptunium (strain ATCC 15444). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Hyphomonadaceae; Hyphomonas. OX NCBI_TaxID=228405 {ECO:0000313|EMBL:ABI77825.1, ECO:0000313|Proteomes:UP000001959}; RN [1] {ECO:0000313|EMBL:ABI77825.1, ECO:0000313|Proteomes:UP000001959} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 15444 {ECO:0000313|EMBL:ABI77825.1, RC ECO:0000313|Proteomes:UP000001959}; RX PubMed=16980487; DOI=10.1128/JB.00111-06; RA Badger J.H., Hoover T.R., Brun Y.V., Weiner R.M., Laub M.T., RA Alexandre G., Mrazek J., Ren Q., Paulsen I.T., Nelson K.E., RA Khouri H.M., Radune D., Sosa J., Dodson R.J., Sullivan S.A., RA Rosovitz M.J., Madupu R., Brinkac L.M., Durkin A.S., Daugherty S.C., RA Kothari S.P., Giglio M.G., Zhou L., Haft D.H., Selengut J.D., RA Davidsen T.M., Yang Q., Zafar N., Ward N.L.; RT "Comparative genomic evidence for a close relationship between the RT dimorphic prosthecate bacteria Hyphomonas neptunium and Caulobacter RT crescentus."; RL J. Bacteriol. 188:6841-6850(2006). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000158; ABI77825.1; -; Genomic_DNA. DR RefSeq; WP_011647004.1; NC_008358.1. DR ProteinModelPortal; Q0C0N9; -. DR STRING; 228405.HNE_2005; -. DR EnsemblBacteria; ABI77825; ABI77825; HNE_2005. DR KEGG; hne:HNE_2005; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000001959; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000001959}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000001959}. FT DOMAIN 205 379 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 164 191 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 442 AA; 48705 MW; 07034B0885512161 CRC64; MTEKLIDRLP APEIAGVVIP WFTPRDRPGP DRLSETAGLV EALGCELGFI RPDHVRQVNS SFLLSGGLLD RMAEDIEQTN ATLAVIDASL TPVQQRNLEK RLGVKVIDRT GLILEIFGLR ARTKEGRLQV ELARLLYERS RLVRTWTHLE RQRGGGGFLS GPGESQLEAD RRMLDDKIVR LRRDLDDVKR TREVQRQGRR RSGKPVVALV GYTNSGKSTL FNRLTGSDVF AKDMPFATLD PTIRRLDLPT LGEAALIDTV GFITDLPTHL IDSFQATLEE SLQADLLIHV RDRASASDME QAEDVALVLE RLEKESGLPL PPMIEAWNKM DALAPERAES LTGLAAITDD PPAAAVSALT GEGVDALLAL IEKSLLRGRT EISLTLGPAD GKARAWLHQN GEVLTETQRE DGQTDLTLRL STERLGQFRG EFPEQAAGVS IL // ID Q0DNY0_ORYSJ Unreviewed; 568 AA. AC Q0DNY0; DT 17-OCT-2006, integrated into UniProtKB/TrEMBL. DT 17-OCT-2006, sequence version 1. DT 30-AUG-2017, entry version 69. DE SubName: Full=Os03g0727900 protein {ECO:0000313|EMBL:BAF13058.1}; GN Name=Os03g0727900 {ECO:0000313|EMBL:BAF13058.1}; GN ORFNames=OSNPB_030727900 {ECO:0000313|EMBL:BAS86189.1}; OS Oryza sativa subsp. japonica (Rice). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; BOP clade; OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa. OX NCBI_TaxID=39947; RN [1] {ECO:0000313|Proteomes:UP000059680} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Nipponbare {ECO:0000313|Proteomes:UP000059680}; RX PubMed=16100779; DOI=10.1038/nature03895; RG International rice genome sequencing project (IRGSP); RT "The map-based sequence of the rice genome."; RL Nature 436:793-800(2005). RN [2] {ECO:0000313|EMBL:BAF13058.1} RP NUCLEOTIDE SEQUENCE. RG IRGSP(International Rice Genome Sequencing Project); RT "Oryza sativa nipponbare(GA3) genomic DNA, chromosome 3."; RL Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases. RN [3] {ECO:0000313|EMBL:BAF13058.1} RP NUCLEOTIDE SEQUENCE. RG The Rice Annotation Project (RAP); RT "The Second Rice Annotation Project Meeting (RAP2)."; RL Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases. RN [4] {ECO:0000313|EMBL:BAF13058.1} RP NUCLEOTIDE SEQUENCE. RX PubMed=16381971; DOI=10.1093/nar/gkj094; RA Ohyanagi H., Tanaka T., Sakai H., Shigemoto Y., Yamaguchi K., RA Habara T., Fujii Y., Antonio B.A., Nagamura Y., Imanishi T., Ikeo K., RA Itoh T., Gojobori T., Sasaki T.; RT "The Rice Annotation Project Database (RAP-DB): hub for Oryza sativa RT ssp. japonica genome information."; RL Nucleic Acids Res. 34:D741-D744(2006). RN [5] {ECO:0000313|EMBL:BAF13058.1} RP NUCLEOTIDE SEQUENCE. RG The Rice Annotation Project (RAP); RA Itoh T., Tanaka T., Barrero R.A., Yamasaki C., Fujii Y., Hilton P.B., RA Antonio B.A., Aono H., Apweiler R., Bruskiewich R., Bureau T., RA Burr F., Costa de Oliveira A., Fuks G., Habara T., Haberer G., Han B., RA Harada E., Hiraki A.T., Hirochika H., Hoen D., Hokari H., Hosokawa S., RA Hsing Y., Ikawa H., Ikeo K., Imanishi T., Ito Y., Jaiswal P., RA Kanno M., Kawahara Y., Kawamura T., Kawashima H., Khurana J.P., RA Kikuchi S., Komatsu S., Koyanagi K.O., Kubooka H., Lieberherr D., RA Lin Y.C., Lonsdale D., Matsumoto T., Matsuya A., McCombie W.R., RA Messing J., Miyao A., Mulder N., Nagamura Y., Nam J., Namiki N., RA Numa H., Nurimoto S., O'donovan C., Ohyanagi H., Okido T., Oota S., RA Osato N., Palmer L.E., Quetier F., Raghuvanshi S., Saichi N., RA Sakai H., Sakai Y., Sakata K., Sakurai T., Sato F., Sato Y., RA Schoof H., Seki M., Shibata M., Shimizu Y., Shinozaki K., Shinso Y., RA Singh N.K., Smith-White B., Takeda J., Tanino M., Tatusova T., RA Thongjuea S., Todokoro F., Tsugane M., Tyagi A.K., Vanavichit A., RA Wang A., Wing R.A., Yamaguchi K., Yamamoto M., Yamamoto N., Yu Y., RA Zhang H., Zhao Q., Higo K., Burr B., Gojobori T., Sasaki T.; RT "Curated Genome Annotation of Oryza sativa ssp. japonica and RT Comparative Genome Analysis with Arabidopsis thaliana."; RL Genome Res. 17:175-183(2007). RN [6] {ECO:0000313|EMBL:BAF13058.1} RP NUCLEOTIDE SEQUENCE. RG The Rice Annotation Project (RAP); RA Tanaka T., Antonio B.A., Kikuchi S., Matsumoto T., Nagamura Y., RA Numa H., Sakai H., Wu J., Itoh T., Sasaki T., Aono R., Fujii Y., RA Habara T., Harada E., Kanno M., Kawahara Y., Kawashima H., Kubooka H., RA Matsuya A., Nakaoka H., Saichi N., Sanbonmatsu R., Sato Y., Shinso Y., RA Suzuki M., Takeda J., Tanino M., Todokoro F., Yamaguchi K., RA Yamamoto N., Yamasaki C., Imanishi T., Okido T., Tada M., Ikeo K., RA Tateno Y., Gojobori T., Lin Y.C., Wei F.J., Hsing Y.I., Zhao Q., RA Han B., Kramer M.R., McCombie R.W., Lonsdale D., O'Donovan C.C., RA Whitfield E.J., Apweiler R., Koyanagi K.O., Khurana J.P., RA Raghuvanshi S., Singh N.K., Tyagi A.K., Haberer G., Fujisawa M., RA Hosokawa S., Ito Y., Ikawa H., Shibata M., Yamamoto M., RA Bruskiewich R.M., Hoen D.R., Bureau TE., Namiki N., Ohyanagi H., RA Sakai Y., Nobushima S., Sakata K., Barrero R.A., Sato Y., Souvorov A., RA Smith-White B., Tatusova T., An S., An G., OOta S., Fuks G., RA Messing J., Christie K.R., Lieberherr D., Kim H., Zuccolo A., RA Wing R.A., Nobuta K., Green P.J., Lu C., Meyers BC., Chaparro C., RA Piegu B., Panaud O., Echeverria M.; RT "The Rice Annotation Project Database (RAP-DB): 2008 update."; RL Nucleic Acids Res. 36:D1028-D1033(2008). RN [7] {ECO:0000313|EMBL:BAS86189.1} RP NUCLEOTIDE SEQUENCE. RX PubMed=23299411; DOI=10.1093/pcp/pcs183; RA Sakai H., Lee S.S., Tanaka T., Numa H., Kim J., Kawahara Y., RA Wakimoto H., Yang C.C., Iwamoto M., Abe T., Yamada Y., Muto A., RA Inokuchi H., Ikemura T., Matsumoto T., Sasaki T., Itoh T.; RT "Rice Annotation Project Database (RAP-DB): an integrative and RT interactive database for rice genomics."; RL Plant Cell Physiol. 54:E6-E6(2013). RN [8] {ECO:0000313|EMBL:BAS86189.1, ECO:0000313|Proteomes:UP000059680} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Nipponbare {ECO:0000313|Proteomes:UP000059680}; RX PubMed=24280374; DOI=10.1186/1939-8433-6-4; RA Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., RA McCombie W.R., Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., RA Childs K.L., Davidson R.M., Lin H., Quesada-Ocampo L., RA Vaillancourt B., Sakai H., Lee S.S., Kim J., Numa H., Itoh T., RA Buell C.R., Matsumoto T.; RT "Improvement of the Oryza sativa Nipponbare reference genome using RT next generation sequence and optical map data."; RL Rice 6:4-4(2013). RN [9] {ECO:0000313|EMBL:BAS86189.1} RP NUCLEOTIDE SEQUENCE. RA Millard Andrew; RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AP008209; BAF13058.1; -; Genomic_DNA. DR EMBL; AP014959; BAS86189.1; -; Genomic_DNA. DR UniGene; Os.11933; -. DR EnsemblPlants; OS03T0727900-01; OS03T0727900-01; OS03G0727900. DR Gramene; OS03T0727900-01; OS03T0727900-01; OS03G0727900. DR InParanoid; Q0DNY0; -. DR OMA; NGPEAIS; -. DR OrthoDB; EOG09360975; -. DR Proteomes; UP000059680; Chromosome 3. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR GO; GO:0043022; F:ribosome binding; IBA:GO_Central. DR CDD; cd01878; HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 2. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000059680}; KW Reference proteome {ECO:0000313|Proteomes:UP000059680}. FT DOMAIN 275 540 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 568 AA; 62397 MW; 3FA9EDAF6DEE58A5 CRC64; MLRAAVSRLR AHLHPHPHAH HHHGLPSVTP APPRDPERPP RLLVVQPRLR PGSLLDSKLA EALNLANSLE EPRDGFYKEG LAAKGAPPHL VAQNPSSRGR SHVDKFFGPG TVDNVKCYLR TSESEEGVDA VFVNAILTGI QQRNLEVAWG KPVLDRVGLI IEIFNAHAET KEAKLQSELA ALMYMKTRLV RVRGPGGRLT FGSSGEAEVV SARGRGSGGR GFISGAGETE LQLQRRRIQE CRVRLLAQIE DVRRTRAIQR SNRKRHGNSF GQELVTVAVV GYTNAGKSTL VSALSETDLY SDDRLFATVD PRLRSVILPS GRKALLSDTV GFISDLPVQL VEAFHATLEE VVEADMLVHV LDSSAPNIEE HRSTVLQVLQ QIGVSQDKIN SMIEVWNKID IVDNNDNDVT DDIEDEIFLT EGEEDKEEEL FSENDVPAEE SSFESLDDGT DSEYLSEENL EGNNGEISSS LEPSEMRAMN SVSSSSKDCF GELCGPETIS TDSCSSTQPM STCHVKTSAV TGTGLQELLE LIDKKLTERQ TIVERSYGPF DRKWRPSSSV VGEKAAEQ // ID Q0F2W5_9PROT Unreviewed; 433 AA. AC Q0F2W5; DT 17-OCT-2006, integrated into UniProtKB/TrEMBL. DT 17-OCT-2006, sequence version 1. DT 07-JUN-2017, entry version 60. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=SPV1_05128 {ECO:0000313|EMBL:EAU56176.1}; OS Mariprofundus ferrooxydans PV-1. OC Bacteria; Proteobacteria; Zetaproteobacteria; Mariprofundales; OC Mariprofundaceae; Mariprofundus. OX NCBI_TaxID=314345 {ECO:0000313|EMBL:EAU56176.1, ECO:0000313|Proteomes:UP000005297}; RN [1] {ECO:0000313|EMBL:EAU56176.1, ECO:0000313|Proteomes:UP000005297} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=PV-1 {ECO:0000313|EMBL:EAU56176.1, RC ECO:0000313|Proteomes:UP000005297}; RA Emerson D., Ferriera S., Johnson J., Kravitz S., Halpern A., RA Remington K., Beeson K., Tran B., Rogers Y.-H., Friedman R., RA Venter J.C.; RL Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EAU56176.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AATS01000001; EAU56176.1; -; Genomic_DNA. DR RefSeq; WP_009851320.1; NZ_DS022295.1. DR ProteinModelPortal; Q0F2W5; -. DR STRING; 314345.SPV1_05128; -. DR EnsemblBacteria; EAU56176; EAU56176; SPV1_05128. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000005297; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000005297}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000005297}. FT DOMAIN 207 375 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 433 AA; 47962 MW; E9A3BBE4B68E3E5C CRC64; MSGEWELAEE PDRVISVHPE LVSRRLGEQL WKARAEEFDL LVGAAACEIV ASQRLSVRKA AAATLLGQGQ VEEIARQVEI LEADVVFVDH PLSPVQQRNL ETAWNAKVVD RTGLILEIFA ARARTREGVL QVELASLNYQ LGRLVRSWTH LERQRGGFGF MGGPGERQIE LDRRMIRNSI GALERDLAKV KRMRATQRSG RQRKDIPTVA LVGYTNAGKS TLFNRLTTSD VFVANQLFAT LDPTLRLLEL PGGLRLMLSD TVGFVQELPH ELVDAFRATL EEVIEADLIL HVRDASDPMQ AEHAKVVHDT LQQLGVVGDG APQVVEILNK KDRVPELASF HGEGITTSRL AISALTGEGL DELTDLLGSW LQRDMHELHL RLAISDGRSL AYCHAHGSIL SSRADDDVLD LVVRMGPADA SRFNIESDVH FLN // ID Q0F554_9RHOB Unreviewed; 431 AA. AC Q0F554; DT 17-OCT-2006, integrated into UniProtKB/TrEMBL. DT 17-OCT-2006, sequence version 1. DT 30-AUG-2017, entry version 56. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=OM2255_00192 {ECO:0000313|EMBL:EAU49256.1}; OS Rhodobacterales bacterium HTCC2255. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales. OX NCBI_TaxID=367336 {ECO:0000313|EMBL:EAU49256.1, ECO:0000313|Proteomes:UP000009381}; RN [1] {ECO:0000313|EMBL:EAU49256.1, ECO:0000313|Proteomes:UP000009381} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=HTCC2255 {ECO:0000313|EMBL:EAU49256.1, RC ECO:0000313|Proteomes:UP000009381}; RA Giovannoni S., Cho J.-C., Ferriera S., Johnson J., Kravitz S., RA Halpern A., Remington K., Beeson K., Tran B., Rogers Y.-H., RA Friedman R., Venter J.C.; RL Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EAU49256.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AATR01000029; EAU49256.1; -; Genomic_DNA. DR RefSeq; WP_008037111.1; NZ_DS022288.1. DR ProteinModelPortal; Q0F554; -. DR STRING; 367336.OM2255_00192; -. DR EnsemblBacteria; EAU49256; EAU49256; OM2255_00192. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000009381; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000009381}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000009381}. FT DOMAIN 198 365 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 431 AA; 48530 MW; F70A562DC9B09DD0 CRC64; MFERYAAGEL AILVHIDFAD DSSKEDIHEL QMLVSSAGVD SAEVITASRN APHPKYFVGS GKAEEISAMV KAHEANVVIF NHALSPSQER NLEALCQCRV LDRTGLILDI FAQRARTHEG KLQVELAQLR HISTRLIRGW THLERQKGGI GLRGPGETQL ETDRRLLRAR IKTILKRLEK VQKQREQGRR ARKRNEIPTL SLVGYTNAGK STLFNTITDA NVYAADQLFA TLDPTLRKIE LADVGTAILA DTVGFIRHLP HDLVAAFKAT LQETQEADLL LHVVDYADDQ YGENMTQVND VLEEIDAGDI PQLIICNKID RLEGITPRID YDEDGRPIRV WISAQQGLGV ELLQTALTEC LAQTMQVQTL NIPPSDGKMR GVLYEYHCIT AEHYDEQGNW IVTIRLPMTV WNQLNKRLDG AFTRYHLNDD I // ID Q0FAH9_9RHOB Unreviewed; 417 AA. AC Q0FAH9; DT 17-OCT-2006, integrated into UniProtKB/TrEMBL. DT 17-OCT-2006, sequence version 1. DT 07-JUN-2017, entry version 52. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=OM2255_03582 {ECO:0000313|EMBL:EAU51316.1}; OS Rhodobacterales bacterium HTCC2255. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales. OX NCBI_TaxID=367336 {ECO:0000313|EMBL:EAU51316.1, ECO:0000313|Proteomes:UP000009381}; RN [1] {ECO:0000313|EMBL:EAU51316.1, ECO:0000313|Proteomes:UP000009381} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=HTCC2255 {ECO:0000313|EMBL:EAU51316.1, RC ECO:0000313|Proteomes:UP000009381}; RA Giovannoni S., Cho J.-C., Ferriera S., Johnson J., Kravitz S., RA Halpern A., Remington K., Beeson K., Tran B., Rogers Y.-H., RA Friedman R., Venter J.C.; RL Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EAU51316.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AATR01000006; EAU51316.1; -; Genomic_DNA. DR RefSeq; WP_008033619.1; NZ_DS022282.1. DR ProteinModelPortal; Q0FAH9; -. DR STRING; 367336.OM2255_03582; -. DR EnsemblBacteria; EAU51316; EAU51316; OM2255_03582. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000009381; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000009381}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000009381}. FT DOMAIN 195 366 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 417 AA; 46744 MW; 294E3E6844E71AE9 CRC64; MHVSVLHPNL LNPNKRRTPE HSLEEAVSLA NALDIEILHE AVIPLKKPNA GTLFGSGKLL ELSQIFKSND IDLVIIDGPL TPIQQRNLEK EWNLKVLDRT GLILEIFGDR AQTREGVLQV DLAALNYQRS RLVRTWTHLE RQRGGLSFIG GAGETQIESD RRQIDDAILR LKKQLEKVVK TRELHRSARK KIPYPIVALV GYTNAGKSTL FNYMTGAKVF AKDMLFATLD PTMREVELPS GQKIILSDTV GFISELPTQL IAAFRATLEE VLDANLILHV RDISHPETEA QANDVNDILE ELDVSDNTKS NILEVWNKTD LLSNDELINA KNISDRSEKI RTVSALTGDG LSVLLSEIDE NLKEITVSDV VKLALTEGGR RAWLYKNNLV KNEVSNENFI ELSVTWTPKQ AAQFLKV // ID Q0FTF1_PELBH Unreviewed; 417 AA. AC Q0FTF1; DT 17-OCT-2006, integrated into UniProtKB/TrEMBL. DT 17-OCT-2006, sequence version 1. DT 07-JUN-2017, entry version 55. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=R2601_26221 {ECO:0000313|EMBL:EAU47501.1}; OS Pelagibaca bermudensis (strain JCM 13377 / KCTC 12554 / HTCC2601). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae; Pelagibaca. OX NCBI_TaxID=314265 {ECO:0000313|EMBL:EAU47501.1, ECO:0000313|Proteomes:UP000006230}; RN [1] {ECO:0000313|EMBL:EAU47501.1, ECO:0000313|Proteomes:UP000006230} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=JCM 13377 / KCTC 12554 / HTCC2601 RC {ECO:0000313|Proteomes:UP000006230}; RX PubMed=20729358; DOI=10.1128/JB.00873-10; RA Thrash J.C., Cho J.C., Ferriera S., Johnson J., Vergin K.L., RA Giovannoni S.J.; RT "Genome sequences of Pelagibaca bermudensis HTCC2601T and RT Maritimibacter alkaliphilus HTCC2654T, the type strains of two marine RT Roseobacter genera."; RL J. Bacteriol. 192:5552-5553(2010). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EAU47501.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AATQ01000006; EAU47501.1; -; Genomic_DNA. DR RefSeq; WP_007800964.1; NZ_DS022276.1. DR ProteinModelPortal; Q0FTF1; -. DR STRING; 314265.R2601_26221; -. DR EnsemblBacteria; EAU47501; EAU47501; R2601_26221. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000006230; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000006230}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000006230}. FT DOMAIN 197 366 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 417 AA; 46535 MW; A83CB31D8FF0CCE2 CRC64; MTRAWVLHPD IRSDRDRRDA DMALEEAVAL AAALPDLEIV GSAVVPLRDP HPGHLFGTGK IEELREQIHD AEVELVLVDG PVSPVQQRNL EKEWKVKLLD RTGLILEIFS DRAATREGVL QVEMAALSYQ RTRLVRAWTH LERQRGGLGF VGGPGETQIE ADRRAIDEQL VRLRRQLERV VKTRDLHRKA RAKVPFPIVA LVGYTNAGKS TLFNRLTGAE VMAKDMLFAT LDPTMRAVKL PTGIDVILSD TVGFISDLPT ELVAAFRATL EEVLAADIIV HVRDISHPNT EEQAADVAAI LDSLGVDEEV PLVELWNKTD RLAPDVHEGV LQRAAREENI FAVSALTGEG LDTMLEAITE RLQGETLEEE LRLAFDDGKR RSWLFKKGLV QGEAQDEDGF VLQVRWSAKD RAQFETL // ID Q0G797_9RHIZ Unreviewed; 459 AA. AC Q0G797; DT 17-OCT-2006, integrated into UniProtKB/TrEMBL. DT 17-OCT-2006, sequence version 1. DT 07-JUN-2017, entry version 53. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=FP2506_06496 {ECO:0000313|EMBL:EAU42467.1}; OS Fulvimarina pelagi HTCC2506. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Aurantimonadaceae; Fulvimarina. OX NCBI_TaxID=314231 {ECO:0000313|EMBL:EAU42467.1, ECO:0000313|Proteomes:UP000004310}; RN [1] {ECO:0000313|EMBL:EAU42467.1, ECO:0000313|Proteomes:UP000004310} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=HTCC2506 {ECO:0000313|EMBL:EAU42467.1, RC ECO:0000313|Proteomes:UP000004310}; RX PubMed=20639329; DOI=10.1128/JB.00761-10; RA Kang I., Oh H.M., Lim S.I., Ferriera S., Giovannoni S.J., Cho J.C.; RT "Genome sequence of Fulvimarina pelagi HTCC2506T, a Mn(II)-oxidizing RT alphaproteobacterium possessing an aerobic anoxygenic photosynthetic RT gene cluster and Xanthorhodopsin."; RL J. Bacteriol. 192:4798-4799(2010). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EAU42467.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AATP01000001; EAU42467.1; -; Genomic_DNA. DR RefSeq; WP_007066441.1; NZ_DS022272.1. DR ProteinModelPortal; Q0G797; -. DR STRING; 314231.FP2506_06496; -. DR EnsemblBacteria; EAU42467; EAU42467; FP2506_06496. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000004310; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000004310}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000004310}. FT DOMAIN 223 397 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 182 216 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 459 AA; 50889 MW; C5F55AE0AB82BFFF CRC64; MAEYSGIGPK GPIEHKADPT RSAVYVPVFK DTGPKEPGSN LEVRRSPDAK LEEALGLAAA IQLEIVDSGI ITQRAPRPAT LIGQGKVEEL KGVVVAEEIG LVIIDHPLTP VQQRNLEREL NAKVLDRTAL ILEIFGERAR TKEGRLQVEL AHLNYQRGRL VRSWTHLERQ RGGAGFLGGP GETQIEADRR QLQSKIKALE VELEKVRSTR QLHRAKRRKR PHPIVALVGY TNAGKSTLFN RMTGADVFAQ NLLFATLDPT MRRTTLAHGT EILFSDTVGF ISELPTHLVA AFRATLEEVI EADIILHIRD VSDPDSLAQA EDVRQILRDL EIDADDTDHV VEVWNKIDRV DGSERERIET LAANEAEKER PHVVSAWTGE GIEALLADIE RRIAGKIAEL AVTLDPDGLR YLSWIYENAS VLDREDLEDG SIHLQIKVTE QGASELVRLK AAGEGIQFG // ID Q0K968_CUPNH Unreviewed; 420 AA. AC Q0K968; DT 03-OCT-2006, integrated into UniProtKB/TrEMBL. DT 03-OCT-2006, sequence version 1. DT 07-JUN-2017, entry version 86. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:CAJ93453.1}; GN OrderedLocusNames=H16_A2358 {ECO:0000313|EMBL:CAJ93453.1}; OS Cupriavidus necator (strain ATCC 17699 / H16 / DSM 428 / Stanier 337) OS (Ralstonia eutropha). OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Cupriavidus. OX NCBI_TaxID=381666 {ECO:0000313|EMBL:CAJ93453.1, ECO:0000313|Proteomes:UP000008210}; RN [1] {ECO:0000313|EMBL:CAJ93453.1, ECO:0000313|Proteomes:UP000008210} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 17699 / H16 / DSM 428 / Stanier 337 RC {ECO:0000313|Proteomes:UP000008210}; RX PubMed=16964242; DOI=10.1038/nbt1244; RA Pohlmann A., Fricke W.F., Reinecke F., Kusian B., Liesegang H., RA Cramm R., Eitinger T., Ewering C., Potter M., Schwartz E., RA Strittmatter A., Voss I., Gottschalk G., Steinbuechel A., RA Friedrich B., Bowien B.; RT "Genome sequence of the bioplastic-producing 'Knallgas' bacterium RT Ralstonia eutropha H16."; RL Nat. Biotechnol. 24:1257-1262(2006). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AM260479; CAJ93453.1; -; Genomic_DNA. DR RefSeq; WP_010809432.1; NC_008313.1. DR ProteinModelPortal; Q0K968; -. DR STRING; 381666.H16_A2358; -. DR EnsemblBacteria; CAJ93453; CAJ93453; H16_A2358. DR KEGG; reh:H16_A2358; -. DR PATRIC; fig|381666.6.peg.2765; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR Proteomes; UP000008210; Chromosome 1. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000008210}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Hydrolase {ECO:0000313|EMBL:CAJ93453.1}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000008210}. FT DOMAIN 202 372 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 161 195 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 420 AA; 45888 MW; 57A5B702FB87C2A7 CRC64; MDPRATSNTA PSRAILVGVD FGKHDFQESL SELALLTSTA GSVPVHTLTG RRSRPDPALF IGSGKAEELK EAADALDADV VVFNHALSPA QQRNLERFLN RHVIDRTGLI LDIFGQRAQS HVGKVQVELA QVQYRASRLV RAWSHLERQK GGIGMRGGPG ERQLELDRRM LDERAKRLKS DLSRLQRQHS TQRRARARND TLSISLVGYT NAGKSTLFNA LTKAGAYAAD QLFATLDTTS RRLFLDGLGN VVLSDTVGFI RDLPTQLVAA FRATLDETVH ADLLLHVVDA SSPVRHEQIE QVNRVLAEIN ALDIPQIVVM NKIDAAPELL EQGPRLERDE DGIPTRVFLS AREGMGLDAL REAVVEVAQW LASRPPEPQP YDPRLADVPQ YADAGDDGSA DEGGVADGSD DADAGDSDRL // ID Q0RDY0_FRAAA Unreviewed; 491 AA. AC Q0RDY0; DT 05-SEP-2006, integrated into UniProtKB/TrEMBL. DT 05-SEP-2006, sequence version 1. DT 07-JUN-2017, entry version 85. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=FRAAL5704 {ECO:0000313|EMBL:CAJ64336.1}; OS Frankia alni (strain ACN14a). OC Bacteria; Actinobacteria; Frankiales; Frankiaceae; Frankia. OX NCBI_TaxID=326424 {ECO:0000313|EMBL:CAJ64336.1, ECO:0000313|Proteomes:UP000000657}; RN [1] {ECO:0000313|EMBL:CAJ64336.1, ECO:0000313|Proteomes:UP000000657} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ACN14a {ECO:0000313|Proteomes:UP000000657}; RX PubMed=17151343; DOI=10.1101/gr.5798407; RA Normand P., Lapierre P., Tisa L.S., Gogarten J.P., Alloisio N., RA Bagnarol E., Bassi C.A., Berry A.M., Bickhart D.M., Choisne N., RA Couloux A., Cournoyer B., Cruveiller S., Daubin V., Demange N., RA Francino M.P., Goltsman E., Huang Y., Kopp O.R., Labarre L., RA Lapidus A., Lavire C., Marechal J., Martinez M., Mastronunzio J.E., RA Mullin B.C., Niemann J., Pujic P., Rawnsley T., Rouy Z., RA Schenowitz C., Sellstedt A., Tavares F., Tomkins J.P., Vallenet D., RA Valverde C., Wall L.G., Wang Y., Medigue C., Benson D.R.; RT "Genome characteristics of facultatively symbiotic Frankia sp. strains RT reflect host range and host plant biogeography."; RL Genome Res. 17:7-15(2007). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CT573213; CAJ64336.1; -; Genomic_DNA. DR ProteinModelPortal; Q0RDY0; -. DR STRING; 326424.FRAAL5704; -. DR KEGG; fal:FRAAL5704; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR Proteomes; UP000000657; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000000657}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000000657}. FT DOMAIN 273 437 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 232 259 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 491 AA; 52583 MW; 83EB7BCD85555E9A CRC64; MRTDGMTLPA DALTASTFDR SLIDLADADS AYLSGFYDDS GDGFDLEERA ALRRVPGLAT ELDDVTEVEY RQLRLEQVVL IGVWTSGSLR SAEASMAELA ALATTAGSVV LDALVQRRDR PDASTYVGSG KARELAEVVA ATGADTVICD GELTPGQLRQ LEEVVKVKVI DRTALILDIF AQHATSREGK AQVELAQLQY MLPRLRGWGE SMSRAAASGG GRAPIGTRGP GETKIETDRR RLRARMARLR RELAGMATVR ETKRSARRRG EVPAVAIAGY TNAGKSSLLN RLTGAGVLVE DALFATLDPT VRRATLPDGR AFTLTDTVGF VRHLPHQIVE AFRSTLEEVA DADLILHVVD GSAPDPAAQI SAVREVLNDI DAGNVAELIV VNKVDATEPT VLAGLRQLAP DAVFVSARTG EGLTALVDAL CARVPHPDVE MKVLVPYTRG DLVSRVHAHG EVLELEHTAD GTRLLARVSP SLAAELHAFQ P // ID Q0S1N6_RHOJR Unreviewed; 484 AA. AC Q0S1N6; DT 05-SEP-2006, integrated into UniProtKB/TrEMBL. DT 05-SEP-2006, sequence version 1. DT 07-JUN-2017, entry version 81. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=RHA1_ro06778 {ECO:0000313|EMBL:ABG98550.1}; OS Rhodococcus jostii (strain RHA1). OC Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae; OC Rhodococcus. OX NCBI_TaxID=101510 {ECO:0000313|EMBL:ABG98550.1, ECO:0000313|Proteomes:UP000008710}; RN [1] {ECO:0000313|Proteomes:UP000008710} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=RHA1 {ECO:0000313|Proteomes:UP000008710}; RX PubMed=17030794; DOI=10.1073/pnas.0607048103; RA McLeod M.P., Warren R.L., Hsiao W.W.L., Araki N., Myhre M., RA Fernandes C., Miyazawa D., Wong W., Lillquist A.L., Wang D., RA Dosanjh M., Hara H., Petrescu A., Morin R.D., Yang G., Stott J.M., RA Schein J.E., Shin H., Smailus D., Siddiqui A.S., Marra M.A., RA Jones S.J.M., Holt R., Brinkman F.S.L., Miyauchi K., Fukuda M., RA Davies J.E., Mohn W.W., Eltis L.D.; RT "The complete genome of Rhodococcus sp. RHA1 provides insights into a RT catabolic powerhouse."; RL Proc. Natl. Acad. Sci. U.S.A. 103:15582-15587(2006). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000431; ABG98550.1; -; Genomic_DNA. DR RefSeq; WP_011598570.1; NC_008268.1. DR ProteinModelPortal; Q0S1N6; -. DR STRING; 101510.RHA1_ro06778; -. DR PRIDE; Q0S1N6; -. DR EnsemblBacteria; ABG98550; ABG98550; RHA1_ro06778. DR GeneID; 4224329; -. DR KEGG; rha:RHA1_ro06778; -. DR PATRIC; fig|101510.16.peg.6839; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000008710; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000008710}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000008710}. FT DOMAIN 260 429 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 219 253 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 484 AA; 52534 MW; 4C800FBECFD22B1A CRC64; MTKTHRTEES PISDSTEFAY DDGRPSVGEM QLEDRSALRR VAGLSTELTD VTEVEYRQLR LERVVLVGVW TQGTAAQAES SMAELAALAE TAGSEVLEGL VQRRDKPDAA TYIGSGKAEE LREVVLSTGA DTVICDGELT PAQLTALEKV VKVKVIDRTA LILDIFAQHA TSREGKAQVA LAQMEYMLPR LRGWGESMSR QAGGRAGSNG GVGLRGPGET KIETDRRRIR ERMAKLRREI KGMKAARDTK RTRRLRSETP SIAIVGYTNA GKSSLLNALT GSGVLVQNAL FATLDPTTRR AALDDGREYV LTDTVGFVRH LPTQLIEAFR STLEEVTDAD LLLHVVDGSD PLPTDQIRAV HEVITEVIRE NDAAAPPELI VVNKIDAADP VTLTQLRGLL PGASFVSART GEGIAELRAH LSDVLIRPEI EVSVLLPYNR GDLMARIHSD GQILDSSHEE DGTRVHARVP EALASALVQY NGSA // ID Q0VME8_ALCBS Unreviewed; 480 AA. AC Q0VME8; DT 05-SEP-2006, integrated into UniProtKB/TrEMBL. DT 05-SEP-2006, sequence version 1. DT 30-AUG-2017, entry version 79. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:CAL17650.1}; GN OrderedLocusNames=ABO_2202 {ECO:0000313|EMBL:CAL17650.1}; OS Alcanivorax borkumensis (strain ATCC 700651 / DSM 11573 / NCIMB 13689 OS / SK2). OC Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales; OC Alcanivoracaceae; Alcanivorax. OX NCBI_TaxID=393595 {ECO:0000313|EMBL:CAL17650.1, ECO:0000313|Proteomes:UP000008871}; RN [1] {ECO:0000313|EMBL:CAL17650.1, ECO:0000313|Proteomes:UP000008871} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700651 / DSM 11573 / NCIMB 13689 / SK2 RC {ECO:0000313|Proteomes:UP000008871}; RX PubMed=16878126; DOI=10.1038/nbt1232; RA Schneiker S., Martins dos Santos V.A.P., Bartels D., Bekel T., RA Brecht M., Buhrmester J., Chernikova T.N., Denaro R., Ferrer M., RA Gertler C., Goesmann A., Golyshina O.V., Kaminski F., Khachane A.N., RA Lang S., Linke B., McHardy A.C., Meyer F., Nechitaylo T., Puehler A., RA Regenhardt D., Rupp O., Sabirova J.S., Selbitschka W., Yakimov M.M., RA Timmis K.N., Vorhoelter F.-J., Weidner S., Kaiser O., Golyshin P.N.; RT "Genome sequence of the ubiquitous hydrocarbon-degrading marine RT bacterium Alcanivorax borkumensis."; RL Nat. Biotechnol. 24:997-1004(2006). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AM286690; CAL17650.1; -; Genomic_DNA. DR ProteinModelPortal; Q0VME8; -. DR STRING; 393595.ABO_2202; -. DR EnsemblBacteria; CAL17650; CAL17650; ABO_2202. DR KEGG; abo:ABO_2202; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000008871; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000008871}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000008871}. FT DOMAIN 228 394 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 480 AA; 53929 MW; E7029F9A96C9ADCE CRC64; MHFLPFHHLP GLNWGYLSPY PHPMDLFDRT EQTRTEAGER AILVHLELPD AMGREDLDEF HHLVTSSGVL PVIQLTGKRD RPDPALFIGT GKTDELAAMV SEHQADVVLF NHALSPGQER NLERVVKCRV LDRTGLILDI FAQRARTHEG RLQVELAQLR HLSSRLVRGW THLERQKGGI GLRGPGETQL ETDRRLLRDR IRGIESRLEK VRKQRAQGRR ARQRSETPLI SLVGYTNAGK STLFNAITTG DVYVADQLFA TLDPTLRKVK VPGVGPAILA DTVGFIRHLP HRLVQAFRAT LEETVNANLL LHVTDCSAEE RDNNVVAVNE VLEEIGGDKL PVLHVYNKVD NLDQPPRLER DEHGQPWRVW VSAQTGDGFD LLFDAIAERL AAGWVDCWVR LPASAGRLRA RLHEAGEVLE EQTGNNGDML LRVNVNRVHF ERLLREQGLK EEELVIPAPA VAAEDAPSYN SEHSTNASHH // ID Q0W2G5_METAR Unreviewed; 425 AA. AC Q0W2G5; DT 05-SEP-2006, integrated into UniProtKB/TrEMBL. DT 05-SEP-2006, sequence version 1. DT 07-JUN-2017, entry version 81. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=RCIX2332 {ECO:0000313|EMBL:CAJ37428.1}; OS Methanocella arvoryzae (strain DSM 22066 / NBRC 105507 / MRE50). OC Archaea; Euryarchaeota; Methanomicrobia; Methanocellales; OC Methanocellaceae; Methanocella. OX NCBI_TaxID=351160 {ECO:0000313|EMBL:CAJ37428.1, ECO:0000313|Proteomes:UP000000663}; RN [1] {ECO:0000313|EMBL:CAJ37428.1, ECO:0000313|Proteomes:UP000000663} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 22066 / NBRC 105507 / MRE50 RC {ECO:0000313|Proteomes:UP000000663}; RX PubMed=16857943; DOI=10.1126/science.1127062; RA Erkel C., Kube M., Reinhardt R., Liesack W.; RT "Genome of rice cluster I archaea -- the key methane producers in the RT rice rhizosphere."; RL Science 313:370-372(2006). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AM114193; CAJ37428.1; -; Genomic_DNA. DR RefSeq; WP_012035153.1; NC_009464.1. DR ProteinModelPortal; Q0W2G5; -. DR STRING; 351160.RCIX2332; -. DR EnsemblBacteria; CAJ37428; CAJ37428; RCIX2332. DR GeneID; 5144054; -. DR KEGG; rci:RCIX2332; -. DR PATRIC; fig|351160.9.peg.853; -. DR eggNOG; arCOG00353; Archaea. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG093Z07D6; -. DR BioCyc; MARV351160:G12X7-841-MONOMER; -. DR Proteomes; UP000000663; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000000663}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000000663}. FT DOMAIN 189 358 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 425 AA; 47771 MW; 85165797EB4B6199 CRC64; MPGAILIKRI NPQHRDQNLD ELEELAKSAG YEVLDKITQV RPLPDKAYCI GRGKAEEVSE LLAAERPDKV IFDEKLNAVQ AYNLSKLFQV EVIDRFNLIL EIFAQRARTK EARLQVELAN LIYERPRARM KVTLARRGEQ PGFKGLGQYQ ADIYESEITG RIAKIKEELA VIRKRQDQTR LRRKERGFDM VALAGYTNAG KSTLMNALVG ETVVAKDQLF TTLVPTTRMM EAGRRRVLLT DTVGFIKDLP HFMVEAFRST LEEIYLADLI ILVVDASEPP EVVLEKLATC HDTLWGKIGP IPVITALNKI DKIDLPTLER TEAAIKNLAP HPVAVSARTG DGLEELRATV EFFLPKWVSA ELTLPHTEEG LSTLSQLYDE AIVRDVQYGT GPKGPCIRVS VDARESVLSR LAERTQDWMQ KGACQ // ID Q0YPP2_9CHLB Unreviewed; 434 AA. AC Q0YPP2; DT 05-SEP-2006, integrated into UniProtKB/TrEMBL. DT 05-SEP-2006, sequence version 1. DT 07-JUN-2017, entry version 49. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=CferDRAFT_0236 {ECO:0000313|EMBL:EAT58250.1}; OS Chlorobium ferrooxidans DSM 13031. OC Bacteria; Chlorobi; Chlorobia; Chlorobiales; Chlorobiaceae; OC Chlorobium/Pelodictyon group; Chlorobium. OX NCBI_TaxID=377431 {ECO:0000313|EMBL:EAT58250.1, ECO:0000313|Proteomes:UP000004162}; RN [1] {ECO:0000313|EMBL:EAT58250.1, ECO:0000313|Proteomes:UP000004162} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 13031 {ECO:0000313|EMBL:EAT58250.1, RC ECO:0000313|Proteomes:UP000004162}; RG US DOE Joint Genome Institute (JGI-ORNL); RA Larimer F., Land M., Hauser L.; RT "Annotation of the draft genome assembly of Chlorobium ferroxidans DSM RT 13031."; RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:EAT58250.1, ECO:0000313|Proteomes:UP000004162} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 13031 {ECO:0000313|EMBL:EAT58250.1, RC ECO:0000313|Proteomes:UP000004162}; RG US DOE Joint Genome Institute (JGI-PGF); RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., RA Dalin E., Tice H., Bruce D., Pitluck S., Richardson P.; RT "Sequencing of the draft genome and assembly of Chlorobium ferroxidans RT DSM 13031."; RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EAT58250.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AASE01000025; EAT58250.1; -; Genomic_DNA. DR RefSeq; WP_006367124.1; NZ_AASE01000025.1. DR ProteinModelPortal; Q0YPP2; -. DR STRING; 377431.CferDRAFT_0236; -. DR EnsemblBacteria; EAT58250; EAT58250; CferDRAFT_0236. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR Proteomes; UP000004162; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000004162}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000004162}. FT DOMAIN 202 369 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 434 AA; 49245 MW; 94AD540A67B4010A CRC64; MNTLPSDNKR EKAVLVGLCS QPETPRALVE EYLAELAFLA DTAGADVIES YIQEKKIRDP AYCIGKGKVD ELIPFVKEHE VDLVIFDDDL TPGQARNLER ALECKVIDRT GLILQIFAIR AQSAQARMQV ELAQLEYMLP RLSGAWTHLS KQKGGIGSKG PGETQIETDR RLVRNRISLL KKKLREVSLQ HNTQTRGRQT VPRVALVGYT NAGKSTLMNI LCPEAEAFAE NRLFATLDTK TRRLELSINK LVLLSDTVGF IRKLPHHLVE SFKSTLDEVL QADFLLHVID ISHPGFEDQM QVVRETLKEL GVDHENFIEV FNKIDALEDQ ELLKSIRAKY PDAVFISAAR GVNIPVLKEI IGKYVARDYK ERKILTHVSN YKLIGYLYEN TEVIEKRYLD EDVELTFRVH KNRIKHIDAL VGASEPLQYD TTDS // ID Q10X14_TRIEI Unreviewed; 574 AA. AC Q10X14; DT 22-AUG-2006, integrated into UniProtKB/TrEMBL. DT 22-AUG-2006, sequence version 1. DT 07-JUN-2017, entry version 78. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Tery_4208 {ECO:0000313|EMBL:ABG53210.1}; OS Trichodesmium erythraeum (strain IMS101). OC Bacteria; Cyanobacteria; Oscillatoriophycideae; Oscillatoriales; OC Microcoleaceae; Trichodesmium. OX NCBI_TaxID=203124 {ECO:0000313|EMBL:ABG53210.1, ECO:0000313|Proteomes:UP000008878}; RN [1] {ECO:0000313|EMBL:ABG53210.1, ECO:0000313|Proteomes:UP000008878} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=IMS101 {ECO:0000313|EMBL:ABG53210.1, RC ECO:0000313|Proteomes:UP000008878}; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., RA Pitluck S., Kiss H., Munk A.C., Brettin T., Bruce D., Han C., RA Tapia R., Gilna P., Schmutz J., Larimer F., Land M., Hauser L., RA Kyrpides N., Kim E., Richardson P.; RT "Complete sequence of Trichodesmium erythraeum IMS101."; RL Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000393; ABG53210.1; -; Genomic_DNA. DR RefSeq; WP_011613540.1; NC_008312.1. DR ProteinModelPortal; Q10X14; -. DR STRING; 203124.Tery_4208; -. DR EnsemblBacteria; ABG53210; ABG53210; Tery_4208. DR KEGG; ter:Tery_4208; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; EREVIIT; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000008878; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000008878}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000008878}. FT DOMAIN 402 574 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 361 398 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 574 AA; 63209 MW; 03F9C4B1AACD39B1 CRC64; MPIETIYGNL KGLKSSQLKQ LQRLYHQRLT SDRLTTSEFA QRVASISTEV GQSICVYINR RGQIIRVGVG TPHQTQIPPL ELPRYGNGRL SGIRCIATNL KAEDPSEAAL TAMVIQRLDA LVILTLTGEG FKRRGGGATG YIKQAYLAHL LPIPTHEGVN TDIQKLNFWS VSPPLSLDAL AKQDFIDLID GLEAEFQREF IAQEVDSDQD LVLLVGLKID KMTNQQFEDG LAELARLVET AGGKVLKTVD QKRSHPHPQT VVGEGKVQEI ALSVQTVGAN LVVFDQDLSP AQVRNLETKI GVRVVDRTEV ILDIFAQRAQ SRAGKLQVEL AQLKYTIPHL TGQGEAMSRL GGGIGTRGPG ETKLETERRA INARISRLQK EVNQLQAHRS RLRQHRQHQE VPTVAIVGYT NAGKSTLLNT LTNSEVYAAD KLFATLDPIT RRLNVPDTVT GKPTTIVITD TVGFIHELPP TLMNAFRATL EEVTDADALL HVVDLSHPAW QSQIRSVMTI LQEMPETPGP ALVAFNKIDE VDGDTLKFAH EEYPMAVFIS AAKALGLETL RQRLAQLIDY VVAS // ID Q11HW8_CHESB Unreviewed; 460 AA. AC Q11HW8; DT 22-AUG-2006, integrated into UniProtKB/TrEMBL. DT 22-AUG-2006, sequence version 1. DT 07-JUN-2017, entry version 79. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Meso_1612 {ECO:0000313|EMBL:ABG63007.1}; OS Chelativorans sp. (strain BNC1). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Phyllobacteriaceae; Chelativorans. OX NCBI_TaxID=266779 {ECO:0000313|EMBL:ABG63007.1, ECO:0000313|Proteomes:UP000001820}; RN [1] {ECO:0000313|Proteomes:UP000001820} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BNC1 {ECO:0000313|Proteomes:UP000001820}; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., RA Pitluck S., Chertkov O., Brettin T., Bruce D., Han C., Tapia R., RA Gilna P., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., RA Mikhailova N., Richardson P.; RT "Complete sequence of chromosome of Mesorhizobium sp. BNC1."; RL Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000390; ABG63007.1; -; Genomic_DNA. DR RefSeq; WP_011580950.1; NC_008254.1. DR ProteinModelPortal; Q11HW8; -. DR STRING; 266779.Meso_1612; -. DR EnsemblBacteria; ABG63007; ABG63007; Meso_1612. DR KEGG; mes:Meso_1612; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000001820; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000001820}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000001820}. FT DOMAIN 230 401 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 460 AA; 50752 MW; D6F7E89A792B10BA CRC64; MAGKPKAHHA AGVAQDGAGA SARTKAVVVA PSVAARARAA VEDGEQRRHI PLSPQAKLDE AVGLAEAIDL EITHSEFFTV AQPRPATLIG AGKVKDLANI VAETGAELVI IDHQLTPVQQ RNLERELKAK VLDRTGLILE IFGRRARTKE GRLQVDLAHL EYQRGRLVRS WTHLERQRGG GGFMGGPGET QIEADRRLLQ ERIIRIKREL ETVRRTRDLH RTKRRKVPFP IVAIVGYTNA GKSTLFNRLT GASVLAEDML FATLDPTLRR VRFPHGTVVI LSDTVGFISD LPPHLVAAFR ATLEEVVEAD VILHLRDISD PDTAAHARDV EQVLASLGVD TSDPARAVEV WNKIDRLSEA DRERLLRDDI NKTAPIAISA ITGEGIEDLM ALVEERLSGE VSEVLFTLSS EQMGLMDWIY RHARVTNRKD NEDGGSTVKI RATQAAREEI SRRLSRNNKG // ID Q11NE1_CYTH3 Unreviewed; 392 AA. AC Q11NE1; DT 22-AUG-2006, integrated into UniProtKB/TrEMBL. DT 22-AUG-2006, sequence version 1. DT 07-JUN-2017, entry version 83. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:ABG61072.1}; GN OrderedLocusNames=CHU_3840 {ECO:0000313|EMBL:ABG61072.1}; OS Cytophaga hutchinsonii (strain ATCC 33406 / NCIMB 9469). OC Bacteria; Bacteroidetes; Cytophagia; Cytophagales; Cytophagaceae; OC Cytophaga. OX NCBI_TaxID=269798 {ECO:0000313|EMBL:ABG61072.1, ECO:0000313|Proteomes:UP000001822}; RN [1] {ECO:0000313|EMBL:ABG61072.1, ECO:0000313|Proteomes:UP000001822} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33406 / NCIMB 9469 {ECO:0000313|Proteomes:UP000001822}; RX PubMed=17400776; DOI=10.1128/AEM.00225-07; RA Xie G., Bruce D.C., Challacombe J.F., Chertkov O., Detter J.C., RA Gilna P., Han C.S., Lucas S., Misra M., Myers G.L., Richardson P., RA Tapia R., Thayer N., Thompson L.S., Brettin T.S., Henrissat B., RA Wilson D.B., McBride M.J.; RT "Genome sequence of the cellulolytic gliding bacterium Cytophaga RT hutchinsonii."; RL Appl. Environ. Microbiol. 73:3536-3546(2007). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000383; ABG61072.1; -; Genomic_DNA. DR RefSeq; WP_011587177.1; NZ_FPJX01000004.1. DR STRING; 269798.CHU_3840; -. DR EnsemblBacteria; ABG61072; ABG61072; CHU_3840. DR KEGG; chu:CHU_3840; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000001822; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000001822}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Hydrolase {ECO:0000313|EMBL:ABG61072.1}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000001822}. SQ SEQUENCE 392 AA; 44851 MW; 9DE52B03239F633D CRC64; MMQEETGFST HKIADKAILI GLSHRNQPQE KTIEYLDELD FLARTAGLEV VYRFTQKLDR PDIRTYIGKG KLADVKLYIQ THSIPVIIFD DELSPSQLRN LEKELACKIY DRSLLILDIF SLRAQTAQSR TQVELARLQY LLPRLTNMWT HLERQRGGTG TRGGSGEKEI ETDRRIIRDQ ISLLKTRLAK INKQSETQRK SRDGIVRVAL VGYTNVGKST LMQRLSKSDV FAENKLFATV DSTVRKVVLN EIPFLLTDTV GFIRKLPHGL IESFKSTLDE VREADILLHV IDLPHPSYEE HMQVVQSTLA EIKANDKIVV LVFNKVDVYL KNIQNDPDAL SLQEIDKMYT GKENSNRVFI SATENLNIDK LRAVLIEKVT TVHCTIYPNY LL // ID Q12AC4_POLSJ Unreviewed; 386 AA. AC Q12AC4; DT 22-AUG-2006, integrated into UniProtKB/TrEMBL. DT 22-AUG-2006, sequence version 1. DT 05-JUL-2017, entry version 80. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Bpro_2602 {ECO:0000313|EMBL:ABE44518.1}; OS Polaromonas sp. (strain JS666 / ATCC BAA-500). OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Comamonadaceae; Polaromonas. OX NCBI_TaxID=296591 {ECO:0000313|EMBL:ABE44518.1, ECO:0000313|Proteomes:UP000001983}; RN [1] {ECO:0000313|Proteomes:UP000001983} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=JS666 / ATCC BAA-500 {ECO:0000313|Proteomes:UP000001983}; RX PubMed=18723656; DOI=10.1128/AEM.00197-08; RA Mattes T.E., Alexander A.K., Richardson P.M., Munk A.C., Han C.S., RA Stothard P., Coleman N.V.; RT "The genome of Polaromonas sp. strain JS666: insights into the RT evolution of a hydrocarbon- and xenobiotic-degrading bacterium, and RT features of relevance to biotechnology."; RL Appl. Environ. Microbiol. 74:6405-6416(2008). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000316; ABE44518.1; -; Genomic_DNA. DR ProteinModelPortal; Q12AC4; -. DR STRING; 296591.Bpro_2602; -. DR EnsemblBacteria; ABE44518; ABE44518; Bpro_2602. DR KEGG; pol:Bpro_2602; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000001983; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000001983}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Hydrolase {ECO:0000313|EMBL:ABE44518.1}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000001983}. FT DOMAIN 195 374 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 386 AA; 42321 MW; 32971F74F9ADB66D CRC64; MKTPTLALLV GVDLGLPNFD ADLQELGLLA QTAGLQPVAR VTCRRKAPDA ALFIGSGKAD EIKMLALDTG ASEILFDQSL SPAQQRNLER HLELPVNDRT LLILEIFAQR AHSHEGKLQV ELARLQYVST RLVRRWSHLE RQTGGAGVRG GPGEKQIELD KRMIGDAIKR TKERLGKVKK QRQTQRKQRE RRNSFTISLV GYTNAGKSTL FNALVKARAY AADQLFATLD TTTRQLYLGD AARSVSLSDT VGFIRDLPHG LIDAFAATLQ EAADADLLLH VVDGSNPDYL EQIEQVQRVL AEIGAADVPQ ILVFNKLDAV EKGNSPLSLR DMFELRDAFE GASRSVDRVF VSALTGEGLP LLRELLASHV ASMVTGEILQ TADDLA // ID Q12J96_SHEDO Unreviewed; 435 AA. AC Q12J96; DT 22-AUG-2006, integrated into UniProtKB/TrEMBL. DT 22-AUG-2006, sequence version 1. DT 30-AUG-2017, entry version 79. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Sden_3204 {ECO:0000313|EMBL:ABE56480.1}; OS Shewanella denitrificans (strain OS217 / ATCC BAA-1090 / DSM 15013). OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales; OC Shewanellaceae; Shewanella. OX NCBI_TaxID=318161 {ECO:0000313|EMBL:ABE56480.1, ECO:0000313|Proteomes:UP000001982}; RN [1] {ECO:0000313|EMBL:ABE56480.1, ECO:0000313|Proteomes:UP000001982} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=OS217 / ATCC BAA-1090 / DSM 15013 RC {ECO:0000313|Proteomes:UP000001982}; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., RA Pitluck S., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Kiss H., RA Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Lykidis A., RA Richardson P.; RT "Complete sequence of Shewanella denitrificans OS217."; RL Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000302; ABE56480.1; -; Genomic_DNA. DR RefSeq; WP_011497625.1; NC_007954.1. DR ProteinModelPortal; Q12J96; -. DR STRING; 318161.Sden_3204; -. DR EnsemblBacteria; ABE56480; ABE56480; Sden_3204. DR KEGG; sdn:Sden_3204; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000001982; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000001982}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000001982}. FT DOMAIN 198 364 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 164 191 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 435 AA; 49024 MW; E4AB0213C9C33FFA CRC64; MFDRYEAGET AVLVHIDFSD DERREDLVEL QLLVESAGAR SVGVITGSRR APDRKFFVGT GKAEELAAMV AATEAKVVIF NHALSPAQER NLERVCHCRV LDRTTLILDI FAQRARTHEG KLQVELAQLR HMSTRLIRGW THLERQKGGI GMRGPGETQL ETDRRLLRGR IKNINRRLDK VDKQREQSRR SRKRSDLATV SLVGYTNAGK STLFNGLTSS DVYAADQLFA TLDPTLRKLD LPDGAVILAD TVGFIRHLPH DLVAAFKATL QETRQAELLL HIVDCADDNM QDNFDQVQDV LKEIDADEIP QLVVCNKIDL LEDFAPRIDY AEDGTPERVW LSAQKGQGFD LLLQAITELV GNIVLELTLK VPATGGHYIG QMYKLDVIEH KDYDDLGNCI VKIRLLDADW RRMIKQSQGE LETFVFEASE TDVIL // ID Q12TG4_METBU Unreviewed; 413 AA. AC Q12TG4; DT 22-AUG-2006, integrated into UniProtKB/TrEMBL. DT 22-AUG-2006, sequence version 1. DT 07-JUN-2017, entry version 86. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Mbur_2411 {ECO:0000313|EMBL:ABE53262.1}; OS Methanococcoides burtonii (strain DSM 6242 / NBRC 107633 / OCM 468 / OS ACE-M). OC Archaea; Euryarchaeota; Methanomicrobia; Methanosarcinales; OC Methanosarcinaceae; Methanococcoides. OX NCBI_TaxID=259564 {ECO:0000313|EMBL:ABE53262.1, ECO:0000313|Proteomes:UP000001979}; RN [1] {ECO:0000313|Proteomes:UP000001979} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 6242 / NBRC 107633 / OCM 468 / ACE-M RC {ECO:0000313|Proteomes:UP000001979}; RX PubMed=19404327; DOI=10.1038/ismej.2009.45; RA Allen M.A., Lauro F.M., Williams T.J., Burg D., Siddiqui K.S., RA De Francisci D., Chong K.W., Pilak O., Chew H.H., De Maere M.Z., RA Ting L., Katrib M., Ng C., Sowers K.R., Galperin M.Y., Anderson I.J., RA Ivanova N., Dalin E., Martinez M., Lapidus A., Hauser L., Land M., RA Thomas T., Cavicchioli R.; RT "The genome sequence of the psychrophilic archaeon, Methanococcoides RT burtonii: the role of genome evolution in cold adaptation."; RL ISME J. 3:1012-1035(2009). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000300; ABE53262.1; -; Genomic_DNA. DR RefSeq; WP_011500397.1; NC_007955.1. DR ProteinModelPortal; Q12TG4; -. DR STRING; 259564.Mbur_2411; -. DR EnsemblBacteria; ABE53262; ABE53262; Mbur_2411. DR GeneID; 3999001; -. DR KEGG; mbu:Mbur_2411; -. DR eggNOG; arCOG00353; Archaea. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG093Z07D6; -. DR Proteomes; UP000001979; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000001979}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000001979}. FT DOMAIN 191 360 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 413 AA; 47027 MW; 797D7F591EA1DF03 CRC64; MKKVILVQRN EPGTDHGTNE RKFVELKELA RAAHYNVVGV LTQTRYPDRK YQVGRGKVDE LAELVEALDA EKVIFNHQLS TTQIYNISET CKCEVIDRFN LILEIFASRA TTRRAKLQVE LAKLQYELPK ARAIVSLLKK DERPGFMGLG GYEDSYEQDV KKRIVRIRNE IHNSCKGGES LRSFRHERGF SLVALAGYTN AGKSTLFQSL VKEGVEVEDM LFTTLSPTTR SLSIKQRRVL LTDTVGFIED LPHWMVDAFR STLDEIFLAD VILLVVDMSD PLDVIRQKLV VSHDIFWKRT EGAEIVAVLN KADMVDPDDL ERKVDAISYL APHLVLVSAS SGDGFEVLLD TIYENLPHWS RSSISLDMSE DSLSIVSWLY DEGIVHSIDY GEYIVLEVEA REEILRKVRK YSI // ID Q13X34_PARXL Unreviewed; 404 AA. AC Q13X34; DT 22-AUG-2006, integrated into UniProtKB/TrEMBL. DT 22-AUG-2006, sequence version 1. DT 07-JUN-2017, entry version 80. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=Bxe_A1600 {ECO:0000313|EMBL:ABE31355.1}; OS Paraburkholderia xenovorans (strain LB400). OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Paraburkholderia. OX NCBI_TaxID=266265 {ECO:0000313|EMBL:ABE31355.1, ECO:0000313|Proteomes:UP000001817}; RN [1] {ECO:0000313|EMBL:ABE31355.1, ECO:0000313|Proteomes:UP000001817} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=LB400 {ECO:0000313|EMBL:ABE31355.1, RC ECO:0000313|Proteomes:UP000001817}; RX PubMed=17030797; DOI=10.1073/pnas.0606924103; RA Chain P.S.G., Denef V.J., Konstantinidis K.T., Vergez L.M., Agullo L., RA Reyes V.L., Hauser L., Cordova M., Gomez L., Gonzalez M., Land M., RA Lao V., Larimer F., LiPuma J.J., Mahenthiralingam E., Malfatti S.A., RA Marx C.J., Parnell J.J., Ramette A., Richardson P., Seeger M., RA Smith D., Spilker T., Sul W.J., Tsoi T.V., Ulrich L.E., Zhulin I.B., RA Tiedje J.M.; RT "Burkholderia xenovorans LB400 harbors a multi-replicon, 9.73-Mbp RT genome shaped for versatility."; RL Proc. Natl. Acad. Sci. U.S.A. 103:15280-15287(2006). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000270; ABE31355.1; -; Genomic_DNA. DR ProteinModelPortal; Q13X34; -. DR STRING; 266265.Bxe_A1600; -. DR EnsemblBacteria; ABE31355; ABE31355; Bxe_A1600. DR KEGG; bxe:Bxe_A1600; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000001817; Chromosome 1. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000001817}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Hydrolase {ECO:0000313|EMBL:ABE31355.1}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000001817}. FT DOMAIN 205 376 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 171 198 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 404 AA; 44379 MW; E520AB8DBFE0D1F7 CRC64; MAITPGRLIL ISSNLINAAL VGIDFGKIDF EASLEELSLL AQSAGANPLV TLTGRRSSPD AKMFVGSGKA EELRLACEAN DIELVIFNHA LAPAQQRNLE QALNRRVIDR TSLILDIFAQ RARSHEGKLQ VELAQLQYLS TRLIRAWTHL ERQKGGIGLR GPGETQLETD RRLIGERIKA LKTRLEKLRR QHGTQRRARS RNQTMSVSLV GYTNAGKSTL FNALTKAQAY AADQLFATLD TTSRRVYLGD EAGQVVVSDT VGFIRELPHQ LVAAFRATLE ETIHADLLLH VVDASSAVRL DQIDQVNEVL HAIGADTIRQ VLVFNKIDAV PELAARGDAV ERDEYGNISR VFLSARTGQG LDTLRAAIAE IATAEPLPET LVDLSEEDRS AAPRDDRKVP ELGH // ID Q15NQ9_PSEA6 Unreviewed; 432 AA. AC Q15NQ9; DT 25-JUL-2006, integrated into UniProtKB/TrEMBL. DT 25-JUL-2006, sequence version 1. DT 30-AUG-2017, entry version 82. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Patl_3979 {ECO:0000313|EMBL:ABG42479.1}; OS Pseudoalteromonas atlantica (strain T6c / ATCC BAA-1087). OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales; OC Pseudoalteromonadaceae; Pseudoalteromonas. OX NCBI_TaxID=342610 {ECO:0000313|EMBL:ABG42479.1, ECO:0000313|Proteomes:UP000001981}; RN [1] {ECO:0000313|EMBL:ABG42479.1, ECO:0000313|Proteomes:UP000001981} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=T6c / ATCC BAA-1087 {ECO:0000313|Proteomes:UP000001981}; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., RA Pitluck S., Saunders E., Brettin T., Bruce D., Han C., Tapia R., RA Gilna P., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., RA Kim E., Karls A.C., Bartlett D., Higgins B.P., Richardson P.; RT "Complete sequence of Pseudoalteromonas atlantica T6c."; RL Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000388; ABG42479.1; -; Genomic_DNA. DR RefSeq; WP_011576680.1; NC_008228.1. DR ProteinModelPortal; Q15NQ9; -. DR STRING; 342610.Patl_3979; -. DR EnsemblBacteria; ABG42479; ABG42479; Patl_3979. DR KEGG; pat:Patl_3979; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000001981; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000001981}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Hydrolase {ECO:0000313|EMBL:ABG42479.1}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000001981}. FT DOMAIN 198 365 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 432 AA; 48578 MW; 33B6E245A0EE2782 CRC64; MFDRYEAGEQ AVLVHIDFSD DNSKEDLLEL QLLATSAGVN AVDVVTGSRN APHTRYFVGS GKAEEIANTV RASEADVVIF NHSLSPSQER NLEQLCKCRV LDRTGLILDI FAQRARTHEG KLQVELAQLK HISTRLIRGW THLERQKGGI GLRGPGETQL ETDRRLLRAR IKSIQGRLRK VQKQREQGRR ARVRAEIPTL ALVGYTNAGK STLFNTITQS EVYAADQLFA TLDPTLRRIE LQDVGPAILA DTVGFIRHLP HDLVAAFKAT LQETQQADLL LHVVDYSDDQ FRENIDQVNE VLDEIDSDEI PQLMICNKID RMDGVEPRID RDENGVPTRV WMSAQQGLGT ELLFEALSDC LAQNMVRHQL RIPPQEGKLR GDLFNLNCIS EESYADNGDW LVEIHMPLAD WQRLAKHSDA DLAALIVKST EA // ID Q165Q7_ROSDO Unreviewed; 432 AA. AC Q165Q7; DT 25-JUL-2006, integrated into UniProtKB/TrEMBL. DT 25-JUL-2006, sequence version 1. DT 07-JUN-2017, entry version 82. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:ABG32286.1}; GN OrderedLocusNames=RD1_2754 {ECO:0000313|EMBL:ABG32286.1}; OS Roseobacter denitrificans (strain ATCC 33942 / OCh 114) (Erythrobacter OS sp. (strain OCh 114)) (Roseobacter denitrificans). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae; Roseobacter. OX NCBI_TaxID=375451 {ECO:0000313|EMBL:ABG32286.1, ECO:0000313|Proteomes:UP000007029}; RN [1] {ECO:0000313|EMBL:ABG32286.1, ECO:0000313|Proteomes:UP000007029} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33942 / OCh 114 {ECO:0000313|Proteomes:UP000007029}; RX PubMed=17098896; DOI=10.1128/JB.01390-06; RA Swingley W.D., Sadekar S., Mastrian S.D., Matthies H.J., Hao J., RA Ramos H., Acharya C.R., Conrad A.L., Taylor H.L., Dejesa L.C., RA Shah M.K., O'huallachain M.E., Lince M.T., Blankenship R.E., RA Beatty J.T., Touchman J.W.; RT "The complete genome sequence of Roseobacter denitrificans reveals a RT mixotrophic rather than photosynthetic metabolism."; RL J. Bacteriol. 189:683-690(2007). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000362; ABG32286.1; -; Genomic_DNA. DR RefSeq; WP_011568903.1; NZ_FOOO01000002.1. DR ProteinModelPortal; Q165Q7; -. DR STRING; 375451.RD1_2754; -. DR EnsemblBacteria; ABG32286; ABG32286; RD1_2754. DR KEGG; rde:RD1_2754; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; FNNHAHV; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000007029; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000007029}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000007029}. FT DOMAIN 212 381 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 432 AA; 48144 MW; D1BEBEBB0468EE2D CRC64; MSKPPFQIDE TIQTRVTRAW VLHPEIKSDP DRRLAEHALA EAVSLARALP ELEVVGADIV PLKTVRAGML FGSGKIDEIK KSLHDEEIEL VLVDGPVSPV QQRNLEKAWG VKLLDRTGLI LEIFSDRAAT REGVLQVEMA ALSYQRTRLV RAWTHLERQR GGLGFVGGPG ETQIEADRRA IDDQLTRLRR QLEKVVKTRA LHRAARAKIP YPIIALVGYT NAGKSTLFNH LTGADVMAKD MLFATLDPTM RRLRLPDGPE VILSDTVGFI SDLPTELVAA FRATLEEVLA ADVICHVRDI SHPETEAQAK DVQDIMTTLG VEEDRPTFEL WNKLDLLSEG EADAMRARAD RDPSVFAISA LSGEGLDGLL AAVTQTLQGK KRAATLTLSF SEGRKRAWLF EQELVEEEHQ TEDGFEIAVR WTVDQEAKYE RL // ID Q16ZN7_AEDAE Unreviewed; 518 AA. AC Q16ZN7; DT 25-JUL-2006, integrated into UniProtKB/TrEMBL. DT 25-JUL-2006, sequence version 1. DT 30-AUG-2017, entry version 74. DE SubName: Full=AAEL008133-PA {ECO:0000313|EMBL:EAT40121.1}; DE SubName: Full=GTP-binding protein hflx {ECO:0000313|VectorBase:AAEL008133-PA}; GN Name=5570158 {ECO:0000313|VectorBase:AAEL008133-PA}; GN ORFNames=AAEL008133 {ECO:0000313|EMBL:EAT40121.1}; OS Aedes aegypti (Yellowfever mosquito) (Culex aegypti). OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; OC Pterygota; Neoptera; Holometabola; Diptera; Nematocera; Culicoidea; OC Culicidae; Culicinae; Aedini; Aedes; Stegomyia. OX NCBI_TaxID=7159 {ECO:0000313|EMBL:EAT40121.1, ECO:0000313|Proteomes:UP000008820}; RN [1] {ECO:0000313|EMBL:EAT40121.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=Liverpool {ECO:0000313|EMBL:EAT40121.1}; RA Loftus B.J., Nene V.M., Hannick L.I., Bidwell S., Haas B., Amedeo P., RA Orvis J., Wortman J.R., White O.R., Salzberg S., Shumway M., Koo H., RA Zhao Y., Holmes M., Miller J., Schatz M., Pop M., Pai G., RA Utterback T., Rogers Y.-H., Kravitz S., Fraser C.M.; RL Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:EAT40121.1, ECO:0000313|Proteomes:UP000008820, ECO:0000313|VectorBase:AAEL008133-PA} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Liverpool {ECO:0000313|EMBL:EAT40121.1}, and RC Liverpool/LVPib12 {ECO:0000313|Proteomes:UP000008820, RC ECO:0000313|VectorBase:AAEL008133-PA}; RX PubMed=17510324; DOI=10.1126/science.1138878; RA Nene V., Wortman J.R., Lawson D., Haas B.J., Kodira C.D., Tu Z.J., RA Loftus B.J., Xi Z., Megy K., Grabherr M., Ren Q., Zdobnov E.M., RA Lobo N.F., Campbell K.S., Brown S.E., Bonaldo M.F., Zhu J., RA Sinkins S.P., Hogenkamp D.G., Amedeo P., Arensburger P., RA Atkinson P.W., Bidwell S.L., Biedler J., Birney E., Bruggner R.V., RA Costas J., Coy M.R., Crabtree J., Crawford M., DeBruyn B., RA DeCaprio D., Eiglmeier K., Eisenstadt E., El-Dorry H., Gelbart W.M., RA Gomes S.L., Hammond M., Hannick L.I., Hogan J.R., Holmes M.H., RA Jaffe D., Johnston S.J., Kennedy R.C., Koo H., Kravitz S., RA Kriventseva E.V., Kulp D., Labutti K., Lee E., Li S., Lovin D.D., RA Mao C., Mauceli E., Menck C.F., Miller J.R., Montgomery P., Mori A., RA Nascimento A.L., Naveira H.F., Nusbaum C., O'Leary S.B., Orvis J., RA Pertea M., Quesneville H., Reidenbach K.R., Rogers Y.-H.C., Roth C.W., RA Schneider J.R., Schatz M., Shumway M., Stanke M., Stinson E.O., RA Tubio J.M.C., Vanzee J.P., Verjovski-Almeida S., Werner D., RA White O.R., Wyder S., Zeng Q., Zhao Q., Zhao Y., Hill C.A., RA Raikhel A.S., Soares M.B., Knudson D.L., Lee N.H., Galagan J., RA Salzberg S.L., Paulsen I.T., Dimopoulos G., Collins F.H., Bruce B., RA Fraser-Liggett C.M., Severson D.W.; RT "Genome sequence of Aedes aegypti, a major arbovirus vector."; RL Science 316:1718-1723(2007). RN [3] {ECO:0000313|EMBL:EAT40121.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=Liverpool {ECO:0000313|EMBL:EAT40121.1}; RG VectorBase; RL Submitted (SEP-2012) to the EMBL/GenBank/DDBJ databases. RN [4] {ECO:0000313|VectorBase:AAEL008133-PA} RP IDENTIFICATION. RC STRAIN=Liverpool/LVPib12 {ECO:0000313|VectorBase:AAEL008133-PA}; RG VectorBase; RL Submitted (FEB-2017) to UniProtKB. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CH477487; EAT40121.1; -; Genomic_DNA. DR RefSeq; XP_001658960.1; XM_001658910.1. DR UniGene; Aae.2934; -. DR ProteinModelPortal; Q16ZN7; -. DR STRING; 7159.AAEL008133-PA; -. DR PRIDE; Q16ZN7; -. DR EnsemblMetazoa; AAEL008133-RA; AAEL008133-PA; AAEL008133. DR GeneID; 5570158; -. DR KEGG; aag:AaeL_AAEL008133; -. DR VectorBase; AAEL008133-RA; AAEL008133-PA; AAEL008133. DR eggNOG; KOG0410; Eukaryota. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000045792; -. DR InParanoid; Q16ZN7; -. DR OMA; MDTVGFM; -. DR OrthoDB; EOG091G0852; -. DR PhylomeDB; Q16ZN7; -. DR Proteomes; UP000008820; Unassembled WGS sequence. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR CDD; cd01878; HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008820}; KW Reference proteome {ECO:0000313|Proteomes:UP000008820}. FT DOMAIN 287 456 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 518 AA; 58286 MW; 78A78C465E76C510 CRC64; MATSLMRRCF RGALIRGALM GRTTVKLGSI SASFRCKYTD ANKFKGFKGK HKPMVFVDDG EVDRGNGSER FDFEDAEYDA VVNSAMHVQK RLQNEQHVLV IQPYVKWGPK KSGSQPEHQL QEAEALVRSL PKWRVEYSLK VPLESLEKKQ LFGAGKLEEI KAILSDLQTS GKLITCVFIS KGTLTLGQKQ LLEQHFKLPV MDRYSVVIQI LRLHAISTEA KLQVAMAEIP YIWSQMKDQD ASKGRVYFTE SQKQMLRLRE RKLKNELATI RSHRELLRNK RKQKAYPIVA VVGYTNAGKT SLIKALTEEK SLEPKDQLFA TLDVTAHAGL LPCKLEVLFM DTVGFMADIP TGLIECFVAT LEDAMLADVI VHVQDVSHEN FLEQKKHVET TLSSLLKTTG VASSHPKLDN VINVGNKVDL LPTTEKPTDM HLVSSKTLHG INELLQEIER QILQVTGRQK IIIRVPMGGS EVAWLYKNAA VTETAADPKD SQRMLVSAVI TEAKLQQFRH QFVRNGAR // ID Q185Z9_PEPD6 Unreviewed; 425 AA. AC Q185Z9; DT 25-JUL-2006, integrated into UniProtKB/TrEMBL. DT 25-JUL-2006, sequence version 1. DT 05-JUL-2017, entry version 79. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=CD630_22090 {ECO:0000313|EMBL:CAJ69094.1}; OS Peptoclostridium difficile (strain 630) (Clostridium difficile). OC Bacteria; Firmicutes; Clostridia; Clostridiales; OC Peptostreptococcaceae; Clostridioides. OX NCBI_TaxID=272563 {ECO:0000313|EMBL:CAJ69094.1, ECO:0000313|Proteomes:UP000001978}; RN [1] {ECO:0000313|EMBL:CAJ69094.1, ECO:0000313|Proteomes:UP000001978} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=630 {ECO:0000313|EMBL:CAJ69094.1, RC ECO:0000313|Proteomes:UP000001978}; RX PubMed=16804543; DOI=10.1038/ng1830; RA Sebaihia M., Wren B.W., Mullany P., Fairweather N.F., Minton N., RA Stabler R., Thomson N.R., Roberts A.P., Cerdeno-Tarraga A.M., Wang H., RA Holden M.T.G., Wright A., Churcher C., Quail M.A., Baker S., Bason N., RA Brooks K., Chillingworth T., Cronin A., Davis P., Dowd L., Fraser A., RA Feltwell T., Hance Z., Holroyd S., Jagels K., Moule S., Mungall K., RA Price C., Rabbinowitsch R., Sharp S., Simmonds M., Steven K., RA Unwin L., Whithead S., Dupuy B., Dougan G., Barrell B.and.Parkhill.J.; RT "The multidrug-resistant human pathogen Clostridium difficile has a RT highly mobile, mosaic genome."; RL Nat. Genet. 38:779-786(2006). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AM180355; CAJ69094.1; -; Genomic_DNA. DR RefSeq; WP_011861493.1; NC_009089.1. DR RefSeq; YP_001088723.1; NC_009089.1. DR ProteinModelPortal; Q185Z9; -. DR STRING; 272563.CD2209; -. DR EnsemblBacteria; CAJ69094; CAJ69094; CD630_22090. DR GeneID; 31353805; -. DR GeneID; 4914544; -. DR KEGG; cdf:CD630_22090; -. DR PATRIC; fig|272563.8.peg.2324; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; FNNHAHV; -. DR BioCyc; PDIF272563:G12WB-2364-MONOMER; -. DR Proteomes; UP000001978; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000001978}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000001978}. FT DOMAIN 198 371 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 157 184 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 425 AA; 48391 MW; 69A7C9BAC8933332 CRC64; MDMAKKGITV GLNINNKSED FNELMIELEN LCSACDIDVV GSITQNAKQV NRAFYIGTGK VEEILNLIKK ENIEIVIFYN ELSTSQLKNL EEKLNCEIID RTALILDIFA QRAKTREAKL QVEVASLKYM LPRLIGSNEN LGRQSGGVGT KNRGSGEKKL ELDRRRIEEK ITSLNRELDD LKFQRETQRS MRRKSNLPNV ALVGYTNAGK SSIMNKLVDI FKNSEEKKVF EKNMLFATLE TSVRNIVLAN NKEFLLSDTV GFVSNLPHDL VKAFRSTLEE ACEADVLLHV IDISNPSYKS HIKVTEDTLK QIGADGIPMI HVYNKIDLID VEVLDRILDS IDKEGIFVSV KKDINIDKMI KCICDSIFKD YVRCKFLIPY DKGHVVSYFN ENTSIINTEY REDGAILDVE CSNIEYNKYK KYALE // ID Q189Y8_PEPD6 Unreviewed; 427 AA. AC Q189Y8; DT 25-JUL-2006, integrated into UniProtKB/TrEMBL. DT 25-JUL-2006, sequence version 1. DT 05-JUL-2017, entry version 83. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=CD630_07880 {ECO:0000313|EMBL:CAJ67622.1}; OS Peptoclostridium difficile (strain 630) (Clostridium difficile). OC Bacteria; Firmicutes; Clostridia; Clostridiales; OC Peptostreptococcaceae; Clostridioides. OX NCBI_TaxID=272563 {ECO:0000313|EMBL:CAJ67622.1, ECO:0000313|Proteomes:UP000001978}; RN [1] {ECO:0000313|EMBL:CAJ67622.1, ECO:0000313|Proteomes:UP000001978} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=630 {ECO:0000313|EMBL:CAJ67622.1, RC ECO:0000313|Proteomes:UP000001978}; RX PubMed=16804543; DOI=10.1038/ng1830; RA Sebaihia M., Wren B.W., Mullany P., Fairweather N.F., Minton N., RA Stabler R., Thomson N.R., Roberts A.P., Cerdeno-Tarraga A.M., Wang H., RA Holden M.T.G., Wright A., Churcher C., Quail M.A., Baker S., Bason N., RA Brooks K., Chillingworth T., Cronin A., Davis P., Dowd L., Fraser A., RA Feltwell T., Hance Z., Holroyd S., Jagels K., Moule S., Mungall K., RA Price C., Rabbinowitsch R., Sharp S., Simmonds M., Steven K., RA Unwin L., Whithead S., Dupuy B., Dougan G., Barrell B.and.Parkhill.J.; RT "The multidrug-resistant human pathogen Clostridium difficile has a RT highly mobile, mosaic genome."; RL Nat. Genet. 38:779-786(2006). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AM180355; CAJ67622.1; -; Genomic_DNA. DR RefSeq; WP_009895824.1; NC_009089.1. DR RefSeq; YP_001087265.1; NC_009089.1. DR ProteinModelPortal; Q189Y8; -. DR STRING; 272563.CD0788; -. DR EnsemblBacteria; CAJ67622; CAJ67622; CD630_07880. DR GeneID; 31352346; -. DR GeneID; 4916832; -. DR KEGG; cdf:CD630_07880; -. DR KEGG; pdc:CDIF630_00907; -. DR PATRIC; fig|272563.120.peg.811; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR BioCyc; PDIF272563:G12WB-899-MONOMER; -. DR Proteomes; UP000001978; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000001978}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000001978}. FT DOMAIN 202 372 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 168 195 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 427 AA; 48486 MW; 493FD073B7A4CE22 CRC64; MKEIQEKALL VGLNLTTIVK KNDDIDTNES MEELKELTKA AGAEVVGSLI QNKHSVDAAY YIGKGKVEEI RAYSDSLDAT LVIFNDELSG AQIRNIENVV GRKVIDRTTL ILDIFAQRAL SKEGKLQVEL AQLKYRLPRL YGMGGEMSRT GAGIGTRGPG EQKLEIDKRH ILNKAADIRR ELKEVKKNRE TQRVKRLKSN IPIVALVGYT NAGKSTLLNE LIKTHKDYEQ EKEVFVKDML FATLDVTLRK ALLPNKKEFL VVDTVGFVSK LPHDLVEAFK ATLEEVQYAD LILHVIDATN TSYELQKSTT EGVLKELGVN DKKHILVYNK VDKLELDIYP KSQEDIVYIS AKQGINMDKL LNMIEIALME NTYSVSLMLP YERGDIFSRI KDKYNVENFE YGESGITLDV DLDEEDFNIY REYILEK // ID Q18HS5_HALWD Unreviewed; 561 AA. AC Q18HS5; DT 25-JUL-2006, integrated into UniProtKB/TrEMBL. DT 25-JUL-2006, sequence version 1. DT 07-JUN-2017, entry version 81. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:CAJ52460.1}; GN OrderedLocusNames=HQ_2339A {ECO:0000313|EMBL:CAJ52460.1}; OS Haloquadratum walsbyi (strain DSM 16790 / HBSQ001). OC Archaea; Euryarchaeota; Halobacteria; Haloferacales; Haloferacaceae; OC Haloquadratum. OX NCBI_TaxID=362976 {ECO:0000313|EMBL:CAJ52460.1, ECO:0000313|Proteomes:UP000001975}; RN [1] {ECO:0000313|EMBL:CAJ52460.1, ECO:0000313|Proteomes:UP000001975} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 16790 / HBSQ001 {ECO:0000313|Proteomes:UP000001975}; RX PubMed=16820047; DOI=10.1186/1471-2164-7-169; RA Bolhuis H.H., Palm P.P., Wende A.W., Falb M.M., Rampp M.M., RA Rodriguez-Valera F.F., Pfeiffer F.F., Oesterhelt D.D.; RT "The genome of the square archaeon Haloquadratum walsbyi: life at the RT limits of water activity."; RL BMC Genomics 7:169-169(2006). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AM180088; CAJ52460.1; -; Genomic_DNA. DR RefSeq; WP_011571586.1; NC_008212.1. DR ProteinModelPortal; Q18HS5; -. DR STRING; 362976.HQ2339A; -. DR EnsemblBacteria; CAJ52460; CAJ52460; HQ_2339A. DR GeneID; 4194114; -. DR KEGG; hwa:HQ_2339A; -. DR eggNOG; arCOG00353; Archaea. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG093Z07D6; -. DR Proteomes; UP000001975; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000001975}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000001975}. FT DOMAIN 190 373 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 561 AA; 62705 MW; 035DB1E72AB3B874 CRC64; MTISPVIVAQ RVDPNAVADL SEIADLARAA GYDVSNTLTQ SREEDAAYHF GEGKIEALAR LVKQTDAEAV IVDNRLGPYQ TYNIGGKLPT GVEVIDRFTL ILEIFGQRAN TRKAQLQVEL AELRYELPRV EAKSSLAKRD ERPGFMGLGE YDESRERDIK SQISRISQEL DAIAEKEQTR REQRRESGFD LVALAGYTNA GKSTLLRRLA DDLDITENKN RHPDLEQTAE SEDRLFTTLG TTTRRADTGR RDVLLTDTVG FVSDLPHWLV ESFESTLDSV YRADLVLLVV DASESIDAMR EKLITSHDTL YERNEAPIVT VLNKTDCVEE GELDRKMQSL DALAPNPVAV SGLTGENIEQ LTNRIENELP SWHDERLLLP LSDDAMSLVS WLYNHGHVEN EEYTDTGDAV LIEFSARSTI VKRARAKAAE LEESSSKGAS DESANTHDSN GVNTKTQAQL SERRHDNEIM ESESNPERMD TASDRESTSY EESDTTHQVA SDSPPDRMSD STREIHRNNP SQVTEDDVTQ EDHIDAVDID VNYPLMNEKN SSDTDTNSKA E // ID Q1AW37_RUBXD Unreviewed; 432 AA. AC Q1AW37; DT 11-JUL-2006, integrated into UniProtKB/TrEMBL. DT 11-JUL-2006, sequence version 1. DT 07-JUN-2017, entry version 76. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Rxyl_1429 {ECO:0000313|EMBL:ABG04391.1}; OS Rubrobacter xylanophilus (strain DSM 9941 / NBRC 16129). OC Bacteria; Actinobacteria; Rubrobacteria; Rubrobacterales; OC Rubrobacteraceae; Rubrobacter. OX NCBI_TaxID=266117 {ECO:0000313|EMBL:ABG04391.1, ECO:0000313|Proteomes:UP000006637}; RN [1] {ECO:0000313|EMBL:ABG04391.1, ECO:0000313|Proteomes:UP000006637} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 9941 / NBRC 16129 {ECO:0000313|Proteomes:UP000006637}; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., RA Pitluck S., Munk A.C., Brettin T., Bruce D., Han C., Tapia R., RA Gilna P., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., RA Lykidis A., da Costa M.S., Rainey F.A., Empadinhas N., Jolivet E., RA Battista J.R., Richardson P.; RT "Complete sequence of Rubrobacter xylanophilus DSM 9941."; RL Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000386; ABG04391.1; -; Genomic_DNA. DR RefSeq; WP_011564408.1; NC_008148.1. DR ProteinModelPortal; Q1AW37; -. DR STRING; 266117.Rxyl_1429; -. DR EnsemblBacteria; ABG04391; ABG04391; Rxyl_1429. DR KEGG; rxy:Rxyl_1429; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; FNNHAHV; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000006637; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000006637}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000006637}. FT DOMAIN 198 375 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 432 AA; 47074 MW; 8EC8A73014621B56 CRC64; MTEERSADNN RAVLVAAGEE RHLDELGRLA GTLGLEVAGR LEQARRDGAG YLGRGKREEL RELVEASGAS FVVADDELSA SQARVLERDA GATVVDRTEL IIRIFEAHAH DAASRLQVEL ADLEYRLPRL KGRNPELSRL AGGGGGGGRG ATRGPGEQQL EYDRRAIRDR ISVIRRKLRA EEASREVRAS RLRESGPPKV ALVGYTNAGK TTILNALSDA GKSTRDWLFE TLETTTRLVE GSSSDGVFRP GFVVTDTVGF IRKLPAQLVH SFASTLEAAR DADILILCAD SSSPDLEEEI QVVRRTLSDL LTGGGDAAGP PPAEILCLNK KDLLPDHRII QLRNRHPEAV MISALEEGGC GPLVERVYAE ISGMWERVGL LIPHSEYGAA SRLYGRAEIH SRRHTEEGVL LDVTLPREDV ARYEAYRVAA AS // ID Q1D1U2_MYXXD Unreviewed; 476 AA. AC Q1D1U2; DT 11-JUL-2006, integrated into UniProtKB/TrEMBL. DT 11-JUL-2006, sequence version 1. DT 07-JUN-2017, entry version 78. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=MXAN_5229 {ECO:0000313|EMBL:ABF92406.1}; OS Myxococcus xanthus (strain DK 1622). OC Bacteria; Proteobacteria; Deltaproteobacteria; Myxococcales; OC Cystobacterineae; Myxococcaceae; Myxococcus. OX NCBI_TaxID=246197 {ECO:0000313|EMBL:ABF92406.1, ECO:0000313|Proteomes:UP000002402}; RN [1] {ECO:0000313|EMBL:ABF92406.1, ECO:0000313|Proteomes:UP000002402} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DK 1622 {ECO:0000313|EMBL:ABF92406.1, RC ECO:0000313|Proteomes:UP000002402}; RX PubMed=17015832; DOI=10.1073/pnas.0607335103; RA Goldman B.S., Nierman W.C., Kaiser D., Slater S.C., Durkin A.S., RA Eisen J., Ronning C.M., Barbazuk W.B., Blanchard M., Field C., RA Halling C., Hinkle G., Iartchuk O., Kim H.S., Mackenzie C., Madupu R., RA Miller N., Shvartsbeyn A., Sullivan S.A., Vaudin M., Wiegand R., RA Kaplan H.B.; RT "Evolution of sensory complexity recorded in a myxobacterial genome."; RL Proc. Natl. Acad. Sci. U.S.A. 103:15200-15205(2006). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000113; ABF92406.1; -; Genomic_DNA. DR RefSeq; WP_011555196.1; NC_008095.1. DR ProteinModelPortal; Q1D1U2; -. DR STRING; 246197.MXAN_5229; -. DR EnsemblBacteria; ABF92406; ABF92406; MXAN_5229. DR KEGG; mxa:MXAN_5229; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; VILEIFH; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000002402; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 2. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000002402}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000002402}. FT DOMAIN 257 422 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 476 AA; 52113 MW; C14FFF78629FF7B3 CRC64; MRMAISTFPE RLRAVLVGVQ LPGVSDEEHA ADFAELRRLV HTLGYDTVAT VSQKRTRLAT GTVLGTGKLK ELAALTGGSG VIASGASDRT SKAREKWEAA ANTEPDSEDE VVEEEADGVE TEDALLPPPS EEDDKAEPRP TVVVVDHELS PGQLRNLEKA TGAMVLDRAG VIVDIFHRHA KSHEARMQVE IARLNYLAPR LRESTGGRER QQGRGAGDSA LELDRRKIRD RLAELREGLA AIQKDQDHRR YARRDLLRVA LVGYTNAGKS SLMRALTGST VLVADQLFAT LDTTVRAMQP ETRPRILVSD TVGFIQKLPH DLVASFRSTL DEALEASLLL YVVDASDPTW AAQLEVTRTV LRDIGADAVP SKLLFNKADR LDAAAKEALL AKHPDALLLS AHLPDDVAML RKNIIAFFES SMVEADLVIP YSRQGRISEV YEHTTVVSQA YDESGSRLRV RGLPGAIAKL TQSFQE // ID Q1DCL0_MYXXD Unreviewed; 550 AA. AC Q1DCL0; DT 11-JUL-2006, integrated into UniProtKB/TrEMBL. DT 11-JUL-2006, sequence version 1. DT 07-JUN-2017, entry version 78. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:ABF90422.1}; GN OrderedLocusNames=MXAN_1356 {ECO:0000313|EMBL:ABF90422.1}; OS Myxococcus xanthus (strain DK 1622). OC Bacteria; Proteobacteria; Deltaproteobacteria; Myxococcales; OC Cystobacterineae; Myxococcaceae; Myxococcus. OX NCBI_TaxID=246197 {ECO:0000313|EMBL:ABF90422.1, ECO:0000313|Proteomes:UP000002402}; RN [1] {ECO:0000313|EMBL:ABF90422.1, ECO:0000313|Proteomes:UP000002402} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DK 1622 {ECO:0000313|EMBL:ABF90422.1, RC ECO:0000313|Proteomes:UP000002402}; RX PubMed=17015832; DOI=10.1073/pnas.0607335103; RA Goldman B.S., Nierman W.C., Kaiser D., Slater S.C., Durkin A.S., RA Eisen J., Ronning C.M., Barbazuk W.B., Blanchard M., Field C., RA Halling C., Hinkle G., Iartchuk O., Kim H.S., Mackenzie C., Madupu R., RA Miller N., Shvartsbeyn A., Sullivan S.A., Vaudin M., Wiegand R., RA Kaplan H.B.; RT "Evolution of sensory complexity recorded in a myxobacterial genome."; RL Proc. Natl. Acad. Sci. U.S.A. 103:15200-15205(2006). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000113; ABF90422.1; -; Genomic_DNA. DR ProteinModelPortal; Q1DCL0; -. DR STRING; 246197.MXAN_1356; -. DR EnsemblBacteria; ABF90422; ABF90422; MXAN_1356. DR KEGG; mxa:MXAN_1356; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; EREVIIT; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000002402; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000002402}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000002402}. FT DOMAIN 378 542 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 337 364 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 550 AA; 60967 MW; D3B408AF245CFE4B CRC64; MKEIYGNTLG LKSSEQHRLR NTFRRRVPPH EIVSPELARH LTELSRELNR QVGVLVNRKG EIEHVIVGNA HKLELPDIGR ARAGQVRLRG LRLVHTHLKG EPLTKDDLTD LALLRLDCVA AVGVGHEGLP GVLHYAYLIP ENGSGDFWHV ETLPSVHVAQ PDLMDTLGAL EEEFNRKAAS RKVGGREKAI LVAVCLDGNR ALAESSLAEL KELARTAGVE VIDSVLQVKR EADPRYLIGR GKLEELNLRS MQTMVDLLIF DKDLTPSQGR HIGEATSLKI LDRSQLILDI FAQRAQSAEG KLQVELAQLK YRLPRLVQSD DSLSRLMGGI GGRGPGETKL EIDRRRVRER ITHLEKRIDA IGRERSVRRA QRNRRELPVI SIVGYTNAGK STLLNAITNA EVLAENKLFA TLDPTSRRLR FPQEREVIIT DTVGFIRDLP KDLVAAFRAT LEELYDASLL LHVVDAADPA RDEQVEAVEN ILESLDLMEK PRLMVWNKAD LLPPDEVAAL LRTRGGVAIS AATREGLATL LAKADTTLFA EGATEAIGAI // ID Q1G8E1_LACDA Unreviewed; 426 AA. AC Q1G8E1; DT 27-JUN-2006, integrated into UniProtKB/TrEMBL. DT 27-JUN-2006, sequence version 1. DT 07-JUN-2017, entry version 83. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Ldb2012 {ECO:0000313|EMBL:CAI98750.1}; OS Lactobacillus delbrueckii subsp. bulgaricus (strain ATCC 11842 / DSM OS 20081 / JCM 1002 / NBRC 13953 / NCIMB 11778). OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; OC Lactobacillus. OX NCBI_TaxID=390333 {ECO:0000313|EMBL:CAI98750.1, ECO:0000313|Proteomes:UP000001259}; RN [1] {ECO:0000313|EMBL:CAI98750.1, ECO:0000313|Proteomes:UP000001259} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 11842 / DSM 20081 / JCM 1002 / NBRC 13953 / NCIMB 11778 RC {ECO:0000313|Proteomes:UP000001259}; RX PubMed=16754859; DOI=10.1073/pnas.0603024103; RA van de Guchte M., Penaud S., Grimaldi C., Barbe V., Bryson K., RA Nicolas P., Robert C., Oztas S., Mangenot S., Couloux A., Loux V., RA Dervyn R., Bossy R., Bolotin A., Batto J.-M., Walunas T., RA Gibrat J.-F., Bessieres P., Weissenbach J., Ehrlich S.D., Maguin E.; RT "The complete genome sequence of Lactobacillus bulgaricus reveals RT extensive and ongoing reductive evolution."; RL Proc. Natl. Acad. Sci. U.S.A. 103:9274-9279(2006). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CR954253; CAI98750.1; -; Genomic_DNA. DR RefSeq; WP_011544279.1; NZ_JQAV01000029.1. DR ProteinModelPortal; Q1G8E1; -. DR STRING; 390333.Ldb2012; -. DR EnsemblBacteria; CAI98750; CAI98750; Ldb2012. DR GeneID; 4085227; -. DR KEGG; ldb:Ldb2012; -. DR PATRIC; fig|390333.13.peg.1233; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR Proteomes; UP000001259; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000001259}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000001259}. FT DOMAIN 205 373 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 426 AA; 46766 MW; 54A9B8D6DA574996 CRC64; MIDNQAHSVK AYLAGVNLDD PNFDYSMTEL ANLAEANNFT VVGSSQQKAE NIVASSYLGK GKVAEIKDLA QGLGASVLIV NDELTPVQIR NLEHMTKLRV IDRTELILEI FSSRARTKQA KLQVQLARLQ YELPRLHPSE NNLDQQHGSG GSTGGGFANR GAGESKLEMN RRTIGKQISA IKHELKEISG QEEIKAARRN QSQLPKVALV GYTNAGKSTT MNGLLKAFGA GNEDKQVMAK DMLFATLDTS VRRIDLDGFS FILSDTVGFV SKLPHKLVDS FKATLQEAKD ADLLINVVDA ADPNMNQMIK TTLEVLDEIG VKDLPMITAY NKADLTDRNY PQIEGGDLLY SAVDSASIQA LAKLITTRLF SNYQITGLRL PLTAGKDLAY LHQHSRVLKE DYQADGIEVS ARLSPQDRAR FSAYQI // ID Q1GGX8_RUEST Unreviewed; 423 AA. AC Q1GGX8; DT 27-JUN-2006, integrated into UniProtKB/TrEMBL. DT 27-JUN-2006, sequence version 1. DT 07-JUN-2017, entry version 81. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=TM1040_1355 {ECO:0000313|EMBL:ABF64088.1}; OS Ruegeria sp. (strain TM1040) (Silicibacter sp.). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae; Ruegeria. OX NCBI_TaxID=292414 {ECO:0000313|EMBL:ABF64088.1, ECO:0000313|Proteomes:UP000000636}; RN [1] {ECO:0000313|Proteomes:UP000000636} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=TM1040 {ECO:0000313|Proteomes:UP000000636}; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., RA Pitluck S., Brettin T., Bruce D., Han C., Tapia R., Goodwin L., RA Thompson L.S., Gilna P., Schmutz J., Larimer F., Land M., Hauser L., RA Kyrpides N., Kim E., Belas R., Moran M.A., Buchan A., Gonzalez J.M., RA Schell M.A., Sun F., Richardson P.; RT "Complete sequence of chromosome of Silicibacter sp. TM1040."; RL Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000377; ABF64088.1; -; Genomic_DNA. DR RefSeq; WP_011538694.1; NC_008044.1. DR ProteinModelPortal; Q1GGX8; -. DR STRING; 292414.TM1040_1355; -. DR EnsemblBacteria; ABF64088; ABF64088; TM1040_1355. DR KEGG; sit:TM1040_1355; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000000636; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000000636}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000000636}. FT DOMAIN 203 372 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 423 AA; 47374 MW; F7255CDAA4DC47FB CRC64; MEHDRKQTRA WVLHPDIKSD RDRRDAVPAL EEGVALAAAL PDLEVVGSTV VGLPKAHPGM LFGSGKIEEL KTLFKAEEVE LVLIDGPVSP VQQRNLEKAW KVKILDRTGL ILEIFSDRAR TREGVLQVEM AALSYQRTRL VRAWTHLERQ RGGLGFVGGP GETQIEADRR AIDEQLVRLR RQLDKVVKTR TLHRAARAKV PYPIVALVGY TNAGKSTLFN RLTGAEVMAK DMLFATLDPT MRRVELPDGP EVILSDTVGF ISDLPTELVA SFRATLEEVL AADVILHVRD ISHSDTEHQA EDVEQILSSL GVDEDRTVIE VWNKIDQLSE EEADACRQRA DRNDSLYAIS AITGEGLPQL LHDIAMKLQG VRVDEVLTLD FSQGKQRAWL FKQDVVQEEN QTDTGFEISV RWTEKQKAQY AAL // ID Q1GTN7_SPHAL Unreviewed; 432 AA. AC Q1GTN7; DT 27-JUN-2006, integrated into UniProtKB/TrEMBL. DT 27-JUN-2006, sequence version 1. DT 07-JUN-2017, entry version 79. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Sala_1271 {ECO:0000313|EMBL:ABF52985.1}; OS Sphingopyxis alaskensis (strain DSM 13593 / LMG 18877 / RB2256) OS (Sphingomonas alaskensis). OC Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales; OC Sphingomonadaceae; Sphingopyxis. OX NCBI_TaxID=317655 {ECO:0000313|EMBL:ABF52985.1, ECO:0000313|Proteomes:UP000006578}; RN [1] {ECO:0000313|EMBL:ABF52985.1, ECO:0000313|Proteomes:UP000006578} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 13593 / LMG 18877 / RB2256 RC {ECO:0000313|Proteomes:UP000006578}; RX PubMed=19805210; DOI=10.1073/pnas.0903507106; RA Lauro F.M., McDougald D., Thomas T., Williams T.J., Egan S., Rice S., RA DeMaere M.Z., Ting L., Ertan H., Johnson J., Ferriera S., Lapidus A., RA Anderson I., Kyrpides N., Munk A.C., Detter C., Han C.S., Brown M.V., RA Robb F.T., Kjelleberg S., Cavicchioli R.; RT "The genomic basis of trophic strategy in marine bacteria."; RL Proc. Natl. Acad. Sci. U.S.A. 106:15527-15533(2009). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000356; ABF52985.1; -; Genomic_DNA. DR RefSeq; WP_011541568.1; NC_008048.1. DR ProteinModelPortal; Q1GTN7; -. DR STRING; 317655.Sala_1271; -. DR EnsemblBacteria; ABF52985; ABF52985; Sala_1271. DR KEGG; sal:Sala_1271; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; FNNHAHV; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000006578; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000006578}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000006578}. FT DOMAIN 192 372 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 432 AA; 47477 MW; CB38F0A36DD18099 CRC64; MIIVPEWHGQ RLARDLDARA EEAKGLALAI GLDVVAIHRL RLRQTRAATL LGVGQIEAIV PDIAARGVQL VVVDASLTAI QQRNLETAFG TKVIDRTGLI LEIFGERAAT AEGRLQVELA HLDYQAGRLV RSWTHLERQR GGFGFLGGPG ETQIEADRRM IRNRMARIRR SLEDARRTRQ LQRTKRQRAP WPVIALVGYT NAGKSTFFNR LTGSDVMAED MLFATLDPTM REIRLPGIDK AILSDTVGFV SDLPTELVAA FRATLEEVTT ADLIVHVRDI VHPDTDAQYE DVRAILDSLG VNGPQDGEGA DTASAIPQIE IWNKVDTANV DRRAAIEDMA ARRSDVAIIS AATGEGVEAA RTLMASQLTA RHQVQRIYLG YEQGDAAAWL HARGEVLADE AEGEGHVLTV RLDPADRARF ERLWPANGPP SP // ID Q1H0Y1_METFK Unreviewed; 375 AA. AC Q1H0Y1; DT 27-JUN-2006, integrated into UniProtKB/TrEMBL. DT 27-JUN-2006, sequence version 1. DT 30-AUG-2017, entry version 89. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Mfla_1588 {ECO:0000313|EMBL:ABE49856.1}; OS Methylobacillus flagellatus (strain KT / ATCC 51484 / DSM 6875). OC Bacteria; Proteobacteria; Betaproteobacteria; Nitrosomonadales; OC Methylophilaceae; Methylobacillus. OX NCBI_TaxID=265072 {ECO:0000313|EMBL:ABE49856.1, ECO:0000313|Proteomes:UP000002440}; RN [1] {ECO:0000313|EMBL:ABE49856.1, ECO:0000313|Proteomes:UP000002440} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=KT / ATCC 51484 / DSM 6875 {ECO:0000313|Proteomes:UP000002440}; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., RA Pitluck S., Brettin T., Bruce D., Han C., Tapia R., Saunders E., RA Gilna P., Schmutz J., Larimer F., Land M., Kyrpides N., Anderson I., RA Richardson P.; RT "Complete sequence of Methylobacillus flagellatus KT."; RL Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000284; ABE49856.1; -; Genomic_DNA. DR RefSeq; WP_011479810.1; NC_007947.1. DR ProteinModelPortal; Q1H0Y1; -. DR STRING; 265072.Mfla_1588; -. DR DNASU; 4000467; -. DR EnsemblBacteria; ABE49856; ABE49856; Mfla_1588. DR KEGG; mfa:Mfla_1588; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000002440; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000002440}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Hydrolase {ECO:0000313|EMBL:ABE49856.1}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000002440}. FT DOMAIN 199 365 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 158 192 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 375 AA; 41429 MW; F52CD34284769D8C CRC64; MFDRPVGGDA SVLVSVDFGD PGYEESLQEL RQLVVSAGMS IAGTVEARRP KPDPKFFVGS GKADELLAVV KTTDAKVAVF NHDLSPSQQR NLERLLEVRV VDRTGLILDI FALRAQSHEG KLQVELAQLE HLSTRLVRGW THLERQKGGI GVRGGPGETQ LELDRRMLRI RVKQLREKLA KLKQQRGMQR RARRRSQVLS VSLVGYTNAG KSTLFNRLTQ SGVYAADQLF ATLDTTSRKL YIPDGGPVVM SDTVGFIKHL PHALVEAFGA TLEEAVQADL LLHIVDVASD SRDEQVEQVN LVLSEIGAQD VPQVLVLNQI DRVGIPPGLD RDEYGRISKV RVSAKTGEGL DLLRQALLEH QQGLQDQLTQ SYQNA // ID Q1IIG0_KORVE Unreviewed; 451 AA. AC Q1IIG0; DT 13-JUN-2006, integrated into UniProtKB/TrEMBL. DT 13-JUN-2006, sequence version 1. DT 07-JUN-2017, entry version 75. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Acid345_4340 {ECO:0000313|EMBL:ABF43340.1}; OS Koribacter versatilis (strain Ellin345). OC Bacteria; Acidobacteria; Acidobacteriales; Acidobacteriaceae; OC Candidatus Koribacter. OX NCBI_TaxID=204669 {ECO:0000313|EMBL:ABF43340.1, ECO:0000313|Proteomes:UP000002432}; RN [1] {ECO:0000313|EMBL:ABF43340.1, ECO:0000313|Proteomes:UP000002432} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Ellin345 {ECO:0000313|EMBL:ABF43340.1, RC ECO:0000313|Proteomes:UP000002432}; RX PubMed=19201974; DOI=10.1128/AEM.02294-08; RA Ward N.L., Challacombe J.F., Janssen P.H., Henrissat B., RA Coutinho P.M., Wu M., Xie G., Haft D.H., Sait M., Badger J., RA Barabote R.D., Bradley B., Brettin T.S., Brinkac L.M., Bruce D., RA Creasy T., Daugherty S.C., Davidsen T.M., DeBoy R.T., Detter J.C., RA Dodson R.J., Durkin A.S., Ganapathy A., Gwinn-Giglio M., Han C.S., RA Khouri H., Kiss H., Kothari S.P., Madupu R., Nelson K.E., Nelson W.C., RA Paulsen I., Penn K., Ren Q., Rosovitz M.J., Selengut J.D., RA Shrivastava S., Sullivan S.A., Tapia R., Thompson L.S., Watkins K.L., RA Yang Q., Yu C., Zafar N., Zhou L., Kuske C.R.; RT "Three genomes from the phylum Acidobacteria provide insight into the RT lifestyles of these microorganisms in soils."; RL Appl. Environ. Microbiol. 75:2046-2056(2009). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000360; ABF43340.1; -; Genomic_DNA. DR RefSeq; WP_011525137.1; NC_008009.1. DR ProteinModelPortal; Q1IIG0; -. DR STRING; 204669.Acid345_4340; -. DR EnsemblBacteria; ABF43340; ABF43340; Acid345_4340. DR KEGG; aba:Acid345_4340; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000002432; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000002432}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000002432}. FT DOMAIN 233 397 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 199 226 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 451 AA; 49171 MW; DD1824B07DC09A12 CRC64; MAQERAFLVG VEFTSRRFKN GPSDRKSEAA SPIPPSAKIA RSAASSAPVA DAHSEVPPED VLDELRELTL SAGAGVVGEM LQRRDRPDSA TLIGSGKLEE LQGAVAASDA DLVIFDHDLS PSQQRNIERA LEARVIDRTQ LILDIFAKHA RTAEGQLQVE LAQLQYLLPR LGGRGIEMSQ LGGGIGTRGP GETQLETDRR KINRRIRHVQ KQLEDVRRIR RQQRARRENV PVAVVALVGY TNAGKSTLFN ALTKAGVYAS SKMFATLDPT LRGVMLPSKR QVLLSDTVGF IRNLPTTLVS AFRATLEEVQ RAALLLHVAD ATSPVALEQQ RQVEDVLGEL EVQDKPQIHV MNKIDLLATS KRAALINSGK VVHVSAKSGL GMEALLHAID EAITEDPVKT ARLKIPQADG KALSLVEAKA RVKKRSYRGS NVHLEVEAPE SVLRKLGEYV V // ID Q1IWT4_DEIGD Unreviewed; 569 AA. AC Q1IWT4; DT 13-JUN-2006, integrated into UniProtKB/TrEMBL. DT 13-JUN-2006, sequence version 1. DT 05-JUL-2017, entry version 79. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Dgeo_2006 {ECO:0000313|EMBL:ABF46300.1}; OS Deinococcus geothermalis (strain DSM 11300). OC Bacteria; Deinococcus-Thermus; Deinococci; Deinococcales; OC Deinococcaceae; Deinococcus. OX NCBI_TaxID=319795 {ECO:0000313|EMBL:ABF46300.1, ECO:0000313|Proteomes:UP000002431}; RN [1] {ECO:0000313|Proteomes:UP000002431} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 11300 {ECO:0000313|Proteomes:UP000002431}; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., RA Pitluck S., Brettin T., Bruce D., Han C., Tapia R., Saunders E., RA Gilna P., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., RA Kim E., Daly M.J., Fredrickson J.K., Makarova K.S., Gaidamakova E.K., RA Zhai M., Richardson P.; RT "Complete sequence of chromosome 1 of Deinococcus geothermalis DSM RT 11300."; RL Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000359; ABF46300.1; -; Genomic_DNA. DR ProteinModelPortal; Q1IWT4; -. DR STRING; 319795.Dgeo_2006; -. DR EnsemblBacteria; ABF46300; ABF46300; Dgeo_2006. DR KEGG; dge:Dgeo_2006; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; EREVIIT; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000002431; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000002431}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Hydrolase {ECO:0000313|EMBL:ABF46300.1}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000002431}. FT DOMAIN 382 551 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 569 AA; 61980 MW; 5D2C164926911BBD CRC64; MHGNTSGLKP AQLKALGNLY RRRIEPGRVG SPELARNLAE LSADIRREIS VLIDRRGRVV SVSVADAKGA ALPDLRRGEQ RLAGFHLLHT HPRGGPLSKG DLSTLFLKRL DAVSVIEVRD EGQPGLVHTA HLTPPGTVGE EEDWRILPPV PSFQIGDFDL GAQVSALEEE IARAAGGREA QKDRERAILV QIDQGEFDAE ERLDELAELA RTAGAEVVHR ELIYRRNLKP GTLVGAGKLE ELTSRAYHLD ADLLIFGQEL GPAQAREIEA ATGLKVLDRT QLILDIFALH AQGVESRLQV ELAQLRYMKP RLLGAGAQLS RIGGSAGSAA GGAIGTRGPG ETKLELDRRR INDRISFLEK QLEDVAVRRE ERRKGRARGG VPVISIVGYT NAGKSTLLNA FTHAAEEPRR VLAENKLFAT LRPTSRQGFL EGIGPVILTD TVGFIRDLPR DLARAFRATL EEIGDADVLL HVVDVASPGA DLRLEAVNRI LEDLGFRELP TVTALNKADA ADPDTLEREI ERTNGIPISA LRNLGLANLK EALADAVASV QRQELAQREA ARERAAEYH // ID Q1LLJ7_CUPMC Unreviewed; 411 AA. AC Q1LLJ7; DT 30-MAY-2006, integrated into UniProtKB/TrEMBL. DT 30-MAY-2006, sequence version 1. DT 07-JUN-2017, entry version 90. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:ABF08979.1}; GN OrderedLocusNames=Rmet_2100 {ECO:0000313|EMBL:ABF08979.1}; OS Cupriavidus metallidurans (strain ATCC 43123 / DSM 2839 / NBRC 102507 OS / CH34) (Ralstonia metallidurans). OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Cupriavidus. OX NCBI_TaxID=266264 {ECO:0000313|EMBL:ABF08979.1, ECO:0000313|Proteomes:UP000002429}; RN [1] {ECO:0000313|EMBL:ABF08979.1, ECO:0000313|Proteomes:UP000002429} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43123 / DSM 2839 / NBRC 102507 / CH34 RC {ECO:0000313|Proteomes:UP000002429}; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., RA Martinez M., Goltsman E., Pitluck S., Schmutz J., Larimer F., Land M., RA Hauser L., Kyrpides N., Kim E., Mergeay M., Benotmane M.A., RA Vallaeys T., Michaux A., Monchy S., Dunn J., McCorkle S., Taghavi S., RA van der Lelie D., Richardson P.; RT "Complete sequence of the chromosome of Ralstonia metallidurans RT CH34."; RL Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000352; ABF08979.1; -; Genomic_DNA. DR RefSeq; WP_011516813.1; NC_007973.1. DR ProteinModelPortal; Q1LLJ7; -. DR STRING; 266264.Rmet_2100; -. DR EnsemblBacteria; ABF08979; ABF08979; Rmet_2100. DR GeneID; 24152499; -. DR KEGG; rme:Rmet_2100; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000002429; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000002429}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000002429}. FT DOMAIN 202 372 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 161 195 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 411 AA; 45331 MW; D086A95D940579D2 CRC64; MQPRATSQTE PTRAILVGVD FGKHDFQESL SELALLTTTA GSVPVHTLTG KRSRPDPALF IGSGKAEELR QAADALDADV VVFNHALSPA QQRNLERFLG RHVIDRTGLI LDIFGQRAQS HVGKVQVELA QVQYQASRLV RAWSHLERQK GGIGMRGGPG ERQLELDRRM LDDRAKRLKS DLARLQRQHH TQRRARARND TLSISLVGYT NAGKSTLFNA LTKARAYAAD QLFATLDTTS RRLFLDGFGN VVLSDTVGFI RDLPTQLVAA FRATLDETVH ADLLLHVVDA SSPVRHEQIE QVNRVLAEID ASDIPQIVVM NKIDAAPELL ELGPRVERDE DGVPTKVFVS ARDGLGLDGL REAIVAMAQW LSSRPEAPAP YDPRLEGLQP AQDGEPWDVD DEPDTRQQGA N // ID Q1LSQ6_BAUCH Unreviewed; 427 AA. AC Q1LSQ6; DT 30-MAY-2006, integrated into UniProtKB/TrEMBL. DT 30-MAY-2006, sequence version 1. DT 30-AUG-2017, entry version 78. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:ABF14317.1}; GN OrderedLocusNames=BCI_0580 {ECO:0000313|EMBL:ABF14317.1}; OS Baumannia cicadellinicola subsp. Homalodisca coagulata. OC Bacteria; Proteobacteria; Gammaproteobacteria; Candidatus Baumannia. OX NCBI_TaxID=374463 {ECO:0000313|EMBL:ABF14317.1, ECO:0000313|Proteomes:UP000002427}; RN [1] {ECO:0000313|EMBL:ABF14317.1, ECO:0000313|Proteomes:UP000002427} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Hc {ECO:0000313|EMBL:ABF14317.1}; RX PubMed=16729848; DOI=10.1371/journal.pbio.0040188; RA Wu D., Daugherty S.C., Van Aken S.E., Pai G.H., Watkins K.L., RA Khouri H., Tallon L.J., Zaborsky J.M., Dunbar H.E., Tran P.L., RA Moran N.A., Eisen J.A.; RT "Metabolic complementarity and genomics of the dual bacterial RT symbiosis of sharpshooters."; RL PLoS Biol. 4:1079-1092(2006). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000238; ABF14317.1; -; Genomic_DNA. DR RefSeq; WP_011520741.1; NC_007984.1. DR ProteinModelPortal; Q1LSQ6; -. DR STRING; 374463.BCI_0580; -. DR EnsemblBacteria; ABF14317; ABF14317; BCI_0580. DR KEGG; bci:BCI_0580; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000002427; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000002427}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000002427}. FT DOMAIN 197 364 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 427 AA; 48645 MW; 57B97A38821BF025 CRC64; MFNCSKFGTQ AILVHIFFTK DHNKADIKEF ETLVLSAGLS VLDIVTCSRK EPNSKYFVGE GKAEEIAEKV KISSASVVIF DHALSPAQER NLECLCQCRV IDRTGLILSI FSQRARTHEG KLQVELAQLR YIATRLVRGW THLERQKGGI SLLRGPGETQ LETDRRLLRN RMNTIKLRLA KVERRREQGR YARASIPTIL LVGYTNAGKS TLFNSITEAS VDVADKLFTT LDPTLKRLNI PTIGNIVLAD TVGFIQHLPH HLVASFKSTL QETQQAKLLL HIVDATDQCI NIKIDAVKKV LVEINANHIS TLLVMNKIDQ LDNFIPRIDR NTDNEPVRVW LSAQNADGIT LLMQALSELL IRKHKIIRYN LRLPPQASRL RSLFYQLQAI EQEWSEQDGS IRLLVKIPIV QWYRLCKREV ELLDYLV // ID Q1N274_9GAMM Unreviewed; 436 AA. AC Q1N274; DT 30-MAY-2006, integrated into UniProtKB/TrEMBL. DT 30-MAY-2006, sequence version 1. DT 30-AUG-2017, entry version 52. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=RED65_15663 {ECO:0000313|EMBL:EAT12290.1}; OS Bermanella marisrubri. OC Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales; OC Bermanella. OX NCBI_TaxID=207949 {ECO:0000313|EMBL:EAT12290.1, ECO:0000313|Proteomes:UP000004263}; RN [1] {ECO:0000313|EMBL:EAT12290.1, ECO:0000313|Proteomes:UP000004263} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=RED65 {ECO:0000313|EMBL:EAT12290.1, RC ECO:0000313|Proteomes:UP000004263}; RA Pinhassi J., Pedros-Alio C., Ferriera S., Johnson J., Kravitz S., RA Halpern A., Remington K., Beeson K., Tran B., Rogers Y.-H., RA Friedman R., Venter J.C.; RL Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EAT12290.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AAQH01000008; EAT12290.1; -; Genomic_DNA. DR RefSeq; WP_007018341.1; NZ_CH724116.1. DR ProteinModelPortal; Q1N274; -. DR STRING; 207949.RED65_15663; -. DR EnsemblBacteria; EAT12290; EAT12290; RED65_15663. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000004263; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000004263}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000004263}. FT DOMAIN 199 366 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 436 AA; 49449 MW; F016982B82AFF1B7 CRC64; MFFDRPDTGE GAVLVHIDFP EGDDKEDPAE FEELVRSAGG APLALITGTR SAPDAKTFIG RGKVEEVSDA IEFCEAELVI FNHQLSPSQE RNLEHALKCR VLDRTGLILD IFAQRARTHE GKLQVELAQL QHQSTRLIRG WTHLERQKGG IGLRGPGETQ LETDRRLLRD RIKLIHKRLA KVQTQREQGR RARKRSSTPS VSLVGYTNAG KSTLFNALTE AKVYAADQLF ATLDPTLRRI PIQGLGEVVL VDTVGFIRHL PHKLVEAFKA TLQETQEADL LLHVIDSADE DRQLNMEQVE IVLDEIEALD RPTLQVFNKI DLLPGQKPRI DRDDQGLPWR VWASAKDSQG LELIRQAIGE LLSQTLFEQT IELTPQESQL RALLYDHGAV LHEEFTENGH MMLDVRIEQD DFQQMLAKVG IPLERFIPQE KEFWQL // ID Q1NDV0_SPHSS Unreviewed; 444 AA. AC Q1NDV0; DT 30-MAY-2006, integrated into UniProtKB/TrEMBL. DT 30-MAY-2006, sequence version 1. DT 07-JUN-2017, entry version 49. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=SKA58_09411 {ECO:0000313|EMBL:EAT09169.1}; OS Sphingomonas sp. (strain SKA58). OC Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales; OC Sphingomonadaceae; Sphingomonas. OX NCBI_TaxID=314266 {ECO:0000313|EMBL:EAT09169.1, ECO:0000313|Proteomes:UP000005395}; RN [1] {ECO:0000313|EMBL:EAT09169.1, ECO:0000313|Proteomes:UP000005395} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SKA58 {ECO:0000313|EMBL:EAT09169.1, RC ECO:0000313|Proteomes:UP000005395}; RA Hagstrom A., Ferriera S., Johnson J., Kravitz S., Halpern A., RA Remington K., Beeson K., Tran B., Rogers Y.-H., Friedman R., RA Venter J.C.; RL Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EAT09169.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AAQG01000005; EAT09169.1; -; Genomic_DNA. DR RefSeq; WP_009821649.1; NZ_CH959306.1. DR ProteinModelPortal; Q1NDV0; -. DR STRING; 314266.SKA58_09411; -. DR EnsemblBacteria; EAT09169; EAT09169; SKA58_09411. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000005395; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0016810; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds; IEA:InterPro. DR CDD; cd01878; HflX; 1. DR Gene3D; 2.30.40.10; -; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR011059; Metal-dep_hydrolase_composite. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 2. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000005395}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000005395}. FT DOMAIN 209 390 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 444 AA; 48932 MW; 34F721E7FC6198D6 CRC64; MAVFNRESQD EVSRGARAVV VHAETRGLER RDSDARLEEA RGLALAIGID VRAAQAFRVR DLKPATLFGS GQVDQIATLA RQEEAELIIV DNSLSPVQQS NLEKACEAKV IDRTGLILEI FGERAATNEG RLQVELAHLD YQAGRLVRSW THLERQRGGF GFLGGPGETQ IEADRRMIRD RMAKIRRELD QVTRTRGLHR ARRQRAPWPV IALVGYTNAG KSTLFNRLTG AEVMAEDLLF ATLDPTMRQI ALPGLDKAIL SDTVGFVSDL PTQLIAAFRA TLEEVLSADL IVHVRDIAHP DSDAQRDDVL DVLGELGVTG EAALERGEGT SEPPPIIEAW NKLDLLDADS MSLVREQAAR REDVVILSAL TGEGMDQLQR MISDHMTRGA KVYTFSIPVA DGASLAWLHE HGEVLRSETG DDMTNVEVRL SDASFARFTK SDFA // ID Q1NSQ7_9DELT Unreviewed; 550 AA. AC Q1NSQ7; DT 30-MAY-2006, integrated into UniProtKB/TrEMBL. DT 30-MAY-2006, sequence version 1. DT 07-JUN-2017, entry version 49. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=MldDRAFT_4661 {ECO:0000313|EMBL:EAT04748.1}; OS delta proteobacterium MLMS-1. OC Bacteria; Proteobacteria; Deltaproteobacteria. OX NCBI_TaxID=262489 {ECO:0000313|EMBL:EAT04748.1, ECO:0000313|Proteomes:UP000005853}; RN [1] {ECO:0000313|EMBL:EAT04748.1, ECO:0000313|Proteomes:UP000005853} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MLMS-1 {ECO:0000313|EMBL:EAT04748.1, RC ECO:0000313|Proteomes:UP000005853}; RG US DOE Joint Genome Institute (JGI-ORNL); RA Larimer F., Land M., Hauser L.; RT "Annotation of the draft genome assembly of delta proteobacterium RT MLMS-1."; RL Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:EAT04748.1, ECO:0000313|Proteomes:UP000005853} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MLMS-1 {ECO:0000313|EMBL:EAT04748.1, RC ECO:0000313|Proteomes:UP000005853}; RG US DOE Joint Genome Institute (JGI-PGF); RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Bruce D., RA Pitluck S., Richardson P.; RT "Sequencing of the draft genome and assembly of delta proteobacterium RT MLMS-1."; RL Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EAT04748.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AAQF01000053; EAT04748.1; -; Genomic_DNA. DR RefSeq; WP_007292669.1; NZ_AAQF01000053.1. DR ProteinModelPortal; Q1NSQ7; -. DR EnsemblBacteria; EAT04748; EAT04748; MldDRAFT_4661. DR PATRIC; fig|262489.9.peg.4355; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000005853; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000005853}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000005853}. FT DOMAIN 383 548 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 550 AA; 61539 MW; DB5A03F1EB221A62 CRC64; MKPAQLKQLE RLGRRRLEPD QIATPELARA LAAISREIGR QVGLIIDRTG QVELVLVGDQ RSIMIPELGG SRSAGGRLRG LRCLHTHLGG EGLTRDDFMD LLFLRLDLMS VLEVDAQGLP GKLHSAHLNP RPAGPESEHA APASAAAAGE QAWIILPPAQ VSRKADQLRE RIAALEAEFG RQRPVKEVDK GRDRAILVSV TTSGRRQAEE SLDELSELAA SAGVMVLERV LQRRDKINPR LIMGKGKLGE IILKALQLNA NLLIFDQELN PSQVRSITDH TEMRVIDRTQ LILDIFARRA RSREGKLQIE MAQLKYMLPR LGTRDDALSR LTGGIGGRGP GETRLEIDRR RIRDRLAKLG ADLQKVSRQR HRRRERRRKK EVPVLSLVGY TNAGKSTLLN SLTGSEIMAE DQLFATLDPT SRRLRFPEEL EVIITDTVGF IRHLPAELLQ AFKATLEELD EADVLIHVVD AANPRWEEHI RVVEQLLREL ELAALPRLTV FNKSDLVADQ QLLAQQVDRH GAVAVSVHQQ ATLPPLLERA RKEVLKSWHT // ID Q1QM91_NITHX Unreviewed; 444 AA. AC Q1QM91; DT 16-MAY-2006, integrated into UniProtKB/TrEMBL. DT 16-MAY-2006, sequence version 1. DT 07-JUN-2017, entry version 81. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Nham_1842 {ECO:0000313|EMBL:ABE62656.1}; OS Nitrobacter hamburgensis (strain DSM 10229 / NCIMB 13809 / X14). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Bradyrhizobiaceae; Nitrobacter. OX NCBI_TaxID=323097 {ECO:0000313|EMBL:ABE62656.1, ECO:0000313|Proteomes:UP000001953}; RN [1] {ECO:0000313|EMBL:ABE62656.1, ECO:0000313|Proteomes:UP000001953} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 10229 / NCIMB 13809 / X14 RC {ECO:0000313|Proteomes:UP000001953}; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., RA Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., RA Larimer F., Land M., Hauser L., Kyrpides N., Ivanova N., Ward B., RA Arp D., Klotz M., Stein L., O'Mullan G., Starkenburg S., Sayavedra L., RA Poret-Peterson A.T., Gentry M.E., Bruce D., Richardson P.; RT "Complete sequence of chromosome of Nitrobacter hamburgensis X14."; RL Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000319; ABE62656.1; -; Genomic_DNA. DR ProteinModelPortal; Q1QM91; -. DR STRING; 323097.Nham_1842; -. DR EnsemblBacteria; ABE62656; ABE62656; Nham_1842. DR KEGG; nha:Nham_1842; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000001953; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000001953}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Hydrolase {ECO:0000313|EMBL:ABE62656.1}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000001953}. FT DOMAIN 211 385 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 444 AA; 49179 MW; 95A455EBDC408906 CRC64; MQGKPTGRAI VIGPYLRLRR GNADTPQVGH AMRDTDARLD EAAGLARAID LDVAKAIAAQ VTQIRPATYL GKGKVEELTG LITTEGADLV VMDCALSPIQ QRNLEKAWST KVLDRTGLIL EIFGRRAKTK EGALQVELAH LNYQRSRLVR SWTHLERQRG GFGFMGGPGE TQIEADRRLI GDRIVRLENE LKKVQATRRL HRAGRQRVPY RVVALVGYTN AGKSTLFNRL TRAEVQAADM LFATLDPTLR ALALPHGGKA MLSDTVGFIS NLPTQLVAAF RATLEEVMEA DVILHVRDIS HEDAEAQQHD VEAVLRQLGI DPGHGARILE VWNKIDRFDA DQRENLENIA VRRSAEVPCF LVSAETGEGL DTLLAAIEDR LAATRTTLDL SVDASDGAAI SWLHRNSEVL VKELRDGRYE MTVRVDETKR DILVNRYAAI PHPL // ID Q1QY25_CHRSD Unreviewed; 439 AA. AC Q1QY25; DT 16-MAY-2006, integrated into UniProtKB/TrEMBL. DT 16-MAY-2006, sequence version 1. DT 30-AUG-2017, entry version 82. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Csal_1278 {ECO:0000313|EMBL:ABE58633.1}; OS Chromohalobacter salexigens (strain DSM 3043 / ATCC BAA-138 / NCIMB OS 13768). OC Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales; OC Halomonadaceae; Chromohalobacter. OX NCBI_TaxID=290398 {ECO:0000313|EMBL:ABE58633.1, ECO:0000313|Proteomes:UP000000239}; RN [1] {ECO:0000313|EMBL:ABE58633.1, ECO:0000313|Proteomes:UP000000239} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 3043 / ATCC BAA-138 / NCIMB 13768 RC {ECO:0000313|Proteomes:UP000000239}; RX PubMed=22675587; DOI=10.4056/sigs.2285059; RA Copeland A., O'Connor K., Lucas S., Lapidus A., Berry K.W., RA Detter J.C., Del Rio T.G., Hammon N., Dalin E., Tice H., Pitluck S., RA Bruce D., Goodwin L., Han C., Tapia R., Saunders E., Schmutz J., RA Brettin T., Larimer F., Land M., Hauser L., Vargas C., Nieto J.J., RA Kyrpides N.C., Ivanova N., Goker M., Klenk H.P., Csonka L.N., RA Woyke T.; RT "Complete genome sequence of the halophilic and highly halotolerant RT Chromohalobacter salexigens type strain (1H11(T))."; RL Stand. Genomic Sci. 5:379-388(2011). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000285; ABE58633.1; -; Genomic_DNA. DR RefSeq; WP_011506579.1; NC_007963.1. DR ProteinModelPortal; Q1QY25; -. DR STRING; 290398.Csal_1278; -. DR EnsemblBacteria; ABE58633; ABE58633; Csal_1278. DR KEGG; csa:Csal_1278; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000000239; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000000239}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Hydrolase {ECO:0000313|EMBL:ABE58633.1}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000000239}. FT DOMAIN 199 365 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 439 AA; 49473 MW; 9A94449CE79C8D82 CRC64; MFFERPDAGE TAVLVHVDFH DEQEREDPGE FLELVRSSGV TPATLVEGSR RRPDPKTFIG SGKLEEIREI RELHGADIVI FNHALSPSQE RNLERALKSR VLDRTGLILD IFAQRARTHE GKLQVELAQL EYMSTRLVRG WTHLERQKGG IGLRGPGETQ LETDRRLLGA RIKAIHKRLE KVRTQRDQNR RARARAEIPS VSLVGYTNAG KSTLFNALTE SEVYAADQLF ATLDPTLRRL NVADVGPVVL ADTVGFIRHL PHKLVESFRA TLQEAAEASL LVHVIDAADP DRDFNVAQVD TVLEEIGAGD VPQLLVMNKI DLLGTAPRLE RDEHGRPRIV WLSAREARGF ELLQEALGEL LAEDLLETGL TLAPEQGRLR AALHELNAVQ QEQFDEQGRI LLDIRLPRRD FFQVMARLGE NAEHYLPPGA LDRPEWERP // ID Q1WS88_LACS1 Unreviewed; 419 AA. AC Q1WS88; DT 02-MAY-2006, integrated into UniProtKB/TrEMBL. DT 02-MAY-2006, sequence version 1. DT 07-JUN-2017, entry version 78. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:ABE00241.1}; GN OrderedLocusNames=LSL_1437 {ECO:0000313|EMBL:ABE00241.1}; OS Lactobacillus salivarius (strain UCC118). OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; OC Lactobacillus. OX NCBI_TaxID=362948 {ECO:0000313|EMBL:ABE00241.1, ECO:0000313|Proteomes:UP000006559}; RN [1] {ECO:0000313|EMBL:ABE00241.1, ECO:0000313|Proteomes:UP000006559} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=UCC118 {ECO:0000313|EMBL:ABE00241.1, RC ECO:0000313|Proteomes:UP000006559}; RX PubMed=16617113; DOI=10.1073/pnas.0511060103; RA Claesson M.J., Li Y., Leahy S., Canchaya C., van Pijkeren J.P., RA Cerdeno-Tarraga A.M., Parkhill J., Flynn S., O'Sullivan G.C., RA Collins J.K., Higgins D., Shanahan F., Fitzgerald G.F., RA van Sinderen D., O'Toole P.W.; RT "Multireplicon genome architecture of Lactobacillus salivarius."; RL Proc. Natl. Acad. Sci. U.S.A. 103:6718-6723(2006). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000233; ABE00241.1; -; Genomic_DNA. DR RefSeq; WP_004563879.1; NC_007929.1. DR RefSeq; YP_536324.1; NC_007929.1. DR ProteinModelPortal; Q1WS88; -. DR STRING; 362948.LSL_1437; -. DR EnsemblBacteria; ABE00241; ABE00241; LSL_1437. DR GeneID; 3977699; -. DR KEGG; lsl:LSL_1437; -. DR PATRIC; fig|362948.14.peg.1520; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; FNNHAHV; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000006559; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000006559}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000006559}. FT DOMAIN 197 365 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 156 190 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 419 AA; 47388 MW; 0A5B5AD5FF3FFC60 CRC64; MIPVIIAGLE NDYENFEYKM DELSSLAYAN NMEVIVSVKQ KLEHPIAATY FGKGKAEEIR HVGEINDIDT LIVNAELTPT QLRNLEDITG LQVIDRTALI LEIFASRAQT KEAKLQVQIA KLQYQLPRLR TSSINRMDQQ TAGNTGGGYT NRGSGETKLE LNKRVIEKRI SNLSKELKEI ESVHENQRRA RERSSIKTVA LVGYTNAGKS TTMNGLLKLL EQPTNKEVFE KDMLFATLDT SIRKIKLPDN KEFFLSDTVG FVSDLPHQLV KAFRTTLSEA NQADLLIQVI DGSDEHAKDM IETTKQTLDE IGVKDIPMIY AYNKSDLTST PYPSSVGNQF YYSAKDKKSI EMLINLIKEN LFQDYVTHTY LIPFSEGRYL EIINKQANIL KTDYLAEGTK ITAESTPIMA QQLKQFIID // ID Q1YHZ9_AURMS Unreviewed; 406 AA. AC Q1YHZ9; DT 02-MAY-2006, integrated into UniProtKB/TrEMBL. DT 02-MAY-2006, sequence version 1. DT 07-JUN-2017, entry version 53. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=SI859A1_01685 {ECO:0000313|EMBL:EAS50318.1}; OS Aurantimonas manganoxydans (strain ATCC BAA-1229 / DSM 21871 / OS SI85-9A1). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Aurantimonadaceae; Aurantimonas. OX NCBI_TaxID=287752 {ECO:0000313|EMBL:EAS50318.1, ECO:0000313|Proteomes:UP000000321}; RN [1] {ECO:0000313|EMBL:EAS50318.1, ECO:0000313|Proteomes:UP000000321} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SI85-9A1 {ECO:0000313|EMBL:EAS50318.1, RC ECO:0000313|Proteomes:UP000000321}; RX PubMed=18344346; DOI=10.1128/AEM.01656-07; RA Dick G.J., Podell S., Johnson H.A., Rivera-Espinoza Y., RA Bernier-Latmani R., McCarthy J.K., Torpey J.W., Clement B.G., RA Gaasterland T., Tebo B.M.; RT "Genomic insights into Mn(II) oxidation by the marine RT alphaproteobacterium Aurantimonas sp. strain SI85-9A1."; RL Appl. Environ. Microbiol. 74:2646-2658(2008). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EAS50318.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AAPJ01000003; EAS50318.1; -; Genomic_DNA. DR ProteinModelPortal; Q1YHZ9; -. DR STRING; 287752.SI859A1_01685; -. DR EnsemblBacteria; EAS50318; EAS50318; SI859A1_01685. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR OrthoDB; POG091H0464; -. DR BioCyc; AURANTIMONAS:SI859A1_01685-MONOMER; -. DR Proteomes; UP000000321; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000000321}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000000321}. FT DOMAIN 169 343 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 128 162 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 406 AA; 44860 MW; C628B358A4F95CE0 CRC64; MGLAAAIGLD IVASGVVSGQ RPRPATLIGT GKVEEMKGVI AGEEIGLVVF DHPLTPVQQR NLERELNVKV LDRTGLILEI FGERARTKEG RLQVELAHLN YQRGRLVRSW THLERQRGGA GFLGGPGETQ IESDRRQLQE KIKRLEKDLE QVRRTRQLHR AQRKKAPHPV VALVGYTNAG KSTLFNRLTG AEVMAKDLLF ATLDPTLRRT TLPHGTEILF SDTVGFVSDL PTHLVAAFRA TLEEVIEADI VLHVRDVADP DTLAQAEDVR KILRDLDIDV DDSDHVVEIW NKVDLLDEAG LQHLATMRES LPDTDAVHVV SAVTGFGVDT LLVDIERRIG GGTVTLTVDV APDAMGFVPW IYENATVTAR DDREDGAVSL TMDITKQART ELRRMSEHAS GVSFQR // ID Q1YRY6_9GAMM Unreviewed; 431 AA. AC Q1YRY6; DT 02-MAY-2006, integrated into UniProtKB/TrEMBL. DT 02-MAY-2006, sequence version 1. DT 30-AUG-2017, entry version 64. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=GB2207_04752 {ECO:0000313|EMBL:EAS46909.1}; OS gamma proteobacterium HTCC2207. OC Bacteria; Proteobacteria; Gammaproteobacteria; Cellvibrionales; OC Porticoccaceae; SAR92 clade. OX NCBI_TaxID=314287 {ECO:0000313|EMBL:EAS46909.1, ECO:0000313|Proteomes:UP000005555}; RN [1] {ECO:0000313|EMBL:EAS46909.1, ECO:0000313|Proteomes:UP000005555} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=HTCC2207 {ECO:0000313|EMBL:EAS46909.1, RC ECO:0000313|Proteomes:UP000005555}; RA Giovannoni S.J., Cho J.-C., Ferriera S., Johnson J., Kravitz S., RA Halpern A., Remington K., Beeson K., Tran B., Rogers Y.-H., RA Friedman R., Venter J.C.; RL Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EAS46909.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AAPI01000004; EAS46909.1; -; Genomic_DNA. DR RefSeq; WP_007232436.1; NZ_CH672398.1. DR ProteinModelPortal; Q1YRY6; -. DR STRING; 314287.GB2207_04752; -. DR EnsemblBacteria; EAS46909; EAS46909; GB2207_04752. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000005555; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000005555}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000005555}. FT DOMAIN 201 368 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 431 AA; 48148 MW; 9780D0C1670987BA CRC64; MTLFFERPEF GERAVLVTLK LQSESEPEDP REFEELVLSA GGDPVEVITG SRSAPHAKLF VGTGKLEEIA AAVNSHCAEL VIFNHNLSPS QERNIEAELK CRVLDRTGLI LDIFAQRART HEGKLQVELA QLQHLSTRLV RGWTHLERQR GGIGMRGPGE TQLESDRRMV RDRIKSIQSR LLKVRKQRAQ GRRARVRAEV PAVSLVGYTN AGKSTLFNNL TQADVFVANQ LFATLDPTMR KLEVPEQGEV VFADTVGFIS HLPHRLVDAF RATLEEAANA TLLLHVVDGA AEDRATNIKR VEEVLKEIDA HKLPTLMVYN KVDLLEDFSA RIDRNAEGQP VAVWLSALKN EGLDLLLQAV AERLPGQFVH KTLRLKPDQG ALRASLYSHK AVLDEQVDEN GWINVEIKLS EIDFLRLIKS SGLNVDDLVT V // ID Q1YXJ9_9GAMM Unreviewed; 429 AA. AC Q1YXJ9; DT 02-MAY-2006, integrated into UniProtKB/TrEMBL. DT 02-MAY-2006, sequence version 1. DT 30-AUG-2017, entry version 60. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=P3TCK_13064 {ECO:0000313|EMBL:EAS41038.1}; OS Photobacterium profundum 3TCK. OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; OC Vibrionaceae; Photobacterium. OX NCBI_TaxID=314280 {ECO:0000313|EMBL:EAS41038.1, ECO:0000313|Proteomes:UP000003789}; RN [1] {ECO:0000313|EMBL:EAS41038.1, ECO:0000313|Proteomes:UP000003789} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=3TCK {ECO:0000313|EMBL:EAS41038.1, RC ECO:0000313|Proteomes:UP000003789}; RA Bartlett D.H., Valle G., Lauro F.M., Vezzi A., Simonato F., Eloe E., RA Vitulo N., Stratton T.K., D'angelo M., Ferriera S., Johnson J., RA Kravitz S., Beeson K., Sutton G., Rogers Y., Friedman R., Frazier M., RA Venter J.C.; RL Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EAS41038.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AAPH01000042; EAS41038.1; -; Genomic_DNA. DR RefSeq; WP_006233810.1; NZ_CH724139.1. DR ProteinModelPortal; Q1YXJ9; -. DR EnsemblBacteria; EAS41038; EAS41038; P3TCK_13064. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000003789; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000003789}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}. FT DOMAIN 198 365 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 429 AA; 48463 MW; 287F6772F0135418 CRC64; MFDRYEAGEQ AILVHINFTQ DGEWEDLSEC EMLVSSAGVN TLRVVTGSRK TPLPKYYVGE GKAQEIADAV RAEEAEIVIF NHSLSPAQER NLEQLCQCRV IDRTGLILDI FAQRARTHEG KLQVELAQLR HISTRLIRGW THLERQKGGI GLRGPGETQL ETDRRLLRDR IKTILRRLDK VSKQREQGRR ARNRAEIPTI SLVGYTNAGK STLFNRITDA GVYAADQLFA TLDPTLRKID VADVGTSILA DTVGFIRHLP HDLVAAFKAT LKETQEATLL LHVVDASDER FRENMDAVHL VLDEIDAGDV PRLIVMNKID CLEGAEPRIE RDEDGLPRCV WVSAMEGIGI DLLFQALTER LSGTMVKHTL RLPPENAGRY RSKFYQLGCI LREEYESDGC LMVDIRLPLA DWSRLQKKES NLLDDFIVA // ID Q1Z6E3_9GAMM Unreviewed; 445 AA. AC Q1Z6E3; DT 02-MAY-2006, integrated into UniProtKB/TrEMBL. DT 02-MAY-2006, sequence version 1. DT 07-JUN-2017, entry version 55. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=P3TCK_10993 {ECO:0000313|EMBL:EAS44204.1}; OS Photobacterium profundum 3TCK. OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; OC Vibrionaceae; Photobacterium. OX NCBI_TaxID=314280 {ECO:0000313|EMBL:EAS44204.1, ECO:0000313|Proteomes:UP000003789}; RN [1] {ECO:0000313|EMBL:EAS44204.1, ECO:0000313|Proteomes:UP000003789} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=3TCK {ECO:0000313|EMBL:EAS44204.1, RC ECO:0000313|Proteomes:UP000003789}; RA Bartlett D.H., Valle G., Lauro F.M., Vezzi A., Simonato F., Eloe E., RA Vitulo N., Stratton T.K., D'angelo M., Ferriera S., Johnson J., RA Kravitz S., Beeson K., Sutton G., Rogers Y., Friedman R., Frazier M., RA Venter J.C.; RL Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EAS44204.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AAPH01000006; EAS44204.1; -; Genomic_DNA. DR RefSeq; WP_006230222.1; NZ_CH724134.1. DR ProteinModelPortal; Q1Z6E3; -. DR EnsemblBacteria; EAS44204; EAS44204; P3TCK_10993. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000003789; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000003789}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}. FT DOMAIN 225 357 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 186 220 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 445 AA; 49411 MW; 3513659FBA43BE54 CRC64; MKLTEKASLT NALLISICTP QFKGDEAKDS LAELARLVTT LGFKVVGTQS QKQSSTQRVN VLGAGKLAEI AHLTGNQGSV DDADTEDFFD EIEFEDIPSE NLPFACADVV VFDCDLSPSQ LRNVENQLGV QVYDRTGIII EIFSRHARTR TARLQVEMAR LNYVAPRLRE STVGDNERQM GKGAGETNLE LDRRKVRDQL AELKRELASV QDEMKGRRTQ RSELFCVALV GYTNAGKSSM MRAITGSEVL VEDKLFATLD TTVRALYPIT QPRILVSDTV GFIKKLPHDL VASFHSTLAE AHDASLLLYV VDASDSSFRT QLDVVHEVLE EVGVEGAKKL LVLNKSDQLS TEQQQALMEE FPDAMMTSTR NPLDIAKLHK YIVGVSEHGM IEDEIIVPYT AKGIIGEIRS SMSVTKEEYE YSHIKLTVRS NAIDLARLKK LMLNS // ID Q1ZKC8_PHOAS Unreviewed; 429 AA. AC Q1ZKC8; DT 02-MAY-2006, integrated into UniProtKB/TrEMBL. DT 02-MAY-2006, sequence version 1. DT 30-AUG-2017, entry version 72. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=VAS14_18829 {ECO:0000313|EMBL:EAS62681.1}; OS Photobacterium angustum (strain S14 / CCUG 15956) (Vibrio sp. (strain OS S14 / CCUG 15956)). OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; OC Vibrionaceae; Photobacterium. OX NCBI_TaxID=314292 {ECO:0000313|EMBL:EAS62681.1, ECO:0000313|Proteomes:UP000001603}; RN [1] {ECO:0000313|EMBL:EAS62681.1, ECO:0000313|Proteomes:UP000001603} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=S14 {ECO:0000313|EMBL:EAS62681.1, RC ECO:0000313|Proteomes:UP000001603}; RX PubMed=19805210; DOI=10.1073/pnas.0903507106; RA Lauro F.M., McDougald D., Thomas T., Williams T.J., Egan S., Rice S., RA DeMaere M.Z., Ting L., Ertan H., Johnson J., Ferriera S., Lapidus A., RA Anderson I., Kyrpides N., Munk A.C., Detter C., Han C.S., Brown M.V., RA Robb F.T., Kjelleberg S., Cavicchioli R.; RT "The genomic basis of trophic strategy in marine bacteria."; RL Proc. Natl. Acad. Sci. U.S.A. 106:15527-15533(2009). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EAS62681.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AAOJ01000016; EAS62681.1; -; Genomic_DNA. DR RefSeq; WP_005372817.1; NZ_CH902604.1. DR ProteinModelPortal; Q1ZKC8; -. DR STRING; 314292.VAS14_18829; -. DR EnsemblBacteria; EAS62681; EAS62681; VAS14_18829. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000001603; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000001603}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000001603}. FT DOMAIN 198 365 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 429 AA; 48489 MW; 9EABF8F337F7E00A CRC64; MFDRYEAGEQ AILVHINFTQ DGEWEDLSEF EMLVSSAGVN TLHVVTGSRK TPHPKYYVGE GKAQEIADAV RTAEADIVIF NHSLSPAQER NLEQICQCRV LDRTGLILDI FAQRARTHEG KLQVELAQLR HISTRLIRGW THLERQKGGI GLRGPGETQL ETDRRLLRDR IKTILRRLDK VAKQRDQGRR ARNRAEIPTI SLVGYTNAGK STLFNRITDA GVYAADQLFA TLDPTLRKIA VADVGTAILA DTVGFIRHLP HDLVAAFKAT LKETQEADLL LHVVDASDDR FRENIEAVET VLEEIDAGEV PTLIIMNKID NLEHAEPRIE RDEEGVPRRV WVSAMEGQGI DLLFQALTER LSGTMVAHTL RVPPEMIGRI RSKFYQLGCI LQEEYESDGY LMIDIRLPLA EWSRLQKRES TSLDDFIVA // ID Q20446_CAEEL Unreviewed; 468 AA. AC Q20446; DT 01-NOV-1996, integrated into UniProtKB/TrEMBL. DT 01-NOV-1996, sequence version 1. DT 30-AUG-2017, entry version 111. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:CAA94821.1}; GN ORFNames=CELE_F46B6.4 {ECO:0000313|EMBL:CAA94821.1}, GN F46B6.4 {ECO:0000313|EMBL:CAA94821.1, ECO:0000313|WormBase:F46B6.4}; OS Caenorhabditis elegans. OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida; OC Rhabditoidea; Rhabditidae; Peloderinae; Caenorhabditis. OX NCBI_TaxID=6239 {ECO:0000313|EMBL:CAA94821.1, ECO:0000313|Proteomes:UP000001940}; RN [1] {ECO:0000313|EMBL:CAA94821.1, ECO:0000313|Proteomes:UP000001940} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Bristol N2 {ECO:0000313|EMBL:CAA94821.1, RC ECO:0000313|Proteomes:UP000001940}; RX PubMed=9851916; DOI=https://doi.org/10.1126/science.282.5396.2012; RG The C. elegans sequencing consortium; RA Sulson J.E., Waterston R.; RT "Genome sequence of the nematode C. elegans: a platform for RT investigating biology."; RL Science 282:2012-2018(1998). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BX284605; CAA94821.1; -; Genomic_DNA. DR PIR; T22287; T22287. DR RefSeq; NP_505523.1; NM_073122.1. DR UniGene; Cel.3551; -. DR ProteinModelPortal; Q20446; -. DR SMR; Q20446; -. DR STRING; 6239.F46B6.4; -. DR EPD; Q20446; -. DR PaxDb; Q20446; -. DR PeptideAtlas; Q20446; -. DR EnsemblMetazoa; F46B6.4; F46B6.4; WBGene00009769. DR GeneID; 179372; -. DR KEGG; cel:CELE_F46B6.4; -. DR UCSC; F46B6.4; c. elegans. DR CTD; 179372; -. DR WormBase; F46B6.4; CE05870; WBGene00009769; -. DR eggNOG; KOG0410; Eukaryota. DR eggNOG; COG2262; LUCA. DR GeneTree; ENSGT00390000001397; -. DR InParanoid; Q20446; -. DR OMA; MDTVGFM; -. DR OrthoDB; EOG091G0852; -. DR PhylomeDB; Q20446; -. DR Proteomes; UP000001940; Chromosome V. DR Bgee; WBGene00009769; -. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR CDD; cd01878; HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 1: Evidence at protein level; KW Complete proteome {ECO:0000313|Proteomes:UP000001940}; KW Proteomics identification {ECO:0000213|EPD:Q20446, KW ECO:0000213|PeptideAtlas:Q20446}; KW Reference proteome {ECO:0000313|Proteomes:UP000001940}. FT DOMAIN 235 401 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 468 AA; 52418 MW; C58CA3DFDF239465 CRC64; MFILRLSRQT VLSFRNLSIG SSEVAAPSAF ANDRWSVLVV HPKVRWGSGS ASVLKQADRQ LEEAVALVDN LPNMNAVDSL IMPVDYNTKR KAVWASGNLE KLIARREAAR ATALMVNVDA LSPSQQQELY RIFEVPIFDR YNIVLATFKQ FAKTEEARIQ IAIAEIPYIK HRIHALSSKR LHSRPDILHI DSHYSDIDGD LNEILRKREQ DLRKELKDVT RKNVGQLGVR NSSDAVVAVV GYTNSGKTSL VKKLTGAASL TPKDQLFATL DTTRHLAKLP SGRSAVFTDT IGFLSDLPMH LIAAFEATLA HVKSADVIIH LRDISNPDWK AQEEDVLATL KSIGVTDYVL NERIISVDNK IDKESAFPTS ESNNSVRISC KTGDGMHELI DVINDKVTMV TKCKTIRLRL DARSPVIEWL YHNELVVIEP TIDGNYLIFD VVMNESEIGR FRKKFAHLKK KNSQSVSL // ID Q214Q3_RHOPB Unreviewed; 461 AA. AC Q214Q3; DT 18-APR-2006, integrated into UniProtKB/TrEMBL. DT 18-APR-2006, sequence version 1. DT 07-JUN-2017, entry version 77. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=RPC_2583 {ECO:0000313|EMBL:ABD88133.1}; OS Rhodopseudomonas palustris (strain BisB18). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Bradyrhizobiaceae; Rhodopseudomonas. OX NCBI_TaxID=316056 {ECO:0000313|EMBL:ABD88133.1, ECO:0000313|Proteomes:UP000001948}; RN [1] {ECO:0000313|EMBL:ABD88133.1, ECO:0000313|Proteomes:UP000001948} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BisB18 {ECO:0000313|EMBL:ABD88133.1, RC ECO:0000313|Proteomes:UP000001948}; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., RA Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., RA Larimer F., Land M., Hauser L., Pelletier D.A., Kyrpides N., RA Anderson I., Oda Y., Harwood C.S., Richardson P.; RT "Complete sequence of Rhodopseudomonas palustris BisB18."; RL Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000301; ABD88133.1; -; Genomic_DNA. DR RefSeq; WP_011473029.1; NC_007925.1. DR ProteinModelPortal; Q214Q3; -. DR STRING; 316056.RPC_2583; -. DR EnsemblBacteria; ABD88133; ABD88133; RPC_2583. DR KEGG; rpc:RPC_2583; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000001948; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000001948}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000001948}. FT DOMAIN 226 402 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 461 AA; 50502 MW; 89EFA1E2A80DE939 CRC64; MEPRSFEGDA DRPRPSGNQP TGRAVVIGPY LRARRGDPDP QAEIHAQRSS QARLEEAAGL ALAIDLTVAE AILAPIGQIR PATYLGKGKV EEILGAIKAH EADLVVMDCA LSPIQQRNLE KAWSAKVLDR TGLILEIFGR RAKTKEGALQ VELAHLNYQR SRLVRSWTHL ERQRGGFGFM GGPGETQIEA DRRLIGDRIS KIENEIKKVQ GTRRLHRAGR QRVPYRVVAL VGYTNAGKST LFNRLTRAEV QAADMLFATL DPTLRALTLP HGGKAMLSDT VGFISNLPTQ LVAAFRATLE EVLEADLILH VRDIAHEDAD AQQDDVAAVL RQLGIDPEAG GGGRIIEVWN KIDRFAADEL ANLRNIAARR DPEHPCLLVS AVTGEGIDAL LLAIEDRLAA ARITLDLSID AADGAGVSWL HRNAEVLEKE LEDGRFVMTV RVDPTKRDTV ISRFGAVQHP E // ID Q21HA3_SACD2 Unreviewed; 441 AA. AC Q21HA3; DT 18-APR-2006, integrated into UniProtKB/TrEMBL. DT 18-APR-2006, sequence version 1. DT 30-AUG-2017, entry version 87. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Sde_2666 {ECO:0000313|EMBL:ABD81926.1}; OS Saccharophagus degradans (strain 2-40 / ATCC 43961 / DSM 17024). OC Bacteria; Proteobacteria; Gammaproteobacteria; Cellvibrionales; OC Cellvibrionaceae; Saccharophagus. OX NCBI_TaxID=203122 {ECO:0000313|EMBL:ABD81926.1, ECO:0000313|Proteomes:UP000001947}; RN [1] {ECO:0000313|EMBL:ABD81926.1, ECO:0000313|Proteomes:UP000001947} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=2-40 / ATCC 43961 / DSM 17024 RC {ECO:0000313|Proteomes:UP000001947}; RX PubMed=18516288; DOI=10.1371/journal.pgen.1000087; RA Weiner R.M., Taylor L.E.II., Henrissat B., Hauser L., Land M., RA Coutinho P.M., Rancurel C., Saunders E.H., Longmire A.G., Zhang H., RA Bayer E.A., Gilbert H.J., Larimer F., Zhulin I.B., Ekborg N.A., RA Lamed R., Richardson P.M., Borovok I., Hutcheson S.; RT "Complete genome sequence of the complex carbohydrate-degrading marine RT bacterium, Saccharophagus degradans strain 2-40 T."; RL PLoS Genet. 4:E1000087-E1000087(2008). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000282; ABD81926.1; -; Genomic_DNA. DR RefSeq; WP_011469143.1; NC_007912.1. DR ProteinModelPortal; Q21HA3; -. DR STRING; 203122.Sde_2666; -. DR EnsemblBacteria; ABD81926; ABD81926; Sde_2666. DR KEGG; sde:Sde_2666; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000001947; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000001947}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000001947}. FT DOMAIN 199 366 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 441 AA; 48890 MW; 2A23BC6C85278B17 CRC64; MFFDRPESGE LAVLVHLEIS QAEQSEDPRE FEELVLSAGG DPVDFLTGSR STPSSKYFVG TGKLEELQAM VKQHNAELVI FNHQLTPSQE RNIEHALGCR VLDRTGLILD IFAQRARTHE GKLQVELAQL QHMSTRLIRG WTHLERQKGG IGMRGPGETQ LETDRRLLRA RIKSIHKRLD RVRKQREQGR RARNRAEIPT LSLVGYTNAG KSTLFNAITD AGVYAEDKLF ATLDPTMRRI GLRDVGPAIL ADTVGFISNL PHRLVEAFRA TLEEAASADI LLHVVDAADD ERARNIEQVK LVLNEIGAGD LPVLMVHNKI DLLSNVDARI DRDDLGKPVA VWLSAQSGAG IEQLMEAITE LLSDNIVHQK VLLPASMGSL RARLYRQNAV VGESHQSDGT CVIEIRLPEA DLHRMLSAES LTINDLCWAQ DDDQASSVVA G // ID Q21W34_RHOFT Unreviewed; 382 AA. AC Q21W34; DT 18-APR-2006, integrated into UniProtKB/TrEMBL. DT 18-APR-2006, sequence version 1. DT 07-JUN-2017, entry version 88. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Rfer_2301 {ECO:0000313|EMBL:ABD70019.1}; OS Rhodoferax ferrireducens (strain ATCC BAA-621 / DSM 15236 / T118) OS (Albidiferax ferrireducens). OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Comamonadaceae; Rhodoferax. OX NCBI_TaxID=338969 {ECO:0000313|EMBL:ABD70019.1, ECO:0000313|Proteomes:UP000008332}; RN [1] {ECO:0000313|Proteomes:UP000008332} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-621 / DSM 15236 / T118 RC {ECO:0000313|Proteomes:UP000008332}; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Hammon N., Israni S., Pitluck S., Brettin T., RA Bruce D., Han C., Tapia R., Gilna P., Kiss H., Schmutz J., Larimer F., RA Land M., Kyrpides N., Ivanova N., Richardson P.; RT "Complete sequence of chromosome of Rhodoferax ferrireducens DSM RT 15236."; RL Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000267; ABD70019.1; -; Genomic_DNA. DR RefSeq; WP_011464587.1; NC_007908.1. DR ProteinModelPortal; Q21W34; -. DR STRING; 338969.Rfer_2301; -. DR EnsemblBacteria; ABD70019; ABD70019; Rfer_2301. DR KEGG; rfr:Rfer_2301; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000008332; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000008332}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000008332}. FT DOMAIN 202 375 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 382 AA; 42060 MW; 896657647CA2C5EB CRC64; MTNLQPPDRQ SAPTLLVGVD FGYPNFDGEL AELGLLAQTA GLNPVARITC KRKAPDAALF VGSGKADEIK LLATQSGAVE VLFDQSLSPA QQRNLERHLE LPVNDRTLLI LEIFGQRARS HEGKLQVELA RLQYLSTRLV RRWSHLERQS GGIGMRGGPG ESQIELDRRM IGDNIKKIKE RLLKVKKQRQ TQRRQRERRD AFNISLVGYT NAGKSTLFNA LVKARTYTAD QLFATLDTTT RQLYLGEAGR SISLSDTVGF IRDLPHGLID AFQATLQEAV DADLLLHVVD AASPQFLEQI AEVQRVLGEI GAADIPQILV FNKLDVIDPA QHPLQLEDVF DLNGVPTPRV FLSAKNGEGV AALRQQLARR VSGDVLPDTG AA // ID Q23G59_TETTS Unreviewed; 750 AA. AC Q23G59; DT 18-APR-2006, integrated into UniProtKB/TrEMBL. DT 16-APR-2014, sequence version 2. DT 05-JUL-2017, entry version 66. DE SubName: Full=Small GTP-binding domain protein {ECO:0000313|EMBL:EAR95401.2}; GN ORFNames=TTHERM_00077050 {ECO:0000313|EMBL:EAR95401.2}; OS Tetrahymena thermophila (strain SB210). OC Eukaryota; Alveolata; Ciliophora; Intramacronucleata; OC Oligohymenophorea; Hymenostomatida; Tetrahymenina; Tetrahymenidae; OC Tetrahymena. OX NCBI_TaxID=312017 {ECO:0000313|EMBL:EAR95401.2, ECO:0000313|Proteomes:UP000009168}; RN [1] {ECO:0000313|Proteomes:UP000009168} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SB210 {ECO:0000313|Proteomes:UP000009168}; RX PubMed=16933976; DOI=10.1371/journal.pbio.0040286; RA Eisen J.A., Coyne R.S., Wu M., Wu D., Thiagarajan M., Wortman J.R., RA Badger J.H., Ren Q., Amedeo P., Jones K.M., Tallon L.J., Delcher A.L., RA Salzberg S.L., Silva J.C., Haas B.J., Majoros W.H., Farzad M., RA Carlton J.M., Smith R.K. Jr., Garg J., Pearlman R.E., Karrer K.M., RA Sun L., Manning G., Elde N.C., Turkewitz A.P., Asai D.J., Wilkes D.E., RA Wang Y., Cai H., Collins K., Stewart B.A., Lee S.R., Wilamowska K., RA Weinberg Z., Ruzzo W.L., Wloga D., Gaertig J., Frankel J., Tsao C.-C., RA Gorovsky M.A., Keeling P.J., Waller R.F., Patron N.J., Cherry J.M., RA Stover N.A., Krieger C.J., del Toro C., Ryder H.F., Williamson S.C., RA Barbeau R.A., Hamilton E.P., Orias E.; RT "Macronuclear genome sequence of the ciliate Tetrahymena thermophila, RT a model eukaryote."; RL PLoS Biol. 4:1620-1642(2006). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; GG662704; EAR95401.2; -; Genomic_DNA. DR RefSeq; XP_001015646.2; XM_001015646.3. DR STRING; 5911.EAR95401; -. DR EnsemblProtists; EAR95401; EAR95401; TTHERM_00077050. DR GeneID; 7846841; -. DR KEGG; tet:TTHERM_00077050; -. DR InParanoid; Q23G59; -. DR Proteomes; UP000009168; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR GO; GO:0043022; F:ribosome binding; IBA:GO_Central. DR CDD; cd01878; HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 4: Predicted; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000009168}; KW Reference proteome {ECO:0000313|Proteomes:UP000009168}. FT DOMAIN 466 637 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 423 457 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 750 AA; 88406 MW; DF87DD5FFDFEB2C0 CRC64; MQQLIDINNS RKFQNFYINI NIGLKIQLII FKIKFAFILM IKSLLFRGST FLKQQFVFKQ VYRYSEKEQL DFRKQNLSQD KQQQKQIGYE TNCMVLHPIF FPNKGPLMEL YLAEEAVGLA KSLDWNVQKG PYWKEEYDKK VIQLQEEEQE EQQIEHVEDA NYESKNKRKR KNPKEDNRPK LDEGWQYFDQ TNIKDGDYIY THYFKGTYYK NGIIVDDQSD TEDDGDMFHE WRNKILRESI AKSSLIKMKK IIGKSFFTKG KLMDIGIYIK DNSIDCVFIN TELTPTQHKN LERLWTGIVN GREDEVFFKK NPMMSSDTEA EGDEPIQTSD YDNSSGKKIR VFDRFTMILQ IFAKRAQTQI ARHQIEVCFL NYLKTKLQRE GGTTFNAMYN IFKGDLMTAQ EISLEVVSAK SRAAKGKVQG EGETQLELQR RLVNDKLSKL KKELISLLEN QNFLREKRKK QYNNVPTIAL IGYTNAGKSA LMNALIKKDV VESKDNLFQT LSTTSRKFKL ISGQQAIILD TIGFITDLPH ELVDSFQSTL MEVEHADLVL HVRDISHPHT EDQKKTVLKV LKQLGFDQQF YTNKMIEVWN KMDLLEENVD YQSALKSDFP VVPVSALYNT NIKKLTQILE QKVNHLMNKK YYTIVNPLNT HEERYKWLFA NANISRLENE MYDYKQTKQY PYGNVKFQVL LDDVTFRRFC HTFNIQVETN DNKKGMPPKE WLKGSESYFQ RMREQKEKED QNFLKNKRED // ID Q24X71_DESHY Unreviewed; 530 AA. AC Q24X71; DT 18-APR-2006, integrated into UniProtKB/TrEMBL. DT 18-APR-2006, sequence version 1. DT 07-JUN-2017, entry version 71. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=DSY1582 {ECO:0000313|EMBL:BAE83371.1}; OS Desulfitobacterium hafniense (strain Y51). OC Bacteria; Firmicutes; Clostridia; Clostridiales; Peptococcaceae; OC Desulfitobacterium. OX NCBI_TaxID=138119 {ECO:0000313|EMBL:BAE83371.1, ECO:0000313|Proteomes:UP000001946}; RN [1] {ECO:0000313|EMBL:BAE83371.1, ECO:0000313|Proteomes:UP000001946} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Y51 {ECO:0000313|EMBL:BAE83371.1, RC ECO:0000313|Proteomes:UP000001946}; RX PubMed=16513756; DOI=10.1128/JB.188.6.2262-2274.2006; RA Nonaka H., Keresztes G., Shinoda Y., Ikenaga Y., Abe M., Naito K., RA Inatomi K., Furukawa K., Inui M., Yukawa H.; RT "Complete genome sequence of the dehalorespiring bacterium RT Desulfitobacterium hafniense Y51 and comparison with Dehalococcoides RT ethenogenes 195."; RL J. Bacteriol. 188:2262-2274(2006). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AP008230; BAE83371.1; -; Genomic_DNA. DR RefSeq; WP_011459781.1; NC_007907.1. DR ProteinModelPortal; Q24X71; -. DR STRING; 138119.DSY1582; -. DR EnsemblBacteria; BAE83371; BAE83371; DSY1582. DR KEGG; dsy:DSY1582; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; EREVIIT; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000001946; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000001946}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000001946}. FT DOMAIN 362 530 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 321 348 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 530 AA; 58558 MW; 8055F0F1A7C58EB1 CRC64; MDILGDISGI RGTQLKELKD LTSLRTDRPE LIHDDLLMGI CRLTSLWNKE IALYINRSGM VIAVAIGQHA AVKLPPLPAR QAGRLRCLHT HPSGNPQLSP MDLSALSSAG LESMSSIGVS NGQITGVEIA FSGDSDYQIL ALNPKEFVNF SYDGAVNDYR SRPASPSLKV SEQEKAFLVA LEEEELGLEL LTELTELAHS SGVEVVGQLL QPKRYGSPVS YLGKGKLQEM TQHLQNSGAN VLICDDELLP VQLRTLEQAT GVKVLDRTTL ILDIFAQRAK SREGKLQVEL AQLKHLLPRL TGQGLSLSRL GGGVGTRGPG ESKLEMDKRR VRKKINLLEN ELGEIRKTRT TQRRQREKSG IPLIALVGYT NAGKTTFLQK AMEQTRSKGE SVKGEDKLFA TLDPIVRGIR LDQRTEILLS DTVGFIQKLP HQLLHAFLAT LEEVQNADVL IHVLDASHPR ALERADTVHK ILEQLECHHK PRLTLLNKID QLDHPSDLSR LAQELSHPIP MSLIANTSLT PVWNKVLELL // ID Q26GV0_FLABB Unreviewed; 408 AA. AC Q26GV0; DT 18-APR-2006, integrated into UniProtKB/TrEMBL. DT 18-APR-2006, sequence version 1. DT 07-JUN-2017, entry version 64. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=BBFL7_01656 {ECO:0000313|EMBL:EAS20766.1}; OS Flavobacteria bacterium (strain BBFL7). OC Bacteria; Bacteroidetes; Flavobacteriia. OX NCBI_TaxID=156586 {ECO:0000313|EMBL:EAS20766.1, ECO:0000313|Proteomes:UP000002172}; RN [1] {ECO:0000313|EMBL:EAS20766.1, ECO:0000313|Proteomes:UP000002172} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BBFL7 {ECO:0000313|EMBL:EAS20766.1, RC ECO:0000313|Proteomes:UP000002172}; RA Azam F., Beardsley C., Gaasterland T., Malfatti F., Mayali X., RA Podell S., Samo T., Smriga S., Ferriera S., Johnson J., Kravitz S., RA Halpern A., Remington K., Beeson K., Tran B., Rogers Y.-H., RA Friedman R., Venter J.C.; RL Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EAS20766.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AAPD01000001; EAS20766.1; -; Genomic_DNA. DR RefSeq; WP_006796536.1; NZ_CH672374.1. DR ProteinModelPortal; Q26GV0; -. DR STRING; 156586.BBFL7_01656; -. DR EnsemblBacteria; EAS20766; EAS20766; BBFL7_01656. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR Proteomes; UP000002172; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000002172}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000002172}. FT DOMAIN 200 385 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 408 AA; 47260 MW; 066DD0315C0F39A2 CRC64; MLEREKHEYE KAILVGVVTQ QQSEEKLTEY LDELEFLAYT AGATIHKRFS QKMQKPNPKT FLGSGKMEDI KAYVDAHNID TVIFDDELSP AQQKNIEKIL EVKIIDRTYL ILDIFAQRAE TSYARTQVEL AQYEYLLPRL VGLWTHLERQ KGGIGMRGPG ETEIETDRRI VRDRITLLKK KLLTIDKQMA TQRGNRGKMV RVALVGYTNV GKSTLMNVIS KSEVFAENKL FATLDTTVRK VVVKNLPFLL TDTVGFIRKL PTQLVESFKS TLDEVRESDL LLHVVDIAHG SFEDHIASVN KILSEIDAVD KPTIMVFNKI DQYVAEDYDP EDLLEERTTA HYSLEEWKRT WMAKMGENVV FISAIEKENI ESFKKKVYDQ VREIHVKRFP YNAFLFPDWE ELLESEEE // ID Q28Q50_JANSC Unreviewed; 435 AA. AC Q28Q50; DT 04-APR-2006, integrated into UniProtKB/TrEMBL. DT 04-APR-2006, sequence version 1. DT 05-JUL-2017, entry version 80. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Jann_2245 {ECO:0000313|EMBL:ABD55162.1}; OS Jannaschia sp. (strain CCS1). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae; Jannaschia. OX NCBI_TaxID=290400 {ECO:0000313|EMBL:ABD55162.1, ECO:0000313|Proteomes:UP000008326}; RN [1] {ECO:0000313|Proteomes:UP000008326} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CCS1 {ECO:0000313|Proteomes:UP000008326}; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Hammon N., Israni S., Pitluck S., Brettin T., RA Bruce D., Han C., Tapia R., Gilna P., Chertkov O., Saunders E., RA Schmutz J., Larimer F., Land M., Kyrpides N., Lykidis A., Moran M.A., RA Belas R., Ye W., Buchan A., Gonzalez J.M., Schell M.A., Richardson P.; RT "Complete sequence of chromosome of Jannaschia sp. CCS1."; RL Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000264; ABD55162.1; -; Genomic_DNA. DR ProteinModelPortal; Q28Q50; -. DR STRING; 290400.Jann_2245; -. DR EnsemblBacteria; ABD55162; ABD55162; Jann_2245. DR KEGG; jan:Jann_2245; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; FNNHAHV; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000008326; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000008326}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Hydrolase {ECO:0000313|EMBL:ABD55162.1}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000008326}. FT DOMAIN 215 384 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 435 AA; 47601 MW; 54A6DEB12D60AABE CRC64; MSAGLRATDG DDEGLEKGPM RALVLHPDIK SDRTRRDPAF ALEEGVALAA ALPDLEVVDA QVVRLPRAQP GLLFGSGKIQ ELHDLIEALD IGLVLIDGPV TPVQQRNLER EWGCKLLDRT GLILEIFADR AATREGVLQV ELAALSYQRT RLVRAWTHLE RQRGGLGFVG GPGETQIEAD RRAIDEAVTR IKRQLAKVVK TRALHRSARA KVPYPIVALV GYTNAGKSTL FNRLTGADVM AKDMLFATLD PTMRAVTLPD GTDVILSDTV GFISDLPTQL VAAFRATLEE VLDADLIVHV RDISHPQTVE QAEDVHAILG DLGVSDQSAQ LEVWNKVDLL DEAAQTARQV EADRNEAIFA TSALTGAGMD DFLTAVSHTL SPPRLEAVVE LPHSDGRKRA WLFEQGVVER EEPTEIGTQL TVLWTTRQQK AFRAL // ID Q296H6_DROPS Unreviewed; 525 AA. AC Q296H6; DT 04-APR-2006, integrated into UniProtKB/TrEMBL. DT 14-OCT-2008, sequence version 2. DT 30-AUG-2017, entry version 61. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EAL28481.2}; GN Name=Dpse\GA18671 {ECO:0000313|EMBL:EAL28481.2}; GN ORFNames=Dpse_GA18671 {ECO:0000313|EMBL:EAL28481.2}, GN GA18671 {ECO:0000313|FlyBase:FBgn0078671}; OS Drosophila pseudoobscura pseudoobscura (Fruit fly). OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; OC Pterygota; Neoptera; Holometabola; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila; Sophophora. OX NCBI_TaxID=46245 {ECO:0000313|EMBL:EAL28481.2, ECO:0000313|Proteomes:UP000001819}; RN [1] {ECO:0000313|EMBL:EAL28481.2, ECO:0000313|Proteomes:UP000001819} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MV2-25 / Tucson 14011-0121.94 RC {ECO:0000313|Proteomes:UP000001819}; RX PubMed=15632085; DOI=10.1101/gr.3059305; RA Richards S., Liu Y., Bettencourt B.R., Hradecky P., Letovsky S., RA Nielsen R., Thornton K., Hubisz M.J., Chen R., Meisel R.P., RA Couronne O., Hua S., Smith M.A., Zhang P., Liu J., Bussemaker H.J., RA van Batenburg M.F., Howells S.L., Scherer S.E., Sodergren E., RA Matthews B.B., Crosby M.A., Schroeder A.J., Ortiz-Barrientos D., RA Rives C.M., Metzker M.L., Muzny D.M., Scott G., Steffen D., RA Wheeler D.A., Worley K.C., Havlak P., Durbin K.J., Egan A., Gill R., RA Hume J., Morgan M.B., Miner G., Hamilton C., Huang Y., Waldron L., RA Verduzco D., Clerc-Blankenburg K.P., Dubchak I., Noor M.A., RA Anderson W., White K.P., Clark A.G., Schaeffer S.W., Gelbart W., RA Weinstock G.M., Gibbs R.A.; RT "Comparative genome sequencing of Drosophila pseudoobscura: RT chromosomal, gene, and cis-element evolution."; RL Genome Res. 15:1-18(2005). RN [2] {ECO:0000313|EMBL:EAL28481.2, ECO:0000313|Proteomes:UP000001819} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MV2-25 / Tucson 14011-0121.94 RC {ECO:0000313|Proteomes:UP000001819}; RX PubMed=17994087; DOI=10.1038/nature06341; RG Drosophila 12 Genomes Consortium; RA Clark A.G., Eisen M.B., Smith D.R., Bergman C.M., Oliver B., RA Markow T.A., Kaufman T.C., Kellis M., Gelbart W., Iyer V.N., RA Pollard D.A., Sackton T.B., Larracuente A.M., Singh N.D., Abad J.P., RA Abt D.N., Adryan B., Aguade M., Akashi H., Anderson W.W., RA Aquadro C.F., Ardell D.H., Arguello R., Artieri C.G., Barbash D.A., RA Barker D., Barsanti P., Batterham P., Batzoglou S., Begun D., RA Bhutkar A., Blanco E., Bosak S.A., Bradley R.K., Brand A.D., RA Brent M.R., Brooks A.N., Brown R.H., Butlin R.K., Caggese C., RA Calvi B.R., Bernardo de Carvalho A., Caspi A., Castrezana S., RA Celniker S.E., Chang J.L., Chapple C., Chatterji S., Chinwalla A., RA Civetta A., Clifton S.W., Comeron J.M., Costello J.C., Coyne J.A., RA Daub J., David R.G., Delcher A.L., Delehaunty K., Do C.B., Ebling H., RA Edwards K., Eickbush T., Evans J.D., Filipski A., Findeiss S., RA Freyhult E., Fulton L., Fulton R., Garcia A.C., Gardiner A., RA Garfield D.A., Garvin B.E., Gibson G., Gilbert D., Gnerre S., RA Godfrey J., Good R., Gotea V., Gravely B., Greenberg A.J., RA Griffiths-Jones S., Gross S., Guigo R., Gustafson E.A., Haerty W., RA Hahn M.W., Halligan D.L., Halpern A.L., Halter G.M., Han M.V., RA Heger A., Hillier L., Hinrichs A.S., Holmes I., Hoskins R.A., RA Hubisz M.J., Hultmark D., Huntley M.A., Jaffe D.B., Jagadeeshan S., RA Jeck W.R., Johnson J., Jones C.D., Jordan W.C., Karpen G.H., RA Kataoka E., Keightley P.D., Kheradpour P., Kirkness E.F., RA Koerich L.B., Kristiansen K., Kudrna D., Kulathinal R.J., Kumar S., RA Kwok R., Lander E., Langley C.H., Lapoint R., Lazzaro B.P., Lee S.J., RA Levesque L., Li R., Lin C.F., Lin M.F., Lindblad-Toh K., Llopart A., RA Long M., Low L., Lozovsky E., Lu J., Luo M., Machado C.A., RA Makalowski W., Marzo M., Matsuda M., Matzkin L., McAllister B., RA McBride C.S., McKernan B., McKernan K., Mendez-Lago M., Minx P., RA Mollenhauer M.U., Montooth K., Mount S.M., Mu X., Myers E., Negre B., RA Newfeld S., Nielsen R., Noor M.A., O'Grady P., Pachter L., RA Papaceit M., Parisi M.J., Parisi M., Parts L., Pedersen J.S., RA Pesole G., Phillippy A.M., Ponting C.P., Pop M., Porcelli D., RA Powell J.R., Prohaska S., Pruitt K., Puig M., Quesneville H., RA Ram K.R., Rand D., Rasmussen M.D., Reed L.K., Reenan R., Reily A., RA Remington K.A., Rieger T.T., Ritchie M.G., Robin C., Rogers Y.H., RA Rohde C., Rozas J., Rubenfield M.J., Ruiz A., Russo S., Salzberg S.L., RA Sanchez-Gracia A., Saranga D.J., Sato H., Schaeffer S.W., Schatz M.C., RA Schlenke T., Schwartz R., Segarra C., Singh R.S., Sirot L., Sirota M., RA Sisneros N.B., Smith C.D., Smith T.F., Spieth J., Stage D.E., RA Stark A., Stephan W., Strausberg R.L., Strempel S., Sturgill D., RA Sutton G., Sutton G.G., Tao W., Teichmann S., Tobari Y.N., RA Tomimura Y., Tsolas J.M., Valente V.L., Venter E., Venter J.C., RA Vicario S., Vieira F.G., Vilella A.J., Villasante A., Walenz B., RA Wang J., Wasserman M., Watts T., Wilson D., Wilson R.K., Wing R.A., RA Wolfner M.F., Wong A., Wong G.K., Wu C.I., Wu G., Yamamoto D., RA Yang H.P., Yang S.P., Yorke J.A., Yoshida K., Zdobnov E., Zhang P., RA Zhang Y., Zimin A.V., Baldwin J., Abdouelleil A., Abdulkadir J., RA Abebe A., Abera B., Abreu J., Acer S.C., Aftuck L., Alexander A., RA An P., Anderson E., Anderson S., Arachi H., Azer M., Bachantsang P., RA Barry A., Bayul T., Berlin A., Bessette D., Bloom T., Blye J., RA Boguslavskiy L., Bonnet C., Boukhgalter B., Bourzgui I., Brown A., RA Cahill P., Channer S., Cheshatsang Y., Chuda L., Citroen M., RA Collymore A., Cooke P., Costello M., D'Aco K., Daza R., De Haan G., RA DeGray S., DeMaso C., Dhargay N., Dooley K., Dooley E., Doricent M., RA Dorje P., Dorjee K., Dupes A., Elong R., Falk J., Farina A., Faro S., RA Ferguson D., Fisher S., Foley C.D., Franke A., Friedrich D., RA Gadbois L., Gearin G., Gearin C.R., Giannoukos G., Goode T., RA Graham J., Grandbois E., Grewal S., Gyaltsen K., Hafez N., Hagos B., RA Hall J., Henson C., Hollinger A., Honan T., Huard M.D., Hughes L., RA Hurhula B., Husby M.E., Kamat A., Kanga B., Kashin S., Khazanovich D., RA Kisner P., Lance K., Lara M., Lee W., Lennon N., Letendre F., RA LeVine R., Lipovsky A., Liu X., Liu J., Liu S., Lokyitsang T., RA Lokyitsang Y., Lubonja R., Lui A., MacDonald P., Magnisalis V., RA Maru K., Matthews C., McCusker W., McDonough S., Mehta T., Meldrim J., RA Meneus L., Mihai O., Mihalev A., Mihova T., Mittelman R., Mlenga V., RA Montmayeur A., Mulrain L., Navidi A., Naylor J., Negash T., Nguyen T., RA Nguyen N., Nicol R., Norbu C., Norbu N., Novod N., O'Neill B., RA Osman S., Markiewicz E., Oyono O.L., Patti C., Phunkhang P., RA Pierre F., Priest M., Raghuraman S., Rege F., Reyes R., Rise C., RA Rogov P., Ross K., Ryan E., Settipalli S., Shea T., Sherpa N., Shi L., RA Shih D., Sparrow T., Spaulding J., Stalker J., Stange-Thomann N., RA Stavropoulos S., Stone C., Strader C., Tesfaye S., Thomson T., RA Thoulutsang Y., Thoulutsang D., Topham K., Topping I., Tsamla T., RA Vassiliev H., Vo A., Wangchuk T., Wangdi T., Weiand M., Wilkinson J., RA Wilson A., Yadav S., Young G., Yu Q., Zembek L., Zhong D., Zimmer A., RA Zwirko Z., Jaffe D.B., Alvarez P., Brockman W., Butler J., Chin C., RA Gnerre S., Grabherr M., Kleber M., Mauceli E., MacCallum I.; RT "Evolution of genes and genomes on the Drosophila phylogeny."; RL Nature 450:203-218(2007). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CM000070; EAL28481.2; -; Genomic_DNA. DR RefSeq; XP_001359336.2; XM_001359299.3. DR ProteinModelPortal; Q296H6; -. DR STRING; 7237.FBpp0284400; -. DR EnsemblMetazoa; FBtr0285962; FBpp0284400; FBgn0078671. DR GeneID; 4802413; -. DR KEGG; dpo:Dpse_GA18671; -. DR FlyBase; FBgn0078671; Dpse\GA18671. DR InParanoid; Q296H6; -. DR OMA; MDTVGFM; -. DR Proteomes; UP000001819; Chromosome 2. DR Bgee; FBgn0078671; -. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR CDD; cd01878; HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 4: Predicted; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000001819}; KW Reference proteome {ECO:0000313|Proteomes:UP000001819}. FT DOMAIN 298 468 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 259 291 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 525 AA; 59016 MW; 0F5BDD7C3A060F8A CRC64; MTSLRPLMRL ARALPLRPAM VGVLHSRFKY TQHQGVKGIR NRKSFFEAQM QAGQHGDEDY EEAKRGDSNG NLADMRFLDD RAYDEVAGGA MRISRDIASA QQVLILQPYV KWSAKRQNTP SDVRPEDQLA EASALIHSLP NWQVAKALKV PLESLERKTL FGSGKMVELK ALIADLRQEK HLTCLFVSKG TLSFAQKRFL EAEFRLPVMD RYSVVIQILR LHATTAEARL QVAMAELPYI WSQAKDASVT QTRRQGYSLT DLQKEILRTR ERKLRAELDR VRRQRQLLRQ KRKQQNYPIV AVVGYTNAGK TSLIKALTVE DALQPRNQLF ATLDVTAHAG QLPCNLQVIY MDTVGFMSDL PTGLFECFVA TLEDAMLADV IVHVQDLSHP CHAAQRSHVE STLRSLAFNV SGGDPATSQL PPIINVYNKC DLVSQPSSDA AVHHISARAQ TGLEPLLADI EEQILAATGR RKLQMRVPSG GPEMAWLYKN AAVVDTVADE AYPNRLMMHV VISQRTLDQF KREFL // ID Q2BIN5_NEPCE Unreviewed; 418 AA. AC Q2BIN5; DT 04-APR-2006, integrated into UniProtKB/TrEMBL. DT 04-APR-2006, sequence version 1. DT 05-JUL-2017, entry version 65. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=MED92_00490 {ECO:0000313|EMBL:EAR60362.1}; OS Neptuniibacter caesariensis. OC Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales; OC Neptuniibacter. OX NCBI_TaxID=207954 {ECO:0000313|EMBL:EAR60362.1, ECO:0000313|Proteomes:UP000002171}; RN [1] {ECO:0000313|EMBL:EAR60362.1, ECO:0000313|Proteomes:UP000002171} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MED92 {ECO:0000313|EMBL:EAR60362.1, RC ECO:0000313|Proteomes:UP000002171}; RA Pinhassi J., Pedros-Alio C., Ferriera S., Johnson J., Kravitz S., RA Halpern A., Remington K., Beeson K., Tran B., Rogers Y.-H., RA Friedman R., Venter J.C.; RL Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EAR60362.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AAOW01000019; EAR60362.1; -; Genomic_DNA. DR ProteinModelPortal; Q2BIN5; -. DR STRING; 207954.MED92_00490; -. DR EnsemblBacteria; EAR60362; EAR60362; MED92_00490. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000002171; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000002171}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000002171}. FT DOMAIN 183 350 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 418 AA; 47444 MW; 14FE88624CC4E55D CRC64; MNLAAEADQE SPKELEELAL SAGADPVEFL TGSLSHPNPK FFIGQGKLEE LRELVHMHDA KLVIFNHALS PAQERNIERE IQCRVLDRTG LILDIFAQRA RTHEGKLQVE LAQLDHMSTR LVRGWTHLER QKGGIGLRGP GETQLETDRR LLRARMKSIH KRLEKVRKQR DQGRRSRMRA EVPTLSLVGY TNAGKSTLFN ALTTSEVYAA DQLFATLDPT LRRIEVEDIG QAILADTVGF IRHLPHKLVE AFRATLQETI EATLLLHVID SHDDDRHDHV AEVENVLREI GADEVPVLEV YNKIDLIEGR KPRIDRDEEG NPIRVWLSAV SGEGHDLLFQ AVNELLADDV FHDNVSLQPH EGQFRARLYE SGAVLSEQVD EKGSIILEVR MQKKDMLQLL SRLGMSRERC FPAEVNPW // ID Q2CHZ1_OCEGH Unreviewed; 430 AA. AC Q2CHZ1; DT 04-APR-2006, integrated into UniProtKB/TrEMBL. DT 04-APR-2006, sequence version 1. DT 07-JUN-2017, entry version 51. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=OG2516_01914 {ECO:0000313|EMBL:EAR52153.1}; OS Oceanicola granulosus (strain ATCC BAA-861 / DSM 15982 / KCTC 12143 / OS HTCC2516). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae; Oceanicola. OX NCBI_TaxID=314256 {ECO:0000313|EMBL:EAR52153.1, ECO:0000313|Proteomes:UP000003635}; RN [1] {ECO:0000313|EMBL:EAR52153.1, ECO:0000313|Proteomes:UP000003635} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-861 / DSM 15982 / KCTC 12143 / HTCC2516 RC {ECO:0000313|Proteomes:UP000003635}; RX PubMed=20418400; DOI=10.1128/JB.00412-10; RA Thrash J.C., Cho J.C., Vergin K.L., Giovannoni S.J.; RT "Genome sequences of Oceanicola granulosus HTCC2516(T) and Oceanicola RT batsensis HTCC2597(TDelta)."; RL J. Bacteriol. 192:3549-3550(2010). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EAR52153.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AAOT01000005; EAR52153.1; -; Genomic_DNA. DR RefSeq; WP_007253913.1; NZ_CH724107.1. DR ProteinModelPortal; Q2CHZ1; -. DR STRING; 314256.OG2516_01914; -. DR EnsemblBacteria; EAR52153; EAR52153; OG2516_01914. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000003635; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000003635}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000003635}. FT DOMAIN 210 379 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 169 196 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 430 AA; 47833 MW; C1A9AF01E55972C9 CRC64; MTFDPETGDR REKPTRAFVL HPDIKTRGQR RDPTPALEEA VALAAALPGL EVIGAEVVRL QQVHPGHLFG TGKIAELKQR LKAEEAELVL VDGPVSPVQQ RNLEKEWGVK LLDRTGLILE IFSDRARTRE GVLQVEMAAL SYQRTRLVRA WTHLERQRGG LGFVGGPGET QIEADRRAID EQLARLRKQL EKVVKTRTLH RASRAKVPFP IVALVGYTNA GKSTLFNRLT GAEVMAKDML FATLDPTMRK VELPSGQEVI LSDTVGFISD LPTELVAAFR ATLEEVLDAD LILHVRDVAH AETEEQAEDV RTILSGIGVG EDAPLLEVWN KIDLLPPEER EGRATQAARR DDVFAVSALE GIGLDPLLAA VSARVSEPRS RDVLHLGHED GRRRAWLFEQ GIVSDETRDD DGTRLTVDWT ERQKARYGRL // ID Q2FYY9_STAA8 Unreviewed; 412 AA. AC Q2FYY9; DT 21-MAR-2006, integrated into UniProtKB/TrEMBL. DT 21-MAR-2006, sequence version 1. DT 07-JUN-2017, entry version 81. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=SAOUHSC_01283 {ECO:0000313|EMBL:ABD30383.1}; OS Staphylococcus aureus (strain NCTC 8325). OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae; OC Staphylococcus. OX NCBI_TaxID=93061 {ECO:0000313|EMBL:ABD30383.1, ECO:0000313|Proteomes:UP000008816}; RN [1] {ECO:0000313|Proteomes:UP000008816} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NCTC 8325 {ECO:0000313|Proteomes:UP000008816}; RA Gillaspy A.F., Worrell V., Orvis J., Roe B.A., Dyer D.W., RA Iandolo J.J.; RT "The Staphylococcus aureus NCTC 8325 genome."; RL (In) Fischetti V., Novick R., Ferretti J., Portnoy D., Rood J. (eds.); RL Gram positive pathogens, 2nd edition, pp.381-412, ASM Press, RL Washington D.C (2006). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000253; ABD30383.1; -; Genomic_DNA. DR RefSeq; WP_000068617.1; NC_007795.1. DR RefSeq; YP_499815.1; NC_007795.1. DR ProteinModelPortal; Q2FYY9; -. DR SMR; Q2FYY9; -. DR STRING; 93061.SAOUHSC_01283; -. DR EnsemblBacteria; ABD30383; ABD30383; SAOUHSC_01283. DR GeneID; 3919935; -. DR KEGG; sao:SAOUHSC_01283; -. DR PATRIC; fig|93061.5.peg.1176; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR Proteomes; UP000008816; Chromosome. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0043022; F:ribosome binding; IBA:GO_Central. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000008816}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000008816}. FT DOMAIN 206 369 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 179 202 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 412 AA; 47336 MW; F2C92D43D5DCD049 CRC64; MAQQQIHDTK NKLEKAVLVG VHAQDDKQFN FESTMEELSS LSETCQLEVL GQITQNRDRV DRKYYVGKGK IEEIQAFIEF KDIDVVITND ELTTAQSKSL NEALGVKIID RTQLILEIFA LRARSKEGKL QVELAQLDYL LPRLQGHGKS LSRLGGGIGT RGPGETKLEM DRRHIRTRMN EIKHQLRTVE EHRERYRNKR NQNQVFQVAL VGYTNAGKSS WFNVLANEET YEKDQLFATL DPKTRQIQIN DGFNLIISDT VGFIQKLPTT LIAAFKSTLE EAKGADLLVH VVDSSHPEYR TQYDTVNDLI KQLDMSHISQ IVIFNKKDLC DHASNRPASD LPNVFVSSKN DGDKLLVKTL FIDEIKRQLT YYDETIATNN ADRLYFLKQH TLVTELKYDE IENVYRIKGF KK // ID Q2G701_NOVAD Unreviewed; 426 AA. AC Q2G701; DT 21-MAR-2006, integrated into UniProtKB/TrEMBL. DT 21-MAR-2006, sequence version 1. DT 07-JUN-2017, entry version 89. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Saro_1932 {ECO:0000313|EMBL:ABD26372.1}; OS Novosphingobium aromaticivorans (strain ATCC 700278 / DSM 12444 / CIP OS 105152 / NBRC 16084 / F199). OC Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales; OC Sphingomonadaceae; Novosphingobium. OX NCBI_TaxID=279238 {ECO:0000313|EMBL:ABD26372.1, ECO:0000313|Proteomes:UP000009134}; RN [1] {ECO:0000313|Proteomes:UP000009134} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700278 / DSM 12444 / CIP 105152 / NBRC 16084 / F199 RC {ECO:0000313|Proteomes:UP000009134}; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., RA Hammon N., Israni S., Pitluck S., Chain P., Malfatti S., Shin M., RA Vergez L., Schmutz J., Larimer F., Land M., Kyrpides N., Ivanova N., RA Fredrickson J., Balkwill D., Romine M.F., Richardson P.; RT "Complete sequence of Novosphingobium aromaticivorans DSM 12444."; RL Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000248; ABD26372.1; -; Genomic_DNA. DR ProteinModelPortal; Q2G701; -. DR STRING; 279238.Saro_1932; -. DR EnsemblBacteria; ABD26372; ABD26372; Saro_1932. DR KEGG; nar:Saro_1932; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000009134; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000009134}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000009134}. FT DOMAIN 194 370 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 153 187 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 426 AA; 46606 MW; BA4BBD669382784B CRC64; MVVLPDIRQR GGGLGADAES RLEEGQGLAR AIGIEVVEAF ILPIRTVRPA TLFGEGQVER IAVACNQSDA ELVIVDGALS AIQQRNLEEK LKRKVIDRTG LILEIFGERA ATAEGRLQVE LAHLDYQAGR LVRSWTHLER QRGGFGFLGG PGETQIEADR RLIRNRMARL RRELEQVRRT RGLHRERRQR APWPVIALVG YTNAGKSTLF NRLTGADVMA EDLLFATLDP TMRAIRLPGV EKAILSDTVG FISDLPTQLV AAFRATLEEV TAADVIVHVR DVANLASADQ KAEVEQILAD LGVIGEAGST IPIVEAWNKW DLLTPEEQAM RQDLIAAKIA EVPVVPISAL TGAGVETLLD KLGEMLTGSA QTLELTVPLS DGQRLAWLHA HGDIISENQV DIAEIGPAMR IKVRLTPREL GRFTSL // ID Q2IMF2_ANADE Unreviewed; 608 AA. AC Q2IMF2; DT 07-MAR-2006, integrated into UniProtKB/TrEMBL. DT 07-MAR-2006, sequence version 1. DT 07-JUN-2017, entry version 77. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Adeh_0203 {ECO:0000313|EMBL:ABC79980.1}; OS Anaeromyxobacter dehalogenans (strain 2CP-C). OC Bacteria; Proteobacteria; Deltaproteobacteria; Myxococcales; OC Cystobacterineae; Anaeromyxobacteraceae; Anaeromyxobacter. OX NCBI_TaxID=290397 {ECO:0000313|EMBL:ABC79980.1, ECO:0000313|Proteomes:UP000001935}; RN [1] {ECO:0000313|EMBL:ABC79980.1, ECO:0000313|Proteomes:UP000001935} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=2CP-C {ECO:0000313|EMBL:ABC79980.1, RC ECO:0000313|Proteomes:UP000001935}; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., RA Hammon N., Israni S., Pitluck S., Brettin T., Bruce D., Han C., RA Tapia R., Gilna P., Kiss H., Schmutz J., Larimer F., Land M., RA Kyrpides N., Anderson I., Sanford R.A., Ritalahti K.M., Thomas H.S., RA Kirby J.R., Zhulin I.B., Loeffler F.E., Richardson P.; RT "Complete sequence of Anaeromyxobacter dehalogenans 2CP-C."; RL Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Proteomes:UP000001935} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=2CP-C {ECO:0000313|Proteomes:UP000001935}; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., RA Hammon N., Israni S., Pitluck S., Brettin T., Bruce D., Han C., RA Tapia R., Gilna P., Kiss H., Schmutz J., Larimer F., Land M., RA Kyrpides N., Anderson I., Sanford R.A., Ritalahti K.M., Thomas H.S., RA Kirby J.R., Zhulin I.B., Loeffler F.E., Richardson P.; RT "Complete sequence of Anaeromyxobacter dehalogenans 2CP-C."; RL Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000251; ABC79980.1; -; Genomic_DNA. DR RefSeq; WP_011419263.1; NC_007760.1. DR ProteinModelPortal; Q2IMF2; -. DR STRING; 290397.Adeh_0203; -. DR EnsemblBacteria; ABC79980; ABC79980; Adeh_0203. DR KEGG; ade:Adeh_0203; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; EREVIIT; -. DR Proteomes; UP000001935; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000001935}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Hydrolase {ECO:0000313|EMBL:ABC79980.1}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000001935}. FT DOMAIN 379 543 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 338 365 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 608 AA; 65971 MW; 9E87C8FF61817DB4 CRC64; MQEVHGNTLG LKPSQLHALR RTYRRRVDAQ SIVSPELARH LAEVSRETNR QVGVLLDRKG DVQAVVVGDA RKLDLPDVGR GRAGESRLRG LRLVHTHLNG EPLTRDDHTD LALLRLDLVA AIEVREDGLP GRVHYAHLLP ENPQGAMWKD EEAPTVHELA YDALSGALAL EDEFARARAA RRTGGRERAI LVGFGGKGRG RAEAEASLEE LKELARTAGV EVLEATLQLR RDPDPRYLIG KGKLEDIVLR SMQRMATVIV FDAELSPSQA RHIAEATSLK ILDRTQLILD IFAQRAQSAD GKLQVELAQL KYLYPRLVGR DDSLSRLAGG IGGRGPGETK LEIDRRRVRD RITALERRIE GLGADRTLRR KQRNARGLPV LSIVGYTNAG KSTLLNALTD SAVLAEDKLF ATLDPTSRRL RFPRDREVII TDTVGFIRDL PPDLVNAFRA TLEELGDADL LLHVVDASDP RQEEQIAAVE EILRGLGLDG KRRLLVLNKV DRLPPETQAA LAQRRDAAAV SAVTRAGLGG LLARCEQLLW TDGRVALGDV IAAAPAGEEG AGAAGHLAGD AAPEPLAPEP PAPAAASVPG PGEPGPPRLL PASLRRVS // ID Q2J778_FRACC Unreviewed; 486 AA. AC Q2J778; DT 07-MAR-2006, integrated into UniProtKB/TrEMBL. DT 07-MAR-2006, sequence version 1. DT 05-JUL-2017, entry version 88. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Francci3_3511 {ECO:0000313|EMBL:ABD12864.1}; OS Frankia casuarinae (strain DSM 45818 / CECT 9043 / CcI3). OC Bacteria; Actinobacteria; Frankiales; Frankiaceae; Frankia. OX NCBI_TaxID=106370 {ECO:0000313|EMBL:ABD12864.1, ECO:0000313|Proteomes:UP000001937}; RN [1] {ECO:0000313|EMBL:ABD12864.1, ECO:0000313|Proteomes:UP000001937} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 45818 / CECT 9043 / CcI3 RC {ECO:0000313|Proteomes:UP000001937}; RX PubMed=17151343; DOI=10.1101/gr.5798407; RA Normand P., Lapierre P., Tisa L.S., Gogarten J.P., Alloisio N., RA Bagnarol E., Bassi C.A., Berry A.M., Bickhart D.M., Choisne N., RA Couloux A., Cournoyer B., Cruveiller S., Daubin V., Demange N., RA Francino M.P., Goltsman E., Huang Y., Kopp O.R., Labarre L., RA Lapidus A., Lavire C., Marechal J., Martinez M., Mastronunzio J.E., RA Mullin B.C., Niemann J., Pujic P., Rawnsley T., Rouy Z., RA Schenowitz C., Sellstedt A., Tavares F., Tomkins J.P., Vallenet D., RA Valverde C., Wall L.G., Wang Y., Medigue C., Benson D.R.; RT "Genome characteristics of facultatively symbiotic Frankia sp. strains RT reflect host range and host plant biogeography."; RL Genome Res. 17:7-15(2007). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000249; ABD12864.1; -; Genomic_DNA. DR RefSeq; WP_011437889.1; NC_007777.1. DR ProteinModelPortal; Q2J778; -. DR STRING; 106370.Francci3_3511; -. DR EnsemblBacteria; ABD12864; ABD12864; Francci3_3511. DR GeneID; 32158358; -. DR KEGG; fra:Francci3_3511; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000001937; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000001937}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Hydrolase {ECO:0000313|EMBL:ABD12864.1}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000001937}. FT DOMAIN 268 432 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 227 254 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 486 AA; 52148 MW; A0AFDE356C36B4DB CRC64; MTLPADAFDA STLDRSLIKL TEADSSYLPN FFDDSGDGFD LEDRAALRRV PGLATELDDV TEVEYRQLRL ERVVLIGVWT SGSPRSAESS MAELAALATT AGSVVLDALV QRRDRPDAAT YVGSGKAREL AEVVAATGAD TVVCDGELTP GQLRQLEEVV KVKVIDRTAL ILDIFAQHAT SREGKAQVEL AQLQYMLPRL RGWGESMSRA AASGGGRAPI GTRGPGETKI ETDRRRLRAR MARLRRELAA MTTVRETKRS ARRRGEVPSV AIAGYTNAGK SSLLNRLTGA GVLVEDALFA TLDPTVRRAT LPDGRAFTLT DTVGFVRHLP HQIVEAFRST LEEVADADLI LHVVDGSSPE PAAQISAVRE VLNDIDAGGV PELIVVNKVD AVEPTVVAGL RQLAPDAVFV SARTGEGLAA LVDALCARVP HPDVEMRVLV PYTRGDLVSR VHANGEVLTM EHTETGTRLS ARVSSGLAAE LHAYRA // ID Q2JPB2_SYNJB Unreviewed; 588 AA. AC Q2JPB2; DT 07-MAR-2006, integrated into UniProtKB/TrEMBL. DT 07-MAR-2006, sequence version 1. DT 05-JUL-2017, entry version 79. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=CYB_0382 {ECO:0000313|EMBL:ABD01378.1}; OS Synechococcus sp. (strain JA-2-3B'a(2-13)) (Cyanobacteria bacterium OS Yellowstone B-Prime). OC Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; OC Synechococcus. OX NCBI_TaxID=321332 {ECO:0000313|EMBL:ABD01378.1, ECO:0000313|Proteomes:UP000001938}; RN [1] {ECO:0000313|EMBL:ABD01378.1, ECO:0000313|Proteomes:UP000001938} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=JA-2-3B'a(2-13) {ECO:0000313|Proteomes:UP000001938}; RX PubMed=18059494; DOI=10.1038/ismej.2007.46; RA Bhaya D., Grossman A.R., Steunou A.S., Khuri N., Cohan F.M., RA Hamamura N., Melendrez M.C., Bateson M.M., Ward D.M., Heidelberg J.F.; RT "Population level functional diversity in a microbial community RT revealed by comparative genomic and metagenomic analyses."; RL ISME J. 1:703-713(2007). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000240; ABD01378.1; -; Genomic_DNA. DR ProteinModelPortal; Q2JPB2; -. DR STRING; 321332.CYB_0382; -. DR EnsemblBacteria; ABD01378; ABD01378; CYB_0382. DR KEGG; cyb:CYB_0382; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; EREVIIT; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000001938; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000001938}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000001938}. FT DOMAIN 411 576 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 370 407 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 588 AA; 65460 MW; FE3B6D8F4E4D55DD CRC64; MPRASTSRHQ TDPRFSSAIA PRRFPEQAKG LKPHQQKQLQ RLYQLRLPPD RLVTVEFAQR LGSLTQDLEG QPISVYLNRR GQVIRVGVGS PFETQIPAWE LPRQGAERLS GIRCITTQMG EGGPGQKALT AMALQRLDAL ITLSVSKSGG HRRRGGAATG FVHRAYLAHL LPEGERRWQV SEPLPLGILA EQDLQELVAE LEDGFRRQVT ARQVDLDQDR AILVGLQESG QSYEDLMDGL AELSRLVESA GGQVLQALWQ RREGPNSATV IGSGKVQELA LLVQDLGANL VVFDRELTPS QVRTLEEAVG VRVVDRSEVI LDIFAQRART RAGKLQVELA QLQYLLPRLA GRGRTMSRLG GGIGTRGPGE TQLEMERRAI QRRISKLRQE VEELRRHRQR LRQRREASQI PVVALVGYTN AGKSTLLNAL THAQVYVADQ LFATLDPTTR RLELPDQQAV LLTDTVGFLT ELPDQLVDAF QATLEEVTEA DALLHVVDLS HPNWEGQIEA VETLLDKLPL ATGPRQLVFN KIDRLDPEWV EDVRLLYPKA LFVSATTGQN LDQLHHTLAQ FAAVLSPNPF DSQEPKDP // ID Q2K8U5_RHIEC Unreviewed; 441 AA. AC Q2K8U5; DT 07-MAR-2006, integrated into UniProtKB/TrEMBL. DT 07-MAR-2006, sequence version 1. DT 07-JUN-2017, entry version 79. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:ABC90741.1}; GN OrderedLocusNames=RHE_CH01955 {ECO:0000313|EMBL:ABC90741.1}; OS Rhizobium etli (strain CFN 42 / ATCC 51251). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium. OX NCBI_TaxID=347834 {ECO:0000313|EMBL:ABC90741.1, ECO:0000313|Proteomes:UP000001936}; RN [1] {ECO:0000313|EMBL:ABC90741.1, ECO:0000313|Proteomes:UP000001936} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CFN 42 / ATCC 51251 {ECO:0000313|Proteomes:UP000001936}; RX PubMed=16505379; DOI=10.1073/pnas.0508502103; RA Gonzalez V., Santamaria R.I., Bustos P., Hernandez-Gonzalez I., RA Medrano-Soto A., Moreno-Hagelsieb G., Janga S.C., Ramirez M.A., RA Jimenez-Jacinto V., Collado-Vides J., Davila G.; RT "The partitioned Rhizobium etli genome: genetic and metabolic RT redundancy in seven interacting replicons."; RL Proc. Natl. Acad. Sci. U.S.A. 103:3834-3839(2006). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000133; ABC90741.1; -; Genomic_DNA. DR RefSeq; WP_011425230.1; NC_007761.1. DR ProteinModelPortal; Q2K8U5; -. DR STRING; 347834.RHE_CH01955; -. DR EnsemblBacteria; ABC90741; ABC90741; RHE_CH01955. DR GeneID; 24301362; -. DR KEGG; ret:RHE_CH01955; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR KO; K03665; -. DR OMA; HPATYIG; -. DR Proteomes; UP000001936; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000001936}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000001936}. FT DOMAIN 203 375 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 162 196 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 441 AA; 48935 MW; C3BFC507611DDBE7 CRC64; MRATVVVPVL KSRSRGGQTE SASTRTPESR LEEATGLAQA IDLDVVNGSI VPVNDPRPAT LLGTGKIEEI KALLDERDSG LVIVDHPLTP VQQRNLEKEW NAKVIDRTGL ILEIFGRRAS TKEGTLQVDL AHLNYQKGRL VRSWTHLERQ RGGGGFMGGP GETQIEADRR LLQDRIIKLE RELEQVVRTR QLHRAKRRKV PHPIVALVGY TNAGKSTLFN RITGAGVLAE DMLFATLDPT LRRMKLPHGR TVILSDTVGF ISDLPTHLVA AFRATLEEVL EADLILHVRD MSDPDNQAQS SDVMRILGDL GIDEAEAEKR LIEVWNKIDR LEPEVHDAMV QRAAGASNVV AVSAVSGEGV DTLMEEISRR LSGVMTETTI RLPVDKLALL PWLYDHAIVD GREDNEDGSI TLDLRLSETE AAELERRIGN GPKPPREDWE R // ID Q2KYA1_BORA1 Unreviewed; 368 AA. AC Q2KYA1; DT 07-MAR-2006, integrated into UniProtKB/TrEMBL. DT 07-MAR-2006, sequence version 1. DT 07-JUN-2017, entry version 73. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:CAJ49947.1}; GN OrderedLocusNames=BAV2337 {ECO:0000313|EMBL:CAJ49947.1}; OS Bordetella avium (strain 197N). OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Alcaligenaceae; Bordetella. OX NCBI_TaxID=360910 {ECO:0000313|EMBL:CAJ49947.1, ECO:0000313|Proteomes:UP000001977}; RN [1] {ECO:0000313|EMBL:CAJ49947.1, ECO:0000313|Proteomes:UP000001977} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=197N {ECO:0000313|EMBL:CAJ49947.1, RC ECO:0000313|Proteomes:UP000001977}; RX PubMed=16885469; DOI=10.1128/JB.01927-05; RA Sebaihia M., Preston A., Maskell D.J., Kuzmiak H., Connell T.D., RA King N.D., Orndorff P.E., Miyamoto D.M., Thomson N.R., Harris D., RA Goble A., Lord A., Murphy L., Quail M.A., Rutter S., Squares R., RA Squares S., Woodward J., Parkhill J., Temple L.M.; RT "Comparison of the genome sequence of the poultry pathogen Bordetella RT avium with those of B. bronchiseptica, B. pertussis, and B. RT parapertussis reveals extensive diversity in surface structures RT associated with host interaction."; RL J. Bacteriol. 188:6002-6015(2006). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AM167904; CAJ49947.1; -; Genomic_DNA. DR RefSeq; WP_012417998.1; NC_010645.1. DR ProteinModelPortal; Q2KYA1; -. DR STRING; 360910.BAV2337; -. DR EnsemblBacteria; CAJ49947; CAJ49947; BAV2337. DR KEGG; bav:BAV2337; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR BioCyc; BAVI360910:GCKI-2357-MONOMER; -. DR Proteomes; UP000001977; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000001977}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000001977}. FT DOMAIN 190 354 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 156 183 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 368 AA; 40377 MW; 7B3C483F2B552F5F CRC64; MRALIISVDL GDPDHQAHAE EFVMLAEGAG AEIVATLNAR RDRPDAKFFI GSGKVEEGVA LAGASLADIV LFDQPLSPAQ QRNLEREFNL RVVDRVALIL DIFALRAKSH EGKLQVELAQ LQHLSTRLTR LWSHLERQRG GIGMRGPGES QLEMDRRMIG AKVKMLRERL ERVERQRVTQ RRARARGGAL SVSLVGYTNA GKSTLFNALT RAGAYAADQL FATLDTTTRR FWIEGAGSVV LSDTVGFIRE LPPNLIAAFR ATLEETVHAD LLLHVVDAAS PQREEQIFEV NKVLAEIGAA DIPTILVYNK IDRAGLEPRV ERDAHGTIAR VFVSATERAG LDALRGAIAE IGQIVGNNAS NHQNLQPE // ID Q2LWR4_SYNAS Unreviewed; 555 AA. AC Q2LWR4; DT 21-FEB-2006, integrated into UniProtKB/TrEMBL. DT 21-FEB-2006, sequence version 1. DT 07-JUN-2017, entry version 76. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=SYN_01762 {ECO:0000313|EMBL:ABC78528.1}; OS Syntrophus aciditrophicus (strain SB). OC Bacteria; Proteobacteria; Deltaproteobacteria; Syntrophobacterales; OC Syntrophaceae; Syntrophus. OX NCBI_TaxID=56780 {ECO:0000313|EMBL:ABC78528.1, ECO:0000313|Proteomes:UP000001933}; RN [1] {ECO:0000313|Proteomes:UP000001933} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SB {ECO:0000313|Proteomes:UP000001933}; RA Gunsalus R., Rohlin L., Kim U., Krupp R., Bhattacharyya A., RA Campbell J., Mclerney M., Moutakki H., Rio-Hernandez L.; RT "The genome of the syntrophic bacterium Syntrophus aciditrophicus: RT Life dependent on negative change in electrical potential."; RL Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000252; ABC78528.1; -; Genomic_DNA. DR RefSeq; WP_011418547.1; NC_007759.1. DR ProteinModelPortal; Q2LWR4; -. DR STRING; 56780.SYN_01762; -. DR EnsemblBacteria; ABC78528; ABC78528; SYN_01762. DR KEGG; sat:SYN_01762; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; EREVIIT; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000001933; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000001933}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000001933}. FT DOMAIN 387 552 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 555 AA; 62386 MW; 06EC116B0DA87041 CRC64; MRLFQKELST IQKIYGNLTG LKPIQIKRLE QFYRRRVPPD AIVTQEMARQ LTELSRELNR QLGVLLSRRG EVACVIVGTH KGILIPSLEG FRSSSARFKG LRLIHTHLGP DPLNAEDLSD LALLRLDLIC AVETGPDGLP GIVHTAHLIP ENPDGGYWRV EPPQRISDLK ADFLSFIGAL ENEFARTQRS RKVDSADRAI LLRVETNPLF DSEGSLEELR ELAHSCNVEV FDRIIQHRPQ LDPRYLLGKG KLADVIIKAL QIGANLLIFD HELTPAQVRS IADFTEMKVI DRTQVILDIF AQRAHSREGK IQVELAQLKY LLPRLATRHT GMSRLTGGIG GRGPGETKLE VNRRRVRDRI LHLEEDIRNI EKARGQRRLK RERTGLPVIS IVGYTNAGKS TLLNTLTKSR VFTEDRLFAT LDPKSSRLRF PRDAEAVITD TVGFIRDLPA DLFAAFKATL EELYEADILL HVIDVSNPGF ESHIAAVEKI LEEIGIQGKA TLRVFNKADR FADKALLSTL CRRFNAIAVS ALQPDSLGPL MEQLEEIVSP PDETR // ID Q2NAE8_ERYLH Unreviewed; 433 AA. AC Q2NAE8; DT 07-FEB-2006, integrated into UniProtKB/TrEMBL. DT 07-FEB-2006, sequence version 1. DT 07-JUN-2017, entry version 88. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=ELI_06255 {ECO:0000313|EMBL:ABC63343.1}; OS Erythrobacter litoralis (strain HTCC2594). OC Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales; OC Erythrobacteraceae; Erythrobacter. OX NCBI_TaxID=314225 {ECO:0000313|EMBL:ABC63343.1, ECO:0000313|Proteomes:UP000008808}; RN [1] {ECO:0000313|Proteomes:UP000008808} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=HTCC2594 {ECO:0000313|Proteomes:UP000008808}; RX PubMed=19168610; DOI=10.1128/JB.00026-09; RA Oh H.M., Giovannoni S.J., Ferriera S., Johnson J., Cho J.C.; RT "Complete genome sequence of Erythrobacter litoralis HTCC2594."; RL J. Bacteriol. 191:2419-2420(2009). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000157; ABC63343.1; -; Genomic_DNA. DR RefSeq; WP_011414179.1; NC_007722.1. DR ProteinModelPortal; Q2NAE8; -. DR STRING; 314225.ELI_06255; -. DR EnsemblBacteria; ABC63343; ABC63343; ELI_06255. DR KEGG; eli:ELI_06255; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000008808; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000008808}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000008808}. FT DOMAIN 202 377 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 433 AA; 47938 MW; B40CC2FBB6561889 CRC64; MGEVSRGARA LVVCPDIRRE SYDLDPDARL EEITGLTLAI GIEVIESYIL PIRQVQPNTL LGSGQVERVS TDCELHEIEL VVIDGALSPI QQRNLEEKFK RKVIDRTGLI LEIFGERAAT AEGRLQVELA HLDYQQSRLV RSWTHLERQR GGFGFLGGPG ETQIEADRRM IRQRMGRLRK ELEQVRKTRG LHRERRGRAP WPVIALVGYT NAGKSTLFNR LTGAEVMAED LLFATLDPTM RAIALPGVEK AILSDTVGFI SDLPTQLVAA FRATLEEVTA ADLILHVRDI ANSSSAAQKS QVLEVLQDLG VIDGEDGESS IPILEVWNKW DLLDQDSAEE LSGVAEGDDS VIPVSAATGW HVDVLQERLG QVLTAQAQTR EFLLSVSEGR KIAWLHQHGD VLADEDGGEG DEGPMRKLTV RLNPKELGQY ETL // ID Q2NW62_SODGM Unreviewed; 424 AA. AC Q2NW62; DT 07-FEB-2006, integrated into UniProtKB/TrEMBL. DT 07-FEB-2006, sequence version 1. DT 30-AUG-2017, entry version 79. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=SG0338 {ECO:0000313|EMBL:BAE73613.1}; OS Sodalis glossinidius (strain morsitans). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; OC Pectobacteriaceae; Sodalis. OX NCBI_TaxID=343509 {ECO:0000313|EMBL:BAE73613.1, ECO:0000313|Proteomes:UP000001932}; RN [1] {ECO:0000313|EMBL:BAE73613.1, ECO:0000313|Proteomes:UP000001932} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=morsitans {ECO:0000313|Proteomes:UP000001932}; RX PubMed=16365377; DOI=10.1101/gr.4106106; RA Toh H., Weiss B.L., Perkin S.A.H., Yamashita A., Oshima K., RA Hattori M., Aksoy S.; RT "Massive genome erosion and functional adaptations provide insights RT into the symbiotic lifestyle of Sodalis glossinidius in the tsetse RT host."; RL Genome Res. 16:149-156(2006). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AP008232; BAE73613.1; -; Genomic_DNA. DR RefSeq; WP_011410201.1; NC_007712.1. DR ProteinModelPortal; Q2NW62; -. DR STRING; 343509.SG0338; -. DR EnsemblBacteria; BAE73613; BAE73613; SG0338. DR KEGG; sgl:SG0338; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000001932; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000001932}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000001932}. FT DOMAIN 196 363 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 424 AA; 47692 MW; 7339BC5DB2097C38 CRC64; MFDRYDAGEQ AILVHIFFSQ DKDMEDLQEF ESLVSSAGVA ALHVVTGSRK APHPKYFVGE GKAEEIAEAV KTSSASVVLF DHALSPAQER NLERLCECRV IDRTGLILDI FAQRARTHEG KLQVELAQLR HLATRLVRGW THLERQKGGI GLRGPGETQL ETDRRLLRNR ISQILSRLEK VEKQREQGRR ARADVPTVSL VGYTNAGKST LFNRMTEAGV YAADQLFATL DPTLRRINVG DVGDTVLADT VGFIRHLPHD LVAAFKATLQ ETRQATLLLH IVDAADTRIS ENIDAVDQVL AEIEANDIPT LLVMNKIDLL DDFVPRIDRD EENRPVRVWL SAHNGEGMAL LMQALTERLA GEIARHELRL PPQAGRLRSR FYQLQAIEKE WVEEDGSMGL VVRLPIIGWH RLCKQEMALV DYLV // ID Q2R1U5_ORYSJ Unreviewed; 552 AA. AC Q2R1U5; DT 24-JAN-2006, integrated into UniProtKB/TrEMBL. DT 24-JAN-2006, sequence version 1. DT 30-AUG-2017, entry version 88. DE SubName: Full=Os11g0592700 protein {ECO:0000313|EMBL:BAT14691.1}; DE SubName: Full=Small GTP-binding protein domain containing protein, expressed {ECO:0000313|EMBL:ABA94562.1}; GN Name=Os11g0592700 {ECO:0000313|EMBL:BAT14691.1}; GN OrderedLocusNames=LOC_Os11g38020 {ECO:0000313|EMBL:ABA94562.1}; GN ORFNames=OSNPB_110592700 {ECO:0000313|EMBL:BAT14691.1}; OS Oryza sativa subsp. japonica (Rice). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; BOP clade; OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa. OX NCBI_TaxID=39947 {ECO:0000313|EMBL:ABA94562.1}; RN [1] {ECO:0000313|EMBL:ABA94562.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16188032; DOI=10.1186/1741-7007-3-20; RG The rice chromosomes 11 and 12 sequencing consortia; RT "The sequence of rice chromosomes 11 and 12, rich in disease RT resistance genes and recent gene duplications."; RL BMC Biol. 3:20-20(2005). RN [2] {ECO:0000313|Proteomes:UP000059680} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Nipponbare {ECO:0000313|Proteomes:UP000059680}; RX PubMed=16100779; DOI=10.1038/nature03895; RG International rice genome sequencing project (IRGSP); RT "The map-based sequence of the rice genome."; RL Nature 436:793-800(2005). RN [3] {ECO:0000313|EMBL:ABA94562.1} RP NUCLEOTIDE SEQUENCE. RA Buell C.R., Wing R.A., McCombie W.A., Ouyang S.; RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases. RN [4] {ECO:0000313|EMBL:ABA94562.1} RP NUCLEOTIDE SEQUENCE. RA Buell R.; RL Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases. RN [5] {ECO:0000313|EMBL:BAT14691.1} RP NUCLEOTIDE SEQUENCE. RX PubMed=23299411; DOI=10.1093/pcp/pcs183; RA Sakai H., Lee S.S., Tanaka T., Numa H., Kim J., Kawahara Y., RA Wakimoto H., Yang C.C., Iwamoto M., Abe T., Yamada Y., Muto A., RA Inokuchi H., Ikemura T., Matsumoto T., Sasaki T., Itoh T.; RT "Rice Annotation Project Database (RAP-DB): an integrative and RT interactive database for rice genomics."; RL Plant Cell Physiol. 54:E6-E6(2013). RN [6] {ECO:0000313|EMBL:BAT14691.1, ECO:0000313|Proteomes:UP000059680} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Nipponbare {ECO:0000313|Proteomes:UP000059680}; RX PubMed=24280374; DOI=10.1186/1939-8433-6-4; RA Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., RA McCombie W.R., Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., RA Childs K.L., Davidson R.M., Lin H., Quesada-Ocampo L., RA Vaillancourt B., Sakai H., Lee S.S., Kim J., Numa H., Itoh T., RA Buell C.R., Matsumoto T.; RT "Improvement of the Oryza sativa Nipponbare reference genome using RT next generation sequence and optical map data."; RL Rice 6:4-4(2013). RN [7] {ECO:0000313|EMBL:BAT14691.1} RP NUCLEOTIDE SEQUENCE. RA Millard Andrew; RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; DP000010; ABA94562.1; -; Genomic_DNA. DR EMBL; AP014967; BAT14691.1; -; Genomic_DNA. DR RefSeq; XP_015615566.1; XM_015760080.1. DR STRING; 39947.LOC_Os11g38020.1; -. DR PaxDb; Q2R1U5; -. DR EnsemblPlants; OS11T0592700-00; OS11T0592700-00; OS11G0592700. DR GeneID; 4350828; -. DR Gramene; OS11T0592700-00; OS11T0592700-00; OS11G0592700. DR KEGG; osa:4350828; -. DR eggNOG; KOG0410; Eukaryota. DR eggNOG; COG2262; LUCA. DR KO; K03665; -. DR OMA; VILEIFH; -. DR OrthoDB; EOG093609UJ; -. DR Proteomes; UP000059680; Chromosome 11. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000059680}; KW Reference proteome {ECO:0000313|Proteomes:UP000059680}. FT DOMAIN 328 493 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 294 321 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 552 AA; 60736 MW; 9BD066B73EB83E26 CRC64; MRAACFFTGA AATASLPLPS TSASASSCCQ RRPASLRCSR PRRSFGVARA LDERLVEAAP PAETEVEEPG VADGGGEGEG EVEDSAPSGE EEEEEEPARA PVRSRRRQEE EEEEAAPGHD RFKLINGKEI FQEKAYLVGV ECKRSGGSMF SIEESLEELE QLADTAGLMV VGSTYQKLST PNPRTYIGSG KVAEIKSAIH AHDVETVIFD DELSPGQLRN LEKSFGGGVR VCDRTALILD IFNQRAATHE AALQVTLAQM EYQLPRLTKM WSHLERQSGG QVKGMGEKQI EVDKRILRTQ ISALRKELES VRKHRKLYRN RRQSVPIPVV SLVGYTNAGK STLLNRLTGA DVLAEDKLFA TLDPTTRRVL MKNGTEFLLT DTVGFIQKLP TMLVAAFRAT LEEISESSVI VHLVDISHPL AQQQIDAVDK VLKELDIESI PKLVVWNKID NTDDTLRVKE EAEKQGIICI SAINGDGLEE FCNAIQAKLK DSLVPIEAFV PYDKGELLSD IHKVGMVEKT EYTENGTFVK AHVPLPLARL LTPLRQQVAA VS // ID Q2RTR0_RHORT Unreviewed; 418 AA. AC Q2RTR0; DT 24-JAN-2006, integrated into UniProtKB/TrEMBL. DT 24-JAN-2006, sequence version 1. DT 07-JUN-2017, entry version 94. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Rru_A1685 {ECO:0000313|EMBL:ABC22485.1}; OS Rhodospirillum rubrum (strain ATCC 11170 / ATH 1.1.1 / DSM 467 / LMG OS 4362 / NCIB 8255 / S1). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales; OC Rhodospirillaceae; Rhodospirillum. OX NCBI_TaxID=269796 {ECO:0000313|EMBL:ABC22485.1, ECO:0000313|Proteomes:UP000001929}; RN [1] {ECO:0000313|Proteomes:UP000001929} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 11170 / ATH 1.1.1 / DSM 467 / LMG 4362 / NCIB 8255 / S1 RC {ECO:0000313|Proteomes:UP000001929}; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., RA Hammon N., Israni S., Pitluck S., Munk A.C., Brettin T., Bruce D., RA Han C., Tapia R., Gilna P., Schmutz J., Larimer F., Land M., RA Kyrpides N., Mavrommatis K., Richardson P., Zhang Y., Roberts G., RA Reslewic S., Zhou S., Schwartz D.C.; RT "Complete sequence of the chromosome of Rhodospirillum rubrum ATCC RT 11170."; RL Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000230; ABC22485.1; -; Genomic_DNA. DR RefSeq; WP_011389375.1; NC_007643.1. DR RefSeq; YP_426772.1; NC_007643.1. DR ProteinModelPortal; Q2RTR0; -. DR STRING; 269796.Rru_A1685; -. DR EnsemblBacteria; ABC22485; ABC22485; Rru_A1685. DR GeneID; 3835105; -. DR KEGG; rru:Rru_A1685; -. DR PATRIC; fig|269796.9.peg.1763; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; FNNHAHV; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000001929; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000001929}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000001929}. FT DOMAIN 192 363 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 418 AA; 45797 MW; C2680B04E8513315 CRC64; MLHPFLRKGR PAARSPEARL AEANGLAEAI SLDVALSETV PMARVVPATY IGGGAVERMA GIIAAEAISL VVVDTQLSPI QQRNLERAWA CKVIDRTGLI LEIFGERART AEGQMQVELA HLTYQRSRLV RSWTHLERQR GGVGFLGGPG ETQIELDRRL IGDRITRLRK DLEEVRRTRG LHREARARVP YPVVALVGYT NSGKSTLFNR LTAGGVLAKD MLFATLDPTM RSLDLPSGRK VILSDTVGFV SDLPHELVAA FRATLEEVKA ADVIVHVRDI AGIDSDAQKA DVEVVLREME LDERVESGLI EALNKIDLLD SERQAQLVED TAGRDTLVPV SAVTGAGTDA LLARIDARLA ESRIVLGLSI PLSDGATLAW VYRKGEVLER HDDEEQAHLT VRLDPADIGR LDPRLRTP // ID Q2RZX0_SALRD Unreviewed; 427 AA. AC Q2RZX0; DT 24-JAN-2006, integrated into UniProtKB/TrEMBL. DT 24-JAN-2006, sequence version 1. DT 07-JUN-2017, entry version 97. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=SRU_2412 {ECO:0000313|EMBL:ABC43564.1}; OS Salinibacter ruber (strain DSM 13855 / M31). OC Bacteria; Bacteroidetes; Bacteroidetes Order II. Incertae sedis; OC Rhodothermaceae; Salinibacter. OX NCBI_TaxID=309807 {ECO:0000313|EMBL:ABC43564.1, ECO:0000313|Proteomes:UP000008674}; RN [1] {ECO:0000313|EMBL:ABC43564.1, ECO:0000313|Proteomes:UP000008674} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 13855 / M31 {ECO:0000313|Proteomes:UP000008674}; RX PubMed=16330755; DOI=10.1073/pnas.0509073102; RA Mongodin E.F., Nelson K.E., Daugherty S., Deboy R.T., Wister J., RA Khouri H., Weidman J., Walsh D.A., Papke R.T., Sanchez Perez G., RA Sharma A.K., Nesbo C.L., MacLeod D., Bapteste E., Doolittle W.F., RA Charlebois R.L., Legault B., Rodriguez-Valera F.; RT "The genome of Salinibacter ruber: convergence and gene exchange among RT hyperhalophilic bacteria and archaea."; RL Proc. Natl. Acad. Sci. U.S.A. 102:18147-18152(2005). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000159; ABC43564.1; -; Genomic_DNA. DR RefSeq; WP_011405129.1; NC_007677.1. DR RefSeq; YP_446511.1; NC_007677.1. DR ProteinModelPortal; Q2RZX0; -. DR STRING; 309807.SRU_2412; -. DR EnsemblBacteria; ABC43564; ABC43564; SRU_2412. DR GeneID; 3852501; -. DR KEGG; sru:SRU_2412; -. DR PATRIC; fig|309807.25.peg.2512; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000008674; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000008674}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000008674}. FT DOMAIN 174 340 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 427 AA; 48102 MW; 053870CF869139F5 CRC64; MRDHLNELEH LARTAGADVT DRLTQSLNSP SPATFIGSGK VKELARLTKE RDSDLVISDD ELSPVQVKNI EKKIDCKLLD RTGLILDIFA SRAQTRAAKT QVELAQLGYL RSRLTRRWTH LSRQEGGIGT KGPGEKQIEM DRRIIDKRMA KLREKLDEID RQRTTQRKGR EGYTTASLVG YTNAGKSTLL NALADEDLEA EDRLFATLDA TTRTVELDSN KEVLMSDTVG FIRKLPHRLI ESFRSTLDEV RESDVLIHVV DVTHPNYEEQ MRVVAETLGE LEARDKPTLV VFNKIDAMED RTLLRRLRRN HPDAVFASAL RGIGLETLKE DLLDLIEQDY VERVAYIPVS EPEVIAQVHR LGDVIEESYE YAENGGLESL NGEVEGAQAV ARIHFRAAPR NDARLQEALD PRGALRPAET EEPVLNA // ID Q2SBC3_HAHCH Unreviewed; 430 AA. AC Q2SBC3; DT 24-JAN-2006, integrated into UniProtKB/TrEMBL. DT 24-JAN-2006, sequence version 1. DT 30-AUG-2017, entry version 93. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=HCH_05382 {ECO:0000313|EMBL:ABC32051.1}; OS Hahella chejuensis (strain KCTC 2396). OC Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales; OC Hahellaceae; Hahella. OX NCBI_TaxID=349521 {ECO:0000313|EMBL:ABC32051.1, ECO:0000313|Proteomes:UP000000238}; RN [1] {ECO:0000313|EMBL:ABC32051.1, ECO:0000313|Proteomes:UP000000238} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=KCTC 2396 {ECO:0000313|EMBL:ABC32051.1, RC ECO:0000313|Proteomes:UP000000238}; RX PubMed=16352867; DOI=10.1093/nar/gki1016; RA Jeong H., Yim J.H., Lee C., Choi S.-H., Park Y.K., Yoon S.H., RA Hur C.-G., Kang H.-Y., Kim D., Lee H.H., Park K.H., Park S.-H., RA Park H.-S., Lee H.K., Oh T.K., Kim J.F.; RT "Genomic blueprint of Hahella chejuensis, a marine microbe producing RT an algicidal agent."; RL Nucleic Acids Res. 33:7066-7073(2005). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000155; ABC32051.1; -; Genomic_DNA. DR RefSeq; WP_011399115.1; NC_007645.1. DR ProteinModelPortal; Q2SBC3; -. DR STRING; 349521.HCH_05382; -. DR EnsemblBacteria; ABC32051; ABC32051; HCH_05382. DR KEGG; hch:HCH_05382; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000000238; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000000238}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000000238}. FT DOMAIN 198 365 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 430 AA; 48571 MW; EAE0EF130190D36C CRC64; MFERPKAGER AVLVHLDMLE EKDREDPREL TELALSAGAE PVALVTGTRN QPSPRYFVGS GKLEEIRVAV IEHEAEVVLF NHSLTPSQER NLEKDLQVRV LDRTGLILDI FAQRARTHEG KLQVELAQLE HLSTRLVRGW THLERQKGGI GLRGPGETQL ETDRRLIRGR IKSIHKRLEK VRKQREQGRR ARRRAEVPTI SLVGYTNAGK STLFNRISLS DVYAADQLFA TLDPTLRRIN LENYGPVVLA DTVGFIRHLP HKLVDAFRAT LEETCNASLL LHVVDASDPK RRENIEQVEE VLKEIGADDI PSLFVFNKVD RLEVAEPRLE LNENGEPIRV WVSAVTGEGL KLLEQATGKL LGADMVDETL CIPPALGRLR ARLYEREAVL SEEVREDGSF SVHIKMPKTD WLQLAHKEGV KLEQLTGQVC // ID Q2W4P8_MAGSA Unreviewed; 435 AA. AC Q2W4P8; DT 10-JAN-2006, integrated into UniProtKB/TrEMBL. DT 10-JAN-2006, sequence version 1. DT 07-JUN-2017, entry version 80. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=amb2373 {ECO:0000313|EMBL:BAE51177.1}; OS Magnetospirillum magneticum (strain AMB-1 / ATCC 700264). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales; OC Rhodospirillaceae; Magnetospirillum. OX NCBI_TaxID=342108 {ECO:0000313|EMBL:BAE51177.1, ECO:0000313|Proteomes:UP000007058}; RN [1] {ECO:0000313|EMBL:BAE51177.1, ECO:0000313|Proteomes:UP000007058} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=AMB-1 / ATCC 700264 {ECO:0000313|Proteomes:UP000007058}; RX PubMed=16303747; DOI=10.1093/dnares/dsi002; RA Matsunaga T., Okamura Y., Fukuda Y., Wahyudi A.T., Murase Y., RA Takeyama H.; RT "Complete genome sequence of the facultative anaerobic magnetotactic RT bacterium Magnetospirillum sp. strain AMB-1."; RL DNA Res. 12:157-166(2005). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AP007255; BAE51177.1; -; Genomic_DNA. DR RefSeq; WP_011384769.1; NC_007626.1. DR ProteinModelPortal; Q2W4P8; -. DR STRING; 342108.amb2373; -. DR EnsemblBacteria; BAE51177; BAE51177; amb2373. DR KEGG; mag:amb2373; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000007058; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000007058}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000007058}. FT DOMAIN 206 377 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 172 202 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 435 AA; 47967 MW; 45B88B8CD03AC9A2 CRC64; MGEPGSQKTA PSRAMVVHPA FKGGEGNRLP EARLAEAVGL AGAINLDIVA AEAVNVSKVR PATLIGKGAV ERLAELVEER DIALAVVDGH LTPVQQRNLE KAWGCKVIDR TGLILEIFGA RARTREGTLQ VELAALSYQR SRLVRSWTHL ERQRGGFGFL GGPGETQIEA DRRMIGERIV KLERELEDVK RTRDLHRKAR RRVPYPIVAL VGYTNAGKST LFNQLTRAEV LAKDMLFATL DPTMRDLVLP SGRKIILSDT VGFISDLPHE LVAAFRATLE EVLEADVVVH VRDVSHPDTE AQAADVDTVL KELGLAEVVD RGLVEALNKI DLLDDERRQE VLNQARRREG VMALSAVTGQ GVDELLAELD RRLGHARETI DVALSLGDGA SIAWLYRHGE VVARRDDEAQ AFMRVKLDPA DVKRFHQRKA EGRGH // ID Q2YBW7_NITMU Unreviewed; 394 AA. AC Q2YBW7; DT 20-DEC-2005, integrated into UniProtKB/TrEMBL. DT 20-DEC-2005, sequence version 1. DT 07-JUN-2017, entry version 99. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Nmul_A0446 {ECO:0000313|EMBL:ABB73754.1}; GN ORFNames=SAMN05216403_101169 {ECO:0000313|EMBL:SEF41127.1}; OS Nitrosospira multiformis (strain ATCC 25196 / NCIMB 11849 / C 71). OC Bacteria; Proteobacteria; Betaproteobacteria; Nitrosomonadales; OC Nitrosomonadaceae; Nitrosospira. OX NCBI_TaxID=323848 {ECO:0000313|EMBL:ABB73754.1, ECO:0000313|Proteomes:UP000002718}; RN [1] {ECO:0000313|EMBL:ABB73754.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 25196 {ECO:0000313|EMBL:ABB73754.1}; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., RA Hammon N., Israni S., Pitluck S., Chain P., Malfatti S., Shin M., RA Vergez L., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., RA Lykidis A., Richardson P.; RT "Complete sequence of Chromosome 1 of Nitrosospira multiformis ATCC RT 25196."; RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Proteomes:UP000002718} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 25196 / NCIMB 11849 / C 71 RC {ECO:0000313|Proteomes:UP000002718}; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., RA Hammon N., Israni S., Pitluck S., Chain P., Malfatti S., Shin M., RA Vergez L., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., RA Lykidis A., Richardson P.; RT "Complete sequence of chromosome 1 of Nitrosospira multiformis ATCC RT 25196."; RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases. RN [3] {ECO:0000313|EMBL:ABB73754.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 25196 {ECO:0000313|EMBL:ABB73754.1}; RX PubMed=18390676; DOI=10.1128/AEM.02722-07; RA Norton J.M., Klotz M.G., Stein L.Y., Arp D.J., Bottomley P.J., RA Chain P.S., Hauser L.J., Land M.L., Larimer F.W., Shin M.W., RA Starkenburg S.R.; RT "Complete genome sequence of Nitrosospira multiformis, an ammonia- RT oxidizing bacterium from the soil environment."; RL Appl. Environ. Microbiol. 74:3559-3572(2008). RN [4] {ECO:0000313|EMBL:SEF41127.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=Nl13 {ECO:0000313|EMBL:SEF41127.1}; RA de Groot N.N.; RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000103; ABB73754.1; -; Genomic_DNA. DR EMBL; FNVK01000001; SEF41127.1; -; Genomic_DNA. DR RefSeq; WP_011379808.1; NC_007614.1. DR STRING; 323848.Nmul_A0446; -. DR DNASU; 3785914; -. DR EnsemblBacteria; ABB73754; ABB73754; Nmul_A0446. DR KEGG; nmu:Nmul_A0446; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; FNNHAHV; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000002718; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000002718}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Hydrolase {ECO:0000313|EMBL:ABB73754.1}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000002718}. FT DOMAIN 206 379 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 172 199 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 394 AA; 43513 MW; DD9032BE1A4EB730 CRC64; MLDSSSGNAP DTHAAVDSAV LVSLDLNDSD SAENLEELRQ LAASDRLAIS AVVLGKRLRP DPATFAGSGK VDEIMGAVEQ TGASLVIFNH DLSPAQQRNL EQRLRRRVID RTSLILDIFA QRAKSHEGKL QVELAQLEHL ATRLVRGWTH LERQKGGIGL RGPGETQLET DRRLLGKRVK VLKEKLAKFE RQRALQRRAR RRAQVMSVSL VGYTNAGKST LFNRLTRGHT YVADQLFATL DATTRKLFIA DRGPLVLSDT VGFIRDLPHT LVAAFRATLE ETVQADLLLH VVDTSSSNRS EQIDEVNKVL KEIGADRIPQ ILVLNKTDLV DLPASSPGYQ RDEYGRIVQV RLSAKTGEGL EFINLALSEA LGERAALREP DNQSEAQDIT SGYH // ID Q2YPX0_BRUA2 Unreviewed; 472 AA. AC Q2YPX0; DT 07-FEB-2006, integrated into UniProtKB/TrEMBL. DT 07-FEB-2006, sequence version 1. DT 07-JUN-2017, entry version 80. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=BAB1_1133 {ECO:0000313|EMBL:CAJ11089.1}; OS Brucella abortus (strain 2308). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Brucellaceae; Brucella. OX NCBI_TaxID=359391 {ECO:0000313|EMBL:CAJ11089.1, ECO:0000313|Proteomes:UP000002719}; RN [1] {ECO:0000313|EMBL:CAJ11089.1, ECO:0000313|Proteomes:UP000002719} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=2308 {ECO:0000313|EMBL:CAJ11089.1, RC ECO:0000313|Proteomes:UP000002719}; RX PubMed=16299333; DOI=10.1128/IAI.73.12.8353-8361.2005; RG Microbial Genomics Group; RG Lawrence Livermore National Laboratory; RG and the Genome Analysis Group; RG Oak Ridge National Laboratory; RA Chain P., Comerci D.J., Tolmasky M.E., Larimer F.W., Malfatti S., RA Vergez L.M., Aguero F., Land M.L., Ugalde R.A., Garcia E.; RT "Whole-genome analyses of speciation events in pathogenic Brucellae."; RL Infect. Immun. 73:8353-8361(2005). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AM040264; CAJ11089.1; -; Genomic_DNA. DR RefSeq; WP_002964238.1; NZ_KN046823.1. DR ProteinModelPortal; Q2YPX0; -. DR EnsemblBacteria; CAJ11089; CAJ11089; BAB1_1133. DR KEGG; bmf:BAB1_1133; -. DR PATRIC; fig|359391.11.peg.33; -. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR Proteomes; UP000002719; Chromosome I. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000002719}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000002719}. FT DOMAIN 233 407 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 472 AA; 52108 MW; 1C74D3EB49ED690C CRC64; MSKPKDKKAA SLDGSKGFAL SEPEPTRAAV IVPVLPDRYN SGSAGEDGAR SQFQRSNEAR LEEAIGLARA IDLDIEHAEI AIVTNPRPAT LLGAGKAQSI AEVVKEKAIG LVVVDHALTP VQQRNLEKEW NAKVIDRTGL ILEIFGERAR TKEGALQVEL AHLNYQKGRL VRSWTHLERQ RGGGGFLGGP GETQIEADRR LLQEKILRIK RELETVVRTR ALHRQKRRKV PHPIVALVGY TNAGKSTLFN RMTGAQVLAE DMLFATLDPT LRRIRLPHGE TVILSDTVGF ISNLPHHLVA AFRATLEEVV EADLILHVRD ISDPDNAAQA EDVENILAGL GIEPQDHARV VEVWNKIDNL DESAREAALR LAAVGSEEGR PIPVSAITGE GVDRLLSLIE TRIAGALGSV DLVLSPFDLH LLDWIYQHGS DVQRENLEDG SVRIKARLTE IARRMLDEKR GIRPEKPEID WE // ID Q316G9_DESAG Unreviewed; 490 AA. AC Q316G9; DT 06-DEC-2005, integrated into UniProtKB/TrEMBL. DT 06-DEC-2005, sequence version 1. DT 05-JUL-2017, entry version 95. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Dde_0376 {ECO:0000313|EMBL:ABB37177.1}; OS Desulfovibrio alaskensis (strain G20) (Desulfovibrio desulfuricans OS (strain G20)). OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfovibrionales; OC Desulfovibrionaceae; Desulfovibrio. OX NCBI_TaxID=207559 {ECO:0000313|EMBL:ABB37177.1, ECO:0000313|Proteomes:UP000002710}; RN [1] {ECO:0000313|EMBL:ABB37177.1, ECO:0000313|Proteomes:UP000002710} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=G20 {ECO:0000313|EMBL:ABB37177.1, RC ECO:0000313|Proteomes:UP000002710}; RX PubMed=21685289; DOI=10.1128/JB.05400-11; RA Hauser L.J., Land M.L., Brown S.D., Larimer F., Keller K.L., RA Rapp-Giles B.J., Price M.N., Lin M., Bruce D.C., Detter J.C., RA Tapia R., Han C.S., Goodwin L.A., Cheng J.F., Pitluck S., Copeland A., RA Lucas S., Nolan M., Lapidus A.L., Palumbo A.V., Wall J.D.; RT "Complete genome sequence and updated annotation of Desulfovibrio RT alaskensis G20."; RL J. Bacteriol. 193:4268-4269(2011). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000112; ABB37177.1; -; Genomic_DNA. DR ProteinModelPortal; Q316G9; -. DR STRING; 207559.Dde_0376; -. DR EnsemblBacteria; ABB37177; ABB37177; Dde_0376. DR KEGG; dde:Dde_0376; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; EREVIIT; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000002710; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000002710}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000002710}. FT DOMAIN 323 489 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 104 131 {ECO:0000256|SAM:Coils}. FT COILED 282 309 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 490 AA; 54345 MW; 74CD56ED3200AC33 CRC64; MLDRQGRVSL VIVGDTGSIY IPELPRARTG AGRLRGLRLL HTHLTDSLLS QEDLMDMLFL RLDDVGVLTV DQHGGPASFQ HAHLLPGGTQ PYMVHDPQGW DRVITDFTAQ AQALEEELSR ITADARETGS ESGRAVLVSV SPDPRSVQES SLAELAELAD TAGLTVAGTM VQRVRQLNYK FILGKGKLAE LEVLALTANA GVILFDGELS PAQLHNLADI TERKVIDRTQ LILDIFAQRA STRAGKLQVE LAQLQYTQPR LTGKNRAMDR LAGGIGGRGP GETKLETDRR KVRERIARIK QDLKALRTQR GFTRGRRAKA RVPVASLVGY TNAGKSTLLN TLTNADVLAE DKLFATLDTT TRRLRFPQER ELIVTDTVGF IRSLPKELKE AFRATLEELE AADLLLHVAD AGHPELEMQL RAVEEILDEL ELQDIPRLLV LNKWETLDDE TRLALAALYP AAIRVSARTR LGLDDLTAEI IRRIDWERML // ID Q31GP1_THICR Unreviewed; 436 AA. AC Q31GP1; DT 06-DEC-2005, integrated into UniProtKB/TrEMBL. DT 06-DEC-2005, sequence version 1. DT 07-JUN-2017, entry version 93. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Tcr_1087 {ECO:0000313|EMBL:ABB41682.1}; OS Thiomicrospira crunogena (strain XCL-2). OC Bacteria; Proteobacteria; Gammaproteobacteria; Thiotrichales; OC Piscirickettsiaceae; Thiomicrospira. OX NCBI_TaxID=317025 {ECO:0000313|EMBL:ABB41682.1, ECO:0000313|Proteomes:UP000002713}; RN [1] {ECO:0000313|Proteomes:UP000002713} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=XCL-2 {ECO:0000313|Proteomes:UP000002713}; RX PubMed=17105352; DOI=10.1371/journal.pbio.0040383; RA Scott K.M., Sievert S.M., Abril F.N., Ball L.A., Barrett C.J., RA Blake R.A., Boller A.J., Chain P.S.G., Clark J.A., Davis C.R., RA Detter C., Do K.F., Dobrinski K.P., Faza B.I., Fitzpatrick K.A., RA Freyermuth S.K., Harmer T.L., Hauser L.J., Huegler M., Kerfeld C.A., RA Klotz M.G., Kong W.W., Land M., Lapidus A., Larimer F.W., Longo D.L., RA Lucas S., Malfatti S.A., Massey S.E., Martin D.D., McCuddin Z., RA Meyer F., Moore J.L., Ocampo L.H. Jr., Paul J.H., Paulsen I.T., RA Reep D.K., Ren Q., Ross R.L., Sato P.Y., Thomas P., Tinkham L.E., RA Zeruth G.T.; RT "The genome of deep-sea vent chemolithoautotroph Thiomicrospira RT crunogena XCL-2."; RL PLoS Biol. 4:1-17(2006). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000109; ABB41682.1; -; Genomic_DNA. DR RefSeq; WP_011370509.1; NC_007520.2. DR ProteinModelPortal; Q31GP1; -. DR STRING; 317025.Tcr_1087; -. DR EnsemblBacteria; ABB41682; ABB41682; Tcr_1087. DR KEGG; tcx:Tcr_1087; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000002713; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000002713}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000002713}. FT DOMAIN 201 370 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 160 194 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 436 AA; 49047 MW; F5C12BDFC9EF1DDB CRC64; MELFGKLEQK QLEKAILVHV DFYHEADREV LEEFYELVDS AGAEVAELIT TKRQSPDPKF FIGKGKAEEI KAAVETHQAD VVIVNHALSP AQERNLSQFL DCQVLDRVGL ILDIFAQRAR SHEGKLQVEL AQLKRMSTRL VKGWSHLDRQ GGIGARGPGE TQLETDRRLV QGKIKQLEAR IEKVRQQRSL GRRSRKKSDL PTITIIGYTN AGKSTLFNQM TRASVYAEDR LFATLDSTLR KVHLPGAGPV IFADTVGFIR HIPHDLVAAF RSTLEETSEA DLLIHLVDAA DPHRAEKMTD VEEVIKEVGA EDVPQLTVFN KIDRLKDPEV QPHVDLNDEG LPERVWISAK ESEGIELMLD AVAAHFRGKF HTVELVLDVK AGKKRAELYT LGTILDEGFD EEGNSVFKMS LTENEWAHVQ QWKEVLSSKV LSDETV // ID Q31KE1_SYNE7 Unreviewed; 535 AA. AC Q31KE1; DT 06-DEC-2005, integrated into UniProtKB/TrEMBL. DT 06-DEC-2005, sequence version 1. DT 07-JUN-2017, entry version 71. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Synpcc7942_2448 {ECO:0000313|EMBL:ABB58478.1}; OS Synechococcus elongatus (strain PCC 7942) (Anacystis nidulans R2). OC Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; OC Synechococcus. OX NCBI_TaxID=1140 {ECO:0000313|EMBL:ABB58478.1, ECO:0000313|Proteomes:UP000002717}; RN [1] {ECO:0000313|Proteomes:UP000002717} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=PCC 7942 {ECO:0000313|Proteomes:UP000002717}; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., RA Hammon N., Israni S., Pitluck S., Schmutz J., Larimer F., Land M., RA Kyrpides N., Lykidis A., Richardson P.; RT "Complete sequence of chromosome 1 of Synechococcus elongatus PCC RT 7942."; RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000100; ABB58478.1; -; Genomic_DNA. DR RefSeq; WP_011378466.1; NC_007604.1. DR ProteinModelPortal; Q31KE1; -. DR STRING; 1140.Synpcc7942_2448; -. DR PRIDE; Q31KE1; -. DR EnsemblBacteria; ABB58478; ABB58478; Synpcc7942_2448. DR KEGG; syf:Synpcc7942_2448; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OrthoDB; POG091H0464; -. DR BioCyc; SYNEL:SYNPCC7942_2448-MONOMER; -. DR Proteomes; UP000002717; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000002717}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000002717}. FT DOMAIN 363 533 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 324 358 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 535 AA; 58727 MW; CFA7AD666EE21A33 CRC64; MRLSLDCLAT PEFAERLAAI SADIEQPITV YLDRRGHVTR VGVGNVRQTR IPPVELPRYG AGRLCGLRCL TTSLSPEPPD EGALTTMALQ RLDALIWLCV TRQGKTRRGG GATGYVAQTY LAHLLAHPDQ RWTVSPELDL EDLTQQPCVE FVEALEEELQ RGLTSQAVAE GRDRVLLVGV KTQGISDCRF QEGLLELQRL VETAGGEVAS ILQQKRLRPH PQTVVGEGKV AEVALAAQTL GVNLVAFDRD LSPAQARNLE REIGLRVVDR TEVILDIFAQ RAQSGAGKLQ VELAQLEYKL PRLTGQGQAL SRLGGGIGTR GPGETKLETE RRAIQRRITR LQRQVTELQA HRSRLRQHRQ TLPSIAIVGY TNAGKSTLLN ILTQAEVYAA DQLFATLDPT TRRLVLNANP GSEPDVVLLT DTVGFIHELP PPLVDAFRAT LEEVTEADAL LHLVDLSHPA WYAQIQSVMS ILREMPVTPG PILLAFNKID AATSETLAIA QAEYPQAVFL SASRGLGLET LRQRLGQLVH YARTH // ID Q328F2_SHIDS Unreviewed; 426 AA. AC Q328F2; DT 06-DEC-2005, integrated into UniProtKB/TrEMBL. DT 06-DEC-2005, sequence version 1. DT 30-AUG-2017, entry version 87. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:ABB64303.1}; GN OrderedLocusNames=SDY_4416 {ECO:0000313|EMBL:ABB64303.1}; OS Shigella dysenteriae serotype 1 (strain Sd197). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; OC Enterobacteriaceae; Shigella. OX NCBI_TaxID=300267 {ECO:0000313|EMBL:ABB64303.1, ECO:0000313|Proteomes:UP000002716}; RN [1] {ECO:0000313|EMBL:ABB64303.1, ECO:0000313|Proteomes:UP000002716} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Sd197 {ECO:0000313|EMBL:ABB64303.1, RC ECO:0000313|Proteomes:UP000002716}; RX PubMed=16275786; DOI=10.1093/nar/gki954; RA Yang F., Yang J., Zhang X., Chen L., Jiang Y., Yan Y., Tang X., RA Wang J., Xiong Z., Dong J., Xue Y., Zhu Y., Xu X., Sun L., Chen S., RA Nie H., Peng J., Xu J., Wang Y., Yuan Z., Wen Y., Yao Z., Shen Y., RA Qiang B., Hou Y., Yu J., Jin Q.; RT "Genome dynamics and diversity of Shigella species, the etiologic RT agents of bacillary dysentery."; RL Nucleic Acids Res. 33:6445-6458(2005). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000034; ABB64303.1; -; Genomic_DNA. DR RefSeq; WP_000460358.1; NC_007606.1. DR RefSeq; YP_405794.1; NC_007606.1. DR ProteinModelPortal; Q328F2; -. DR PRIDE; Q328F2; -. DR EnsemblBacteria; ABB64303; ABB64303; SDY_4416. DR GeneID; 3797378; -. DR KEGG; sdy:SDY_4416; -. DR PATRIC; fig|300267.13.peg.5214; -. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000002716; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000002716}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Hydrolase {ECO:0000313|EMBL:ABB64303.1}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Protease {ECO:0000313|EMBL:ABB64303.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000002716}. FT DOMAIN 198 365 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 164 191 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 426 AA; 48273 MW; 8B384798F2FEE33A CRC64; MFDRYDAGEQ AVLVHIYFTQ DKDMEDLQEF ESLVSSAGVE ALQVITGSRK APHPKYFVGE GKAVEIAEAV KATGASVVLF DHALSPAQER NLERLCECRV IDRTGLILDI FAQRARTHEG KLQVELAQLR HLATRLVRGW THLERQKGGI GLRGPGETQL ETDRRLLRNR IVQIQSRLER VEKQREQGRQ SRIKADVPTV SLVGYTNAGK STLFNRITEA RVYAADQLFA TLDPTLRRID VADVGETVLA DTVGFIRHLP HDLVAAFKAT LQETRQATLL LHVIDAADVR VQENIEAVNT VLEEIDAHEI PTLLVMNKID MLEDFEPCID RDEENKPIRV WLSAQTGAGI PQLFQALTER LSGEVAQHTL RLPPQEGRLR SRFYQLQAIE KEWMEEDGSV SLQVRMPIVD WRRLCKQEPA LIDYLI // ID Q38ZF9_LACSS Unreviewed; 423 AA. AC Q38ZF9; DT 22-NOV-2005, integrated into UniProtKB/TrEMBL. DT 22-NOV-2005, sequence version 1. DT 07-JUN-2017, entry version 80. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=LCA_0120 {ECO:0000313|EMBL:CAI54418.1}; OS Lactobacillus sakei subsp. sakei (strain 23K). OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; OC Lactobacillus. OX NCBI_TaxID=314315 {ECO:0000313|EMBL:CAI54418.1, ECO:0000313|Proteomes:UP000002707}; RN [1] {ECO:0000313|Proteomes:UP000002707} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=23K {ECO:0000313|Proteomes:UP000002707}; RX PubMed=16273110; DOI=10.1038/nbt1160; RA Chaillou S., Champomier-Verges M.-C., Cornet M., Crutz-Le Coq A.-M., RA Dudez A.-M., Martin V., Beaufils S., Darbon-Rongere E., Bossy R., RA Loux V., Zagorec M.; RT "The complete genome sequence of the meat-borne lactic acid bacterium RT Lactobacillus sakei 23K."; RL Nat. Biotechnol. 23:1527-1533(2005). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CR936503; CAI54418.1; -; Genomic_DNA. DR RefSeq; WP_011373832.1; NC_007576.1. DR ProteinModelPortal; Q38ZF9; -. DR STRING; 314315.LSA0120; -. DR EnsemblBacteria; CAI54418; CAI54418; LCA_0120. DR GeneID; 29638293; -. DR KEGG; lsa:LCA_0120; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; FNNHAHV; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000002707; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000002707}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000002707}. FT DOMAIN 199 369 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 423 AA; 47662 MW; 8E48C22783EE5437 CRC64; MQETKMAQKR VLITGVSNRQ TNFDYTMREL GELARADNLE VVGEVRQNID QASHRTYFGK GKVQEIKAEA AQADADIIVV NDELSPSQIR NLEKELEMSI LDRTQLILEI FASRAKTKEA QLQVAIAEAK YQLPRLHPSE NKLDQQGGGG STNRGAGETQ LELDRRLIEK RITKLKGELA QIDQQQEVQR RQRTKNAVPD VALVGYTNAG KSTTMNRILQ RLNPDTPEKQ VFEKDMLFAT LDTSVREIVL PNKQKFLLSD TVGFVTKLPH HLIQAFKSTL AEAADADLLI HVVDYSDPNY LDMMKTTQET LDSLGVKDIP VIEAYNKADL KPDTRYPEVD GTQIVYSARD EVAIDALIAL INKQLFEQYP TLDFLIPFTE GQAVAYLSER ANILEQSYEE EGTKIRAQIS PDLLGAVQKY VQE // ID Q39SJ8_GEOMG Unreviewed; 556 AA. AC Q39SJ8; DT 22-NOV-2005, integrated into UniProtKB/TrEMBL. DT 31-OCT-2012, sequence version 2. DT 07-JUN-2017, entry version 93. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Gmet_2557 {ECO:0000313|EMBL:ABB32776.2}; OS Geobacter metallireducens (strain GS-15 / ATCC 53774 / DSM 7210). OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfuromonadales; OC Geobacteraceae; Geobacter. OX NCBI_TaxID=269799 {ECO:0000313|EMBL:ABB32776.2, ECO:0000313|Proteomes:UP000007073}; RN [1] {ECO:0000313|EMBL:ABB32776.2, ECO:0000313|Proteomes:UP000007073} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=GS-15 / ATCC 53774 / DSM 7210 RC {ECO:0000313|Proteomes:UP000007073}; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., RA Hammon N., Israni S., Pitluck S., Di Bartolo G., Chain P., Schmutz J., RA Larimer F., Land M., Kyrpides N., Ivanova N., Richardson P.; RT "Complete sequence of Geobacter metallireducens GS-15."; RL Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000148; ABB32776.2; -; Genomic_DNA. DR STRING; 269799.Gmet_2557; -. DR EnsemblBacteria; ABB32776; ABB32776; Gmet_2557. DR KEGG; gme:Gmet_2557; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; EREVIIT; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000007073; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR Gene3D; 1.10.10.10; -; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR011991; WHTH_DNA-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000007073}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000007073}. FT DOMAIN 380 553 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 195 222 {ECO:0000256|SAM:Coils}. FT COILED 339 373 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 556 AA; 62989 MW; 66A638BB3B3D0426 CRC64; MKQLHGNLIG LKPNQIASLE RLYRRRVPPD ELITAELAGR MVEISREIRR QIGVLIDRHG AVEYVIIGDE KGIFIPELSD YPLGRRLLRG LRYIHTHLKG ESFSEDDLTD LALLRFDLMA ILQIHPDDRR VAIQTASLTP TAGAAHPYRV EASEPLATFR MDFGSSVSHL ERELEKAVAT EAREVAASGE RAILISVTKE SREEAEDSLE ELKELARTAG VAVLDVVIQR PRQFNPRYLM GEGKMREVVI RALQLGATIL IFDQELSPAQ VRSISEMTEL KVIDRSQLIL DIFARRATSL DGKVQVELAQ LKYILPRLTG RGVQMSRLMG GIGGRGPGET KLETDRRRIR DRIAKLEREL EELSRGRQQR RQKRVRAGLP IVSIVGYTNA GKSTLLNALT RSHVFTENLL FATLDTSTRR LRFPREREVI ITDTVGFIRS LPKSLMGAFK ATLEELQDAD LLLHLVDCTN PRVEEQIHQV ETILEELDLG DKQRLMVFNK VDILPELKKK SPLGFMKVRQ LSRRFNAITV SATNPSSLES LLQEMERRFW PSSPQS // ID Q3A2X3_PELCD Unreviewed; 547 AA. AC Q3A2X3; DT 22-NOV-2005, integrated into UniProtKB/TrEMBL. DT 22-NOV-2005, sequence version 1. DT 07-JUN-2017, entry version 86. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Pcar_2043 {ECO:0000313|EMBL:ABA89284.1}; OS Pelobacter carbinolicus (strain DSM 2380 / NBRC 103641 / GraBd1). OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfuromonadales; OC Desulfuromonadaceae; Pelobacter. OX NCBI_TaxID=338963 {ECO:0000313|EMBL:ABA89284.1, ECO:0000313|Proteomes:UP000002534}; RN [1] {ECO:0000313|Proteomes:UP000002534} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 2380 / NBRC 103641 / GraBd1 RC {ECO:0000313|Proteomes:UP000002534}; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., RA Hammon N., Israni S., Pitluck S., Chertkov O., Schmutz J., Larimer F., RA Land M., Kyrpides N., Ivanova N., Richardson P.; RT "Complete sequence of Pelobacter carbinolicus DSM 2380."; RL Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000142; ABA89284.1; -; Genomic_DNA. DR RefSeq; WP_011341795.1; NC_007498.2. DR ProteinModelPortal; Q3A2X3; -. DR STRING; 338963.Pcar_2043; -. DR EnsemblBacteria; ABA89284; ABA89284; Pcar_2043. DR KEGG; pca:Pcar_2043; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; EREVIIT; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000002534; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000002534}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000002534}. FT DOMAIN 378 542 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 337 364 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 547 AA; 61486 MW; 40E8AB0AFC9EAB8A CRC64; MVVHGNLTGL KASQVKALER IYRRRVPPDQ VVTPELARYL TEQSLEIRRQ IGLIIDRSGS VRYVIVGDGR EIVIPDLSGY GRGRSGLRGL RCIHTHLAGE SLSEDDLTDL ALLCLDLMVC IGVGEQGLPG RVEYAHLMPP NPEGKQVETN IVASVYDLDL DMGVFLRSLD QELESKMAET VDLSDPREKG ILVSVSQQPR YEAEDSLEEL AELARTAEVV VLDRFIQRPR QINPKYLLGE GKIKEVVIRA LQQGATLLIF DQDLTPAQIR AIAQITDLKV IDRSQLILDI FARRAHTRDG KVQVELAQLK YILPRLSGRG IAMSRLMGGI GGRGPGETKL EIDRRRIRER ITRLENQLKN LSKGRLQRRQ RRIRSGVPII SIVGYTNAGK STLLNALTQS EVFTEDLLFA TLDTSSRRLR FPMEREVIIT DTVGFIRKLP KSLVGAFRAT LEELEDADLL LHVVDVSHPR FEEHISAVEA ILNELDLGRI PRQLVFNKID LVSSQQVEAL CRRFQAVAVS ARNRKTFEPL LTMLEGRFWP GEMEGPD // ID Q3ARD9_CHLCH Unreviewed; 431 AA. AC Q3ARD9; DT 22-NOV-2005, integrated into UniProtKB/TrEMBL. DT 22-NOV-2005, sequence version 1. DT 07-JUN-2017, entry version 81. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Cag_1174 {ECO:0000313|EMBL:ABB28436.1}; OS Chlorobium chlorochromatii (strain CaD3). OC Bacteria; Chlorobi; Chlorobia; Chlorobiales; Chlorobiaceae; OC Chlorobium/Pelodictyon group; Chlorobium. OX NCBI_TaxID=340177 {ECO:0000313|EMBL:ABB28436.1, ECO:0000313|Proteomes:UP000002708}; RN [1] {ECO:0000313|EMBL:ABB28436.1, ECO:0000313|Proteomes:UP000002708} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CaD3 {ECO:0000313|EMBL:ABB28436.1, RC ECO:0000313|Proteomes:UP000002708}; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., RA Hammon N., Israni S., Pitluck S., Bryant D., Schmutz J., Larimer F., RA Land M., Kyrpides N., Ivanova N., Richardson P.; RT "Complete sequence of Chlorobium chlorochromatii CaD3."; RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000108; ABB28436.1; -; Genomic_DNA. DR RefSeq; WP_011362200.1; NC_007514.1. DR ProteinModelPortal; Q3ARD9; -. DR STRING; 340177.Cag_1174; -. DR EnsemblBacteria; ABB28436; ABB28436; Cag_1174. DR KEGG; cch:Cag_1174; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000002708; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000002708}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Hydrolase {ECO:0000313|EMBL:ABB28436.1}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000002708}. FT DOMAIN 202 369 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 431 AA; 49147 MW; 697CAC7F35751E75 CRC64; MNTVTPENQR EKAFLVGIYS PPEVPRSLVE EYLAELAFLA DTAGADVLDT FIQERKVRDP SYCIGRGKVD EMEAYIKSEK IDVVIFDDDL SPGQARNLER AWGCKVIDRT GLILHIFAIR AQSTQAKMQV ELAQLEYILP RLSGAWTHLS KQKGGIGNKG PGETQIETDR RLVRNRIALL KKKLREVERQ HYTRTRSRQN VSRVSLVGYT NAGKSTLMNA LCPQAEAFAE NRLFATLDTK TRRLELKINK LVLLSDTVGF IRKLPHTLVE SFKSTLDEVL QADFLLHVID ISHPSFEEQI AVVRDTLREI GVQHDQIIEV FNKIDALEEP TLLREMGDKY PNAVFISAVR GINLSLLKEI IGEQLARDYT ERHVRLHVSN YRLISYLYDH TEVVEKKHED EMVELTIHVR NHQLPQIDAM IQAAAEAPHE P // ID Q3B367_CHLL7 Unreviewed; 435 AA. AC Q3B367; DT 22-NOV-2005, integrated into UniProtKB/TrEMBL. DT 22-NOV-2005, sequence version 1. DT 07-JUN-2017, entry version 79. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Plut_1355 {ECO:0000313|EMBL:ABB24214.1}; OS Chlorobium luteolum (strain DSM 273 / 2530) (Pelodictyon luteolum). OC Bacteria; Chlorobi; Chlorobia; Chlorobiales; Chlorobiaceae; OC Chlorobium/Pelodictyon group; Pelodictyon. OX NCBI_TaxID=319225 {ECO:0000313|EMBL:ABB24214.1, ECO:0000313|Proteomes:UP000002709}; RN [1] {ECO:0000313|Proteomes:UP000002709} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 273 / 2530 {ECO:0000313|Proteomes:UP000002709}; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., RA Hammon N., Israni S., Pitluck S., Bryant D., Schmutz J., Larimer F., RA Land M., Kyrpides N., Ivanova N., Richardson P.; RT "Complete sequence of Pelodictyon luteolum DSM 273."; RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000096; ABB24214.1; -; Genomic_DNA. DR RefSeq; WP_011358086.1; NC_007512.1. DR ProteinModelPortal; Q3B367; -. DR STRING; 319225.Plut_1355; -. DR EnsemblBacteria; ABB24214; ABB24214; Plut_1355. DR KEGG; plt:Plut_1355; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000002709; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000002709}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Hydrolase {ECO:0000313|EMBL:ABB24214.1}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000002709}. FT DOMAIN 203 370 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 435 AA; 49128 MW; 2CE4FC52E9E7BDA0 CRC64; MPNTPVTEHP RERAILVGLP SPPEIPRSLV EEYLVELAFL ADTAGADVVR TLIQERKLRD PAYCIGRGKV DELLEMTKED QVDIVIFDDD LTPGQTRNLE RALDCKVIDR TGLILQIFAI RAKSHQAKMQ VELAQLEYLL PRLSGQWTHL SKQKGGIGTK GPGETQIETD RRLVRNRIAS LKQKLRDVSL QHDTQTGSRR SVPRVALVGY TNAGKSTLMN QLCPDAGAYA EDRLFATLDT RTRRLELKIN KLVLLSDTVG FIRKLPHTLV ESFRSTLDEV LQADFLLHVV DLSHPGFEEQ MQVVQSTLRE IGVKHQHIID VFNKIDALAD PSVLRDLRAR YPDAVFISAA RGINLTALRE CIAEHVGRDY SERRIRVHVA DYKIIGYLYE HTEVTGRRCV DEEVELTYRV HKNRLKHIDA LTGHSEEAGH AVADS // ID Q3IEY9_PSEHT Unreviewed; 429 AA. AC Q3IEY9; DT 08-NOV-2005, integrated into UniProtKB/TrEMBL. DT 08-NOV-2005, sequence version 1. DT 30-AUG-2017, entry version 99. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:CAI85371.1}; GN OrderedLocusNames=PSHAa0272 {ECO:0000313|EMBL:CAI85371.1}; OS Pseudoalteromonas haloplanktis (strain TAC 125). OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales; OC Pseudoalteromonadaceae; Pseudoalteromonas. OX NCBI_TaxID=326442 {ECO:0000313|EMBL:CAI85371.1, ECO:0000313|Proteomes:UP000006843}; RN [1] {ECO:0000313|EMBL:CAI85371.1, ECO:0000313|Proteomes:UP000006843} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=TAC 125 {ECO:0000313|Proteomes:UP000006843}; RX PubMed=16169927; DOI=10.1101/gr.4126905; RA Medigue C., Krin E., Pascal G., Barbe V., Bernsel A., Bertin P., RA Cheung F., Cruveiller S., Damico S., Duilio A., Fang G., Feller G., RA Mangenot S., Marino G., Nilsson J., Parilli E., Rocha E., Rouy Z., RA Sekowska A., Tutino M.L., Vallenet D., von Heijne G., Danchin A.; RT "Coping with cold: the genome of the versatile marine Antarctica RT bacterium Pseudoalteromonas haloplanktis TAC125."; RL Genome Res. 15:1325-1335(2005). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CR954246; CAI85371.1; -; Genomic_DNA. DR RefSeq; WP_011326985.1; NC_007481.1. DR ProteinModelPortal; Q3IEY9; -. DR STRING; 326442.PSHAa0272; -. DR EnsemblBacteria; CAI85371; CAI85371; PSHAa0272. DR GeneID; 32566477; -. DR KEGG; pha:PSHAa0272; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000006843; Chromosome I. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000006843}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Hydrolase {ECO:0000313|EMBL:CAI85371.1}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Protease {ECO:0000313|EMBL:CAI85371.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000006843}. FT DOMAIN 198 365 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 429 AA; 48325 MW; 8B46FF0A4C3946E6 CRC64; MFDRYKSGEQ AVLVHIDFPK EGDREDLHEL ELLVSSAGVS SLAVVQGSRQ APHPKLFVGT GKAEEIAETV KIHNADVVIF NHQLRPSQER NLERILQCRV LDRTTLILDI FAQRARTHEG KLQVELAQLR HMSTRLIRGW THLERQKGGV GLRGPGETQL ETDRRLLRAR LQNIRARLDK VAVQREQGRR ARSRNEIPTV SLVGYTNAGK STLFNRITNS DVYAADQLFA TLDPTLRKLE LGDVGPVILA DTVGFIRHLP HDLVAAFKAT LTETREADLQ LHVIDVADAR LKENIEQVQS VLKEIEADEV PQLLVYNKID ALDDITARID RDDEGQPIRV WLSAQTGEGC ELLSEAISEL LAKQMLSETL LLAPQYGRLR SSLFSLSAVS DERFDEQGNW LLDVRLPVVE WNRLIKEFGP EIAGFIVCD // ID Q3IL84_PSEHT Unreviewed; 450 AA. AC Q3IL84; DT 08-NOV-2005, integrated into UniProtKB/TrEMBL. DT 08-NOV-2005, sequence version 1. DT 07-JUN-2017, entry version 81. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=PSHAa1393 {ECO:0000313|EMBL:CAI86468.1}; OS Pseudoalteromonas haloplanktis (strain TAC 125). OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales; OC Pseudoalteromonadaceae; Pseudoalteromonas. OX NCBI_TaxID=326442 {ECO:0000313|EMBL:CAI86468.1, ECO:0000313|Proteomes:UP000006843}; RN [1] {ECO:0000313|EMBL:CAI86468.1, ECO:0000313|Proteomes:UP000006843} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=TAC 125 {ECO:0000313|Proteomes:UP000006843}; RX PubMed=16169927; DOI=10.1101/gr.4126905; RA Medigue C., Krin E., Pascal G., Barbe V., Bernsel A., Bertin P., RA Cheung F., Cruveiller S., Damico S., Duilio A., Fang G., Feller G., RA Mangenot S., Marino G., Nilsson J., Parilli E., Rocha E., Rouy Z., RA Sekowska A., Tutino M.L., Vallenet D., von Heijne G., Danchin A.; RT "Coping with cold: the genome of the versatile marine Antarctica RT bacterium Pseudoalteromonas haloplanktis TAC125."; RL Genome Res. 15:1325-1335(2005). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CR954246; CAI86468.1; -; Genomic_DNA. DR RefSeq; WP_011328074.1; NC_007481.1. DR ProteinModelPortal; Q3IL84; -. DR STRING; 326442.PSHAa1393; -. DR EnsemblBacteria; CAI86468; CAI86468; PSHAa1393. DR KEGG; pha:PSHAa1393; -. DR PATRIC; fig|326442.8.peg.1348; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; VILEIFH; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000006843; Chromosome I. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000006843}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000006843}. FT DOMAIN 230 395 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 191 225 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 450 AA; 49621 MW; 421208CEA967FF5E CRC64; MQLTAKASLP NALLISISTP HFKGDEAIES LAELARLVTT LGFKVVGTQS QKQSSTQKVN VLGSGKLAEI AHLTGNKGSA ADEKEGENFL DDDPLSDMPS EIPSDGLDFA CADVVVFDCD LTPSQLRNVE NQLGVEVFDR TGIIIEIFSR HARTKTAKLQ VEIARLNYVA PRLRETSTGD KERQMGKGAG ETTLELNRRK VRDQLAELKR ELVNVQDVMM DRREQRSELF SVALIGYTNA GKSSMMRAIT GSDVEGENKL FATLDTTVRA LYPITQPRIL VSDTVGFIKK LPHDLVASFH STLAEAHDAS LLLYVVDASD ASFRSQLDVV HNVLAEVGVQ GSKKLLVLNK SDQLSDAQQQ ALMAEFPDAM MTSTRNPADI AKLHKYIVDT AQSDMIEEEV IIPYTAKGIV GEIRSTMSVI KEEYEYSHIK LTVRSNAIDL ERLKKRMLDL // ID Q3J2L8_RHOS4 Unreviewed; 447 AA. AC Q3J2L8; DT 08-NOV-2005, integrated into UniProtKB/TrEMBL. DT 22-JAN-2014, sequence version 2. DT 07-JUN-2017, entry version 92. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=RSP_2844 {ECO:0000313|EMBL:ABA78966.2}; OS Rhodobacter sphaeroides (strain ATCC 17023 / 2.4.1 / NCIB 8253 / DSM OS 158). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae; Rhodobacter. OX NCBI_TaxID=272943 {ECO:0000313|EMBL:ABA78966.2, ECO:0000313|Proteomes:UP000002703}; RN [1] {ECO:0000313|Proteomes:UP000002703} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 17023 / 2.4.1 / NCIB 8253 / DSM 158 RC {ECO:0000313|Proteomes:UP000002703}; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., RA Hammon N., Israni S., Pitluck S., Richardson P., Mackenzie C., RA Choudhary M., Larimer F., Hauser L.J., Land M., Donohue T.J., RA Kaplan S.; RT "Complete sequence of chromosome 1 of Rhodobacter sphaeroides 2.4.1."; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000143; ABA78966.2; -; Genomic_DNA. DR RefSeq; WP_017140208.1; NZ_AKVW01000001.1. DR RefSeq; YP_352867.2; NC_007493.2. DR STRING; 272943.RSP_2844; -. DR EnsemblBacteria; ABA78966; ABA78966; RSP_2844. DR GeneID; 3720542; -. DR KEGG; rsp:RSP_2844; -. DR PATRIC; fig|272943.9.peg.1735; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; FNNHAHV; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000002703; Chromosome 1. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000002703}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000002703}. FT DOMAIN 227 396 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 447 AA; 49460 MW; 67DDD86276EFC4D5 CRC64; MTDPEEGEEE PRNEGDRESQ AASDGATKSQ PMRAFVLHPD IRTERSRRLP DLRLAEAVSL AAALPDMEIV GQEVVRLPRA QPGLLFGTGK VEELKARFKG LDVGLVLVDG PVSPVQQRNL EKEWGVKLLD RTGLILEIFA DRARTREGVL QVELAALSYQ RTRLVRAWTH LERQRGGLGF VGGPGETQIE ADRRAIDEQV IRIRRQLDKV VKTRELHRAS RRKVPFPIVA LVGYTNAGKS TLFNRMTGAD VLAKDMLFAT LDPTMRGVTL PSGRKVILSD TVGFISDLPT QLVAAFRATL EEVLEADLIL HVRDIAHPET AEQAADVAEI LQSLGVKGAT PQVEVWNKLD LVEGAAHEQL LAQAAKSETI FALSALTGEG LPDLLEAVSA TFDEEKTERQ LTLGFADGRR RAWLHAEGVV TGEAETEEGH RIDVRWTARQ EKRFRDL // ID Q3J804_NITOC Unreviewed; 382 AA. AC Q3J804; DT 08-NOV-2005, integrated into UniProtKB/TrEMBL. DT 08-NOV-2005, sequence version 1. DT 07-JUN-2017, entry version 77. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Noc_2589 {ECO:0000313|EMBL:ABA59042.1}; OS Nitrosococcus oceani (strain ATCC 19707 / BCRC 17464 / NCIMB 11848 / OS C-107). OC Bacteria; Proteobacteria; Gammaproteobacteria; Chromatiales; OC Chromatiaceae; Nitrosococcus. OX NCBI_TaxID=323261 {ECO:0000313|EMBL:ABA59042.1, ECO:0000313|Proteomes:UP000006838}; RN [1] {ECO:0000313|Proteomes:UP000006838} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 19707 / BCRC 17464 / NCIMB 11848 / C-107 RC {ECO:0000313|Proteomes:UP000006838}; RX PubMed=16957257; DOI=10.1128/AEM.00463-06; RA Klotz M.G., Arp D.J., Chain P.S.G., El-Sheikh A.F., Hauser L.J., RA Hommes N.G., Larimer F.W., Malfatti S.A., Norton J.M., RA Poret-Peterson A.T., Vergez L.M., Ward B.B.; RT "Complete genome sequence of the marine, chemolithoautotrophic, RT ammonia-oxidizing bacterium Nitrosococcus oceani ATCC 19707."; RL Appl. Environ. Microbiol. 72:6299-6315(2006). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000127; ABA59042.1; -; Genomic_DNA. DR RefSeq; WP_004269186.1; NC_007484.1. DR ProteinModelPortal; Q3J804; -. DR STRING; 323261.Noc_2589; -. DR EnsemblBacteria; ABA59042; ABA59042; Noc_2589. DR KEGG; noc:Noc_2589; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000006838; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000006838}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Hydrolase {ECO:0000313|EMBL:ABA59042.1}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000006838}. FT DOMAIN 203 370 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 169 196 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 382 AA; 43459 MW; F98D509300BAE731 CRC64; MLFSHSEGGR GYDYSAILVH IDFHEPAYHE MQAEFIELVS STGIEIVTVL SGKRQSPHSK YFIGRGKVDE IRVWVDAEQA DLVVFNHDLS PSQERNLEQS LQCRVLDRTE LILDIFSQRA RSHEGKLQVE LAQLQHLSTR LVRGWSHLER QKGGIGLRGP GETQLETDRR LIGNRIRQLR KRLERVRKQR DQGRRSRHKA RVPTVSLVGY TNAGKSTLFN RLTAARVLVD DRLFATLDPT LRRLRLALTQ PLILADTVGF IRNLPHDLVE AFRSTLEETR DAALLLHVID ASSEGRCDLI AQVNKVLQTI GAEGVPQLEV YNKIDRVEGC QPRLERDASG RVHRVWLSAT SGEGLELLRQ ALAEYFPAKR SVDPQQEIHA YQ // ID Q3SJ54_THIDA Unreviewed; 458 AA. AC Q3SJ54; DT 11-OCT-2005, integrated into UniProtKB/TrEMBL. DT 11-OCT-2005, sequence version 1. DT 30-AUG-2017, entry version 80. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Tbd_1363 {ECO:0000313|EMBL:AAZ97316.1}; OS Thiobacillus denitrificans (strain ATCC 25259). OC Bacteria; Proteobacteria; Betaproteobacteria; Nitrosomonadales; OC Thiobacillaceae; Thiobacillus. OX NCBI_TaxID=292415 {ECO:0000313|EMBL:AAZ97316.1, ECO:0000313|Proteomes:UP000008291}; RN [1] {ECO:0000313|EMBL:AAZ97316.1, ECO:0000313|Proteomes:UP000008291} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 25259 {ECO:0000313|EMBL:AAZ97316.1, RC ECO:0000313|Proteomes:UP000008291}; RX PubMed=16452431; DOI=10.1128/JB.188.4.1473-1488.2006; RA Beller H.R., Chain P.S., Letain T.E., Chakicherla A., Larimer F.W., RA Richardson P.M., Coleman M.A., Wood A.P., Kelly D.P.; RT "The genome sequence of the obligately chemolithoautotrophic, RT facultatively anaerobic bacterium Thiobacillus denitrificans."; RL J. Bacteriol. 188:1473-1488(2006). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000116; AAZ97316.1; -; Genomic_DNA. DR RefSeq; WP_011311875.1; NC_007404.1. DR ProteinModelPortal; Q3SJ54; -. DR STRING; 292415.Tbd_1363; -. DR EnsemblBacteria; AAZ97316; AAZ97316; Tbd_1363. DR KEGG; tbd:Tbd_1363; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; VILEIFH; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000008291; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000008291}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000008291}. FT DOMAIN 232 402 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 190 224 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 458 AA; 50607 MW; C5E17DFEAE87CCB9 CRC64; MPLQVEDKPA YAVVAAVQLP QVSDLEFEAS LTELRELAKT LGFTVIRTFT QKRPGFDTTA YLGVGKRQEL TRFVRGGEEE AEADPAAPYA LHRVEGQDDV SPHPIDVLFV DHEISPSQAR NLENEVGCQV MDRTMVILEI FHRNARSPAA RAQVEIARLG YLAPRLREAA KLAGPQGRQR SGVGGRGAGE SHTELDKRKI RDRIAELQKE IAAMDADRKT QRARRQAHQG LASVALVGYT NAGKSTLMRA LTGSEVLVAN KLFATLDTTV RTLHPEGVPR VLVSDTVGFI KNLPHGLVAS FKSTLEEALD ASLLLHVIDA SDPGFVRQIE TTEDVLEEID AQDVPRLRIF NKIDHLGDAV AQAEREAALR AAYPGCIVMS ARRPEDVAKL HDAILTFFQK DLVEAELFLP WSAQQLRGEI FARCQVLEER SDEDGAFFHV RGEQETLNGL RDQLGHAR // ID Q3SL62_THIDA Unreviewed; 389 AA. AC Q3SL62; DT 11-OCT-2005, integrated into UniProtKB/TrEMBL. DT 11-OCT-2005, sequence version 1. DT 30-AUG-2017, entry version 82. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Tbd_0602 {ECO:0000313|EMBL:AAZ96555.1}; OS Thiobacillus denitrificans (strain ATCC 25259). OC Bacteria; Proteobacteria; Betaproteobacteria; Nitrosomonadales; OC Thiobacillaceae; Thiobacillus. OX NCBI_TaxID=292415 {ECO:0000313|EMBL:AAZ96555.1, ECO:0000313|Proteomes:UP000008291}; RN [1] {ECO:0000313|EMBL:AAZ96555.1, ECO:0000313|Proteomes:UP000008291} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 25259 {ECO:0000313|EMBL:AAZ96555.1, RC ECO:0000313|Proteomes:UP000008291}; RX PubMed=16452431; DOI=10.1128/JB.188.4.1473-1488.2006; RA Beller H.R., Chain P.S., Letain T.E., Chakicherla A., Larimer F.W., RA Richardson P.M., Coleman M.A., Wood A.P., Kelly D.P.; RT "The genome sequence of the obligately chemolithoautotrophic, RT facultatively anaerobic bacterium Thiobacillus denitrificans."; RL J. Bacteriol. 188:1473-1488(2006). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000116; AAZ96555.1; -; Genomic_DNA. DR RefSeq; WP_011311114.1; NC_007404.1. DR ProteinModelPortal; Q3SL62; -. DR STRING; 292415.Tbd_0602; -. DR EnsemblBacteria; AAZ96555; AAZ96555; Tbd_0602. DR KEGG; tbd:Tbd_0602; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000008291; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000008291}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000008291}. FT DOMAIN 198 372 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 389 AA; 42520 MW; 6A0DB38CA26BA4D2 CRC64; MFDRHQGGER VVLAALDLGD PDFAESMAEL RLLARGAGLD IRGEVQGRRS RPDAALFVGS GKADEIAALV AATDAEVVIF NHELSPAQER NLERRLHCRV IDRVSLILDI FARRARSAEG KLQVELAQLQ HLSTRLVRGW THLERQRGGV GMRGPGEKQL ETDRRLIGIR VKALRERLAK LGKQRRTQRR SRSRHRVLSV ALVGYTNAGK STLFNALTRA GTYAADQLFA TLDTTTRKIF LPRLADADEP GSGEVVLSDT VGFITRLPHD LVAAFRATLE ATAEADLLLH VIDASSPVRE RQIEAVDQVL REIGADAVPQ LRVYNKLDLT AAAPGVGRDE YDRLQSVYVS AQTGAGLELL RDALSETLLA ARETGASETP SSPSTVHSA // ID Q3SSN0_NITWN Unreviewed; 442 AA. AC Q3SSN0; DT 11-OCT-2005, integrated into UniProtKB/TrEMBL. DT 11-OCT-2005, sequence version 1. DT 07-JUN-2017, entry version 78. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Nwi_1450 {ECO:0000313|EMBL:ABA04711.1}; OS Nitrobacter winogradskyi (strain ATCC 25391 / DSM 10237 / CIP 104748 / OS NCIMB 11846 / Nb-255). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Bradyrhizobiaceae; Nitrobacter. OX NCBI_TaxID=323098 {ECO:0000313|EMBL:ABA04711.1, ECO:0000313|Proteomes:UP000002531}; RN [1] {ECO:0000313|EMBL:ABA04711.1, ECO:0000313|Proteomes:UP000002531} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 25391 / DSM 10237 / CIP 104748 / NCIMB 11846 / Nb-255 RC {ECO:0000313|Proteomes:UP000002531}; RX PubMed=16517654; DOI=10.1128/AEM.72.3.2050-2063.2006; RA Starkenburg S.R., Chain P.S., Sayavedra-Soto L.A., Hauser L., RA Land M.L., Larimer F.W., Malfatti S.A., Klotz M.G., Bottomley P.J., RA Arp D.J., Hickey W.J.; RT "Genome sequence of the chemolithoautotrophic nitrite-oxidizing RT bacterium Nitrobacter winogradskyi Nb-255."; RL Appl. Environ. Microbiol. 72:2050-2063(2006). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000115; ABA04711.1; -; Genomic_DNA. DR ProteinModelPortal; Q3SSN0; -. DR STRING; 323098.Nwi_1450; -. DR EnsemblBacteria; ABA04711; ABA04711; Nwi_1450. DR KEGG; nwi:Nwi_1450; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000002531; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000002531}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Hydrolase {ECO:0000313|EMBL:ABA04711.1}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000002531}. FT DOMAIN 209 383 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 442 AA; 48925 MW; 815706C76C36D188 CRC64; MRGEPTGRAI VIGPYVRTRG GDAETPRRSL RNTDARLDEA AGLAKAIDLH VIQAIVAPVS QIRPATYLGK GKVEELQGLI AADGAGLVVM DCALSPIQQR NLEKAWSTKV LDRTGLILEI FGRRAKTKEG ALQVELAHLN YQRSRLVRSW THLERQRGGF GFMGGPGETQ IEADRRLIGD RITRLENELK KVQATRRLHR AGRQRVPYRV VALVGYTNAG KSTLFNRLTR ADVQAADMLF ATLDPTLRSL ALPHGGKAML SDTVGFISNL PTQLVAAFRA TLEEVMEADV ILHVRDISHE DTEPQQHDVE AVLHQLGIDP DGPARMIEVW NKIDRFDADQ RKDLENVAAR RSTDVPRFLV SAETGEGVET LLAAIEDRLA ATRTTLDLSV DASDGAAISW LHRNSEVLAK ELRDGRYDMT VRVDETKRDI LVNRYGAAPR PL // ID Q3XX72_ENTFC Unreviewed; 409 AA. AC Q3XX72; DT 11-OCT-2005, integrated into UniProtKB/TrEMBL. DT 11-OCT-2005, sequence version 1. DT 07-JUN-2017, entry version 63. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:AFK59794.1}; GN ORFNames=HMPREF0351_12170 {ECO:0000313|EMBL:AFK59794.1}; OS Enterococcus faecium DO. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Enterococcaceae; OC Enterococcus. OX NCBI_TaxID=333849 {ECO:0000313|EMBL:AFK59794.1, ECO:0000313|Proteomes:UP000005269}; RN [1] {ECO:0000313|EMBL:AFK59794.1, ECO:0000313|Proteomes:UP000005269} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DO {ECO:0000313|EMBL:AFK59794.1, RC ECO:0000313|Proteomes:UP000005269}; RX PubMed=22769602; DOI=10.1186/1471-2180-12-135; RA Qin X., Galloway-Pena J.R., Sillanpaa J., Hyeob Roh J., RA Nallapareddy S.R., Chowdhury S., Bourgogne A., Choudhury T., RA Munzy D.M., Buhay C.J., Ding Y., Dugan-Rocha S., Liu W., Kovar C., RA Sodergren E., Highlander S., Petrosino J.F., Worley K.C., Gibbs R.A., RA Weinstock G.M., Murray B.E.; RT "Complete genome sequence of Enterococcus faecium strain TX16 and RT comparative genomic analysis of Enterococcus faecium genomes."; RL BMC Microbiol. 12:135-135(2012). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP003583; AFK59794.1; -; Genomic_DNA. DR RefSeq; WP_002289406.1; NZ_AAAK03000091.1. DR RefSeq; YP_006376776.1; NC_017960.1. DR ProteinModelPortal; Q3XX72; -. DR EnsemblBacteria; AFK59794; AFK59794; HMPREF0351_12170. DR GeneID; 13000870; -. DR KEGG; efu:HMPREF0351_12170; -. DR KO; K03665; -. DR Proteomes; UP000005269; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000005269}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000005269}. FT DOMAIN 194 356 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 409 AA; 46591 MW; 3A48ED333F8554FB CRC64; MEEKVIIVGV ETEANQRYFS ESMEELVQLT NTASGEVVFT ITQKRPQVDR QTIIGKGKLQ ELVQQADAHE ADLIIFNHEL TPRQSQLITD AVGLPVIDRV QLILDIFAMR ARSKEGKLQV ELAQLEYLLP RLVGQGKTLS RLGGGIGTRG PGETKLETDR RHIRNKIFAV KKELKEVEAH RERNRQKRKN SEIFQIGLIG YTNAGKSTIL NLLTQADTYS KDQLFATLDP LTKRWRFAEG FEITVTDTVG FIQDLPTQLI DAFHSTLEES QNMDLLLHVV DASSPDRILQ EQTVLKLMDE LNMKEMPILT VYNKADQIDP AMFTPTLFPN VLISTQTKEG KMALIEAIKR QLMELMTPYT LSVPSNEGQK LSELRRQTMV LDEAYMEETN EYEVKGFAKT NSKWLRKNQ // ID Q3Z8H7_DEHM1 Unreviewed; 380 AA. AC Q3Z8H7; DT 27-SEP-2005, integrated into UniProtKB/TrEMBL. DT 27-SEP-2005, sequence version 1. DT 07-JUN-2017, entry version 82. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=DET0737 {ECO:0000313|EMBL:AAW40006.1}; OS Dehalococcoides mccartyi (strain ATCC BAA-2266 / KCTC 15142 / 195) OS (Dehalococcoides ethenogenes (strain 195)). OC Bacteria; Chloroflexi; Dehalococcoidia; Dehalococcoidales; OC Dehalococcoidaceae; Dehalococcoides. OX NCBI_TaxID=243164 {ECO:0000313|EMBL:AAW40006.1, ECO:0000313|Proteomes:UP000008289}; RN [1] {ECO:0000313|EMBL:AAW40006.1, ECO:0000313|Proteomes:UP000008289} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-2266 / KCTC 15142 / 195 RC {ECO:0000313|Proteomes:UP000008289}; RX PubMed=15637277; DOI=10.1126/science.1102226; RA Seshadri R., Adrian L., Fouts D.E., Eisen J.A., Phillippy A.M., RA Methe B.A., Ward N.L., Nelson W.C., DeBoy R.T., Khouri H.M., RA Kolonay J.F., Dodson R.J., Daugherty S.C., Brinkac L.M., RA Sullivan S.A., Madupu R., Nelson K.E., Kang K.H., Impraim M., Tran K., RA Robinson J.M., Forberger H.A., Fraser C.M., Zinder S.H., RA Heidelberg J.F.; RT "Genome sequence of the PCE-dechlorinating bacterium Dehalococcoides RT ethenogenes."; RL Science 307:105-108(2005). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000027; AAW40006.1; -; Genomic_DNA. DR ProteinModelPortal; Q3Z8H7; -. DR STRING; 243164.DET0737; -. DR EnsemblBacteria; AAW40006; AAW40006; DET0737. DR KEGG; det:DET0737; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000008289; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; ISS:TIGR. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000008289}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000008289}. FT DOMAIN 188 364 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 147 181 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 380 AA; 42316 MW; 7BAE2AE22624B4A5 CRC64; MAVDTDNNAN WDIEDSLDEL AQLVLTAGAT VVGRLTQKLQ APARNSYLGK GKLDELVELK KELGYNLVIF DDELSPIQQR LLEEALGVKV IDRVALILDI FAKHAHTREG QLQVELAQMQ YILPRLAGQW SHLERLGGGI GTRGPGESQL ETDKRIIRTK IRNLQEQLDD VTTHRDLYRE RRRMRGVPVV SLVGYTNSGK SSLLNAVVKA DVLAENKLFA TLDPTTRRMY INGLGNVLLT DTVGFIRKLP PAIVKAFRAT LEEINQADLL VHVVDITAKN AFEQCQTVEK ILGDMGVAEK PRLTAMNKID LKLDNSRKWT EDEALSLLKA ECPVAEDTVL ISAAKHWGLA EFNLRLKEKL IGMGFNPGYA VYDEDVGGKK // ID Q46FK7_METBF Unreviewed; 436 AA. AC Q46FK7; DT 13-SEP-2005, integrated into UniProtKB/TrEMBL. DT 13-SEP-2005, sequence version 1. DT 07-JUN-2017, entry version 92. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Mbar_A0351 {ECO:0000313|EMBL:AAZ69335.1}; OS Methanosarcina barkeri (strain Fusaro / DSM 804). OC Archaea; Euryarchaeota; Methanomicrobia; Methanosarcinales; OC Methanosarcinaceae; Methanosarcina. OX NCBI_TaxID=269797 {ECO:0000313|EMBL:AAZ69335.1, ECO:0000313|Proteomes:UP000008156}; RN [1] {ECO:0000313|Proteomes:UP000008156} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Fusaro / DSM 804 {ECO:0000313|Proteomes:UP000008156}; RX PubMed=16980466; DOI=10.1128/JB.00810-06; RA Maeder D.L., Anderson I., Brettin T.S., Bruce D.C., Gilna P., RA Han C.S., Lapidus A., Metcalf W.W., Saunders E., Tapia R., RA Sowers K.R.; RT "The Methanosarcina barkeri genome: comparative analysis with RT Methanosarcina acetivorans and Methanosarcina mazei reveals extensive RT rearrangement within methanosarcinal genomes."; RL J. Bacteriol. 188:7922-7931(2006). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000099; AAZ69335.1; -; Genomic_DNA. DR RefSeq; WP_011305388.1; NC_007355.1. DR ProteinModelPortal; Q46FK7; -. DR STRING; 269797.Mbar_A0351; -. DR EnsemblBacteria; AAZ69335; AAZ69335; Mbar_A0351. DR GeneID; 3626595; -. DR KEGG; mba:Mbar_A0351; -. DR eggNOG; arCOG00353; Archaea. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG093Z07D6; -. DR Proteomes; UP000008156; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000008156}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Hydrolase {ECO:0000313|EMBL:AAZ69335.1}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}. FT DOMAIN 206 375 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 172 199 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 436 AA; 49390 MW; 4C5AA8FD93119807 CRC64; MKISAEQKSN NGSGNGNRVI LVKRTIPNSD PEREEYLLQE LRELAKAAGY LPVGELKQTR YPDSKYQLGR GKIEELAELV RSTGVEKVIF YNRLSTTQLF NISEICRCQI IDKFQLILEI FAKRATTHRS KLQVELARLR YEVPRARAVV SLLKKEERAG FMGLGDYEDS YEQDLKKRIT RIRNELESAE KDDESLRALR HRKGFSLISL AGYTNAGKST LFNAIVDESV EAKNMLFTTL VPMTRALDLG GRKALLTDTV GFIEDLPHWL VDAFKSTLDE IFLSDLILLV VDASEKPETI LQKLSTSHDT LWDRIQGVPI ITVLNKADLV DESKLDAIME QIGYMAPNPV FVSAKKGTGM AALKAEIIKH LPPWCFCSLS LPNSEKGMSI LSWLYEEGIV HRVEFGERIF LDYEARTEII NRAHSLLEPQ EAQINE // ID Q47BS2_DECAR Unreviewed; 384 AA. AC Q47BS2; DT 13-SEP-2005, integrated into UniProtKB/TrEMBL. DT 13-SEP-2005, sequence version 1. DT 30-AUG-2017, entry version 79. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Daro_2979 {ECO:0000313|EMBL:AAZ47709.1}; OS Dechloromonas aromatica (strain RCB). OC Bacteria; Proteobacteria; Betaproteobacteria; Rhodocyclales; OC Azonexaceae; Dechloromonas. OX NCBI_TaxID=159087 {ECO:0000313|EMBL:AAZ47709.1, ECO:0000313|Proteomes:UP000000550}; RN [1] {ECO:0000313|Proteomes:UP000000550} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=RCB {ECO:0000313|Proteomes:UP000000550}; RX PubMed=19650930; DOI=10.1186/1471-2164-10-351; RA Salinero K.K., Keller K., Feil W.S., Feil H., Trong S., Di Bartolo G., RA Lapidus A.; RT "Metabolic analysis of the soil microbe Dechloromonas aromatica str. RT RCB: indications of a surprisingly complex life-style and cryptic RT anaerobic pathways for aromatic degradation."; RL BMC Genomics 10:351-351(2009). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000089; AAZ47709.1; -; Genomic_DNA. DR RefSeq; WP_011288707.1; NC_007298.1. DR ProteinModelPortal; Q47BS2; -. DR STRING; 159087.Daro_2979; -. DR EnsemblBacteria; AAZ47709; AAZ47709; Daro_2979. DR KEGG; dar:Daro_2979; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000000550; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000000550}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Hydrolase {ECO:0000313|EMBL:AAZ47709.1}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000000550}. FT DOMAIN 198 364 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 384 AA; 42264 MW; EE19580E63348D38 CRC64; MIERPAAGER AVIVQLDFGQ LDLEDQLEEV RLLAESAGGV VVAEVGGRRQ SPDPKTFAGK GKVDEIEAMI AATSADLVIF NHDLSPAQQR NLERALRCRV IDRTSLILDI FALRASSAEG KLQVELAQLE HLSTRLVRGW THLERQRGGI GMRGPGEKQL ETDRRLLGNR VKLLKERLNK LSRQRGVQRK ARKRGDVLSV SLVGYTNAGK STLFNALTHA GVYAADKLFA TLDTTSRKLW IEGAGNIVIS DTVGFIRNLP HSLVDAFHAT LEAATDADIL LHVVDSASHA RDEQMIEVNK VLQEIGADAV RQVIAWNKID LTDASPGVER DEYGNIARVR VSARSGEGLD LLRESLAEYA RAKAQARQKA LAEAEKQAQY DYIN // ID Q47CI1_DECAR Unreviewed; 468 AA. AC Q47CI1; DT 13-SEP-2005, integrated into UniProtKB/TrEMBL. DT 13-SEP-2005, sequence version 1. DT 30-AUG-2017, entry version 75. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Daro_2720 {ECO:0000313|EMBL:AAZ47450.1}; OS Dechloromonas aromatica (strain RCB). OC Bacteria; Proteobacteria; Betaproteobacteria; Rhodocyclales; OC Azonexaceae; Dechloromonas. OX NCBI_TaxID=159087 {ECO:0000313|EMBL:AAZ47450.1, ECO:0000313|Proteomes:UP000000550}; RN [1] {ECO:0000313|Proteomes:UP000000550} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=RCB {ECO:0000313|Proteomes:UP000000550}; RX PubMed=19650930; DOI=10.1186/1471-2164-10-351; RA Salinero K.K., Keller K., Feil W.S., Feil H., Trong S., Di Bartolo G., RA Lapidus A.; RT "Metabolic analysis of the soil microbe Dechloromonas aromatica str. RT RCB: indications of a surprisingly complex life-style and cryptic RT anaerobic pathways for aromatic degradation."; RL BMC Genomics 10:351-351(2009). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000089; AAZ47450.1; -; Genomic_DNA. DR ProteinModelPortal; Q47CI1; -. DR STRING; 159087.Daro_2720; -. DR EnsemblBacteria; AAZ47450; AAZ47450; Daro_2720. DR KEGG; dar:Daro_2720; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; VILEIFH; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000000550; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000000550}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Hydrolase {ECO:0000313|EMBL:AAZ47450.1}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000000550}. FT DOMAIN 243 413 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 201 235 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 468 AA; 51478 MW; 46019D120527440C CRC64; MAAPSVLAGT ICLCPFKRSN PGMRSEVEDK TRYAVAAAVQ LPNVSDIEFE ASLTELRELA KTLGFKVVHT FVQKRAGFDT TGYLGIGKRQ EIHDFVNHGV EGEGAIPGAA AFSGQIDAIL VDHEISPSQA RNLEKEVGCE VMDRTMVILE IFHNNARSRA ARAQVEIARL GYMAPRLREA AKLAGPQGRQ RSGAGGRGGG ESHTELDRRK IRDRIAELQQ EIVAMDVERK TQRARRQERQ GLAGVALVGY TNAGKSTLMR ALTGSEVLVA NKLFATLDTT VRTLHPESVP RVLVSDTVGF IKNLPHGLVA SFKSTLEEAL DASLLLHVID ASDPGFERQL QVTDDVLHEI GADAVPRIRV FNKIDHVGDS EAQAECEAAL REKYPDCVVM SARRPDEVAR LRLTIISFFQ QGLVEAELFL PWSAQQLRGE LYASCEVLEE RADEEGAFFR VRGEPDTLMI LREQFAQA // ID Q47RQ9_THEFY Unreviewed; 493 AA. AC Q47RQ9; DT 13-SEP-2005, integrated into UniProtKB/TrEMBL. DT 13-SEP-2005, sequence version 1. DT 07-JUN-2017, entry version 95. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Tfu_0820 {ECO:0000313|EMBL:AAZ54858.1}; OS Thermobifida fusca (strain YX). OC Bacteria; Actinobacteria; Streptosporangiales; Nocardiopsaceae; OC Thermobifida. OX NCBI_TaxID=269800 {ECO:0000313|EMBL:AAZ54858.1, ECO:0000313|Proteomes:UP000000434}; RN [1] {ECO:0000313|Proteomes:UP000000434} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=YX {ECO:0000313|Proteomes:UP000000434}; RX PubMed=17209016; DOI=10.1128/JB.01899-06; RA Lykidis A., Mavromatis K., Ivanova N., Anderson I., Land M., RA DiBartolo G., Martinez M., Lapidus A., Lucas S., Copeland A., RA Richardson P., Wilson D.B., Kyrpides N.; RT "Genome sequence and analysis of the soil cellulolytic actinomycete RT Thermobifida fusca YX."; RL J. Bacteriol. 189:2477-2486(2007). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000088; AAZ54858.1; -; Genomic_DNA. DR RefSeq; WP_011291267.1; NC_007333.1. DR ProteinModelPortal; Q47RQ9; -. DR STRING; 269800.Tfu_0820; -. DR EnsemblBacteria; AAZ54858; AAZ54858; Tfu_0820. DR KEGG; tfu:Tfu_0820; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000000434; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000000434}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000000434}. FT DOMAIN 272 437 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 493 AA; 54006 MW; 53730583A952D5D4 CRC64; MDMTRTSLNL NDHTLRTGSS VDTEDSVPAH FDGIDTTTPG EAELQDRLAL RRVNGLSTEL HDITEVEYRS LRLERVVLIG VWTSGTQEDA DNSLFELKQL AETAGAVVLA GLTQRRSKPD PATYIGSGKA AELRDIVEAT GADTVICDGE LTPGQLRQLE EAVKVKVIDR TALILDIFAQ HARSREGKAQ VELAQLTYLL PRLRGWGEAL SRQTGTSGGG NGGVGLRGPG ETKLETDRRR IHRRMAKLRR ELAHMAVARE VKRDRRRSRK VPAVAIAGYT NAGKSSLLNR ITGAGVLVED ALFATLDPTV RRARTPDGRL FTLSDTVGFV RHLPHQLVEA FRSTLEEVTE ADLILHVVDG SHPDPEQQIA SVRQVFAEID ATDIPELIVI NKIDAADETQ LRQLRTKYPG MVEVSARTGE GIGELLQAIA EALPESEHEV TVLLPYERGD LVSRIHQEGR ILSEEHTASG TVLHAWVSPE LAGQLDRYAT VAS // ID Q481U6_COLP3 Unreviewed; 455 AA. AC Q481U6; DT 13-SEP-2005, integrated into UniProtKB/TrEMBL. DT 13-SEP-2005, sequence version 1. DT 07-JUN-2017, entry version 77. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=CPS_2456 {ECO:0000313|EMBL:AAZ26711.1}; OS Colwellia psychrerythraea (strain 34H / ATCC BAA-681) (Vibrio OS psychroerythus). OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales; OC Colwelliaceae; Colwellia. OX NCBI_TaxID=167879 {ECO:0000313|EMBL:AAZ26711.1, ECO:0000313|Proteomes:UP000000547}; RN [1] {ECO:0000313|EMBL:AAZ26711.1, ECO:0000313|Proteomes:UP000000547} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=34H / ATCC BAA-681 {ECO:0000313|Proteomes:UP000000547}; RX PubMed=16043709; DOI=10.1073/pnas.0504766102; RA Methe B.A., Nelson K.E., Deming J.W., Momen B., Melamud E., Zhang X., RA Moult J., Madupu R., Nelson W.C., Dodson R.J., Brinkac L.M., RA Daugherty S.C., Durkin A.S., DeBoy R.T., Kolonay J.F., Sullivan S.A., RA Zhou L., Davidsen T.M., Wu M., Huston A.L., Lewis M., Weaver B., RA Weidman J.F., Khouri H., Utterback T.R., Feldblyum T.V., Fraser C.M.; RT "The psychrophilic lifestyle as revealed by the genome sequence of RT Colwellia psychrerythraea 34H through genomic and proteomic RT analyses."; RL Proc. Natl. Acad. Sci. U.S.A. 102:10913-10918(2005). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000083; AAZ26711.1; -; Genomic_DNA. DR RefSeq; WP_011043266.1; NC_003910.7. DR ProteinModelPortal; Q481U6; -. DR STRING; 167879.CPS_2456; -. DR EnsemblBacteria; AAZ26711; AAZ26711; CPS_2456. DR KEGG; cps:CPS_2456; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; VILEIFH; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000000547; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000000547}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000000547}. FT DOMAIN 235 400 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 196 230 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 455 AA; 50312 MW; 1CB581627C656589 CRC64; MQLTAKASLT NALLISICTP DFKGDEATES LAELARLVTT LGFKVVGTQS QKQSSTKKVN VLGLGKLAEI AHLTGNQGEV EDMEEVEDLS VGEQTDDVEF MVNSSDIPSD NLPFACADVV VFDCDLSPSQ LRNVENQLGV EVFDRTGIII EIFSRHARTK TAKLQVEIAR LNYVAPRLRE TSCGDKERQM GKGAGETTLE LNRRAVRDQL AELKRELVSV QHEMKGRRTQ RSELFCVALV GYTNAGKSSM MRAITGSDVE GENKLFATLD TTVRALFPIT QPRILVSDTV GFIKKLPHDL VASFHSTLAE AQDASLLLYV VDASDPSFRA QLDVVHEVLD EVGVEDSKKL LVLNKSDQLS IEQQQALMEE FPNAMMTSAR NPADVSKLHK YIVGIAQEEM IEEEIIVPYT ANGIIGEIRS RMSVTKEEYE NSHIKLTVRS NAIDLARLKK RMLSL // ID Q48A21_COLP3 Unreviewed; 428 AA. AC Q48A21; DT 13-SEP-2005, integrated into UniProtKB/TrEMBL. DT 13-SEP-2005, sequence version 1. DT 30-AUG-2017, entry version 77. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:AAZ24566.1}; GN OrderedLocusNames=CPS_0326 {ECO:0000313|EMBL:AAZ24566.1}; OS Colwellia psychrerythraea (strain 34H / ATCC BAA-681) (Vibrio OS psychroerythus). OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales; OC Colwelliaceae; Colwellia. OX NCBI_TaxID=167879 {ECO:0000313|EMBL:AAZ24566.1, ECO:0000313|Proteomes:UP000000547}; RN [1] {ECO:0000313|EMBL:AAZ24566.1, ECO:0000313|Proteomes:UP000000547} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=34H / ATCC BAA-681 {ECO:0000313|Proteomes:UP000000547}; RX PubMed=16043709; DOI=10.1073/pnas.0504766102; RA Methe B.A., Nelson K.E., Deming J.W., Momen B., Melamud E., Zhang X., RA Moult J., Madupu R., Nelson W.C., Dodson R.J., Brinkac L.M., RA Daugherty S.C., Durkin A.S., DeBoy R.T., Kolonay J.F., Sullivan S.A., RA Zhou L., Davidsen T.M., Wu M., Huston A.L., Lewis M., Weaver B., RA Weidman J.F., Khouri H., Utterback T.R., Feldblyum T.V., Fraser C.M.; RT "The psychrophilic lifestyle as revealed by the genome sequence of RT Colwellia psychrerythraea 34H through genomic and proteomic RT analyses."; RL Proc. Natl. Acad. Sci. U.S.A. 102:10913-10918(2005). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000083; AAZ24566.1; -; Genomic_DNA. DR RefSeq; WP_011041199.1; NC_003910.7. DR ProteinModelPortal; Q48A21; -. DR STRING; 167879.CPS_0326; -. DR EnsemblBacteria; AAZ24566; AAZ24566; CPS_0326. DR KEGG; cps:CPS_0326; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000000547; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000000547}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000000547}. FT DOMAIN 198 365 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 428 AA; 48568 MW; 0CC5682DFA72C5C0 CRC64; MFERYQAGEQ AVLVHLDFPD ESSREDLSEF KMLVSSAGVQ ALTVVTGKRN TPHPRFFVGS GKAEEIRDAV HLVGANVVLF NHSLTPSQEK NIEALCECRV VDRTTLILDI FAQRARTHEG KLQVELAQLR HMSSRLIRGW THLERQKGGI GLRGPGETQL ETDRRLLRER MVNIRKRLGK VEVQRQQGRR ARTRAELPTL SLVGYTNAGK STLFNTLTQS DVYAADQLFA TLDPTLRKID LFGVGRVILA DTVGFIRHLP HDLVAAFKAT LTETREAELL LHVVDISDDR RSENIEQVEY VLKEIEANDV PQLIICNKID NLDDIEPRID RDDQGMPIRV WLSAQANIGT ELLFTALAER LDIQVVNHQL SIPPSAGKLR GELYKLNCVT SETYDEQGHC HLEVNMPSRE WERLISTKYS ELVDYIEH // ID Q49X99_STAS1 Unreviewed; 411 AA. AC Q49X99; DT 13-SEP-2005, integrated into UniProtKB/TrEMBL. DT 13-SEP-2005, sequence version 1. DT 05-JUL-2017, entry version 86. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=SSP1454 {ECO:0000313|EMBL:BAE18599.1}; OS Staphylococcus saprophyticus subsp. saprophyticus (strain ATCC 15305 / OS DSM 20229). OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae; OC Staphylococcus. OX NCBI_TaxID=342451 {ECO:0000313|EMBL:BAE18599.1, ECO:0000313|Proteomes:UP000006371}; RN [1] {ECO:0000313|EMBL:BAE18599.1, ECO:0000313|Proteomes:UP000006371} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 15305 / DSM 20229 {ECO:0000313|Proteomes:UP000006371}; RX PubMed=16135568; DOI=10.1073/pnas.0502950102; RA Kuroda M., Yamashita A., Hirakawa H., Kumano M., Morikawa K., RA Higashide M., Maruyama A., Inose Y., Matoba K., Toh H., Kuhara S., RA Hattori M., Ohta T.; RT "Whole genome sequence of Staphylococcus saprophyticus reveals the RT pathogenesis of uncomplicated urinary tract infection."; RL Proc. Natl. Acad. Sci. U.S.A. 102:13272-13277(2005). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AP008934; BAE18599.1; -; Genomic_DNA. DR RefSeq; WP_011303222.1; NZ_MTGA01000034.1. DR ProteinModelPortal; Q49X99; -. DR STRING; 342451.SSP1454; -. DR EnsemblBacteria; BAE18599; BAE18599; SSP1454. DR GeneID; 3615081; -. DR KEGG; ssp:SSP1454; -. DR PATRIC; fig|342451.11.peg.1458; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000006371; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000006371}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000006371}. FT DOMAIN 206 364 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 411 AA; 46901 MW; CAE37591B13FAD43 CRC64; MTQQQTYTTE QSLETAILVG VHAQTDEDFN FESTMEELSS LSQTCQLNVK AQFSQNRTNV DNKFYVGKGK LDEIKAYVEF HDIDVVVAND ELTTAQSKTL NGNLNVKIID RTQLILEIFA LRARSKEGKL QVELAQLDYL MPRLQGHGRS LSRLGGGIGT RGPGETKLEM DRRHIRTRMN EIKHQLETVV EHRERYRNKR EQNHVFQVAL VGYTNAGKSS WFNALAKEST YEKKLLFATL DPKTRQIQIN DGFNLIISDT VGFIQKLPTT LIAAFKSTLE EAKNADLLLH VVDSSHPEYR AQYDTVNQIV NDLDMGQIPQ AIIFNKKDLH DGSLPATNKP HVFVSSKDEK DIEKVKSLLF NQIKQVLTYY EESVPSANAD RLYFLKQHTL ISELVFDEIN ANYQVKGYKK E // ID Q4C413_CROWT Unreviewed; 491 AA. AC Q4C413; DT 13-SEP-2005, integrated into UniProtKB/TrEMBL. DT 13-SEP-2005, sequence version 1. DT 07-JUN-2017, entry version 53. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=CwatDRAFT_3747 {ECO:0000313|EMBL:EAM50918.1}; OS Crocosphaera watsonii WH 8501. OC Bacteria; Cyanobacteria; Oscillatoriophycideae; Chroococcales; OC Aphanothecaceae; Crocosphaera. OX NCBI_TaxID=165597 {ECO:0000313|EMBL:EAM50918.1, ECO:0000313|Proteomes:UP000003922}; RN [1] {ECO:0000313|EMBL:EAM50918.1, ECO:0000313|Proteomes:UP000003922} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=WH 8501 {ECO:0000313|EMBL:EAM50918.1, RC ECO:0000313|Proteomes:UP000003922}; RG DOE Joint Genome Institute; RL Submitted (FEB-2004) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:EAM50918.1, ECO:0000313|Proteomes:UP000003922} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=WH 8501 {ECO:0000313|EMBL:EAM50918.1, RC ECO:0000313|Proteomes:UP000003922}; RG US DOE Joint Genome Institute (JGI-ORNL); RA Larimer F., Land M.; RT "Annotation of the draft genome assembly of Crocosphaera watsonii WH RT 8501."; RL Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases. RN [3] {ECO:0000313|EMBL:EAM50918.1, ECO:0000313|Proteomes:UP000003922} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=WH 8501 {ECO:0000313|EMBL:EAM50918.1, RC ECO:0000313|Proteomes:UP000003922}; RG US DOE Joint Genome Institute (JGI-PGF); RA Copeland A., Lucas S., Lapidus A., Barry K., Detter C., Glavina T., RA Hammon N., Israni S., Pitluck S., Richardson P.; RT "Sequencing of the draft genome and assembly of Crocosphaera watsonii RT WH 8501."; RL Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EAM50918.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AADV02000012; EAM50918.1; -; Genomic_DNA. DR RefSeq; WP_007305438.1; NZ_AADV02000012.1. DR ProteinModelPortal; Q4C413; -. DR EnsemblBacteria; EAM50918; EAM50918; CwatDRAFT_3747. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000003922; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000003922}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000003922}. FT DOMAIN 316 486 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 275 312 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 491 AA; 54662 MW; DA2582131A351DD1 CRC64; MPRYGAERLC GIRCIATQLK SDPPKESSLT AMVLQRLDSL VVLSITSEGK TRRGGGATGY IKEAYIAHLL PPSEFNPNHA YYWTVSPAMT IETLSEQDFF GLVEGLEEEF SREYVAQQVE GDHERVLIVG LQTDKMSDRA FAEELAEVKR LVDTAGGETV ETIQQKRPKP HPQTLVGKGK VEEIALRVQT LRANLVVFSL DLSPAQVRNL ETQLGVKVVD RTEVILDIFA QRAQSRAGKL QVELAQLEYM LPRLVGRGQA MSRLGGGIGT RGPGETKLET ERRAIQKRIS RLQQEVNKLQ SHRSRLRQQR QKQEVPSIAI VGYTNAGKST LINALTNAEV YTADQLFATL DPTTRRLSGI DDNTGQPYTF LLTDTVGFIH ELPPSLVDAF RATLEEVTEA DALLHLVDLS HPAWQHHIQS VMNILQEMPL VPGPILLVFN KIDTVDGETL KVAQEEYPLA VFISASQRLG LETLRHKLSQ LVQYALKNSS F // ID Q4FUT4_PSYA2 Unreviewed; 489 AA. AC Q4FUT4; DT 30-AUG-2005, integrated into UniProtKB/TrEMBL. DT 30-AUG-2005, sequence version 1. DT 30-AUG-2017, entry version 83. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:AAZ18224.1}; GN OrderedLocusNames=Psyc_0355 {ECO:0000313|EMBL:AAZ18224.1}; OS Psychrobacter arcticus (strain DSM 17307 / 273-4). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Moraxellaceae; Psychrobacter. OX NCBI_TaxID=259536 {ECO:0000313|EMBL:AAZ18224.1, ECO:0000313|Proteomes:UP000000546}; RN [1] {ECO:0000313|EMBL:AAZ18224.1, ECO:0000313|Proteomes:UP000000546} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 17307 / 273-4 {ECO:0000313|Proteomes:UP000000546}; RX PubMed=20154119; DOI=10.1128/AEM.02101-09; RA Ayala-del-Rio H.L., Chain P.S., Grzymski J.J., Ponder M.A., RA Ivanova N., Bergholz P.W., Di Bartolo G., Hauser L., Land M., RA Bakermans C., Rodrigues D., Klappenbach J., Zarka D., Larimer F., RA Richardson P., Murray A., Thomashow M., Tiedje J.M.; RT "The genome sequence of Psychrobacter arcticus 273-4, a psychroactive RT Siberian permafrost bacterium, reveals mechanisms for adaptation to RT low-temperature growth."; RL Appl. Environ. Microbiol. 76:2304-2312(2010). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000082; AAZ18224.1; -; Genomic_DNA. DR RefSeq; WP_011279662.1; NC_007204.1. DR ProteinModelPortal; Q4FUT4; -. DR STRING; 259536.Psyc_0355; -. DR EnsemblBacteria; AAZ18224; AAZ18224; Psyc_0355. DR KEGG; par:Psyc_0355; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000000546; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000000546}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000000546}. FT DOMAIN 200 365 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 456 480 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 489 AA; 55019 MW; 01811F2432B0AB45 CRC64; MEYFERHTGG ERAIIVHLDI RQIQDPDDLG EFELLADSAG ADRLALVTGS RARPDARYFV GSGKAEEIAE LVREHDADIV LFNHSLSPSQ ERNIEALVQC RVLDRTGLIL DIFAQRARTY EGKLQVELAQ LNHLSTRLVR GWTHLERQKG GIGLRGPGET QLETDRRLLQ VRVMQLKSRI EKVRQTRAQG RARRQKSDVP TISLVGYTNA GKSTLFNRLV DENIYAADKL FATLDPTLRR LDWQGVGRVV LVDTVGFVRH LPHELVESFH ATLEETLEAD LLLHVIDSSS EDMHEQIQAV KDVLAEIDND VPVLNVYNKI DLTDEPARIG YASEGQPNRV YVSSRENLGM EELSLAVQQL LTGTLTTFDL TLPYNAGQLK NALYELGVIQ EESYDDSGHE CLTIRLPSDR LRQLLGQANL EPLDVLPLAQ ATLLMPILEE FEKPDEDEEQ TMTDAEEKAF AEFEALNAEA ERAAQDLITE DIQTPDSQK // ID Q4JV85_CORJK Unreviewed; 484 AA. AC Q4JV85; DT 02-AUG-2005, integrated into UniProtKB/TrEMBL. DT 02-AUG-2005, sequence version 1. DT 07-JUN-2017, entry version 84. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=jk1108 {ECO:0000313|EMBL:CAI37272.1}; OS Corynebacterium jeikeium (strain K411). OC Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae; OC Corynebacterium. OX NCBI_TaxID=306537 {ECO:0000313|EMBL:CAI37272.1, ECO:0000313|Proteomes:UP000000545}; RN [1] {ECO:0000313|EMBL:CAI37272.1, ECO:0000313|Proteomes:UP000000545} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K411 {ECO:0000313|EMBL:CAI37272.1, RC ECO:0000313|Proteomes:UP000000545}; RX PubMed=15968079; DOI=10.1128/JB.187.13.4671-4682.2005; RA Tauch A., Kaiser O., Hain T., Goesmann A., Weisshaar B., RA Albersmeier A., Bekel T., Bischoff N., Brune I., Chakraborty T., RA Kalinowski J., Meyer F., Rupp O., Schneiker S., Viehoever P., RA Puehler A.; RT "Complete genome sequence and analysis of the multiresistant RT nosocomial pathogen Corynebacterium jeikeium K411, a lipid-requiring RT bacterium of the human skin flora."; RL J. Bacteriol. 187:4671-4682(2005). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CR931997; CAI37272.1; -; Genomic_DNA. DR RefSeq; WP_011273658.1; NC_007164.1. DR ProteinModelPortal; Q4JV85; -. DR STRING; 306537.jk1108; -. DR EnsemblBacteria; CAI37272; CAI37272; jk1108. DR GeneID; 3432871; -. DR KEGG; cjk:jk1108; -. DR PATRIC; fig|306537.10.peg.1121; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000000545; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000000545}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000000545}. FT DOMAIN 260 436 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 219 253 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 484 AA; 52577 MW; B2687681FFC3977B CRC64; MTEKTDKTEH TTHLYDSPAA PTVGELDLEA RSSLRRLSRG VNTYTDEQSD GYDVEYRKLR LEKVVLVGVW TTGTIAQVEA SLEELRALAE TAGSEVAEML YQRRDKPDSG TYIGRGKVEE LKSVVLETGA DTVVCDGELS PGQMIALEKA LDVKVIDRTM LILDIFAQHA KSKEGKAQVS LAQMEYLITR VRGWGGALSR QAGGRAGSNG GVGLRGPGET KIEADRRRLR SDMAKLRKEI AAMKTSREVK RERRDASAIP QIAIAGYTNA GKSSLINALT GAGVLVEDAL FATLDPTTRR ANLADGRAVV FSDTVGFVRH LPTQLVEAFR STLEEVLAAD VVLHVVDGSD PFPLEQIKAV NTVIGGIVEE SGQEAPPEIL VINKIDAADP LVLAELRHRI PDAVYVSAKT GEGIPELEAQ LELFLNSLDT HVTLHVPFDR GDVVAKLHEL GTVLEEDYDA DGTRLNVRLP KVVAAELEQF VVAE // ID Q4KJ72_PSEF5 Unreviewed; 433 AA. AC Q4KJ72; DT 02-AUG-2005, integrated into UniProtKB/TrEMBL. DT 02-AUG-2005, sequence version 1. DT 30-AUG-2017, entry version 78. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:AAY95976.1}; GN OrderedLocusNames=PFL_0567 {ECO:0000313|EMBL:AAY95976.1}; OS Pseudomonas fluorescens (strain ATCC BAA-477 / NRRL B-23932 / Pf-5). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=220664 {ECO:0000313|EMBL:AAY95976.1, ECO:0000313|Proteomes:UP000008540}; RN [1] {ECO:0000313|EMBL:AAY95976.1, ECO:0000313|Proteomes:UP000008540} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-477 / NRRL B-23932 / Pf-5 RC {ECO:0000313|Proteomes:UP000008540}; RX PubMed=15980861; DOI=10.1038/nbt1110; RA Paulsen I.T., Press C.M., Ravel J., Kobayashi D.Y., Myers G.S., RA Mavrodi D.V., DeBoy R.T., Seshadri R., Ren Q., Madupu R., Dodson R.J., RA Durkin A.S., Brinkac L.M., Daugherty S.C., Sullivan S.A., RA Rosovitz M.J., Gwinn M.L., Zhou L., Schneider D.J., Cartinhour S.W., RA Nelson W.C., Weidman J., Watkins K., Tran K., Khouri H., Pierson E.A., RA Pierson L.S.III., Thomashow L.S., Loper J.E.; RT "Complete genome sequence of the plant commensal Pseudomonas RT fluorescens Pf-5."; RL Nat. Biotechnol. 23:873-878(2005). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000076; AAY95976.1; -; Genomic_DNA. DR RefSeq; WP_011058939.1; NC_004129.6. DR ProteinModelPortal; Q4KJ72; -. DR STRING; 220664.PFL_0567; -. DR EnsemblBacteria; AAY95976; AAY95976; PFL_0567. DR GeneID; 29824265; -. DR KEGG; pfl:PFL_0567; -. DR PATRIC; fig|220664.5.peg.585; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000008540; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000008540}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000008540}. FT DOMAIN 199 366 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 165 192 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 433 AA; 48978 MW; 587A52E658669327 CRC64; MFFERHGGGE RAILVHLDGQ DPEAREDPQE FQELALSAGA ETVAFVSVPR HRPTAKYLVG SGKVEELRDL VKAEQVDLVI FNHILTPSQE RNLERVFECR VIDRTGLILD IFAQRARTHE GKLQVELAQL EHMSTRLVRG WTHLERQKGG IGLRGPGETQ LETDRRLLRV RLRQIKARLE KVRSQREQAR RGRKRADIPS VSLVGYTNAG KSTLFNAVTA SDVFAADQLF ATLDPTLRRL ELDDLGPIVL ADTVGFIRHL PHKLVEAFRA TLEESSNSDL LLHVIDAHEP ERMAQIEQVM VVLGEIGAQD LPILEVYNKL DLLEGVEPQI QRDPDGKPQR VWLSARDGQG LDLLKQAIAE LLGEDLFVGT LRLPQRFARL RAQFFQLNAV QKEDHDDEGV SLLAVRLPRA ELNRLVSREG MQPSEFIEQH TLQ // ID Q4W571_NEIMB Unreviewed; 392 AA. AC Q4W571; DT 05-JUL-2005, integrated into UniProtKB/TrEMBL. DT 05-JUL-2005, sequence version 1. DT 07-JUN-2017, entry version 73. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=NMB1041 {ECO:0000313|EMBL:AAY52150.1}; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAY52150.1, ECO:0000313|Proteomes:UP000000425}; RN [1] {ECO:0000313|EMBL:AAY52150.1, ECO:0000313|Proteomes:UP000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 {ECO:0000313|EMBL:AAY52150.1, RC ECO:0000313|Proteomes:UP000000425}; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., RA Nelson W.C., Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., RA Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., RA Mason T., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., RA Cotton M.D., Utterback T.R., Khouri H., Qin H., Vamathevan J., RA Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., RA Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE002098; AAY52150.1; -; Genomic_DNA. DR RefSeq; NP_274075.1; NC_003112.2. DR RefSeq; WP_002219225.1; NC_003112.2. DR ProteinModelPortal; Q4W571; -. DR STRING; 122586.NMB1041; -. DR PaxDb; Q4W571; -. DR DNASU; 903190; -. DR EnsemblBacteria; AAY52150; AAY52150; NMB1041. DR GeneID; 903190; -. DR KEGG; nme:NMB1041; -. DR PATRIC; fig|122586.8.peg.1326; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; FNNHAHV; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000000425}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000000425}. FT DOMAIN 215 384 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 181 208 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 392 AA; 42296 MW; 5EE467264CECA7EC CRC64; MTGRTGGNGS TQAQPERVML VGVMLDKDGT GSSAARLNGF QTALAEAVEL VKAAGGDSVR VETAKRDRPH TALFVGTGKA AELSEAVAAD GIDLVVFNHE LTPTQERNLE KELKCRVLDR VGLILAIFAR RARTQEGRLQ VELAQLSHLA GRLIRGYGHL QSQRGGIGMK GPGETKLETD RRLIAHRINA LKKQLANLKK QRALRRKSRE SGTIKTFALV GYTNVGKSSL FNRLTKSGIY AKDQLFATLD TTARRLYISP ECSIILTDTV GFVSDLPHKL ISAFSATLEE TAQADVLLHV VDAAAPNSGQ QIEDVENVLQ EIHAGDIPCI KVYNKTDLLP SEEQNTGIWR DAAGKIAAVR ISVAENTGID ALREAIAESC AAAPNTDETE MP // ID Q4XU05_PLACH Unreviewed; 371 AA. AC Q4XU05; DT 05-JUL-2005, integrated into UniProtKB/TrEMBL. DT 05-JUL-2005, sequence version 1. DT 30-AUG-2017, entry version 47. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:CAH79607.1}; DE Flags: Fragment; GN ORFNames=PC000388.03.0 {ECO:0000313|EMBL:CAH79607.1}; OS Plasmodium chabaudi. OC Eukaryota; Alveolata; Apicomplexa; Aconoidasida; Haemosporida; OC Plasmodiidae; Plasmodium; Plasmodium (Vinckeia). OX NCBI_TaxID=5825 {ECO:0000313|Proteomes:UP000002509}; RN [1] {ECO:0000313|EMBL:CAH79607.1, ECO:0000313|Proteomes:UP000002509} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=AS {ECO:0000313|Proteomes:UP000002509}; RX PubMed=15637271; DOI=10.1126/science.1103717; RA Hall N., Karras M., Raine J.D., Carlton J.M., Kooij T.W.A., RA Berriman M., Florens L., Janssen C.S., Pain A., Christophides G.K., RA James K., Rutherford K., Harris B., Harris D., Churcher C.M., RA Quail M.A., Ormond D., Doggett J., Trueman H.E., Mendoza J., RA Bidwell S.L., Rajandream M.A., Carucci D.J., Yates J.R. III, RA Kafatos F.C., Janse C.J., Barrell B.G., Turner C.M.R., Waters A.P., RA Sinden R.S.; RT "A comprehensive survey of the Plasmodium life cycle by genomic, RT transcriptomic, and proteomic analyses."; RL Science 307:82-86(2005). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CAAJ01003171; CAH79607.1; -; Genomic_DNA. DR STRING; 5825.PCHAS_091020; -. DR EnsemblProtists; CAH79607; CAH79607; PC000388.03.0. DR EuPathDB; PlasmoDB:PCHAS_0910200; -. DR eggNOG; KOG0410; Eukaryota. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000282270; -. DR InParanoid; Q4XU05; -. DR Proteomes; UP000002509; Unassembled WGS sequence. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR SUPFAM; SSF52540; SSF52540; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000002509}; KW Reference proteome {ECO:0000313|Proteomes:UP000002509}. FT DOMAIN 11 65 GTP-bdg_N. {ECO:0000259|Pfam:PF13167}. FT DOMAIN 324 365 G (guanine nucleotide-binding). FT {ECO:0000259|Pfam:PF01926}. FT NON_TER 371 371 {ECO:0000313|EMBL:CAH79607.1}. SQ SEQUENCE 371 AA; 44173 MW; 2EECA82583247B3F CRC64; MINPKYEDVE RKIAESILIK VNRIDNKFYF NQGKINEISK YYLKNPTPYI FINTILSPEQ FQNLDFLFNS ILKSYHDELK LNNKKHMETN YLSSSRLLES HFDNELSDDM NDNNDITINR SAYFDMYNNY VDVEDAEEDS EKMEFPEDEE VEDPEDIEET YSYESSIEID KKKKKKHIPL YVEIFDRYSI ILYILKSRAK SNLSKLQLEL ARANFIFNTY SDNNRSRIKY IKYIENNVLG KSFIDQEDKY DKQNIFDIDN KKKNFKMDYE YLGYNCNFIK STETYKEYEK RIINNIYNKL KKELIKCKNN NNLQNNSRKH KALIAIVGYT NVGKTKLINC LTNSNLKAKN LLFQTLDNSY KSLNIANSHS T // ID Q5E2C9_VIBF1 Unreviewed; 433 AA. AC Q5E2C9; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 30-AUG-2017, entry version 102. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:AAW86817.1}; GN OrderedLocusNames=VF_2322 {ECO:0000313|EMBL:AAW86817.1}; OS Vibrio fischeri (strain ATCC 700601 / ES114). OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; OC Vibrionaceae; Aliivibrio. OX NCBI_TaxID=312309 {ECO:0000313|EMBL:AAW86817.1, ECO:0000313|Proteomes:UP000000537}; RN [1] {ECO:0000313|EMBL:AAW86817.1, ECO:0000313|Proteomes:UP000000537} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700601 / ES114 {ECO:0000313|Proteomes:UP000000537}; RX PubMed=15703294; DOI=10.1073/pnas.0409900102; RA Ruby E.G., Urbanowski M., Campbell J., Dunn A., Faini M., Gunsalus R., RA Lostroh P., Lupp C., McCann J., Millikan D., Schaefer A., Stabb E., RA Stevens A., Visick K., Whistler C., Greenberg E.P.; RT "Complete genome sequence of Vibrio fischeri: a symbiotic bacterium RT with pathogenic congeners."; RL Proc. Natl. Acad. Sci. U.S.A. 102:3004-3009(2005). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000020; AAW86817.1; -; Genomic_DNA. DR RefSeq; WP_011262724.1; NC_006840.2. DR RefSeq; YP_205705.1; NC_006840.2. DR ProteinModelPortal; Q5E2C9; -. DR STRING; 312309.VF_2322; -. DR EnsemblBacteria; AAW86817; AAW86817; VF_2322. DR GeneID; 3279424; -. DR KEGG; vfi:VF_2322; -. DR PATRIC; fig|312309.11.peg.2361; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000000537; Chromosome I. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000000537}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000000537}. FT DOMAIN 198 365 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 433 AA; 49005 MW; 22064C354658E9D5 CRC64; MFDRYESGEQ AILVHIDFTY QGEIEDLNEC KMLISSAGVN TVGVVTGTRQ SPLPKYYVGE GKAQEIADAV RANNADIVIF NHALSPAQER NLEQLCQCRV IDRTGLILDI FAQRARTYEG KLQVELAQLR HISTRLIRGW THLERQKGGI GLRGPGETQL ETDRRLLRER IKAILRRLGK VAKQREQGRR ARHRAEIPTI SLVGYTNAGK STLFNRITEA GVYAADQLFA TLDPTLRKIE VADVGTSILA DTVGFIRHLP HDLVAAFKAT LQETQEANIL LHVVDASDER FRENIEAVDI VLEEIDANEV PTLLVMNKID NLEDQQPRIE RDEEGIPRCV WVSAMEGKGI ELLFQALTER LSGQMVEHSL LLPPDWVGRL RSKFFQMQCI LNEEYQDDGS LLVDVRMQQV DWSKLEKRED APLSDFIITK ESA // ID Q5E680_VIBF1 Unreviewed; 452 AA. AC Q5E680; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 07-JUN-2017, entry version 79. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=VF_0971 {ECO:0000313|EMBL:AAW85466.1}; OS Vibrio fischeri (strain ATCC 700601 / ES114). OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; OC Vibrionaceae; Aliivibrio. OX NCBI_TaxID=312309 {ECO:0000313|EMBL:AAW85466.1, ECO:0000313|Proteomes:UP000000537}; RN [1] {ECO:0000313|EMBL:AAW85466.1, ECO:0000313|Proteomes:UP000000537} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700601 / ES114 {ECO:0000313|Proteomes:UP000000537}; RX PubMed=15703294; DOI=10.1073/pnas.0409900102; RA Ruby E.G., Urbanowski M., Campbell J., Dunn A., Faini M., Gunsalus R., RA Lostroh P., Lupp C., McCann J., Millikan D., Schaefer A., Stabb E., RA Stevens A., Visick K., Whistler C., Greenberg E.P.; RT "Complete genome sequence of Vibrio fischeri: a symbiotic bacterium RT with pathogenic congeners."; RL Proc. Natl. Acad. Sci. U.S.A. 102:3004-3009(2005). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000020; AAW85466.1; -; Genomic_DNA. DR RefSeq; WP_011261607.1; NC_006840.2. DR RefSeq; YP_204354.1; NC_006840.2. DR ProteinModelPortal; Q5E680; -. DR STRING; 312309.VF_0971; -. DR EnsemblBacteria; AAW85466; AAW85466; VF_0971. DR GeneID; 3277507; -. DR KEGG; vfi:VF_0971; -. DR PATRIC; fig|312309.11.peg.969; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; VILEIFH; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000000537; Chromosome I. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000000537}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000000537}. FT DOMAIN 225 390 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 186 220 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 452 AA; 50233 MW; 6CDCB057983E21A7 CRC64; MKLTEKPLLN NALLISICTP QFKGEEAKQS LAELARLVTT LGFKVVGTQS QKQTSTQKMS VLGAGKLAEI AHITGNQGEG TDADTEDFFD ETDFDDIPSE NLPFGCADVV VFDCDLSPSQ LRNVENQLGV QVYDRTGIII EIFSRHARTR TARLQVEMAR LNYVAPRLRE SSIGDSERQM GKGSGETSLE LDRRKVRDQL AELRRELDSV QDELKGRRAQ RSELFCVALV GYTNAGKSSM MRALTGSEVL VENKLFATLD TTVRALYPET QPRILVSDTV GFIKKLPHDL VASFHSTLAE AHDASLLLYV VDASDPTFRT QLDVVHEVLG EVGVDGIDKL LVLNKSDQLT PEQQQALMEE FPDAMMTSTR NPLDVAKLHQ YIVNASEKGM IEEELIVPYD AKGIMGEIRS SMSVVNEEYD YDHMKLTVRS SAIDLARLKK LMSNVLNEND SE // ID Q5F8S6_NEIG1 Unreviewed; 392 AA. AC Q5F8S6; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 2. DT 07-JUN-2017, entry version 79. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=NGO_0684 {ECO:0000313|EMBL:AAW89411.2}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89411.2, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE004969; AAW89411.2; -; Genomic_DNA. DR ProteinModelPortal; Q5F8S6; -. DR DNASU; 3281914; -. DR EnsemblBacteria; AAW89411; AAW89411; NGO_0684. DR KEGG; ngo:NGO_0684; -. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 215 384 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 181 208 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 392 AA; 42693 MW; 50062913B9A31013 CRC64; MSGRTGRNSA TQAQPERVML VGVMLDKDDT GSNAARLNGF QTALAEAVEL VKAAGGDSVR VETAKRDRPH TALFVGTGKA AELSEAVAAD GIDLVVFNHE LTPTQERNLE KILQCRVLDR VGLILAIFAR RARTQEGRLQ VELAQLSHLA GRLIRGYGHL QSQRGGIGMK GPGETKLETD RRLTAHRINA LKKQLANLKK QRALRRKSRE SGRIKTFALV GYTNVGKSSL FNRLTKSGIY AKDQLFATLD TTARRLYISP ACSIILTDTV GFVSDLPHKL ISAFSATLEE TVQADVLLHV VDAAARNSGQ QIEDVENVLQ EIHAHDIPCI KVYNKTDLLP SEEQNTGIWR DAAGKIAAVR ISVAENTGID ALREAIAEYC AAAPNTDETE MP // ID Q5FIC4_LACAC Unreviewed; 421 AA. AC Q5FIC4; DT 01-MAR-2005, integrated into UniProtKB/TrEMBL. DT 01-MAR-2005, sequence version 1. DT 07-JUN-2017, entry version 79. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:AAV43550.1}; GN OrderedLocusNames=LBA1738 {ECO:0000313|EMBL:AAV43550.1}; OS Lactobacillus acidophilus (strain ATCC 700396 / NCK56 / N2 / NCFM). OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; OC Lactobacillus. OX NCBI_TaxID=272621 {ECO:0000313|Proteomes:UP000006381}; RN [1] {ECO:0000313|EMBL:AAV43550.1, ECO:0000313|Proteomes:UP000006381} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700396 / NCK56 / N2 / NCFM RC {ECO:0000313|Proteomes:UP000006381}; RX PubMed=15671160; DOI=10.1073/pnas.0409188102; RA Altermann E., Russell W.M., Azcarate-Peril M.A., Barrangou R., RA Buck B.L., McAuliffe O., Souther N., Dobson A., Duong T., Callanan M., RA Lick S., Hamrick A., Cano R., Klaenhammer T.R.; RT "Complete genome sequence of the probiotic lactic acid bacterium RT Lactobacillus acidophilus NCFM."; RL Proc. Natl. Acad. Sci. U.S.A. 102:3906-3912(2005). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000033; AAV43550.1; -; Genomic_DNA. DR RefSeq; WP_003549861.1; NC_006814.3. DR RefSeq; YP_194581.1; NC_006814.3. DR ProteinModelPortal; Q5FIC4; -. DR STRING; 272621.LBA1738; -. DR EnsemblBacteria; AAV43550; AAV43550; LBA1738. DR GeneID; 3251443; -. DR KEGG; lac:LBA1738; -. DR PATRIC; fig|272621.13.peg.1659; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR Proteomes; UP000006381; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000006381}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000006381}. FT DOMAIN 199 368 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 421 AA; 47113 MW; 150C0B5C9210364F CRC64; MIDNQPKKTK AYIAGVNLKD PNFDYYMTEL ANLTEANNME VVGQSSQNAE SIVAGTYFGV GKINEIKSMA QGLKAKVLVL NDELTPVQIR NLEKLTKMRV IDRTELILEI FASRARTKQA KLQVQLARLQ YELPRLHPSE NNLDQQRGGG FSNRGAGESK LELNRRTIGK QISAIKKELK AVASQEEIKS ARRNQSRIPK VALVGYTNAG KSTTMNGLLR EFSKEGSDKE VFVKNMLFAT LDTSVRRIDL KDNFSFILSD TVGFISKLPH NLVESFKATL QETRDADLLI NVVDASDPNM VQMIRTTQNV LDEIGVKGIP MITAYNKADK TDRNYPQIEG SDILYSATDP KSIKLLADLI TKRVFSDYGK FNLTLPLSAG KELAYLHENA QILSENYEDD GVHIEANIAP DDQGRFKEYL V // ID Q5GYM2_XANOR Unreviewed; 439 AA. AC Q5GYM2; DT 01-MAR-2005, integrated into UniProtKB/TrEMBL. DT 01-MAR-2005, sequence version 1. DT 05-JUL-2017, entry version 95. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:AAW76199.1}; GN OrderedLocusNames=XOO2945 {ECO:0000313|EMBL:AAW76199.1}; OS Xanthomonas oryzae pv. oryzae (strain KACC10331 / KXO85). OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales; OC Xanthomonadaceae; Xanthomonas. OX NCBI_TaxID=291331 {ECO:0000313|EMBL:AAW76199.1, ECO:0000313|Proteomes:UP000006735}; RN [1] {ECO:0000313|EMBL:AAW76199.1, ECO:0000313|Proteomes:UP000006735} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=KACC10331 / KXO85 {ECO:0000313|Proteomes:UP000006735}; RX PubMed=15673718; DOI=10.1093/nar/gki206; RA Lee B.M., Park Y.J., Park D.S., Kang H.W., Kim J.G., Song E.S., RA Park I.C., Yoon U.H., Hahn J.H., Koo B.S., Lee G.B., Kim H., RA Park H.S., Yoon K.O., Kim J.H., Jung C.H., Koh N.H., Seo J.S., RA Go S.J.; RT "The genome sequence of Xanthomonas oryzae pathovar oryzae KACC10331, RT the bacterial blight pathogen of rice."; RL Nucleic Acids Res. 33:577-586(2005). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE013598; AAW76199.1; -; Genomic_DNA. DR ProteinModelPortal; Q5GYM2; -. DR EnsemblBacteria; AAW76199; AAW76199; XOO2945. DR KEGG; xoo:XOO2945; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR Proteomes; UP000006735; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000006735}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000006735}. FT DOMAIN 199 369 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 158 192 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 439 AA; 48647 MW; 912087C1DFABB58A CRC64; MFDRSRKGEH ALLIQTHSGG PAEDDGMEEF ADLAKSAGAT VAATLTARID KPSPSTLIGS GKLEEVKAAA EATGADLVLV NHTLSPGQER NLEKYLERRV IDRTGLILDI FAQRARSHEG KLQVELAQLR HMATRLVRGW THLERQRGGS IGLRGPGETQ LETDRRLLQK RVEQLQQRLE KVEVQRTQMR RARMRSELPR IALVGYTNAG KSTLFNALTG AEAYVADQLF ATLDPTVRRI ALPGGSAILA DTVGFVRDLP HELVAAFRST LSEARDADLL LHIVDAADPL REERILQVDE VLQAVGAGDL PQLLVFNKID KIDGAEVRHD AQDGIPDPAR RERVWVSARD GRGLEELQHA LGQRLDLCHL TGQLRLPPSA GRLRSRLHQL EVVRNEQSDE EGWLLDVDLP MVEAERLAAG EDGAPLRAML PDRREDWEA // ID Q5HPN5_STAEQ Unreviewed; 416 AA. AC Q5HPN5; DT 15-FEB-2005, integrated into UniProtKB/TrEMBL. DT 15-FEB-2005, sequence version 1. DT 05-JUL-2017, entry version 89. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=SERP0873 {ECO:0000313|EMBL:AAW54280.1}; OS Staphylococcus epidermidis (strain ATCC 35984 / RP62A). OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae; OC Staphylococcus. OX NCBI_TaxID=176279 {ECO:0000313|EMBL:AAW54280.1, ECO:0000313|Proteomes:UP000000531}; RN [1] {ECO:0000313|EMBL:AAW54280.1, ECO:0000313|Proteomes:UP000000531} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 35984 / RP62A {ECO:0000313|Proteomes:UP000000531}; RX PubMed=15774886; DOI=10.1128/JB.187.7.2426-2438.2005; RA Gill S.R., Fouts D.E., Archer G.L., Mongodin E.F., Deboy R.T., RA Ravel J., Paulsen I.T., Kolonay J.F., Brinkac L., Beanan M., RA Dodson R.J., Daugherty S.C., Madupu R., Angiuoli S.V., Durkin A.S., RA Haft D.H., Vamathevan J., Khouri H., Utterback T., Lee C., RA Dimitrov G., Jiang L., Qin H., Weidman J., Tran K., Kang K., RA Hance I.R., Nelson K.E., Fraser C.M.; RT "Insights on evolution of virulence and resistance from the complete RT genome analysis of an early methicillin-resistant Staphylococcus RT aureus strain and a biofilm-producing methicillin-resistant RT Staphylococcus epidermidis strain."; RL J. Bacteriol. 187:2426-2438(2005). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000029; AAW54280.1; -; Genomic_DNA. DR RefSeq; WP_002439586.1; NC_002976.3. DR ProteinModelPortal; Q5HPN5; -. DR STRING; 176279.SERP0873; -. DR PRIDE; Q5HPN5; -. DR EnsemblBacteria; AAW54280; AAW54280; SERP0873. DR KEGG; ser:SERP0873; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR Proteomes; UP000000531; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000000531}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000000531}. FT DOMAIN 209 372 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 416 AA; 47768 MW; 4409C931BD45408E CRC64; MYNVTQHATY KTKNKRETAV LIGVHAQTDR QFNFESTMEE LDALSQTCQL NVKGQITQNR EQFDHKYYVG KGKIDEIKSF IEFHDIDVVV TNDELTTAQS KTLNDNLGIK IIDRTQLILE IFALRARSRE GKLQVELAQL DYLLPRLHGH GKSLSRLGGG IGTRGPGETK LEMDRRHIRT RMNEIKHQLK TVVDHRERYR NKREQNQVFQ IALVGYTNAG KSSWFNVLAN EETYEKNILF ATLDPKTRQI QVNEGFNLII SDTVGFIQKL PTTLVAAFKS TLEEAKGADV LMHVVDASHS EYRTQIDTVN QIINDLDMDH IPQVVIFNKK DLCNEQMDVP VSKSAHVFVS SRDENDKQKV KNLVIQEIKN SLSPYEEIVD SADADRLYFL KQHTLVTELI FDETQASYRI KGFKKL // ID Q5L0C7_GEOKA Unreviewed; 415 AA. AC Q5L0C7; DT 01-FEB-2005, integrated into UniProtKB/TrEMBL. DT 01-FEB-2005, sequence version 1. DT 05-JUL-2017, entry version 83. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=GK1324 {ECO:0000313|EMBL:BAD75609.1}; OS Geobacillus kaustophilus (strain HTA426). OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus; OC Geobacillus thermoleovorans group. OX NCBI_TaxID=235909 {ECO:0000313|EMBL:BAD75609.1, ECO:0000313|Proteomes:UP000001172}; RN [1] {ECO:0000313|EMBL:BAD75609.1, ECO:0000313|Proteomes:UP000001172} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=HTA426 {ECO:0000313|EMBL:BAD75609.1, RC ECO:0000313|Proteomes:UP000001172}; RX PubMed=15576355; DOI=10.1093/nar/gkh970; RA Takami H., Takaki Y., Chee G.J., Nishi S., Shimamura S., Suzuki H., RA Matsui S., Uchiyama I.; RT "Thermoadaptation trait revealed by the genome sequence of RT thermophilic Geobacillus kaustophilus."; RL Nucleic Acids Res. 32:6292-6303(2004). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BA000043; BAD75609.1; -; Genomic_DNA. DR RefSeq; WP_011230823.1; NC_006510.1. DR ProteinModelPortal; Q5L0C7; -. DR STRING; 235909.GK1324; -. DR EnsemblBacteria; BAD75609; BAD75609; GK1324. DR GeneID; 32063220; -. DR KEGG; gka:GK1324; -. DR PATRIC; fig|235909.7.peg.1431; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000001172; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000001172}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Hydrolase {ECO:0000313|EMBL:BAD75609.1}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Protease {ECO:0000313|EMBL:BAD75609.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000001172}. FT DOMAIN 197 358 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 415 AA; 46265 MW; 5674A88F868FD5D5 CRC64; MSREQAILVG CQLAGVDDER FRYSMEELAS LVATANGEVV AEVTQKREAP HPATYIGKGK TEELAAIVKQ LEPDVVIFNS ELSPSQARNL TKMLGEVKVI DRTQLILDIF ARRARSKEGK LQVELAQLEY MLPRLSGQGE ALSRLGGGIG TRGPGETKLE TDRRHIRRRI DDIKAELVRI AEHRGRYRER RQKNQAFQVA LVGYTNAGKS TIFNRLTAAD SLEENLLFAT LDPLTRKCVL PCGYTVLVTD TVGFIQDLPT TLVAAFRSTL EEVTEADLLL HVVDSSHPDY VAHERTVSRL LAELGASSIP MVTVYNKSDQ KASEFIPTTT ASIMISALSA ADIDRLRYFL EEAVKQQMAR YDVSIPSGEG KLLARLKSDT ILHEWHYNEQ GGTYDCQGYV LPTHPLYGEL QSFQR // ID Q5LHN0_BACFN Unreviewed; 417 AA. AC Q5LHN0; DT 21-JUN-2005, integrated into UniProtKB/TrEMBL. DT 21-JUN-2005, sequence version 1. DT 07-JUN-2017, entry version 98. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=BF9343_0571 {ECO:0000313|EMBL:CAH06350.1}; OS Bacteroides fragilis (strain ATCC 25285 / DSM 2151 / JCM 11019 / NCTC OS 9343). OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae; OC Bacteroides. OX NCBI_TaxID=272559 {ECO:0000313|EMBL:CAH06350.1, ECO:0000313|Proteomes:UP000006731}; RN [1] {ECO:0000313|EMBL:CAH06350.1, ECO:0000313|Proteomes:UP000006731} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 25285 / DSM 2151 / JCM 11019 / NCTC 9343 RC {ECO:0000313|Proteomes:UP000006731}; RX PubMed=15746427; DOI=10.1126/science.1107008; RA Cerdeno-Tarraga A.-M., Patrick S., Crossman L.C., Blakely G., RA Abratt V., Lennard N., Poxton I., Duerden B., Harris B., Quail M.A., RA Barron A., Clark L., Corton C., Doggett J., Holden M.T.G., Larke N., RA Line A., Lord A., Norbertczak H., Ormond D., Price C., RA Rabbinowitsch E., Woodward J., Barrell B.G., Parkhill J.; RT "Extensive DNA inversions in the B. fragilis genome control variable RT gene expression."; RL Science 307:1463-1465(2005). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CR626927; CAH06350.1; -; Genomic_DNA. DR RefSeq; WP_005796343.1; NC_003228.3. DR ProteinModelPortal; Q5LHN0; -. DR STRING; 272559.BF0598; -. DR EnsemblBacteria; CAH06350; CAH06350; BF9343_0571. DR KEGG; bfs:BF9343_0571; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR KO; K03665; -. DR OMA; HPATYIG; -. DR BioCyc; BFRA272559:GKF0-577-MONOMER; -. DR Proteomes; UP000006731; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000006731}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000006731}. FT DOMAIN 215 399 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 417 AA; 47516 MW; EBEA7A7435AF7B24 CRC64; MKEFVISEAK VETAVLVGLI TQTQDERKTN EYLDELAFLA ETAGAEVVKR FTQKLPTANS VTYVGKGKLE EIKEYIRIEA EEDREVGMVI FDDELSAKQI RNIEAELKVK ILDRTSLILD IFAMRAQTAN AKTQVELAQY KYMLPRLQRL WTHLERQGGG SGSGKGGSVG LRGPGETQLE MDRRIILNRM SLLKERLAEI DKQKSTQRKN RGRMIRVALV GYTNVGKSTM MNLLAKSEVF AENKLFATLD TTVRKVIIDN LPFLLSDTVG FIRKLPTDLV DSFKSTLDEV READLLVHVV DISHPGFEEQ IEVVNKTLAD IGGGGKPMIL IFNKIDAYTY VEKAPDDLTP KTKENLTLEE LMKTWMAKME DNCLFISARE KINIDELKSV VYQRVKELHV QKYPYNDFLY QTYEEEE // ID Q5LRP5_RUEPO Unreviewed; 424 AA. AC Q5LRP5; DT 01-FEB-2005, integrated into UniProtKB/TrEMBL. DT 01-FEB-2005, sequence version 1. DT 07-JUN-2017, entry version 97. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:AAV95351.1}; GN OrderedLocusNames=SPO2080 {ECO:0000313|EMBL:AAV95351.1}; OS Ruegeria pomeroyi (strain ATCC 700808 / DSM 15171 / DSS-3) OS (Silicibacter pomeroyi). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae; Ruegeria. OX NCBI_TaxID=246200 {ECO:0000313|EMBL:AAV95351.1, ECO:0000313|Proteomes:UP000001023}; RN [1] {ECO:0000313|EMBL:AAV95351.1, ECO:0000313|Proteomes:UP000001023} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700808 / DSM 15171 / DSS-3 RC {ECO:0000313|Proteomes:UP000001023}; RX PubMed=15602564; DOI=10.1038/nature03170; RA Moran M.A., Buchan A., Gonzalez J.M., Heidelberg J.F., Whitman W.B., RA Kiene R.P., Henriksen J.R., King G.M., Belas R., Fuqua C., Brinkac L., RA Lewis M., Johri S., Weaver B., Pai G., Eisen J.A., Rahe E., RA Sheldon W.M., Ye W., Miller T.R., Carlton J., Rasko D.A., RA Paulsen I.T., Ren Q., Daugherty S.C., Deboy R.T., Dodson R.J., RA Durkin A.S., Madupu R., Nelson W.C., Sullivan S.A., Rosovitz M.J., RA Haft D.H., Selengut J., Ward N.; RT "Genome sequence of Silicibacter pomeroyi reveals adaptations to the RT marine environment."; RL Nature 432:910-913(2004). RN [2] {ECO:0000313|EMBL:AAV95351.1, ECO:0000313|Proteomes:UP000001023} RP GENOME REANNOTATION. RC STRAIN=ATCC 700808 / DSM 15171 / DSS-3 RC {ECO:0000313|Proteomes:UP000001023}; RX PubMed=25780504; DOI=10.1186/1944-3277-9-11; RA Rivers A.R., Smith C.B., Moran M.A.; RT "An updated genome annotation for the model marine bacterium Ruegeria RT pomeroyi DSS-3."; RL Stand. Genomic Sci. 9:11-11(2014). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000031; AAV95351.1; -; Genomic_DNA. DR ProteinModelPortal; Q5LRP5; -. DR STRING; 246200.SPO2080; -. DR EnsemblBacteria; AAV95351; AAV95351; SPO2080. DR KEGG; sil:SPO2080; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000001023; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000001023}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000001023}. FT DOMAIN 204 373 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 424 AA; 47081 MW; 4DBD1E2C70054D7A CRC64; MMEHDRARTR AWVLHPELKS DLDRRDPVPA LEEAVALAAA LPDLDVVGSG IVRLPKPHPG HLFGSGKVEE LATLFHDNEV ELVLIDGPLS PVQQRNLEKA WKVKILDRTG LILEIFSDRA RTREGVLQVE MAALSYQRTR LVRAWTHLER QRGGLGFVGG PGETQIEADR RAIDEQLVRL KRQLDKVVKT RELHRKARAK VPYPIVALVG YTNAGKSTLF NRLTGAEVMA KDMLFATLDP TMRRVVLPDG PEVILSDTVG FISDLPTELV AAFRATLEEV LAADLIVHVR DIHHAATEEQ ARDVETILAS LGVDEGRPKF EVWNKVDLLD PDKRAALRER TARDPSLFAV SAVTGEGLES LLTAIAEALA ETRSEAVLTL GFADGKRRAW LFAQDVVQAE EQSDDGFRLT VLWTPRQAAR YAAL // ID Q5M3Y1_STRT2 Unreviewed; 412 AA. AC Q5M3Y1; DT 01-FEB-2005, integrated into UniProtKB/TrEMBL. DT 01-FEB-2005, sequence version 1. DT 07-JUN-2017, entry version 94. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:AAV60862.1}; GN OrderedLocusNames=stu1228 {ECO:0000313|EMBL:AAV60862.1}; OS Streptococcus thermophilus (strain ATCC BAA-250 / LMG 18311). OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=264199 {ECO:0000313|EMBL:AAV60862.1, ECO:0000313|Proteomes:UP000001170}; RN [1] {ECO:0000313|EMBL:AAV60862.1, ECO:0000313|Proteomes:UP000001170} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-250 / LMG 18311 {ECO:0000313|Proteomes:UP000001170}; RX PubMed=15543133; DOI=10.1038/nbt1034; RA Bolotin A., Quinquis B., Renault P., Sorokin A., Ehrlich S.D., RA Kulakauskas S., Lapidus A., Goltsman E., Mazur M., Pusch G.D., RA Fonstein M., Overbeek R., Kyprides N., Purnelle B., Prozzi D., RA Ngui K., Masuy D., Hancy F., Burteau S., Boutry M., Delcour J., RA Goffeau A., Hols P.; RT "Complete sequence and comparative genome analysis of the dairy RT bacterium Streptococcus thermophilus."; RL Nat. Biotechnol. 22:1554-1558(2004). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000023; AAV60862.1; -; Genomic_DNA. DR RefSeq; WP_011226137.1; NC_006448.1. DR ProteinModelPortal; Q5M3Y1; -. DR STRING; 264199.stu1228; -. DR DNASU; 3164884; -. DR EnsemblBacteria; AAV60862; AAV60862; stu1228. DR KEGG; stl:stu1228; -. DR PATRIC; fig|264199.4.peg.1210; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR Proteomes; UP000001170; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000001170}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000001170}. FT DOMAIN 199 359 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 158 192 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 412 AA; 46892 MW; C81556727E7B50BB CRC64; MIETAKQQER AILVGVELQE TENFDMSMEE LASLAKTAGA EVVASYTQKR ERYDSKSFVG SGKLEEIKAM VDTDEITTVI VNNRLTPRQN TNLEAAFGVK VIDRMQLILD IFAMRARSHE GKLQVHLAQL KYMLPRLSGQ GIMLSRQAGG IGSRGPGESQ LELNRRSIRN QIADIERQLK IVEKNRETIR EKRVDSTTFK IGLIGYTNAG KSTIMNLMTD DKQYEANELF ATLDATTKKI YLKDQFQVTL TDTVGFIQDL PTELVAAFKS TLEESRNVDL LLHVIDASDP NHEEHENVVL DILKELDMTD IPRLAIYNKM DVANNLVATV FPNVRLSARD KGSREALRKL LIDEIQQNFE HFSIKVNQDQ AYKLYQLSQL ALLDSYSFET EVEEITGYIS PKNKWKLEEF YD // ID Q5NH40_FRATT Unreviewed; 435 AA. AC Q5NH40; DT 01-FEB-2005, integrated into UniProtKB/TrEMBL. DT 01-FEB-2005, sequence version 1. DT 30-AUG-2017, entry version 90. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:CAG45264.1}; GN OrderedLocusNames=FTT_0631 {ECO:0000313|EMBL:CAG45264.1}; OS Francisella tularensis subsp. tularensis (strain SCHU S4 / Schu 4). OC Bacteria; Proteobacteria; Gammaproteobacteria; Thiotrichales; OC Francisellaceae; Francisella. OX NCBI_TaxID=177416 {ECO:0000313|EMBL:CAG45264.1, ECO:0000313|Proteomes:UP000001174}; RN [1] {ECO:0000313|EMBL:CAG45264.1, ECO:0000313|Proteomes:UP000001174} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SCHU S4 / Schu 4 {ECO:0000313|Proteomes:UP000001174}; RX PubMed=15640799; DOI=10.1038/ng1499; RA Larsson P., Oyston P.C.F., Chain P., Chu M., Duffield M., RA Fuxelius H.H., Garcia E., Halltorp G., Johansson D., Isherwood K., RA Karp P., Larsson E., Lui Y., Michell S., Prior J., Prior R., RA Sjostedt A., Svensson K., Thompson N., Vergez L., Wagg J., Wren B., RA Lindler L.E., Andersson S.G., Forsman M., Titball R.W.; RT "The complete genome sequence of Francisella tularensis, the causative RT agent of tularemia."; RL Nat. Genet. 37:153-159(2005). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AJ749949; CAG45264.1; -; Genomic_DNA. DR RefSeq; WP_003020374.1; NZ_CP010290.1. DR RefSeq; YP_169652.1; NC_006570.2. DR IntAct; Q5NH40; 1. DR STRING; 177416.FTT_0631; -. DR DNASU; 3192427; -. DR EnsemblBacteria; AJI68568; AJI68568; BZ14_188. DR EnsemblBacteria; CAG45264; CAG45264; FTT_0631. DR GeneID; 3192427; -. DR KEGG; ftu:FTT_0631; -. DR PATRIC; fig|177416.36.peg.191; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR Proteomes; UP000001174; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000001174}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Hydrolase {ECO:0000313|EMBL:CAG45264.1}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Protease {ECO:0000313|EMBL:CAG45264.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000001174}. SQ SEQUENCE 435 AA; 50150 MW; 253938DE179F39F1 CRC64; MEFFQSYQAG SKCLLVNINF KYHRELNADL TELEGLVIAA EKVVLQSLDF NHPEPDIKYF CGMGKIEMIK NKRDELEADL VVFNHPLTPS QERNIEKFLE CRVMDRTRLI LEIFSLRAKT YEGKLQVELA QLNYQSTRLV KGWTHLERQK GGIGVRGGPG ETQLEIDRRL IRQRIKQIAQ KLEKVKHHRD LSRSSRKKNN IPTISFVGYT NAGKSTLFNK ITNADVLAKD QLFATLDPTL RKVIVPKLGE VIFSDTVGFI KNLPHNLVEA FHATLEEAIE SDLLVHVIDY ADEDHKSYIE QVEKVLSEIG IADKETICVY NKIDKLENIK PSFVPLEDSD SSVVSRVYLS AQNGDGLVEF YQALATFFNK TWINQTLYLP PKYSKVRAKM YELGVIDKEE ISEHGNYLLQ IKISQDDFER FKRELNLDLE EFFVK // ID Q5NQN2_ZYMMO Unreviewed; 460 AA. AC Q5NQN2; DT 01-FEB-2005, integrated into UniProtKB/TrEMBL. DT 01-FEB-2005, sequence version 1. DT 07-JUN-2017, entry version 86. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=ZMO0348 {ECO:0000313|EMBL:AAV88972.1}; OS Zymomonas mobilis subsp. mobilis (strain ATCC 31821 / ZM4 / CP4). OC Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales; OC Sphingomonadaceae; Zymomonas. OX NCBI_TaxID=264203 {ECO:0000313|EMBL:AAV88972.1, ECO:0000313|Proteomes:UP000001173}; RN [1] {ECO:0000313|EMBL:AAV88972.1, ECO:0000313|Proteomes:UP000001173} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 31821 / ZM4 / CP4 {ECO:0000313|Proteomes:UP000001173}; RX PubMed=15592456; DOI=10.1038/nbt1045; RA Seo J.S., Chong H., Park H.S., Yoon K.O., Jung C., Kim J.J., RA Hong J.H., Kim H., Kim J.H., Kil J.I., Park C.J., Oh H.M., Lee J.S., RA Jin S.J., Um H.W., Lee H.J., Oh S.J., Kim J.Y., Kang H.L., Lee S.Y., RA Lee K.J., Kang H.S.; RT "The genome sequence of the ethanologenic bacterium Zymomonas mobilis RT ZM4."; RL Nat. Biotechnol. 23:63-68(2005). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE008692; AAV88972.1; -; Genomic_DNA. DR RefSeq; WP_011240271.1; NC_006526.2. DR ProteinModelPortal; Q5NQN2; -. DR EnsemblBacteria; AAV88972; AAV88972; ZMO0348. DR KEGG; zmo:ZMO0348; -. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR Proteomes; UP000001173; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000001173}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000001173}. FT DOMAIN 209 385 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 460 AA; 50894 MW; 329F9204C5D5BB3B CRC64; MSGFVRSEAD GVSHGARVLI VLPELEDNNK RSTEARLEEA TGLACAIGLD VVSKLAFHLR APKASTLFGP GQVEQIVTAA RDEEVDLVIV DGPLTPIQQR NLETSLDVKV IDRTGLILEI FGARAATAEG RLQVELAHLD YQAGRLVRTW THLERQRGGF GFLGGPGETQ IEADRRMIRD RMAKLRRDLA QVTRTRGLHR ARRKKAPWPV VALVGYTNAG KSTLFNRMTG ADVMAKDLLF ATLDPTMRQI TLPGIDKAIL SDTVGFVSDL PTQLVAAFRA TLEEVTAADL ILHVRDIAQE DSESEREDVE RVLAEIGIAP VEDGGEFAIP VIEAWNKSDL LSEEAHESLA AEAARRDDVA LISAWTGEGI EDLRELVSQR LSEAHRLRHI DIPVTEGQAM AWLYAHGEVV SDVMNDETGK MEFDVRMSDE NWGRFIERFG FLYQDMSSSE DESEDLHPSL // ID Q5P7B9_AROAE Unreviewed; 385 AA. AC Q5P7B9; DT 04-JAN-2005, integrated into UniProtKB/TrEMBL. DT 04-JAN-2005, sequence version 1. DT 07-JUN-2017, entry version 84. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:CAI06792.1}; GN ORFNames=ebA1254 {ECO:0000313|EMBL:CAI06792.1}; OS Aromatoleum aromaticum (strain EbN1) (Azoarcus sp. (strain EbN1)). OC Bacteria; Proteobacteria; Betaproteobacteria; Rhodocyclales; OC Rhodocyclaceae; Aromatoleum. OX NCBI_TaxID=76114 {ECO:0000313|EMBL:CAI06792.1, ECO:0000313|Proteomes:UP000006552}; RN [1] {ECO:0000313|EMBL:CAI06792.1, ECO:0000313|Proteomes:UP000006552} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=EbN1 {ECO:0000313|EMBL:CAI06792.1, RC ECO:0000313|Proteomes:UP000006552}; RX PubMed=15551059; DOI=10.1007/s00203-004-0742-9; RA Rabus R., Kube M., Heider J., Beck A., Heitmann K., Widdel F., RA Reinhardt R.; RT "The genome sequence of an anaerobic aromatic-degrading denitrifying RT bacterium, strain EbN1."; RL Arch. Microbiol. 183:27-36(2005). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CR555306; CAI06792.1; -; Genomic_DNA. DR RefSeq; WP_011236520.1; NC_006513.1. DR ProteinModelPortal; Q5P7B9; -. DR STRING; 76114.ebA1254; -. DR EnsemblBacteria; CAI06792; CAI06792; ebA1254. DR KEGG; eba:ebA1254; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000006552; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000006552}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000006552}. FT DOMAIN 198 364 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 385 AA; 41757 MW; 8EBA53A660BAC093 CRC64; MFERPASGER AVLVQLDLNQ GALDERLSEL RLLAVSAGAS VEAVIGGRRA KPDPALFAGR GKVDEIAEAL RVHDADLVIF NHALSPAQQR NLERSLECRV IDRTALILDI FAQRARSHEG KLQVELAQLD HLSTRLVRGW THLERQKGGI GLRGPGETQL ETDRRLLGMR VRTLKERLAR IEKQRRVRRR GRLGRGVLSV SLVGYTNAGK STLFNALTKA GAYAADQLFA TLDTTSRRLY VGEGGNVVLS DTVGFIRDLP HSLVAAFHST LEETASADLL LHVVDAASED REAQVDAVNR VLVEIGAGDV PQIMVMNKID LTQAEAAANR DEYGKIDRVF LSARTGEGLG LLRDALAEAA RAAAAAPEDP AGSSPNLTDI DPIQT // ID Q5P8I2_AROAE Unreviewed; 467 AA. AC Q5P8I2; DT 04-JAN-2005, integrated into UniProtKB/TrEMBL. DT 04-JAN-2005, sequence version 1. DT 07-JUN-2017, entry version 84. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=ebA503 {ECO:0000313|EMBL:CAI06377.1}; OS Aromatoleum aromaticum (strain EbN1) (Azoarcus sp. (strain EbN1)). OC Bacteria; Proteobacteria; Betaproteobacteria; Rhodocyclales; OC Rhodocyclaceae; Aromatoleum. OX NCBI_TaxID=76114 {ECO:0000313|EMBL:CAI06377.1, ECO:0000313|Proteomes:UP000006552}; RN [1] {ECO:0000313|EMBL:CAI06377.1, ECO:0000313|Proteomes:UP000006552} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=EbN1 {ECO:0000313|EMBL:CAI06377.1, RC ECO:0000313|Proteomes:UP000006552}; RX PubMed=15551059; DOI=10.1007/s00203-004-0742-9; RA Rabus R., Kube M., Heider J., Beck A., Heitmann K., Widdel F., RA Reinhardt R.; RT "The genome sequence of an anaerobic aromatic-degrading denitrifying RT bacterium, strain EbN1."; RL Arch. Microbiol. 183:27-36(2005). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CR555306; CAI06377.1; -; Genomic_DNA. DR ProteinModelPortal; Q5P8I2; -. DR STRING; 76114.ebA503; -. DR EnsemblBacteria; CAI06377; CAI06377; ebA503. DR KEGG; eba:ebA503; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; VILEIFH; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000006552; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000006552}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000006552}. FT DOMAIN 241 411 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 199 233 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 467 AA; 52271 MW; F9C533A797A531C7 CRC64; MLWRSSPNRP SPKCTIRLCP LTRRNLRMQS EVQGKPTYAV AAAVQLPNVS DVEFEASLTE LRELAKTLGL TVVHTFIQKR SGFDTTAYLG TGKRQEIREF VDAGGVVDGK SHEIDVILVD HEISPSQARH LELEVGCEVT DRTMVILEIF HRNARSRAAR AQVEIARLGY MAPRLREAAK LAGPQGRQRS GTGGRGAGES HTELDRRKVR DRIAELQEEI DAMEVERKTQ RARRQGRQSV ANVALVGYTN AGKSTLMRAL TGSEVLVANK LFATLDTTVR VIYPESVPRV LVSDTVGFIK NLPHGLVASF KSTLDEALDA SLLLHVIDAS DPGFERQREV TDQVLAEIGA DVLPRLRVFN KIDHVGDAEA QAEREAALRA QYPDCVVMSA RRPEDVAKLR QRIVTFFQQD LVAAELFLPW SAQQWRKDIY ANCEVVDERA DDEGAFFHVR GERDTVESLR EQFEQVR // ID Q5QW98_IDILO Unreviewed; 428 AA. AC Q5QW98; DT 04-JAN-2005, integrated into UniProtKB/TrEMBL. DT 04-JAN-2005, sequence version 1. DT 30-AUG-2017, entry version 82. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:AAV81177.1}; GN OrderedLocusNames=IL0334 {ECO:0000313|EMBL:AAV81177.1}; OS Idiomarina loihiensis (strain ATCC BAA-735 / DSM 15497 / L2-TR). OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales; OC Idiomarinaceae; Idiomarina. OX NCBI_TaxID=283942 {ECO:0000313|EMBL:AAV81177.1, ECO:0000313|Proteomes:UP000001171}; RN [1] {ECO:0000313|EMBL:AAV81177.1, ECO:0000313|Proteomes:UP000001171} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-735 / DSM 15497 / L2-TR RC {ECO:0000313|Proteomes:UP000001171}; RX PubMed=15596722; DOI=10.1073/pnas.0407638102; RA Hou S., Saw J.H., Lee K.S., Freitas T.A., Belisle C., Kawarabayasi Y., RA Donachie S.P., Pikina A., Galperin M.Y., Koonin E.V., Makarova K.S., RA Omelchenko M.V., Sorokin A., Wolf Y.I., Li Q.X., Keum Y.S., RA Campbell S., Denery J., Aizawa S., Shibata S., Malahoff A., Alam M.; RT "Genome sequence of the deep-sea gamma-proteobacterium Idiomarina RT loihiensis reveals amino acid fermentation as a source of carbon and RT energy."; RL Proc. Natl. Acad. Sci. U.S.A. 101:18036-18041(2004). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE017340; AAV81177.1; -; Genomic_DNA. DR RefSeq; WP_011233596.1; NC_006512.1. DR ProteinModelPortal; Q5QW98; -. DR STRING; 283942.IL0334; -. DR EnsemblBacteria; AAV81177; AAV81177; IL0334. DR KEGG; ilo:IL0334; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000001171; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000001171}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000001171}. FT DOMAIN 198 365 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 428 AA; 48080 MW; AF02959245EF149C CRC64; MFDRYEGGDY AILVHVDLPA EVDREDLSEL QLLADSSGVK TMGVMTTSRN SPTPRYFVGS GKAEEIAEQV KLLDANIVIF NHALSPTQER NLEAICKCRV LDRTGLILDI FAQRARTHEG KLQVELAQLR HISTRLVRGW THLERQKGGI GLRGPGETQL ETDRRLIRGR IKNILKRLEK VQKQREQGRR ARKKADIPTV SLVGYTNAGK STLFNRLTEA GVYAADQLFA TLDPTLRKLA VEDIGEVILA DTVGFIRHLP HDLVAAFKAT LQETQEADLL LHVVDVSDEQ QQNNIDQVAE VLEEIDAGDV PQLIICNKID QVEGAEPRID YDDNQKPIRV WVSAQQGLGI EEVLEALRQI LGPQMVELTL KIPHSMGKLR GTLYRWNSVT SEDVNENGEL ALQVRMSSVD WQRLHKAYGN QLDDLVVQ // ID Q5SKS7_THET8 Unreviewed; 503 AA. AC Q5SKS7; DT 21-DEC-2004, integrated into UniProtKB/TrEMBL. DT 21-DEC-2004, sequence version 1. DT 07-JUN-2017, entry version 79. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=TTHA0566 {ECO:0000313|EMBL:BAD70389.1}; OS Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579). OC Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; OC Thermus. OX NCBI_TaxID=300852 {ECO:0000313|EMBL:BAD70389.1, ECO:0000313|Proteomes:UP000000532}; RN [1] {ECO:0000313|EMBL:BAD70389.1, ECO:0000313|Proteomes:UP000000532} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=HB8 / ATCC 27634 / DSM 579 {ECO:0000313|Proteomes:UP000000532}; RA Masui R., Kurokawa K., Nakagawa N., Tokunaga F., Koyama Y., RA Shibata T., Oshima T., Yokoyama S., Yasunaga T., Kuramitsu S.; RT "Complete genome sequence of Thermus thermophilus HB8."; RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AP008226; BAD70389.1; -; Genomic_DNA. DR RefSeq; WP_011228029.1; NC_006461.1. DR RefSeq; YP_143832.1; NC_006461.1. DR ProteinModelPortal; Q5SKS7; -. DR STRING; 300852.TTHA0566; -. DR EnsemblBacteria; BAD70389; BAD70389; BAD70389. DR GeneID; 3168867; -. DR KEGG; ttj:TTHA0566; -. DR PATRIC; fig|300852.9.peg.565; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; EREVIIT; -. DR PhylomeDB; Q5SKS7; -. DR Proteomes; UP000000532; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000000532}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000000532}. FT DOMAIN 330 493 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 289 323 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 503 AA; 55817 MW; 22A17C40C69498CE CRC64; MGRPLSLVLD REGRVVRVAV GDAKDVPFPE EGWSERRLSG YRLLHTHLGP GGLSRPDLSV LFLRRLDNLA ALEVEADGRP GLLHLAFLSP PRALEEDWRV LPPKPFHQYL DLDLWGEVMA LEEELSRQAR VLEVRDGSGE RALLVGVDTG EGPEAEAVLR ELAELTRTAG GVPVRQILVF RKSLDPRYLV GLGKLEELKS LAYHENASTL IFGVDLTPAQ AREIERVTGL KVLDRTQLIL DIFALHAKTP EAQAQVELAQ LRYLLPRLVG KGKEMSRLGG GIGTRGPGET KLEVDRRRLQ DRIAHLSRKL QDYALRRQEA RQKRKRRGVP LVAVVGYTNA GKTTLLRALT RAGEEGEDKL FATLRPLTRR GFLPGVGEVL FTDTVGFIRH MPEELLTAFR ATLEEVREAD VLVHVLDASE EGALERHRVV RDLLLDLGVE APVVLALNKA DRAAPYDLYF LGERLGGVPV SALKGTGLKE LKEALARALL DLGVRPQAWA QYT // ID Q5WK06_BACSK Unreviewed; 420 AA. AC Q5WK06; DT 23-NOV-2004, integrated into UniProtKB/TrEMBL. DT 23-NOV-2004, sequence version 1. DT 07-JUN-2017, entry version 82. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=ABC0760 {ECO:0000313|EMBL:BAD63299.1}; OS Bacillus clausii (strain KSM-K16). OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus. OX NCBI_TaxID=66692 {ECO:0000313|EMBL:BAD63299.1, ECO:0000313|Proteomes:UP000001168}; RN [1] {ECO:0000313|Proteomes:UP000001168} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=KSM-K16 {ECO:0000313|Proteomes:UP000001168}; RA Takaki Y., Kageyama Y., Shimamura S., Suzuki H., Nishi S., Hatada Y., RA Kawai S., Ito S., Horikoshi K.; RT "The complete genome sequence of the alkaliphilic Bacillus clausii RT KSM-K16."; RL Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AP006627; BAD63299.1; -; Genomic_DNA. DR ProteinModelPortal; Q5WK06; -. DR STRING; 66692.ABC0760; -. DR EnsemblBacteria; BAD63299; BAD63299; ABC0760. DR KEGG; bcl:ABC0760; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; FNNHAHV; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000001168; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000001168}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000001168}. FT DOMAIN 199 363 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 158 192 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 420 AA; 47758 MW; FD448A951379846A CRC64; MRQTTQPTII VGVELQKDTD FHYSMEELNN LADALDLQVV GQLTQKLPVP NQATYIGAGK ASELSMMCES LGATLVVFND ELSPSQIRNL EKLLEVTVYD RTMLILDIFG ERAKTKEAQL QVEMARLRYL LPRLVGMRAS LSRQGGSGTG LANRGAGETK LELDRRKIEA RIHALEKDLE EIVKRRELQR KRRKKQALPV VALVGYTNAG KSSLMNAMLD NAEEKRVFEK DMLFATLDTS VRKVELDKNH SVLLADTVGF VSKLPTHLVK AFRSTLEEAR EADLLLHVVD YSNERHREMA KTTNETLQAM EIDRPMIYVY NKMDRLKEAF PQAHGDELFI SAKTKQGLDL LAQKIASYVF QDLEKHLFIV PYRDGEAAAY LNNHAHVHTQ RAEEDGWHIV ADLHERDLKR VESYCVSKEQ // ID Q5YT15_NOCFA Unreviewed; 548 AA. AC Q5YT15; DT 23-NOV-2004, integrated into UniProtKB/TrEMBL. DT 23-NOV-2004, sequence version 1. DT 07-JUN-2017, entry version 84. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=NFA_38280 {ECO:0000313|EMBL:BAD58676.1}; OS Nocardia farcinica (strain IFM 10152). OC Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae; Nocardia. OX NCBI_TaxID=247156 {ECO:0000313|EMBL:BAD58676.1, ECO:0000313|Proteomes:UP000006820}; RN [1] {ECO:0000313|EMBL:BAD58676.1, ECO:0000313|Proteomes:UP000006820} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=IFM 10152 {ECO:0000313|EMBL:BAD58676.1, RC ECO:0000313|Proteomes:UP000006820}; RX PubMed=15466710; DOI=10.1073/pnas.0406410101; RA Ishikawa J., Yamashita A., Mikami Y., Hoshino Y., Kurita H., Hotta K., RA Shiba T., Hattori M.; RT "The complete genomic sequence of Nocardia farcinica IFM 10152."; RL Proc. Natl. Acad. Sci. U.S.A. 101:14925-14930(2004). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AP006618; BAD58676.1; -; Genomic_DNA. DR ProteinModelPortal; Q5YT15; -. DR STRING; 247156.nfa38280; -. DR EnsemblBacteria; BAD58676; BAD58676; NFA_38280. DR KEGG; nfa:NFA_38280; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000006820; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000006820}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000006820}. FT DOMAIN 313 482 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 272 306 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 548 AA; 58929 MW; 25703A4661EDF44A CRC64; MHATPPAWQH GWCMRKSETF DITSTSGAND DADQAEFTSD IDLTDGDVTD ENDDYAREGD VLAERAARMK RNGWTAEPTA GELQLEERSS LRRVAGLSTE LTDITEVEYR QLRLERVVLV GVWTSGTAAQ AEASMAELAA LAETAGSQVL EALIQRRDKP DPATYIGSGK ADELRAVVLE TGADTVICDG ELTPAQLTAL EKVVKVKVID RTALILDIFA QHATSSEGKA QVSLAQMEYM LPRLRGWGES MSRQAGGRAG SNGGVGLRGP GETKIETDRR RIRERMAKLR REIREMKTAR ETKRARRASS GIPQVAIVGY TNAGKSSLMN ALTGSGVLVQ DALFATLDPT TRRAELDDGR EVVFTDTVGF VRHLPTQLVE AFRSTLEEVT GADLLLHVVD GSDPDPAGQI KAVREVIADV IKESGAAAPP ELLVVNKIDA ISPMRRTELR GLLPDAEFVS AHTGAGVDGL RARLNEVLGG LDVEVGVLLP YTRGDLLARV HADGRILESA HEEGGTRLRA RVPHALAAAL SEYAHAGAAG EPVGAERT // ID Q5ZZK0_LEGPH Unreviewed; 419 AA. AC Q5ZZK0; DT 23-NOV-2004, integrated into UniProtKB/TrEMBL. DT 23-NOV-2004, sequence version 1. DT 30-AUG-2017, entry version 95. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=lpg0010 {ECO:0000313|EMBL:AAU26118.1}; OS Legionella pneumophila subsp. pneumophila (strain Philadelphia 1 / OS ATCC 33152 / DSM 7513). OC Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales; OC Legionellaceae; Legionella. OX NCBI_TaxID=272624 {ECO:0000313|EMBL:AAU26118.1, ECO:0000313|Proteomes:UP000000609}; RN [1] {ECO:0000313|EMBL:AAU26118.1, ECO:0000313|Proteomes:UP000000609} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Philadelphia 1 / ATCC 33152 / DSM 7513 RC {ECO:0000313|Proteomes:UP000000609}; RX PubMed=15448271; DOI=10.1126/science.1099776; RA Chien M., Morozova I., Shi S., Sheng H., Chen J., Gomez S.M., RA Asamani G., Hill K., Nuara J., Feder M., Rineer J., Greenberg J.J., RA Steshenko V., Park S.H., Zhao B., Teplitskaya E., Edwards J.R., RA Pampou S., Georghiou A., Chou I.C., Iannuccilli W., Ulz M.E., RA Kim D.H., Geringer-Sameth A., Goldsberry C., Morozov P., Fischer S.G., RA Segal G., Qu X., Rzhetsky A., Zhang P., Cayanis E., De Jong P.J., RA Ju J., Kalachikov S., Shuman H.A., Russo J.J.; RT "The genomic sequence of the accidental pathogen Legionella RT pneumophila."; RL Science 305:1966-1968(2004). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE017354; AAU26118.1; -; Genomic_DNA. DR RefSeq; WP_010945772.1; NC_002942.5. DR RefSeq; YP_094065.1; NC_002942.5. DR ProteinModelPortal; Q5ZZK0; -. DR STRING; 272624.lpg0010; -. DR PaxDb; Q5ZZK0; -. DR EnsemblBacteria; AAU26118; AAU26118; lpg0010. DR GeneID; 19831577; -. DR KEGG; lpn:lpg0010; -. DR PATRIC; fig|272624.6.peg.11; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; FNNHAHV; -. DR Proteomes; UP000000609; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000000609}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000000609}. FT DOMAIN 203 368 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 419 AA; 47119 MW; 99762D19D0E247CD CRC64; MGIRVVFERP QGGERAVLVQ LALPGVDADK ALAEFEELAL SAKAEVLDCV LGARATPDAK YYVGKGKAEE IAHLVNMLDA DLVLVNHELS PSQERNLERL FGCRVVDRSG LILDIFAQRA RTFEGKLQVE LAQLQHLSTR LIRGWTHLER QKGGIGLRGP GETQLETDRR LLRERIRYIN KRLEKVRCSR DQNRQARRKA SMPTVSLVGY TNAGKSTLFN VLTGEHTYVA DQLFATLDPT MRKLELPGSS AAILADTVGF IRDLPHHLVE AFRATLEETQ QADLLLHVID ISDPNWRETV FEVQKVLDEL KVNNIPVIQV FNKIDLQEGW QPKIDYTEDS CKVWLSATTG AGLDLLKEAI ATQLHGMILI EDIVIKPDQA KLRAQLYQLG AVLKESVDEN GDWLMKIRIT ADQKRRLLS // ID Q606N4_METCA Unreviewed; 433 AA. AC Q606N4; DT 23-NOV-2004, integrated into UniProtKB/TrEMBL. DT 23-NOV-2004, sequence version 1. DT 07-JUN-2017, entry version 93. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=MCA1982 {ECO:0000313|EMBL:AAU91986.1}; OS Methylococcus capsulatus (strain ATCC 33009 / NCIMB 11132 / Bath). OC Bacteria; Proteobacteria; Gammaproteobacteria; Methylococcales; OC Methylococcaceae; Methylococcus. OX NCBI_TaxID=243233 {ECO:0000313|EMBL:AAU91986.1, ECO:0000313|Proteomes:UP000006821}; RN [1] {ECO:0000313|EMBL:AAU91986.1, ECO:0000313|Proteomes:UP000006821} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33009 / NCIMB 11132 / Bath RC {ECO:0000313|Proteomes:UP000006821}; RX PubMed=15383840; DOI=10.1371/journal.pbio.0020303; RA Ward N.L., Larsen O., Sakwa J., Bruseth L., Khouri H.M., Durkin A.S., RA Dimitrov G., Jiang L., Scanlan D., Kang K.H., Lewis M.R., Nelson K.E., RA Methe B.A., Wu M., Heidelberg J.F., Paulsen I.T., Fouts D.E., RA Ravel J., Tettelin H., Ren Q., Read T.D., DeBoy R.T., Seshadri R., RA Salzberg S.L., Jensen H.B., Birkeland N.K., Nelson W.C., Dodson R.J., RA Grindhaug S.H., Holt I.E., Eidhammer I., Jonasen I., Vanaken S., RA Utterback T.R., Feldblyum T.V., Fraser C.M., Lillehaug J.R., RA Eisen J.A.; RT "Genomic insights into methanotrophy: the complete genome sequence of RT Methylococcus capsulatus (Bath)."; RL PLoS Biol. 2:1616-1628(2004). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE017282; AAU91986.1; -; Genomic_DNA. DR RefSeq; WP_010961227.1; NC_002977.6. DR ProteinModelPortal; Q606N4; -. DR STRING; 243233.MCA1982; -. DR EnsemblBacteria; AAU91986; AAU91986; MCA1982. DR KEGG; mca:MCA1982; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000006821; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000006821}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000006821}. FT DOMAIN 197 363 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 163 190 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 433 AA; 47845 MW; CAC11BB0C87CA498 CRC64; MFDRPGIGSR AVLVHMPLAG PDQEDLDEFR LLSLSAGAEA VATLAGRLRA VDPRFYIGQG KLEELAETVK VHEADLVLFN HALTPSQERN LEKALNIRVV DRNGLILDIF AQRARSFEGR LQVELAQLKH LSTRLVRGWT HLERQKGGIG LRGPGETQLE TDKRLLANRI RQIQKRLQQV EVQRDQGRQA RRRAQVPVVG LVGYTNAGKS TLFNALTRAD VYAADQLFAT LDPTLRRLSA GGLDMVLADT VGFIRHLPHE LVAAFRSTLQ ESAEADLLLH VVDATDERMD ETIAEVRQVL AEIGADRIPC VEVYNKVDGL DGVVPHVERN ASGRPARVWI SARSGAGLDL LKGLLEEVLG GGVERRILTL TAGQGQLRAR LYREARILWD EPDGEGGWRL SVEFPASARA LRRAIGDAPE RADCEDLLTV SPR // ID Q63US7_BURPS Unreviewed; 392 AA. AC Q63US7; DT 25-OCT-2004, integrated into UniProtKB/TrEMBL. DT 25-OCT-2004, sequence version 1. DT 07-JUN-2017, entry version 94. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:CAH35520.1}; GN OrderedLocusNames=BPSL1519 {ECO:0000313|EMBL:CAH35520.1}; OS Burkholderia pseudomallei (strain K96243). OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Burkholderia; pseudomallei group. OX NCBI_TaxID=272560 {ECO:0000313|EMBL:CAH35520.1, ECO:0000313|Proteomes:UP000000605}; RN [1] {ECO:0000313|EMBL:CAH35520.1, ECO:0000313|Proteomes:UP000000605} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K96243 {ECO:0000313|EMBL:CAH35520.1, RC ECO:0000313|Proteomes:UP000000605}; RX PubMed=15377794; DOI=10.1073/pnas.0403302101; RA Holden M.T.G., Titball R.W., Peacock S.J., Cerdeno-Tarraga A.M., RA Atkins T., Crossman L.C., Pitt T., Churcher C., Mungall K., RA Bentley S.D., Sebaihia M., Thomson N.R., Bason N., Beacham I.R., RA Brooks K., Brown K.A., Brown N.F., Challis G.L., Cherevach I., RA Chillingworth T., Cronin A., Crosset B., Davis P., DeShazer D., RA Feltwell T., Fraser A., Hance Z., Hauser H., Holroyd S., Jagels K., RA Keith K.E., Maddison M., Moule S., Price C., Quail M.A., RA Rabbinowitsch E., Rutherford K., Sanders M., Simmonds M., RA Songsivilai S., Stevens K., Tumapa S., Vesaratchavest M., RA Whitehead S., Yeats C., Barrell B.G., Oyston P.C.F., Parkhill J.; RT "Genomic plasticity of the causative agent of melioidosis, RT Burkholderia pseudomallei."; RL Proc. Natl. Acad. Sci. U.S.A. 101:14240-14245(2004). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BX571965; CAH35520.1; -; Genomic_DNA. DR RefSeq; WP_011205018.1; NZ_CP009538.1. DR RefSeq; YP_108139.1; NC_006350.1. DR ProteinModelPortal; Q63US7; -. DR STRING; 272560.BPSL1519; -. DR EnsemblBacteria; CAH35520; CAH35520; BPSL1519. DR GeneID; 3092452; -. DR KEGG; bps:BPSL1519; -. DR PATRIC; fig|272560.6.peg.1707; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR Proteomes; UP000000605; Chromosome 1. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000000605}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000000605}. FT DOMAIN 196 367 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 162 189 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 392 AA; 42861 MW; 3C10BF56D61BFEBC CRC64; MTSDNLINAA LVGIDFGKTD FEASLEELSL LASSAGAHPA VTLTGRRSSP DAALFVGSGK ADELRLACEA NDVEIVIFNH ALAPAQQRNL ERVLNRRVID RTSLILDIFA QRARSHEGKL QVELAQLQYL ATRLIRAWTH LERQKGGIGL RGPGETQLET DRRLIGERIK MLKSRLDKLR RQHHTQRRQR ARSGTLSVSL VGYTNAGKST LFNALTKAQA YAADQLFATL DTTSRRVYLG DEVGQIVVSD TVGFIRELPH QLVAAFRATL EETIHADLLL HVVDASSAVR LEQIEQVNDV LREIGADSIR QILVFNKIDA VPELAARGGA VERDEYGNIS RVFLSARTGQ GLDSLRAAIA EIATAEHLVG AAPLDGAPAL PHEDHPVSEH GR // ID Q65J82_BACLD Unreviewed; 420 AA. AC Q65J82; Q62UN8; DT 25-OCT-2004, integrated into UniProtKB/TrEMBL. DT 25-OCT-2004, sequence version 1. DT 07-JUN-2017, entry version 100. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=ynbA {ECO:0000313|EMBL:AAU23521.1}; GN Synonyms=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=BL03236 {ECO:0000313|EMBL:AAU23521.1}; OS Bacillus licheniformis (strain ATCC 14580 / DSM 13 / JCM 2505 / NBRC OS 12200 / NCIMB 9375 / NRRL NRS-1264 / Gibson 46). OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus. OX NCBI_TaxID=279010 {ECO:0000313|EMBL:AAU23521.1, ECO:0000313|Proteomes:UP000000606}; RN [1] {ECO:0000313|EMBL:AAU23521.1, ECO:0000313|Proteomes:UP000000606} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 14580 / DSM 13 / JCM 2505 / NBRC 12200 / NCIMB 9375 / NRRL RC NRS-1264 / Gibson 46 {ECO:0000313|Proteomes:UP000000606}; RX PubMed=15461803; DOI=10.1186/gb-2004-5-10-r77; RA Rey M.W., Ramaiya P., Nelson B.A., Brody-Karpin S.D., Zaretsky E.J., RA Tang M., Lopez de Leon A., Xiang H., Gusti V., Clausen I.G., RA Olsen P.B., Rasmussen M.D., Andersen J.T., Jorgensen P.L., RA Larsen T.S., Sorokin A., Bolotin A., Lapidus A., Galleron N., RA Ehrlich S.D., Berka R.M.; RT "Complete genome sequence of the industrial bacterium Bacillus RT licheniformis and comparisons with closely related Bacillus species."; RL Genome Biol. 5:R77.1-R77.12(2004). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000002; AAU23521.1; -; Genomic_DNA. DR RefSeq; WP_003182138.1; NC_006322.1. DR ProteinModelPortal; Q65J82; -. DR STRING; 279010.BLi01990; -. DR EnsemblBacteria; AAU23521; AAU23521; BL03236. DR GeneID; 3031229; -. DR KEGG; bli:BL03236; -. DR PATRIC; fig|279010.13.peg.1995; -. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR Proteomes; UP000000606; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000000606}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000000606}. FT DOMAIN 201 363 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 287 311 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 420 AA; 47601 MW; E3EA98B001B03139 CRC64; MNEQEVMKEK AILVGCQLPH VSDERFSYSM EELAALTKTA DGTVVSTVTQ KRNRVDAATY IGKGKVDELA VLCEELSPDV LIFNDELSPS QLKALVTTLD VKIIDRTQLI LDIFAKRART REGKLQIELA QLQYALPRLS GQGINLSRQG GGIGTRGPGE TKLETDRRHI RNRIHEINVQ LSTVIRHRSR YRERRKKNGV LQIALVGYTN AGKSTWFNRL TDADSYEENL LFATLDPMTR KMMLPSGYSV LLSDTVGFIQ DLPTTLIAAF RSTLEEVKEA DLILHMIDSS HEDYEGHEET VKRLLEELEA DDIPVLTVYN KRDRKRPDFI PSSGRGHIMT SAKIDGDLPL FKQAVEDYLK KELLVPYDVR IPASEGRLLS RIKSETMTNS TVFDEDREAY EVEGYILPDQ NILGELKKYM // ID Q65SD4_MANSM Unreviewed; 448 AA. AC Q65SD4; DT 25-OCT-2004, integrated into UniProtKB/TrEMBL. DT 25-OCT-2004, sequence version 1. DT 30-AUG-2017, entry version 83. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:AAU38126.1}; GN OrderedLocusNames=MS1519 {ECO:0000313|EMBL:AAU38126.1}; OS Mannheimia succiniciproducens (strain MBEL55E). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Basfia. OX NCBI_TaxID=221988 {ECO:0000313|EMBL:AAU38126.1, ECO:0000313|Proteomes:UP000000607}; RN [1] {ECO:0000313|EMBL:AAU38126.1, ECO:0000313|Proteomes:UP000000607} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MBEL55E {ECO:0000313|EMBL:AAU38126.1, RC ECO:0000313|Proteomes:UP000000607}; RX PubMed=15378067; DOI=10.1038/nbt1010; RA Hong S.H., Kim J.S., Lee S.Y., In Y.H., Choi S.S., Rih J.-K., RA Kim C.H., Jeong H., Hur C.G., Kim J.J.; RT "The genome sequence of the capnophilic rumen bacterium Mannheimia RT succiniciproducens."; RL Nat. Biotechnol. 22:1275-1281(2004). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE016827; AAU38126.1; -; Genomic_DNA. DR RefSeq; WP_011200692.1; NC_006300.1. DR ProteinModelPortal; Q65SD4; -. DR STRING; 221988.MS1519; -. DR EnsemblBacteria; AAU38126; AAU38126; MS1519. DR KEGG; msu:MS1519; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000000607; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000000607}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000000607}. FT DOMAIN 218 385 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 184 214 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 448 AA; 50137 MW; CD748A50EFF540D8 CRC64; MNNDVNISKS AVNFTALSSI SAPRSDQSDN AIVVHVFFSQ DKNPEDLDEF QQLAQSANVN ILQVITAARS TPQAKYFVGQ GKAEEIAQAV ETHNADVVLV NHSLTPAQAR NLESLCQCRV VDRTGLILDI FAQRARSHEG KLQVELAQLK HLATRLVRRK TGLDQQKGAV GLRGPGETQL ETDRRLIKVR IAQLQNRLAK VEKQRNQNRQ TRQKADIPTI SLVGYTNAGK STLFNRITQA NVYAADQLFA TLDPTLRRLQ IQDVGTTILA DTVGFIRDLP HDLVSAFKST LQETTEAGLL LHIIDAADPR KLENIEAVNA VLEEIKAADL PTLLVYNKID TLENLEPHIE YDDQHIPVAV YLSAISAEGI DLLFAAIREK LKNEILHLQL NLSPNEGKIR HQLYLLDCIR REEISDQGEF LLEIQIDKIQ WLKLAKKFPQ LEKCGKNL // ID Q67MI5_SYMTH Unreviewed; 464 AA. AC Q67MI5; DT 11-OCT-2004, integrated into UniProtKB/TrEMBL. DT 11-OCT-2004, sequence version 1. DT 07-JUN-2017, entry version 83. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=STH2123 {ECO:0000313|EMBL:BAD41108.1}; OS Symbiobacterium thermophilum (strain T / IAM 14863). OC Bacteria; Firmicutes; Clostridia; Clostridiales; Symbiobacteriaceae; OC Symbiobacterium. OX NCBI_TaxID=292459 {ECO:0000313|EMBL:BAD41108.1, ECO:0000313|Proteomes:UP000000417}; RN [1] {ECO:0000313|EMBL:BAD41108.1, ECO:0000313|Proteomes:UP000000417} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=T / IAM 14863 {ECO:0000313|Proteomes:UP000000417}; RX PubMed=15383646; DOI=10.1093/nar/gkh830; RA Ueda K., Yamashita A., Ishikawa J., Shimada M., Watsuji T., RA Morimura K., Ikeda H., Hattori M., Beppu T.; RT "Genome sequence of Symbiobacterium thermophilum, an uncultivable RT bacterium that depends on microbial commensalism."; RL Nucleic Acids Res. 32:4937-4944(2004). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AP006840; BAD41108.1; -; Genomic_DNA. DR ProteinModelPortal; Q67MI5; -. DR STRING; 292459.STH2123; -. DR EnsemblBacteria; BAD41108; BAD41108; STH2123. DR KEGG; sth:STH2123; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000000417; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000000417}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000000417}. FT DOMAIN 245 410 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 204 241 {ECO:0000256|SAM:Coils}. FT COILED 388 415 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 464 AA; 51844 MW; 3A112741E843ABC6 CRC64; MGLRPFCVAE AAAPARVGPT GEGPGELNRN NDKEWPFMNE TELRNRQATA FLVGLELPSA YRDGWSAAES LDELERLVDT AGATVVGREV QSRPAPDVAT YIGRGKAEEI ELLRRELDFD FVIFDDELTP VQQRNLEKII ECQVLDRTAV ILDIFALRAR TREAKLQVEL AQLGYRLPRL TGKGVELSRQ AGSAGTVFNR GPGETKLEVD RRRIRDRMAA LRRELEEIKA HRERLRAERR ESAVPVVALT GYTNAGKSTL HRVLAGSDVL AEDRLFATLD ATTRRVQPAE GEPYLLVDTV GFIHNLPHHL VAAFRSTLEE VNQADLLLHV VDASHPKRAE QMATVHRVLE ELGAGDKPTL VVYNKIDRVD PAELDHLMRQ TPGAVAVAAA LGRNLDRLQA AIQQALHERR EVLEVVIPYA RSAWLSWVHE RGRVLTEEHR EDGTYVTVEL ERGLAARLRA ALDE // ID Q6A8Z3_PROAC Unreviewed; 483 AA. AC Q6A8Z3; DT 13-SEP-2004, integrated into UniProtKB/TrEMBL. DT 13-SEP-2004, sequence version 1. DT 07-JUN-2017, entry version 92. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=PPA1021 {ECO:0000313|EMBL:AAT82773.1}; OS Propionibacterium acnes (strain KPA171202 / DSM 16379). OC Bacteria; Actinobacteria; Propionibacteriales; Propionibacteriaceae; OC Cutibacterium. OX NCBI_TaxID=267747 {ECO:0000313|EMBL:AAT82773.1, ECO:0000313|Proteomes:UP000000603}; RN [1] {ECO:0000313|EMBL:AAT82773.1, ECO:0000313|Proteomes:UP000000603} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=KPA171202 / DSM 16379 {ECO:0000313|Proteomes:UP000000603}; RX PubMed=15286373; DOI=10.1126/science.1100330; RA Bruggemann H., Henne A., Hoster F., Liesegang H., Wiezer A., RA Strittmatter A., Hujer S., Durre P., Gottschalk G.; RT "The complete genome sequence of Propionibacterium acnes, a commensal RT of human skin."; RL Science 305:671-673(2004). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE017283; AAT82773.1; -; Genomic_DNA. DR ProteinModelPortal; Q6A8Z3; -. DR STRING; 267747.PPA1021; -. DR EnsemblBacteria; AAT82773; AAT82773; PPA1021. DR KEGG; pac:PPA1021; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR Proteomes; UP000000603; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000000603}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000000603}. FT DOMAIN 263 428 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 483 AA; 52299 MW; 6325AF19BDD39A5E CRC64; MSEIEQIDNE REDALKNNNG FSEDQSDYDG DQFDLDARLS LTRVPGMSTD LSDISEVEYR QLRLERVVLC SVWTQGTAAD AENAMAELKA LAETAGSQVL EAVMQHRTTP DPATYIGSGK VAELAEVVWA TGADTVICDG ELDAAQLRNL EDRVKVKVVD RTALILDIFA QHARSVEGRT QVELAQLNYL KQRLRGWGGN LSRQTGGRAA GGAGIGGRGP GETRIETDRR RISHRIAVLR RRLTHIESTR ASKRADRIRN KVPSVAIVGY TNAGKSSLLN RLTRAGVLVE NALFATLDPT TRRATTSDGR VYTLTDTVGF VRHLPHDLVE AFASTLEETA MADVLLHVVD ADDPDPLGQV DAVRGVLSGI GASNIPEILV LNKIDRLSDE TILTLRSTFP GAYLVSAHTG EGIDKLVEAI EAGLPIPSQR VDVVIPYARG DLMDKIHHNG TIGLIDHTAD GTHVVAHLHP ALAAEVEEAC DGV // ID Q6AE07_LEIXX Unreviewed; 489 AA. AC Q6AE07; DT 13-SEP-2004, integrated into UniProtKB/TrEMBL. DT 13-SEP-2004, sequence version 1. DT 07-JUN-2017, entry version 79. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:AAT89389.1}; GN OrderedLocusNames=Lxx15960 {ECO:0000313|EMBL:AAT89389.1}; OS Leifsonia xyli subsp. xyli (strain CTCB07). OC Bacteria; Actinobacteria; Micrococcales; Microbacteriaceae; Leifsonia. OX NCBI_TaxID=281090 {ECO:0000313|EMBL:AAT89389.1, ECO:0000313|Proteomes:UP000001306}; RN [1] {ECO:0000313|EMBL:AAT89389.1, ECO:0000313|Proteomes:UP000001306} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CTCB07 {ECO:0000313|EMBL:AAT89389.1, RC ECO:0000313|Proteomes:UP000001306}; RX PubMed=15305603; RA Monteiro-Vitorello C.B., Camargo L.E.A., Van Sluys M.A., RA Kitajima J.P., Truffi D., do Amaral A.M., Harakava R., RA de Oliveira J.C.F., Wood D., de Oliveira M.C., Miyaki C.Y., RA Takita M.A., da Silva A.C.R., Furlan L.R., Carraro D.M., Camarotte G., RA Almeida N.F. Jr., Carrer H., Coutinho L.L., El-Dorry H.A., RA Ferro M.I.T., Gagliardi P.R., Giglioti E., Goldman M.H.S., RA Goldman G.H., Kimura E.T., Ferro E.S., Kuramae E.E., Lemos E.G.M., RA Lemos M.V.F., Mauro S.M.Z., Machado M.A., Marino C.L., Menck C.F., RA Nunes L.R., Oliveira R.C., Pereira G.G., Siqueira W., de Souza A.A., RA Tsai S.M., Zanca A.S., Simpson A.J.G., Brumbley S.M., Setubal J.C.; RT "The genome sequence of the Gram-positive sugarcane pathogen Leifsonia RT xyli subsp. xyli."; RL Mol. Plant Microbe Interact. 17:827-836(2004). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE016822; AAT89389.1; -; Genomic_DNA. DR ProteinModelPortal; Q6AE07; -. DR STRING; 281090.Lxx15960; -. DR EnsemblBacteria; AAT89389; AAT89389; Lxx15960. DR KEGG; lxx:Lxx15960; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000001306; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 2. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000001306}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000001306}. FT DOMAIN 271 436 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 489 AA; 52786 MW; F45264C7A2031B50 CRC64; MVARVLATQQ NRAPVTLFGA GAQALQTTGT DGHLDDGEQL DREERAALRR VSGLSTELED VTEVEYRQLR LENVVLIGVY SQGSQQVAEN SLRELAALAE TAGAAVLDGL LQRRPHPDPG TYFGRGKAEE LAGVVSALGA DTVIADTELA PSQRRALEDV VKVKVIDRTA VILDIFSQHA KSCEGKAQVE LAQLEYLLPR LRGWGESMSR QAGGQVGGAG AAMGSRGPGE TKIELDRRRI HTRMAKLRKQ IAGFKPAREA KRANRNRNAV PSVAIAGYTN AGKSSLLNRV TKAGVLVENA LFATLDATVR RSVTADGRLY TLADTVGFVR NLPHQLVEAF RSTLEEVADS DVIVHVVDGS HPDPASQLAT VRDVIGDVGA RDIPEIVVFN KADLIPEDER LVLRGLEPGA IFASARTGEG VEEVLAAIAR LLPDPSVEVE LIVPYDRGDL VSALHERGRV LSTEYTEEGA RVRARIMPEY RAVFEPFAP // ID Q6AJ33_DESPS Unreviewed; 511 AA. AC Q6AJ33; DT 13-SEP-2004, integrated into UniProtKB/TrEMBL. DT 13-SEP-2004, sequence version 1. DT 07-JUN-2017, entry version 96. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=DP2918 {ECO:0000313|EMBL:CAG37647.1}; OS Desulfotalea psychrophila (strain LSv54 / DSM 12343). OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfobacterales; OC Desulfobulbaceae; Desulfotalea. OX NCBI_TaxID=177439 {ECO:0000313|EMBL:CAG37647.1, ECO:0000313|Proteomes:UP000000602}; RN [1] {ECO:0000313|Proteomes:UP000000602} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=LSv54 / DSM 12343 {ECO:0000313|Proteomes:UP000000602}; RX PubMed=15305914; DOI=10.1111/j.1462-2920.2004.00665.x; RA Rabus R., Ruepp A., Frickey T., Rattei T., Fartmann B., Stark M., RA Bauer M., Zibat A., Lombardot T., Becker I., Amann J., Gellner K., RA Teeling H., Leuschner W.D., Gloeckner F.-O., Lupas A.N., Amann R., RA Klenk H.-P.; RT "The genome of Desulfotalea psychrophila, a sulfate-reducing bacterium RT from permanently cold Arctic sediments."; RL Environ. Microbiol. 6:887-902(2004). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CR522870; CAG37647.1; -; Genomic_DNA. DR RefSeq; WP_011190159.1; NC_006138.1. DR ProteinModelPortal; Q6AJ33; -. DR STRING; 177439.DP2918; -. DR EnsemblBacteria; CAG37647; CAG37647; DP2918. DR KEGG; dps:DP2918; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; EREVIIT; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000000602; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000000602}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000000602}. FT DOMAIN 341 506 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 511 AA; 56736 MW; 430368482C30A027 CRC64; MARSLGQISA EINRQIGLLI HRSGKLEMII VGTHKAIMIP SLAHLRGGGG RLKGVRLVHT HLRGEEISDE DLMDLLFLRL DMLSVLQVAK DGQVQSLHSA HLQPARDGAS SWTFLDPVHP SQQRGSVEDI IAEVEAGFSR VRSLSVADDG DRAILVSVTA EVKMLAEESL TELGELARSA NVKVLDTVLQ RSRKANPRFI LGKGKLADIM ILALQLDANL LVFNQDLNPS QVRSITDFTE MRVIDRTQLI LDIFASRALS REGKLQVEMA QLKYALPRLS SRDDALSRLS GGIGARGPGE TKLELDRRRI NDRLSGLARE LKHVGEERYR RRAQRRRRDV PVLSLVGYTN AGKSTLLNVL TGSHIVAEDK LFATLDPTSR RLRFPTEMEV IITDTVGFIR NLPAELIKAF MATLEELEEA DLLIHVIDVS NPCYRDHIEV VERLLSELDL GHIPCLKVFN KIDLLADPAV GLLEDLSEQG VLVSALQPET LKPFLARAEK MLGRILAEKD L // ID Q6D068_PECAS Unreviewed; 426 AA. AC Q6D068; DT 16-AUG-2004, integrated into UniProtKB/TrEMBL. DT 16-AUG-2004, sequence version 1. DT 30-AUG-2017, entry version 89. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:CAG76830.1}; GN OrderedLocusNames=ECA3933 {ECO:0000313|EMBL:CAG76830.1}; OS Pectobacterium atrosepticum (strain SCRI 1043 / ATCC BAA-672) (Erwinia OS carotovora subsp. atroseptica). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; OC Pectobacteriaceae; Pectobacterium. OX NCBI_TaxID=218491 {ECO:0000313|EMBL:CAG76830.1, ECO:0000313|Proteomes:UP000007966}; RN [1] {ECO:0000313|Proteomes:UP000007966} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SCRI 1043 / ATCC BAA-672 {ECO:0000313|Proteomes:UP000007966}; RX PubMed=15263089; DOI=10.1073/pnas.0402424101; RA Bell K.S., Sebaihia M., Pritchard L., Holden M.T.G., Hyman L.J., RA Holeva M.C., Thomson N.R., Bentley S.D., Churcher L.J.C., Mungall K., RA Atkin R., Bason N., Brooks K., Chillingworth T., Clark K., Doggett J., RA Fraser A., Hance Z., Hauser H., Jagels K., Moule S., Norbertczak H., RA Ormond D., Price C., Quail M.A., Sanders M., Walker D., Whitehead S., RA Salmond G.P.C., Birch P.R.J., Parkhill J., Toth I.K.; RT "Genome sequence of the enterobacterial phytopathogen Erwinia RT carotovora subsp. atroseptica and characterization of virulence RT factors."; RL Proc. Natl. Acad. Sci. U.S.A. 101:11105-11110(2004). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BX950851; CAG76830.1; -; Genomic_DNA. DR RefSeq; WP_011095428.1; NC_004547.2. DR ProteinModelPortal; Q6D068; -. DR STRING; 218491.ECA3933; -. DR PRIDE; Q6D068; -. DR EnsemblBacteria; CAG76830; CAG76830; ECA3933. DR KEGG; eca:ECA3933; -. DR PATRIC; fig|218491.5.peg.3998; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000007966; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000007966}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000007966}. FT DOMAIN 198 365 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 426 AA; 48269 MW; EC42C20787BB5609 CRC64; MFDRYESGER AILVHVFFSQ DRDTDDLLEF ESLVSSAGIE SLQVVTGSRK APHPKYFVGE GKAEEIAQAV KETGAFVVLF NHALTPAQER NLERLCECRV IDRTGLILDI FAQRARTHEG KLQVELAQLR HLATRLVRGW THLERQKGGI GLRGPGETQL ETDRRLLRNR ISQILLRLER VEKQREQGRR SRVRADVPTV SLVGYTNAGK STLFNKITSA GVYVADQLFA TLDPTLRRIQ VDDVGDTVLA DTVGFIRQLP HDLVAAFKAT LQETRQASLL LHVVDAADPR LDENIDAVND VLAEIEADEI PALLVMNKID MLDDFVPRID RNEENLPIRV WLSAQTGDGI PLLFQALTER LSGEIAQYTL HLPPQAGRLR SRFYQLQAIE KEWIEEDGQI GLVIRMPIAD WRRLCKKEQE LMDYIA // ID Q6F8A4_ACIAD Unreviewed; 444 AA. AC Q6F8A4; DT 19-JUL-2004, integrated into UniProtKB/TrEMBL. DT 19-JUL-2004, sequence version 1. DT 07-JUN-2017, entry version 86. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:CAG69711.1}; GN OrderedLocusNames=ACIAD3005 {ECO:0000313|EMBL:CAG69711.1}; OS Acinetobacter baylyi (strain ATCC 33305 / BD413 / ADP1). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Moraxellaceae; Acinetobacter. OX NCBI_TaxID=62977 {ECO:0000313|EMBL:CAG69711.1, ECO:0000313|Proteomes:UP000000430}; RN [1] {ECO:0000313|EMBL:CAG69711.1, ECO:0000313|Proteomes:UP000000430} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33305 / BD413 / ADP1 {ECO:0000313|Proteomes:UP000000430}; RX PubMed=15514110; DOI=10.1093/nar/gkh910; RA Barbe V., Vallenet D., Fonknechten N., Kreimeyer A., Oztas S., RA Labarre L., Cruveiller S., Robert C., Duprat S., Wincker P., RA Ornston L.N., Weissenbach J., Marliere P., Cohen G.N., Medigue C.; RT "Unique features revealed by the genome sequence of Acinetobacter sp. RT ADP1, a versatile and naturally transformation competent bacterium."; RL Nucleic Acids Res. 32:5766-5779(2004). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CR543861; CAG69711.1; -; Genomic_DNA. DR RefSeq; WP_004929642.1; NC_005966.1. DR ProteinModelPortal; Q6F8A4; -. DR STRING; 62977.ACIAD3005; -. DR EnsemblBacteria; CAG69711; CAG69711; ACIAD3005. DR KEGG; aci:ACIAD3005; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000000430; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000000430}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000000430}. FT DOMAIN 200 365 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 444 AA; 49553 MW; 09A8350615CE39F5 CRC64; MESLDQDQGK ERVILVSVSV NILDDLDAEE FALLASSAGA ERLEHIYAQR VKPDAKLFIG SGKAEEIAER VEALDASLVI FDHALSPAQE RNLEKIMKCR VIDRTGLILD IFAQRARTHE GKLQVELAQL KHLSTRLVRG WSGGFEQQKG GIGLRGPGET QLETDRRLIR IRMIQLKDKL DKVQQTRLQG RAARQKAAIP TVSLVGYTNA GKSTLFNHLA NSDVYAADQL FATLDPTLRR LDWDGIGTVV LADTVGFVRN LQHDLIESFK ATLEETLEAT LLLHIIDSSS PDMLEQIEAV EGVLKEIGAD APVLRVYNKI DVSGDEAKII YARPHEPERV YVSAHSGAGI DLLKKAVQEC LMGQRQAFDL ILKPIHGKLR TQLYNLNVID SEHFDDQGQL HLHVVMAPQK LEQLIRQAHL SLDEILGEQA QGFKRPLEEF EIKS // ID Q6LHG0_PHOPR Unreviewed; 445 AA. AC Q6LHG0; DT 05-JUL-2004, integrated into UniProtKB/TrEMBL. DT 05-JUL-2004, sequence version 1. DT 07-JUN-2017, entry version 83. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=CV2840 {ECO:0000313|EMBL:CAG23270.1}; GN Synonyms=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=PBPRB1403 {ECO:0000313|EMBL:CAG23270.1}; OS Photobacterium profundum (strain SS9). OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; OC Vibrionaceae; Photobacterium. OX NCBI_TaxID=298386 {ECO:0000313|EMBL:CAG23270.1, ECO:0000313|Proteomes:UP000000593}; RN [1] {ECO:0000313|Proteomes:UP000000593} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-1253 / SS9 {ECO:0000313|Proteomes:UP000000593}; RX PubMed=15746425; DOI=10.1126/science.1103341; RA Vezzi A., Campanaro S., D'Angelo M., Simonato F., Vitulo N., RA Lauro F.M., Cestaro A., Malacrida G., Simionati B., Cannata N., RA Romualdi C., Bartlett D.H., Valle G.; RT "Life at depth: Photobacterium profundum genome sequence and RT expression analysis."; RL Science 307:1459-1461(2005). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CR378679; CAG23270.1; -; Genomic_DNA. DR RefSeq; WP_011221446.1; NC_006371.1. DR ProteinModelPortal; Q6LHG0; -. DR STRING; 298386.PBPRB1403; -. DR EnsemblBacteria; CAG23270; CAG23270; PBPRB1403. DR KEGG; ppr:PBPRB1403; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000000593; Chromosome 2. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000000593}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000000593}. FT DOMAIN 225 357 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 186 220 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 445 AA; 49357 MW; ECFC591AB12B3216 CRC64; MKLTEKASLT NALLISICTP QFKGDEAKDS LAELARLVTT LGFKVVGTQS QKQSSTQRVN VLGAGKLAEI AHLTGNQGSV DDADTEDFFD ETDFEDIPSE NLPFACADVV VFDCDLSPSQ LRNVENQLGV QVYDRTGIII EIFSRHARTR TARLQVEMAR LNYVAPRLRE STVGDNERQM GKGAGETNLE LDRRKVRDQL AELKRELASV QDEMKGRRTQ RSELFCVALV GYTNAGKSSM MRAITGSEVL VEDKLFATLD TTVRALYPVT QPRILVSDTV GFIKKLPHDL VASFHSTLAE AHDASLLLYV VDASDSSFRT QLDVVHEVLE EVGVEGAKKL LVLNKSDQLS TDQQQALMEE FPDAMMTSTR NPLDIAKLHK YIVGVSEHGM IEDEIIVPYT AKGIIGEIRS SMSVTKEEYE YSHIKLTVRS NAIDLARLKK LMLNS // ID Q6LM31_PHOPR Unreviewed; 429 AA. AC Q6LM31; DT 05-JUL-2004, integrated into UniProtKB/TrEMBL. DT 05-JUL-2004, sequence version 1. DT 30-AUG-2017, entry version 87. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=STM4362 {ECO:0000313|EMBL:CAG21647.1}; GN Synonyms=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=PBPRA3349 {ECO:0000313|EMBL:CAG21647.1}; OS Photobacterium profundum (strain SS9). OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; OC Vibrionaceae; Photobacterium. OX NCBI_TaxID=298386 {ECO:0000313|EMBL:CAG21647.1, ECO:0000313|Proteomes:UP000000593}; RN [1] {ECO:0000313|Proteomes:UP000000593} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-1253 / SS9 {ECO:0000313|Proteomes:UP000000593}; RX PubMed=15746425; DOI=10.1126/science.1103341; RA Vezzi A., Campanaro S., D'Angelo M., Simonato F., Vitulo N., RA Lauro F.M., Cestaro A., Malacrida G., Simionati B., Cannata N., RA Romualdi C., Bartlett D.H., Valle G.; RT "Life at depth: Photobacterium profundum genome sequence and RT expression analysis."; RL Science 307:1459-1461(2005). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CR378673; CAG21647.1; -; Genomic_DNA. DR RefSeq; WP_011219893.1; NC_006370.1. DR ProteinModelPortal; Q6LM31; -. DR STRING; 298386.PBPRA3349; -. DR PRIDE; Q6LM31; -. DR EnsemblBacteria; CAG21647; CAG21647; PBPRA3349. DR KEGG; ppr:PBPRA3349; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000000593; Chromosome 1. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000000593}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000000593}. FT DOMAIN 198 365 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 429 AA; 48506 MW; D8A0CA23BE4C6D16 CRC64; MFDRYETGEQ AILVHINFTQ DGEWEDLSEC EMLVSSAGVN TLRVVTGSRK TPLPKYYVGE GKAQEIADAV RAEEAEIVIF NHSLSPAQER NLEQLCQCRV IDRTGLILDI FAQRARTHEG KLQVELAQLR HISTRLIRGW THLERQKGGI GLRGPGETQL ETDRRLLRDR IKTILRRLDK VSKQREQGRR ARNRAEIPTI SLVGYTNAGK STLFNRITDA GVYVADQLFA TLDPTLRKID VADVGTAILA DTVGFIRHLP HDLVAAFKAT LKETQEATLL LHVVDASDER FRENMDAVHL VLDEIDAGDV PRLIVMNKID CLDGAEPRIE RDEDGLPRCV WVSAMEGIGI DLLFQALTER LSGTMIKHTL RLPPENAGRY RSTFYQLGCI LREEYESDGC LMVDIRLPLA DWSRLQKRES NLLDDFIVA // ID Q6MAA9_PARUW Unreviewed; 444 AA. AC Q6MAA9; DT 05-JUL-2004, integrated into UniProtKB/TrEMBL. DT 05-JUL-2004, sequence version 1. DT 07-JUN-2017, entry version 99. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=pc1766 {ECO:0000313|EMBL:CAF24490.1}; OS Protochlamydia amoebophila (strain UWE25). OC Bacteria; Chlamydiae; Parachlamydiales; Parachlamydiaceae; OC Candidatus Protochlamydia. OX NCBI_TaxID=264201 {ECO:0000313|EMBL:CAF24490.1, ECO:0000313|Proteomes:UP000000529}; RN [1] {ECO:0000313|EMBL:CAF24490.1, ECO:0000313|Proteomes:UP000000529} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=UWE25 {ECO:0000313|EMBL:CAF24490.1, RC ECO:0000313|Proteomes:UP000000529}; RX PubMed=15073324; DOI=10.1126/science.1096330; RA Horn M., Collingro A., Schmitz-Esser S., Beier C.L., Purkhold U., RA Fartmann B., Brandt P., Nyakatura G.J., Droege M., Frishman D., RA Rattei T., Mewes H.-W., Wagner M.; RT "Illuminating the evolutionary history of chlamydiae."; RL Science 304:728-730(2004). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BX908798; CAF24490.1; -; Genomic_DNA. DR RefSeq; WP_011176311.1; NC_005861.1. DR ProteinModelPortal; Q6MAA9; -. DR STRING; 264201.pc1766; -. DR EnsemblBacteria; CAF24490; CAF24490; pc1766. DR KEGG; pcu:pc1766; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000000529; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000000529}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000000529}. FT DOMAIN 221 387 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 180 207 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 444 AA; 50344 MW; 038AA81BCAF94876 CRC64; MKNDKTVKDE SDFILHEEEK NQKALLISVY QGNKQLRLCE EHLEELALLA YTFGIEVAKK EPCSLRKFDA STYVSKGKLE ELIQIANELA VDLIIFDDEI TPAQQRNLQA AFNKPVIDRT ELILGVFAQR AHTKEARLQI ELAKIKYEAP RLKRLWTHLS RQQGTSGSGG GGAYLKGEGE KQIEIDKRIL KRKMDVLQKE IDDVKAVRET QRLSRVRSAI PVFAIIGYTN AGKSTLLNAL TDAGVFVEDK LFATLDTTTR KFTLPNNQDI LIVDTVGFIR KLPHLLVAAF KSTLEEAIEA DILLHLIDVS HPMAEEQAAT TYEVLQELGA GKKPIITVLN KIDQCEHPHM IHRIRMSYPK NVQISALKKI GFEELQEAMI QELSRQRQVA EFRIPQSDYG SVSEIIRLGH ILSQDYEDND VLLKVDLPAL IVDKYAHYQI LAER // ID Q6MIB6_BDEBA Unreviewed; 487 AA. AC Q6MIB6; DT 05-JUL-2004, integrated into UniProtKB/TrEMBL. DT 05-JUL-2004, sequence version 1. DT 07-JUN-2017, entry version 81. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:CAE78064.1}; GN OrderedLocusNames=Bd3249 {ECO:0000313|EMBL:CAE78064.1}; OS Bdellovibrio bacteriovorus (strain ATCC 15356 / DSM 50701 / NCIB 9529 OS / HD100). OC Bacteria; Proteobacteria; Deltaproteobacteria; Bdellovibrionales; OC Bdellovibrionaceae; Bdellovibrio. OX NCBI_TaxID=264462 {ECO:0000313|EMBL:CAE78064.1, ECO:0000313|Proteomes:UP000008080}; RN [1] {ECO:0000313|EMBL:CAE78064.1, ECO:0000313|Proteomes:UP000008080} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 15356 / DSM 50701 / NCIB 9529 / HD100 RC {ECO:0000313|Proteomes:UP000008080}; RX PubMed=14752164; DOI=10.1126/science.1093027; RA Rendulic S., Jagtap P., Rosinus A., Eppinger M., Baar C., Lanz C., RA Keller H., Lambert C., Evans K.J., Goesmann A., Meyer F., RA Sockett R.E., Schuster S.C.; RT "A predator unmasked: life cycle of Bdellovibrio bacteriovorus from a RT genomic perspective."; RL Science 303:689-692(2004). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BX842655; CAE78064.1; -; Genomic_DNA. DR RefSeq; WP_011165602.1; NC_005363.1. DR ProteinModelPortal; Q6MIB6; -. DR STRING; 264462.Bd3249; -. DR EnsemblBacteria; CAE78064; CAE78064; Bd3249. DR KEGG; bba:Bd3249; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; VILEIFH; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000008080; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 2. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000008080}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000008080}. FT DOMAIN 250 415 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 211 245 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 487 AA; 54085 MW; A45C1D931B828719 CRC64; MNETTPLKAV LVGIQLQRTS DQELKGSLTE LSRLVTTLGY EVVGQMSQRR SSTKTATVLG DGKLKELAEW TGGTGKISPN FTKKKHKAAL RFKKDEEEDD LFGDDVEEVF EVEEGAEDMD SSGDTTPQEK AQVVVIDCDL SPSQLRNLES ATGAQVLDRT GVIIEIFSRH ARTRAARLQV EIARLTYVAP RMRESTAGDD RQGGGGKGAG ETSIELDRRK IRDRIKELKQ ELASISQELD TRRARREQEL TVALVGYTNA GKSSLMRALT GSDVLIADKL FATLDTTVRI LYPETKPKIL VSDTVGFIKK LPHDLVASFK STLDEAANAS LLLYTVDCSD PTFRSQLEVT RTVLAEVGAQ DIPSKLIFNK RDRLSPEEEA ELAKEFPEAH FMSAKNADDV ATLHSMLVKH FENEMVEEDV LIPYTTQGAI GEIRGKMRVL NESYEANGVV LKIRAHREDL QSMKERYGLI PGKGKKKNNL SWNIDED // ID Q6MM17_BDEBA Unreviewed; 421 AA. AC Q6MM17; DT 05-JUL-2004, integrated into UniProtKB/TrEMBL. DT 05-JUL-2004, sequence version 1. DT 07-JUN-2017, entry version 82. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:CAE79689.1}; GN OrderedLocusNames=Bd1831 {ECO:0000313|EMBL:CAE79689.1}; OS Bdellovibrio bacteriovorus (strain ATCC 15356 / DSM 50701 / NCIB 9529 OS / HD100). OC Bacteria; Proteobacteria; Deltaproteobacteria; Bdellovibrionales; OC Bdellovibrionaceae; Bdellovibrio. OX NCBI_TaxID=264462 {ECO:0000313|EMBL:CAE79689.1, ECO:0000313|Proteomes:UP000008080}; RN [1] {ECO:0000313|EMBL:CAE79689.1, ECO:0000313|Proteomes:UP000008080} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 15356 / DSM 50701 / NCIB 9529 / HD100 RC {ECO:0000313|Proteomes:UP000008080}; RX PubMed=14752164; DOI=10.1126/science.1093027; RA Rendulic S., Jagtap P., Rosinus A., Eppinger M., Baar C., Lanz C., RA Keller H., Lambert C., Evans K.J., Goesmann A., Meyer F., RA Sockett R.E., Schuster S.C.; RT "A predator unmasked: life cycle of Bdellovibrio bacteriovorus from a RT genomic perspective."; RL Science 303:689-692(2004). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BX842651; CAE79689.1; -; Genomic_DNA. DR RefSeq; WP_011164291.1; NC_005363.1. DR ProteinModelPortal; Q6MM17; -. DR STRING; 264462.Bd1831; -. DR EnsemblBacteria; CAE79689; CAE79689; Bd1831. DR KEGG; bba:Bd1831; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000008080; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000008080}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000008080}. FT DOMAIN 204 367 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 421 AA; 47458 MW; E6127440BD5A47DA CRC64; MNNQAQVKDQ DRAIVIGVGL KTEPLTEIKE NLLELEELVS AAGGEVVGSI IQVLPQWNPA TLIGTGKVEE VAEMVRDSGA TIVVMDHQLS GVQQRNLQQI VKARVIDRNQ LILDIFAQRA QTFEGKLQVE LAQLLDQMPR NVGAWLDSLS RQGGGIGTRG PGETALENDR RRIRERVALI KKKLESVRQN RAQHRQSRRR HEIPSFALVG YTNSGKSSIL NRLTGAQVMT KNQVFATLDP TTRKIFLPDA PPAVVTDTVG FIRKLPTQLI EAFKATLEES SEADVLLHVV DLSSPNMERQ IEVVEALIKE FNWQDKKIIH VFNKCDVAPL ERQFRVKAYP RVFVSALTGQ GMEQLKKLMA QTVSEMQQDV QLYFPRAEEY KIFDLGREAQ ILRKETATEG TVCYTQLTPT LINRWKDYLV K // ID Q6N6L7_RHOPA Unreviewed; 424 AA. AC Q6N6L7; DT 05-JUL-2004, integrated into UniProtKB/TrEMBL. DT 05-JUL-2004, sequence version 1. DT 07-JUN-2017, entry version 87. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=RPA2598 {ECO:0000313|EMBL:CAE28039.1}; OS Rhodopseudomonas palustris (strain ATCC BAA-98 / CGA009). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Bradyrhizobiaceae; Rhodopseudomonas. OX NCBI_TaxID=258594 {ECO:0000313|EMBL:CAE28039.1, ECO:0000313|Proteomes:UP000001426}; RN [1] {ECO:0000313|EMBL:CAE28039.1, ECO:0000313|Proteomes:UP000001426} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-98 / CGA009 {ECO:0000313|Proteomes:UP000001426}; RX PubMed=14704707; DOI=10.1038/nbt923; RA Larimer F.W., Chain P., Hauser L., Lamerdin J., Malfatti S., Do L., RA Land M.L., Pelletier D.A., Beatty T.J., Lang A.S., Tabita F.R., RA Gibson J.L., Hanson T.E., Torres y Torres J., Peres C., Harrison F.H., RA Gibson J., Harwood C.S.; RT "Complete genome sequence of the metabolically versatile RT photosynthetic bacterium Rhodopseudomonas palustris."; RL Nat. Biotechnol. 22:55-61(2004). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BX572601; CAE28039.1; -; Genomic_DNA. DR ProteinModelPortal; Q6N6L7; -. DR STRING; 258594.RPA2598; -. DR EnsemblBacteria; CAE28039; CAE28039; RPA2598. DR KEGG; rpa:RPA2598; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR PhylomeDB; Q6N6L7; -. DR Proteomes; UP000001426; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000001426}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000001426}. FT DOMAIN 192 365 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 424 AA; 46997 MW; 628F5677AB826A3B CRC64; MRRGDPDAVD TAVRDNDARL DEAAGLARAI DLDVVEAVLT PISQIRPATY LGKGKVEEIV GLIAAHGADL IVMDCALSPI QQRNLEKAWN AKVLDRTGLI LEIFGRRAKT REGTLQVELA HLNYQRSRLV RSWTHLERQR GGFGFMGGPG ETQIEADRRL IGERITKLEA ELKKVQATRR LHRAGRQRVP YRVVALVGYT NAGKSTLFNR LTRADVQAAD MLFATLDPTL RAIQLPHGGK AMLSDTVGFI SNLPTQLVAA FRATLEEVLE ADLILHVRDI SHEDAEAQQH DVDNVLRQLG VDAASGRIVE VWNKIDRFEP EQRDELKNIA ARRPEDHPCL LVSAVSGEGV DELLLSIEQR LAATRTVLDL SIDAADGAGV SWLHRNTEVL AKDLVDGRYA MTVRVEDNKR DIVIDRFGAV PRPD // ID Q6NGR9_CORDI Unreviewed; 536 AA. AC Q6NGR9; DT 05-JUL-2004, integrated into UniProtKB/TrEMBL. DT 05-JUL-2004, sequence version 1. DT 30-AUG-2017, entry version 87. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=DIP1439 {ECO:0000313|EMBL:CAE49967.1}; OS Corynebacterium diphtheriae (strain ATCC 700971 / NCTC 13129 / Biotype OS gravis). OC Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae; OC Corynebacterium. OX NCBI_TaxID=257309 {ECO:0000313|Proteomes:UP000002198}; RN [1] {ECO:0000313|EMBL:CAE49967.1, ECO:0000313|Proteomes:UP000002198} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700971 / NCTC 13129 / Biotype gravis RC {ECO:0000313|Proteomes:UP000002198}; RX PubMed=14602910; DOI=10.1093/nar/gkg874; RA Cerdeno-Tarraga A.M., Efstratiou A., Dover L.G., Holden M.T.G., RA Pallen M., Bentley S.D., Besra G.S., Churcher C., James K.D., RA De Zoysa A., Chillingworth T., Cronin A., Dowd L., Feltwell T., RA Hamlin N., Holroyd S., Jagels K., Moule S., Quail M.A., RA Rabbinowitsch E., Rutherford K., Thomson N.R., Unwin L., Whitehead S., RA Barrell B.G.Parkhill.J.; RT "The complete genome sequence and analysis of Corynebacterium RT diphtheriae NCTC13129."; RL Nucleic Acids Res. 31:6516-6523(2003). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BX248358; CAE49967.1; -; Genomic_DNA. DR RefSeq; WP_003851848.1; NC_002935.2. DR ProteinModelPortal; Q6NGR9; -. DR EnsemblBacteria; CAE49967; CAE49967; DIP1439. DR KEGG; cdi:DIP1439; -. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR Proteomes; UP000002198; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000002198}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000002198}. FT DOMAIN 313 489 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 272 299 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 536 AA; 58249 MW; 9FB8BBDF87E150B3 CRC64; MTNNTFKNSE LGAQSHILAG QGEKNYSSHD ELLARAFRDH KPVSRSADDG EDFTGLIATK SVSEGHTNVS DHTPTVGELD LEARSSLRSL TRGSEIHATD QDDGYDVEYR KLRLERVILV GVWTKGTTAE IEANMNELAS LAETAGADVV EVLYQKRDKP DPGTYIGSGK VSELKEIVSS TGVDTVICDG ELSPSQMIAL EKALDVKVID RTMLILDIFA QHAKSKEGKA QVSLAQMEYL ITRVRGWGGA LSRQAGGRAG SNGGVGLRGP GETKIEADRR RLRSDMAKLR KEIAGMKTAR EVKRSQRKQS TIPQIAIAGY TNAGKSSLIN AMTGAGVLVE DALFATLDPT TRRAELADGR AVVFTDTVGF VRHLPTQLVE SFRSTLEEVV DADLVLHVVD GSDPFPLKQI EAVNTVVSEI VRELKVDAPP EIIVVNKIDQ ADPLVLAELR HALDDVVFVS AKTAEGIPEL EMRVEQFLNT LDTHVRLLVP YTRGDIVSRL HSNGTVLSEE YEAEGTLIDV RLPAAIAAEL GELRVD // ID Q725J4_DESVH Unreviewed; 547 AA. AC Q725J4; DT 05-JUL-2004, integrated into UniProtKB/TrEMBL. DT 05-JUL-2004, sequence version 1. DT 07-JUN-2017, entry version 105. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:AAS97706.1}; GN OrderedLocusNames=DVU_3236 {ECO:0000313|EMBL:AAS97706.1}; OS Desulfovibrio vulgaris (strain Hildenborough / ATCC 29579 / DSM 644 / OS NCIMB 8303). OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfovibrionales; OC Desulfovibrionaceae; Desulfovibrio. OX NCBI_TaxID=882 {ECO:0000313|EMBL:AAS97706.1, ECO:0000313|Proteomes:UP000002194}; RN [1] {ECO:0000313|EMBL:AAS97706.1, ECO:0000313|Proteomes:UP000002194} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Hildenborough / ATCC 29579 / DSM 644 / NCIMB 8303 RC {ECO:0000313|Proteomes:UP000002194}; RX PubMed=15077118; DOI=10.1038/nbt959; RA Heidelberg J.F., Seshadri R., Haveman S.A., Hemme C.L., Paulsen I.T., RA Kolonay J.F., Eisen J.A., Ward N., Methe B., Brinkac L.M., RA Daugherty S.C., Deboy R.T., Dodson R.J., Durkin A.S., Madupu R., RA Nelson W.C., Sullivan S.A., Fouts D., Haft D.H., Selengut J., RA Peterson J.D., Davidsen T.M., Zafar N., Zhou L., Radune D., RA Dimitrov G., Hance M., Tran K., Khouri H., Gill J., Utterback T.R., RA Feldblyum T.V., Wall J.D., Voordouw G., Fraser C.M.; RT "The genome sequence of the anaerobic, sulfate-reducing bacterium RT Desulfovibrio vulgaris Hildenborough."; RL Nat. Biotechnol. 22:554-559(2004). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE017285; AAS97706.1; -; Genomic_DNA. DR RefSeq; WP_010940494.1; NC_002937.3. DR RefSeq; YP_012446.1; NC_002937.3. DR ProteinModelPortal; Q725J4; -. DR STRING; 882.DVU3236; -. DR PaxDb; Q725J4; -. DR EnsemblBacteria; AAS97706; AAS97706; DVU_3236. DR GeneID; 2793886; -. DR KEGG; dvu:DVU3236; -. DR PATRIC; fig|882.5.peg.2943; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR KO; K03665; -. DR OMA; EREVIIT; -. DR OrthoDB; POG091H0464; -. DR PhylomeDB; Q725J4; -. DR Proteomes; UP000002194; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000002194}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000002194}. FT DOMAIN 331 497 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 297 324 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 547 AA; 60708 MW; 0096F0EF028E7691 CRC64; MGRQLGLLID RQGRVEMIIV GDTGAIFIPE LPRARSGAGR LRGLRLVHTH LTPELISQED LMDLLFLRLD GLAVLTVDAH GGPQQLQRAH LLPPNPEKRH YTVHPATPWD RVETDFVAEV EALEEEMTRA MPEVREASDG PAAVLVSVAA LPRPVQELNL EELRELARTA GVDVVGTMIQ RVPSVNPKFI LGKGKLTELE VLALQGNASM IVFDGELSPA QLRNIAEVTE RKVLDRTQLI LDIFAQHATT RAGKLQVEMA QLKYTQPRLV GKNRAMDRLA GGIGGRGPGE TKLETDRRRI RDRITRIKGE LDTLRKQRAF ARARRAKQRV PLASLVGYTN AGKSTLLNAL TNAEVLAENK LFATLDPTTR RLRFPEEREL ILADTVGFIR NLPKELVEAF RATLEELEAA DLLIHVADAG HPELDRQLRA VEDILVEMEM HDIPRLLVLN KWDTVPEELR ETLLLAHPEA IPVAALQREG LDALAHGIAS RIDWERTMRP ADGTDGEWCD EGTDASPSGT VDPDAWGSDT DDGLPYEWPC SCEDPVQ // ID Q73W22_MYCPA Unreviewed; 482 AA. AC Q73W22; DT 05-JUL-2004, integrated into UniProtKB/TrEMBL. DT 05-JUL-2004, sequence version 1. DT 07-JUN-2017, entry version 81. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:AAS05156.1}; GN OrderedLocusNames=MAP_2839c {ECO:0000313|EMBL:AAS05156.1}; OS Mycobacterium paratuberculosis (strain ATCC BAA-968 / K-10). OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae; OC Mycobacterium; Mycobacterium avium complex (MAC). OX NCBI_TaxID=262316 {ECO:0000313|EMBL:AAS05156.1, ECO:0000313|Proteomes:UP000000580}; RN [1] {ECO:0000313|EMBL:AAS05156.1, ECO:0000313|Proteomes:UP000000580} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-968 / K-10 {ECO:0000313|Proteomes:UP000000580}; RX PubMed=16116077; DOI=10.1073/pnas.0505662102; RA Li L., Bannantine J.P., Zhang Q., Amonsin A., May B.J., Alt D., RA Banerji N., Kanjilal S., Kapur V.; RT "The complete genome sequence of Mycobacterium avium subspecies RT paratuberculosis."; RL Proc. Natl. Acad. Sci. U.S.A. 102:12344-12349(2005). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE016958; AAS05156.1; -; Genomic_DNA. DR ProteinModelPortal; Q73W22; -. DR STRING; 262316.MAP2839c; -. DR EnsemblBacteria; AAS05156; AAS05156; MAP_2839c. DR KEGG; mpa:MAP_2839c; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000000580; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000000580}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000000580}. FT DOMAIN 259 428 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 218 252 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 482 AA; 51948 MW; CEAF7E5C911ECDF8 CRC64; MHHLLLPMTH PEFRDDAPAI TEPSTGELAL EDRSALRRVA GLSTELTDIS EVEYRQLRLE RVVLVGVWTD GTAADSRASM AELAALAETA GSQVLEGLIQ RRDKPDPSTY IGSGKAAELR DVVLATGADT VICDGELSPA QLTALEKAVK VKVIDRTALI LDIFAQHATS REGKAQVSLA QMEYMLPRLR GWGESMSRQA GGRAGGSGGG VGLRGPGETK IETDRRRIRE RMAKLRREIK DMKQVRDTQR SRRLHSDVPS IAIVGYTNAG KSSLLNALTG AGVLVQDALF ATLEPTTRRA EWDDGRAFVL TDTVGFVRHL PTQLVEAFRS TLEEVVDADL LVHVVDGSDV NPLAQIDAVH QVISEVIADH HGDPPPELLA VNKTDAAGDV ALAKLRHALP GAVFVSAATG DGIDGLRRRI AELAVPAEAA VDVVIPYHRG DLVARLHADG RVQQEEHNAE GTRIKARVPL ALAGRLREFA AP // ID Q74EF3_GEOSL Unreviewed; 555 AA. AC Q74EF3; DT 05-JUL-2004, integrated into UniProtKB/TrEMBL. DT 05-JUL-2004, sequence version 1. DT 07-JUN-2017, entry version 98. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=GSU1009 {ECO:0000313|EMBL:AAR34336.1}; OS Geobacter sulfurreducens (strain ATCC 51573 / DSM 12127 / PCA). OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfuromonadales; OC Geobacteraceae; Geobacter. OX NCBI_TaxID=243231 {ECO:0000313|EMBL:AAR34336.1, ECO:0000313|Proteomes:UP000000577}; RN [1] {ECO:0000313|EMBL:AAR34336.1, ECO:0000313|Proteomes:UP000000577} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51573 / DSM 12127 / PCA RC {ECO:0000313|Proteomes:UP000000577}; RX PubMed=14671304; DOI=10.1126/science.1088727; RA Methe B.A., Nelson K.E., Eisen J.A., Paulsen I.T., Nelson W., RA Heidelberg J.F., Wu D., Wu M., Ward N., Beanan M.J., Dodson R.J., RA Madupu R., Brinkac L.M., Daugherty S.C., DeBoy R.T., Durkin A.S., RA Gwinn M., Kolonay J.F., Sullivan S.A., Haft D.H., Selengut J., RA Davidsen T.M., Zafar N., White O., Tran B., Romero C., Forberger H.A., RA Weidman J., Khouri H., Feldblyum T.V., Utterback T.R., Van Aken S.E., RA Lovley D.R., Fraser C.M.; RT "Genome of Geobacter sulfurreducens: metal reduction in subsurface RT environments."; RL Science 302:1967-1969(2003). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE017180; AAR34336.1; -; Genomic_DNA. DR RefSeq; NP_952063.1; NC_002939.5. DR RefSeq; WP_010941674.1; NC_002939.5. DR ProteinModelPortal; Q74EF3; -. DR STRING; 243231.GSU1009; -. DR EnsemblBacteria; AAR34336; AAR34336; GSU1009. DR GeneID; 2687473; -. DR KEGG; gsu:GSU1009; -. DR PATRIC; fig|243231.5.peg.1011; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR InParanoid; Q74EF3; -. DR KO; K03665; -. DR OMA; EREVIIT; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000000577; Chromosome. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0043022; F:ribosome binding; IBA:GO_Central. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000000577}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000000577}. FT DOMAIN 372 545 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 331 365 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 555 AA; 62559 MW; EA90C4165331CAF4 CRC64; MGLKPSQVAA LERLYRRKVP PDELITPELA ARMVDITRDI RRRVGILVNR HGSVEYVIIG DERGLFIPDL SEYPLGRRLL RGLRYIHTNL RGGSFTEDDL TDLALLRFDL MAVIQVHEDD RRLAIQTASL NPSDDSAHPY RVESAEPLAA HRMDFGAFIS NLERSLEKAV ATDSREVAAG TERAILISVT KHPREEAEDS MDELRELART AGVAVLDIAI QRPRQFNPRY LMGEGKMREV VIRALQLGAT LLIFDQELSP AQVRSISALT ELKVIDRSQL ILDIFARRAT SLDGKVQVEL AQLKYILPRL TGRGVQMSRL MGGIGGRGPG ETKLEIDRRR IRDRIAKLER ELEELSRGRQ QRRQKRVRAG LPIVSIVGYT NAGKSTLLNA LTKSDVFTEN LLFATLDTST RRLRFPRERE VIITDTVGFI RSLPASLLGA FKATLEELQD ADLLLHLVDC ANPRIEEQIE QVGKILEELK LGDKPRLVVF NKGDLVPELK RKAPLAFMKI RQLARRHGAI TISATDRSSL EPLLLEMERR FWPDEAGQDV PSDLS // ID Q74HR8_LACJO Unreviewed; 426 AA. AC Q74HR8; DT 05-JUL-2004, integrated into UniProtKB/TrEMBL. DT 05-JUL-2004, sequence version 1. DT 07-JUN-2017, entry version 87. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=LJ_0599 {ECO:0000313|EMBL:AAS09622.1}; OS Lactobacillus johnsonii (strain CNCM I-12250 / La1 / NCC 533). OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; OC Lactobacillus. OX NCBI_TaxID=257314 {ECO:0000313|EMBL:AAS09622.1, ECO:0000313|Proteomes:UP000000581}; RN [1] {ECO:0000313|EMBL:AAS09622.1, ECO:0000313|Proteomes:UP000000581} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CNCM I-1225 / La1 / NCC 533 RC {ECO:0000313|Proteomes:UP000000581}; RX PubMed=14983040; DOI=10.1073/pnas.0307327101; RA Pridmore R.D., Berger B., Desiere F., Vilanova D., Barretto C., RA Pittet A.-C., Zwahlen M.-C., Rouvet M., Altermann E., Barrangou R., RA Mollet B., Mercenier A., Klaenhammer T., Arigoni F., Schell M.A.; RT "The genome sequence of the probiotic intestinal bacterium RT Lactobacillus johnsonii NCC 533."; RL Proc. Natl. Acad. Sci. U.S.A. 101:2512-2517(2004). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE017198; AAS09622.1; -; Genomic_DNA. DR RefSeq; WP_011162496.1; NC_005362.1. DR ProteinModelPortal; Q74HR8; -. DR STRING; 257314.LJ0599; -. DR EnsemblBacteria; AAS09622; AAS09622; LJ_0599. DR KEGG; ljo:LJ_0599; -. DR PATRIC; fig|257314.6.peg.1678; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR KO; K03665; -. DR OMA; HPATYIG; -. DR Proteomes; UP000000581; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000000581}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000000581}. FT DOMAIN 204 373 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 426 AA; 47942 MW; E677716866FDB563 CRC64; MIDNQPKKIK AFIAGVNLND PNFDYYMTEL RELALANNLD VVGQASQKAE NIVAGTYFGV GKLNQIKNMA RELHAKTLVI NDELSPTQIR NIESMTKLNV LDRTELILEI FSNRACSRQA KLQVQLARLQ YELPRLHPSE NNLDQQRGSG GASGGFANRG SGETKLELNR RTIGKQISAI KKELKDISKQ EEIKSARRNN SRLPQVALVG YTNAGKSTTM NELLNVFSEE ASKKQVFEKN MLFATLDTSV RRIDLKDDLS FILSDTVGFI SKLPHNLIES FKATLQEAKD ADLIINVVDA SDHNMVQMIK TTQKVLDELK ITNVPMITAY NKADLTDRNY PQIEGNDILY SAKDPESIKQ LADLIVKKVF DNYEKVNLVL PLSDGKNLAY LHEYGQILNE DFKDDGVHVT VRLSPKDLEK FKIKTV // ID Q7CKM1_YERPE Unreviewed; 428 AA. AC Q7CKM1; Q74XB5; DT 05-JUL-2004, integrated into UniProtKB/TrEMBL. DT 05-JUL-2004, sequence version 1. DT 30-AUG-2017, entry version 98. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:CAL19056.1}; GN OrderedLocusNames=YPO0374 {ECO:0000313|EMBL:CAL19056.1}; OS Yersinia pestis. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; OC Yersiniaceae; Yersinia. OX NCBI_TaxID=632 {ECO:0000313|Proteomes:UP000000815}; RN [1] {ECO:0000313|EMBL:CAL19056.1, ECO:0000313|Proteomes:UP000000815} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CO-92 / Biovar Orientalis {ECO:0000313|Proteomes:UP000000815}; RX PubMed=11586360; DOI=10.1038/35097083; RA Parkhill J., Wren B.W., Thomson N.R., Titball R.W., Holden M.T.G., RA Prentice M.B., Sebaihia M., James K.D., Churcher C., Mungall K.L., RA Baker S., Basham D., Bentley S.D., Brooks K., Cerdeno-Tarraga A.M., RA Chillingworth T., Cronin A., Davies R.M., Davis P., Dougan G., RA Feltwell T., Hamlin N., Holroyd S., Jagels K., Leather S., RA Karlyshev A.V., Moule S., Oyston P.C.F., Quail M., Rutherford K., RA Simmonds M., Skelton J., Stevens K., Whitehead S., Barrell B.G.; RT "Genome sequence of Yersinia pestis, the causative agent of plague."; RL Nature 413:523-527(2001). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AL590842; CAL19056.1; -; Genomic_DNA. DR PIR; AF0046; AF0046. DR RefSeq; WP_002209152.1; NZ_LQBA01000080.1. DR RefSeq; YP_002345452.1; NC_003143.1. DR STRING; 187410.y0632; -. DR DNASU; 1145578; -. DR EnsemblBacteria; AAM84219; AAM84219; y0632. DR EnsemblBacteria; AAS60800; AAS60800; YP_0530. DR GeneID; 1173220; -. DR KEGG; ype:YPO0374; -. DR KEGG; ypj:CH55_3389; -. DR KEGG; ypk:y0632; -. DR KEGG; ypl:CH46_540; -. DR KEGG; ypm:YP_0530; -. DR KEGG; ypv:BZ15_3197; -. DR KEGG; ypw:CH59_1487; -. DR PATRIC; fig|214092.21.peg.611; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR Proteomes; UP000000815; Chromosome. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0043022; F:ribosome binding; IBA:GO_Central. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000000815}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000000815}. SQ SEQUENCE 428 AA; 48031 MW; A7B0F5BEA28FA2D2 CRC64; MFDRYEAGEQ AVLVHIYFSQ NKDTEDLREF EALVSSAGVE ALQIVTGSRK APHPKYFVGE GKAEEIADAV KASGASVVLF DHALSAAQER NLERLCQCRV IDRTGLILDI FAQRARTHEG KLQVELAQLR HIATRLVRGW THLERQKGGI GLRGPGETQL ETDRRLLRDR ISLILSRLER VAKQREQGRR ARTRADIPTV SLVGYTNAGK SSLFNKITAA DVYAADQLFA TLDPTLRRIN VADVGDTVLA DTVGFIRHLP HDLVAAFKAT LQETRQASLL LHIIDAADPR VAENMAAVDT VLAEIEADEI PTLLVMNKID LLDDFVPRID RNEDNLPVRV WLSAQTGAGI PLLFQALTER LSGEIAHFEL RLPPQAGRLR SRFYQLQAIE KEWIDEDGNV GMVVRMPIVD WRRLCKQEQE LVSYIQNN // ID Q7MH03_VIBVY Unreviewed; 429 AA. AC Q7MH03; DT 15-DEC-2003, integrated into UniProtKB/TrEMBL. DT 15-DEC-2003, sequence version 1. DT 30-AUG-2017, entry version 97. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=VV3070 {ECO:0000313|EMBL:BAC95834.1}; OS Vibrio vulnificus (strain YJ016). OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; OC Vibrionaceae; Vibrio. OX NCBI_TaxID=196600 {ECO:0000313|EMBL:BAC95834.1, ECO:0000313|Proteomes:UP000002675}; RN [1] {ECO:0000313|EMBL:BAC95834.1, ECO:0000313|Proteomes:UP000002675} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=YJ016 {ECO:0000313|EMBL:BAC95834.1, RC ECO:0000313|Proteomes:UP000002675}; RX PubMed=14656965; DOI=10.1101/gr.1295503; RA Chen C.Y., Wu K.M., Chang Y.C., Chang C.H., Tsai H.C., Liao T.L., RA Liu Y.M., Chen H.J., Shen A.B., Li J.C., Su T.L., Shao C.P., Lee C.T., RA Hor L.I., Tsai S.F.; RT "Comparative genome analysis of Vibrio vulnificus, a marine RT pathogen."; RL Genome Res. 13:2577-2587(2003). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BA000037; BAC95834.1; -; Genomic_DNA. DR RefSeq; WP_011079277.1; NC_005139.1. DR ProteinModelPortal; Q7MH03; -. DR EnsemblBacteria; BAC95834; BAC95834; BAC95834. DR GeneID; 2625919; -. DR KEGG; vvy:VV3070; -. DR PATRIC; fig|196600.6.peg.3047; -. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000002675; Chromosome I. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000002675}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000002675}. FT DOMAIN 198 365 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 429 AA; 48783 MW; 46AFB80DBB0C87FA CRC64; MFDRYESGER AVLVHVNFTQ QGEWEDLAEC EMLVSSSGVE TLQVITASRQ SPHAKYYVGE GKAQEIAQAV QLTGAEIVIF NHALSPAQER NLERLCQCRV IDRTGLILDI FAQRARTHEG KLQVELAQLR HISTRLIRGW THLERQKGGI GLRGPGETQL ETDRRLLRER IKAILRRLEK VAKQREQGRR ARNRAEIPTI SLVGYTNAGK STLFNRITEA GVYAADQLFA TLDPTLRKIE LADVGPAILA DTVGFIRHLP HDLVAAFKAT LQETQEADIL LHVVDASDER FRENIQAVHV VLEEINAHEI PTLVVMNKID NMEDQRPRIE RDDEGVPQVV WLSAMDGQGI DLLFEALTER LASSMVECQL RIPPQHQGRF RSTFFQMKCI QQEEYDQDGN LLIDIRMQQV DWSRLEKREG AVLSDFIVT // ID Q7MTR0_PORGI Unreviewed; 406 AA. AC Q7MTR0; DT 15-DEC-2003, integrated into UniProtKB/TrEMBL. DT 15-DEC-2003, sequence version 1. DT 07-JUN-2017, entry version 103. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:AAQ66870.1}; GN OrderedLocusNames=PG_1886 {ECO:0000313|EMBL:AAQ66870.1}; OS Porphyromonas gingivalis (strain ATCC BAA-308 / W83). OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; OC Porphyromonadaceae; Porphyromonas. OX NCBI_TaxID=242619 {ECO:0000313|EMBL:AAQ66870.1, ECO:0000313|Proteomes:UP000000588}; RN [1] {ECO:0000313|EMBL:AAQ66870.1, ECO:0000313|Proteomes:UP000000588} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-308 / W83 {ECO:0000313|Proteomes:UP000000588}; RX PubMed=12949112; DOI=10.1128/JB.185.18.5591-5601.2003; RA Nelson K., Fleishmann R., DeBoy R., Paulsen I., Fouts D., Eisen J., RA Daugherty S., Dodson R., Durkin A., Gwinn M., Haft D., Kolonay J., RA Nelson W., White O., Mason T., Tallon L., Gray J., Granger D., RA Tettelin H., Dong H., Galvin J., Duncan M., Dewhirst F., Fraser C.; RT "Complete genome sequence of the oral pathogenic bacterium RT Porphyromonas gingivalis strain W83."; RL J. Bacteriol. 185:5591-5601(2003). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE015924; AAQ66870.1; -; Genomic_DNA. DR RefSeq; WP_004583549.1; NC_002950.2. DR ProteinModelPortal; Q7MTR0; -. DR STRING; 242619.PG1886; -. DR EnsemblBacteria; AAQ66870; AAQ66870; PG_1886. DR GeneID; 29256966; -. DR KEGG; pgi:PG_1886; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR KO; K03665; -. DR OMA; HPATYIG; -. DR Proteomes; UP000000588; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000000588}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000000588}. FT DOMAIN 202 387 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 163 197 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 406 AA; 46320 MW; 17431CD6528672A8 CRC64; MKEFIISEAR TEPTVLVGLI TPQQSETQVR EYLDELAFLC ETAGAQPIAR FTQKLDQPNS VTFVGKGKLD EIRAYVQENE IGMVVFDDEL SPKQLRNIEK ELQTKILDRT GLILDIFARR AQTAHAKTQV ELAQYQYMLP RLTGLWTHLE RQRGGVGMRG PGEKQLETDR RIVLDKIARL KEELRDIDKQ KSVQRKNRGK MVRVALVGYT NVGKSTLMNV LSKSEVFAEN KLFATLDTTV RKVIIDNLPF LLSDTVGFIR KLPTQLVESF KSTLDEVREA DLLVHVVDMS HPAFEEQIEV VNQTLAEITA GEEKPMLLLF NKIDAFSFTP KDEDDLTPRT KENISAEELQ QTWMAKLGND CLFVSAKKGT GMDALKALLY ERAKAIHITR FPYNDFLFQD YSEEME // ID Q7MYU1_PHOLL Unreviewed; 426 AA. AC Q7MYU1; DT 15-DEC-2003, integrated into UniProtKB/TrEMBL. DT 15-DEC-2003, sequence version 1. DT 30-AUG-2017, entry version 92. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:CAE16952.1}; GN OrderedLocusNames=plu4580 {ECO:0000313|EMBL:CAE16952.1}; OS Photorhabdus luminescens subsp. laumondii (strain DSM 15139 / CIP OS 105565 / TT01). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; OC Morganellaceae; Photorhabdus. OX NCBI_TaxID=243265 {ECO:0000313|EMBL:CAE16952.1, ECO:0000313|Proteomes:UP000002514}; RN [1] {ECO:0000313|Proteomes:UP000002514} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 15139 / CIP 105565 / TT01 RC {ECO:0000313|Proteomes:UP000002514}; RX PubMed=14528314; DOI=10.1038/nbt886; RA Duchaud E., Rusniok C., Frangeul L., Buchrieser C., Givaudan A., RA Taourit S., Bocs S., Boursaux-Eude C., Chandler M., Charles J.-F., RA Dassa E., Derose R., Derzelle S., Freyssinet G., Gaudriault S., RA Medigue C., Lanois A., Powell K., Siguier P., Vincent R., Wingate V., RA Zouine M., Glaser P., Boemare N., Danchin A., Kunst F.; RT "The genome sequence of the entomopathogenic bacterium Photorhabdus RT luminescens."; RL Nat. Biotechnol. 21:1307-1313(2003). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BX571874; CAE16952.1; -; Genomic_DNA. DR RefSeq; WP_011148653.1; NC_005126.1. DR ProteinModelPortal; Q7MYU1; -. DR STRING; 243265.plu4580; -. DR EnsemblBacteria; CAE16952; CAE16952; plu4580. DR KEGG; plu:plu4580; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000002514; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000002514}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000002514}. FT DOMAIN 198 365 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 164 191 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 426 AA; 48068 MW; 3455903FAB798B86 CRC64; MFERYEGGEQ AVVVHVFFSQ DKDTDNLSEF ESLVTSAGVV PVQIVTGSRK APHPKYFVGE GKAEEIAEAV QASGADVVLF NHALSPAQER NLERLCQCRV IDRTGVILDI FAQRARTHEG KLQVELAQLR HLSTRLVRGW THLERQKGGI GLRGPGETQL ETDRRLLRDK IRQILNRLSR VEKQREQGRQ ARNKADIPTV SLVGYTNAGK SSLFNRMTAA EVYAADQLFA TLDPTLRRID VNDVGTVVLA DTVGFIRHLP HDLVAAFKAT LQETRQATLL LHIVDAADSR IDENIAAVDS VLEEIEAHEI PVLLVMNKID MLDSFTPRID RNEDNLPVRV WLSAQTGEGI PLLLQALTER LSGEIAHYEL RLPPEAGRLR SRFYQLQAIE KEWIEEDGKV GIEVRMPIVD WHRLCKQEQD LFDYVV // ID Q7NDU0_GLOVI Unreviewed; 586 AA. AC Q7NDU0; DT 15-DEC-2003, integrated into UniProtKB/TrEMBL. DT 15-DEC-2003, sequence version 1. DT 07-JUN-2017, entry version 90. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=glr4142 {ECO:0000313|EMBL:BAC92083.1}; OS Gloeobacter violaceus (strain PCC 7421). OC Bacteria; Cyanobacteria; Gloeobacteria; Gloeobacterales; OC Gloeobacteraceae; Gloeobacter. OX NCBI_TaxID=251221 {ECO:0000313|EMBL:BAC92083.1, ECO:0000313|Proteomes:UP000000557}; RN [1] {ECO:0000313|EMBL:BAC92083.1, ECO:0000313|Proteomes:UP000000557} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=PCC 7421 {ECO:0000313|EMBL:BAC92083.1, RC ECO:0000313|Proteomes:UP000000557}; RX PubMed=14621292; DOI=10.1093/dnares/10.4.137; RA Nakamura Y., Kaneko T., Sato S., Mimuro M., Miyashita H., Tsuchiya T., RA Sasamoto S., Watanabe A., Kawashima K., Kishida Y., Kiyokawa C., RA Kohara M., Matsumoto M., Matsuno A., Nakazaki N., Shimpo S., RA Takeuchi C., Yamada M., Tabata S.; RT "Complete genome structure of Gloeobacter violaceus PCC 7421, a RT cyanobacterium that lacks thylakoids."; RL DNA Res. 10:137-145(2003). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BA000045; BAC92083.1; -; Genomic_DNA. DR RefSeq; NP_927088.1; NC_005125.1. DR RefSeq; WP_011144128.1; NC_005125.1. DR ProteinModelPortal; Q7NDU0; -. DR STRING; 251221.glr4142; -. DR EnsemblBacteria; BAC92083; BAC92083; BAC92083. DR GeneID; 2602545; -. DR KEGG; gvi:glr4142; -. DR PATRIC; fig|251221.4.peg.4175; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR InParanoid; Q7NDU0; -. DR KO; K03665; -. DR OMA; EREVIIT; -. DR OrthoDB; POG091H0464; -. DR PhylomeDB; Q7NDU0; -. DR Proteomes; UP000000557; Chromosome. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0043022; F:ribosome binding; IBA:GO_Central. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000000557}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000000557}. FT DOMAIN 403 568 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 369 396 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 586 AA; 64890 MW; F1018842B77F36C3 CRC64; MAIDSTITAF REPAIDKIYG PHKGLKPAQL RQLSRLYSRP FPVNRFLSPE FAERLAALSA ELETPLCVYA NRRGQVVRVG VGTPKETQFS PDELPRQGAE RLSGLRCVAT RLDGDGPSRG DLTALALQRL DALVILDVAI QGYRRQGGGL SGFVQRVHIA NLVPDPLAKW VVSTPQPLGQ VSNQDFDEFL GDLEDEFRRE WTARVVESDR ERVLLIDFFS TRTSQRAMEE ELSELVQLVT SAGGEVLKVF YQRREQPDPS TLIGRGKLEE VALSVQELGA NLVVCGRELT SSQARNLELA LGVRVVDRTE LILDIFARRA RSHEGKLQVE LAQLQYLMPR LTGKGEALSR LGGGIGTRGP GETKLETDRR VIRRRIAKLQ GEVDDLQAHR ARMRARRQRK EVPVFALVGY TNAGKSTLLN ALTGAGTLVA DQLFATLDPT TRRLELPTGD AVLLTDTVGF VHDLPPQLID AFRATLEEVT EADALLHVVD LSNPAWMNHI QAVQHILESL PIATGPQLLV FNKVDRVSSQ VRAFAEQEYP LAIFISAKNG WGFLALREAL TRWMRSLSDL WPPMAESGTG GETDLN // ID Q7NS94_CHRVO Unreviewed; 376 AA. AC Q7NS94; DT 15-DEC-2003, integrated into UniProtKB/TrEMBL. DT 15-DEC-2003, sequence version 1. DT 07-JUN-2017, entry version 93. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:AAQ61194.1}; GN OrderedLocusNames=CV_3532 {ECO:0000313|EMBL:AAQ61194.1}; OS Chromobacterium violaceum (strain ATCC 12472 / DSM 30191 / JCM 1249 / OS NBRC 12614 / NCIMB 9131 / NCTC 9757). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Chromobacteriaceae; Chromobacterium. OX NCBI_TaxID=243365 {ECO:0000313|EMBL:AAQ61194.1, ECO:0000313|Proteomes:UP000001424}; RN [1] {ECO:0000313|EMBL:AAQ61194.1, ECO:0000313|Proteomes:UP000001424} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 12472 / DSM 30191 / JCM 1249 / NBRC 12614 / NCIMB 9131 / RC NCTC 9757 {ECO:0000313|Proteomes:UP000001424}; RX PubMed=14500782; DOI=10.1073/pnas.1832124100; RA Vasconcelos A.T.R., de Almeida D.F., Almeida F.C., de Almeida L.G.P., RA de Almeida R., Goncalves J.A.A., Andrade E.M., Antonio R.V., RA Araripe J., de Araujo M.F.F., Filho S.A., Azevedo V., Batista A.J., RA Bataus L.A.M., Batista J.S., Belo A., vander Berg C., Blamey J., RA Bogo M., Bonato S., Bordignon J., Brito C.A., Brocchi M., Burity H.A., RA Camargo A.A., Cardoso D.D.P., Carneiro N.P., Carraro D.M., RA Carvalho C.M.B., Cascardo J.C.M., Cavada B.S., Chueire L.M.O., RA Pasa T.B.C., Duran N., Fagundes N., Falcao C.L., Fantinatti F., RA Farias I.P., Felipe M.S.S., Ferrari L.P., Ferro J.A., Ferro M.I.T., RA Franco G.R., Freitas N.S.A., Furlan L.R., Gazzinelli R.T., Gomes E.A., RA Goncalves P.R., Grangeiro T.B., Grattapaglia D., Grisard E.C., RA Guimaraes C.T., Hanna E.S., Hungria M., Jardim S.N., Laurino J., RA Leoi L.C.T., Fassarella L., Lima A., Loureiro M.F., Lyra M.C.P., RA Macedo M., Madeira H.M.F., Manfio G.P., Maranhao A.Q., Martins W.S., RA di Mauro S.M.Z., de Medeiros S.R.B., Meissner R.D.V., Menck C.F.M., RA Moreira M.A.M., Nascimento F.F., Nicolas M.F., Oliveira J.G., RA Oliveira S.C., Paixao R.F.C., Parente J.A., Pedrosa F.O., Pena S.J.D., RA Perreira J.O., Perreira M., Pinto L.S.R.C., Pinto L.S., Porto J.I.R., RA Potrich D.P., Neto C.E.R., Reis A.M.M., Rigo L.U., Rondinelli E., RA dos Santos E.B.P., Santos F.R., Schneider M.P.C., Seuanez H.N., RA Silva A.M.R., da Silva A.L.C., Silva D.W., Silva R., Simoes I.C., RA Simon D., Soares C.M.A., Soares R.B.A., Souza E.M., Souza K.R.L., RA Souza R.C., Steffens M.B.R., Steindel M., Teixeira S.R., Urmenyi T., RA Vettore A., Wassem R., Zaha A., Simpson A.J.G.; RT "The complete genome sequence of Chromobacterium violaceum reveals RT remarkable and exploitable bacterial adaptability."; RL Proc. Natl. Acad. Sci. U.S.A. 100:11660-11665(2003). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE016825; AAQ61194.1; -; Genomic_DNA. DR RefSeq; WP_011137079.1; NC_005085.1. DR ProteinModelPortal; Q7NS94; -. DR STRING; 243365.CV_3532; -. DR DNASU; 2547626; -. DR EnsemblBacteria; AAQ61194; AAQ61194; CV_3532. DR GeneID; 24948784; -. DR KEGG; cvi:CV_3532; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; FNNHAHV; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000001424; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000001424}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000001424}. FT DOMAIN 198 364 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 376 AA; 41588 MW; 85C84C81797574D7 CRC64; MFDRPDLGDQ AILVSLDFGD ADYQESVAEC AELVRGSKVE ILGMVQGKRQ RPDAALFAGK GKVEEIASMV RATGANVVIF NHALSPGQER NLERALQCRV IDRNSLILDI FAQRARSHEG KLQVELAQLS HLSTRLVRGW THLERQKGGV GLRGPGETQL ETDRRLLGIR VKALKDRLAQ VQKQRNTQRR SRNRAGVSSV SIVGYTNAGK STLFNALTKA NIYAADQLFA TLDTTSRKLF LNHDCSVVLS DTVGFIRDLP HTLVAAFRAT LEETVQANLL LHVVDCANET RDAQIDEVNK VLAEIDADGI PQLIVWNKGD LRELPPEIER DEDGVAVAVR VSALKGEGLE LLREAIAERV QPFANNHKEP YEHVAE // ID Q7NU63_CHRVO Unreviewed; 462 AA. AC Q7NU63; DT 15-DEC-2003, integrated into UniProtKB/TrEMBL. DT 15-DEC-2003, sequence version 1. DT 07-JUN-2017, entry version 94. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=CV_2840 {ECO:0000313|EMBL:AAQ60508.1}; OS Chromobacterium violaceum (strain ATCC 12472 / DSM 30191 / JCM 1249 / OS NBRC 12614 / NCIMB 9131 / NCTC 9757). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Chromobacteriaceae; Chromobacterium. OX NCBI_TaxID=243365 {ECO:0000313|EMBL:AAQ60508.1, ECO:0000313|Proteomes:UP000001424}; RN [1] {ECO:0000313|EMBL:AAQ60508.1, ECO:0000313|Proteomes:UP000001424} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 12472 / DSM 30191 / JCM 1249 / NBRC 12614 / NCIMB 9131 / RC NCTC 9757 {ECO:0000313|Proteomes:UP000001424}; RX PubMed=14500782; DOI=10.1073/pnas.1832124100; RA Vasconcelos A.T.R., de Almeida D.F., Almeida F.C., de Almeida L.G.P., RA de Almeida R., Goncalves J.A.A., Andrade E.M., Antonio R.V., RA Araripe J., de Araujo M.F.F., Filho S.A., Azevedo V., Batista A.J., RA Bataus L.A.M., Batista J.S., Belo A., vander Berg C., Blamey J., RA Bogo M., Bonato S., Bordignon J., Brito C.A., Brocchi M., Burity H.A., RA Camargo A.A., Cardoso D.D.P., Carneiro N.P., Carraro D.M., RA Carvalho C.M.B., Cascardo J.C.M., Cavada B.S., Chueire L.M.O., RA Pasa T.B.C., Duran N., Fagundes N., Falcao C.L., Fantinatti F., RA Farias I.P., Felipe M.S.S., Ferrari L.P., Ferro J.A., Ferro M.I.T., RA Franco G.R., Freitas N.S.A., Furlan L.R., Gazzinelli R.T., Gomes E.A., RA Goncalves P.R., Grangeiro T.B., Grattapaglia D., Grisard E.C., RA Guimaraes C.T., Hanna E.S., Hungria M., Jardim S.N., Laurino J., RA Leoi L.C.T., Fassarella L., Lima A., Loureiro M.F., Lyra M.C.P., RA Macedo M., Madeira H.M.F., Manfio G.P., Maranhao A.Q., Martins W.S., RA di Mauro S.M.Z., de Medeiros S.R.B., Meissner R.D.V., Menck C.F.M., RA Moreira M.A.M., Nascimento F.F., Nicolas M.F., Oliveira J.G., RA Oliveira S.C., Paixao R.F.C., Parente J.A., Pedrosa F.O., Pena S.J.D., RA Perreira J.O., Perreira M., Pinto L.S.R.C., Pinto L.S., Porto J.I.R., RA Potrich D.P., Neto C.E.R., Reis A.M.M., Rigo L.U., Rondinelli E., RA dos Santos E.B.P., Santos F.R., Schneider M.P.C., Seuanez H.N., RA Silva A.M.R., da Silva A.L.C., Silva D.W., Silva R., Simoes I.C., RA Simon D., Soares C.M.A., Soares R.B.A., Souza E.M., Souza K.R.L., RA Souza R.C., Steffens M.B.R., Steindel M., Teixeira S.R., Urmenyi T., RA Vettore A., Wassem R., Zaha A., Simpson A.J.G.; RT "The complete genome sequence of Chromobacterium violaceum reveals RT remarkable and exploitable bacterial adaptability."; RL Proc. Natl. Acad. Sci. U.S.A. 100:11660-11665(2003). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE016825; AAQ60508.1; -; Genomic_DNA. DR RefSeq; WP_011136387.1; NC_005085.1. DR ProteinModelPortal; Q7NU63; -. DR STRING; 243365.CV_2840; -. DR EnsemblBacteria; AAQ60508; AAQ60508; CV_2840. DR GeneID; 24945926; -. DR KEGG; cvi:CV_2840; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; VILEIFH; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000001424; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000001424}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000001424}. FT DOMAIN 226 396 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 189 221 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 462 AA; 51616 MW; 6BC6950CFA4FB516 CRC64; MQTEVKETPR YAIVASVQLP EVSDAEFEAS LTELSELAKT LGFQVVQTFV QKRSSFDRTA YMGVGKLDEI SMYVKRGIRA DELEDEPQEL DASSVAIDAL LVDHEISPSQ ARNLELAVGC EVMDRTMVIL EIFHRNARSR AARAQVEIAR LGYMAPRLRE AAKLAGPQGR QRSGMGGRGA GESHTELDRR KVRDRIAELQ REIVAMELER KTQRARRLER QGLGLGGVSL VGYTNAGKST LMRALTGSEV LVANKLFATL DTTVRVLHPE SVPRVLVSDT VGFIKNLPHG LVASFKSTLE EALDASLLLH AIDASDPGFQ RQLEVTDEVL REIGADDVPR IRVFNKIDHV GDEAEQAAWT AELRQRYPGC VVMSALRPED VASLRAAIVA FFQQDLVEDE LLLPWSAQQL RGEIYSHCQV LEERAEEEGC WFRVRGEPEK LRSLREQLNP GSQGREKEYW EA // ID Q7P539_FUSNV Unreviewed; 600 AA. AC Q7P539; DT 15-DEC-2003, integrated into UniProtKB/TrEMBL. DT 15-DEC-2003, sequence version 1. DT 05-JUL-2017, entry version 58. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=FNV0690 {ECO:0000313|EMBL:EAA23778.1}; OS Fusobacterium nucleatum subsp. vincentii ATCC 49256. OC Bacteria; Fusobacteria; Fusobacteriales; Fusobacteriaceae; OC Fusobacterium. OX NCBI_TaxID=209882 {ECO:0000313|EMBL:EAA23778.1, ECO:0000313|Proteomes:UP000006454}; RN [1] {ECO:0000313|EMBL:EAA23778.1, ECO:0000313|Proteomes:UP000006454} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 49256 {ECO:0000313|EMBL:EAA23778.1, RC ECO:0000313|Proteomes:UP000006454}; RX PubMed=12799352; DOI=10.1101/gr.566003; RA Kapatral V., Ivanova N., Anderson I., Reznik G., Bhattacharyya A., RA Gardner W.L., Mikhailova N., Lapidus A., Larsen N., D'Souza M., RA Walunas T., Haselkorn R., Overbeek R., Kyrpides N.; RT "Genome analysis of F. nucleatum sub spp vincentii and its comparison RT with the genome of F. nucleatum ATCC 25586."; RL Genome Res. 13:1180-1189(2003). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EAA23778.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AABF01000085; EAA23778.1; -; Genomic_DNA. DR ProteinModelPortal; Q7P539; -. DR EnsemblBacteria; EAA23778; EAA23778; FNV0690. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000006454; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000006454}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}. FT DOMAIN 361 546 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 600 AA; 68389 MW; DE3DB944438E6630 CRC64; MINGNTSGLK EYILENLDKL YSTKIEKGKI INQEIVNYIS EISNKINREI NIAIDRNGNI IDISIGDSST VNLPVVPVYD KKLSGVRIIH THPGGNPHLS SVDISALIKL KLDCIVSIGV SEEGITGYEV AICNIVNDEL TYDRTLLKNL NDFDYLEEIK EVEENLRKRN ITEDDKEYAL LIGIDEEEYL DELEELASAC DVKVVGRFFQ KRSKPDPVFL IGSGKVQELA LVRQVRKANL LIFDEELSGL QLKMIEEVTG CKVIDRTTLI LEIFARRART REAKLQVELA QLKYRSNRLI GFGVTMSRLG GGVGTKGSGE KKLEIDRRVI KKTISYLNNE LENIKKVRNT QRSKREDSGI PRVSLVGYTN VGKSTLRNVL VDMYQNDKTL KKEEVLSQDM LFATLDTTTR TIELKDKRIV SLTDTVGFIQ KLPHDLVESF KSTLEEVIFS DLIIHVADIS SKNVIEQIDA VEKVLEELNC LDKTKILLLN KIDYVTKDNS FPLMEKKIEE IKEKYSNYQI LIISAKNRFN IDELMDLIKK NLIVKTYNCK LLIPYVNTEI AARVHRNTIV KSESFVDEGI ILEVVMNEKE YNKFKDFILN // ID Q7PML7_ANOGA Unreviewed; 543 AA. AC Q7PML7; DT 15-DEC-2003, integrated into UniProtKB/TrEMBL. DT 23-OCT-2007, sequence version 4. DT 30-AUG-2017, entry version 87. DE SubName: Full=AGAP003969-PA {ECO:0000313|EMBL:EAA13619.5}; DE SubName: Full=GTP-binding protein 6 {ECO:0000313|VectorBase:AGAP003969-PA}; GN Name=1278789 {ECO:0000313|VectorBase:AGAP003969-PA}; GN ORFNames=AgaP_AGAP003969 {ECO:0000313|EMBL:EAA13619.5}; OS Anopheles gambiae (African malaria mosquito). OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; OC Pterygota; Neoptera; Holometabola; Diptera; Nematocera; Culicoidea; OC Culicidae; Anophelinae; Anopheles. OX NCBI_TaxID=7165 {ECO:0000313|Proteomes:UP000007062}; RN [1] {ECO:0000313|VectorBase:AGAP003969-PA} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=PEST {ECO:0000313|VectorBase:AGAP003969-PA}; RX PubMed=9087549; DOI=10.1111/j.1365-2583.1993.tb00131.x; RA Beard C.B., Hamm D.M., Collins F.H.; RT "The mitochondrial genome of the mosquito Anopheles gambiae: DNA RT sequence, genome organization, and comparisons with mitochondrial RT sequences of other insects."; RL Insect Mol. Biol. 2:103-124(1993). RN [2] {ECO:0000313|EMBL:EAA13619.5, ECO:0000313|Proteomes:UP000007062} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=PEST {ECO:0000313|EMBL:EAA13619.5, RC ECO:0000313|Proteomes:UP000007062}; RX PubMed=12364791; DOI=10.1126/science.1076181; RA Holt R.A., Subramanian G.M., Halpern A., Sutton G.G., Charlab R., RA Nusskern D.R., Wincker P., Clark A.G., Ribeiro J.M., Wides R., RA Salzberg S.L., Loftus B., Yandell M., Majoros W.H., Rusch D.B., RA Lai Z., Kraft C.L., Abril J.F., Anthouard V., Arensburger P., RA Atkinson P.W., Baden H., de Berardinis V., Baldwin D., Benes V., RA Biedler J., Blass C., Bolanos R., Boscus D., Barnstead M., Cai S., RA Center A., Chaturverdi K., Christophides G.K., Chrystal M.A., RA Clamp M., Cravchik A., Curwen V., Dana A., Delcher A., Dew I., RA Evans C.A., Flanigan M., Grundschober-Freimoser A., Friedli L., Gu Z., RA Guan P., Guigo R., Hillenmeyer M.E., Hladun S.L., Hogan J.R., RA Hong Y.S., Hoover J., Jaillon O., Ke Z., Kodira C., Kokoza E., RA Koutsos A., Letunic I., Levitsky A., Liang Y., Lin J.J., Lobo N.F., RA Lopez J.R., Malek J.A., McIntosh T.C., Meister S., Miller J., RA Mobarry C., Mongin E., Murphy S.D., O'Brochta D.A., Pfannkoch C., RA Qi R., Regier M.A., Remington K., Shao H., Sharakhova M.V., RA Sitter C.D., Shetty J., Smith T.J., Strong R., Sun J., Thomasova D., RA Ton L.Q., Topalis P., Tu Z., Unger M.F., Walenz B., Wang A., Wang J., RA Wang M., Wang X., Woodford K.J., Wortman J.R., Wu M., Yao A., RA Zdobnov E.M., Zhang H., Zhao Q., Zhao S., Zhu S.C., Zhimulev I., RA Coluzzi M., della Torre A., Roth C.W., Louis C., Kalush F., RA Mural R.J., Myers E.W., Adams M.D., Smith H.O., Broder S., RA Gardner M.J., Fraser C.M., Birney E., Bork P., Brey P.T., Venter J.C., RA Weissenbach J., Kafatos F.C., Collins F.H., Hoffman S.L.; RT "The genome sequence of the malaria mosquito Anopheles gambiae."; RL Science 298:129-149(2002). RN [3] {ECO:0000313|EMBL:EAA13619.5} RP NUCLEOTIDE SEQUENCE. RC STRAIN=PEST {ECO:0000313|EMBL:EAA13619.5}; RG The Anopheles Genome Sequencing Consortium; RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases. RN [4] {ECO:0000313|EMBL:EAA13619.5} RP NUCLEOTIDE SEQUENCE. RC STRAIN=PEST {ECO:0000313|EMBL:EAA13619.5}; RX PubMed=14747013; DOI=10.1016/j.pt.2003.11.003; RA Mongin E., Louis C., Holt R.A., Birney E., Collins F.H.; RT "The Anopheles gambiae genome: an update."; RL Trends Parasitol. 20:49-52(2004). RN [5] {ECO:0000313|EMBL:EAA13619.5} RP NUCLEOTIDE SEQUENCE. RC STRAIN=PEST {ECO:0000313|EMBL:EAA13619.5}; RX PubMed=17210077; DOI=10.1186/gb-2007-8-1-r5; RA Sharakhova M.V., Hammond M.P., Lobo N.F., Krzywinski J., Unger M.F., RA Hillenmeyer M.E., Bruggner R.V., Birney E., Collins F.H.; RT "Update of the Anopheles gambiae PEST genome assembly."; RL Genome Biol. 8:R5-R5(2007). RN [6] {ECO:0000313|EMBL:EAA13619.5} RP NUCLEOTIDE SEQUENCE. RC STRAIN=PEST {ECO:0000313|EMBL:EAA13619.5}; RG VectorBase; RL Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases. RN [7] {ECO:0000313|VectorBase:AGAP003969-PA} RP IDENTIFICATION. RC STRAIN=PEST {ECO:0000313|VectorBase:AGAP003969-PA}; RG VectorBase; RL Submitted (FEB-2017) to UniProtKB. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AAAB01008978; EAA13619.5; -; Genomic_DNA. DR RefSeq; XP_318421.4; XM_318421.4. DR ProteinModelPortal; Q7PML7; -. DR STRING; 7165.AGAP003969-PA; -. DR PaxDb; Q7PML7; -. DR EnsemblMetazoa; AGAP003969-RA; AGAP003969-PA; AGAP003969. DR GeneID; 1278789; -. DR KEGG; aga:AgaP_AGAP003969; -. DR VectorBase; AGAP003969-RA; AGAP003969-PA; AGAP003969. DR eggNOG; KOG0410; Eukaryota. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000045792; -. DR InParanoid; Q7PML7; -. DR OMA; MDTVGFM; -. DR OrthoDB; EOG091G0852; -. DR PhylomeDB; Q7PML7; -. DR Proteomes; UP000007062; Chromosome 2R. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR GO; GO:0043022; F:ribosome binding; IBA:GO_Central. DR CDD; cd01878; HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 2. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000007062}; KW Reference proteome {ECO:0000313|Proteomes:UP000007062}. FT DOMAIN 305 482 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 543 AA; 61532 MW; 6D03F523F14FA50A CRC64; MLGLSVRSIV RKACVKNVFL QSFQPKCRNE VERCRQLTQL FFCREKYTDS SKYKGGKQAG QRQKAIASKH EDDDEALDET MNQRTELIED REYDTVASSA MHVTKQILNV QHVVIIQPYI KWGPRKNPTK PDLLLQEAEA LVRSLPRWNI ELSMKVPVET LDKRQLFGTG KLEELKGIIQ ARQETGTPLT CVFISKGTLT YGQKQTLEQV FRLPVMDRYS VVVQILRLHA VSMEAKLQVA LAELPYIWSQ VKDQEGSTKG GGRIFLSDSQ RQMLQLRERK LRNELATIRT HRELLRNRRR QKNFPVVAVV GYTNAGKTSL IKALTEEQSL QPRDQLFATL DVTAHAGLLP CKLEVLYMDT VGFMADIPTG LIECFVATLE DAMLADVIVH VQDMAHENCA EQRAHVERTL GKLMQQGNNG AGALTPERII NVGNKIDLVA DPADLRMDSD GEQQRLHLIS SRTLVGVHEL LLEVERRVLR ATGRQRMVIR VPMGGQELAW LYKNAAVTES AADPNNAERL LVSVVITEAK LQQFRHLFIR NRG // ID Q7U4A5_SYNPX Unreviewed; 562 AA. AC Q7U4A5; DT 01-OCT-2003, integrated into UniProtKB/TrEMBL. DT 01-OCT-2003, sequence version 1. DT 07-JUN-2017, entry version 87. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=SYNW2166 {ECO:0000313|EMBL:CAE08681.1}; OS Synechococcus sp. (strain WH8102). OC Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; OC Synechococcus. OX NCBI_TaxID=84588 {ECO:0000313|EMBL:CAE08681.1, ECO:0000313|Proteomes:UP000001422}; RN [1] {ECO:0000313|EMBL:CAE08681.1, ECO:0000313|Proteomes:UP000001422} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=WH8102 {ECO:0000313|EMBL:CAE08681.1, RC ECO:0000313|Proteomes:UP000001422}; RX PubMed=12917641; DOI=10.1038/nature01943; RA Palenik B., Brahamsha B., Larimer F., Land M., Hauser L., Chain P., RA Lamerdin J., Regala W., Allen E.A., McCarren J., Paulsen I., RA Dufresne A., Partensky F., Webb E., Waterbury J.; RT "The genome of a motile marine Synechococcus."; RL Nature 424:1037-1042(2003). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BX569694; CAE08681.1; -; Genomic_DNA. DR RefSeq; WP_011129021.1; NC_005070.1. DR ProteinModelPortal; Q7U4A5; -. DR STRING; 84588.SYNW2166; -. DR EnsemblBacteria; CAE08681; CAE08681; SYNW2166. DR KEGG; syw:SYNW2166; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; NPQTLWG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000001422; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000001422}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000001422}. FT DOMAIN 375 547 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 336 370 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 562 AA; 62320 MW; A5CB8AC5E3CCBE0C CRC64; MKQAHLGGRT RGLRPGQQRQ LDRLSHRRHP EGSGADLLTL ERMAGLVQEL EQSMHLVLDG RGLCRLLWLG PLQSSEALRQ HLPQAPRRRG GGWRLLSCPF SRHGLHQDMA EAVIALDLNP ICWLRFAPVP ARDGLRNAEL LQPDREEAHG WRQLDQGDLR HLCQQDLNSG AITTPELSPA SAGTAIESVL LLTLTSGEAD RSERELAELE GLVRSAGAQP VAVVTQRAGS ANPQTLWGTG KLQEAALEVR RRGASLVVTD RELTPVQARN LERLLACPVS DRSELILDIF AQRAGSAAGR LQVELAQLRY RLPRLLGRGR SLSRQGGGIG TRGPGETQLE KDRRAISRRI DRLLRDQQQL QQHRSRLRDQ RRGLPRVALV GYTNAGKSSL LNALCGRRES DRVLAENKLF ATLDPTTRRL DLPQPGQRPD RLLITDTVGF IRDLPKPLVE AFRATLEEAL DADVLLVVVD LADPDWSGQL STVHRLLDSL GSTAMRRVVA NQIDRCPLDA VETIRRQDAQ TLFLSAKRGD GLRGLQDWLR EQFFDPGAES DLDAGPPPEW PS // ID Q7UPD7_RHOBA Unreviewed; 459 AA. AC Q7UPD7; DT 01-OCT-2003, integrated into UniProtKB/TrEMBL. DT 01-OCT-2003, sequence version 1. DT 07-JUN-2017, entry version 88. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:CAD75125.1}; GN OrderedLocusNames=RB7008 {ECO:0000313|EMBL:CAD75125.1}; OS Rhodopirellula baltica (strain DSM 10527 / NCIMB 13988 / SH1). OC Bacteria; Planctomycetes; Planctomycetia; Planctomycetales; OC Planctomycetaceae; Rhodopirellula. OX NCBI_TaxID=243090 {ECO:0000313|EMBL:CAD75125.1, ECO:0000313|Proteomes:UP000001025}; RN [1] {ECO:0000313|EMBL:CAD75125.1, ECO:0000313|Proteomes:UP000001025} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 10527 / NCIMB 13988 / SH1 RC {ECO:0000313|Proteomes:UP000001025}; RX PubMed=12835416; DOI=10.1073/pnas.1431443100; RA Gloeckner F.O., Kube M., Bauer M., Teeling H., Lombardot T., RA Ludwig W., Gade D., Beck A., Borzym K., Heitmann K., Rabus R., RA Schlesner H., Amann R., Reinhardt R.; RT "Complete genome sequence of the marine planctomycete Pirellula sp. RT strain 1."; RL Proc. Natl. Acad. Sci. U.S.A. 100:8298-8303(2003). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BX294145; CAD75125.1; -; Genomic_DNA. DR RefSeq; NP_867578.1; NC_005027.1. DR RefSeq; WP_011121200.1; NC_005027.1. DR ProteinModelPortal; Q7UPD7; -. DR STRING; 243090.RB7008; -. DR EnsemblBacteria; CAD75125; CAD75125; RB7008. DR GeneID; 1796986; -. DR KEGG; rba:RB7008; -. DR PATRIC; fig|243090.15.peg.3392; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR InParanoid; Q7UPD7; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000001025; Chromosome. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0043022; F:ribosome binding; IBA:GO_Central. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000001025}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000001025}. FT DOMAIN 202 368 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 163 190 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 459 AA; 51138 MW; 7C95C96C2567DDE7 CRC64; MSDKHITLHD DAPERSILAR LILPDTVVEE DPLEELHGLA TTSGTEVVDE LIQRRSTPDH STYLGKGKVE ELRLMVERHE ADVVIFDNDL SPAQIRNLEK KTNAKVIDRT ELILDIFAAG ARTHESRLAV ELAQLEYSLP RLKRMWTHLS RQSMGVGMRG PGEKQLEVDR RLAQKRIHDL KTELKSVELR RERQVAARSD SPTVSLVGYT NAGKSTLMNA LTDAGVMAQD KLFATLDTRT RRWHLPEWGH VLLSDTVGFI RDLPHSLVAS FKSTLEETRQ AELLLHVADA SSSQVFEQIS AVYQVLEELG IEAKDTLLVL NKIDAITSPR DLNRVLDRYP NAIPVSARSR SGLKPLAQAV GEALSREFLD VEIGVAHHDG KLLSFLSATG KIESREFGND HVIVRVRMPA SAMGTVNRSA LSVTPTTLEM WKQTASEEEL EDSSEDSSEE SVERSSDVA // ID Q7V5D8_PROMM Unreviewed; 558 AA. AC Q7V5D8; DT 01-OCT-2003, integrated into UniProtKB/TrEMBL. DT 01-OCT-2003, sequence version 1. DT 07-JUN-2017, entry version 91. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=PMT_1626 {ECO:0000313|EMBL:CAE21801.1}; OS Prochlorococcus marinus (strain MIT 9313). OC Bacteria; Cyanobacteria; Synechococcales; Prochloraceae; OC Prochlorococcus. OX NCBI_TaxID=74547 {ECO:0000313|EMBL:CAE21801.1, ECO:0000313|Proteomes:UP000001423}; RN [1] {ECO:0000313|EMBL:CAE21801.1, ECO:0000313|Proteomes:UP000001423} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MIT 9313 {ECO:0000313|Proteomes:UP000001423}; RX PubMed=12917642; DOI=10.1038/nature01947; RA Rocap G., Larimer F.W., Lamerdin J.E., Malfatti S., Chain P., RA Ahlgren N.A., Arellano A., Coleman M., Hauser L., Hess W.R., RA Johnson Z.I., Land M.L., Lindell D., Post A.F., Regala W., Shah M., RA Shaw S.L., Steglich C., Sullivan M.B., Ting C.S., Tolonen A., RA Webb E.A., Zinser E.R., Chisholm S.W.; RT "Genome divergence in two Prochlorococcus ecotypes reflects oceanic RT niche differentiation."; RL Nature 424:1042-1047(2003). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BX548175; CAE21801.1; -; Genomic_DNA. DR RefSeq; WP_011130993.1; NC_005071.1. DR ProteinModelPortal; Q7V5D8; -. DR STRING; 74547.PMT1626; -. DR EnsemblBacteria; CAE21801; CAE21801; PMT_1626. DR KEGG; pmt:PMT_1626; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR KO; K03665; -. DR OMA; NPQTLWG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000001423; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000001423}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000001423}. FT DOMAIN 375 547 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 336 370 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 558 AA; 62333 MW; 603CEB2943BDFD7D CRC64; MKQAHLAGRT KGLRPSQQRQ LERLSHRRHP EREGADQLTL ERLAEKVIEL CQPLHLVLDS RGLCRLLWVG PLDGSGQLLA HLPESPRRKS AGWRLISCSL TLQRNNLRPE QHDAIVALDL APNSWLRFAP TSDRGGRRIA ALWQPDPKEI SGWSLIEANG LSELCQHSQG STVKPEVTPL PSKDSRERVL LLTLTGPEQS RSERDLAELE GLVRSAGGHP VAVVRQKQGA PNPQTLWGKG KLQETALEVR RHSASLVITD RELNPVQVRN LERYLDCPVM DRSELILDIF AQRASSAAGR LQVELAQLRY RMPRLMGRGR SLSRQGGGIG TRGPGETQLE KDRRAITRRI EHLLREVRQL QNHRARLRNR REGLPRVALV GYTNAGKSSL LNALCSRNEH NKVLAENKLF ATLDPTTRRL LIPQTGGKPL ELLITDTVGF IRELPAPLVE AFRATLEETL EADLLLVVVD LSDTDWQAQL DTVHQLLNSL GSESIRQVIA NQIDRCDSSA LETIRSIDPK VIYLSAASGA GLQGLKHWLK DQFWGHRAES APLHSVNT // ID Q7VN45_HAEDU Unreviewed; 449 AA. AC Q7VN45; DT 01-OCT-2003, integrated into UniProtKB/TrEMBL. DT 01-OCT-2003, sequence version 1. DT 07-JUN-2017, entry version 91. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:AAP95650.1}; GN OrderedLocusNames=HD_0740 {ECO:0000313|EMBL:AAP95650.1}; OS Haemophilus ducreyi (strain 35000HP / ATCC 700724). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=233412 {ECO:0000313|EMBL:AAP95650.1, ECO:0000313|Proteomes:UP000001022}; RN [1] {ECO:0000313|Proteomes:UP000001022} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=35000HP / ATCC 700724 {ECO:0000313|Proteomes:UP000001022}; RA Munson R.S. Jr., Ray W.C., Mahairas G., Sabo P., Mungur R., RA Johnson L., Nguyen D., Wang J., Forst C., Hood L.; RT "The complete genome sequence of Haemophilus ducreyi."; RL Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE017143; AAP95650.1; -; Genomic_DNA. DR RefSeq; WP_010944702.1; NC_002940.2. DR ProteinModelPortal; Q7VN45; -. DR STRING; 233412.HD0740; -. DR EnsemblBacteria; AAP95650; AAP95650; HD_0740. DR GeneID; 24943670; -. DR KEGG; hdu:HD_0740; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000001022; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000001022}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000001022}. FT DOMAIN 214 381 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 173 207 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 449 AA; 50469 MW; B5D145D92A9B96A7 CRC64; MSNTESTPVF DVCLSEKSFP HAQDKAILVH VFLSQTKDID NLTEFQTLAE SAGVELLSTL TTSRNAPHIK YFVGQGKAEE IAQAVENLGA TVVLINHQLS PAQTRNLQNL CGCRIVDRSG LILDIFAQRA RSHEGKLQVE LAQLRHLSTR LVRRLGNQDQ QKGGSVGLRG PGETQLETDR RLIKVRIQQL QNQLDKVNKK RHQNRKTRQK ADIPTVSLVG YTNAGKSTLF NAITQAGVYA ADQLFATLDP TLRRMQIQDV GTTILADTVG FIRFLPHDLV SAFKSTLQET TEANLLLHVV DIADERKNDN ITAVNQVLDE IGALTLPSLL IYNKVDKITD ITPHIERNQE GKPIAVYLSA HTNQGIDLLY QAIRECLRNE LVCQKILLPT TAGQIYAQIR NQNCIKQEHF NQFGDRLIDI EVNAVQWQKW LKQYPALIEY VAFAKWENE // ID Q7VQP4_BLOFL Unreviewed; 372 AA. AC Q7VQP4; DT 01-OCT-2003, integrated into UniProtKB/TrEMBL. DT 01-OCT-2003, sequence version 1. DT 07-JUN-2017, entry version 102. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:CAD83603.1}; GN OrderedLocusNames=Bfl080 {ECO:0000313|EMBL:CAD83603.1}; OS Blochmannia floridanus. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; OC Enterobacteriaceae; ant endosymbionts; Candidatus Blochmannia. OX NCBI_TaxID=203907 {ECO:0000313|EMBL:CAD83603.1, ECO:0000313|Proteomes:UP000002192}; RN [1] {ECO:0000313|EMBL:CAD83603.1, ECO:0000313|Proteomes:UP000002192} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=12886019; DOI=10.1073/pnas.1533499100; RA Gil R., Silva F.J., Zientz E., Delmotte F., Gonzalez-Candelas F., RA Latorre A., Rausell C., Kramerbeek J., Gadau J., Hoelldobler B., RA van Ham R.C.H.J., Gross R., Moya A.; RT "The genome sequence of Blochmannia floridanus: comparative analysis RT of reduced genomes."; RL Proc. Natl. Acad. Sci. U.S.A. 100:9388-9393(2003). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BX248583; CAD83603.1; -; Genomic_DNA. DR RefSeq; WP_011126373.1; NC_005061.1. DR ProteinModelPortal; Q7VQP4; -. DR STRING; 203907.Bfl080; -. DR EnsemblBacteria; CAD83603; CAD83603; Bfl080. DR KEGG; bfl:Bfl080; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000002192; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000002192}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000002192}. FT DOMAIN 201 368 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 372 AA; 42499 MW; 0872C6C2EBFCAD70 CRC64; MIILNNINEH AILVYVLFSK SEDVDWNIKE CLDLAASNFI RVSNTLISSC KVINSKYFIG TGKVLALKSM LEHDPDVSVV LFNCTLSPNQ ERNLVRFLRC KIIDRNQLIL NIFAKHARTY EGKLQVKLAQ LRYFNSRLTH EWSHLERQRG GIGVRGGPGE MQLEKDRRLL SKKIFRVLSD LKKIENQRKQ NRCRRIRVGM STISLVGYTN AGKSTLFNVM TSSCVDVAEK LFVTLDPTFR RIIHGKKSNI ILIDTVGFIQ NLPKDLITAF KSTLQETMQS KLLIHVVDAS SKKVKQNIDI VNVILNEVNI YNVPKLVVMN KIDQMSKVQP HIDRDIDGFP IKVWISARNR VGIELLNQAI HELLSGDMIG YE // ID Q7VWL7_BORPE Unreviewed; 368 AA. AC Q7VWL7; DT 01-OCT-2003, integrated into UniProtKB/TrEMBL. DT 01-OCT-2003, sequence version 1. DT 07-JUN-2017, entry version 85. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:CAE42470.1}; GN OrderedLocusNames=BP2192 {ECO:0000313|EMBL:CAE42470.1}; OS Bordetella pertussis (strain Tohama I / ATCC BAA-589 / NCTC 13251). OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Alcaligenaceae; Bordetella. OX NCBI_TaxID=257313 {ECO:0000313|Proteomes:UP000002676}; RN [1] {ECO:0000313|Proteomes:UP000002676} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Tohama I / ATCC BAA-589 / NCTC 13251 RC {ECO:0000313|Proteomes:UP000002676}; RX PubMed=12910271; DOI=10.1038/ng1227; RA Parkhill J., Sebaihia M., Preston A., Murphy L.D., Thomson N., RA Harris D.E., Holden M.T., Churcher C.M., Bentley S.D., Mungall K.L., RA Cerdeno-Tarraga A.M., Temple L., James K., Harris B., Quail M.A., RA Achtman M., Atkin R., Baker S., Basham D., Bason N., Cherevach I., RA Chillingworth T., Collins M., Cronin A., Davis P., Doggett J., RA Feltwell T., Goble A., Hamlin N., Hauser H., Holroyd S., Jagels K., RA Leather S., Moule S., Norberczak H., O'Neil S., Ormond D., Price C., RA Rabbinowitsch E., Rutter S., Sanders M., Saunders D., Seeger K., RA Sharp S., Simmonds M., Skelton J., Squares R., Squares S., Stevens K., RA Unwin L., Whitehead S., Barrell B.G., Maskell D.J.; RT "Comparative analysis of the genome sequences of Bordetella pertussis, RT Bordetella parapertussis and Bordetella bronchiseptica."; RL Nat. Genet. 35:32-40(2003). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BX640417; CAE42470.1; -; Genomic_DNA. DR RefSeq; NP_880840.1; NC_002929.2. DR RefSeq; WP_010930789.1; NC_002929.2. DR ProteinModelPortal; Q7VWL7; -. DR STRING; 257313.BP2192; -. DR EnsemblBacteria; CAE42470; CAE42470; BP2192. DR GeneID; 2667292; -. DR KEGG; bpe:BP2192; -. DR PATRIC; fig|257313.5.peg.2366; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR Proteomes; UP000002676; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000002676}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000002676}. FT DOMAIN 190 354 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 368 AA; 40224 MW; 3F040BBB5171EBA4 CRC64; MRALIISVDL GNPDYPAHAE EFAMLAKGAG AEIVGTLTAR RDRPDAKFFI GSGKVEEGVA MAGALLADII LFDQPLSPAQ QRNLEREFNL RVVDRVALIL DIFALRAKSH EGKLQVELAQ LQHLATRLTR MWSHLERQRG GIGMRGPGEA QLEMDRRMIG AKVKVLRERL DRVERQRVTQ RRARARGGAL SVSLVGYTNA GKSTLFNAMT RAGAYAADQL FATLDTTTRR IWIDGAGSVV LSDTVGFIRD LPHNLIAAFR ATLEETVYAD LLLHVVDAAS AQRDEQIAEV DKVLAEIGAA QIPTILVYNK IDRAGLEPRV DRDAHGTIAR VFVSATERAG LDALRGAIAE IGQIVGNNVS NHQTLQSE // ID Q81A76_BACCR Unreviewed; 425 AA. AC Q81A76; DT 01-JUN-2003, integrated into UniProtKB/TrEMBL. DT 01-JUN-2003, sequence version 1. DT 07-JUN-2017, entry version 95. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=BC_3708 {ECO:0000313|EMBL:AAP10636.1}; OS Bacillus cereus (strain ATCC 14579 / DSM 31 / JCM 2152 / NBRC 15305 / OS NCIMB 9373 / NRRL B-3711). OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=226900 {ECO:0000313|EMBL:AAP10636.1, ECO:0000313|Proteomes:UP000001417}; RN [1] {ECO:0000313|EMBL:AAP10636.1, ECO:0000313|Proteomes:UP000001417} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 14579 / DSM 31 / JCM 2152 / NBRC 15305 / NCIMB 9373 / NRRL RC B-3711 {ECO:0000313|Proteomes:UP000001417}; RX PubMed=12721630; DOI=10.1038/nature01582; RA Ivanova N., Sorokin A., Anderson I., Galleron N., Candelon B., RA Kapatral V., Bhattacharyya A., Reznik G., Mikhailova N., Lapidus A., RA Chu L., Mazur M., Goltsman E., Larsen N., D'Souza M., Walunas T., RA Grechkin Y., Pusch G., Haselkorn R., Fonstein M., Ehrlich S.D., RA Overbeek R., Kyrpides N.; RT "Genome sequence of Bacillus cereus and comparative analysis with RT Bacillus anthracis."; RL Nature 423:87-91(2003). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE016877; AAP10636.1; -; Genomic_DNA. DR RefSeq; NP_833435.1; NC_004722.1. DR RefSeq; WP_011110320.1; NC_004722.1. DR ProteinModelPortal; Q81A76; -. DR STRING; 226900.BC3708; -. DR EnsemblBacteria; AAP10636; AAP10636; BC_3708. DR GeneID; 1206053; -. DR KEGG; bce:BC3708; -. DR PATRIC; fig|226900.8.peg.3817; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR KO; K03665; -. DR OMA; HPATYIG; -. DR Proteomes; UP000001417; Chromosome. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0043022; F:ribosome binding; IBA:GO_Central. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000001417}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000001417}. FT DOMAIN 198 360 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 425 AA; 48577 MW; F74B25D39C979C63 CRC64; MMEEKEKVIL VGCQLPQDDD EKFMHSMKEL ASLAKTARAE LLVSTTQKRP KFHPATYIGK GKLEELTMLT EELEPDVIVF NNELTPSQIR NLSSVLDARV IDRTQLILDI FAQRAKSREG KLQVELAQLQ YTMPRLMGQG LSLSRLGGGI GTRGPGETKL ETDRRHIRSR IDEIKKQLAV VVEHRKRYRE RRKDNKVFQV SLIGYTNAGK STLFNRLTEA DTFEENLLFA TLDPTTRKMP LPSGYTVLLT DTVGFIQDLP TSLIAAFRST LEEAGEADVI LHVVDSADPN YIGHEKTVKR LLSELEINHI PIITLYNKKD ELHQNFIPFP KSDFLMTSAF EESDVLRIKE AIEMKMKKEM DRYRVEIPPS EGKLLTLLKT ETLLAKMEFL EDKFVYDCAG YIFTHSSLNV QLKRFLVEEG ENKNV // ID Q81F41_BACCR Unreviewed; 419 AA. AC Q81F41; DT 01-JUN-2003, integrated into UniProtKB/TrEMBL. DT 01-JUN-2003, sequence version 1. DT 07-JUN-2017, entry version 97. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=BC_1761 {ECO:0000313|EMBL:AAP08737.1}; OS Bacillus cereus (strain ATCC 14579 / DSM 31 / JCM 2152 / NBRC 15305 / OS NCIMB 9373 / NRRL B-3711). OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=226900 {ECO:0000313|EMBL:AAP08737.1, ECO:0000313|Proteomes:UP000001417}; RN [1] {ECO:0000313|EMBL:AAP08737.1, ECO:0000313|Proteomes:UP000001417} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 14579 / DSM 31 / JCM 2152 / NBRC 15305 / NCIMB 9373 / NRRL RC B-3711 {ECO:0000313|Proteomes:UP000001417}; RX PubMed=12721630; DOI=10.1038/nature01582; RA Ivanova N., Sorokin A., Anderson I., Galleron N., Candelon B., RA Kapatral V., Bhattacharyya A., Reznik G., Mikhailova N., Lapidus A., RA Chu L., Mazur M., Goltsman E., Larsen N., D'Souza M., Walunas T., RA Grechkin Y., Pusch G., Haselkorn R., Fonstein M., Ehrlich S.D., RA Overbeek R., Kyrpides N.; RT "Genome sequence of Bacillus cereus and comparative analysis with RT Bacillus anthracis."; RL Nature 423:87-91(2003). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE016877; AAP08737.1; -; Genomic_DNA. DR RefSeq; NP_831536.1; NC_004722.1. DR RefSeq; WP_000393283.1; NC_004722.1. DR ProteinModelPortal; Q81F41; -. DR STRING; 226900.BC1761; -. DR EnsemblBacteria; AAP08737; AAP08737; BC_1761. DR GeneID; 1204110; -. DR KEGG; bce:BC1761; -. DR PATRIC; fig|226900.8.peg.1750; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR KO; K03665; -. DR OMA; FNNHAHV; -. DR Proteomes; UP000001417; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000001417}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000001417}. FT DOMAIN 198 366 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 157 191 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 419 AA; 47724 MW; 9AED3B34C17A70A3 CRC64; MEEVLQRAVL VGVNVGNEDD FAYSMEELTN LAEACDVEVI GQVTQNLQRV NPSHYIGKGK IEEVAAYVQE IDANMVIFND ELSPSQIRNL EEDLDCKVID RTILILDIFA QRAKTKEAQL QVEVAHLQYM MPRLIGLRES LGRQSGGVGT KNKGVGEKKL ELDRRKIEEQ ISVLNKDLEA LVAQRQTQRK QRKKNEIPVV ALVGYTNAGK STTMNAMLEI YNGTEEKQVF EKDMLFATLE TSVRNIDLPD NKSFLLTDTV GFVSKLPHHL VKAFRSTLEE VAEADLLIHV VDYANPNYEQ LIDITNETLK KIGVENIPTI YAYNKSDMVD VEIPKVQEDR VYLSAKKHVG IEELVEMIRS HIYKEYTKCE MLIPYDQGQV VSYFNNHAHV LSTSYENEGT KLQIECKTSD YEKYKHFAI // ID Q81S48_BACAN Unreviewed; 419 AA. AC Q81S48; E9R9U3; E9R9U4; Q6I0C7; Q6KU98; DT 01-JUN-2003, integrated into UniProtKB/TrEMBL. DT 01-JUN-2003, sequence version 1. DT 30-AUG-2017, entry version 126. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=ynbA {ECO:0000313|EMBL:BAR77434.1}; GN Synonyms=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=GBAA_1828 {ECO:0000313|EMBL:AAT30941.1}; GN ORFNames=BASH2_04027 {ECO:0000313|EMBL:BAR77434.1}; OS Bacillus anthracis. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=1392 {ECO:0000313|EMBL:AAT30941.1, ECO:0000313|Proteomes:UP000000594}; RN [1] {ECO:0000313|EMBL:AAT30941.1, ECO:0000313|Proteomes:UP000000594} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Ames Ancestor {ECO:0000313|EMBL:AAT30941.1}, and RC Ames ancestor {ECO:0000313|Proteomes:UP000000594}; RX PubMed=18952800; DOI=10.1128/JB.01347-08; RA Ravel J., Jiang L., Stanley S.T., Wilson M.R., Decker R.S., Read T.D., RA Worsham P., Keim P.S., Salzberg S.L., Fraser-Liggett C.M., Rasko D.A.; RT "The complete genome sequence of Bacillus anthracis Ames 'Ancestor'."; RL J. Bacteriol. 191:445-446(2009). RN [2] {ECO:0000313|EMBL:BAR77434.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=Shikan-NIID {ECO:0000313|EMBL:BAR77434.1}; RA Okutani A., Morikawa S., Inoue S.; RT "Bacillus anthracis whole genome sequence."; RL Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE017334; AAT30941.1; -; Genomic_DNA. DR EMBL; AP014833; BAR77434.1; -; Genomic_DNA. DR RefSeq; WP_000391894.1; NZ_MVKJ01000002.1. DR IntAct; Q81S48; 2. DR STRING; 260799.BAS1693; -. DR DNASU; 1086704; -. DR EnsemblBacteria; AAT30941; AAT30941; GBAA_1828. DR EnsemblBacteria; ANH86069; ANH86069; A8C77_09170. DR KEGG; banh:HYU01_09175; -. DR KEGG; bar:GBAA_1828; -. DR PATRIC; fig|1392.230.peg.1786; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR Proteomes; UP000000594; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000000594}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000000594}. FT DOMAIN 198 366 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 157 191 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 419 AA; 47541 MW; 60798BF371BF4E5A CRC64; MEELLQRAVL VGVNLGNEDD SAYSMEELTN LAEACDVEVI GQVTQNLQRV NPSHYIGKGK IEEVAAYVNE VDANMVIFND ELSPSQIRNL EADLDCKVID RTILILDIFA QRAKTKEAQL QVEVAHLQYM MPRLIGLRES LGRQSGGVGT KNKGVGEKKL ELDRRKIEEQ ISVLNKDLEA LVAQRQTQRK QRKKNEIPVV ALVGYTNAGK STTMNAMLEI YNGTEEKQVF EKDMLFATLE TSVRNIDLPG NKSFLLTDTV GFVSKLPHHL VKAFRSTLEE VAEADLLIHV VDYANPNYEQ LIDITNETLK KIGVENIPTI YAYNKSDMVD VEIPKVQEDR VYLSAKKHVG IEELVEMIRS HIYKEYTKCE MLIPYDQGQV VSYFNTHAHV LSTSYENEGT KLEVECKTSD YEKYKRFAI // ID Q82KD3_STRAW Unreviewed; 497 AA. AC Q82KD3; DT 01-JUN-2003, integrated into UniProtKB/TrEMBL. DT 01-JUN-2003, sequence version 1. DT 07-JUN-2017, entry version 106. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=SAVERM_2470 {ECO:0000313|EMBL:BAC70181.1}; OS Streptomyces avermitilis (strain ATCC 31267 / DSM 46492 / JCM 5070 / OS NBRC 14893 / NCIMB 12804 / NRRL 8165 / MA-4680). OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae; OC Streptomyces. OX NCBI_TaxID=227882 {ECO:0000313|EMBL:BAC70181.1, ECO:0000313|Proteomes:UP000000428}; RN [1] {ECO:0000313|EMBL:BAC70181.1, ECO:0000313|Proteomes:UP000000428} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 31267 / DSM 46492 / JCM 5070 / NBRC 14893 / NCIMB 12804 / RC NRRL 8165 / MA-4680 {ECO:0000313|Proteomes:UP000000428}; RX PubMed=11572948; DOI=10.1073/pnas.211433198; RA Omura S., Ikeda H., Ishikawa J., Hanamoto A., Takahashi C., RA Shinose M., Takahashi Y., Horikawa H., Nakazawa H., Osonoe T., RA Kikuchi H., Shiba T., Sakaki Y., Hattori M.; RT "Genome sequence of an industrial microorganism Streptomyces RT avermitilis: deducing the ability of producing secondary RT metabolites."; RL Proc. Natl. Acad. Sci. U.S.A. 98:12215-12220(2001). RN [2] {ECO:0000313|EMBL:BAC70181.1, ECO:0000313|Proteomes:UP000000428} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 31267 / DSM 46492 / JCM 5070 / NBRC 14893 / NCIMB 12804 / RC NRRL 8165 / MA-4680 {ECO:0000313|Proteomes:UP000000428}; RX PubMed=12692562; DOI=10.1038/nbt820; RA Ikeda H., Ishikawa J., Hanamoto A., Shinose M., Kikuchi H., Shiba T., RA Sakaki Y., Hattori M., Omura S.; RT "Complete genome sequence and comparative analysis of the industrial RT microorganism Streptomyces avermitilis."; RL Nat. Biotechnol. 21:526-531(2003). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BA000030; BAC70181.1; -; Genomic_DNA. DR RefSeq; WP_010983907.1; NZ_JZJK01000086.1. DR ProteinModelPortal; Q82KD3; -. DR STRING; 227882.SAV_2470; -. DR EnsemblBacteria; BAC70181; BAC70181; SAVERM_2470. DR KEGG; sma:SAV_2470; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000000428; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 2. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000000428}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000000428}. FT DOMAIN 275 440 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 497 AA; 54166 MW; 72E83A3B4F6C1CE9 CRC64; MTSSSSPSQD AQSFAHTYPE GLRADALMEE DVAWSQEIDG DRDGDQFDRS ERAALRRVAG LSTELEDVTE VEYRQLRLER VVLVGVWTSG TIQDSENSLA ELAALAETAG ALVLDGVVQR RDKPDAATYI GSGKANELRD IVLETGADTV ICDGELSPGQ LIHLEDVVKV KVIDRTALIL DIFAQHAKSR EGKAQVALAQ MQYMLPRLRG WGQSLSRQMG GGKGGGLATR GPGETKIETD RRRIREKMAK MRREIADMKT GREIKRQERR RNKVPSVAIA GYTNAGKSSL LNRLTGAGVL VENALFATLD PTVRRAETPS GRLYTLADTV GFVRHLPHHL VEAFRSTMEE VGDSDLILHV VDGSHPVPEE QLAAVREVIR DVGATGVPEI VVINKADAAD PLVLQRLMRN EKRSIAVSAR TGQGIAELLA LIDNELPRPS VEIEALVPYT HGKLVARAHT EGEVISEEHT PEGTLLKARV HEELAADLAP YVPAPLA // ID Q82V24_NITEU Unreviewed; 396 AA. AC Q82V24; DT 01-JUN-2003, integrated into UniProtKB/TrEMBL. DT 01-JUN-2003, sequence version 1. DT 07-JUN-2017, entry version 110. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=NE1286 {ECO:0000313|EMBL:CAD85197.1}; OS Nitrosomonas europaea (strain ATCC 19718 / CIP 103999 / KCTC 2705 / OS NBRC 14298). OC Bacteria; Proteobacteria; Betaproteobacteria; Nitrosomonadales; OC Nitrosomonadaceae; Nitrosomonas. OX NCBI_TaxID=228410 {ECO:0000313|EMBL:CAD85197.1, ECO:0000313|Proteomes:UP000001416}; RN [1] {ECO:0000313|EMBL:CAD85197.1, ECO:0000313|Proteomes:UP000001416} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 19718 / CIP 103999 / KCTC 2705 / NBRC 14298 RC {ECO:0000313|Proteomes:UP000001416}; RX PubMed=12700255; DOI=10.1128/JB.185.9.2759-2773.2003; RA Chain P., Lamerdin J., Larimer F., Regala W., Land M., Hauser L., RA Hooper A., Klotz M., Norton J., Sayavedra-Soto L., Arciero D., RA Hommes N., Whittaker M., Arp D.; RT "Complete genome sequence of the ammonia-oxidizing bacterium and RT obligate chemolithoautotroph Nitrosomonas europaea."; RL J. Bacteriol. 185:2759-2773(2003). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AL954747; CAD85197.1; -; Genomic_DNA. DR RefSeq; WP_011111864.1; NC_004757.1. DR ProteinModelPortal; Q82V24; -. DR STRING; 228410.NE1286; -. DR DNASU; 1082230; -. DR EnsemblBacteria; CAD85197; CAD85197; NE1286. DR KEGG; neu:NE1286; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; FNNHAHV; -. DR OrthoDB; POG091H0464; -. DR PhylomeDB; Q82V24; -. DR Proteomes; UP000001416; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000001416}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000001416}. FT DOMAIN 201 376 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 167 197 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 396 AA; 44410 MW; 516F160A47252409 CRC64; MSHDVATGTV ADNTAILVDI DFGEGDKESL EELRELARSD RLSVVAVVEG TRKQPDPATF IGKGKAEEIS QILAQTHAAM VIFNHELSPV QQRNLSMVLA CRIIDRTSLI LDIFAQRAKS HEGKLQVELA QLEYLSTRLV RGWTHLERQK GGIGLRGPGE TQLETDRRLL AKRVKLLKEK LTKLKRQREV RRRARKRAEI LSVSIVGYTN AGKSTLFNRL VRTDTYAADK LFATLDTTTR RLTLPGRGTI VISDTVGFIR ELPHTLVAAF RATLEETIQA DLLLHVVDAS SSNRDAQISE VNKLLREIGA DTIPQILILN KIDLLEQYPS GNYMRDEYGR IKSIHLSART GAGFSYLYDA LAEVFDQNLK RLEQHSATPE SMNDNVRATF INNEKD // ID Q832Q8_ENTFA Unreviewed; 413 AA. AC Q832Q8; DT 01-JUN-2003, integrated into UniProtKB/TrEMBL. DT 01-JUN-2003, sequence version 1. DT 07-JUN-2017, entry version 94. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=EF_2161 {ECO:0000313|EMBL:AAO81893.1}; OS Enterococcus faecalis (strain ATCC 700802 / V583). OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Enterococcaceae; OC Enterococcus. OX NCBI_TaxID=226185 {ECO:0000313|EMBL:AAO81893.1, ECO:0000313|Proteomes:UP000001415}; RN [1] {ECO:0000313|EMBL:AAO81893.1, ECO:0000313|Proteomes:UP000001415} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700802 / V583 {ECO:0000313|Proteomes:UP000001415}; RX PubMed=12663927; DOI=10.1126/science.1080613; RA Paulsen I., Banerjei L., Myers G.S.A., Nelson K.E., Seshadri R., RA Read T.D., Fouts D.E., Eisen J.A., Gill S.R., Heidelberg J.F., RA Tettelin H., Dodson R.J., Umayam L., Brinkac L., Beanan M., RA Daugherty S., DeBoy R.T., Durkin S., Kolonay J., Madupu R., Nelson W., RA Vamathevan J., Tran B., Upton J., Hansen T., Shetty J., Khouri H., RA Utterback T., Radune D., Ketchum K.A., Dougherty B.A., Fraser C.M.; RT "Role of mobile DNA in the evolution of vancomycin-resistant RT Enterococcus faecalis."; RL Science 299:2071-2074(2003). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE016830; AAO81893.1; -; Genomic_DNA. DR RefSeq; NP_815823.1; NC_004668.1. DR RefSeq; WP_002379600.1; NZ_KE136528.1. DR ProteinModelPortal; Q832Q8; -. DR STRING; 226185.EF2161; -. DR EnsemblBacteria; AAO81893; AAO81893; EF_2161. DR GeneID; 1201037; -. DR KEGG; efa:EF2161; -. DR PATRIC; fig|226185.45.peg.1367; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR KO; K03665; -. DR OMA; HPATYIG; -. DR Proteomes; UP000001415; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000001415}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000001415}. FT DOMAIN 196 354 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 413 AA; 47021 MW; 37464CC3DA31BEEB CRC64; MTTHEKVILV GVETEKNYQT FSASMEELAN LTETANGEVV FVLTQKRPQV DRQTVIGKGK LEELIQLTDA YEADLVIFNH ELTPRQNQLL SEALAVRVID RVQLILDIFA LRARSKEGKL QVELAQLDYL LPRLAGQGKQ LSRLGGGIGT RGPGETKLES DRRHIRNKIL GIRRELKEVT AHRERSRQKR QNSELFQIGL IGYTNAGKST ILNMLTTAGT YSEDQLFATL DPLTKKWQLP QGMEVTLTDT VGFIQDLPTQ LIEAFQSTLE ESRTMDLLLH VVDASAPDRL QHERTVQTLM KELALENIPC LTVYNKRDQV DSKEFVPTLF PNVLISTKIS EDKERLVQAI RAQMMELLEP YQLEISPTDG QLLSELRRMT LMISEEYAEN ENRYIVKGFA KKKSKWLAES EKE // ID Q83CV3_COXBU Unreviewed; 454 AA. AC Q83CV3; DT 01-JUN-2003, integrated into UniProtKB/TrEMBL. DT 04-NOV-2008, sequence version 2. DT 05-JUL-2017, entry version 110. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:AAO90520.2}; GN OrderedLocusNames=CBU_0999 {ECO:0000313|EMBL:AAO90520.2}; OS Coxiella burnetii (strain RSA 493 / Nine Mile phase I). OC Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales; OC Coxiellaceae; Coxiella. OX NCBI_TaxID=227377 {ECO:0000313|EMBL:AAO90520.2, ECO:0000313|Proteomes:UP000002671}; RN [1] {ECO:0000313|EMBL:AAO90520.2, ECO:0000313|Proteomes:UP000002671} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=RSA 493 / Nine Mile phase I RC {ECO:0000313|Proteomes:UP000002671}; RX PubMed=12704232; DOI=10.1073/pnas.0931379100; RA Seshadri R., Paulsen I.T., Eisen J.A., Read T.D., Nelson K.E., RA Nelson W.C., Ward N.L., Tettelin H., Davidsen T.M., Beanan M.J., RA Deboy R.T., Daugherty S.C., Brinkac L.M., Madupu R., Dodson R.J., RA Khouri H.M., Lee K.H., Carty H.A., Scanlan D., Heinzen R.A., RA Thompson H.A., Samuel J.E., Fraser C.M., Heidelberg J.F.; RT "Complete genome sequence of the Q-fever pathogen, Coxiella RT burnetii."; RL Proc. Natl. Acad. Sci. U.S.A. 100:5455-5460(2003). RN [2] {ECO:0000313|EMBL:AAO90520.2, ECO:0000313|Proteomes:UP000002671} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=RSA 493 / Nine Mile phase I RC {ECO:0000313|Proteomes:UP000002671}; RX PubMed=19047403; DOI=10.1128/IAI.01141-08; RA Beare P.A., Unsworth N., Andoh M., Voth D.E., Omsland A., Gilk S.D., RA Williams K.P., Sobral B.W., Kupko J.J.III., Porcella S.F., RA Samuel J.E., Heinzen R.A.; RT "Comparative genomics reveal extensive transposon-mediated genomic RT plasticity and diversity among potential effector proteins within the RT genus Coxiella."; RL Infect. Immun. 77:642-656(2009). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE016828; AAO90520.2; -; Genomic_DNA. DR RefSeq; NP_820006.2; NC_002971.3. DR RefSeq; WP_010957944.1; NC_002971.4. DR ProteinModelPortal; Q83CV3; -. DR STRING; 227377.CBU_0999; -. DR PRIDE; Q83CV3; -. DR EnsemblBacteria; AAO90520; AAO90520; CBU_0999. DR GeneID; 1208895; -. DR KEGG; cbu:CBU_0999; -. DR PATRIC; fig|227377.7.peg.992; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR Proteomes; UP000002671; Chromosome. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0043022; F:ribosome binding; IBA:GO_Central. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000002671}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000002671}. FT DOMAIN 204 371 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 454 AA; 51583 MW; EE0164CBE89E9B48 CRC64; MRQTRRYFID RHEGGERIIL VHIDFPTTQP DSLSEFKELA HSSGGDVLTV VKGKRNQPES KYFVGTGKAE EIQQTVHDFN ADLVLFNHEL SPAQERNLEK LFQCRVLDRT GLILDIFAQR AHTFEGKLQV ELAQLKHLST RLVRGWGHLE RQRGGIGLRG PGETQLETDR RLIGGRIKMI NKRLDKVVRQ RQQGQRARKR SAVPTVSLVG YTNAGKSTLF NAITEANVYT ADQLFATLDP TFRQLELPTL GKIILVDTVG FIRDLPHDLI AAFRATLEES RQADLLLHVV DAHSPDSSVM LEEVQKVLET IGAEEVPQLF IYNKIDLLES RKPRIDYDEK GKPRRVWLSA LTGVGIDLLN PAIVELLGDT ILTCEVTLEA NEGKLRSTLY KMGVIKAEKI DPEGHIQLTL EIQRKDYQRL FEYRARPVAC AKRSQRRTRD VLRVPAAKPR DDQI // ID Q87L08_VIBPA Unreviewed; 429 AA. AC Q87L08; DT 01-JUN-2003, integrated into UniProtKB/TrEMBL. DT 01-JUN-2003, sequence version 1. DT 30-AUG-2017, entry version 90. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=VP2816 {ECO:0000313|EMBL:BAC61079.1}; OS Vibrio parahaemolyticus serotype O3:K6 (strain RIMD 2210633). OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; OC Vibrionaceae; Vibrio. OX NCBI_TaxID=223926 {ECO:0000313|EMBL:BAC61079.1, ECO:0000313|Proteomes:UP000002493}; RN [1] {ECO:0000313|EMBL:BAC61079.1, ECO:0000313|Proteomes:UP000002493} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=RIMD 2210633 {ECO:0000313|Proteomes:UP000002493}; RX PubMed=12620739; DOI=10.1016/S0140-6736(03)12659-1; RA Makino K., Oshima K., Kurokawa K., Yokoyama K., Uda T., Tagomori K., RA Iijima Y., Najima M., Nakano M., Yamashita A., Kubota Y., Kimura S., RA Yasunaga T., Honda T., Shinagawa H., Hattori M., Iida T.; RT "Genome sequence of Vibrio parahaemolyticus: a pathogenic mechanism RT distinct from that of V. cholerae."; RL Lancet 361:743-749(2003). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BA000031; BAC61079.1; -; Genomic_DNA. DR RefSeq; NP_799195.1; NC_004603.1. DR RefSeq; WP_005480048.1; NC_004603.1. DR ProteinModelPortal; Q87L08; -. DR STRING; 223926.VP2816; -. DR EnsemblBacteria; BAC61079; BAC61079; BAC61079. DR GeneID; 1190366; -. DR KEGG; vpa:VP2816; -. DR PATRIC; fig|223926.6.peg.2707; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR Proteomes; UP000002493; Chromosome 1. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000002493}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000002493}. FT DOMAIN 198 365 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 429 AA; 48843 MW; 9710CE37FE0A5AD6 CRC64; MFDRYESGER AVLVHINFTQ EGEWEDLAEF EMLVSSAGVE TLQVVTGSRQ SPHPKYYVGE GKAQEIATTV HLTGAEIVIF NHSLSPAQER NLEALCKCRV LDRTGLILDI FAQRARTHEG KLQVELAQLR HISTRLIRGW THLERQKGGI GLRGPGETQL ETDRRLLRER IKAILRRLEK VAKQREQGRR ARNRAEIPTI SLVGYTNAGK STLFNRITEA GVYAADQLFA TLDPTLRKME LADVGPAILA DTVGFIRHLP HDLVAAFKAT LQETQEADIL LHVVDASDER FRENIQAVHE VLEEIDAHEV PTLVVMNKID NLESQTPRIE RDEEGVPRAV WVSAMEGLGI ELLFDALTER LASQMVEHQL RIPPQYQGRF RSTFFQMKCI QREEYDQDGN LLIDIRMQQV DWSRLEKREG AVLTDFIVT // ID Q87VJ5_PSESM Unreviewed; 433 AA. AC Q87VJ5; DT 01-JUN-2003, integrated into UniProtKB/TrEMBL. DT 01-JUN-2003, sequence version 1. DT 30-AUG-2017, entry version 102. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:AAO58369.1}; GN OrderedLocusNames=PSPTO_4941 {ECO:0000313|EMBL:AAO58369.1}; OS Pseudomonas syringae pv. tomato (strain ATCC BAA-871 / DC3000). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=223283 {ECO:0000313|EMBL:AAO58369.1, ECO:0000313|Proteomes:UP000002515}; RN [1] {ECO:0000313|EMBL:AAO58369.1, ECO:0000313|Proteomes:UP000002515} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-871 / DC3000 {ECO:0000313|Proteomes:UP000002515}; RX PubMed=12928499; DOI=10.1073/pnas.1731982100; RA Buell C.R., Joardar V., Lindeberg M., Selengut J., Paulsen I.T., RA Gwinn M.L., Dodson R.J., Deboy R.T., Durkin A.S., Kolonay J.F., RA Madupu R., Daugherty S., Brinkac L., Beanan M.J., Haft D.H., RA Nelson W.C., Davidsen T., Zafar N., Zhou L., Liu J., Yuan Q., RA Khouri H., Fedorova N., Tran B., Russell D., Berry K., Utterback T., RA Van Aken S.E., Feldblyum T.V., D'Ascenzo M., Deng W.L., Ramos A.R., RA Alfano J.R., Cartinhour S., Chatterjee A.K., Delaney T.P., RA Lazarowitz S.G., Martin G.B., Schneider D.J., Tang X., Bender C.L., RA White O., Fraser C.M., Collmer A.; RT "The complete genome sequence of the Arabidopsis and tomato pathogen RT Pseudomonas syringae pv. tomato DC3000."; RL Proc. Natl. Acad. Sci. U.S.A. 100:10181-10186(2003). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE016853; AAO58369.1; -; Genomic_DNA. DR RefSeq; NP_794674.1; NC_004578.1. DR RefSeq; WP_005736856.1; NC_004578.1. DR ProteinModelPortal; Q87VJ5; -. DR STRING; 223283.PSPTO_4941; -. DR EnsemblBacteria; AAO58369; AAO58369; PSPTO_4941. DR GeneID; 1186626; -. DR KEGG; pst:PSPTO_4941; -. DR PATRIC; fig|223283.9.peg.5055; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR PhylomeDB; Q87VJ5; -. DR Proteomes; UP000002515; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; ISS:JCVI. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000002515}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000002515}. FT DOMAIN 199 366 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 433 AA; 48711 MW; F273A228C37087E7 CRC64; MFFERHSGGE RAILVHLDGQ DPEAREDPQE FQELAISAGA DTVAFINVPR HRPSAKYLIG SGKVEELRDQ VKAEQADLVI FNHTLTPSQE RNLERVFECR VLDRTGLILD IFAQRARTHE GKLQVELAQL EHMSTRLVRG WTHLERQKGG IGLRGPGETQ LETDRRLLRV RLRQIKGRLE KVRSQRDQAR RGRRRADIPS VSLVGYTNAG KSTLFNSVTD SDVFAADQLF ATLDPTLRRL QLNDLGPIVL ADTVGFIRHL PHKLVEAFRA TLEESSNSDL LLHVIDSHEP DRMSQIEQVM AVLGEIGAEG LPILEVYNKL DLLEGVEPQI QRDADGKPQR VWVSARDGRG LDLLKQAIAE LLGDDLFVGT LLLPQSLARL RAQFFELGAV QSETHDEDGA SVLAVRLPRV ELNRLVSREG LQPLEFIEQH TLQ // ID Q88DD4_PSEPK Unreviewed; 433 AA. AC Q88DD4; DT 01-JUN-2003, integrated into UniProtKB/TrEMBL. DT 01-JUN-2003, sequence version 1. DT 30-AUG-2017, entry version 92. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:AAN70460.1}; GN OrderedLocusNames=PP_4893 {ECO:0000313|EMBL:AAN70460.1}; OS Pseudomonas putida (strain ATCC 47054 / DSM 6125 / NCIMB 11950 / OS KT2440). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=160488 {ECO:0000313|EMBL:AAN70460.1, ECO:0000313|Proteomes:UP000000556}; RN [1] {ECO:0000313|EMBL:AAN70460.1, ECO:0000313|Proteomes:UP000000556} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 47054 / DSM 6125 / NCIMB 11950 / KT2440 RC {ECO:0000313|Proteomes:UP000000556}; RX PubMed=12534463; DOI=10.1046/j.1462-2920.2002.00366.x; RA Nelson K.E., Weinel C., Paulsen I.T., Dodson R.J., Hilbert H., RA Martins dos Santos V.A., Fouts D.E., Gill S.R., Pop M., Holmes M., RA Brinkac L., Beanan M., DeBoy R.T., Daugherty S., Kolonay J., RA Madupu R., Nelson W., White O., Peterson J., Khouri H., Hance I., RA Chris Lee P., Holtzapple E., Scanlan D., Tran K., Moazzez A., RA Utterback T., Rizzo M., Lee K., Kosack D., Moestl D., Wedler H., RA Lauber J., Stjepandic D., Hoheisel J., Straetz M., Heim S., RA Kiewitz C., Eisen J.A., Timmis K.N., Dusterhoft A., Tummler B., RA Fraser C.M.; RT "Complete genome sequence and comparative analysis of the RT metabolically versatile Pseudomonas putida KT2440."; RL Environ. Microbiol. 4:799-808(2002). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE015451; AAN70460.1; -; Genomic_DNA. DR RefSeq; NP_746996.1; NC_002947.4. DR RefSeq; WP_003249534.1; NC_002947.4. DR ProteinModelPortal; Q88DD4; -. DR STRING; 160488.PP_4893; -. DR EnsemblBacteria; AAN70460; AAN70460; PP_4893. DR GeneID; 1044733; -. DR KEGG; ppu:PP_4893; -. DR PATRIC; fig|160488.4.peg.5228; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR Proteomes; UP000000556; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000000556}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Hydrolase {ECO:0000313|EMBL:AAN70460.1}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000000556}. FT DOMAIN 199 366 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 165 192 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 433 AA; 48883 MW; 9113BA5396E80CE0 CRC64; MFFERHGGGE RALLVHLEGQ NPEAREDPQE FQELALSAGA DIVSLVTVTR HQPSAKYLIG SGKVEELHDL VHAEQVDLVI FNHTLTPSQE RNLERVFECR VLDRTGLILD IFAQRARTHE GKLQVELAQL EHMSTRLVRG WTHLERQKGG IGLRGPGETQ LETDRRLLRV RIRQIKSRLE KVRSQREQAR RGRKRADIPS VSLVGYTNAG KSTLFNALTE SEVYAADQLF ATLDPTLRRL ELNDLGPIVL ADTVGFIRHL PHKLVEAFRA TLEESSNSDL LLHVIDAHEP ERMEQIEQVL AVLGEIGAEG LPILEVYNKL DLLEDVEPQI QRNADGKPER VWVSARDGRG LELVGQAVAE LLGDDLFVGT LCLEQRFARL RAQFFALGAV QSEEHDEEGR SLLSVRLPMV ELNRLVSREG MEPQVFVQQH TLQ // ID Q891Y6_CLOTE Unreviewed; 593 AA. AC Q891Y6; DT 01-JUN-2003, integrated into UniProtKB/TrEMBL. DT 01-JUN-2003, sequence version 1. DT 07-JUN-2017, entry version 109. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:AAO36709.1}; GN OrderedLocusNames=CTC_02227 {ECO:0000313|EMBL:AAO36709.1}; OS Clostridium tetani (strain Massachusetts / E88). OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=212717 {ECO:0000313|EMBL:AAO36709.1, ECO:0000313|Proteomes:UP000001412}; RN [1] {ECO:0000313|EMBL:AAO36709.1, ECO:0000313|Proteomes:UP000001412} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Massachusetts / E88 {ECO:0000313|Proteomes:UP000001412}; RX PubMed=12552129; DOI=10.1073/pnas.0335853100; RA Brueggemann H., Baumer S., Fricke W.F., Wiezer A., Liesegang H., RA Decker I., Herzberg C., Martinez-Arias R., Merkl R., Henne A., RA Gottschalk G.; RT "The genome sequence of Clostridium tetani, the causative agent of RT tetanus disease."; RL Proc. Natl. Acad. Sci. U.S.A. 100:1316-1321(2003). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE015927; AAO36709.1; -; Genomic_DNA. DR RefSeq; WP_011100370.1; NC_004557.1. DR ProteinModelPortal; Q891Y6; -. DR STRING; 212717.CTC02227; -. DR EnsemblBacteria; AAO36709; AAO36709; CTC_02227. DR GeneID; 24254473; -. DR KEGG; ctc:CTC_02227; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000001412; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000001412}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000001412}. FT DOMAIN 362 539 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 593 AA; 67215 MW; 47406158EAC64946 CRC64; MIYGNTNGVR DTVLEKLEEI YIMKIAKDEI CSRELISVLA YFTELIGREI SVAINRRGTV ESVTLGDSST VELPILEIKQ KKLSGIRIVH THPSGNSTLS SLDLSALLKL KLDCIVAIGV LEGEAKEITV GFCDIENDLL KWDSTKKLSV DEFLSMNILE KLDYIEDIIK GSKVEEDYGE KAIIVGIENE ESLEELAELA RACEVSVLGR IFQKRSKMDP ALYIGSGKVS EVGYLAQKTR ANVIIFDDEL SGSQLRNLEK YLGIKVIDRT TLILEIFSKR AKSREGKIQV ELAQLKYRLP RLIGMGAVLS RTGGGIGTRG PGEQKLETDR RHIKNRIYDL SKELEKIKKI RKTQRASRNE VPKVSLVGYT NSGKSTLRNY MYNLFQSKEL SKKDNVLEAD MLFATLDTTT RAIYLPDNRD ITLTDTVGFI RKLPHDLVES FKSTLEEVMD ADLLLHVVDI SSIHYLEQIE AVNNVLRELN ALNKPSIILI NKIDKINEDE LETKLENLKN YKYVCISAKE GINIDVLLKE IINKLPNKLK KAEYLIPYNK QDVVAYLHRN AKVHEENYKD NGTYVRAEVD DLVYNVCNEY MIK // ID Q89LQ1_BRADU Unreviewed; 437 AA. AC Q89LQ1; DT 01-JUN-2003, integrated into UniProtKB/TrEMBL. DT 01-JUN-2003, sequence version 1. DT 05-JUL-2017, entry version 97. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflx {ECO:0000313|EMBL:BAC49757.1}; GN Synonyms=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; OS Bradyrhizobium diazoefficiens (strain JCM 10833 / IAM 13628 / NBRC OS 14792 / USDA 110). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Bradyrhizobiaceae; Bradyrhizobium. OX NCBI_TaxID=224911 {ECO:0000313|EMBL:BAC49757.1, ECO:0000313|Proteomes:UP000002526}; RN [1] {ECO:0000313|Proteomes:UP000002526} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=JCM 10833 / IAM 13628 / NBRC 14792 / USDA 110 RC {ECO:0000313|Proteomes:UP000002526}; RX PubMed=12597275; DOI=10.1093/dnares/9.6.189; RA Kaneko T., Nakamura Y., Sato S., Minamisawa K., Uchiumi T., RA Sasamoto S., Watanabe A., Idesawa K., Iriguchi M., Kawashima K., RA Kohara M., Matsumoto M., Shimpo S., Tsuruoka H., Wada T., Yamada M., RA Tabata S.; RT "Complete genomic sequence of nitrogen-fixing symbiotic bacterium RT Bradyrhizobium japonicum USDA110."; RL DNA Res. 9:189-197(2002). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BA000040; BAC49757.1; -; Genomic_DNA. DR RefSeq; NP_771132.1; NC_004463.1. DR RefSeq; WP_011087263.1; NZ_CP011360.1. DR ProteinModelPortal; Q89LQ1; -. DR STRING; 224911.blr4492; -. DR EnsemblBacteria; BAC49757; BAC49757; BAC49757. DR GeneID; 1052644; -. DR KEGG; bja:blr4492; -. DR PATRIC; fig|224911.5.peg.4547; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR InParanoid; Q89LQ1; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR PhylomeDB; Q89LQ1; -. DR Proteomes; UP000002526; Chromosome. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0043022; F:ribosome binding; IBA:GO_Central. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000002526}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000002526}. FT DOMAIN 203 377 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 437 AA; 48299 MW; EBB8F5E0C3EDAF79 CRC64; MLVIGPYLRV RAGGTDAQSE SHVVRDAEAR LDEAAGLARA IDLIIADAII APISQIRPAT YIGKGKVEEI AALAKSLDVE LVVMDCALAP IQQRNLEKEL HAKVLDRTGL ILEIFGRRAK TKEGSLQVEL AHLNYQRSRL VRSWTHLERQ RGGFGFMGGP GETQIEADRR LIQERISKLE GELKKVQATR RLHRAGRQRV PYRVVALVGY TNAGKSTLFN RLTRADVQAA DMLFATLDPT LRALTLPHGG KAMLSDTVGF ISNLPTQLIA AFRATLEEVL EADVILHVRD ISHEDAEAQQ SDVDAVLRQL GINPDDSGRI IEVWNKIDRY DAEQREELLN IAARRPEDHP AMLVSAVSGE GVDALLAAIE ERLAAKRTTL DLSIDAGDGA GISWLHRNSE VLTKELHDGR FDMTVRVDET KRDIVVNRFD AVPRLSA // ID Q8A5I1_BACTN Unreviewed; 419 AA. AC Q8A5I1; DT 01-JUN-2003, integrated into UniProtKB/TrEMBL. DT 01-JUN-2003, sequence version 1. DT 07-JUN-2017, entry version 103. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=BT_2258 {ECO:0000313|EMBL:AAO77365.1}; OS Bacteroides thetaiotaomicron (strain ATCC 29148 / DSM 2079 / NCTC OS 10582 / E50 / VPI-5482). OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae; OC Bacteroides. OX NCBI_TaxID=226186 {ECO:0000313|EMBL:AAO77365.1, ECO:0000313|Proteomes:UP000001414}; RN [1] {ECO:0000313|EMBL:AAO77365.1, ECO:0000313|Proteomes:UP000001414} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29148 / DSM 2079 / NCTC 10582 / E50 / VPI-5482 RC {ECO:0000313|Proteomes:UP000001414}; RX PubMed=12663928; DOI=10.1126/science.1080029; RA Xu J., Bjursell M.K., Himrod J., Deng S., Carmichael L.K., RA Chiang H.C., Hooper L.V., Gordon J.I.; RT "A genomic view of the human-Bacteroides thetaiotaomicron symbiosis."; RL Science 299:2074-2076(2003). RN [2] {ECO:0000313|EMBL:AAO77365.1, ECO:0000313|Proteomes:UP000001414} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29148 / DSM 2079 / NCTC 10582 / E50 / VPI-5482 RC {ECO:0000313|Proteomes:UP000001414}; RX PubMed=19321416; DOI=10.1073/pnas.0901529106; RA Mahowald M.A., Rey F.E., Seedorf H., Turnbaugh P.J., Fulton R.S., RA Wollam A., Shah N., Wang C., Magrini V., Wilson R.K., Cantarel B.L., RA Coutinho P.M., Henrissat B., Crock L.W., Russell A., Verberkmoes N.C., RA Hettich R.L., Gordon J.I.; RT "Characterizing a model human gut microbiota composed of members of RT its two dominant bacterial phyla."; RL Proc. Natl. Acad. Sci. U.S.A. 106:5859-5864(2009). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE015928; AAO77365.1; -; Genomic_DNA. DR RefSeq; NP_811171.1; NC_004663.1. DR RefSeq; WP_008759581.1; NC_004663.1. DR ProteinModelPortal; Q8A5I1; -. DR STRING; 226186.BT_2258; -. DR PaxDb; Q8A5I1; -. DR DNASU; 1076121; -. DR EnsemblBacteria; AAO77365; AAO77365; BT_2258. DR GeneID; 1076121; -. DR KEGG; bth:BT_2258; -. DR PATRIC; fig|226186.12.peg.2323; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR InParanoid; Q8A5I1; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000001414; Chromosome. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0043022; F:ribosome binding; IBA:GO_Central. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000001414}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000001414}. FT DOMAIN 217 401 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 419 AA; 47841 MW; C5B976789B3373CC CRC64; MKEFIISEAK VETAVLVGLI TQMQDERKTN EYLDELAFLA ETAGAEVVKR FTQKLPTANS VTYVGKGKLE EIRQYIRTEE EEEREVGMVI FDDELSAKQI RNIEAELKVK ILDRTSLILD IFAMRAQTAN AKTQVELAQY KYMLPRLQRL WTHLERQGGG SGSGSGKGGS VGLRGPGETQ LEMDRRIILN RMSLLKERLA EIDKQKATQR KNRGRMIRVA LVGYTNVGKS TIMNLLAKSE VFAENKLFAT LDTTVRKVII DNLPFLLSDT VGFIRKLPTD LVDSFKSTLD EVREADLLVH VVDISHPGFE EQIEVVNKTL ADIGGGGKPM ILIFNKIDAY TYVEKAPDDL TPRTKENLTL EELMKTWMAK MEDNCLFISA RERINIDELK DVVYQRVKEL HVQKYPYNDF LYQTYEEEE // ID Q8DQN2_STRR6 Unreviewed; 412 AA. AC Q8DQN2; DT 01-MAR-2003, integrated into UniProtKB/TrEMBL. DT 01-MAR-2003, sequence version 1. DT 07-JUN-2017, entry version 103. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=spr0589 {ECO:0000313|EMBL:AAK99393.1}; OS Streptococcus pneumoniae (strain ATCC BAA-255 / R6). OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=171101 {ECO:0000313|EMBL:AAK99393.1, ECO:0000313|Proteomes:UP000000586}; RN [1] {ECO:0000313|EMBL:AAK99393.1, ECO:0000313|Proteomes:UP000000586} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-255 / R6 {ECO:0000313|Proteomes:UP000000586}; RX PubMed=11544234; DOI=10.1128/JB.183.19.5709-5717.2001; RA Hoskins J.A., Alborn W.Jr., Arnold J., Blaszczak L., Burgett S., RA DeHoff B.S., Estrem S., Fritz L., Fu D.-J., Fuller W., Geringer C., RA Gilmour R., Glass J.S., Khoja H., Kraft A., LaGace R., LeBlanc D.J., RA Lee L.N., Lefkowitz E.J., Lu J., Matsushima P., McAhren S., RA McHenney M., McLeaster K., Mundy C., Nicas T.I., Norris F.H., RA O'Gara M., Peery R., Robertson G.T., Rockey P., Sun P.-M., RA Winkler M.E., Yang Y., Young-Bellido M., Zhao G., Zook C., Baltz R.H., RA Jaskunas S.Richard., Rosteck P.R.Jr., Skatrud P.L., Glass J.I.; RT "Genome of the bacterium Streptococcus pneumoniae strain R6."; RL J. Bacteriol. 183:5709-5717(2001). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE007317; AAK99393.1; -; Genomic_DNA. DR PIR; E97945; E97945. DR PIR; H95077; H95077. DR RefSeq; NP_358183.1; NC_003098.1. DR RefSeq; WP_000573197.1; NC_003098.1. DR ProteinModelPortal; Q8DQN2; -. DR STRING; 171101.spr0589; -. DR EnsemblBacteria; AAK99393; AAK99393; spr0589. DR GeneID; 933192; -. DR KEGG; spr:spr0589; -. DR PATRIC; fig|171101.6.peg.656; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR Proteomes; UP000000586; Chromosome. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0043022; F:ribosome binding; IBA:GO_Central. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000000586}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000000586}. FT DOMAIN 199 359 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 158 192 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 412 AA; 46712 MW; 06696A5659C212A1 CRC64; MIETEKKEER VLLIGVELQG MDSFDLSMEE LASLAKTAGA VVVDSYRQKR EKYDSKTFVG SGKLEEIALM VDAEEITTVI VNNRLTPRQN VNLEEVLGVK VIDRMQLILD IFAMRARSHE GKLQVHLAQL KYLLPRLVGQ GIMLSRQAGG IGSRGPGESQ LELNRRSVRN QITDIERQLK VVEKNRATVR EKRLESSTFK IGLIGYTNAG KSTIMNILTS KTQYEADELF ATLDATTKSI HLGGNLQVTL TDTVGFIQDL PTELVSSFKS TLEESKHVDL LVHVIDASNP YHEEHEKTVL SIMKDLDMED IPHLTLYNKA DLVEDFTPTQ TPYTLISAKS EDSRENLQAL LLDKIKEIFE AFTLRVPFSK SYKIHDLESV AILEERDYQE DGEVITGYIS EKNKWRLEEF YD // ID Q8DT88_STRMU Unreviewed; 415 AA. AC Q8DT88; DT 01-MAR-2003, integrated into UniProtKB/TrEMBL. DT 01-MAR-2003, sequence version 1. DT 07-JUN-2017, entry version 101. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=SMU_1476c {ECO:0000313|EMBL:AAN59132.1}; OS Streptococcus mutans serotype c (strain ATCC 700610 / UA159). OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=210007 {ECO:0000313|EMBL:AAN59132.1, ECO:0000313|Proteomes:UP000002512}; RN [1] {ECO:0000313|EMBL:AAN59132.1, ECO:0000313|Proteomes:UP000002512} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700610 / UA159 {ECO:0000313|Proteomes:UP000002512}; RX PubMed=12397186; DOI=10.1073/pnas.172501299; RA Ajdic D., McShan W.M., McLaughlin R.E., Savic G., Chang J., RA Carson M.B., Primeaux C., Tian R., Kenton S., Jia H., Lin S., Qian Y., RA Li S., Zhu H., Najar F., Lai H., White J., Roe B.A., Ferretti J.J.; RT "Genome sequence of Streptococcus mutans UA159, a cariogenic dental RT pathogen."; RL Proc. Natl. Acad. Sci. U.S.A. 99:14434-14439(2002). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE014133; AAN59132.1; -; Genomic_DNA. DR RefSeq; NP_721826.1; NC_004350.2. DR RefSeq; WP_002263070.1; NC_004350.2. DR ProteinModelPortal; Q8DT88; -. DR STRING; 210007.SMU_1476c; -. DR DNASU; 1028718; -. DR EnsemblBacteria; AAN59132; AAN59132; SMU_1476c. DR GeneID; 1028718; -. DR KEGG; smu:SMU_1476c; -. DR PATRIC; fig|210007.7.peg.1313; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR KO; K03665; -. DR OMA; HPATYIG; -. DR PhylomeDB; Q8DT88; -. DR Proteomes; UP000002512; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000002512}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000002512}. FT DOMAIN 199 359 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 158 192 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 415 AA; 47328 MW; 4B547AB7DAC507AE CRC64; MIETRQKQER VILIGVALPN SENFDLSMEE LASLAKTAGA EVVQTHTQKR DHYDSKSFIG SGKLLEIKQI IATDAIDSVI VNNRLTPRQN AYLEAELGVK VIDRMQLILD IFAMRARSHE GKLQVHLAQL KYMLPRLVGQ GIMLSRQAGG IGSRGPGESQ LELNRRSIRK QIADIERQLK NAEKNRETNR EKRLDSQIFK IGLIGYTNAG KSTIMNVLTD NKQYEADELF ATLDATTKQI YLTDHFQATL TDTVGFIQDL PTELVAAFKS TLEESRQVDL LLHVIDASDP NHEEHEKVVH DLLKELGMTA IPRLLVYNKM DKAENFIASQ FPHISLSAKS DEAAALLRQS ILEKIKTLFV PFTITWRQEK SYKLYELDKI ALLTSYDVKQ ELQEIKGYIS EKNKWRLEEF YRELS // ID Q8DZ97_STRA5 Unreviewed; 412 AA. AC Q8DZ97; DT 01-MAR-2003, integrated into UniProtKB/TrEMBL. DT 01-MAR-2003, sequence version 1. DT 07-JUN-2017, entry version 97. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:AAN00094.1}; GN OrderedLocusNames=SAG1212 {ECO:0000313|EMBL:AAN00094.1}; OS Streptococcus agalactiae serotype V (strain ATCC BAA-611 / 2603 V/R). OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=208435 {ECO:0000313|EMBL:AAN00094.1, ECO:0000313|Proteomes:UP000000821}; RN [1] {ECO:0000313|EMBL:AAN00094.1, ECO:0000313|Proteomes:UP000000821} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-611 / 2603 V/R {ECO:0000313|Proteomes:UP000000821}; RX PubMed=12200547; DOI=10.1073/pnas.182380799; RA Tettelin H., Masignani V., Cieslewicz M.J., Eisen J.A., Peterson S., RA Wessels M.R., Paulsen I.T., Nelson K.E., Margarit I., Read T.D., RA Madoff L.C., Wolf A.M., Beanan M.J., Brinkac L.M., Daugherty S.C., RA DeBoy R.T., Durkin S., Kolonay J.F., Umayam L.A., Madupu R., RA Lewis M.R., Radune D., Fedorova N.B., Scanlan D., Khouri H., RA Mulligan S., Carty H.A., Cline R.T., Gill J., Scarselli M., Mora M., RA Iacobini E.T., Brettoni C., Galli G., Mariani M., Vegni F., Maione D., RA Rinaudo D., Rappuoli R., Telford J.L., Kasper D.L., Grandi G., RA Fraser C.M.; RT "Complete genome sequence and comparative genomic analysis of an RT emerging human pathogen, serotype V Streptococcus agalactiae."; RL Proc. Natl. Acad. Sci. U.S.A. 99:12391-12396(2002). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE009948; AAN00094.1; -; Genomic_DNA. DR RefSeq; NP_688221.1; NC_004116.1. DR RefSeq; WP_000573348.1; NC_004116.1. DR ProteinModelPortal; Q8DZ97; -. DR EnsemblBacteria; AAN00094; AAN00094; SAG1212. DR GeneID; 1014019; -. DR KEGG; sag:SAG1212; -. DR PATRIC; fig|208435.3.peg.1218; -. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR Proteomes; UP000000821; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000000821}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000000821}. FT DOMAIN 199 359 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 165 192 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 412 AA; 47457 MW; 8558C117951DD483 CRC64; MIETKEEQER VILVGVELQD TENFEMSMEE LASLAKTAGA NVVNHYYQKR DKYDSKSFIG SGKLEEIKAI VEADEIDTVV VNNRLTPRQN SNLEAELGVK VIDRMQLILD IFAMRARSHE GKLQVHLAQL KYMLPRLVGQ GIMLSRQAGG IGSRGPGESQ LELNRRSIRH QISDIERQLK IVEKNRETVR ERRVDSTTFK IGLIGYTNAG KSTIMNVLTD DKQYEANELF ATLDATTKQI YLQNQFQVTL TDTVGFIQDL PTELVAAFKS TLEESRHVDL LFHVIDASDP NHEEHEKVVM EILKDLDMID IPRLAIYNKM DVTEQLNATT FPNVRIAAKK QGSKDLLRRL IVDEIRHIFD EFSIRVHQNQ AYKLYDLNKI ALLDTYTFEE EYENITGYIS PKQKWKLEEF YD // ID Q8EJ68_SHEON Unreviewed; 435 AA. AC Q8EJ68; DT 01-MAR-2003, integrated into UniProtKB/TrEMBL. DT 01-MAR-2003, sequence version 1. DT 30-AUG-2017, entry version 97. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:AAN53682.1}; GN OrderedLocusNames=SO_0604 {ECO:0000313|EMBL:AAN53682.1}; OS Shewanella oneidensis (strain MR-1). OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales; OC Shewanellaceae; Shewanella. OX NCBI_TaxID=211586 {ECO:0000313|EMBL:AAN53682.1, ECO:0000313|Proteomes:UP000008186}; RN [1] {ECO:0000313|EMBL:AAN53682.1, ECO:0000313|Proteomes:UP000008186} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MR-1 {ECO:0000313|EMBL:AAN53682.1, RC ECO:0000313|Proteomes:UP000008186}; RX PubMed=12368813; DOI=10.1038/nbt749; RA Heidelberg J.F., Paulsen I.T., Nelson K.E., Gaidos E.J., Nelson W.C., RA Read T.D., Eisen J.A., Seshadri R., Ward N., Methe B., Clayton R.A., RA Meyer T., Tsapin A., Scott J., Beanan M., Brinkac L., Daugherty S., RA DeBoy R.T., Dodson R.J., Durkin A.S., Haft D.H., Kolonay J.F., RA Madupu R., Peterson J.D., Umayam L.A., White O., Wolf A.M., RA Vamathevan J., Weidman J., Impraim M., Lee K., Berry K., Lee C., RA Mueller J., Khouri H., Gill J., Utterback T.R., McDonald L.A., RA Feldblyum T.V., Smith H.O., Venter J.C., Nealson K.H., Fraser C.M.; RT "Genome sequence of the dissimilatory metal ion-reducing bacterium RT Shewanella oneidensis."; RL Nat. Biotechnol. 20:1118-1123(2002). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE014299; AAN53682.1; -; Genomic_DNA. DR RefSeq; NP_716237.1; NC_004347.2. DR RefSeq; WP_011070935.1; NC_004347.2. DR ProteinModelPortal; Q8EJ68; -. DR STRING; 211586.SO_0604; -. DR PaxDb; Q8EJ68; -. DR DNASU; 1168471; -. DR EnsemblBacteria; AAN53682; AAN53682; SO_0604. DR GeneID; 1168471; -. DR KEGG; son:SO_0604; -. DR PATRIC; fig|211586.12.peg.583; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR PhylomeDB; Q8EJ68; -. DR Proteomes; UP000008186; Chromosome. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0043022; F:ribosome binding; IBA:GO_Central. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000008186}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Hydrolase {ECO:0000313|EMBL:AAN53682.1}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000008186}. FT DOMAIN 198 364 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 164 191 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 435 AA; 49150 MW; AA7BC7930215CC0F CRC64; MFDRYEAGET AVLVHIDFSD EERREDLVEL QLLVESAGAR SVGVITGSRR SPDRKFFIGS GKAEELAALV AATEANVVIF NHALSPAQER NLEQVCQCRV LDRTSLILDI FAQRARTHEG KLQVELAQLR HMSTRLVRGW THLERQKGGI GLRGPGETQL ETDRRLLRGR IKNINKRLER VDKQREQSRR ARKRSDMPTV SLVGYTNAGK STLFNALTSS DVYAADQLFA TLDPTLRKLD LPDGAVILAD TVGFIRHLPH DLVAAFKATL QETRQAELLL HIVDCADENM ADNFEQVQSV LKEIDADEVM QLIVCNKIDL LEDVTPRIEY DDRGKPVRVW VSAHKRLGFD LLLKAITELI GEVIHEFTLR IPATAGHYLG QFYRLDAIQQ KEYDDLGNCI LSVRLSDADW RRLAKQSQGE LETFIFDPSI EKAVC // ID Q8EQP6_OCEIH Unreviewed; 413 AA. AC Q8EQP6; DT 01-MAR-2003, integrated into UniProtKB/TrEMBL. DT 01-MAR-2003, sequence version 1. DT 07-JUN-2017, entry version 98. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=OB1648 {ECO:0000313|EMBL:BAC13604.1}; OS Oceanobacillus iheyensis (strain DSM 14371 / CIP 107618 / JCM 11309 / OS KCTC 3954 / HTE831). OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; OC Oceanobacillus. OX NCBI_TaxID=221109 {ECO:0000313|EMBL:BAC13604.1, ECO:0000313|Proteomes:UP000000822}; RN [1] {ECO:0000313|EMBL:BAC13604.1, ECO:0000313|Proteomes:UP000000822} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 14371 / CIP 107618 / JCM 11309 / KCTC 3954 / HTE831 RC {ECO:0000313|Proteomes:UP000000822}; RX PubMed=12235376; DOI=10.1093/nar/gkf526; RA Takami H., Takaki Y., Uchiyama I.; RT "Genome sequence of Oceanobacillus iheyensis isolated from the Iheya RT Ridge and its unexpected adaptive capabilities to extreme RT environments."; RL Nucleic Acids Res. 30:3927-3935(2002). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BA000028; BAC13604.1; -; Genomic_DNA. DR RefSeq; WP_011066049.1; NC_004193.1. DR ProteinModelPortal; Q8EQP6; -. DR STRING; 221109.OB1648; -. DR EnsemblBacteria; BAC13604; BAC13604; BAC13604. DR KEGG; oih:OB1648; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000000822; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000000822}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Hydrolase {ECO:0000313|EMBL:BAC13604.1}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Protease {ECO:0000313|EMBL:BAC13604.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000822}. FT DOMAIN 196 358 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 413 AA; 47293 MW; 4727F99D01CCFACC CRC64; MTQEKVLVIA VNQTKQDDTR FQSSLHELVS LCKTAGGTVE EVITQKRDRI HPATYMGEGK LQEIREIVED KDIDIVVANN ELAAGQIRNL SDEFGVRVLD RSQLILDIFA MRAQTKEGKL QVELAQLEYL LPRLHGQGTQ LSRLGAGIGT RGPGETKLET DRRHIERRIY DIKRRLQLVV KQRSQYRQRR KANDVFQIAI VGYTNAGKST LFNRLTKSSS LEEDQLFATL DPLTRRVKLP SDMICLITDT VGFIQDLPTA LIAAFKSTLE EVAEADFLLH VVDASDSDLN QQQKTVQKLL EELNANHIPM LTVYNKKDLI QGEDFIANQF PNVLVSAYDE NDLQHMMLQV ESILKEEWNF YTTHVHPEKG DLLYRLKTET LITNREFNED KEEYVVQGFV RHNHPLNRLV EGK // ID Q8F063_LEPIN Unreviewed; 518 AA. AC Q8F063; DT 01-MAR-2003, integrated into UniProtKB/TrEMBL. DT 01-MAR-2003, sequence version 1. DT 07-JUN-2017, entry version 105. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:AAN50832.1}; GN OrderedLocusNames=LA_3634 {ECO:0000313|EMBL:AAN50832.1}; OS Leptospira interrogans serogroup Icterohaemorrhagiae serovar Lai OS (strain 56601). OC Bacteria; Spirochaetes; Leptospirales; Leptospiraceae; Leptospira. OX NCBI_TaxID=189518 {ECO:0000313|EMBL:AAN50832.1, ECO:0000313|Proteomes:UP000001408}; RN [1] {ECO:0000313|EMBL:AAN50832.1, ECO:0000313|Proteomes:UP000001408} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=56601 {ECO:0000313|EMBL:AAN50832.1, RC ECO:0000313|Proteomes:UP000001408}; RX PubMed=12712204; DOI=10.1038/nature01597; RA Ren S.X., Fu G., Jiang X.G., Zeng R., Miao Y.G., Xu H., Zhang Y.X., RA Xiong H., Lu G., Lu L.F., Jiang H.Q., Jia J., Tu Y.F., Jiang J.X., RA Gu W.Y., Zhang Y.Q., Cai Z., Sheng H.H., Yin H.F., Zhang Y., Zhu G.F., RA Wan M., Huang H.L., Qian Z., Wang S.Y., Ma W., Yao Z.J., Shen Y., RA Qiang B.Q., Xia Q.C., Guo X.K., Danchin A., Saint Girons I., RA Somerville R.L., Wen Y.M., Shi M.H., Chen Z., Xu J.G., Zhao G.P.; RT "Unique physiological and pathogenic features of Leptospira RT interrogans revealed by whole-genome sequencing."; RL Nature 422:888-893(2003). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE010300; AAN50832.1; -; Genomic_DNA. DR RefSeq; NP_713814.1; NC_004342.2. DR RefSeq; WP_000960087.1; NC_004342.2. DR ProteinModelPortal; Q8F063; -. DR STRING; 189518.LA_3634; -. DR EnsemblBacteria; AAN50832; AAN50832; LA_3634. DR GeneID; 1152976; -. DR KEGG; lil:LA_3634; -. DR PATRIC; fig|189518.3.peg.3609; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR InParanoid; Q8F063; -. DR KO; K03665; -. DR OMA; EREVIIT; -. DR Proteomes; UP000001408; Chromosome I. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0043022; F:ribosome binding; IBA:GO_Central. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000001408}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000001408}. FT DOMAIN 315 507 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 281 308 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 518 AA; 58962 MW; 0EA9439A27F1CC25 CRC64; MLVGSDNSIE IPFLDRLRIS EARLRGLRLV HTHLKGEPLN QEDLTDLALL RLDYFTAIVM DHFGNPNGYY SAHLNPESED ELWTVLPKQY PGQLTEGILE EILEIESRLS RSKKNLKDAQ KENRAFLVGV YPERNVGRHP SLSMEELKEL CKTAEVHVVD TFIQRKNRLD PSTVLGKGKL EEIILKAIQK HVELLVFDLE LTPSQAKKIS DIADIKVIDR TQLILDIFAR NAKSRDGKLQ VELAQLKYLK GRLTELDDNM SRLTGGIGGR GPGETKLEIG KRRVEERITR LEVELKSLKK RREINRRQRK KNELPAVGIV GYTNAGKSTF LNALTNSEVL SENKLFATLD PTTRRIRFPE EREIIISDTV GFIHDLPPEL SNAFKATLEE LGDSDLLVHV VDVSNPDYKL QMEAVEKILE ELELSHIPMI QVFNKIDRLE KFKIWVIENG YKKSSSVNHG PGLEAITDLK EELGIDTFSD SILVSAFQGW GLKTFLDLLE DRIYNLSRSN YSNTSSVY // ID Q8FPE5_COREF Unreviewed; 535 AA. AC Q8FPE5; C8NPE1; DT 01-MAR-2003, integrated into UniProtKB/TrEMBL. DT 01-MAR-2003, sequence version 1. DT 30-AUG-2017, entry version 99. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; OS Corynebacterium efficiens (strain DSM 44549 / YS-314 / AJ 12310 / JCM OS 11189 / NBRC 100395). OC Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae; OC Corynebacterium. OX NCBI_TaxID=196164 {ECO:0000313|EMBL:BAC18643.1, ECO:0000313|Proteomes:UP000001409}; RN [1] {ECO:0000313|EMBL:BAC18643.1, ECO:0000313|Proteomes:UP000001409} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 44549 / YS-314 / AJ 12310 / JCM 11189 / NBRC 100395 RC {ECO:0000313|Proteomes:UP000001409}; RX PubMed=12840036; DOI=10.1101/gr.1285603; RA Nishio Y., Nakamura Y., Kawarabayasi Y., Usuda Y., Kimura E., RA Sugimoto S., Matsui K., Yamagishi A., Kikuchi H., Ikeo K., RA Gojobori T.; RT "Comparative complete genome sequence analysis of the amino acid RT replacements responsible for the thermostability of Corynebacterium RT efficiens."; RL Genome Res. 13:1572-1579(2003). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BA000035; BAC18643.1; -; Genomic_DNA. DR RefSeq; WP_006767832.1; NZ_GG700683.1. DR ProteinModelPortal; Q8FPE5; -. DR STRING; 196164.HMPREF0290_1866; -. DR EnsemblBacteria; BAC18643; BAC18643; BAC18643. DR KEGG; cef:CE1833; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000001409; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000001409}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000001409}. FT DOMAIN 295 464 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 535 AA; 58382 MW; 5FDD858AE6568597 CRC64; MDEKNKINHE DLLAQAFHDH VKREPLTETT GFDLSGLIPA DTTRRPAESR STHDGDTPSV GELDLEDREA IRRRETTIHS DDAADIYEVE YRKLRLERVI LVGVWTEGTT AEIDASLAEL AALADTAGAE VIESLYQKRD KPDPGTYIGS GKVRELKEII EATGADTVVC DGELSPSQLV ALERELNIKV IDRTMLVLDI FAQHAKSREG KAQVALAQME YLITRVRGWG GNLSRQAGGR AGSNGGVGLR GPGETKIEAD RRRLRSDMAR LRRELSGMDT ARGIKRSQRS ESLVPQIAIA GYTNAGKSSL INAMTGAGVL VEDALFATLD PTTRKAELAD GRHVVFTDTV GFIRHLPTSL VEAFKSTLEE VLEADLMLHV VDGSDPFPLK QIEAVNSVIS DIIRTTGETP PPEIIVVNKI DQADPLTLAE LRHALDDVVF VSALTGEGIK ELEARIELFL NSRDTRLTVL IPFTRGDIVS RIHQYGTVLS EEYSADGTLM EVRIPAQLAA ELKQYAVDAG TGDAPHNEDD EAAAS // ID Q8G4R8_BIFLO Unreviewed; 501 AA. AC Q8G4R8; DT 01-MAR-2003, integrated into UniProtKB/TrEMBL. DT 01-MAR-2003, sequence version 1. DT 07-JUN-2017, entry version 102. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:AAN25107.1}; GN OrderedLocusNames=BL1307 {ECO:0000313|EMBL:AAN25107.1}; OS Bifidobacterium longum (strain NCC 2705). OC Bacteria; Actinobacteria; Bifidobacteriales; Bifidobacteriaceae; OC Bifidobacterium. OX NCBI_TaxID=206672 {ECO:0000313|EMBL:AAN25107.1, ECO:0000313|Proteomes:UP000000439}; RN [1] {ECO:0000313|EMBL:AAN25107.1, ECO:0000313|Proteomes:UP000000439} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NCC 2705 {ECO:0000313|Proteomes:UP000000439}; RX PubMed=12381787; DOI=10.1073/pnas.212527599; RA Schell M.A., Karmirantzou M., Snel B., Vilanova D., Berger B., RA Pessi G., Zwahlen M.-C., Desiere F., Bork P., Delley M., RA Pridmore R.D., Arigoni F.; RT "The genome sequence of Bifidobacterium longum reflects its adaptation RT to the human gastrointestinal tract."; RL Proc. Natl. Acad. Sci. U.S.A. 99:14422-14427(2002). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE014295; AAN25107.1; -; Genomic_DNA. DR RefSeq; NP_696471.1; NC_004307.2. DR RefSeq; WP_011067980.1; NC_004307.2. DR ProteinModelPortal; Q8G4R8; -. DR STRING; 206672.BL1307; -. DR EnsemblBacteria; AAN25107; AAN25107; BL1307. DR GeneID; 1022789; -. DR KEGG; blo:BL1307; -. DR PATRIC; fig|206672.9.peg.157; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR PhylomeDB; Q8G4R8; -. DR Proteomes; UP000000439; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000000439}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000000439}. FT DOMAIN 281 447 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 501 AA; 54679 MW; 78A09760B57C711C CRC64; MTDNTQYTDI NRGNNDVTPE GVLAEQSEVL LDDSQRATGW HEDANQEWEE REARNELKHV AGLGELQDVT EVEYRKVRLE RVVLVGVWSS AVTTQAKAEE SLRELAALAE TAGAVVCDGL LQHRSKPDAA TYVGSGKAKE IAGIVAREEA DTIIVDDDLP PSQRRALEDA AKVKVVDRTA VILDIFAQHA TSREGKAQVE LAQLEYMLPR LRGWGGSLSR QAGGRAAGAD AGIGSRGPGE TKIEMDRRVI RTRIARLRRQ IREMAPAREV KRGSRRRFGL PTVAVVGYTN AGKSSLTNRL TGSAELVENA LFATLDTAVR RAKTRDGRAY AYVDTVGFVR RLPTQLVEAF KSTLEEVAEA DVILHVVDGS HPDPFSQVDA VNDVLADIEG TASIPRILVF NKADQADEAT RERLAALQPD AFIVSAYTGE GLDELRTAVE SLLPVPHVHV NALLPYAAGS LISRVREYGK VDKVEYRDDG IQLEADVDAH LAAQVVEQSI D // ID Q8IIM7_PLAF7 Unreviewed; 698 AA. AC Q8IIM7; DT 01-MAR-2003, integrated into UniProtKB/TrEMBL. DT 01-MAR-2003, sequence version 1. DT 07-JUN-2017, entry version 89. DE SubName: Full=GTP-binding protein, putative {ECO:0000313|EMBL:CZT98795.1}; GN ORFNames=PF11_0143 {ECO:0000313|EMBL:AAN35727.1}, GN PF3D7_1113500 {ECO:0000313|EMBL:CZT98795.1}; OS Plasmodium falciparum (isolate 3D7). OC Eukaryota; Alveolata; Apicomplexa; Aconoidasida; Haemosporida; OC Plasmodiidae; Plasmodium; Plasmodium (Laverania). OX NCBI_TaxID=36329 {ECO:0000313|EMBL:AAN35727.1, ECO:0000313|Proteomes:UP000001450}; RN [1] {ECO:0000313|EMBL:AAN35727.1, ECO:0000313|Proteomes:UP000001450} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=3D7 {ECO:0000313|EMBL:AAN35727.1}, and RC Isolate 3D7 {ECO:0000313|Proteomes:UP000001450}; RX PubMed=12368864; DOI=10.1038/nature01097; RA Gardner M.J., Hall N., Fung E., White O., Berriman M., Hyman R.W., RA Carlton J.M., Pain A., Nelson K.E., Bowman S., Paulsen I.T., James K., RA Eisen J.A., Rutherford K., Salzberg S.L., Craig A., Kyes S., RA Chan M.S., Nene V., Shallom S.J., Suh B., Peterson J., Angiuoli S., RA Pertea M., Allen J., Selengut J., Haft D., Mather M.W., Vaidya A.B., RA Martin D.M., Fairlamb A.H., Fraunholz M.J., Roos D.S., Ralph S.A., RA McFadden G.I., Cummings L.M., Subramanian G.M., Mungall C., RA Venter J.C., Carucci D.J., Hoffman S.L., Newbold C., Davis R.W., RA Fraser C.M., Barrell B.; RT "Genome sequence of the human malaria parasite Plasmodium RT falciparum."; RL Nature 419:498-511(2002). RN [2] {ECO:0000313|EMBL:CZT98795.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=3D7 {ECO:0000313|EMBL:CZT98795.1}; RG P. falciparum Genome Sequencing Consortium; RA Aslett M., Brunk B., Gardner M., Berriman M.; RL Submitted (JUL-2009) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE014838; AAN35727.1; -; Genomic_DNA. DR EMBL; LN999945; CZT98795.1; -; Genomic_DNA. DR RefSeq; XP_001347814.1; XM_001347778.1. DR SMR; Q8IIM7; -. DR EnsemblProtists; CZT98795; CZT98795; PF3D7_1113500. DR GeneDB; PF3D7_1113500.1:pep; -. DR GeneID; 810690; -. DR KEGG; pfa:PF11_0143; -. DR EuPathDB; PlasmoDB:PF3D7_1113500; -. DR HOGENOM; HOG000282270; -. DR InParanoid; Q8IIM7; -. DR OMA; IIVLHPI; -. DR Proteomes; UP000001450; Chromosome 11. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR GO; GO:0043022; F:ribosome binding; IBA:GO_Central. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000001450}; KW Reference proteome {ECO:0000313|Proteomes:UP000001450}. FT DOMAIN 459 629 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 698 AA; 81678 MW; FD385C7811AB7D0C CRC64; MGRILFLLKN VNKIEKRYFT NKSNIYYHNE SQKKEIIVLH PILKRSKNNS NKLFQEIIYD AQEALGLAKS ANFQIAKGIS MPLGGWYLKN EKQKKKNDPK NDKIDEGQVP NKELSQNNEH HHVFEKSEKE IPNEMSFTTD KSSSKYINYD EIERKVAESI LIKVNHIDNK FYFSKGKLNE LSKYYLKNPT PCIFINTLLS PEQFRNLEFL FNSLLKSYQD ELILNNKRER DNSEMYERVS DVKFDNCDSD DIIIDNSSYC LDAYNNFLDK EDEQCDDVDL EQNMNVLNEH IGDTSCEQAN DIPYEQISDT QECSKNIPMY VELFDRYSMI LYILKSRAKN NLSKLQLELA RANFVLNTYS EDSKSRMKYI KYIENNVLGG SCIDYEEKYT KLNFFTVGKQ NKKSNVNFSG YTSNYIKSNE TYKEYEKRII NNLYSKLKNE LIKCKNNMIL QNNSRKHKAI IAIVGYTNVG KTKLINYLTK SNLKARNLLF QTLDNAYKNL NISTCYSTIF VDSIGFIQNI PYSLYESFKI SLEAIKTADV IIHVIDVSHP YKDKHKKCVL ETLNKIGISD EFIKNNVIEV WNKIDKLTDN ELYTLCKNKP KNALPISAKY GTNCNYLIQI IEHLINQIKD VHILNLQFPT SEAKERINFL MKNYKVVPHS ISYSDDGNTT FIKLVENKSN LKKYYEKFEI KETYKSDN // ID Q8KCN0_CHLTE Unreviewed; 441 AA. AC Q8KCN0; DT 01-OCT-2002, integrated into UniProtKB/TrEMBL. DT 01-OCT-2002, sequence version 1. DT 07-JUN-2017, entry version 90. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:AAM72613.1}; GN OrderedLocusNames=CT1384 {ECO:0000313|EMBL:AAM72613.1}; OS Chlorobium tepidum (strain ATCC 49652 / DSM 12025 / NBRC 103806 / OS TLS). OC Bacteria; Chlorobi; Chlorobia; Chlorobiales; Chlorobiaceae; OC Chlorobaculum. OX NCBI_TaxID=194439 {ECO:0000313|EMBL:AAM72613.1, ECO:0000313|Proteomes:UP000001007}; RN [1] {ECO:0000313|EMBL:AAM72613.1, ECO:0000313|Proteomes:UP000001007} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 49652 / DSM 12025 / NBRC 103806 / TLS RC {ECO:0000313|Proteomes:UP000001007}; RX PubMed=12093901; DOI=10.1073/pnas.132181499; RA Eisen J.A., Nelson K.E., Paulsen I.T., Heidelberg J.F., Wu M., RA Dodson R.J., Deboy R., Gwinn M.L., Nelson W.C., Haft D.H., RA Hickey E.K., Peterson J.D., Durkin A.S., Kolonay J.L., Yang F., RA Holt I., Umayam L.A., Mason T., Brenner M., Shea T.P., Parksey D., RA Nierman W.C., Feldblyum T.V., Hansen C.L., Craven M.B., Radune D., RA Vamathevan J., Khouri H., White O., Gruber T.M., Ketchum K.A., RA Venter J.C., Tettelin H., Bryant D.A., Fraser C.M.; RT "The complete genome sequence of Chlorobium tepidum TLS, a RT photosynthetic, anaerobic, green-sulfur bacterium."; RL Proc. Natl. Acad. Sci. U.S.A. 99:9509-9514(2002). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE006470; AAM72613.1; -; Genomic_DNA. DR RefSeq; NP_662271.1; NC_002932.3. DR RefSeq; WP_010933052.1; NC_002932.3. DR ProteinModelPortal; Q8KCN0; -. DR STRING; 194439.CT1384; -. DR PRIDE; Q8KCN0; -. DR EnsemblBacteria; AAM72613; AAM72613; CT1384. DR GeneID; 1006775; -. DR KEGG; cte:CT1384; -. DR PATRIC; fig|194439.7.peg.1258; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000001007; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000001007}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000001007}. FT DOMAIN 202 369 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 441 AA; 49111 MW; 14637F1C7209B2C2 CRC64; MTTIPSPEPR ERAVLVGITS TPDIPRHLVE EYLDELKFLA DTAGADVITS IIQEKKQPDP ATCIGSGKAE DLAGLVEADS IDIVIFDDDL TPVQVRNLER ILKCKVIDRT GLILQIFAIR AKSAQARTQV ELAQLEYLLP RLSGAWTHLS KQKGGIGTKG PGETQIETDR RLVRNRIASL KKKLRAVSLQ HDTQTRGRAA VPRVALVGYT NAGKSTLMNA LCPEAGAYAE NRLFATLDTK TRRLELKINK LVLLSDTVGF IRKLPHTLVE SFKSTLDEVL QADFLLHVID VSHPGFEEHM QVVRETLKEI GVKHDHIIEV FNKIDALDDP AILTGLRGKY PDAVFISAVR GLNLSALKET IANYVARDYK TRKVKTHVSN YKLIGYLYDH AEVIDKKHVD EDVLLTIRVH RNNLKQIDAM LKASASKNHA AANLQHHETH D // ID Q8NP76_CORGL Unreviewed; 486 AA. AC Q8NP76; DT 01-OCT-2002, integrated into UniProtKB/TrEMBL. DT 01-OCT-2002, sequence version 1. DT 30-AUG-2017, entry version 93. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Cgl1940 {ECO:0000313|EMBL:BAB99333.1}; OS Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / JCM 1318 / OS LMG 3730 / NCIMB 10025). OC Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae; OC Corynebacterium. OX NCBI_TaxID=196627 {ECO:0000313|EMBL:BAB99333.1, ECO:0000313|Proteomes:UP000000582}; RN [1] {ECO:0000313|Proteomes:UP000000582} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025 RC {ECO:0000313|Proteomes:UP000000582}; RX PubMed=12743753; DOI=10.1007/s00253-003-1328-1; RA Ikeda M., Nakagawa S.; RT "The Corynebacterium glutamicum genome: features and impacts on RT biotechnological processes."; RL Appl. Microbiol. Biotechnol. 62:99-109(2003). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BA000036; BAB99333.1; -; Genomic_DNA. DR RefSeq; NP_601147.2; NC_003450.3. DR RefSeq; WP_011014769.1; NC_006958.1. DR ProteinModelPortal; Q8NP76; -. DR STRING; 196627.NCgl1865; -. DR EnsemblBacteria; BAB99333; BAB99333; BAB99333. DR GeneID; 1019897; -. DR KEGG; cgl:NCgl1865; -. DR PATRIC; fig|196627.13.peg.1878; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR KO; K03665; -. DR OMA; HPATYIG; -. DR BioCyc; CORYNE:G18NG-11532-MONOMER; -. DR Proteomes; UP000000582; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000000582}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000000582}. FT DOMAIN 259 428 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 218 245 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 486 AA; 52835 MW; BE0780EB93DAF289 CRC64; MRPGSDETSG FDLSGFIRAE EPSTGDLDLE ARDAQRRRDT EIHADEAADG YEVEYRKLRL ERVILVGVWT EGTTAEIDAS LAELAALADT AGAEVIETLY QKRDKPDPGT YIGSGKVREL KEIIEATSAD TVVCDGELSP SQLVALEREL DIKVIDRTML ILDIFAQHAK SREGKAQVAL AQMEYLISRV RGWGGNLSRQ AGGRAGSNGG VGLRGPGETK IEADRRRLRS DMARLRRELS GLDTSRSIKR AQRAASLVPQ IAIAGYTNAG KSSLINAMTG AGVLVENALF ATLDPTTRKA ELADGRHVVF TDTVGFVRHL PTSLVEAFKS TLEEVVEADL MLHVVDGSDP FPLKQIDAVN TVISDIVRST GAVPPPEIIV VNKIDQADPL TLAELRHAVD DVVFVSALTG EGIKELEARI ELFLNSRDAH LLLKIPFTRG DIVSRLHQHG TVLSEDYAED GTLMDVRIPT QLAQELQSYV VEPTSA // ID Q8P9X6_XANCP Unreviewed; 439 AA. AC Q8P9X6; DT 01-OCT-2002, integrated into UniProtKB/TrEMBL. DT 01-OCT-2002, sequence version 1. DT 07-JUN-2017, entry version 105. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:AAM41011.1}; GN OrderedLocusNames=XCC1717 {ECO:0000313|EMBL:AAM41011.1}; OS Xanthomonas campestris pv. campestris (strain ATCC 33913 / DSM 3586 / OS NCPPB 528 / LMG 568 / P 25). OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales; OC Xanthomonadaceae; Xanthomonas. OX NCBI_TaxID=190485 {ECO:0000313|EMBL:AAM41011.1, ECO:0000313|Proteomes:UP000001010}; RN [1] {ECO:0000313|EMBL:AAM41011.1, ECO:0000313|Proteomes:UP000001010} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33913 / DSM 3586 / NCPPB 528 / LMG 568 / P 25 RC {ECO:0000313|Proteomes:UP000001010}; RX PubMed=12024217; DOI=10.1038/417459a; RA da Silva A.C.R., Ferro J.A., Reinach F.C., Farah C.S., Furlan L.R., RA Quaggio R.B., Monteiro-Vitorello C.B., Van Sluys M.A., RA Almeida N.F.Jr., Alves L.M.C., do Amaral A.M., Bertolini M.C., RA Camargo L.E.A., Camarotte G., Cannavan F., Cardozo J., Chambergo F., RA Ciapina L.P., Cicarelli R.M.B., Coutinho L.L., Cursino-Santos J.R., RA El-Dorry H., Faria J.B., Ferreira A.J.S., Ferreira R.C.C., RA Ferro M.I.T., Formighieri E.F., Franco M.C., Greggio C.C., Gruber A., RA Katsuyama A.M., Kishi L.T., Leite R.P.Jr., Lemos E.G.M., Lemos M.V.F., RA Locali E.C., Machado M.A., Madeira A.M.B.N., Martinez-Rossi N.M., RA Martins E.C., Meidanis J., Menck C.F.M., Miyaki C.Y., Moon D.H., RA Moreira L.M., Novo M.T.M., Okura V.K., Oliveira M.C., Oliveira V.R., RA Pereira H.A.Jr., Rossi A., Sena J.A.D., Silva C., de Souza R.F., RA Spinola L.A.F., Takita M.A., Tamura R.E., Teixeira E.C., Tezza R.I.D., RA Trindade dos Santos M., Truffi D., Tsai S.M., White F.F., RA Setubal J.C., Kitajima J.P.; RT "Comparison of the genomes of two Xanthomonas pathogens with differing RT host specificities."; RL Nature 417:459-463(2002). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE008922; AAM41011.1; -; Genomic_DNA. DR RefSeq; NP_637087.1; NC_003902.1. DR RefSeq; WP_011036894.1; NC_003902.1. DR ProteinModelPortal; Q8P9X6; -. DR STRING; 190485.XCC1717; -. DR DNASU; 999347; -. DR EnsemblBacteria; AAM41011; AAM41011; XCC1717. DR GeneID; 999347; -. DR KEGG; xcc:XCC1717; -. DR PATRIC; fig|190485.4.peg.1832; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR Proteomes; UP000001010; Chromosome. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0043022; F:ribosome binding; IBA:GO_Central. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000001010}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000001010}. FT DOMAIN 199 369 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 158 192 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 439 AA; 48781 MW; 985C068F69EE7584 CRC64; MFDRSRKGEH ALLIQTHSGG PAEEDVLEEF AELAKSAGAT VAATLTARID KPSPSTLIGS GKLEEVKAAA EATGADLVLV NHTLSPGQER NLERYLERRV IDRTGLILDI FAQRARSHEG KLQVELAQLR HMATRLVRGW THLERQRGGA IGLRGPGETQ LETDRRLLQK RVEQLQKRLE KVEVQRTQMR RARMRSELPR IALVGYTNAG KSTLFNALTG ADAYAADQLF ATLDPTVRRI ALPGGSAVLA DTVGFVRDLP HELVAAFRST LSEARDADLL LHIVDAADPL REERIHQVDE VLQAVGAGDL PQLLVFNKID KIEGAEVRHD AQDGIPDQAR RERVWISARD GRGLEELQRA LGHRLDLRHI TGSLRLPASA GRLRSKLHQL EVIRSEQVDE EGWLLEVDLP YVEAERLAAG EDGAPLRALL PDRREDWET // ID Q8PZI3_METMA Unreviewed; 355 AA. AC Q8PZI3; DT 01-OCT-2002, integrated into UniProtKB/TrEMBL. DT 01-OCT-2002, sequence version 1. DT 05-JUL-2017, entry version 104. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:AAM30206.1}; GN OrderedLocusNames=MM_0510 {ECO:0000313|EMBL:AAM30206.1}; OS Methanosarcina mazei (strain ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / OS JCM 11833 / OCM 88) (Methanosarcina frisia). OC Archaea; Euryarchaeota; Methanomicrobia; Methanosarcinales; OC Methanosarcinaceae; Methanosarcina. OX NCBI_TaxID=192952 {ECO:0000313|EMBL:AAM30206.1, ECO:0000313|Proteomes:UP000000595}; RN [1] {ECO:0000313|EMBL:AAM30206.1, ECO:0000313|Proteomes:UP000000595} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88 RC {ECO:0000313|Proteomes:UP000000595}; RX PubMed=12125824; RA Deppenmeier U., Johann A., Hartsch T., Merkl R., Schmitz R.A., RA Martinez-Arias R., Henne A., Wiezer A., Baumer S., Jacobi C., RA Bruggemann H., Lienard T., Christmann A., Bomeke M., Steckel S., RA Bhattacharyya A., Lykidis A., Overbeek R., Klenk H.P., Gunsalus R.P., RA Fritz H.J., Gottschalk G.; RT "The genome of Methanosarcina mazei: evidence for lateral gene RT transfer between Bacteria and Archaea."; RL J. Mol. Microbiol. Biotechnol. 4:453-461(2002). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE008384; AAM30206.1; -; Genomic_DNA. DR ProteinModelPortal; Q8PZI3; -. DR STRING; 192952.MM_0510; -. DR EnsemblBacteria; AAM30206; AAM30206; MM_0510. DR KEGG; mma:MM_0510; -. DR PATRIC; fig|192952.21.peg.608; -. DR eggNOG; arCOG00353; Archaea. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG093Z07D6; -. DR Proteomes; UP000000595; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000000595}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000000595}. FT DOMAIN 127 296 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 355 AA; 40422 MW; D0477996E385D569 CRC64; MRQKRAGKVI FYNRLSTIQL FNISEICGCQ VMDKFQLILE IFAKRATTRR SKLQVELARL KYEIPRARAI VSLVKKEERA GFMGLGDYED AYEQDLKKRI ARIEDELESA GKDDESLRAF RHRKGFSLVA LAGYTNAGKS TLFNAIVNES VEARNMLFTT LVPTTRALDL GGRKALLTDT VGFIEELPHW LVDAFKSTLD EIFLSDLILL VVDAGEKPET ILQKLSTSHD TLWDRIQGVP IITVLNKIDL LEEAQLEALM EEIGYMAPNP VFVSAKKKIG MQELKDEIIK HLPAWSFYSF SLPNSEKGMS VLSWLYDEGI VHRVEYGERI SVDYEAREDI INRIKSLELN PDEQG // ID Q8RF93_FUSNN Unreviewed; 600 AA. AC Q8RF93; DT 01-JUN-2002, integrated into UniProtKB/TrEMBL. DT 01-JUN-2002, sequence version 1. DT 07-JUN-2017, entry version 88. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=FN0823 {ECO:0000313|EMBL:AAL95019.1}; OS Fusobacterium nucleatum subsp. nucleatum (strain ATCC 25586 / CIP OS 101130 / JCM 8532 / LMG 13131). OC Bacteria; Fusobacteria; Fusobacteriales; Fusobacteriaceae; OC Fusobacterium. OX NCBI_TaxID=190304 {ECO:0000313|EMBL:AAL95019.1, ECO:0000313|Proteomes:UP000002521}; RN [1] {ECO:0000313|EMBL:AAL95019.1, ECO:0000313|Proteomes:UP000002521} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 25586 / CIP 101130 / JCM 8532 / LMG 13131 RC {ECO:0000313|Proteomes:UP000002521}; RX PubMed=11889109; DOI=10.1128/JB.184.7.2005-2018.2002; RA Kapatral V., Anderson I., Ivanova N., Reznik G., Los T., Lykidis A., RA Bhattacharyya A., Bartman A., Gardner W., Grechkin G., Zhu L., RA Vasieva O., Chu L., Kogan Y., Chaga O., Goltsman E., Bernal A., RA Larsen N., D'Souza M., Walunas T., Pusch G., Haselkorn R., RA Fonstein M., Kyrpides N., Overbeek R.; RT "Genome sequence and analysis of the oral bacterium Fusobacterium RT nucleatum strain ATCC 25586."; RL J. Bacteriol. 184:2005-2018(2002). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE009951; AAL95019.1; -; Genomic_DNA. DR RefSeq; NP_603720.1; NC_003454.1. DR RefSeq; WP_011016675.1; NC_003454.1. DR ProteinModelPortal; Q8RF93; -. DR STRING; 190304.FN0823; -. DR EnsemblBacteria; AAL95019; AAL95019; FN0823. DR GeneID; 992913; -. DR KEGG; fnu:FN0823; -. DR PATRIC; fig|190304.8.peg.1384; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR InParanoid; Q8RF93; -. DR KO; K03665; -. DR OMA; EREVIIT; -. DR Proteomes; UP000002521; Chromosome. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0043022; F:ribosome binding; IBA:GO_Central. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000002521}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000002521}. FT DOMAIN 361 546 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 600 AA; 68392 MW; FB54021269D8A3FE CRC64; MINGNTSGLK EYILENLDKL YSTKIEKGKI INQEIVDYIS EISNKINREI NVAIDRNGNI IDISIGDSST VNLPVIPVYD KKLSGVRIIH THPSGNPHLS SVDISALIKL KLDCIVSIGV SEEGVTGYEV AICSIVNDEL TYDRTLLENL DDFDYLEEIK EVEENLRKRN ITEDDKEYAL LIGIDKEEYL DELEELASAC DVKVVGRFFQ KRSKPDPLFL IGSGKIQELA LTRQVRKVNL LIFDEELSGL QLKMIEEVTG CKVIDRTTLI LEIFARRART REAKLQVELA QLKYRSNRLI GFGVTMSRLG GGVGTKGPGE KKLEIDRRVI KKTIAYLNNE LENIKKIRNT QRSKREDSGM PRVSLVGYTN VGKSTLRNVL VDMYQNDKTL KKEEVLSQDM LFATLDTTTR TIELKDKRIV SLTDTVGFIQ KLPHDLVESF KSTLEEVIFS DLIIHVADIS SKNVIEQIDA VEDVLEELNC LDKTKILLLN KIDNVTKDNS FPLMEKKIEE IKAKYSNYQI LIISAKNRFN IDELMELIKK NLIVKTYNCK LLIPYVNTEI AARVHRNTIV KSESFVDEGI ILEVVMNEKE YNKFKDFIFN // ID Q8TK03_METAC Unreviewed; 353 AA. AC Q8TK03; DT 01-JUN-2002, integrated into UniProtKB/TrEMBL. DT 01-JUN-2002, sequence version 1. DT 05-JUL-2017, entry version 105. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=MA_3622 {ECO:0000313|EMBL:AAM06977.1}; OS Methanosarcina acetivorans (strain ATCC 35395 / DSM 2834 / JCM 12185 / OS C2A). OC Archaea; Euryarchaeota; Methanomicrobia; Methanosarcinales; OC Methanosarcinaceae; Methanosarcina. OX NCBI_TaxID=188937 {ECO:0000313|EMBL:AAM06977.1, ECO:0000313|Proteomes:UP000002487}; RN [1] {ECO:0000313|EMBL:AAM06977.1, ECO:0000313|Proteomes:UP000002487} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 35395 / DSM 2834 / JCM 12185 / C2A RC {ECO:0000313|Proteomes:UP000002487}; RX PubMed=11932238; DOI=10.1101/gr.223902; RA Galagan J.E., Nusbaum C., Roy A., Endrizzi M.G., Macdonald P., RA FitzHugh W., Calvo S., Engels R., Smirnov S., Atnoor D., Brown A., RA Allen N., Naylor J., Stange-Thomann N., DeArellano K., Johnson R., RA Linton L., McEwan P., McKernan K., Talamas J., Tirrell A., Ye W., RA Zimmer A., Barber R.D., Cann I., Graham D.E., Grahame D.A., Guss A., RA Hedderich R., Ingram-Smith C., Kuettner C.H., Krzycki J.A., RA Leigh J.A., Li W., Liu J., Mukhopadhyay B., Reeve J.N., Smith K., RA Springer T.A., Umayam L.A., White O., White R.H., de Macario E.C., RA Ferry J.G., Jarrell K.F., Jing H., Macario A.J.L., Paulsen I., RA Pritchett M., Sowers K.R., Swanson R.V., Zinder S.H., Lander E., RA Metcalf W.W., Birren B.; RT "The genome of Methanosarcina acetivorans reveals extensive metabolic RT and physiological diversity."; RL Genome Res. 12:532-542(2002). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE010299; AAM06977.1; -; Genomic_DNA. DR ProteinModelPortal; Q8TK03; -. DR STRING; 188937.MA3622; -. DR EnsemblBacteria; AAM06977; AAM06977; MA_3622. DR KEGG; mac:MA_3622; -. DR eggNOG; arCOG00353; Archaea. DR eggNOG; COG2262; LUCA. DR InParanoid; Q8TK03; -. DR KO; K03665; -. DR OMA; CNARTEE; -. DR OrthoDB; POG093Z07D6; -. DR PhylomeDB; Q8TK03; -. DR Proteomes; UP000002487; Chromosome. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0043022; F:ribosome binding; IBA:GO_Central. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000002487}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000002487}. FT DOMAIN 127 296 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 353 AA; 40176 MW; 23329B6E9E4FDAEB CRC64; MRMKRASKVI FYNRLSTIQL FNISEICGCQ IIDKFQLILE IFAKRATTRR SKLQVELARL RYEVPRARAI VSLVKKEERA GFMGLGDYED AYEQDLKKRI SRIENELESA EKDDESLRAF RHRKGFSLVS FAGYTNAGKS TLFNAIVDES VEAQDKLFTT LVPTTRALDL GGRKALLTDT VGFIEELPHW LVDAFKSTLD EIFLSDLILL VVDVSEKPET ILQKLSTSHD TLWDRIQGVP VITVLNKTDL LEASELEAAM EEIGYMAPNP VFVSAKEKLG MKELKAEIIK HLPAWSSYSF TLPNSEKGMS VLSWLYDEGI VHRVDYGERI SVDYEARTEI INRIKALELN QGE // ID Q8TY50_METKA Unreviewed; 423 AA. AC Q8TY50; DT 01-JUN-2002, integrated into UniProtKB/TrEMBL. DT 01-JUN-2002, sequence version 1. DT 07-JUN-2017, entry version 96. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=MK0456 {ECO:0000313|EMBL:AAM01671.1}; OS Methanopyrus kandleri (strain AV19 / DSM 6324 / JCM 9639 / NBRC OS 100938). OC Archaea; Euryarchaeota; Methanopyri; Methanopyrales; Methanopyraceae; OC Methanopyrus. OX NCBI_TaxID=190192 {ECO:0000313|EMBL:AAM01671.1, ECO:0000313|Proteomes:UP000001826}; RN [1] {ECO:0000313|EMBL:AAM01671.1, ECO:0000313|Proteomes:UP000001826} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=AV19 / DSM 6324 / JCM 9639 / NBRC 100938 RC {ECO:0000313|Proteomes:UP000001826}; RX PubMed=11930014; DOI=10.1073/pnas.032671499; RA Slesarev A.I., Mezhevaya K.V., Makarova K.S., Polushin N.N., RA Shcherbinina O.V., Shakhova V.V., Belova G.I., Aravind L., RA Natale D.A., Rogozin I.B., Tatusov R.L., Wolf Y.I., Stetter K.O., RA Malykh A.G., Koonin E.V., Kozyavkin S.A.; RT "The complete genome of hyperthermophile Methanopyrus kandleri AV19 RT and monophyly of archaeal methanogens."; RL Proc. Natl. Acad. Sci. U.S.A. 99:4644-4649(2002). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE009439; AAM01671.1; -; Genomic_DNA. DR ProteinModelPortal; Q8TY50; -. DR STRING; 190192.MK0456; -. DR EnsemblBacteria; AAM01671; AAM01671; MK0456. DR KEGG; mka:MK0456; -. DR PATRIC; fig|190192.8.peg.486; -. DR eggNOG; arCOG00353; Archaea. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG093Z07D6; -. DR Proteomes; UP000001826; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000001826}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000001826}. FT DOMAIN 190 359 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 105 139 {ECO:0000256|SAM:Coils}. FT COILED 152 183 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 423 AA; 48729 MW; 77770E572ACAAE16 CRC64; MPSRPRAVLV ERLEWRQESR IDELKELAES AGYDVVGSFR QVRHEDPRYH IGEGKVKELA EFVRENDVDK VIFENEIKPV QAFNLAGELG VEVIDRFQLI LEIFAQRART REAKLQVKLA QLKYELPRAR EMVNLAKKEE RPGFRGLGKY EADKYEEMIR RKIAKIEREL RRIEKDRELK RKHRHRLGFE LVTLAGYTCA GKSTLMRALT DETVYVDSKM FSTLDTKTRA VDLDGHRVLL TDTVGFVDNL PHWLVESFKS TLEETAQADL VLLVVDVSDE LPEIKRKLRV CHRTLEEIGA EGPIVTALNK ADLIGWEEAE RRLRELEGYV SHPVVVSAKT GEGLDDLKAE MRTVLSRYWK NVRIELPMRN ETMRVVSKLH ELGNVLDERW SNDGVEVFLE VSEKALGTVR GTVKGFGKVE VLD // ID Q8U1M9_PYRFU Unreviewed; 431 AA. AC Q8U1M9; DT 01-JUN-2002, integrated into UniProtKB/TrEMBL. DT 01-JUN-2002, sequence version 1. DT 07-JUN-2017, entry version 94. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=PF1177 {ECO:0000313|EMBL:AAL81301.1}; OS Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1). OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae; OC Pyrococcus. OX NCBI_TaxID=186497 {ECO:0000313|EMBL:AAL81301.1, ECO:0000313|Proteomes:UP000001013}; RN [1] {ECO:0000313|EMBL:AAL81301.1, ECO:0000313|Proteomes:UP000001013} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1 RC {ECO:0000313|Proteomes:UP000001013}; RX PubMed=10430560; RA Maeder D.L., Weiss R.B., Dunn D.M., Cherry J.L., Gonzalez J.M., RA DiRuggiero J., Robb F.T.; RT "Divergence of the hyperthermophilic archaea Pyrococcus furiosus and RT P. horikoshii inferred from complete genomic sequences."; RL Genetics 152:1299-1305(1999). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE009950; AAL81301.1; -; Genomic_DNA. DR ProteinModelPortal; Q8U1M9; -. DR STRING; 186497.PF1177; -. DR EnsemblBacteria; AAL81301; AAL81301; PF1177. DR KEGG; pfu:PF1177; -. DR PATRIC; fig|186497.12.peg.1237; -. DR eggNOG; arCOG00353; Archaea. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG093Z07D6; -. DR Proteomes; UP000001013; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000001013}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000001013}. FT DOMAIN 187 362 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 431 AA; 49544 MW; F433BD3C16731335 CRC64; MMRAIGVIRK SRQERISREE FEDLLRSAGY EILAIVEQVR EEHPRYNIGP GKVEELKSLV KELKPDKVVF ANKLTPSQAY NLWKELRVDI IDKWQLVLEI FEKRAHSKEA KLQVELANLQ YELPLVKEAI RRIKMGDRAG FKGMGEYQVH QYFKHIRYRM GKIREELEKI KAERDIRRKK REEDGFVLVA LAGYTNAGKS TLLNALTGEN VEAKNQMFTT LDTTTRRFKL GGKLLLITDT VGFIDNLPPF IVEAFHSTLE EIVKADIIVL VLDSSEAWPE IRRKFFASLN VLRELKALER PMIIALNKID KVTPEDAETK KMLLKEIADG RVNLVEVVKI SAKNGILEEL YTALEKALLK LPKFQFFEIV VKDPTQVGKI LSLVYSVGDV LEVTYNGGEE TTIKAYMQSG MIRELTKLGV EIKRLQIREE A // ID Q8U5B2_AGRFC Unreviewed; 444 AA. AC Q8U5B2; DT 01-JUN-2002, integrated into UniProtKB/TrEMBL. DT 15-JAN-2008, sequence version 2. DT 07-JUN-2017, entry version 91. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflx {ECO:0000313|EMBL:AAK87243.2}; GN Synonyms=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=Atu1451 {ECO:0000313|EMBL:AAK87243.2}; OS Agrobacterium fabrum (strain C58 / ATCC 33970) (Agrobacterium OS tumefaciens (strain C58)). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Rhizobiaceae; Rhizobium/Agrobacterium group; Agrobacterium; OC Agrobacterium tumefaciens complex. OX NCBI_TaxID=176299 {ECO:0000313|EMBL:AAK87243.2, ECO:0000313|Proteomes:UP000000813}; RN [1] {ECO:0000313|EMBL:AAK87243.2, ECO:0000313|Proteomes:UP000000813} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C58 / ATCC 33970 {ECO:0000313|Proteomes:UP000000813}; RX PubMed=11743193; DOI=10.1126/science.1066804; RA Wood D.W., Setubal J.C., Kaul R., Monks D.E., Kitajima J.P., RA Okura V.K., Zhou Y., Chen L., Wood G.E., Almeida N.F.Jr., Woo L., RA Chen Y., Paulsen I.T., Eisen J.A., Karp P.D., Bovee D.Sr., Chapman P., RA Clendenning J., Deatherage G., Gillet W., Grant C., Kutyavin T., RA Levy R., Li M.J., McClelland E., Palmieri A., Raymond C., Rouse G., RA Saenphimmachak C., Wu Z., Romero P., Gordon D., Zhang S., Yoo H., RA Tao Y., Biddle P., Jung M., Krespan W., Perry M., Gordon-Kamm B., RA Liao L., Kim S., Hendrick C., Zhao Z.Y., Dolan M., Chumley F., RA Tingey S.V., Tomb J.F., Gordon M.P., Olson M.V., Nester E.W.; RT "The genome of the natural genetic engineer Agrobacterium tumefaciens RT C58."; RL Science 294:2317-2323(2001). RN [2] {ECO:0000313|EMBL:AAK87243.2, ECO:0000313|Proteomes:UP000000813} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C58 / ATCC 33970 {ECO:0000313|Proteomes:UP000000813}; RX PubMed=11743194; DOI=10.1126/science.1066803; RA Goodner B., Hinkle G., Gattung S., Miller N., Blanchard M., RA Qurollo B., Goldman B.S., Cao Y., Askenazi M., Halling C., Mullin L., RA Houmiel K., Gordon J., Vaudin M., Iartchouk O., Epp A., Liu F., RA Wollam C., Allinger M., Doughty D., Scott C., Lappas C., Markelz B., RA Flanagan C., Crowell C., Gurson J., Lomo C., Sear C., Strub G., RA Cielo C., Slater S.; RT "Genome sequence of the plant pathogen and biotechnology agent RT Agrobacterium tumefaciens C58."; RL Science 294:2323-2328(2001). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE007869; AAK87243.2; -; Genomic_DNA. DR RefSeq; NP_354458.2; NC_003062.2. DR RefSeq; WP_010971630.1; NC_003062.2. DR ProteinModelPortal; Q8U5B2; -. DR STRING; 176299.Atu1451; -. DR EnsemblBacteria; AAK87243; AAK87243; Atu1451. DR GeneID; 1133489; -. DR KEGG; atu:Atu1451; -. DR PATRIC; fig|176299.10.peg.1472; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR BioCyc; AGRO:ATU1451-MONOMER; -. DR Proteomes; UP000000813; Chromosome circular. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000000813}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000000813}. FT DOMAIN 206 378 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 165 199 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 444 AA; 49299 MW; 924E129CBFD93FCE CRC64; MRAVVLVPFL KQQRENRDAA SAPAAPGRSV EAKLEEAKGL ALAIDLEVTQ GLVVPVNQPR PATLFGTGKI EEIGHLLDET NSGLVIVDHP LTPVQQRNLE KQWNAKVIDR TGLILEIFGR RASTKEGTLQ VDLAHLNYQK GRLVRSWTHL ERQRGGAGFM GGPGETQIEA DRRLLQDRIV KLEKELEQVV RTRQLHRAKR RKVPHPIVAL VGYTNAGKST LFNRITGAGV LAEDMLFATL DPTLRRMKLP HGRTVILSDT VGFISDLPTH LVAAFRATLE EVLEADLVLH VRDMSDPDNA AQSADVLRIL GDLGIDEKEA EKRIIEVWNK VDRLEPEAHD AIMQRAEGRS DIRAVSAITG EGVDALMEEI SKRLSGVLTE TTVVLSVEQL PLISWVYSNS IVDNREDHED GSVALDVRLS EAQAVELERK LGKTAGRERE DWER // ID Q8XJ04_CLOPE Unreviewed; 597 AA. AC Q8XJ04; DT 01-MAR-2002, integrated into UniProtKB/TrEMBL. DT 01-MAR-2002, sequence version 1. DT 07-JUN-2017, entry version 95. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:BAB81665.1}; OS Clostridium perfringens (strain 13 / Type A). OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=195102 {ECO:0000313|EMBL:BAB81665.1, ECO:0000313|Proteomes:UP000000818}; RN [1] {ECO:0000313|EMBL:BAB81665.1, ECO:0000313|Proteomes:UP000000818} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=13 / Type A {ECO:0000313|Proteomes:UP000000818}; RX PubMed=11792842; DOI=10.1073/pnas.022493799; RA Shimizu T., Ohtani K., Hirakawa H., Ohshima K., Yamashita A., RA Shiba T., Ogasawara N., Hattori M., Kuhara S., Hayashi H.; RT "Complete genome sequence of Clostridium perfringens, an anaerobic RT flesh-eater."; RL Proc. Natl. Acad. Sci. U.S.A. 99:996-1001(2002). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BA000016; BAB81665.1; -; Genomic_DNA. DR RefSeq; WP_003451503.1; NC_003366.1. DR ProteinModelPortal; Q8XJ04; -. DR EnsemblBacteria; BAB81665; BAB81665; BAB81665. DR GeneID; 29570679; -. DR KEGG; cpe:CPE1959; -. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000000818; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000000818}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000000818}. FT DOMAIN 364 544 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 597 AA; 67079 MW; 5B8227727AC429AB CRC64; MIHGNTDGIR NSVLKELEEL YKINVPKYSV CTEDMINIIS RLSSQIEREI SVGINRKGKV ISVAIGDSSS VEIPLIDIHE KRLSGVRIIH THPSGVSRLS ALDISALMKL KLDTIMAIAV EEGKAKDASL GFCYVENEIL ISEEAPHLTI DKCLQINILD KINHVEEVIK TSNVEEDDSE RAILVGCDTR ESLDELEELA KACDIPTLEK VFQNRSKIDA SFYIGRGKVL EIANIRQLTR ANLVIFDDEL SGAQVKNLEA NLGVKVIDRT TLILEIFSRR AKTREAKIQV ELAQLKYRAA RLMGLGTVMS RTGGGIGTRG PGEKKLEIDR RHIRERIYDL QAELKKIKKI RETQRERRSK DKTSQVSLVG YTNAGKSTLR NTLCAESAST LATQAKDKVF EADMLFATLD TTTRAIKLPD NRDITLTDTV GFVSKLPHEL VEAFKSTLEE VIYSDLLCHV VDASSDNAQE EIIAVEKVLG ELKALESAKI LVLNKIDKAD EEKLNELEAK YSSIYNKVVK ISARERINLD DLLEAISEEL PYTLKSKEYI IPYTAQQVVA YLHRNANVSE EEYREEGTYI KAEVDEEVEN KCREYEL // ID Q8Y024_RALSO Unreviewed; 417 AA. AC Q8Y024; DT 01-MAR-2002, integrated into UniProtKB/TrEMBL. DT 01-MAR-2002, sequence version 1. DT 07-JUN-2017, entry version 95. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=RSc1221 {ECO:0000313|EMBL:CAD14923.1}; OS Ralstonia solanacearum (strain GMI1000) (Pseudomonas solanacearum). OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Ralstonia. OX NCBI_TaxID=267608 {ECO:0000313|EMBL:CAD14923.1, ECO:0000313|Proteomes:UP000001436}; RN [1] {ECO:0000313|EMBL:CAD14923.1, ECO:0000313|Proteomes:UP000001436} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=GMI1000 {ECO:0000313|EMBL:CAD14923.1, RC ECO:0000313|Proteomes:UP000001436}; RX PubMed=11823852; DOI=10.1038/415497a; RA Salanoubat M., Genin S., Artiguenave F., Gouzy J., Mangenot S., RA Arlat M., Billault A., Brottier P., Camus J.C., Cattolico L., RA Chandler M., Choisne N., Claudel-Renard C., Cunnac S., Demange N., RA Gaspin C., Lavie M., Moisan A., Robert C., Saurin W., Schiex T., RA Siguier P., Thebault P., Whalen M., Wincker P., Levy M., RA Weissenbach J., Boucher C.A.; RT "Genome sequence of the plant pathogen Ralstonia solanacearum."; RL Nature 415:497-502(2002). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AL646052; CAD14923.1; -; Genomic_DNA. DR RefSeq; WP_011001170.1; NC_003295.1. DR ProteinModelPortal; Q8Y024; -. DR STRING; 267608.RSc1221; -. DR EnsemblBacteria; CAD14923; CAD14923; RSc1221. DR GeneID; 1220043; -. DR KEGG; rso:RSc1221; -. DR PATRIC; fig|267608.8.peg.1240; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000001436; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000001436}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000001436}. FT DOMAIN 202 372 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 161 195 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 417 AA; 46129 MW; 62C690826AE27CE5 CRC64; MPSHPTSSTE PTRAILVAVD FGKHDFQESL SELALLASTA GSEPVRAVTG RRSRPDAALF IGAGKAEEVK IAADEDDAEI VIFNHALSPA QQRNLERFFG RHVVDRTGLI LDIFSQRAQS HVGKVQVELA RVRYQASRLV RAWSHLERQK GGIGMRGGPG ERQLELDRRM LDERAKRLSA ELDRLQRQHD TQRRARSRND AFSVSLVGYT NAGKSTLFNA LTKARAYAAN QLFATLDTTS RRLYLEGLGN VVLSDTVGFI RDLPTQLVAA FRATLEETVH ADVLLHVVDA ASAVKHEQME QVDRVLAEIN ASDIPQILVM NKIDAAEELR SQGPRIERDE AGAVRRVFVS ALEGAGLELL REALVETAIR LREHPSSRDG DFDPRFDTRR ETSSAQRDEL SQVPPASALP AERGGRD // ID Q8Y7I2_LISMO Unreviewed; 407 AA. AC Q8Y7I2; DT 01-MAR-2002, integrated into UniProtKB/TrEMBL. DT 01-MAR-2002, sequence version 1. DT 07-JUN-2017, entry version 95. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=lmo1296 {ECO:0000313|EMBL:CAC99374.1}; OS Listeria monocytogenes serovar 1/2a (strain ATCC BAA-679 / EGD-e). OC Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria. OX NCBI_TaxID=169963 {ECO:0000313|EMBL:CAC99374.1, ECO:0000313|Proteomes:UP000000817}; RN [1] {ECO:0000313|EMBL:CAC99374.1, ECO:0000313|Proteomes:UP000000817} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-679 / EGD-e {ECO:0000313|Proteomes:UP000000817}; RX PubMed=11679669; DOI=10.1126/science.1063447; RA Glaser P., Frangeul L., Buchrieser C., Rusniok C., Amend A., RA Baquero F., Berche P., Bloecker H., Brandt P., Chakraborty T., RA Charbit A., Chetouani F., Couve E., de Daruvar A., Dehoux P., RA Domann E., Dominguez-Bernal G., Duchaud E., Durant L., Dussurget O., RA Entian K.D., Fsihi H., Portillo F.G., Garrido P., Gautier L., RA Goebel W., Gomez-Lopez N., Hain T., Hauf J., Jackson D., Jones L.M., RA Kaerst U., Kreft J., Kuhn M., Kunst F., Kurapkat G., Madueno E., RA Maitournam A., Vicente J.M., Ng E., Nedjari H., Nordsiek G., RA Novella S., de Pablos B., Perez-Diaz J.C., Purcell R., Remmel B., RA Rose M., Schlueter T., Simoes N., Tierrez A., Vazquez-Boland J.A., RA Voss H., Wehland J., Cossart P.; RT "Comparative genomics of Listeria species."; RL Science 294:849-852(2001). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AL591978; CAC99374.1; -; Genomic_DNA. DR PIR; AH1236; AH1236. DR RefSeq; NP_464821.1; NC_003210.1. DR RefSeq; WP_010989727.1; NC_003210.1. DR ProteinModelPortal; Q8Y7I2; -. DR STRING; 169963.lmo1296; -. DR PaxDb; Q8Y7I2; -. DR EnsemblBacteria; CAC99374; CAC99374; CAC99374. DR GeneID; 985125; -. DR KEGG; lmo:lmo1296; -. DR PATRIC; fig|169963.11.peg.1331; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR PhylomeDB; Q8Y7I2; -. DR Proteomes; UP000000817; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000000817}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000000817}. FT DOMAIN 196 357 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 407 AA; 46198 MW; 1435F26A13A0A283 CRC64; MEREKIILVG VFLPNKTEEA FWNSMKELHS LAKTANAEVM DELIQKLERV NQASFIGSGK LDELAALVEM HEADVVIFNS ELSATQVRNI SAAVEARIID RTQLILDIFA MCAKSREGKL QVAYAQYKYL LPRLSGQGIS LSKLGGGIGS RGPGESKLEM DKRHIREKMH DIKAQLTHVE QHRKRIIERR NTQSVFRFGL IGYTNAGKST IFNRLTNETT LQENKLFATL DPTTRKVRFS GGFQTLLTDT VGFIQDLPTT LIAAFRSTLE ETANVDVLIH VVDASNPDYL QHETTVISLL EELEMNHLPT LVIYNKMDHA PATFVPDQPE SLLISALDQE APDTIKQRMI QLIEKNWAFF TIELSEEKGK ELAQIKQQAW VTKLEYIESK QSYHIEGYKP RKELNNE // ID Q8Y8Y0_LISMO Unreviewed; 418 AA. AC Q8Y8Y0; DT 01-MAR-2002, integrated into UniProtKB/TrEMBL. DT 01-MAR-2002, sequence version 1. DT 07-JUN-2017, entry version 93. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=lmo0762 {ECO:0000313|EMBL:CAC98840.1}; OS Listeria monocytogenes serovar 1/2a (strain ATCC BAA-679 / EGD-e). OC Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria. OX NCBI_TaxID=169963 {ECO:0000313|EMBL:CAC98840.1, ECO:0000313|Proteomes:UP000000817}; RN [1] {ECO:0000313|EMBL:CAC98840.1, ECO:0000313|Proteomes:UP000000817} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-679 / EGD-e {ECO:0000313|Proteomes:UP000000817}; RX PubMed=11679669; DOI=10.1126/science.1063447; RA Glaser P., Frangeul L., Buchrieser C., Rusniok C., Amend A., RA Baquero F., Berche P., Bloecker H., Brandt P., Chakraborty T., RA Charbit A., Chetouani F., Couve E., de Daruvar A., Dehoux P., RA Domann E., Dominguez-Bernal G., Duchaud E., Durant L., Dussurget O., RA Entian K.D., Fsihi H., Portillo F.G., Garrido P., Gautier L., RA Goebel W., Gomez-Lopez N., Hain T., Hauf J., Jackson D., Jones L.M., RA Kaerst U., Kreft J., Kuhn M., Kunst F., Kurapkat G., Madueno E., RA Maitournam A., Vicente J.M., Ng E., Nedjari H., Nordsiek G., RA Novella S., de Pablos B., Perez-Diaz J.C., Purcell R., Remmel B., RA Rose M., Schlueter T., Simoes N., Tierrez A., Vazquez-Boland J.A., RA Voss H., Wehland J., Cossart P.; RT "Comparative genomics of Listeria species."; RL Science 294:849-852(2001). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AL591976; CAC98840.1; -; Genomic_DNA. DR PIR; AB1170; AB1170. DR RefSeq; NP_464289.1; NC_003210.1. DR RefSeq; WP_003721879.1; NC_003210.1. DR ProteinModelPortal; Q8Y8Y0; -. DR STRING; 169963.lmo0762; -. DR PaxDb; Q8Y8Y0; -. DR EnsemblBacteria; CAC98840; CAC98840; CAC98840. DR GeneID; 985496; -. DR KEGG; lmo:lmo0762; -. DR PATRIC; fig|169963.11.peg.785; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; FNNHAHV; -. DR PhylomeDB; Q8Y8Y0; -. DR Proteomes; UP000000817; Chromosome. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0043022; F:ribosome binding; IBA:GO_Central. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000000817}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000000817}. FT DOMAIN 194 363 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 418 AA; 47550 MW; 3C7E3A0860E87717 CRC64; MEKKVLIVGI SQKQKDFDYS MEELANLAAA NNMEVVGEIR QNIDRENRAT YVGKGKVDEI KGLAEMQDAR LIIFNDELSP SQIRNLEEAL ELDVMDRTGL ILAIFANRAK TKEAQLQVQI AKLQYELPRI FGQGEDMDQQ SGKGGLSNRG SGEKKIETDR RTIKHQIRHL QKELDMLVDD REVRRRKRKK NEIPVVSLVG YTNAGKSTTM NGLVRAYSET ADKQVFEKDM LFATLETSVR EIVLPDNKQF LLTDTVGFVS KLPHQLVKAF RSTLEEARDA DLLIHVVDYS DPHYKTMMKT TEETLKVVGV EDVPVIYAYN KADLLEDEMY PKQTGNTIIF SAREEESLEF LTEVIRKELF ASYEKATFLI PFEAGQVVAY LNEHADILET EYLENGTQIV AEVSPADLQK LAEYQVAE // ID Q8YQG9_NOSS1 Unreviewed; 528 AA. AC Q8YQG9; DT 01-MAR-2002, integrated into UniProtKB/TrEMBL. DT 01-MAR-2002, sequence version 1. DT 07-JUN-2017, entry version 89. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=all3862 {ECO:0000313|EMBL:BAB75561.1}; OS Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576). OC Bacteria; Cyanobacteria; Nostocales; Nostocaceae; Nostoc. OX NCBI_TaxID=103690 {ECO:0000313|EMBL:BAB75561.1, ECO:0000313|Proteomes:UP000002483}; RN [1] {ECO:0000313|EMBL:BAB75561.1, ECO:0000313|Proteomes:UP000002483} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=PCC 7120 / SAG 25.82 / UTEX 2576 RC {ECO:0000313|Proteomes:UP000002483}; RX PubMed=11759840; DOI=10.1093/dnares/8.5.205; RA Kaneko T., Nakamura Y., Wolk C.P., Kuritz T., Sasamoto S., RA Watanabe A., Iriguchi M., Ishikawa A., Kawashima K., Kimura T., RA Kishida Y., Kohara M., Matsumoto M., Matsuno A., Muraki A., RA Nakazaki N., Shimpo S., Sugimoto M., Takazawa M., Yamada M., RA Yasuda M., Tabata S.; RT "Complete genomic sequence of the filamentous nitrogen-fixing RT cyanobacterium Anabaena sp. strain PCC 7120."; RL DNA Res. 8:205-213(2001). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BA000019; BAB75561.1; -; Genomic_DNA. DR PIR; AG2288; AG2288. DR RefSeq; WP_010998003.1; NC_003272.1. DR ProteinModelPortal; Q8YQG9; -. DR STRING; 103690.all3862; -. DR EnsemblBacteria; BAB75561; BAB75561; BAB75561. DR KEGG; ana:all3862; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; EREVIIT; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000002483; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000002483}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000002483}. FT DOMAIN 355 525 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 314 348 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 528 AA; 57934 MW; 40E17A8EAEA1D0A0 CRC64; MCAYVNRRGQ VIRVGVGTPR QTQIPPMELP RYGAERLSGI RCIATHLKTE PPNEAALTAM AMQRLDALVV INITGTGFTR RGGGATGYVK EAYLAHLVPQ DANALIPSGA IASSNNGQSP SWNISPPLDL DDLGQQDFID LVEGLEAEFS REFIAEEVDA DHDRVLIVGV MTDKMSLQQF HDTLVELARL VDTAGGEVLQ TVQQKRSRIH PQTVIGEGKV QEVALTAQTL GCNLVVFDRD LSPSQIRNLE AQIGLRVVDR TEVILDIFAQ RAQSRAGKLQ VELAQLEYML PRLTGRGQAM SRLGGGIGTR GPGETKLETE RRAIQKRISR LQQEVDQLQA HRSRLRQRRQ HREVPSVALV GYTNAGKSTL LNALTNAEVY TADQLFATLD PTTRRLVIPH AETGEPQGIL ITDTVGFIHE LPASLMDAFR ATLEEVTEAD ALLHLVDLSH PAWLSHIRAV REILAQMPVT PGPALVAFNK IDQVDSATLA LAQEEFPLAV FISASQRLGL ETLRLRLSLL IQYAVDSQ // ID Q8ZKA5_SALTY Unreviewed; 426 AA. AC Q8ZKA5; DT 01-MAR-2002, integrated into UniProtKB/TrEMBL. DT 01-MAR-2002, sequence version 1. DT 30-AUG-2017, entry version 101. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:AAL23182.1}; GN OrderedLocusNames=STM4362 {ECO:0000313|EMBL:AAL23182.1}; OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; OC Enterobacteriaceae; Salmonella. OX NCBI_TaxID=99287 {ECO:0000313|EMBL:AAL23182.1, ECO:0000313|Proteomes:UP000001014}; RN [1] {ECO:0000313|EMBL:AAL23182.1, ECO:0000313|Proteomes:UP000001014} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=LT2 / SGSC1412 / ATCC 700720 RC {ECO:0000313|Proteomes:UP000001014}; RX PubMed=11677609; DOI=10.1038/35101614; RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P., RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D., RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E., RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., RA Waterston R., Wilson R.K.; RT "Complete genome sequence of Salmonella enterica serovar Typhimurium RT LT2."; RL Nature 413:852-856(2001). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE006468; AAL23182.1; -; Genomic_DNA. DR RefSeq; NP_463223.1; NC_003197.2. DR RefSeq; WP_000460338.1; NC_003197.2. DR ProteinModelPortal; Q8ZKA5; -. DR STRING; 99287.STM4362; -. DR PaxDb; Q8ZKA5; -. DR PRIDE; Q8ZKA5; -. DR DNASU; 1255888; -. DR EnsemblBacteria; AAL23182; AAL23182; STM4362. DR GeneID; 1255888; -. DR KEGG; stm:STM4362; -. DR PATRIC; fig|99287.12.peg.4586; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR KO; K03665; -. DR OMA; HPATYIG; -. DR PhylomeDB; Q8ZKA5; -. DR Proteomes; UP000001014; Chromosome. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0043022; F:ribosome binding; IBA:GO_Central. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000001014}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000001014}. FT DOMAIN 198 365 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 164 191 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 426 AA; 48262 MW; 229CAE358920A78F CRC64; MFDRYDAGEQ AVLVHIYFSQ DKDMEDLQEF ESLVSSAGVE AMQVITGSRK APHPKYFVGE GKAVEIAEAV KATGAAVVLF DHALSPAQER NLERLCECRV IDRTGLILDI FAQRARTHEG KLQVELAQLR HLATRLVRGW THLERQKGGI GLRGPGETQL ETDRRLLRNR IVQIQSRLEK VEKQREQGRQ SRIKADVPTV SLVGYTNAGK STLFNQITEA RVYAADQLFA TLDPTLRRID VADVGETVLA DTVGFIRHLP HDLVAAFKAT LQETRQATLL LHVVDAADVR VQENIEAVNT VLEEIDAHEI PTLMVMNKID MLDDFEPRID RDEENKPIRV WLSAQSGVGI PQLFQALTER LSGEVAQHTL RLPPQEGRLR SRFYQLQAIE KEWMEEDGSV SLQVRMPIVD WRRLCKQEPA LIEYVI // ID Q8ZYG9_PYRAE Unreviewed; 386 AA. AC Q8ZYG9; DT 01-MAR-2002, integrated into UniProtKB/TrEMBL. DT 01-MAR-2002, sequence version 1. DT 07-JUN-2017, entry version 95. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=PAE0782 {ECO:0000313|EMBL:AAL63024.1}; OS Pyrobaculum aerophilum (strain ATCC 51768 / IM2 / DSM 7523 / JCM 9630 OS / NBRC 100827). OC Archaea; Crenarchaeota; Thermoprotei; Thermoproteales; OC Thermoproteaceae; Pyrobaculum. OX NCBI_TaxID=178306 {ECO:0000313|EMBL:AAL63024.1, ECO:0000313|Proteomes:UP000002439}; RN [1] {ECO:0000313|EMBL:AAL63024.1, ECO:0000313|Proteomes:UP000002439} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51768 / IM2 / DSM 7523 / JCM 9630 / NBRC 100827 RC {ECO:0000313|Proteomes:UP000002439}; RX PubMed=11792869; DOI=10.1073/pnas.241636498; RA Fitz-Gibbon S.T., Ladner H., Kim U.J., Stetter K.O., Simon M.I., RA Miller J.H.; RT "Genome sequence of the hyperthermophilic crenarchaeon Pyrobaculum RT aerophilum."; RL Proc. Natl. Acad. Sci. U.S.A. 99:984-989(2002). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE009441; AAL63024.1; -; Genomic_DNA. DR ProteinModelPortal; Q8ZYG9; -. DR STRING; 178306.PAE0782; -. DR EnsemblBacteria; AAL63024; AAL63024; PAE0782. DR KEGG; pai:PAE0782; -. DR PATRIC; fig|178306.9.peg.571; -. DR eggNOG; arCOG00353; Archaea. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR InParanoid; Q8ZYG9; -. DR KO; K03665; -. DR OMA; FNNHAHV; -. DR OrthoDB; POG093Z07D6; -. DR Proteomes; UP000002439; Chromosome. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0043022; F:ribosome binding; IBA:GO_Central. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000002439}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000002439}. FT DOMAIN 186 352 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 386 AA; 43824 MW; D6B7186CB92FCA1A CRC64; MRNKALLAYV GPKTPNLGYK LEEFLSLVEV AGFEVAEVVT QFGRADTRFY LGSGKAKEIA NKDFDVFVAY HSLTPLQVFN LERLFRRKVI DRVFVILMIF DKRAGSLESK LQIELARLRY ELPKVKEYLR RAKMGEQLGF MGAGEYVIDA YYRHMVRRIS TIRRKLEEIK RGRAMHIMKR KEKGVPEVVL TGYTSAGKTT LFNSLVNENK LVDGRPFATL ETYSRALDLW GKRIVLTDTI GFIDDLPPLL IESFYSTLQE IIDADRILLV IDGSEPLEEI TRKVETSVKT LGEVGIGRER IIPVLNKVDK ISVEKVRDIR RGLEKYFTWF VPVSALTGFG IEALKAVLFL QVPGYDIIKA SANSGAKGLR IGDVVLVPIL RNNRES // ID Q92Q83_RHIME Unreviewed; 465 AA. AC Q92Q83; DT 01-DEC-2001, integrated into UniProtKB/TrEMBL. DT 01-DEC-2001, sequence version 1. DT 07-JUN-2017, entry version 98. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:CAC46044.1}; GN ORFNames=SMc01049 {ECO:0000313|EMBL:CAC46044.1}; OS Rhizobium meliloti (strain 1021) (Ensifer meliloti) (Sinorhizobium OS meliloti). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium. OX NCBI_TaxID=266834 {ECO:0000313|EMBL:CAC46044.1, ECO:0000313|Proteomes:UP000001976}; RN [1] {ECO:0000313|EMBL:CAC46044.1, ECO:0000313|Proteomes:UP000001976} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=1021 {ECO:0000313|EMBL:CAC46044.1, RC ECO:0000313|Proteomes:UP000001976}; RX PubMed=11481430; DOI=10.1073/pnas.161294398; RA Capela D., Barloy-Hubler F., Gouzy J., Bothe G., Ampe F., Batut J., RA Boistard P., Becker A., Boutry M., Cadieu E., Dreano S., Gloux S., RA Godrie T., Goffeau A., Kahn D., Kiss E., Lelaure V., Masuy D., RA Pohl T., Portetelle D., Puehler A., Purnelle B., Ramsperger U., RA Renard C., Thebault P., Vandenbol M., Weidner S., Galibert F.; RT "Analysis of the chromosome sequence of the legume symbiont RT Sinorhizobium meliloti strain 1021."; RL Proc. Natl. Acad. Sci. U.S.A. 98:9877-9882(2001). RN [2] {ECO:0000313|Proteomes:UP000001976} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=1021 {ECO:0000313|Proteomes:UP000001976}; RX PubMed=11474104; DOI=10.1126/science.1060966; RA Galibert F., Finan T.M., Long S.R., Puehler A., Abola P., Ampe F., RA Barloy-Hubler F., Barnett M.J., Becker A., Boistard P., Bothe G., RA Boutry M., Bowser L., Buhrmester J., Cadieu E., Capela D., Chain P., RA Cowie A., Davis R.W., Dreano S., Federspiel N.A., Fisher R.F., RA Gloux S., Godrie T., Goffeau A., Golding B., Gouzy J., Gurjal M., RA Hernandez-Lucas I., Hong A., Huizar L., Hyman R.W., Jones T., Kahn D., RA Kahn M.L., Kalman S., Keating D.H., Kiss E., Komp C., Lelaure V., RA Masuy D., Palm C., Peck M.C., Pohl T.M., Portetelle D., Purnelle B., RA Ramsperger U., Surzycki R., Thebault P., Vandenbol M., RA Vorhoelter F.J., Weidner S., Wells D.H., Wong K., Yeh K.-C., Batut J.; RT "The composite genome of the legume symbiont Sinorhizobium meliloti."; RL Science 293:668-672(2001). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AL591688; CAC46044.1; -; Genomic_DNA. DR RefSeq; NP_385571.1; NC_003047.1. DR RefSeq; WP_003535430.1; NC_003047.1. DR ProteinModelPortal; Q92Q83; -. DR STRING; 266834.SMc01049; -. DR EnsemblBacteria; CAC46044; CAC46044; SMc01049. DR GeneID; 1233118; -. DR KEGG; sme:SMc01049; -. DR PATRIC; fig|266834.11.peg.2884; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR Proteomes; UP000001976; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000001976}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000001976}. FT DOMAIN 229 401 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 188 222 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 465 AA; 51439 MW; B2FC26A6B70BB6B3 CRC64; MRNITKRDSK SSSIIPELER LRDDSRAVVV VPILKKTGKA SADIVAQPAT RSDESRLEEA TGLALAIDLD VVHGMIVSVA QPKPGTLLGT GKIEEIGHVL SEKDAGLVIV DHPLTPVQQR NLEKEWNAKV IDRTGLILEI FGRRASTREG TLQVDLAHLN YQKGRLVRSW THLERQRGGA GFMGGPGETQ IEADRRLLQD RIVKLERELE QVRRTRQLHR SKRKKVPHPI VALVGYTNAG KSTLFNRMTG AGVLAEDMLF ATLDPTLRRL KLPHGRMVIL SDTVGFISDL PTHLVAAFRA TLEEVLEADL VLHVRDLSDP DNQAQASDVL RILADLGIDE KEGAERIVEV WNKIDKVEPE VREALVKKAA SADNTVAVSA MTGEGVDDLL TEIGRRLSGV MTECTVVLGL DQLQLLPWVY QHAIVDGRED LEDGRVSLDL RLTEGEATEL ERRLGNGPKA VEEDW // ID Q975U0_SULTO Unreviewed; 350 AA. AC Q975U0; DT 01-DEC-2001, integrated into UniProtKB/TrEMBL. DT 01-DEC-2001, sequence version 1. DT 07-JUN-2017, entry version 97. DE SubName: Full=GTPase HflX {ECO:0000313|EMBL:BAB65309.1}; GN Name=hflX {ECO:0000313|EMBL:BAB65309.1}; GN Synonyms=ST0332 {ECO:0000313|EMBL:BAB65309.1}; GN OrderedLocusNames=STK_03320 {ECO:0000313|EMBL:BAB65309.1}; OS Sulfolobus tokodaii (strain DSM 16993 / JCM 10545 / NBRC 100140 / 7). OC Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae; OC Sulfolobus. OX NCBI_TaxID=273063 {ECO:0000313|EMBL:BAB65309.1, ECO:0000313|Proteomes:UP000001015}; RN [1] {ECO:0000313|Proteomes:UP000001015} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 16993 / JCM 10545 / NBRC 100140 / 7 RC {ECO:0000313|Proteomes:UP000001015}; RX PubMed=11572479; DOI=10.1093/dnares/8.4.123; RA Kawarabayasi Y., Hino Y., Horikawa H., Jin-no K., Takahashi M., RA Sekine M., Baba S., Ankai A., Kosugi H., Hosoyama A., Fukui S., RA Nagai Y., Nishijima K., Otsuka R., Nakazawa H., Takamiya M., Kato Y., RA Yoshizawa T., Tanaka T., Kudoh Y., Yamazaki J., Kushida N., Oguchi A., RA Aoki K., Masuda S., Yanagii M., Nishimura M., Yamagishi A., Oshima T., RA Kikuchi H.; RT "Complete genome sequence of an aerobic thermoacidophilic RT Crenarchaeon, Sulfolobus tokodaii strain7."; RL DNA Res. 8:123-140(2001). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BA000023; BAB65309.1; -; Genomic_DNA. DR RefSeq; WP_010978292.1; NC_003106.2. DR ProteinModelPortal; Q975U0; -. DR STRING; 273063.ST0332; -. DR EnsemblBacteria; BAB65309; BAB65309; STK_03320. DR GeneID; 1458246; -. DR KEGG; sto:STK_03320; -. DR PATRIC; fig|273063.9.peg.388; -. DR eggNOG; arCOG00353; Archaea. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG093Z07D6; -. DR Proteomes; UP000001015; Chromosome. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR CDD; cd01878; HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 4: Predicted; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000001015}; KW Reference proteome {ECO:0000313|Proteomes:UP000001015}. FT DOMAIN 176 350 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 145 176 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 350 AA; 39676 MW; 352AD6F757B7B87E CRC64; MKAILFTAEE YKDEALSLAE TAFYEITKIY KIPKKPNPNF YIQKDKVEEI KKLNDIDAII IFDLLKSRHF INLNKELLGK KILDKVILLL EIFALHAGSK EAKLQIELAK LKYELPILKD MYKKTKITEQ QGPLGAGVYG VESTIRLYQR RIVKIRKELE EIKKAKEDQV RRVNFNSIAI VGYTNAGKTT IFNYLTGLNQ KVDSSMFTTT SPKRYAIPID GKKIMLVDTV GFIRGIPPQI IEAFFVTLSE AKYANALLLV LDSSLSSTLL IEMLQSSLEI LRELGISGKP MIIVLNKIDK NNEEKEVEEK VSLVKELANS LYTPIIDVIP VSALKGINMN ILRDKILALI // ID Q97GR7_CLOAB Unreviewed; 593 AA. AC Q97GR7; DT 01-OCT-2001, integrated into UniProtKB/TrEMBL. DT 01-OCT-2001, sequence version 1. DT 07-JUN-2017, entry version 98. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:AAK80255.1}; GN OrderedLocusNames=CA_C2299 {ECO:0000313|EMBL:AAK80255.1}; OS Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG OS 5710 / VKM B-1787). OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=272562 {ECO:0000313|EMBL:AAK80255.1, ECO:0000313|Proteomes:UP000000814}; RN [1] {ECO:0000313|EMBL:AAK80255.1, ECO:0000313|Proteomes:UP000000814} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787 RC {ECO:0000313|Proteomes:UP000000814}; RX PubMed=11466286; DOI=10.1128/JB.183.16.4823-4838.2001; RA Nolling J., Breton G., Omelchenko M.V., Makarova K.S., Zeng Q., RA Gibson R., Lee H.M., Dubois J., Qiu D., Hitti J., Wolf Y.I., RA Tatusov R.L., Sabathe F., Doucette-Stamm L., Soucaille P., Daly M.J., RA Bennett G.N., Koonin E.V., Smith D.R.; RT "Genome sequence and comparative analysis of the solvent-producing RT bacterium Clostridium acetobutylicum."; RL J. Bacteriol. 183:4823-4838(2001). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE001437; AAK80255.1; -; Genomic_DNA. DR PIR; D97183; D97183. DR RefSeq; NP_348915.1; NC_003030.1. DR RefSeq; WP_010965596.1; NC_003030.1. DR ProteinModelPortal; Q97GR7; -. DR STRING; 272562.CA_C2299; -. DR EnsemblBacteria; AAK80255; AAK80255; CA_C2299. DR GeneID; 1118482; -. DR KEGG; cac:CA_C2299; -. DR PATRIC; fig|272562.8.peg.2496; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; FNNHAHV; -. DR Proteomes; UP000000814; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000000814}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000000814}. FT DOMAIN 363 540 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 593 AA; 66483 MW; 8D351FC1B4A04287 CRC64; MISGNVQGVK NSLLNELEKL YDMYSKENIF TAELIKLICS VTNIIEREIS VGINRKGKVV SVSIGDARSV ETPVFDFKEK RLSGIRIIHT HPSGNPELSD IDISSLLNSR LDSIVAVGTV DGKVTGVTIG FCDVEDNSII PKIVKTASFE EALNYKFMDE INYAEEHMDK LELDYDDSER AIIVGVDTLE SLDELKELAD ACGVLTAEKV IQKKEKIDNA YFIGKGKVDE IRLLAQQCRA NIIVFDDELS GAQVRNLEEA IGLKVIDRTT LILEIFARRA GSKEAKLQVE LAQLKYRLPR LMGLGKVLSR TGAGIGTKGP GEKKLEVDRR HINERVYEIQ KELKKIKKTR QVQRERRVSE NLPCISLVGY TNAGKSTLRN AICEIAAPLD NLGKENVLEK DMLFATLDVT TRAIKLEDGR KAVLTDTVGF VRKLPHDLVE AFKSTLEEVI YSDLLVHVVD ASSDTFLQQI EAVNGVLEEL GANDKTQILV LNKIDKISEE ELLKIEESIK EKELVKISAK QKINLDLLMN KIAEKIPSSI REVEYLVPYS DQKVAAYIHE TSVVKKEEFE NEGTHIVAIV DNEVYNRCKE YMM // ID Q98MX1_RHILO Unreviewed; 431 AA. AC Q98MX1; DT 01-OCT-2001, integrated into UniProtKB/TrEMBL. DT 01-OCT-2001, sequence version 1. DT 07-JUN-2017, entry version 90. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=mlr0403 {ECO:0000313|EMBL:BAB47992.1}; OS Rhizobium loti (strain MAFF303099) (Mesorhizobium loti). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Phyllobacteriaceae; Mesorhizobium. OX NCBI_TaxID=266835 {ECO:0000313|EMBL:BAB47992.1, ECO:0000313|Proteomes:UP000000552}; RN [1] {ECO:0000313|EMBL:BAB47992.1, ECO:0000313|Proteomes:UP000000552} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MAFF303099 {ECO:0000313|EMBL:BAB47992.1, RC ECO:0000313|Proteomes:UP000000552}; RX PubMed=11214968; DOI=10.1093/dnares/7.6.331; RA Kaneko T., Nakamura Y., Sato S., Asamizu E., Kato T., Sasamoto S., RA Watanabe A., Idesawa K., Ishikawa A., Kawashima K., Kimura T., RA Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., RA Mochizuki Y., Nakayama S., Nakazaki N., Shimpo S., Sugimoto M., RA Takeuchi C., Yamada M., Tabata S.; RT "Complete genome structure of the nitrogen-fixing symbiotic bacterium RT Mesorhizobium loti."; RL DNA Res. 7:331-338(2000). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BA000012; BAB47992.1; -; Genomic_DNA. DR ProteinModelPortal; Q98MX1; -. DR STRING; 266835.mlr0403; -. DR EnsemblBacteria; BAB47992; BAB47992; BAB47992. DR KEGG; mlo:mlr0403; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000000552; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000000552}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000000552}. FT DOMAIN 199 372 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 158 185 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 431 AA; 47583 MW; 098A677BC9B73961 CRC64; MPVLTRQPRG DDDTNRPRLT RSADARHDEA VGLARAINLD PVHTAVVTVN DPRPATLLGS GKVEEFAQIV KDNDAELVIV DHPLTPVQQR NLEKELHAKV LDRTGLILEI FGERARTKEG TLQVELAHLN YQKGRLVRSW THLERQRGGA GFLGGPGETQ IESDRRQLQE KIIKLKHELE TVRRTRDLHR AKRKKVPFPV VAIVGYTNAG KSTLFNRLTG ADVLAQDMLF ATLDPTLRRV RLPHGTPIIL SDTVGFISDL PTHLIAAFRA TLEEVVEADL VIHLRDISDP DTAAQAEDVE RILADLGVDA GDTKRVIEVW NKVDLLDEGN RSRLLADAVD GSKGPPIAIS AVTGEGIEAL KAVIETRMAG ELEDLTVTIE PAQFGLVDWL YRNGDIVSRA DNEDGSATIS LKATQSAREE IESRLRRKNN G // ID Q9A058_STRP1 Unreviewed; 412 AA. AC Q9A058; Q48Z77; DT 01-JUN-2001, integrated into UniProtKB/TrEMBL. DT 01-JUN-2001, sequence version 1. DT 07-JUN-2017, entry version 104. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=SPy_0922 {ECO:0000313|EMBL:AAK33837.1}; OS Streptococcus pyogenes serotype M1. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=301447 {ECO:0000313|Proteomes:UP000000750}; RN [1] {ECO:0000313|EMBL:AAK33837.1, ECO:0000313|Proteomes:UP000000750} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700294 / SF370 / Serotype M1 RC {ECO:0000313|Proteomes:UP000000750}; RX PubMed=11296296; DOI=10.1073/pnas.071559398; RA Ferretti J.J., McShan W.M., Adjic D., Savic D., Savic G., Lyon K., RA Primeaux C., Sezate S.S., Surorov A.N., Kenton S., Lai H., Lin S., RA Qian Y., Jia H.G., Najar F.Z., Ren Q., Zhu H., Song L., White J., RA Yuan X., Clifton S.W., Roe B.A., McLaughlin R.E.; RT "Complete genome sequence of an M1 strain of Streptococcus pyogenes."; RL Proc. Natl. Acad. Sci. U.S.A. 98:4658-4663(2001). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE004092; AAK33837.1; -; Genomic_DNA. DR RefSeq; NP_269116.1; NC_002737.2. DR ProteinModelPortal; Q9A058; -. DR STRING; 160490.SPy_0922; -. DR PaxDb; Q9A058; -. DR PRIDE; Q9A058; -. DR EnsemblBacteria; AAK33837; AAK33837; SPy_0922. DR GeneID; 901075; -. DR KEGG; spy:SPy_0922; -. DR PATRIC; fig|160490.10.peg.793; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR Proteomes; UP000000750; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000000750}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000000750}. FT DOMAIN 199 359 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 158 192 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 412 AA; 47183 MW; D63EB6C1588CA4B8 CRC64; MIETKRQQER VILLGVELQT TEHFDMSMTE LANLAKTAGV KVMASFSQKR ERYDSKTFIG SGKLDEIKAI VEADEIDAVI VNNRLTARQN ANLEAVLEVK VIDRMQLILD IFAMRARSHE GKLQVHLAQL KYMLPRLVGQ GIMLSRQAGG IGSRGPGESQ LELNRRSIRH QIADIERQLT QVEKNRQTIR DRRVGSDTFK IGLIGYTNAG KSTIMNLLTD DSHYEANELF ATLDATTKQL YLENQFQATL TDTVGFIQDL PTELVAAFKS TLEESKYVDL LLHVIDASDP NHSEQEKVVL NLLKELDMLN IPRLAIYNKV DIAEQFTATA FPNIRISARS KDSKILLRRL IIDQIRDQFV PFRIKVHQDK AYKLYDLNRV ALLDHYTFDQ EIEDISGYIS PKQQWRLDDF YE // ID Q9A7H7_CAUCR Unreviewed; 427 AA. AC Q9A7H7; DT 01-JUN-2001, integrated into UniProtKB/TrEMBL. DT 01-JUN-2001, sequence version 1. DT 30-AUG-2017, entry version 93. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=CC_1746 {ECO:0000313|EMBL:AAK23722.1}; OS Caulobacter crescentus (strain ATCC 19089 / CB15). OC Bacteria; Proteobacteria; Alphaproteobacteria; Caulobacterales; OC Caulobacteraceae; Caulobacter. OX NCBI_TaxID=190650 {ECO:0000313|EMBL:AAK23722.1, ECO:0000313|Proteomes:UP000001816}; RN [1] {ECO:0000313|EMBL:AAK23722.1, ECO:0000313|Proteomes:UP000001816} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 19089 / CB15 {ECO:0000313|Proteomes:UP000001816}; RX PubMed=11259647; DOI=10.1073/pnas.061029298; RA Nierman W.C., Feldblyum T.V., Laub M.T., Paulsen I.T., Nelson K.E., RA Eisen J.A., Heidelberg J.F., Alley M.R., Ohta N., Maddock J.R., RA Potocka I., Nelson W.C., Newton A., Stephens C., Phadke N.D., Ely B., RA DeBoy R.T., Dodson R.J., Durkin A.S., Gwinn M.L., Haft D.H., RA Kolonay J.F., Smit J., Craven M.B., Khouri H., Shetty J., Berry K., RA Utterback T., Tran K., Wolf A., Vamathevan J., Ermolaeva M., White O., RA Salzberg S.L., Venter J.C., Shapiro L., Fraser C.M.; RT "Complete genome sequence of Caulobacter crescentus."; RL Proc. Natl. Acad. Sci. U.S.A. 98:4136-4141(2001). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE005673; AAK23722.1; -; Genomic_DNA. DR PIR; F87465; F87465. DR RefSeq; NP_420554.1; NC_002696.2. DR RefSeq; WP_010919614.1; NC_002696.2. DR ProteinModelPortal; Q9A7H7; -. DR STRING; 190650.CC_1746; -. DR EnsemblBacteria; AAK23722; AAK23722; CC_1746. DR GeneID; 942104; -. DR KEGG; ccr:CC_1746; -. DR PATRIC; fig|190650.5.peg.1770; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR BioCyc; CAULO:CC1746-MONOMER; -. DR Proteomes; UP000001816; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000001816}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000001816}. FT DOMAIN 195 365 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 427 AA; 46896 MW; 07309F6047921432 CRC64; MIHPARPLRG QAALEARDPN ARLEEAVGLA VALDLNVVEA LVAPLRVVTP ATLFGKGKVE EFAAICEVEH IDVAVFDDQL TPIQQRNLEK ALKVKVVDRT GLILEIFARR ARTREGRLQV ELARLDYERS RLVRTWTHLE RQRGGTGSTG GPGETQIEID RRLIAGTILK LKKELEEVRR TRTLHRSARK KVPYPTVALV GYTNAGKSTL FNRLTEAEVL AKDMLFATLD PTLRTVKLPD GRPAIMSDTV GFISDLPHEL VEAFRATLEE VQEADVVLHV RDVANPDSEA QARDVETVLA ELGVTLDEGK TVVEVWNKVD LLSEDDREIV EGQARRNDAS AVSAVTGEGC EALLRRIAGL IDDSPPVEVS LAAQDGQALA WIYRNGRVLS RYDGPGGEVT LVARLDAQAL GRFERQFPGA QVSAAVD // ID Q9CCC0_MYCLE Unreviewed; 488 AA. AC Q9CCC0; DT 01-JUN-2001, integrated into UniProtKB/TrEMBL. DT 01-JUN-2001, sequence version 1. DT 07-JUN-2017, entry version 90. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=ML0997 {ECO:0000313|EMBL:CAC31378.1}; OS Mycobacterium leprae (strain TN). OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae; OC Mycobacterium. OX NCBI_TaxID=272631 {ECO:0000313|Proteomes:UP000000806}; RN [1] {ECO:0000313|EMBL:CAC31378.1, ECO:0000313|Proteomes:UP000000806} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=TN {ECO:0000313|EMBL:CAC31378.1, RC ECO:0000313|Proteomes:UP000000806}; RX PubMed=11234002; DOI=10.1038/35059006; RA Cole S.T., Eiglmeier K., Parkhill J., James K.D., Thomson N.R., RA Wheeler P.R., Honore N., Garnier T., Churcher C.M., Harris D.E., RA Mungall K.L., Basham D., Brown D., Chillingworth T., Connor R., RA Davies R.M., Devlin K., Duthoy S., Feltwell T., Fraser A., Hamlin N., RA Holroyd S., Hornsby T., Jagels K., Lacroix C., Maclean J., Moule S., RA Murphy L.D., Oliver K., Quail M.A., Rajandream M.A., Rutherford K.M., RA Rutter S., Seeger K., Simon S., Simmonds M., Skelton J., Squares R., RA Squares S., Stevens K., Taylor K., Whitehead S., Woodward J.R., RA Barrell B.G.; RT "Massive gene decay in the leprosy bacillus."; RL Nature 409:1007-1011(2001). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AL583920; CAC31378.1; -; Genomic_DNA. DR PIR; G87033; G87033. DR RefSeq; NP_301739.1; NC_002677.1. DR RefSeq; WP_010908063.1; NC_002677.1. DR ProteinModelPortal; Q9CCC0; -. DR STRING; 272631.ML0997; -. DR EnsemblBacteria; CAC31378; CAC31378; CAC31378. DR GeneID; 910021; -. DR KEGG; mle:ML0997; -. DR PATRIC; fig|272631.5.peg.1805; -. DR Leproma; ML0997; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000000806; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000000806}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000000806}. FT DOMAIN 261 433 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 488 AA; 52801 MW; 188918856F9774AA CRC64; MKYPDSSDRG SADFPDLWDS SDSVPSTGEL ALHDRLALRR IAGLSTELAD VSEVEYRQLR LERVVLVGVW TEGSAADNQA SMAELATLAE TAGSQVLEGL IQRRDRPDPS TYIGSGKAAE LREVVLATGA DTVICDGELS PAQLTALEKA VKVKVIDRTA LILDIFAQHA TSREGKAQVL LAQMAYMLPR LRGWGESMSR QVGGRAGGSG GGVGLRGPGE TKIETDRRRI RERMAKLRRD IGAMKQARDT QRSRRLHSDI PSIAIVGYTN AGKSSVLNAL TGAWVLVQDA LFVTLEPTTR HAEFDNGQPF VFTDTVGFVR HLPTQLVEAF RSTLEEVVDA DLLLHVVDGS DANPLAQINA VRQVIFEVIS DHQDGGVEVP HELLVVNKID AASALMLAKL RHGLPGAVFI SARTGDGIDV LRRRIAELVV ATDTAVDVVI PYDRGDLVAR LHANGRVQQA EHNSNGTRIK ARVPVALAAC LQEFSADR // ID Q9CIY3_LACLA Unreviewed; 386 AA. AC Q9CIY3; DT 01-JUN-2001, integrated into UniProtKB/TrEMBL. DT 01-JUN-2001, sequence version 1. DT 07-JUN-2017, entry version 90. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:AAK04321.1}; GN ORFNames=L0162 {ECO:0000313|EMBL:AAK04321.1}; OS Lactococcus lactis subsp. lactis (strain IL1403) (Streptococcus OS lactis). OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Lactococcus. OX NCBI_TaxID=272623 {ECO:0000313|EMBL:AAK04321.1, ECO:0000313|Proteomes:UP000002196}; RN [1] {ECO:0000313|EMBL:AAK04321.1, ECO:0000313|Proteomes:UP000002196} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=IL1403 {ECO:0000313|EMBL:AAK04321.1, RC ECO:0000313|Proteomes:UP000002196}; RX PubMed=11337471; DOI=10.1101/gr.GR-1697R; RA Bolotin A., Wincker P., Mauger S., Jaillon O., Malarme K., RA Weissenbach J., Ehrlich S.D., Sorokin A.; RT "The complete genome sequence of the lactic acid bacterium Lactococcus RT lactis ssp. lactis IL1403."; RL Genome Res. 11:731-753(2001). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE005176; AAK04321.1; -; Genomic_DNA. DR PIR; G86652; G86652. DR ProteinModelPortal; Q9CIY3; -. DR STRING; 272623.L0162; -. DR PaxDb; Q9CIY3; -. DR EnsemblBacteria; AAK04321; AAK04321; L0162. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR OMA; HPATYIG; -. DR Proteomes; UP000002196; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000002196}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000002196}. FT DOMAIN 172 335 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 145 168 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 386 AA; 43451 MW; 94D6DD90D1FAEA3A CRC64; MIELAELTKT AGGLVIDQFT QKRERPDSRT MIGSGKLEQM RWAIEVGEID TVIFNDRLSP RQNVNLEEAL GVKVIDRMQL ILDIFAMRAR SHEGMLQVEE AQLNYLLPRL VGQGIMLSRQ GGGIGSKGPG ETKLETDRRY IRTRIENIDK ALKKVEKTRE NIRQKRSKSG IFRIGLIGYT NAGKSSIMNA LVGLDKEQYE QNELFATLDA TTKAVKLVED FTVSLTDTVG FIQNLPTELI KAFKSTLEES ANVDLLIHVV DASNPHHEIH EQTVLKIMED LKLTNIPVLN VYNKMDIAPS DFLPTLSPSL QLSIKSESGV QWLKTAILEK LHELFDAFEL ELPYEKAYQL PELRKSALVQ SVVEGEKGYL IKGLIAPELS WKLPNN // ID Q9CMC5_PASMU Unreviewed; 448 AA. AC Q9CMC5; DT 01-JUN-2001, integrated into UniProtKB/TrEMBL. DT 01-JUN-2001, sequence version 1. DT 30-AUG-2017, entry version 91. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:AAK02991.1}; GN OrderedLocusNames=PM0907 {ECO:0000313|EMBL:AAK02991.1}; OS Pasteurella multocida (strain Pm70). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Pasteurella. OX NCBI_TaxID=272843 {ECO:0000313|EMBL:AAK02991.1, ECO:0000313|Proteomes:UP000000809}; RN [1] {ECO:0000313|EMBL:AAK02991.1, ECO:0000313|Proteomes:UP000000809} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Pm70 {ECO:0000313|EMBL:AAK02991.1, RC ECO:0000313|Proteomes:UP000000809}; RX PubMed=11248100; DOI=10.1073/pnas.051634598; RA May B.J., Zhang Q., Li L.L., Paustian M.L., Whittam T.S., Kapur V.; RT "Complete genomic sequence of Pasteurella multocida Pm70."; RL Proc. Natl. Acad. Sci. U.S.A. 98:3460-3465(2001). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE004439; AAK02991.1; -; Genomic_DNA. DR RefSeq; WP_010906911.1; NC_002663.1. DR ProteinModelPortal; Q9CMC5; -. DR STRING; 272843.PM0907; -. DR EnsemblBacteria; AAK02991; AAK02991; PM0907. DR KEGG; pmu:PM0907; -. DR PATRIC; fig|272843.6.peg.917; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; FNNHAHV; -. DR Proteomes; UP000000809; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000000809}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000000809}. FT DOMAIN 220 387 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 186 213 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 448 AA; 50105 MW; 1B87A67BB8865609 CRC64; MNTFIASAVD LQNESTALSS LPSPHSESLF DRAIIVHCFL AQDRNNDDLL EFKLLAKSAN VDILSVITST RHTPQAKYFV GQGKAEEIAE AVQNTQADVV LVNHALTPAQ TRNLESLCQC RVVDRTGVIL DIFAQRARSH EGKLQVELAQ LKHLSTRLVR RKTGLDQQKG AVGLRGPGET QLETDRRLIK VRISQLQSRL AKVEKQRHQN RQTRQKADIP TISLVGYTNA GKSTLFNLIT QANVYAADQL FATLDPTLRR LQIQDVGTTI LADTVGFIRH LPHDLVSAFK STLQETTEAA LLLHVIDCAD PRKLENIHAV EAVLKEINAG DIPTLLVYNK IDQVAHIEPH IEYDQEQRPI AVYMSAQTGI GLHLLLDAIS LCLKNEILDL ALTLPVHTGK IRHALYQQDC IQHEQINEQG EFLLAIRIDK VAWLKLLKQF PELETFIC // ID Q9FJM0_ARATH Unreviewed; 540 AA. AC Q9FJM0; DT 01-MAR-2001, integrated into UniProtKB/TrEMBL. DT 01-MAR-2001, sequence version 1. DT 05-JUL-2017, entry version 112. DE SubName: Full=GTP binding protein-like {ECO:0000313|EMBL:BAB08866.1}; DE SubName: Full=GTP-binding protein, HflX {ECO:0000313|EMBL:AED96978.1}; GN Name=MTI20.22 {ECO:0000313|EMBL:AED96978.1}; GN Synonyms=MTI20_22 {ECO:0000313|EMBL:AED96978.1}; GN OrderedLocusNames=At5g57960 {ECO:0000313|Araport:AT5G57960, GN ECO:0000313|EMBL:AED96978.1}; OS Arabidopsis thaliana (Mouse-ear cress). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae; OC Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae; OC Arabidopsis. OX NCBI_TaxID=3702; RN [1] {ECO:0000313|EMBL:BAB08866.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=9734815; DOI=10.1093/dnares/5.3.203; RA Kotani H., Nakamura Y., Sato S., Asamizu E., Kaneko T., Miyajima N., RA Tabata S.; RT "Structural analysis of Arabidopsis thaliana chromosome 5. VI. RT Sequence features of the regions of 1,367,185 bp covered by 19 RT physically assigned P1 and TAC clones."; RL DNA Res. 5:203-216(1998). RN [2] {ECO:0000313|EMBL:AED96978.1, ECO:0000313|Proteomes:UP000006548} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Columbia {ECO:0000313|Proteomes:UP000006548}; RX PubMed=11130714; DOI=10.1038/35048507; RG Kazusa DNA Research Institute; RG Cold Spring Harbor and Washington University in St Louis Sequencing Consortium; RG European Union Arabidopsis Genome Sequencing Consortium; RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E., RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., RA Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S., RA Nakazaki N., Naruo K., Okumura S., Shinpo S., Takeuchi C., Wada T., RA Watanabe A., Yamada M., Yasuda M., Sato S., de la Bastide M., RA Huang E., Spiegel L., Gnoj L., O'Shaughnessy A., Preston R., RA Habermann K., Murray J., Johnson D., Rohlfing T., Nelson J., RA Stoneking T., Pepin K., Spieth J., Sekhon M., Armstrong J., Becker M., RA Belter E., Cordum H., Cordes M., Courtney L., Courtney W., Dante M., RA Du H., Edwards J., Fryman J., Haakensen B., Lamar E., Latreille P., RA Leonard S., Meyer R., Mulvaney E., Ozersky P., Riley A., Strowmatt C., RA Wagner-McPherson C., Wollam A., Yoakum M., Bell M., Dedhia N., RA Parnell L., Shah R., Rodriguez M., See L.H., Vil D., Baker J., RA Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M., RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I., RA Volckaert G., Wambutt R., Dusterhoft A., Stiekema W., Pohl T., RA Entian K.D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.A., RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U., RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W., RA Mooijman P., Lankhorst R.K., Weitzenegger T., Bothe G., Rose M., RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S., RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G., RA Mayer K., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.W., RA Bevan M., Fransz P.; RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis RT thaliana."; RL Nature 408:823-826(2000). RN [3] {ECO:0000313|EMBL:AED96978.1} RP NUCLEOTIDE SEQUENCE. RG TAIR; RA Swarbreck D., Lamesch P., Wilks C., Huala E.; RL Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases. RN [4] {ECO:0000313|EMBL:AED96978.1, ECO:0000313|Proteomes:UP000006548} RP GENOME REANNOTATION. RC STRAIN=cv. Columbia {ECO:0000313|Proteomes:UP000006548}; RG The Arabidopsis Information Portal (Araport); RL Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002688; AED96978.1; -; Genomic_DNA. DR EMBL; AB013396; BAB08866.1; -; Genomic_DNA. DR RefSeq; NP_200604.1; NM_125181.5. DR UniGene; At.7661; -. DR SMR; Q9FJM0; -. DR STRING; 3702.AT5G57960.1; -. DR EnsemblPlants; AT5G57960.1; AT5G57960.1; AT5G57960. DR GeneID; 835907; -. DR Gramene; AT5G57960.1; AT5G57960.1; AT5G57960. DR Araport; AT5G57960; -. DR TAIR; locus:2174458; AT5G57960. DR eggNOG; KOG0410; Eukaryota. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR OMA; VILEIFH; -. DR OrthoDB; EOG093609UJ; -. DR BioCyc; ARA:GQT-2358-MONOMER; -. DR Proteomes; UP000006548; Chromosome 5. DR GO; GO:0009507; C:chloroplast; IDA:TAIR. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR GO; GO:0043022; F:ribosome binding; IBA:GO_Central. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 2. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000006548}; KW Reference proteome {ECO:0000313|Proteomes:UP000006548}. FT DOMAIN 310 476 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 540 AA; 60528 MW; 4A9D39277D0E31E9 CRC64; MSSFYLSSSP IFKLQWHANH KPKPNRAIVS FPPSRLHANC YSWRLSCNLA QHGIELEETV EEDEILQVLD LPTEETNLDN ETIASPSKML RKKKGDEESL DDRFKLRNGK EIFEEKAYLV GVERKGDGEC LFNIEESLEE LEQLADTAGL AVVGSTYQKL ASPNPRTYIG SGKVAEIKSA INALDVETVI FDDELSPGQL RNLEKAFGGD VRVCDRTALI LDIFNQRAAT HEAALQVALA QMEYQLPRLT RMWTHLERQS GGQVKGMGEK QIEVDKRILR TQIGVLKKEL ESVRKHRKQY RSRRVAIPVP VVSLVGYTNA GKSTLLNQLT GANVLAENRL FATLDPTTRR VQMQNGKEFL LTDTVGFIQK LPTTLVAAFR ATLEEIAESS LLVHVVDISH PLAEQQIEAV EKVMSELDVS SIPKLVVWNK VDRVDDPQKV KLEAEETGDT ICISALTGEG LDDFCNAVHE KLKDSMVWVE ALLPFDKGDL LSTIHKVGMV KETEYTENGT LIRAHVPLRF AQLLKPMRHL VKDTSISQRG // ID Q9HMC2_HALSA Unreviewed; 429 AA. AC Q9HMC2; DT 01-MAR-2001, integrated into UniProtKB/TrEMBL. DT 01-MAR-2001, sequence version 1. DT 07-JUN-2017, entry version 96. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX1 {ECO:0000313|EMBL:AAG20649.1}; GN Synonyms=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=VNG_2611G {ECO:0000313|EMBL:AAG20649.1}; OS Halobacterium salinarum (strain ATCC 700922 / JCM 11081 / NRC-1) OS (Halobacterium halobium). OC Archaea; Euryarchaeota; Halobacteria; Halobacteriales; OC Halobacteriaceae; Halobacterium. OX NCBI_TaxID=64091 {ECO:0000313|EMBL:AAG20649.1, ECO:0000313|Proteomes:UP000000554}; RN [1] {ECO:0000313|EMBL:AAG20649.1, ECO:0000313|Proteomes:UP000000554} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700922 / JCM 11081 / NRC-1 RC {ECO:0000313|Proteomes:UP000000554}; RX PubMed=11016950; DOI=10.1073/pnas.190337797; RA Ng W.V., Kennedy S.P., Mahairas G.G., Berquist B., Pan M., RA Shukla H.D., Lasky S.R., Baliga N.S., Thorsson V., Sbrogna J., RA Swartzell S., Weir D., Hall J., Dahl T.A., Welti R., Goo Y.A., RA Leithauser B., Keller K., Cruz R., Danson M.J., Hough D.W., RA Maddocks D.G., Jablonski P.E., Krebs M.P., Angevine C.M., Dale H., RA Isenbarger T.A., Peck R.F., Pohlschroder M., Spudich J.L., Jung K.W., RA Alam M., Freitas T., Hou S., Daniels C.J., Dennis P.P., Omer A.D., RA Ebhardt H., Lowe T.M., Liang P., Riley M., Hood L., DasSarma S.; RT "Genome sequence of Halobacterium species NRC-1."; RL Proc. Natl. Acad. Sci. U.S.A. 97:12176-12181(2000). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE004437; AAG20649.1; -; Genomic_DNA. DR PIR; E84410; E84410. DR RefSeq; WP_010903952.1; NC_002607.1. DR ProteinModelPortal; Q9HMC2; -. DR STRING; 64091.VNG2611G; -. DR PaxDb; Q9HMC2; -. DR EnsemblBacteria; AAG20649; AAG20649; VNG_2611G. DR GeneID; 5953462; -. DR KEGG; hal:VNG_2611G; -. DR PATRIC; fig|64091.14.peg.2023; -. DR eggNOG; arCOG00353; Archaea. DR eggNOG; COG2262; LUCA. DR InParanoid; Q9HMC2; -. DR KO; K03665; -. DR OMA; FNNHAHV; -. DR OrthoDB; POG093Z03AS; -. DR PhylomeDB; Q9HMC2; -. DR Proteomes; UP000000554; Chromosome. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0043022; F:ribosome binding; IBA:GO_Central. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000000554}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000000554}. FT DOMAIN 191 371 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 106 133 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 429 AA; 47197 MW; D5F99F4DEC26DF2F CRC64; MTDRRNSTAV VAKRRTDTPI ETDEIRALCE AAGVEVVAER TQARPRDPTY DLGDGAVADI AGLVERRSAD LVVVDDHLDP GRAHNLQEAV GAEVVDRARL VLDIFGERAE TKRARLEVRL AELRYELPRA QARVERGETQ GRQGFRSGGE RPAAQLKADY RQRITDRRAE LDRLDDADDG LREARRESGF DLVALAGYTN AGKSTLLRRL ADDLAVDEND GHGDRTDTAA SRDRLFETLN TTTRRATVGE RRVLLTDTVG FVDDLPRWLL SSFRTTLAAA READAVLLVV DATDDREGIR AKVEASRDEL ADAEGTLVPV LNKRDAATDL DAKRRLLAEH AGHAPVVTSA TGAEGLDALR ERLTDALPDR RRVSLSVPNT DAGNAFVSWC HDRGTVHEPD YGERIAFGFE ARPEVTAKAT GRAEQLNED // ID Q9HUM1_PSEAE Unreviewed; 433 AA. AC Q9HUM1; DT 01-MAR-2001, integrated into UniProtKB/TrEMBL. DT 01-MAR-2001, sequence version 1. DT 30-AUG-2017, entry version 101. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=PA4943 {ECO:0000313|EMBL:AAG08328.1}; OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / OS JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=208964 {ECO:0000313|EMBL:AAG08328.1, ECO:0000313|Proteomes:UP000002438}; RN [1] {ECO:0000313|EMBL:AAG08328.1, ECO:0000313|Proteomes:UP000002438} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / RC 1C / PRS 101 / PAO1 {ECO:0000313|Proteomes:UP000002438}; RX PubMed=10984043; DOI=10.1038/35023079; RA Stover C.K., Pham X.Q., Erwin A.L., Mizoguchi S.D., Warrener P., RA Hickey M.J., Brinkman F.S., Hufnagle W.O., Kowalik D.J., Lagrou M., RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y., RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R., RA Smith K., Spencer D., Wong G.K., Wu Z., Paulsen I.T., Reizer J., RA Saier M.H., Hancock R.E., Lory S., Olson M.V.; RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an RT opportunistic pathogen."; RL Nature 406:959-964(2000). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE004091; AAG08328.1; -; Genomic_DNA. DR PIR; C83028; C83028. DR RefSeq; NP_253630.1; NC_002516.2. DR RefSeq; WP_003113930.1; NC_002516.2. DR ProteinModelPortal; Q9HUM1; -. DR STRING; 208964.PA4943; -. DR PaxDb; Q9HUM1; -. DR EnsemblBacteria; AAG08328; AAG08328; PA4943. DR GeneID; 877756; -. DR KEGG; pae:PA4943; -. DR PATRIC; fig|208964.12.peg.5176; -. DR PseudoCAP; PA4943; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR InParanoid; Q9HUM1; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR PhylomeDB; Q9HUM1; -. DR Proteomes; UP000002438; Chromosome. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0043022; F:ribosome binding; IBA:GO_Central. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000002438}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000002438}. FT DOMAIN 199 366 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 165 192 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 433 AA; 48607 MW; F6433F50AE346E67 CRC64; MFFERPGGGE QAVLVHLEGQ NPEAREDPQE FQELVRSAGA ETVAFVSVSR HQPSAKYLIG SGKVEELHDL VKAENVELVI FNHTLTPSQE RNLERAFECR VLDRTGLILD IFAQRARTHE GKLQVELAQL EHMSTRLVRG WTHLERQKGG IGLRGPGETQ LETDRRLLRV RIRQIKQRLE KVRSQREQAR RGRKRADIPA VSLVGYTNAG KSTLFNSLTA SEVYAANQLF ATLDPTLRRL QLDDLGPVVL ADTVGFIRHL PHKLVEAFRA TLEESSNADL LLHVIDAYEP ERDAQVEQVL AVLGEIGANE LPMLEVYNKV DLLPSVEPHI QRDDSGKPVR VWLSAQTGEG LDLLRQAIAE LLGEDLFVGT LRLPQRLGRL RAQLFELGAV QSEAHDEEGC TLLQVRLPRA ELNRLASRAG WQPAEFVAQH TLQ // ID Q9KAC7_BACHD Unreviewed; 418 AA. AC Q9KAC7; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 07-JUN-2017, entry version 100. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=BH2362 {ECO:0000313|EMBL:BAB06081.1}; OS Bacillus halodurans (strain ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM OS 9153 / C-125). OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus. OX NCBI_TaxID=272558 {ECO:0000313|EMBL:BAB06081.1, ECO:0000313|Proteomes:UP000001258}; RN [1] {ECO:0000313|EMBL:BAB06081.1, ECO:0000313|Proteomes:UP000001258} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125 RC {ECO:0000313|Proteomes:UP000001258}; RX PubMed=11058132; DOI=10.1093/nar/28.21.4317; RA Takami H., Nakasone K., Takaki Y., Maeno G., Sasaki R., Masui N., RA Fuji F., Hirama C., Nakamura Y., Ogasawara N., Kuhara S., RA Horikoshi K.; RT "Complete genome sequence of the alkaliphilic bacterium Bacillus RT halodurans and genomic sequence comparison with Bacillus subtilis."; RL Nucleic Acids Res. 28:4317-4331(2000). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BA000004; BAB06081.1; -; Genomic_DNA. DR PIR; B83945; B83945. DR ProteinModelPortal; Q9KAC7; -. DR STRING; 272558.BH2362; -. DR EnsemblBacteria; BAB06081; BAB06081; BAB06081. DR KEGG; bha:BH2362; -. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000001258; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000001258}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000001258}. FT DOMAIN 202 364 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 418 AA; 47722 MW; 2EEDF4E40A4F6DFD CRC64; MEHLKETNAE RVFLVACQLP NMTDEQFEAS LEELEALTLT AQGTVIDRLT QKREAIEPAT YIGRGKLDEL AIKMEEQEAD LVIVNGELSG SQVRNLTNRL GVRVIDRTQL ILDIFAGRAK SREGKLQVEL AQLNYLLPRI VGQGQGLSRL GGGIGTRGPG ETKLETDRRH IRKRMADIDK QLKHTVKHRD RYRARRERNQ TFRIALVGYT NAGKSTLLNR LTASDSYEED LLFATLDPMT RKMRLPSGME VILSDTVGFI NQLPTTLVAA FRSTLEEVKH ADLLLHVVDR SSEQLQAHME TVSELLHQLE VDQSQMLVVY NKADKPNLPI IPVHQQNGIE MSAHKREDIQ RLRQMIERTL VDLFTPYVTE LASDEGNKLA KLRRETIMTE MKWDEDRECY QVKGYVHPNH AWAEQLLD // ID Q9KV10_VIBCH Unreviewed; 429 AA. AC Q9KV10; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 30-AUG-2017, entry version 92. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=VC_0348 {ECO:0000313|EMBL:AAF93521.1}; OS Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961). OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; OC Vibrionaceae; Vibrio. OX NCBI_TaxID=243277 {ECO:0000313|EMBL:AAF93521.1, ECO:0000313|Proteomes:UP000000584}; RN [1] {ECO:0000313|EMBL:AAF93521.1, ECO:0000313|Proteomes:UP000000584} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 39315 / El Tor Inaba N16961 RC {ECO:0000313|Proteomes:UP000000584}; RX PubMed=10952301; DOI=10.1038/35020000; RA Heidelberg J.F., Eisen J.A., Nelson W.C., Clayton R.A., Gwinn M.L., RA Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Umayam L.A., RA Gill S.R., Nelson K.E., Read T.D., Tettelin H., Richardson D., RA Ermolaeva M.D., Vamathevan J., Bass S., Qin H., Dragoi I., Sellers P., RA McDonald L., Utterback T., Fleishmann R.D., Nierman W.C., White O., RA Salzberg S.L., Smith H.O., Colwell R.R., Mekalanos J.J., Venter J.C., RA Fraser C.M.; RT "DNA sequence of both chromosomes of the cholera pathogen Vibrio RT cholerae."; RL Nature 406:477-483(2000). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE003852; AAF93521.1; -; Genomic_DNA. DR PIR; D82334; D82334. DR RefSeq; NP_230002.1; NC_002505.1. DR RefSeq; WP_000460377.1; NC_002505.1. DR ProteinModelPortal; Q9KV10; -. DR STRING; 243277.VC0348; -. DR DNASU; 2615061; -. DR EnsemblBacteria; AAF93521; AAF93521; VC_0348. DR GeneID; 2615061; -. DR KEGG; vch:VC0348; -. DR PATRIC; fig|243277.26.peg.325; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR KO; K03665; -. DR OMA; HPATYIG; -. DR BioCyc; VCHO:VC0348-MONOMER; -. DR Proteomes; UP000000584; Chromosome 1. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0005525; F:GTP binding; ISS:TIGR. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0043022; F:ribosome binding; IBA:GO_Central. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000000584}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000000584}. FT DOMAIN 198 365 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 429 AA; 48793 MW; A1E570A6277AE1A7 CRC64; MFDRYEAGER AVLVHVNFTQ RGEWEDLSEC KMLISSAGVT TLHVVTGSRQ TPHPKYFVGE GKAQEIAEAV QMHVANVVIF NHALSPAQER NLERLCQCRV IDRTGLILDI FAQRARTHEG KLQVELAQLR HISTRLIRGW THLERQKGGI GLRGPGETQL ETDRRLLRER IKAILRRLEK VAKQREQGRR ARSRAEIPTI SLVGYTNAGK STLFNRITEA GVYAADQLFA TLDPTLRKID LVDVGPAVLA DTVGFIRHLP HDLVAAFKAT LQETQEADIL LHVVDASDER FRENIQAVET VLQEIDAHEV PTLLVMNKID NLEEQSPRIE RDDEGVPRVV WISAMQGAGT ELLFEALSER LASQVVEHHL RIPPRHQGRI RSTFFQMNCI QQEEYDPEGN LLITVRMQQV DWARLEKREQ ADLCDFIVT // ID Q9PH58_XYLFA Unreviewed; 450 AA. AC Q9PH58; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 07-JUN-2017, entry version 111. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=XF_0088 {ECO:0000313|EMBL:AAF82901.1}; OS Xylella fastidiosa (strain 9a5c). OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales; OC Xanthomonadaceae; Xylella. OX NCBI_TaxID=160492 {ECO:0000313|EMBL:AAF82901.1, ECO:0000313|Proteomes:UP000000812}; RN [1] {ECO:0000313|EMBL:AAF82901.1, ECO:0000313|Proteomes:UP000000812} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=9a5c {ECO:0000313|EMBL:AAF82901.1, RC ECO:0000313|Proteomes:UP000000812}; RX PubMed=10910347; DOI=10.1038/35018003; RA Simpson A.J., Reinach F.C., Arruda P., Abreu F.A., Acencio M., RA Alvarenga R., Alves L.M., Araya J.E., Baia G.S., Baptista C.S., RA Barros M.H., Bonaccorsi E.D., Bordin S., Bove J.M., Briones M.R., RA Bueno M.R., Camargo A.A., Camargo L.E., Carraro D.M., Carrer H., RA Colauto N.B., Colombo C., Costa F.F., Costa M.C., Costa-Neto C.M., RA Coutinho L.L., Cristofani M., Dias-Neto E., Docena C., El-Dorry H., RA Facincani A.P., Ferreira A.J., Ferreira V.C., Ferro J.A., Fraga J.S., RA Franca S.C., Franco M.C., Frohme M., Furlan L.R., Garnier M., RA Goldman G.H., Goldman M.H., Gomes S.L., Gruber A., Ho P.L., RA Hoheisel J.D., Junqueira M.L., Kemper E.L., Kitajima J.P., RA Krieger J.E., Kuramae E.E., Laigret F., Lambais M.R., Leite L.C., RA Lemos E.G., Lemos M.V., Lopes S.A., Lopes C.R., Machado J.A., RA Machado M.A., Madeira A.M., Madeira H.M., Marino C.L., Marques M.V., RA Martins E.A., Martins E.M., Matsukuma A.Y., Menck C.F., Miracca E.C., RA Miyaki C.Y., Monteriro-Vitorello C.B., Moon D.H., Nagai M.A., RA Nascimento A.L., Netto L.E., Nhani A.Jr., Nobrega F.G., Nunes L.R., RA Oliveira M.A., de Oliveira M.C., de Oliveira R.C., Palmieri D.A., RA Paris A., Peixoto B.R., Pereira G.A., Pereira H.A.Jr., Pesquero J.B., RA Quaggio R.B., Roberto P.G., Rodrigues V., de M Rosa A.J., RA de Rosa V.E.Jr., de Sa R.G., Santelli R.V., Sawasaki H.E., RA da Silva A.C., da Silva A.M., da Silva F.R., da Silva W.A.Jr., RA da Silveira J.F., Silvestri M.L., Siqueira W.J., de Souza A.A., RA de Souza A.P., Terenzi M.F., Truffi D., Tsai S.M., Tsuhako M.H., RA Vallada H., Van Sluys M.A., Verjovski-Almeida S., Vettore A.L., RA Zago M.A., Zatz M., Meidanis J., Setubal J.C.; RT "The genome sequence of the plant pathogen Xylella fastidiosa."; RL Nature 406:151-159(2000). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE003849; AAF82901.1; -; Genomic_DNA. DR PIR; F82848; F82848. DR RefSeq; WP_010892635.1; NC_002488.3. DR ProteinModelPortal; Q9PH58; -. DR STRING; 160492.XF0088; -. DR EnsemblBacteria; AAF82901; AAF82901; XF_0088. DR GeneID; 1125605; -. DR KEGG; xfa:XF_0088; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR KO; K03665; -. DR OMA; HPATYIG; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000000812; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000000812}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000000812}. FT DOMAIN 199 369 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 158 192 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 450 AA; 50277 MW; A5321DF06F2E9465 CRC64; MFDRSRKGEY ALLIQPLTDH SAEDGALEEF ADLTRSAGAT VAGSLAVRIN RPNPSTLIGS GKLKEIKATA DATGADLILI NHSLSPVQER NLEKSLERRV IDRTGLILDI FAQRACSHEG KLQVELAQLR HLATRLVRGW THLERQRGGA IGLRGPGETQ LETDRRLLQK RVEQLQKRLS KVEVQRTQMR RARVRSEVPR IALVGYTNSG KSTLFNALTG ASAYTADQLF ATLDPKVRRI VLPGSSAMLA DTVGFVRHLP HELVAAFRST LSEAREADLL LHVIDAADPL REERIDQVDE VLQAIGAGEL PQLLVFNKID CIEGAEVRQD TQDGIPDQAR RERVWLSARH GHGVELLQQV LDHRLKMQNV QGELRLLPSA GRLRARLHEL KGVREEQTDE HGWLLKIDLS LAEIERLAAS DYGIPLRALL QYHRDAWTPT LHSKYVSPGY // ID Q9RY13_DEIRA Unreviewed; 525 AA. AC Q9RY13; DT 01-MAY-2000, integrated into UniProtKB/TrEMBL. DT 01-MAY-2000, sequence version 1. DT 05-JUL-2017, entry version 107. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=DR_0139 {ECO:0000313|EMBL:AAF09728.1}; OS Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / OS LMG 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422). OC Bacteria; Deinococcus-Thermus; Deinococci; Deinococcales; OC Deinococcaceae; Deinococcus. OX NCBI_TaxID=243230 {ECO:0000313|EMBL:AAF09728.1, ECO:0000313|Proteomes:UP000002524}; RN [1] {ECO:0000313|EMBL:AAF09728.1, ECO:0000313|Proteomes:UP000002524} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / RC NCIMB 9279 / R1 / VKM B-1422 {ECO:0000313|Proteomes:UP000002524}; RX PubMed=10567266; DOI=10.1126/science.286.5444.1571; RA White O., Eisen J.A., Heidelberg J.F., Hickey E.K., Peterson J.D., RA Dodson R.J., Haft D.H., Gwinn M.L., Nelson W.C., Richardson D.L., RA Moffat K.S., Qin H., Jiang L., Pamphile W., Crosby M., Shen M., RA Vamathevan J.J., Lam P., McDonald L., Utterback T., Zalewski C., RA Makarova K.S., Aravind L., Daly M.J., Minton K.W., Fleischmann R.D., RA Ketchum K.A., Nelson K.E., Salzberg S., Smith H.O., Venter J.C., RA Fraser C.M.; RT "Genome sequence of the radioresistant bacterium Deinococcus RT radiodurans R1."; RL Science 286:1571-1577(1999). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000513; AAF09728.1; -; Genomic_DNA. DR PIR; H75555; H75555. DR RefSeq; NP_293865.1; NC_001263.1. DR RefSeq; WP_010886787.1; NZ_CP015081.1. DR ProteinModelPortal; Q9RY13; -. DR STRING; 243230.DR_0139; -. DR EnsemblBacteria; AAF09728; AAF09728; DR_0139. DR GeneID; 1799293; -. DR KEGG; dra:DR_0139; -. DR PATRIC; fig|243230.17.peg.304; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR InParanoid; Q9RY13; -. DR KO; K03665; -. DR OMA; EREVIIT; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000002524; Chromosome I. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0043022; F:ribosome binding; IBA:GO_Central. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000002524}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000002524}. FT DOMAIN 338 507 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 120 143 {ECO:0000256|SAM:Coils}. FT COILED 297 324 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 525 AA; 57453 MW; 71E997E0B682401A CRC64; MRREVGVLID RRGRVISVSV ADARGTEFPD LRLGENRLAG FHLLHAHPRG GALSKGDLST LFLKRLDAVS AIEVGNDGRP GLVHTAHLTP PGTVGEEEDW RILPPAQPFE IDEFDLGAQV SALEEEIARA ARTREAKKDH ERALLVQIDG GEFDAEERLE ELGELARTAG AEVVYKELIY RRNLKPGTLV GAGKLEELTS KAYHLDADLL IFGQELGPAQ AREIEAATGL KVVDRTQLIL DIFALHAQGV ESRLQVELAQ LRYMKPRLLG AGAQLSRIGG GGGSAGGGAI GTRGPGETKL ELDRRRINDR LSFLEKQLEG VSQRREERRK SRERNDVPVV SIVGYTNAGK STLLNSFTHA AEEPRRVLAE NKLFATLRPT SRQGYIEGIG QVIFTDTVGF IRDLPKDLSR AFRSTLEEIG DADVLLHVVD AASPGAEQRL DAVNRILDDL GFRDMPTVVA LNKADRAEPE VLAREQERTG GIPVSALKNI GLTELKEALG DAVASVQRAE LARQEEARAA RVEWR // ID Q9UZR3_PYRAB Unreviewed; 423 AA. AC Q9UZR3; DT 01-MAY-2000, integrated into UniProtKB/TrEMBL. DT 01-MAY-2000, sequence version 1. DT 07-JUN-2017, entry version 112. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX-like {ECO:0000313|EMBL:CAB49993.1}; GN Synonyms=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=PAB0722 {ECO:0000313|EMBL:CAB49993.1}; OS Pyrococcus abyssi (strain GE5 / Orsay). OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae; OC Pyrococcus. OX NCBI_TaxID=272844 {ECO:0000313|EMBL:CAB49993.1, ECO:0000313|Proteomes:UP000000810}; RN [1] {ECO:0000313|EMBL:CAB49993.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=Orsay {ECO:0000313|EMBL:CAB49993.1}; RA Genoscope; RL Submitted (JUL-1999) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:CAB49993.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=Orsay {ECO:0000313|EMBL:CAB49993.1}; RX PubMed=10736225; DOI=10.1006/jmbi.2000.3593; RA Gaspin C., Cavaille J., Erauso G.; RT "Archaeal homologs of eukaryotic methylation guide small nucleolar RT RNAs: lessons from the Pyrococcus genomes."; RL J. Mol. Biol. 297:895-906(2000). RN [3] {ECO:0000313|EMBL:CAB49993.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=Orsay {ECO:0000313|EMBL:CAB49993.1}; RX PubMed=11381026; DOI=10.1101/gr.GR1653R; RA Lecompte O., Ripp R., Puzos-Barbe V., Duprat S., Heilig R., RA Dietrich J., Thierry J.C., Poch O.; RT "Genome evolution at the genus level: comparison of three complete RT genomes of hyperthermophilic archaea."; RL Genome Res. 11:981-993(2001). RN [4] {ECO:0000313|EMBL:CAB49993.1, ECO:0000313|Proteomes:UP000000810} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=GE5 / Orsay {ECO:0000313|Proteomes:UP000000810}, and RC Orsay {ECO:0000313|EMBL:CAB49993.1}; RX PubMed=12622808; DOI=10.1046/j.1365-2958.2003.03381.x; RA Cohen G., Barbe V., Flament D., Galperin M., Heilig R., Ripp R., RA Lecompte O., Prieur D., Poch O., Quellerou J., Thierry J.C., RA Van der Oost J., Weissenbach J., Zivanovic Y., Forterre P.; RT "An integrated analysis of the genome of the hyperthermophilic RT archaeon Pyrococcus abyssi."; RL Mol. Microbiol. 47:1495-1512(2003). RN [5] {ECO:0000313|EMBL:CCE70493.1, ECO:0000313|Proteomes:UP000009139} RP GENOME REANNOTATION. RC STRAIN=GE5 {ECO:0000313|EMBL:CCE70493.1}, and RC GE5 / Orsay {ECO:0000313|Proteomes:UP000009139}; RX PubMed=22057919; DOI=10.1007/s00284-011-0035-x; RA Gao J., Wang J.; RT "Re-annotation of two hyperthermophilic archaea Pyrococcus abyssi GE5 RT and Pyrococcus furiosus DSM 3638."; RL Curr. Microbiol. 64:118-129(2012). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AJ248286; CAB49993.1; -; Genomic_DNA. DR EMBL; HE613800; CCE70493.1; -; Genomic_DNA. DR PIR; D75086; D75086. DR RefSeq; WP_010868200.1; NC_000868.1. DR STRING; 272844.PAB0722; -. DR EnsemblBacteria; CAB49993; CAB49993; PAB0722. DR GeneID; 1496438; -. DR KEGG; pab:PAB0722; -. DR PATRIC; fig|272844.11.peg.1137; -. DR eggNOG; arCOG00353; Archaea. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; FNNHAHV; -. DR OrthoDB; POG093Z07D6; -. DR Proteomes; UP000000810; Chromosome. DR Proteomes; UP000009139; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000000810, KW ECO:0000313|Proteomes:UP000009139}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}. FT DOMAIN 186 361 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 423 AA; 49135 MW; 944B9F58BC84BB40 CRC64; MRAIGVIRKS RRERVSREEF EELLRSAGYE ILAIVEQVRE EHPRFNIGPG KLEEIKELVR ELNPDKVVFA NRLTPSQAYN LWKELRVDII DKWQLVLEIF EKRAHSKEAK LQVELANLQY ELPLVKEAIR RIKMGDRAGF KGMGEYQVHQ YFKHIRYRMG KIKDELEKIR SEREIRRKKR EEEGFVLVAL AGYTNAGKST LLNALSGDYV EAKNQMFTTL STTTRRFRVR GKMLLVTDTV GFIDGLPPFI VEAFHSTLEE IVKADIIVLV LDASEPWREV RRKFFASLDV LRELKALDRP MIIALNKIDL VSEEDVQEKE LLLRELLDGR TNAIGIAKIS AKHKKLEELY ELIDRALTKL PKFQTFEIKV KDPSKLGKIL AMLHSMGEVL EVSYGNETRI RAYIQTGLIR ELNKLGVKLR RIN // ID Q9VBQ7_DROME Unreviewed; 526 AA. AC Q9VBQ7; DT 01-MAY-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2002, sequence version 2. DT 30-AUG-2017, entry version 122. DE SubName: Full=CG5116, isoform A {ECO:0000313|EMBL:AAF56472.2}; DE SubName: Full=CG5116, isoform B {ECO:0000313|EMBL:AHN57528.1}; DE SubName: Full=FI04601p {ECO:0000313|EMBL:ACS68164.1}; GN Name=CG5116-RA {ECO:0000313|EMBL:ACS68164.1}; GN ORFNames=CG5116 {ECO:0000313|EMBL:AAF56472.2, GN ECO:0000313|FlyBase:FBgn0039339}, GN Dmel_CG5116 {ECO:0000313|EMBL:AAF56472.2}; OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; OC Pterygota; Neoptera; Holometabola; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila; Sophophora. OX NCBI_TaxID=7227 {ECO:0000313|EMBL:AAF56472.2, ECO:0000313|Proteomes:UP000000803}; RN [1] {ECO:0000313|EMBL:AAF56472.2, ECO:0000313|Proteomes:UP000000803} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803}; RX PubMed=10731132; DOI=10.1126/science.287.5461.2185; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.H., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Gabor G.L., RA Abril J.F., Agbayani A., An H.J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., WoodageT, Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., RA Yeh R.F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [2] {ECO:0000313|EMBL:AAF56472.2, ECO:0000313|Proteomes:UP000000803} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803}; RX PubMed=12537568; RA Celniker S.E., Wheeler D.A., Kronmiller B., Carlson J.W., Halpern A., RA Patel S., Adams M., Champe M., Dugan S.P., Frise E., Hodgson A., RA George R.A., Hoskins R.A., Laverty T., Muzny D.M., Nelson C.R., RA Pacleb J.M., Park S., Pfeiffer B.D., Richards S., Sodergren E.J., RA Svirskas R., Tabor P.E., Wan K., Stapleton M., Sutton G.G., Venter C., RA Weinstock G., Scherer S.E., Myers E.W., Gibbs R.A., Rubin G.M.; RT "Finishing a whole-genome shotgun: release 3 of the Drosophila RT melanogaster euchromatic genome sequence."; RL Genome Biol. 3:RESEARCH0079-RESEARCH0079(2002). RN [3] {ECO:0000313|EMBL:AAF56472.2, ECO:0000313|Proteomes:UP000000803} RP GENOME REANNOTATION. RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803}; RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfied E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [4] {ECO:0000313|EMBL:AAF56472.2, ECO:0000313|Proteomes:UP000000803} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803}; RX PubMed=12537573; RA Kaminker J.S., Bergman C.M., Kronmiller B., Carlson J., Svirskas R., RA Patel S., Frise E., Wheeler D.A., Lewis S.E., Rubin G.M., RA Ashburner M., Celniker S.E.; RT "The transposable elements of the Drosophila melanogaster euchromatin: RT a genomics perspective."; RL Genome Biol. 3:RESEARCH0084-RESEARCH0084(2002). RN [5] {ECO:0000313|EMBL:AAF56472.2, ECO:0000313|Proteomes:UP000000803} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803}; RX PubMed=12537574; RA Hoskins R.A., Smith C.D., Carlson J.W., Carvalho A.B., Halpern A., RA Kaminker J.S., Kennedy C., Mungall C.J., Sullivan B.A., Sutton G.G., RA Yasuhara J.C., Wakimoto B.T., Myers E.W., Celniker S.E., Rubin G.M., RA Karpen G.H.; RT "Heterochromatic sequences in a Drosophila whole-genome shotgun RT assembly."; RL Genome Biol. 3:RESEARCH0085-RESEARCH0085(2002). RN [6] {ECO:0000313|EMBL:AAF56472.2, ECO:0000313|Proteomes:UP000000803} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803}; RX PubMed=16110336; DOI=10.1371/journal.pcbi.0010022; RA Quesneville H., Bergman C.M., Andrieu O., Autard D., Nouaud D., RA Ashburner M., Anxolabehere D.; RT "Combined evidence annotation of transposable elements in genome RT sequences."; RL PLoS Comput. Biol. 1:166-175(2005). RN [7] {ECO:0000313|EMBL:AAF56472.2} RP NUCLEOTIDE SEQUENCE. RG Berkeley Drosophila Genome Project; RA Celniker S., Carlson J., Wan K., Pfeiffer B., Frise E., George R., RA Hoskins R., Stapleton M., Pacleb J., Park S., Svirskas R., Smith E., RA Yu C., Rubin G.; RT "Drosophila melanogaster release 4 sequence."; RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases. RN [8] {ECO:0000313|EMBL:AAF56472.2} RP NUCLEOTIDE SEQUENCE. RA Celniker S., Carlson J., Wan K., Frise E., Hoskins R., Park S., RA Svirskas R., Rubin G.; RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases. RN [9] {ECO:0000313|EMBL:AAF56472.2, ECO:0000313|Proteomes:UP000000803} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803}; RX PubMed=17569856; DOI=10.1126/science.1139815; RA Smith C.D., Shu S., Mungall C.J., Karpen G.H.; RT "The Release 5.1 annotation of Drosophila melanogaster RT heterochromatin."; RL Science 316:1586-1591(2007). RN [10] {ECO:0000313|EMBL:AAF56472.2, ECO:0000313|Proteomes:UP000000803} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803}; RX PubMed=17569867; DOI=10.1126/science.1139816; RA Hoskins R.A., Carlson J.W., Kennedy C., Acevedo D., Evans-Holm M., RA Frise E., Wan K.H., Park S., Mendez-Lago M., Rossi F., Villasante A., RA Dimitri P., Karpen G.H., Celniker S.E.; RT "Sequence finishing and mapping of Drosophila melanogaster RT heterochromatin."; RL Science 316:1625-1628(2007). RN [11] {ECO:0000313|EMBL:ACS68164.1} RP NUCLEOTIDE SEQUENCE. RA Carlson J., Booth B., Frise E., Park S., Wan K., Yu C., Celniker S.; RL Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases. RN [12] {ECO:0000313|EMBL:AAF56472.2} RP NUCLEOTIDE SEQUENCE. RG FlyBase; RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE014297; AAF56472.2; -; Genomic_DNA. DR EMBL; BT088847; ACS68164.1; -; mRNA. DR EMBL; AE014297; AHN57528.1; -; Genomic_DNA. DR RefSeq; NP_001287529.1; NM_001300600.1. DR RefSeq; NP_651399.2; NM_143142.4. DR UniGene; Dm.20256; -. DR SMR; Q9VBQ7; -. DR STRING; 7227.FBpp0084251; -. DR EnsemblMetazoa; FBtr0084877; FBpp0084251; FBgn0039339. DR EnsemblMetazoa; FBtr0343172; FBpp0309866; FBgn0039339. DR GeneID; 43081; -. DR KEGG; dme:Dmel_CG5116; -. DR UCSC; CG5116-RA; d. melanogaster. DR FlyBase; FBgn0039339; CG5116. DR eggNOG; KOG0410; Eukaryota. DR eggNOG; COG2262; LUCA. DR GeneTree; ENSGT00390000001397; -. DR OMA; MDTVGFM; -. DR OrthoDB; EOG091G0852; -. DR GenomeRNAi; 43081; -. DR Proteomes; UP000000803; Chromosome 3R. DR Bgee; FBgn0039339; -. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR GO; GO:0043022; F:ribosome binding; IBA:GO_Central. DR CDD; cd01878; HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 1: Evidence at protein level; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000000803}; KW Proteomics identification {ECO:0000213|PeptideAtlas:Q9VBQ7}; KW Reference proteome {ECO:0000313|Proteomes:UP000000803}. FT DOMAIN 296 468 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 257 289 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 526 AA; 59213 MW; B37A38E87DF5C465 CRC64; MSALRILARF VSTRTLRIRP ILEIPARCKY TQHQGVKGIR NRKSFFEAQI QAGQQGEEDA DLERTANSDL ADMRFLDDRA YDEVAGGAMR ITRDIASSQQ VLILQPYVKW AAKRQNAPVD VRPEDQLAEA TALIHSLPNW QVARALKVPL ESLEKKTLFG SGKLVELKEL VAELRQERHL TCLFVSKGTL SFAQKRFLEA EFRLPVMDRY SVVIQILRLH ATSAEAKLQV AMAELPYIWA QAKDASVTQT RRQGYALTDL QKEILRTRER KLRAELDRVR RQRQLLRQKR KQQNYPIVAV VGYTNAGKTS LIKALTVEDA LQPRNQLFAT LDVTAHAGCL PCNLEVIYMD TVGFMSDLPT GLFECFVATL EDAMLADVIV HVQDLSHPCH AAQRSHVEAT LRSLAFNVAG GDSTASQLPP IINVYNKCDL VSQEAQSSAD PVHHISARAQ TGLEPLLDDI EQQILTATGR RKLQMRVPSG GPEMAWLYKN AAVVETTADA ENPERLMMHV VISQRTLDQF KRQFCR // ID Q9WYZ7_THEMA Unreviewed; 406 AA. AC Q9WYZ7; G4FDU4; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 07-JUN-2017, entry version 120. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN OrderedLocusNames=TM_0527 {ECO:0000313|EMBL:AAD35612.1}; OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga. OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35612.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35612.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 RC {ECO:0000313|Proteomes:UP000008183}; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000512; AAD35612.1; -; Genomic_DNA. DR PIR; E72366; E72366. DR RefSeq; NP_228337.1; NC_000853.1. DR RefSeq; WP_004081386.1; NZ_CP011107.1. DR STRING; 243274.TM0527; -. DR EnsemblBacteria; AAD35612; AAD35612; TM_0527. DR EnsemblBacteria; AGL49449; AGL49449; Tmari_0524. DR GeneID; 897579; -. DR KEGG; tma:TM0527; -. DR KEGG; tmm:Tmari_0524; -. DR KEGG; tmw:THMA_0540; -. DR PATRIC; fig|243274.17.peg.526; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR KO; K03665; -. DR OMA; HPATYIG; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0043022; F:ribosome binding; IBA:GO_Central. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000008183}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT COILED 153 180 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 406 AA; 46476 MW; 7E4B3DEC1145160A CRC64; MIVAVGKDEE KIKESLEEMK GLCKTLGVEV VEWLWQKRAK PDPATYLGKG KLQKLKEVVE FCEADLVVVD DEITPVQYKN MQSELNVDVL DRTQVILEIF ARHATSEEGK LQVEMASLLY ELPRLVGKGE ELSRLGGGIG TRGPGEPLLE VLRRHIKNRI AQLRKRLKEI EQERNTQRKQ RLEKKIPHVS IVGYTNAGKS TLLKVLTDSD VYVADKLFAT LEPVTRRLKL KSGRVILVSD TVGFIRKLPH TIVSAFKATL EEIKYSDVLI HLVDASDPYL EEKMKASEKV LEEIGADKIP RILVFNKIDL CPRERIETLK WKYPEALFIS AEKRIGLDQL LDRLEEVISQ RDVQETLKVP LEKIGQIYAL KDRLEILNED YREGYALITL KTDRETLEML KRKVAS // ID Q9XCC1_STRFR Unreviewed; 425 AA. AC Q9XCC1; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 10-MAY-2017, entry version 69. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=SFRA_26395 {ECO:0000313|EMBL:KDS85058.1}; OS Streptomyces fradiae (Streptomyces roseoflavus). OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae; OC Streptomyces. OX NCBI_TaxID=1906 {ECO:0000313|EMBL:AAD40807.1}; RN [1] {ECO:0000313|EMBL:AAD40807.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=T59235 {ECO:0000313|EMBL:AAD40807.1}; RX PubMed=10467127; DOI=10.1016/S1074-5521(99)80113-6; RA Bate N., Butler A.R., Gandecha A.R., Cundliffe E.; RT "Multiple regulatory genes in the tylosin biosynthetic cluster of RT Streptomyces fradiae."; RL Chem. Biol. 6:617-624(1999). RN [2] {ECO:0000313|EMBL:KDS85058.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 19609 {ECO:0000313|EMBL:KDS85058.1}; RA Bekker O.B., Klimina K.M., Vatlin A.A., Zakharevich N.V., RA Danilenko V.N.; RT "Genome Sequence of Streptomyces fradiae ATCC 19609."; RL Submitted (MAY-2014) to the EMBL/GenBank/DDBJ databases. RN [3] {ECO:0000313|Proteomes:UP000028058} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 19609 {ECO:0000313|Proteomes:UP000028058}; RA Bekker O.B., Klimina K.M., Vatlin A.A., Zakharevich N.V., RA Danilenko V.N.; RT "Genome sequence of Streptomyces fradiae ATCC 19609."; RL Submitted (MAY-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AF145049; AAD40807.1; -; Genomic_DNA. DR EMBL; JNAD01000058; KDS85058.1; -; Genomic_DNA. DR PIR; T44592; T44592. DR ProteinModelPortal; Q9XCC1; -. DR EnsemblBacteria; KDS85058; KDS85058; SFRA_26395. DR Proteomes; UP000028058; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000313|EMBL:KDS85058.1}; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000028058}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900, KW ECO:0000313|EMBL:KDS85058.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000028058}. FT DOMAIN 200 364 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 159 186 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 425 AA; 45424 MW; 224ED78AFBFFEC4F CRC64; MSSTERVMLV GVWTSGTAED AAGDLAELAA LVEAAGAEVV HEVVQRRDKP DPATYIGSGK AAELTGLVAD LEVDTIVCDG ELSPAQLVRL ADLVDAKVID RTALILDIFA QRATSREGRA QVALAQMQYM MPRLRGLGRS LSRLSGGSGG GLATRGPGET KIETDRRRLR DNMESVRREL EQMENGRALR RKRRRGSNIP SVALAGYTNA GKSSLLNRLT GADVLVKDAL FATLDPTVRR VRAGGRVCTL TDTVGFVSRL PHHLVDAFRS TLEEVTEADL VLHVVDSSHP DPLRQIETVR AVIGDIGGAG VPEILVANKA DAAPEGALER LLAAEPAAEV VSARTGAGVD RLLDRVAERL SGTGLQMELL LPYTEGGLLT RIHDEGTVLR EEHTGTGVRL TARVPERLAA EVEPHRERQD GPGGP // ID Q9YAD2_AERPE Unreviewed; 372 AA. AC Q9YAD2; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 07-JUN-2017, entry version 114. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:BAA81017.1}; GN OrderedLocusNames=APE_2007 {ECO:0000313|EMBL:BAA81017.1}; OS Aeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC OS 100138 / K1). OC Archaea; Crenarchaeota; Thermoprotei; Desulfurococcales; OC Desulfurococcaceae; Aeropyrum. OX NCBI_TaxID=272557 {ECO:0000313|EMBL:BAA81017.1, ECO:0000313|Proteomes:UP000002518}; RN [1] {ECO:0000313|EMBL:BAA81017.1, ECO:0000313|Proteomes:UP000002518} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1 RC {ECO:0000313|Proteomes:UP000002518}; RX PubMed=10382966; DOI=10.1093/dnares/6.2.83; RA Kawarabayasi Y., Hino Y., Horikawa H., Yamazaki S., Haikawa Y., RA Jin-no K., Takahashi M., Sekine M., Baba S., Ankai A., Kosugi H., RA Hosoyama A., Fukui S., Nagai Y., Nishijima K., Nakazawa H., RA Takamiya M., Masuda S., Funahashi T., Tanaka T., Kudoh Y., RA Yamazaki J., Kushida N., Oguchi A., Aoki K., Kubota K., Nakamura Y., RA Nomura N., Sako Y., Kikuchi H.; RT "Complete genome sequence of an aerobic hyper-thermophilic RT crenarchaeon, Aeropyrum pernix K1."; RL DNA Res. 6:83-101(1999). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BA000002; BAA81017.1; -; Genomic_DNA. DR PIR; A72504; A72504. DR ProteinModelPortal; Q9YAD2; -. DR STRING; 272557.APE_2007; -. DR EnsemblBacteria; BAA81017; BAA81017; APE_2007. DR KEGG; ape:APE_2007; -. DR PATRIC; fig|272557.25.peg.1339; -. DR eggNOG; arCOG00353; Archaea. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000260368; -. DR KO; K03665; -. DR OMA; FNNHAHV; -. DR OrthoDB; POG093Z07D6; -. DR Proteomes; UP000002518; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000002518}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000002518}. FT DOMAIN 184 361 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 372 AA; 41246 MW; 3E21998581F23F0D CRC64; MKSRRKALMV IPRLLERHLD EALALAETAG YDVARLWRNR HPRIIKKGLL DAIKDEARSS GAEALIYYGD LQPSSKFTVM RETGLNVVDR VMLILEIFAL HASSREALLQ IEAARIKHEI PLAREFVRRS KMGEYPGFLG PGMYAADQYL RHLRRRLVKI RRELDKMRST RESRLSSRAK SGLKQVSIVG YASAGKTSLF NLLTGEDRPV GPEYFTTLQP KHSRITWGGV EGVLAADTVG FIRDVPPEIV EAFHATLAEV KHSDAIVFVI DAAEPPSDIE EKLHAGIDTL ARIGALSAPM VIAANKIDAL QPPEIGERIA LIEREASILP HSPPVIPISA KTGYGVDRLV RSIIKIVDGD RLEGLLEAGH MD // ID R0GPS1_9BRAS Unreviewed; 540 AA. AC R0GPS1; DT 26-JUN-2013, integrated into UniProtKB/TrEMBL. DT 26-JUN-2013, sequence version 1. DT 07-JUN-2017, entry version 18. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EOA13173.1}; GN ORFNames=CARUB_v10026197mg {ECO:0000313|EMBL:EOA13173.1}; OS Capsella rubella. OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae; OC Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae; OC Capsella. OX NCBI_TaxID=81985 {ECO:0000313|EMBL:EOA13173.1, ECO:0000313|Proteomes:UP000029121}; RN [1] {ECO:0000313|Proteomes:UP000029121} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=23749190; DOI=10.1038/ng.2669; RA Slotte T., Hazzouri K.M., Agren J.A., Koenig D., Maumus F., Guo Y.L., RA Steige K., Platts A.E., Escobar J.S., Newman L.K., Wang W., RA Mandakova T., Vello E., Smith L.M., Henz S.R., Steffen J., Takuno S., RA Brandvain Y., Coop G., Andolfatto P., Hu T.T., Blanchette M., RA Clark R.M., Quesneville H., Nordborg M., Gaut B.S., Lysak M.A., RA Jenkins J., Grimwood J., Chapman J., Prochnik S., Shu S., Rokhsar D., RA Schmutz J., Weigel D., Wright S.I.; RT "The Capsella rubella genome and the genomic consequences of rapid RT mating system evolution."; RL Nat. Genet. 45:831-835(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; KB870812; EOA13173.1; -; Genomic_DNA. DR RefSeq; XP_006280275.1; XM_006280213.1. DR GeneID; 17877341; -. DR KEGG; crb:CARUB_v10026197mg; -. DR KO; K03665; -. DR Proteomes; UP000029121; Unassembled WGS sequence. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000029121}; KW Reference proteome {ECO:0000313|Proteomes:UP000029121}. FT DOMAIN 310 476 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 540 AA; 60557 MW; 2B27E7BD4B21DC3A CRC64; MSSFYLSSSP ISKLQWHANP KPKPNRPVVR LPLSRLHANC YSWRLSCNVA QHGLDFEETV EEDESPQLLE LSSEEPSIDE EKVAAPSRML RKKKEDEESL NDRFKLRNGK EVFEEKAYLV GVERKGDGEC LFDIEESLEE LEQLADTAGL AVVGSTYQKL ASPNPRTYIG SGKVAEIKSA INALDVETVI FDDELSPGQL RNLEKAFGGE VRVCDRTALI LDIFNQRAAT HEAALQVALA QMEYQLPRLT RMWTHLERQS GGQVKGMGEK QIEVDKRILR TQIGVLKKEL ESVRKHRKQY RSRRVAIPVP VVSLVGYTNA GKSTLLNQLT GANVLAENRL FATLDPTTRR VQMHNGKEFL LTDTVGFIQK LPTTLVAAFR ATLEEISESS LLVHVVDISH PLAQQQIEAV EKVMSELDVS SIPKLVVWNK VDRVDDPQKV KLEAEKSGDT ICISALTGEG LDDFCNAVHE KLKDSMVWVE ALLPFDKGDL LSTIHKVGMV KETEYTENGT LIRAHVPLRF AQLLKPMRHL VRDVPISQKG // ID R0HK50_9BRAS Unreviewed; 643 AA. AC R0HK50; DT 26-JUN-2013, integrated into UniProtKB/TrEMBL. DT 26-JUN-2013, sequence version 1. DT 07-JUN-2017, entry version 17. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EOA25585.1}; GN ORFNames=CARUB_v10018932mg {ECO:0000313|EMBL:EOA25585.1}; OS Capsella rubella. OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae; OC Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae; OC Capsella. OX NCBI_TaxID=81985 {ECO:0000313|EMBL:EOA25585.1, ECO:0000313|Proteomes:UP000029121}; RN [1] {ECO:0000313|Proteomes:UP000029121} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=23749190; DOI=10.1038/ng.2669; RA Slotte T., Hazzouri K.M., Agren J.A., Koenig D., Maumus F., Guo Y.L., RA Steige K., Platts A.E., Escobar J.S., Newman L.K., Wang W., RA Mandakova T., Vello E., Smith L.M., Henz S.R., Steffen J., Takuno S., RA Brandvain Y., Coop G., Andolfatto P., Hu T.T., Blanchette M., RA Clark R.M., Quesneville H., Nordborg M., Gaut B.S., Lysak M.A., RA Jenkins J., Grimwood J., Chapman J., Prochnik S., Shu S., Rokhsar D., RA Schmutz J., Weigel D., Wright S.I.; RT "The Capsella rubella genome and the genomic consequences of rapid RT mating system evolution."; RL Nat. Genet. 45:831-835(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; KB870809; EOA25585.1; -; Genomic_DNA. DR RefSeq; XP_006292687.1; XM_006292625.1. DR GeneID; 17886988; -. DR KEGG; crb:CARUB_v10018932mg; -. DR Proteomes; UP000029121; Unassembled WGS sequence. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR CDD; cd01878; HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 2. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000029121}; KW Reference proteome {ECO:0000313|Proteomes:UP000029121}. FT DOMAIN 362 605 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 643 AA; 72145 MW; 2683C30C04E25548 CRC64; MSTTESVGIW LNHLNFGDQA TFLYKNTKIP LWNRQASEIS KLSNPRLNRI SMLRTLSHAR SRLRSETTSL PLARNRLRSK TPSSSPLSSP YSSKRHAPKT SEVEDYSRAK DSVLLYPKDP SSAPKLFLVQ PRLTPPKFLQ AKLNEALCLA NSLEEQRYGY FESDFFDKEL PSHVVVQNPV RRSSKPRADT YFGPGTVDNI KCHLNAEDSK EEVDAVFVNA MLTAIQQRNL ERIWAKPVLD RVGLIIEIFN AHAHTKEAKL QAELAALMYK KSRLVRVRGT DGRHSFGQFG EAEVVSARGR AASGTGGGFV GGAGETELQL QRRRIADRRL RLLSQIKETQ RTRLLQRAGR KKRVGNKDES SATIAVVGYT NAGKSTLTSA LTKTALYCNE RLFATLDPTL KSCHLPSGKS VLLSDTVGFI SDLPIQLVEA FQSTLEEVVE ADILMHVVDS TAPNIEEHRS TVFHVLNQIG VSEEKLQNMI EVWNKIDYEV EEEVEDVKFL GEGEGEGEGE GEEEEEAELN DGLKAEETVD AFVDEGEIKN QDDDSDGWLL CEDENVSESE LWKVPEVAKL DAVQNKGPHV RVSALTGVGL KELLYLINEK VEVLVEKRLK PQTIVESSEL HRRKWRPPRD DDEDARLLPL DQR // ID R0L396_ANAPL Unreviewed; 409 AA. AC R0L396; DT 26-JUN-2013, integrated into UniProtKB/TrEMBL. DT 26-JUN-2013, sequence version 1. DT 30-AUG-2017, entry version 25. DE SubName: Full=GTP binding protein 6 (putative) {ECO:0000313|Ensembl:ENSAPLP00000005156}; DE SubName: Full=Putative GTP-binding protein 6 {ECO:0000313|EMBL:EOB00064.1}; DE Flags: Fragment; GN Name=GTPBP6 {ECO:0000313|Ensembl:ENSAPLP00000005156}; GN ORFNames=Anapl_12528 {ECO:0000313|EMBL:EOB00064.1}; OS Anas platyrhynchos (Mallard) (Anas boschas). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda; OC Coelurosauria; Aves; Neognathae; Galloanserae; Anseriformes; Anatidae; OC Anas. OX NCBI_TaxID=8839 {ECO:0000313|EMBL:EOB00064.1}; RN [1] {ECO:0000313|EMBL:EOB00064.1, ECO:0000313|Ensembl:ENSAPLP00000005156} RP NUCLEOTIDE SEQUENCE. RA Li N.; RT "The genome sequence and transcriptome of duck provide insight into RT the interaction host."; RL Submitted (APR-2010) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Ensembl:ENSAPLP00000005156} RP NUCLEOTIDE SEQUENCE. RX PubMed=23749191; DOI=10.1038/ng.2657; RA Huang Y., Li Y., Burt D.W., Chen H., Zhang Y., Qian W., Kim H., RA Gan S., Zhao Y., Li J., Yi K., Feng H., Zhu P., Li B., Liu Q., RA Fairley S., Magor K.E., Du Z., Hu X., Goodman L., Tafer H., Vignal A., RA Lee T., Kim K.W., Sheng Z., An Y., Searle S., Herrero J., RA Groenen M.A., Crooijmans R.P., Faraut T., Cai Q., Webster R.G., RA Aldridge J.R., Warren W.C., Bartschat S., Kehr S., Marz M., RA Stadler P.F., Smith J., Kraus R.H., Zhao Y., Ren L., Fei J., RA Morisson M., Kaiser P., Griffin D.K., Rao M., Pitel F., Wang J., RA Li N.; RT "The duck genome and transcriptome provide insight into an avian RT influenza virus reservoir species."; RL Nat. Genet. 45:776-783(2013). RN [3] {ECO:0000313|Ensembl:ENSAPLP00000005156} RP IDENTIFICATION. RG Ensembl; RL Submitted (SEP-2013) to UniProtKB. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADON01083696; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; KB743240; EOB00064.1; -; Genomic_DNA. DR Ensembl; ENSAPLT00000005784; ENSAPLP00000005156; ENSAPLG00000005592. DR GeneTree; ENSGT00390000001397; -. DR OMA; MDTVGFM; -. DR OrthoDB; EOG091G0852; -. DR Proteomes; UP000016666; Unassembled WGS sequence. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR CDD; cd01878; HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000016666}; KW Reference proteome {ECO:0000313|Proteomes:UP000016666}. FT DOMAIN 183 347 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT NON_TER 1 1 {ECO:0000313|EMBL:EOB00064.1}. FT NON_TER 409 409 {ECO:0000313|EMBL:EOB00064.1}. SQ SEQUENCE 409 AA; 46237 MW; C5CDAB684FA9C693 CRC64; VSKAELQIAE AVALVDTLPN WTVLDKIIIP TKNPDKKFVF GKGNFDVLTE KIKKMPHVTA VFLNVERISS VTKKELEDAW GVKVFDRYTV VLHIFRCNAR TKEAKLQIAL AEIPLLRSNL KNEVSQLDQQ RGGSRYIMGS GETFMETQNR LLKEKELKIR HVLEKLRRKR SLLRTQRRKR EFPVISVMGY TNCGKTTLIK ALTGEAGLQP RDQLFATLDI TAHAGYLPSH MAVIYVDTIG FLSDLPHNLV ESFSATLEEV AYSDLIVHVR DITHPETVLQ KASVLSVLKN LNLPSHLLES MVEVHNKVDL IERYEPTEEN TLAISALHGH GLEELKEEIE KKILKATGKK ILTIKVNLQG PQLSWLYKEA TVQEVEVMPE DGTAMVTVII SNSAFGKYRN LFPSSTFFI // ID R1AVL3_9CLOT Unreviewed; 428 AA. AC R1AVL3; DT 26-JUN-2013, integrated into UniProtKB/TrEMBL. DT 26-JUN-2013, sequence version 1. DT 07-JUN-2017, entry version 30. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=L21TH_1303 {ECO:0000313|EMBL:EOD00702.1}; OS Caldisalinibacter kiritimatiensis. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Caldisalinibacter. OX NCBI_TaxID=1304284 {ECO:0000313|EMBL:EOD00702.1, ECO:0000313|Proteomes:UP000013378}; RN [1] {ECO:0000313|EMBL:EOD00702.1, ECO:0000313|Proteomes:UP000013378} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=L21-TH-D2 {ECO:0000313|EMBL:EOD00702.1, RC ECO:0000313|Proteomes:UP000013378}; RA Ben Hania W., Joseph M., Fiebig A., Bunk B., Klenk H.-P., RA Fardeau M.-L., Spring S.; RT "Caldisalinibacter kiritimatiensis gen. nov., sp. nov., a moderately RT thermohalophilic thiosulfate-reducing bacterium from a hypersaline RT microbial mat."; RL Geomicrobiol. J. 32:347-354(2015). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EOD00702.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ARZA01000130; EOD00702.1; -; Genomic_DNA. DR RefSeq; WP_006312101.1; NZ_ARZA01000130.1. DR EnsemblBacteria; EOD00702; EOD00702; L21TH_1303. DR PATRIC; fig|1304284.3.peg.1273; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000013378; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000013378}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000013378}. FT DOMAIN 203 374 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 169 196 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 428 AA; 48850 MW; 1432065515E8AF58 CRC64; MLTDIKNNKK ERVLLVGVDT KKINDFNIKS SIEELKELAL AAETEVVECI IQKRDSIDPR LYIGKGKATE IARYCDELDV DTVVFNDELS GAQLRNLEEV IDRKIIDRTN LILDIFAKRA TSKEGKLQVE LAQLKYRLPR LIGLGNQLSR TGGGIGTRGP GEKKLEIDRR HILKRISEIE KQLQGLEEVR ETKRKKRQGS SLPIVALVGY TNAGKSTLLN TLISKDETYT KEKEVFAYDM LFATLDTTLR RGTLPNGQNF LITDTVGFVS KLPTHLIEAF KGTLEEVKYA DLILHVVDIT NEDLDIQVKT TLEILKDLEV LNKPIITVFN KVDKGHIDEI HYKIDGTKVY ISAKEGKNID LLFKMIEENI PDKFYDVKLL IPYDNSKISS YLFDNTKVVK FEYRDNGTLI ETILNEIDYK KYSEYIVD // ID R1B8D5_EMIHU Unreviewed; 113 AA. AC R1B8D5; DT 26-JUN-2013, integrated into UniProtKB/TrEMBL. DT 26-JUN-2013, sequence version 1. DT 07-JUN-2017, entry version 20. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EOD05898.1, ECO:0000313|EnsemblProtists:EOD05898}; DE Flags: Fragment; GN ORFNames=EMIHUDRAFT_47551 {ECO:0000313|EMBL:EOD05898.1}; OS Emiliania huxleyi (Pontosphaera huxleyi). OC Eukaryota; Haptophyceae; Isochrysidales; Noelaerhabdaceae; Emiliania. OX NCBI_TaxID=2903 {ECO:0000313|EMBL:EOD05898.1}; RN [1] {ECO:0000313|EMBL:EOD05898.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=CCMP1516 {ECO:0000313|EMBL:EOD05898.1}; RG DOE Joint Genome Institute; RA Read B., Kegel J., Klute M., Kuo A., Lefebvre S.C., Maumus F., RA Mayer C., Miller J., Allen A., Bidle K., Borodovsky M., Bowler C., RA Brownlee C., Claverie J.-M., Cock M., De Vargas C., Elias M., RA Frickenhaus S., Gladyshev V.N., Gonzalez K., Guda C., Hadaegh A., RA Herman E., Iglesias-Rodriguez D., Jones B., Lawson T., Leese F., RA Lin Y.-C., Lindquist E., Lobanov A., Lucas S., Malik S.-H.B., RA Marsh M.E., Mock T., Monier A., Moreau H., Mueller-Roeber B., RA Napier J., Ogata H., Parker M., Probert I., Quesneville H., Raines C., RA Rensing S., Riano-Pachon D.M., Richier S., Rokitta S., Salamov A., RA Sarno A.F., Schmutz J., Schroeder D., Shiraiwa Y., Soanes D.M., RA Valentin K., Van Der Giezen M., Van Der Peer Y., Vardi A., Verret F., RA Von Dassow P., Wheeler G., Williams B., Wilson W., Wolfe G., RA Wurch L.L., Young J., Dacks J.B., Delwiche C.F., Dyhrman S., RA Glockner G., John U., Richards T., Worden A.Z., Zhang X., RA Grigoriev I.V.; RT "Genome variability drives Emilianias global distribution."; RL Submitted (JUL-2012) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EnsemblProtists:EOD05898, ECO:0000313|Proteomes:UP000013827} RP NUCLEOTIDE SEQUENCE. RC STRAIN=CCMP1516 {ECO:0000313|EnsemblProtists:EOD05898, RC ECO:0000313|Proteomes:UP000013827}; RX PubMed=23760476; DOI=10.1038/nature12221; RA Read B.A., Kegel J., Klute M.J., Kuo A., Lefebvre S.C., Maumus F., RA Mayer C., Miller J., Monier A., Salamov A., Young J., Aguilar M., RA Claverie J.M., Frickenhaus S., Gonzalez K., Herman E.K., Lin Y.C., RA Napier J., Ogata H., Sarno A.F., Shmutz J., Schroeder D., RA de Vargas C., Verret F., von Dassow P., Valentin K., Van de Peer Y., RA Wheeler G., Dacks J.B., Delwiche C.F., Dyhrman S.T., Glockner G., RA John U., Richards T., Worden A.Z., Zhang X., Grigoriev I.V., RA Allen A.E., Bidle K., Borodovsky M., Bowler C., Brownlee C., RA Cock J.M., Elias M., Gladyshev V.N., Groth M., Guda C., Hadaegh A., RA Iglesias-Rodriguez M.D., Jenkins J., Jones B.M., Lawson T., Leese F., RA Lindquist E., Lobanov A., Lomsadze A., Malik S.B., Marsh M.E., RA Mackinder L., Mock T., Mueller-Roeber B., Pagarete A., Parker M., RA Probert I., Quesneville H., Raines C., Rensing S.A., RA Riano-Pachon D.M., Richier S., Rokitta S., Shiraiwa Y., Soanes D.M., RA van der Giezen M., Wahlund T.M., Williams B., Wilson W., Wolfe G., RA Wurch L.L.; RT "Pan genome of the phytoplankton Emiliania underpins its global RT distribution."; RL Nature 499:209-213(2013). RN [3] {ECO:0000313|EnsemblProtists:EOD05898} RP IDENTIFICATION. RG EnsemblProtists; RL Submitted (JAN-2017) to UniProtKB. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; KB869934; EOD05898.1; -; Genomic_DNA. DR RefSeq; XP_005758327.1; XM_005758270.1. DR EnsemblProtists; EOD05898; EOD05898; EMIHUDRAFT_47551. DR GeneID; 17252107; -. DR KEGG; ehx:EMIHUDRAFT_47551; -. DR KO; K03665; -. DR Proteomes; UP000013827; Unassembled WGS sequence. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000013827}; KW Reference proteome {ECO:0000313|Proteomes:UP000013827}. FT DOMAIN 2 76 GTP-bdg_N. {ECO:0000259|Pfam:PF13167}. FT DOMAIN 91 113 GTP-bdg_M. {ECO:0000259|Pfam:PF16360}. FT NON_TER 1 1 {ECO:0000313|EMBL:EOD05898.1}. FT NON_TER 113 113 {ECO:0000313|EMBL:EOD05898.1}. SQ SEQUENCE 113 AA; 12471 MW; F67767F5EB16B9E5 CRC64; DSLDELKRLC DTAGLDVRGR CCQAVQHPSA ATFVGSGKLE EIRDSVEALA PGGDGGGTVV FDDELSPAQQ RNLQLTRPRP VPLRLQIFAQ RARTREAKLQ VTLARMRYML PRL // ID R1DW15_EMIHU Unreviewed; 549 AA. AC R1DW15; DT 26-JUN-2013, integrated into UniProtKB/TrEMBL. DT 26-JUN-2013, sequence version 1. DT 07-JUN-2017, entry version 25. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EOD18700.1, ECO:0000313|EnsemblProtists:EOD18700}; GN ORFNames=EMIHUDRAFT_470200 {ECO:0000313|EMBL:EOD18700.1}; OS Emiliania huxleyi (Pontosphaera huxleyi). OC Eukaryota; Haptophyceae; Isochrysidales; Noelaerhabdaceae; Emiliania. OX NCBI_TaxID=2903 {ECO:0000313|EMBL:EOD18700.1}; RN [1] {ECO:0000313|EMBL:EOD18700.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=CCMP1516 {ECO:0000313|EMBL:EOD18700.1}; RG DOE Joint Genome Institute; RA Read B., Kegel J., Klute M., Kuo A., Lefebvre S.C., Maumus F., RA Mayer C., Miller J., Allen A., Bidle K., Borodovsky M., Bowler C., RA Brownlee C., Claverie J.-M., Cock M., De Vargas C., Elias M., RA Frickenhaus S., Gladyshev V.N., Gonzalez K., Guda C., Hadaegh A., RA Herman E., Iglesias-Rodriguez D., Jones B., Lawson T., Leese F., RA Lin Y.-C., Lindquist E., Lobanov A., Lucas S., Malik S.-H.B., RA Marsh M.E., Mock T., Monier A., Moreau H., Mueller-Roeber B., RA Napier J., Ogata H., Parker M., Probert I., Quesneville H., Raines C., RA Rensing S., Riano-Pachon D.M., Richier S., Rokitta S., Salamov A., RA Sarno A.F., Schmutz J., Schroeder D., Shiraiwa Y., Soanes D.M., RA Valentin K., Van Der Giezen M., Van Der Peer Y., Vardi A., Verret F., RA Von Dassow P., Wheeler G., Williams B., Wilson W., Wolfe G., RA Wurch L.L., Young J., Dacks J.B., Delwiche C.F., Dyhrman S., RA Glockner G., John U., Richards T., Worden A.Z., Zhang X., RA Grigoriev I.V.; RT "Genome variability drives Emilianias global distribution."; RL Submitted (JUL-2012) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EnsemblProtists:EOD18700, ECO:0000313|Proteomes:UP000013827} RP NUCLEOTIDE SEQUENCE. RC STRAIN=CCMP1516 {ECO:0000313|EnsemblProtists:EOD18700, RC ECO:0000313|Proteomes:UP000013827}; RX PubMed=23760476; DOI=10.1038/nature12221; RA Read B.A., Kegel J., Klute M.J., Kuo A., Lefebvre S.C., Maumus F., RA Mayer C., Miller J., Monier A., Salamov A., Young J., Aguilar M., RA Claverie J.M., Frickenhaus S., Gonzalez K., Herman E.K., Lin Y.C., RA Napier J., Ogata H., Sarno A.F., Shmutz J., Schroeder D., RA de Vargas C., Verret F., von Dassow P., Valentin K., Van de Peer Y., RA Wheeler G., Dacks J.B., Delwiche C.F., Dyhrman S.T., Glockner G., RA John U., Richards T., Worden A.Z., Zhang X., Grigoriev I.V., RA Allen A.E., Bidle K., Borodovsky M., Bowler C., Brownlee C., RA Cock J.M., Elias M., Gladyshev V.N., Groth M., Guda C., Hadaegh A., RA Iglesias-Rodriguez M.D., Jenkins J., Jones B.M., Lawson T., Leese F., RA Lindquist E., Lobanov A., Lomsadze A., Malik S.B., Marsh M.E., RA Mackinder L., Mock T., Mueller-Roeber B., Pagarete A., Parker M., RA Probert I., Quesneville H., Raines C., Rensing S.A., RA Riano-Pachon D.M., Richier S., Rokitta S., Shiraiwa Y., Soanes D.M., RA van der Giezen M., Wahlund T.M., Williams B., Wilson W., Wolfe G., RA Wurch L.L.; RT "Pan genome of the phytoplankton Emiliania underpins its global RT distribution."; RL Nature 499:209-213(2013). RN [3] {ECO:0000313|EnsemblProtists:EOD18700} RP IDENTIFICATION. RG EnsemblProtists; RL Submitted (JAN-2017) to UniProtKB. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; KB866402; EOD18700.1; -; Genomic_DNA. DR RefSeq; XP_005771129.1; XM_005771072.1. DR EnsemblProtists; EOD18700; EOD18700; EMIHUDRAFT_470200. DR GeneID; 17264252; -. DR KEGG; ehx:EMIHUDRAFT_470200; -. DR KO; K03665; -. DR Proteomes; UP000013827; Unassembled WGS sequence. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR CDD; cd01878; HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000013827}; KW Reference proteome {ECO:0000313|Proteomes:UP000013827}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1 17 {ECO:0000256|SAM:SignalP}. FT CHAIN 18 549 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5009720815. FT DOMAIN 295 470 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 549 AA; 57960 MW; 3DAD0136A1C543A5 CRC64; MPALLFLPCA AAAVVLPLRP APCARAAAAA MQAGSEQTIS SGGAFGSEDI TIRSGAAYLV GLDIRRERYK TLAGNAERGA AWTLDDSLDE LKRLCDTAGL DVRGRCCQAV QHPSAATFVG SGKLEEIRDS VEALAPGGDG GGVFFPPLAR PRLAPQALRI ETVVFDDELS PAQQRNLQSA LGVVDRTMLI LQAPSPPPSL SEPVVAVAMT GARLTRPRPV PLRLQIFAQR ARTREAKLQV TLARMRYMLP RLKSFMTTGA GMDAKGGAAG GGKGAQRALP LEGRRWDASP TCTMPLVALV GYTNAGKSSL LNQLCAKVEG GEEVYADDQL FATLDPTLRR LRLAWRAGGV GFIQKLPTKL VSAFRATLEA SVCEDADVVL HVVDSSSPIG RQQAWSVQQI LREVGAEHTP QILALNKADA VLAATAKLPA PTEWVSLHDT VSPTYAVAIS ATQGKNLPKL LSAALLSLSV RVSCVLPYAN GELLAEMHKV GTIVEEEYVD TGCRVVAYVP RPLASRLGKL LGDGEGRSRV EIGAGSKALE SVGDSSPAD // ID R2Q8C9_9ENTE Unreviewed; 413 AA. AC R2Q8C9; DT 26-JUN-2013, integrated into UniProtKB/TrEMBL. DT 26-JUN-2013, sequence version 1. DT 07-JUN-2017, entry version 28. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=UAW_02796 {ECO:0000313|EMBL:EOH92757.1}; OS Enterococcus haemoperoxidus ATCC BAA-382. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Enterococcaceae; OC Enterococcus. OX NCBI_TaxID=1158608 {ECO:0000313|EMBL:EOH92757.1, ECO:0000313|Proteomes:UP000013858}; RN [1] {ECO:0000313|EMBL:EOH92757.1, ECO:0000313|Proteomes:UP000013858} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-382 {ECO:0000313|EMBL:EOH92757.1, RC ECO:0000313|Proteomes:UP000013858}; RG The Broad Institute Genome Sequencing Platform; RG The Broad Institute Genome Sequencing Center for Infectious Disease; RA Earl A.M., Gilmore M.S., Lebreton F., Walker B., Young S.K., Zeng Q., RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L., RA Arachchi H.M., Berlin A.M., Chapman S.B., Dewar J., Goldberg J., RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Larimer J., RA McCowan C., Murphy C., Neiman D., Pearson M., Priest M., Roberts A., RA Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C., RA Birren B.; RT "The Genome Sequence of Enterococcus haemoperoxidus BAA-382."; RL Submitted (FEB-2013) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EOH92757.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AJAR01000027; EOH92757.1; -; Genomic_DNA. DR RefSeq; WP_010762954.1; NZ_KE136479.1. DR EnsemblBacteria; EOH92757; EOH92757; UAW_02796. DR GeneID; 29839726; -. DR PATRIC; fig|1158608.3.peg.2732; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000013858; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000013858}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000013858}. FT DOMAIN 197 359 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 413 AA; 46708 MW; 95BED040C6CF3301 CRC64; MDKIAEKVIL VGVETEGNYT RFEGSMKELK NLTKTAQGEV VFSLTQKRPR IDSQTVIGKG KVEELMQLVD AYEADIVIFN HELTPRQNQL IVEAVGVKVI DRVQLILDIF AMRARSKEGK LQVELAQLNY LLPRLVGQGK QLSRLGGGIG TRGPGETKLE SDRRHIRDKI IAIKRELKEV SAHRERSRQK RQSSDLFQIG LLGYTNAGKS TILNLLTTAG TYSENQLFAT LDPLTKKWQL PQGMIVTLTD TVGFIQDLPT QLIEAFQSTL EESRGMDLLL HVVDASAEDR LQHEQTVVDL LNDLDLEKIP VLTVYNKSDQ VDEADFVPTL FPNILVSARS TLGKEELTKA VREKMMELLV PYELDIPSNQ GQQLSELKRH TLLLSETFEE EENVYHVKGF AKKDSKWTRE LDE // ID R2QHY5_9ENTE Unreviewed; 414 AA. AC R2QHY5; DT 26-JUN-2013, integrated into UniProtKB/TrEMBL. DT 26-JUN-2013, sequence version 1. DT 07-JUN-2017, entry version 29. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=UAU_00851 {ECO:0000313|EMBL:EOH96202.1}; OS Enterococcus pallens ATCC BAA-351. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Enterococcaceae; OC Enterococcus. OX NCBI_TaxID=1158607 {ECO:0000313|EMBL:EOH96202.1, ECO:0000313|Proteomes:UP000013782}; RN [1] {ECO:0000313|EMBL:EOH96202.1, ECO:0000313|Proteomes:UP000013782} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-351 {ECO:0000313|EMBL:EOH96202.1, RC ECO:0000313|Proteomes:UP000013782}; RG The Broad Institute Genome Sequencing Platform; RG The Broad Institute Genome Sequencing Center for Infectious Disease; RA Earl A.M., Gilmore M.S., Lebreton F., Walker B., Young S.K., Zeng Q., RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L., RA Arachchi H.M., Berlin A.M., Chapman S.B., Dewar J., Goldberg J., RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Larimer J., RA McCowan C., Murphy C., Neiman D., Pearson M., Priest M., Roberts A., RA Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C., RA Birren B.; RT "The Genome Sequence of Enterococcus pallens BAA-351."; RL Submitted (FEB-2013) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EOH96202.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AJAQ01000008; EOH96202.1; -; Genomic_DNA. DR RefSeq; WP_010755907.1; NZ_KB946300.1. DR EnsemblBacteria; EOH96202; EOH96202; UAU_00851. DR PATRIC; fig|1158607.3.peg.851; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000013782; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000013782}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000013782}. FT DOMAIN 194 360 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 160 190 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 414 AA; 46941 MW; 147AEC82A69BA48D CRC64; MSEKVILVGV ETEENKQNYL ESMHELAGLT KTAHGEIVFS MTQKRPKVDR QTIIGKGKVE ELAQLVDAHE AELVIFNHAM TPRQSQTVEE IIGVPVIDRI QLILDIFAQR ARSKEGKLQV ELAQLNYLLP RLMGQGHSLS RLGGGIGTRG PGETKLETDR RHIRNRISAI KKELKNVEAH RERSRQKRQQ SNIFQMGLIG YTNAGKSTIL NLLTNAETYS KDQLFATLDP LTKRWQLPQG MQATITDTVG FIQDLPTQLI DAFHSTLEES KGMDLLLHVV DASSEDRLQQ EQTVMNLLKE LEMDDIPILT IYNKADRIDP FAFTPTLFPN TLISAKSSKG KEILAEAIKK EIMELLEPYL LTIKAEDGQS LHAIRRESLV LSETFEEEKE VYQIRGFAKK SSVWIRRMDD ELDS // ID R2SCR9_9ENTE Unreviewed; 413 AA. AC R2SCR9; DT 26-JUN-2013, integrated into UniProtKB/TrEMBL. DT 26-JUN-2013, sequence version 1. DT 07-JUN-2017, entry version 29. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=UAS_00400 {ECO:0000313|EMBL:EOH90671.1}; OS Enterococcus asini ATCC 700915. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Enterococcaceae; OC Enterococcus. OX NCBI_TaxID=1158606 {ECO:0000313|EMBL:EOH90671.1, ECO:0000313|Proteomes:UP000013777}; RN [1] {ECO:0000313|EMBL:EOH90671.1, ECO:0000313|Proteomes:UP000013777} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700915 {ECO:0000313|EMBL:EOH90671.1, RC ECO:0000313|Proteomes:UP000013777}; RG The Broad Institute Genome Sequencing Platform; RG The Broad Institute Genome Sequencing Center for Infectious Disease; RA Earl A.M., Gilmore M.S., Lebreton F., Walker B., Young S.K., Zeng Q., RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L., RA Arachchi H.M., Berlin A.M., Chapman S.B., Dewar J., Goldberg J., RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Larimer J., RA McCowan C., Murphy C., Neiman D., Pearson M., Priest M., Roberts A., RA Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C., RA Birren B.; RT "The Genome Sequence of Enterococcus asini ATCC_700915."; RL Submitted (FEB-2013) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EOH90671.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AJAP01000004; EOH90671.1; -; Genomic_DNA. DR EnsemblBacteria; EOH90671; EOH90671; UAS_00400. DR PATRIC; fig|1158606.3.peg.385; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000013777; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000013777}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000013777}. FT DOMAIN 196 358 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 413 AA; 46491 MW; BBDA703AEE9DF899 CRC64; MEAKQERVIL VGVETEETWR NFGESMLELK GLTKTAKGTV CFSLIQKRPQ VDRQTVIGKG KLAELRQLVE AHEADLVIFN HELSPRQSQL IQDQVEVPVI DRVQLILDIF AMRARSKEGK LQVELAQLEY LLPRLVGQGK NLSRLGGGIG TRGPGETKLE TDRRHIRNRI TGIKRELKEV AAHRERTRQK RQSQVFQIGL IGYTNAGKST ILNLLTSAAT YEQDALFATL DPLTKQWCLP EGFQVTVTDT VGFIQDLPTQ LIDAFHSTLE ESRNMDLLLH VVDAASPDRQ QQEATVMALM EELDFAHIPL LTVYNKADKL EGAQFVPTLF PNVLISAKSS RGKADLTEAI KLRLMEILEP YSLAVPQSEG KWLSRLKKET LLLSEEYQED SQSYLVKGFV PEGASVVRKK EEP // ID R3X406_9ENTE Unreviewed; 417 AA. AC R3X406; DT 26-JUN-2013, integrated into UniProtKB/TrEMBL. DT 26-JUN-2013, sequence version 1. DT 07-JUN-2017, entry version 30. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=UC3_00326 {ECO:0000313|EMBL:EOL48775.1}; OS Enterococcus phoeniculicola ATCC BAA-412. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Enterococcaceae; OC Enterococcus. OX NCBI_TaxID=1158610 {ECO:0000313|EMBL:EOL48775.1, ECO:0000313|Proteomes:UP000013785}; RN [1] {ECO:0000313|EMBL:EOL48775.1, ECO:0000313|Proteomes:UP000013785} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-412 {ECO:0000313|EMBL:EOL48775.1, RC ECO:0000313|Proteomes:UP000013785}; RG The Broad Institute Genome Sequencing Platform; RG The Broad Institute Genome Sequencing Center for Infectious Disease; RA Earl A.M., Gilmore M.S., Lebreton F., Walker B., Young S.K., Zeng Q., RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L., RA Arachchi H.M., Berlin A.M., Chapman S.B., Dewar J., Goldberg J., RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Larimer J., RA McCowan C., Murphy C., Neiman D., Pearson M., Priest M., Roberts A., RA Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C., RA Birren B.; RT "The Genome Sequence of Enterococcus phoeniculicola BAA-412."; RL Submitted (FEB-2013) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EOL48775.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AJAT01000007; EOL48775.1; -; Genomic_DNA. DR RefSeq; WP_010767001.1; NZ_KB946326.1. DR EnsemblBacteria; EOL48775; EOL48775; UC3_00326. DR PATRIC; fig|1158610.3.peg.300; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000013785; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000013785}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000013785}. FT DOMAIN 197 367 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 417 AA; 47560 MW; C03E991372F532E7 CRC64; MEKPQEKVII VGVETDENTK NFQESMEELK SLTKTANGEV VYSVTQKRKQ VDRQTLIGKG KLEELVQLAD AYEADLIIFN HELSPRQSQL INDAIGLPVI DRVQLILDIF AMRARSKEGK LQVALAQLNY LLPRLVGQGK ALSRLGGGIG TRGPGETKLE TDRRHIRNKI TVIKRELKEV SAHRQRNRQK RKQADVFQIG LIGYTNAGKS TLLNLLTNGE TYAKDQLFAT LDPLTKKWRL PEGLEVTLTD TVGFIQDLPT QLIDAFHSTL EESKEMNLLL HVVDASAEDR IQQEATVMQL IEELQLNQLP ILTVYNKADQ IEEDQFTPTL FPNVLISARS QEGKQAVTKA IRLQLMELME PYALEIPSHE GQELNEIKRK TFVFSEEYEE QTNDYAIKGF AMKNSRWVRK TEDREFF // ID R4K5I8_CLOPA Unreviewed; 594 AA. AC R4K5I8; DT 24-JUL-2013, integrated into UniProtKB/TrEMBL. DT 24-JUL-2013, sequence version 1. DT 07-JUN-2017, entry version 30. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=Clopa_3010 {ECO:0000313|EMBL:AGK97838.1}; OS Clostridium pasteurianum BC1. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=86416 {ECO:0000313|EMBL:AGK97838.1, ECO:0000313|Proteomes:UP000013523}; RN [1] {ECO:0000313|EMBL:AGK97838.1, ECO:0000313|Proteomes:UP000013523} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BC1 {ECO:0000313|EMBL:AGK97838.1, RC ECO:0000313|Proteomes:UP000013523}; RG US DOE Joint Genome Institute; RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S., RA Peters L., Mikhailova N., Teshima H., Detter J.C., Han C., Tapia R., RA Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Dunn J., RA Taghavi S., Francis A., van der Lelie D., Woyke T.; RT "Complete sequence of chromosome of Clostridium pasteurianum BC1."; RL Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP003261; AGK97838.1; -; Genomic_DNA. DR RefSeq; WP_015616130.1; NC_021182.1. DR EnsemblBacteria; AGK97838; AGK97838; Clopa_3010. DR KEGG; cpas:Clopa_3010; -. DR PATRIC; fig|86416.3.peg.2997; -. DR KO; K03665; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000013523; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000013523}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000013523}. FT DOMAIN 364 541 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 594 AA; 66874 MW; 28459C50F03D6FE6 CRC64; MILGNIDGIK NSLLEKLEEI YEMKIPKYNV ITEELADIIC NVTGIINREI SVAIDRRGKV ISVAVGDSST VELPLIDVKE GKLAGVRIVH THPGGNSRLS MIDISALIKL KLDCMVAVGV NEGNITDITI GFCGVYNNVL KPELFGPMNL HKAMDLDLMD KLKYIQDAIK SENIKEDNSE RAILVGIDSE ESLEELAELA RACNVQCVYS VLQKKDKMDT ALYIGSGKVE EISVIRQRLS ANVIIFDDEL AGSQVRNLEE VLGVKVIDRT TLILEIFAKR ARSREAKIQA ELAQLKYRAA RLMGLGSVLS RTGGGIGTRG PGEKKLEIDR RHIRERVYDL TKELEKVRKN REIQREKRTN ENIPKISLVG YTNAGKSTLR NKLCEMAAPN DSAKKESVFE ADMLFATLDV TTRAIVLPDN RIATLTDTVG FVRKLPHDLV EAFKSTLEEV IYADLLLHVI DTSNENVIKQ IEAVERVLLE LGAGKKPVIL ILNKIDKAEV SQIQYIENKY KTLHIVEISA KENRNLDVLL EEICKDLPNN LKRVEYLIPY TSQSEVAYLH RNSKIYEEEF LEEGTKIVAE VDDRIYNRYL KYRV // ID R4KTF9_9FIRM Unreviewed; 596 AA. AC R4KTF9; DT 24-JUL-2013, integrated into UniProtKB/TrEMBL. DT 24-JUL-2013, sequence version 1. DT 07-JUN-2017, entry version 27. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=Desgi_4663 {ECO:0000313|EMBL:AGL03890.1}; OS Desulfotomaculum gibsoniae DSM 7213. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Peptococcaceae; OC Desulfotomaculum. OX NCBI_TaxID=767817 {ECO:0000313|EMBL:AGL03890.1, ECO:0000313|Proteomes:UP000013520}; RN [1] {ECO:0000313|EMBL:AGL03890.1, ECO:0000313|Proteomes:UP000013520} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 7213 {ECO:0000313|EMBL:AGL03890.1, RC ECO:0000313|Proteomes:UP000013520}; RG US DOE Joint Genome Institute; RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S., RA Peters L., Ovchinnikova G., Teshima H., Detter J.C., Han C., Tapia R., RA Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Parshina S., RA Plugge C., Muyzer G., Kuever J., Ivanova A., Nazina T., Klenk H.-P., RA Brambilla E., Spring S., Stams A.F., Woyke T.; RT "Complete sequence of Desulfotomaculum gibsoniae DSM 7213."; RL Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP003273; AGL03890.1; -; Genomic_DNA. DR RefSeq; WP_006522266.1; NC_021184.1. DR EnsemblBacteria; AGL03890; AGL03890; Desgi_4663. DR KEGG; dgi:Desgi_4663; -. DR KO; K03665; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000013520; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000013520}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000013520}. FT DOMAIN 375 540 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 341 368 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 596 AA; 65909 MW; 0EFEF4D1CC2BDE89 CRC64; MTKTVYGNTR GLKKVDLDLL QGIYELAIDK NMIISLEIAQ IMAVISSSNQ RELVVFMDRQ GRVASVGVGD AATVQLKAQS RRRGEHRLAG LRCIHTHPSG SGQLSAVDYA ALYDMRLDVM VALGVQDGKI KEACLACLEP RDGQLTQNFQ NFGPMSFAQL AAFPLTALIQ DIEDSIKPPA AVSTSKTRQI EKAILVTIAG EDTLDELALL ADTAGATPVA RVTQHRKKPD TAFFIGRGKV EELALHRQSL GAELVIFDDE LTPTQARNLE HAIGCRIVDR TTLILDIFAQ RARTKEGKLQ VELAQLRYLL PRLTGLGTAL SRLGGGIGTR GPGETKLETD RRHIRRRIDE LTNALEQVRR HRQQQRQNRR ESASPVVALV GYTNAGKSTL LNALTQAQVY TANQLFATLD TTTRRLQLPG NREVLLTDTV GFIRKLPHHL VKAFRATLEE VIEADLLLHV VDASHAGLAE QIAAVEAVLK ELGVQDKHTI LVFNKIDQPV NHQLLEQVKL SYHCQFVEVS AHTGTGLEQL KELIAQNTLH QQRLLKGRLP YDRTDLVALL HQHGKVYSEK YGPEGIQVEA AVDECYWAAL APYLKT // ID R4LLJ1_9ACTN Unreviewed; 465 AA. AC R4LLJ1; DT 24-JUL-2013, integrated into UniProtKB/TrEMBL. DT 24-JUL-2013, sequence version 1. DT 07-JUN-2017, entry version 28. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:AGL20247.1}; GN ORFNames=L083_6737 {ECO:0000313|EMBL:AGL20247.1}; OS Actinoplanes sp. N902-109. OC Bacteria; Actinobacteria; Micromonosporales; Micromonosporaceae; OC Actinoplanes. OX NCBI_TaxID=649831 {ECO:0000313|EMBL:AGL20247.1, ECO:0000313|Proteomes:UP000013541}; RN [1] {ECO:0000313|EMBL:AGL20247.1, ECO:0000313|Proteomes:UP000013541} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=N902-109 {ECO:0000313|EMBL:AGL20247.1, RC ECO:0000313|Proteomes:UP000013541}; RA Hu H., Huang H., Lu X., Zhu B.; RT "Comparative analysis of rapamycin biosynthesis clusters between RT Streptomyces hygroscopicus ATCC 29253 and Actinoplanes sp. N902-109."; RL Submitted (MAY-2013) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP005929; AGL20247.1; -; Genomic_DNA. DR RefSeq; WP_015624804.1; NC_021191.1. DR EnsemblBacteria; AGL20247; AGL20247; L083_6737. DR KEGG; actn:L083_6737; -. DR PATRIC; fig|649831.3.peg.6669; -. DR KO; K03665; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000013541; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 2. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000013541}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000013541}. FT DOMAIN 247 412 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 206 233 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 465 AA; 50813 MW; FCEB247328474802 CRC64; MRTELFEPDV TTGELELEER HSLRRVAGLS TELTDITEVE YRQLRLERVV LVGVWTEGSV ADAENSLTEL AALAETAGSE VLEGLIQRRG RPDPATFIGR GKVDELRDVV VASGADTVIC DGELSPSQLR NLEQQTKVKV IDRTALILDI FAQHAKSKEG KAQVELAQLQ YFLPRLRGWG ESLSRQGGGA GGGSGGGGVG TRGPGETKLE TDRRRINQRI AKLRREIKAM RTVRQTKRSR RSTSGVPAVA IAGYTNAGKS SLLNRLTSAG VLVEDALFAT LDPTTRRTAA EDGRVFTLSD TVGFVRHLPH QIVEAFRSTL EEVAYADLVV HVVDGAHPDP EGQVSAVREV LAEVGADRIP ELLVVNKVDA ADEETMLRLK RTWPDAVFAS ARSGLGIADV HAAIAQRLPR PAVDLRVLLP YDRGDLVARI HRRGQVLDTR HTDEGSELRV RVDEHLAADL AQFRL // ID R4SQS3_AMYOR Unreviewed; 477 AA. AC R4SQS3; DT 24-JUL-2013, integrated into UniProtKB/TrEMBL. DT 24-JUL-2013, sequence version 1. DT 07-JUN-2017, entry version 32. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:AGM04945.1}; GN ORFNames=AORI_2357 {ECO:0000313|EMBL:AGM04945.1}; OS Amycolatopsis orientalis HCCB10007. OC Bacteria; Actinobacteria; Pseudonocardiales; Pseudonocardiaceae; OC Amycolatopsis. OX NCBI_TaxID=1156913 {ECO:0000313|EMBL:AGM04945.1, ECO:0000313|Proteomes:UP000013968}; RN [1] {ECO:0000313|EMBL:AGM04945.1, ECO:0000313|Proteomes:UP000013968} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=HCCB10007 {ECO:0000313|EMBL:AGM04945.1}; RX PubMed=23627759; DOI=10.1186/1471-2164-14-289; RA Tang B., Wang Q., Yang M., Xie F., Zhu Y., Zhuo Y., Wang S., Gao H., RA Ding X., Zhang L., Zhao G., Zheng H.; RT "ContigScape: a Cytoscape plugin facilitating microbial genome gap RT closing."; RL BMC Genomics 14:289-289(2013). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP003410; AGM04945.1; -; Genomic_DNA. DR RefSeq; WP_016332733.1; NC_021252.1. DR EnsemblBacteria; AGM04945; AGM04945; AORI_2357. DR KEGG; aoi:AORI_2357; -. DR PATRIC; fig|1156913.3.peg.2413; -. DR KO; K03665; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000013968; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 2. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000013968}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000013968}. FT DOMAIN 250 419 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 477 AA; 51600 MW; F13B139F2B78A92C CRC64; MTELTHNDLN DMDPSTGELE LEDRASLRRV AGLSTELADV TEVEYRQLRL ERVVLVGVWT EGSALQSEAS LAELARLAET AGSEVLEGLV QRRIRPDPAT YIGSGKVKEL RGIVAATGAD TVICDGELSP GQLRQLEEKV KVKVIDRTAL ILDIFAQHAR SKEGKAQVEL AQLQYLIPRL RGWGAALSRQ AGGRAGGANG GVGLRGPGET KLETDRRRIN KRVAKLRREI AAMDTIRETK RGRRVANEVP SVAIVGYTNA GKSSLLNALT GAGVLVEDAL FATLDPTTRR AQTPDGRTYT LTDTVGFVRH LPHQLVDAFR STLEEAASAD LLVHVVDGSD PTPEEQVNAV REVLAEITKR RSEPLPPELL VINKADAADE VSLARLRHQM AGSVQVSART GTGITELAEV IAERLPRPEV VVEVLIPYSR GELVSRAHAD GEVLEEEHVE TGTRLVVRGR PELAAALSDF QTNGSAL // ID R4V6I0_9GAMM Unreviewed; 427 AA. AC R4V6I0; DT 24-JUL-2013, integrated into UniProtKB/TrEMBL. DT 24-JUL-2013, sequence version 1. DT 30-AUG-2017, entry version 32. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=SPISAL_02725 {ECO:0000313|EMBL:AGM40640.1}; OS Spiribacter salinus M19-40. OC Bacteria; Proteobacteria; Gammaproteobacteria; Chromatiales; OC Ectothiorhodospiraceae; Spiribacter. OX NCBI_TaxID=1260251 {ECO:0000313|EMBL:AGM40640.1, ECO:0000313|Proteomes:UP000017881}; RN [1] {ECO:0000313|EMBL:AGM40640.1, ECO:0000313|Proteomes:UP000017881} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=M19-40 {ECO:0000313|EMBL:AGM40640.1}; RX PubMed=23409269; RA Leon M.J., Ghai R., Fernandez A.B., Sanchez-Porro C., RA Rodriguez-Valera F., Ventosa A.; RT "Draft Genome of Spiribacter salinus M19-40, an Abundant RT Gammaproteobacterium in Aquatic Hypersaline Environments."; RL Genome Announc. 1:E00179-12(2013). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP005963; AGM40640.1; -; Genomic_DNA. DR EnsemblBacteria; AGM40640; AGM40640; SPISAL_02725. DR KEGG; ssal:SPISAL_02725; -. DR PATRIC; fig|1260251.3.peg.549; -. DR KO; K03665; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000017881; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000017881}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000017881}. FT DOMAIN 187 353 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 427 AA; 47267 MW; 68D89945E7811CF0 CRC64; MLVQIDDGFL DADEALREFE ALAVSAGADV CGYQTGRGRR PDAKTYLGPG KVAELQALKS AEQADLVLIN HPLSPVQERN LERELQCRVL DRTGLILDIF AQRARSHEGK LQVELAQLRH IASRLVRGWS HLERQKGGIG LRGPGETQLE MDRRMLGVRI KQLERRLGRV RQQRDQGRQA RRRKDLPAVS MVGYTNAGKS TLFNRVAGSQ VYSANQLFAT LDTTMRRIEL SGGEAAVIAD TVGFIRDLPP QLVAAFRSTL EEVVEAQLLV HVIDASDPLR EDNAREVNSV LDALGADAVP QLLVYNKIDL RGLAPRLERD DEGVARAVWL SAATNEGLDL LREAIAERVA VEQAKGVIEL SPAEGRLRAK FYALGDVLEE EYTEAGHVRL TVEMPQRALN RLYRHEGLEA EWVPLSSSAL PAGRVAH // ID R4VVW8_9EURY Unreviewed; 469 AA. AC R4VVW8; DT 24-JUL-2013, integrated into UniProtKB/TrEMBL. DT 24-JUL-2013, sequence version 1. DT 07-JUN-2017, entry version 23. DE SubName: Full=GTP-binding protein HflX {ECO:0000313|EMBL:AGN00406.1}; GN ORFNames=L593_02275 {ECO:0000313|EMBL:AGN00406.1}; OS Salinarchaeum sp. Harcht-Bsk1. OC Archaea; Euryarchaeota; Halobacteria; Natrialbales; Natrialbaceae; OC Salinarchaeum. OX NCBI_TaxID=1333523 {ECO:0000313|EMBL:AGN00406.1, ECO:0000313|Proteomes:UP000014072}; RN [1] {ECO:0000313|EMBL:AGN00406.1, ECO:0000313|Proteomes:UP000014072} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Harcht-Bsk1 {ECO:0000313|EMBL:AGN00406.1}; RX PubMed=23868130; RA Dominova I.N., Sorokin D.Y., Kublanov I.V., Patrushev M.V., RA Toshchakov S.V.; RT "Complete Genome Sequence of Salinarchaeum sp. Strain HArcht-Bsk1T, RT Isolated from Hypersaline Lake Baskunchak, Russia."; RL Genome Announc. 1:E00505-13(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP005962; AGN00406.1; -; Genomic_DNA. DR RefSeq; WP_020445300.1; NC_021313.1. DR EnsemblBacteria; AGN00406; AGN00406; L593_02275. DR GeneID; 16182861; -. DR KEGG; sali:L593_02275; -. DR PATRIC; fig|1333523.5.peg.461; -. DR KO; K03665; -. DR OrthoDB; POG093Z07D6; -. DR BioCyc; SSP1333523:G13D5-459-MONOMER; -. DR Proteomes; UP000014072; Chromosome. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 2. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 2. DR SUPFAM; SSF52540; SSF52540; 2. DR PROSITE; PS51705; G_HFLX; 1. PE 4: Predicted; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000014072}; KW Reference proteome {ECO:0000313|Proteomes:UP000014072}. FT DOMAIN 188 408 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 102 136 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 469 AA; 51337 MW; 9BC2A5B11BF8688F CRC64; MQAIAVRRRR DEPIDATELR GLAETAGYEV IETVGQRRAE DSTYHVGRGK AEELADLAAE TAADAILVDD RVTPQQAYHL EELCPPETRV LGRYRLVLEI FADRATDRAA QLQVELAELR YERKRVRAAL KLEEDAANER RTLGEFEASE QGEIKHVDER IEALESALES TQVVVEQRRE RRSEQGFDHV AVAGYTNAGK STLLRRLADD EAMTHGSRGA NDDPSAPSGD PIVASEDQSA ANDDPTAAND ANSKHDDLAE RVTVEDRLFE TLETTTRRAT IEGRRVLLTD TVGVVSDLPH WLVRSFRSTL RAVGTADAVL LVLDASAPVD RFETRLATAI ETLTGRTDAP VLPVLNKVDA TDEGTVAERR EQVRERLPET EPIAISALAG SGIDTLGRRL DDALPAERVE LTLPNCSATM GLVSKAYDEL SVADVSYEGD TVELLANGHP AAVERLRGQA EELPESPAQ // ID R4W770_9EURY Unreviewed; 436 AA. AC R4W770; DT 24-JUL-2013, integrated into UniProtKB/TrEMBL. DT 24-JUL-2013, sequence version 1. DT 07-JUN-2017, entry version 29. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=L593_13840 {ECO:0000313|EMBL:AGN02707.1}; OS Salinarchaeum sp. Harcht-Bsk1. OC Archaea; Euryarchaeota; Halobacteria; Natrialbales; Natrialbaceae; OC Salinarchaeum. OX NCBI_TaxID=1333523 {ECO:0000313|EMBL:AGN02707.1, ECO:0000313|Proteomes:UP000014072}; RN [1] {ECO:0000313|EMBL:AGN02707.1, ECO:0000313|Proteomes:UP000014072} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Harcht-Bsk1 {ECO:0000313|EMBL:AGN02707.1}; RX PubMed=23868130; RA Dominova I.N., Sorokin D.Y., Kublanov I.V., Patrushev M.V., RA Toshchakov S.V.; RT "Complete Genome Sequence of Salinarchaeum sp. Strain HArcht-Bsk1T, RT Isolated from Hypersaline Lake Baskunchak, Russia."; RL Genome Announc. 1:E00505-13(2013). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP005962; AGN02707.1; -; Genomic_DNA. DR RefSeq; WP_020447601.1; NC_021313.1. DR EnsemblBacteria; AGN02707; AGN02707; L593_13840. DR GeneID; 16181863; -. DR KEGG; sali:L593_13840; -. DR PATRIC; fig|1333523.5.peg.2832; -. DR KO; K03665; -. DR OrthoDB; POG093Z07D6; -. DR Proteomes; UP000014072; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000014072}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000014072}. FT DOMAIN 190 373 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 156 186 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 436 AA; 48905 MW; D45D0292F8945FA3 CRC64; MSATDRAVVA KRADAGEPET EEIEHLARSA GYEVAAVVTQ TRTEDPALEF GEGKAEELAR IVEREDADTV LFDNELGPYQ TYNLGQLLPK GVEVLDRFTL ILEIFGQRAE TRTAQLQVEL AELRYELPRA EAKTSLAKRE EHPGFMGLGE YDESREQDIK SRISRIRDEL DQIEQTEQHR REQRRESGFD LVALAGYTNA GKSTLLRRLA EELDVDENEE LHQDLESTAE SEDQLFTTLG TTTRRADFEG RDVLVTDTVG FISDLPHWLV ESFKSTLDAA YRADLVLLVV DVSEPVESIR EKLVTSHDTL YERNEAPIVT VLNKADLVDD EELERKREAL SALAPNPVAV SAKEGLGIDE LSERVRLALP PLEEERLVMP MTDDTMSVVS WLHDNARVDD VTYGDDDVLV EFAARPAVVE QSRSKAEALQ PRAESA // ID R4YPE2_OLEAN Unreviewed; 448 AA. AC R4YPE2; DT 24-JUL-2013, integrated into UniProtKB/TrEMBL. DT 24-JUL-2013, sequence version 1. DT 07-JUN-2017, entry version 26. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=OLEAN_C27900 {ECO:0000313|EMBL:CCK76966.1}; OS Oleispira antarctica RB-8. OC Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales; OC Oleispira. OX NCBI_TaxID=698738 {ECO:0000313|EMBL:CCK76966.1, ECO:0000313|Proteomes:UP000032749}; RN [1] {ECO:0000313|EMBL:CCK76966.1, ECO:0000313|Proteomes:UP000032749} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=23877221; DOI=10.1038/ncomms3156; RA Kube M., Chernikova T.N., Al-Ramahi Y., Beloqui A., Lopez-Cortez N., RA Guazzaroni M.E., Heipieper H.J., Klages S., Kotsyurbenko O.R., RA Langer I., Nechitaylo T.Y., Lunsdorf H., Fernandez M., Juarez S., RA Ciordia S., Singer A., Kagan O., Egorova O., Petit P.A., Stogios P., RA Kim Y., Tchigvintsev A., Flick R., Denaro R., Genovese M., Albar J.P., RA Reva O.N., Martinez-Gomariz M., Tran H., Ferrer M., Savchenko A., RA Yakunin A.F., Yakimov M.M., Golyshina O.V., Reinhardt R., RA Golyshin P.N.; RT "Genome sequence and functional genomic analysis of the oil-degrading RT bacterium Oleispira antarctica."; RL Nat. Commun. 4:2156-2156(2013). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; FO203512; CCK76966.1; -; Genomic_DNA. DR EnsemblBacteria; CCK76966; CCK76966; OLEAN_C27900. DR KEGG; oai:OLEAN_C27900; -. DR PATRIC; fig|698738.3.peg.2895; -. DR KO; K03665; -. DR Proteomes; UP000032749; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000032749}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000032749}. FT DOMAIN 223 393 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 181 215 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 448 AA; 49188 MW; 4B2D7B282B8C51B4 CRC64; MSNPEKQHIP RALIVAVQLD NVSDVEFESS LAELADLAKT LGLEVVGQFT QKRSAFDSTA YMGVGKREEI RQFLESDKAD SARLARTDPQ AANNPIEFIL VDHEISPSQS LNLENEVDCE VMDRTVVILE IFHRNASSHA AKVQVEIARL TYMAPRLREA AKREGPSGRQ RSGTGGRGTG QSRAQTDSQK VRDRIAELQK EIDAMEAARD TQRALRLQQS GVSQVALVGY TNAGKSTLMR ALTGKEILVA NKLFATLDTK VRTLIPPSVP KVLVSDTVGF IKNLPHGLVA SFKSTLDEAL SASLLLHVID AGDPGFEAQL AVTDKVLAEI GADVVPRIRV FNKIDYLPDA ASEEERTAEL EAKYPGCIVL SARREDDIAN LHQSIVQVFQ KDLIESEIFL PWSAQALRGE IFTSCEVLEE RADEEGALFR FRASADVVAR LSKLADDK // ID R4YUB5_OLEAN Unreviewed; 440 AA. AC R4YUB5; DT 24-JUL-2013, integrated into UniProtKB/TrEMBL. DT 24-JUL-2013, sequence version 1. DT 07-JUN-2017, entry version 26. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=OLEAN_C35720 {ECO:0000313|EMBL:CCK77748.1}; OS Oleispira antarctica RB-8. OC Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales; OC Oleispira. OX NCBI_TaxID=698738 {ECO:0000313|EMBL:CCK77748.1, ECO:0000313|Proteomes:UP000032749}; RN [1] {ECO:0000313|EMBL:CCK77748.1, ECO:0000313|Proteomes:UP000032749} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=23877221; DOI=10.1038/ncomms3156; RA Kube M., Chernikova T.N., Al-Ramahi Y., Beloqui A., Lopez-Cortez N., RA Guazzaroni M.E., Heipieper H.J., Klages S., Kotsyurbenko O.R., RA Langer I., Nechitaylo T.Y., Lunsdorf H., Fernandez M., Juarez S., RA Ciordia S., Singer A., Kagan O., Egorova O., Petit P.A., Stogios P., RA Kim Y., Tchigvintsev A., Flick R., Denaro R., Genovese M., Albar J.P., RA Reva O.N., Martinez-Gomariz M., Tran H., Ferrer M., Savchenko A., RA Yakunin A.F., Yakimov M.M., Golyshina O.V., Reinhardt R., RA Golyshin P.N.; RT "Genome sequence and functional genomic analysis of the oil-degrading RT bacterium Oleispira antarctica."; RL Nat. Commun. 4:2156-2156(2013). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; FO203512; CCK77748.1; -; Genomic_DNA. DR RefSeq; WP_046010403.1; NZ_FO203512.1. DR EnsemblBacteria; CCK77748; CCK77748; OLEAN_C35720. DR KEGG; oai:OLEAN_C35720; -. DR PATRIC; fig|698738.3.peg.3719; -. DR KO; K03665; -. DR Proteomes; UP000032749; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000032749}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000032749}. FT DOMAIN 203 370 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 440 AA; 49676 MW; 967D637107DBD609 CRC64; MFFDRPEAGN KSGDIAILVH IDFPEGDNRE DPNEFKELVL SAGGRPVEFI TGSRKAPDPK TFVGKGKVEE IKAMAEAHQA DIILFNHALT PSQERNLEEA LEFRVLDRTG LILDIFALRA RTHEGKLQVE LAQLQHQTTR LIRGWTHLER QQGGIGSRGA GESQLETDRR LVATRETLIR NRLKKVRSQR EQGRRARKRS EVPTIALVGY TNAGKSTLFN ALTNAKVFAA DQLFATLDPT MRRLKVMDVG EVVLADTVGF IRHLPHKLVE AFRATLQETT EANLLLHVID SASDERDHNI QQVELVLDEI EASEVPQLKV YNKIDLLEHA EPRIDRDEHG TPIAVWLSAQ AKVGFELLTQ AISELVAEEL FQKTIQLTPA DSRLRALLYD QAAVAEETFA ENGDNLLRLR LQLDDFKQLL AKTGTRADRF IPVELEYWQK // ID R4Z519_9ACTN Unreviewed; 482 AA. AC R4Z519; DT 24-JUL-2013, integrated into UniProtKB/TrEMBL. DT 24-JUL-2013, sequence version 1. DT 07-JUN-2017, entry version 28. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:CCM65793.1}; GN ORFNames=BN381_80323 {ECO:0000313|EMBL:CCM65793.1}; OS Candidatus Microthrix parvicella RN1. OC Bacteria; Actinobacteria; Acidimicrobiia; Acidimicrobiales; OC Microthrixaceae; Candidatus Microthrix. OX NCBI_TaxID=1229780 {ECO:0000313|EMBL:CCM65793.1, ECO:0000313|Proteomes:UP000018291}; RN [1] {ECO:0000313|EMBL:CCM65793.1, ECO:0000313|Proteomes:UP000018291} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=RN1 {ECO:0000313|EMBL:CCM65793.1, RC ECO:0000313|Proteomes:UP000018291}; RX PubMed=23446830; DOI=10.1038/ismej.2013.6; RA Jon McIlroy S., Kristiansen R., Albertsen M., Michael Karst S., RA Rossetti S., Lund Nielsen J., Tandoi V., James Seviour R., RA Nielsen P.H.; RT "Metabolic model for the filamentous 'Candidatus Microthrix RT parvicella' based on genomic and metagenomic analyses."; RL ISME J. 7:1161-1172(2013). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:CCM65793.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CANL01000078; CCM65793.1; -; Genomic_DNA. DR RefSeq; WP_012230854.1; NZ_HG422565.1. DR Proteomes; UP000018291; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000018291}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000018291}. FT DOMAIN 261 424 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 220 247 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 482 AA; 51571 MW; 2E5902E1D15FFB35 CRC64; MSIDEDGWEP TVVGQAGQVA GPNSEPVQEA DAEPVTAGHP AETAETHRGG FGEFGGESRG LIERTFREKI LLVAVVVDGH DDDTDASLDE LELLVDTAGA DVVGRLTQRR RAPDPATYVG SGKAAEIKQM AEATDCDTVV FDDQLSPAQQ FNLEKLLGRS AIDRTAVILD IFAQNASSQE GKAQVELAQL RYLAPRLKGR GKALSQQAGG LGGARRGPGE KALETDRRRL DRRVHKLEAE LREVRQHRST QSKARRRSGV AHVVIVGYTN AGKSSLENRL TDAGVLVEDR LFATLDPTTR KLALPGGEVV LLTDTVGFVR KLPHELVEAF KTTLSVVPEA DLLVHVVDAS APDPAGEIAV VRAIMAEIGG GDRPELLVFN KADRGADAAR LAAATPGSVA VSAATGQGID GLVQAIGNRL RSQRPVIELH IPWARGDVIA AVHALGEVLS EVSEEEQMVM RTRLPEEQRG RFSEFEPVAV GE // ID R5A5G3_9CLOT Unreviewed; 415 AA. AC R5A5G3; DT 24-JUL-2013, integrated into UniProtKB/TrEMBL. DT 24-JUL-2013, sequence version 1. DT 12-APR-2017, entry version 24. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=BN452_02225 {ECO:0000313|EMBL:CCX38345.1}; OS Clostridium sp. CAG:1013. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium; environmental samples. OX NCBI_TaxID=1262769 {ECO:0000313|EMBL:CCX38345.1, ECO:0000313|Proteomes:UP000018382}; RN [1] {ECO:0000313|EMBL:CCX38345.1, ECO:0000313|Proteomes:UP000018382} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MGS:1013 {ECO:0000313|Proteomes:UP000018382}; RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., RA Sunagawa S., Plichta D., Gautier L., Le Chatelier E., Peletier E., RA Bonde I., Nielsen T., Manichanh C., Arumugam M., Batto J., RA Santos M.B.Q.D., Blom N., Borruel N., Burgdorf K.S., Boumezbeur F., RA Casellas F., Dore J., Guarner F., Hansen T., Hildebrand F., Kaas R.S., RA Kennedy S., Kristiansen K., Kultima J.R., Leonard P., Levenez F., RA Lund O., Moumen B., Le Paslier D., Pons N., Pedersen O., Prifti E., RA Qin J., Raes J., Tap J., Tims S., Ussery D.W., Yamada T., RA MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P., Wang J., RA Brunak S., Ehrlich S.D.; RT "Dependencies among metagenomic species, viruses, plasmids and units RT of genetic variation."; RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:CCX38345.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CAWF010000230; CCX38345.1; -; Genomic_DNA. DR Proteomes; UP000018382; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000018382}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000018382}. FT DOMAIN 198 360 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 415 AA; 45487 MW; 6C9BA8A2296516A6 CRC64; MYENEIRPQR AMLVSLDTGE YDAEISLAEL EELTRTAGAE PALTLTQKRP APETATCIGS GMVEQVAELC AQQEIDLLIF DRELTPTQIR NLEKACGVRV IDRTTLILDI FAQRARSKEG KLQVELAQLR YLLPRLSGQG TALSRLGGGI GTRGPGETKL ETDRRHIRRR IGSLREQLRD VEAAREVIDR RRKKDGTVTV ALVGYTNAGK STLMNQLTQA GVLAEDKLFA TLDPTARALK LPCGKTVMLI DTVGLIRRLP HHLVEAFKST LEQAATADIL LNVCDASSGE ARDHLDVTNS LLNELGAAGH PIIPVLNKWD AVEDPDTAPR LPGAVRISAL TGEGIDRLLE AIEENLPEKT FPVELLLPFA KTGLAAKLRE EGAVLSEEYV PEGLRLSAQV DQRLYGLVKD YEITP // ID R5AHA4_9FIRM Unreviewed; 427 AA. AC R5AHA4; DT 24-JUL-2013, integrated into UniProtKB/TrEMBL. DT 24-JUL-2013, sequence version 1. DT 12-APR-2017, entry version 23. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=BN453_01210 {ECO:0000313|EMBL:CCX40272.1}; OS Firmicutes bacterium CAG:102. OC Bacteria; Firmicutes; environmental samples. OX NCBI_TaxID=1262998 {ECO:0000313|EMBL:CCX40272.1, ECO:0000313|Proteomes:UP000018112}; RN [1] {ECO:0000313|EMBL:CCX40272.1, ECO:0000313|Proteomes:UP000018112} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MGS:102 {ECO:0000313|EMBL:CCX40272.1, RC ECO:0000313|Proteomes:UP000018112}; RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., RA Sunagawa S., Plichta D., Gautier L., Le Chatelier E., Peletier E., RA Bonde I., Nielsen T., Manichanh C., Arumugam M., Batto J., RA Santos M.B.Q.D., Blom N., Borruel N., Burgdorf K.S., Boumezbeur F., RA Casellas F., Dore J., Guarner F., Hansen T., Hildebrand F., Kaas R.S., RA Kennedy S., Kristiansen K., Kultima J.R., Leonard P., Levenez F., RA Lund O., Moumen B., Le Paslier D., Pons N., Pedersen O., Prifti E., RA Qin J., Raes J., Tap J., Tims S., Ussery D.W., Yamada T., RA MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P., Wang J., RA Brunak S., Ehrlich S.D.; RT "Dependencies among metagenomic species, viruses, plasmids and units RT of genetic variation."; RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:CCX40272.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CAWG010000062; CCX40272.1; -; Genomic_DNA. DR Proteomes; UP000018112; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000018112}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000018112}. FT DOMAIN 208 372 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 167 201 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 427 AA; 47538 MW; C9513733E119BA40 CRC64; MAKELHELNE LEERVILVAV EMDERSSRSA MDTDACLDEL EELVKTAGGT AVARSVQKRE RIHPGHYLGT GKIEELKAML SAYDATGIVC DDELSPAQLR NLEQMLGTKV MDRTIVILDI FAARALSGEG KIQVELAQLK YRLSRLTGMG ASMSRLGGGI GTRGPGEKKL ETDRRYIKER IAELNKDAQE IRTHRELLRA QRSKKGTPVI SLVGYTNAGK STILNRLSDA GVLAEDKLFA TLDTTTRKIE LPGGSEVFLT DTVGFIQKLP HHLVQAFRAT LEELQYADIL LHVVDASDAN RAEHIEVVYD TLRSLGCEDT PVITVFNKMD REVELPLPMD TMARDIVQVS AQNGDGMDVL LERVEKLLQS FRKSITALVP YTEGSLIGWI HGRCEIIREE HTGEGVLLEV YVDEESANRL EKFKVNE // ID R5AP53_9CLOT Unreviewed; 335 AA. AC R5AP53; DT 24-JUL-2013, integrated into UniProtKB/TrEMBL. DT 24-JUL-2013, sequence version 1. DT 12-APR-2017, entry version 24. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=BN454_01756 {ECO:0000313|EMBL:CCX42497.1}; OS Clostridium sp. CAG:1024. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium; environmental samples. OX NCBI_TaxID=1262770 {ECO:0000313|EMBL:CCX42497.1, ECO:0000313|Proteomes:UP000017946}; RN [1] {ECO:0000313|EMBL:CCX42497.1, ECO:0000313|Proteomes:UP000017946} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MGS:1024 {ECO:0000313|Proteomes:UP000017946}; RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., RA Sunagawa S., Plichta D., Gautier L., Le Chatelier E., Peletier E., RA Bonde I., Nielsen T., Manichanh C., Arumugam M., Batto J., RA Santos M.B.Q.D., Blom N., Borruel N., Burgdorf K.S., Boumezbeur F., RA Casellas F., Dore J., Guarner F., Hansen T., Hildebrand F., Kaas R.S., RA Kennedy S., Kristiansen K., Kultima J.R., Leonard P., Levenez F., RA Lund O., Moumen B., Le Paslier D., Pons N., Pedersen O., Prifti E., RA Qin J., Raes J., Tap J., Tims S., Ussery D.W., Yamada T., RA MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P., Wang J., RA Brunak S., Ehrlich S.D.; RT "Dependencies among metagenomic species, viruses, plasmids and units RT of genetic variation."; RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:CCX42497.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CAWJ010000252; CCX42497.1; -; Genomic_DNA. DR Proteomes; UP000017946; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000017946}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000017946}. FT DOMAIN 122 281 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 81 108 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 335 AA; 37562 MW; A57A9E1337CABE36 CRC64; MIFDDELSAL QMRNLEDVLG VPIIDRTMLI LDIFASRAES REGKLQVELA QLKYRLPRLL GMGRALSRQG GSGVGMRGPG EKKLEIDRRR IRRRIFELQQ ELDEIEKQRA LRRVKRGKNA VPVVALVGYT NAGKSTLLNA LSGANVLAED QLFATLDPVV RRITLPNGTE CLLSDTVGFI NKLPHDLVQA FRSTLEEVRD ADLLLHVIDS SSPYYDVQMR VVEEVVSSLG AADTPCIQVF NKIDKNTENT LRPDACRISA MTDAGVSELL EDIETQLSHS RVRVELTVPY DRYETMQQLR AFGTILSESH EADGTHVTVL LDEGLLWKVK KGLER // ID R5AU21_9FIRM Unreviewed; 426 AA. AC R5AU21; DT 24-JUL-2013, integrated into UniProtKB/TrEMBL. DT 24-JUL-2013, sequence version 1. DT 12-APR-2017, entry version 23. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=BN455_00247 {ECO:0000313|EMBL:CCX46855.1}; OS Firmicutes bacterium CAG:103. OC Bacteria; Firmicutes; environmental samples. OX NCBI_TaxID=1262999 {ECO:0000313|EMBL:CCX46855.1, ECO:0000313|Proteomes:UP000018290}; RN [1] {ECO:0000313|EMBL:CCX46855.1, ECO:0000313|Proteomes:UP000018290} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MGS:103 {ECO:0000313|Proteomes:UP000018290}; RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., RA Sunagawa S., Plichta D., Gautier L., Le Chatelier E., Peletier E., RA Bonde I., Nielsen T., Manichanh C., Arumugam M., Batto J., RA Santos M.B.Q.D., Blom N., Borruel N., Burgdorf K.S., Boumezbeur F., RA Casellas F., Dore J., Guarner F., Hansen T., Hildebrand F., Kaas R.S., RA Kennedy S., Kristiansen K., Kultima J.R., Leonard P., Levenez F., RA Lund O., Moumen B., Le Paslier D., Pons N., Pedersen O., Prifti E., RA Qin J., Raes J., Tap J., Tims S., Ussery D.W., Yamada T., RA MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P., Wang J., RA Brunak S., Ehrlich S.D.; RT "Dependencies among metagenomic species, viruses, plasmids and units RT of genetic variation."; RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:CCX46855.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CAWL010000204; CCX46855.1; -; Genomic_DNA. DR Proteomes; UP000018290; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000018290}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000018290}. FT DOMAIN 208 368 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 167 201 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 426 AA; 47376 MW; 830C3F490333FEB6 CRC64; MQSTKQKIER AALAGLAAAS MDERERSTDI SLAELAALVE TAGGQPVVTL LQNKPTPDPR TFLGEGKVAE LRERIVANDC DLAVFDNELS PSQMRVLEEE LGVRVLDRSG LILDIFAQRA QTREGQLQVE LAQYQYLLPR LTGMWTHLVR QTASGGSSPI GTRGPGETQL ETDRRHIRRK IQKLQAELED VRKIRRTQRR RREKNALPVV ALVGYTNAGK STLLNCLTGS DIPANDRLFD TLDTTTRRWR IDAAQEVLLS DTVGFIRKLP THLVEAFKAT LEELTYADVL LHVIDLSNPE WEAQAEVVDR LIDQLGAAQT PCIRVFNKCD AYLGILPHGE NIVCISARSG EGAAELTECV RAILGRADHH VMLLLPYAQG ALLETLHRDC AVLHTDYRDD GIALEVIIHP EQWPRLEPFV IAGEEG // ID R5AWH2_9BACT Unreviewed; 407 AA. AC R5AWH2; DT 24-JUL-2013, integrated into UniProtKB/TrEMBL. DT 24-JUL-2013, sequence version 1. DT 12-APR-2017, entry version 23. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=BN456_01278 {ECO:0000313|EMBL:CCX45052.1}; OS Prevotella sp. CAG:1031. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Prevotellaceae; OC Prevotella; environmental samples. OX NCBI_TaxID=1262917 {ECO:0000313|EMBL:CCX45052.1, ECO:0000313|Proteomes:UP000018183}; RN [1] {ECO:0000313|EMBL:CCX45052.1, ECO:0000313|Proteomes:UP000018183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MGS:1031 {ECO:0000313|Proteomes:UP000018183}; RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., RA Sunagawa S., Plichta D., Gautier L., Le Chatelier E., Peletier E., RA Bonde I., Nielsen T., Manichanh C., Arumugam M., Batto J., RA Santos M.B.Q.D., Blom N., Borruel N., Burgdorf K.S., Boumezbeur F., RA Casellas F., Dore J., Guarner F., Hansen T., Hildebrand F., Kaas R.S., RA Kennedy S., Kristiansen K., Kultima J.R., Leonard P., Levenez F., RA Lund O., Moumen B., Le Paslier D., Pons N., Pedersen O., Prifti E., RA Qin J., Raes J., Tap J., Tims S., Ussery D.W., Yamada T., RA MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P., Wang J., RA Brunak S., Ehrlich S.D.; RT "Dependencies among metagenomic species, viruses, plasmids and units RT of genetic variation."; RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:CCX45052.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CAWK010000152; CCX45052.1; -; Genomic_DNA. DR Proteomes; UP000018183; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000018183}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000018183}. FT DOMAIN 202 387 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 407 AA; 46605 MW; 29EF8CD61AA9FFDF CRC64; MKEQIISEAT TERAVLVGLI TENQNEAQAK EYLDELEFLA DTAGAVCVRK FLQKIPYANP RTFVGKGKLE EIKQFVETND IGLAIFDDEL TSKQVANIEK ELQVKILDRT SLILDIFARR AQTANAKTQV ELAQYQYLLP RLTRMWTHLE RQRGGIGMRG PGETQIETDR RIILTRIAWL KEQLRAIDRQ KAVQRKNRGK LTRVALVGYT NVGKSTLMNL LSKSDVFAEN KLFATLDTTV RKVVIDNLPM LLTDTVGFIR KLPTHLVESF KSTLDEVREA DLLIHVVDIS HPNFEEQIKV VNETLNDICG GCEKPVIMVF NKIDAYTHVE KDADDLTPRT RENITLEELK ESWMSRLGGD AVFISAKKEL NIPELKDMIY EKAKEIHLTR FPYNDFLYQT YDDLGED // ID R5B5T0_9CLOT Unreviewed; 592 AA. AC R5B5T0; DT 24-JUL-2013, integrated into UniProtKB/TrEMBL. DT 24-JUL-2013, sequence version 1. DT 12-APR-2017, entry version 24. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=BN545_00969 {ECO:0000313|EMBL:CCX49529.1}; OS Clostridium sp. CAG:226. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium; environmental samples. OX NCBI_TaxID=1262781 {ECO:0000313|EMBL:CCX49529.1, ECO:0000313|Proteomes:UP000018047}; RN [1] {ECO:0000313|EMBL:CCX49529.1, ECO:0000313|Proteomes:UP000018047} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MGS:226 {ECO:0000313|Proteomes:UP000018047}; RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., RA Sunagawa S., Plichta D., Gautier L., Le Chatelier E., Peletier E., RA Bonde I., Nielsen T., Manichanh C., Arumugam M., Batto J., RA Santos M.B.Q.D., Blom N., Borruel N., Burgdorf K.S., Boumezbeur F., RA Casellas F., Dore J., Guarner F., Hansen T., Hildebrand F., Kaas R.S., RA Kennedy S., Kristiansen K., Kultima J.R., Leonard P., Levenez F., RA Lund O., Moumen B., Le Paslier D., Pons N., Pedersen O., Prifti E., RA Qin J., Raes J., Tap J., Tims S., Ussery D.W., Yamada T., RA MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P., Wang J., RA Brunak S., Ehrlich S.D.; RT "Dependencies among metagenomic species, viruses, plasmids and units RT of genetic variation."; RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:CCX49529.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CAWN010000029; CCX49529.1; -; Genomic_DNA. DR Proteomes; UP000018047; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000018047}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000018047}. FT DOMAIN 376 536 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 592 AA; 65063 MW; FCF7CCBE56043697 CRC64; MQKKVNGNTE GIRDAVLERI AAIYDMTQGQ YEFASHELIA ELCALTGAIR REISVYISRS GSIEDVSVGD GSKVSMPSMR LVRNEDRLCG VRCLHTHPGG DGRLSGVDIG TLRSMRLDCM AAVGVKEDGT ATSLYAGYIG EAAGEEREAL VYGPLRPYKL PQRQLIEEIY VSDDRLKSST KDTKDDIPER TVLVGLENDE GYDTIEELAE LAKTAGANVV ARSIQKRRTP DNATYIGSGK VDELSLLCSE TEAELVIFDD ELTGSQLRNL ETRLGVKVID RTALILDIFA QRAVSREGAL QVELAQMKYN LTRLTGQGTA LSRLGGGIGT RGPGEKKLEI DRRRIRRRIF ELGEELKEVE KQRSLRRERR EKNATPLVAL VGYTNAGKST FLNAVSNAGV LAEDKLFATL DPVVRQITLP NGLDILLSDT VGFINKLPHD LIEAFKSTLE EVSNADLILH VVDISCDHYD AQMRVVEDVI ASLGAGDTPR INVYNKIDRI DSRPRGTEDD AFVSAATGEG MESLLERVEK LLSASHSTIE LTIPYDKYEA VALLHSEARI LSEEHTETGT KICAACEDGT LRKLQKLVGE NI // ID R5B5U6_9BACE Unreviewed; 409 AA. AC R5B5U6; DT 24-JUL-2013, integrated into UniProtKB/TrEMBL. DT 24-JUL-2013, sequence version 1. DT 12-APR-2017, entry version 24. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=BN813_01494 {ECO:0000313|EMBL:CCX48312.1}; OS Bacteroides sp. CAG:927. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae; OC Bacteroides; environmental samples. OX NCBI_TaxID=1262753 {ECO:0000313|EMBL:CCX48312.1, ECO:0000313|Proteomes:UP000017907}; RN [1] {ECO:0000313|EMBL:CCX48312.1, ECO:0000313|Proteomes:UP000017907} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MGS:927 {ECO:0000313|Proteomes:UP000017907}; RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., RA Sunagawa S., Plichta D., Gautier L., Le Chatelier E., Peletier E., RA Bonde I., Nielsen T., Manichanh C., Arumugam M., Batto J., RA Santos M.B.Q.D., Blom N., Borruel N., Burgdorf K.S., Boumezbeur F., RA Casellas F., Dore J., Guarner F., Hansen T., Hildebrand F., Kaas R.S., RA Kennedy S., Kristiansen K., Kultima J.R., Leonard P., Levenez F., RA Lund O., Moumen B., Le Paslier D., Pons N., Pedersen O., Prifti E., RA Qin J., Raes J., Tap J., Tims S., Ussery D.W., Yamada T., RA MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P., Wang J., RA Brunak S., Ehrlich S.D.; RT "Dependencies among metagenomic species, viruses, plasmids and units RT of genetic variation."; RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:CCX48312.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CAWM010000051; CCX48312.1; -; Genomic_DNA. DR Proteomes; UP000017907; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000017907}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000017907}. FT DOMAIN 202 387 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 170 197 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 409 AA; 46650 MW; 28AC05B32DC62642 CRC64; MKDLIIEKES SERTILIGIV TPQQSEAKTM EYLDELEFLA DTAGAVTVHK FIQKLNGPDS RTYVGSGKLE EIRSYVEEND IGMAIFDDDL TPKQVANIER ELKIKILDRT SLILDIFAKR AQTANAKTQV ELAQYQYLLP RLTRLWTHLE RQRGGIGMRG PGERQIETDR RIILDKISRL KAELKDIDRQ KSMQRKNRGK LTRVALVGYT NVGKSTLMNL LSKSEVFAEN KLFATLDTTV RKVIIDNLPF LLTDTVGFIR KLPTHLVESF KSTLDEVRDA DVLLHVVDIS HPNFEEQIEV VNRTLADVCG SVNKPVIMVF NKVDAFTYTP KAEDDLTERT RSNISLEELK ASWMAKMGSD AVFVSAKTGL NIEELKQKIY EKAKEVHLSR FPYNDFLFQK YDDLADTTD // ID R5BLN4_9BACE Unreviewed; 395 AA. AC R5BLN4; DT 24-JUL-2013, integrated into UniProtKB/TrEMBL. DT 24-JUL-2013, sequence version 1. DT 12-APR-2017, entry version 23. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=BN459_00251 {ECO:0000313|EMBL:CCX56475.1}; OS Bacteroides sp. CAG:1060. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae; OC Bacteroides; environmental samples. OX NCBI_TaxID=1262734 {ECO:0000313|EMBL:CCX56475.1, ECO:0000313|Proteomes:UP000018006}; RN [1] {ECO:0000313|EMBL:CCX56475.1, ECO:0000313|Proteomes:UP000018006} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MGS:1060 {ECO:0000313|Proteomes:UP000018006}; RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., RA Sunagawa S., Plichta D., Gautier L., Le Chatelier E., Peletier E., RA Bonde I., Nielsen T., Manichanh C., Arumugam M., Batto J., RA Santos M.B.Q.D., Blom N., Borruel N., Burgdorf K.S., Boumezbeur F., RA Casellas F., Dore J., Guarner F., Hansen T., Hildebrand F., Kaas R.S., RA Kennedy S., Kristiansen K., Kultima J.R., Leonard P., Levenez F., RA Lund O., Moumen B., Le Paslier D., Pons N., Pedersen O., Prifti E., RA Qin J., Raes J., Tap J., Tims S., Ussery D.W., Yamada T., RA MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P., Wang J., RA Brunak S., Ehrlich S.D.; RT "Dependencies among metagenomic species, viruses, plasmids and units RT of genetic variation."; RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:CCX56475.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CAWQ010000174; CCX56475.1; -; Genomic_DNA. DR Proteomes; UP000018006; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000018006}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000018006}. FT DOMAIN 201 384 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 169 196 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 395 AA; 45713 MW; AF90D8F0E52D2731 CRC64; METTERKEER AVFVGIIKQN DDERKVNEYL EELVFLAETA GVAGDKKFIQ KVDKPEKATY IRTGKLEEIA AYCEENLINY VIFDDELTGM QQRNIEKVIK TAAVIDRTSL ILEIFSQRAK TAYAKMQVEL ARYNYMLPRL AGMWTHLERQ RGGIGMRGGM GESQIEIDRR IVRERIAKLK EQLKKVDKQM ATQRSNRGQL VRLSLVGYTN VGKSTLMNLL AKSDVFAENK LFATLDTTVR KVVIGNVPFL LSDTVGFIRK LPTQLIEAFK STLDEVREAD ILIHVVDISH PDYEEQMEVV EKTLKDISAN DKPVYVIFNK IDSYQNEEYD DYSLEPRTER HFTLDEVKSK WMERNIPCIF VSALKKEGIN KLKDDIYKMV AEIHAGRYPF NNFLW // ID R5BU75_9FIRM Unreviewed; 411 AA. AC R5BU75; DT 24-JUL-2013, integrated into UniProtKB/TrEMBL. DT 24-JUL-2013, sequence version 1. DT 12-APR-2017, entry version 23. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=BN499_01145 {ECO:0000313|EMBL:CCX57764.1}; OS Blautia hydrogenotrophica CAG:147. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Lachnospiraceae; OC Blautia; environmental samples. OX NCBI_TaxID=1263061 {ECO:0000313|EMBL:CCX57764.1, ECO:0000313|Proteomes:UP000018163}; RN [1] {ECO:0000313|EMBL:CCX57764.1, ECO:0000313|Proteomes:UP000018163} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MGS:147 {ECO:0000313|Proteomes:UP000018163}; RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., RA Sunagawa S., Plichta D., Gautier L., Le Chatelier E., Peletier E., RA Bonde I., Nielsen T., Manichanh C., Arumugam M., Batto J., RA Santos M.B.Q.D., Blom N., Borruel N., Burgdorf K.S., Boumezbeur F., RA Casellas F., Dore J., Guarner F., Hansen T., Hildebrand F., Kaas R.S., RA Kennedy S., Kristiansen K., Kultima J.R., Leonard P., Levenez F., RA Lund O., Moumen B., Le Paslier D., Pons N., Pedersen O., Prifti E., RA Qin J., Raes J., Tap J., Tims S., Ussery D.W., Yamada T., RA MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P., Wang J., RA Brunak S., Ehrlich S.D.; RT "Dependencies among metagenomic species, viruses, plasmids and units RT of genetic variation."; RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:CCX57764.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CAWR010000028; CCX57764.1; -; Genomic_DNA. DR ProteinModelPortal; R5BU75; -. DR Proteomes; UP000018163; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000018163}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000018163}. FT DOMAIN 199 363 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 158 195 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 411 AA; 46582 MW; ED825B6178938E1B CRC64; MYDLEELEER VVLIGVQEND GEEVESSLEE LGELARTAGA LVAGIVVQRR EKIHPGTYIG KGKIEEVRML VLAQDATGVI CDDELSPAQF HNLQRELDCK VMDRTLLILD IFASHAVTRE GKIQVELAQL RYRAARLAGL GSSLSRLGGG IGTRGPGEKK LEMDRRLIRT RISQLKKELE EVVRHRELVR DQRQRMNQKI AALVGYSSAG KSSTMNYLTG ASILEDEMLF STLDTTTRVL QLSGKQEILL TDTVGFIRKL PHQLIEAFKS TLEEVCYADI IIHVVDASNP QRETQMHVVY ETLRQLKVSD KPVITLFNKQ DKLEEKQKFR DFRAEYSILS STKTGEGMEE LKAALEEILR SGQIYIERLY PYQKAGILQL IRKKGEILEE EYLAEGIAVK AYVSREIYEK V // ID R5CER8_9BACE Unreviewed; 422 AA. AC R5CER8; DT 24-JUL-2013, integrated into UniProtKB/TrEMBL. DT 24-JUL-2013, sequence version 1. DT 12-APR-2017, entry version 24. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=BN727_01372 {ECO:0000313|EMBL:CCX63302.1}; OS Bacteroides sp. CAG:598. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae; OC Bacteroides; environmental samples. OX NCBI_TaxID=1262743 {ECO:0000313|EMBL:CCX63302.1, ECO:0000313|Proteomes:UP000017916}; RN [1] {ECO:0000313|EMBL:CCX63302.1, ECO:0000313|Proteomes:UP000017916} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MGS:598 {ECO:0000313|Proteomes:UP000017916}; RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., RA Sunagawa S., Plichta D., Gautier L., Le Chatelier E., Peletier E., RA Bonde I., Nielsen T., Manichanh C., Arumugam M., Batto J., RA Santos M.B.Q.D., Blom N., Borruel N., Burgdorf K.S., Boumezbeur F., RA Casellas F., Dore J., Guarner F., Hansen T., Hildebrand F., Kaas R.S., RA Kennedy S., Kristiansen K., Kultima J.R., Leonard P., Levenez F., RA Lund O., Moumen B., Le Paslier D., Pons N., Pedersen O., Prifti E., RA Qin J., Raes J., Tap J., Tims S., Ussery D.W., Yamada T., RA MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P., Wang J., RA Brunak S., Ehrlich S.D.; RT "Dependencies among metagenomic species, viruses, plasmids and units RT of genetic variation."; RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:CCX63302.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CAWS010000182; CCX63302.1; -; Genomic_DNA. DR Proteomes; UP000017916; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000017916}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000017916}. FT DOMAIN 218 402 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 422 AA; 48121 MW; 6A2AC282EF9E13C9 CRC64; MAMKEFVISE AQVETAVLVG LITKTQDERK TNEYLDELAF LAETAGAEVV KRFTQKLDQA NSVTYVGKGK LDEIKQYIKD EEEAEREIGM VIFDDELSAK QIRNIEAELK VKILDRTSLI LDIFAMRAQT ANAKTQVELA QYKYMLPRLQ RLWTHLERQG GGSGAGGGKG SVGLRGPGET QLEMDRRIIL NRMSLLKERL AEIDKQKATQ RKNRGRLIRV ALVGYTNVGK STLMNLLAKS EVFAENKLFA TLDTTVRKVI IDNLPFLLSD TVGFIRKLPT DLVDSFKSTL DEVREADLLL HIVDISHPDF EEQIEVVNKT LADIGAAGKP MILVFNKIDA YTYVKKDDDD LTPRTKENLS LEELMKTWMA KLEDNCMFIS AREKTNIEEM KTMVYQRVKE LHVQKYPYND FLYQTYDENG EL // ID R5CGQ7_9BACT Unreviewed; 414 AA. AC R5CGQ7; DT 24-JUL-2013, integrated into UniProtKB/TrEMBL. DT 24-JUL-2013, sequence version 1. DT 12-APR-2017, entry version 22. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=BN458_00490 {ECO:0000313|EMBL:CCX67150.1}; OS Prevotella sp. CAG:1058. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Prevotellaceae; OC Prevotella; environmental samples. OX NCBI_TaxID=1262918 {ECO:0000313|EMBL:CCX67150.1, ECO:0000313|Proteomes:UP000018314}; RN [1] {ECO:0000313|EMBL:CCX67150.1, ECO:0000313|Proteomes:UP000018314} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MGS:1058 {ECO:0000313|Proteomes:UP000018314}; RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., RA Sunagawa S., Plichta D., Gautier L., Le Chatelier E., Peletier E., RA Bonde I., Nielsen T., Manichanh C., Arumugam M., Batto J., RA Santos M.B.Q.D., Blom N., Borruel N., Burgdorf K.S., Boumezbeur F., RA Casellas F., Dore J., Guarner F., Hansen T., Hildebrand F., Kaas R.S., RA Kennedy S., Kristiansen K., Kultima J.R., Leonard P., Levenez F., RA Lund O., Moumen B., Le Paslier D., Pons N., Pedersen O., Prifti E., RA Qin J., Raes J., Tap J., Tims S., Ussery D.W., Yamada T., RA MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P., Wang J., RA Brunak S., Ehrlich S.D.; RT "Dependencies among metagenomic species, viruses, plasmids and units RT of genetic variation."; RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:CCX67150.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CAWU010000179; CCX67150.1; -; Genomic_DNA. DR Proteomes; UP000018314; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000018314}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000018314}. FT DOMAIN 216 400 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 414 AA; 47087 MW; 1FAE2EA2F9135230 CRC64; MKEFVISEVK AETAILVGLI TQEQDEAKTK EYLDELEFLA DTAGAVTVKR FTQKVGGPNQ TTYVGKGKLE EIKQYIQMEE EAEREIGMVI FDDELSAKQI RNIEGELKVK ILDRTSLILD IFAMRAQTAS AKTQVELAQY RYMLPRLQRL WTHLERQGGG SGSGGGKGSV GLRGPGETQL EMDRRIILQR MSLLKQRLAE IDKQKTTQRK NRGRLIRVAL VGYTNVGKST IMNLLAKSEV FAENKLFATL DTTVRKVVIE NLPFLLADTV GFIRKLPTDL VDSFKSTLDE VREADLLLHV VDISHPDFEE QITVVDNTLK DLGCADKPSM IIFNKIDAYT WVDKEPDDLT PATKENITLD ELKQTWMAKL NDNCLFISAK NKTNIEEMRN TIYNLVRELH VQKYPYNDFL YPTE // ID R5CQW6_9FIRM Unreviewed; 435 AA. AC R5CQW6; DT 24-JUL-2013, integrated into UniProtKB/TrEMBL. DT 24-JUL-2013, sequence version 1. DT 10-MAY-2017, entry version 24. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=BN785_00182 {ECO:0000313|EMBL:CCX66096.1}; OS Firmicutes bacterium CAG:791. OC Bacteria; Firmicutes; environmental samples. OX NCBI_TaxID=1262993 {ECO:0000313|EMBL:CCX66096.1, ECO:0000313|Proteomes:UP000018038}; RN [1] {ECO:0000313|EMBL:CCX66096.1, ECO:0000313|Proteomes:UP000018038} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MGS:791 {ECO:0000313|Proteomes:UP000018038}; RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., RA Sunagawa S., Plichta D., Gautier L., Le Chatelier E., Peletier E., RA Bonde I., Nielsen T., Manichanh C., Arumugam M., Batto J., RA Santos M.B.Q.D., Blom N., Borruel N., Burgdorf K.S., Boumezbeur F., RA Casellas F., Dore J., Guarner F., Hansen T., Hildebrand F., Kaas R.S., RA Kennedy S., Kristiansen K., Kultima J.R., Leonard P., Levenez F., RA Lund O., Moumen B., Le Paslier D., Pons N., Pedersen O., Prifti E., RA Qin J., Raes J., Tap J., Tims S., Ussery D.W., Yamada T., RA MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P., Wang J., RA Brunak S., Ehrlich S.D.; RT "Dependencies among metagenomic species, viruses, plasmids and units RT of genetic variation."; RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:CCX66096.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CAWT010000187; CCX66096.1; -; Genomic_DNA. DR Proteomes; UP000018038; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000018038}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000018038}. FT DOMAIN 205 378 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 164 198 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 435 AA; 48919 MW; CF06348FDE04E2EF CRC64; MIELQPSAEK KRAVLVGLNT EKSPERYLSS MKELAQLAEA CDLEVTSSIV QNAPVVTQKT LFGRGKVEEI KTAVLADDAD IVIVQESLTP MQVRNLEDFL DTEVMDRTGI ILQIFSTRAR TREARLQVKS AQLQYMLPRL VGMRKNLSRQ GGGSGRLSNK GAGEEKLELD RRHIEHQLAE INRQLKEVEK ERSTQRSRRL RSGLPLVSLV GYTNAGKSTL MNGLLSLCPN PSDSAQDRTV LEKDMLFATL DTSVRSIRIP GHSPFLLSDT VGFISDLPHT LVKAFRSTLD EVKYADLLVE VVDYSDPEWQ EQLKVTRRTL DEIGASDIPT LVVYNKADLC EDLPVLRSFP DHIYFSARNR DGYEPLLDLL DQTLDGKKEQ HTYLLPYSCG GLLNEMQKKY PDSRVEYLPE GVKLDITLTE KDAKLLNDMQ LPSSS // ID R5CX99_9BACT Unreviewed; 414 AA. AC R5CX99; DT 24-JUL-2013, integrated into UniProtKB/TrEMBL. DT 24-JUL-2013, sequence version 1. DT 12-APR-2017, entry version 22. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=BN567_00629 {ECO:0000313|EMBL:CCX69317.1}; OS Prevotella sp. CAG:255. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Prevotellaceae; OC Prevotella; environmental samples. OX NCBI_TaxID=1262923 {ECO:0000313|EMBL:CCX69317.1, ECO:0000313|Proteomes:UP000017913}; RN [1] {ECO:0000313|EMBL:CCX69317.1, ECO:0000313|Proteomes:UP000017913} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MGS:255 {ECO:0000313|Proteomes:UP000017913}; RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., RA Sunagawa S., Plichta D., Gautier L., Le Chatelier E., Peletier E., RA Bonde I., Nielsen T., Manichanh C., Arumugam M., Batto J., RA Santos M.B.Q.D., Blom N., Borruel N., Burgdorf K.S., Boumezbeur F., RA Casellas F., Dore J., Guarner F., Hansen T., Hildebrand F., Kaas R.S., RA Kennedy S., Kristiansen K., Kultima J.R., Leonard P., Levenez F., RA Lund O., Moumen B., Le Paslier D., Pons N., Pedersen O., Prifti E., RA Qin J., Raes J., Tap J., Tims S., Ussery D.W., Yamada T., RA MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P., Wang J., RA Brunak S., Ehrlich S.D.; RT "Dependencies among metagenomic species, viruses, plasmids and units RT of genetic variation."; RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:CCX69317.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CAWV010000114; CCX69317.1; -; Genomic_DNA. DR Proteomes; UP000017913; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000017913}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000017913}. FT DOMAIN 216 400 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 414 AA; 47126 MW; 8D020DAD22229F25 CRC64; MKEFVISEVK AETAILVGLI TQEQNEAKTK EYLDELEFLA DTAGAVTVKR FTQKVGGPNQ TTYVGKGKLE EIKQYIKDEE DAEREIGMVI FDDELSAKQI RNIENELKVK ILDRTSLILD IFAMRAQTAN AKTQVELAQY RYMLPRLQRL WTHLERQGGG SGSGGGKGSV GLRGPGETQL EMDRRIILQR MSLLKQRLAE IDKQKTTQRK NRGRLIRVAL VGYTNVGKST TMNLLAKSDV FAENKLFATL DTTVRKVVIE NLPFLLADTV GFIRKLPTDL VDSFKSTLDE VREADLLLHV VDISHPDFEE QIKVVDNTLK DLGCADKPSM IIFNKIDSYT WVEKDPDDLT PATKENVTLD ELKKTWMAKL NDSCLFISAK NKTNIDELRE TLYNKVRELH VQKYPYNDFL YPIE // ID R5CZ23_9FIRM Unreviewed; 436 AA. AC R5CZ23; DT 24-JUL-2013, integrated into UniProtKB/TrEMBL. DT 24-JUL-2013, sequence version 1. DT 10-MAY-2017, entry version 24. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=BN795_01367 {ECO:0000313|EMBL:CCX73133.1}; OS Firmicutes bacterium CAG:83. OC Bacteria; Firmicutes; environmental samples. OX NCBI_TaxID=1262992 {ECO:0000313|EMBL:CCX73133.1, ECO:0000313|Proteomes:UP000018101}; RN [1] {ECO:0000313|EMBL:CCX73133.1, ECO:0000313|Proteomes:UP000018101} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MGS:83 {ECO:0000313|Proteomes:UP000018101}; RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., RA Sunagawa S., Plichta D., Gautier L., Le Chatelier E., Peletier E., RA Bonde I., Nielsen T., Manichanh C., Arumugam M., Batto J., RA Santos M.B.Q.D., Blom N., Borruel N., Burgdorf K.S., Boumezbeur F., RA Casellas F., Dore J., Guarner F., Hansen T., Hildebrand F., Kaas R.S., RA Kennedy S., Kristiansen K., Kultima J.R., Leonard P., Levenez F., RA Lund O., Moumen B., Le Paslier D., Pons N., Pedersen O., Prifti E., RA Qin J., Raes J., Tap J., Tims S., Ussery D.W., Yamada T., RA MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P., Wang J., RA Brunak S., Ehrlich S.D.; RT "Dependencies among metagenomic species, viruses, plasmids and units RT of genetic variation."; RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:CCX73133.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CAWX010000092; CCX73133.1; -; Genomic_DNA. DR Proteomes; UP000018101; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000018101}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000018101}. FT DOMAIN 213 374 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 179 206 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 436 AA; 48953 MW; 81E7418B27543FB4 CRC64; MERRTLEENR ENKRDYAVLV GLRSPVLRED NADEESLAEL AALVETAGGQ AVGTILQSRE KPDPHSFIGE GKVEEVRRMV QEEEATMVIF DNDLSPSQIR VLTEMTGVQV LDRSGLILDI FAQRAKTKEG CLQVELAQYQ YLLPRLVGMW THLERQAGTS GKGPIGSKGP GETQLETDRR HIHRKIDKLK AELEEVRRVR STQRQRRQKN EIPVVAIVGY TNAGKSTLLN AITGAGIPAN NRLFDTLDTT TRLLTVSDTL DVVISDTVGF IRKLPHQLVE AFKATLEELE YADLLLHVID VSNPQWQQQA AIVEDLIHEL KADQIPCIRV YNKCDVAFSG ERSHEEDAVS ISAKTGEGIP ALMEAIDRRL DKGTRRVVIH LPYDKAGMLD SLYREAKVED VAYQESIDVT AVCPPKVLGQ LKDYIEGWTE PKEDWE // ID R5D1F9_9FIRM Unreviewed; 432 AA. AC R5D1F9; DT 24-JUL-2013, integrated into UniProtKB/TrEMBL. DT 24-JUL-2013, sequence version 1. DT 12-APR-2017, entry version 23. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=BN705_01602 {ECO:0000313|EMBL:CCX70767.1}; OS Firmicutes bacterium CAG:555. OC Bacteria; Firmicutes; environmental samples. OX NCBI_TaxID=1263030 {ECO:0000313|EMBL:CCX70767.1, ECO:0000313|Proteomes:UP000018402}; RN [1] {ECO:0000313|EMBL:CCX70767.1, ECO:0000313|Proteomes:UP000018402} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MGS:555 {ECO:0000313|Proteomes:UP000018402}; RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., RA Sunagawa S., Plichta D., Gautier L., Le Chatelier E., Peletier E., RA Bonde I., Nielsen T., Manichanh C., Arumugam M., Batto J., RA Santos M.B.Q.D., Blom N., Borruel N., Burgdorf K.S., Boumezbeur F., RA Casellas F., Dore J., Guarner F., Hansen T., Hildebrand F., Kaas R.S., RA Kennedy S., Kristiansen K., Kultima J.R., Leonard P., Levenez F., RA Lund O., Moumen B., Le Paslier D., Pons N., Pedersen O., Prifti E., RA Qin J., Raes J., Tap J., Tims S., Ussery D.W., Yamada T., RA MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P., Wang J., RA Brunak S., Ehrlich S.D.; RT "Dependencies among metagenomic species, viruses, plasmids and units RT of genetic variation."; RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:CCX70767.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CAWW010000012; CCX70767.1; -; Genomic_DNA. DR Proteomes; UP000018402; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000018402}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000018402}. FT DOMAIN 208 368 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 167 201 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 432 AA; 48326 MW; 509F028527CEB7F4 CRC64; MENNEVKTER AVLCGLAASS MDISERSTDI SMDELAALVE TAGGETVGMM MQNRPTPDPR SFIGDGKVAE LKEFIDANDI DLAVFDNELS PSQMRVLSEE LGVKVLDRSG LILDIFAQRA QTREGQLQVE LAQYKYLLPR LTGMWTHLVR QTASGGSSPI GTRGPGETQL ETDRRHIRRK IQKLEEELAA VRKVRSTQRR KREKNDMPIV ALVGYTNAGK STLLNCLTNS DIPANDRLFD TLDTTTRKLR IDELTEVLIS DTVGFIRKLP HHLIEAFKAT LEELAYADVL LHVIDISNPD WEEQARVVDL LINQLGAEQT PCIRVFNKCD AYMGILPHGE NIVCLSAKSG EGVQELVQKL SELLDRGSHH VTLRIPYSDA GIMDLLNREA SVRSTEYTDE GIEAEVIVPP EIFGRVKRYI PGYAEPKEDW ED // ID R5D5W0_9FIRM Unreviewed; 413 AA. AC R5D5W0; DT 24-JUL-2013, integrated into UniProtKB/TrEMBL. DT 24-JUL-2013, sequence version 1. DT 12-APR-2017, entry version 23. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=BN457_01835 {ECO:0000313|EMBL:CCX74199.1}; OS Dorea sp. CAG:105. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Lachnospiraceae; OC Dorea; environmental samples. OX NCBI_TaxID=1262872 {ECO:0000313|EMBL:CCX74199.1, ECO:0000313|Proteomes:UP000017921}; RN [1] {ECO:0000313|EMBL:CCX74199.1, ECO:0000313|Proteomes:UP000017921} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MGS:105 {ECO:0000313|Proteomes:UP000017921}; RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., RA Sunagawa S., Plichta D., Gautier L., Le Chatelier E., Peletier E., RA Bonde I., Nielsen T., Manichanh C., Arumugam M., Batto J., RA Santos M.B.Q.D., Blom N., Borruel N., Burgdorf K.S., Boumezbeur F., RA Casellas F., Dore J., Guarner F., Hansen T., Hildebrand F., Kaas R.S., RA Kennedy S., Kristiansen K., Kultima J.R., Leonard P., Levenez F., RA Lund O., Moumen B., Le Paslier D., Pons N., Pedersen O., Prifti E., RA Qin J., Raes J., Tap J., Tims S., Ussery D.W., Yamada T., RA MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P., Wang J., RA Brunak S., Ehrlich S.D.; RT "Dependencies among metagenomic species, viruses, plasmids and units RT of genetic variation."; RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:CCX74199.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CAWY010000047; CCX74199.1; -; Genomic_DNA. DR Proteomes; UP000017921; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000017921}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000017921}. FT DOMAIN 199 363 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 158 192 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 413 AA; 46187 MW; EF070E824F7DF4F1 CRC64; MIELKQDKER VVLVGVELPG EESMEDSLSE LSELATTAGA ETVGRVIQNR EQVHPGTYVG KGKIEEIKDL LWELEATGII CDDELSPAQM KNLQDELNVK VMDRTLLILD IFAARASTSE GKIQVELAQL KYRQTRLTGF GTAMSRLGGG IGTRGPGEKK LEMDRRLIKS RIAALNRELK EVKRHREVTR EQRSKSYVPV VAIVGYTNAG KSTLLNRLTG ADILAEDKLF ATLDPTTRGL KLPGGQEVLL TDTVGFIKKL PHHLIEAFKS TLEEAKYADV ILHVVDTSSP QMDSQMYTVY ETLSNLGVKD KAIITAFNKQ DKLEDAPLIR DFKADYTVKI SAKTGAGLTD LTDTMEAVLR EQKVFLECLY EYRDAAKIQL IRKYGELLEE KYQEDGIFVR AYVPAELYSR VTV // ID R5DR57_9FIRM Unreviewed; 416 AA. AC R5DR57; DT 24-JUL-2013, integrated into UniProtKB/TrEMBL. DT 24-JUL-2013, sequence version 1. DT 10-MAY-2017, entry version 24. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=BN462_01733 {ECO:0000313|EMBL:CCX81294.1}; OS Ruminococcus sp. CAG:108. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Ruminococcaceae; OC Ruminococcus; environmental samples. OX NCBI_TaxID=1262950 {ECO:0000313|EMBL:CCX81294.1, ECO:0000313|Proteomes:UP000018037}; RN [1] {ECO:0000313|EMBL:CCX81294.1, ECO:0000313|Proteomes:UP000018037} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MGS:108 {ECO:0000313|Proteomes:UP000018037}; RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., RA Sunagawa S., Plichta D., Gautier L., Le Chatelier E., Peletier E., RA Bonde I., Nielsen T., Manichanh C., Arumugam M., Batto J., RA Santos M.B.Q.D., Blom N., Borruel N., Burgdorf K.S., Boumezbeur F., RA Casellas F., Dore J., Guarner F., Hansen T., Hildebrand F., Kaas R.S., RA Kennedy S., Kristiansen K., Kultima J.R., Leonard P., Levenez F., RA Lund O., Moumen B., Le Paslier D., Pons N., Pedersen O., Prifti E., RA Qin J., Raes J., Tap J., Tims S., Ussery D.W., Yamada T., RA MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P., Wang J., RA Brunak S., Ehrlich S.D.; RT "Dependencies among metagenomic species, viruses, plasmids and units RT of genetic variation."; RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:CCX81294.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CAXD010000007; CCX81294.1; -; Genomic_DNA. DR Proteomes; UP000018037; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000018037}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000018037}. FT DOMAIN 200 362 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 159 193 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 416 AA; 45835 MW; CD08390DD8FB9E86 CRC64; MELKSNEEKI TRALLVSVDT GEYDAQASLD ELFELVKSAG ADPVLSVTQN LQKIEKGTFV GTGKLAEIAE ICESQEIDLL VFDSELSPTQ IKNIEAETDV RVIDRTTLIL DIFAQRARSK EGKLQVELAQ LKYMLPRLTG KGIAMSRLGG GIGTRGPGET KLETDRRHIR RRIESLKEEL SDLEKHRQML RSRRKKDGVI TCAIVGYTNA GKSTLMNCLT DAGVLAQDKL FATLDPTSRA LKLPSGVTVM MIDTVGLVRR LPHHLVEAFR STLEEAAQSD IILNVCDASS DEARTHMQVT TDLLESLGCG DTPIITVLNK CDLLDETMLA QDFKACVRIS AKNGTGIDEL LNAIENNLPV RMKRVKILLP FAQAGLANEI RNKGTLIYEE YVAEGLSVEA VVDEALYAKL AKYECE // ID R5E6A9_9FIRM Unreviewed; 414 AA. AC R5E6A9; DT 24-JUL-2013, integrated into UniProtKB/TrEMBL. DT 24-JUL-2013, sequence version 1. DT 12-APR-2017, entry version 23. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=BN798_02159 {ECO:0000313|EMBL:CCX83671.1}; OS Eubacterium sp. CAG:86. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Eubacteriaceae; OC Eubacterium; environmental samples. OX NCBI_TaxID=1262895 {ECO:0000313|EMBL:CCX83671.1, ECO:0000313|Proteomes:UP000017940}; RN [1] {ECO:0000313|EMBL:CCX83671.1, ECO:0000313|Proteomes:UP000017940} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MGS:86 {ECO:0000313|Proteomes:UP000017940}; RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., RA Sunagawa S., Plichta D., Gautier L., Le Chatelier E., Peletier E., RA Bonde I., Nielsen T., Manichanh C., Arumugam M., Batto J., RA Santos M.B.Q.D., Blom N., Borruel N., Burgdorf K.S., Boumezbeur F., RA Casellas F., Dore J., Guarner F., Hansen T., Hildebrand F., Kaas R.S., RA Kennedy S., Kristiansen K., Kultima J.R., Leonard P., Levenez F., RA Lund O., Moumen B., Le Paslier D., Pons N., Pedersen O., Prifti E., RA Qin J., Raes J., Tap J., Tims S., Ussery D.W., Yamada T., RA MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P., Wang J., RA Brunak S., Ehrlich S.D.; RT "Dependencies among metagenomic species, viruses, plasmids and units RT of genetic variation."; RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:CCX83671.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CAXC010000116; CCX83671.1; -; Genomic_DNA. DR Proteomes; UP000017940; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000017940}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000017940}. FT DOMAIN 202 366 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 168 195 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 414 AA; 46401 MW; E3F4C29E59CB30A7 CRC64; MAQIYETDEE IERVLLIGVA LDDNDEAESS LDELAELAKT AGAVTVGRLI QPREYFHPAT YIGKGKLEEV RLIADELDAT GIICDDELTP AQLRNLEDVL NLKIMDRTMV ILDIFASRAN TSEGKIQVEM AQLKYRMTRL SGLGTTLSRL GGGIGTRGPG EKKIETDRRL IRDRISRLNA QLKEIENHRE IQRQKRSDST IPVAAIVGYT NAGKSTLLNK LTNAGVLSED KLFATLDPTT RVLKLPNTDK VLLTDTVGFI RKLPHNLIEA FKSTLEEAKY ADIIIHVVDS VHPDMDRQIA AVYETLDELQ VGDKPVITLF NKTDLAGNAE TIKDMRAKCS MRVSAKTGEG IDEFLDELGK ILRENRIHIN RCFKYQDAGR IQLIREFGTL ISEEYTQDGI EVEAYVPKEI YDKL // ID R5EBK5_9CLOT Unreviewed; 412 AA. AC R5EBK5; DT 24-JUL-2013, integrated into UniProtKB/TrEMBL. DT 24-JUL-2013, sequence version 1. DT 12-APR-2017, entry version 23. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=BN724_00214 {ECO:0000313|EMBL:CCX88624.1}; OS Clostridium sp. CAG:590. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium; environmental samples. OX NCBI_TaxID=1262825 {ECO:0000313|EMBL:CCX88624.1, ECO:0000313|Proteomes:UP000017939}; RN [1] {ECO:0000313|EMBL:CCX88624.1, ECO:0000313|Proteomes:UP000017939} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MGS:590 {ECO:0000313|Proteomes:UP000017939}; RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., RA Sunagawa S., Plichta D., Gautier L., Le Chatelier E., Peletier E., RA Bonde I., Nielsen T., Manichanh C., Arumugam M., Batto J., RA Santos M.B.Q.D., Blom N., Borruel N., Burgdorf K.S., Boumezbeur F., RA Casellas F., Dore J., Guarner F., Hansen T., Hildebrand F., Kaas R.S., RA Kennedy S., Kristiansen K., Kultima J.R., Leonard P., Levenez F., RA Lund O., Moumen B., Le Paslier D., Pons N., Pedersen O., Prifti E., RA Qin J., Raes J., Tap J., Tims S., Ussery D.W., Yamada T., RA MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P., Wang J., RA Brunak S., Ehrlich S.D.; RT "Dependencies among metagenomic species, viruses, plasmids and units RT of genetic variation."; RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:CCX88624.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CAXF010000157; CCX88624.1; -; Genomic_DNA. DR Proteomes; UP000017939; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000017939}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000017939}. FT DOMAIN 202 366 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 161 195 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 412 AA; 46810 MW; C144140EFA9CA493 CRC64; MTRFYENGTE QEKVILVSVY EKGRFQDEES LKELEELTKT AGAVCVGTLT QNLEAPNPVT YLGAGKLEEL RTMLVAYHAT GIVCDTELTP VQMKNLSQIL DIKIMDRTMI ILDIFAARAN TREGKIQVEL AQLKYNATML VGLRPSLSRL GGGIGTRGPG EKKLEMDRRL IREQISKLKR DLEQVKQHRA TQRKQRSEGS YPVVCIVGYT NAGKSTLLNH LTQADVLEED KLFATLDPTT RTLKMPNGQT VLLTDTVGFI SKLPHHLIQA FRSTLEEAKY SDLILHVVDA SNPEMDRQMF AVYETLRQLE IGDKPVITVF NKIDRLEDKP ILKDLKAEAT VMISAKQEIG FDHLFDAVEY VVRSHQVYIE KIVPYKDTAR LANVRKYGQL LEEEYKEDGI HIKAYVRRQE DI // ID R5EJF9_9FIRM Unreviewed; 422 AA. AC R5EJF9; DT 24-JUL-2013, integrated into UniProtKB/TrEMBL. DT 24-JUL-2013, sequence version 1. DT 12-APR-2017, entry version 23. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=BN466_01851 {ECO:0000313|EMBL:CCX92548.1}; OS Firmicutes bacterium CAG:110. OC Bacteria; Firmicutes; environmental samples. OX NCBI_TaxID=1263000 {ECO:0000313|EMBL:CCX92548.1, ECO:0000313|Proteomes:UP000018021}; RN [1] {ECO:0000313|EMBL:CCX92548.1, ECO:0000313|Proteomes:UP000018021} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MGS:110 {ECO:0000313|Proteomes:UP000018021}; RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., RA Sunagawa S., Plichta D., Gautier L., Le Chatelier E., Peletier E., RA Bonde I., Nielsen T., Manichanh C., Arumugam M., Batto J., RA Santos M.B.Q.D., Blom N., Borruel N., Burgdorf K.S., Boumezbeur F., RA Casellas F., Dore J., Guarner F., Hansen T., Hildebrand F., Kaas R.S., RA Kennedy S., Kristiansen K., Kultima J.R., Leonard P., Levenez F., RA Lund O., Moumen B., Le Paslier D., Pons N., Pedersen O., Prifti E., RA Qin J., Raes J., Tap J., Tims S., Ussery D.W., Yamada T., RA MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P., Wang J., RA Brunak S., Ehrlich S.D.; RT "Dependencies among metagenomic species, viruses, plasmids and units RT of genetic variation."; RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:CCX92548.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CAXG010000311; CCX92548.1; -; Genomic_DNA. DR Proteomes; UP000018021; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000018021}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000018021}. FT DOMAIN 205 366 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 164 198 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 422 AA; 46675 MW; 1665AB2308D042A0 CRC64; MEERFDKQAQ ERAVLVGLNA DCFAEEDTAT ESTLDELEDL LETAGGFCTG KVLQNRHTPD SHSFIGEGKA QEVRMLAEAT QSTMVIFDNE LSPGNIRALE EIIGLPVLDR SALILDIFAQ RAKTKEGRLQ VELAQYKYLL PRLSGMGTSL SRQGGGIGTR GPGETKLESD RRHIRERINR LEEELEQVRK VRSVQRERRM KNSVPVVAIV GYTNAGKSTL LNQLTGAGIP ANNRLFDTLD TTSRLLTVSD NLDVILSDTV GFIAKLPHHL VDAFRATLEE LEFADLLLHV IDASDPHLEE HIAVVDRLIS QLAKPETPVL KCYNKADLVY SDDIPVGKNI VAISAKRGIN MDGLLKAIES ALNHARHHIV VRLPYAMGGM VETLHDGAQV KKVDYTPEGI EIEAVVDGIL YGRLREYIIG EC // ID R5EQG1_9GAMM Unreviewed; 447 AA. AC R5EQG1; DT 24-JUL-2013, integrated into UniProtKB/TrEMBL. DT 24-JUL-2013, sequence version 1. DT 30-AUG-2017, entry version 23. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=BN779_01484 {ECO:0000313|EMBL:CCX93574.1}; OS Succinatimonas sp. CAG:777. OC Bacteria; Proteobacteria; Gammaproteobacteria; Aeromonadales; OC Succinivibrionaceae; Succinatimonas; environmental samples. OX NCBI_TaxID=1262974 {ECO:0000313|EMBL:CCX93574.1, ECO:0000313|Proteomes:UP000018241}; RN [1] {ECO:0000313|EMBL:CCX93574.1, ECO:0000313|Proteomes:UP000018241} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MGS:777 {ECO:0000313|Proteomes:UP000018241}; RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., RA Sunagawa S., Plichta D., Gautier L., Le Chatelier E., Peletier E., RA Bonde I., Nielsen T., Manichanh C., Arumugam M., Batto J., RA Santos M.B.Q.D., Blom N., Borruel N., Burgdorf K.S., Boumezbeur F., RA Casellas F., Dore J., Guarner F., Hansen T., Hildebrand F., Kaas R.S., RA Kennedy S., Kristiansen K., Kultima J.R., Leonard P., Levenez F., RA Lund O., Moumen B., Le Paslier D., Pons N., Pedersen O., Prifti E., RA Qin J., Raes J., Tap J., Tims S., Ussery D.W., Yamada T., RA MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P., Wang J., RA Brunak S., Ehrlich S.D.; RT "Dependencies among metagenomic species, viruses, plasmids and units RT of genetic variation."; RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:CCX93574.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CAXH010000114; CCX93574.1; -; Genomic_DNA. DR Proteomes; UP000018241; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000018241}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000018241}. FT DOMAIN 200 367 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 447 AA; 49271 MW; A02DF0A8A6DC7EDD CRC64; MPQSEFESLG STLLVHVELP QAQSQEDLKE LQLLAESGGG DVVFCVSCKR EAPDPSTFIG SGKVVEVSDA VKAYEVQTVI FNNKLTPAQE RNLEKAFGVR VMDRVALILT IFAQRARTYE GKLQVELAQL QYEQARLVRG WTHLERQKGG FGLRGGPGET QIELDRRALR ERIAAIKKDL DVVALRREQN RSLRKKNAVP VVSFVGYTNA GKSTLFNRLT NSDVYAANQL FATLDPTLRT VELPVIGKAV FADTVGFIRH LPHDLVAAFR GTLEETAQAD LLLHVVDASD EHKEANIEAV NAVLKQVGAE DIKTLVVYNK ADLIEDSADE IIRDDNGAPH RVYVSALTGF GIDKLLSAVS ELLSDNLCEF TVKIDGRHGK LRSLLYASNA VDSEQYDENG NCLLDVKITA VDAAIIDSKT NGALSDTCMQ EKKPWIQSNE FDFDSVN // ID R5F9V0_9BACT Unreviewed; 415 AA. AC R5F9V0; DT 24-JUL-2013, integrated into UniProtKB/TrEMBL. DT 24-JUL-2013, sequence version 1. DT 12-APR-2017, entry version 24. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=BN812_00149 {ECO:0000313|EMBL:CCY01668.1}; OS Prevotella sp. CAG:924. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Prevotellaceae; OC Prevotella; environmental samples. OX NCBI_TaxID=1262938 {ECO:0000313|EMBL:CCY01668.1, ECO:0000313|Proteomes:UP000018357}; RN [1] {ECO:0000313|EMBL:CCY01668.1, ECO:0000313|Proteomes:UP000018357} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MGS:924 {ECO:0000313|Proteomes:UP000018357}; RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., RA Sunagawa S., Plichta D., Gautier L., Le Chatelier E., Peletier E., RA Bonde I., Nielsen T., Manichanh C., Arumugam M., Batto J., RA Santos M.B.Q.D., Blom N., Borruel N., Burgdorf K.S., Boumezbeur F., RA Casellas F., Dore J., Guarner F., Hansen T., Hildebrand F., Kaas R.S., RA Kennedy S., Kristiansen K., Kultima J.R., Leonard P., Levenez F., RA Lund O., Moumen B., Le Paslier D., Pons N., Pedersen O., Prifti E., RA Qin J., Raes J., Tap J., Tims S., Ussery D.W., Yamada T., RA MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P., Wang J., RA Brunak S., Ehrlich S.D.; RT "Dependencies among metagenomic species, viruses, plasmids and units RT of genetic variation."; RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:CCY01668.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CAXK010000024; CCY01668.1; -; Genomic_DNA. DR Proteomes; UP000018357; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000018357}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000018357}. FT DOMAIN 216 400 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 415 AA; 47564 MW; C33D3453325A6156 CRC64; MKEFVISEVK AETAVLVGLI TPQQDEAKTK EYLDELEFLA DTAGAQTVKR FTQRVNGPNS VTYVGKGKLE EIKQYIHDED EADREVGMVI FDDELSAKQI RNIEKELQVK ILDRTSLILD IFAMRAQTAA AKTQVELAQY RYMLPRLQRL WTHLERQGGG SGSGGGKGSV GLRGPGETQL EMDRRIILQR MSLLKRRLEE IDKQKTTQRK NRGRLIRVAL VGYTNVGKST LMNLLAKSDV FAENKLFATL DTTVRKVVVE NLPFLLADTV GFIRKLPTDL VDSFKSTLDE VREADLLLHV VDISHPDFEE QIEVVNQTLK ELGAADKPSM IIFNKIDQYQ WVDKEPDDLT PSTRENVTLD ELRHTWMARL GDNCLFISAR EKTNIDEFRN VLYRRVRELH VQKYPYNDFL YPSEE // ID R5FIN2_9FIRM Unreviewed; 527 AA. AC R5FIN2; DT 24-JUL-2013, integrated into UniProtKB/TrEMBL. DT 24-JUL-2013, sequence version 1. DT 07-JUN-2017, entry version 23. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=BN468_00124 {ECO:0000313|EMBL:CCY04900.1}; OS Faecalibacterium sp. CAG:1138. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Ruminococcaceae; OC Faecalibacterium; environmental samples. OX NCBI_TaxID=1262896 {ECO:0000313|EMBL:CCY04900.1, ECO:0000313|Proteomes:UP000018132}; RN [1] {ECO:0000313|EMBL:CCY04900.1, ECO:0000313|Proteomes:UP000018132} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MGS:1138 {ECO:0000313|Proteomes:UP000018132}; RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., RA Sunagawa S., Plichta D., Gautier L., Le Chatelier E., Peletier E., RA Bonde I., Nielsen T., Manichanh C., Arumugam M., Batto J., RA Santos M.B.Q.D., Blom N., Borruel N., Burgdorf K.S., Boumezbeur F., RA Casellas F., Dore J., Guarner F., Hansen T., Hildebrand F., Kaas R.S., RA Kennedy S., Kristiansen K., Kultima J.R., Leonard P., Levenez F., RA Lund O., Moumen B., Le Paslier D., Pons N., Pedersen O., Prifti E., RA Qin J., Raes J., Tap J., Tims S., Ussery D.W., Yamada T., RA MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P., Wang J., RA Brunak S., Ehrlich S.D.; RT "Dependencies among metagenomic species, viruses, plasmids and units RT of genetic variation."; RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:CCY04900.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CAXL010000061; CCY04900.1; -; Genomic_DNA. DR Proteomes; UP000018132; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000018132}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000018132}. FT DOMAIN 369 527 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 328 355 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 527 AA; 58201 MW; 40EBCB33ED27F44C CRC64; MIYGNTKGVK RVTLETLENL ITDYDKNAFV DRELLATVAE ISGKLNREIC VYISRSGRVM AIAMGDAGTV ELKEFSLRRG SDRFSGVRVI HTHPNGNGRL SDMDLSALKH LRLDAMAAVG VNRGETTDME VAFLEGNGFQ GFYFKSAEMA DDDKILKKIT ELEKDISVGA ESTEAVPGTA ILVNVTQNAN GKTELSELAR LADTAGLTVV AEVLQPKASP DKMFCVGQGK LDEVKRLIQT KRADYVVFNN GLTGSQLKNL EEATGVKVLD RSMLILNIFA RHATSNEGKL QVELAMMKYT LPKLLGRGKE LSRIGGGSGS SFTRGSGETK LEEDRRRLRR QIFELSERIE KLKSERDLRR ERRRKSGVKT VAIVGYTNAG KSTLMNNVTK AGVLEEDKLF ATLDPVTRKI FVDIKKEYLL TDTVGFIDNL PHEFIDAFRS TLEEAAYADV LVHVVDASSE DRFRQMKVVD DVLESLGAGG KPTVIAYNKC DLVPDFEIPS GENAVMISAK NGKGIWELKQ KIEGMLF // ID R5FP76_9ACTN Unreviewed; 440 AA. AC R5FP76; DT 24-JUL-2013, integrated into UniProtKB/TrEMBL. DT 24-JUL-2013, sequence version 1. DT 10-MAY-2017, entry version 24. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=BN494_01091 {ECO:0000313|EMBL:CCY06673.1}; OS Eggerthella sp. CAG:1427. OC Bacteria; Actinobacteria; Coriobacteriia; Eggerthellales; OC Eggerthellaceae; Eggerthella; environmental samples. OX NCBI_TaxID=1262874 {ECO:0000313|EMBL:CCY06673.1, ECO:0000313|Proteomes:UP000018393}; RN [1] {ECO:0000313|EMBL:CCY06673.1, ECO:0000313|Proteomes:UP000018393} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MGS:1427 {ECO:0000313|Proteomes:UP000018393}; RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., RA Sunagawa S., Plichta D., Gautier L., Le Chatelier E., Peletier E., RA Bonde I., Nielsen T., Manichanh C., Arumugam M., Batto J., RA Santos M.B.Q.D., Blom N., Borruel N., Burgdorf K.S., Boumezbeur F., RA Casellas F., Dore J., Guarner F., Hansen T., Hildebrand F., Kaas R.S., RA Kennedy S., Kristiansen K., Kultima J.R., Leonard P., Levenez F., RA Lund O., Moumen B., Le Paslier D., Pons N., Pedersen O., Prifti E., RA Qin J., Raes J., Tap J., Tims S., Ussery D.W., Yamada T., RA MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P., Wang J., RA Brunak S., Ehrlich S.D.; RT "Dependencies among metagenomic species, viruses, plasmids and units RT of genetic variation."; RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:CCY06673.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CAXM010000143; CCY06673.1; -; Genomic_DNA. DR Proteomes; UP000018393; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000018393}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000018393}. FT DOMAIN 219 384 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 440 AA; 48986 MW; 43C1D9CDA1CFB4B0 CRC64; MAEYVFDEVK QHGPSTIIEK PRERAILVGV DRPNQEWSLE SSLAELERLA WTAGADMVAK TSQKLESPNP RTFVGSGKAE EIASLCRTYA ADVVIFDDEL TPSQQSNLEK VVGKDVKVID RTALILDIFA LHATSKEGRL QVKLAQNQYL YPRLRGMWAH LASNRMGGGV GSRFGEGESQ LEVDRRLIRN RITSIKRELA NVSKKRDLQR KRRKESGVFK VALAGYTNAG KSSLLNAITG SDVLSYDKLF ATLDSTTRQL VLPEGREITL TDTVGFIQKL PTTLVEAFKS TLDEINGADL ILHVVDASDP QHSRQIDTVN MVLEQIGAHE IGRIEVFNKK DLLGELQYSA LATRFPHAVF TSTKTGEGLD ELIHRIGLVA SAQDELIEVL IPYQKGNIVS FAHQRCTILN ESYEEQGTRL VLRAGKQALS RLNEYRITSE // ID R5FZQ7_9PORP Unreviewed; 412 AA. AC R5FZQ7; DT 24-JUL-2013, integrated into UniProtKB/TrEMBL. DT 24-JUL-2013, sequence version 1. DT 12-APR-2017, entry version 23. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=BN460_01245 {ECO:0000313|EMBL:CCY10515.1}; OS Porphyromonas sp. CAG:1061. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; OC Porphyromonadaceae; Porphyromonas; environmental samples. OX NCBI_TaxID=1262916 {ECO:0000313|EMBL:CCY10515.1, ECO:0000313|Proteomes:UP000018064}; RN [1] {ECO:0000313|EMBL:CCY10515.1, ECO:0000313|Proteomes:UP000018064} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MGS:1061 {ECO:0000313|Proteomes:UP000018064}; RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., RA Sunagawa S., Plichta D., Gautier L., Le Chatelier E., Peletier E., RA Bonde I., Nielsen T., Manichanh C., Arumugam M., Batto J., RA Santos M.B.Q.D., Blom N., Borruel N., Burgdorf K.S., Boumezbeur F., RA Casellas F., Dore J., Guarner F., Hansen T., Hildebrand F., Kaas R.S., RA Kennedy S., Kristiansen K., Kultima J.R., Leonard P., Levenez F., RA Lund O., Moumen B., Le Paslier D., Pons N., Pedersen O., Prifti E., RA Qin J., Raes J., Tap J., Tims S., Ussery D.W., Yamada T., RA MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P., Wang J., RA Brunak S., Ehrlich S.D.; RT "Dependencies among metagenomic species, viruses, plasmids and units RT of genetic variation."; RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:CCY10515.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CAXO010000177; CCY10515.1; -; Genomic_DNA. DR Proteomes; UP000018064; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000018064}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000018064}. FT DOMAIN 203 389 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 171 198 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 412 AA; 46987 MW; DA21DF2C60D4E1B8 CRC64; MRDFIKTDAA TDRAYLVGLV TPDVSEQEVN EYLEELAFLA HTAQIQAVES FTQRLEHPNG ATFIGSGKLQ EIADKIEEDE IGTVIFDDEL SPNQMRNIEQ KLKVRVLDRT SLILDIFASR ARTAHAKTQV ELAQYNYLLP RLTRLWSHLD RQRGGGALMR GPGETQLETD RRIVLDKIAK LKEELDKIAK QKVVQRKNRG KMVRVALVGY TNVGKSTILN LLAKSEVFAE NKLFATLDTT VRKVVVKNLP FLLSDTVGFI RKLPTELIES FKSTLDEVKE SDILIHVVDV SHPAFEEQIA VVNQTLSEIL DGEKKPTILI FNKVDAFTFE PKDEDDLTPA TKENISLEEL KKTWMAKQGE EDVLFISAKE GLGIEELKER LYERVKEIHV TRFPYDDFLF SYYDETGEEM SH // ID R5G2I0_9FIRM Unreviewed; 419 AA. AC R5G2I0; DT 24-JUL-2013, integrated into UniProtKB/TrEMBL. DT 24-JUL-2013, sequence version 1. DT 12-APR-2017, entry version 23. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=BN756_00451 {ECO:0000313|EMBL:CCY07132.1}; OS Coprobacillus sp. CAG:698. OC Bacteria; Firmicutes; Erysipelotrichia; Erysipelotrichales; OC Erysipelotrichaceae; Coprobacillus; environmental samples. OX NCBI_TaxID=1262856 {ECO:0000313|EMBL:CCY07132.1, ECO:0000313|Proteomes:UP000018297}; RN [1] {ECO:0000313|EMBL:CCY07132.1, ECO:0000313|Proteomes:UP000018297} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MGS:698 {ECO:0000313|Proteomes:UP000018297}; RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., RA Sunagawa S., Plichta D., Gautier L., Le Chatelier E., Peletier E., RA Bonde I., Nielsen T., Manichanh C., Arumugam M., Batto J., RA Santos M.B.Q.D., Blom N., Borruel N., Burgdorf K.S., Boumezbeur F., RA Casellas F., Dore J., Guarner F., Hansen T., Hildebrand F., Kaas R.S., RA Kennedy S., Kristiansen K., Kultima J.R., Leonard P., Levenez F., RA Lund O., Moumen B., Le Paslier D., Pons N., Pedersen O., Prifti E., RA Qin J., Raes J., Tap J., Tims S., Ussery D.W., Yamada T., RA MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P., Wang J., RA Brunak S., Ehrlich S.D.; RT "Dependencies among metagenomic species, viruses, plasmids and units RT of genetic variation."; RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:CCY07132.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CAXN010000018; CCY07132.1; -; Genomic_DNA. DR Proteomes; UP000018297; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000018297}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000018297}. FT DOMAIN 197 366 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 8 35 {ECO:0000256|SAM:Coils}. FT COILED 163 190 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 419 AA; 47838 MW; 53A060CF091D4AB6 CRC64; MKAILVGVKL DNIQINDFED EMSELKNLSE ACDIEVVDSI KQNLDSFNPV TYIGSGKIEE IKMSVEANEA DVVICNDELT PLQISKLSEK IDVQIYDRTY LILEIFKRRA KTKEAILQVE IASLTYLLPR LAGMRQGLSR QRGAGGGFAH GRGAGETKLE LDRRINSDKI SQLKKELKEL EKVRRVQREK RTASDLAKVC LVGYTNSGKS TLMNKFLEIT NSKDEKKVFQ KDMLFATLET SSRKIDYKNG GFILTDTVGF IEKLPHNLIE AFKSTLEEIK ECDLIIHVVD GSNSKHLSQI KATNEVLNEL DVKDIPVIYA FNKIDKIDNY LYIPNEFPEA IRISALNGYN IDELLKLIFK KTYGEYESVE MLIPYGMEND YYKIKNKSII ETTSYEEKGI YVKCQINNEV KNKYGKYII // ID R5GLM8_9BACT Unreviewed; 417 AA. AC R5GLM8; DT 24-JUL-2013, integrated into UniProtKB/TrEMBL. DT 24-JUL-2013, sequence version 1. DT 12-APR-2017, entry version 24. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=BN773_00684 {ECO:0000313|EMBL:CCY16609.1}; OS Prevotella sp. CAG:755. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Prevotellaceae; OC Prevotella; environmental samples. OX NCBI_TaxID=1262935 {ECO:0000313|EMBL:CCY16609.1, ECO:0000313|Proteomes:UP000018353}; RN [1] {ECO:0000313|EMBL:CCY16609.1, ECO:0000313|Proteomes:UP000018353} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MGS:755 {ECO:0000313|Proteomes:UP000018353}; RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., RA Sunagawa S., Plichta D., Gautier L., Le Chatelier E., Peletier E., RA Bonde I., Nielsen T., Manichanh C., Arumugam M., Batto J., RA Santos M.B.Q.D., Blom N., Borruel N., Burgdorf K.S., Boumezbeur F., RA Casellas F., Dore J., Guarner F., Hansen T., Hildebrand F., Kaas R.S., RA Kennedy S., Kristiansen K., Kultima J.R., Leonard P., Levenez F., RA Lund O., Moumen B., Le Paslier D., Pons N., Pedersen O., Prifti E., RA Qin J., Raes J., Tap J., Tims S., Ussery D.W., Yamada T., RA MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P., Wang J., RA Brunak S., Ehrlich S.D.; RT "Dependencies among metagenomic species, viruses, plasmids and units RT of genetic variation."; RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:CCY16609.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CAXR010000182; CCY16609.1; -; Genomic_DNA. DR Proteomes; UP000018353; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000018353}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000018353}. FT DOMAIN 216 400 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 417 AA; 47547 MW; 726522B1F5F76EA8 CRC64; MKEFVLSEAQ TETAVLVALI TRTQDERKTN EYLDELAFLA ETAGARTVKR FTQRLDQPLA ATYVGKGKLD EIRQYIEEEE EADREVGMVI FDDELSAKQL RNIERELKVK ILDRTSLILD IFAMRAQTAN AKTQVELAQY KYMLPRLQRL WTHLERQGGG SGSGGGKGSV GLRGPGETQL EMDRRIILNR MALLKQRLAD IDRQKATQRK NRGRLIRVAL VGYTNVGKST LINLLAKSDV FAENKLFATL DTTVRKVIIG NLPFLLSDTV GFIRKIPTDL VDSFKSTLDE VREADLLLHV VDLSHPDFEE QIDVVNRTLA DLGCAEKPVI IVFNKIDAYT WTEKAADDLT PATKENISLE ELQRTWMAKM GEGCIFISAR QRENIEALKD LLYRRVRELH VQKYPYNDFL FDTYEEA // ID R5GSB9_9FIRM Unreviewed; 410 AA. AC R5GSB9; DT 24-JUL-2013, integrated into UniProtKB/TrEMBL. DT 24-JUL-2013, sequence version 1. DT 12-APR-2017, entry version 23. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=BN782_00358 {ECO:0000313|EMBL:CCY20315.1}; OS Eubacterium sp. CAG:786. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Eubacteriaceae; OC Eubacterium; environmental samples. OX NCBI_TaxID=1262893 {ECO:0000313|EMBL:CCY20315.1, ECO:0000313|Proteomes:UP000018127}; RN [1] {ECO:0000313|EMBL:CCY20315.1, ECO:0000313|Proteomes:UP000018127} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MGS:786 {ECO:0000313|Proteomes:UP000018127}; RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., RA Sunagawa S., Plichta D., Gautier L., Le Chatelier E., Peletier E., RA Bonde I., Nielsen T., Manichanh C., Arumugam M., Batto J., RA Santos M.B.Q.D., Blom N., Borruel N., Burgdorf K.S., Boumezbeur F., RA Casellas F., Dore J., Guarner F., Hansen T., Hildebrand F., Kaas R.S., RA Kennedy S., Kristiansen K., Kultima J.R., Leonard P., Levenez F., RA Lund O., Moumen B., Le Paslier D., Pons N., Pedersen O., Prifti E., RA Qin J., Raes J., Tap J., Tims S., Ussery D.W., Yamada T., RA MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P., Wang J., RA Brunak S., Ehrlich S.D.; RT "Dependencies among metagenomic species, viruses, plasmids and units RT of genetic variation."; RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:CCY20315.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CAXS010000310; CCY20315.1; -; Genomic_DNA. DR Proteomes; UP000018127; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000018127}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000018127}. FT DOMAIN 196 356 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 155 189 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 410 AA; 44954 MW; 36149A0DC1E06E4F CRC64; MEEKHLTRAI LIGADTGEYD AESSMDELAE LAQTAGAEEL ARVIQKREAY EAATVIGEGK LAEVKELCGS LGAELLIFDC ELTASQIRNV EDETDVRVID RTMLILDIFA GRAVSREGKL QVELAQLKYR LPRLMGIGAS LSRLGGGIGT RGPGETQLET DRRHIRRRID KLSAELRELE ERRGFTRNRR KKDSVQVGAI VGYTNAGKST LLNLLTGAGV LAEDKLFATL DPTARSIELP DGRSLLLIDT VGLIRRLPHH LVEAFKSTLE EAASADIIIH VCDAADPEAT EKADVTLKTL ADLGAAEIPV VTVLNKCDLL TEHIPEDSAT VKISAKNNQG IDRLLQVIAA NLPETAKRMK LLLPYDKAGY TAKLRENGKV FSEEYTENGV LVDALVDQML ITQMEQYKTE // ID R5GXC1_9FIRM Unreviewed; 442 AA. AC R5GXC1; DT 24-JUL-2013, integrated into UniProtKB/TrEMBL. DT 24-JUL-2013, sequence version 1. DT 12-APR-2017, entry version 24. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=BN555_01586 {ECO:0000313|EMBL:CCY21883.1}; OS Firmicutes bacterium CAG:24. OC Bacteria; Firmicutes; environmental samples. OX NCBI_TaxID=1263012 {ECO:0000313|EMBL:CCY21883.1, ECO:0000313|Proteomes:UP000017963}; RN [1] {ECO:0000313|EMBL:CCY21883.1, ECO:0000313|Proteomes:UP000017963} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MGS:24 {ECO:0000313|Proteomes:UP000017963}; RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., RA Sunagawa S., Plichta D., Gautier L., Le Chatelier E., Peletier E., RA Bonde I., Nielsen T., Manichanh C., Arumugam M., Batto J., RA Santos M.B.Q.D., Blom N., Borruel N., Burgdorf K.S., Boumezbeur F., RA Casellas F., Dore J., Guarner F., Hansen T., Hildebrand F., Kaas R.S., RA Kennedy S., Kristiansen K., Kultima J.R., Leonard P., Levenez F., RA Lund O., Moumen B., Le Paslier D., Pons N., Pedersen O., Prifti E., RA Qin J., Raes J., Tap J., Tims S., Ussery D.W., Yamada T., RA MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P., Wang J., RA Brunak S., Ehrlich S.D.; RT "Dependencies among metagenomic species, viruses, plasmids and units RT of genetic variation."; RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:CCY21883.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CAXU010000091; CCY21883.1; -; Genomic_DNA. DR Proteomes; UP000017963; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000017963}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000017963}. FT DOMAIN 204 374 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 163 197 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 442 AA; 49172 MW; 99A3258ED4877404 CRC64; MQKAILVGVN LNENLDFDHS MEELENLAEA CEIEAAAQIV QNLPMVNNAF YIGTGKVEEV KNLVSMLDAD CVIFDNSLTP SQQRNLQNQL EVPVWDRTNL ILEIFDRRAR TKEARLQVES ANLQYLLPRL VGMRDALSRQ GGGAGAGGGA GAGGGLSNKG AGEKKLELDR RRIEKRISEL NRELKVMEKD RETQRKRRKE SELPSVALVG YTNAGKSTLM NKMLDIWMGD TEKKVLEKDM LFATLDTTVR RISPGDNRDF LLSDTVGFIS QLPHTLVKAF RSTLEEACTA DLLLQVVDFS DPHHREQMEV TQETLKELQA GQIPCLYVMN KADLVMEESE LPKVLGDRIY LSAKQGIGLA ELLELIQKKL FGDYRECTFL IPYTDGAAVS RLQEQALVRS ISYEADGVLI SVSCKESDAG RYAAYAVSTS DDAETAFERE GA // ID R5HCD5_9FIRM Unreviewed; 435 AA. AC R5HCD5; DT 24-JUL-2013, integrated into UniProtKB/TrEMBL. DT 24-JUL-2013, sequence version 1. DT 12-APR-2017, entry version 24. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=BN469_00762 {ECO:0000313|EMBL:CCY25789.1}; OS Firmicutes bacterium CAG:114. OC Bacteria; Firmicutes; environmental samples. OX NCBI_TaxID=1263001 {ECO:0000313|EMBL:CCY25789.1, ECO:0000313|Proteomes:UP000018090}; RN [1] {ECO:0000313|EMBL:CCY25789.1, ECO:0000313|Proteomes:UP000018090} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MGS:114 {ECO:0000313|Proteomes:UP000018090}; RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., RA Sunagawa S., Plichta D., Gautier L., Le Chatelier E., Peletier E., RA Bonde I., Nielsen T., Manichanh C., Arumugam M., Batto J., RA Santos M.B.Q.D., Blom N., Borruel N., Burgdorf K.S., Boumezbeur F., RA Casellas F., Dore J., Guarner F., Hansen T., Hildebrand F., Kaas R.S., RA Kennedy S., Kristiansen K., Kultima J.R., Leonard P., Levenez F., RA Lund O., Moumen B., Le Paslier D., Pons N., Pedersen O., Prifti E., RA Qin J., Raes J., Tap J., Tims S., Ussery D.W., Yamada T., RA MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P., Wang J., RA Brunak S., Ehrlich S.D.; RT "Dependencies among metagenomic species, viruses, plasmids and units RT of genetic variation."; RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:CCY25789.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CAXW010000022; CCY25789.1; -; Genomic_DNA. DR Proteomes; UP000018090; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR Gene3D; 3.40.50.620; -; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR014729; Rossmann-like_a/b/a_fold. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000018090}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000018090}. FT DOMAIN 210 371 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 176 203 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 435 AA; 48201 MW; 3B634A2C24B1B6DD CRC64; MTDHTMEEKR NHAVLVGLHA SSLSQEENAS DATLEELEAL LETAGGVCVG SVLQNRETPE ARTFIGEGKV AEVAALVQAQ GADLVVFDNE LSPSQQRVLT EEVGAQVIDR AGLILDIFAQ RARTKEGRLQ VELAQYKYLL PRLTGMWGHL VRQTASGGKS PIGTRGPGET QLETDRRHIR RKIAKLTEDL EEVRRIRAVQ RDRREKNEIP VVAIVGYTNA GKSTLLNALT HAGIPARNRL FDTLDTTTRT LEISDTCTVL ISDTVGFIRK LPHHLVEAFK ATLEELAYAD LILHVIDASN PEWREQAEVV EGLIRQLGAE ATPRLEVFNK SDIYVGEIRP HGEDIVSISA KTGEGLDQLL AMIGKRLDTG FYRVTLSVPY DKGGVVDMLY REAKVESVEY GQTIQVVAVC GEKTVGQVRE YVIDGWQPSK EFWED // ID R5HPG1_9FIRM Unreviewed; 414 AA. AC R5HPG1; DT 24-JUL-2013, integrated into UniProtKB/TrEMBL. DT 24-JUL-2013, sequence version 1. DT 12-APR-2017, entry version 24. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=BN501_00979 {ECO:0000313|EMBL:CCY31613.1}; OS Roseburia inulinivorans CAG:15. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Lachnospiraceae; OC Roseburia; environmental samples. OX NCBI_TaxID=1263105 {ECO:0000313|EMBL:CCY31613.1, ECO:0000313|Proteomes:UP000018212}; RN [1] {ECO:0000313|EMBL:CCY31613.1, ECO:0000313|Proteomes:UP000018212} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MGS:15 {ECO:0000313|Proteomes:UP000018212}; RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., RA Sunagawa S., Plichta D., Gautier L., Le Chatelier E., Peletier E., RA Bonde I., Nielsen T., Manichanh C., Arumugam M., Batto J., RA Santos M.B.Q.D., Blom N., Borruel N., Burgdorf K.S., Boumezbeur F., RA Casellas F., Dore J., Guarner F., Hansen T., Hildebrand F., Kaas R.S., RA Kennedy S., Kristiansen K., Kultima J.R., Leonard P., Levenez F., RA Lund O., Moumen B., Le Paslier D., Pons N., Pedersen O., Prifti E., RA Qin J., Raes J., Tap J., Tims S., Ussery D.W., Yamada T., RA MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P., Wang J., RA Brunak S., Ehrlich S.D.; RT "Dependencies among metagenomic species, viruses, plasmids and units RT of genetic variation."; RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:CCY31613.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CAXY010000266; CCY31613.1; -; Genomic_DNA. DR Proteomes; UP000018212; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000018212}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000018212}. FT DOMAIN 202 366 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 161 195 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 414 AA; 46210 MW; 875B422D6FFAE50F CRC64; MAEAFKIEEI EEKVILVGVS EQDGDDAEDS VAELAELVKT AGATVVGTMI QKRELIHPGT YIGSGKVAEL KLLVEELGAT GIVCDDELSP AQLRNLEDML DTKVMDRTLI ILDIFAARAT TSEGKIQVEL AQLKYRLSRL TGLGRSMSRL GGGIGTRGPG EKKLEIDRRL IKDRIAQLNR ELKEVRQHRD ITRAQREKNQ MPVAAIVGYT NAGKSTLINT LTNAGVLEED KLFATLDPTT RVLELSGRQQ ILVTDTIGFI RKLPHHLIEA FKSTLEEAKY ADYILHVVDA SNPQHEKQML IVYETLANLD VKDKTVITLF NKQDARMDSE PLHDFKADHT LPISAKNGTG LEELKNLLSE LLRENKVLVE RTVPYANAGV IQLVRKSGEL LEEEYREDGI YIRAYVPMEI YAKL // ID R5I867_9FIRM Unreviewed; 411 AA. AC R5I867; DT 24-JUL-2013, integrated into UniProtKB/TrEMBL. DT 24-JUL-2013, sequence version 1. DT 10-MAY-2017, entry version 23. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=BN729_02145 {ECO:0000313|EMBL:CCY33167.1}; OS Ruminococcus sp. CAG:60. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Ruminococcaceae; OC Ruminococcus; environmental samples. OX NCBI_TaxID=1262964 {ECO:0000313|EMBL:CCY33167.1, ECO:0000313|Proteomes:UP000017995}; RN [1] {ECO:0000313|EMBL:CCY33167.1, ECO:0000313|Proteomes:UP000017995} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MGS:60 {ECO:0000313|Proteomes:UP000017995}; RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., RA Sunagawa S., Plichta D., Gautier L., Le Chatelier E., Peletier E., RA Bonde I., Nielsen T., Manichanh C., Arumugam M., Batto J., RA Santos M.B.Q.D., Blom N., Borruel N., Burgdorf K.S., Boumezbeur F., RA Casellas F., Dore J., Guarner F., Hansen T., Hildebrand F., Kaas R.S., RA Kennedy S., Kristiansen K., Kultima J.R., Leonard P., Levenez F., RA Lund O., Moumen B., Le Paslier D., Pons N., Pedersen O., Prifti E., RA Qin J., Raes J., Tap J., Tims S., Ussery D.W., Yamada T., RA MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P., Wang J., RA Brunak S., Ehrlich S.D.; RT "Dependencies among metagenomic species, viruses, plasmids and units RT of genetic variation."; RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:CCY33167.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CAYA010000188; CCY33167.1; -; Genomic_DNA. DR Proteomes; UP000017995; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000017995}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000017995}. FT DOMAIN 199 362 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 158 185 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 411 AA; 45602 MW; 990669EC58215D6D CRC64; MEYIEEIQER VILVGVQLDE NDNVKESLDE LEELADTAGA VTVGKIIQNR ETVHPGTYIG KGKIEEVRAL MLATDATGII CDDELSPAQM NNLEHELECK VMDRTLLILD IFAKHATTSE GKIQVELAQL RYRASRLVGL GASLSRLGGG IGTRGPGEKK LESDRRLIRK RITALKEELS QVEKHRELLR TGRTRGKMKT AAIVGYTNAG KSTLLNTLTG AGVLSEDKLF ATLDPTTRAL TLDDGQQILL TDTVGFIRKL PHNLVEAFKS TLEEAKYADY IIHVVDCSNP QAEQQMEVVY DTLHELEVQG KKTITLFNKV DVGAAIRMRD SMADHTLKVS AKTGEGLDEL KALLGKILSE EQIYVEKLFG YQEAGKIQLI REYGQLLSEE YTDSGIMVKA RVPQEIHGKI M // ID R5IAQ0_9BACT Unreviewed; 410 AA. AC R5IAQ0; DT 24-JUL-2013, integrated into UniProtKB/TrEMBL. DT 24-JUL-2013, sequence version 1. DT 30-AUG-2017, entry version 25. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=BN472_00439 {ECO:0000313|EMBL:CCY39105.1}; OS Tannerella sp. CAG:118. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Tannerellaceae; OC Tannerella; environmental samples. OX NCBI_TaxID=1262978 {ECO:0000313|EMBL:CCY39105.1, ECO:0000313|Proteomes:UP000018396}; RN [1] {ECO:0000313|EMBL:CCY39105.1, ECO:0000313|Proteomes:UP000018396} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MGS:118 {ECO:0000313|Proteomes:UP000018396}; RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., RA Sunagawa S., Plichta D., Gautier L., Le Chatelier E., Peletier E., RA Bonde I., Nielsen T., Manichanh C., Arumugam M., Batto J., RA Santos M.B.Q.D., Blom N., Borruel N., Burgdorf K.S., Boumezbeur F., RA Casellas F., Dore J., Guarner F., Hansen T., Hildebrand F., Kaas R.S., RA Kennedy S., Kristiansen K., Kultima J.R., Leonard P., Levenez F., RA Lund O., Moumen B., Le Paslier D., Pons N., Pedersen O., Prifti E., RA Qin J., Raes J., Tap J., Tims S., Ussery D.W., Yamada T., RA MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P., Wang J., RA Brunak S., Ehrlich S.D.; RT "Dependencies among metagenomic species, viruses, plasmids and units RT of genetic variation."; RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:CCY39105.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CAYC010000236; CCY39105.1; -; Genomic_DNA. DR Proteomes; UP000018396; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000018396}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000018396}. FT DOMAIN 202 387 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 410 AA; 47225 MW; F00E19794584525F CRC64; MKEFILTKQE TERTILVGII TQAQNEAKAN EYLDELAFLA ETAGAEPVKK FLQRLEYPNP TTFVGAGKLQ EIKTYIEENE IGLAIFDDDL TPKQLKNIEH ELQVKILDRT SLILDIFAKR AQTAHAKSQV ELAQYQYLLP RLTRLWTHLE RQRGGIGMRG PGETQIETDR RIILDKIARL KVELKQIDKQ KAIQRKNRGK MVRVALVGYT NVGKSTLMNL LSKSEVFAEN KLFATLDTTV RKVIIDNLPF LLSDTVGFIR KLPTHLVESF KSTLDEVREA DLLVHVVDIS HPAFEEQIDI VNRTLHEVCD SADKPMIIVF NKTDAFSYIE KDADDLTPCT KENISLEELK TTWMAKMNDN CIFISAKEKQ NIDELKEMLY NKVKEIHVTR FPYNDFLYQK YDDNDTSIEE // ID R5IC90_9FIRM Unreviewed; 421 AA. AC R5IC90; DT 24-JUL-2013, integrated into UniProtKB/TrEMBL. DT 24-JUL-2013, sequence version 1. DT 12-APR-2017, entry version 24. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=BN480_01040 {ECO:0000313|EMBL:CCY39713.1}; OS Firmicutes bacterium CAG:124. OC Bacteria; Firmicutes; environmental samples. OX NCBI_TaxID=1263002 {ECO:0000313|EMBL:CCY39713.1, ECO:0000313|Proteomes:UP000018269}; RN [1] {ECO:0000313|EMBL:CCY39713.1, ECO:0000313|Proteomes:UP000018269} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MGS:124 {ECO:0000313|Proteomes:UP000018269}; RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., RA Sunagawa S., Plichta D., Gautier L., Le Chatelier E., Peletier E., RA Bonde I., Nielsen T., Manichanh C., Arumugam M., Batto J., RA Santos M.B.Q.D., Blom N., Borruel N., Burgdorf K.S., Boumezbeur F., RA Casellas F., Dore J., Guarner F., Hansen T., Hildebrand F., Kaas R.S., RA Kennedy S., Kristiansen K., Kultima J.R., Leonard P., Levenez F., RA Lund O., Moumen B., Le Paslier D., Pons N., Pedersen O., Prifti E., RA Qin J., Raes J., Tap J., Tims S., Ussery D.W., Yamada T., RA MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P., Wang J., RA Brunak S., Ehrlich S.D.; RT "Dependencies among metagenomic species, viruses, plasmids and units RT of genetic variation."; RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:CCY39713.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CAYD010000018; CCY39713.1; -; Genomic_DNA. DR Proteomes; UP000018269; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000018269}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000018269}. FT DOMAIN 204 365 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 421 AA; 46807 MW; E19C20F512D2F4A0 CRC64; MEELNRKTID RAVLVGLNAD CFTKEETATE TTLDELEALL NTAGGECAGK VLQNKHTPDP RSFIGEGKAE EVRQLVLETG ANMVIFDNDL TPSQTRTLED ILKTTVLDRS ALILDIFAQR AKTREGKLQV ELAQYQYYLP RLTVWNEEMG RLGGGIGTRG PGETQLETDK RYIRSRIQKL RENLELVRKT RAEQRRRRQK NELPVVALVG YTNAGKSTLL NALTGSDIPA NNRLFDTLDT TTRQLTVSDT CQALLSDTVG FIAKLPHHLV EAFRATLEEL EYADLLVHVI DSADPEREDH IAVVNRLIAE LAKPGTPVLE CYNKCDLVPD DEIPRGSDKV AISAASGYGL DALREAIETQ LGRGKHRVKL LLPYQQGGMV AALHDTAQVL SSEYTDNGIQ IDAVLDETLF GKLRQYVIEE V // ID R5IGB7_9BACT Unreviewed; 419 AA. AC R5IGB7; DT 24-JUL-2013, integrated into UniProtKB/TrEMBL. DT 24-JUL-2013, sequence version 1. DT 12-APR-2017, entry version 24. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=BN796_00015 {ECO:0000313|EMBL:CCY35836.1}; OS Alistipes sp. CAG:831. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Rikenellaceae; OC Alistipes; environmental samples. OX NCBI_TaxID=1262698 {ECO:0000313|EMBL:CCY35836.1, ECO:0000313|Proteomes:UP000018094}; RN [1] {ECO:0000313|EMBL:CCY35836.1, ECO:0000313|Proteomes:UP000018094} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MGS:831 {ECO:0000313|Proteomes:UP000018094}; RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., RA Sunagawa S., Plichta D., Gautier L., Le Chatelier E., Peletier E., RA Bonde I., Nielsen T., Manichanh C., Arumugam M., Batto J., RA Santos M.B.Q.D., Blom N., Borruel N., Burgdorf K.S., Boumezbeur F., RA Casellas F., Dore J., Guarner F., Hansen T., Hildebrand F., Kaas R.S., RA Kennedy S., Kristiansen K., Kultima J.R., Leonard P., Levenez F., RA Lund O., Moumen B., Le Paslier D., Pons N., Pedersen O., Prifti E., RA Qin J., Raes J., Tap J., Tims S., Ussery D.W., Yamada T., RA MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P., Wang J., RA Brunak S., Ehrlich S.D.; RT "Dependencies among metagenomic species, viruses, plasmids and units RT of genetic variation."; RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:CCY35836.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CAYB010000082; CCY35836.1; -; Genomic_DNA. DR Proteomes; UP000018094; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000018094}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000018094}. FT DOMAIN 214 398 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 419 AA; 48558 MW; A2CEAB7B14455907 CRC64; MRLPLKRVSL IFLKSMKQEE EAFERIVVVS IVPQGTDERR IKENLDELEF LALTAGAKSE KRFTQKMERA NSRTYVGSGK LAEIKNYIEE HEIKLVIFDD ELTPSQLRNL EKELGCRILD RTNLILDIFA QRAKTAYAKT QVELAQYQYL LPRLTRMWTH LERQRGGIGM RGPGESQIET DRRIILNKIS LLKEQLKKID RQMASQRGNR GSLVRVSLVG YTNAGKSTLM NLLSKSDVFA ENKLFATLDT TVRKVVIENV PFLLSDTVGF IRKLPTELVE SFKSTLDEVR EADILLHVVD ISHPDFEEQI NAVNSTLMDI GAKDKPIFMV FNKIDAYNYK EKSEYDFEEE KPENIPLERL EKMWIAKENS ACIFISAKER INIDKLRKDL YSMVKSIHEG RYPFNNLLYE TYSNEETRS // ID R5J3C0_9CLOT Unreviewed; 422 AA. AC R5J3C0; DT 24-JUL-2013, integrated into UniProtKB/TrEMBL. DT 24-JUL-2013, sequence version 1. DT 10-MAY-2017, entry version 25. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=BN757_02704 {ECO:0000313|EMBL:CCY43432.1}; OS Clostridium sp. CAG:7. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium; environmental samples. OX NCBI_TaxID=1262832 {ECO:0000313|EMBL:CCY43432.1, ECO:0000313|Proteomes:UP000018268}; RN [1] {ECO:0000313|EMBL:CCY43432.1, ECO:0000313|Proteomes:UP000018268} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MGS:7 {ECO:0000313|Proteomes:UP000018268}; RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., RA Sunagawa S., Plichta D., Gautier L., Le Chatelier E., Peletier E., RA Bonde I., Nielsen T., Manichanh C., Arumugam M., Batto J., RA Santos M.B.Q.D., Blom N., Borruel N., Burgdorf K.S., Boumezbeur F., RA Casellas F., Dore J., Guarner F., Hansen T., Hildebrand F., Kaas R.S., RA Kennedy S., Kristiansen K., Kultima J.R., Leonard P., Levenez F., RA Lund O., Moumen B., Le Paslier D., Pons N., Pedersen O., Prifti E., RA Qin J., Raes J., Tap J., Tims S., Ussery D.W., Yamada T., RA MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P., Wang J., RA Brunak S., Ehrlich S.D.; RT "Dependencies among metagenomic species, viruses, plasmids and units RT of genetic variation."; RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:CCY43432.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CAYE010000129; CCY43432.1; -; Genomic_DNA. DR Proteomes; UP000018268; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000018268}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000018268}. FT DOMAIN 199 365 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 422 AA; 47162 MW; 227911AF29EA1B94 CRC64; MIDLKELEER VILAAVSTSE TDMAERSLDE LKELADTAGA KTVGRVIQNR ESVHPGTYLG KGKLQELREM LYETGATGVI CDDELSPAQL KNLEDILDTK VMDRTMVILD IFAARANTRE GKIQVELAQL KYRAIRLVGM RSSLSRLGGG IGTRGPGEKK LETDRRLIHQ RIGQLKKELE DVKRHREVTR QQRGKDHALT AAIVGYTNAG KSTLLNRLTG AGILAEDKLF ATLDPTTRSF TLGDGQQILL TDTVGFINKL PHHLVEAFKS TLEEARYSDI VLHVVDCSNP QMDMHMHVVK ETLRELGITD KTIVTVFNKT DRLEESGLPI PRDFSADYQV RISAKNGDGL KELEEILGNI IRSRRVYLEK TYSYSQAGKL QTIRKYGQLL SEEYTEEGIK VTAYVPAELF AGLYGDGSEE KE // ID R5J4I4_9FIRM Unreviewed; 437 AA. AC R5J4I4; DT 24-JUL-2013, integrated into UniProtKB/TrEMBL. DT 24-JUL-2013, sequence version 1. DT 10-MAY-2017, entry version 24. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=BN738_00961 {ECO:0000313|EMBL:CCY49443.1}; OS Peptostreptococcus anaerobius CAG:621. OC Bacteria; Firmicutes; Clostridia; Clostridiales; OC Peptostreptococcaceae; Peptostreptococcus; environmental samples. OX NCBI_TaxID=1263100 {ECO:0000313|EMBL:CCY49443.1, ECO:0000313|Proteomes:UP000018261}; RN [1] {ECO:0000313|EMBL:CCY49443.1, ECO:0000313|Proteomes:UP000018261} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MGS:621 {ECO:0000313|Proteomes:UP000018261}; RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., RA Sunagawa S., Plichta D., Gautier L., Le Chatelier E., Peletier E., RA Bonde I., Nielsen T., Manichanh C., Arumugam M., Batto J., RA Santos M.B.Q.D., Blom N., Borruel N., Burgdorf K.S., Boumezbeur F., RA Casellas F., Dore J., Guarner F., Hansen T., Hildebrand F., Kaas R.S., RA Kennedy S., Kristiansen K., Kultima J.R., Leonard P., Levenez F., RA Lund O., Moumen B., Le Paslier D., Pons N., Pedersen O., Prifti E., RA Qin J., Raes J., Tap J., Tims S., Ussery D.W., Yamada T., RA MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P., Wang J., RA Brunak S., Ehrlich S.D.; RT "Dependencies among metagenomic species, viruses, plasmids and units RT of genetic variation."; RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:CCY49443.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CAYH010000091; CCY49443.1; -; Genomic_DNA. DR Proteomes; UP000018261; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000018261}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000018261}. FT DOMAIN 212 382 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 437 AA; 49432 MW; AEF1FA3DD7105C6F CRC64; MSDLDIKNKP EDQLVERALC VGLNITSRVM RGSDISIEES MAELKELVKA AGAEFVGELI QNKDKVDTAT YLGSGKIEEI KIYAESLDAT MIVFNDELSG AQIRNIEDII GKKIIDRTTL ILDIFAQRAL SREGKLQVEL AQLKYRLPRL YGMGGQMSRT GAGIGTRGPG EQKLEKDKRH ILNRAAAIRK ELKEVVKHRE IQRSQRQKNK IPIVALVGYT NAGKSTLLNE LIKTHPDYEA EKGVFVKDML FATLDVTLRR ALLPNKREFL LVDTVGFVSK LPHDLIEAFK STLEEVNYAD LILHVIDATN ESSDIQKHTT DSVLKDLGAD EKATITVYNK IDRLNLDIYP KSQEDLVYVS AKQGINLDKL VKLIEKKLTE DSYEVNLLLP YDKGQIFSYL SDKYPIDKFE YTDEGIDLLV SLDEVDFNIY KEYIKTK // ID R5JA03_9FIRM Unreviewed; 430 AA. AC R5JA03; DT 24-JUL-2013, integrated into UniProtKB/TrEMBL. DT 24-JUL-2013, sequence version 1. DT 10-MAY-2017, entry version 15. DE SubName: Full=GTP-binding protein HflX {ECO:0000313|EMBL:CCY49444.1}; GN ORFNames=BN738_00962 {ECO:0000313|EMBL:CCY49444.1}; OS Peptostreptococcus anaerobius CAG:621. OC Bacteria; Firmicutes; Clostridia; Clostridiales; OC Peptostreptococcaceae; Peptostreptococcus; environmental samples. OX NCBI_TaxID=1263100 {ECO:0000313|EMBL:CCY49444.1, ECO:0000313|Proteomes:UP000018261}; RN [1] {ECO:0000313|EMBL:CCY49444.1, ECO:0000313|Proteomes:UP000018261} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MGS:621 {ECO:0000313|Proteomes:UP000018261}; RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., RA Sunagawa S., Plichta D., Gautier L., Le Chatelier E., Peletier E., RA Bonde I., Nielsen T., Manichanh C., Arumugam M., Batto J., RA Santos M.B.Q.D., Blom N., Borruel N., Burgdorf K.S., Boumezbeur F., RA Casellas F., Dore J., Guarner F., Hansen T., Hildebrand F., Kaas R.S., RA Kennedy S., Kristiansen K., Kultima J.R., Leonard P., Levenez F., RA Lund O., Moumen B., Le Paslier D., Pons N., Pedersen O., Prifti E., RA Qin J., Raes J., Tap J., Tims S., Ussery D.W., Yamada T., RA MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P., Wang J., RA Brunak S., Ehrlich S.D.; RT "Dependencies among metagenomic species, viruses, plasmids and units RT of genetic variation."; RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:CCY49444.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CAYH010000091; CCY49444.1; -; Genomic_DNA. DR Proteomes; UP000018261; Unassembled WGS sequence. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000018261}; KW Reference proteome {ECO:0000313|Proteomes:UP000018261}. FT DOMAIN 207 375 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 430 AA; 49065 MW; 091EB79F828E825D CRC64; MEKLIISNKD VSKFDEVAVL LAVNEGEEFH ATTVYESMIE LKELVQAAGS ETKAELVLNQ KIDPDYYVDK ENLEYVAKHA QELEIDMIVT IDSLSGNQIK NMEEVTGLKV VDRTILLLDI FSQSSSRREG KLEIEKAQLK YRSTRIEGFQ GKYKYGSGIG VFSPSKKRLL TDLNEINERI DSIKTDLSVI VKNRFVQRSR KTDVKAPLVA FAGYTNCGKS TIMNKLIELG PDHTKESEVI VKDHMLSTLD VSLRKSMLPN GKDFMIVDTI GFVSDLPGII REAFRSTFEE VSYADLILVI YDASRDDLEA QKSIMDFTFE KIGVSNKRKI EVYNKADKLD PIPESSDNKI YVSAKSGYNL DKLIEAIQFN LFEDNQDASL LIPYSRFDIF NEIKKNRVIE MDDFKHTDFG IELNIVLSKD EFKKYKLFIK // ID R5JUS1_9BACE Unreviewed; 420 AA. AC R5JUS1; DT 24-JUL-2013, integrated into UniProtKB/TrEMBL. DT 24-JUL-2013, sequence version 1. DT 12-APR-2017, entry version 22. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=BN523_01004 {ECO:0000313|EMBL:CCY52786.1}; OS Bacteroides sp. CAG:189. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae; OC Bacteroides; environmental samples. OX NCBI_TaxID=1262737 {ECO:0000313|EMBL:CCY52786.1, ECO:0000313|Proteomes:UP000018406}; RN [1] {ECO:0000313|EMBL:CCY52786.1, ECO:0000313|Proteomes:UP000018406} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MGS:189 {ECO:0000313|Proteomes:UP000018406}; RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., RA Sunagawa S., Plichta D., Gautier L., Le Chatelier E., Peletier E., RA Bonde I., Nielsen T., Manichanh C., Arumugam M., Batto J., RA Santos M.B.Q.D., Blom N., Borruel N., Burgdorf K.S., Boumezbeur F., RA Casellas F., Dore J., Guarner F., Hansen T., Hildebrand F., Kaas R.S., RA Kennedy S., Kristiansen K., Kultima J.R., Leonard P., Levenez F., RA Lund O., Moumen B., Le Paslier D., Pons N., Pedersen O., Prifti E., RA Qin J., Raes J., Tap J., Tims S., Ussery D.W., Yamada T., RA MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P., Wang J., RA Brunak S., Ehrlich S.D.; RT "Dependencies among metagenomic species, viruses, plasmids and units RT of genetic variation."; RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:CCY52786.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CAYI010000294; CCY52786.1; -; Genomic_DNA. DR Proteomes; UP000018406; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000018406}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000018406}. FT DOMAIN 217 401 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 420 AA; 47832 MW; EA527645CC64C5AC CRC64; MKEFVISEAQ VETAILVGLI TQAQDERKTN EYLDELAFLA ETAGAEVVKK FTQKLPTANS VTYVGKGKLE EIKEYILNEE ENEREVGMVI FDDELSAKQI RNIEAELKVK ILDRTSLILD IFAMRAQTAN AKTQVELAQY KYMLPRLQRL WTHLERQGGG SGSGSGKGGS VGLRGPGETQ LEMDRRIILN RMSLLKERLA EIDKQKSTQR KNRGRMIRVA LVGYTNVGKS TMMNLLAKSE VFAENKLFAT LDTTVRKVII DNLPFLLSDT VGFIRKLPTD LVDSFKSTLD EVREADLLLH VVDISHPGFE EQIEVVNKTL ADIGGAGKPM ILIFNKIDAY TYVEKAADDL TPRTKENLTL EELMKTWMAK MEDNCLFISA RERINIEELK SVVYKRVKEL HVQKYPYNDF LYQTYEEEEE // ID R5JV15_9BACE Unreviewed; 418 AA. AC R5JV15; DT 24-JUL-2013, integrated into UniProtKB/TrEMBL. DT 24-JUL-2013, sequence version 1. DT 12-APR-2017, entry version 25. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=BN464_02820 {ECO:0000313|EMBL:CCY56504.1}; OS Bacteroides eggerthii CAG:109. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae; OC Bacteroides; environmental samples. OX NCBI_TaxID=1263043 {ECO:0000313|EMBL:CCY56504.1, ECO:0000313|Proteomes:UP000018152}; RN [1] {ECO:0000313|EMBL:CCY56504.1, ECO:0000313|Proteomes:UP000018152} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MGS:109 {ECO:0000313|Proteomes:UP000018152}; RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., RA Sunagawa S., Plichta D., Gautier L., Le Chatelier E., Peletier E., RA Bonde I., Nielsen T., Manichanh C., Arumugam M., Batto J., RA Santos M.B.Q.D., Blom N., Borruel N., Burgdorf K.S., Boumezbeur F., RA Casellas F., Dore J., Guarner F., Hansen T., Hildebrand F., Kaas R.S., RA Kennedy S., Kristiansen K., Kultima J.R., Leonard P., Levenez F., RA Lund O., Moumen B., Le Paslier D., Pons N., Pedersen O., Prifti E., RA Qin J., Raes J., Tap J., Tims S., Ussery D.W., Yamada T., RA MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P., Wang J., RA Brunak S., Ehrlich S.D.; RT "Dependencies among metagenomic species, viruses, plasmids and units RT of genetic variation."; RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:CCY56504.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CAYK010000103; CCY56504.1; -; Genomic_DNA. DR ProteinModelPortal; R5JV15; -. DR Proteomes; UP000018152; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000018152}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}. FT DOMAIN 216 400 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 418 AA; 47784 MW; 0D925D7EFF71648C CRC64; MKEFVISEAQ VETAVLVGLV TKTQDERKTN EYLDELEFLA ETAGAEVVKR FTQKLDQANS VTYVGKGKLE EIKEYIRNEE EAEREIGMVI FDDELSAKQI RNIEAELKIK ILDRTSLILD IFAMRAQTAN AKTQVELAQY KYMLPRLQRL WTHLERQGGG SGAGGGKGSV GLRGPGETQL EMDRRIILNR MSLLKERLAE IDKQKATQRK NRGRLIRVAL VGYTNVGKST LMTLLSKSEV FAENKLFATL DTTVRKVIIE NLPFLLSDTV GFIRKLPTDL VDSFKSTLDE VREADLLLHI VDISHPDFEE QIEVVNKTLA DIGASGKPMI LVFNKIDAYT YIAKAEDDLT PRTKENLTLE ELMKTWMAKM EDNCLFISAR ERINVEELKS VVYQRVKELH VQKYPYNDFL YQTYEEEV // ID R5JVW1_9CLOT Unreviewed; 413 AA. AC R5JVW1; DT 24-JUL-2013, integrated into UniProtKB/TrEMBL. DT 24-JUL-2013, sequence version 1. DT 12-APR-2017, entry version 23. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=BN743_01736 {ECO:0000313|EMBL:CCY58515.1}; OS Clostridium sp. CAG:632. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium; environmental samples. OX NCBI_TaxID=1262830 {ECO:0000313|EMBL:CCY58515.1, ECO:0000313|Proteomes:UP000018242}; RN [1] {ECO:0000313|EMBL:CCY58515.1, ECO:0000313|Proteomes:UP000018242} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MGS:632 {ECO:0000313|Proteomes:UP000018242}; RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., RA Sunagawa S., Plichta D., Gautier L., Le Chatelier E., Peletier E., RA Bonde I., Nielsen T., Manichanh C., Arumugam M., Batto J., RA Santos M.B.Q.D., Blom N., Borruel N., Burgdorf K.S., Boumezbeur F., RA Casellas F., Dore J., Guarner F., Hansen T., Hildebrand F., Kaas R.S., RA Kennedy S., Kristiansen K., Kultima J.R., Leonard P., Levenez F., RA Lund O., Moumen B., Le Paslier D., Pons N., Pedersen O., Prifti E., RA Qin J., Raes J., Tap J., Tims S., Ussery D.W., Yamada T., RA MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P., Wang J., RA Brunak S., Ehrlich S.D.; RT "Dependencies among metagenomic species, viruses, plasmids and units RT of genetic variation."; RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:CCY58515.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CAYL010000117; CCY58515.1; -; Genomic_DNA. DR Proteomes; UP000018242; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000018242}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000018242}. FT DOMAIN 202 366 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 161 195 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 413 AA; 46584 MW; 6E2C9592AFDBE745 CRC64; MTELYELEER AERLVLVGVA VGDEVTTQDS LTELAELVQT AGGLPVGQFI QNRAGFDIAT YIGSGKVAEL KQYLIMMDAD GIVCDDELTP SQMNNLEREL EVKILDRTMV ILDIFAARAS TREGKIQVEL AQLRYRSTHL IGMGGILSRQ GGGIGTRGPG EKQLEIDRRV IRERISRLKA DLEQVKMNRA TQRKQRLGNG IPVVCIVGYT NAGKSTLLNT LTNSEVLSED KLFATLDPTT RSLELPDGQK ILLTDTVGFI RKLPHHLIQA FRSTLEEAKY SDYILHVVDA SNPQMDIQMH TVYATLRDLE IEGRPILTAF NKTDRENVPE VLKDFRADEV YRISARTGDG LQELLQGISR MIRENRIYFE HVYPYRDAAK IARVRQSGQV IEEVYREDGI LIRAYVDKRG NYV // ID R5JZU7_9FIRM Unreviewed; 424 AA. AC R5JZU7; DT 24-JUL-2013, integrated into UniProtKB/TrEMBL. DT 24-JUL-2013, sequence version 1. DT 12-APR-2017, entry version 24. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=BN781_00967 {ECO:0000313|EMBL:CCY54471.1}; OS Coprococcus sp. CAG:782. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Lachnospiraceae; OC Coprococcus; environmental samples. OX NCBI_TaxID=1262863 {ECO:0000313|EMBL:CCY54471.1, ECO:0000313|Proteomes:UP000018002}; RN [1] {ECO:0000313|EMBL:CCY54471.1, ECO:0000313|Proteomes:UP000018002} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MGS:782 {ECO:0000313|Proteomes:UP000018002}; RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., RA Sunagawa S., Plichta D., Gautier L., Le Chatelier E., Peletier E., RA Bonde I., Nielsen T., Manichanh C., Arumugam M., Batto J., RA Santos M.B.Q.D., Blom N., Borruel N., Burgdorf K.S., Boumezbeur F., RA Casellas F., Dore J., Guarner F., Hansen T., Hildebrand F., Kaas R.S., RA Kennedy S., Kristiansen K., Kultima J.R., Leonard P., Levenez F., RA Lund O., Moumen B., Le Paslier D., Pons N., Pedersen O., Prifti E., RA Qin J., Raes J., Tap J., Tims S., Ussery D.W., Yamada T., RA MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P., Wang J., RA Brunak S., Ehrlich S.D.; RT "Dependencies among metagenomic species, viruses, plasmids and units RT of genetic variation."; RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:CCY54471.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CAYJ010000108; CCY54471.1; -; Genomic_DNA. DR Proteomes; UP000018002; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000018002}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000018002}. FT DOMAIN 203 373 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 162 196 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 424 AA; 47706 MW; F272872D638185DC CRC64; MYDNELDGKK EKVIVFAVAV GDSELQDVEA SLDEMTELLK TAGAETCGRL IQPREYPDHG LYLGKGKIEE LRELICETGA TGVCCDDELS PAQLMNLTDA LDIKVMDRTM VILDIFAAHA GSYEGKLQVE LAQLKFRATR LVGMRSSLSR LGGGIGTRGP GEKKLEIDRR VIRDRISRLK AELREVVSRR DEQRKQRSRS HIPVVSIVGY TNAGKSTLLN YVTGAGVLEE DKLFATLDPT TRNYGLKSGQ QILLTDTVGF IRKLPHHLVE AFKSTLEEAK YSDIILHVVD ASDENRDKNM ETVYDTLRQL KIDEETEKTI ITVFNKTDMI ENKDELYSIK DLISDRTVYI SAKTGWGVEE LFDVIEEILR NSKSYIRHTF PYTEAGKLGI IRKYGELITE EYLEDGIFVE AYVPKAILGQ LGLD // ID R5K0F0_9CLOT Unreviewed; 437 AA. AC R5K0F0; DT 24-JUL-2013, integrated into UniProtKB/TrEMBL. DT 24-JUL-2013, sequence version 1. DT 12-APR-2017, entry version 25. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=BN572_01388 {ECO:0000313|EMBL:CCY60195.1}; OS Clostridium sp. CAG:264. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium; environmental samples. OX NCBI_TaxID=1262786 {ECO:0000313|EMBL:CCY60195.1, ECO:0000313|Proteomes:UP000018342}; RN [1] {ECO:0000313|EMBL:CCY60195.1, ECO:0000313|Proteomes:UP000018342} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MGS:264 {ECO:0000313|Proteomes:UP000018342}; RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., RA Sunagawa S., Plichta D., Gautier L., Le Chatelier E., Peletier E., RA Bonde I., Nielsen T., Manichanh C., Arumugam M., Batto J., RA Santos M.B.Q.D., Blom N., Borruel N., Burgdorf K.S., Boumezbeur F., RA Casellas F., Dore J., Guarner F., Hansen T., Hildebrand F., Kaas R.S., RA Kennedy S., Kristiansen K., Kultima J.R., Leonard P., Levenez F., RA Lund O., Moumen B., Le Paslier D., Pons N., Pedersen O., Prifti E., RA Qin J., Raes J., Tap J., Tims S., Ussery D.W., Yamada T., RA MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P., Wang J., RA Brunak S., Ehrlich S.D.; RT "Dependencies among metagenomic species, viruses, plasmids and units RT of genetic variation."; RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:CCY60195.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CAYM010000039; CCY60195.1; -; Genomic_DNA. DR Proteomes; UP000018342; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000018342}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000018342}. FT DOMAIN 213 383 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 179 206 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 437 AA; 48895 MW; 0743B1BCAB84CC8B CRC64; MEIKSENEQK SGYEVLAETE ERVILFAAAM DGVEVSETEK SLDELEELLK TAGAQSVGRL IQSRDRAASD LYLGRGKVEE LRSMIAMYDA TGVVCDDELS PAQLMNLQDA LEIKVMDRTM VILDIFAAHA GSYEGKLQVE LAQLKFRATR LVGMRDSLSR LGGGIGTRGP GEKKLEIDRR VIRDRISKLK ADLRQVENRR TEQRKQRSRT GIPVISIVGY TNAGKSTLLN KLTDAGVLEE DKLFATLDPA TRNAELPAGQ QVLFTDTVGF IRKLPHHLVE AFKSTLEEAR YSDVILHVVD ASDPNWDDHV ATVYTTLRQL NIDEEKGRPV ITVFNKIDKL PEDADQSSIK DLRADRMVYM SARTGAGIPE LLSVIEEVLR EQKTYIRHTF SYQEAGKPGL IRKYGEMITE EYLEDGIFVE AYVPKSLIGQ IGLSDED // ID R5KCA9_9BACT Unreviewed; 416 AA. AC R5KCA9; DT 24-JUL-2013, integrated into UniProtKB/TrEMBL. DT 24-JUL-2013, sequence version 1. DT 12-APR-2017, entry version 22. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=BN467_01183 {ECO:0000313|EMBL:CCY64360.1}; OS Prevotella sp. CAG:1124. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Prevotellaceae; OC Prevotella; environmental samples. OX NCBI_TaxID=1262920 {ECO:0000313|EMBL:CCY64360.1, ECO:0000313|Proteomes:UP000017956}; RN [1] {ECO:0000313|EMBL:CCY64360.1, ECO:0000313|Proteomes:UP000017956} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MGS:1124 {ECO:0000313|Proteomes:UP000017956}; RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., RA Sunagawa S., Plichta D., Gautier L., Le Chatelier E., Peletier E., RA Bonde I., Nielsen T., Manichanh C., Arumugam M., Batto J., RA Santos M.B.Q.D., Blom N., Borruel N., Burgdorf K.S., Boumezbeur F., RA Casellas F., Dore J., Guarner F., Hansen T., Hildebrand F., Kaas R.S., RA Kennedy S., Kristiansen K., Kultima J.R., Leonard P., Levenez F., RA Lund O., Moumen B., Le Paslier D., Pons N., Pedersen O., Prifti E., RA Qin J., Raes J., Tap J., Tims S., Ussery D.W., Yamada T., RA MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P., Wang J., RA Brunak S., Ehrlich S.D.; RT "Dependencies among metagenomic species, viruses, plasmids and units RT of genetic variation."; RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:CCY64360.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CAYO010000031; CCY64360.1; -; Genomic_DNA. DR Proteomes; UP000017956; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000017956}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000017956}. FT DOMAIN 216 400 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 416 AA; 47300 MW; 24E631C951D7EA0A CRC64; MKEFVISEVK AETAVLVGLV TPDQDEAKTK EYLDELEFLA DTAGAVTVKR FTQKVPAPNQ TTYVGKGKLD EIKQYILAEE EAEREIGMVI FDDELSARQI RNIENELKVK ILDRTSLILD IFAMRAQTAS AKTQVELAQY RYMLPRLQRL WTHLERQGGG SGSGGGKGSV GLRGPGETQL EMDRRIILNR MSLLKQRLAE IDKQKSTQRK NRGRLIRVAL VGYTNVGKST LMNLMAKSEV FAENKLFATL DTTVRKVVIE NLPFLLADTV GFIRKLPTDL VDSFKSTLDE VREADLLLHV VDISHPDFEE QINVVNNTLK DLGCADKPSM IIFNKIDAYT WVDKEPDDLT PPTKENITLD ELKRTWMAKL NDNCLFISAR NKTNIDELRD VLYKQVRELH VQKYPYNDFL YPTADV // ID R5KX02_9FIRM Unreviewed; 410 AA. AC R5KX02; DT 24-JUL-2013, integrated into UniProtKB/TrEMBL. DT 24-JUL-2013, sequence version 1. DT 12-APR-2017, entry version 22. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=BN508_02193 {ECO:0000313|EMBL:CCY69614.1}; OS Eubacterium sp. CAG:161. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Eubacteriaceae; OC Eubacterium; environmental samples. OX NCBI_TaxID=1262881 {ECO:0000313|EMBL:CCY69614.1, ECO:0000313|Proteomes:UP000018318}; RN [1] {ECO:0000313|EMBL:CCY69614.1, ECO:0000313|Proteomes:UP000018318} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MGS:161 {ECO:0000313|Proteomes:UP000018318}; RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., RA Sunagawa S., Plichta D., Gautier L., Le Chatelier E., Peletier E., RA Bonde I., Nielsen T., Manichanh C., Arumugam M., Batto J., RA Santos M.B.Q.D., Blom N., Borruel N., Burgdorf K.S., Boumezbeur F., RA Casellas F., Dore J., Guarner F., Hansen T., Hildebrand F., Kaas R.S., RA Kennedy S., Kristiansen K., Kultima J.R., Leonard P., Levenez F., RA Lund O., Moumen B., Le Paslier D., Pons N., Pedersen O., Prifti E., RA Qin J., Raes J., Tap J., Tims S., Ussery D.W., Yamada T., RA MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P., Wang J., RA Brunak S., Ehrlich S.D.; RT "Dependencies among metagenomic species, viruses, plasmids and units RT of genetic variation."; RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:CCY69614.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CAYQ010000061; CCY69614.1; -; Genomic_DNA. DR Proteomes; UP000018318; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000018318}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000018318}. FT DOMAIN 198 330 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 157 191 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 410 AA; 46098 MW; 780531DF52180943 CRC64; MYETAENTEK IILVAVATGN EDDAMESLDE LEELVNTAGA LVVGRVIQNL DHINNTTYVG SGKVQEIKDL IWETEADAIV CDDELSPAQY KNLEDELDVK VMDRTLIILD IFAGRAKSAE GKIQVELAQL RYRSTRLIGM RNLSRQGGGI GTRGPGEKKL EVDRRLIRNR ISQLKEQVRN MESHRQVTRA KRQDNPVPVV AIVGYTNAGK STLLNTLTAA NVLEEDKLFA TLDPTTRNYK LPNGQEVLLT DTVGFIRKLP HHLIDAFRST LEEAKYSDII IHVVDCSNPS MDKNVHAVYE TLKNLEVKDK IIITVFNKID KVEEKPVLRD FNADYTVSAA IKKNIGLNEI NDAIEVALKS MRVMVEKVYD YSEAGKIGII RKYGQVLSEE YKEDGIHLKA YVPSQIMDRI // ID R5L1I2_9CLOT Unreviewed; 417 AA. AC R5L1I2; DT 24-JUL-2013, integrated into UniProtKB/TrEMBL. DT 24-JUL-2013, sequence version 1. DT 12-APR-2017, entry version 24. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=BN753_00626 {ECO:0000313|EMBL:CCY66917.1}; OS Clostridium sp. CAG:678. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium; environmental samples. OX NCBI_TaxID=1262831 {ECO:0000313|EMBL:CCY66917.1, ECO:0000313|Proteomes:UP000017959}; RN [1] {ECO:0000313|EMBL:CCY66917.1, ECO:0000313|Proteomes:UP000017959} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MGS:678 {ECO:0000313|Proteomes:UP000017959}; RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., RA Sunagawa S., Plichta D., Gautier L., Le Chatelier E., Peletier E., RA Bonde I., Nielsen T., Manichanh C., Arumugam M., Batto J., RA Santos M.B.Q.D., Blom N., Borruel N., Burgdorf K.S., Boumezbeur F., RA Casellas F., Dore J., Guarner F., Hansen T., Hildebrand F., Kaas R.S., RA Kennedy S., Kristiansen K., Kultima J.R., Leonard P., Levenez F., RA Lund O., Moumen B., Le Paslier D., Pons N., Pedersen O., Prifti E., RA Qin J., Raes J., Tap J., Tims S., Ussery D.W., Yamada T., RA MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P., Wang J., RA Brunak S., Ehrlich S.D.; RT "Dependencies among metagenomic species, viruses, plasmids and units RT of genetic variation."; RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:CCY66917.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CAYP010000022; CCY66917.1; -; Genomic_DNA. DR Proteomes; UP000017959; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000017959}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000017959}. FT DOMAIN 202 364 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 417 AA; 45473 MW; DA8EF66D8767F675 CRC64; MDFIETRRDA APEKAVLLSV DTGDFDADAS VNELEELAKT AGAEVLAVVV QRREAPSPST YIGSGRLAQL VAFCGSHEVD LLIADGELSP VQVRNIEDAC GVRTIDRTAL ILDIFAARAR SAEGKIQVEL AQLKYLLPRL SGQGKSLSRL GGGIGTRGPG ETKLETDRRH IRRRIEHLND SLEKIRKRRL ATHTRRQKNA VLSAVIVGYT NAGKSTLMNR LTHAGVLAED KLFATLDPTA RKLILPDGRQ IMLVDTVGLV RRLPHQLVDA FRSTLEEALW ADVILNVCDI SNPECAEHIR VTNDLLSSLG CDGKPIINVL NKCDLAPEVL DHPVIGANVR VSAITGYGIE ALLDAIAKAL PVSRKKVTLL VPFSRGEILH EIRQNGEVLS QAYTDGGIKI EAFADAAYLN KIKEYIL // ID R5L2R0_9CLOT Unreviewed; 422 AA. AC R5L2R0; DT 24-JUL-2013, integrated into UniProtKB/TrEMBL. DT 24-JUL-2013, sequence version 1. DT 12-APR-2017, entry version 24. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=BN811_01034 {ECO:0000313|EMBL:CCY71669.1}; OS Clostridium sp. CAG:921. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium; environmental samples. OX NCBI_TaxID=1262847 {ECO:0000313|EMBL:CCY71669.1, ECO:0000313|Proteomes:UP000018193}; RN [1] {ECO:0000313|EMBL:CCY71669.1, ECO:0000313|Proteomes:UP000018193} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MGS:921 {ECO:0000313|Proteomes:UP000018193}; RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., RA Sunagawa S., Plichta D., Gautier L., Le Chatelier E., Peletier E., RA Bonde I., Nielsen T., Manichanh C., Arumugam M., Batto J., RA Santos M.B.Q.D., Blom N., Borruel N., Burgdorf K.S., Boumezbeur F., RA Casellas F., Dore J., Guarner F., Hansen T., Hildebrand F., Kaas R.S., RA Kennedy S., Kristiansen K., Kultima J.R., Leonard P., Levenez F., RA Lund O., Moumen B., Le Paslier D., Pons N., Pedersen O., Prifti E., RA Qin J., Raes J., Tap J., Tims S., Ussery D.W., Yamada T., RA MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P., Wang J., RA Brunak S., Ehrlich S.D.; RT "Dependencies among metagenomic species, viruses, plasmids and units RT of genetic variation."; RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:CCY71669.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CAYR010000183; CCY71669.1; -; Genomic_DNA. DR Proteomes; UP000018193; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000018193}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000018193}. FT DOMAIN 198 366 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 157 191 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 422 AA; 48286 MW; B9A9CC39E2DDEA00 CRC64; MEIEKEKALI VAVNIKNDDN FEKSVEELFA LCEACNIEPV DKVTQNLNEI NPAFYIGTGK IDEVKKAVNM YGVDVVIFNN ELSHSQLRNL QKHIDTPILD RTSLILQIFA LRARTNEAKI QVEVAKLEYM LPRLVGLHSS LGRQGGSAGV SNKGSGEKKL ELDRRKIEEE IVRLNKELKQ IEKQREVMRK NRKKNNIPIV ALAGYTNAGK STLLNSFVVK YKTENVKKVE EKDMLFATLE TSVRNIKLED KKEFLLSDTV GFISNLPHNL IKAFRSTLEE IKQADLILEV VDYSDDNYKK HIEVTNNTLK EIGAGDIPIV YVFNKCDKVL SKIPLVEGNN IYISAKNMIG IDMLTNLIKS KIFENYTLSS FLFPFERGDI LSYFNKNARI LNVEYTENGT IIDVECKEED YMKYKGYEYF KN // ID R5LQS1_9SPIR Unreviewed; 369 AA. AC R5LQS1; DT 24-JUL-2013, integrated into UniProtKB/TrEMBL. DT 24-JUL-2013, sequence version 1. DT 12-APR-2017, entry version 24. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=BN758_01280 {ECO:0000313|EMBL:CCY75436.1}; OS Brachyspira sp. CAG:700. OC Bacteria; Spirochaetes; Brachyspirales; Brachyspiraceae; Brachyspira; OC environmental samples. OX NCBI_TaxID=1262760 {ECO:0000313|EMBL:CCY75436.1, ECO:0000313|Proteomes:UP000017901}; RN [1] {ECO:0000313|EMBL:CCY75436.1, ECO:0000313|Proteomes:UP000017901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MGS:700 {ECO:0000313|Proteomes:UP000017901}; RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., RA Sunagawa S., Plichta D., Gautier L., Le Chatelier E., Peletier E., RA Bonde I., Nielsen T., Manichanh C., Arumugam M., Batto J., RA Santos M.B.Q.D., Blom N., Borruel N., Burgdorf K.S., Boumezbeur F., RA Casellas F., Dore J., Guarner F., Hansen T., Hildebrand F., Kaas R.S., RA Kennedy S., Kristiansen K., Kultima J.R., Leonard P., Levenez F., RA Lund O., Moumen B., Le Paslier D., Pons N., Pedersen O., Prifti E., RA Qin J., Raes J., Tap J., Tims S., Ussery D.W., Yamada T., RA MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P., Wang J., RA Brunak S., Ehrlich S.D.; RT "Dependencies among metagenomic species, viruses, plasmids and units RT of genetic variation."; RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:CCY75436.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CAYT010000151; CCY75436.1; -; Genomic_DNA. DR Proteomes; UP000017901; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000017901}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000017901}. FT DOMAIN 198 365 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 159 186 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 369 AA; 42415 MW; ACCFD8263D2E8F6C CRC64; MKCKRAYIIF VADNKQNKIN KFNIENILNE LSMLCDTANY KVIERYSFIQ QKIDSRTYIG KGKLESIKEK AIIDKVKYII FDNELSGSQV NSIEENSDIK ALTRTEIILE IFAMRAKTLT AKMQVELAFL EFEYPRLKGK RTNLSQVKGI IGLRGGAGEK QLEYDRRRAR ERIHKLKTQL NKVERVSKIG RKSRENSFRI AIVGYTNAGK SSLFNLLCKE NIYVEDKLFA TLDTHTRKLY LSNDAPVQVI ISDTVGFIDR LPHTLIASFK STLSEVVEAD LLIHLIDSSD KNIEEKIIKV ENTIKEIGAS EIKSLSVFNK IDCIDEIQKN KIQILYNNPI FISAKNNINI ENLRKIILNT ILELNKVEY // ID R5LUR3_9FIRM Unreviewed; 411 AA. AC R5LUR3; DT 24-JUL-2013, integrated into UniProtKB/TrEMBL. DT 24-JUL-2013, sequence version 1. DT 10-MAY-2017, entry version 23. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=BN569_00447 {ECO:0000313|EMBL:CCY76841.1}; OS Butyrivibrio crossotus CAG:259. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Lachnospiraceae; OC Butyrivibrio; environmental samples. OX NCBI_TaxID=1263062 {ECO:0000313|EMBL:CCY76841.1, ECO:0000313|Proteomes:UP000018300}; RN [1] {ECO:0000313|EMBL:CCY76841.1, ECO:0000313|Proteomes:UP000018300} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MGS:259 {ECO:0000313|Proteomes:UP000018300}; RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., RA Sunagawa S., Plichta D., Gautier L., Le Chatelier E., Peletier E., RA Bonde I., Nielsen T., Manichanh C., Arumugam M., Batto J., RA Santos M.B.Q.D., Blom N., Borruel N., Burgdorf K.S., Boumezbeur F., RA Casellas F., Dore J., Guarner F., Hansen T., Hildebrand F., Kaas R.S., RA Kennedy S., Kristiansen K., Kultima J.R., Leonard P., Levenez F., RA Lund O., Moumen B., Le Paslier D., Pons N., Pedersen O., Prifti E., RA Qin J., Raes J., Tap J., Tims S., Ussery D.W., Yamada T., RA MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P., Wang J., RA Brunak S., Ehrlich S.D.; RT "Dependencies among metagenomic species, viruses, plasmids and units RT of genetic variation."; RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:CCY76841.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CAYU010000046; CCY76841.1; -; Genomic_DNA. DR ProteinModelPortal; R5LUR3; -. DR Proteomes; UP000018300; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000018300}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000018300}. FT DOMAIN 199 362 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 411 AA; 45423 MW; E6463A530DF6EBC2 CRC64; MIDNREAEER VILVAVRKSD RENTEQSLDE LCELASTAGA VTVARVIQNL DNFNPATYIG KGKIDEIKEL IIEYDATGII CDDELSPAQM NNLSDALEIK VMDRTLLILD IFAARANTNE GKIQVELAQL RYRSSRLSGL GNALSRLGGG IGTRGPGETK LEMDRRIIHE RIGQLKHELE AVVTHRELTR SQRSRSNIPV VAIVGYTNAG KSTLLNTLTG AGILAENKLF ATLDPTTRGL ELESGQQILL TDTVGFISKL PHHLVEAFKS TLEEAVYADI ILHVVDASNP AMDSQMYVVY DTLEKLGAGD KPIITAFNKI EIAGNKVLKD FKADKTVNIS ALHGDGLTEL KDTIEEVLRE SKIYIEKTYS YTEASKISLI RKYGQLISEE YVAEGIEVKA YVPTEIYDKV K // ID R5M1Y6_9BACE Unreviewed; 419 AA. AC R5M1Y6; DT 24-JUL-2013, integrated into UniProtKB/TrEMBL. DT 24-JUL-2013, sequence version 1. DT 12-APR-2017, entry version 24. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=BN711_00286 {ECO:0000313|EMBL:CCY85503.1}; OS Bacteroides intestinalis CAG:564. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae; OC Bacteroides; environmental samples. OX NCBI_TaxID=1263049 {ECO:0000313|EMBL:CCY85503.1, ECO:0000313|Proteomes:UP000018157}; RN [1] {ECO:0000313|EMBL:CCY85503.1, ECO:0000313|Proteomes:UP000018157} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MGS:564 {ECO:0000313|Proteomes:UP000018157}; RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., RA Sunagawa S., Plichta D., Gautier L., Le Chatelier E., Peletier E., RA Bonde I., Nielsen T., Manichanh C., Arumugam M., Batto J., RA Santos M.B.Q.D., Blom N., Borruel N., Burgdorf K.S., Boumezbeur F., RA Casellas F., Dore J., Guarner F., Hansen T., Hildebrand F., Kaas R.S., RA Kennedy S., Kristiansen K., Kultima J.R., Leonard P., Levenez F., RA Lund O., Moumen B., Le Paslier D., Pons N., Pedersen O., Prifti E., RA Qin J., Raes J., Tap J., Tims S., Ussery D.W., Yamada T., RA MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P., Wang J., RA Brunak S., Ehrlich S.D.; RT "Dependencies among metagenomic species, viruses, plasmids and units RT of genetic variation."; RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:CCY85503.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CAYY010000168; CCY85503.1; -; Genomic_DNA. DR ProteinModelPortal; R5M1Y6; -. DR Proteomes; UP000018157; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000018157}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000018157}. FT DOMAIN 216 400 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 419 AA; 47841 MW; E635A644311E7FCE CRC64; MKEFVISEVQ AETAVLVGLI TKMQDERKTN EYLDELEFLA ETAGAEVVKR FTQKLDQAHS VTYVGKGKLE EIKEYIRSEE EAEREIGMVI FDDELSAKQI RNIEAELKIK ILDRTSLILD IFAMRAQTAN AKTQVELAQY KYMLPRLQRL WTHLERQGGG SGAGGGKGSV GLRGPGETQL EMDRRIILNR MSLLKERLAE IDKQKATQRK NRGRMIRAAL VGYTNVGKST LMNLLAKSEV FAENKLFATL DTTVRKVIID NLPFLLSDTV GFIRKLPTDL VDSFKSTLDE VREADLLLHI VDISHPDFEE QIEVVNKTLA DIGASGKPMI LVFNKIDAYT YVEKAADDLT PRTKENLTLE ELMKTWMAKM EDNCLFISAR EKINLEELKS VVYARVKELH VQKYPYNDFL YQTYEEEEV // ID R5ML26_9FIRM Unreviewed; 417 AA. AC R5ML26; DT 24-JUL-2013, integrated into UniProtKB/TrEMBL. DT 24-JUL-2013, sequence version 1. DT 12-APR-2017, entry version 23. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=BN519_01503 {ECO:0000313|EMBL:CCY92455.1}; OS Eubacterium sp. CAG:180. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Eubacteriaceae; OC Eubacterium; environmental samples. OX NCBI_TaxID=1262882 {ECO:0000313|EMBL:CCY92455.1, ECO:0000313|Proteomes:UP000018411}; RN [1] {ECO:0000313|EMBL:CCY92455.1, ECO:0000313|Proteomes:UP000018411} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MGS:180 {ECO:0000313|Proteomes:UP000018411}; RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., RA Sunagawa S., Plichta D., Gautier L., Le Chatelier E., Peletier E., RA Bonde I., Nielsen T., Manichanh C., Arumugam M., Batto J., RA Santos M.B.Q.D., Blom N., Borruel N., Burgdorf K.S., Boumezbeur F., RA Casellas F., Dore J., Guarner F., Hansen T., Hildebrand F., Kaas R.S., RA Kennedy S., Kristiansen K., Kultima J.R., Leonard P., Levenez F., RA Lund O., Moumen B., Le Paslier D., Pons N., Pedersen O., Prifti E., RA Qin J., Raes J., Tap J., Tims S., Ussery D.W., Yamada T., RA MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P., Wang J., RA Brunak S., Ehrlich S.D.; RT "Dependencies among metagenomic species, viruses, plasmids and units RT of genetic variation."; RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:CCY92455.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CAZC010000064; CCY92455.1; -; Genomic_DNA. DR Proteomes; UP000018411; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000018411}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000018411}. FT DOMAIN 200 362 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 166 193 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 417 AA; 45955 MW; 08738EA6A00CDFA3 CRC64; MEFYENSQSP ERALLIGVDT GEYNAEISME ELALLSETAG AEIIGTVIQK LEAPSPATYI GSGRMAEVAA FCRNNDIDLI IADSELTPSQ INNIETKTDT RVVDRTMLIL DIFAARARSS EGKLQVELAQ LKYSLPFLSG RGKSMSRLGG GIGTRGPGES KLESDKRHIR RRIHSLSEEL KRVEKRRDLI RSRRKKDGVI TVAIVGYTNA GKSTLMNTLT SAGVLSEDKL FATLDPTARR LTLPSKREVM LVDTVGLVRR LPHQLVDAFK STLEEAKNAD LILNVCDASS DECAEHLSVT SSVLKELGAD NIPVISVMNK CDKLQNAYDM PVIGKTVMIS AVKNEGIDRL LEVIEDSLPK TKARAILLVP FSEGHILGEI RKTGVVYSES YKENGTRLDA LVDIDYLEKI KRYIVSM // ID R5NFB2_9BACT Unreviewed; 419 AA. AC R5NFB2; DT 24-JUL-2013, integrated into UniProtKB/TrEMBL. DT 24-JUL-2013, sequence version 1. DT 12-APR-2017, entry version 23. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=BN471_02182 {ECO:0000313|EMBL:CCZ00749.1}; OS Paraprevotella clara CAG:116. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Prevotellaceae; OC Paraprevotella; environmental samples. OX NCBI_TaxID=1263095 {ECO:0000313|EMBL:CCZ00749.1, ECO:0000313|Proteomes:UP000017958}; RN [1] {ECO:0000313|EMBL:CCZ00749.1, ECO:0000313|Proteomes:UP000017958} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MGS:116 {ECO:0000313|Proteomes:UP000017958}; RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., RA Sunagawa S., Plichta D., Gautier L., Le Chatelier E., Peletier E., RA Bonde I., Nielsen T., Manichanh C., Arumugam M., Batto J., RA Santos M.B.Q.D., Blom N., Borruel N., Burgdorf K.S., Boumezbeur F., RA Casellas F., Dore J., Guarner F., Hansen T., Hildebrand F., Kaas R.S., RA Kennedy S., Kristiansen K., Kultima J.R., Leonard P., Levenez F., RA Lund O., Moumen B., Le Paslier D., Pons N., Pedersen O., Prifti E., RA Qin J., Raes J., Tap J., Tims S., Ussery D.W., Yamada T., RA MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P., Wang J., RA Brunak S., Ehrlich S.D.; RT "Dependencies among metagenomic species, viruses, plasmids and units RT of genetic variation."; RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:CCZ00749.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CAZH010000025; CCZ00749.1; -; Genomic_DNA. DR Proteomes; UP000017958; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000017958}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000017958}. FT DOMAIN 216 400 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 419 AA; 47796 MW; 98596EA6F4C44008 CRC64; MKEFVISDAQ AETAVLVGLI TQTQNERKTN EYLDELEFLA HTAGAVTVKR FTQKVNGPNS VTYVGKGKLE EIRAYIEAEE EAEREIGMVI FDDELSAKQL RNIEKELKVK ILDRTSLILD IFAMRAQTAN AKTQVELAQY RYMLPRLQRL WTHLERQGGG SGSGGGKGSV GLRGPGETQL EMDRRIILNR MSLLKQRLAE IDRQKTTQRS NRGRMIRVAL VGYTNVGKST LMNLLSKSDV FAENKLFATL DTTVRKVIID NLPFLLSDTV GFIRKLPTDL VDSFKSTLDE VREADLLLHV VDIAHPDFED QIQVVEKTLG DLGCSDKPCM IVFNKIDAYD WVEKEEDDLT PATKENVSLD DLMKTWMARR NDNCIFISAR EKTNLEELKK VLYDKVRELH VQKYPYNDFL FEKYDEEGA // ID R5NN62_9FIRM Unreviewed; 411 AA. AC R5NN62; DT 24-JUL-2013, integrated into UniProtKB/TrEMBL. DT 24-JUL-2013, sequence version 1. DT 12-APR-2017, entry version 23. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=BN514_00647 {ECO:0000313|EMBL:CCY98806.1}; OS Ruminococcus sp. CAG:17. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Ruminococcaceae; OC Ruminococcus; environmental samples. OX NCBI_TaxID=1262951 {ECO:0000313|EMBL:CCY98806.1, ECO:0000313|Proteomes:UP000018033}; RN [1] {ECO:0000313|EMBL:CCY98806.1, ECO:0000313|Proteomes:UP000018033} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MGS:17 {ECO:0000313|Proteomes:UP000018033}; RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., RA Sunagawa S., Plichta D., Gautier L., Le Chatelier E., Peletier E., RA Bonde I., Nielsen T., Manichanh C., Arumugam M., Batto J., RA Santos M.B.Q.D., Blom N., Borruel N., Burgdorf K.S., Boumezbeur F., RA Casellas F., Dore J., Guarner F., Hansen T., Hildebrand F., Kaas R.S., RA Kennedy S., Kristiansen K., Kultima J.R., Leonard P., Levenez F., RA Lund O., Moumen B., Le Paslier D., Pons N., Pedersen O., Prifti E., RA Qin J., Raes J., Tap J., Tims S., Ussery D.W., Yamada T., RA MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P., Wang J., RA Brunak S., Ehrlich S.D.; RT "Dependencies among metagenomic species, viruses, plasmids and units RT of genetic variation."; RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:CCY98806.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CAZF010000211; CCY98806.1; -; Genomic_DNA. DR Proteomes; UP000018033; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000018033}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000018033}. FT DOMAIN 199 362 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 158 192 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 411 AA; 45805 MW; 1C34B1FB85374A63 CRC64; MEYFEEIQDR VILIGVQANL GDDMEESLDE LGELAATAGA YVAGRIIQNR EAIHPGTYIG KGKIEEVKGL LYALNANGVI CDDELSPAQM NNLERELECK VMDRTLLILD IFAKRAVTSE GKIQVELAQL RYRSARLVGL RSSLSRLGGG IGTRGPGEKK LETDRRLIRN RISALKQELS QVEKHRELLR SRRAAGNLKT AAIVGYTNAG KSTLLNTLTG ASVLSEDKLF ATLDPTTRLL TLDDGQQLLL TDTVGFIRKL PHNLVEAFKS TLEEAKYADY IIHVVDESNP QAEMQMHIVY ETLKELGALG KKTITLFNKQ DRVSGESLRD LRADHTLKIS ARTGEGLEEF KELLSEILAE GQIYMERLFP YSEAGQIQLI REYGQLLSEE YTEGGIAVKA RVPREIYPKV T // ID R5NSU7_9FIRM Unreviewed; 422 AA. AC R5NSU7; DT 24-JUL-2013, integrated into UniProtKB/TrEMBL. DT 24-JUL-2013, sequence version 1. DT 12-APR-2017, entry version 24. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=BN730_01843 {ECO:0000313|EMBL:CCZ05209.1}; OS Eubacterium sp. CAG:603. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Eubacteriaceae; OC Eubacterium; environmental samples. OX NCBI_TaxID=1262891 {ECO:0000313|EMBL:CCZ05209.1, ECO:0000313|Proteomes:UP000018312}; RN [1] {ECO:0000313|EMBL:CCZ05209.1, ECO:0000313|Proteomes:UP000018312} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MGS:603 {ECO:0000313|Proteomes:UP000018312}; RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., RA Sunagawa S., Plichta D., Gautier L., Le Chatelier E., Peletier E., RA Bonde I., Nielsen T., Manichanh C., Arumugam M., Batto J., RA Santos M.B.Q.D., Blom N., Borruel N., Burgdorf K.S., Boumezbeur F., RA Casellas F., Dore J., Guarner F., Hansen T., Hildebrand F., Kaas R.S., RA Kennedy S., Kristiansen K., Kultima J.R., Leonard P., Levenez F., RA Lund O., Moumen B., Le Paslier D., Pons N., Pedersen O., Prifti E., RA Qin J., Raes J., Tap J., Tims S., Ussery D.W., Yamada T., RA MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P., Wang J., RA Brunak S., Ehrlich S.D.; RT "Dependencies among metagenomic species, viruses, plasmids and units RT of genetic variation."; RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:CCZ05209.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CAZI010000100; CCZ05209.1; -; Genomic_DNA. DR Proteomes; UP000018312; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000018312}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000018312}. FT DOMAIN 202 375 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 422 AA; 47364 MW; A4727C8311980D1A CRC64; MEKLYETQEE TEKVILIGVS TSDGDDTEES LMELKELVKT AGAATVATVI QNREAIHAGT YIGKGKIEEV KVLIDELGAT GVVCDDELSP AQLMNLRDAL DTKVMDRTLI ILDIFASRAK TGEGKVQVEL AQLKYRQARL VGLRSSLSRL GGGIGTRGPG EKKLEMDRRL IKDRIAVLRH EVEEMKVHRE LARNQRSKNP TTVISIVGYT NAGKSTLLNE LTGAGVLEEN KLFATLDPTT RRYKLESGQE IMLTDTVGFI RKLPHHLIDA FRSTLEEAKY ADILIHVVDA SNPQMDAQMH IVYETLDSLG VTDKSIITIF NKQDKVAEQI KSNGEAEMPV FKDFRADYTL NASIKNHTGL DKLLEYIEEI LRNKKIYIAK TFGYKEAGQI QKIRKYGELL KEEYRDDGIY VEAYVPVELM PM // ID R5NX72_9CLOT Unreviewed; 411 AA. AC R5NX72; DT 24-JUL-2013, integrated into UniProtKB/TrEMBL. DT 24-JUL-2013, sequence version 1. DT 10-MAY-2017, entry version 23. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=BN482_01494 {ECO:0000313|EMBL:CCZ08810.1}; OS Clostridium sp. CAG:127. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium; environmental samples. OX NCBI_TaxID=1262774 {ECO:0000313|EMBL:CCZ08810.1, ECO:0000313|Proteomes:UP000018025}; RN [1] {ECO:0000313|EMBL:CCZ08810.1, ECO:0000313|Proteomes:UP000018025} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MGS:127 {ECO:0000313|Proteomes:UP000018025}; RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., RA Sunagawa S., Plichta D., Gautier L., Le Chatelier E., Peletier E., RA Bonde I., Nielsen T., Manichanh C., Arumugam M., Batto J., RA Santos M.B.Q.D., Blom N., Borruel N., Burgdorf K.S., Boumezbeur F., RA Casellas F., Dore J., Guarner F., Hansen T., Hildebrand F., Kaas R.S., RA Kennedy S., Kristiansen K., Kultima J.R., Leonard P., Levenez F., RA Lund O., Moumen B., Le Paslier D., Pons N., Pedersen O., Prifti E., RA Qin J., Raes J., Tap J., Tims S., Ussery D.W., Yamada T., RA MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P., Wang J., RA Brunak S., Ehrlich S.D.; RT "Dependencies among metagenomic species, viruses, plasmids and units RT of genetic variation."; RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:CCZ08810.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CAZJ010000104; CCZ08810.1; -; Genomic_DNA. DR Proteomes; UP000018025; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000018025}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000018025}. FT DOMAIN 199 363 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 411 AA; 46208 MW; C72489FDD5AAF959 CRC64; MYENKEEIEK VILFAVDLDN GEQVPANLDE LEELVATAGA ETLGRMIQNK DSIEKATYLG TGKVEDLRDM VERLGATGVV CDDELSPIQM KNLEQELDTK VMDRTMIILD IFAKHATTRE GKLQVELAQL KYRSNRLIGM GQVMSRLGGG IGTRGPGEKK LEVDRRLIRE RISKLSADLK DDIAHREVMR KQRLNSHIPI VSIVGYTNAG KSTLLNHMTQ AGVLEEDKLF ATLDPTSRNY KLPNGQEIIL TDTVGFIRKL PHHLIDAFRS TLEEAKFADI ILHVVDISNP QADLHILTVY DTLRELGVKD KPVVTLFNKI DKVDELPAVK DFQADHTLYI SAKQETGFEK ITDILAEIIN QSRIYIEQTI PYAKAGVIQQ IRKSGNLLEE EYREDGIFVR AYVDAGTKGL L // ID R5P071_9BACT Unreviewed; 416 AA. AC R5P071; DT 24-JUL-2013, integrated into UniProtKB/TrEMBL. DT 24-JUL-2013, sequence version 1. DT 12-APR-2017, entry version 24. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=BN783_02948 {ECO:0000313|EMBL:CCZ07714.1}; OS Odoribacter sp. CAG:788. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Odoribacteraceae; OC Odoribacter; environmental samples. OX NCBI_TaxID=1262909 {ECO:0000313|EMBL:CCZ07714.1, ECO:0000313|Proteomes:UP000018100}; RN [1] {ECO:0000313|EMBL:CCZ07714.1, ECO:0000313|Proteomes:UP000018100} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MGS:788 {ECO:0000313|Proteomes:UP000018100}; RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., RA Sunagawa S., Plichta D., Gautier L., Le Chatelier E., Peletier E., RA Bonde I., Nielsen T., Manichanh C., Arumugam M., Batto J., RA Santos M.B.Q.D., Blom N., Borruel N., Burgdorf K.S., Boumezbeur F., RA Casellas F., Dore J., Guarner F., Hansen T., Hildebrand F., Kaas R.S., RA Kennedy S., Kristiansen K., Kultima J.R., Leonard P., Levenez F., RA Lund O., Moumen B., Le Paslier D., Pons N., Pedersen O., Prifti E., RA Qin J., Raes J., Tap J., Tims S., Ussery D.W., Yamada T., RA MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P., Wang J., RA Brunak S., Ehrlich S.D.; RT "Dependencies among metagenomic species, viruses, plasmids and units RT of genetic variation."; RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:CCZ07714.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CAZK010000033; CCZ07714.1; -; Genomic_DNA. DR Proteomes; UP000018100; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000018100}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000018100}. FT DOMAIN 205 389 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 416 AA; 47789 MW; 5544504B1A126F9B CRC64; MSEYFYTEKE AERAILVGVS LQDAGISYER MNEYLDELAF LAETAGAQTV KIFTQNLDKP VNSTFIGKGK LDEIRQYIEE HGAELVIFDD ELSPTQLRNI ENELKGVKIL DRTNLILDIF ANRARTAHAK TQVELAQYQY LLPRLTGMWT HLERQKGGIG LRGPGETEIE TDRRVIRDKI TRLKEQLCRI DKQMSTQRKN RGKLVRVALV GYTNVGKSTL MNLLSKSEVF AENKLFATLD TTVRKITIRN VPLLLADTVG FIRKLPTHLI ESFKSTLDEV READVILHVV DISHPQFEDQ LKVVNETLAE LIPDPKPTII VFNKIDAFTY IKKDEDDLTP VERANYSLED LKQMWMSKQG RETVYISAAQ KENIEELKDK LYSIVKDIHS ARFPYNEFLY TEYTDETTTG KENPSM // ID R5PP57_9BACT Unreviewed; 419 AA. AC R5PP57; DT 24-JUL-2013, integrated into UniProtKB/TrEMBL. DT 24-JUL-2013, sequence version 1. DT 12-APR-2017, entry version 22. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=BN679_00371 {ECO:0000313|EMBL:CCZ15834.1}; OS Prevotella sp. CAG:487. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Prevotellaceae; OC Prevotella; environmental samples. OX NCBI_TaxID=1262928 {ECO:0000313|EMBL:CCZ15834.1, ECO:0000313|Proteomes:UP000018275}; RN [1] {ECO:0000313|EMBL:CCZ15834.1, ECO:0000313|Proteomes:UP000018275} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MGS:487 {ECO:0000313|Proteomes:UP000018275}; RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., RA Sunagawa S., Plichta D., Gautier L., Le Chatelier E., Peletier E., RA Bonde I., Nielsen T., Manichanh C., Arumugam M., Batto J., RA Santos M.B.Q.D., Blom N., Borruel N., Burgdorf K.S., Boumezbeur F., RA Casellas F., Dore J., Guarner F., Hansen T., Hildebrand F., Kaas R.S., RA Kennedy S., Kristiansen K., Kultima J.R., Leonard P., Levenez F., RA Lund O., Moumen B., Le Paslier D., Pons N., Pedersen O., Prifti E., RA Qin J., Raes J., Tap J., Tims S., Ussery D.W., Yamada T., RA MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P., Wang J., RA Brunak S., Ehrlich S.D.; RT "Dependencies among metagenomic species, viruses, plasmids and units RT of genetic variation."; RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:CCZ15834.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CAZM010000408; CCZ15834.1; -; Genomic_DNA. DR Proteomes; UP000018275; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000018275}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000018275}. FT DOMAIN 216 400 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 419 AA; 47967 MW; 981075EA055B032E CRC64; MKEFVLSEVK TETAVLVGLI TKDQDEDKTK EYLDELEFLA DTAGAVTVKR FTQRVNGPSS VTYVGSGKLE EIKQYIKDEE DAERPVGMAI FDDELSAKQI RNIEKELGVK ILDRTSLILD IFAMRAQTAA AKTQVELAQY RYMLPRLQRL WTHLERQGGG SGSGGGKGSV GLRGPGETQL EMDRRIILQR ITLLKQRLAE IDRQKTTQRK NRGRMIRVAL VGYTNVGKST IMNLMSKSEV FAENKLFATL DTTVRKVVIE NLPFLLADTV GFIRKLPTDL VDSFKSTLDE VREADLLLHV VDISHPDFEE QINVVENTLK DLGCADKPSM IVFNKIDNYT WVDKDDDDLT PPTKENVTLD ELKRTWMARL NENCIFISAR KKQNIDEFRD VLYKKVRELH VQKYPYNDFL YNIEEPYED // ID R5PPP3_9BACT Unreviewed; 414 AA. AC R5PPP3; DT 24-JUL-2013, integrated into UniProtKB/TrEMBL. DT 24-JUL-2013, sequence version 1. DT 12-APR-2017, entry version 23. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=BN465_01198 {ECO:0000313|EMBL:CCZ11886.1}; OS Prevotella sp. CAG:1092. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Prevotellaceae; OC Prevotella; environmental samples. OX NCBI_TaxID=1262919 {ECO:0000313|EMBL:CCZ11886.1, ECO:0000313|Proteomes:UP000017987}; RN [1] {ECO:0000313|EMBL:CCZ11886.1, ECO:0000313|Proteomes:UP000017987} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MGS:1092 {ECO:0000313|Proteomes:UP000017987}; RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., RA Sunagawa S., Plichta D., Gautier L., Le Chatelier E., Peletier E., RA Bonde I., Nielsen T., Manichanh C., Arumugam M., Batto J., RA Santos M.B.Q.D., Blom N., Borruel N., Burgdorf K.S., Boumezbeur F., RA Casellas F., Dore J., Guarner F., Hansen T., Hildebrand F., Kaas R.S., RA Kennedy S., Kristiansen K., Kultima J.R., Leonard P., Levenez F., RA Lund O., Moumen B., Le Paslier D., Pons N., Pedersen O., Prifti E., RA Qin J., Raes J., Tap J., Tims S., Ussery D.W., Yamada T., RA MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P., Wang J., RA Brunak S., Ehrlich S.D.; RT "Dependencies among metagenomic species, viruses, plasmids and units RT of genetic variation."; RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:CCZ11886.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CAZL010000209; CCZ11886.1; -; Genomic_DNA. DR Proteomes; UP000017987; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000017987}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000017987}. FT DOMAIN 216 400 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 414 AA; 47259 MW; C269D5A11DFB9CF3 CRC64; MKEFVISEAK AETAVLVGLI TKEQDEAKTK EYLDELEFLA DTAGAVTVKR FTQRVTGPSQ VTYVGKGKLE EIKQYIKDEE DNEREIGMVI FDDELSAKQI RNIEAELGVK ILDRTSLILD IFAMRAQTAN AKTQVELAQY RYMLPRLQRL WTHLERQGGG SGSGGGKGSV GLRGPGETQL EMDRRIILQR ITLLKQRLVE IEKQTATQRK NRGRMIRVAL VGYTNVGKST IMNLLAKSEV FAENKLFATL DTTVRKVVVD NLPFLLADTV GFIRKLPTDL VESFKSTLDE VREADLLFHV VDISHPDFEE QINVVDNTLK ELGCADKPKV MVFNKIDNYT WTEKEPDDLT PATKENITLD ELEKTWMAKL NDNCIFISAR EKMNVEELRN TLYTRVRELH VQKYPYNDFL YPID // ID R5PWX1_9FIRM Unreviewed; 422 AA. AC R5PWX1; DT 24-JUL-2013, integrated into UniProtKB/TrEMBL. DT 24-JUL-2013, sequence version 1. DT 12-APR-2017, entry version 23. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=BN766_00441 {ECO:0000313|EMBL:CCZ21025.1}; OS Ruminococcus sp. CAG:724. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Ruminococcaceae; OC Ruminococcus; environmental samples. OX NCBI_TaxID=1262966 {ECO:0000313|EMBL:CCZ21025.1, ECO:0000313|Proteomes:UP000018243}; RN [1] {ECO:0000313|EMBL:CCZ21025.1, ECO:0000313|Proteomes:UP000018243} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MGS:724 {ECO:0000313|Proteomes:UP000018243}; RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., RA Sunagawa S., Plichta D., Gautier L., Le Chatelier E., Peletier E., RA Bonde I., Nielsen T., Manichanh C., Arumugam M., Batto J., RA Santos M.B.Q.D., Blom N., Borruel N., Burgdorf K.S., Boumezbeur F., RA Casellas F., Dore J., Guarner F., Hansen T., Hildebrand F., Kaas R.S., RA Kennedy S., Kristiansen K., Kultima J.R., Leonard P., Levenez F., RA Lund O., Moumen B., Le Paslier D., Pons N., Pedersen O., Prifti E., RA Qin J., Raes J., Tap J., Tims S., Ussery D.W., Yamada T., RA MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P., Wang J., RA Brunak S., Ehrlich S.D.; RT "Dependencies among metagenomic species, viruses, plasmids and units RT of genetic variation."; RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:CCZ21025.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CAZP010000188; CCZ21025.1; -; Genomic_DNA. DR Proteomes; UP000018243; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000018243}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000018243}. FT DOMAIN 206 368 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 165 199 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 422 AA; 46439 MW; 3400FFC08B29F714 CRC64; MTENISIKEE KKSKAVLVSL VTRDMNENEA EISLSELERL CETAGVEVFA RMMQNKESPD PRTYIGKGKV GELSELCKNN EVDTVVFDCE LSPSQIRNLE DDIGDVNVID RSMLILDIFA LHAVTGEGKL QVELAQLKYT VPRLVGKGLE LSRLGGGVGT RGPGESKLET DRRHVKRRMD MLEAQIAEMA KNREVQRAQR DRSGIFKFAI AGYTNAGKST LLNRLTDAGI LSEDKLFATL DPTTRKFTLP SGEEVLMTDT VGFIRNLPHH LIKAFRSTFE EVCHADAIVI LADASDPEAD SQLAVTEKLI EELGAGDKPI IYVYNKCDKG IACHHAAPTE NSVYISALTG DGVRELTEKL ESVAMGGKRL CAFEIPNDKL GLINSLYTNA AVQNVEYGES FATVTAIADG KARGMFEKYM KD // ID R5Q4Q1_9PROT Unreviewed; 435 AA. AC R5Q4Q1; DT 24-JUL-2013, integrated into UniProtKB/TrEMBL. DT 24-JUL-2013, sequence version 1. DT 12-APR-2017, entry version 23. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=BN820_00120 {ECO:0000313|EMBL:CCZ21309.1}; OS Acetobacter sp. CAG:977. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales; OC Acetobacteraceae; Acetobacter; environmental samples. OX NCBI_TaxID=1262685 {ECO:0000313|EMBL:CCZ21309.1, ECO:0000313|Proteomes:UP000018259}; RN [1] {ECO:0000313|EMBL:CCZ21309.1, ECO:0000313|Proteomes:UP000018259} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MGS:977 {ECO:0000313|Proteomes:UP000018259}; RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., RA Sunagawa S., Plichta D., Gautier L., Le Chatelier E., Peletier E., RA Bonde I., Nielsen T., Manichanh C., Arumugam M., Batto J., RA Santos M.B.Q.D., Blom N., Borruel N., Burgdorf K.S., Boumezbeur F., RA Casellas F., Dore J., Guarner F., Hansen T., Hildebrand F., Kaas R.S., RA Kennedy S., Kristiansen K., Kultima J.R., Leonard P., Levenez F., RA Lund O., Moumen B., Le Paslier D., Pons N., Pedersen O., Prifti E., RA Qin J., Raes J., Tap J., Tims S., Ussery D.W., Yamada T., RA MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P., Wang J., RA Brunak S., Ehrlich S.D.; RT "Dependencies among metagenomic species, viruses, plasmids and units RT of genetic variation."; RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:CCZ21309.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CAZQ010000010; CCZ21309.1; -; Genomic_DNA. DR Proteomes; UP000018259; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000018259}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000018259}. FT DOMAIN 198 369 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 164 191 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 435 AA; 48292 MW; 6DF0F7C3D70E3E11 CRC64; MSERTFIFCP VLKNETAGAR SVDARVEEAL NLAAAIDLDV FAAEPVYMET VRPSTFIGKG AVERIGEALK NNEASLVIAD CALSPVQQRN LEKAWQCKVI DRTALILEIF GERARTKEGV LQVELAHLNY QKSRLVRSWT HLERQKGGRG FLGGPGETQI ELDRRVITET IVKLKKELEE VKRTRHIHRR ARQRVPYPVV ALVGYTNAGK STLFNRLTNA GVFAKDQLFA TLDPTMRLIK LPSGRKIILS DTVGFVSNLP TELVAAFRAT LEEVLEASLI VHVRDSAHAD SAAQKQDVEN VLRELGLGAK IEQGLLEAMN KIDLLDEQER SALMNVASRK SLVIPVSALT GQGVENLLQA VEDALSAGRR EVELSLPVSD GAALAYLYRN AEVLKRADDD ECCRLTVRMD DAELARLQSH YPEVSHENPR FKPCQ // ID R5Q7I0_9BURK Unreviewed; 360 AA. AC R5Q7I0; DT 24-JUL-2013, integrated into UniProtKB/TrEMBL. DT 24-JUL-2013, sequence version 1. DT 12-APR-2017, entry version 23. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=BN489_01552 {ECO:0000313|EMBL:CCZ17027.1}; OS Sutterella wadsworthensis CAG:135. OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Sutterellaceae; Sutterella; environmental samples. OX NCBI_TaxID=1263111 {ECO:0000313|EMBL:CCZ17027.1, ECO:0000313|Proteomes:UP000018089}; RN [1] {ECO:0000313|EMBL:CCZ17027.1, ECO:0000313|Proteomes:UP000018089} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MGS:135 {ECO:0000313|Proteomes:UP000018089}; RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., RA Sunagawa S., Plichta D., Gautier L., Le Chatelier E., Peletier E., RA Bonde I., Nielsen T., Manichanh C., Arumugam M., Batto J., RA Santos M.B.Q.D., Blom N., Borruel N., Burgdorf K.S., Boumezbeur F., RA Casellas F., Dore J., Guarner F., Hansen T., Hildebrand F., Kaas R.S., RA Kennedy S., Kristiansen K., Kultima J.R., Leonard P., Levenez F., RA Lund O., Moumen B., Le Paslier D., Pons N., Pedersen O., Prifti E., RA Qin J., Raes J., Tap J., Tims S., Ussery D.W., Yamada T., RA MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P., Wang J., RA Brunak S., Ehrlich S.D.; RT "Dependencies among metagenomic species, viruses, plasmids and units RT of genetic variation."; RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:CCZ17027.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CAZN010000211; CCZ17027.1; -; Genomic_DNA. DR ProteinModelPortal; R5Q7I0; -. DR Proteomes; UP000018089; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000018089}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000018089}. FT DOMAIN 155 321 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 121 148 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 360 AA; 40375 MW; 6190BFF5D36CBDAC CRC64; MQAKREKPDP ATFLGSGKIE ELGILAKEAE VDVVVFDIAL SAAQERNIER LIGIPVLDRT ELILDIFRQR AKSREGRLQV ELARLEHLST RLVRGWTHLE RQRGGLGKTG GPGEKQIELD RRMIGTRMKQ LRDQLKRLAR QRGTQRRARS RGDSITVSLA GYTNAGKSTL FNKITRAETY AADQLFATLD TTARKFWLSD EETVVATDTV GFIRGLPHQL IEAFKSTLDE TVHADLILHV VDASSPVREE QIAEVNSVLA DIHADDVPVI LVYNKIDVTG QAPEIVRDQN GRPKAVFVSA LTGAGLDELR QAVSEFSAAW REEHPNEPRE LEDWELERTD EALPRRKTPA EELAELESLL // ID R5QG01_9FIRM Unreviewed; 416 AA. AC R5QG01; DT 24-JUL-2013, integrated into UniProtKB/TrEMBL. DT 24-JUL-2013, sequence version 1. DT 10-MAY-2017, entry version 25. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=BN526_02273 {ECO:0000313|EMBL:CCZ27620.1}; OS Firmicutes bacterium CAG:194. OC Bacteria; Firmicutes; environmental samples. OX NCBI_TaxID=1263008 {ECO:0000313|EMBL:CCZ27620.1, ECO:0000313|Proteomes:UP000018384}; RN [1] {ECO:0000313|EMBL:CCZ27620.1, ECO:0000313|Proteomes:UP000018384} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MGS:194 {ECO:0000313|Proteomes:UP000018384}; RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., RA Sunagawa S., Plichta D., Gautier L., Le Chatelier E., Peletier E., RA Bonde I., Nielsen T., Manichanh C., Arumugam M., Batto J., RA Santos M.B.Q.D., Blom N., Borruel N., Burgdorf K.S., Boumezbeur F., RA Casellas F., Dore J., Guarner F., Hansen T., Hildebrand F., Kaas R.S., RA Kennedy S., Kristiansen K., Kultima J.R., Leonard P., Levenez F., RA Lund O., Moumen B., Le Paslier D., Pons N., Pedersen O., Prifti E., RA Qin J., Raes J., Tap J., Tims S., Ussery D.W., Yamada T., RA MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P., Wang J., RA Brunak S., Ehrlich S.D.; RT "Dependencies among metagenomic species, viruses, plasmids and units RT of genetic variation."; RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:CCZ27620.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CAZT010000009; CCZ27620.1; -; Genomic_DNA. DR Proteomes; UP000018384; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000018384}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000018384}. FT DOMAIN 194 363 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 153 187 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 416 AA; 46425 MW; 1643F4C58CFD6104 CRC64; MDKVYLVGVD TQNDRQFERS MAELAELANA CEMEVVGNCV QHTQINKAIY VGPGKLEQIR EEAEELQADL LLFNDSLTPS QLRNIQDDTG MAVMDRTTLI LEIFASRAKS REAMLQVEVA RLQYLLPRLV GLHEALSRQG GTSGSMSSRG SGEKKLELDR RRAQSRLTEL SRELAEMETE RRTQQKKRAR SAIPRVALVG YTNAGKSTIM NSMVMRYLGD AEKTVMEKDM LFATLDTTVR SITPKENKTV LLSDTVGFID KLPHGLVKAF RSTLSEAASA DLLLHVVDFS DPDYKDHIAV TNETLEEIGA ADIPVLMVYN KVDRMEESSC LRVTESAVYI SAKEESSITL LADEVLKRVY AGHEICHMCL PYARGDIFSY LKEQANVLSE SYEADGISVT VECSQADKGR FAEFLV // ID R5QSI0_9FIRM Unreviewed; 409 AA. AC R5QSI0; DT 24-JUL-2013, integrated into UniProtKB/TrEMBL. DT 24-JUL-2013, sequence version 1. DT 12-APR-2017, entry version 22. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=BN521_00628 {ECO:0000313|EMBL:CCZ31700.1}; OS Coprobacillus sp. CAG:183. OC Bacteria; Firmicutes; Erysipelotrichia; Erysipelotrichales; OC Erysipelotrichaceae; Coprobacillus; environmental samples. OX NCBI_TaxID=1262853 {ECO:0000313|EMBL:CCZ31700.1, ECO:0000313|Proteomes:UP000017960}; RN [1] {ECO:0000313|EMBL:CCZ31700.1, ECO:0000313|Proteomes:UP000017960} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MGS:183 {ECO:0000313|Proteomes:UP000017960}; RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., RA Sunagawa S., Plichta D., Gautier L., Le Chatelier E., Peletier E., RA Bonde I., Nielsen T., Manichanh C., Arumugam M., Batto J., RA Santos M.B.Q.D., Blom N., Borruel N., Burgdorf K.S., Boumezbeur F., RA Casellas F., Dore J., Guarner F., Hansen T., Hildebrand F., Kaas R.S., RA Kennedy S., Kristiansen K., Kultima J.R., Leonard P., Levenez F., RA Lund O., Moumen B., Le Paslier D., Pons N., Pedersen O., Prifti E., RA Qin J., Raes J., Tap J., Tims S., Ussery D.W., Yamada T., RA MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P., Wang J., RA Brunak S., Ehrlich S.D.; RT "Dependencies among metagenomic species, viruses, plasmids and units RT of genetic variation."; RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:CCZ31700.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CAZV010000089; CCZ31700.1; -; Genomic_DNA. DR Proteomes; UP000017960; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000017960}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000017960}. FT DOMAIN 191 354 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 409 AA; 47298 MW; 898ABDDE10149B70 CRC64; MMKALIVGVR YKEMNYDLDN SLIELEELCK ACNIEVIKRC VQNLDKINPS LYIGTGKVQE IKGQLDNLDL VIFNEELSPL QVKNLTDILD IEVTDRTDLI LRIFEVRAKT KEAKLQVEIA KGQYLLPRLA GMKEHLYSQQ GGSGFRGSGE KQIELDRRLV SNQIFNAKKQ LANIVKQRQN QRKRRKDNEM KVIALVGYTN SGKSTLMNAF CLNKNKQVLQ KDMLFATLET ATRHITINQH PCLLTDTVGF IERLPHHLIQ AFRSTLEEVV EADLLIHVVD ASNPNYEQYI NTTNAVLKEL GIKDTPMIYA YNKVDLNKYG FIVPLEPYAF ISAKERIGLE VLEKSISDIL FKDYAIYDLN IPYQDGEVFK YLHQHCLVLE FQYLENSIYM KIEAHPRFMV QYDQYLLKH // ID R5QUG4_9FIRM Unreviewed; 401 AA. AC R5QUG4; DT 24-JUL-2013, integrated into UniProtKB/TrEMBL. DT 24-JUL-2013, sequence version 1. DT 12-APR-2017, entry version 23. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=BN550_02231 {ECO:0000313|EMBL:CCZ24647.1}; OS Coprobacillus sp. CAG:235. OC Bacteria; Firmicutes; Erysipelotrichia; Erysipelotrichales; OC Erysipelotrichaceae; Coprobacillus; environmental samples. OX NCBI_TaxID=1262854 {ECO:0000313|EMBL:CCZ24647.1, ECO:0000313|Proteomes:UP000018196}; RN [1] {ECO:0000313|EMBL:CCZ24647.1, ECO:0000313|Proteomes:UP000018196} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MGS:235 {ECO:0000313|Proteomes:UP000018196}; RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., RA Sunagawa S., Plichta D., Gautier L., Le Chatelier E., Peletier E., RA Bonde I., Nielsen T., Manichanh C., Arumugam M., Batto J., RA Santos M.B.Q.D., Blom N., Borruel N., Burgdorf K.S., Boumezbeur F., RA Casellas F., Dore J., Guarner F., Hansen T., Hildebrand F., Kaas R.S., RA Kennedy S., Kristiansen K., Kultima J.R., Leonard P., Levenez F., RA Lund O., Moumen B., Le Paslier D., Pons N., Pedersen O., Prifti E., RA Qin J., Raes J., Tap J., Tims S., Ussery D.W., Yamada T., RA MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P., Wang J., RA Brunak S., Ehrlich S.D.; RT "Dependencies among metagenomic species, viruses, plasmids and units RT of genetic variation."; RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:CCZ24647.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CAZR010000202; CCZ24647.1; -; Genomic_DNA. DR Proteomes; UP000018196; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000018196}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000018196}. FT DOMAIN 183 346 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 401 AA; 47043 MW; 791C85BA90B1CDF6 CRC64; MKAILVLTST NPFYEEELKS LCEACHIEVV DVVIQKLEKI NPATYIGKGK IEEIKLKLQD EMVIFDNELT PLQVKNLTDL LETEVTDRTD LILRIFDERA KTKEAKLQVE IARDQYLLPR LVGMQEHMSH QQGGSGFRGS GEKQIELDRR IIARKLARSR KELAEIVKQR QVQRQRRKNN QIPVIALVGY TNSGKSTLLN TLCQDKQKKV FEKDMLFATL ETSTRHIKMK NHDCLLTDTV GFIERLPHHL IQAFRSTLEE VKEADLFLHV VDTSFEDYQM QVETTNEVLK SLGVENTPMI YVYNKIDLNK YAYIQPQSPY VFISAKYKRG FDLLEDEISH LLFKDYEVFE LSIPYSQGED FKYLHQHCYV KEIEYLEKSI YLKIEARRQE IKNYLHYCLK H // ID R5QWC3_9FIRM Unreviewed; 411 AA. AC R5QWC3; DT 24-JUL-2013, integrated into UniProtKB/TrEMBL. DT 24-JUL-2013, sequence version 1. DT 12-APR-2017, entry version 24. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=BN747_01870 {ECO:0000313|EMBL:CCZ33095.1}; OS Firmicutes bacterium CAG:646. OC Bacteria; Firmicutes; environmental samples. OX NCBI_TaxID=1262995 {ECO:0000313|EMBL:CCZ33095.1, ECO:0000313|Proteomes:UP000018386}; RN [1] {ECO:0000313|EMBL:CCZ33095.1, ECO:0000313|Proteomes:UP000018386} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MGS:646 {ECO:0000313|Proteomes:UP000018386}; RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., RA Sunagawa S., Plichta D., Gautier L., Le Chatelier E., Peletier E., RA Bonde I., Nielsen T., Manichanh C., Arumugam M., Batto J., RA Santos M.B.Q.D., Blom N., Borruel N., Burgdorf K.S., Boumezbeur F., RA Casellas F., Dore J., Guarner F., Hansen T., Hildebrand F., Kaas R.S., RA Kennedy S., Kristiansen K., Kultima J.R., Leonard P., Levenez F., RA Lund O., Moumen B., Le Paslier D., Pons N., Pedersen O., Prifti E., RA Qin J., Raes J., Tap J., Tims S., Ussery D.W., Yamada T., RA MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P., Wang J., RA Brunak S., Ehrlich S.D.; RT "Dependencies among metagenomic species, viruses, plasmids and units RT of genetic variation."; RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:CCZ33095.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CAZW010000049; CCZ33095.1; -; Genomic_DNA. DR Proteomes; UP000018386; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000018386}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000018386}. FT DOMAIN 199 363 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 411 AA; 46377 MW; 1D708FEDA0EC429C CRC64; MYEMGEQLER VVLAGVQTYD SEDTAESLLE LEELTRTAGA VTVGSVMQSR ESVHPATYLG KGKLEELKEM IYNLDATGVI CDDELTPAQL NNLERELECK VMDRTMVILD IFAGRARTSE GKIQVELAQL KYRAARLVGM RASLSRLGGG IGTRGPGEKK LEMDRRLIHQ RIGQLKEQLE EVQRHRTLIR TQREKSRTKV AAIVGYTNAG KSTLLNALTG AGVLEEDQLF ATLDPTTRVL DLPGKQQILL TDTVGFIRKL PHHLIEAFKS TLEEAKYADI ILHVVDASNP RKETHMHVVY DTLKQLGVEN KKVITLFNKQ DLCLDKEQLR DFQADHVLNI SARTGEGLEE VKEILEQTLR EGQVYIERLY PYEQAGKISV IRKHGQVLQE EYLPEGISVK AYIPMENYHT V // ID R5QWM2_9FIRM Unreviewed; 413 AA. AC R5QWM2; DT 24-JUL-2013, integrated into UniProtKB/TrEMBL. DT 24-JUL-2013, sequence version 1. DT 10-MAY-2017, entry version 24. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=BN734_01241 {ECO:0000313|EMBL:CCZ25377.1}; OS Ruminococcus torques CAG:61. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Ruminococcaceae; OC Ruminococcus; environmental samples. OX NCBI_TaxID=1263108 {ECO:0000313|EMBL:CCZ25377.1, ECO:0000313|Proteomes:UP000017998}; RN [1] {ECO:0000313|EMBL:CCZ25377.1, ECO:0000313|Proteomes:UP000017998} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MGS:61 {ECO:0000313|Proteomes:UP000017998}; RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., RA Sunagawa S., Plichta D., Gautier L., Le Chatelier E., Peletier E., RA Bonde I., Nielsen T., Manichanh C., Arumugam M., Batto J., RA Santos M.B.Q.D., Blom N., Borruel N., Burgdorf K.S., Boumezbeur F., RA Casellas F., Dore J., Guarner F., Hansen T., Hildebrand F., Kaas R.S., RA Kennedy S., Kristiansen K., Kultima J.R., Leonard P., Levenez F., RA Lund O., Moumen B., Le Paslier D., Pons N., Pedersen O., Prifti E., RA Qin J., Raes J., Tap J., Tims S., Ussery D.W., Yamada T., RA MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P., Wang J., RA Brunak S., Ehrlich S.D.; RT "Dependencies among metagenomic species, viruses, plasmids and units RT of genetic variation."; RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:CCZ25377.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CAZS010000008; CCZ25377.1; -; Genomic_DNA. DR Proteomes; UP000017998; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000017998}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000017998}. FT DOMAIN 199 363 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 158 195 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 413 AA; 46016 MW; A9E5C312600AA150 CRC64; MYEMEQIDER VILVGIDTGN EDAANRSLDE LSELAKTAKA AVVGRLIQPR ESAHPGTYIG KGKLTELKDL IWETDATGII CDDELTSAQL GNLEEELSCK IIDRTLLILD IFAARAVSGE GKIQVELAQL RYRASRLAGL GRSLSRLGGG IGTRGPGEKK LEMDRRLIRE RISRLKKELK DVEKHRELIR TQRKQSGLKV AALVGYTSAG KSSIENVLTN AGILEDAMLF STLDTTTRSL VLDNTQEILV TDTVGFIRKL PHHLVEAFKS TLEEAKYADI IIHVVDASNP QMDEQMHVVY DTLRQLGAAD RPVITLFNKQ DKLESAGSYR DFQAEYSIPA SAKTGEGLAE LKKALLEIVR REQIYVERLY DFSEASKIQL IRSRGQLLSE KYVPEGIEVK AYVPKDIYGK VCI // ID R5RAI4_9PROT Unreviewed; 441 AA. AC R5RAI4; DT 24-JUL-2013, integrated into UniProtKB/TrEMBL. DT 24-JUL-2013, sequence version 1. DT 12-APR-2017, entry version 22. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=BN682_01497 {ECO:0000313|EMBL:CCZ29922.1}; OS Proteobacteria bacterium CAG:495. OC Bacteria; Proteobacteria; environmental samples. OX NCBI_TaxID=1262987 {ECO:0000313|EMBL:CCZ29922.1, ECO:0000313|Proteomes:UP000018309}; RN [1] {ECO:0000313|EMBL:CCZ29922.1, ECO:0000313|Proteomes:UP000018309} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MGS:495 {ECO:0000313|Proteomes:UP000018309}; RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., RA Sunagawa S., Plichta D., Gautier L., Le Chatelier E., Peletier E., RA Bonde I., Nielsen T., Manichanh C., Arumugam M., Batto J., RA Santos M.B.Q.D., Blom N., Borruel N., Burgdorf K.S., Boumezbeur F., RA Casellas F., Dore J., Guarner F., Hansen T., Hildebrand F., Kaas R.S., RA Kennedy S., Kristiansen K., Kultima J.R., Leonard P., Levenez F., RA Lund O., Moumen B., Le Paslier D., Pons N., Pedersen O., Prifti E., RA Qin J., Raes J., Tap J., Tims S., Ussery D.W., Yamada T., RA MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P., Wang J., RA Brunak S., Ehrlich S.D.; RT "Dependencies among metagenomic species, viruses, plasmids and units RT of genetic variation."; RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:CCZ29922.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CAZU010000018; CCZ29922.1; -; Genomic_DNA. DR Proteomes; UP000018309; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000018309}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000018309}. FT DOMAIN 212 384 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 441 AA; 49943 MW; 0A803F900C8F7405 CRC64; MTAKNKLPLI EFEKNKKVKA AVIFPEVLNQ PLSLSADSRL EEAVGLALAI NLDVVYKEII KVRAIKPSTF VGQGVLERLK PLLEAEETEL LIVDTSLTPI QQRTLENKLK IKVIDRTALI LEIFGERAQT REGKLQVELA HLTYQRSRLV RSWTHLERQR GGAGFLGGPG ETQIELDRRI IDDKIVRIKK ELEKVRQTRQ IQRSARQRIP YPVIALVGYT NAGKSSLFNQ LSAAGVFAKD LLFATLDPAM RKIRLPSGQE VILSDTVGFI SDLPHELIMA FRATLEEVLS ADVIVHVRDI ANPNTREQQQ DVLKVLRSLG LEDIEQQDSY IELFNKIDLL DDDMRRHLEK QIAARRNRVM VSALTGEGCP QFLRLIDDTL AAHHRTIEVK LPITDGKMIA WLHAHAEVLS RQEMENAVEF KVRIDAAAES RLYKMLDSTL N // ID R5RTP4_9BACE Unreviewed; 393 AA. AC R5RTP4; DT 24-JUL-2013, integrated into UniProtKB/TrEMBL. DT 24-JUL-2013, sequence version 1. DT 12-APR-2017, entry version 23. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=BN702_00707 {ECO:0000313|EMBL:CCZ44615.1}; OS Bacteroides sp. CAG:545. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae; OC Bacteroides; environmental samples. OX NCBI_TaxID=1262742 {ECO:0000313|EMBL:CCZ44615.1, ECO:0000313|Proteomes:UP000018187}; RN [1] {ECO:0000313|EMBL:CCZ44615.1, ECO:0000313|Proteomes:UP000018187} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MGS:545 {ECO:0000313|Proteomes:UP000018187}; RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., RA Sunagawa S., Plichta D., Gautier L., Le Chatelier E., Peletier E., RA Bonde I., Nielsen T., Manichanh C., Arumugam M., Batto J., RA Santos M.B.Q.D., Blom N., Borruel N., Burgdorf K.S., Boumezbeur F., RA Casellas F., Dore J., Guarner F., Hansen T., Hildebrand F., Kaas R.S., RA Kennedy S., Kristiansen K., Kultima J.R., Leonard P., Levenez F., RA Lund O., Moumen B., Le Paslier D., Pons N., Pedersen O., Prifti E., RA Qin J., Raes J., Tap J., Tims S., Ussery D.W., Yamada T., RA MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P., Wang J., RA Brunak S., Ehrlich S.D.; RT "Dependencies among metagenomic species, viruses, plasmids and units RT of genetic variation."; RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:CCZ44615.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CBAA010000106; CCZ44615.1; -; Genomic_DNA. DR Proteomes; UP000018187; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000018187}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000018187}. FT DOMAIN 198 382 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 166 193 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 393 AA; 45208 MW; 70A3FF131E600246 CRC64; MTENVEKAVF VGIITSNDEE SKVMEYLDEL EFLAETAGAT RDKKFVQRLD RPDNATYIRS GKLQEIADYC EQNDIKYVIF DDELSGTQQR NIEKIIKTSS VIDRTSLILE IFAQRAKTAY AKTQVELAKY NYMLPRLAGM WTHLERQRGG MGTRGGMGET QIEIDRRIVK ERISKLKEQL KKVDKQMATQ RGNRGQLVRL ALVGYTNVGK STLMNLLSKS DVFAENKLFA TLDTTVRKVV LENVPFLLSD TVGFIRKLPT QLIEAFKSTL DEVREADILI HVVDISHPGF EEQMEVVENT LRDINADNKP IYVIFNKVDA YTYEEYDEFS LEPKGKNNRS LEELKNSWIA KEKTPCIFIS AKEKIGIDKL RNDIYKMVAE IHAGRYPFNN FLW // ID R5SF01_9CLOT Unreviewed; 420 AA. AC R5SF01; DT 24-JUL-2013, integrated into UniProtKB/TrEMBL. DT 24-JUL-2013, sequence version 1. DT 10-MAY-2017, entry version 24. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=BN771_00468 {ECO:0000313|EMBL:CCZ51728.1}; OS Clostridium sp. CAG:75. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium; environmental samples. OX NCBI_TaxID=1262836 {ECO:0000313|EMBL:CCZ51728.1, ECO:0000313|Proteomes:UP000018032}; RN [1] {ECO:0000313|EMBL:CCZ51728.1, ECO:0000313|Proteomes:UP000018032} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MGS:75 {ECO:0000313|Proteomes:UP000018032}; RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., RA Sunagawa S., Plichta D., Gautier L., Le Chatelier E., Peletier E., RA Bonde I., Nielsen T., Manichanh C., Arumugam M., Batto J., RA Santos M.B.Q.D., Blom N., Borruel N., Burgdorf K.S., Boumezbeur F., RA Casellas F., Dore J., Guarner F., Hansen T., Hildebrand F., Kaas R.S., RA Kennedy S., Kristiansen K., Kultima J.R., Leonard P., Levenez F., RA Lund O., Moumen B., Le Paslier D., Pons N., Pedersen O., Prifti E., RA Qin J., Raes J., Tap J., Tims S., Ussery D.W., Yamada T., RA MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P., Wang J., RA Brunak S., Ehrlich S.D.; RT "Dependencies among metagenomic species, viruses, plasmids and units RT of genetic variation."; RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:CCZ51728.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CBAE010000020; CCZ51728.1; -; Genomic_DNA. DR Proteomes; UP000018032; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000018032}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000018032}. FT DOMAIN 199 363 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 420 AA; 47130 MW; B327BA331E1E0021 CRC64; MFETEEQKER IILVAVATAD GDDTEQSLDE LEELGQTAGA VTVAKVIQNR EKVHAGTYVG KGKIEEIKNL AISLDADAVV CDDELSPAQY HNLQDALEIK VIDRTVMILD IFAKRASTSE GKLQVELAQL RYRASHLVGG RSELSRLGGG IGTRGPGEQK LEMDRRLIKE RITLVKRELE QVKRTRELTR KKRQENPTPV VAIVGYTNAG KSTLLNYLTG AGVLSEDQLF ATLDPTTRKL VREDGEEMLF TDTVGFIRKL PHHLIRAFRS TLEEAKYADI ILHVVDCSNP DLDMQMYTVY ETLRKLEIGD KQIVTAFNKI DRLEGEQVLK DLRADRTVRI SARSGEGVEE MLDALSELLK AGQVLIDKII PYTDGSQINL LRKYGQVLEE SYENDGTKVK AYVPREYAYL FQSADGEDDQ // ID R5SNF5_9FIRM Unreviewed; 435 AA. AC R5SNF5; DT 24-JUL-2013, integrated into UniProtKB/TrEMBL. DT 24-JUL-2013, sequence version 1. DT 12-APR-2017, entry version 23. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=BN483_01571 {ECO:0000313|EMBL:CCZ46472.1}; OS Firmicutes bacterium CAG:129. OC Bacteria; Firmicutes; environmental samples. OX NCBI_TaxID=1263003 {ECO:0000313|EMBL:CCZ46472.1, ECO:0000313|Proteomes:UP000018410}; RN [1] {ECO:0000313|EMBL:CCZ46472.1, ECO:0000313|Proteomes:UP000018410} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MGS:129 {ECO:0000313|Proteomes:UP000018410}; RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., RA Sunagawa S., Plichta D., Gautier L., Le Chatelier E., Peletier E., RA Bonde I., Nielsen T., Manichanh C., Arumugam M., Batto J., RA Santos M.B.Q.D., Blom N., Borruel N., Burgdorf K.S., Boumezbeur F., RA Casellas F., Dore J., Guarner F., Hansen T., Hildebrand F., Kaas R.S., RA Kennedy S., Kristiansen K., Kultima J.R., Leonard P., Levenez F., RA Lund O., Moumen B., Le Paslier D., Pons N., Pedersen O., Prifti E., RA Qin J., Raes J., Tap J., Tims S., Ussery D.W., Yamada T., RA MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P., Wang J., RA Brunak S., Ehrlich S.D.; RT "Dependencies among metagenomic species, viruses, plasmids and units RT of genetic variation."; RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:CCZ46472.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CBAB010000214; CCZ46472.1; -; Genomic_DNA. DR Proteomes; UP000018410; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000018410}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000018410}. FT DOMAIN 212 373 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 178 205 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 435 AA; 48371 MW; 35283D5FC9EC86D4 CRC64; MEENKLNTVE QPRDRVVLVG LSSPVLKADS ADEESMDELA ALVETAGAVS VATVLQNLPS PNPRSFIGEG KVAEIKELIG STEATMAIFD NDLSPSQMRV LTEDLGVQVL DRSGLILDIF AQRAKTKEGR LQVELAQYQY LLPRLIGMWT HLERQAGTSG KGPIGSKGPG ETQLETDRRH IHRKIDKLKE DLDEVRRVRG TQRERRMKNE IPVVAIVGYT NAGKSTLLNA LTGADIPANN RLFDTLDTTT RLLTVSDTLD VVISDTVGFI RKLPHQLIDA FKATLEELEY ADLLLHVIDI SNPEWIAQAE VVDQLIHDLG AEGIPCIRVY NKSDLFYGDI RPHGERAVNL SARTGEGLDE LLRAIDAELD KGTRRVTIHL PYDKGGWLDS LYREAKVESV EYGETIDIVA VCTPRVLGRV KDYVEGYTEP KEDWE // ID R5T5F4_9CLOT Unreviewed; 426 AA. AC R5T5F4; DT 24-JUL-2013, integrated into UniProtKB/TrEMBL. DT 24-JUL-2013, sequence version 1. DT 10-MAY-2017, entry version 24. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=BN544_03196 {ECO:0000313|EMBL:CCZ60773.1}; OS Clostridium hathewayi CAG:224. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium; environmental samples. OX NCBI_TaxID=1263067 {ECO:0000313|EMBL:CCZ60773.1, ECO:0000313|Proteomes:UP000018246}; RN [1] {ECO:0000313|EMBL:CCZ60773.1, ECO:0000313|Proteomes:UP000018246} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MGS:224 {ECO:0000313|Proteomes:UP000018246}; RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., RA Sunagawa S., Plichta D., Gautier L., Le Chatelier E., Peletier E., RA Bonde I., Nielsen T., Manichanh C., Arumugam M., Batto J., RA Santos M.B.Q.D., Blom N., Borruel N., Burgdorf K.S., Boumezbeur F., RA Casellas F., Dore J., Guarner F., Hansen T., Hildebrand F., Kaas R.S., RA Kennedy S., Kristiansen K., Kultima J.R., Leonard P., Levenez F., RA Lund O., Moumen B., Le Paslier D., Pons N., Pedersen O., Prifti E., RA Qin J., Raes J., Tap J., Tims S., Ussery D.W., Yamada T., RA MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P., Wang J., RA Brunak S., Ehrlich S.D.; RT "Dependencies among metagenomic species, viruses, plasmids and units RT of genetic variation."; RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:CCZ60773.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CBAI010000132; CCZ60773.1; -; Genomic_DNA. DR Proteomes; UP000018246; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000018246}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000018246}. FT DOMAIN 203 373 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 162 196 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 426 AA; 48736 MW; BC9408322D0DC712 CRC64; MKQLNETIRP RALLAGVRLN ENQDFEVSMK ELNNLVKACD MEPVARIDQN LASINAAYYI GSGKVGEIRE AAETLRADYV VFNDTLSPSQ LKNLQREIDV PVWDRTYLIL EIFSRRAQTK EARMQVESAR LQYMLPRLMG LRDSLGRQGG ASGSLSNKGS GEKQIELDRR KIEGRISELR RELERMEQER NVQRRKRSRG TCPQAALVGY TNAGKSTLLN KLVELSNGKE EKMVMAKDML FATLDTTVRK ISPNGSQDFL LSDTVGFISR LPHSLVKAFR STLEEIRYAD LLLHVVDFSD EHYKEQMEVT EETLKELGAG DIPRIYIMNK ADSVMEGETL PEISGNRIYM SAKYGIGIPE LLRMMEQILF SEYQEARFLI PYENGNVVHY FNSRAMVHSQ EYQEQGVCLT VSCREGDREK YKQYLT // ID R5TJU7_9CLOT Unreviewed; 415 AA. AC R5TJU7; DT 24-JUL-2013, integrated into UniProtKB/TrEMBL. DT 24-JUL-2013, sequence version 1. DT 12-APR-2017, entry version 24. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=BN544_01472 {ECO:0000313|EMBL:CCZ63569.1}; OS Clostridium hathewayi CAG:224. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium; environmental samples. OX NCBI_TaxID=1263067 {ECO:0000313|EMBL:CCZ63569.1, ECO:0000313|Proteomes:UP000018246}; RN [1] {ECO:0000313|EMBL:CCZ63569.1, ECO:0000313|Proteomes:UP000018246} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MGS:224 {ECO:0000313|Proteomes:UP000018246}; RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., RA Sunagawa S., Plichta D., Gautier L., Le Chatelier E., Peletier E., RA Bonde I., Nielsen T., Manichanh C., Arumugam M., Batto J., RA Santos M.B.Q.D., Blom N., Borruel N., Burgdorf K.S., Boumezbeur F., RA Casellas F., Dore J., Guarner F., Hansen T., Hildebrand F., Kaas R.S., RA Kennedy S., Kristiansen K., Kultima J.R., Leonard P., Levenez F., RA Lund O., Moumen B., Le Paslier D., Pons N., Pedersen O., Prifti E., RA Qin J., Raes J., Tap J., Tims S., Ussery D.W., Yamada T., RA MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P., Wang J., RA Brunak S., Ehrlich S.D.; RT "Dependencies among metagenomic species, viruses, plasmids and units RT of genetic variation."; RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:CCZ63569.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CBAI010000309; CCZ63569.1; -; Genomic_DNA. DR Proteomes; UP000018246; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000018246}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000018246}. FT DOMAIN 202 366 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 415 AA; 46576 MW; 5255447A1F377CB7 CRC64; MADLVELKEI EERVILVAVS TEEGSLAASS LDELEELVET AGAVTVDKMI QNRERIHPGT YLGKGKIEEV KERVWELNAT GIVCDDELSP AQLRNLEDAL DTKVMDRTMV ILDIFASRAT TREGKIQVEL AQLKYRAARL VGLRNSLSRL GGGIGTRGPG EKKLEADRRL IHDRIGQLKA ELEDVKRHRD VARQQRTRNH TPVAAIVGYT NAGKSTLLNT LTDAGILAED KLFATLDPTT RNLELPGGEQ ILLTDTVGFI RKLPHNLIEA FKSTLEEAKY SDIILHVVDC SNPQMDMQMY VVYETLKDLG VHDKEVITVF NKIDAAGEMR IPRDLSSDYQ VKISAKTGEG LDELLNLLES ILRSRKVFLE RVYPYQEAGK IQLIRKYGQL LKEEYRDDGI FVSAYVPAEM YTNLI // ID R5TMA9_9FIRM Unreviewed; 410 AA. AC R5TMA9; DT 24-JUL-2013, integrated into UniProtKB/TrEMBL. DT 24-JUL-2013, sequence version 1. DT 12-APR-2017, entry version 22. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=BN683_01527 {ECO:0000313|EMBL:CCZ64459.1}; OS Roseburia sp. CAG:50. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Lachnospiraceae; OC Roseburia; environmental samples. OX NCBI_TaxID=1262949 {ECO:0000313|EMBL:CCZ64459.1, ECO:0000313|Proteomes:UP000018378}; RN [1] {ECO:0000313|EMBL:CCZ64459.1, ECO:0000313|Proteomes:UP000018378} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MGS:50 {ECO:0000313|Proteomes:UP000018378}; RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., RA Sunagawa S., Plichta D., Gautier L., Le Chatelier E., Peletier E., RA Bonde I., Nielsen T., Manichanh C., Arumugam M., Batto J., RA Santos M.B.Q.D., Blom N., Borruel N., Burgdorf K.S., Boumezbeur F., RA Casellas F., Dore J., Guarner F., Hansen T., Hildebrand F., Kaas R.S., RA Kennedy S., Kristiansen K., Kultima J.R., Leonard P., Levenez F., RA Lund O., Moumen B., Le Paslier D., Pons N., Pedersen O., Prifti E., RA Qin J., Raes J., Tap J., Tims S., Ussery D.W., Yamada T., RA MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P., Wang J., RA Brunak S., Ehrlich S.D.; RT "Dependencies among metagenomic species, viruses, plasmids and units RT of genetic variation."; RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:CCZ64459.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CBAK010000074; CCZ64459.1; -; Genomic_DNA. DR Proteomes; UP000018378; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000018378}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000018378}. FT DOMAIN 202 366 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 410 AA; 46182 MW; 7000529F5FC1DBC2 CRC64; MGIVYENEQP VERVILVGIS ERNGDDTESS LAELAELAAT AGAEVVGTVI QNLEHMHPGT YVGTGKLEEI RDMIWEKEAT GIICDDELSP IQMRNMEQVL DSKVMDRTLL ILDIFAARAR TSEGKIQVEL AQLKYRASRL AGFGRSMSRL GGGIGTRGPG EKKLEIDRRL IGHRTAQLNR ELKEVVRHRE LTRSQRMKSH TKVAAIVGYT NAGKSTLLNT LTDADVLEED QLFATLDPTT RMLELSNHQN LMLTDTVGFI RKLPHHLVDA FKSTLEEAKY ADFIIHVVDA SNPQWDAQMH VVYMTLQDLG VVDKKILTVF NKCDRITGEE ILQDFRADKT LRISAKTGMG LDTLKEVFED MLRDGKVLLK HTFPYEKAGE IQKIRKYGEL LKEEYTPEGI YVEAYVPPEL // ID R5TNL2_9FIRM Unreviewed; 413 AA. AC R5TNL2; DT 24-JUL-2013, integrated into UniProtKB/TrEMBL. DT 24-JUL-2013, sequence version 1. DT 10-MAY-2017, entry version 24. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=BN481_02488 {ECO:0000313|EMBL:CCZ67255.1}; OS Ruminococcus gnavus CAG:126. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Ruminococcaceae; OC Ruminococcus; environmental samples. OX NCBI_TaxID=1263106 {ECO:0000313|EMBL:CCZ67255.1, ECO:0000313|Proteomes:UP000018114}; RN [1] {ECO:0000313|EMBL:CCZ67255.1, ECO:0000313|Proteomes:UP000018114} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MGS:126 {ECO:0000313|Proteomes:UP000018114}; RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., RA Sunagawa S., Plichta D., Gautier L., Le Chatelier E., Peletier E., RA Bonde I., Nielsen T., Manichanh C., Arumugam M., Batto J., RA Santos M.B.Q.D., Blom N., Borruel N., Burgdorf K.S., Boumezbeur F., RA Casellas F., Dore J., Guarner F., Hansen T., Hildebrand F., Kaas R.S., RA Kennedy S., Kristiansen K., Kultima J.R., Leonard P., Levenez F., RA Lund O., Moumen B., Le Paslier D., Pons N., Pedersen O., Prifti E., RA Qin J., Raes J., Tap J., Tims S., Ussery D.W., Yamada T., RA MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P., Wang J., RA Brunak S., Ehrlich S.D.; RT "Dependencies among metagenomic species, viruses, plasmids and units RT of genetic variation."; RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:CCZ67255.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CBAL010000067; CCZ67255.1; -; Genomic_DNA. DR Proteomes; UP000018114; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000018114}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000018114}. FT DOMAIN 201 365 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 160 201 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 413 AA; 46608 MW; 30BAD4A3E654FAB1 CRC64; MALYEMEDAK ERVILVGVQE NDAEPEEESL DELAELARTA GAEVAGRLIQ KREAMHPVTY IGKGKILELK ELLWETDATG IICDDELTSV QLNHLEEELE CKIVDRTLLI LDIFAGRAVS REGKIQVELA QLKYRAARLV GLRNSLSRLG GGIGTRGPGE KKLEMDRRLI RERISRLKKE LREVEEHRER LRTQRKRSNL KVAALVGYTS AGKSSLENAL TGAGVLEDAM LFSTLDTTTR SLRLADTQEI LLSDTVGFIR KLPHHLVEAF KSTLEEAKYA DIIIHVVDAS NPHQDTQMFV VYETLRQLGA EGKPVITVFN KQDKLETPGY FRDFHAEYSI PVSAKTGQGL EELKEALLEI LRRDQVYIER LYSFAEAGKI QLIRTQGQLL SEEYVPDGIE VKAYVPKEIW GKV // ID R5ULE1_9FIRM Unreviewed; 414 AA. AC R5ULE1; DT 24-JUL-2013, integrated into UniProtKB/TrEMBL. DT 24-JUL-2013, sequence version 1. DT 12-APR-2017, entry version 23. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=BN518_00424 {ECO:0000313|EMBL:CCZ79118.1}; OS Roseburia sp. CAG:18. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Lachnospiraceae; OC Roseburia; environmental samples. OX NCBI_TaxID=1262941 {ECO:0000313|EMBL:CCZ79118.1, ECO:0000313|Proteomes:UP000018230}; RN [1] {ECO:0000313|EMBL:CCZ79118.1, ECO:0000313|Proteomes:UP000018230} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MGS:18 {ECO:0000313|Proteomes:UP000018230}; RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., RA Sunagawa S., Plichta D., Gautier L., Le Chatelier E., Peletier E., RA Bonde I., Nielsen T., Manichanh C., Arumugam M., Batto J., RA Santos M.B.Q.D., Blom N., Borruel N., Burgdorf K.S., Boumezbeur F., RA Casellas F., Dore J., Guarner F., Hansen T., Hildebrand F., Kaas R.S., RA Kennedy S., Kristiansen K., Kultima J.R., Leonard P., Levenez F., RA Lund O., Moumen B., Le Paslier D., Pons N., Pedersen O., Prifti E., RA Qin J., Raes J., Tap J., Tims S., Ussery D.W., Yamada T., RA MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P., Wang J., RA Brunak S., Ehrlich S.D.; RT "Dependencies among metagenomic species, viruses, plasmids and units RT of genetic variation."; RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:CCZ79118.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CBAP010000141; CCZ79118.1; -; Genomic_DNA. DR Proteomes; UP000018230; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000018230}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000018230}. FT DOMAIN 202 366 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 161 195 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 414 AA; 46151 MW; E7847A6B956139C2 CRC64; MGEPIVLEDF KERVILVGVS EQDGDDAEDS LAELAELVKT AGASVAGTLI QKRELIHPGT YVGTGKVAEI AELLEHTGAT GIVCDDELSP AQLKNLETML NTKVMDRTLI ILDIFAARAT TSEGKIQVEL AQLKYRLSRL TGLGRSMSRL GGGIGTRGPG EKKLEIDRRL INDRIAQLNR ELKEVVKHRE IARAKRERNA VPVVAIVGYT NAGKSTLLNH LTDAEVLEED KLFATLDPTT RMLELEGHQQ VLLTDTVGFI RKLPHHLIEA FKSTLEEAKY ADYIIHVVDA SNPQRDKQMY IVYETLDHLG VKNKKILTLF NKIDIRTDDD PLQDFRADHV LQISATENAG LDAVKDVLQE MLREDKIYIE RVIPYAQAGV LQLVRNKGEL VSEEYVPEGI SIRAYVPMEV YGKL // ID R5UWB2_9BACT Unreviewed; 405 AA. AC R5UWB2; DT 24-JUL-2013, integrated into UniProtKB/TrEMBL. DT 24-JUL-2013, sequence version 1. DT 12-APR-2017, entry version 24. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=BN754_01031 {ECO:0000313|EMBL:CCZ75426.1}; OS Alistipes finegoldii CAG:68. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Rikenellaceae; OC Alistipes; environmental samples. OX NCBI_TaxID=1263035 {ECO:0000313|EMBL:CCZ75426.1, ECO:0000313|Proteomes:UP000018154}; RN [1] {ECO:0000313|EMBL:CCZ75426.1, ECO:0000313|Proteomes:UP000018154} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MGS:68 {ECO:0000313|Proteomes:UP000018154}; RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., RA Sunagawa S., Plichta D., Gautier L., Le Chatelier E., Peletier E., RA Bonde I., Nielsen T., Manichanh C., Arumugam M., Batto J., RA Santos M.B.Q.D., Blom N., Borruel N., Burgdorf K.S., Boumezbeur F., RA Casellas F., Dore J., Guarner F., Hansen T., Hildebrand F., Kaas R.S., RA Kennedy S., Kristiansen K., Kultima J.R., Leonard P., Levenez F., RA Lund O., Moumen B., Le Paslier D., Pons N., Pedersen O., Prifti E., RA Qin J., Raes J., Tap J., Tims S., Ussery D.W., Yamada T., RA MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P., Wang J., RA Brunak S., Ehrlich S.D.; RT "Dependencies among metagenomic species, viruses, plasmids and units RT of genetic variation."; RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:CCZ75426.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CBAO010000030; CCZ75426.1; -; Genomic_DNA. DR Proteomes; UP000018154; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000018154}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000018154}. FT DOMAIN 210 394 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 171 205 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 405 AA; 46301 MW; 10C44CCB3F6EB75B CRC64; MEENKNKTPN AGTASDGRER AVLVAVVRDD QDPRQAAEFL DELEFLAETA DIESVKRFTQ RLPQPSSRIY VGPGKLEEIA GYCKDQEIDV VIFDDELSPS QTRNIEKAMP CRILDRTRLI LDIFMSRAQT AYAKTQVQLA NYEYMLPRLS GMWTHLERQR GGTGTRGGAG EREIETDRRI IRNRIAKLKE DLRKIDRQMA VQRSNRGSMV RVALVGYTNV GKSTLMNLIS KSEVFAENKL FATLDTTVRK VVFDNLPFLL SDTVGFIRKL PTELIESFKS TLDEVREADL LVHVVDISHP QFEEQIDVVK QTLQDIGAGD KPVYLVFNKV DAYTYVKKDE DDLTPATREN LSLDDLKKSW IARANTPCIF LSARMKTNIE KFRTDLYGMV REIHAGRYPF NNFLY // ID R5UZ19_9BACE Unreviewed; 418 AA. AC R5UZ19; DT 24-JUL-2013, integrated into UniProtKB/TrEMBL. DT 24-JUL-2013, sequence version 1. DT 12-APR-2017, entry version 24. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=BN535_00233 {ECO:0000313|EMBL:CCZ73952.1}; OS Bacteroides caccae CAG:21. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae; OC Bacteroides; environmental samples. OX NCBI_TaxID=1263037 {ECO:0000313|EMBL:CCZ73952.1, ECO:0000313|Proteomes:UP000017990}; RN [1] {ECO:0000313|EMBL:CCZ73952.1, ECO:0000313|Proteomes:UP000017990} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MGS:21 {ECO:0000313|Proteomes:UP000017990}; RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., RA Sunagawa S., Plichta D., Gautier L., Le Chatelier E., Peletier E., RA Bonde I., Nielsen T., Manichanh C., Arumugam M., Batto J., RA Santos M.B.Q.D., Blom N., Borruel N., Burgdorf K.S., Boumezbeur F., RA Casellas F., Dore J., Guarner F., Hansen T., Hildebrand F., Kaas R.S., RA Kennedy S., Kristiansen K., Kultima J.R., Leonard P., Levenez F., RA Lund O., Moumen B., Le Paslier D., Pons N., Pedersen O., Prifti E., RA Qin J., Raes J., Tap J., Tims S., Ussery D.W., Yamada T., RA MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P., Wang J., RA Brunak S., Ehrlich S.D.; RT "Dependencies among metagenomic species, viruses, plasmids and units RT of genetic variation."; RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:CCZ73952.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CBAN010000128; CCZ73952.1; -; Genomic_DNA. DR Proteomes; UP000017990; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000017990}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000017990}. FT DOMAIN 216 400 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 418 AA; 47741 MW; 8C67F06A4FB935A9 CRC64; MKEFVISEAK VEIAVLVGLI TQTQDERKTN EYLDELAFLA ETAGAEVVKR FTQKLPTANS VTYVGKGKLE EIKQYIRNEE EEEREVGMVI FDDELSAKQI RNIEAELKIK ILDRTSLILD IFAMRAQTAN AKTQVELAQY KYMLPRLQRL WTHLERQGGG SGAGGGKGSV GLRGPGETQL EMDRRIILNR MSLLKERLAE IDKQKATQRK NRGRMIRVAL VGYTNVGKST MMNLLSKSEV FAENKLFATL DTTVRKVIID NLPFLLSDTV GFIRKLPTDL VDSFKSTLDE VREADLLVHV VDISHPGFEE QIEVVNKTLA EIGGGGKPMI LVFNKIDAYT YVEKAPDDLT PRTKENLTLE ELMKTWMAKM EDNCLFISAR ERINMDELKS VVYQRVKELH VQKYPYNDFL YQIYEEEE // ID R5V099_9BACT Unreviewed; 411 AA. AC R5V099; DT 24-JUL-2013, integrated into UniProtKB/TrEMBL. DT 24-JUL-2013, sequence version 1. DT 12-APR-2017, entry version 25. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=BN709_00823 {ECO:0000313|EMBL:CCZ81474.1}; OS Odoribacter laneus CAG:561. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Odoribacteraceae; OC Odoribacter; environmental samples. OX NCBI_TaxID=1263089 {ECO:0000313|EMBL:CCZ81474.1, ECO:0000313|Proteomes:UP000017974}; RN [1] {ECO:0000313|EMBL:CCZ81474.1, ECO:0000313|Proteomes:UP000017974} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MGS:561 {ECO:0000313|Proteomes:UP000017974}; RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., RA Sunagawa S., Plichta D., Gautier L., Le Chatelier E., Peletier E., RA Bonde I., Nielsen T., Manichanh C., Arumugam M., Batto J., RA Santos M.B.Q.D., Blom N., Borruel N., Burgdorf K.S., Boumezbeur F., RA Casellas F., Dore J., Guarner F., Hansen T., Hildebrand F., Kaas R.S., RA Kennedy S., Kristiansen K., Kultima J.R., Leonard P., Levenez F., RA Lund O., Moumen B., Le Paslier D., Pons N., Pedersen O., Prifti E., RA Qin J., Raes J., Tap J., Tims S., Ussery D.W., Yamada T., RA MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P., Wang J., RA Brunak S., Ehrlich S.D.; RT "Dependencies among metagenomic species, viruses, plasmids and units RT of genetic variation."; RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:CCZ81474.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CBAQ010000074; CCZ81474.1; -; Genomic_DNA. DR Proteomes; UP000017974; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000017974}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000017974}. FT DOMAIN 205 389 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 411 AA; 47273 MW; EFE6A1207FBCE738 CRC64; MGEFYYTKKE AEKAILVGVA LQEEGINYER MCEYLDELAF LAETAGAETI KVFTQNLDKP VNSTFIGKGK LEEIRQYIEE NETDLVIFDD ELSPTQLRNI ENELKGVKVL DRTNLILDIF ANRARTAHAK TQVELAQYQY LLPRLAGMWT HLERQKGGIG LRGPGETEIE TDRRVIRDKI TRLKEQLTRV DKQMSTQRKN RGKLVRVALV GYTNVGKSTL MNLLSKSEVF AENKLFATLD TTVRKITIKN VPLLLADTVG FIRKLPTHLI ESFKSTLDEV READVILHVV DISHPQFEDQ LKVVNETLAE LIKEPKPTII VFNKIDAFTY TPKDEDDLTP TERCNYSLED LKQMWMSKQG CETVYISAAK KENIEELKEK LYAIVKEIHS ARFPYNDFLY NTEDELPEEI N // ID R5V9C8_9FIRM Unreviewed; 418 AA. AC R5V9C8; DT 24-JUL-2013, integrated into UniProtKB/TrEMBL. DT 24-JUL-2013, sequence version 1. DT 10-MAY-2017, entry version 24. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=BN742_01096 {ECO:0000313|EMBL:CCZ84729.1}; OS Firmicutes bacterium CAG:631. OC Bacteria; Firmicutes; environmental samples. OX NCBI_TaxID=1262996 {ECO:0000313|EMBL:CCZ84729.1, ECO:0000313|Proteomes:UP000018035}; RN [1] {ECO:0000313|EMBL:CCZ84729.1, ECO:0000313|Proteomes:UP000018035} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MGS:631 {ECO:0000313|Proteomes:UP000018035}; RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., RA Sunagawa S., Plichta D., Gautier L., Le Chatelier E., Peletier E., RA Bonde I., Nielsen T., Manichanh C., Arumugam M., Batto J., RA Santos M.B.Q.D., Blom N., Borruel N., Burgdorf K.S., Boumezbeur F., RA Casellas F., Dore J., Guarner F., Hansen T., Hildebrand F., Kaas R.S., RA Kennedy S., Kristiansen K., Kultima J.R., Leonard P., Levenez F., RA Lund O., Moumen B., Le Paslier D., Pons N., Pedersen O., Prifti E., RA Qin J., Raes J., Tap J., Tims S., Ussery D.W., Yamada T., RA MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P., Wang J., RA Brunak S., Ehrlich S.D.; RT "Dependencies among metagenomic species, viruses, plasmids and units RT of genetic variation."; RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:CCZ84729.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CBAS010000004; CCZ84729.1; -; Genomic_DNA. DR Proteomes; UP000018035; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000018035}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000018035}. FT DOMAIN 191 369 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 150 184 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 418 AA; 48373 MW; 97EC8F61EDE9830A CRC64; MKVILVGIDI QEEDFEESFI ELKGLASACN YQVVGTLTQK LKSINKKFYM GSGKLPILKS MIEEHHSDGI VFNNDLTPLQ QKNLEDELQC EILDRTQLIL NIFAKRAKTK EAKLQVEVAR LSYLLPRLVT QDAHFEQQVG GNKNTRGSGE KQLELNKRLI KNRIAQLNKD LAELEKNRQT QRQKRQKNDI PLVAIVGYTN AGKSTLMNAF LERYQKNEKK YVVEKDMLFA TLDTSIRHIK LEDNKEFLLC DTVGFISKLP VGLVKAFRST LEEVLHADLI LHVLDISNPM FLRQMMVTNQ TLLDIGVSPN TPMIYVYNKA ERLGFETLET KENHVFISAK NRINMNVLVS HMKKELFKDY LRCKMFFTYK EGSILSYLSE HANIFKKEYS ETGVLIDLEC SLKDYKKYID HVWLDHKN // ID R5W0Q3_9FIRM Unreviewed; 441 AA. AC R5W0Q3; DT 24-JUL-2013, integrated into UniProtKB/TrEMBL. DT 24-JUL-2013, sequence version 1. DT 12-APR-2017, entry version 23. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=BN751_00023 {ECO:0000313|EMBL:CCZ93649.1}; OS Coprococcus eutactus CAG:665. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Lachnospiraceae; OC Coprococcus; environmental samples. OX NCBI_TaxID=1263071 {ECO:0000313|EMBL:CCZ93649.1, ECO:0000313|Proteomes:UP000017949}; RN [1] {ECO:0000313|EMBL:CCZ93649.1, ECO:0000313|Proteomes:UP000017949} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MGS:665 {ECO:0000313|Proteomes:UP000017949}; RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., RA Sunagawa S., Plichta D., Gautier L., Le Chatelier E., Peletier E., RA Bonde I., Nielsen T., Manichanh C., Arumugam M., Batto J., RA Santos M.B.Q.D., Blom N., Borruel N., Burgdorf K.S., Boumezbeur F., RA Casellas F., Dore J., Guarner F., Hansen T., Hildebrand F., Kaas R.S., RA Kennedy S., Kristiansen K., Kultima J.R., Leonard P., Levenez F., RA Lund O., Moumen B., Le Paslier D., Pons N., Pedersen O., Prifti E., RA Qin J., Raes J., Tap J., Tims S., Ussery D.W., Yamada T., RA MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P., Wang J., RA Brunak S., Ehrlich S.D.; RT "Dependencies among metagenomic species, viruses, plasmids and units RT of genetic variation."; RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:CCZ93649.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CBAW010000144; CCZ93649.1; -; Genomic_DNA. DR Proteomes; UP000017949; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000017949}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000017949}. FT DOMAIN 214 383 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 173 207 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 441 AA; 49243 MW; 55D51583B947C64A CRC64; MAEKKSTMYD LEAEKIREKI IIFAVDTGGY TQKEVSLEVQ ASLDELAELI DTAGGEVVGR LAQNRDKIAN DLYLGRGKVE ELRNMIYELG ATGVCCDDEL SPAQLMNLQD ALDIKVMDRT MVILDIFAAH AGSYEGKLQV ELAQLKFRAT RLIGMRDSLS RLGGGIGTRG PGEKKLEIDR RVIRERISRL KAELRTVEAQ RMQQRKQRQR SAVPVAGIVG YTNAGKSTLL NAMTGAGVLE EDKLFATLDP TTRNYRLPGG QNILLTDTVG FIRKLPHHLV EAFGSTLEEA KYCDVIIHVV DASDVNWDKN IETVYHTLKQ LKIDEKSGKP IITVFNKVDK IEKDDLVGVR DLRADRTIYV SAKNGQGLDE LASAIEEILR NQKIYIRHTF AYSDAGLTGL IHKYGEIKTE EYLDDGIFIE AYVPSSILGR LGLGFEDEEE Y // ID R5W3J9_9BACE Unreviewed; 418 AA. AC R5W3J9; DT 24-JUL-2013, integrated into UniProtKB/TrEMBL. DT 24-JUL-2013, sequence version 1. DT 12-APR-2017, entry version 23. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=BN536_02070 {ECO:0000313|EMBL:CCZ87292.1}; OS Bacteroides plebeius CAG:211. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae; OC Bacteroides; environmental samples. OX NCBI_TaxID=1263052 {ECO:0000313|EMBL:CCZ87292.1, ECO:0000313|Proteomes:UP000018372}; RN [1] {ECO:0000313|EMBL:CCZ87292.1, ECO:0000313|Proteomes:UP000018372} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MGS:211 {ECO:0000313|Proteomes:UP000018372}; RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., RA Sunagawa S., Plichta D., Gautier L., Le Chatelier E., Peletier E., RA Bonde I., Nielsen T., Manichanh C., Arumugam M., Batto J., RA Santos M.B.Q.D., Blom N., Borruel N., Burgdorf K.S., Boumezbeur F., RA Casellas F., Dore J., Guarner F., Hansen T., Hildebrand F., Kaas R.S., RA Kennedy S., Kristiansen K., Kultima J.R., Leonard P., Levenez F., RA Lund O., Moumen B., Le Paslier D., Pons N., Pedersen O., Prifti E., RA Qin J., Raes J., Tap J., Tims S., Ussery D.W., Yamada T., RA MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P., Wang J., RA Brunak S., Ehrlich S.D.; RT "Dependencies among metagenomic species, viruses, plasmids and units RT of genetic variation."; RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:CCZ87292.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CBAT010000133; CCZ87292.1; -; Genomic_DNA. DR Proteomes; UP000018372; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000018372}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000018372}. FT DOMAIN 217 401 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 418 AA; 47658 MW; E99BC821B66A1282 CRC64; MKEFVISEAQ TEKAVLVGLI TQTQNERKTN EYLDELAFLA ETAGAEVVKR FTQKLDTPNS VTYVGKGKLQ EVKEYLELQN ESEETEIGMV IFDDELSAKQ IRNIENELKV KILDRTSLIL DIFAMRAQTA NAKTQVELAQ YKYMLPRLQR LWTHLERQGG GSGAGGGKGS VGLRGPGETQ LEMDRRIILN RMALLKQRLA EIDTQKSTQR KNRGRMIRVA LVGYTNVGKS TLMNLLAKSE VFAENKLFAT LDTTVRKVII ENLPFLLSDT VGFIRKLPTD LVDSFKSTLD EVREADLLVH VVDISHPDFE EQIQVVEKTI ADLGAGGKPS MIVFNKVDAY TYVEKAEDDL TPKTKENITL EELMHTWMAK LNDNCIFISA REKTNIDQFR DLLYKKVKEL HVQKYPYNDF LYQTYDEE // ID R5WDN4_9CLOT Unreviewed; 417 AA. AC R5WDN4; DT 24-JUL-2013, integrated into UniProtKB/TrEMBL. DT 24-JUL-2013, sequence version 1. DT 12-APR-2017, entry version 22. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=BN512_01372 {ECO:0000313|EMBL:CCZ90632.1}; OS Clostridium sp. CAG:167. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium; environmental samples. OX NCBI_TaxID=1262777 {ECO:0000313|EMBL:CCZ90632.1, ECO:0000313|Proteomes:UP000018023}; RN [1] {ECO:0000313|EMBL:CCZ90632.1, ECO:0000313|Proteomes:UP000018023} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MGS:167 {ECO:0000313|Proteomes:UP000018023}; RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., RA Sunagawa S., Plichta D., Gautier L., Le Chatelier E., Peletier E., RA Bonde I., Nielsen T., Manichanh C., Arumugam M., Batto J., RA Santos M.B.Q.D., Blom N., Borruel N., Burgdorf K.S., Boumezbeur F., RA Casellas F., Dore J., Guarner F., Hansen T., Hildebrand F., Kaas R.S., RA Kennedy S., Kristiansen K., Kultima J.R., Leonard P., Levenez F., RA Lund O., Moumen B., Le Paslier D., Pons N., Pedersen O., Prifti E., RA Qin J., Raes J., Tap J., Tims S., Ussery D.W., Yamada T., RA MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P., Wang J., RA Brunak S., Ehrlich S.D.; RT "Dependencies among metagenomic species, viruses, plasmids and units RT of genetic variation."; RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:CCZ90632.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CBAV010000095; CCZ90632.1; -; Genomic_DNA. DR Proteomes; UP000018023; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000018023}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000018023}. FT DOMAIN 205 371 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 417 AA; 47054 MW; 0F257BB932457543 CRC64; MAKVYDTAKE KERVILVAVD LSENSDSTTV DISLDELEEL AETAGAVTVG RVVQKRDAFH PGTYIGKGKM EELRDLVWQQ QADTIVCDDE LSPAQITNLS QELDVKVIDR TVMILDIFAA HAKTSEGKLQ VELAQLRYRS SRLMGLGTAM SRLGGGIGTR GPGEKKLEMD RRLIKDRIAW LNRQLKEVVQ NRDTMRKQRS RNHTPTVAIV GYTNAGKSTL LNALTDAGIL SEDKLFATLD PTTRGLELEN GQKILFTDTV GFISKLPHPL IRAFRSTLEE AKYADMILHV VDVSNEHYER QMEVVYNTLR ELEIGDKKVL TAFNKIDRME AGDQTVYKDP RSDKTVYISA REKSGLDELL EKTEEILNEG MIYLEKVFPY EEAGKIQQIR QHGKLESEEY TEEGIAVKAY IPPFLNM // ID R5WID7_9DELT Unreviewed; 413 AA. AC R5WID7; DT 24-JUL-2013, integrated into UniProtKB/TrEMBL. DT 24-JUL-2013, sequence version 1. DT 12-APR-2017, entry version 24. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=BN495_00762 {ECO:0000313|EMBL:CCZ95541.1}; OS Corallococcus sp. CAG:1435. OC Bacteria; Proteobacteria; Deltaproteobacteria; Myxococcales; OC Cystobacterineae; Myxococcaceae; Corallococcus; environmental samples. OX NCBI_TaxID=1262867 {ECO:0000313|EMBL:CCZ95541.1, ECO:0000313|Proteomes:UP000018256}; RN [1] {ECO:0000313|EMBL:CCZ95541.1, ECO:0000313|Proteomes:UP000018256} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MGS:1435 {ECO:0000313|Proteomes:UP000018256}; RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., RA Sunagawa S., Plichta D., Gautier L., Le Chatelier E., Peletier E., RA Bonde I., Nielsen T., Manichanh C., Arumugam M., Batto J., RA Santos M.B.Q.D., Blom N., Borruel N., Burgdorf K.S., Boumezbeur F., RA Casellas F., Dore J., Guarner F., Hansen T., Hildebrand F., Kaas R.S., RA Kennedy S., Kristiansen K., Kultima J.R., Leonard P., Levenez F., RA Lund O., Moumen B., Le Paslier D., Pons N., Pedersen O., Prifti E., RA Qin J., Raes J., Tap J., Tims S., Ussery D.W., Yamada T., RA MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P., Wang J., RA Brunak S., Ehrlich S.D.; RT "Dependencies among metagenomic species, viruses, plasmids and units RT of genetic variation."; RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:CCZ95541.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CBAX010000134; CCZ95541.1; -; Genomic_DNA. DR Proteomes; UP000018256; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000018256}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000018256}. FT DOMAIN 198 357 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 413 AA; 46397 MW; 5E126C9BBC486226 CRC64; MKTETKHNIQ NVALVYLEQP SHNDDEVSEL YDLIRSAHGE VKLFCKQSRN TPDAKTLVGS GKVEEIKVAV QNLDCQIDVV IFSQKLDSLQ RRNLTEALGV TVIDVVDLIL DIFALRATTA EGKKQVELAQ LSYSLATRSD KDFSRQGGGI GTRGPGETQL ETDKRIAREK MYRLRKELQE IAKQRITTRK QRLDNEIFTV ALVGYTNAGK STMFNSLTGY HVYADDRLFA TLDTTVKKVS LDCFDVLFCD TVGFIRNLPT LLIDAFKSTL EEVTYADLIL NVCDVSSDEV ENHLAVTEEI LAQLGVTAPI IRVYNKCDKT TFSVKPGNHK SVFVSALTGK NMDVLLEMIK QEIYRQYADI KLEVPFADSG KIAAKLQKYA VKITTDYTDC CTVFCATVKR KYVALFGEYL KFD // ID R5WR17_9FIRM Unreviewed; 416 AA. AC R5WR17; DT 24-JUL-2013, integrated into UniProtKB/TrEMBL. DT 24-JUL-2013, sequence version 1. DT 12-APR-2017, entry version 23. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=BN568_01550 {ECO:0000313|EMBL:CDA05005.1}; OS Blautia sp. CAG:257. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Lachnospiraceae; OC Blautia; environmental samples. OX NCBI_TaxID=1262756 {ECO:0000313|EMBL:CDA05005.1, ECO:0000313|Proteomes:UP000018056}; RN [1] {ECO:0000313|EMBL:CDA05005.1, ECO:0000313|Proteomes:UP000018056} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MGS:257 {ECO:0000313|Proteomes:UP000018056}; RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., RA Sunagawa S., Plichta D., Gautier L., Le Chatelier E., Peletier E., RA Bonde I., Nielsen T., Manichanh C., Arumugam M., Batto J., RA Santos M.B.Q.D., Blom N., Borruel N., Burgdorf K.S., Boumezbeur F., RA Casellas F., Dore J., Guarner F., Hansen T., Hildebrand F., Kaas R.S., RA Kennedy S., Kristiansen K., Kultima J.R., Leonard P., Levenez F., RA Lund O., Moumen B., Le Paslier D., Pons N., Pedersen O., Prifti E., RA Qin J., Raes J., Tap J., Tims S., Ussery D.W., Yamada T., RA MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P., Wang J., RA Brunak S., Ehrlich S.D.; RT "Dependencies among metagenomic species, viruses, plasmids and units RT of genetic variation."; RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:CDA05005.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CBBB010000056; CDA05005.1; -; Genomic_DNA. DR Proteomes; UP000018056; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000018056}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000018056}. FT DOMAIN 201 364 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 416 AA; 46420 MW; BD11618DE674E531 CRC64; MQLYDFKEIQ ERVILVGVQT DIGDDVEASL DELQELAETA GAETATKVIQ NREAVHPGTY IGKGKIQEVK NLLTALDANG IICDDELSPS QLNNLERELE CKVMDRTLLI LDIFAGRAVT SEGKIQVELA QLRYRSARLV GLRDSLSRLG GGIGTRGPGE KKLETDRRLI RTRISALKAE LVQVEKHREL IRGSRSKGRL KTAAIVGYTN AGKSTLLNTL TGAGVQAEDK LFATLDPTTR VMELDDGQQI LLTDTVGFIR KLPHHLVEAF KSTLEEAKYA DYIIHVVDAS NPRAETQMQV VYETLKELGV SGKKIITLLN KQDLVPDSEL RDLRADYTVK CSARTGRGLC ELRELLSRLL AESQIYIEEL YAYKEAGKIQ MIREYGQLLS EEYREDGIFV QAKIPAEFFV NVMPRG // ID R5X3T9_9BACT Unreviewed; 398 AA. AC R5X3T9; DT 24-JUL-2013, integrated into UniProtKB/TrEMBL. DT 24-JUL-2013, sequence version 1. DT 12-APR-2017, entry version 23. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=BN505_00524 {ECO:0000313|EMBL:CCZ99262.1}; OS Alistipes sp. CAG:157. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Rikenellaceae; OC Alistipes; environmental samples. OX NCBI_TaxID=1262692 {ECO:0000313|EMBL:CCZ99262.1, ECO:0000313|Proteomes:UP000018346}; RN [1] {ECO:0000313|EMBL:CCZ99262.1, ECO:0000313|Proteomes:UP000018346} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MGS:157 {ECO:0000313|Proteomes:UP000018346}; RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., RA Sunagawa S., Plichta D., Gautier L., Le Chatelier E., Peletier E., RA Bonde I., Nielsen T., Manichanh C., Arumugam M., Batto J., RA Santos M.B.Q.D., Blom N., Borruel N., Burgdorf K.S., Boumezbeur F., RA Casellas F., Dore J., Guarner F., Hansen T., Hildebrand F., Kaas R.S., RA Kennedy S., Kristiansen K., Kultima J.R., Leonard P., Levenez F., RA Lund O., Moumen B., Le Paslier D., Pons N., Pedersen O., Prifti E., RA Qin J., Raes J., Tap J., Tims S., Ussery D.W., Yamada T., RA MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P., Wang J., RA Brunak S., Ehrlich S.D.; RT "Dependencies among metagenomic species, viruses, plasmids and units RT of genetic variation."; RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:CCZ99262.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CBAZ010000138; CCZ99262.1; -; Genomic_DNA. DR Proteomes; UP000018346; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000018346}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000018346}. FT DOMAIN 203 387 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 164 198 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 398 AA; 45472 MW; 8C67804C0CF92EBD CRC64; METTGKEAIQ PERAVLVAVV RERQEVSQSE EYLDELEFLA ETAGITTVKR FMQKLPSPNS RTYVGPGKLE EIAAWTAENE IDVVIFDDEL SPSQTHNIEK ALGRRITDRT RLILDIFVQR AQTAYAKTQV KLAQYEYMLP RLTGMWTHLE RQRGGTGTRG GAGEREIETD RRVIRNNIAK LKEDLKKIDR QMAVQRSNRG SLVRVSLVGY TNVGKSTLMN LISKSDVFAE NKLFATLDTT VRKVVLDNLP FLLSDTVGFI RKLPTQLVES FKSTLDEVRE ADLLLHVVDI SHPNFEEQIA VVRETLREIG AGDKPVFMVF NKVDAFRYKP KEEDDLTPAT RENLSLDEIK RSWMAKGDTP CIFISAKERL NIDKLRTDLY GMVREIHAGR YPFNNFLY // ID R5XLQ3_9FIRM Unreviewed; 421 AA. AC R5XLQ3; DT 24-JUL-2013, integrated into UniProtKB/TrEMBL. DT 24-JUL-2013, sequence version 1. DT 10-MAY-2017, entry version 25. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=BN695_01645 {ECO:0000313|EMBL:CDA13424.1}; OS Anaerotruncus sp. CAG:528. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Ruminococcaceae; OC Anaerotruncus; environmental samples. OX NCBI_TaxID=1262700 {ECO:0000313|EMBL:CDA13424.1, ECO:0000313|Proteomes:UP000018024}; RN [1] {ECO:0000313|EMBL:CDA13424.1, ECO:0000313|Proteomes:UP000018024} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MGS:528 {ECO:0000313|Proteomes:UP000018024}; RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., RA Sunagawa S., Plichta D., Gautier L., Le Chatelier E., Peletier E., RA Bonde I., Nielsen T., Manichanh C., Arumugam M., Batto J., RA Santos M.B.Q.D., Blom N., Borruel N., Burgdorf K.S., Boumezbeur F., RA Casellas F., Dore J., Guarner F., Hansen T., Hildebrand F., Kaas R.S., RA Kennedy S., Kristiansen K., Kultima J.R., Leonard P., Levenez F., RA Lund O., Moumen B., Le Paslier D., Pons N., Pedersen O., Prifti E., RA Qin J., Raes J., Tap J., Tims S., Ussery D.W., Yamada T., RA MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P., Wang J., RA Brunak S., Ehrlich S.D.; RT "Dependencies among metagenomic species, viruses, plasmids and units RT of genetic variation."; RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:CDA13424.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CBBE010000060; CDA13424.1; -; Genomic_DNA. DR Proteomes; UP000018024; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000018024}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000018024}. FT DOMAIN 204 366 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 421 AA; 45986 MW; FAC597C482946EF3 CRC64; MASKLTQIKE ENEYERALLI SVDTGDFAAE ISANELTELA KTAGAEVVGI MIQKREAPSA ASYVGSGRLA EIRDFCAANE IELVIADGEL TPVQARNIEN AADARVVDRT MLILDIFAQR ARSAEGKIQV ELAQLKYSLP RLTGKGTSLS RLGGGIGTRG PGETKLETDK RHIRRRIQYL NESLQKLEKR RLAMHDRRQK NGAQAVAIVG YTNVGKSTLM NCLTKAGVLE ENKLFATLDP TARKLTLPNG EDIMLVDTVG LVRRLPHKLV DAFHSTLEEA LWADVVLNVC DASSPECNEQ IMVTNDLLAS LGCGDKPVIN VMNKCDLVPH VAEFPIIGKC VCISAKNGSG TDKLLEEISA ALPQKRRRVS LLLPFSAGKI AGELEKNGVA FSREYTESGI KMDVLAEISY LDKIKDYILP E // ID R5XM78_9FIRM Unreviewed; 413 AA. AC R5XM78; DT 24-JUL-2013, integrated into UniProtKB/TrEMBL. DT 24-JUL-2013, sequence version 1. DT 10-MAY-2017, entry version 24. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=BN537_01007 {ECO:0000313|EMBL:CDA13629.1}; OS Firmicutes bacterium CAG:212. OC Bacteria; Firmicutes; environmental samples. OX NCBI_TaxID=1263009 {ECO:0000313|EMBL:CDA13629.1, ECO:0000313|Proteomes:UP000018345}; RN [1] {ECO:0000313|EMBL:CDA13629.1, ECO:0000313|Proteomes:UP000018345} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MGS:212 {ECO:0000313|Proteomes:UP000018345}; RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., RA Sunagawa S., Plichta D., Gautier L., Le Chatelier E., Peletier E., RA Bonde I., Nielsen T., Manichanh C., Arumugam M., Batto J., RA Santos M.B.Q.D., Blom N., Borruel N., Burgdorf K.S., Boumezbeur F., RA Casellas F., Dore J., Guarner F., Hansen T., Hildebrand F., Kaas R.S., RA Kennedy S., Kristiansen K., Kultima J.R., Leonard P., Levenez F., RA Lund O., Moumen B., Le Paslier D., Pons N., Pedersen O., Prifti E., RA Qin J., Raes J., Tap J., Tims S., Ussery D.W., Yamada T., RA MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P., Wang J., RA Brunak S., Ehrlich S.D.; RT "Dependencies among metagenomic species, viruses, plasmids and units RT of genetic variation."; RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:CDA13629.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CBBF010000014; CDA13629.1; -; Genomic_DNA. DR Proteomes; UP000018345; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000018345}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000018345}. FT DOMAIN 201 365 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 160 197 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 413 AA; 46233 MW; D96C4CA6EDD0CBCB CRC64; MTMYELKEAE EKVILVGVQL NENEPAEESL DELGELAKTA GAEVVGRMIQ SREYIHPATY IGKGKITELK ELLWETDATG IICDDELTSV QLKNLEQELG CKIIDRTLLI LDIFAARAVS SEGKIQVELA QLKYRASRLI GLGNSLSRLG GGIGTRGPGE KKLEMDRRLI RERISRLKKE LREVEQHREL IRTQRKDSNL KVAALVGYTS AGKSSLENAL TGAGILEDAM LFSTLDTTTR ALELEGKQQV LLTDTVGFIR KLPHHLIEAF KSTLEEAKYA DIIIHVVDAS NPQVDTQMYV VYDTLRQLGV EGKPIITLFN KQDKLEAPQM FRDLHADYTF AVSAKTGQGL DELKGALLDI IRQDQIYVER LYDFSEAGKI QLIRKQGQLL EEEYVAEGIA VKAYVPKSIY GRI // ID R5XME9_9CLOT Unreviewed; 428 AA. AC R5XME9; DT 24-JUL-2013, integrated into UniProtKB/TrEMBL. DT 24-JUL-2013, sequence version 1. DT 10-MAY-2017, entry version 24. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=BN488_00864 {ECO:0000313|EMBL:CDA09811.1}; OS Clostridium bartlettii CAG:1329. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium; environmental samples. OX NCBI_TaxID=1263063 {ECO:0000313|EMBL:CDA09811.1, ECO:0000313|Proteomes:UP000017980}; RN [1] {ECO:0000313|EMBL:CDA09811.1, ECO:0000313|Proteomes:UP000017980} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MGS:1329 {ECO:0000313|Proteomes:UP000017980}; RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., RA Sunagawa S., Plichta D., Gautier L., Le Chatelier E., Peletier E., RA Bonde I., Nielsen T., Manichanh C., Arumugam M., Batto J., RA Santos M.B.Q.D., Blom N., Borruel N., Burgdorf K.S., Boumezbeur F., RA Casellas F., Dore J., Guarner F., Hansen T., Hildebrand F., Kaas R.S., RA Kennedy S., Kristiansen K., Kultima J.R., Leonard P., Levenez F., RA Lund O., Moumen B., Le Paslier D., Pons N., Pedersen O., Prifti E., RA Qin J., Raes J., Tap J., Tims S., Ussery D.W., Yamada T., RA MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P., Wang J., RA Brunak S., Ehrlich S.D.; RT "Dependencies among metagenomic species, viruses, plasmids and units RT of genetic variation."; RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:CDA09811.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CBBD010000025; CDA09811.1; -; Genomic_DNA. DR Proteomes; UP000017980; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000017980}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000017980}. FT DOMAIN 203 373 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 169 196 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 428 AA; 48760 MW; 2941133434F21C7E CRC64; MEEQLQEKAV LVGLNITTNV KKIDDIDINE SMAELKELVK AAGAEVLASV IQNKPARDAA YFIGKGKVEE IRDYCNMLGA TMIVFNDELS GAHMRNIEDV TGLKVIDRTA LILDIFAQRA LSKEGKLQVE LAQLKYRLPR LYGMGGQMSR TGAGIGTRGP GEQKLEVDKR HILNRAADIR KELREVKQNR ETQRVQRLKS NIPIVALVGY TNAGKSTLLN ELIKTHKDYE TEKEVFVKDM LFATLDVTLR KATLPNKRDF LVVDTVGFVS KLPHDLVEAF KATLEEVKYA DLILHVIDAT NSSFELQKQT TESVLKELGA DDKKTIIVYN KIDRLELDIY PRNREDRIYI SAKKGINMDI LLKMIENALM EDTYQVKLLL PYDKGNIFSR IKEKYNVDSF EYVENGTQLE VSLDEEDYNV YKEYIIEE // ID R5Y0F4_9PROT Unreviewed; 419 AA. AC R5Y0F4; DT 24-JUL-2013, integrated into UniProtKB/TrEMBL. DT 24-JUL-2013, sequence version 1. DT 12-APR-2017, entry version 24. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=BN575_00831 {ECO:0000313|EMBL:CDA18259.1}; OS Acetobacter sp. CAG:267. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales; OC Acetobacteraceae; Acetobacter; environmental samples. OX NCBI_TaxID=1262684 {ECO:0000313|EMBL:CDA18259.1, ECO:0000313|Proteomes:UP000017992}; RN [1] {ECO:0000313|EMBL:CDA18259.1, ECO:0000313|Proteomes:UP000017992} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MGS:267 {ECO:0000313|Proteomes:UP000017992}; RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., RA Sunagawa S., Plichta D., Gautier L., Le Chatelier E., Peletier E., RA Bonde I., Nielsen T., Manichanh C., Arumugam M., Batto J., RA Santos M.B.Q.D., Blom N., Borruel N., Burgdorf K.S., Boumezbeur F., RA Casellas F., Dore J., Guarner F., Hansen T., Hildebrand F., Kaas R.S., RA Kennedy S., Kristiansen K., Kultima J.R., Leonard P., Levenez F., RA Lund O., Moumen B., Le Paslier D., Pons N., Pedersen O., Prifti E., RA Qin J., Raes J., Tap J., Tims S., Ussery D.W., Yamada T., RA MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P., Wang J., RA Brunak S., Ehrlich S.D.; RT "Dependencies among metagenomic species, viruses, plasmids and units RT of genetic variation."; RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:CDA18259.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CBBH010000097; CDA18259.1; -; Genomic_DNA. DR Proteomes; UP000017992; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000017992}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000017992}. FT DOMAIN 207 379 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 419 AA; 46714 MW; F003374D07480360 CRC64; MLEIEKDRKT KTAVICPVIK TAAGMMTAEE EAARENEAVG LVLAMGQEVV FCETVRMSAI VPKSFFGKGT LERLKTACEE KGAELLVVDM PVSAVQQRNL EKMLNMKVID RTAVILEIFG QRAQTREGKL QVELAHLTYQ RGRLVRSWTH LERQRGGGGF LGGPGETQIE LDRRHLDERI VKIKKELEKV RQTRSIQRAA RVKVPYPVAA LVGYTNAGKS TLFNLITKAD VFAKDMLFAT LDPTLRKIEL RKGQDIIVSD TVGFISNLPH ELVMAFRATL EEVLEADVIV HVIDASNPDC KTQRQDVLDV LHELGLSKIE HEPNYIEVFN KTDKLDAAAK ARLAERISGN TSAAAVSALS GEGTERLMQL LREKICAKGE LKTVSVPVGD GKRLAEVYRT AEVLERRDDG ERIYLRVRC // ID R5YHH2_9FIRM Unreviewed; 414 AA. AC R5YHH2; DT 24-JUL-2013, integrated into UniProtKB/TrEMBL. DT 24-JUL-2013, sequence version 1. DT 12-APR-2017, entry version 23. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=BN528_01088 {ECO:0000313|EMBL:CDA24199.1}; OS Roseburia sp. CAG:197. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Lachnospiraceae; OC Roseburia; environmental samples. OX NCBI_TaxID=1262943 {ECO:0000313|EMBL:CDA24199.1, ECO:0000313|Proteomes:UP000018336}; RN [1] {ECO:0000313|EMBL:CDA24199.1, ECO:0000313|Proteomes:UP000018336} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MGS:197 {ECO:0000313|Proteomes:UP000018336}; RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., RA Sunagawa S., Plichta D., Gautier L., Le Chatelier E., Peletier E., RA Bonde I., Nielsen T., Manichanh C., Arumugam M., Batto J., RA Santos M.B.Q.D., Blom N., Borruel N., Burgdorf K.S., Boumezbeur F., RA Casellas F., Dore J., Guarner F., Hansen T., Hildebrand F., Kaas R.S., RA Kennedy S., Kristiansen K., Kultima J.R., Leonard P., Levenez F., RA Lund O., Moumen B., Le Paslier D., Pons N., Pedersen O., Prifti E., RA Qin J., Raes J., Tap J., Tims S., Ussery D.W., Yamada T., RA MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P., Wang J., RA Brunak S., Ehrlich S.D.; RT "Dependencies among metagenomic species, viruses, plasmids and units RT of genetic variation."; RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:CDA24199.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CBBL010000051; CDA24199.1; -; Genomic_DNA. DR Proteomes; UP000018336; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000018336}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000018336}. FT DOMAIN 202 366 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 161 195 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 414 AA; 46346 MW; 6BC8CC3A52682C39 CRC64; MAKPQEIEEI EEKVILVGVS EQEGDDAEDS VTELAELVKT AGATVVGTLI QKRETIHPGT YVGTGKVEEI AQLIAQTGAT GIVCDDELSP AQLRNLENML DTKVMDRTLI ILDIFAARAT TSEGKIQVEL AQLKYRLSRL SGLGKTMSRL GGGIGTRGPG EKKLEIDRRL INDRIAQLNR ELKEVVKHRE ITRAKRAKSE VPVVAIVGYT NAGKSTLLNH LTDAEVLEED KLFATLDPTT RMLELDGHQQ VLLTDTVGFI RKLPHHLIEA FKSTLEEAKY ADYIFHVVDA SNPQMDKQMH IVYETLDHLG VKNKKMVTLF NKMDQRTEEE PLQDFRADHI LQISAANNQG LDEIKALLQE MLREDKVYIE RVIPYAQAGI IQLVREKGEL VSEEYVPEGI EIKAYVPMEV YGKL // ID R5Z744_9FIRM Unreviewed; 413 AA. AC R5Z744; DT 24-JUL-2013, integrated into UniProtKB/TrEMBL. DT 24-JUL-2013, sequence version 1. DT 12-APR-2017, entry version 23. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=BN504_01468 {ECO:0000313|EMBL:CDA29966.1}; OS Eubacterium sp. CAG:156. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Eubacteriaceae; OC Eubacterium; environmental samples. OX NCBI_TaxID=1262880 {ECO:0000313|EMBL:CDA29966.1, ECO:0000313|Proteomes:UP000018124}; RN [1] {ECO:0000313|EMBL:CDA29966.1, ECO:0000313|Proteomes:UP000018124} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MGS:156 {ECO:0000313|Proteomes:UP000018124}; RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., RA Sunagawa S., Plichta D., Gautier L., Le Chatelier E., Peletier E., RA Bonde I., Nielsen T., Manichanh C., Arumugam M., Batto J., RA Santos M.B.Q.D., Blom N., Borruel N., Burgdorf K.S., Boumezbeur F., RA Casellas F., Dore J., Guarner F., Hansen T., Hildebrand F., Kaas R.S., RA Kennedy S., Kristiansen K., Kultima J.R., Leonard P., Levenez F., RA Lund O., Moumen B., Le Paslier D., Pons N., Pedersen O., Prifti E., RA Qin J., Raes J., Tap J., Tims S., Ussery D.W., Yamada T., RA MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P., Wang J., RA Brunak S., Ehrlich S.D.; RT "Dependencies among metagenomic species, viruses, plasmids and units RT of genetic variation."; RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:CDA29966.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CBBN010000117; CDA29966.1; -; Genomic_DNA. DR Proteomes; UP000018124; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000018124}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000018124}. FT DOMAIN 201 365 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 160 194 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 413 AA; 46482 MW; 8A613C2BFEA5EFB5 CRC64; MAKLIENKEE IEKVILVAVS LDDSNDADES LDELEELVNT AGAQVVGRTI QNREAVHPGT YVGKGKVEEL KDLIWETQAT AIVCDDELTP AQYKNLEDEL NVKVMDITLI ILDIFAGRAK TAEGKIQVEL AQLRYRSSRL IGMKNLSRQG GGIGTRGPGE KKLEVDRRLI RDRISQLKAE VKDMEAHRNV TRAKRSQNPV PVAAIVGYTN AGKSTLLNTL TDAKVLEEDK LFATLDPTTR NYKLPDGQEI LLTDTVGFIR KLPHHLIDAF RSTLEEAKYS DIIIHVIDSS NPQMDKNIHA VYETLEQLDV KDKIIITVFN KQDRLENKPI LRDFKADYIV NAAIKNKVGI EELNDAISKA LKSMRVHIEK VFSYADAGKP GLIRKYGQLL KEEYRDDGIY VEAYVPSEMM DRL // ID R6AHU5_9BACT Unreviewed; 418 AA. AC R6AHU5; DT 24-JUL-2013, integrated into UniProtKB/TrEMBL. DT 24-JUL-2013, sequence version 1. DT 12-APR-2017, entry version 23. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=BN693_00485 {ECO:0000313|EMBL:CDA46116.1}; OS Prevotella sp. CAG:5226. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Prevotellaceae; OC Prevotella; environmental samples. OX NCBI_TaxID=1262930 {ECO:0000313|EMBL:CDA46116.1, ECO:0000313|Proteomes:UP000018184}; RN [1] {ECO:0000313|EMBL:CDA46116.1, ECO:0000313|Proteomes:UP000018184} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MGS:5226 {ECO:0000313|Proteomes:UP000018184}; RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., RA Sunagawa S., Plichta D., Gautier L., Le Chatelier E., Peletier E., RA Bonde I., Nielsen T., Manichanh C., Arumugam M., Batto J., RA Santos M.B.Q.D., Blom N., Borruel N., Burgdorf K.S., Boumezbeur F., RA Casellas F., Dore J., Guarner F., Hansen T., Hildebrand F., Kaas R.S., RA Kennedy S., Kristiansen K., Kultima J.R., Leonard P., Levenez F., RA Lund O., Moumen B., Le Paslier D., Pons N., Pedersen O., Prifti E., RA Qin J., Raes J., Tap J., Tims S., Ussery D.W., Yamada T., RA MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P., Wang J., RA Brunak S., Ehrlich S.D.; RT "Dependencies among metagenomic species, viruses, plasmids and units RT of genetic variation."; RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:CDA46116.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CBBW010000271; CDA46116.1; -; Genomic_DNA. DR Proteomes; UP000018184; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000018184}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000018184}. FT DOMAIN 217 401 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 418 AA; 47745 MW; BF7DA9BCBE0970BF CRC64; MQGFIETEEI KAETAILVGL ITKNQNERKT NEYLDELQFL AETAGAVTVK RFTQKLDGPS SVTYVGKGKL EEIRAYIEAE EDAEREIGMV IFDDELSAKQ LRNIERALGV KILDRTNLIL DIFAMRAQTA NAKTQVELAQ YRYMLPRLQR LWTHLERQGG GSGSGGGKGS VGLRGPGETQ LEMDRRIILN RMALLKQRLA DIDRQKSTQR KNRGRLIRVA LVGYTNVGKS TLINLLAKTD VFAENKLFAT LDTTVRKVII DNLPFLLADT VGFIRKLPTD LVESFKSTLD EVREADLLVH VVDVSHPDFM EQIEVVNNTL RDLGCAEKPQ LLVFNKMDAY TWTEKDPDDL TPATRENVSL DELKHTWMAK MGDDCIFISA RERQNIDELK ELFYARVKQL HVQKYPYNDF LFEHYEQQ // ID R6AWK8_9CLOT Unreviewed; 593 AA. AC R6AWK8; DT 24-JUL-2013, integrated into UniProtKB/TrEMBL. DT 24-JUL-2013, sequence version 1. DT 12-APR-2017, entry version 23. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=BN491_01366 {ECO:0000313|EMBL:CDA53209.1}; OS Clostridium sp. CAG:138. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium; environmental samples. OX NCBI_TaxID=1262775 {ECO:0000313|EMBL:CDA53209.1, ECO:0000313|Proteomes:UP000017905}; RN [1] {ECO:0000313|EMBL:CDA53209.1, ECO:0000313|Proteomes:UP000017905} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MGS:138 {ECO:0000313|Proteomes:UP000017905}; RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., RA Sunagawa S., Plichta D., Gautier L., Le Chatelier E., Peletier E., RA Bonde I., Nielsen T., Manichanh C., Arumugam M., Batto J., RA Santos M.B.Q.D., Blom N., Borruel N., Burgdorf K.S., Boumezbeur F., RA Casellas F., Dore J., Guarner F., Hansen T., Hildebrand F., Kaas R.S., RA Kennedy S., Kristiansen K., Kultima J.R., Leonard P., Levenez F., RA Lund O., Moumen B., Le Paslier D., Pons N., Pedersen O., Prifti E., RA Qin J., Raes J., Tap J., Tims S., Ussery D.W., Yamada T., RA MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P., Wang J., RA Brunak S., Ehrlich S.D.; RT "Dependencies among metagenomic species, viruses, plasmids and units RT of genetic variation."; RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:CDA53209.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CBBZ010000097; CDA53209.1; -; Genomic_DNA. DR Proteomes; UP000017905; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000017905}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000017905}. FT DOMAIN 377 539 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 336 363 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 593 AA; 65295 MW; B597FA24D21046DE CRC64; MANKPNGNLT GIKSAMLDRL NSLYDFKQGL DEFASFELLS ELCACSGEIN REISVYISRD GSIVDVSVGD SAKVSMPSMR LVRNEDRLCG VRCIHTHPSG DGRLSGVDLG TLRSMKLDCM AAVGVSDGKP TQLYAAYLGD FDEDTGSRAA LVYGPMRPYK LPQKALIAEI FNSDDRFRST TKEVEAVEQE RAVLVGMDND EGYDTLEELN ELAKTAGALV VGKVRVRRRT IDNATYVGSG KANELSLMGS ELEADLFIFD DELSAIQLRT LEEILGARVI DRTTLILDIF AARATSREGK LQVELAQMRY RLPRLIGQGQ VLSRLGGGIG TRGPGEKKLE IDRRRIRRRV FELETELSEI EKQRGLRRES RKANRVPLVA LVGYTNAGKS TMLNALTDSN VLAEDKLFAT LDPVVRKITL SGGTEALLSD TVGFINKLPH DLVEAFKSTL EEVSNSDLIL QVVDISCPYH EKQMRVVDGV LESLHAADIP RIIVFNKADA IASCDLPAES ENRINVSALR GTGIEKLLSA VELKLNSART EVDILVPYSK YEAVSMIRDR GMLLSEEHTE AGTHIRALLD AESIGQLRKI LDF // ID R6BAH3_9BACT Unreviewed; 415 AA. AC R6BAH3; DT 24-JUL-2013, integrated into UniProtKB/TrEMBL. DT 24-JUL-2013, sequence version 1. DT 12-APR-2017, entry version 22. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=BN731_00389 {ECO:0000313|EMBL:CDA57884.1}; OS Prevotella sp. CAG:604. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Prevotellaceae; OC Prevotella; environmental samples. OX NCBI_TaxID=1262932 {ECO:0000313|EMBL:CDA57884.1, ECO:0000313|Proteomes:UP000018295}; RN [1] {ECO:0000313|EMBL:CDA57884.1, ECO:0000313|Proteomes:UP000018295} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MGS:604 {ECO:0000313|Proteomes:UP000018295}; RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., RA Sunagawa S., Plichta D., Gautier L., Le Chatelier E., Peletier E., RA Bonde I., Nielsen T., Manichanh C., Arumugam M., Batto J., RA Santos M.B.Q.D., Blom N., Borruel N., Burgdorf K.S., Boumezbeur F., RA Casellas F., Dore J., Guarner F., Hansen T., Hildebrand F., Kaas R.S., RA Kennedy S., Kristiansen K., Kultima J.R., Leonard P., Levenez F., RA Lund O., Moumen B., Le Paslier D., Pons N., Pedersen O., Prifti E., RA Qin J., Raes J., Tap J., Tims S., Ussery D.W., Yamada T., RA MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P., Wang J., RA Brunak S., Ehrlich S.D.; RT "Dependencies among metagenomic species, viruses, plasmids and units RT of genetic variation."; RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:CDA57884.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CBCB010000193; CDA57884.1; -; Genomic_DNA. DR Proteomes; UP000018295; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000018295}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000018295}. FT DOMAIN 216 400 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 415 AA; 47698 MW; D45940CC149A86E4 CRC64; MKEFVISEVK AETAVLVGLV TKTQDEAKTK EYLDELEFLA DTAGAVTVKR FTQKVISPNQ TTYVGKGKLE EIKQYIKEEE EEDREIGMVI FDDELSAKQI RNIEQELQVK ILDRTSLILD IFAMRAQTAA AKTQVELAQY RYMLPRLQRL WTHLERQGGG SGSGGGKGSV GLRGPGETQL EMDRRIILGR MSLLKERLAE IDKQKTTQRK NRGRLIRVAL VGYTNVGKST IMNLLSKSEV FAENKLFATL DTTVRKVVVE NLPFLLADTV GFIRKLPTDL VDSFKSTLDE TREADLLLHV VDISHPDFEE QIQVVEKTLE ELGCSDKPSM IIFNKIDNYT WVEKEEDDLT PMEKENIPLE DLKKTWMAKL HDDCLFISAK NKDNIDEFRE VLYKKVRELH VQKYPYNDFL YQDYE // ID R6BME5_9CLOT Unreviewed; 415 AA. AC R6BME5; DT 24-JUL-2013, integrated into UniProtKB/TrEMBL. DT 24-JUL-2013, sequence version 1. DT 12-APR-2017, entry version 23. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=BN513_01776 {ECO:0000313|EMBL:CDA62089.1}; OS Clostridium sp. CAG:169. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium; environmental samples. OX NCBI_TaxID=1262778 {ECO:0000313|EMBL:CDA62089.1, ECO:0000313|Proteomes:UP000018302}; RN [1] {ECO:0000313|EMBL:CDA62089.1, ECO:0000313|Proteomes:UP000018302} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MGS:169 {ECO:0000313|Proteomes:UP000018302}; RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., RA Sunagawa S., Plichta D., Gautier L., Le Chatelier E., Peletier E., RA Bonde I., Nielsen T., Manichanh C., Arumugam M., Batto J., RA Santos M.B.Q.D., Blom N., Borruel N., Burgdorf K.S., Boumezbeur F., RA Casellas F., Dore J., Guarner F., Hansen T., Hildebrand F., Kaas R.S., RA Kennedy S., Kristiansen K., Kultima J.R., Leonard P., Levenez F., RA Lund O., Moumen B., Le Paslier D., Pons N., Pedersen O., Prifti E., RA Qin J., Raes J., Tap J., Tims S., Ussery D.W., Yamada T., RA MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P., Wang J., RA Brunak S., Ehrlich S.D.; RT "Dependencies among metagenomic species, viruses, plasmids and units RT of genetic variation."; RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:CDA62089.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CBCF010000183; CDA62089.1; -; Genomic_DNA. DR Proteomes; UP000018302; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000018302}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000018302}. FT DOMAIN 198 359 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 157 191 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 415 AA; 46052 MW; F6BEF71673E231F9 CRC64; MYENKQEEQT AVLAAIDTGE YDAQRSMDEL EELAKSAGAK VMGRVIQKKD RPDPATLMGS GRVEELAEFV QNSQVELVIF DHELSPAQQK NLENALGAAV IDRTTLILDI FAQRAKTSEG RLQVELAQLK YRLPRLAGQG TSLSRLGGGI GTRGPGESKL ESDRRHIRRR IHALEEELEA LEKRRGLLRQ RRKKDDVVTI AIVGYTNVGK STLLNTLTDA GVLAKDMLFA TLDPTSRALD LPDGRRVMLI DTVGLVSRLP HQLVQAFHST LEEAADADLV LNVCDVSSPE FDQQLEVTTG LLKELGAENV PVLTVLNKCD KLPELPLTLD RKTAAISAKT GMGLEKLLEK VALNLPQTHQ HLHLLIPYDK SGLIGEIRQT GKVYTEEYRE DGTYLDANVE LKLCHRVQEY ILLNE // ID R6C9W1_9CLOT Unreviewed; 421 AA. AC R6C9W1; DT 24-JUL-2013, integrated into UniProtKB/TrEMBL. DT 24-JUL-2013, sequence version 1. DT 12-APR-2017, entry version 22. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=BN687_01604 {ECO:0000313|EMBL:CDA69704.1}; OS Clostridium sp. CAG:510. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium; environmental samples. OX NCBI_TaxID=1262816 {ECO:0000313|EMBL:CDA69704.1, ECO:0000313|Proteomes:UP000018120}; RN [1] {ECO:0000313|EMBL:CDA69704.1, ECO:0000313|Proteomes:UP000018120} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MGS:510 {ECO:0000313|Proteomes:UP000018120}; RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., RA Sunagawa S., Plichta D., Gautier L., Le Chatelier E., Peletier E., RA Bonde I., Nielsen T., Manichanh C., Arumugam M., Batto J., RA Santos M.B.Q.D., Blom N., Borruel N., Burgdorf K.S., Boumezbeur F., RA Casellas F., Dore J., Guarner F., Hansen T., Hildebrand F., Kaas R.S., RA Kennedy S., Kristiansen K., Kultima J.R., Leonard P., Levenez F., RA Lund O., Moumen B., Le Paslier D., Pons N., Pedersen O., Prifti E., RA Qin J., Raes J., Tap J., Tims S., Ussery D.W., Yamada T., RA MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P., Wang J., RA Brunak S., Ehrlich S.D.; RT "Dependencies among metagenomic species, viruses, plasmids and units RT of genetic variation."; RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:CDA69704.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CBCI010000125; CDA69704.1; -; Genomic_DNA. DR Proteomes; UP000018120; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000018120}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000018120}. FT DOMAIN 199 329 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 158 192 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 421 AA; 47762 MW; 968DC6CF1CE2C371 CRC64; MEDIREKVIL VGVDTGVADD YDVCMQELKS LAEACHMQVV GILTQKMEAA NKALYIGTGK VEELRELAKM TDAELIVFED SLTPSQLRNL KDECKLPVMD RTNLILDIFA SRAKTREAKL QVEVARLKYL LPRLVGLHDA LSRQGGASGS MSNKGAGEKK LELDRRKIEH RITELSKELE TVSTERRTQR KRRRNSGIPQ VSLAGYTNAG KSTLLNKFVD TYGLPEEKKV LEKDMLFATL ETAVRKIDDG SRKPFYLADT VGFINNLPHG LVKAFRSTLE EIKEADLILQ VIDFSDVNYK KHMEVTEETL KELDAGHIPV IYVYNKADLC MPEIPRCTDN RIYMSAQDET CIRTLLTLVT DTLYAHRIET EFLIPYDKGG IVSELRENAE VLSQDYIENG VRLVVKCSEK EQSKFRMYIS E // ID R6CGX6_9FIRM Unreviewed; 415 AA. AC R6CGX6; DT 24-JUL-2013, integrated into UniProtKB/TrEMBL. DT 24-JUL-2013, sequence version 1. DT 12-APR-2017, entry version 24. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=BN708_00089 {ECO:0000313|EMBL:CDA64507.1}; OS Firmicutes bacterium CAG:56. OC Bacteria; Firmicutes; environmental samples. OX NCBI_TaxID=1263031 {ECO:0000313|EMBL:CDA64507.1, ECO:0000313|Proteomes:UP000018123}; RN [1] {ECO:0000313|EMBL:CDA64507.1, ECO:0000313|Proteomes:UP000018123} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MGS:56 {ECO:0000313|Proteomes:UP000018123}; RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., RA Sunagawa S., Plichta D., Gautier L., Le Chatelier E., Peletier E., RA Bonde I., Nielsen T., Manichanh C., Arumugam M., Batto J., RA Santos M.B.Q.D., Blom N., Borruel N., Burgdorf K.S., Boumezbeur F., RA Casellas F., Dore J., Guarner F., Hansen T., Hildebrand F., Kaas R.S., RA Kennedy S., Kristiansen K., Kultima J.R., Leonard P., Levenez F., RA Lund O., Moumen B., Le Paslier D., Pons N., Pedersen O., Prifti E., RA Qin J., Raes J., Tap J., Tims S., Ussery D.W., Yamada T., RA MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P., Wang J., RA Brunak S., Ehrlich S.D.; RT "Dependencies among metagenomic species, viruses, plasmids and units RT of genetic variation."; RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:CDA64507.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CBCG010000357; CDA64507.1; -; Genomic_DNA. DR Proteomes; UP000018123; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000018123}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000018123}. FT DOMAIN 201 365 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 415 AA; 46466 MW; 389701F4B9C7D5B5 CRC64; MQPYDMKELE ERVIMVGVQE SFSEDVEESL DELAELCETA GALVVGRVIQ NREKIHPGTY VGKGKIEEIA LLMEELGATG IVCDDELSPA QLNNLEKELD CKVMDRTLII LDIFAARANT SEGNIQVELA QLRYRAARLV GLRNSLSRLG GGIGTRGPGE KKLEMDRRLI HARISQLKAE LAQVQKHREL IRSKRKKDQM VVAAIVGYTN AGKSTLLNTL TDAGVLEEDK LFATLDPTTR LLELPGGQNI LLTDTVGFIR KLPHHLIEAF KSTLEEAKYA DIIIHVVDAS NPQKEKQMHV VYETLKDLGV KDQPILTLFN KQDRIENPEI LKDMKADKTL KISAKTGQGL DDLKDELEKI LRARSILLER VFPYEKAGLI QIVRAKGQLL EEEYRGDGIY VKAFVPAEIY GKVAY // ID R6CHE2_9FIRM Unreviewed; 427 AA. AC R6CHE2; DT 24-JUL-2013, integrated into UniProtKB/TrEMBL. DT 24-JUL-2013, sequence version 1. DT 12-APR-2017, entry version 23. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=BN718_01136 {ECO:0000313|EMBL:CDA72289.1}; OS Ruminococcus sp. CAG:579. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Ruminococcaceae; OC Ruminococcus; environmental samples. OX NCBI_TaxID=1262963 {ECO:0000313|EMBL:CDA72289.1, ECO:0000313|Proteomes:UP000018387}; RN [1] {ECO:0000313|EMBL:CDA72289.1, ECO:0000313|Proteomes:UP000018387} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MGS:579 {ECO:0000313|Proteomes:UP000018387}; RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., RA Sunagawa S., Plichta D., Gautier L., Le Chatelier E., Peletier E., RA Bonde I., Nielsen T., Manichanh C., Arumugam M., Batto J., RA Santos M.B.Q.D., Blom N., Borruel N., Burgdorf K.S., Boumezbeur F., RA Casellas F., Dore J., Guarner F., Hansen T., Hildebrand F., Kaas R.S., RA Kennedy S., Kristiansen K., Kultima J.R., Leonard P., Levenez F., RA Lund O., Moumen B., Le Paslier D., Pons N., Pedersen O., Prifti E., RA Qin J., Raes J., Tap J., Tims S., Ussery D.W., Yamada T., RA MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P., Wang J., RA Brunak S., Ehrlich S.D.; RT "Dependencies among metagenomic species, viruses, plasmids and units RT of genetic variation."; RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:CDA72289.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CBCK010000060; CDA72289.1; -; Genomic_DNA. DR Proteomes; UP000018387; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000018387}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000018387}. FT DOMAIN 198 361 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 157 191 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 427 AA; 46475 MW; D5DDBC9C8244173F CRC64; MFETEIKLPR VILCAVDTGE YDAEASMNEL AELARTAGAE VAARVVQKRP VIDNATCIGS GRLAELKELC QNENADQVIF DCELTASQVR NIEDVIGVHT IDRTTLILDI FAQRAVTREG RLQVELAQYK YRLPRLAGMG VSLSRLGGGI GTRGPGETKL ETDKRHIRSR IQKLSEELKE IEKRRGLARS HRKKTGVPVC AVVGYTNAGK STLLNTLTDA DVLAEDKLFA TLETTSRAVT LPDDREIIMA DTVGFISRLP HNLVEAFKST LEEAANADVI IHLCDASDPE CHEKSNVTLK LLEELGCSDI PVITAFNKCD LVPELCEALS HEPQSVLISA KSGAGTDKLL AAVAEALGEN CVSGRFLFPF DKGGVLARVR ELGGVKNEEY TAEGIAADIR LDKKYIGLLE QAAKPLSADK HDEKVSE // ID R6CPN5_9BACT Unreviewed; 415 AA. AC R6CPN5; DT 24-JUL-2013, integrated into UniProtKB/TrEMBL. DT 24-JUL-2013, sequence version 1. DT 12-APR-2017, entry version 23. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=BN510_00387 {ECO:0000313|EMBL:CDA67187.1}; OS Prevotella copri CAG:164. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Prevotellaceae; OC Prevotella; environmental samples. OX NCBI_TaxID=1263102 {ECO:0000313|EMBL:CDA67187.1, ECO:0000313|Proteomes:UP000018361}; RN [1] {ECO:0000313|EMBL:CDA67187.1, ECO:0000313|Proteomes:UP000018361} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MGS:164 {ECO:0000313|Proteomes:UP000018361}; RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., RA Sunagawa S., Plichta D., Gautier L., Le Chatelier E., Peletier E., RA Bonde I., Nielsen T., Manichanh C., Arumugam M., Batto J., RA Santos M.B.Q.D., Blom N., Borruel N., Burgdorf K.S., Boumezbeur F., RA Casellas F., Dore J., Guarner F., Hansen T., Hildebrand F., Kaas R.S., RA Kennedy S., Kristiansen K., Kultima J.R., Leonard P., Levenez F., RA Lund O., Moumen B., Le Paslier D., Pons N., Pedersen O., Prifti E., RA Qin J., Raes J., Tap J., Tims S., Ussery D.W., Yamada T., RA MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P., Wang J., RA Brunak S., Ehrlich S.D.; RT "Dependencies among metagenomic species, viruses, plasmids and units RT of genetic variation."; RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:CDA67187.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CBCH010000224; CDA67187.1; -; Genomic_DNA. DR Proteomes; UP000018361; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000018361}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000018361}. FT DOMAIN 216 400 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 415 AA; 47692 MW; 2E72DD269E8C54D2 CRC64; MKEFVISEVK AETAVLVGLI TKTQDEAKTK EYLDELEFLA DTAGAVTVKR FTQKVVSPNQ TTYVGKGKLE EIKEYIKNEE EEDREVGMVI FDDELSAKQI RNIEQELQVK ILDRTSLILD IFAMRAQTAA AKTQVELAQY RYMLPRLQRL WTHLERQGGG SGSGGGKGSV GLRGPGETQL EMDRRIILGR MSLLKERLAE IDKQKTTQRK NRGRMVRVAL VGYTNVGKST IMNLLSKSEV FAENKLFATL DTTVRKVVVD NLPFLLADTV GFIRKLPTDL VDSFKSTLDE TREADLLLHV VDISHPDFEE QIQVVENTLK ELDCADKPSM IIFNKIDNYS WVEKEEDDLT PMEKENIPLE DLKKTWMAKL NEDCLFISAK NKENIDEFRE ILYKKVRELH VQKYPYNDFL YQDYE // ID R6CUV0_9CLOT Unreviewed; 416 AA. AC R6CUV0; DT 24-JUL-2013, integrated into UniProtKB/TrEMBL. DT 24-JUL-2013, sequence version 1. DT 12-APR-2017, entry version 23. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=BN558_00129 {ECO:0000313|EMBL:CDA76584.1}; OS Clostridium sp. CAG:242. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium; environmental samples. OX NCBI_TaxID=1262783 {ECO:0000313|EMBL:CDA76584.1, ECO:0000313|Proteomes:UP000017919}; RN [1] {ECO:0000313|EMBL:CDA76584.1, ECO:0000313|Proteomes:UP000017919} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MGS:242 {ECO:0000313|Proteomes:UP000017919}; RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., RA Sunagawa S., Plichta D., Gautier L., Le Chatelier E., Peletier E., RA Bonde I., Nielsen T., Manichanh C., Arumugam M., Batto J., RA Santos M.B.Q.D., Blom N., Borruel N., Burgdorf K.S., Boumezbeur F., RA Casellas F., Dore J., Guarner F., Hansen T., Hildebrand F., Kaas R.S., RA Kennedy S., Kristiansen K., Kultima J.R., Leonard P., Levenez F., RA Lund O., Moumen B., Le Paslier D., Pons N., Pedersen O., Prifti E., RA Qin J., Raes J., Tap J., Tims S., Ussery D.W., Yamada T., RA MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P., Wang J., RA Brunak S., Ehrlich S.D.; RT "Dependencies among metagenomic species, viruses, plasmids and units RT of genetic variation."; RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:CDA76584.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CBCM010000057; CDA76584.1; -; Genomic_DNA. DR Proteomes; UP000017919; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000017919}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000017919}. FT DOMAIN 198 359 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 157 191 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 416 AA; 46302 MW; 9B4C1DB93A0DD1CA CRC64; MYENKEKQQT ALLAAVDTGE FDAQRSVDEL EELAKSAGAV VKGRVIQRKE RPDPATLMGA GRLEEVAEFV RANEIDLVIF DHELAPAQQK NLENTLDVAV IDRTTLILDI FAQRAKTSEG RLQVELAQLK YRLPRLSGLG TSLSRLGGGI GTRGPGESKL ESDRRHIRRR IHSLEEELKE LEKRRGLLRQ RRKKDDVISV AIVGYTNVGK STLLNTLTDA GVLAKDMLFA TLDPTSRALT LPDGRKVMLI DTVGLVSRLP HQLVQAFHST LEEAVDADLI LNVCDVSSPE FDQQLEVTTG LLRELGAENV PVLTVLNKCD KLPELPMTLN KSTAAISAKT GMGLEKLLEK IVLNLPETHR HLHLLIPYDK SGLIGEIRQS GKVYTEEYRE DGTFLDANVD LKICHRIQDY ILLNEE // ID R6CXT8_9BACE Unreviewed; 418 AA. AC R6CXT8; DT 24-JUL-2013, integrated into UniProtKB/TrEMBL. DT 24-JUL-2013, sequence version 1. DT 12-APR-2017, entry version 23. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=BN697_00900 {ECO:0000313|EMBL:CDA77699.1}; OS Bacteroides sp. CAG:530. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae; OC Bacteroides; environmental samples. OX NCBI_TaxID=1262741 {ECO:0000313|EMBL:CDA77699.1, ECO:0000313|Proteomes:UP000018392}; RN [1] {ECO:0000313|EMBL:CDA77699.1, ECO:0000313|Proteomes:UP000018392} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MGS:530 {ECO:0000313|Proteomes:UP000018392}; RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., RA Sunagawa S., Plichta D., Gautier L., Le Chatelier E., Peletier E., RA Bonde I., Nielsen T., Manichanh C., Arumugam M., Batto J., RA Santos M.B.Q.D., Blom N., Borruel N., Burgdorf K.S., Boumezbeur F., RA Casellas F., Dore J., Guarner F., Hansen T., Hildebrand F., Kaas R.S., RA Kennedy S., Kristiansen K., Kultima J.R., Leonard P., Levenez F., RA Lund O., Moumen B., Le Paslier D., Pons N., Pedersen O., Prifti E., RA Qin J., Raes J., Tap J., Tims S., Ussery D.W., Yamada T., RA MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P., Wang J., RA Brunak S., Ehrlich S.D.; RT "Dependencies among metagenomic species, viruses, plasmids and units RT of genetic variation."; RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:CDA77699.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CBCL010000164; CDA77699.1; -; Genomic_DNA. DR Proteomes; UP000018392; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000018392}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000018392}. FT DOMAIN 217 401 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 418 AA; 47649 MW; B7A006D4BD0055B5 CRC64; MKEFVISEAQ TEKAVLVGLI TQTQSERKTN EYLDELAFLA ETAGAEVVQR FTQKLDFPNK VTYVGKGKLQ ELKEYLSVQN ESEETEIGMV IFDDELSAKQ IRNIESELKV KILDRTSLIL DIFAMRAQTA NAKTQVELAQ YKYMLPRLQR LWTHLERQGG GSGAGGGKGS VGLRGPGETQ LEMDRRIILN RMALLKQRLA DIDTQKSTQR KNRGRLIRVA LVGYTNVGKS TLMNLLAKSE VFAENKLFAT LDTTVRKVII ENLPFLLSDT VGFIRKLPTD LVDSFKSTLD EVREADLLIH VVDISHPDFE EQIQVVEKTI ADLGAGGKPT MLVFNKIDAY TYVEKAEDDL TPKTKENITL EELMNTWMAK MNDNCIFISA KQKTNIDELK ERVYKKVREL HVQKYPYNDF LYQTYEEE // ID R6D9P2_9FIRM Unreviewed; 435 AA. AC R6D9P2; DT 24-JUL-2013, integrated into UniProtKB/TrEMBL. DT 24-JUL-2013, sequence version 1. DT 12-APR-2017, entry version 23. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=BN516_00926 {ECO:0000313|EMBL:CDA80896.1}; OS Firmicutes bacterium CAG:176. OC Bacteria; Firmicutes; environmental samples. OX NCBI_TaxID=1263007 {ECO:0000313|EMBL:CDA80896.1, ECO:0000313|Proteomes:UP000017932}; RN [1] {ECO:0000313|EMBL:CDA80896.1, ECO:0000313|Proteomes:UP000017932} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MGS:176 {ECO:0000313|Proteomes:UP000017932}; RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., RA Sunagawa S., Plichta D., Gautier L., Le Chatelier E., Peletier E., RA Bonde I., Nielsen T., Manichanh C., Arumugam M., Batto J., RA Santos M.B.Q.D., Blom N., Borruel N., Burgdorf K.S., Boumezbeur F., RA Casellas F., Dore J., Guarner F., Hansen T., Hildebrand F., Kaas R.S., RA Kennedy S., Kristiansen K., Kultima J.R., Leonard P., Levenez F., RA Lund O., Moumen B., Le Paslier D., Pons N., Pedersen O., Prifti E., RA Qin J., Raes J., Tap J., Tims S., Ussery D.W., Yamada T., RA MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P., Wang J., RA Brunak S., Ehrlich S.D.; RT "Dependencies among metagenomic species, viruses, plasmids and units RT of genetic variation."; RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:CDA80896.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CBCO010000003; CDA80896.1; -; Genomic_DNA. DR Proteomes; UP000017932; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000017932}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000017932}. FT DOMAIN 212 373 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 171 205 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 435 AA; 48506 MW; 75F70CD3E9A72B13 CRC64; MERKTIEENK NGARDYAVLV GLRSPVLGAD SADEESLAEL AALVETAGGE SVGMILQSRE KPDPHSFIGE GKVEEVKRMV ENSEATMVIF DNDLSPSQVR VLTELCGVQV LDRSGLILDI FAQRARTKEG CLQVELAQYQ YLLPRLIGMW SHLERQGGTG GSPIGTKGPG ETQLETDRRH IRRKIDKLKE ELEEVRRVRA TQRQRRRKNE IPVVAIVGYT NAGKSTLLNA ITGADIPANN RLFDTLDTTT RLLTVSDTLD VVISDTVGFI RKLPHQLVEA FKATLEELEY ADLLLHVIDA SNPEWQEQAR IVDDLIRELG AENIPCIRVY NKSDLAFAFQ RDKEGDAVSV SAKTGEGLDR LLSAIDKKLD KGTKRVTLHL PYDKVGALDS LYREAKVESV EYGETVDVVA VCTPRIIGQL KDYIEGWTEP KEEWE // ID R6DSV8_9CLOT Unreviewed; 428 AA. AC R6DSV8; DT 24-JUL-2013, integrated into UniProtKB/TrEMBL. DT 24-JUL-2013, sequence version 1. DT 12-APR-2017, entry version 24. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=BN547_02090 {ECO:0000313|EMBL:CDA87964.1}; OS Clostridium sp. CAG:230. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium; environmental samples. OX NCBI_TaxID=1262782 {ECO:0000313|EMBL:CDA87964.1, ECO:0000313|Proteomes:UP000017961}; RN [1] {ECO:0000313|EMBL:CDA87964.1, ECO:0000313|Proteomes:UP000017961} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MGS:230 {ECO:0000313|Proteomes:UP000017961}; RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., RA Sunagawa S., Plichta D., Gautier L., Le Chatelier E., Peletier E., RA Bonde I., Nielsen T., Manichanh C., Arumugam M., Batto J., RA Santos M.B.Q.D., Blom N., Borruel N., Burgdorf K.S., Boumezbeur F., RA Casellas F., Dore J., Guarner F., Hansen T., Hildebrand F., Kaas R.S., RA Kennedy S., Kristiansen K., Kultima J.R., Leonard P., Levenez F., RA Lund O., Moumen B., Le Paslier D., Pons N., Pedersen O., Prifti E., RA Qin J., Raes J., Tap J., Tims S., Ussery D.W., Yamada T., RA MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P., Wang J., RA Brunak S., Ehrlich S.D.; RT "Dependencies among metagenomic species, viruses, plasmids and units RT of genetic variation."; RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:CDA87964.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CBCQ010000192; CDA87964.1; -; Genomic_DNA. DR Proteomes; UP000017961; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000017961}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000017961}. FT DOMAIN 203 367 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 428 AA; 48510 MW; FBB994976933E167 CRC64; MGDMMHDTAE QEEKIILVGV ATAENDDTEQ SLDELEELGQ TAGAVTLAKV IQNREKVHSA TYIGKGKIQE VKELVEKYDA DCVVCDDELT PAQYNNLQEE IGVKVIDRTV MILDIFAKRA STSEGKLQVE LAQLRYRASH LVGGRSELSR LGGGIGTRGP GEQKLEMDRR LIRERITFVR KELAQVQKNR EVTRKKRQEN PIPVVAIVGY TNAGKSTLLN HLTGAGVLSE DKLFATLDPT TRKFSLENGE EMLFTDTVGF IRKLPHHLIQ AFRSTLEEAK YADAILHVVD CSNPDMDAQM HTVYDTLNQL EVGDKPIVTA FNKIDRYEAS ESLKDLHADK TVRISAKYGQ GIEEMLESIS NVLKANKVLL EKVFSYEEGE KTNLLRKYGQ VLEEEYQNEG VYMKAYIDRE YLYLFEEPKE RTKEPWEE // ID R6E3Z3_9BACE Unreviewed; 393 AA. AC R6E3Z3; DT 24-JUL-2013, integrated into UniProtKB/TrEMBL. DT 24-JUL-2013, sequence version 1. DT 12-APR-2017, entry version 23. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=BN760_00465 {ECO:0000313|EMBL:CDA95338.1}; OS Bacteroides sp. CAG:709. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae; OC Bacteroides; environmental samples. OX NCBI_TaxID=1262748 {ECO:0000313|EMBL:CDA95338.1, ECO:0000313|Proteomes:UP000018293}; RN [1] {ECO:0000313|EMBL:CDA95338.1, ECO:0000313|Proteomes:UP000018293} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MGS:709 {ECO:0000313|Proteomes:UP000018293}; RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., RA Sunagawa S., Plichta D., Gautier L., Le Chatelier E., Peletier E., RA Bonde I., Nielsen T., Manichanh C., Arumugam M., Batto J., RA Santos M.B.Q.D., Blom N., Borruel N., Burgdorf K.S., Boumezbeur F., RA Casellas F., Dore J., Guarner F., Hansen T., Hildebrand F., Kaas R.S., RA Kennedy S., Kristiansen K., Kultima J.R., Leonard P., Levenez F., RA Lund O., Moumen B., Le Paslier D., Pons N., Pedersen O., Prifti E., RA Qin J., Raes J., Tap J., Tims S., Ussery D.W., Yamada T., RA MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P., Wang J., RA Brunak S., Ehrlich S.D.; RT "Dependencies among metagenomic species, viruses, plasmids and units RT of genetic variation."; RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:CDA95338.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CBCT010000088; CDA95338.1; -; Genomic_DNA. DR Proteomes; UP000018293; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000018293}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000018293}. FT DOMAIN 198 382 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 166 193 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 393 AA; 45425 MW; CDC91C6F6CBFCD95 CRC64; MTENIEKAVF VGIITDKDEE SRVMEYLDEL EFLAETAGAT RDKKFVQRLE RPDNATYIRS GKLKEIAEYC EENEIKYVIF DDELSGTQQR NIEKIIKTFS VIDRTSLILE IFAQRAKTAY AKMQVELARY NYMLPRLAGM WTHLERQRGG MGTRGGMGET QIEIDRRIVK ERISKLKEQL KKVDKQMATQ RGNRGQLVRL ALVGYTNVGK STLMNLLSKS DVFAENKLFA TLDTTVRKVV LENVPFLLSD TVGFIRKLPT QLIEAFKSTL DEVREADILV HVVDISHPGF EEQMEVVEQT LRDIKADNKP VYVVFNKVDA YTYEEYDEFS LEPKGKNNRS LDELKNSWIA KEKTPCIFIS AKEKIGIDKL RNDIYKMVAE IHAGRYPFNN FLW // ID R6E7E1_9BACE Unreviewed; 418 AA. AC R6E7E1; DT 24-JUL-2013, integrated into UniProtKB/TrEMBL. DT 24-JUL-2013, sequence version 1. DT 12-APR-2017, entry version 23. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=BN772_03948 {ECO:0000313|EMBL:CDA86177.1}; OS Bacteroides sp. CAG:754. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae; OC Bacteroides; environmental samples. OX NCBI_TaxID=1262750 {ECO:0000313|EMBL:CDA86177.1, ECO:0000313|Proteomes:UP000017906}; RN [1] {ECO:0000313|EMBL:CDA86177.1, ECO:0000313|Proteomes:UP000017906} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MGS:754 {ECO:0000313|Proteomes:UP000017906}; RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., RA Sunagawa S., Plichta D., Gautier L., Le Chatelier E., Peletier E., RA Bonde I., Nielsen T., Manichanh C., Arumugam M., Batto J., RA Santos M.B.Q.D., Blom N., Borruel N., Burgdorf K.S., Boumezbeur F., RA Casellas F., Dore J., Guarner F., Hansen T., Hildebrand F., Kaas R.S., RA Kennedy S., Kristiansen K., Kultima J.R., Leonard P., Levenez F., RA Lund O., Moumen B., Le Paslier D., Pons N., Pedersen O., Prifti E., RA Qin J., Raes J., Tap J., Tims S., Ussery D.W., Yamada T., RA MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P., Wang J., RA Brunak S., Ehrlich S.D.; RT "Dependencies among metagenomic species, viruses, plasmids and units RT of genetic variation."; RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:CDA86177.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CBCP010000250; CDA86177.1; -; Genomic_DNA. DR Proteomes; UP000017906; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000017906}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000017906}. FT DOMAIN 216 400 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 418 AA; 47910 MW; 63CC84D994230778 CRC64; MKEFVISEAK VETAVLVGLI TQTQDERKTN EYLDELAFLA ETAGAEVVKR FTQKLPTAHS VTYVGKGKLE EIRQYIRNEE EEEREVGMVI FDDELSAKQL RNIEAELKVK ILDRTSLILD IFAMRAQTAN AKTQVELAQY KYMLPRLQRL WTHLERQGGG SGAGGGKGSV GLRGPGETQL EMDRRIILNR MSLLKERLAE IDKQKATQRK NRGRMIRVAL VGYTNVGKST MMNLLAKSEV FAENKLFATL DTTVRKVIIE NLPFLLSDTV GFIRKLPTDL VESFKSTLDE VREADLLVHV VDISHPGFEE QIEVVNKTLA EIDGAGKPMI LVFNKIDAYT YVEKALDDLT PRTKENLTLE ELMKTWMAKM EDNCLFISAR ERINMDELKD VVYRRVKELH VQKYPYNDFL YQTYEEEE // ID R6EM25_9FIRM Unreviewed; 436 AA. AC R6EM25; DT 24-JUL-2013, integrated into UniProtKB/TrEMBL. DT 24-JUL-2013, sequence version 1. DT 10-MAY-2017, entry version 24. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=BN538_01242 {ECO:0000313|EMBL:CDA98179.1}; OS Lachnospiraceae bacterium CAG:215. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Lachnospiraceae; OC environmental samples. OX NCBI_TaxID=1262985 {ECO:0000313|EMBL:CDA98179.1, ECO:0000313|Proteomes:UP000018007}; RN [1] {ECO:0000313|EMBL:CDA98179.1, ECO:0000313|Proteomes:UP000018007} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MGS:215 {ECO:0000313|Proteomes:UP000018007}; RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., RA Sunagawa S., Plichta D., Gautier L., Le Chatelier E., Peletier E., RA Bonde I., Nielsen T., Manichanh C., Arumugam M., Batto J., RA Santos M.B.Q.D., Blom N., Borruel N., Burgdorf K.S., Boumezbeur F., RA Casellas F., Dore J., Guarner F., Hansen T., Hildebrand F., Kaas R.S., RA Kennedy S., Kristiansen K., Kultima J.R., Leonard P., Levenez F., RA Lund O., Moumen B., Le Paslier D., Pons N., Pedersen O., Prifti E., RA Qin J., Raes J., Tap J., Tims S., Ussery D.W., Yamada T., RA MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P., Wang J., RA Brunak S., Ehrlich S.D.; RT "Dependencies among metagenomic species, viruses, plasmids and units RT of genetic variation."; RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:CDA98179.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CBCV010000143; CDA98179.1; -; Genomic_DNA. DR Proteomes; UP000018007; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000018007}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000018007}. FT DOMAIN 228 392 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 187 224 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 436 AA; 49051 MW; 7FD3D20337D432AD CRC64; MKFSRDFYGT GYLGARTFTN RKRVGQKMEL YEQKEHVERV ILVGIQTGDS DPAEASLDEL GELAKTAGAV VVGRMIQNRE QMHPATYIGK GKILELKEMI WETDATGIIC DDELSSAQLG NLEQELECKV MDRTLLILDI FAARAVSSEG KIQVELAQLR YRASRLVGLG HSLSRLGGGI GTRGPGEKKL EMDRRLIRER ISRLKKELKE VEQHRELIRT QRKESHRKVA ALVGYTSAGK SSIENALTGA GILEDAMLFS TLDTTTRALE LGGKQTVLLT DTVGFIRKLP HHLVEAFKST LEEAIYADII IHVVDASNPQ MDTQMYVVYE TLRQLGVKEK PIVTLFNKQD QVETPGAFRD FQADYTVCTS ARTGEGLEEL KQVLLEILRK DLVYVERLYP FPEAGKIQRI RENGELLEEE YVPEGIQIKA YVPYGF // ID R6ENE5_9FIRM Unreviewed; 415 AA. AC R6ENE5; DT 24-JUL-2013, integrated into UniProtKB/TrEMBL. DT 24-JUL-2013, sequence version 1. DT 10-MAY-2017, entry version 24. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=BN710_01216 {ECO:0000313|EMBL:CDA91492.1}; OS Ruminococcus sp. CAG:563. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Ruminococcaceae; OC Ruminococcus; environmental samples. OX NCBI_TaxID=1262961 {ECO:0000313|EMBL:CDA91492.1, ECO:0000313|Proteomes:UP000018082}; RN [1] {ECO:0000313|EMBL:CDA91492.1, ECO:0000313|Proteomes:UP000018082} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MGS:563 {ECO:0000313|Proteomes:UP000018082}; RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., RA Sunagawa S., Plichta D., Gautier L., Le Chatelier E., Peletier E., RA Bonde I., Nielsen T., Manichanh C., Arumugam M., Batto J., RA Santos M.B.Q.D., Blom N., Borruel N., Burgdorf K.S., Boumezbeur F., RA Casellas F., Dore J., Guarner F., Hansen T., Hildebrand F., Kaas R.S., RA Kennedy S., Kristiansen K., Kultima J.R., Leonard P., Levenez F., RA Lund O., Moumen B., Le Paslier D., Pons N., Pedersen O., Prifti E., RA Qin J., Raes J., Tap J., Tims S., Ussery D.W., Yamada T., RA MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P., Wang J., RA Brunak S., Ehrlich S.D.; RT "Dependencies among metagenomic species, viruses, plasmids and units RT of genetic variation."; RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:CDA91492.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CBCR010000087; CDA91492.1; -; Genomic_DNA. DR Proteomes; UP000018082; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000018082}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000018082}. FT DOMAIN 200 361 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 159 193 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 415 AA; 45545 MW; 604C2736DFFC6FD2 CRC64; MEFYENSQEP EVAVLVGIDM GLYNAQVSMD ELEELARTAG AVVAAKIIQK RDKPDSATYV GSGRLEEIKA FTEANDVDLL IFDGELTPSQ QRNIEDETDI RVIDRTTLIL DIFAARARSN EGKIQVELAQ LKYSLPRLGG KGAEMSRLGG GIGTRGPGES KLESDRRHIH RRIQSLQEEL VQIAKRRENL RARREKDGVE TVAIVGYTNA GKSTLMNTLT NAGVLAENKL FATLDPTSRA LTLPDGRTVM LIDTVGLVRR LPHQLVDAFR STLEEAANAT VILNLCDASD ECCTEHLNVT MNLLAALGCA DKPIISVLNK CDLCGGSFVL PAQGEFVMIS AKTGEGLGNL LAKIQLSLPL TRRKAELLIP YNEGGLVNYI REEGILIKED YRADGIYVKA VVDIQFLDKH KDLIV // ID R6EPT1_9FIRM Unreviewed; 426 AA. AC R6EPT1; DT 24-JUL-2013, integrated into UniProtKB/TrEMBL. DT 24-JUL-2013, sequence version 1. DT 10-MAY-2017, entry version 26. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=BN497_01941 {ECO:0000313|EMBL:CDB02573.1}; OS Firmicutes bacterium CAG:145. OC Bacteria; Firmicutes; environmental samples. OX NCBI_TaxID=1263005 {ECO:0000313|EMBL:CDB02573.1, ECO:0000313|Proteomes:UP000018044}; RN [1] {ECO:0000313|EMBL:CDB02573.1, ECO:0000313|Proteomes:UP000018044} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MGS:145 {ECO:0000313|Proteomes:UP000018044}; RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., RA Sunagawa S., Plichta D., Gautier L., Le Chatelier E., Peletier E., RA Bonde I., Nielsen T., Manichanh C., Arumugam M., Batto J., RA Santos M.B.Q.D., Blom N., Borruel N., Burgdorf K.S., Boumezbeur F., RA Casellas F., Dore J., Guarner F., Hansen T., Hildebrand F., Kaas R.S., RA Kennedy S., Kristiansen K., Kultima J.R., Leonard P., Levenez F., RA Lund O., Moumen B., Le Paslier D., Pons N., Pedersen O., Prifti E., RA Qin J., Raes J., Tap J., Tims S., Ussery D.W., Yamada T., RA MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P., Wang J., RA Brunak S., Ehrlich S.D.; RT "Dependencies among metagenomic species, viruses, plasmids and units RT of genetic variation."; RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:CDB02573.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CBCX010000052; CDB02573.1; -; Genomic_DNA. DR Proteomes; UP000018044; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000018044}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000018044}. FT DOMAIN 204 372 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 426 AA; 48177 MW; 4F2E29BC3D9087D7 CRC64; MLRFTDDNKV LREDRYNAIL VGVQRDEDIS YSMEELEGLA EAAGARVLGT MIQNMERPNT ATLIGKGKVE ELKELADSME ADMIIFNDEL TGMQLRNLED TIGIRIIDRT ILILDIFATR ATSREGKLQV ELAQLKYRMP RLTGFGKSLS RLGGGIGTRG PGEKKLETDR RHIQRRVTDI KDELTHLKNT RSVQRARREK SSIPVVALVG YTNSGKSAIM NRILSDVQKA DKTVLEKDML FATLDVQQRN VTLESGREFI LIDTVGFVSR LPHSLIEAFK ATLEEVTYAD LLLHVVDASY ENYDFHIKVT EKVMGEMGAG EKEKIMVFNK TDLAHDDIIP VRGCDNVEIS AKCGTNIDVL INKIESKIFG DYTPAAFLVP YDRGDISSYL CSQSEVKKME YTDEGTYFEV VLKQEDRKRL EKYEVV // ID R6EWD8_9BACT Unreviewed; 418 AA. AC R6EWD8; DT 24-JUL-2013, integrated into UniProtKB/TrEMBL. DT 24-JUL-2013, sequence version 1. DT 12-APR-2017, entry version 24. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=BN487_00856 {ECO:0000313|EMBL:CDA94232.1}; OS Prevotella sp. CAG:1320. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Prevotellaceae; OC Prevotella; environmental samples. OX NCBI_TaxID=1262922 {ECO:0000313|EMBL:CDA94232.1, ECO:0000313|Proteomes:UP000018111}; RN [1] {ECO:0000313|EMBL:CDA94232.1, ECO:0000313|Proteomes:UP000018111} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MGS:1320 {ECO:0000313|Proteomes:UP000018111}; RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., RA Sunagawa S., Plichta D., Gautier L., Le Chatelier E., Peletier E., RA Bonde I., Nielsen T., Manichanh C., Arumugam M., Batto J., RA Santos M.B.Q.D., Blom N., Borruel N., Burgdorf K.S., Boumezbeur F., RA Casellas F., Dore J., Guarner F., Hansen T., Hildebrand F., Kaas R.S., RA Kennedy S., Kristiansen K., Kultima J.R., Leonard P., Levenez F., RA Lund O., Moumen B., Le Paslier D., Pons N., Pedersen O., Prifti E., RA Qin J., Raes J., Tap J., Tims S., Ussery D.W., Yamada T., RA MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P., Wang J., RA Brunak S., Ehrlich S.D.; RT "Dependencies among metagenomic species, viruses, plasmids and units RT of genetic variation."; RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:CDA94232.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CBCU010000037; CDA94232.1; -; Genomic_DNA. DR Proteomes; UP000018111; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000018111}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000018111}. FT DOMAIN 216 400 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 418 AA; 47660 MW; AEAD1EC32E7BCFD0 CRC64; MKEFVISEAK AETAILVGLI TQEQDEAKTK EYLDELEFLA DTAGAVTVKR FTQRVAAPSQ VTYVGKGKLE EIKLYIKQEE EADREIGMVI FDDELSAKQI RNIEAELGVK ILDRTSLILD IFAMRAQTAN AKTQVELAQY RYMLPRLQRL WTHLERQGGG SGSGGGKGSV GLRGPGETQL EMDRRIILQR VSLLKQRLQE IDRQKATQRK NRGRLIRVAL VGYTNVGKST LMNLLAKSEV FAENKLFATL DTTVRKVVID NLPFLLADTV GFIRKLPTDL VDSFKSTLDE VREADLLLHV VDISHPDFEE QIQVVENTLK DLGCAEKPSM IIFNKIDSYT WVEKEEDDLT PATRENVTLE ELKRTWMGKL SDSCLFISAK QRENIDELRD ILYKKVRELH VQKYPYNDFL YPQVEDSL // ID R6F437_9BACT Unreviewed; 415 AA. AC R6F437; DT 24-JUL-2013, integrated into UniProtKB/TrEMBL. DT 24-JUL-2013, sequence version 1. DT 12-APR-2017, entry version 23. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=BN691_01014 {ECO:0000313|EMBL:CDB04144.1}; OS Prevotella sp. CAG:520. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Prevotellaceae; OC Prevotella; environmental samples. OX NCBI_TaxID=1262929 {ECO:0000313|EMBL:CDB04144.1, ECO:0000313|Proteomes:UP000018359}; RN [1] {ECO:0000313|EMBL:CDB04144.1, ECO:0000313|Proteomes:UP000018359} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MGS:520 {ECO:0000313|Proteomes:UP000018359}; RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., RA Sunagawa S., Plichta D., Gautier L., Le Chatelier E., Peletier E., RA Bonde I., Nielsen T., Manichanh C., Arumugam M., Batto J., RA Santos M.B.Q.D., Blom N., Borruel N., Burgdorf K.S., Boumezbeur F., RA Casellas F., Dore J., Guarner F., Hansen T., Hildebrand F., Kaas R.S., RA Kennedy S., Kristiansen K., Kultima J.R., Leonard P., Levenez F., RA Lund O., Moumen B., Le Paslier D., Pons N., Pedersen O., Prifti E., RA Qin J., Raes J., Tap J., Tims S., Ussery D.W., Yamada T., RA MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P., Wang J., RA Brunak S., Ehrlich S.D.; RT "Dependencies among metagenomic species, viruses, plasmids and units RT of genetic variation."; RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:CDB04144.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CBCY010000025; CDB04144.1; -; Genomic_DNA. DR Proteomes; UP000018359; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000018359}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000018359}. FT DOMAIN 216 400 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 415 AA; 47420 MW; 7EF5803B7F055938 CRC64; MKEFVISEVK AETAILVGLI TKDQDEAKTK EYLDELEFLA DTAGAVTVKR FTQRVGGPSA VTYVGSGKLE EIREYIEAEE DAERPVGMVI FDDELSAKQM RNIEKVLQVK ILDRTSLILD IFAMRAQTAA AKTQVELAQY RYMLPRLQRL WTHLERQGGG SGSGGGKGSV GLRGPGETQL EMDRRIILNR ITLLKQRLVE IDKQMSTQRK NRGRTIRVAL VGYTNVGKST IMNMLAKSEV FAENKLFATL DTTVRKVVID NLPFLLADTV GFIRKLPTDL VDSFKSTLDE TREADLLLHV VDISHPDFEE QIRVVENTLK ELGCADKPSM IVFNKIDNYT WTEKEEDDLT PMTKENITLD ELKRTWMARL GENCMFISAK EKLNIDEFRE TIYRKVRELH VQKYPYNDFL YMDVE // ID R6FD62_9FIRM Unreviewed; 422 AA. AC R6FD62; DT 24-JUL-2013, integrated into UniProtKB/TrEMBL. DT 24-JUL-2013, sequence version 1. DT 10-MAY-2017, entry version 23. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=BN749_02314 {ECO:0000313|EMBL:CDA99992.1}; OS Firmicutes bacterium CAG:65. OC Bacteria; Firmicutes; environmental samples. OX NCBI_TaxID=1262994 {ECO:0000313|EMBL:CDA99992.1, ECO:0000313|Proteomes:UP000018207}; RN [1] {ECO:0000313|EMBL:CDA99992.1, ECO:0000313|Proteomes:UP000018207} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MGS:65 {ECO:0000313|Proteomes:UP000018207}; RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., RA Sunagawa S., Plichta D., Gautier L., Le Chatelier E., Peletier E., RA Bonde I., Nielsen T., Manichanh C., Arumugam M., Batto J., RA Santos M.B.Q.D., Blom N., Borruel N., Burgdorf K.S., Boumezbeur F., RA Casellas F., Dore J., Guarner F., Hansen T., Hildebrand F., Kaas R.S., RA Kennedy S., Kristiansen K., Kultima J.R., Leonard P., Levenez F., RA Lund O., Moumen B., Le Paslier D., Pons N., Pedersen O., Prifti E., RA Qin J., Raes J., Tap J., Tims S., Ussery D.W., Yamada T., RA MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P., Wang J., RA Brunak S., Ehrlich S.D.; RT "Dependencies among metagenomic species, viruses, plasmids and units RT of genetic variation."; RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:CDA99992.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CBCW010000165; CDA99992.1; -; Genomic_DNA. DR Proteomes; UP000018207; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000018207}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000018207}. FT DOMAIN 199 329 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 158 192 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 422 AA; 47873 MW; 547EA334C8C88DE9 CRC64; MQEAPVKVLL VGVDIGEEAD FEYSMEELAS LAEAAEKEVV GQIVQRLDHV NKALYIGTGK VDDVRRLAEE RGAQEVVFDN SLTPSQVRNL GKELELTVID RTNLILDIFA IRAQTREAKL QVETARLQYM LPRLVGMYDA LSRQGGASGS MSNKGTGEKK LELDRRKIEH RITELKKELE DVSRTRDVQR RKRQQSRTPQ VALVGYTNAG KSTILNRMVE QFGELPEKTV MEKDMLFATL ETSVRSIDTG HNKPFFLTDT VGFIHKLPHG LVKAFRSTLE EVKYADLLVQ VVDFSDENYR QQMQVTADTL KELGAGDIPQ IVVYNKADKC GMEPLPQKRQ EHWYLAAGQN TGIRELAEAI EQQVYADNVD CTFLIPYSAG NVASYLMEEA QVFSTEYRED GILIHADCHR QDMERYKTYM TQ // ID R6FKB7_9BACE Unreviewed; 422 AA. AC R6FKB7; DT 24-JUL-2013, integrated into UniProtKB/TrEMBL. DT 24-JUL-2013, sequence version 1. DT 12-APR-2017, entry version 23. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=BN744_01175 {ECO:0000313|EMBL:CDB09844.1}; OS Bacteroides sp. CAG:633. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae; OC Bacteroides; environmental samples. OX NCBI_TaxID=1262744 {ECO:0000313|EMBL:CDB09844.1, ECO:0000313|Proteomes:UP000018121}; RN [1] {ECO:0000313|EMBL:CDB09844.1, ECO:0000313|Proteomes:UP000018121} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MGS:633 {ECO:0000313|Proteomes:UP000018121}; RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., RA Sunagawa S., Plichta D., Gautier L., Le Chatelier E., Peletier E., RA Bonde I., Nielsen T., Manichanh C., Arumugam M., Batto J., RA Santos M.B.Q.D., Blom N., Borruel N., Burgdorf K.S., Boumezbeur F., RA Casellas F., Dore J., Guarner F., Hansen T., Hildebrand F., Kaas R.S., RA Kennedy S., Kristiansen K., Kultima J.R., Leonard P., Levenez F., RA Lund O., Moumen B., Le Paslier D., Pons N., Pedersen O., Prifti E., RA Qin J., Raes J., Tap J., Tims S., Ussery D.W., Yamada T., RA MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P., Wang J., RA Brunak S., Ehrlich S.D.; RT "Dependencies among metagenomic species, viruses, plasmids and units RT of genetic variation."; RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:CDB09844.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CBDA010000063; CDB09844.1; -; Genomic_DNA. DR Proteomes; UP000018121; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000018121}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000018121}. FT DOMAIN 218 402 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 422 AA; 48255 MW; A07BE21AD1119E81 CRC64; MAMKEFVISE AQVETAVLVG LITKTQDERK TNEYLDELAF LAETAGAEVV KRFTQKLDQA NSVTYVGKGK LDEIKQYIHD EEEAEREVGM VIFDDELSAK QIRNIEGELK VKILDRTSLI LDIFAMRAQT ANAKTQVELA QYKYMLPRLQ RLWTHLERQG GGSGAGGGKG SVGLRGPGET QLEMDRRIIL NRMSLLKERL VEIDKQKATQ RKNRGRLIRV ALVGYTNVGK STLMNLLAKS EVFAENKLFA TLDTTVRKVI IDNLPFLLSD TVGFIRKLPT DLVDSFKSTL DEVREADLLL HVVDISHPDF EEQIEVVNKT LADIGAAGKP MMLVFNKIDA YTYVQKDEDD LTPRTKENWT LEELMRTWMA KMEDNCLFIS ARERINLEEM KNAVYKRVKE LHVQKYPYND FLYQNYDENG EV // ID R6FW54_9FIRM Unreviewed; 411 AA. AC R6FW54; DT 24-JUL-2013, integrated into UniProtKB/TrEMBL. DT 24-JUL-2013, sequence version 1. DT 12-APR-2017, entry version 23. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=BN525_01453 {ECO:0000313|EMBL:CDB13594.1}; OS Eubacterium sp. CAG:192. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Eubacteriaceae; OC Eubacterium; environmental samples. OX NCBI_TaxID=1262883 {ECO:0000313|EMBL:CDB13594.1, ECO:0000313|Proteomes:UP000017943}; RN [1] {ECO:0000313|EMBL:CDB13594.1, ECO:0000313|Proteomes:UP000017943} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MGS:192 {ECO:0000313|Proteomes:UP000017943}; RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., RA Sunagawa S., Plichta D., Gautier L., Le Chatelier E., Peletier E., RA Bonde I., Nielsen T., Manichanh C., Arumugam M., Batto J., RA Santos M.B.Q.D., Blom N., Borruel N., Burgdorf K.S., Boumezbeur F., RA Casellas F., Dore J., Guarner F., Hansen T., Hildebrand F., Kaas R.S., RA Kennedy S., Kristiansen K., Kultima J.R., Leonard P., Levenez F., RA Lund O., Moumen B., Le Paslier D., Pons N., Pedersen O., Prifti E., RA Qin J., Raes J., Tap J., Tims S., Ussery D.W., Yamada T., RA MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P., Wang J., RA Brunak S., Ehrlich S.D.; RT "Dependencies among metagenomic species, viruses, plasmids and units RT of genetic variation."; RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:CDB13594.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CBDB010000410; CDB13594.1; -; Genomic_DNA. DR Proteomes; UP000017943; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000017943}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000017943}. FT DOMAIN 198 362 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 157 191 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 411 AA; 46119 MW; 5231B7F762A85D12 CRC64; MYENKEELEK VILVAVSTGN EEDAQESLDE LEELVSTAGA VVVGRVVQNL EHINNTTYVG TGKVKEIKDL IWETDADAIV CDDELSPAQY KNLEDELEVK VMDRTLIILD IFAGRAKTAE GKIQVELAQL RYRSTRLIGM RNLSRQGGGI GTRGPGEKKL EVDRRLIRNR ISQLKEQVSE MENHRQVTRA KRQDNPVPVV AIVGYTNAGK STLLNTVTNA EVLEEDKLFA TLDPTTRNYK LPDGQEVLLT DTVGFIRKLP HHLIDAFRST LEEAKYSDII IHVVDASNPS MDKNVHAVYE TLDNLGVKDK TIITVFNKED KLETKPILRD FKADYVVHGA IKKGIGIDDI NEAIENAVKS MRVLYENVFT YAEAGKTGLI RKYGQLLEEE YKEDGIHVKA YVPTSLIGRL N // ID R6G660_9CLOT Unreviewed; 599 AA. AC R6G660; DT 24-JUL-2013, integrated into UniProtKB/TrEMBL. DT 24-JUL-2013, sequence version 1. DT 12-APR-2017, entry version 22. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=BN542_02004 {ECO:0000313|EMBL:CDB16826.1}; OS Clostridium sp. CAG:221. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium; environmental samples. OX NCBI_TaxID=1262780 {ECO:0000313|EMBL:CDB16826.1, ECO:0000313|Proteomes:UP000018176}; RN [1] {ECO:0000313|EMBL:CDB16826.1, ECO:0000313|Proteomes:UP000018176} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MGS:221 {ECO:0000313|Proteomes:UP000018176}; RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., RA Sunagawa S., Plichta D., Gautier L., Le Chatelier E., Peletier E., RA Bonde I., Nielsen T., Manichanh C., Arumugam M., Batto J., RA Santos M.B.Q.D., Blom N., Borruel N., Burgdorf K.S., Boumezbeur F., RA Casellas F., Dore J., Guarner F., Hansen T., Hildebrand F., Kaas R.S., RA Kennedy S., Kristiansen K., Kultima J.R., Leonard P., Levenez F., RA Lund O., Moumen B., Le Paslier D., Pons N., Pedersen O., Prifti E., RA Qin J., Raes J., Tap J., Tims S., Ussery D.W., Yamada T., RA MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P., Wang J., RA Brunak S., Ehrlich S.D.; RT "Dependencies among metagenomic species, viruses, plasmids and units RT of genetic variation."; RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:CDB16826.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CBDC010000117; CDB16826.1; -; Genomic_DNA. DR Proteomes; UP000018176; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000018176}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000018176}. FT DOMAIN 364 541 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 599 AA; 67195 MW; 97D91A9FCAFCEDB5 CRC64; MIYGNIDGIR KSALEELESL YKAKTPKDEV CSLSIMETIS RVSSFIEREI SVAIDRRGNT VSVAIGDSTS VEIPTLDISE KKLAGVRIIH THPNGFSNLS ALDISALLKL KLDAIVAIGI YEGKIIDCSL GMLTVMNDTL DYEEEQHIKV EDLTSMHILN KIAYIDSLIK ERDIIEDEVE SAILVGSDTK ESLEELKELT KACEIPVLDS VFQSRSKIDA AFYIGRGKVL EIATLRQKLR ANVIIFDDEL SGSQVRNLEA ALGAKVIDRT TLILEIFARR AKSREAKIQV ELAQLKYRAS RLQGLGTILS RTGGGIGTRG PGEKKLETDR RHIKEQIYDL NAELKKIKKI RETQREKRNK ESIPKVSLVG YTNAGKSTLR NALCDVAAQK EVQGKEKVFE ADMLFATLDI TTRAIILKNK GIITLTDTVG FVRKLPHDLV EAFKSTLEEV IYADLLCHVV DASSETALEQ IKAVEEVLHE LDALDKKTIL VLNKIDKAEP ALLEEIKVAT EHYNTVEISA KEGTNLEKLL DEIEENLPYT MKKCEYLIPY DRSDMVSFLH RNGRVFEEDY KENGTFMIVE VDDESYNKSS EFVIKLINE // ID R6G9M2_9FIRM Unreviewed; 432 AA. AC R6G9M2; DT 24-JUL-2013, integrated into UniProtKB/TrEMBL. DT 24-JUL-2013, sequence version 1. DT 12-APR-2017, entry version 21. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=BN476_01532 {ECO:0000313|EMBL:CDB17981.1}; OS Eubacterium hallii CAG:12. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Eubacteriaceae; OC Eubacterium; environmental samples. OX NCBI_TaxID=1263078 {ECO:0000313|EMBL:CDB17981.1, ECO:0000313|Proteomes:UP000018069}; RN [1] {ECO:0000313|EMBL:CDB17981.1, ECO:0000313|Proteomes:UP000018069} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MGS:12 {ECO:0000313|Proteomes:UP000018069}; RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., RA Sunagawa S., Plichta D., Gautier L., Le Chatelier E., Peletier E., RA Bonde I., Nielsen T., Manichanh C., Arumugam M., Batto J., RA Santos M.B.Q.D., Blom N., Borruel N., Burgdorf K.S., Boumezbeur F., RA Casellas F., Dore J., Guarner F., Hansen T., Hildebrand F., Kaas R.S., RA Kennedy S., Kristiansen K., Kultima J.R., Leonard P., Levenez F., RA Lund O., Moumen B., Le Paslier D., Pons N., Pedersen O., Prifti E., RA Qin J., Raes J., Tap J., Tims S., Ussery D.W., Yamada T., RA MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P., Wang J., RA Brunak S., Ehrlich S.D.; RT "Dependencies among metagenomic species, viruses, plasmids and units RT of genetic variation."; RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:CDB17981.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CBDD010000116; CDB17981.1; -; Genomic_DNA. DR ProteinModelPortal; R6G9M2; -. DR Proteomes; UP000018069; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000018069}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000018069}. FT DOMAIN 198 329 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 157 191 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 432 AA; 49080 MW; 87D7158DB9842985 CRC64; MEERTKALLV GVNLNNDPEF ETALKELESL AEACNMEVVG VETQNVSQIN TGVYVGTGRV EEIKAVAHMM GAEVIIFDNT LSPMQLRNLK DIIERPVFDR THLILQIFSS RARTREAQIQ VETARLQYEL PRLTGMGEIL SRQGGGSGGL SNKGAGEKKL ELDKRKIRHR ISELKKELRE VEKNRETQRK RRLVQGIPQV ALVGYTNAGK STLLNAFIDK YEENEEKKED RKVMAKNMLF ATLDTTVRKI HLPDKREFLL SDTVGFISKL PHNLVEAFHS TLEEVKFANL LLEVVDYSDE HYMDHMEVTR QTLKELGADE IPCIHVFNKC DIAKANGRED VPAELPHIGK DCIYMAAGQN IGLEELVQLI SNHIYQDYVE CTMLIPYTEG ALVSYFNENA TVKETEYEAE GTKITMSCLL KDLKKYKEYV IL // ID R6GQI6_9FIRM Unreviewed; 434 AA. AC R6GQI6; DT 24-JUL-2013, integrated into UniProtKB/TrEMBL. DT 24-JUL-2013, sequence version 1. DT 12-APR-2017, entry version 23. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=BN557_01210 {ECO:0000313|EMBL:CDB27678.1}; OS Oscillibacter sp. CAG:241. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Oscillospiraceae; OC Oscillibacter; environmental samples. OX NCBI_TaxID=1262911 {ECO:0000313|EMBL:CDB27678.1, ECO:0000313|Proteomes:UP000018113}; RN [1] {ECO:0000313|EMBL:CDB27678.1, ECO:0000313|Proteomes:UP000018113} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MGS:241 {ECO:0000313|Proteomes:UP000018113}; RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., RA Sunagawa S., Plichta D., Gautier L., Le Chatelier E., Peletier E., RA Bonde I., Nielsen T., Manichanh C., Arumugam M., Batto J., RA Santos M.B.Q.D., Blom N., Borruel N., Burgdorf K.S., Boumezbeur F., RA Casellas F., Dore J., Guarner F., Hansen T., Hildebrand F., Kaas R.S., RA Kennedy S., Kristiansen K., Kultima J.R., Leonard P., Levenez F., RA Lund O., Moumen B., Le Paslier D., Pons N., Pedersen O., Prifti E., RA Qin J., Raes J., Tap J., Tims S., Ussery D.W., Yamada T., RA MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P., Wang J., RA Brunak S., Ehrlich S.D.; RT "Dependencies among metagenomic species, viruses, plasmids and units RT of genetic variation."; RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:CDB27678.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CBDI010000126; CDB27678.1; -; Genomic_DNA. DR Proteomes; UP000018113; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000018113}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000018113}. FT DOMAIN 210 371 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 176 203 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 434 AA; 48296 MW; 80AB5C74D1460730 CRC64; MEQTIIQEKK RDYAVLVGLR SPVLGDDSAD EESLAELAAL VDTAGGQAVG TILQSRDKPD PHSFIGEGKV EEVRRMVQEE NATMVIFDND LSPSQLRVLT EMTGVQVLDR SGLILDIFAQ RARTREGRLQ VELAQYQYLL PRLIGMWTHL ERQAGTSGKG PIGSKGPGET QLETDRRHIH RKIDKLKAEL EEVRRVRGTQ RQRRMKNEIP VVAIVGYTNA GKSTLLNAIT GAGIPANNRL FDTLDTTTRL LTVSDTLDVV ISDTVGFIRK LPHQLVEAFK ATLEELEYAD LLLHVIDVSN PQWQQQAAIV ESLIRELKAD HIPCLRVYNK CDLAFSGQRS AGEDTVSISA KTGEGVPELL ACIDKKLDKG TRRVTLHLPY DKAGLLDGLY REAKVESVEY AASIDVVAVC PPKVLGQVKD YVEGWREEKE DWEL // ID R6H2Y1_9FIRM Unreviewed; 411 AA. AC R6H2Y1; DT 24-JUL-2013, integrated into UniProtKB/TrEMBL. DT 24-JUL-2013, sequence version 1. DT 12-APR-2017, entry version 23. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=BN690_00211 {ECO:0000313|EMBL:CDB20642.1}; OS Blautia sp. CAG:52. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Lachnospiraceae; OC Blautia; environmental samples. OX NCBI_TaxID=1262758 {ECO:0000313|EMBL:CDB20642.1, ECO:0000313|Proteomes:UP000018177}; RN [1] {ECO:0000313|EMBL:CDB20642.1, ECO:0000313|Proteomes:UP000018177} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MGS:52 {ECO:0000313|Proteomes:UP000018177}; RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., RA Sunagawa S., Plichta D., Gautier L., Le Chatelier E., Peletier E., RA Bonde I., Nielsen T., Manichanh C., Arumugam M., Batto J., RA Santos M.B.Q.D., Blom N., Borruel N., Burgdorf K.S., Boumezbeur F., RA Casellas F., Dore J., Guarner F., Hansen T., Hildebrand F., Kaas R.S., RA Kennedy S., Kristiansen K., Kultima J.R., Leonard P., Levenez F., RA Lund O., Moumen B., Le Paslier D., Pons N., Pedersen O., Prifti E., RA Qin J., Raes J., Tap J., Tims S., Ussery D.W., Yamada T., RA MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P., Wang J., RA Brunak S., Ehrlich S.D.; RT "Dependencies among metagenomic species, viruses, plasmids and units RT of genetic variation."; RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:CDB20642.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CBDE010000146; CDB20642.1; -; Genomic_DNA. DR Proteomes; UP000018177; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000018177}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000018177}. FT DOMAIN 199 363 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 172 195 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 411 AA; 46308 MW; 82E1A72611676665 CRC64; MYEMGEQLER VILAGVQTYE SDDTVQSLYE LRELAETAGA VTVGTIMQSR ETIHPATYLG KGKLEELKEL LYDLDATGVI CDDELSPAQL NNLEQELECK VMDRTMVILD IFAQRAKTSE GKIQVELAQL KYRAARLVGM RASLSRLGGG IGTRGPGEKK LEMDRRLIHS RIGQLKEQLE QVQKHRELIR SQRDKSRVKV AAIVGYTNAG KSTLLNTMTQ AGVLEENQLF ATLDPTTRAL DLPGKQQILL TDTVGFIRKL PHHLIEAFKS TLEEAKYADM ILHVVDASNP QMDEHMQVVY DTLRQLGVSD KKMITLFNKQ DLCTDKEQLR DFQADHVLQI SAKNGQGLEE LKELLADVLR EGQIYIERLV PYDQAGSIAR IRKYGQVVQE EFLAEGISVK AYVPMEVYSQ I // ID R6H6M8_9FIRM Unreviewed; 419 AA. AC R6H6M8; DT 24-JUL-2013, integrated into UniProtKB/TrEMBL. DT 24-JUL-2013, sequence version 1. DT 10-MAY-2017, entry version 24. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=BN490_00771 {ECO:0000313|EMBL:CDB29514.1}; OS Firmicutes bacterium CAG:137. OC Bacteria; Firmicutes; environmental samples. OX NCBI_TaxID=1263004 {ECO:0000313|EMBL:CDB29514.1, ECO:0000313|Proteomes:UP000018011}; RN [1] {ECO:0000313|EMBL:CDB29514.1, ECO:0000313|Proteomes:UP000018011} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MGS:137 {ECO:0000313|Proteomes:UP000018011}; RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., RA Sunagawa S., Plichta D., Gautier L., Le Chatelier E., Peletier E., RA Bonde I., Nielsen T., Manichanh C., Arumugam M., Batto J., RA Santos M.B.Q.D., Blom N., Borruel N., Burgdorf K.S., Boumezbeur F., RA Casellas F., Dore J., Guarner F., Hansen T., Hildebrand F., Kaas R.S., RA Kennedy S., Kristiansen K., Kultima J.R., Leonard P., Levenez F., RA Lund O., Moumen B., Le Paslier D., Pons N., Pedersen O., Prifti E., RA Qin J., Raes J., Tap J., Tims S., Ussery D.W., Yamada T., RA MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P., Wang J., RA Brunak S., Ehrlich S.D.; RT "Dependencies among metagenomic species, viruses, plasmids and units RT of genetic variation."; RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:CDB29514.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CBDK010000099; CDB29514.1; -; Genomic_DNA. DR Proteomes; UP000018011; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000018011}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000018011}. FT DOMAIN 202 363 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 161 195 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 419 AA; 45937 MW; F5CD41E943BEF01D CRC64; MPQEHTIERA VLVGLNADCF SKEETASEAS LEELEALLET AGGLCTAKIL QNRHTPDART LIGAGKAEEI RQLIQATEAG MAIFDNPLSP SQIRVLEELL GVTVLDRSAL ILDIFAQRAK TAEGRLQVEL AQYKYLLPRL SGMGISLSRQ GGGIGTRGPG ETQLETDRRH IRARIAKLEE ELAQVRQVRA MQRRQRIKNS VPVVALVGYT NAGKSTLLNQ LTGAEIPANN RLFDTLDTTS RQLEVNDTLQ VILSDTVGFI SKLPHHLVDA FRATLEELSY ADLLIHVIDA SDPEREAHIA VVEQLVEQLA KPGVPVIQCF NKADLVMAED LPVGQNRVAV SAKKGSGLEA LLRLVADNLN RGQHRCFLLL PYAQGGILDR LHRDAQVLAV EYAPEGIQVE AICGPIVYGQ LKKFVIREI // ID R6HI38_9ACTN Unreviewed; 438 AA. AC R6HI38; DT 24-JUL-2013, integrated into UniProtKB/TrEMBL. DT 24-JUL-2013, sequence version 1. DT 10-MAY-2017, entry version 24. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=BN534_01385 {ECO:0000313|EMBL:CDB33649.1}; OS Eggerthella sp. CAG:209. OC Bacteria; Actinobacteria; Coriobacteriia; Eggerthellales; OC Eggerthellaceae; Eggerthella; environmental samples. OX NCBI_TaxID=1262875 {ECO:0000313|EMBL:CDB33649.1, ECO:0000313|Proteomes:UP000018042}; RN [1] {ECO:0000313|EMBL:CDB33649.1, ECO:0000313|Proteomes:UP000018042} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MGS:209 {ECO:0000313|Proteomes:UP000018042}; RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., RA Sunagawa S., Plichta D., Gautier L., Le Chatelier E., Peletier E., RA Bonde I., Nielsen T., Manichanh C., Arumugam M., Batto J., RA Santos M.B.Q.D., Blom N., Borruel N., Burgdorf K.S., Boumezbeur F., RA Casellas F., Dore J., Guarner F., Hansen T., Hildebrand F., Kaas R.S., RA Kennedy S., Kristiansen K., Kultima J.R., Leonard P., Levenez F., RA Lund O., Moumen B., Le Paslier D., Pons N., Pedersen O., Prifti E., RA Qin J., Raes J., Tap J., Tims S., Ussery D.W., Yamada T., RA MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P., Wang J., RA Brunak S., Ehrlich S.D.; RT "Dependencies among metagenomic species, viruses, plasmids and units RT of genetic variation."; RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:CDB33649.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CBDM010000160; CDB33649.1; -; Genomic_DNA. DR Proteomes; UP000018042; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000018042}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000018042}. FT DOMAIN 217 382 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 438 AA; 48649 MW; 1693E2657D5E565F CRC64; MIEFDEVKQH GPKTVIEKPR ERAILVGVER PNQEWSLESS LAELERLAWT AGADTVARTS QKLDSPNPRT FVGSGKAEEI ADLARSYAAD VVIFDDELTP SQQSNLEKVV GKDVKVIDRT ALILDIFALH ATSKEGRLQV RLAQNQYLYP RLRGMWAHLA SNRMGGGVGS RFGEGESQLE VDRRLIRNRI TSIRRELALL SKKRDLQRKQ RKESGIYKVA LAGYTNAGKS SLLNAITGSE VLSYDKLFAT LDSTTRQLVL PKGREVTLTD TVGFIQKLPT TLVEAFKSTL DEINGADLIL HVVDSSDPNA DRQIDTVNMV LEQIGAEEIG RVEVFNKKDL LLPEQYEAMT IRYPNAVFTS TVTREGINDL VSRIGLVASS QEEILELLIP YSRGDMVSYA HQRCTILNEE YKDTGTLLTV RAGAQAVAKL KAFSCVAE // ID R6HXX8_9FIRM Unreviewed; 416 AA. AC R6HXX8; DT 24-JUL-2013, integrated into UniProtKB/TrEMBL. DT 24-JUL-2013, sequence version 1. DT 10-MAY-2017, entry version 24. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=BN517_01899 {ECO:0000313|EMBL:CDB41885.1}; OS Ruminococcus sp. CAG:177. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Ruminococcaceae; OC Ruminococcus; environmental samples. OX NCBI_TaxID=1262952 {ECO:0000313|EMBL:CDB41885.1, ECO:0000313|Proteomes:UP000018315}; RN [1] {ECO:0000313|EMBL:CDB41885.1, ECO:0000313|Proteomes:UP000018315} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MGS:177 {ECO:0000313|Proteomes:UP000018315}; RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., RA Sunagawa S., Plichta D., Gautier L., Le Chatelier E., Peletier E., RA Bonde I., Nielsen T., Manichanh C., Arumugam M., Batto J., RA Santos M.B.Q.D., Blom N., Borruel N., Burgdorf K.S., Boumezbeur F., RA Casellas F., Dore J., Guarner F., Hansen T., Hildebrand F., Kaas R.S., RA Kennedy S., Kristiansen K., Kultima J.R., Leonard P., Levenez F., RA Lund O., Moumen B., Le Paslier D., Pons N., Pedersen O., Prifti E., RA Qin J., Raes J., Tap J., Tims S., Ussery D.W., Yamada T., RA MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P., Wang J., RA Brunak S., Ehrlich S.D.; RT "Dependencies among metagenomic species, viruses, plasmids and units RT of genetic variation."; RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:CDB41885.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CBDQ010000065; CDB41885.1; -; Genomic_DNA. DR Proteomes; UP000018315; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000018315}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000018315}. FT DOMAIN 201 363 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 167 201 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 416 AA; 45844 MW; B4AB728325D1FEF8 CRC64; MTELFENIQK PETAVLVGVD LGEYDCEASL DELEELAKTA GAEVEARVTQ RRETPDSATF IGSGRLKEIK NFCADNDVDL LIFDSELTPS QQRNIEDITD VRVVDRTQLI LDIFAARARS GEGKLQVELA QLKYLLPRLG GKGTSMSRLG GGIGTRGPGE TKLESDRRHI RRRIKNLEDG IEALSRRRKL ARERREKDEV ETVAIVGYTN AGKSTLMNAL TQAGVLAEDK LFATLDPTSR ALTLPDGRRV MLIDTVGFIR RLPHGLVEAF KSTLEEAASA TLILNVCDAS SPDCAEHLEV TNRLLEELGC KGKPIIAVFN KCDAAPDLSW LSAGLHSVKI SALTGEGLDR LLNEMVRALP PTRKKVTLLL PYSMGSDAAL LREKGALDRE EYRPDGLKMT VTADAKLLER YKDYIV // ID R6HZC9_9FIRM Unreviewed; 412 AA. AC R6HZC9; DT 24-JUL-2013, integrated into UniProtKB/TrEMBL. DT 24-JUL-2013, sequence version 1. DT 12-APR-2017, entry version 23. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=BN556_00797 {ECO:0000313|EMBL:CDB43293.1}; OS Firmicutes bacterium CAG:240. OC Bacteria; Firmicutes; environmental samples. OX NCBI_TaxID=1263013 {ECO:0000313|EMBL:CDB43293.1, ECO:0000313|Proteomes:UP000018051}; RN [1] {ECO:0000313|EMBL:CDB43293.1, ECO:0000313|Proteomes:UP000018051} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MGS:240 {ECO:0000313|Proteomes:UP000018051}; RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., RA Sunagawa S., Plichta D., Gautier L., Le Chatelier E., Peletier E., RA Bonde I., Nielsen T., Manichanh C., Arumugam M., Batto J., RA Santos M.B.Q.D., Blom N., Borruel N., Burgdorf K.S., Boumezbeur F., RA Casellas F., Dore J., Guarner F., Hansen T., Hildebrand F., Kaas R.S., RA Kennedy S., Kristiansen K., Kultima J.R., Leonard P., Levenez F., RA Lund O., Moumen B., Le Paslier D., Pons N., Pedersen O., Prifti E., RA Qin J., Raes J., Tap J., Tims S., Ussery D.W., Yamada T., RA MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P., Wang J., RA Brunak S., Ehrlich S.D.; RT "Dependencies among metagenomic species, viruses, plasmids and units RT of genetic variation."; RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:CDB43293.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CBDR010000066; CDB43293.1; -; Genomic_DNA. DR Proteomes; UP000018051; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000018051}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000018051}. FT DOMAIN 188 348 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 147 181 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 412 AA; 46092 MW; 5DB1A15FA599E44B CRC64; MEQSERSSEI SMQELAALVE TAGGQAVGMM IQNRPTPDPR SFIGDGKVAE LKEFIEMNNC DLAVFDNELS PSQMRVLGEE LGVKVLDRSG LILDIFAQRA QTREGQLQVE LAQYKYLLPR LTGMWTHLVR QTASGGSSPI GTRGPGETQL ETDRRHIRRK IQKLEEELAA VRKVRSTQRR KREKNDVPVV ALVGYTNAGK STLLNCLTDA GIPANDRLFD TLDTTTRKLR IDEVTEVLIS DTVGFIRKLP HHLVEAFKAT LEELSYADVL LHVIDISNPD WEEQARVVDE LICQLGAEQT PCIRVFNKCD AYLGILPHGE DVICLSAKSG EGVQELVQRL SALLDRGNHK VTLRIPYSDA GIMDLLNREA AVTSLEYLDD GIKVEVTVPP EVFGKVKRYI PNYTEPKEDW ED // ID R6IB09_9FIRM Unreviewed; 604 AA. AC R6IB09; DT 24-JUL-2013, integrated into UniProtKB/TrEMBL. DT 24-JUL-2013, sequence version 1. DT 12-APR-2017, entry version 26. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=BN574_01297 {ECO:0000313|EMBL:CDB35197.1}; OS Phascolarctobacterium sp. CAG:266. OC Bacteria; Firmicutes; Negativicutes; Acidaminococcales; OC Acidaminococcaceae; Phascolarctobacterium. OX NCBI_TaxID=1262915 {ECO:0000313|EMBL:CDB35197.1, ECO:0000313|Proteomes:UP000014925}; RN [1] {ECO:0000313|EMBL:CDB35197.1, ECO:0000313|Proteomes:UP000014925} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MGS:266 {ECO:0000313|Proteomes:UP000014925}; RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., RA Sunagawa S., Plichta D., Gautier L., Le Chatelier E., Peletier E., RA Bonde I., Nielsen T., Manichanh C., Arumugam M., Batto J., RA Santos M.B.Q.D., Blom N., Borruel N., Burgdorf K.S., Boumezbeur F., RA Casellas F., Dore J., Guarner F., Hansen T., Hildebrand F., Kaas R.S., RA Kennedy S., Kristiansen K., Kultima J.R., Leonard P., Levenez F., RA Lund O., Moumen B., Le Paslier D., Pons N., Pedersen O., Prifti E., RA Qin J., Raes J., Tap J., Tims S., Ussery D.W., Yamada T., RA MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P., Wang J., RA Brunak S., Ehrlich S.D.; RT "Dependencies among metagenomic species, viruses, plasmids and units RT of genetic variation."; RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:CDB35197.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CBDN010000077; CDB35197.1; -; Genomic_DNA. DR Proteomes; UP000014925; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000014925}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000014925}. FT DOMAIN 382 548 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 604 AA; 67290 MW; 6BA44BE1D9DF44F9 CRC64; MREIKGNIKG IRDSVIAELQ KMYDMQSPQL VSQELAVKLA DITEYINREI SVYITRSGQI IEIAVGDNAT VELPSFSGRR GAGRLSGIRC IHTHPGGNPY LSGVDISALK NNKYDAMVAI GVVSPDFTKS ELTFGLITGI DSNENYTAEC YGPYSIEDAE NINFVNTVST IERILDKQTG TASLQVMSER AILIGMEWGR NDSLWTVDDS LEELKQLADT AGATVIKKFI QKRPKPDPAF FIGRGKVQEL ALYAQQENID LCIFDDELSP AQQRNIESVM GIRILDRTAL ILDIFAQRAR TNEGKLQVEL AQLQYTLPRI MGKGLMLSRL GGGIGTRGPG ETKLEVDRRR IRDRIAFIKD QIEKVKAVRS LHRSKRKKNN VFEVSLVGYT NAGKSTLLNT LTNSDIYAKD QLFATLDPTT RQLTLPNKQE IIITDTVGFI QRLPHQLIAA FRSTLEVVTE ADLLVHVIDV SHELYKEQAA AVHEVLKEIG AETKPVITVY NKIDKLPPDS KLTDRLALEE DTVCISAAKK LNLETLQQMI ESHLKSKAVE VTLCIPYAET AKAAQLHETA NVLEQEYTEN GAVMKVILPV EDLEAYNEYI LKSE // ID R6IPY6_9PROT Unreviewed; 440 AA. AC R6IPY6; DT 24-JUL-2013, integrated into UniProtKB/TrEMBL. DT 24-JUL-2013, sequence version 1. DT 12-APR-2017, entry version 22. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=BN570_00399 {ECO:0000313|EMBL:CDB40037.1}; OS Azospirillum sp. CAG:260. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales; OC Rhodospirillaceae; Azospirillum; environmental samples. OX NCBI_TaxID=1262706 {ECO:0000313|EMBL:CDB40037.1, ECO:0000313|Proteomes:UP000018110}; RN [1] {ECO:0000313|EMBL:CDB40037.1, ECO:0000313|Proteomes:UP000018110} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MGS:260 {ECO:0000313|Proteomes:UP000018110}; RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., RA Sunagawa S., Plichta D., Gautier L., Le Chatelier E., Peletier E., RA Bonde I., Nielsen T., Manichanh C., Arumugam M., Batto J., RA Santos M.B.Q.D., Blom N., Borruel N., Burgdorf K.S., Boumezbeur F., RA Casellas F., Dore J., Guarner F., Hansen T., Hildebrand F., Kaas R.S., RA Kennedy S., Kristiansen K., Kultima J.R., Leonard P., Levenez F., RA Lund O., Moumen B., Le Paslier D., Pons N., Pedersen O., Prifti E., RA Qin J., Raes J., Tap J., Tims S., Ussery D.W., Yamada T., RA MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P., Wang J., RA Brunak S., Ehrlich S.D.; RT "Dependencies among metagenomic species, viruses, plasmids and units RT of genetic variation."; RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:CDB40037.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CBDP010000047; CDB40037.1; -; Genomic_DNA. DR Proteomes; UP000018110; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000018110}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000018110}. FT DOMAIN 215 387 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 440 AA; 49138 MW; 1B3C00331B499A4C CRC64; MISKSVKTEL PGFETHKNYR PKAAVVFPSL PTSLIQLSPE ARLEEACGLA LAINLDVVFA DIVKLREVKP ATFLGHGYLE KLQEIIGSRD IELLIVDISL TPIQQRNLEK KLNIKVIDRT ALILEIFGER AKTREGKLQV ELAHLNYQRS RLVRSWTHLE RQRGGAGFLG GPGETQIELD RRIIDDKIVK IKKELQKVKQ TRALQRNARQ RVPYPVVALV GYTNAGKSSL FNRLAGADVF AKDLLFATLD PTMRRLRLPS GREIILSDTV GFISDLPHEL IMAFRATLEE VLEANLIVHV RDIANPNSGE QKKDVLSVLD NLGLKEVEQQ DKYIEVLNKT DLLTPEDHAS VLSLCERRLN VVPTSAVTGE GTGAFLRLVE EKLSAAHRQT QIKIPAADGR LLAWIYSNSE VLDCQTKGEN LLLNIKINAV NLAKLEAKLS // ID R6IXN6_9PROT Unreviewed; 436 AA. AC R6IXN6; DT 24-JUL-2013, integrated into UniProtKB/TrEMBL. DT 24-JUL-2013, sequence version 1. DT 12-APR-2017, entry version 22. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=BN554_00622 {ECO:0000313|EMBL:CDB54035.1}; OS Azospirillum sp. CAG:239. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales; OC Rhodospirillaceae; Azospirillum; environmental samples. OX NCBI_TaxID=1262705 {ECO:0000313|EMBL:CDB54035.1, ECO:0000313|Proteomes:UP000018213}; RN [1] {ECO:0000313|EMBL:CDB54035.1, ECO:0000313|Proteomes:UP000018213} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MGS:239 {ECO:0000313|Proteomes:UP000018213}; RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., RA Sunagawa S., Plichta D., Gautier L., Le Chatelier E., Peletier E., RA Bonde I., Nielsen T., Manichanh C., Arumugam M., Batto J., RA Santos M.B.Q.D., Blom N., Borruel N., Burgdorf K.S., Boumezbeur F., RA Casellas F., Dore J., Guarner F., Hansen T., Hildebrand F., Kaas R.S., RA Kennedy S., Kristiansen K., Kultima J.R., Leonard P., Levenez F., RA Lund O., Moumen B., Le Paslier D., Pons N., Pedersen O., Prifti E., RA Qin J., Raes J., Tap J., Tims S., Ussery D.W., Yamada T., RA MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P., Wang J., RA Brunak S., Ehrlich S.D.; RT "Dependencies among metagenomic species, viruses, plasmids and units RT of genetic variation."; RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:CDB54035.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CBDV010000130; CDB54035.1; -; Genomic_DNA. DR Proteomes; UP000018213; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000018213}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000018213}. FT DOMAIN 206 378 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 436 AA; 48959 MW; D943F149E9700985 CRC64; MAYVEIDRNY QVRAAVVFPN VLADSVSVTP ETRLEEAVGL ARAINLNVAY REIVKLREIK PSAYFSRGFV DRVKPLLETE EIELMIVDAS LTPIQQRNLE KTLKIKVIDR TALILEIFGE RAKTKEGRLQ VELAHLTYQR SRLVRSWTHL ERQRGGAGFL GGPGETQIEL DRRIIDDKIV RIRKELEKVK KTRELQRSAR KRIPYPVVAL VGYTNAGKST LFNCLSSAGV FAENLLFATL DPTMRRIRLP GGREVILSDT VGFISDLPHE LIMSFRATLE EVLEADVIVH VRDIANENSL AQKKDVLNVL KSLGLKNIEN ESGYIEVLNK IDLLDEAGRR YLEENAARNA NVVPLSAVSG EGTERFLRLV EDKLSASFRM VEVTTDAADG KLISWIYKNT DVISAAAKGE RMILRLKADD AAISKLKNKT PVRTLG // ID R6J0J6_9CLOT Unreviewed; 418 AA. AC R6J0J6; DT 24-JUL-2013, integrated into UniProtKB/TrEMBL. DT 24-JUL-2013, sequence version 1. DT 12-APR-2017, entry version 23. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=BN539_01104 {ECO:0000313|EMBL:CDB51206.1}; OS Clostridium sp. CAG:217. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium; environmental samples. OX NCBI_TaxID=1262779 {ECO:0000313|EMBL:CDB51206.1, ECO:0000313|Proteomes:UP000018364}; RN [1] {ECO:0000313|EMBL:CDB51206.1, ECO:0000313|Proteomes:UP000018364} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MGS:217 {ECO:0000313|Proteomes:UP000018364}; RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., RA Sunagawa S., Plichta D., Gautier L., Le Chatelier E., Peletier E., RA Bonde I., Nielsen T., Manichanh C., Arumugam M., Batto J., RA Santos M.B.Q.D., Blom N., Borruel N., Burgdorf K.S., Boumezbeur F., RA Casellas F., Dore J., Guarner F., Hansen T., Hildebrand F., Kaas R.S., RA Kennedy S., Kristiansen K., Kultima J.R., Leonard P., Levenez F., RA Lund O., Moumen B., Le Paslier D., Pons N., Pedersen O., Prifti E., RA Qin J., Raes J., Tap J., Tims S., Ussery D.W., Yamada T., RA MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P., Wang J., RA Brunak S., Ehrlich S.D.; RT "Dependencies among metagenomic species, viruses, plasmids and units RT of genetic variation."; RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:CDB51206.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CBDU010000037; CDB51206.1; -; Genomic_DNA. DR Proteomes; UP000018364; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000018364}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000018364}. FT DOMAIN 203 365 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 162 196 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 418 AA; 45622 MW; AF1BC8591771BBB1 CRC64; MAYQWTKTDA AAPERVLLIG LDCGDYDAEA SMAELERLTD TAGGLVVGHT VQKRPAPEGA TYIGSGLVES LAEFCRQNEV DLTVADGSLT PVQARNLERA LGTAVIDRTA LILDIFAARA RSSEGKLQVE LAQLQYRLPR LGGQGNSLSR LGGGIGTRGP GESKLESDRR HIRRRITALQ RELKTVQERR ERMHLRRQKN RALTVALVGY TNAGKSTLMN ALTDAGVLVA DQLFATLDPT ARRLVLPSGR QVMLVDTVGL VQRLPHELVD AFRSTLAEAA WADVILDVCD ASDPACNSQM QVTAQVLDSL SCGGKPLLHV LNKCDRVPEE ERFPLLGTSV RISARTGEGL PQLLAEIDRL LPGQWARAAL CIPFDRGDLT DRLHREGKVL AEDYTPAGTR LQVLADPALL EELRPYFI // ID R6J8G5_9FIRM Unreviewed; 603 AA. AC R6J8G5; DT 24-JUL-2013, integrated into UniProtKB/TrEMBL. DT 24-JUL-2013, sequence version 1. DT 10-MAY-2017, entry version 26. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=BN533_01603 {ECO:0000313|EMBL:CDB46547.1}; OS Phascolarctobacterium sp. CAG:207. OC Bacteria; Firmicutes; Negativicutes; Acidaminococcales; OC Acidaminococcaceae; Phascolarctobacterium. OX NCBI_TaxID=1262914 {ECO:0000313|EMBL:CDB46547.1, ECO:0000313|Proteomes:UP000014944}; RN [1] {ECO:0000313|EMBL:CDB46547.1, ECO:0000313|Proteomes:UP000014944} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MGS:207 {ECO:0000313|Proteomes:UP000014944}; RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., RA Sunagawa S., Plichta D., Gautier L., Le Chatelier E., Peletier E., RA Bonde I., Nielsen T., Manichanh C., Arumugam M., Batto J., RA Santos M.B.Q.D., Blom N., Borruel N., Burgdorf K.S., Boumezbeur F., RA Casellas F., Dore J., Guarner F., Hansen T., Hildebrand F., Kaas R.S., RA Kennedy S., Kristiansen K., Kultima J.R., Leonard P., Levenez F., RA Lund O., Moumen B., Le Paslier D., Pons N., Pedersen O., Prifti E., RA Qin J., Raes J., Tap J., Tims S., Ussery D.W., Yamada T., RA MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P., Wang J., RA Brunak S., Ehrlich S.D.; RT "Dependencies among metagenomic species, viruses, plasmids and units RT of genetic variation."; RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:CDB46547.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CBDS010000087; CDB46547.1; -; Genomic_DNA. DR Proteomes; UP000014944; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000014944}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000014944}. FT DOMAIN 384 550 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 603 AA; 66915 MW; 546AD72361ABAAE6 CRC64; MREILGNKKG IRDSVLNELI ALYDVQVPLG QLISAELALK LADITEFINR EISLYISRSG QITNIVIGGN DSVELPAVEG RRGIGRLSGI RCVHTHPNGN PVLSGVDFSA LKNNKFDAMV TIGVTAPDYT QSIISFGMIV GLDKEEQFIC DEYGPFSLEE AEAINFLNVI NTIERILDKQ TSSSSLAVAA EKTILVGMDW GQIKGGWTAE DSLEELKQLA DTAGAVVVNR FIQRRAKPDP AFFIGKGKVQ ELALHAQQEN IDLCIFDDEL TPAQQRNIEQ VMGVRILDRT ALILDIFAQR ARTNEGKLQV ELAQLQYNLP RIMGKGLILS RLGGGIGTRG PGETKLEVDR RRIRDRIAFI KDSIEKVRAV RTLHRIKRAK NQVPSISLVG YTNAGKSTLL NLLTQSDIYA KDQLFATLDP TTRQLILPDK HEAILTDTVG FIQRLPHQLV AAFRSTLEEV AEADLLLHVI DVSHELYQEQ SDAVYKVLEQ IGAQNKTILT VYNKIDKLPS ENALAQRLAQ QENSVCISAK SGIGIEELLA LISENLKLKS IEVTLLIPYT ESEKAAKLHT IGTVLEQEYK ENGTFMKVRL ASEQLEDFEK FII // ID R6JTB0_9CLOT Unreviewed; 426 AA. AC R6JTB0; DT 24-JUL-2013, integrated into UniProtKB/TrEMBL. DT 24-JUL-2013, sequence version 1. DT 12-APR-2017, entry version 24. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=BN486_00761 {ECO:0000313|EMBL:CDB64510.1}; OS Clostridium clostridioforme CAG:132. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium; environmental samples. OX NCBI_TaxID=1263065 {ECO:0000313|EMBL:CDB64510.1, ECO:0000313|Proteomes:UP000018009}; RN [1] {ECO:0000313|EMBL:CDB64510.1, ECO:0000313|Proteomes:UP000018009} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MGS:132 {ECO:0000313|Proteomes:UP000018009}; RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., RA Sunagawa S., Plichta D., Gautier L., Le Chatelier E., Peletier E., RA Bonde I., Nielsen T., Manichanh C., Arumugam M., Batto J., RA Santos M.B.Q.D., Blom N., Borruel N., Burgdorf K.S., Boumezbeur F., RA Casellas F., Dore J., Guarner F., Hansen T., Hildebrand F., Kaas R.S., RA Kennedy S., Kristiansen K., Kultima J.R., Leonard P., Levenez F., RA Lund O., Moumen B., Le Paslier D., Pons N., Pedersen O., Prifti E., RA Qin J., Raes J., Tap J., Tims S., Ussery D.W., Yamada T., RA MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P., Wang J., RA Brunak S., Ehrlich S.D.; RT "Dependencies among metagenomic species, viruses, plasmids and units RT of genetic variation."; RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:CDB64510.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CBDY010000433; CDB64510.1; -; Genomic_DNA. DR Proteomes; UP000018009; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000018009}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000018009}. FT DOMAIN 202 375 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 426 AA; 48002 MW; 48A1F2CC6C9304BD CRC64; MAELIDLSEL QEKVILVAVS TAEEEDTPAS LDELEELAST AGAVTVARII QNREKVHPGT YLGKGKIDEV RELLWDTRAT GVICDDELSP AQLRNLEDAL DTKVMDRTMV ILDIFASRAS TREGKIQVEL AQLKYRAVRL VGMRNSLSRL GGGIGTRGPG EKKLETDRRL IHQRIGQLKE ELADVKRHRE VTRQQREKNF ALSAAIVGYT NAGKSTLLNR LTGAGILAED KLFATLDPTT RSYTLEDGQQ ILLTDTVGFI RKLPHHLIEA FKSTLEEARY SDIVLHVVDC SNPQMDMQMH VVKETLKELE IVDKTIVTVF NKVDRFRELE AMGDSSVMQI PRDFSSDYQV RISARTGEGM EELQKVLQAI IRSRRILLEK VFPYSRAGRI QTIRKYGQLL EEEYQEDGIA VKAYVPAELF GKLYSD // ID R6KBT5_9BACE Unreviewed; 419 AA. AC R6KBT5; DT 24-JUL-2013, integrated into UniProtKB/TrEMBL. DT 24-JUL-2013, sequence version 1. DT 12-APR-2017, entry version 23. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=BN506_03697 {ECO:0000313|EMBL:CDB72583.1}; OS Bacteroides cellulosilyticus CAG:158. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae; OC Bacteroides; environmental samples. OX NCBI_TaxID=1263038 {ECO:0000313|EMBL:CDB72583.1, ECO:0000313|Proteomes:UP000018191}; RN [1] {ECO:0000313|EMBL:CDB72583.1, ECO:0000313|Proteomes:UP000018191} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MGS:158 {ECO:0000313|Proteomes:UP000018191}; RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., RA Sunagawa S., Plichta D., Gautier L., Le Chatelier E., Peletier E., RA Bonde I., Nielsen T., Manichanh C., Arumugam M., Batto J., RA Santos M.B.Q.D., Blom N., Borruel N., Burgdorf K.S., Boumezbeur F., RA Casellas F., Dore J., Guarner F., Hansen T., Hildebrand F., Kaas R.S., RA Kennedy S., Kristiansen K., Kultima J.R., Leonard P., Levenez F., RA Lund O., Moumen B., Le Paslier D., Pons N., Pedersen O., Prifti E., RA Qin J., Raes J., Tap J., Tims S., Ussery D.W., Yamada T., RA MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P., Wang J., RA Brunak S., Ehrlich S.D.; RT "Dependencies among metagenomic species, viruses, plasmids and units RT of genetic variation."; RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:CDB72583.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CBEB010000321; CDB72583.1; -; Genomic_DNA. DR Proteomes; UP000018191; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000018191}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000018191}. FT DOMAIN 216 400 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 419 AA; 47866 MW; 87789EAE1CDDEA97 CRC64; MKEFVISEVQ AETAVLVGLI TKTQDERKTN EYLDELEFLA ETAGAEVVKR FTQKLDQAHS VTYVGKGKLE EIKEYIRNEE EAEREIGMVI FDDELSAKQI RNIEAELKIK ILDRTSLILD IFAMRAQTAN AKTQVELAQY KYMLPRLQRL WTHLERQGGG SGAGGGKGSV GLRGPGETQL EMDRRIILNR MSLLKERLAE IDKQKSTQRK NRGRMIRAAL VGYTNVGKST LMNLLAKSEV FAENKLFATL DTTVRKVIID NLPFLLSDTV GFIRKLPTDL VDSFKSTLDE VREADLLLHI VDISHPDFEE QIEVVNKTLA DIGASGKPII LVFNKIDAYT YVEKAADDLT PRTKENLTLE ELMKTWMAKM EDNCLFISAR EKINLEELKS VVYARVKELH VQKYPYNDFL YQTYEEEEE // ID R6L1Z5_9FIRM Unreviewed; 415 AA. AC R6L1Z5; DT 24-JUL-2013, integrated into UniProtKB/TrEMBL. DT 24-JUL-2013, sequence version 1. DT 10-MAY-2017, entry version 25. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=BN552_02247 {ECO:0000313|EMBL:CDB77474.1}; OS Blautia sp. CAG:237. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Lachnospiraceae; OC Blautia; environmental samples. OX NCBI_TaxID=1262755 {ECO:0000313|EMBL:CDB77474.1, ECO:0000313|Proteomes:UP000017983}; RN [1] {ECO:0000313|EMBL:CDB77474.1, ECO:0000313|Proteomes:UP000017983} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MGS:237 {ECO:0000313|Proteomes:UP000017983}; RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., RA Sunagawa S., Plichta D., Gautier L., Le Chatelier E., Peletier E., RA Bonde I., Nielsen T., Manichanh C., Arumugam M., Batto J., RA Santos M.B.Q.D., Blom N., Borruel N., Burgdorf K.S., Boumezbeur F., RA Casellas F., Dore J., Guarner F., Hansen T., Hildebrand F., Kaas R.S., RA Kennedy S., Kristiansen K., Kultima J.R., Leonard P., Levenez F., RA Lund O., Moumen B., Le Paslier D., Pons N., Pedersen O., Prifti E., RA Qin J., Raes J., Tap J., Tims S., Ussery D.W., Yamada T., RA MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P., Wang J., RA Brunak S., Ehrlich S.D.; RT "Dependencies among metagenomic species, viruses, plasmids and units RT of genetic variation."; RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:CDB77474.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CBED010000107; CDB77474.1; -; Genomic_DNA. DR Proteomes; UP000017983; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000017983}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000017983}. FT DOMAIN 201 364 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 415 AA; 45980 MW; 0CE8E9BF20BC9934 CRC64; MQFYEFKETQ ERVILIGVQT EVGDDVEASL DELEELAETA GAETVAKVIQ NREAVHPGTY IGKGKIEEVA SLLRALDANG VICDDELSPA QLNNLERELD CKVMDRTLLI LDIFAGRAVS SEGKIQVELA QLRYRAARLV GLRESLSRLG GGIGTRGPGE KKLETDRRLI RTRISALKAE LAQVEKHREL IRGKRSRGNL KTAAIVGYTN AGKSTLLNTL TGAGILAEDK LFATLDPTTR VLELKDGQQI LLTDTVGFIR KLPHHLVEAF KSTLEEAKYA DYIIHVVDAS NPQAELQMFT VYETLRELGA TGKKIVTLLN KQDQVTGSGI RDLKADYTVK CSARTGEGLD EFKDVLAKLL AEDQIYLEEL YPYSEAGKIQ KIREFGSLLS EEYREDGIFV KARVPAEIFV SVMPK // ID R6LH44_9FIRM Unreviewed; 413 AA. AC R6LH44; DT 24-JUL-2013, integrated into UniProtKB/TrEMBL. DT 24-JUL-2013, sequence version 1. DT 12-APR-2017, entry version 24. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=BN524_01940 {ECO:0000313|EMBL:CDB85155.1}; OS Coprococcus comes CAG:19. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Lachnospiraceae; OC Coprococcus; environmental samples. OX NCBI_TaxID=1263070 {ECO:0000313|EMBL:CDB85155.1, ECO:0000313|Proteomes:UP000017957}; RN [1] {ECO:0000313|EMBL:CDB85155.1, ECO:0000313|Proteomes:UP000017957} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MGS:19 {ECO:0000313|Proteomes:UP000017957}; RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., RA Sunagawa S., Plichta D., Gautier L., Le Chatelier E., Peletier E., RA Bonde I., Nielsen T., Manichanh C., Arumugam M., Batto J., RA Santos M.B.Q.D., Blom N., Borruel N., Burgdorf K.S., Boumezbeur F., RA Casellas F., Dore J., Guarner F., Hansen T., Hildebrand F., Kaas R.S., RA Kennedy S., Kristiansen K., Kultima J.R., Leonard P., Levenez F., RA Lund O., Moumen B., Le Paslier D., Pons N., Pedersen O., Prifti E., RA Qin J., Raes J., Tap J., Tims S., Ussery D.W., Yamada T., RA MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P., Wang J., RA Brunak S., Ehrlich S.D.; RT "Dependencies among metagenomic species, viruses, plasmids and units RT of genetic variation."; RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:CDB85155.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CBEG010000088; CDB85155.1; -; Genomic_DNA. DR Proteomes; UP000017957; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000017957}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000017957}. FT DOMAIN 201 365 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 160 194 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 413 AA; 46651 MW; D97F4744985D56F8 CRC64; MALYEIKEEK ERVILVGVST RENDDTEDSL DELKDLVKTA GAEAVGRVIQ KRELVHPGTY VGKGKIEEIR ELLWELDATG IVCDDELSPA QMNNLTDILD VKVMDRTMVI LDIFAGRAST SEGKIQVELA QLKYRQSQLT GAGRAMSRLG GGIGTRGPGE KKLEMDRRLI KNRIAQLNRE LREVKRHREL TREQRTKNRI PVVAIVGYTN AGKSTLLNTL TGAGVLQEDQ LFATLDPTTR SRKLPSGQEI LLTDTVGFIR KLPHHLIDAF KSTLEEAKYA DLILHVVDAS NPQMDEQMYV VYETLQRLEA MDKPVVTAFN KMDRIGESLT VRDFKADRIV QVSAKTGEGL EALLQAIEEI LREQKIYIER VYSYQESGKI QLIRKYGELL EEEYKEDGIH VSAYVPKELD GRV // ID R6LIK4_9FIRM Unreviewed; 417 AA. AC R6LIK4; DT 24-JUL-2013, integrated into UniProtKB/TrEMBL. DT 24-JUL-2013, sequence version 1. DT 12-APR-2017, entry version 23. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=BN515_01511 {ECO:0000313|EMBL:CDB87318.1}; OS Firmicutes bacterium CAG:170. OC Bacteria; Firmicutes; environmental samples. OX NCBI_TaxID=1263006 {ECO:0000313|EMBL:CDB87318.1, ECO:0000313|Proteomes:UP000018279}; RN [1] {ECO:0000313|EMBL:CDB87318.1, ECO:0000313|Proteomes:UP000018279} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MGS:170 {ECO:0000313|Proteomes:UP000018279}; RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., RA Sunagawa S., Plichta D., Gautier L., Le Chatelier E., Peletier E., RA Bonde I., Nielsen T., Manichanh C., Arumugam M., Batto J., RA Santos M.B.Q.D., Blom N., Borruel N., Burgdorf K.S., Boumezbeur F., RA Casellas F., Dore J., Guarner F., Hansen T., Hildebrand F., Kaas R.S., RA Kennedy S., Kristiansen K., Kultima J.R., Leonard P., Levenez F., RA Lund O., Moumen B., Le Paslier D., Pons N., Pedersen O., Prifti E., RA Qin J., Raes J., Tap J., Tims S., Ussery D.W., Yamada T., RA MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P., Wang J., RA Brunak S., Ehrlich S.D.; RT "Dependencies among metagenomic species, viruses, plasmids and units RT of genetic variation."; RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:CDB87318.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CBEH010000171; CDB87318.1; -; Genomic_DNA. DR Proteomes; UP000018279; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000018279}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000018279}. FT DOMAIN 203 363 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 169 196 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 417 AA; 46402 MW; 877CCC018880B0DE CRC64; MEEKKIIIDR AILVGLNADC FTPEETSDEK TLDELEALLE TAGGECAGKV LQNKHTPDPH SFIGEGKADE VRQMVQSSGA NLVIFDNDLT PSQLRTLEDL MKAPVLDRSA LILDIFAQRA KTREGKLQVE LAQYQYYLPR LTVWNEEMGR LGGGIGTRGP GETQLETDKR YIRSRIQKLR AELEEVRKVR AVQRRRRIKN DVPVVALVGY TNAGKSTLLN YLTGADIPAN NRLFDTLDTT TRQLSLSDTC DVLLSDTVGF IAKLPHHLVE AFKATLEELQ YADLLIHVID ASDPEREAHM QVVERLIGEL AKPGVPVIDC YNKCDIAENG APRGENNVEI SARTGEGIDA LKALAERLLE RGLHHVRLCL PYSMGGMVDT LHSQAKVLSC RYEAEGILVE AIMDETLYGR LLPYVTE // ID R6MSW9_9FIRM Unreviewed; 416 AA. AC R6MSW9; DT 24-JUL-2013, integrated into UniProtKB/TrEMBL. DT 24-JUL-2013, sequence version 1. DT 12-APR-2017, entry version 23. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=BN531_00283 {ECO:0000313|EMBL:CDC02803.1}; OS Eubacterium sp. CAG:202. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Eubacteriaceae; OC Eubacterium; environmental samples. OX NCBI_TaxID=1262884 {ECO:0000313|EMBL:CDC02803.1, ECO:0000313|Proteomes:UP000017996}; RN [1] {ECO:0000313|EMBL:CDC02803.1, ECO:0000313|Proteomes:UP000017996} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MGS:202 {ECO:0000313|Proteomes:UP000017996}; RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., RA Sunagawa S., Plichta D., Gautier L., Le Chatelier E., Peletier E., RA Bonde I., Nielsen T., Manichanh C., Arumugam M., Batto J., RA Santos M.B.Q.D., Blom N., Borruel N., Burgdorf K.S., Boumezbeur F., RA Casellas F., Dore J., Guarner F., Hansen T., Hildebrand F., Kaas R.S., RA Kennedy S., Kristiansen K., Kultima J.R., Leonard P., Levenez F., RA Lund O., Moumen B., Le Paslier D., Pons N., Pedersen O., Prifti E., RA Qin J., Raes J., Tap J., Tims S., Ussery D.W., Yamada T., RA MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P., Wang J., RA Brunak S., Ehrlich S.D.; RT "Dependencies among metagenomic species, viruses, plasmids and units RT of genetic variation."; RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:CDC02803.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CBEO010000139; CDC02803.1; -; Genomic_DNA. DR Proteomes; UP000017996; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR Gene3D; 3.40.640.10; -; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major_sub1. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000017996}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000017996}. FT DOMAIN 200 362 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 166 193 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 416 AA; 45787 MW; 372D40C185A945C1 CRC64; MEMISNEEKI TQAVLVSVDT GDYDAEASLA ELKELVKSAG AEPVFTVTQN LKRPETGTYV GTGKLQEIAD ICKQQEIDLL VFDCELSPTQ IRNIEAETDT RTIDRTMLIL DIFALRARSK EGKLQVELAQ LKYLMPRLTG KGVAMSRLGG GIGTRGPGET KLETDRRHIS RRMETLKSEL AEVEQHRSML RKRREKDGVI TCAIVGYTNA GKSTLMNYLT DAGVLAQDKL FATLDPTSRA LKLPSGVTVM MIDTVGLVRR LPHHLVEAFR STLEEAALSD IILNVCDASS DEARVHMQVT TDLLNSLGCG DTPIITVLNK CDLLEEESFP QEIGSYVKIS AKNGTGIDDL LKAVDDNLPV RVKRVSLLIP FSDAGLVAEI RKSATLISEE YVAEGIKVEA ILDEKLYSKA EKYIVD // ID R6MT73_9BACE Unreviewed; 418 AA. AC R6MT73; DT 24-JUL-2013, integrated into UniProtKB/TrEMBL. DT 24-JUL-2013, sequence version 1. DT 12-APR-2017, entry version 23. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=BN659_00424 {ECO:0000313|EMBL:CDB99074.1}; OS Bacteroides sp. CAG:443. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae; OC Bacteroides; environmental samples. OX NCBI_TaxID=1262739 {ECO:0000313|EMBL:CDB99074.1, ECO:0000313|Proteomes:UP000018098}; RN [1] {ECO:0000313|EMBL:CDB99074.1, ECO:0000313|Proteomes:UP000018098} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MGS:443 {ECO:0000313|Proteomes:UP000018098}; RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., RA Sunagawa S., Plichta D., Gautier L., Le Chatelier E., Peletier E., RA Bonde I., Nielsen T., Manichanh C., Arumugam M., Batto J., RA Santos M.B.Q.D., Blom N., Borruel N., Burgdorf K.S., Boumezbeur F., RA Casellas F., Dore J., Guarner F., Hansen T., Hildebrand F., Kaas R.S., RA Kennedy S., Kristiansen K., Kultima J.R., Leonard P., Levenez F., RA Lund O., Moumen B., Le Paslier D., Pons N., Pedersen O., Prifti E., RA Qin J., Raes J., Tap J., Tims S., Ussery D.W., Yamada T., RA MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P., Wang J., RA Brunak S., Ehrlich S.D.; RT "Dependencies among metagenomic species, viruses, plasmids and units RT of genetic variation."; RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:CDB99074.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CBEN010000071; CDB99074.1; -; Genomic_DNA. DR Proteomes; UP000018098; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000018098}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000018098}. FT DOMAIN 217 401 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 418 AA; 47529 MW; CD1A5C2A1EC3094C CRC64; MKEFVISEAQ TEKAALVGLI TQTQNERKTN EYLDELAFLA ETAGAEVVKR FTQKLDTPNS VTYVGKGKLQ EIKEYLLQQH EEGGEEVGMV IFDDELSAKQ IRNIEKELNV KILDRTSLIL DIFAMRAQTA NAKTQVELAQ YKYMLPRLQR LWTHLERQGG GSGAGGGKGS VGLRGPGETQ LEMDRRIILN RMALLKQRLA DIDTQKSTQR KNRGRLIRVA LVGYTNVGKS TLMNLLAKSE VFAENKLFAT LDTTVRKVII DNLPFLLSDT VGFIRKLPTD LVDSFKSTLD EVREADLLLH VVDISHPDFE EQIQVVDKTI ADLGAGGKPT MIIFNKIDAY TYVEKAEDDL TPKTKENITL EELMHTWMAK MNDNCIFISA RNKTNIDELK DIVYKKVREL HVQKYPYNDF LYQTYDEE // ID R6MU69_9CLOT Unreviewed; 427 AA. AC R6MU69; DT 24-JUL-2013, integrated into UniProtKB/TrEMBL. DT 24-JUL-2013, sequence version 1. DT 12-APR-2017, entry version 23. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=BN565_01565 {ECO:0000313|EMBL:CDB89372.1}; OS Clostridium sp. CAG:253. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium; environmental samples. OX NCBI_TaxID=1262785 {ECO:0000313|EMBL:CDB89372.1, ECO:0000313|Proteomes:UP000018071}; RN [1] {ECO:0000313|EMBL:CDB89372.1, ECO:0000313|Proteomes:UP000018071} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MGS:253 {ECO:0000313|Proteomes:UP000018071}; RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., RA Sunagawa S., Plichta D., Gautier L., Le Chatelier E., Peletier E., RA Bonde I., Nielsen T., Manichanh C., Arumugam M., Batto J., RA Santos M.B.Q.D., Blom N., Borruel N., Burgdorf K.S., Boumezbeur F., RA Casellas F., Dore J., Guarner F., Hansen T., Hildebrand F., Kaas R.S., RA Kennedy S., Kristiansen K., Kultima J.R., Leonard P., Levenez F., RA Lund O., Moumen B., Le Paslier D., Pons N., Pedersen O., Prifti E., RA Qin J., Raes J., Tap J., Tims S., Ussery D.W., Yamada T., RA MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P., Wang J., RA Brunak S., Ehrlich S.D.; RT "Dependencies among metagenomic species, viruses, plasmids and units RT of genetic variation."; RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:CDB89372.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CBEI010000063; CDB89372.1; -; Genomic_DNA. DR Proteomes; UP000018071; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000018071}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000018071}. FT DOMAIN 203 367 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 169 196 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 427 AA; 48350 MW; A6F5CA30CD970FEB CRC64; MEEKLYDTSE QKERIIVVGV ATSENDDTDK SLDELIELGQ TAGVETVAKV IQNREKVHPG TYIGKGKIEE VRELVIKHKA DTVVCDDELT PAQFNNLSQM LDVKVVDRTV MILDIFAKRA STSEGKLQVE LAQLRYRASH LIGGRSELSR LGGGIGTRGP GEQKLEMDRR LIKERITQVR KELEQVKRTR ELTRKKRQEN PIPVVAIVGY TNAGKSTLLN HLTGAGVLSE DKLFATLDPT TRKLVRENGE EILFTDTVGF IRKLPHHLIQ AFRSTLEEAK YADLILHVVD CSNEDMDSQM YTVYETLKKL EVGDKKIITA FNKIDVCDRE ETLKDLAADR TVRISAKTGQ GIEQMLSAIS EVIAEGKQLL DKVFGYDEAG AVSNVRKYGQ VMEEEYRNEG IYIKALIPRE YMYLFVEEKK KKEAWEE // ID R6N001_9FIRM Unreviewed; 419 AA. AC R6N001; DT 24-JUL-2013, integrated into UniProtKB/TrEMBL. DT 24-JUL-2013, sequence version 1. DT 12-APR-2017, entry version 23. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=BN647_00266 {ECO:0000313|EMBL:CDB99661.1}; OS Firmicutes bacterium CAG:41. OC Bacteria; Firmicutes; environmental samples. OX NCBI_TaxID=1263021 {ECO:0000313|EMBL:CDB99661.1, ECO:0000313|Proteomes:UP000018139}; RN [1] {ECO:0000313|EMBL:CDB99661.1, ECO:0000313|Proteomes:UP000018139} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MGS:41 {ECO:0000313|Proteomes:UP000018139}; RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., RA Sunagawa S., Plichta D., Gautier L., Le Chatelier E., Peletier E., RA Bonde I., Nielsen T., Manichanh C., Arumugam M., Batto J., RA Santos M.B.Q.D., Blom N., Borruel N., Burgdorf K.S., Boumezbeur F., RA Casellas F., Dore J., Guarner F., Hansen T., Hildebrand F., Kaas R.S., RA Kennedy S., Kristiansen K., Kultima J.R., Leonard P., Levenez F., RA Lund O., Moumen B., Le Paslier D., Pons N., Pedersen O., Prifti E., RA Qin J., Raes J., Tap J., Tims S., Ussery D.W., Yamada T., RA MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P., Wang J., RA Brunak S., Ehrlich S.D.; RT "Dependencies among metagenomic species, viruses, plasmids and units RT of genetic variation."; RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:CDB99661.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CBEM010000189; CDB99661.1; -; Genomic_DNA. DR Proteomes; UP000018139; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000018139}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000018139}. FT DOMAIN 203 366 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 162 196 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 419 AA; 46892 MW; 6D739C1C208A5EC8 CRC64; MEYNEQKQER VILAGVHRGM RDALWDTTEE SIHELGELVK TAGGIVVGEM IQNKADLESA TYMGEGKLDE LKIAIETLNA DMIVFDDELS PVQMRNISDF LEIKVLDRSM LILDIFAMRA KSGEGKLQVE LAQLKYRLPR LRGFGVEMSR TGAGIGTRGP GETRLESDRR HIRRRISALE EEIKELKKHR GLIRDRRKKD GVITAALVGY TNAGKSTLLN TLTDAQVFAE DKLFATLDPT SRAITLDDNR KILLVDTVGF IRKLPHHLIE AFKSTLEEAV VADVLLHVID ASGEEMDNQI TVVEQVLSDI GAVGKPVVAV FNKCDRLEDY PITNLKSDKC VYISAKHRTN IDKLIEAIAD TAPGKKQKVK ACIPYSAGSL VNELHENQKV ISEEYGENGT VMELMVDAQM YDKIREYIL // ID R6N549_9CLOT Unreviewed; 419 AA. AC R6N549; DT 24-JUL-2013, integrated into UniProtKB/TrEMBL. DT 24-JUL-2013, sequence version 1. DT 12-APR-2017, entry version 23. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=BN578_01313 {ECO:0000313|EMBL:CDC06145.1}; OS Clostridium leptum CAG:27. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium; environmental samples. OX NCBI_TaxID=1263068 {ECO:0000313|EMBL:CDC06145.1, ECO:0000313|Proteomes:UP000018168}; RN [1] {ECO:0000313|EMBL:CDC06145.1, ECO:0000313|Proteomes:UP000018168} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MGS:27 {ECO:0000313|Proteomes:UP000018168}; RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., RA Sunagawa S., Plichta D., Gautier L., Le Chatelier E., Peletier E., RA Bonde I., Nielsen T., Manichanh C., Arumugam M., Batto J., RA Santos M.B.Q.D., Blom N., Borruel N., Burgdorf K.S., Boumezbeur F., RA Casellas F., Dore J., Guarner F., Hansen T., Hildebrand F., Kaas R.S., RA Kennedy S., Kristiansen K., Kultima J.R., Leonard P., Levenez F., RA Lund O., Moumen B., Le Paslier D., Pons N., Pedersen O., Prifti E., RA Qin J., Raes J., Tap J., Tims S., Ussery D.W., Yamada T., RA MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P., Wang J., RA Brunak S., Ehrlich S.D.; RT "Dependencies among metagenomic species, viruses, plasmids and units RT of genetic variation."; RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:CDC06145.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CBEP010000145; CDC06145.1; -; Genomic_DNA. DR ProteinModelPortal; R6N549; -. DR Proteomes; UP000018168; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000018168}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000018168}. FT DOMAIN 200 362 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 159 196 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 419 AA; 46493 MW; 4CCBEC308CA46D7B CRC64; MEFYENEVRP ERAFLVSVDT GEFDAEASMS ELYELTESAG AQPVGAMIQK REKPDGATCI GSGRLEELKE VCQSQEIDLI IFDCELSPTQ IRNLEFETEV RIIDRTMLIL DIFASRARSR EGKLQVELAQ LKYLLPRLTG KGAAMSRLGG GIGTRGPGES KLETDRRHIR RRLESLREQL AQVEQHRNQL RRRREKEGII TAAIVGYTNA GKSTLMNTLT DAGVLAEDKL FATLDPTSRA LKLPNGVSVM LIDTVGLVRR LPHHLVEAFH STLEEAALAD MILNVCDASS PEAQVHLEVT RKLLADLGCT GRPVIPVMNK CDLVPSLLDI PMIGNAVRIS AKTGEGIGDL LAAVEENLPV SLRRVCLLLP FDQAGLVAQI RKDHVLYQEE YRPDGIFVSA LLDPVLYGRV REYEILENT // ID R6NIV0_9FIRM Unreviewed; 416 AA. AC R6NIV0; DT 24-JUL-2013, integrated into UniProtKB/TrEMBL. DT 24-JUL-2013, sequence version 1. DT 12-APR-2017, entry version 24. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=BN662_02196 {ECO:0000313|EMBL:CDC12053.1}; OS Roseburia sp. CAG:45. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Lachnospiraceae; OC Roseburia; environmental samples. OX NCBI_TaxID=1262947 {ECO:0000313|EMBL:CDC12053.1, ECO:0000313|Proteomes:UP000018173}; RN [1] {ECO:0000313|EMBL:CDC12053.1, ECO:0000313|Proteomes:UP000018173} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MGS:45 {ECO:0000313|Proteomes:UP000018173}; RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., RA Sunagawa S., Plichta D., Gautier L., Le Chatelier E., Peletier E., RA Bonde I., Nielsen T., Manichanh C., Arumugam M., Batto J., RA Santos M.B.Q.D., Blom N., Borruel N., Burgdorf K.S., Boumezbeur F., RA Casellas F., Dore J., Guarner F., Hansen T., Hildebrand F., Kaas R.S., RA Kennedy S., Kristiansen K., Kultima J.R., Leonard P., Levenez F., RA Lund O., Moumen B., Le Paslier D., Pons N., Pedersen O., Prifti E., RA Qin J., Raes J., Tap J., Tims S., Ussery D.W., Yamada T., RA MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P., Wang J., RA Brunak S., Ehrlich S.D.; RT "Dependencies among metagenomic species, viruses, plasmids and units RT of genetic variation."; RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:CDC12053.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CBET010000075; CDC12053.1; -; Genomic_DNA. DR Proteomes; UP000018173; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000018173}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000018173}. FT DOMAIN 202 366 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 168 198 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 416 AA; 46481 MW; 1E0DC61F754ABA00 CRC64; MPEFFENNEM EERVILVGVS SQDGDDTEDS LDELEELVKT AGAVTVGRVI QNRQTIHPGL YIGSGKVEEL LDEIAWTNAT GIVCDDELSP AQFRNLSDAL NVKVMDRTLI ILDIFAARAS TSEGKIQVEL AQLRYRMSRL SGIGKSMSRL GGGIGTRGPG EKKLEVDRRL IASRISQLKR ELEEVKRHRE VNRVARQRNH VPVAAIVGYT NAGKSTLLNA LTGAGILAED KLFATLDPTT RMLELPGSQK LLLTDTVGFI RKLPHHLIDA FRSTLEEAKY ADFIIHVVDA SNPQAAKQMH IVYETLHQLE VTDKKILTLF NKQDAITDRE PLRDGRADIT LRVSAARGDG LEELKDCLAR ILRENKRYLE TVLPYDKGGL LQQIRETGEL IAEEYLPEGI RIEAYVPPEL FEKIHA // ID R6NM19_9FIRM Unreviewed; 416 AA. AC R6NM19; DT 24-JUL-2013, integrated into UniProtKB/TrEMBL. DT 24-JUL-2013, sequence version 1. DT 10-MAY-2017, entry version 25. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=BN627_00288 {ECO:0000313|EMBL:CDC09404.1}; OS Lachnospiraceae bacterium CAG:364. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Lachnospiraceae; OC environmental samples. OX NCBI_TaxID=1262983 {ECO:0000313|EMBL:CDC09404.1, ECO:0000313|Proteomes:UP000017986}; RN [1] {ECO:0000313|EMBL:CDC09404.1, ECO:0000313|Proteomes:UP000017986} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MGS:364 {ECO:0000313|Proteomes:UP000017986}; RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., RA Sunagawa S., Plichta D., Gautier L., Le Chatelier E., Peletier E., RA Bonde I., Nielsen T., Manichanh C., Arumugam M., Batto J., RA Santos M.B.Q.D., Blom N., Borruel N., Burgdorf K.S., Boumezbeur F., RA Casellas F., Dore J., Guarner F., Hansen T., Hildebrand F., Kaas R.S., RA Kennedy S., Kristiansen K., Kultima J.R., Leonard P., Levenez F., RA Lund O., Moumen B., Le Paslier D., Pons N., Pedersen O., Prifti E., RA Qin J., Raes J., Tap J., Tims S., Ussery D.W., Yamada T., RA MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P., Wang J., RA Brunak S., Ehrlich S.D.; RT "Dependencies among metagenomic species, viruses, plasmids and units RT of genetic variation."; RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:CDC09404.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CBER010000111; CDC09404.1; -; Genomic_DNA. DR Proteomes; UP000017986; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000017986}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000017986}. FT DOMAIN 201 365 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 16 43 {ECO:0000256|SAM:Coils}. FT COILED 160 194 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 416 AA; 47275 MW; 03502FB48A2243D6 CRC64; MELYELKEEQ EKVILVGVQT RENDDTEDSL EELKELVKTA GAEVLGTVIQ AREAVHPGYY VGTGKLDEIR MMLDGYGATG IVCDDELSPS QINNLERELQ CKIMDRTMVI LDIFAARANT SEGKIQVELA QLRYRAARLT GLGNSMSRLG GGIGTRGPGE KKLEMDRRLI KLRISQLKKE LEQVKRHRQV LREGRSRENI MTAAIVGYTN AGKSTLLNTL TDAKVLEEDK LFATLDPTTR ILELPGKQKL YLTDTVGFIR KLPHHLIEAF KSTLEEAKYA DFIIHVVDIS NPQREKQMFV VYETLQELGV EDKKIVTLFN KQDKLQDAET IRDFKADYIV KTAIKTGQGL EELKEVLEKI LTENQIYLER ILDYQEAGQI QLIRKYGQLI SEEYTDRGIE IKARVPQNIY GKIGGR // ID R6P600_9FIRM Unreviewed; 422 AA. AC R6P600; DT 24-JUL-2013, integrated into UniProtKB/TrEMBL. DT 24-JUL-2013, sequence version 1. DT 12-APR-2017, entry version 23. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=BN582_00436 {ECO:0000313|EMBL:CDC19783.1}; OS Eubacterium sp. CAG:274. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Eubacteriaceae; OC Eubacterium; environmental samples. OX NCBI_TaxID=1262888 {ECO:0000313|EMBL:CDC19783.1, ECO:0000313|Proteomes:UP000017904}; RN [1] {ECO:0000313|EMBL:CDC19783.1, ECO:0000313|Proteomes:UP000017904} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MGS:274 {ECO:0000313|Proteomes:UP000017904}; RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., RA Sunagawa S., Plichta D., Gautier L., Le Chatelier E., Peletier E., RA Bonde I., Nielsen T., Manichanh C., Arumugam M., Batto J., RA Santos M.B.Q.D., Blom N., Borruel N., Burgdorf K.S., Boumezbeur F., RA Casellas F., Dore J., Guarner F., Hansen T., Hildebrand F., Kaas R.S., RA Kennedy S., Kristiansen K., Kultima J.R., Leonard P., Levenez F., RA Lund O., Moumen B., Le Paslier D., Pons N., Pedersen O., Prifti E., RA Qin J., Raes J., Tap J., Tims S., Ussery D.W., Yamada T., RA MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P., Wang J., RA Brunak S., Ehrlich S.D.; RT "Dependencies among metagenomic species, viruses, plasmids and units RT of genetic variation."; RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:CDC19783.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CBEX010000059; CDC19783.1; -; Genomic_DNA. DR Proteomes; UP000017904; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000017904}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000017904}. FT DOMAIN 199 364 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 166 193 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 422 AA; 46885 MW; D855A8705FB56B00 CRC64; MFETEKEVER VILVAVDDGT NEFDAESCLD ELEDLANTAD AVVVGRMIQK LGAINRATYL GSGKIDELKA FAEMKDATGV ICDDELSPVQ IRNLENALNL KVMSRTLVIL DIFAKRAMSA EGKVQVELAQ LRYNLSHLTG RGKEMSRLGG GIGTRGPGEK KLEVDRRRIA DRISDLNKNL KEIERHRSLL RENRNNQTPV IALVGYTNAG KSTLLNALTG AGVLAEDKLF ATLDTTTRAV ETQSGANYLF TDTVGFIQKL PHGLIKAFRA TLEEAKYADL LVHVVDASNP KRREQMNTVY KTLAELGADK KPIVTVYNKI DKDDIEMPLT KDNRAMETLA ISAGTGIGLP EMIAKVEDII KSFKKSIKVL IPYDKGQLLS IVHGKCEITA SENKDEGYYF ELYADNETEN RLREYIINDR TI // ID R6PUV9_9CLOT Unreviewed; 416 AA. AC R6PUV9; DT 24-JUL-2013, integrated into UniProtKB/TrEMBL. DT 24-JUL-2013, sequence version 1. DT 12-APR-2017, entry version 24. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=BN618_02116 {ECO:0000313|EMBL:CDC22301.1}; OS Clostridium nexile CAG:348. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium; environmental samples. OX NCBI_TaxID=1263069 {ECO:0000313|EMBL:CDC22301.1, ECO:0000313|Proteomes:UP000018368}; RN [1] {ECO:0000313|EMBL:CDC22301.1, ECO:0000313|Proteomes:UP000018368} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MGS:348 {ECO:0000313|Proteomes:UP000018368}; RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., RA Sunagawa S., Plichta D., Gautier L., Le Chatelier E., Peletier E., RA Bonde I., Nielsen T., Manichanh C., Arumugam M., Batto J., RA Santos M.B.Q.D., Blom N., Borruel N., Burgdorf K.S., Boumezbeur F., RA Casellas F., Dore J., Guarner F., Hansen T., Hildebrand F., Kaas R.S., RA Kennedy S., Kristiansen K., Kultima J.R., Leonard P., Levenez F., RA Lund O., Moumen B., Le Paslier D., Pons N., Pedersen O., Prifti E., RA Qin J., Raes J., Tap J., Tims S., Ussery D.W., Yamada T., RA MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P., Wang J., RA Brunak S., Ehrlich S.D.; RT "Dependencies among metagenomic species, viruses, plasmids and units RT of genetic variation."; RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:CDC22301.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CBEY010000017; CDC22301.1; -; Genomic_DNA. DR Proteomes; UP000018368; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000018368}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000018368}. FT DOMAIN 202 366 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 161 195 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 416 AA; 46873 MW; 3D954DE35F722EAD CRC64; MAEMIELKQV KEKVILVGVS TDDHDDTEKS LDELEELAST AGAVTVGRVV QNLSQIHPVT YVGKGKLDEI KDLLWETEAT GIICDDELSP IQLGNMEDAL NTKIMDRTLI ILDIFANRAS TNEGKIQVEL AQLKYRQSRL VGLGKSLSRL GGGIGTRGPG EKKLEMDRRL IKGRIAQLNR ELKDVKRHRE VTREQRSRNQ VPVIAIVGYT NAGKSTLLNT LTGADVLEED KLFATLDPTT RNLKLPSKQE VLLTDTVGFI RKLPHHLIEA FKSTLEEAKY ADIILHVVDA SNPQMDEQMY IVYETLMNLE VKNKPVITAF NKQDKVDGEA ILRDFKADHV VNISAKTGEG LENLQNVIEE VLREQKILIE QLYPYADAGK IQLIRKYGEL LEEEYREEGI FAKGYIPIEI YEKVKL // ID R6PXU5_9FIRM Unreviewed; 427 AA. AC R6PXU5; DT 24-JUL-2013, integrated into UniProtKB/TrEMBL. DT 24-JUL-2013, sequence version 1. DT 12-APR-2017, entry version 23. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=BN668_01868 {ECO:0000313|EMBL:CDC25579.1}; OS Firmicutes bacterium CAG:466. OC Bacteria; Firmicutes; environmental samples. OX NCBI_TaxID=1263025 {ECO:0000313|EMBL:CDC25579.1, ECO:0000313|Proteomes:UP000018338}; RN [1] {ECO:0000313|EMBL:CDC25579.1, ECO:0000313|Proteomes:UP000018338} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MGS:466 {ECO:0000313|Proteomes:UP000018338}; RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., RA Sunagawa S., Plichta D., Gautier L., Le Chatelier E., Peletier E., RA Bonde I., Nielsen T., Manichanh C., Arumugam M., Batto J., RA Santos M.B.Q.D., Blom N., Borruel N., Burgdorf K.S., Boumezbeur F., RA Casellas F., Dore J., Guarner F., Hansen T., Hildebrand F., Kaas R.S., RA Kennedy S., Kristiansen K., Kultima J.R., Leonard P., Levenez F., RA Lund O., Moumen B., Le Paslier D., Pons N., Pedersen O., Prifti E., RA Qin J., Raes J., Tap J., Tims S., Ussery D.W., Yamada T., RA MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P., Wang J., RA Brunak S., Ehrlich S.D.; RT "Dependencies among metagenomic species, viruses, plasmids and units RT of genetic variation."; RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:CDC25579.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CBFA010000029; CDC25579.1; -; Genomic_DNA. DR Proteomes; UP000018338; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000018338}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000018338}. FT DOMAIN 208 372 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 167 201 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 427 AA; 47665 MW; 2C5EAE2D34B52FDB CRC64; MAKELHENKD TEERLILVGI ELEDKDSPSA MAVEACLDEL EELVNTAGAT AVARTIQRRE KVHPAHYLGK GKIEELKMMI HTYDATGIVC DDELSPAQLK NLEKMLETKV MDRTIVILDI FAGRAISGEG KIQVELAQLK YRMSRLTGMG ASMSRLGGGI GTRGPGEKKL ETDRRHIKER IAELNRDLKE IQTHRELLRS QRNKKGTPVV SLVGYTNAGK STTLNVLTQA GVLAEDKLFA TLDTTTRKVE LPGGSEILLT DTVGFIQKLP HHLIQAFRAT LEELKYADIL LHVVDASNPN REEQMRVVYD TLRGLGCEDT PVITVYNKMD REVELPLPMD RMAREIVQIS AGKQMGLEQM LATIEKLLKS FRKSMTVLLP YTEGALAGWV HGRCEIIREE HTAEGVLLEV YVDEEAANRL KSFAVEA // ID R6Q5D4_9BACT Unreviewed; 415 AA. AC R6Q5D4; DT 24-JUL-2013, integrated into UniProtKB/TrEMBL. DT 24-JUL-2013, sequence version 1. DT 12-APR-2017, entry version 22. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=BN637_00632 {ECO:0000313|EMBL:CDC28244.1}; OS Prevotella sp. CAG:386. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Prevotellaceae; OC Prevotella; environmental samples. OX NCBI_TaxID=1262925 {ECO:0000313|EMBL:CDC28244.1, ECO:0000313|Proteomes:UP000018046}; RN [1] {ECO:0000313|EMBL:CDC28244.1, ECO:0000313|Proteomes:UP000018046} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MGS:386 {ECO:0000313|Proteomes:UP000018046}; RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., RA Sunagawa S., Plichta D., Gautier L., Le Chatelier E., Peletier E., RA Bonde I., Nielsen T., Manichanh C., Arumugam M., Batto J., RA Santos M.B.Q.D., Blom N., Borruel N., Burgdorf K.S., Boumezbeur F., RA Casellas F., Dore J., Guarner F., Hansen T., Hildebrand F., Kaas R.S., RA Kennedy S., Kristiansen K., Kultima J.R., Leonard P., Levenez F., RA Lund O., Moumen B., Le Paslier D., Pons N., Pedersen O., Prifti E., RA Qin J., Raes J., Tap J., Tims S., Ussery D.W., Yamada T., RA MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P., Wang J., RA Brunak S., Ehrlich S.D.; RT "Dependencies among metagenomic species, viruses, plasmids and units RT of genetic variation."; RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:CDC28244.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CBEZ010000218; CDC28244.1; -; Genomic_DNA. DR Proteomes; UP000018046; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000018046}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000018046}. FT DOMAIN 216 400 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 415 AA; 47706 MW; 0BE9A3895178B210 CRC64; MKEFVISEVK AETAVLVGLI TKEQDEAKTK EYLDELEFLA DTAGAVTVKR FTQKVVAPNQ TTYVGKGKLE EIKQYIKEEE EEDREIGMVI FDDELSAKQI RNIEQELQVK ILDRTSLILD IFAMRAQTAA AKTQVELAQY RYMLPRLQRL WTHLERQGGG SGSGGGKGSV GLRGPGETQL EMDRRIILGR MSLLKERLAE IDKQKTTQRK NRGRLIRVAL VGYTNVGKST IMNLLSKSEV FAENKLFATL DTTVRKVVVE NLPFLLADTV GFIRKLPTDL VDSFKSTLDE TREADLLLHV VDISHPDFEE QIQVVEKTLK ELGCADKPSM IIFNKIDNYS WVEKEEDDLT PIQKENITLD ELKRTWMAKL HDDCLFISAK NKENIDEFRD ILYKKVRELH VQKYPYNDFL YQDYE // ID R6QCK0_9FIRM Unreviewed; 421 AA. AC R6QCK0; DT 24-JUL-2013, integrated into UniProtKB/TrEMBL. DT 24-JUL-2013, sequence version 1. DT 30-AUG-2017, entry version 27. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=BN792_00074 {ECO:0000313|EMBL:CDC30819.1}; OS Faecalibacterium sp. CAG:82. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Ruminococcaceae; OC Faecalibacterium; environmental samples. OX NCBI_TaxID=1262898 {ECO:0000313|EMBL:CDC30819.1, ECO:0000313|Proteomes:UP000018070}; RN [1] {ECO:0000313|EMBL:CDC30819.1, ECO:0000313|Proteomes:UP000018070} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MGS:82 {ECO:0000313|Proteomes:UP000018070}; RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., RA Sunagawa S., Plichta D., Gautier L., Le Chatelier E., Peletier E., RA Bonde I., Nielsen T., Manichanh C., Arumugam M., Batto J., RA Santos M.B.Q.D., Blom N., Borruel N., Burgdorf K.S., Boumezbeur F., RA Casellas F., Dore J., Guarner F., Hansen T., Hildebrand F., Kaas R.S., RA Kennedy S., Kristiansen K., Kultima J.R., Leonard P., Levenez F., RA Lund O., Moumen B., Le Paslier D., Pons N., Pedersen O., Prifti E., RA Qin J., Raes J., Tap J., Tims S., Ussery D.W., Yamada T., RA MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P., Wang J., RA Brunak S., Ehrlich S.D.; RT "Dependencies among metagenomic species, viruses, plasmids and units RT of genetic variation."; RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:CDC30819.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CBFB010000145; CDC30819.1; -; Genomic_DNA. DR Proteomes; UP000018070; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000018070}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000018070}. FT DOMAIN 209 368 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 175 202 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 421 AA; 45586 MW; 4F541E7516B4C02D CRC64; MSELYDILVE TPPTKVILLA LDQGLWDCER SLAELSALCE ANHMEAVAEV TQKRQTPETG IVLGSGKLEE AAAAAAELGA ECAVFDGELT GSQIRNISTA LGGMEVIDRT MLILEIFRSR AVTNEGKLQT ELALLRYRLP RLQGMGESLS RQGGGGGGGG GARRGAGETK LELDRRHVHA RIDALAEKLA EMEKRRGESR KARAKTGMPV VSLVGYTNVG KSSLMNALCG PSVAEADMLF ATLDPTSRKL VLPSGMAVLL VDTVGFVSRL PHNLVEAFKS TLEEAAWSDV IVRVADAGDE QREEQLAVTD EVLDGLDCAD IPRLTVYNKC DKPGALSFDP DILLTSAKTG YGLEALLKKL DETLSDRVHT IRVLLPYDKL GLAAPMRERG SVQVEEYRED GLYLEGIVKT EDLHCFEGYL C // ID R6QHV2_9FIRM Unreviewed; 412 AA. AC R6QHV2; DT 24-JUL-2013, integrated into UniProtKB/TrEMBL. DT 24-JUL-2013, sequence version 1. DT 12-APR-2017, entry version 24. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=BN583_00728 {ECO:0000313|EMBL:CDC35355.1}; OS Anaerostipes sp. CAG:276. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Lachnospiraceae; OC Anaerostipes; environmental samples. OX NCBI_TaxID=1262699 {ECO:0000313|EMBL:CDC35355.1, ECO:0000313|Proteomes:UP000018135}; RN [1] {ECO:0000313|EMBL:CDC35355.1, ECO:0000313|Proteomes:UP000018135} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MGS:276 {ECO:0000313|Proteomes:UP000018135}; RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., RA Sunagawa S., Plichta D., Gautier L., Le Chatelier E., Peletier E., RA Bonde I., Nielsen T., Manichanh C., Arumugam M., Batto J., RA Santos M.B.Q.D., Blom N., Borruel N., Burgdorf K.S., Boumezbeur F., RA Casellas F., Dore J., Guarner F., Hansen T., Hildebrand F., Kaas R.S., RA Kennedy S., Kristiansen K., Kultima J.R., Leonard P., Levenez F., RA Lund O., Moumen B., Le Paslier D., Pons N., Pedersen O., Prifti E., RA Qin J., Raes J., Tap J., Tims S., Ussery D.W., Yamada T., RA MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P., Wang J., RA Brunak S., Ehrlich S.D.; RT "Dependencies among metagenomic species, viruses, plasmids and units RT of genetic variation."; RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:CDC35355.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CBFE010000070; CDC35355.1; -; Genomic_DNA. DR Proteomes; UP000018135; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000018135}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000018135}. FT DOMAIN 200 364 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 412 AA; 45917 MW; 226A9E63F031C681 CRC64; MEEILEQKKE RVILVGVALG DSQEAEESLE ELKELAETAG AEVAGSIIQA REQIHSGTYV GKGKIEEIRD LLFETEADGI VCDDELSPAQ LANLSQTLDI KVMDRTLVIL DIFAKRAQTK EGKIQVELAQ LRYRATKLTG KGVSLSRLGG GIGTRGPGEK KLEMDRRLIR TRISHLKTEL AGVIKHREVQ RKQRQKNHTP VVCIVGYTNA GKSTLLNHFT DAGVLEEDQL FATLDPTTKS VELNSGQTVL MTDTVGFIRK LPHHLVDAFK STLEEAKYSD IILHVVDCSN PFMEQQMEAV YETLGQLGIK DTPVITAFNK IDRTGKNSLL KDVRADETVK ISAKEGTGTS DLLRVIEDVL KKQKIYLEKK YGYDEAGKIQ AIRTHGQLLK EEYREDGIYV EAYIPKEILG MV // ID R6QP71_9FIRM Unreviewed; 432 AA. AC R6QP71; DT 24-JUL-2013, integrated into UniProtKB/TrEMBL. DT 24-JUL-2013, sequence version 1. DT 10-MAY-2017, entry version 24. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=BN563_00772 {ECO:0000313|EMBL:CDC32666.1}; OS Eubacterium sp. CAG:251. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Eubacteriaceae; OC Eubacterium; environmental samples. OX NCBI_TaxID=1262886 {ECO:0000313|EMBL:CDC32666.1, ECO:0000313|Proteomes:UP000018414}; RN [1] {ECO:0000313|EMBL:CDC32666.1, ECO:0000313|Proteomes:UP000018414} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MGS:251 {ECO:0000313|Proteomes:UP000018414}; RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., RA Sunagawa S., Plichta D., Gautier L., Le Chatelier E., Peletier E., RA Bonde I., Nielsen T., Manichanh C., Arumugam M., Batto J., RA Santos M.B.Q.D., Blom N., Borruel N., Burgdorf K.S., Boumezbeur F., RA Casellas F., Dore J., Guarner F., Hansen T., Hildebrand F., Kaas R.S., RA Kennedy S., Kristiansen K., Kultima J.R., Leonard P., Levenez F., RA Lund O., Moumen B., Le Paslier D., Pons N., Pedersen O., Prifti E., RA Qin J., Raes J., Tap J., Tims S., Ussery D.W., Yamada T., RA MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P., Wang J., RA Brunak S., Ehrlich S.D.; RT "Dependencies among metagenomic species, viruses, plasmids and units RT of genetic variation."; RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:CDC32666.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CBFD010000029; CDC32666.1; -; Genomic_DNA. DR Proteomes; UP000018414; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000018414}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000018414}. FT DOMAIN 206 375 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 165 199 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 432 AA; 47887 MW; 58C4CE5301A182E7 CRC64; MDNQTNENEI FNEDKKERAL LISVDTGDFN AEVSMEELEE LAKTAGAKVV GTSIQKRQTP VAATYIGKGA LYEMTRFCEN MNIDLIIADS ELSPVQIRNL EDETNTRVID RTTLILDIFA GRARSKEGKL QIELAQLKYS LPRLTGKGTQ LSRLGGGIGT RGPGETKLES DKRHIRRRIQ NIRQELDKVK SRREMIHERR KKNGALSVAI VGYTNAGKST LMNKLTDAGV LQEDKLFATL DPTARKLSLP NGQSIMLIDT VGFISRLPHQ LVDAFRSTLE EATYADVILN VCDTSSPYCY DNIDVTKEIL SSLFPDGAIT VPVITVFNKC DITHSPSAIA FPFADAKTSV KISAKTGEGL DELLLAIQNA LPQTKKRLKL LVPFSKGSIL ADIRQDGVIH SEEYTPDGTL IDATVDIIYL EKNKQYIKII DE // ID R6QQ39_9FIRM Unreviewed; 412 AA. AC R6QQ39; DT 24-JUL-2013, integrated into UniProtKB/TrEMBL. DT 24-JUL-2013, sequence version 1. DT 10-MAY-2017, entry version 25. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=BN606_01310 {ECO:0000313|EMBL:CDC38743.1}; OS Butyrivibrio sp. CAG:318. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Lachnospiraceae; OC Butyrivibrio; environmental samples. OX NCBI_TaxID=1262761 {ECO:0000313|EMBL:CDC38743.1, ECO:0000313|Proteomes:UP000018075}; RN [1] {ECO:0000313|EMBL:CDC38743.1, ECO:0000313|Proteomes:UP000018075} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MGS:318 {ECO:0000313|Proteomes:UP000018075}; RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., RA Sunagawa S., Plichta D., Gautier L., Le Chatelier E., Peletier E., RA Bonde I., Nielsen T., Manichanh C., Arumugam M., Batto J., RA Santos M.B.Q.D., Blom N., Borruel N., Burgdorf K.S., Boumezbeur F., RA Casellas F., Dore J., Guarner F., Hansen T., Hildebrand F., Kaas R.S., RA Kennedy S., Kristiansen K., Kultima J.R., Leonard P., Levenez F., RA Lund O., Moumen B., Le Paslier D., Pons N., Pedersen O., Prifti E., RA Qin J., Raes J., Tap J., Tims S., Ussery D.W., Yamada T., RA MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P., Wang J., RA Brunak S., Ehrlich S.D.; RT "Dependencies among metagenomic species, viruses, plasmids and units RT of genetic variation."; RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:CDC38743.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CBFF010000051; CDC38743.1; -; Genomic_DNA. DR Proteomes; UP000018075; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000018075}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000018075}. FT DOMAIN 199 363 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 412 AA; 45708 MW; 6F113FE6AFE31819 CRC64; MVETKQTEER VILVAVRQSD DDNTDRSLDE LEELASTAGA VTVTRIIQNR EAIHPGTYVG KGKIEEIRDA IYMYDATGII CDDELSPAQM TNLEEALEVK IMDRTLVILD IFAARANTGE GKIQVELAQL KYRATRLVGL RSSLSRLGGG IGTRGPGETK LEMDRRLIHQ RIAQLKRELA DVVTHRELTR NQRKRAGVPV IAIVGYTNAG KSTLLNTLTG ADVLEEDKLF ATLDPTTRSL TLESGQEVLL TDTVGFISKL PHQLVDAFKS TLEEAVYADM LIHVVDASNP DMDAQMYTVY DTLDKLGASD KPVITAFNKT DRIIEGIHAK DLRAEHTVRI SAKHGDGLDK LKAVIEEVLR ENKVYIERVF DYSEAGKISL IRKYGELLSE EYTAEGIAVK AYAPVEIADK IR // ID R6QW18_9CLOT Unreviewed; 414 AA. AC R6QW18; DT 24-JUL-2013, integrated into UniProtKB/TrEMBL. DT 24-JUL-2013, sequence version 1. DT 10-MAY-2017, entry version 24. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=BN621_00197 {ECO:0000313|EMBL:CDC37204.1}; OS Clostridium sp. CAG:352. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium; environmental samples. OX NCBI_TaxID=1262798 {ECO:0000313|EMBL:CDC37204.1, ECO:0000313|Proteomes:UP000018340}; RN [1] {ECO:0000313|EMBL:CDC37204.1, ECO:0000313|Proteomes:UP000018340} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MGS:352 {ECO:0000313|Proteomes:UP000018340}; RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., RA Sunagawa S., Plichta D., Gautier L., Le Chatelier E., Peletier E., RA Bonde I., Nielsen T., Manichanh C., Arumugam M., Batto J., RA Santos M.B.Q.D., Blom N., Borruel N., Burgdorf K.S., Boumezbeur F., RA Casellas F., Dore J., Guarner F., Hansen T., Hildebrand F., Kaas R.S., RA Kennedy S., Kristiansen K., Kultima J.R., Leonard P., Levenez F., RA Lund O., Moumen B., Le Paslier D., Pons N., Pedersen O., Prifti E., RA Qin J., Raes J., Tap J., Tims S., Ussery D.W., Yamada T., RA MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P., Wang J., RA Brunak S., Ehrlich S.D.; RT "Dependencies among metagenomic species, viruses, plasmids and units RT of genetic variation."; RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:CDC37204.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CBFG010000011; CDC37204.1; -; Genomic_DNA. DR Proteomes; UP000018340; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000018340}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000018340}. FT DOMAIN 200 361 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 159 193 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 414 AA; 46124 MW; F1C36970186743F6 CRC64; MQMYDNIERP QRAILISIDT GDYDAEASLE ELKELMRSAG GETIATVSQK RDKPDSATCL GSGRLLEVKE FAQTNDIDLL VFDCELTPTQ IRNLEAETDI RTIDRTMLIL DIFALHAKTN EGKLQVELAQ LKYLMPRLTG KGREMSRLGG GIGTRGPGES KLETDRRHIR RRIETLKEEL SHITDRRNQL RSRRSKDGII TVAIVGYTNA GKSTLMNTLT QAGVLSEDKL FATLDPTSRS LKLPNGVSVM MIDTVGLVRR LPHHLVEAFK STLEEAALAD IIVNVCDATS EEYQLHLDVT TSLLHDLGCE NSPIITAFNK CDLLSPDDIP HNSGSVLISA KTGNGIDKLL EAIEENLPVQ IKRFNMLLPF QKANLIAPLR YMGALISEEY TADGILVTAN IEKPKWHIYE PYEI // ID R6RBW9_9CLOT Unreviewed; 416 AA. AC R6RBW9; DT 24-JUL-2013, integrated into UniProtKB/TrEMBL. DT 24-JUL-2013, sequence version 1. DT 12-APR-2017, entry version 24. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=BN719_01228 {ECO:0000313|EMBL:CDC46393.1}; OS Clostridium sp. CAG:58. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium; environmental samples. OX NCBI_TaxID=1262824 {ECO:0000313|EMBL:CDC46393.1, ECO:0000313|Proteomes:UP000018263}; RN [1] {ECO:0000313|EMBL:CDC46393.1, ECO:0000313|Proteomes:UP000018263} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MGS:58 {ECO:0000313|Proteomes:UP000018263}; RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., RA Sunagawa S., Plichta D., Gautier L., Le Chatelier E., Peletier E., RA Bonde I., Nielsen T., Manichanh C., Arumugam M., Batto J., RA Santos M.B.Q.D., Blom N., Borruel N., Burgdorf K.S., Boumezbeur F., RA Casellas F., Dore J., Guarner F., Hansen T., Hildebrand F., Kaas R.S., RA Kennedy S., Kristiansen K., Kultima J.R., Leonard P., Levenez F., RA Lund O., Moumen B., Le Paslier D., Pons N., Pedersen O., Prifti E., RA Qin J., Raes J., Tap J., Tims S., Ussery D.W., Yamada T., RA MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P., Wang J., RA Brunak S., Ehrlich S.D.; RT "Dependencies among metagenomic species, viruses, plasmids and units RT of genetic variation."; RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:CDC46393.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CBFK010000074; CDC46393.1; -; Genomic_DNA. DR Proteomes; UP000018263; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000018263}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000018263}. FT DOMAIN 202 366 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 416 AA; 46652 MW; 14008ED60A66C30C CRC64; MAEMIELKEQ EERVILVAVS TGEDDDTAAS VDELEELAST AGAVTVGKVI QNRENVHPGT YLGKGKIEEV KELLWELDAT GIICDDELSP AQLKNLEDAL DTKVMDRTMV ILDIFASRAR TREGKIQVEL AQLRYRAVRL VGLRNSLSRL GGGIGTRGPG EKKLEVDRRL IHERISQLKS ELEDVKRHRE VVRKKRENGG ALTAAIVGYT NAGKSTLLNR LTQAGILAED KLFATLDPTT RALTLPGGER ILLTDTVGFI RKLPHHLIEA FKSTLEEAKY SDVILHVVDC SNPQMDMQMH VVYETLRQLE ITDKEIVTVF NKIDREGADT AGRDMAADYR VKISAKTGEG LPDLLGVLET ILRSRRIYFE KVFSYAEAGR IQRIRKNGRL LSEEYKEDGI HVTAYVPVEL FEELYR // ID R6RQP8_9FIRM Unreviewed; 416 AA. AC R6RQP8; DT 24-JUL-2013, integrated into UniProtKB/TrEMBL. DT 24-JUL-2013, sequence version 1. DT 12-APR-2017, entry version 23. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=BN652_01887 {ECO:0000313|EMBL:CDC47664.1}; OS Firmicutes bacterium CAG:424. OC Bacteria; Firmicutes; environmental samples. OX NCBI_TaxID=1263022 {ECO:0000313|EMBL:CDC47664.1, ECO:0000313|Proteomes:UP000018167}; RN [1] {ECO:0000313|EMBL:CDC47664.1, ECO:0000313|Proteomes:UP000018167} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MGS:424 {ECO:0000313|Proteomes:UP000018167}; RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., RA Sunagawa S., Plichta D., Gautier L., Le Chatelier E., Peletier E., RA Bonde I., Nielsen T., Manichanh C., Arumugam M., Batto J., RA Santos M.B.Q.D., Blom N., Borruel N., Burgdorf K.S., Boumezbeur F., RA Casellas F., Dore J., Guarner F., Hansen T., Hildebrand F., Kaas R.S., RA Kennedy S., Kristiansen K., Kultima J.R., Leonard P., Levenez F., RA Lund O., Moumen B., Le Paslier D., Pons N., Pedersen O., Prifti E., RA Qin J., Raes J., Tap J., Tims S., Ussery D.W., Yamada T., RA MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P., Wang J., RA Brunak S., Ehrlich S.D.; RT "Dependencies among metagenomic species, viruses, plasmids and units RT of genetic variation."; RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:CDC47664.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CBFI010000092; CDC47664.1; -; Genomic_DNA. DR Proteomes; UP000018167; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000018167}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000018167}. FT DOMAIN 201 365 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 167 194 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 416 AA; 47241 MW; 0FA5F569C2596BDF CRC64; MELYEFKEEQ ERVILVGVQT RDGDDTLDSL EELKDLVKTA GAEAVGMVVQ SRESIHPGYY VGTGKLEEIR MMARAYDATG IVCDDELSPS QMNNLERELE LKIMDRTMVI LDIFAARART SEGKIQVELA QLRYRSSRLT GLGTSMSRLG GGIGTRGPGE KKLEMDRRLI KVRISQLKKE LEQVKRHREL LREGRSRENI MTAAIVGYTN AGKSTLLNTL TDAQVLEEDK LFATLDPTTR ILELPGKQRL YLTDTVGFIR KLPHHLIEAF KSTLEEAKYA DFIIHVVDAS NPQRDEQMYV VYETLKELEV GDKKIVTLFN KQDKVLEPEI FRDFKADYVL KTAVKTGEGL EELKEVLEKV ITEDQIYLER TLGYHETGQI QMIRKYGQLL SEEYTAEGIE IKAKVPGNIY GKIGGK // ID R6S080_9FIRM Unreviewed; 415 AA. AC R6S080; DT 24-JUL-2013, integrated into UniProtKB/TrEMBL. DT 24-JUL-2013, sequence version 1. DT 12-APR-2017, entry version 23. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=BN586_01284 {ECO:0000313|EMBL:CDC54598.1}; OS Dorea formicigenerans CAG:28. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Lachnospiraceae; OC Dorea; environmental samples. OX NCBI_TaxID=1263073 {ECO:0000313|EMBL:CDC54598.1, ECO:0000313|Proteomes:UP000018109}; RN [1] {ECO:0000313|EMBL:CDC54598.1, ECO:0000313|Proteomes:UP000018109} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MGS:28 {ECO:0000313|Proteomes:UP000018109}; RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., RA Sunagawa S., Plichta D., Gautier L., Le Chatelier E., Peletier E., RA Bonde I., Nielsen T., Manichanh C., Arumugam M., Batto J., RA Santos M.B.Q.D., Blom N., Borruel N., Burgdorf K.S., Boumezbeur F., RA Casellas F., Dore J., Guarner F., Hansen T., Hildebrand F., Kaas R.S., RA Kennedy S., Kristiansen K., Kultima J.R., Leonard P., Levenez F., RA Lund O., Moumen B., Le Paslier D., Pons N., Pedersen O., Prifti E., RA Qin J., Raes J., Tap J., Tims S., Ussery D.W., Yamada T., RA MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P., Wang J., RA Brunak S., Ehrlich S.D.; RT "Dependencies among metagenomic species, viruses, plasmids and units RT of genetic variation."; RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:CDC54598.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CBFN010000043; CDC54598.1; -; Genomic_DNA. DR Proteomes; UP000018109; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000018109}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000018109}. FT DOMAIN 199 363 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 158 192 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 415 AA; 46119 MW; 7AEE2F1D102D5008 CRC64; MIELKKETER VILVGVCLPG QEDIDASLEE LSELAKTAGA VTVGKVVQSR DQVHPGTYVG KGKIDEIKSL LWELDATGII CDDELSPAQM KNLQDELDAK VMDRTLVILD IFAARASTSE GKIQVELAQL KYRQTRLAGF GTAMSRLGGG IGTRGPGEKK LEMDRRLIKN RIALLNRELK SVKQHREVTR EKRAKSRIPV AAIVGYTNAG KSTLLNALTG ADILAEDKLF ATLDPTTRSL KLPSGQEILL TDTVGFIRKL PHHLIDAFKS TLEEAKYADM ILHVVDVSNP QADEQMFTVY ETLQGLKVQD KPIITVFNKQ DRLEGIPVIR DFKADYTVSI SAKTKAGLGN LLETIEALLR QQKVYIEEVY PYSEAGKIQL IRKYGELLEE NYTEEGIQVT AYVPADIYPQ IVVNR // ID R6S5T3_9BACE Unreviewed; 418 AA. AC R6S5T3; DT 24-JUL-2013, integrated into UniProtKB/TrEMBL. DT 24-JUL-2013, sequence version 1. DT 12-APR-2017, entry version 22. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=BN532_00752 {ECO:0000313|EMBL:CDC52934.1}; OS Bacteroides finegoldii CAG:203. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae; OC Bacteroides; environmental samples. OX NCBI_TaxID=1263045 {ECO:0000313|EMBL:CDC52934.1, ECO:0000313|Proteomes:UP000018058}; RN [1] {ECO:0000313|EMBL:CDC52934.1, ECO:0000313|Proteomes:UP000018058} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MGS:203 {ECO:0000313|Proteomes:UP000018058}; RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., RA Sunagawa S., Plichta D., Gautier L., Le Chatelier E., Peletier E., RA Bonde I., Nielsen T., Manichanh C., Arumugam M., Batto J., RA Santos M.B.Q.D., Blom N., Borruel N., Burgdorf K.S., Boumezbeur F., RA Casellas F., Dore J., Guarner F., Hansen T., Hildebrand F., Kaas R.S., RA Kennedy S., Kristiansen K., Kultima J.R., Leonard P., Levenez F., RA Lund O., Moumen B., Le Paslier D., Pons N., Pedersen O., Prifti E., RA Qin J., Raes J., Tap J., Tims S., Ussery D.W., Yamada T., RA MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P., Wang J., RA Brunak S., Ehrlich S.D.; RT "Dependencies among metagenomic species, viruses, plasmids and units RT of genetic variation."; RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:CDC52934.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CBFL010000143; CDC52934.1; -; Genomic_DNA. DR ProteinModelPortal; R6S5T3; -. DR Proteomes; UP000018058; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000018058}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000018058}. FT DOMAIN 216 400 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 418 AA; 47731 MW; 0CA4A345B203770D CRC64; MKEFVISEAK VETAILVGLI TQTQDERKTN EYLDELAFLA ETAGAEVVKR FTQKLPTANS VTYVGKGKLE EIRTYIRNEE EEEREVGMVI FDDELSAKQI RNIEAELKVK ILDRTSLILD IFAMRAQTAN AKTQVELAQY KYMLPRLQRL WTHLERQGGG SGAGGGKGSV GLRGPGETQL EMDRRIILNR MSLLKERLAD IDKQKATQRK NRGRMIRVAL VGYTNVGKST IMNLLSKSEV FAENKLFATL DTTVRKVIIE NLPFLLSDTV GFIRKLPTDL VDSFKSTLDE VREADLLVHV VDISHPGFEE QIEVVNKTLA EIGGGGKPMI LVFNKIDAYT YIEKASDDLT PRTKENLTLE ELMKTWMAKM EDNCLFISAR ERINMDELKN VVYQRVKELH VQKYPYNDFL YQTYEEEE // ID R6SZZ8_9BACE Unreviewed; 393 AA. AC R6SZZ8; DT 24-JUL-2013, integrated into UniProtKB/TrEMBL. DT 24-JUL-2013, sequence version 1. DT 12-APR-2017, entry version 23. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=BN777_01183 {ECO:0000313|EMBL:CDC63089.1}; OS Bacteroides sp. CAG:770. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae; OC Bacteroides; environmental samples. OX NCBI_TaxID=1262751 {ECO:0000313|EMBL:CDC63089.1, ECO:0000313|Proteomes:UP000018390}; RN [1] {ECO:0000313|EMBL:CDC63089.1, ECO:0000313|Proteomes:UP000018390} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MGS:770 {ECO:0000313|Proteomes:UP000018390}; RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., RA Sunagawa S., Plichta D., Gautier L., Le Chatelier E., Peletier E., RA Bonde I., Nielsen T., Manichanh C., Arumugam M., Batto J., RA Santos M.B.Q.D., Blom N., Borruel N., Burgdorf K.S., Boumezbeur F., RA Casellas F., Dore J., Guarner F., Hansen T., Hildebrand F., Kaas R.S., RA Kennedy S., Kristiansen K., Kultima J.R., Leonard P., Levenez F., RA Lund O., Moumen B., Le Paslier D., Pons N., Pedersen O., Prifti E., RA Qin J., Raes J., Tap J., Tims S., Ussery D.W., Yamada T., RA MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P., Wang J., RA Brunak S., Ehrlich S.D.; RT "Dependencies among metagenomic species, viruses, plasmids and units RT of genetic variation."; RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:CDC63089.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CBFR010000019; CDC63089.1; -; Genomic_DNA. DR Proteomes; UP000018390; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR Gene3D; 3.40.20.10; -; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR029006; ADF-H/Gelsolin-like_dom. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000018390}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000018390}. FT DOMAIN 198 382 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 166 193 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 393 AA; 45440 MW; 63BF1A795E1A995A CRC64; MTNNTEKAVF VGIITDKDDE RKVYEYLDEL EFLAETAGAT RDKKFVQRLD RPDNATYIRS GKLQEIAEYC EENEIRYVIF DDELSGTQQR NIEKIIKTSS VIDRTSLILE IFAQRAKTAY AKMQVELAKY NYMLPRLAGM WTHLERQRGG MGTRGGMGET QIEIDRRIVK ERISKLKEQL KKVDRQMATQ RGNRGQLVRL ALVGYTNVGK STLMNLLSKS DVFAENKLFA TLDTTVRKVV LENVPFLLSD TVGFIRKLPT QLIEAFKSTL DEVREADILI HVVDISHPGF EEQMEVVEQT LRDIKADNKP IYVIFNKIDS YTYEEYDEFS LEPKGKNNVS LEELKNSWIA KEKTPCIFIS AKEKIGIDKL RNDIYKMVAE IHAGRYPFNN FLW // ID R6T3G6_9FIRM Unreviewed; 420 AA. AC R6T3G6; DT 24-JUL-2013, integrated into UniProtKB/TrEMBL. DT 24-JUL-2013, sequence version 1. DT 12-APR-2017, entry version 23. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=BN714_02098 {ECO:0000313|EMBL:CDC66740.1}; OS Ruminococcus sp. CAG:57. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Ruminococcaceae; OC Ruminococcus; environmental samples. OX NCBI_TaxID=1262962 {ECO:0000313|EMBL:CDC66740.1, ECO:0000313|Proteomes:UP000018131}; RN [1] {ECO:0000313|EMBL:CDC66740.1, ECO:0000313|Proteomes:UP000018131} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MGS:57 {ECO:0000313|Proteomes:UP000018131}; RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., RA Sunagawa S., Plichta D., Gautier L., Le Chatelier E., Peletier E., RA Bonde I., Nielsen T., Manichanh C., Arumugam M., Batto J., RA Santos M.B.Q.D., Blom N., Borruel N., Burgdorf K.S., Boumezbeur F., RA Casellas F., Dore J., Guarner F., Hansen T., Hildebrand F., Kaas R.S., RA Kennedy S., Kristiansen K., Kultima J.R., Leonard P., Levenez F., RA Lund O., Moumen B., Le Paslier D., Pons N., Pedersen O., Prifti E., RA Qin J., Raes J., Tap J., Tims S., Ussery D.W., Yamada T., RA MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P., Wang J., RA Brunak S., Ehrlich S.D.; RT "Dependencies among metagenomic species, viruses, plasmids and units RT of genetic variation."; RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:CDC66740.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CBFS010000171; CDC66740.1; -; Genomic_DNA. DR Proteomes; UP000018131; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000018131}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000018131}. FT DOMAIN 201 363 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 167 194 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 420 AA; 46307 MW; 0A7C8B07639C14DC CRC64; MAEMFDNTIK KDRVLLAAVD TGSYDVELSL DELEELTETA GGEVIARVTQ KRPSFDSGTC IGSGRLEELA EICRNENIDR IVFDCELTAT QIRNIEDVCG VFTIDRTMLI LDIFAQRATT REGRLQVEIA QNKYRLPRLA GMGTNMSRLG GGIGTRGPGE SKLETDKRHI RTRIAALSDE LKEIEKRRGL MRKRRKKDGV LTAAIVGYTN VGKSTLLNYL TEAGVLAENK LFATLETTSR AIELPDGRSV TLIDTVGLIR RLPHQLVEAF KSTLEEAASA DVIIHVCDAS ADDCEEQAKV TLELLKELGC EGIPVVTVFN KCDKVPYINE LDTSGEAVKI SAKNGTGIDS LLAAIQKALP ENSVRCRLLL PFDKAGLVNT IRQEGRIFSE DYTAEGIVLD ALVDIKVYHL VESYKVKNEE // ID R6TC23_9STAP Unreviewed; 427 AA. AC R6TC23; DT 24-JUL-2013, integrated into UniProtKB/TrEMBL. DT 24-JUL-2013, sequence version 1. DT 10-MAY-2017, entry version 25. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=BN609_01177 {ECO:0000313|EMBL:CDC70958.1}; OS Staphylococcus sp. CAG:324. OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae; OC Staphylococcus; environmental samples. OX NCBI_TaxID=1262969 {ECO:0000313|EMBL:CDC70958.1, ECO:0000313|Proteomes:UP000018360}; RN [1] {ECO:0000313|EMBL:CDC70958.1, ECO:0000313|Proteomes:UP000018360} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MGS:324 {ECO:0000313|Proteomes:UP000018360}; RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., RA Sunagawa S., Plichta D., Gautier L., Le Chatelier E., Peletier E., RA Bonde I., Nielsen T., Manichanh C., Arumugam M., Batto J., RA Santos M.B.Q.D., Blom N., Borruel N., Burgdorf K.S., Boumezbeur F., RA Casellas F., Dore J., Guarner F., Hansen T., Hildebrand F., Kaas R.S., RA Kennedy S., Kristiansen K., Kultima J.R., Leonard P., Levenez F., RA Lund O., Moumen B., Le Paslier D., Pons N., Pedersen O., Prifti E., RA Qin J., Raes J., Tap J., Tims S., Ussery D.W., Yamada T., RA MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P., Wang J., RA Brunak S., Ehrlich S.D.; RT "Dependencies among metagenomic species, viruses, plasmids and units RT of genetic variation."; RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:CDC70958.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CBFU010000021; CDC70958.1; -; Genomic_DNA. DR Proteomes; UP000018360; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000018360}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000018360}. FT DOMAIN 203 373 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 162 196 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 427 AA; 48408 MW; 1440DB7CB671F59F CRC64; MENEMIKIKT IIVGVNHTND EEFNYQIQEL EALCEACDLD VVASLVQNMP TLNNATYLGS GKLEELKNVK DLYQASLVVF LEELSPVQLR NIKDVIDVDV MDRTMLILEI FKKRAKTKEA ILQVEIANLK YMLPRLAGSY TNLSRLGGGG SGSGGARRGS GETKLEEDRR HIERRITKAE KELAEIVASR KNARKKRLAN EMKTVAFVGY TNAGKSSSIN TLIHMFQGDK KKEVFVKNML FATLETATRR IKLPTNEEFI ITDTVGFVSN LPHHLIESFK STLEEVKEAS LIVHVVDASS PYANLQIQTT NQVLTSLGVK DIPMVYLLNK YDLVKNDMFM PTIIGDQIRT SNLDQRGFDE LIAYIKDKLF DDVVKVKLLI PYDKGEIFNL LKEKSNVHAF SYHDDGIVVD TIVSKYLYNL YHQYEIQ // ID R6THU6_9BACE Unreviewed; 418 AA. AC R6THU6; DT 24-JUL-2013, integrated into UniProtKB/TrEMBL. DT 24-JUL-2013, sequence version 1. DT 12-APR-2017, entry version 24. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=BN612_00738 {ECO:0000313|EMBL:CDC58287.1}; OS Bacteroides coprophilus CAG:333. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae; OC Bacteroides; environmental samples. OX NCBI_TaxID=1263041 {ECO:0000313|EMBL:CDC58287.1, ECO:0000313|Proteomes:UP000018018}; RN [1] {ECO:0000313|EMBL:CDC58287.1, ECO:0000313|Proteomes:UP000018018} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MGS:333 {ECO:0000313|Proteomes:UP000018018}; RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., RA Sunagawa S., Plichta D., Gautier L., Le Chatelier E., Peletier E., RA Bonde I., Nielsen T., Manichanh C., Arumugam M., Batto J., RA Santos M.B.Q.D., Blom N., Borruel N., Burgdorf K.S., Boumezbeur F., RA Casellas F., Dore J., Guarner F., Hansen T., Hildebrand F., Kaas R.S., RA Kennedy S., Kristiansen K., Kultima J.R., Leonard P., Levenez F., RA Lund O., Moumen B., Le Paslier D., Pons N., Pedersen O., Prifti E., RA Qin J., Raes J., Tap J., Tims S., Ussery D.W., Yamada T., RA MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P., Wang J., RA Brunak S., Ehrlich S.D.; RT "Dependencies among metagenomic species, viruses, plasmids and units RT of genetic variation."; RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:CDC58287.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CBFM010000180; CDC58287.1; -; Genomic_DNA. DR Proteomes; UP000018018; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000018018}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000018018}. FT DOMAIN 217 401 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 418 AA; 47804 MW; 05E64813087A6EE1 CRC64; MKEFVISEAQ TEKAVLVGLV TQTQNERKTN EYLDELAFLA ETAGAEVVKR FTQKLDTPNS VTYVGKGKLQ EIREYLQQQA EEEENEIGMV IFDDELSAKQ IRNIENELKV KILDRTSLIL DIFAMRAQTA NAKTQVELAQ YKYMLPRLQR LWTHLERQGG GSGAGGGKGS VGLRGPGETQ LEMDRRIILN RMALLKQRLA DIDTQKSTQR KNRGRMIRVA LVGYTNVGKS TLMNLMAKSD VFAENKLFAT LDTTVRKVII ENLPFLLSDT VGFIRKLPTD LVDSFKSTLD EVREADLLVH VVDISHPDFE EQIQVVDKTI TDLGAGGKPT MIVFNKIDAY TYVEKAEDDL TPKTKENITL EELMKTWMAK MNDNCIFISA RNRTNIEELR DLLYKKVREL HVQKYPYNDF LYQNYEEE // ID R6TR42_9CLOT Unreviewed; 440 AA. AC R6TR42; DT 24-JUL-2013, integrated into UniProtKB/TrEMBL. DT 24-JUL-2013, sequence version 1. DT 12-APR-2017, entry version 21. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=BN660_01038 {ECO:0000313|EMBL:CDC61082.1}; OS Clostridium sp. CAG:448. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium; environmental samples. OX NCBI_TaxID=1262808 {ECO:0000313|EMBL:CDC61082.1, ECO:0000313|Proteomes:UP000018074}; RN [1] {ECO:0000313|EMBL:CDC61082.1, ECO:0000313|Proteomes:UP000018074} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MGS:448 {ECO:0000313|Proteomes:UP000018074}; RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., RA Sunagawa S., Plichta D., Gautier L., Le Chatelier E., Peletier E., RA Bonde I., Nielsen T., Manichanh C., Arumugam M., Batto J., RA Santos M.B.Q.D., Blom N., Borruel N., Burgdorf K.S., Boumezbeur F., RA Casellas F., Dore J., Guarner F., Hansen T., Hildebrand F., Kaas R.S., RA Kennedy S., Kristiansen K., Kultima J.R., Leonard P., Levenez F., RA Lund O., Moumen B., Le Paslier D., Pons N., Pedersen O., Prifti E., RA Qin J., Raes J., Tap J., Tims S., Ussery D.W., Yamada T., RA MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P., Wang J., RA Brunak S., Ehrlich S.D.; RT "Dependencies among metagenomic species, viruses, plasmids and units RT of genetic variation."; RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:CDC61082.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CBFP010000132; CDC61082.1; -; Genomic_DNA. DR Proteomes; UP000018074; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000018074}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000018074}. FT DOMAIN 213 333 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 172 206 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 440 AA; 48444 MW; BF5FB4386BCD360E CRC64; MTETNRTSET NQEIQTRAVL VGMITREISE EEAEKGLNEL ERLLDTAGGA CVARVLQSKD TPDPATAIGS GKVREIRELC ENLDADLAVF DFELSPSQIR NLEDGIGTQT HEVRVIDRSM LILDIFALHA VTGEGKLQVE LAQLKYTAPR LSGHGKEMSR LGGGIGTRGP GESKLESDRR HMQRRITALE SELAVMEKNR RTMRASRDRS GLKKVAIVGY TNAGKSTLLN RLTDAGILAE DKLFATLDPT TRKFRLPGGE SILLTDTVGF IRKLPHHLVK AFRSTLDEAV YADMIIVLID ASDPECGEQL KVTENLLAEL GAADKPVLYV YNKCDRGVAH RPAIGKSAEQ AHIAYISALT GQGCEAMAET VEKMLHADQR RVTFRIPNAE QSALHTLYRD ATVESVEYGD DCVTAVAVVD RKTHGQLERY ALEKLPVKEE // ID R6U0Y0_9CLOT Unreviewed; 421 AA. AC R6U0Y0; DT 24-JUL-2013, integrated into UniProtKB/TrEMBL. DT 24-JUL-2013, sequence version 1. DT 12-APR-2017, entry version 23. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=BN667_00582 {ECO:0000313|EMBL:CDC79338.1}; OS Clostridium sp. CAG:465. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium; environmental samples. OX NCBI_TaxID=1262811 {ECO:0000313|EMBL:CDC79338.1, ECO:0000313|Proteomes:UP000018244}; RN [1] {ECO:0000313|EMBL:CDC79338.1, ECO:0000313|Proteomes:UP000018244} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MGS:465 {ECO:0000313|Proteomes:UP000018244}; RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., RA Sunagawa S., Plichta D., Gautier L., Le Chatelier E., Peletier E., RA Bonde I., Nielsen T., Manichanh C., Arumugam M., Batto J., RA Santos M.B.Q.D., Blom N., Borruel N., Burgdorf K.S., Boumezbeur F., RA Casellas F., Dore J., Guarner F., Hansen T., Hildebrand F., Kaas R.S., RA Kennedy S., Kristiansen K., Kultima J.R., Leonard P., Levenez F., RA Lund O., Moumen B., Le Paslier D., Pons N., Pedersen O., Prifti E., RA Qin J., Raes J., Tap J., Tims S., Ussery D.W., Yamada T., RA MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P., Wang J., RA Brunak S., Ehrlich S.D.; RT "Dependencies among metagenomic species, viruses, plasmids and units RT of genetic variation."; RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:CDC79338.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CBFY010000044; CDC79338.1; -; Genomic_DNA. DR Proteomes; UP000018244; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000018244}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000018244}. FT DOMAIN 197 366 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 156 190 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 421 AA; 48107 MW; 9D9ADF40B617FC31 CRC64; MEEKQKVLLV GVNLNDEFYF FKSMSELEEL VKACQMLPIG SIVQNLKEIN SAFYVGSGKL EEIKDKINEL HPDLVVFNNE LSPSQLKNLE LKLDIQILDR TSIILNIFAL RAKTNEAKMQ VEIAKLRYML PRLSGLHLSL GRQGGGSGFS NKGSGEKQIE LDRRIIEDRI SKLNKELSEI ETRRNIQRRK RSDSQIPLVS LVGYTNAGKS TLLNALVDLS LSDESKKVYE EDMLFATLET SIRKIKIKDG KEFLLSDTVG FIRELPHMLI KAFRSTLDEV KNSDLLLHVV DFSDEDYEEN IRVTNSTLKE IGADNIPVIY VFNKCDKVND SKLPYVDGNK VCISAKNNIG INELINVISN NIFKEYVTCK MQIPFKRGDI VSYLKEKYDF ISTQYTNDGT LIEICLNKKD YGKYKNYIIE E // ID R6U137_9FIRM Unreviewed; 432 AA. AC R6U137; DT 24-JUL-2013, integrated into UniProtKB/TrEMBL. DT 24-JUL-2013, sequence version 1. DT 12-APR-2017, entry version 23. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=BN580_01347 {ECO:0000313|EMBL:CDC73841.1}; OS Firmicutes bacterium CAG:272. OC Bacteria; Firmicutes; environmental samples. OX NCBI_TaxID=1263015 {ECO:0000313|EMBL:CDC73841.1, ECO:0000313|Proteomes:UP000017938}; RN [1] {ECO:0000313|EMBL:CDC73841.1, ECO:0000313|Proteomes:UP000017938} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MGS:272 {ECO:0000313|Proteomes:UP000017938}; RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., RA Sunagawa S., Plichta D., Gautier L., Le Chatelier E., Peletier E., RA Bonde I., Nielsen T., Manichanh C., Arumugam M., Batto J., RA Santos M.B.Q.D., Blom N., Borruel N., Burgdorf K.S., Boumezbeur F., RA Casellas F., Dore J., Guarner F., Hansen T., Hildebrand F., Kaas R.S., RA Kennedy S., Kristiansen K., Kultima J.R., Leonard P., Levenez F., RA Lund O., Moumen B., Le Paslier D., Pons N., Pedersen O., Prifti E., RA Qin J., Raes J., Tap J., Tims S., Ussery D.W., Yamada T., RA MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P., Wang J., RA Brunak S., Ehrlich S.D.; RT "Dependencies among metagenomic species, viruses, plasmids and units RT of genetic variation."; RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:CDC73841.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CBFW010000182; CDC73841.1; -; Genomic_DNA. DR Proteomes; UP000017938; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000017938}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000017938}. FT DOMAIN 210 376 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 169 203 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 432 AA; 47409 MW; C483EE11AC212AB9 CRC64; MEITGKIDTE RAATVGIITY DNPEDEVNAS LDELERLLET AGGRAVIRLV QSKENPDVRT FLGSGKMKEL AELCRGNDVT LVVCDSELSP SQIRNMEDIL DSGDPERPIR VIDRSMLILD IFALHATSAE GKLQVELAQL KYTAPRLIGK GIEMSRQGGG NIAMRGPGET KLESDRRHIR RRMQALEGEI AAIEQRRATQ RKQRDRSGIC RAAIVGYTNA GKSTLLNRLT DAGILAEDKL FATLDPTTRK FTLPGGTDVL LVDTVGFIRN LPHHLIKAFR STLDEAVYAD IVIMMTDASD PEAPAQLSVT ENLLCELGAS GKPTLCVFNK CDLEGDTIPS PPRSVPQENV FYVSAKTGEN IGALVSRLEE VVNEKTSRVT FVIPMAKQDV VAKLYRFAKV EEVTYDGENT VVTAICDGKA KGMFREYAAK PE // ID R6UBA5_9FIRM Unreviewed; 423 AA. AC R6UBA5; DT 24-JUL-2013, integrated into UniProtKB/TrEMBL. DT 24-JUL-2013, sequence version 1. DT 12-APR-2017, entry version 23. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=BN503_00114 {ECO:0000313|EMBL:CDC68017.1}; OS Oscillibacter sp. CAG:155. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Oscillospiraceae; OC Oscillibacter; environmental samples. OX NCBI_TaxID=1262910 {ECO:0000313|EMBL:CDC68017.1, ECO:0000313|Proteomes:UP000017942}; RN [1] {ECO:0000313|EMBL:CDC68017.1, ECO:0000313|Proteomes:UP000017942} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MGS:155 {ECO:0000313|Proteomes:UP000017942}; RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., RA Sunagawa S., Plichta D., Gautier L., Le Chatelier E., Peletier E., RA Bonde I., Nielsen T., Manichanh C., Arumugam M., Batto J., RA Santos M.B.Q.D., Blom N., Borruel N., Burgdorf K.S., Boumezbeur F., RA Casellas F., Dore J., Guarner F., Hansen T., Hildebrand F., Kaas R.S., RA Kennedy S., Kristiansen K., Kultima J.R., Leonard P., Levenez F., RA Lund O., Moumen B., Le Paslier D., Pons N., Pedersen O., Prifti E., RA Qin J., Raes J., Tap J., Tims S., Ussery D.W., Yamada T., RA MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P., Wang J., RA Brunak S., Ehrlich S.D.; RT "Dependencies among metagenomic species, viruses, plasmids and units RT of genetic variation."; RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:CDC68017.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CBFT010000024; CDC68017.1; -; Genomic_DNA. DR Proteomes; UP000017942; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000017942}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000017942}. FT DOMAIN 208 370 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 174 201 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 423 AA; 47041 MW; 4A630D27000D9381 CRC64; MQQTEEVRDK VVLVGLSSPV LKKEENADED TMEELSSLVE TAGAETVGIV LQNRPSPDPR TFIGEGKVAE VQLYCENVGA TMVIFDNDLS PSQQRVLTDL LGVQVLDRCG LILDIFAQRA KTKEGRLQVE LAQYQYLLPR LTGMWTHLER QAGTSGKGPI GSKGPGETQL ETDRRHIHRK IDKLREDLEE VRRVRGTQRE RRRKNEVPVV AIVGYTNAGK STLLNRLTGA GIPANNRLFD TLDTTSRLLS VSDTLDVVIS DTVGFIRKLP HQLVEAFKAT LEELEYADLL LHVIDVSNPE WQQQAQVVEN LILELGAGEL PRIDVFNKAD CLPVGEIMPH GEDICAISAK TGEGVDRLLE MIDQRLDKGT RRVTIRLPYD KGGLLDMLYR EAKVESVDYG ETINVVAVCG PRTLGQVEPF VTQ // ID R6UL44_9CLOT Unreviewed; 417 AA. AC R6UL44; DT 24-JUL-2013, integrated into UniProtKB/TrEMBL. DT 24-JUL-2013, sequence version 1. DT 10-MAY-2017, entry version 24. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=BN818_01757 {ECO:0000313|EMBL:CDC82724.1}; OS Clostridium sp. CAG:964. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium; environmental samples. OX NCBI_TaxID=1262848 {ECO:0000313|EMBL:CDC82724.1, ECO:0000313|Proteomes:UP000018136}; RN [1] {ECO:0000313|EMBL:CDC82724.1, ECO:0000313|Proteomes:UP000018136} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MGS:964 {ECO:0000313|Proteomes:UP000018136}; RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., RA Sunagawa S., Plichta D., Gautier L., Le Chatelier E., Peletier E., RA Bonde I., Nielsen T., Manichanh C., Arumugam M., Batto J., RA Santos M.B.Q.D., Blom N., Borruel N., Burgdorf K.S., Boumezbeur F., RA Casellas F., Dore J., Guarner F., Hansen T., Hildebrand F., Kaas R.S., RA Kennedy S., Kristiansen K., Kultima J.R., Leonard P., Levenez F., RA Lund O., Moumen B., Le Paslier D., Pons N., Pedersen O., Prifti E., RA Qin J., Raes J., Tap J., Tims S., Ussery D.W., Yamada T., RA MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P., Wang J., RA Brunak S., Ehrlich S.D.; RT "Dependencies among metagenomic species, viruses, plasmids and units RT of genetic variation."; RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:CDC82724.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CBFZ010000096; CDC82724.1; -; Genomic_DNA. DR Proteomes; UP000018136; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000018136}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000018136}. FT DOMAIN 200 363 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 159 193 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 417 AA; 46018 MW; 0D8858B8B7940352 CRC64; MELYENEAKP QRALLVCVDT GDYDAQSSLD ELWELAESAG AVPVATLTQK KEKPDTATYV GSGRLEEITS FCENQDIDLL IFDCELTPTQ IRNIEEAANV RTIDRTMLIL DIFALRARSK EGKLQVELAQ LKYMLPRLTG KGAAMSRLGG GIGTRGPGES KLETDRRHIR KRMETLKEQL ADVELHRNML KSRRKKDGII TVAIVGYTNA GKSTLMNCLT DAGVLAEDKL FATLDPTSRA LKLPNGVTVM LIDTVGLVRR LPHHLVEAFK STLEEAAEAD IILNVCDASS PEAYLHLQVT RELLQSLGCG DTPVIPVLNK WDKVDTQLGV LPSVSRSVRI SAKNAVGIDK LLAAIEENLP VQIKRVKLLI PFEKAGAVAD IRKRATLISE EYTAQGIMAE ALLEPELYGR LKQYICE // ID R6UTE6_9FIRM Unreviewed; 417 AA. AC R6UTE6; DT 24-JUL-2013, integrated into UniProtKB/TrEMBL. DT 24-JUL-2013, sequence version 1. DT 12-APR-2017, entry version 24. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=BN746_02539 {ECO:0000313|EMBL:CDC83461.1}; OS Erysipelotrichaceae bacterium CAG:64. OC Bacteria; Firmicutes; Erysipelotrichia; Erysipelotrichales; OC Erysipelotrichaceae; environmental samples. OX NCBI_TaxID=1262981 {ECO:0000313|EMBL:CDC83461.1, ECO:0000313|Proteomes:UP000018179}; RN [1] {ECO:0000313|EMBL:CDC83461.1, ECO:0000313|Proteomes:UP000018179} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MGS:64 {ECO:0000313|Proteomes:UP000018179}; RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., RA Sunagawa S., Plichta D., Gautier L., Le Chatelier E., Peletier E., RA Bonde I., Nielsen T., Manichanh C., Arumugam M., Batto J., RA Santos M.B.Q.D., Blom N., Borruel N., Burgdorf K.S., Boumezbeur F., RA Casellas F., Dore J., Guarner F., Hansen T., Hildebrand F., Kaas R.S., RA Kennedy S., Kristiansen K., Kultima J.R., Leonard P., Levenez F., RA Lund O., Moumen B., Le Paslier D., Pons N., Pedersen O., Prifti E., RA Qin J., Raes J., Tap J., Tims S., Ussery D.W., Yamada T., RA MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P., Wang J., RA Brunak S., Ehrlich S.D.; RT "Dependencies among metagenomic species, viruses, plasmids and units RT of genetic variation."; RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:CDC83461.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CBGA010000053; CDC83461.1; -; Genomic_DNA. DR Proteomes; UP000018179; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000018179}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}. FT DOMAIN 189 358 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 148 182 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 417 AA; 47919 MW; EB35DDFEF89310DD CRC64; MQQVIIVLAD TTEQAEKNEE FIELVQAADM EIKETFTQNL KSITLRTYIG TGKCEEIHAY LQEQEIQRVV FNHDLSPLQI RNLEEILQTP VMDRTELILA IFESRAVTRT ARLQIECAQL KKLLPRLIGA NTQLGRQSGS GKNKGAGEKQ LELDRRRINA RIQELQRELK KIEAQRFNQR RARQKSMLPL VSLVGYTNAG KSTIMNMLLE HSSPYEEDKK VLEKDMLFAT LDTSIRHIDL PDGKSFLLSD TVGFVSDLPH DLVEAFHSTL EEVQYASLLV QVVDVSSEEY ARQMEITQET LQQIKAADIP MITVYNKCDQ SGYQYPQVHA HDLYMSAKEK AGLQELLDLI HSHLYPDEKH VELHIPYQQT GIYSLLMKHA HVISRRDEED GIHLDAVLSD TLYQKYRNYV ICLKEEG // ID R6V743_9FIRM Unreviewed; 415 AA. AC R6V743; DT 24-JUL-2013, integrated into UniProtKB/TrEMBL. DT 24-JUL-2013, sequence version 1. DT 12-APR-2017, entry version 23. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=BN546_00390 {ECO:0000313|EMBL:CDC94033.1}; OS Firmicutes bacterium CAG:227. OC Bacteria; Firmicutes; environmental samples. OX NCBI_TaxID=1263010 {ECO:0000313|EMBL:CDC94033.1, ECO:0000313|Proteomes:UP000018294}; RN [1] {ECO:0000313|EMBL:CDC94033.1, ECO:0000313|Proteomes:UP000018294} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MGS:227 {ECO:0000313|Proteomes:UP000018294}; RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., RA Sunagawa S., Plichta D., Gautier L., Le Chatelier E., Peletier E., RA Bonde I., Nielsen T., Manichanh C., Arumugam M., Batto J., RA Santos M.B.Q.D., Blom N., Borruel N., Burgdorf K.S., Boumezbeur F., RA Casellas F., Dore J., Guarner F., Hansen T., Hildebrand F., Kaas R.S., RA Kennedy S., Kristiansen K., Kultima J.R., Leonard P., Levenez F., RA Lund O., Moumen B., Le Paslier D., Pons N., Pedersen O., Prifti E., RA Qin J., Raes J., Tap J., Tims S., Ussery D.W., Yamada T., RA MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P., Wang J., RA Brunak S., Ehrlich S.D.; RT "Dependencies among metagenomic species, viruses, plasmids and units RT of genetic variation."; RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:CDC94033.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CBGC010000231; CDC94033.1; -; Genomic_DNA. DR Proteomes; UP000018294; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000018294}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000018294}. FT DOMAIN 201 365 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 160 194 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 415 AA; 46709 MW; E4D0E5E08DFC7A2E CRC64; MEVFDLSDKT ERVILVGVQE NDGDDTEESL QELAELAKTA GAEVVGTVIQ KRERIHPGTY VGKGKIDEIR TLLNALDATG IICDDELSPV QMNHLQQELE SKIMDRTLLI LDIFASRAVT KEGKIQVELA QLRYRAVRLV GLGSSLSRLG GGIGTRGPGE KKLEMDRRLI KERISQLKKE LEHVKKHREL LREGRKKDRV MTAAIVGYTN AGKSTLLNTL TDAGVLSEDK LFATLDPTTR LLELDGGQRI YLTDTVGFIR KLPHHLIEAF KSTLEEAKYA DVILHVVDAS NPQVEEQMFI VYETLRELGV KDKTIVTLFN KQDRLAGNEI LRDFKADYVL KISARTGLGL DELKNTLEKI LIGNQIYIER VLDYKDAGML QLVRKYGQLI EEKYTENGIE IKARVPKDIY GRLGE // ID R6W184_9FIRM Unreviewed; 416 AA. AC R6W184; DT 24-JUL-2013, integrated into UniProtKB/TrEMBL. DT 24-JUL-2013, sequence version 1. DT 12-APR-2017, entry version 23. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=BN636_01476 {ECO:0000313|EMBL:CDD03150.1}; OS Ruminococcus sp. CAG:382. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Ruminococcaceae; OC Ruminococcus; environmental samples. OX NCBI_TaxID=1262957 {ECO:0000313|EMBL:CDD03150.1, ECO:0000313|Proteomes:UP000018166}; RN [1] {ECO:0000313|EMBL:CDD03150.1, ECO:0000313|Proteomes:UP000018166} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MGS:382 {ECO:0000313|Proteomes:UP000018166}; RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., RA Sunagawa S., Plichta D., Gautier L., Le Chatelier E., Peletier E., RA Bonde I., Nielsen T., Manichanh C., Arumugam M., Batto J., RA Santos M.B.Q.D., Blom N., Borruel N., Burgdorf K.S., Boumezbeur F., RA Casellas F., Dore J., Guarner F., Hansen T., Hildebrand F., Kaas R.S., RA Kennedy S., Kristiansen K., Kultima J.R., Leonard P., Levenez F., RA Lund O., Moumen B., Le Paslier D., Pons N., Pedersen O., Prifti E., RA Qin J., Raes J., Tap J., Tims S., Ussery D.W., Yamada T., RA MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P., Wang J., RA Brunak S., Ehrlich S.D.; RT "Dependencies among metagenomic species, viruses, plasmids and units RT of genetic variation."; RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:CDD03150.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CBGH010000186; CDD03150.1; -; Genomic_DNA. DR Proteomes; UP000018166; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000018166}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000018166}. FT DOMAIN 200 362 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 159 186 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 416 AA; 45820 MW; 7F256A93DD7F8E98 CRC64; METEIKLTGA VLCALSENTS DDGLDASLDE LERLLDTAGG QCVARMVQYR DKPDVRTYFG KGKIEELADF IRKDGTVELV VFNNELSPSQ IANIGDEVGV RVIDRTMLIL DIFAKNAVTA EGKLQVEIAC LRYSAPRLVG HGKDMSRLGG GIGTRGPGES KLESDRRHLN RRIAALQAQL DELESNRTVQ HSARRKSNIK TAAIVGYTNA GKSTLLNYLT GAGILAEDKL FATLDPTTRR LKLPDGQDML LTDTVGFIDR LPTHLVKAFK STLDELKYAD IIIEVTDASE CEDERRRKRA VTESLIDELG GGGKPLVLVY NKCDQETDSD FIPPEAVRIS AKSGDNIDGF LETLNGIVNA GRRRVWLKFP HSRAGELNNL YKNASVLETD YTDDGVRVFV ECGSDIYGKY ADFTEP // ID R6W1U2_9BACT Unreviewed; 420 AA. AC R6W1U2; DT 24-JUL-2013, integrated into UniProtKB/TrEMBL. DT 24-JUL-2013, sequence version 1. DT 12-APR-2017, entry version 23. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=BN725_00793 {ECO:0000313|EMBL:CDD03390.1}; OS Prevotella sp. CAG:592. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Prevotellaceae; OC Prevotella; environmental samples. OX NCBI_TaxID=1262931 {ECO:0000313|EMBL:CDD03390.1, ECO:0000313|Proteomes:UP000018343}; RN [1] {ECO:0000313|EMBL:CDD03390.1, ECO:0000313|Proteomes:UP000018343} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MGS:592 {ECO:0000313|Proteomes:UP000018343}; RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., RA Sunagawa S., Plichta D., Gautier L., Le Chatelier E., Peletier E., RA Bonde I., Nielsen T., Manichanh C., Arumugam M., Batto J., RA Santos M.B.Q.D., Blom N., Borruel N., Burgdorf K.S., Boumezbeur F., RA Casellas F., Dore J., Guarner F., Hansen T., Hildebrand F., Kaas R.S., RA Kennedy S., Kristiansen K., Kultima J.R., Leonard P., Levenez F., RA Lund O., Moumen B., Le Paslier D., Pons N., Pedersen O., Prifti E., RA Qin J., Raes J., Tap J., Tims S., Ussery D.W., Yamada T., RA MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P., Wang J., RA Brunak S., Ehrlich S.D.; RT "Dependencies among metagenomic species, viruses, plasmids and units RT of genetic variation."; RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:CDD03390.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CBGI010000003; CDD03390.1; -; Genomic_DNA. DR Proteomes; UP000018343; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000018343}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000018343}. FT DOMAIN 216 400 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 420 AA; 48062 MW; 122664256109F331 CRC64; MKEFVISEVK AETAVLVGLI TKEQDEAKTK EYLDELEFLA DTAGAVTVKR FTQRVNGPNQ TTYVGKGKLE EIKQYILDEE DAEREIGMVI FDDELSAKQI RNIENELKVK ILDRTSLILD IFAMRAQTAN AKTQVELAQY RYMLPRLQRL WTHLERQGGG SGSGGGKGSV GLRGPGETQL EMDRRIILQR MSLLKERLAE IDKQKTTQRK NRGRLIRVAL VGYTNVGKST LMNLMSKSEV FAENKLFATL DTTVRKVVVE NLPFLLADTV GFIRKLPTDL VDSFKSTLDE VREADLLLHV VDISHPDFEE QIKVVDKTLA DLGCADKPSM IIFNKIDAYT WVEKEADDLT PATKENMTLD DLKKTWMAKM GDDCLFISAR EKINIQEMRD VIYKRVRELH VQKYPYNDFL YQDYSEEEQN // ID R6W3N3_9BACT Unreviewed; 411 AA. AC R6W3N3; DT 24-JUL-2013, integrated into UniProtKB/TrEMBL. DT 24-JUL-2013, sequence version 1. DT 12-APR-2017, entry version 23. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=BN576_00937 {ECO:0000313|EMBL:CDC98806.1}; OS Alistipes sp. CAG:268. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Rikenellaceae; OC Alistipes; environmental samples. OX NCBI_TaxID=1262693 {ECO:0000313|EMBL:CDC98806.1, ECO:0000313|Proteomes:UP000018329}; RN [1] {ECO:0000313|EMBL:CDC98806.1, ECO:0000313|Proteomes:UP000018329} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MGS:268 {ECO:0000313|Proteomes:UP000018329}; RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., RA Sunagawa S., Plichta D., Gautier L., Le Chatelier E., Peletier E., RA Bonde I., Nielsen T., Manichanh C., Arumugam M., Batto J., RA Santos M.B.Q.D., Blom N., Borruel N., Burgdorf K.S., Boumezbeur F., RA Casellas F., Dore J., Guarner F., Hansen T., Hildebrand F., Kaas R.S., RA Kennedy S., Kristiansen K., Kultima J.R., Leonard P., Levenez F., RA Lund O., Moumen B., Le Paslier D., Pons N., Pedersen O., Prifti E., RA Qin J., Raes J., Tap J., Tims S., Ussery D.W., Yamada T., RA MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P., Wang J., RA Brunak S., Ehrlich S.D.; RT "Dependencies among metagenomic species, viruses, plasmids and units RT of genetic variation."; RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:CDC98806.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CBGE010000166; CDC98806.1; -; Genomic_DNA. DR Proteomes; UP000018329; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000018329}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000018329}. FT DOMAIN 216 400 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 177 211 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 411 AA; 47193 MW; E935B42262523777 CRC64; MNQKDISKEN SKNSSPAAQP ADWKERAVLV AVVRDNQDPR QAEEYLDELE FLAETADIVS VKRFTQRLAQ PSARIYVGPG KLQEIADYCR EEEIDVVIFD DELSPSQTRN IEKEMPCRLL DRTRLILDIF MSRAQTAYAK TQVQLANYEY MLPRLSGLWT HLERQRGGTG TRGGAGEREI ETDRRIIRNR IAKLKEDLKK IDRQMAVQRS NRGAMVRVAL VGYTNVGKST LMNLISKSEV FAENKLFATL DTTVRKVVFD NLPFLLSDTV GFIRKLPTEL IESFKSTLDE VREADLLVHV VDISHPQFED QIAVVKQTLQ EIGAGDKPVY LVFNKVDAYT YIKKEEDDLT PSTRENRSLD DLRQSWIARA NTPCIFLSAL ERTNIEKFRS DLYGMVREIH AGRYPFNNFL Y // ID R6WUV7_9FIRM Unreviewed; 415 AA. AC R6WUV7; DT 24-JUL-2013, integrated into UniProtKB/TrEMBL. DT 24-JUL-2013, sequence version 1. DT 12-APR-2017, entry version 23. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=BN605_01267 {ECO:0000313|EMBL:CDD07836.1}; OS Dorea sp. CAG:317. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Lachnospiraceae; OC Dorea; environmental samples. OX NCBI_TaxID=1262873 {ECO:0000313|EMBL:CDD07836.1, ECO:0000313|Proteomes:UP000018262}; RN [1] {ECO:0000313|EMBL:CDD07836.1, ECO:0000313|Proteomes:UP000018262} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MGS:317 {ECO:0000313|Proteomes:UP000018262}; RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., RA Sunagawa S., Plichta D., Gautier L., Le Chatelier E., Peletier E., RA Bonde I., Nielsen T., Manichanh C., Arumugam M., Batto J., RA Santos M.B.Q.D., Blom N., Borruel N., Burgdorf K.S., Boumezbeur F., RA Casellas F., Dore J., Guarner F., Hansen T., Hildebrand F., Kaas R.S., RA Kennedy S., Kristiansen K., Kultima J.R., Leonard P., Levenez F., RA Lund O., Moumen B., Le Paslier D., Pons N., Pedersen O., Prifti E., RA Qin J., Raes J., Tap J., Tims S., Ussery D.W., Yamada T., RA MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P., Wang J., RA Brunak S., Ehrlich S.D.; RT "Dependencies among metagenomic species, viruses, plasmids and units RT of genetic variation."; RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:CDD07836.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CBGJ010000080; CDD07836.1; -; Genomic_DNA. DR Proteomes; UP000018262; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000018262}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000018262}. FT DOMAIN 199 363 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 158 192 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 415 AA; 46498 MW; 2385103FC30AD1C7 CRC64; MIELKKESER VLLVGVGLPG QDDVEDSLKE LSELAATAGA QTVGQVIQSR EQIHPGTYVG KGKIDEIKDL LWELDATGII CDDELSPVQM KNLQDELDVK VMDRTLVILD IFAGRASTSE GKIQVELAQL KYRQTRLTGF GTALSRLGGG IGTRGPGEKK LEMDRRLIKN RIAQLNRELK EVKRHREVTR ERRSKNHVPV AAIVGYTNAG KSTLLNALTG ADILAEDQLF ATLDPTTRSL KLPKGQEILL TDTVGFIKKL PHHLIEAFKS TLEEAKYADI ILHVVDTSSP QMDSQMYTVY ETLQNLGVKD KPIITVFNKQ DRLEEDSVIR DFKADYTVKT SAKTGAGLIE LQETIEAVLR EQKVFLERVY PYSDAAKLQL IRKYGELETE EYREDGIFVR AYVPVQVYAK VSEPM // ID R6WWX3_9BACT Unreviewed; 403 AA. AC R6WWX3; DT 24-JUL-2013, integrated into UniProtKB/TrEMBL. DT 24-JUL-2013, sequence version 1. DT 30-AUG-2017, entry version 24. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=BN675_02256 {ECO:0000313|EMBL:CDD13840.1}; OS Parabacteroides merdae CAG:48. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Tannerellaceae; OC Parabacteroides; environmental samples. OX NCBI_TaxID=1263094 {ECO:0000313|EMBL:CDD13840.1, ECO:0000313|Proteomes:UP000018407}; RN [1] {ECO:0000313|EMBL:CDD13840.1, ECO:0000313|Proteomes:UP000018407} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MGS:48 {ECO:0000313|Proteomes:UP000018407}; RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., RA Sunagawa S., Plichta D., Gautier L., Le Chatelier E., Peletier E., RA Bonde I., Nielsen T., Manichanh C., Arumugam M., Batto J., RA Santos M.B.Q.D., Blom N., Borruel N., Burgdorf K.S., Boumezbeur F., RA Casellas F., Dore J., Guarner F., Hansen T., Hildebrand F., Kaas R.S., RA Kennedy S., Kristiansen K., Kultima J.R., Leonard P., Levenez F., RA Lund O., Moumen B., Le Paslier D., Pons N., Pedersen O., Prifti E., RA Qin J., Raes J., Tap J., Tims S., Ussery D.W., Yamada T., RA MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P., Wang J., RA Brunak S., Ehrlich S.D.; RT "Dependencies among metagenomic species, viruses, plasmids and units RT of genetic variation."; RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:CDD13840.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CBGM010000220; CDD13840.1; -; Genomic_DNA. DR Proteomes; UP000018407; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000018407}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000018407}. FT DOMAIN 202 386 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 403 AA; 46753 MW; 3DC9B2F947802375 CRC64; MKEFIISEAQ TEKAVLVGLI TPEQNEQKVK EYLDELAFLA DTAGVEAVKR FYQKLDYPNS VTFVGSGKLQ EIKEYVVENE IGLVIFDDEL SAKQLRNIEK ELQVKILDRT NLILDIFARR AQTAHAKTQV ELAQYKYMLP RLTRLWTHLE RQRGGVGMRG PGETQLETDK RIILDKISKL KRDLVEIDKQ KSVQRKNRGK MVRVALVGYT NVGKSTLMNL LSKSEVFAEN KLFATLDTTV RKVIVDNLPF LLSDTVGFIR KLPTELVESF KSTLDEVREA DLLVHVVDIS HPTFEEQIEV VNRTLSEIDK TEKPMIMVFN KIDAFTFVPK DEDDLTPRTR ENIDLDELKR TWMNKMQDNC IFISAKKRTN IDALKALLYE RVKQIHITRF PYNDFLFQQY DEE // ID R6WXQ0_9CLOT Unreviewed; 527 AA. AC R6WXQ0; DT 24-JUL-2013, integrated into UniProtKB/TrEMBL. DT 24-JUL-2013, sequence version 1. DT 07-JUN-2017, entry version 25. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=BN619_00981 {ECO:0000313|EMBL:CDD08826.1}; OS Clostridium sp. CAG:349. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium; environmental samples. OX NCBI_TaxID=1262797 {ECO:0000313|EMBL:CDD08826.1, ECO:0000313|Proteomes:UP000018231}; RN [1] {ECO:0000313|EMBL:CDD08826.1, ECO:0000313|Proteomes:UP000018231} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MGS:349 {ECO:0000313|Proteomes:UP000018231}; RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., RA Sunagawa S., Plichta D., Gautier L., Le Chatelier E., Peletier E., RA Bonde I., Nielsen T., Manichanh C., Arumugam M., Batto J., RA Santos M.B.Q.D., Blom N., Borruel N., Burgdorf K.S., Boumezbeur F., RA Casellas F., Dore J., Guarner F., Hansen T., Hildebrand F., Kaas R.S., RA Kennedy S., Kristiansen K., Kultima J.R., Leonard P., Levenez F., RA Lund O., Moumen B., Le Paslier D., Pons N., Pedersen O., Prifti E., RA Qin J., Raes J., Tap J., Tims S., Ussery D.W., Yamada T., RA MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P., Wang J., RA Brunak S., Ehrlich S.D.; RT "Dependencies among metagenomic species, viruses, plasmids and units RT of genetic variation."; RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:CDD08826.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CBGK010000030; CDD08826.1; -; Genomic_DNA. DR Proteomes; UP000018231; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000018231}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000018231}. FT DOMAIN 370 527 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 527 AA; 58019 MW; BA5C9C7F4998AE09 CRC64; MVYGNTKGIK QTVLARLDAL IGAYDKNLLI DRTVLSTIAE ITEKINREIC VFIARNGQVV AVGVGDSGTV SLEDFSLKRS DKRFQGVRCV HTHPKGSGKL SDMDTSALTS MRLDAMIAVG VLHGGANDVE VAFINGKKID RFYFKSASKI DDADMISKIT EYERKSVIPD VVENTPKTRG AILVNVGTGS DLDVEIEELK RLADTMGLDV KGAVLQKQNP DKGYCAGLGK LEEIKRLVQV ENAEFVIFNN MLTGSQLNNI EEYVGAKVID RPMLILEIFA RHATSNEGKL QVQLAMMKYT LPKLLGQGKE LSRIGGGGSG GAATKGSGET KLETDRRRIR RSIYELSERI EILKKERDLR RERRKKSGIK TVAIVGYTNA GKSTLMNLLT KAGVKAEDKL FATLDPVTRK IFVDIGKEYL LTDTVGFIDN LPHEFVDAFR STLEEATYAD LILHVADCSS KDLERQEKVV KDVLTSLGVT DTPIITVYNK VDENAGFFTD EKNAVVISAK TGDGVNKLKE MIVEKLF // ID R6WZK4_9BACT Unreviewed; 415 AA. AC R6WZK4; DT 24-JUL-2013, integrated into UniProtKB/TrEMBL. DT 24-JUL-2013, sequence version 1. DT 12-APR-2017, entry version 23. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=BN673_00530 {ECO:0000313|EMBL:CDC99567.1}; OS Prevotella sp. CAG:474. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Prevotellaceae; OC Prevotella; environmental samples. OX NCBI_TaxID=1262926 {ECO:0000313|EMBL:CDC99567.1, ECO:0000313|Proteomes:UP000018116}; RN [1] {ECO:0000313|EMBL:CDC99567.1, ECO:0000313|Proteomes:UP000018116} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MGS:474 {ECO:0000313|Proteomes:UP000018116}; RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., RA Sunagawa S., Plichta D., Gautier L., Le Chatelier E., Peletier E., RA Bonde I., Nielsen T., Manichanh C., Arumugam M., Batto J., RA Santos M.B.Q.D., Blom N., Borruel N., Burgdorf K.S., Boumezbeur F., RA Casellas F., Dore J., Guarner F., Hansen T., Hildebrand F., Kaas R.S., RA Kennedy S., Kristiansen K., Kultima J.R., Leonard P., Levenez F., RA Lund O., Moumen B., Le Paslier D., Pons N., Pedersen O., Prifti E., RA Qin J., Raes J., Tap J., Tims S., Ussery D.W., Yamada T., RA MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P., Wang J., RA Brunak S., Ehrlich S.D.; RT "Dependencies among metagenomic species, viruses, plasmids and units RT of genetic variation."; RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:CDC99567.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CBGF010000077; CDC99567.1; -; Genomic_DNA. DR Proteomes; UP000018116; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000018116}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000018116}. FT DOMAIN 216 400 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 415 AA; 47826 MW; 51BB5C38E3587F30 CRC64; MKEFVISEVK AETAILVGLI TKDQDEEKTT EYLDELEFLA DTAGAVTVKR FTQKVNGPNT VTYVGKGKLE EIKQYIEDEE DNDREIGMVI FDDELSAKQM RNIENELKVK ILDRTSLILD IFAMRAQTAN AKTQVELAQY RYMLPRLQRL WTHLERQGGG SGSGGGKGSV GLRGPGETQL EMDRRIILQR ITLLKQRLLE IDKQKTTQRK NRGRMVRVAL VGYTNVGKST IMNLLAKSEV FAENKLFATL DTTVRKVVID NLPFLLADTV GFIRKLPTDL VDSFKSTLDE VREADLLVHV VDISHPDFEE QIEVVNQTLK DLDSADKPMV LVFNKIDNYH WVEKEADDLT PMTRENITLD ELRRTWMAKM SDNCIFISAR ERENIDHFRD VLYRKIRELH VQKYPYNDFL YPSEE // ID R6X485_9BACT Unreviewed; 393 AA. AC R6X485; DT 24-JUL-2013, integrated into UniProtKB/TrEMBL. DT 24-JUL-2013, sequence version 1. DT 12-APR-2017, entry version 23. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=BN655_01203 {ECO:0000313|EMBL:CDD18348.1}; OS Alistipes sp. CAG:435. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Rikenellaceae; OC Alistipes; environmental samples. OX NCBI_TaxID=1262695 {ECO:0000313|EMBL:CDD18348.1, ECO:0000313|Proteomes:UP000017965}; RN [1] {ECO:0000313|EMBL:CDD18348.1, ECO:0000313|Proteomes:UP000017965} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MGS:435 {ECO:0000313|Proteomes:UP000017965}; RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., RA Sunagawa S., Plichta D., Gautier L., Le Chatelier E., Peletier E., RA Bonde I., Nielsen T., Manichanh C., Arumugam M., Batto J., RA Santos M.B.Q.D., Blom N., Borruel N., Burgdorf K.S., Boumezbeur F., RA Casellas F., Dore J., Guarner F., Hansen T., Hildebrand F., Kaas R.S., RA Kennedy S., Kristiansen K., Kultima J.R., Leonard P., Levenez F., RA Lund O., Moumen B., Le Paslier D., Pons N., Pedersen O., Prifti E., RA Qin J., Raes J., Tap J., Tims S., Ussery D.W., Yamada T., RA MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P., Wang J., RA Brunak S., Ehrlich S.D.; RT "Dependencies among metagenomic species, viruses, plasmids and units RT of genetic variation."; RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:CDD18348.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CBGN010000072; CDD18348.1; -; Genomic_DNA. DR Proteomes; UP000017965; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000017965}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000017965}. FT DOMAIN 198 382 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 166 193 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 393 AA; 45312 MW; 1187D233F4B71AAD CRC64; MEELIEKAVF VGIIRQNDDD RKVMEYLDEL EFLAETAGAK GDKKFVQRLD KPEKATYIRS GKLQEIAEYC EENEIKYVIF DDELTGMQQR NIEKVINCSS VIDRTSLILE IFAQRAKTSY AKMQVELARY NYMLPRLAGM WTHLERQRGG MGTRGGMGET QIEIDRRIVK ERIARLKEQL KKVDKQMATQ RGNRGSMVRL SLVGYTNVGK STIMNLLAKS DVFAENKLFA TLDTTVRKVV IENVPFLLSD TVGFIRKLPT QLVEAFKSTL DEVREADILL HVVDISHPGF EEQMEVVERT LQEIGASNKP VFVIFNKIDA YTYEEYDEFS LTPKGKENRS LDELKNSWIA QEKTPCIFIS AINKTNIEKL RSDIYKMVAE IHAGRYPFNN FLW // ID R6XU78_9BACT Unreviewed; 415 AA. AC R6XU78; DT 24-JUL-2013, integrated into UniProtKB/TrEMBL. DT 24-JUL-2013, sequence version 1. DT 12-APR-2017, entry version 22. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=BN769_02219 {ECO:0000313|EMBL:CDD19836.1}; OS Prevotella sp. CAG:732. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Prevotellaceae; OC Prevotella; environmental samples. OX NCBI_TaxID=1262934 {ECO:0000313|EMBL:CDD19836.1, ECO:0000313|Proteomes:UP000018039}; RN [1] {ECO:0000313|EMBL:CDD19836.1, ECO:0000313|Proteomes:UP000018039} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MGS:732 {ECO:0000313|Proteomes:UP000018039}; RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., RA Sunagawa S., Plichta D., Gautier L., Le Chatelier E., Peletier E., RA Bonde I., Nielsen T., Manichanh C., Arumugam M., Batto J., RA Santos M.B.Q.D., Blom N., Borruel N., Burgdorf K.S., Boumezbeur F., RA Casellas F., Dore J., Guarner F., Hansen T., Hildebrand F., Kaas R.S., RA Kennedy S., Kristiansen K., Kultima J.R., Leonard P., Levenez F., RA Lund O., Moumen B., Le Paslier D., Pons N., Pedersen O., Prifti E., RA Qin J., Raes J., Tap J., Tims S., Ussery D.W., Yamada T., RA MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P., Wang J., RA Brunak S., Ehrlich S.D.; RT "Dependencies among metagenomic species, viruses, plasmids and units RT of genetic variation."; RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:CDD19836.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CBGP010000087; CDD19836.1; -; Genomic_DNA. DR Proteomes; UP000018039; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000018039}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000018039}. FT DOMAIN 216 400 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 415 AA; 47651 MW; 23CF89E2D5E92819 CRC64; MKEFVISEVK AETAILVGLV TKEQDEAKTK EYLDELEFLA DTAGAVTVKR FTQKVVAPNQ TSYVGKGKLE EIKQYIKDEE EEDREIGMVI FDDELSAKQI RNIENELQVK ILDRTSLILD IFAMRAQTAA AKTQVELAQY RYMLPRLQRL WTHLERQGGG SGSGGGKGSV GLRGPGETQL EMDRRIILGR MSLLKERLAE IDKQKTTQRK NRGRLIRVAL VGYTNVGKST IMNLLSKSEV FAENKLFATL DTTVRKVVVE NLPFLLADTV GFIRKLPTDL VDSFKSTLDE TREADLLLHV VDISHPDFEE QIQVVENTLK ELGCSDKPSM IIFNKIDNYS WVEKEEDDLT PMQKENIPLE DLKKTWMAKL HDDCLFISAK NKENIEEFRN VLYKKVRELH VQKYPYNDFL YQDYE // ID R6XY62_9FIRM Unreviewed; 427 AA. AC R6XY62; DT 24-JUL-2013, integrated into UniProtKB/TrEMBL. DT 24-JUL-2013, sequence version 1. DT 10-MAY-2017, entry version 24. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=BN602_00301 {ECO:0000313|EMBL:CDD21281.1}; OS Firmicutes bacterium CAG:313. OC Bacteria; Firmicutes; environmental samples. OX NCBI_TaxID=1263017 {ECO:0000313|EMBL:CDD21281.1, ECO:0000313|Proteomes:UP000018373}; RN [1] {ECO:0000313|EMBL:CDD21281.1, ECO:0000313|Proteomes:UP000018373} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MGS:313 {ECO:0000313|Proteomes:UP000018373}; RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., RA Sunagawa S., Plichta D., Gautier L., Le Chatelier E., Peletier E., RA Bonde I., Nielsen T., Manichanh C., Arumugam M., Batto J., RA Santos M.B.Q.D., Blom N., Borruel N., Burgdorf K.S., Boumezbeur F., RA Casellas F., Dore J., Guarner F., Hansen T., Hildebrand F., Kaas R.S., RA Kennedy S., Kristiansen K., Kultima J.R., Leonard P., Levenez F., RA Lund O., Moumen B., Le Paslier D., Pons N., Pedersen O., Prifti E., RA Qin J., Raes J., Tap J., Tims S., Ussery D.W., Yamada T., RA MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P., Wang J., RA Brunak S., Ehrlich S.D.; RT "Dependencies among metagenomic species, viruses, plasmids and units RT of genetic variation."; RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:CDD21281.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CBGQ010000007; CDD21281.1; -; Genomic_DNA. DR Proteomes; UP000018373; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000018373}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000018373}. FT DOMAIN 203 373 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 162 189 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 427 AA; 48066 MW; FB377FD8EB47B02D CRC64; MQEIEELTKA IIVGVNTGNE EYFSYQFTEL ANLCEARGIE VVDNVIQNLP HPNNKSYVGS GKLTEIATLK DAYGIDLIVV LDELSPVQLK NMEDALNCEV IDRTMLILEI FQLRAKTKEA ILQVEIANLK YMLPRLVGSY TNLSRIGGGG GGGTGARRGS GETKLEEDRR HIERRIQKAT EELKEIVLSR QVARKARKAN NTKTVAFVGY TNAGKSSTIN TLLNYFDKDS DKQVFVKNML FATLETSTRS IKLPTNQEFL ITDTVGFVSN LPHHLIESFK STLEEIKEAD LIVHVVDASS PYAQTQIATT IEVLNEIGVI DIPTVYALNK VDLVKNKMFL PKVNKDAIRI SNETNEGIKD LIEYIKNSLF NDEITCKLLL PYDKGDIFTT LKEKAHVHNF SYENNGIVVE VTLSRYLYNL YNKYLKK // ID R6XYJ3_9BACT Unreviewed; 405 AA. AC R6XYJ3; DT 24-JUL-2013, integrated into UniProtKB/TrEMBL. DT 24-JUL-2013, sequence version 1. DT 12-APR-2017, entry version 24. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=BN590_01150 {ECO:0000313|EMBL:CDD24074.1}; OS Alistipes sp. CAG:29. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Rikenellaceae; OC Alistipes; environmental samples. OX NCBI_TaxID=1262694 {ECO:0000313|EMBL:CDD24074.1, ECO:0000313|Proteomes:UP000018138}; RN [1] {ECO:0000313|EMBL:CDD24074.1, ECO:0000313|Proteomes:UP000018138} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MGS:29 {ECO:0000313|Proteomes:UP000018138}; RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., RA Sunagawa S., Plichta D., Gautier L., Le Chatelier E., Peletier E., RA Bonde I., Nielsen T., Manichanh C., Arumugam M., Batto J., RA Santos M.B.Q.D., Blom N., Borruel N., Burgdorf K.S., Boumezbeur F., RA Casellas F., Dore J., Guarner F., Hansen T., Hildebrand F., Kaas R.S., RA Kennedy S., Kristiansen K., Kultima J.R., Leonard P., Levenez F., RA Lund O., Moumen B., Le Paslier D., Pons N., Pedersen O., Prifti E., RA Qin J., Raes J., Tap J., Tims S., Ussery D.W., Yamada T., RA MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P., Wang J., RA Brunak S., Ehrlich S.D.; RT "Dependencies among metagenomic species, viruses, plasmids and units RT of genetic variation."; RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:CDD24074.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CBGS010000016; CDD24074.1; -; Genomic_DNA. DR Proteomes; UP000018138; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000018138}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000018138}. FT DOMAIN 210 394 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 178 205 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 405 AA; 46369 MW; 40F73A989C0D27C9 CRC64; MTENKNITPN SEAVPDCRER AVMVAVIRDN QDPRQAEEFL DELEFLAETA DIVSVKRFTQ RLPQPSARIY VGPGKLEEIA GYCREQQIDV VIFDDELSPS QTRNIEKAMP CRILDRTRLI LDIFMSRAQT AYAKTQVQLA NYEYMLPRLS GMWTHLERQR GGTGTRGGAG EREIETDRRI IRNRISKLKE DLQKIDRQMA VQRSNRGSMV RVALVGYTNV GKSTLMNLIS KSEVFAENKL FATLDTTVRK VVFDNLPFLL SDTVGFIRKL PTELIESFKS TLDEVREADL LVHVVDISHP QFEEQIDVVK QTLQDIGAGD KPVYLVFNKV DAYTYVRKDD DDLTPATREN LSLDDLKKSW IARANTPCIF LSALAKTNIE KFRSDLYGMV REIHAGRYPF NNFLY // ID R6YA93_9FIRM Unreviewed; 414 AA. AC R6YA93; DT 24-JUL-2013, integrated into UniProtKB/TrEMBL. DT 24-JUL-2013, sequence version 1. DT 12-APR-2017, entry version 24. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=BN815_02032 {ECO:0000313|EMBL:CDD30845.1}; OS Firmicutes bacterium CAG:94. OC Bacteria; Firmicutes; environmental samples. OX NCBI_TaxID=1262989 {ECO:0000313|EMBL:CDD30845.1, ECO:0000313|Proteomes:UP000018237}; RN [1] {ECO:0000313|EMBL:CDD30845.1, ECO:0000313|Proteomes:UP000018237} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MGS:94 {ECO:0000313|Proteomes:UP000018237}; RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., RA Sunagawa S., Plichta D., Gautier L., Le Chatelier E., Peletier E., RA Bonde I., Nielsen T., Manichanh C., Arumugam M., Batto J., RA Santos M.B.Q.D., Blom N., Borruel N., Burgdorf K.S., Boumezbeur F., RA Casellas F., Dore J., Guarner F., Hansen T., Hildebrand F., Kaas R.S., RA Kennedy S., Kristiansen K., Kultima J.R., Leonard P., Levenez F., RA Lund O., Moumen B., Le Paslier D., Pons N., Pedersen O., Prifti E., RA Qin J., Raes J., Tap J., Tims S., Ussery D.W., Yamada T., RA MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P., Wang J., RA Brunak S., Ehrlich S.D.; RT "Dependencies among metagenomic species, viruses, plasmids and units RT of genetic variation."; RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:CDD30845.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CBGU010000333; CDD30845.1; -; Genomic_DNA. DR Proteomes; UP000018237; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000018237}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000018237}. FT DOMAIN 198 360 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 414 AA; 45217 MW; 594AF49AEEE8AD07 CRC64; MYENETRPQR ALLVSLDTGE YNAEVSLGEL EELAHTAGAE PVLTLTQKRP APDTATCIGS GMVEQAAQLC QQEEIDLLIF DRELTPTQIR NLEKACGVQV IDRTTLILDI FAQRARSKEG KLQVELAQLK YLLPRLGGQG TSLSRLGGGI GTRGPGETKL ETDRRHIRRR ISSLKEQLRD VEAARGLINR RREKDGTVTV ALVGYTNAGK STLMNQLTQA GVLAEDKLFA TLDPTARALK LPCGKTVMLI DTVGLIRRLP HHLVEAFKST LEQAATADIL LNVCDASSGE ARDHLEVTNT LLNELGAAGH PIIPVLNKWD AVEDPELAPR LPGAVRISAL HGDGIPELLK AIEDSLPEKT FPVELLLPFS KTGLAAKLRE EGAVTSEEYV PEGLRVSAQV DQRLYALVKE FEIQ // ID R6YP53_9BACE Unreviewed; 419 AA. AC R6YP53; DT 24-JUL-2013, integrated into UniProtKB/TrEMBL. DT 24-JUL-2013, sequence version 1. DT 12-APR-2017, entry version 23. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=BN762_00932 {ECO:0000313|EMBL:CDD33214.1}; OS Bacteroides sp. CAG:714. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae; OC Bacteroides; environmental samples. OX NCBI_TaxID=1262749 {ECO:0000313|EMBL:CDD33214.1, ECO:0000313|Proteomes:UP000018068}; RN [1] {ECO:0000313|EMBL:CDD33214.1, ECO:0000313|Proteomes:UP000018068} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MGS:714 {ECO:0000313|Proteomes:UP000018068}; RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., RA Sunagawa S., Plichta D., Gautier L., Le Chatelier E., Peletier E., RA Bonde I., Nielsen T., Manichanh C., Arumugam M., Batto J., RA Santos M.B.Q.D., Blom N., Borruel N., Burgdorf K.S., Boumezbeur F., RA Casellas F., Dore J., Guarner F., Hansen T., Hildebrand F., Kaas R.S., RA Kennedy S., Kristiansen K., Kultima J.R., Leonard P., Levenez F., RA Lund O., Moumen B., Le Paslier D., Pons N., Pedersen O., Prifti E., RA Qin J., Raes J., Tap J., Tims S., Ussery D.W., Yamada T., RA MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P., Wang J., RA Brunak S., Ehrlich S.D.; RT "Dependencies among metagenomic species, viruses, plasmids and units RT of genetic variation."; RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:CDD33214.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CBGW010000100; CDD33214.1; -; Genomic_DNA. DR Proteomes; UP000018068; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000018068}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000018068}. FT DOMAIN 217 401 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 419 AA; 47766 MW; 8BCDABF94330F59B CRC64; MKEFVISEAQ TEKAVLVGLI TQTQDERKTN EYLDELAFLA ETAGAEVVKR FTQKLDTPNS VTYVGKGKLQ EIKEYLELQN ESEETEIGMV IFDDELSAKQ IRNIEGELKV KILDRTSLIL DIFAMRAQTA NAKTQVELAQ YKYMLPRLQR LWTHLERQGG GSGAGGGKGS VGLRGPGETQ LEMDRRIILN RMALLKQRLA EIDTQKSTQR KNRGRLIRVA LVGYTNVGKS TLMNLLAKSE VFAENKLFAT LDTTVRKVII ENLPFLLSDT VGFIRKLPTD LVESFKSTLD EVREADLLVH VVDISHPDFE EQIQIVDKTI ADLGAAGKPT MIIFNKIDAY TYVEKAEDDL TPKTKENITL EELMNTWMAK LNDNCIFISA KNKVNIEELR ERLYKKVKEL HVQKYPYNDF LYQSYEEEQ // ID R6YWW7_9CLOT Unreviewed; 415 AA. AC R6YWW7; DT 24-JUL-2013, integrated into UniProtKB/TrEMBL. DT 24-JUL-2013, sequence version 1. DT 12-APR-2017, entry version 24. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=BN593_00992 {ECO:0000313|EMBL:CDD38420.1}; OS Clostridium sp. CAG:299. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium; environmental samples. OX NCBI_TaxID=1262792 {ECO:0000313|EMBL:CDD38420.1, ECO:0000313|Proteomes:UP000017929}; RN [1] {ECO:0000313|EMBL:CDD38420.1, ECO:0000313|Proteomes:UP000017929} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MGS:299 {ECO:0000313|Proteomes:UP000017929}; RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., RA Sunagawa S., Plichta D., Gautier L., Le Chatelier E., Peletier E., RA Bonde I., Nielsen T., Manichanh C., Arumugam M., Batto J., RA Santos M.B.Q.D., Blom N., Borruel N., Burgdorf K.S., Boumezbeur F., RA Casellas F., Dore J., Guarner F., Hansen T., Hildebrand F., Kaas R.S., RA Kennedy S., Kristiansen K., Kultima J.R., Leonard P., Levenez F., RA Lund O., Moumen B., Le Paslier D., Pons N., Pedersen O., Prifti E., RA Qin J., Raes J., Tap J., Tims S., Ussery D.W., Yamada T., RA MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P., Wang J., RA Brunak S., Ehrlich S.D.; RT "Dependencies among metagenomic species, viruses, plasmids and units RT of genetic variation."; RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:CDD38420.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CBGZ010000043; CDD38420.1; -; Genomic_DNA. DR Proteomes; UP000017929; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000017929}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000017929}. FT DOMAIN 202 366 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 415 AA; 46439 MW; 43CE5F7BAE0BEE72 CRC64; MAELYDMREE EERVILVAVS TGDGDDTEES VDELAELVKT AGAVAADRII QNRERVHPGT YLGKGKIEEV RERVLALQAT GVVCDDELSP AQLRNLEDAL QTKVMDRTMV ILDIFASHAV TREGKIQVEL AQLRYRAARL VGLRNSLSRL GGGIGTRGPG EKKLESDRRL IHERIGQLKA ELEDVKRHRE VARQQRDRDC TVSAAIVGYT NAGKSTLLNY LTDAGILAED KLFATLDPTT RMLKLPSGQN ILLTDTVGFI RKLPHNLIEA FKSTLEEARY SDIILHVADV SNPQLDTQIH IVYETLRQLE IRDKTIVTVF NKMDKLTGDV ILRDFSSDFQ VKISAKTGEG IPDLLETLEG ILRSRRVYLN KVFSYGEAGK IQSIRKYGEL LKEEYTEAGI QVEAYVPAEI YGSLM // ID R6ZC17_9FIRM Unreviewed; 438 AA. AC R6ZC17; DT 24-JUL-2013, integrated into UniProtKB/TrEMBL. DT 24-JUL-2013, sequence version 1. DT 12-APR-2017, entry version 24. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=BN699_01517 {ECO:0000313|EMBL:CDD45948.1}; OS Firmicutes bacterium CAG:534. OC Bacteria; Firmicutes; environmental samples. OX NCBI_TaxID=1263027 {ECO:0000313|EMBL:CDD45948.1, ECO:0000313|Proteomes:UP000018220}; RN [1] {ECO:0000313|EMBL:CDD45948.1, ECO:0000313|Proteomes:UP000018220} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MGS:534 {ECO:0000313|Proteomes:UP000018220}; RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., RA Sunagawa S., Plichta D., Gautier L., Le Chatelier E., Peletier E., RA Bonde I., Nielsen T., Manichanh C., Arumugam M., Batto J., RA Santos M.B.Q.D., Blom N., Borruel N., Burgdorf K.S., Boumezbeur F., RA Casellas F., Dore J., Guarner F., Hansen T., Hildebrand F., Kaas R.S., RA Kennedy S., Kristiansen K., Kultima J.R., Leonard P., Levenez F., RA Lund O., Moumen B., Le Paslier D., Pons N., Pedersen O., Prifti E., RA Qin J., Raes J., Tap J., Tims S., Ussery D.W., Yamada T., RA MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P., Wang J., RA Brunak S., Ehrlich S.D.; RT "Dependencies among metagenomic species, viruses, plasmids and units RT of genetic variation."; RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:CDD45948.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CBHC010000033; CDD45948.1; -; Genomic_DNA. DR Proteomes; UP000018220; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000018220}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000018220}. FT DOMAIN 197 367 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 156 190 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 438 AA; 49999 MW; 16F00F30F718C660 CRC64; MEERVLLAGA DFERNPGEFE RSMEELEKLA QACNMEVAGI VTQRMGEMNK GLYVGSGKVQ EIKEAVKALE AELVIFNDTL TPSQLRNLSE ELSCAVMDRT SLILDIFETR AKTREAKLQV ETARLQYLLP RLVGMHQALT RQGGTSGSMS SRGAGEKKLE LDRRRIEHRI SELNKELKEV EREREVQRKK RLSSRLPLVA LVGYTNAGKS TIMNGLVERY VGEETKKVLE KDMLFATLDT TVRRIDTGNN HDFLLSDTVG FIHKLPHGLV KAFRSTLEEV KNADLLLQVV DRSDPYYREQ METTQKTLQE LGAEKIPMLV VYNKVDRLAG ELSYPKRMED KLYLSAKEET SLTLLVQTVL QKVYADLLEK TFLIPYDQGN LVSYLRENAQ VLCQEYEEEG TLLRVRCHLA DAEKYRQYLD TRALDHMALE GEENGKTE // ID R6ZIS3_9ACTN Unreviewed; 429 AA. AC R6ZIS3; DT 24-JUL-2013, integrated into UniProtKB/TrEMBL. DT 24-JUL-2013, sequence version 1. DT 12-APR-2017, entry version 25. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=BN642_01193 {ECO:0000313|EMBL:CDD43329.1}; OS Collinsella sp. CAG:398. OC Bacteria; Actinobacteria; Coriobacteriia; Coriobacteriales; OC Coriobacteriaceae; Collinsella; environmental samples. OX NCBI_TaxID=1262852 {ECO:0000313|EMBL:CDD43329.1, ECO:0000313|Proteomes:UP000018185}; RN [1] {ECO:0000313|EMBL:CDD43329.1, ECO:0000313|Proteomes:UP000018185} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MGS:398 {ECO:0000313|Proteomes:UP000018185}; RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., RA Sunagawa S., Plichta D., Gautier L., Le Chatelier E., Peletier E., RA Bonde I., Nielsen T., Manichanh C., Arumugam M., Batto J., RA Santos M.B.Q.D., Blom N., Borruel N., Burgdorf K.S., Boumezbeur F., RA Casellas F., Dore J., Guarner F., Hansen T., Hildebrand F., Kaas R.S., RA Kennedy S., Kristiansen K., Kultima J.R., Leonard P., Levenez F., RA Lund O., Moumen B., Le Paslier D., Pons N., Pedersen O., Prifti E., RA Qin J., Raes J., Tap J., Tims S., Ussery D.W., Yamada T., RA MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P., Wang J., RA Brunak S., Ehrlich S.D.; RT "Dependencies among metagenomic species, viruses, plasmids and units RT of genetic variation."; RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:CDD43329.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CBHB010000126; CDD43329.1; -; Genomic_DNA. DR Proteomes; UP000018185; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000018185}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000018185}. FT DOMAIN 210 375 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 429 AA; 47259 MW; 6E3776020955E3C3 CRC64; MARFTPVSTS PVPERAVLVG IEQRGSSWPV DRSLDELERL ADTAGAECVA RVMQRLERPN PRTFIGSGKV AEVCGLVSRL DADVVIFDDD LSPSQQANLE KAVGEPVKII DRTALILDIF GLHAQTREGR LQVQLAQLQY LLPRLRGMWS HLAKEQTRGG IGSRFGQGES QLEVDRRMVR NRIAAVRREL AVVERRRSVQ SKERIASPAF RVALAGYTNA GKSSLLNRLT GSTVLAQDKL FATLDPTTRA YRLPGGRSMT ITDTVGFIQK LPHGLVDAFK STLSEVREAD LILMVADASD DNLSRQLDAV HRVLEEIGAG ESRSLVVFNK IDLIDAETLL DLRRIYPDAV LVSARTGEHI DDLVERVALE AAALDKLIDV HIPYANGSLV QLIRQSGHVL EESFEETSTH LVAKVPPRIA GYLSAYYSS // ID R7A3E6_9BACE Unreviewed; 432 AA. AC R7A3E6; DT 24-JUL-2013, integrated into UniProtKB/TrEMBL. DT 24-JUL-2013, sequence version 1. DT 12-APR-2017, entry version 24. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=BN656_00194 {ECO:0000313|EMBL:CDD55328.1}; OS Bacteroides pectinophilus CAG:437. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae; OC Bacteroides; environmental samples. OX NCBI_TaxID=1263051 {ECO:0000313|EMBL:CDD55328.1, ECO:0000313|Proteomes:UP000018141}; RN [1] {ECO:0000313|EMBL:CDD55328.1, ECO:0000313|Proteomes:UP000018141} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MGS:437 {ECO:0000313|Proteomes:UP000018141}; RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., RA Sunagawa S., Plichta D., Gautier L., Le Chatelier E., Peletier E., RA Bonde I., Nielsen T., Manichanh C., Arumugam M., Batto J., RA Santos M.B.Q.D., Blom N., Borruel N., Burgdorf K.S., Boumezbeur F., RA Casellas F., Dore J., Guarner F., Hansen T., Hildebrand F., Kaas R.S., RA Kennedy S., Kristiansen K., Kultima J.R., Leonard P., Levenez F., RA Lund O., Moumen B., Le Paslier D., Pons N., Pedersen O., Prifti E., RA Qin J., Raes J., Tap J., Tims S., Ussery D.W., Yamada T., RA MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P., Wang J., RA Brunak S., Ehrlich S.D.; RT "Dependencies among metagenomic species, viruses, plasmids and units RT of genetic variation."; RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:CDD55328.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CBHH010000006; CDD55328.1; -; Genomic_DNA. DR Proteomes; UP000018141; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000018141}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000018141}. FT DOMAIN 204 371 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 432 AA; 48460 MW; B5BED414D6650812 CRC64; MAKTHDMEER EERFILVAVQ TDERDDTRQS LTELRELVKT AGAQVCDVVI QNREAVHPGT YIGKGKIEEL ACLAAQYDAD GIVCDDELSP AQLKNLEEEL NCKVLDRTLV ILDIFAARAS TSEGKIQVEM AQLKYRMSRL AGLGLGLSMS RLGGGVGTRG PGEKKIEMDR RLIRDRIAQL KSELDEVVRH REVTRQQRKK TSMPVAAIVG YTNAGKSTLL NRLTDADVLS EDKLFATLDP TTRELVLADK SRVLLTDTVG FIRKLPHHLI DAFRSTLEEA RYADIIVHVV DASNDDMERQ MEIVYDTLQE LEVGDKPVIT LFNKCDMLDM TDSSAKPRDF KADKTVYISA KTGQGLDEFE EALGDILRGS KVYIEHCYGF ADAGKIQVIR QYGQLMSEDY TADGIMVKGY IGKEYLDRAG LSSYLKKEDN EY // ID R7A621_9CLOT Unreviewed; 416 AA. AC R7A621; DT 24-JUL-2013, integrated into UniProtKB/TrEMBL. DT 24-JUL-2013, sequence version 1. DT 10-MAY-2017, entry version 25. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=BN653_01357 {ECO:0000313|EMBL:CDD56253.1}; OS Clostridium sp. CAG:43. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium; environmental samples. OX NCBI_TaxID=1262805 {ECO:0000313|EMBL:CDD56253.1, ECO:0000313|Proteomes:UP000018284}; RN [1] {ECO:0000313|EMBL:CDD56253.1, ECO:0000313|Proteomes:UP000018284} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MGS:43 {ECO:0000313|Proteomes:UP000018284}; RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., RA Sunagawa S., Plichta D., Gautier L., Le Chatelier E., Peletier E., RA Bonde I., Nielsen T., Manichanh C., Arumugam M., Batto J., RA Santos M.B.Q.D., Blom N., Borruel N., Burgdorf K.S., Boumezbeur F., RA Casellas F., Dore J., Guarner F., Hansen T., Hildebrand F., Kaas R.S., RA Kennedy S., Kristiansen K., Kultima J.R., Leonard P., Levenez F., RA Lund O., Moumen B., Le Paslier D., Pons N., Pedersen O., Prifti E., RA Qin J., Raes J., Tap J., Tims S., Ussery D.W., Yamada T., RA MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P., Wang J., RA Brunak S., Ehrlich S.D.; RT "Dependencies among metagenomic species, viruses, plasmids and units RT of genetic variation."; RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:CDD56253.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CBHG010000227; CDD56253.1; -; Genomic_DNA. DR Proteomes; UP000018284; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000018284}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000018284}. FT DOMAIN 202 366 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 416 AA; 46740 MW; F4AF4C7464668E6E CRC64; MAELFDMKEL EERVILVAVS TSDEDDTEAS LDELEELADT AGATAIGRLV QNREKIHPGT YLGSGKIGEL REMVWEMGAT GVICDDELSP AQLRNLESAL DTKVMDRTMV ILDIFAAHAT TSEGKIQVEL AQLRYRAARL VGLRSSLSRL GGGIGTRGPG EKKLEMDRRL IHERIGQLKS ELEDVKRHRE VTRKQRDRKY TLSAAIVGYT NAGKSTLLNT LTGAGILAQD KLFATLDPTT RGLKLASGQE ILLTDTVGFI RKLPHHLIEA FKSTLEEARY SDIVLHVVDA SNLQMDTQMY VVYDTLRQLE IGDKTVVTVF NKMDQVEQPE TLKDLHSDYQ VQISAKTGAG LDELKDILEM ILRNRKIYLE KVFSYQEAGR IQTIRKYGQL LKEEYREDGI YVEAYVPTEL YAGLMR // ID R7A8B3_9BACE Unreviewed; 418 AA. AC R7A8B3; DT 24-JUL-2013, integrated into UniProtKB/TrEMBL. DT 24-JUL-2013, sequence version 1. DT 07-JUN-2017, entry version 25. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=BN800_00270 {ECO:0000313|EMBL:CDD51759.1}; OS Bacteroides sp. CAG:875. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae; OC Bacteroides; environmental samples. OX NCBI_TaxID=1262752 {ECO:0000313|EMBL:CDD51759.1, ECO:0000313|Proteomes:UP000018287}; RN [1] {ECO:0000313|EMBL:CDD51759.1, ECO:0000313|Proteomes:UP000018287} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MGS:875 {ECO:0000313|Proteomes:UP000018287}; RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., RA Sunagawa S., Plichta D., Gautier L., Le Chatelier E., Peletier E., RA Bonde I., Nielsen T., Manichanh C., Arumugam M., Batto J., RA Santos M.B.Q.D., Blom N., Borruel N., Burgdorf K.S., Boumezbeur F., RA Casellas F., Dore J., Guarner F., Hansen T., Hildebrand F., Kaas R.S., RA Kennedy S., Kristiansen K., Kultima J.R., Leonard P., Levenez F., RA Lund O., Moumen B., Le Paslier D., Pons N., Pedersen O., Prifti E., RA Qin J., Raes J., Tap J., Tims S., Ussery D.W., Yamada T., RA MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P., Wang J., RA Brunak S., Ehrlich S.D.; RT "Dependencies among metagenomic species, viruses, plasmids and units RT of genetic variation."; RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:CDD51759.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CBHD010000190; CDD51759.1; -; Genomic_DNA. DR Proteomes; UP000018287; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000018287}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}. FT DOMAIN 217 401 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 418 AA; 47553 MW; A61B7B4CDCE51802 CRC64; MKEFVISDAQ TEKAALVGLI TQTQNERKTN EYLDELAFLA ETAGAEVVKR FTQKLDTPNS VTYVGKGKLQ EIKEYLAAQN ESEETEIGMV IFDDELSAKQ IRNIENELKV KILDRTSLIL DIFAMRAQTA NAKTQVELAQ YKYMLPRLQR LWTHLERQGG GSGAGGGKGS VGLRGPGETQ LEMDRRIILN RMALLKQRLA EIDTQKSTQR KNRGRLIRVA LVGYTNVGKS TLMNLLAKSD VFAENKLFAT LDTTVRKVII ENLPFLLSDT VGFIRKLPTD LVDSFKSTLD EVREADLLVH VVDISHPDFE EQIQVVEKTI ADLGAGGKPS MIVFNKVDAY TYVEKAEDDL TPKTKENITL EELMHTWMAK LNDNCIFISA REKTNIEQFR ELLYKKVREL HVQKYPYNDF LYQTYDEE // ID R7B736_9ACTN Unreviewed; 432 AA. AC R7B736; DT 24-JUL-2013, integrated into UniProtKB/TrEMBL. DT 24-JUL-2013, sequence version 1. DT 10-MAY-2017, entry version 24. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=BN592_01295 {ECO:0000313|EMBL:CDD60322.1}; OS Eggerthella sp. CAG:298. OC Bacteria; Actinobacteria; Coriobacteriia; Eggerthellales; OC Eggerthellaceae; Eggerthella; environmental samples. OX NCBI_TaxID=1262876 {ECO:0000313|EMBL:CDD60322.1, ECO:0000313|Proteomes:UP000018266}; RN [1] {ECO:0000313|EMBL:CDD60322.1, ECO:0000313|Proteomes:UP000018266} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MGS:298 {ECO:0000313|Proteomes:UP000018266}; RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., RA Sunagawa S., Plichta D., Gautier L., Le Chatelier E., Peletier E., RA Bonde I., Nielsen T., Manichanh C., Arumugam M., Batto J., RA Santos M.B.Q.D., Blom N., Borruel N., Burgdorf K.S., Boumezbeur F., RA Casellas F., Dore J., Guarner F., Hansen T., Hildebrand F., Kaas R.S., RA Kennedy S., Kristiansen K., Kultima J.R., Leonard P., Levenez F., RA Lund O., Moumen B., Le Paslier D., Pons N., Pedersen O., Prifti E., RA Qin J., Raes J., Tap J., Tims S., Ussery D.W., Yamada T., RA MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P., Wang J., RA Brunak S., Ehrlich S.D.; RT "Dependencies among metagenomic species, viruses, plasmids and units RT of genetic variation."; RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:CDD60322.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CBHI010000077; CDD60322.1; -; Genomic_DNA. DR Proteomes; UP000018266; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000018266}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000018266}. FT DOMAIN 211 376 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 432 AA; 48262 MW; 0529EECCB09DA234 CRC64; MAKLHVKKIP QDYAERAVLV GVKRPNQQWP TESSLAELER LAQTAGAEVV ATTFQRLESP NPRTFIGSGK VDEVAQLCRS YAADLVIFDD ELTPSQQSNL EKQVGKDIKI IDRTALILDI FALHATSREG RLQVRLAQNE YLLPRLRGMW AHLASNRMGG GVGSRFGEGE SQLEVDRRMV RKRITSIKRE LADISKTRTL QRKQRYHSGI FKVALAGYTN AGKSSLLNTI TDAEVLSYDK LFATLDSTTR KLVIPDGREL TLTDTVGFIQ KLPTTLVEAF KSTLDEISGA DLILHVVDAS DANFKEQIDT VNEVLAQIDA DEISRIEVFN KIDLLDEEQL SAYRMRFPHA LFTSTLTGEG IDELIKRIGL AAEAHQVLME VLIPFTKGEL VSLAHKRCSI LAEEYTEEGT RMSLRVSPEL SAQFSSYRIG EE // ID R7BCU4_9FIRM Unreviewed; 419 AA. AC R7BCU4; DT 24-JUL-2013, integrated into UniProtKB/TrEMBL. DT 24-JUL-2013, sequence version 1. DT 12-APR-2017, entry version 24. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=BN803_01181 {ECO:0000313|EMBL:CDD63481.1}; OS Firmicutes bacterium CAG:882. OC Bacteria; Firmicutes; environmental samples. OX NCBI_TaxID=1262991 {ECO:0000313|EMBL:CDD63481.1, ECO:0000313|Proteomes:UP000017928}; RN [1] {ECO:0000313|EMBL:CDD63481.1, ECO:0000313|Proteomes:UP000017928} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MGS:882 {ECO:0000313|Proteomes:UP000017928}; RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., RA Sunagawa S., Plichta D., Gautier L., Le Chatelier E., Peletier E., RA Bonde I., Nielsen T., Manichanh C., Arumugam M., Batto J., RA Santos M.B.Q.D., Blom N., Borruel N., Burgdorf K.S., Boumezbeur F., RA Casellas F., Dore J., Guarner F., Hansen T., Hildebrand F., Kaas R.S., RA Kennedy S., Kristiansen K., Kultima J.R., Leonard P., Levenez F., RA Lund O., Moumen B., Le Paslier D., Pons N., Pedersen O., Prifti E., RA Qin J., Raes J., Tap J., Tims S., Ussery D.W., Yamada T., RA MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P., Wang J., RA Brunak S., Ehrlich S.D.; RT "Dependencies among metagenomic species, viruses, plasmids and units RT of genetic variation."; RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:CDD63481.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CBHL010000012; CDD63481.1; -; Genomic_DNA. DR Proteomes; UP000017928; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000017928}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000017928}. FT DOMAIN 206 370 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 419 AA; 46308 MW; 7D939A1BB8488254 CRC64; MAELIDTAKD VEKVILIGVC TSENDDTEES LDELEELVKT AGAVTLEKVI QNRESIHPGT YIGTGKIEEV RELAERIGAT GVVCDDELSP AQLRNLESEL MMKVMDRTMV ILDIFAKRAV TSEGKIQVEA AQLKYSLARL VGLRSSLSRV GGNMAGSIGT RGPGEKKLEL DRRLIKDRIV QLGRELEDIE SHRSLARTQR MRSSVPVAAI VGYTNAGKST LLNKLTQAGV LAEDKLFATL DPTTRGIELE SGQNVLMTDT VGFIRKLPHH LIEAFKSTLE EAKYADIIVH VVDSSSPQMD TQMHVVYSTL ADLGAGDKPV ITLFNKRDKC ECDELPKDFK AERVIYGSAK TGEGLDELKS AIEEILRAQK IYIETVYPYD MAGKIQLIRK FGQLLSEEYT ESGIAVKAYV PSEIYEKVK // ID R7BNV8_9ACTN Unreviewed; 437 AA. AC R7BNV8; DT 24-JUL-2013, integrated into UniProtKB/TrEMBL. DT 24-JUL-2013, sequence version 1. DT 10-MAY-2017, entry version 24. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=BN629_01134 {ECO:0000313|EMBL:CDD67479.1}; OS Eggerthella sp. CAG:368. OC Bacteria; Actinobacteria; Coriobacteriia; Eggerthellales; OC Eggerthellaceae; Eggerthella; environmental samples. OX NCBI_TaxID=1262877 {ECO:0000313|EMBL:CDD67479.1, ECO:0000313|Proteomes:UP000018088}; RN [1] {ECO:0000313|EMBL:CDD67479.1, ECO:0000313|Proteomes:UP000018088} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MGS:368 {ECO:0000313|Proteomes:UP000018088}; RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., RA Sunagawa S., Plichta D., Gautier L., Le Chatelier E., Peletier E., RA Bonde I., Nielsen T., Manichanh C., Arumugam M., Batto J., RA Santos M.B.Q.D., Blom N., Borruel N., Burgdorf K.S., Boumezbeur F., RA Casellas F., Dore J., Guarner F., Hansen T., Hildebrand F., Kaas R.S., RA Kennedy S., Kristiansen K., Kultima J.R., Leonard P., Levenez F., RA Lund O., Moumen B., Le Paslier D., Pons N., Pedersen O., Prifti E., RA Qin J., Raes J., Tap J., Tims S., Ussery D.W., Yamada T., RA MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P., Wang J., RA Brunak S., Ehrlich S.D.; RT "Dependencies among metagenomic species, viruses, plasmids and units RT of genetic variation."; RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:CDD67479.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CBHM010000053; CDD67479.1; -; Genomic_DNA. DR Proteomes; UP000018088; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000018088}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000018088}. FT DOMAIN 217 382 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 437 AA; 48649 MW; E355BB17D0077614 CRC64; MTDQERVIQH GPKTVFESPR ERAILVGVER PNAEWSLTSS LAELERLADT AGADTVAATT QKLEAPNPRT FVGSGKAEEI ASLCRSYAAD IVIFDDELSP SQQSNLEKMV GKDVKVIDRT ALILDIFALH ASSKEGRLQV KLAQNQYLLP RLRGMWAHLA SNRMGGGVGS RFGEGESQLE VDRRLVRKRI TSIKRELEEV SRYRSLQREK RYSSGIFKVA LAGYTNAGKS SLLNTLTKSE VLSYDKLFAT LDSTTRQLQL SSGRKVTLTD TVGFIQKLPT TLVEAFKSTL DEINGSDLIL QVVDSTDENF IKQIDTVNEI LEQIGADTIS RVEVFNKIDA LQKDELEALR KRFPYAVFTS TITKEGISTL IQRIGSVASA QEEQIEVLVP FNRGDLVSFA HQNCHILHEE YTEKGTRISL RVAPVFKAKF GETIIEP // ID R7BZ44_9FIRM Unreviewed; 412 AA. AC R7BZ44; DT 24-JUL-2013, integrated into UniProtKB/TrEMBL. DT 24-JUL-2013, sequence version 1. DT 12-APR-2017, entry version 24. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=BN579_01541 {ECO:0000313|EMBL:CDD71154.1}; OS Firmicutes bacterium CAG:270. OC Bacteria; Firmicutes; environmental samples. OX NCBI_TaxID=1263014 {ECO:0000313|EMBL:CDD71154.1, ECO:0000313|Proteomes:UP000018350}; RN [1] {ECO:0000313|EMBL:CDD71154.1, ECO:0000313|Proteomes:UP000018350} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MGS:270 {ECO:0000313|Proteomes:UP000018350}; RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., RA Sunagawa S., Plichta D., Gautier L., Le Chatelier E., Peletier E., RA Bonde I., Nielsen T., Manichanh C., Arumugam M., Batto J., RA Santos M.B.Q.D., Blom N., Borruel N., Burgdorf K.S., Boumezbeur F., RA Casellas F., Dore J., Guarner F., Hansen T., Hildebrand F., Kaas R.S., RA Kennedy S., Kristiansen K., Kultima J.R., Leonard P., Levenez F., RA Lund O., Moumen B., Le Paslier D., Pons N., Pedersen O., Prifti E., RA Qin J., Raes J., Tap J., Tims S., Ussery D.W., Yamada T., RA MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P., Wang J., RA Brunak S., Ehrlich S.D.; RT "Dependencies among metagenomic species, viruses, plasmids and units RT of genetic variation."; RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:CDD71154.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CBHP010000094; CDD71154.1; -; Genomic_DNA. DR Proteomes; UP000018350; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000018350}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}. FT DOMAIN 200 364 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 15 42 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 412 AA; 46086 MW; 9C4EEDB5C934266F CRC64; MEEIKKEIIE KVILVAVADQ DVREAEESLD ELEELVKTAG AVVAARVIQV REAPHPGTYI GKGKIDEVKA LLYGTDAIGI VCDDELSPAQ MGNLSDVLDT KVMDRTLIIL DIFAKRAFTR EGKIQVELAQ LKYRASKLTG QGKALSRLGG GIGTRGPGEK KLEMDRRLIR TRISRLKAEL RDVVKHREVQ RKQRQKNHLP VVCIVGYTNA GKSTLLNHFT NAGVYEEDQL FATLDPTTKS LDLSGGQTIL MTDTVGFIRK LPHHLVEAFK STLEEAKYSD LILHVVDASN PQKEKQMEAV YETLKQLGAN ESPIVTAFNK IDLLNGDEIL KDQNAEAVVR ISGKTGEGTD QLLENIEKIL QKQKLYLEKL YDYQDAGKIQ QIRTHGQLLK EEYREDGIYV EAYIPKEILG NI // ID R7BZ72_9BURK Unreviewed; 403 AA. AC R7BZ72; DT 24-JUL-2013, integrated into UniProtKB/TrEMBL. DT 24-JUL-2013, sequence version 1. DT 12-APR-2017, entry version 23. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=BN641_01439 {ECO:0000313|EMBL:CDD70777.1}; OS Sutterella sp. CAG:397. OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Sutterellaceae; Sutterella; environmental samples. OX NCBI_TaxID=1262976 {ECO:0000313|EMBL:CDD70777.1, ECO:0000313|Proteomes:UP000018105}; RN [1] {ECO:0000313|EMBL:CDD70777.1, ECO:0000313|Proteomes:UP000018105} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MGS:397 {ECO:0000313|Proteomes:UP000018105}; RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., RA Sunagawa S., Plichta D., Gautier L., Le Chatelier E., Peletier E., RA Bonde I., Nielsen T., Manichanh C., Arumugam M., Batto J., RA Santos M.B.Q.D., Blom N., Borruel N., Burgdorf K.S., Boumezbeur F., RA Casellas F., Dore J., Guarner F., Hansen T., Hildebrand F., Kaas R.S., RA Kennedy S., Kristiansen K., Kultima J.R., Leonard P., Levenez F., RA Lund O., Moumen B., Le Paslier D., Pons N., Pedersen O., Prifti E., RA Qin J., Raes J., Tap J., Tims S., Ussery D.W., Yamada T., RA MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P., Wang J., RA Brunak S., Ehrlich S.D.; RT "Dependencies among metagenomic species, viruses, plasmids and units RT of genetic variation."; RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:CDD70777.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CBHO010000096; CDD70777.1; -; Genomic_DNA. DR Proteomes; UP000018105; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000018105}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000018105}. FT DOMAIN 205 369 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 164 198 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 403 AA; 44743 MW; FABE99D6C0FA7CC4 CRC64; MTKFRYESAR EAEPTRAFLV TAAIGRTVWA DAGDELAELV RSDGLVPAGY LAARRDKPDA ATFLGSGKIE EIKNLAQAAK ASIVVFDAAL SAAQERNIAQ ACGIAVMDRT ELILEIFRRR AKSKEGRLQV ELARLEHLAT RLVRGWTHLE RQRGGLGKTG GPGEKQIELD RRLLSNRVKQ LRDQLKKLQK QRDTQRKSRS EGETMTVSLV GYTNAGKSTL FNRLTRAETY AADQLFATLD TTARRCWLEG EDWIVASDTV GFIRGLPHQL VNAFKSTLDE TVHADLLLHV VDSSSAVKDE QIASVNEVLR EIEADTVPVI TVFNKIDRSG MTPGIVRRDD GTVKSVTVSA LTGEGIDDLR HAVAEFKHVW AEENKSLPRE PEDWEREAAE ILDGNDNFSD PKN // ID R7C7I1_9CLOT Unreviewed; 412 AA. AC R7C7I1; DT 24-JUL-2013, integrated into UniProtKB/TrEMBL. DT 24-JUL-2013, sequence version 1. DT 12-APR-2017, entry version 23. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=BN737_00417 {ECO:0000313|EMBL:CDD74134.1}; OS Clostridium sp. CAG:62. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium; environmental samples. OX NCBI_TaxID=1262828 {ECO:0000313|EMBL:CDD74134.1, ECO:0000313|Proteomes:UP000018137}; RN [1] {ECO:0000313|EMBL:CDD74134.1, ECO:0000313|Proteomes:UP000018137} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MGS:62 {ECO:0000313|Proteomes:UP000018137}; RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., RA Sunagawa S., Plichta D., Gautier L., Le Chatelier E., Peletier E., RA Bonde I., Nielsen T., Manichanh C., Arumugam M., Batto J., RA Santos M.B.Q.D., Blom N., Borruel N., Burgdorf K.S., Boumezbeur F., RA Casellas F., Dore J., Guarner F., Hansen T., Hildebrand F., Kaas R.S., RA Kennedy S., Kristiansen K., Kultima J.R., Leonard P., Levenez F., RA Lund O., Moumen B., Le Paslier D., Pons N., Pedersen O., Prifti E., RA Qin J., Raes J., Tap J., Tims S., Ussery D.W., Yamada T., RA MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P., Wang J., RA Brunak S., Ehrlich S.D.; RT "Dependencies among metagenomic species, viruses, plasmids and units RT of genetic variation."; RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:CDD74134.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CBHQ010000076; CDD74134.1; -; Genomic_DNA. DR Proteomes; UP000018137; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000018137}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000018137}. FT DOMAIN 202 367 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 412 AA; 46335 MW; 362FF4F735FC5305 CRC64; MAKTYETEQV QEKFLLAAVD LEDGTDVSYS LDELAELTET AGGIVVGRLI QKRESVHPGT YVGKGKIEEL RELIMQTDAD GIVCDDELTP AQLTNLQEEL QVKVLDRTVM ILDIFAAHAR TSEGKLQVEL AQLRYRSSRL TGLGKSLSRL GGGIGTRGPG EKKLEMDRRL IKERISMLNR QLKEVVKNRE VQRHKRTQNP TKTVAIVGYT NAGKSTLLNT LTKAAVLEED KLFATLDPTT RVLEKEDGQK ILFTDTVGFI SKLPHSLIRA FRSTLEEAKY ADMILHVVDV SNPKYDLQME VVYDTLRELN IGDKKVITAF NKIDCLEYKP DGLKDKNSEA SLMISAKQKI GLDKLVEKIE EVLDEGMVKI EKVFAYDEAG KIQAIREFGR LEQEEYREDG IFVKAVIPPH LL // ID R7CD63_9FIRM Unreviewed; 411 AA. AC R7CD63; DT 24-JUL-2013, integrated into UniProtKB/TrEMBL. DT 24-JUL-2013, sequence version 1. DT 12-APR-2017, entry version 22. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=BN806_01028 {ECO:0000313|EMBL:CDD76046.1}; OS Ruminococcus sp. CAG:9. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Ruminococcaceae; OC Ruminococcus; environmental samples. OX NCBI_TaxID=1262967 {ECO:0000313|EMBL:CDD76046.1, ECO:0000313|Proteomes:UP000018027}; RN [1] {ECO:0000313|EMBL:CDD76046.1, ECO:0000313|Proteomes:UP000018027} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MGS:9 {ECO:0000313|Proteomes:UP000018027}; RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., RA Sunagawa S., Plichta D., Gautier L., Le Chatelier E., Peletier E., RA Bonde I., Nielsen T., Manichanh C., Arumugam M., Batto J., RA Santos M.B.Q.D., Blom N., Borruel N., Burgdorf K.S., Boumezbeur F., RA Casellas F., Dore J., Guarner F., Hansen T., Hildebrand F., Kaas R.S., RA Kennedy S., Kristiansen K., Kultima J.R., Leonard P., Levenez F., RA Lund O., Moumen B., Le Paslier D., Pons N., Pedersen O., Prifti E., RA Qin J., Raes J., Tap J., Tims S., Ussery D.W., Yamada T., RA MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P., Wang J., RA Brunak S., Ehrlich S.D.; RT "Dependencies among metagenomic species, viruses, plasmids and units RT of genetic variation."; RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:CDD76046.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CBHS010000008; CDD76046.1; -; Genomic_DNA. DR Proteomes; UP000018027; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000018027}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000018027}. FT DOMAIN 199 362 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 411 AA; 45954 MW; 47A086DBD0023A18 CRC64; MEEFGKLEER VVLVGVQTDD HDNVEESLDE LKELASTAGA VTVGRIIQNR ESVHPGTYIG KGKIEEVRAL VYAMDATGII CDDELSPAQL NNLERELDCK VMDRTLLILD IFAARAITSE GKIQVELAQL RYRSARLVGL RESLSRLGGG IGTRGPGEKK LETDRRLIRT RISALKQELS QVEKHRELIR SSRARGNMRT AAIVGYTNAG KSTLLNTLTG SEVLSEDKLF ATLDPTTRLL NLKDGQQILL TDTVGFIHKL PHHLVEAFKS TLEEAKYVDY IIHVVDSSNQ QAEMQMHVVY ETLKELGVMG KKIITLFNKQ DAPGACVLRD FKSDYTLKVS AKTGEGLADL NDLLKKLLAE EQIYVERLFP YQEAGKIQLI REYGQLISEE YTEEGIAVKA RVPKEIYARV V // ID R7CXF1_9BACE Unreviewed; 421 AA. AC R7CXF1; DT 24-JUL-2013, integrated into UniProtKB/TrEMBL. DT 24-JUL-2013, sequence version 1. DT 12-APR-2017, entry version 24. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=BN666_02342 {ECO:0000313|EMBL:CDD83039.1}; OS Bacteroides sp. CAG:462. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae; OC Bacteroides; environmental samples. OX NCBI_TaxID=1262740 {ECO:0000313|EMBL:CDD83039.1, ECO:0000313|Proteomes:UP000018063}; RN [1] {ECO:0000313|EMBL:CDD83039.1, ECO:0000313|Proteomes:UP000018063} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MGS:462 {ECO:0000313|Proteomes:UP000018063}; RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., RA Sunagawa S., Plichta D., Gautier L., Le Chatelier E., Peletier E., RA Bonde I., Nielsen T., Manichanh C., Arumugam M., Batto J., RA Santos M.B.Q.D., Blom N., Borruel N., Burgdorf K.S., Boumezbeur F., RA Casellas F., Dore J., Guarner F., Hansen T., Hildebrand F., Kaas R.S., RA Kennedy S., Kristiansen K., Kultima J.R., Leonard P., Levenez F., RA Lund O., Moumen B., Le Paslier D., Pons N., Pedersen O., Prifti E., RA Qin J., Raes J., Tap J., Tims S., Ussery D.W., Yamada T., RA MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P., Wang J., RA Brunak S., Ehrlich S.D.; RT "Dependencies among metagenomic species, viruses, plasmids and units RT of genetic variation."; RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:CDD83039.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CBHU010000148; CDD83039.1; -; Genomic_DNA. DR Proteomes; UP000018063; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000018063}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000018063}. FT DOMAIN 216 400 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 421 AA; 48150 MW; 03D26D7FE6EC1FA8 CRC64; MKEFVISQAQ TEKAVLVGLV TRLQDERKTN EYLDELEFLA DTAGAEVVKR FTQKLDMPNS VTYIGKGKLE EIRAYLESCE EDPETEIGMV IFDDELSAKQ IRNIEKELKV KILDRTSLIL DIFAMRAQTA SAKTQVELAQ YKYMLPRLQR LWTHLERQGG GSGSGKGGSV GLRGPGETQL EMDRRIILNR MSLLKQQLAE IDRQKSTQRK NRGRLIRVAL VGYTNVGKST LMNLLAKSEV FAENKLFATL DTTVRKVIID NLPFLLSDTV GFIRKLPTDL VDSFKSTLDE VREADLLIHV VDISHPDFEE QITVVDKTLA DLGCADKPTI LVFNKIDAYT YVEKDADDLT PRTKENITLE ELMQTWMAKM HDNCIFISAR QKTNIDELKA MFYKKVKELH VQKYPYNDFL YQTYEEDGNP E // ID R7D8V3_9ACTN Unreviewed; 445 AA. AC R7D8V3; DT 24-JUL-2013, integrated into UniProtKB/TrEMBL. DT 24-JUL-2013, sequence version 1. DT 10-MAY-2017, entry version 22. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=BN589_01276 {ECO:0000313|EMBL:CDD86795.1}; OS Collinsella sp. CAG:289. OC Bacteria; Actinobacteria; Coriobacteriia; Coriobacteriales; OC Coriobacteriaceae; Collinsella; environmental samples. OX NCBI_TaxID=1262851 {ECO:0000313|EMBL:CDD86795.1, ECO:0000313|Proteomes:UP000017952}; RN [1] {ECO:0000313|EMBL:CDD86795.1, ECO:0000313|Proteomes:UP000017952} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MGS:289 {ECO:0000313|Proteomes:UP000017952}; RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., RA Sunagawa S., Plichta D., Gautier L., Le Chatelier E., Peletier E., RA Bonde I., Nielsen T., Manichanh C., Arumugam M., Batto J., RA Santos M.B.Q.D., Blom N., Borruel N., Burgdorf K.S., Boumezbeur F., RA Casellas F., Dore J., Guarner F., Hansen T., Hildebrand F., Kaas R.S., RA Kennedy S., Kristiansen K., Kultima J.R., Leonard P., Levenez F., RA Lund O., Moumen B., Le Paslier D., Pons N., Pedersen O., Prifti E., RA Qin J., Raes J., Tap J., Tims S., Ussery D.W., Yamada T., RA MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P., Wang J., RA Brunak S., Ehrlich S.D.; RT "Dependencies among metagenomic species, viruses, plasmids and units RT of genetic variation."; RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:CDD86795.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CBHV010000122; CDD86795.1; -; Genomic_DNA. DR Proteomes; UP000017952; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000017952}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000017952}. FT DOMAIN 210 321 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 169 203 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 445 AA; 49185 MW; 06937C16CDF3CAFD CRC64; MSRFSFLSTE PEPERVLLVG VDFRNGAWPV DRSLDELERL AHTAGALTVG RVVQRLDKPI PKSFIGSGKV EEVRRLVAAH DVNTVIFDDD LTPAQQSHLE KTIGEPTKII DRTALILDIF GLHAKTREGR IQVQLAQLQY LLPRLRGMWS HLAKEQTRGG IGSRFGQGES QLEVDRRLIR NKIASLRREL NGLEKRRSVQ TKSRKESTAF RVALAGYTNA GKSTLLNALT DAGVLSEDKL FATLDPTTRS YSLPGGRVVT ITDTVGFIQK LPHGLVEAFK STLAEVLEAD LILKIVDYSD EDADLHLEAV NRVLDEIGAG EQLSVTVNNK CDRFEASYVH ALESRYPDQV FCSAYTGYGI DSLIDTLALR ASASDQLLTV MLPYANASLR AQIHEQGVIL NEEFIPEGML ITAKVPSKLA GLLRQYEQRP AGKAECESLP LATED // ID R7DD78_9FIRM Unreviewed; 418 AA. AC R7DD78; DT 24-JUL-2013, integrated into UniProtKB/TrEMBL. DT 24-JUL-2013, sequence version 1. DT 12-APR-2017, entry version 24. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=BN639_01803 {ECO:0000313|EMBL:CDD87372.1}; OS Ruminococcus obeum CAG:39. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Ruminococcaceae; OC Ruminococcus; environmental samples. OX NCBI_TaxID=1263107 {ECO:0000313|EMBL:CDD87372.1, ECO:0000313|Proteomes:UP000018059}; RN [1] {ECO:0000313|EMBL:CDD87372.1, ECO:0000313|Proteomes:UP000018059} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MGS:39 {ECO:0000313|Proteomes:UP000018059}; RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., RA Sunagawa S., Plichta D., Gautier L., Le Chatelier E., Peletier E., RA Bonde I., Nielsen T., Manichanh C., Arumugam M., Batto J., RA Santos M.B.Q.D., Blom N., Borruel N., Burgdorf K.S., Boumezbeur F., RA Casellas F., Dore J., Guarner F., Hansen T., Hildebrand F., Kaas R.S., RA Kennedy S., Kristiansen K., Kultima J.R., Leonard P., Levenez F., RA Lund O., Moumen B., Le Paslier D., Pons N., Pedersen O., Prifti E., RA Qin J., Raes J., Tap J., Tims S., Ussery D.W., Yamada T., RA MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P., Wang J., RA Brunak S., Ehrlich S.D.; RT "Dependencies among metagenomic species, viruses, plasmids and units RT of genetic variation."; RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:CDD87372.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CBHW010000207; CDD87372.1; -; Genomic_DNA. DR Proteomes; UP000018059; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000018059}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000018059}. FT DOMAIN 201 364 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 418 AA; 46393 MW; DE4C7DEB306A4DA1 CRC64; MQFYDFKEIE ERVILIGVQT EQDEDVAASL DELEELAATA GAVTVGKVIQ NREAVHPGTY IGKGKIEEVA ALLAAYDANG VICDDELSPA QMNNLERELG CKVMDRTLLI LDIFAGRATT SEGKIQVELA QLRYRSARLV GLRESLSRLG GGIGTRGPGE KKLETDRRLI RTRISALKAE LAQVEKHREL IRGKRTRGNL KTAAIVGYTN AGKSTLLNTL TGAGILAEDK LFATLDPTTR VLELKDGQQI LLTDTVGFIR KLPHHLVEAF KSTLEEAKYA DYIIHVVDAS NPQAELQMHT VYETLRELGA TGKKIITLLN KQDQVQGEAL RDFRADYTVK CSARTGEGLE ELKDVLAKLL AESQIYLEEL YTYKEAGKIQ IIREYGSLLS EEYREDGIFV KARVPAEIFV SVMPKSRK // ID R7DJU9_9BACT Unreviewed; 407 AA. AC R7DJU9; DT 24-JUL-2013, integrated into UniProtKB/TrEMBL. DT 24-JUL-2013, sequence version 1. DT 30-AUG-2017, entry version 25. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=BN686_00876 {ECO:0000313|EMBL:CDD90854.1}; OS Tannerella sp. CAG:51. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Tannerellaceae; OC Tannerella; environmental samples. OX NCBI_TaxID=1262979 {ECO:0000313|EMBL:CDD90854.1, ECO:0000313|Proteomes:UP000018150}; RN [1] {ECO:0000313|EMBL:CDD90854.1, ECO:0000313|Proteomes:UP000018150} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MGS:51 {ECO:0000313|Proteomes:UP000018150}; RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., RA Sunagawa S., Plichta D., Gautier L., Le Chatelier E., Peletier E., RA Bonde I., Nielsen T., Manichanh C., Arumugam M., Batto J., RA Santos M.B.Q.D., Blom N., Borruel N., Burgdorf K.S., Boumezbeur F., RA Casellas F., Dore J., Guarner F., Hansen T., Hildebrand F., Kaas R.S., RA Kennedy S., Kristiansen K., Kultima J.R., Leonard P., Levenez F., RA Lund O., Moumen B., Le Paslier D., Pons N., Pedersen O., Prifti E., RA Qin J., Raes J., Tap J., Tims S., Ussery D.W., Yamada T., RA MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P., Wang J., RA Brunak S., Ehrlich S.D.; RT "Dependencies among metagenomic species, viruses, plasmids and units RT of genetic variation."; RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:CDD90854.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CBHX010000230; CDD90854.1; -; Genomic_DNA. DR Proteomes; UP000018150; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000018150}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000018150}. FT DOMAIN 202 387 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 170 197 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 407 AA; 47141 MW; 311F9127AD87F525 CRC64; MKEFILTKQE SERTILVGII TQTQNETKAN EYLDELAFLA ETAGAEPVKK FLQRLEYPNP VTFVGAGKLQ EIKDYVEENE IGLVIFDDDL SPKQLKNIEK ELQVKILDRT SLILDIFAKR AQTANAKSQV ELAQYQYLLP RLTRLWTHLE RQRGGIGMRG PGETQIETDR RIILDKISRL KAELKQIDKQ KEMQRKNRGK MVRVALVGYT NVGKSTLMNL LSKSEVFAEN KLFATLDTTV RKVIIDNLPF LLTDTVGFIR KLPTHLVESF KSTLDEVRDA DLLVHVVDIS HPSFEEQIEI VNQTLHEVCN SSDKPMIIVF NKIDAFSYVE KDPDDLSPKT KKNISLDELK ETWMARMNEN CIFISAKEKN NIEELKKLLY ERVKEIHVTR FPYNDFLFQK YDEEENI // ID R7E7J8_9BACE Unreviewed; 418 AA. AC R7E7J8; DT 24-JUL-2013, integrated into UniProtKB/TrEMBL. DT 24-JUL-2013, sequence version 1. DT 12-APR-2017, entry version 25. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=BN604_00427 {ECO:0000313|EMBL:CDD98271.1}; OS Bacteroides intestinalis CAG:315. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae; OC Bacteroides; environmental samples. OX NCBI_TaxID=1263048 {ECO:0000313|EMBL:CDD98271.1, ECO:0000313|Proteomes:UP000018219}; RN [1] {ECO:0000313|EMBL:CDD98271.1, ECO:0000313|Proteomes:UP000018219} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MGS:315 {ECO:0000313|Proteomes:UP000018219}; RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., RA Sunagawa S., Plichta D., Gautier L., Le Chatelier E., Peletier E., RA Bonde I., Nielsen T., Manichanh C., Arumugam M., Batto J., RA Santos M.B.Q.D., Blom N., Borruel N., Burgdorf K.S., Boumezbeur F., RA Casellas F., Dore J., Guarner F., Hansen T., Hildebrand F., Kaas R.S., RA Kennedy S., Kristiansen K., Kultima J.R., Leonard P., Levenez F., RA Lund O., Moumen B., Le Paslier D., Pons N., Pedersen O., Prifti E., RA Qin J., Raes J., Tap J., Tims S., Ussery D.W., Yamada T., RA MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P., Wang J., RA Brunak S., Ehrlich S.D.; RT "Dependencies among metagenomic species, viruses, plasmids and units RT of genetic variation."; RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:CDD98271.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CBHY010000483; CDD98271.1; -; Genomic_DNA. DR Proteomes; UP000018219; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000018219}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000018219}. FT DOMAIN 216 400 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 418 AA; 47724 MW; 88B9ED747237146F CRC64; MKEFVISEVQ AETAVLVGLI TKMQDERKTN EYLDELEFLA ETAGAEVVKR FTQKLDQAHS VTYVGKGKLE EIKEYIRSEE EAEREIGMVI FDDELSAKQI RNIEAELKIK ILDRTSLILD IFAMRAQTAN AKTQVELAQY KYMLPRLQRL WTHLERQGGG SGAGGGKGSV GLRGPGETQL EMDRRIILNR MSLLKERLAE IDKQKSTQRK NRGRMIRAAL VGYTNVGKST LMNLLAKSEV FAENKLFATL DTTVRKVIID NLPFLLSDTV GFIRKLPTDL VDSFKSTLDE VREADLLLHI VDISHPDFEE QIEVVNKTLA DIGASGKPII LVFNKIDAYT YVEKAADDLT PRTKENLTLE ELMKTWMAKM EDNCLFISAR EKINLEELKS VVYARVKELH VQKYPYNDFL YQTYEEEL // ID R7EII1_9BACE Unreviewed; 418 AA. AC R7EII1; DT 24-JUL-2013, integrated into UniProtKB/TrEMBL. DT 24-JUL-2013, sequence version 1. DT 12-APR-2017, entry version 23. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=BN594_03205 {ECO:0000313|EMBL:CDE02490.1}; OS Bacteroides uniformis CAG:3. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae; OC Bacteroides; environmental samples. OX NCBI_TaxID=1263055 {ECO:0000313|EMBL:CDE02490.1, ECO:0000313|Proteomes:UP000018282}; RN [1] {ECO:0000313|EMBL:CDE02490.1, ECO:0000313|Proteomes:UP000018282} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MGS:3 {ECO:0000313|Proteomes:UP000018282}; RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., RA Sunagawa S., Plichta D., Gautier L., Le Chatelier E., Peletier E., RA Bonde I., Nielsen T., Manichanh C., Arumugam M., Batto J., RA Santos M.B.Q.D., Blom N., Borruel N., Burgdorf K.S., Boumezbeur F., RA Casellas F., Dore J., Guarner F., Hansen T., Hildebrand F., Kaas R.S., RA Kennedy S., Kristiansen K., Kultima J.R., Leonard P., Levenez F., RA Lund O., Moumen B., Le Paslier D., Pons N., Pedersen O., Prifti E., RA Qin J., Raes J., Tap J., Tims S., Ussery D.W., Yamada T., RA MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P., Wang J., RA Brunak S., Ehrlich S.D.; RT "Dependencies among metagenomic species, viruses, plasmids and units RT of genetic variation."; RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:CDE02490.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CBIC010000097; CDE02490.1; -; Genomic_DNA. DR ProteinModelPortal; R7EII1; -. DR Proteomes; UP000018282; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000018282}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000018282}. FT DOMAIN 216 400 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 418 AA; 47668 MW; 976C680197963305 CRC64; MKEFVISEAQ AETAVLVGLV TKTQDERKTN EYLDELAFLA ETAGAEVVKR FTQKLDAAHS VTYVGKGKLE EIKEYIRNEE EAEREIGMVI FDDELSAKQI RNIEAELKIK ILDRTSLILD IFAMRAQTAN AKTQVELAQY KYMLPRLQRL WTHLERQGGG SGAGGGKGSV GLRGPGETQL EMDRRIILNR MSLLKERLAE IDKQKSTQRK NRGRLIRVAL VGYTNVGKST LMTLLSKSEV FAENKLFATL DTTVRKVIIE NLPFLLSDTV GFIRKLPTDL VDSFKSTLDE VREADLLLHI VDISHPDFEE QIEVVNKTLA DIGAAGKPMI LVFNKIDAYT YIEKAADDLT PRTKENLTLE ELMKTWMAKM EDNCLFISAR EKINMEELKS VVYQRVKELH VQKYPYNDFL YQTYEEEV // ID R7EV76_9FIRM Unreviewed; 427 AA. AC R7EV76; DT 24-JUL-2013, integrated into UniProtKB/TrEMBL. DT 24-JUL-2013, sequence version 1. DT 12-APR-2017, entry version 23. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=BN640_01526 {ECO:0000313|EMBL:CDE05392.1}; OS Anaerotruncus sp. CAG:390. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Ruminococcaceae; OC Anaerotruncus; environmental samples. OX NCBI_TaxID=1262703 {ECO:0000313|EMBL:CDE05392.1, ECO:0000313|Proteomes:UP000018385}; RN [1] {ECO:0000313|EMBL:CDE05392.1, ECO:0000313|Proteomes:UP000018385} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MGS:390 {ECO:0000313|Proteomes:UP000018385}; RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., RA Sunagawa S., Plichta D., Gautier L., Le Chatelier E., Peletier E., RA Bonde I., Nielsen T., Manichanh C., Arumugam M., Batto J., RA Santos M.B.Q.D., Blom N., Borruel N., Burgdorf K.S., Boumezbeur F., RA Casellas F., Dore J., Guarner F., Hansen T., Hildebrand F., Kaas R.S., RA Kennedy S., Kristiansen K., Kultima J.R., Leonard P., Levenez F., RA Lund O., Moumen B., Le Paslier D., Pons N., Pedersen O., Prifti E., RA Qin J., Raes J., Tap J., Tims S., Ussery D.W., Yamada T., RA MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P., Wang J., RA Brunak S., Ehrlich S.D.; RT "Dependencies among metagenomic species, viruses, plasmids and units RT of genetic variation."; RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:CDE05392.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CBID010000220; CDE05392.1; -; Genomic_DNA. DR Proteomes; UP000018385; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000018385}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000018385}. FT DOMAIN 206 373 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 165 199 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 427 AA; 46435 MW; E42E37DE1149ACC0 CRC64; MILNDIKSDE SSVRAVLVGV DTSDMKEGEC DVSLDELERL ADTAGADVAA RLVQAREKPD VRTVIGSGKL AELRTVCEEC GAELCVFDCE MTPSQIRNVE DELGEVRVID RSMLILDIFA QHAATAEGKL QVELAQLKYT APRLVGKGKQ LSRLGGGIGT RGPGESKLES DKRHLARRIA SLEAELDAVE NTRRTTRAAR ERSGLPRVAI VGYTNAGKST LLNRLTDAGI LAEDKLFATL DPTTRKFTLP GGESVLLTDT VGFIRRLPHH LVKAFRSTLE EAALADILLH IVDASDPEYP DEMKVTEDLL TELGAGGKPV LTVYNKCDHE AEGIPAPTVV PNGRNRAVCV SALTGQGIDE MVAMLEKIVR EGKIRVRFRF PNSDAGQLAV LYRLAAVEDV EYGDEYITAT AVADARTRGV LEKYELK // ID R7EYR9_9BACT Unreviewed; 413 AA. AC R7EYR9; DT 24-JUL-2013, integrated into UniProtKB/TrEMBL. DT 24-JUL-2013, sequence version 1. DT 12-APR-2017, entry version 24. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=BN677_01132 {ECO:0000313|EMBL:CDE06607.1}; OS Prevotella sp. CAG:485. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Prevotellaceae; OC Prevotella; environmental samples. OX NCBI_TaxID=1262927 {ECO:0000313|EMBL:CDE06607.1, ECO:0000313|Proteomes:UP000018062}; RN [1] {ECO:0000313|EMBL:CDE06607.1, ECO:0000313|Proteomes:UP000018062} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MGS:485 {ECO:0000313|Proteomes:UP000018062}; RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., RA Sunagawa S., Plichta D., Gautier L., Le Chatelier E., Peletier E., RA Bonde I., Nielsen T., Manichanh C., Arumugam M., Batto J., RA Santos M.B.Q.D., Blom N., Borruel N., Burgdorf K.S., Boumezbeur F., RA Casellas F., Dore J., Guarner F., Hansen T., Hildebrand F., Kaas R.S., RA Kennedy S., Kristiansen K., Kultima J.R., Leonard P., Levenez F., RA Lund O., Moumen B., Le Paslier D., Pons N., Pedersen O., Prifti E., RA Qin J., Raes J., Tap J., Tims S., Ussery D.W., Yamada T., RA MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P., Wang J., RA Brunak S., Ehrlich S.D.; RT "Dependencies among metagenomic species, viruses, plasmids and units RT of genetic variation."; RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:CDE06607.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CBIE010000026; CDE06607.1; -; Genomic_DNA. DR Proteomes; UP000018062; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000018062}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000018062}. FT DOMAIN 206 391 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 413 AA; 47145 MW; 8F58203EB3D0ADBC CRC64; MNKEKEQAEI TADECERCVL VGLVTPQQGE AKSAEYLDEL AFLADTAGAE AAKRFTQRLD YPNPRTYVGK GKLEELKQYI EEEEIPLVIF DDELSPKQVA NIEKELQVKV LDRTSLILDI FAKRAQTATA RTQVELAQYQ YLLPRLTRMW THLERQRGGI GMRGPGETQI ETDRRIILDR ISRLKAQLAD IAKQKEVQRK NRGKLTRVAL VGYTNAGKST LMNLLSKSNV FAENKLFATL DTTVRKVVIE NLPFLLSDTV GFIRKLPTHL VKSFKSTLDE VRDSDILLHV VDISHPGFEE QIEVVNKTLS EICGDNPKPV ILVFNKVDAF TYTPKDADDL TEATAANRSL EDLKQTWMAK MAPDCVFISA KERENIDELK KLIYDKARKV HAERFPYNDF LYEKYESTEE EPE // ID R7FRE9_9FIRM Unreviewed; 421 AA. AC R7FRE9; DT 24-JUL-2013, integrated into UniProtKB/TrEMBL. DT 24-JUL-2013, sequence version 1. DT 12-APR-2017, entry version 23. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=BN797_01292 {ECO:0000313|EMBL:CDE17201.1}; OS Eubacterium sp. CAG:841. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Eubacteriaceae; OC Eubacterium; environmental samples. OX NCBI_TaxID=1262894 {ECO:0000313|EMBL:CDE17201.1, ECO:0000313|Proteomes:UP000017924}; RN [1] {ECO:0000313|EMBL:CDE17201.1, ECO:0000313|Proteomes:UP000017924} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MGS:841 {ECO:0000313|Proteomes:UP000017924}; RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., RA Sunagawa S., Plichta D., Gautier L., Le Chatelier E., Peletier E., RA Bonde I., Nielsen T., Manichanh C., Arumugam M., Batto J., RA Santos M.B.Q.D., Blom N., Borruel N., Burgdorf K.S., Boumezbeur F., RA Casellas F., Dore J., Guarner F., Hansen T., Hildebrand F., Kaas R.S., RA Kennedy S., Kristiansen K., Kultima J.R., Leonard P., Levenez F., RA Lund O., Moumen B., Le Paslier D., Pons N., Pedersen O., Prifti E., RA Qin J., Raes J., Tap J., Tims S., Ussery D.W., Yamada T., RA MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P., Wang J., RA Brunak S., Ehrlich S.D.; RT "Dependencies among metagenomic species, viruses, plasmids and units RT of genetic variation."; RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:CDE17201.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CBIL010000021; CDE17201.1; -; Genomic_DNA. DR Proteomes; UP000017924; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000017924}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000017924}. FT DOMAIN 203 368 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 162 196 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 421 AA; 46267 MW; D8A4E8DCC3DBEA75 CRC64; MENLIGKDTI TNVVLVGVFL PEDDERGFEA SLDELERLTE TAGGKVFARL TQNRENPEPR TYIGPGKVTE LRELCKNNDI DTVIFDCELS PSQIKNLEDD TELKVIDRSM LILDIFALHA VSGEGKLQVE LAQLKYTVPR LTGKGSELSR LGGGIGTRGP GESKLETDRR HVKRRIDALR EQLSRLEKNR ATQRSQRKNS GIFSVAIVGY TNAGKSTLLN ALTGAGILAE DKLFATLDTT TRKYALPSGE EILLTDTVGF IRNLLHHLID AFKSTLEELK YADALLVVVD ASDPECSAQI EVTEKLISEL GAGALPMLYV FNKCDMGIRD IPVSPDGAKK ERVFISAKTG EGLGEFEEKL EKLAHGGKKQ LTFVFPHNGL SKKAILYKNS TVISEEYGDG GVTVVAVVDE KTEGQLKEYI K // ID R7G2E5_9FIRM Unreviewed; 422 AA. AC R7G2E5; DT 24-JUL-2013, integrated into UniProtKB/TrEMBL. DT 24-JUL-2013, sequence version 1. DT 12-APR-2017, entry version 23. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=BN651_01041 {ECO:0000313|EMBL:CDE21624.1}; OS Dorea longicatena CAG:42. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Lachnospiraceae; OC Dorea; environmental samples. OX NCBI_TaxID=1263074 {ECO:0000313|EMBL:CDE21624.1, ECO:0000313|Proteomes:UP000018333}; RN [1] {ECO:0000313|EMBL:CDE21624.1, ECO:0000313|Proteomes:UP000018333} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MGS:42 {ECO:0000313|Proteomes:UP000018333}; RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., RA Sunagawa S., Plichta D., Gautier L., Le Chatelier E., Peletier E., RA Bonde I., Nielsen T., Manichanh C., Arumugam M., Batto J., RA Santos M.B.Q.D., Blom N., Borruel N., Burgdorf K.S., Boumezbeur F., RA Casellas F., Dore J., Guarner F., Hansen T., Hildebrand F., Kaas R.S., RA Kennedy S., Kristiansen K., Kultima J.R., Leonard P., Levenez F., RA Lund O., Moumen B., Le Paslier D., Pons N., Pedersen O., Prifti E., RA Qin J., Raes J., Tap J., Tims S., Ussery D.W., Yamada T., RA MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P., Wang J., RA Brunak S., Ehrlich S.D.; RT "Dependencies among metagenomic species, viruses, plasmids and units RT of genetic variation."; RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:CDE21624.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CBIK010000263; CDE21624.1; -; Genomic_DNA. DR Proteomes; UP000018333; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000018333}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000018333}. FT DOMAIN 199 363 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 158 192 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 422 AA; 47517 MW; 9E51BCA589E6A662 CRC64; MIEIKNETEK VILVGVSLSD QDDTKESLEE LKDLVSTAGA ETVGMVIQNR EQQHPGTYVG KGKIEELKSM IWELRATGIV CDDELSPAQM KNLQDELDVK VMDRTLIILD IFAARASTSE GKIQVELAQL KYQQTRLAGF GKAMSRLGGG IGTRGPGEKK LEMDRRLIKS RIAQLNRELK DVKKHREVTR EQRSRSHIPV AAIVGYTNAG KSTLLNTLTG AGILAEDKLF ATLDPTTRDL KLPSGQEILM TDTVGFIRKL PHHLIEAFRS TLEEARYADI ILHVVDASNP QMDEQMHTVY ETLQNLGVKD KPVITVFNKI DRMEDIWVPR DLHADYYVKI SARTGEGITE FLQAVEAVLR EQKVEIEALY PYKEAGKIQL IRKYGELQEE EYREDGIFVR AFVPAELYGQ VRPEGVTPNN CL // ID R7G3N8_9PROT Unreviewed; 416 AA. AC R7G3N8; DT 24-JUL-2013, integrated into UniProtKB/TrEMBL. DT 24-JUL-2013, sequence version 1. DT 12-APR-2017, entry version 23. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=BN767_01476 {ECO:0000313|EMBL:CDE21571.1}; OS Acidiphilium sp. CAG:727. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales; OC Acetobacteraceae; Acidiphilium; environmental samples. OX NCBI_TaxID=1262689 {ECO:0000313|EMBL:CDE21571.1, ECO:0000313|Proteomes:UP000018053}; RN [1] {ECO:0000313|EMBL:CDE21571.1, ECO:0000313|Proteomes:UP000018053} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MGS:727 {ECO:0000313|Proteomes:UP000018053}; RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., RA Sunagawa S., Plichta D., Gautier L., Le Chatelier E., Peletier E., RA Bonde I., Nielsen T., Manichanh C., Arumugam M., Batto J., RA Santos M.B.Q.D., Blom N., Borruel N., Burgdorf K.S., Boumezbeur F., RA Casellas F., Dore J., Guarner F., Hansen T., Hildebrand F., Kaas R.S., RA Kennedy S., Kristiansen K., Kultima J.R., Leonard P., Levenez F., RA Lund O., Moumen B., Le Paslier D., Pons N., Pedersen O., Prifti E., RA Qin J., Raes J., Tap J., Tims S., Ussery D.W., Yamada T., RA MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P., Wang J., RA Brunak S., Ehrlich S.D.; RT "Dependencies among metagenomic species, viruses, plasmids and units RT of genetic variation."; RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:CDE21571.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CBIM010000219; CDE21571.1; -; Genomic_DNA. DR Proteomes; UP000018053; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000018053}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000018053}. FT DOMAIN 200 358 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 166 193 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 416 AA; 46346 MW; A1F5FF10C35A8A19 CRC64; MITTDKRKKT EKVFLLFALY DKTDISTRIE ELSSLVKTAG AEVVGSEYQF IREVCPATIF GKGKLEQFKT EIREANVDTV IFDGTLSPSK TQNLSDILDI KVIDRTTLIL DIFAINATTA EGKLQVELAQ LEYLLPRLKG QGKALSRLGG GIGTRGPGET RLETNKRYIR NRINSLKNSL KDLENRRNAV GERRKKNGAI VVALAGYTNA GKSTLLNLLS GSDVIAEDKL FATLDPTARK VKIGDFNVIF VDTVGFIRDI PTSLIEAFRS TLQSVENADV VLNVCDVSSS NLIEQAEVAN NEIIRIKPTA NIIKVYNKAD KISYFEFLPT DGIIISAKQN KGIDALVAAI KKEIESQFEQ IKIIVPHEKI GEFYKLTQFL ENYKIDYGDD GAEISFTIRK SVYPKIRESI KNIRVN // ID R7G410_9FIRM Unreviewed; 409 AA. AC R7G410; DT 24-JUL-2013, integrated into UniProtKB/TrEMBL. DT 24-JUL-2013, sequence version 1. DT 12-APR-2017, entry version 24. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=BN631_00742 {ECO:0000313|EMBL:CDE21890.1}; OS Eubacterium dolichum CAG:375. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Eubacteriaceae; OC Eubacterium; environmental samples. OX NCBI_TaxID=1263076 {ECO:0000313|EMBL:CDE21890.1, ECO:0000313|Proteomes:UP000018093}; RN [1] {ECO:0000313|EMBL:CDE21890.1, ECO:0000313|Proteomes:UP000018093} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MGS:375 {ECO:0000313|Proteomes:UP000018093}; RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., RA Sunagawa S., Plichta D., Gautier L., Le Chatelier E., Peletier E., RA Bonde I., Nielsen T., Manichanh C., Arumugam M., Batto J., RA Santos M.B.Q.D., Blom N., Borruel N., Burgdorf K.S., Boumezbeur F., RA Casellas F., Dore J., Guarner F., Hansen T., Hildebrand F., Kaas R.S., RA Kennedy S., Kristiansen K., Kultima J.R., Leonard P., Levenez F., RA Lund O., Moumen B., Le Paslier D., Pons N., Pedersen O., Prifti E., RA Qin J., Raes J., Tap J., Tims S., Ussery D.W., Yamada T., RA MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P., Wang J., RA Brunak S., Ehrlich S.D.; RT "Dependencies among metagenomic species, viruses, plasmids and units RT of genetic variation."; RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:CDE21890.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CBIN010000031; CDE21890.1; -; Genomic_DNA. DR Proteomes; UP000018093; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000018093}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000018093}. FT DOMAIN 189 356 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 103 130 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 409 AA; 47061 MW; A72121914C7809B3 CRC64; MEQVAVVFGA QTLHEEDIQE FKELVAACDM EIVQEFRQVL RQIHGNTWIG KGKCAEIHTF LQAHALDAVL FFNDLSPLQI RNLEAYWNIN VMDRSDLILE IFARRAKSKA ARLQIENAQL KRQRSRLIGS KKHLGRQSAS GQNKGLGEKQ LELDRRRIAS RIVSTTRELK QLEKTRMTQR NARLQSRLPL VSLIGYTNAG KSTIMNALLQ YSNSSKEKYV YEKDMLFATL DTSLRRIDLG HQSFLLSDTV GFVRDLPHEL IEAFHSTLEE ACYADLLIEV IDTSYADYEQ QMKVTSDTLQ ALHIGNLPIL HVFNKCDQTD IPYPSMHGEH LFISAKNKEC IEELINQIRL RLFPPTTMVK LCIPYEKSNL YGRLLTQAQI LQRDDFEDGI HLEVALPNDL LETYKAYMH // ID R7GKC5_9CLOT Unreviewed; 418 AA. AC R7GKC5; DT 24-JUL-2013, integrated into UniProtKB/TrEMBL. DT 24-JUL-2013, sequence version 1. DT 12-APR-2017, entry version 22. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=BN598_00558 {ECO:0000313|EMBL:CDE26437.1}; OS Clostridium sp. CAG:307. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium; environmental samples. OX NCBI_TaxID=1262795 {ECO:0000313|EMBL:CDE26437.1, ECO:0000313|Proteomes:UP000018128}; RN [1] {ECO:0000313|EMBL:CDE26437.1, ECO:0000313|Proteomes:UP000018128} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MGS:307 {ECO:0000313|Proteomes:UP000018128}; RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., RA Sunagawa S., Plichta D., Gautier L., Le Chatelier E., Peletier E., RA Bonde I., Nielsen T., Manichanh C., Arumugam M., Batto J., RA Santos M.B.Q.D., Blom N., Borruel N., Burgdorf K.S., Boumezbeur F., RA Casellas F., Dore J., Guarner F., Hansen T., Hildebrand F., Kaas R.S., RA Kennedy S., Kristiansen K., Kultima J.R., Leonard P., Levenez F., RA Lund O., Moumen B., Le Paslier D., Pons N., Pedersen O., Prifti E., RA Qin J., Raes J., Tap J., Tims S., Ussery D.W., Yamada T., RA MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P., Wang J., RA Brunak S., Ehrlich S.D.; RT "Dependencies among metagenomic species, viruses, plasmids and units RT of genetic variation."; RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:CDE26437.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CBIO010000102; CDE26437.1; -; Genomic_DNA. DR Proteomes; UP000018128; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000018128}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000018128}. FT DOMAIN 191 358 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 418 AA; 47475 MW; 3F37DD40B4941620 CRC64; MKRAILIGID SKEDKYDINY SLNELKALAS ECDILSCATM IQKSEINKVS YIGSGKLLEL KVEIKMYNAD IVIFNDELSP LMLKTLNDTL EIEVIDRSLL ILDIFLKNAH TNEAKMEIKL AHLKYLYPRL SSLRDGFDRQ GGIGSKGSGE TQLELDRRHI SNEIIRLERD LEATHKMKEN QIKRRQKDGI KTVALVGYTN AGKSTTMNSI IEYTDNLTSK KVLAENRLFA TLTTSVRRIE YNNTTFLLSD TVGFVSKIPN HLIHSFNETL LEASNADLII VVLDASSKYA YLELETTINT LYRLGLSDKK MLILLNKIDL CEAIPKISGA DFMPFSNVNL EYMDKLLTYI TKTLNEGKIE MTVLIPFTDG KILNFIRENT QVISQIYLDS GIQITLKCDS KYYKKLSLYE PNDSTLES // ID R7GLM5_9FIRM Unreviewed; 401 AA. AC R7GLM5; DT 24-JUL-2013, integrated into UniProtKB/TrEMBL. DT 24-JUL-2013, sequence version 1. DT 12-APR-2017, entry version 23. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=BN591_00050 {ECO:0000313|EMBL:CDE28264.1}; OS Catenibacterium sp. CAG:290. OC Bacteria; Firmicutes; Erysipelotrichia; Erysipelotrichales; OC Erysipelotrichaceae; Catenibacterium; environmental samples. OX NCBI_TaxID=1262767 {ECO:0000313|EMBL:CDE28264.1, ECO:0000313|Proteomes:UP000018308}; RN [1] {ECO:0000313|EMBL:CDE28264.1, ECO:0000313|Proteomes:UP000018308} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MGS:290 {ECO:0000313|Proteomes:UP000018308}; RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., RA Sunagawa S., Plichta D., Gautier L., Le Chatelier E., Peletier E., RA Bonde I., Nielsen T., Manichanh C., Arumugam M., Batto J., RA Santos M.B.Q.D., Blom N., Borruel N., Burgdorf K.S., Boumezbeur F., RA Casellas F., Dore J., Guarner F., Hansen T., Hildebrand F., Kaas R.S., RA Kennedy S., Kristiansen K., Kultima J.R., Leonard P., Levenez F., RA Lund O., Moumen B., Le Paslier D., Pons N., Pedersen O., Prifti E., RA Qin J., Raes J., Tap J., Tims S., Ussery D.W., Yamada T., RA MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P., Wang J., RA Brunak S., Ehrlich S.D.; RT "Dependencies among metagenomic species, viruses, plasmids and units RT of genetic variation."; RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:CDE28264.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CBIQ010000093; CDE28264.1; -; Genomic_DNA. DR Proteomes; UP000018308; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000018308}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000018308}. FT DOMAIN 183 346 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 401 AA; 46770 MW; 483F6ED0A6120ADD CRC64; MKAILVMTSD NPFYIDELKS LCIACDIEVE DVVIQKLEKI NPATYIGKGK IEEIRLRLDG EMVIFDDELS PLQVKNLTDQ LQTEVTDRTD LILRIFEQRA QTKEAKLQVE IARDQYLLPR LAGMQEHMSH QQGGSGFRGS GEKQIELDRR IISRKLSRSR KELAQIVKQR QTQRERRKRN NVPVIALVGY TNSGKSTLLN TLCQNKEKKV FEKDMLFATL QTSTRNIKIK NHTCLLTDTV GFIERLPHNL IQAFRSTLEE VKEADLLLHV VDSSFEDYQL QVDTTNKVLE ELGVENTPMI YVYNKVDLNK YGYVHPVTPY VFISAKEKIG LDLLEDEISH ILFKDYETFQ LGIPYDKGED FKYLYENTYV EQVDYRDDYI YLQIEAKRQD IKDYLMYILL N // ID R7H618_9FIRM Unreviewed; 419 AA. AC R7H618; DT 24-JUL-2013, integrated into UniProtKB/TrEMBL. DT 24-JUL-2013, sequence version 1. DT 10-MAY-2017, entry version 24. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=BN634_01979 {ECO:0000313|EMBL:CDE35124.1}; OS Eubacterium sp. CAG:38. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Eubacteriaceae; OC Eubacterium; environmental samples. OX NCBI_TaxID=1262889 {ECO:0000313|EMBL:CDE35124.1, ECO:0000313|Proteomes:UP000017954}; RN [1] {ECO:0000313|EMBL:CDE35124.1, ECO:0000313|Proteomes:UP000017954} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MGS:38 {ECO:0000313|Proteomes:UP000017954}; RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., RA Sunagawa S., Plichta D., Gautier L., Le Chatelier E., Peletier E., RA Bonde I., Nielsen T., Manichanh C., Arumugam M., Batto J., RA Santos M.B.Q.D., Blom N., Borruel N., Burgdorf K.S., Boumezbeur F., RA Casellas F., Dore J., Guarner F., Hansen T., Hildebrand F., Kaas R.S., RA Kennedy S., Kristiansen K., Kultima J.R., Leonard P., Levenez F., RA Lund O., Moumen B., Le Paslier D., Pons N., Pedersen O., Prifti E., RA Qin J., Raes J., Tap J., Tims S., Ussery D.W., Yamada T., RA MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P., Wang J., RA Brunak S., Ehrlich S.D.; RT "Dependencies among metagenomic species, viruses, plasmids and units RT of genetic variation."; RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:CDE35124.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CBIU010000008; CDE35124.1; -; Genomic_DNA. DR Proteomes; UP000017954; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000017954}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000017954}. FT DOMAIN 202 369 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 168 195 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 419 AA; 46533 MW; 4DF9F8D66199A41E CRC64; MAQGYDTEEQ KERVLLVGVQ LDNQEDMESS LEELKALAKT AGAETVGKVI QPRDAYHPAT YIGKGKLEEV RSLIEETGAT GIICDDELSP AQLRNLEDAL GTKVMDRTMV ILDIFASRAT TSEGKIQVEV AQLKYRSTRL TGLGTTLSRL GGGIGTRGPG EKKLETDRRI IRDRISRLSK DLEEIKNHRE VARQNRSRTA VPVAAIVGYT NAGKSTLLNY MTDAGILSED KLFATLDPTT RAMNLPNGEK ILLTDTVGFI RKLPHNLIEA FKSTLEEAKY ADIIVHVVDA SSPDRDIQMD VVYKTLKELE VGDKPVVTLF NKCDKFENGD TEAPILRDFK ADETAYISAR TGRGIADFEA ILEKIIRESR VHLVQTFAYA DAGKIQQIRA QGQLIKEEYT ENGIEVEAYV PKALYQKLQ // ID R7HRP2_9BACT Unreviewed; 409 AA. AC R7HRP2; DT 24-JUL-2013, integrated into UniProtKB/TrEMBL. DT 24-JUL-2013, sequence version 1. DT 12-APR-2017, entry version 23. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=BN585_00857 {ECO:0000313|EMBL:CDE41936.1}; OS Prevotella sp. CAG:279. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Prevotellaceae; OC Prevotella; environmental samples. OX NCBI_TaxID=1262924 {ECO:0000313|EMBL:CDE41936.1, ECO:0000313|Proteomes:UP000018375}; RN [1] {ECO:0000313|EMBL:CDE41936.1, ECO:0000313|Proteomes:UP000018375} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MGS:279 {ECO:0000313|Proteomes:UP000018375}; RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., RA Sunagawa S., Plichta D., Gautier L., Le Chatelier E., Peletier E., RA Bonde I., Nielsen T., Manichanh C., Arumugam M., Batto J., RA Santos M.B.Q.D., Blom N., Borruel N., Burgdorf K.S., Boumezbeur F., RA Casellas F., Dore J., Guarner F., Hansen T., Hildebrand F., Kaas R.S., RA Kennedy S., Kristiansen K., Kultima J.R., Leonard P., Levenez F., RA Lund O., Moumen B., Le Paslier D., Pons N., Pedersen O., Prifti E., RA Qin J., Raes J., Tap J., Tims S., Ussery D.W., Yamada T., RA MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P., Wang J., RA Brunak S., Ehrlich S.D.; RT "Dependencies among metagenomic species, viruses, plasmids and units RT of genetic variation."; RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:CDE41936.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CBIX010000153; CDE41936.1; -; Genomic_DNA. DR Proteomes; UP000018375; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000018375}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000018375}. FT DOMAIN 203 388 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 409 AA; 47481 MW; 8261E8A42C0474CD CRC64; MIDEKTITED IGERAVLVGL ITPTQNEAKA NEYLAELAFL AETAGAKSEK RFLQRVDNPN PRTFVGKGKL EEIRQYIEDN AIDLAIFDDD LTSKQVQNIE NELKVKILDR TNLILDIFAK RAQTATARTQ VELAQYQYLL PRLTRMWTHL ERQRGGIGMR GPGETQIETD RRIILDKISR LKVELKNIDR QKSIQRKNRG KLTRIALVGY TNVGKSTLMN LLSKSDVFAE NKLFATLDTT VRKVIIDNLP FLLTDTIGFI RKLPTHLVDS FKSTLDEVRD ADILVHVVDI SHPQFEEQIE VVNRTLQEVC ESKDKPMILV FNKVDAFTYV KKDDDDLTPR LRENIPLEEL KQTWMAKMND NCIFISARER INIDELKSRL YEMAKEIHMK RFPYNDFLFQ KYDEEDLMQ // ID R7I332_9CLOT Unreviewed; 418 AA. AC R7I332; DT 24-JUL-2013, integrated into UniProtKB/TrEMBL. DT 24-JUL-2013, sequence version 1. DT 12-APR-2017, entry version 24. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=BN648_02234 {ECO:0000313|EMBL:CDE44922.1}; OS Clostridium sp. CAG:411. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium; environmental samples. OX NCBI_TaxID=1262802 {ECO:0000313|EMBL:CDE44922.1, ECO:0000313|Proteomes:UP000018022}; RN [1] {ECO:0000313|EMBL:CDE44922.1, ECO:0000313|Proteomes:UP000018022} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MGS:411 {ECO:0000313|Proteomes:UP000018022}; RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., RA Sunagawa S., Plichta D., Gautier L., Le Chatelier E., Peletier E., RA Bonde I., Nielsen T., Manichanh C., Arumugam M., Batto J., RA Santos M.B.Q.D., Blom N., Borruel N., Burgdorf K.S., Boumezbeur F., RA Casellas F., Dore J., Guarner F., Hansen T., Hildebrand F., Kaas R.S., RA Kennedy S., Kristiansen K., Kultima J.R., Leonard P., Levenez F., RA Lund O., Moumen B., Le Paslier D., Pons N., Pedersen O., Prifti E., RA Qin J., Raes J., Tap J., Tims S., Ussery D.W., Yamada T., RA MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P., Wang J., RA Brunak S., Ehrlich S.D.; RT "Dependencies among metagenomic species, viruses, plasmids and units RT of genetic variation."; RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:CDE44922.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CBIY010000091; CDE44922.1; -; Genomic_DNA. DR Proteomes; UP000018022; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000018022}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000018022}. FT DOMAIN 202 367 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 418 AA; 47429 MW; C3099C5934D6CA92 CRC64; MSEMLDIKDL EERVILISVE ESPTDDTEAC LDELEELAKT AGATVVGRMI QKREKIHPGT YIGKGKVEEL LLYIEECQAT GVICDDELSP AQLKNLEELL QIKVIDRTIM ILDIFARHAT TREGKIQVEL AQLKYRATRL VGLRSSLSRL GGGIGTRGPG EKKLEMDRRL IRERISLLKR DLEGIKKARE IARKQRSKNP IPIIAIVGYT NAGKSTLLNT LTNANVLEED KLFATLDPTT RNLEMEDGQQ VLLTDTVGFI RKLPHHLIEA FRSTLEEAKY ADLILHVVDS SSPSAYVHMH TVYETLEMLG AGDKTVITVF NKIDKVEDKT ETVKDCKADV TVRISAKKKI GLEELVQQIE KILREQKIYV ERVFSYNEAG KIQLIRKYGQ LLEEEYKETG IFVRAYLPKE LYYQIGEQ // ID R7I6E6_9FIRM Unreviewed; 590 AA. AC R7I6E6; DT 24-JUL-2013, integrated into UniProtKB/TrEMBL. DT 24-JUL-2013, sequence version 1. DT 12-APR-2017, entry version 23. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=BN770_01024 {ECO:0000313|EMBL:CDE46798.1}; OS Faecalibacterium sp. CAG:74. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Ruminococcaceae; OC Faecalibacterium; environmental samples. OX NCBI_TaxID=1262897 {ECO:0000313|EMBL:CDE46798.1, ECO:0000313|Proteomes:UP000018328}; RN [1] {ECO:0000313|EMBL:CDE46798.1, ECO:0000313|Proteomes:UP000018328} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MGS:74 {ECO:0000313|Proteomes:UP000018328}; RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., RA Sunagawa S., Plichta D., Gautier L., Le Chatelier E., Peletier E., RA Bonde I., Nielsen T., Manichanh C., Arumugam M., Batto J., RA Santos M.B.Q.D., Blom N., Borruel N., Burgdorf K.S., Boumezbeur F., RA Casellas F., Dore J., Guarner F., Hansen T., Hildebrand F., Kaas R.S., RA Kennedy S., Kristiansen K., Kultima J.R., Leonard P., Levenez F., RA Lund O., Moumen B., Le Paslier D., Pons N., Pedersen O., Prifti E., RA Qin J., Raes J., Tap J., Tims S., Ussery D.W., Yamada T., RA MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P., Wang J., RA Brunak S., Ehrlich S.D.; RT "Dependencies among metagenomic species, viruses, plasmids and units RT of genetic variation."; RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:CDE46798.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CBJB010000026; CDE46798.1; -; Genomic_DNA. DR Proteomes; UP000018328; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000018328}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000018328}. FT DOMAIN 368 531 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 327 354 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 590 AA; 66101 MW; 257464C6D8066E88 CRC64; MKQQVHGNVA GVRDTLIEAL GQLYDYEVDE DTFLPRELMQ VLARFTGVLN REIAVYITRD GEVVDVSIGT DRDVELRDYR LRRNTQRLSC VRCIHTHPNG DGRLSDVDLS ALRSFRYDAM VAIGCLKGEP TFVQSAFLVE KQNLLMDEPV RWYKTPDNDW MRQITESDRI VGWEADEKGT HAKERAVLMG IESMESLDEL ARLADTAGAE VVGQFLQKKD KPDTALFIGR GRADELCRQC QALEADLCIF DEELTGIQAR NLEEILRVKV VDRTTLILDI FAQRASSAEG KLQVELAQLQ YQSSRLIGQG LVLSRLAGGI GTRGPGESKL EMNRRHIRER MTELRRRLDA VEKQRELRRK SREKNEIPVV ALVGYTNAGK STLLNQMTGS DVYVQDQLFA TLDAVSRRIE TAEHTPFLLV DTVGFIRKLP HALVSAFRST LEEAVLADVL VIVNDGASEE ITQQHDTVLQ VLSDLGATEQ PRIEVINKCD LYTDEAGAPM LIPGAVRLSA KTGEGIAELH ARIAEQLQKT YAPVTFVLPF DRFGLVGQIR PLGRVVNEEY TDTGLELTVV LANADRDRLV SKYGKEILKG // ID R7IHJ6_9BURK Unreviewed; 386 AA. AC R7IHJ6; DT 24-JUL-2013, integrated into UniProtKB/TrEMBL. DT 24-JUL-2013, sequence version 1. DT 12-APR-2017, entry version 23. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=BN620_01483 {ECO:0000313|EMBL:CDE50077.1}; OS Sutterella sp. CAG:351. OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Sutterellaceae; Sutterella; environmental samples. OX NCBI_TaxID=1262975 {ECO:0000313|EMBL:CDE50077.1, ECO:0000313|Proteomes:UP000018107}; RN [1] {ECO:0000313|EMBL:CDE50077.1, ECO:0000313|Proteomes:UP000018107} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MGS:351 {ECO:0000313|Proteomes:UP000018107}; RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., RA Sunagawa S., Plichta D., Gautier L., Le Chatelier E., Peletier E., RA Bonde I., Nielsen T., Manichanh C., Arumugam M., Batto J., RA Santos M.B.Q.D., Blom N., Borruel N., Burgdorf K.S., Boumezbeur F., RA Casellas F., Dore J., Guarner F., Hansen T., Hildebrand F., Kaas R.S., RA Kennedy S., Kristiansen K., Kultima J.R., Leonard P., Levenez F., RA Lund O., Moumen B., Le Paslier D., Pons N., Pedersen O., Prifti E., RA Qin J., Raes J., Tap J., Tims S., Ussery D.W., Yamada T., RA MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P., Wang J., RA Brunak S., Ehrlich S.D.; RT "Dependencies among metagenomic species, viruses, plasmids and units RT of genetic variation."; RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:CDE50077.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CBJA010000219; CDE50077.1; -; Genomic_DNA. DR Proteomes; UP000018107; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000018107}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000018107}. FT DOMAIN 190 356 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 149 183 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 386 AA; 42963 MW; 3D45AB9F087EDE36 CRC64; MAWLVCVSLG RDFRPDASEE LSLLVTSDAL IPVGLTEAHR DKPDPATYLG SGKIEEIATA AREAGADVLI FDTPLSAAQE RNIEKAAHIA VLDRTELILE IFQKRAKSRE GRLQVELAKL EHLSTRLVRG WTHLERQRGG LSKTGGPGEK QIELDRRMLN ERVKQLKVQL KKLERQRDTQ RRSRTRGDQM TVSLVGYTNA GKSTLFNRLT RSDAYVANQL FATLDTTARR CWVGGSEMVV LSDTVGFIRD LPTQLVEAFK STLEETVHAD LLLHVVDSSS EVREDQIDSV NQVLSQIDAD TIPTILVYNK IDRALAAAGV VRDEKGRVRS VGVSAVTGEG LDELRAAILE FAEHWHKDHP VKARELEPWE QAKLEAEARR AGKPTA // ID R7IXE9_9FIRM Unreviewed; 417 AA. AC R7IXE9; DT 24-JUL-2013, integrated into UniProtKB/TrEMBL. DT 24-JUL-2013, sequence version 1. DT 12-APR-2017, entry version 23. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=BN596_00683 {ECO:0000313|EMBL:CDE56240.1}; OS Roseburia sp. CAG:303. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Lachnospiraceae; OC Roseburia; environmental samples. OX NCBI_TaxID=1262944 {ECO:0000313|EMBL:CDE56240.1, ECO:0000313|Proteomes:UP000018355}; RN [1] {ECO:0000313|EMBL:CDE56240.1, ECO:0000313|Proteomes:UP000018355} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MGS:303 {ECO:0000313|Proteomes:UP000018355}; RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., RA Sunagawa S., Plichta D., Gautier L., Le Chatelier E., Peletier E., RA Bonde I., Nielsen T., Manichanh C., Arumugam M., Batto J., RA Santos M.B.Q.D., Blom N., Borruel N., Burgdorf K.S., Boumezbeur F., RA Casellas F., Dore J., Guarner F., Hansen T., Hildebrand F., Kaas R.S., RA Kennedy S., Kristiansen K., Kultima J.R., Leonard P., Levenez F., RA Lund O., Moumen B., Le Paslier D., Pons N., Pedersen O., Prifti E., RA Qin J., Raes J., Tap J., Tims S., Ussery D.W., Yamada T., RA MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P., Wang J., RA Brunak S., Ehrlich S.D.; RT "Dependencies among metagenomic species, viruses, plasmids and units RT of genetic variation."; RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:CDE56240.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CBJD010000287; CDE56240.1; -; Genomic_DNA. DR Proteomes; UP000018355; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000018355}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000018355}. FT DOMAIN 203 369 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 169 196 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 417 AA; 46731 MW; F677AAFFBB10E6F0 CRC64; MEKMYETAQK PERVILVGVN EGGDEKEVRE SLDELGELVK TAGAEPVAVL VQNREKIHPG TYIGKGKIEE LRNAISLSQA TGIVCDDELS PAQLKNLEQE LETKVMDRTL IILDIFAGRA MTREGKIQVE LAQLKYRASR LVGLRSSLSR LGGGIGTRGP GEKKLEIDRR LINDRISVLR REVEELKNHR SLAREKRSRN PIPVVAIVGY TNAGKSTLLN TLTDAGILAE DKLFATLDPT TRNYKLPGGQ EVLLTDTVGF IRKLPHHLID AFRSTLEEAR YADLILHVVD SSSEQMDAHM DIVYETLKNL DVRDKQIITF FNKMDKLPEN ADRIFKDLRA DRTVCGSIKE NQGLQELVDV LEKMISERSI YVEKVIPYAD AGKIQLIRQY GQLLGEEYTE GGIAIKAYIP GELEGRI // ID R7J335_9BACT Unreviewed; 414 AA. AC R7J335; DT 24-JUL-2013, integrated into UniProtKB/TrEMBL. DT 24-JUL-2013, sequence version 1. DT 12-APR-2017, entry version 23. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=BN799_00266 {ECO:0000313|EMBL:CDE58186.1}; OS Prevotella sp. CAG:873. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Prevotellaceae; OC Prevotella; environmental samples. OX NCBI_TaxID=1262936 {ECO:0000313|EMBL:CDE58186.1, ECO:0000313|Proteomes:UP000018078}; RN [1] {ECO:0000313|EMBL:CDE58186.1, ECO:0000313|Proteomes:UP000018078} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MGS:873 {ECO:0000313|Proteomes:UP000018078}; RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., RA Sunagawa S., Plichta D., Gautier L., Le Chatelier E., Peletier E., RA Bonde I., Nielsen T., Manichanh C., Arumugam M., Batto J., RA Santos M.B.Q.D., Blom N., Borruel N., Burgdorf K.S., Boumezbeur F., RA Casellas F., Dore J., Guarner F., Hansen T., Hildebrand F., Kaas R.S., RA Kennedy S., Kristiansen K., Kultima J.R., Leonard P., Levenez F., RA Lund O., Moumen B., Le Paslier D., Pons N., Pedersen O., Prifti E., RA Qin J., Raes J., Tap J., Tims S., Ussery D.W., Yamada T., RA MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P., Wang J., RA Brunak S., Ehrlich S.D.; RT "Dependencies among metagenomic species, viruses, plasmids and units RT of genetic variation."; RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:CDE58186.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CBJF010000206; CDE58186.1; -; Genomic_DNA. DR Proteomes; UP000018078; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000018078}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000018078}. FT DOMAIN 202 388 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 170 197 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 414 AA; 47579 MW; 8EBE4B5EF27EDEBD CRC64; MKEFVISQET NERAVLVALA TREQPEEKAR EYLDELAFLA DTAGAVTVKT FIQKCEYPNP RTFVGKGKLD EIKQFVEAND IGLVVFDDDL STKQVSNIER ELQVKILDRT SLILDIFARR AQTAHAKTQV ELAQYQYMLP RLTRLWTHLE RQRGGIGMRG PGETQIETDR RIILDKIARL KQELASIDRQ KALQRKNRGK LTRVALVGYT NVGKSTIMNL LSKSDVFAEN KLFATLDTTV RKIAIDNLPI LLTDTVGFIR KLPTHLVESF KSTLDEVREA DVLVHVVDIS HPNFEEQIQV VEQTLREVIG KDADTPVILV FNKIDAFTYQ PKDEDDLTER TTRNMSLEQL RTSWMARMGD DCVFISAKKN LNIAELKSRI YDKAVEVHRR RFPYNDFLYQ KYDDLAENQM PDGE // ID R7J7N3_9BACT Unreviewed; 403 AA. AC R7J7N3; DT 24-JUL-2013, integrated into UniProtKB/TrEMBL. DT 24-JUL-2013, sequence version 1. DT 30-AUG-2017, entry version 24. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=BN646_00656 {ECO:0000313|EMBL:CDE58892.1}; OS Parabacteroides sp. CAG:409. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Tannerellaceae; OC Parabacteroides; environmental samples. OX NCBI_TaxID=1262913 {ECO:0000313|EMBL:CDE58892.1, ECO:0000313|Proteomes:UP000018199}; RN [1] {ECO:0000313|EMBL:CDE58892.1, ECO:0000313|Proteomes:UP000018199} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MGS:409 {ECO:0000313|Proteomes:UP000018199}; RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., RA Sunagawa S., Plichta D., Gautier L., Le Chatelier E., Peletier E., RA Bonde I., Nielsen T., Manichanh C., Arumugam M., Batto J., RA Santos M.B.Q.D., Blom N., Borruel N., Burgdorf K.S., Boumezbeur F., RA Casellas F., Dore J., Guarner F., Hansen T., Hildebrand F., Kaas R.S., RA Kennedy S., Kristiansen K., Kultima J.R., Leonard P., Levenez F., RA Lund O., Moumen B., Le Paslier D., Pons N., Pedersen O., Prifti E., RA Qin J., Raes J., Tap J., Tims S., Ussery D.W., Yamada T., RA MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P., Wang J., RA Brunak S., Ehrlich S.D.; RT "Dependencies among metagenomic species, viruses, plasmids and units RT of genetic variation."; RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:CDE58892.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CBJG010000053; CDE58892.1; -; Genomic_DNA. DR Proteomes; UP000018199; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000018199}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000018199}. FT DOMAIN 202 386 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 403 AA; 46648 MW; E34833B559ED59BF CRC64; MKEFIISEAQ SEKAVLVGLI TPQQNEQKVK EYLDELAFLA DTAGVEAVKC FYQKLDGPNS VTFVGTGKLQ EIKEYVVENE IGLVIFDDEL SAKQLRNIEK ELQVKILDRT NLILDIFARR AQTAHAKTQV ELAQYRYMLP RLTRLWTHLE RQRGGVGMRG PGETQLETDK RLILDKISRL KKELVDIDKQ KSVQRKNRGK MVRVALVGYT NVGKSTLMNL LSKSDVFAEN KLFATLDTTV RKVIIENLPF LLSDTVGFIR KLPTELVESF KSTLDEVREA DLLVHVVDIS HPTFEEQIEV VNKTLAEIDD REKPMIMVFN KVDAFTFVPK DEDDLTPRKR ENIDLDELKR TWMAKMQDNC IFISAKEKTN IEELKALLYE RVKQIHVTRF PYNDFLFQQY EEE // ID R7JLR4_9BACT Unreviewed; 407 AA. AC R7JLR4; DT 24-JUL-2013, integrated into UniProtKB/TrEMBL. DT 24-JUL-2013, sequence version 1. DT 12-APR-2017, entry version 23. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=BN752_00798 {ECO:0000313|EMBL:CDE64553.1}; OS Alistipes putredinis CAG:67. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Rikenellaceae; OC Alistipes; environmental samples. OX NCBI_TaxID=1263036 {ECO:0000313|EMBL:CDE64553.1, ECO:0000313|Proteomes:UP000018026}; RN [1] {ECO:0000313|EMBL:CDE64553.1, ECO:0000313|Proteomes:UP000018026} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MGS:67 {ECO:0000313|Proteomes:UP000018026}; RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., RA Sunagawa S., Plichta D., Gautier L., Le Chatelier E., Peletier E., RA Bonde I., Nielsen T., Manichanh C., Arumugam M., Batto J., RA Santos M.B.Q.D., Blom N., Borruel N., Burgdorf K.S., Boumezbeur F., RA Casellas F., Dore J., Guarner F., Hansen T., Hildebrand F., Kaas R.S., RA Kennedy S., Kristiansen K., Kultima J.R., Leonard P., Levenez F., RA Lund O., Moumen B., Le Paslier D., Pons N., Pedersen O., Prifti E., RA Qin J., Raes J., Tap J., Tims S., Ussery D.W., Yamada T., RA MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P., Wang J., RA Brunak S., Ehrlich S.D.; RT "Dependencies among metagenomic species, viruses, plasmids and units RT of genetic variation."; RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:CDE64553.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CBJI010000068; CDE64553.1; -; Genomic_DNA. DR Proteomes; UP000018026; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000018026}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000018026}. FT DOMAIN 212 396 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 180 207 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 407 AA; 46360 MW; 5BBFC273A8CDED58 CRC64; MEQNKEIVTK NDQPASGAGF ERAVLVAVIR DQQDPRQAEE YLAELEFLAE TAGIVGVRRF TQRLPQPSAR IYVGPGKLEE IAAYCKEEEI DVAIFDDELS PSQTRNIEAA MPCRILDRTR LILDIFMSRA QTAYAKTQVQ LANYQYMLPR LSGMWTHLER QRGGTGTRGG AGEREIETDR RIIRNRISKL KEDLQKIDRQ MAVQRSNRGS MVRVALVGYT NVGKSTLMNL ISKSEVFAEN KLFATLDTTV RKVVFDNLPF LLSDTVGFIR KLPTELIESF KSTLDEVREA DLLLHVVDIS HPQFEDQIAV VKQTLQDIGA GDKPVYLVFN KVDAYTYVEK EPDDLTPSTR ENRSLEDLKQ SWIARANTPC IFISAVEKIN IEKLRSDLYG MVREIHSGRY PFNNFLY // ID R7JQT4_9FIRM Unreviewed; 411 AA. AC R7JQT4; DT 24-JUL-2013, integrated into UniProtKB/TrEMBL. DT 24-JUL-2013, sequence version 1. DT 12-APR-2017, entry version 23. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=BN630_01132 {ECO:0000313|EMBL:CDE65968.1}; OS Blautia sp. CAG:37. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Lachnospiraceae; OC Blautia; environmental samples. OX NCBI_TaxID=1262757 {ECO:0000313|EMBL:CDE65968.1, ECO:0000313|Proteomes:UP000018204}; RN [1] {ECO:0000313|EMBL:CDE65968.1, ECO:0000313|Proteomes:UP000018204} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MGS:37 {ECO:0000313|Proteomes:UP000018204}; RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., RA Sunagawa S., Plichta D., Gautier L., Le Chatelier E., Peletier E., RA Bonde I., Nielsen T., Manichanh C., Arumugam M., Batto J., RA Santos M.B.Q.D., Blom N., Borruel N., Burgdorf K.S., Boumezbeur F., RA Casellas F., Dore J., Guarner F., Hansen T., Hildebrand F., Kaas R.S., RA Kennedy S., Kristiansen K., Kultima J.R., Leonard P., Levenez F., RA Lund O., Moumen B., Le Paslier D., Pons N., Pedersen O., Prifti E., RA Qin J., Raes J., Tap J., Tims S., Ussery D.W., Yamada T., RA MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P., Wang J., RA Brunak S., Ehrlich S.D.; RT "Dependencies among metagenomic species, viruses, plasmids and units RT of genetic variation."; RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:CDE65968.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CBJJ010000084; CDE65968.1; -; Genomic_DNA. DR Proteomes; UP000018204; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000018204}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000018204}. FT DOMAIN 199 363 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 158 195 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 411 AA; 45765 MW; 2876BFA0889991B3 CRC64; MFDLREEQER VILVGVQENG GANAEESLDE LAELASTAGA KVEGRLVQVR EAIHPGTYIG KGKLEELKIL VRACDATGII CDDELSSIQL KGLEEALECK IMDRTLLILD IFAARAVSSE GKIQVELAQL KYRASRLSGL GTSLSRLGGG IGTRGPGEKK LETDRRLIRT RITQLKRELE EVRQHRELLR EGRKRSKIPV AALVGYTSAG KSSLLNALTG SEILADAMLF STLDTTTRSL TLPDGQEILL TDTVGFINKL PHHLIDAFRS TLEEARYADY ILHVVDTSNP QMELQMQVVY DTLRELKVED KKIVTLLNKQ DKLLDPVVVK DFRADASLAV SAKTGQGLED LKNLLSSWMM EGKIYIERLY PYDKAGTISL IRGYGILLEE EYLPEGIRVK AYVPRDIYPR V // ID R7JWL5_9CLOT Unreviewed; 378 AA. AC R7JWL5; DT 24-JUL-2013, integrated into UniProtKB/TrEMBL. DT 24-JUL-2013, sequence version 1. DT 10-MAY-2017, entry version 24. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=BN584_02077 {ECO:0000313|EMBL:CDE68046.1}; OS Clostridium sp. CAG:277. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium; environmental samples. OX NCBI_TaxID=1262790 {ECO:0000313|EMBL:CDE68046.1, ECO:0000313|Proteomes:UP000018281}; RN [1] {ECO:0000313|EMBL:CDE68046.1, ECO:0000313|Proteomes:UP000018281} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MGS:277 {ECO:0000313|Proteomes:UP000018281}; RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., RA Sunagawa S., Plichta D., Gautier L., Le Chatelier E., Peletier E., RA Bonde I., Nielsen T., Manichanh C., Arumugam M., Batto J., RA Santos M.B.Q.D., Blom N., Borruel N., Burgdorf K.S., Boumezbeur F., RA Casellas F., Dore J., Guarner F., Hansen T., Hildebrand F., Kaas R.S., RA Kennedy S., Kristiansen K., Kultima J.R., Leonard P., Levenez F., RA Lund O., Moumen B., Le Paslier D., Pons N., Pedersen O., Prifti E., RA Qin J., Raes J., Tap J., Tims S., Ussery D.W., Yamada T., RA MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P., Wang J., RA Brunak S., Ehrlich S.D.; RT "Dependencies among metagenomic species, viruses, plasmids and units RT of genetic variation."; RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:CDE68046.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CBJK010000015; CDE68046.1; -; Genomic_DNA. DR Proteomes; UP000018281; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000018281}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000018281}. FT DOMAIN 157 321 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 116 150 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 378 AA; 42754 MW; 0A4DEAB4AAA22BBA CRC64; MGMVIQKRER MHPGTYIGKG KIEEVAALVS QCNADTVVCD DELSPAQLRN LSDALDVKVI DRTVMILDIF AKHATTNEGK LQVELAQLRY RSSHLIGERT ELSRLGGGIG TRGPGEQKLE QDRRLIRNRI SQLKKELEQV TRTRTLTRKK RQENPIPVIA IVGYTNAGKS TLLNYLTGAG VLSQDKLFAT LDPTTRKLTT QEGEEFLFTD TVGFIRKLPH HLIQAFRSTL EEAKYADMIL HVVDCANPDM DAQMFTVYET LRRLEVGDKK VITAFNKIDL RDDAGVLKDL NADETVRISA KTGEGLEELL HTVSKVAREG KLVVEKTFSY AEGSVVSQIR SIGKILEEDY RNEGIYIKAE IPREYEYLFV EKKKQEEW // ID R7KHF1_9BURK Unreviewed; 398 AA. AC R7KHF1; DT 24-JUL-2013, integrated into UniProtKB/TrEMBL. DT 24-JUL-2013, sequence version 1. DT 12-APR-2017, entry version 24. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=BN692_01137 {ECO:0000313|EMBL:CDE75844.1}; OS Sutterella sp. CAG:521. OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Sutterellaceae; Sutterella; environmental samples. OX NCBI_TaxID=1262977 {ECO:0000313|EMBL:CDE75844.1, ECO:0000313|Proteomes:UP000018289}; RN [1] {ECO:0000313|EMBL:CDE75844.1, ECO:0000313|Proteomes:UP000018289} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MGS:521 {ECO:0000313|Proteomes:UP000018289}; RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., RA Sunagawa S., Plichta D., Gautier L., Le Chatelier E., Peletier E., RA Bonde I., Nielsen T., Manichanh C., Arumugam M., Batto J., RA Santos M.B.Q.D., Blom N., Borruel N., Burgdorf K.S., Boumezbeur F., RA Casellas F., Dore J., Guarner F., Hansen T., Hildebrand F., Kaas R.S., RA Kennedy S., Kristiansen K., Kultima J.R., Leonard P., Levenez F., RA Lund O., Moumen B., Le Paslier D., Pons N., Pedersen O., Prifti E., RA Qin J., Raes J., Tap J., Tims S., Ussery D.W., Yamada T., RA MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P., Wang J., RA Brunak S., Ehrlich S.D.; RT "Dependencies among metagenomic species, viruses, plasmids and units RT of genetic variation."; RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:CDE75844.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CBJP010000044; CDE75844.1; -; Genomic_DNA. DR Proteomes; UP000018289; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000018289}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000018289}. FT DOMAIN 213 379 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 398 AA; 44391 MW; 1ABBBA3CE258180A CRC64; MARSFCPYRM TVFQIDSAEE KSPRAYLVCI STSRITIADA AEELTELVRS DALEPVGLMM AKRDKPDPAT YLGSGKIGEL ADEVKRLDIG VVVFDVALSA AQQRNIERIV GVAVLDRTQL ILEIFQRRAK SREGRLQVEL ARLEHLSTRL VRGWTHLERQ RGGLGKTGGP GEKQIELDRR MIGVRVKQLK EQLKKLAKQR NTQRKGRSRS DIVSLSIVGY TNAGKSTLFN ALTKSDIYAA DQLFATLDTT ARRCYVGEGE SVVLSDTVGF IRGLPHQLVE AFKSTLDETV HADILLHVVD ASSAAKDDQI VEVNKVLEEI DAHEIPTILV LNKIDRTDLE PEILRNASGE IEAVRISALT GVGLDLLREA ILEKSREVKE ANKSLPRELE DWEKEEME // ID R7KZN3_9FIRM Unreviewed; 417 AA. AC R7KZN3; DT 24-JUL-2013, integrated into UniProtKB/TrEMBL. DT 24-JUL-2013, sequence version 1. DT 12-APR-2017, entry version 23. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=BN622_02320 {ECO:0000313|EMBL:CDE81889.1}; OS Ruminococcus sp. CAG:353. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Ruminococcaceae; OC Ruminococcus; environmental samples. OX NCBI_TaxID=1262955 {ECO:0000313|EMBL:CDE81889.1, ECO:0000313|Proteomes:UP000017936}; RN [1] {ECO:0000313|EMBL:CDE81889.1, ECO:0000313|Proteomes:UP000017936} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MGS:353 {ECO:0000313|Proteomes:UP000017936}; RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., RA Sunagawa S., Plichta D., Gautier L., Le Chatelier E., Peletier E., RA Bonde I., Nielsen T., Manichanh C., Arumugam M., Batto J., RA Santos M.B.Q.D., Blom N., Borruel N., Burgdorf K.S., Boumezbeur F., RA Casellas F., Dore J., Guarner F., Hansen T., Hildebrand F., Kaas R.S., RA Kennedy S., Kristiansen K., Kultima J.R., Leonard P., Levenez F., RA Lund O., Moumen B., Le Paslier D., Pons N., Pedersen O., Prifti E., RA Qin J., Raes J., Tap J., Tims S., Ussery D.W., Yamada T., RA MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P., Wang J., RA Brunak S., Ehrlich S.D.; RT "Dependencies among metagenomic species, viruses, plasmids and units RT of genetic variation."; RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:CDE81889.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CBJQ010000162; CDE81889.1; -; Genomic_DNA. DR Proteomes; UP000017936; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000017936}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000017936}. FT DOMAIN 202 364 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 168 195 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 417 AA; 45933 MW; A7153EAB792BB69C CRC64; MAELTPTYDE QPVKAIIVTV DTGEFDAELS LGELEELAHT AGAEVVGSVL QKRPSPDTAT YIGSGRLEEL VPQIEALEAD LLIFDCELTA NQTKNIEAVT DVRVIDRTTL ILDIFAQRAL SAEGRIQVEL AQQKYRLAHL AGKGVSLSRL GGGIGTRGPG ESKLETDRRH IRRRIEILEG DLKEIRKRRD LIRNRRKKDN VITAAIVGYT NVGKSTLLNA LTDAGVLAEN KLFATLDVTS RAIELPDGRS VLLADTVGLI RRLPHNLVEA FKSTLEEAAN ADIILNIIDI SSDDAYGQAQ VTEELLNELG CEGIPRINVL NKCDKLAGWE NIPEDDNTVK ISAKEKIGFD RLLECIATNL PETSVRGSFV IPYDKGNLLN VIRDEGKIFS EEYTADGTLI DALVDNKVYY LVEKYKQ // ID R7LDQ3_9BACT Unreviewed; 417 AA. AC R7LDQ3; DT 24-JUL-2013, integrated into UniProtKB/TrEMBL. DT 24-JUL-2013, sequence version 1. DT 12-APR-2017, entry version 22. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=BN805_01455 {ECO:0000313|EMBL:CDE86779.1}; OS Prevotella sp. CAG:891. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Prevotellaceae; OC Prevotella; environmental samples. OX NCBI_TaxID=1262937 {ECO:0000313|EMBL:CDE86779.1, ECO:0000313|Proteomes:UP000018147}; RN [1] {ECO:0000313|EMBL:CDE86779.1, ECO:0000313|Proteomes:UP000018147} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MGS:891 {ECO:0000313|Proteomes:UP000018147}; RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., RA Sunagawa S., Plichta D., Gautier L., Le Chatelier E., Peletier E., RA Bonde I., Nielsen T., Manichanh C., Arumugam M., Batto J., RA Santos M.B.Q.D., Blom N., Borruel N., Burgdorf K.S., Boumezbeur F., RA Casellas F., Dore J., Guarner F., Hansen T., Hildebrand F., Kaas R.S., RA Kennedy S., Kristiansen K., Kultima J.R., Leonard P., Levenez F., RA Lund O., Moumen B., Le Paslier D., Pons N., Pedersen O., Prifti E., RA Qin J., Raes J., Tap J., Tims S., Ussery D.W., Yamada T., RA MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P., Wang J., RA Brunak S., Ehrlich S.D.; RT "Dependencies among metagenomic species, viruses, plasmids and units RT of genetic variation."; RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:CDE86779.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CBJT010000120; CDE86779.1; -; Genomic_DNA. DR Proteomes; UP000018147; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000018147}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000018147}. FT DOMAIN 216 400 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 417 AA; 47786 MW; 8EB0BD79AD52DC5B CRC64; MKEFIKTEVK AETAVLVGLI TRTQDERKTA EYLDELEFLA ETAGAVTVKR FTQRLDSPSS VTYVGKGKLE EIKCYIEAEE EAEREIGMVI FDDELSAKQL RNIEKELKVK ILDRTSLILD IFAMRAQTAN AKTQVELAQY RYMLPRLQRL WTHLERQGGG SGSGGGKGSV GLRGPGETQL EMDRRIILNR MALLKQRLAD IDRQKTTQRK NRGRMIRVAL VGYTNVGKST LINLLAKTEV FAENKLFATL DTTVRKVIID NLPFLLADTV GFIRKLPTDL VDSFKSTLDE VREADLLVHV VDVSHPDFEE QIQVVDQTLS DLGCADKPRL MVFNKMDAYE WTEKDPDDLT PATRENVSLN ELQHTWMARL GDDCIFISAR ERLNIDNLKD LFYSRVKQLH VQKYPYNDFL FEHYEEN // ID R7MJ42_9FIRM Unreviewed; 420 AA. AC R7MJ42; DT 24-JUL-2013, integrated into UniProtKB/TrEMBL. DT 24-JUL-2013, sequence version 1. DT 12-APR-2017, entry version 24. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=BN739_01085 {ECO:0000313|EMBL:CDF01129.1}; OS Ruminococcus sp. CAG:624. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Ruminococcaceae; OC Ruminococcus; environmental samples. OX NCBI_TaxID=1262965 {ECO:0000313|EMBL:CDF01129.1, ECO:0000313|Proteomes:UP000017977}; RN [1] {ECO:0000313|EMBL:CDF01129.1, ECO:0000313|Proteomes:UP000017977} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MGS:624 {ECO:0000313|Proteomes:UP000017977}; RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., RA Sunagawa S., Plichta D., Gautier L., Le Chatelier E., Peletier E., RA Bonde I., Nielsen T., Manichanh C., Arumugam M., Batto J., RA Santos M.B.Q.D., Blom N., Borruel N., Burgdorf K.S., Boumezbeur F., RA Casellas F., Dore J., Guarner F., Hansen T., Hildebrand F., Kaas R.S., RA Kennedy S., Kristiansen K., Kultima J.R., Leonard P., Levenez F., RA Lund O., Moumen B., Le Paslier D., Pons N., Pedersen O., Prifti E., RA Qin J., Raes J., Tap J., Tims S., Ussery D.W., Yamada T., RA MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P., Wang J., RA Brunak S., Ehrlich S.D.; RT "Dependencies among metagenomic species, viruses, plasmids and units RT of genetic variation."; RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:CDF01129.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CBKC010000176; CDF01129.1; -; Genomic_DNA. DR Proteomes; UP000017977; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000017977}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000017977}. FT DOMAIN 200 362 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 420 AA; 46623 MW; 68695DCC92D09FA7 CRC64; MYENKTKEQP VKAILASVDT GEFNAESSIE ELAELAETAN AEVVGVIIQK KDSYDSATCM GAGRLEELKG QLEELRAELV IFDHELTGVQ VRNIENIIDV RVIDRTTLIL DIFAQRARTK EGKLQVELAQ QKYRLPRLTG MGTSLSRLGG GIGTRGPGET KLETDKRHIR KRISYLEAEL EDLKKHRNFS RSRRRKDGVL CAAIVGYTNV GKSTLLNALT DAGVLAEDKL FATLDITSRS LELPDGRSVM LIDTVGLIRR LPHNLVEAFK STLEEAASAD IILNVQDLSS PEQEEQAEVT RKLLSELGCD GIPQINVMNK VDAALNPDTV FEDSLTVAIS AKHHQGFERL LKCIAENLPE TAKRMKLLIP YDKTSLIGKI RLEGKIFSEE YIENGTLIDA LVDKKLISQA EQYKIKADTP // ID R7N7A1_9FIRM Unreviewed; 502 AA. AC R7N7A1; DT 24-JUL-2013, integrated into UniProtKB/TrEMBL. DT 24-JUL-2013, sequence version 1. DT 07-JUN-2017, entry version 23. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=BN816_02648 {ECO:0000313|EMBL:CDF07962.1}; OS Firmicutes bacterium CAG:95. OC Bacteria; Firmicutes; environmental samples. OX NCBI_TaxID=1262988 {ECO:0000313|EMBL:CDF07962.1, ECO:0000313|Proteomes:UP000018182}; RN [1] {ECO:0000313|EMBL:CDF07962.1, ECO:0000313|Proteomes:UP000018182} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MGS:95 {ECO:0000313|Proteomes:UP000018182}; RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., RA Sunagawa S., Plichta D., Gautier L., Le Chatelier E., Peletier E., RA Bonde I., Nielsen T., Manichanh C., Arumugam M., Batto J., RA Santos M.B.Q.D., Blom N., Borruel N., Burgdorf K.S., Boumezbeur F., RA Casellas F., Dore J., Guarner F., Hansen T., Hildebrand F., Kaas R.S., RA Kennedy S., Kristiansen K., Kultima J.R., Leonard P., Levenez F., RA Lund O., Moumen B., Le Paslier D., Pons N., Pedersen O., Prifti E., RA Qin J., Raes J., Tap J., Tims S., Ussery D.W., Yamada T., RA MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P., Wang J., RA Brunak S., Ehrlich S.D.; RT "Dependencies among metagenomic species, viruses, plasmids and units RT of genetic variation."; RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:CDF07962.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CBKF010000172; CDF07962.1; -; Genomic_DNA. DR Proteomes; UP000018182; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 2. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 2. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000018182}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000018182}. FT DOMAIN 211 343 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 170 204 {ECO:0000256|SAM:Coils}. FT COILED 353 375 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 502 AA; 57799 MW; 62CF4697E14A0EBF CRC64; MEEYWDIFLE EQQNRELERV LLVGVDTGEE QNFDNSMEEL KQLAKACFME PVGTVTQRME FVHKALYIGT GKVQEVRDAA QALDAQLILI NDTLTPSQIK NLQNELKTPV IDRTTLILNI FEMRARTREA RLQVETAKLQ YLLPRLVGMH EALTRQGGTS GSMSSRGAGE KKLELDRRHI EHRISELRKE LDAISRERET QRKRRGQSRI PLVALVGYTN AGKSTIMNHM VERFVGDEEK KVLERDMLFA TLDTTIRRIN TGNNQDFLLT DTVGFIHKLP HGLVKAFHST LEEIKGADLL LQVVDVSDPG YQEQMETTRE TLRELGAGDI PMLIVFNKAD RLTNTANTTG KPRNQMEQEQ KLQNQKLQNQ KLQDQKLQDQ KLQDQNPQNQ MLQLHKTPDQ EKELQQMSLG ETTYPRTAGT NKIYISARQP ESIELLVKEI IRRVYADYEE VRLLIPYDKG SIVSYLQENA QILEQSYEPE GTRLRVNCHH ADAGKYEQYV VK // ID R7NES2_9FIRM Unreviewed; 413 AA. AC R7NES2; DT 24-JUL-2013, integrated into UniProtKB/TrEMBL. DT 24-JUL-2013, sequence version 1. DT 12-APR-2017, entry version 23. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=BN774_01232 {ECO:0000313|EMBL:CDF10613.1}; OS Eubacterium sp. CAG:76. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Eubacteriaceae; OC Eubacterium; environmental samples. OX NCBI_TaxID=1262892 {ECO:0000313|EMBL:CDF10613.1, ECO:0000313|Proteomes:UP000018156}; RN [1] {ECO:0000313|EMBL:CDF10613.1, ECO:0000313|Proteomes:UP000018156} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MGS:76 {ECO:0000313|Proteomes:UP000018156}; RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., RA Sunagawa S., Plichta D., Gautier L., Le Chatelier E., Peletier E., RA Bonde I., Nielsen T., Manichanh C., Arumugam M., Batto J., RA Santos M.B.Q.D., Blom N., Borruel N., Burgdorf K.S., Boumezbeur F., RA Casellas F., Dore J., Guarner F., Hansen T., Hildebrand F., Kaas R.S., RA Kennedy S., Kristiansen K., Kultima J.R., Leonard P., Levenez F., RA Lund O., Moumen B., Le Paslier D., Pons N., Pedersen O., Prifti E., RA Qin J., Raes J., Tap J., Tims S., Ussery D.W., Yamada T., RA MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P., Wang J., RA Brunak S., Ehrlich S.D.; RT "Dependencies among metagenomic species, viruses, plasmids and units RT of genetic variation."; RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:CDF10613.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CBKG010000098; CDF10613.1; -; Genomic_DNA. DR Proteomes; UP000018156; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000018156}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000018156}. FT DOMAIN 201 365 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 413 AA; 45893 MW; CDAE488A1F3D2AEB CRC64; MALYDTDDEQ EKVVLVGVEL NPLDDCGKSL EELAELAKTA GAVTVGKMIQ PRDSFHPATY IGKGKLEELR LMIDELGATG IICDDELSPA QLRNLEDVLN TKIMDRTMVI LDIFAARASS SEGKIQVEMA QLKYRSTRLA GLGTTLSRLG GGIGTRGPGE KKIETDRRII RDRIAHLSGE LKEIKSHRDV QRQNRQDSST PVAAIVGYTN AGKSTLLNRL TDAGVLSEDK LFATLDPTTR ALTLPNKEKV LMTDTVGFIR KLPHNLIEAF KSTLEEAKYA DMIIHVVDCS NDDYERHMAT VYETLKQLDV GDKPIITLFN KCDKYGELPI LKDSKADYVE NISARTGVGI DEFLEDVQDI ILKSRIRIER VFPYSDAGKI QLIREYGQLE SEEYTQEGIS VKGYVPAWVG GKL // ID R7NPB5_9FIRM Unreviewed; 416 AA. AC R7NPB5; DT 24-JUL-2013, integrated into UniProtKB/TrEMBL. DT 24-JUL-2013, sequence version 1. DT 10-MAY-2017, entry version 24. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=BN720_00523 {ECO:0000313|EMBL:CDF15234.1}; OS Eubacterium sp. CAG:581. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Eubacteriaceae; OC Eubacterium; environmental samples. OX NCBI_TaxID=1262890 {ECO:0000313|EMBL:CDF15234.1, ECO:0000313|Proteomes:UP000017975}; RN [1] {ECO:0000313|EMBL:CDF15234.1, ECO:0000313|Proteomes:UP000017975} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MGS:581 {ECO:0000313|Proteomes:UP000017975}; RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., RA Sunagawa S., Plichta D., Gautier L., Le Chatelier E., Peletier E., RA Bonde I., Nielsen T., Manichanh C., Arumugam M., Batto J., RA Santos M.B.Q.D., Blom N., Borruel N., Burgdorf K.S., Boumezbeur F., RA Casellas F., Dore J., Guarner F., Hansen T., Hildebrand F., Kaas R.S., RA Kennedy S., Kristiansen K., Kultima J.R., Leonard P., Levenez F., RA Lund O., Moumen B., Le Paslier D., Pons N., Pedersen O., Prifti E., RA Qin J., Raes J., Tap J., Tims S., Ussery D.W., Yamada T., RA MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P., Wang J., RA Brunak S., Ehrlich S.D.; RT "Dependencies among metagenomic species, viruses, plasmids and units RT of genetic variation."; RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:CDF15234.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CBKI010000219; CDF15234.1; -; Genomic_DNA. DR Proteomes; UP000017975; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000017975}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000017975}. FT DOMAIN 200 362 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 159 196 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 416 AA; 46205 MW; A05300699EFEF070 CRC64; MELKSNEEKV TRAVLISVNT GEYDADTSLL ELVELAKTAG AETVATVMQN LDRPETATYV GKGKLLEISE FCESQEIDLL IFDSELSPTQ IRNIEEETGV RVIDRTMLIL DIFAMRARSK EGKLQVELAQ LKYMMPRLTG MGTAMSRLGG GIGTRGPGET KLETDRRHIR RRMETLKEQL KDVEHHREQL RKRRRKDNVI TVAIVGYTNA GKSTLMNYLT DAGVLAENKL FATLDPTSRA LKLPNGVTVM LIDTVGLVRR LPHHLVDAFR STLEEAAEAD IILNVCDVSS EEASLHLKVT RELLESLGCK DKPIIPVLNK CDLVSGGVTV PQIGTGVRIS AKEGKGIDEL LHAIEDNLPV KVKRVKALLP FDKLGISAEI REKCILNSEE YVADGLLIDA VISEEMYSKI RDYIVE // ID R7NRS9_9BACE Unreviewed; 421 AA. AC R7NRS9; DT 24-JUL-2013, integrated into UniProtKB/TrEMBL. DT 24-JUL-2013, sequence version 1. DT 12-APR-2017, entry version 23. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=BN821_02309 {ECO:0000313|EMBL:CDF14832.1}; OS Bacteroides sp. CAG:98. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae; OC Bacteroides; environmental samples. OX NCBI_TaxID=1262754 {ECO:0000313|EMBL:CDF14832.1, ECO:0000313|Proteomes:UP000018115}; RN [1] {ECO:0000313|EMBL:CDF14832.1, ECO:0000313|Proteomes:UP000018115} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MGS:98 {ECO:0000313|Proteomes:UP000018115}; RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., RA Sunagawa S., Plichta D., Gautier L., Le Chatelier E., Peletier E., RA Bonde I., Nielsen T., Manichanh C., Arumugam M., Batto J., RA Santos M.B.Q.D., Blom N., Borruel N., Burgdorf K.S., Boumezbeur F., RA Casellas F., Dore J., Guarner F., Hansen T., Hildebrand F., Kaas R.S., RA Kennedy S., Kristiansen K., Kultima J.R., Leonard P., Levenez F., RA Lund O., Moumen B., Le Paslier D., Pons N., Pedersen O., Prifti E., RA Qin J., Raes J., Tap J., Tims S., Ussery D.W., Yamada T., RA MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P., Wang J., RA Brunak S., Ehrlich S.D.; RT "Dependencies among metagenomic species, viruses, plasmids and units RT of genetic variation."; RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:CDF14832.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CBKJ010000078; CDF14832.1; -; Genomic_DNA. DR Proteomes; UP000018115; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000018115}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000018115}. FT DOMAIN 216 400 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 421 AA; 48045 MW; 8BD09B43E8E9E771 CRC64; MKEFVISEAQ VETAILVGLV TQTQDERKTM EYLDELEFLA ETAGATVVKR YTQKLPSANS VTYVGKGKLE EIKEYIHREE EEEREIGMVI FDDELSAKQI RNIEAELKVK ILDRTSLILD IFAMRAQTAN AKTQVELAQY KYMLPRLQRL WTHLERQGGG SGAGGGKGSV GLRGPGETQL EMDRRIILNR MSLLKERLAE IDKQKMTQRK NRGRMIRVAL VGYTNVGKST LMNLLSKSEV FAENKLFATL DTTVRKVIID NLPFLLTDTV GFIRKLPTDL VDSFKSTLDE VREADLLIHV VDISHPDFEE QIAVVDKTIA DLGAGGKPTM IVFNKIDAYT YIEKPEDDLT PKTKENITLD ELMNTWMAKL NDNCIFISAK EKTNLEELKE VIYNKVRELH VQKYPYNDFL YQTYDETDVS L // ID R7PD67_9BACT Unreviewed; 426 AA. AC R7PD67; DT 24-JUL-2013, integrated into UniProtKB/TrEMBL. DT 24-JUL-2013, sequence version 1. DT 12-APR-2017, entry version 22. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=BN736_00206 {ECO:0000313|EMBL:CDF22262.1}; OS Prevotella sp. CAG:617. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Prevotellaceae; OC Prevotella; environmental samples. OX NCBI_TaxID=1262933 {ECO:0000313|EMBL:CDF22262.1, ECO:0000313|Proteomes:UP000018057}; RN [1] {ECO:0000313|EMBL:CDF22262.1, ECO:0000313|Proteomes:UP000018057} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MGS:617 {ECO:0000313|Proteomes:UP000018057}; RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., RA Sunagawa S., Plichta D., Gautier L., Le Chatelier E., Peletier E., RA Bonde I., Nielsen T., Manichanh C., Arumugam M., Batto J., RA Santos M.B.Q.D., Blom N., Borruel N., Burgdorf K.S., Boumezbeur F., RA Casellas F., Dore J., Guarner F., Hansen T., Hildebrand F., Kaas R.S., RA Kennedy S., Kristiansen K., Kultima J.R., Leonard P., Levenez F., RA Lund O., Moumen B., Le Paslier D., Pons N., Pedersen O., Prifti E., RA Qin J., Raes J., Tap J., Tims S., Ussery D.W., Yamada T., RA MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P., Wang J., RA Brunak S., Ehrlich S.D.; RT "Dependencies among metagenomic species, viruses, plasmids and units RT of genetic variation."; RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:CDF22262.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CBKM010000122; CDF22262.1; -; Genomic_DNA. DR Proteomes; UP000018057; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000018057}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000018057}. FT DOMAIN 216 400 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 426 AA; 48539 MW; 72A033ABB30BDF44 CRC64; MKEFIISEAQ AETAVLVALV TKTQNEQKTA EYLDELEFLA ETAGAVTIKR FTQKMDGPSS VTYVGKGKLE EIRAFIEQEE EQEREVGMVI FDDELSAKQL RNIEQALKVK ILDRTSLILD IFAMRAQTAN AKTQVELAQY RYMLPRLQRL WTHLERQGGG SGSGGGKGSV GLRGPGETQL EMDRRIILNR MSLLKQRLAD IDRQKTTQRK NRGRLIRVAL VGYTNVGKST LINLLAKTEV LAENKLFATL DTTVRKVIIE NLPFLLSDTV GFIRKIPTDL VDSFKSTLDE VREADLLLHV VDISHPDFGE QIEVVNRTLA DLGCAETPRL LIFNKIDAYQ WEPKDEDDLT PMTRRNISLE ELERTWMAKT SDECIFISAA KRQNIDALKK LLYKRIRQLH VQKYPYNDFL YPAPEDEDDS NDTSLQ // ID R7R5D5_9FIRM Unreviewed; 419 AA. AC R7R5D5; DT 24-JUL-2013, integrated into UniProtKB/TrEMBL. DT 24-JUL-2013, sequence version 1. DT 12-APR-2017, entry version 23. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=BN450_01544 {ECO:0000313|EMBL:CDF44925.1}; OS Roseburia sp. CAG:100. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Lachnospiraceae; OC Roseburia; environmental samples. OX NCBI_TaxID=1262940 {ECO:0000313|EMBL:CDF44925.1, ECO:0000313|Proteomes:UP000018092}; RN [1] {ECO:0000313|EMBL:CDF44925.1, ECO:0000313|Proteomes:UP000018092} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MGS:100 {ECO:0000313|Proteomes:UP000018092}; RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., RA Sunagawa S., Plichta D., Gautier L., Le Chatelier E., Peletier E., RA Bonde I., Nielsen T., Manichanh C., Arumugam M., Batto J., RA Santos M.B.Q.D., Blom N., Borruel N., Burgdorf K.S., Boumezbeur F., RA Casellas F., Dore J., Guarner F., Hansen T., Hildebrand F., Kaas R.S., RA Kennedy S., Kristiansen K., Kultima J.R., Leonard P., Levenez F., RA Lund O., Moumen B., Le Paslier D., Pons N., Pedersen O., Prifti E., RA Qin J., Raes J., Tap J., Tims S., Ussery D.W., Yamada T., RA MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P., Wang J., RA Brunak S., Ehrlich S.D.; RT "Dependencies among metagenomic species, viruses, plasmids and units RT of genetic variation."; RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:CDF44925.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CBKV010000120; CDF44925.1; -; Genomic_DNA. DR Proteomes; UP000018092; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000018092}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000018092}. FT DOMAIN 195 365 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 154 181 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 419 AA; 47189 MW; D8A03A8E1C8D0BBA CRC64; MERAFIVGVN LDGDSNFELS MDELASLAQA CEMEVVGRAE QNMEYANTAT YIGAGKVEEV RQAAEYLEAD IVIFDNALSP VQLRNLQREL DKPVMDRTTL ILEIFSTRAK TREAKLQVEV ARLQYMLPRL VGLHDALSRQ GGASGAMSNK GAGEKKLELD RRRLEQRLTN MKRELDLIAG ERRTQRQKRA RSGIPRVALV GYTNAGKSTI MNMLLGAYVK DEEKQVLEKD MLFATLDTTV RRIAPPDRNP FLLSDTVGFI SKLPHALVKA FHSTLEEAKE ADLLLQIIDY SDEHYREYMK VTEDTLRELG ADTIPMIYVF NKADKCGMGK FAMVQGEDKI FMSAKSMDGI DTLLTLIEGK LAGGYCDCEL LIPYTRGDIV SYLNDNAVVY QCDYREDGVY MHANLQVSDA GRYEKFILK // ID R7RSJ4_9CLOT Unreviewed; 601 AA. AC R7RSJ4; DT 24-JUL-2013, integrated into UniProtKB/TrEMBL. DT 24-JUL-2013, sequence version 1. DT 07-JUN-2017, entry version 28. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=TCEL_00402 {ECO:0000313|EMBL:CDF58356.1}; OS Thermobrachium celere DSM 8682. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Thermobrachium. OX NCBI_TaxID=941824 {ECO:0000313|EMBL:CDF58356.1, ECO:0000313|Proteomes:UP000014923}; RN [1] {ECO:0000313|EMBL:CDF58356.1, ECO:0000313|Proteomes:UP000014923} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 8682 {ECO:0000313|EMBL:CDF58356.1, RC ECO:0000313|Proteomes:UP000014923}; RA Ciranna A., Larjo A., Kivisto A., Santala V., Roos C., Karp M.; RT "Draft genome sequence of the hydrogen-ethanol-producing anaerobic RT alkalithermophilic Caloramator celere."; RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:CDF58356.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CAVN010000097; CDF58356.1; -; Genomic_DNA. DR RefSeq; WP_018662357.1; NZ_HF952018.1. DR EnsemblBacteria; CDF58356; CDF58356; TCEL_00402. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000014923; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000014923}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000014923}. FT DOMAIN 376 547 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 335 369 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 601 AA; 68075 MW; 99942196BBADBAD4 CRC64; MIYGNTEGIK KFYLDRLEAL YEFDCDKNIL VPMEVVSTIS EVSYSINREI AVYINRRGKI INILIGDNLT APLEFMSEKR SDRGLNGIRC IHTHLSEDAR LSTPDITALI DMKFDTMVAI SVVEGIPKSF SFGYLKIEEG QIKNEAYIEG PYSIDDINDV NFLELVTDLE KRIEYTAHEV KPSDKERVIL VGCKSDDGYS VEESLEELKE LAETAGAEVV YKVVQNKSKI DPAYFIGSGK AREIALLRQS LLADAVIFDD ELNGVQTRNL EETIGCKVID RTTLILDIFA QRAKSMEGKL QVELAQLKYR LPRLTGLGQM LSRTGGGIGT RGPGEKKLEI DKRHIRERIY DLEKELEKVK KNRSIQREKR KQNEIPVVAF VGYTNVGKST LRNKLCELYG KDKEKVLEAN MLFATLDTTT RIITLPSGRD VLFSDTVGFI RKLPHDLVEA FKSTLEEVVE SDLIVHVVDG SNENAIVQIE TVNKVLREIG AENKECILAI NKIDIAKEEN IHAIKAKYNN CVEISAIKEI NLDLLLKEVE LRIFSKIITE KLLIPYTEAR IVSALHELNC VKSEEYLEDG IEVVIETTED IINKYKKFLQ K // ID R7WP75_9NOCA Unreviewed; 507 AA. AC R7WP75; DT 24-JUL-2013, integrated into UniProtKB/TrEMBL. DT 24-JUL-2013, sequence version 1. DT 07-JUN-2017, entry version 29. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=Rrhod_1580 {ECO:0000313|EMBL:EOM77113.1}; OS Rhodococcus rhodnii LMG 5362. OC Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae; OC Rhodococcus. OX NCBI_TaxID=1273125 {ECO:0000313|EMBL:EOM77113.1, ECO:0000313|Proteomes:UP000013525}; RN [1] {ECO:0000313|EMBL:EOM77113.1, ECO:0000313|Proteomes:UP000013525} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=LMG 5362 {ECO:0000313|EMBL:EOM77113.1, RC ECO:0000313|Proteomes:UP000013525}; RX PubMed=23788540; RA Pachebat J.A., van Keulen G., Whitten M.M., Girdwood S., Del Sol R., RA Dyson P.J., Facey P.D.; RT "Draft Genome Sequence of Rhodococcus rhodnii Strain LMG5362, a RT Symbiont of Rhodnius prolixus (Hemiptera, Reduviidae, Triatominae), RT the Principle Vector of Trypanosoma cruzi."; RL Genome Announc. 1:e00329-13(2013). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EOM77113.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; APMY01000053; EOM77113.1; -; Genomic_DNA. DR EnsemblBacteria; EOM77113; EOM77113; Rrhod_1580. DR PATRIC; fig|1273125.3.peg.1525; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000013525; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 2. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000013525}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000013525}. FT DOMAIN 281 451 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 240 274 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 507 AA; 54049 MW; F611F1588AE5FEB1 CRC64; MTNTHAADAA TEPDAAADAG ASFSSDSSDR TAADAGPRVS RGGIAPSTGE MQLDDRGALR RVAGLSTELA DVTEVEYRQL RLERVVLVGV WTSGSAAQAD ASMAELAALA ETAGSEVLEG LVQRRDRPDA ATYIGSGKAE ELRAIVLATG ADTVICDGEL TPAQLTALER VVKVKVIDRT ALILDIFAQH ATSREGKAQV ALAQMEYMMP RLRGWGESMS RQAGGRAGSN GGVGLRGPGE TKIETDRRRI RERMAKLRRE IKAMKAARDT KRDRRVHGAT PNVAIVGYTN AGKSSLLNAL TGSGVLVQDA LFATLDPTSR RAKLDDGREY VLTDTVGFVR HLPTQLVEAF RSTLEEVTDA DLLMHVVDGS DALPTEQIKA VREVVTEVLR ESDAPPPPEL IVVNKIDAAD PTTITQLRGL LTGAVFVSAR TGEGIDELRA RLDDLLDRPD VEIDVVIPYT RGDLVARVHA EGRILESAHE GDGTHLRALV APPLAGVLAE FTGSPAR // ID R7XSE1_9ACTN Unreviewed; 495 AA. AC R7XSE1; DT 24-JUL-2013, integrated into UniProtKB/TrEMBL. DT 24-JUL-2013, sequence version 1. DT 07-JUN-2017, entry version 28. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=CF8_3885 {ECO:0000313|EMBL:EON22252.1}; OS Nocardioides sp. CF8. OC Bacteria; Actinobacteria; Propionibacteriales; Nocardioidaceae; OC Nocardioides. OX NCBI_TaxID=110319 {ECO:0000313|EMBL:EON22252.1, ECO:0000313|Proteomes:UP000015971}; RN [1] {ECO:0000313|EMBL:EON22252.1, ECO:0000313|Proteomes:UP000015971} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CF8 {ECO:0000313|EMBL:EON22252.1}; RX PubMed=23833136; RA Kimbrel J.A., Chang J., Arp D.J., Sayavedra-Soto L.A.; RT "The Draft Genome Sequence of Nocardioides sp. Strain CF8 Reveals the RT Scope of Its Metabolic Capabilities."; RL Genome Announc. 1:e00439-e00439(2013). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EON22252.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ASEP01000108; EON22252.1; -; Genomic_DNA. DR RefSeq; WP_010834669.1; NZ_CM001852.1. DR EnsemblBacteria; EON22252; EON22252; CF8_3885. DR PATRIC; fig|110319.3.peg.455; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000015971; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 2. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000015971}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000015971}. FT DOMAIN 277 442 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 243 270 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 495 AA; 53901 MW; 37660273D82EC386 CRC64; MTNAPDFNLD AALDATDDWD DLESGDADEL VSPDGPDPEE ELTTGEQDLA ERHALRRVDG LRTELEDITE VEYRQLRLEK VILVGVWTSG TVADAENSMA ELALLAETAG SEVLDAIYQR RQTPDPATFI GRGKVEGLFE IVQASGADTV ILDGDLAPSQ LRNLEDKLKV KAIDRTGLIL DIFAQHAKSK EGQAQVELAQ LNYMKQRLRG WGGNLSRQAG GRVSGGEGIG GRGPGETKIE TDRRRINTKI AKLRKELKEL KGTRATMRQE RSRNHIPSVS IAGYTNAGKS SILNRLTDAG VLVDDSLFAT LDPTTRRTTT KDGRVYTMSD TVGFVRHLPH QLVEAFRSTL EEVADSDLIL HVVDGSHPDP EGQLAAVREV FAEIHASKVP ELVLINKADA ADPMVIARLR AREPHSVVVS ARTGEGIDDA LAAIEAELPR PSVQFEALLP YERGDLLNRL HQQGEIESLE HTGDGTLVKG RANADLASDL AAYAV // ID R7ZYF4_9BACT Unreviewed; 425 AA. AC R7ZYF4; DT 24-JUL-2013, integrated into UniProtKB/TrEMBL. DT 24-JUL-2013, sequence version 1. DT 07-JUN-2017, entry version 31. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=ADIS_0356 {ECO:0000313|EMBL:EON79127.1}; OS Lunatimonas lonarensis. OC Bacteria; Bacteroidetes; Cytophagia; Cytophagales; Cyclobacteriaceae. OX NCBI_TaxID=1232681 {ECO:0000313|EMBL:EON79127.1, ECO:0000313|Proteomes:UP000013909}; RN [1] {ECO:0000313|EMBL:EON79127.1, ECO:0000313|Proteomes:UP000013909} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=AK24 {ECO:0000313|EMBL:EON79127.1, RC ECO:0000313|Proteomes:UP000013909}; RA Singh A.; RT "A novel strain isolated from Lonar lake, Maharashtra, India."; RL Submitted (FEB-2013) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EON79127.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AQHR01000015; EON79127.1; -; Genomic_DNA. DR RefSeq; WP_010852508.1; NZ_AQHR01000015.1. DR EnsemblBacteria; EON79127; EON79127; ADIS_0356. DR PATRIC; fig|1288963.3.peg.357; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000013909; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000013909}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000013909}. FT DOMAIN 210 399 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 425 AA; 48643 MW; 0C50FC91A55623CC CRC64; MSKYTRKIKK LIDTAPEQEK AILVALIHQQ DTDRLIQDHL DELALLTETL GATTVHRFTQ RLEKPDVKTF VGSGKLEEIK SYIEFFDVKI VIFDDDLSPS QMRNLENELK IKVYDRSLLI LDIFLQRAQT AQAKTQVELA RFQYLLPRLT RMWTHLERQR GGTSTRGGAG EKEIETDKRD IRAKITLLKE KLQKIEKQGI TQRKGREGIV RVAMVGYTNV GKSTLMRLMT KADVLAENKL FATVDSTVRK VVLDNFPFLL SDTVGFIRKL PTHLIESFKS TLAEIKEADL LVHVVDVSHP SFEDQINVVN QTLNELGAGD KPVILAFNKI DIAPKMPEEA EMMEMSEIEV EEAGYIDFEK LEQSYAKKSP IKPVFMAAES GLNVEEFRKV LTAEVLKIHQ KIYPHYLEDE VVDMSRFKEG EDEAY // ID R8AMA1_PLESH Unreviewed; 432 AA. AC R8AMA1; DT 24-JUL-2013, integrated into UniProtKB/TrEMBL. DT 24-JUL-2013, sequence version 1. DT 30-AUG-2017, entry version 29. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=PLESHI_15904 {ECO:0000313|EMBL:EON87460.1}; OS Plesiomonas shigelloides 302-73. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; OC unclassified Enterobacterales; Plesiomonas. OX NCBI_TaxID=1315976 {ECO:0000313|EMBL:EON87460.1, ECO:0000313|Proteomes:UP000014012}; RN [1] {ECO:0000313|EMBL:EON87460.1, ECO:0000313|Proteomes:UP000014012} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=302-73 {ECO:0000313|EMBL:EON87460.1, RC ECO:0000313|Proteomes:UP000014012}; RX PubMed=23814109; RA Pique N., Aquilini E., Alioto T., Minana-Galbis D., Tomas J.M.; RT "Genome Sequence of Plesiomonas shigelloides Strain 302-73 (Serotype RT O1)."; RL Genome Announc. 1:e00404-13(2013). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EON87460.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AQQO01000360; EON87460.1; -; Genomic_DNA. DR RefSeq; WP_010864771.1; NZ_KB944511.1. DR EnsemblBacteria; EON87460; EON87460; PLESHI_15904. DR PATRIC; fig|1315976.3.peg.3040; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000014012; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000014012}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000014012}. FT DOMAIN 198 365 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 432 AA; 48485 MW; 0BEA50F13351BB25 CRC64; MFDRYEAGEQ AILVHINFPQ ERDVEDLREF ETLVSSAGVT AVQVITGSRR APHSKYFVGE GKAEEIAAAV AATGASVILF NHALSPAQER NLEGLCQCRV IDRTGLILDI FAQRARTHEG KLQVELAQLR HLATRLVRGW THLERQKGGI GLRGPGETQL ETDRRLLKER VRVILSRLEK VAKQRQQGRR ARNRAEIPTV SLVGYTNAGK SSLFNTITEA GVYAADQLFA TLDPTLRRID VTDVGPVVLA DTVGFIRHLP HDLVSAFKAT LQETQEATLL LHVIDAADPR IDDNIQAVEH VLHEIEADEI PVLRVMNKID LIDEVVPRIA RNDEGVPTHV WVSAHTGAGM DLLFQAISEL LAQDIVEYQL HLSPRLWRLR SRLYQLDALV DERIDEEDGS LWLNIRMPAV DWRRLCKQET ELEATIHTEV SA // ID R8W1G3_9CLOT Unreviewed; 421 AA. AC R8W1G3; DT 24-JUL-2013, integrated into UniProtKB/TrEMBL. DT 24-JUL-2013, sequence version 1. DT 07-JUN-2017, entry version 29. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=HMPREF1526_01841 {ECO:0000313|EMBL:EOQ38800.1}; OS Butyricicoccus pullicaecorum 1.2. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Butyricicoccus. OX NCBI_TaxID=1203606 {ECO:0000313|EMBL:EOQ38800.1, ECO:0000313|Proteomes:UP000013981}; RN [1] {ECO:0000313|EMBL:EOQ38800.1, ECO:0000313|Proteomes:UP000013981} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=1.2 {ECO:0000313|EMBL:EOQ38800.1, RC ECO:0000313|Proteomes:UP000013981}; RG The Broad Institute Genome Sequencing Platform; RA Earl A., Ward D., Feldgarden M., Gevers D., Van Immerseel F., RA Eeckhaut V., Walker B., Young S.K., Zeng Q., Gargeya S., RA Fitzgerald M., Haas B., Abouelleil A., Alvarado L., Arachchi H.M., RA Berlin A.M., Chapman S.B., Dewar J., Goldberg J., Griggs A., Gujja S., RA Hansen M., Howarth C., Imamovic A., Larimer J., McCowan C., Murphy C., RA Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T., RA Sisk P., Sykes S., Wortman J., Nusbaum C., Birren B.; RT "The Genome Sequence of Butyricicoccus pullicaecorum 1.2."; RL Submitted (JAN-2013) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EOQ38800.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AQOB01000004; EOQ38800.1; -; Genomic_DNA. DR RefSeq; WP_016147977.1; NZ_KB976103.1. DR EnsemblBacteria; EOQ38800; EOQ38800; HMPREF1526_01841. DR PATRIC; fig|1203606.4.peg.1792; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000013981; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000013981}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000013981}. FT DOMAIN 206 365 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 165 199 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 421 AA; 46674 MW; 3269D825E74CAC3A CRC64; MMEMEFDKPK KERAVLVGLR CHSFGMDENA DEETLAELAA LVETAGAETV AMTLQTRPAP DARTFIGEGK AQEVKELAEA NEADLIIFDN ELSPSQMRVL EEMTDKTVLD RSALILDIFA QRARTGEGKL QVELAQYQYI LPRLAGLGHA MSRLGGGIGT RGPGESKLES DRRHIRRRID KLREDLEQVR QVRAVQRRQR KKTELPLVAI VGYTNAGKST LLNLLTDAGI EANDRLFDTL DPTTRKKRIS DTQEILLSDT VGFIRKLPHH LVSAFKATLE ELAYADLLLH VVDVSDPNWE IHAATVDKVI EQLGAQEIPR VMVYNKADKC DELPAARDGV LFSAKTGEGT EALLAAIEKA LGRGKHEMHL CIPYSDGAAL DVLHREGQVK SIEYGEAGTL VTVIVDDKLC GQMQKYRVEE A // ID R9B9Z8_9GAMM Unreviewed; 443 AA. AC R9B9Z8; DT 24-JUL-2013, integrated into UniProtKB/TrEMBL. DT 24-JUL-2013, sequence version 1. DT 30-AUG-2017, entry version 30. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=I593_00139 {ECO:0000313|EMBL:EOR11359.1}; OS Acinetobacter tandoii DSM 14970 = CIP 107469. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Moraxellaceae; Acinetobacter. OX NCBI_TaxID=1120927 {ECO:0000313|EMBL:EOR11359.1, ECO:0000313|Proteomes:UP000016201}; RN [1] {ECO:0000313|EMBL:EOR11359.1, ECO:0000313|Proteomes:UP000016201} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CIP 107469 {ECO:0000313|EMBL:EOR11359.1, RC ECO:0000313|Proteomes:UP000016201}; RG The Broad Institute Genome Sequencing Platform; RG The Broad Institute Genome Sequencing Center for Infectious Disease; RA Cerqueira G., Feldgarden M., Courvalin P., Perichon B., RA Grillot-Courvalin C., Clermont D., Rocha E., Yoon E.-J., Nemec A., RA Walker B., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B., RA Abouelleil A., Alvarado L., Arachchi H.M., Berlin A.M., Chapman S.B., RA Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M., Howarth C., RA Imamovic A., Larimer J., McCowan C., Murphy C., Neiman D., Pearson M., RA Priest M., Roberts A., Saif S., Shea T., Sisk P., Sykes S., RA Wortman J., Nusbaum C., Birren B.; RT "The Genome Sequence of Acinetobacter tandoii CIP 107469."; RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EOR11359.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AQFM01000005; EOR11359.1; -; Genomic_DNA. DR RefSeq; WP_016165399.1; NZ_KE007375.1. DR EnsemblBacteria; EOR11359; EOR11359; I593_00139. DR PATRIC; fig|1120927.3.peg.136; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000016201; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000016201}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000016201}. FT DOMAIN 199 364 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 443 AA; 49363 MW; 8B4BB9C0795C7A27 CRC64; MANLKRHQGG ERIILVSVSV QMLENLDAEE FNLLAQSAGA EILAHIHAQR VKPDAKLFIG SGKAEEIAEL VAEYEVDLVI FDHALTPAQA RNLEYILKCR VVDRNELILD IFAQRARTFE GKLQVELAQL QHLSSRLIRS RGTLDSQKGG IGLRGPGETL LETDRRLLKI RMGQLKAKLD KVRQTRLQGR VARQKAAVPT VSLVGYTNAG KSTLFNVLAN SDVYAADQLF ATLDPTLRRL SWEGIGTVVL ADTVGFVRNL SHSLVESFKA TLEETLEATL LLHVIDSSSS EMLEQIEAVE KVLKEIGADV PVLRVYNKID QSAEDAKIVY SQPNCPERVY VSAHTGQGIE LLQQAVHECL MGQIQNFDLT LKPAYGKLRT QLYTLNVIQS EHYDDEGNLH LNVKIAPAKL EQLIRQAHLP LDQILGEKAA LFERTLEEFE IKS // ID R9GNJ0_9SPHI Unreviewed; 392 AA. AC R9GNJ0; DT 24-JUL-2013, integrated into UniProtKB/TrEMBL. DT 24-JUL-2013, sequence version 1. DT 07-JUN-2017, entry version 27. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=ADIARSV_3750 {ECO:0000313|EMBL:EOR93090.1}; OS Arcticibacter svalbardensis MN12-7. OC Bacteria; Bacteroidetes; Sphingobacteriia; Sphingobacteriales; OC Sphingobacteriaceae; Arcticibacter. OX NCBI_TaxID=1150600 {ECO:0000313|EMBL:EOR93090.1, ECO:0000313|Proteomes:UP000014174}; RN [1] {ECO:0000313|EMBL:EOR93090.1, ECO:0000313|Proteomes:UP000014174} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MN12-7 {ECO:0000313|EMBL:EOR93090.1, RC ECO:0000313|Proteomes:UP000014174}; RX PubMed=23846277; RA Shivaji S., Ara S., Prasad S., Manasa B.P., Begum Z., Singh A., RA Kumar Pinnaka A.; RT "Draft Genome Sequence of Arcticibacter svalbardensis Strain MN12-7T, RT a Member of the Family Sphingobacteriaceae Isolated from an Arctic RT Soil Sample."; RL Genome Announc. 1:E00484-13(2013). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EOR93090.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AQPN01000130; EOR93090.1; -; Genomic_DNA. DR RefSeq; WP_016196975.1; NZ_AQPN01000130.1. DR EnsemblBacteria; EOR93090; EOR93090; ADIARSV_3750. DR PATRIC; fig|1150600.3.peg.3717; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000014174; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000014174}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000014174}. FT DOMAIN 204 381 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 392 AA; 44685 MW; 7BA75EDB2DC9F0C7 CRC64; MPRQESFDTT IKQERAVLVG VITQGESEAK VQEYLEELEF LVDTAGGITE KIFTQKITTA DRATFVGKGK LEEIQAYVRS EEIDLVVFDD ELTPSQIRNI ENELEVKILD RSNLILDIFA SRAQTAQAKA QVELAQLQYL LPRLTRLWTH LERQKGGIGM RGPGESQIES DRRIIQTKIS ILKEKLKLID KQNGTQRKNR GQLIRVALVG YTNVGKSTIM NMLSKSDVFA ENKLFATLDT TVRKVVIDNL PFLLSDTVGF IRKLPVHLVE CFKSTLDEVR EADILMHVVD ISHPNFEDQI RIVNETLKEL GVADKKTITV FNKIDAWKSE SGQEAESLTL DDFRNSWMGK HNSPAVFISA LNKENLEELK QLVYEQTKAM HTVRYPYDNL LY // ID R9IWY4_9FIRM Unreviewed; 425 AA. AC R9IWY4; DT 24-JUL-2013, integrated into UniProtKB/TrEMBL. DT 24-JUL-2013, sequence version 1. DT 07-JUN-2017, entry version 29. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=C806_01031 {ECO:0000313|EMBL:EOS26296.1}; OS Lachnospiraceae bacterium 3-1. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Lachnospiraceae. OX NCBI_TaxID=397288 {ECO:0000313|EMBL:EOS26296.1, ECO:0000313|Proteomes:UP000014188}; RN [1] {ECO:0000313|EMBL:EOS26296.1, ECO:0000313|Proteomes:UP000014188} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=3-1 {ECO:0000313|EMBL:EOS26296.1, RC ECO:0000313|Proteomes:UP000014188}; RG The Broad Institute Genomics Platform; RG The Broad Institute Genome Sequencing Center for Infectious Disease; RA Earl A., Xavier R., Elson C., Duck W., Walker B., Young S., Zeng Q., RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., RA Alvarado L., Arachchi H.M., Berlin A.M., Chapman S.B., RA Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M., RA Howarth C., Imamovic A., Ireland A., Larimer J., McCowan C., RA Murphy C., Pearson M., Poon T.W., Priest M., Roberts A., Saif S., RA Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C., Birren B.; RT "The Genome Sequence of Lachnospiraceae bacterium 3-1."; RL Submitted (APR-2013) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EOS26296.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ASST01000006; EOS26296.1; -; Genomic_DNA. DR RefSeq; WP_016286081.1; NZ_KE159582.1. DR EnsemblBacteria; EOS26296; EOS26296; C806_01031. DR PATRIC; fig|397288.3.peg.1119; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000014188; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000014188}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000014188}. FT DOMAIN 202 366 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 425 AA; 47801 MW; 144396C84B5E31ED CRC64; MSESLKIEEI IEQVVLVGVS QQENDDDEDS LTELAELAET AGAQVVGMTI QNRESVHPGT YVGKGKLQEL RQMVLELEAT GIICDDELSP AQLRNMEEIL ECKVMDRTLV ILDIFASRAS TSEGKIQVEL AQLKYRMSRL IGLGISMSRL GGGIGTRGPG EKKLEMDRRL IKSRIAQLNR ELSQVQMHRE VNRGQRERSQ VKVAAIVGYT NAGKSTLLNR LTHASVLEED KLFATLDPTT RNLKLGSGQE ILLTDTVGFI RKLPHHLIEA FRSTLEEAKY ADIIIHVVDS SNPQREKQMH IVYETLQNLG VSGKKMITLF NKQDQVEEDA VGKDAKADKT LKISAKTGEG LEQLLEVLEE ILREDKQFLE GIFPYDKGGQ LTVIRKYGEL LEEEYRENGI YVKAFVPVEL YKNLEVNLEK VPKRE // ID R9JDX7_9FIRM Unreviewed; 421 AA. AC R9JDX7; DT 24-JUL-2013, integrated into UniProtKB/TrEMBL. DT 24-JUL-2013, sequence version 1. DT 07-JUN-2017, entry version 30. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=C807_00646 {ECO:0000313|EMBL:EOS32415.1}; OS Lachnospiraceae bacterium 28-4. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Lachnospiraceae. OX NCBI_TaxID=397287 {ECO:0000313|EMBL:EOS32415.1, ECO:0000313|Proteomes:UP000014112}; RN [1] {ECO:0000313|EMBL:EOS32415.1, ECO:0000313|Proteomes:UP000014112} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=28-4 {ECO:0000313|EMBL:EOS32415.1, RC ECO:0000313|Proteomes:UP000014112}; RG The Broad Institute Genomics Platform; RG The Broad Institute Genome Sequencing Center for Infectious Disease; RA Earl A., Xavier R., Elson C., Duck W., Walker B., Young S., Zeng Q., RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., RA Alvarado L., Arachchi H.M., Berlin A.M., Chapman S.B., RA Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M., RA Howarth C., Imamovic A., Ireland A., Larimer J., McCowan C., RA Murphy C., Pearson M., Poon T.W., Priest M., Roberts A., Saif S., RA Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C., Birren B.; RT "The Genome Sequence of Lachnospiraceae bacterium 28-4."; RL Submitted (APR-2013) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EOS32415.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ASSU01000009; EOS32415.1; -; Genomic_DNA. DR RefSeq; WP_016290455.1; NZ_KE159598.1. DR EnsemblBacteria; EOS32415; EOS32415; C807_00646. DR PATRIC; fig|397287.3.peg.698; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000014112; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000014112}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000014112}. FT DOMAIN 198 367 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 157 191 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 421 AA; 48083 MW; 5716B8E195B1B3EF CRC64; MEEKEKAILV GADTGEDENF ERSMEELGEL ARACGMSVEG TVTQKMDSIN KAFYIGTGKV QEVREYAEAL EADIILFDNS LTPSQLRNLQ KETGKPVMDR TAVILDIFSN RARTREAKLQ VETARLQYLM SRLVGMHDAL TRQGGASGSM SSKGAGEKKL ELDRRKIEKR LAQLRRELEE VEKERENQSK RRAGSRIPKV SLVGYTNAGK STLMNAMIDR YMQDEEKKVL EKDMLFATLD TTVRNIDMGN RREILLADTV GFIHKLPHGL VKAFRSTLEE VKNADLLLYV VDYSDQEYQQ QIKVTEKTLL EIGAADIPVI YVYNKADLCD MEQIPRVMND KIYMSARTSQ GLEELAQMIV EKVYADYVQT EFLFPYNRGG ETAYFMDHAQ VLEQEYMENG IRLKVNCHRA DIGKYEEFLV K // ID R9JNQ9_9FIRM Unreviewed; 431 AA. AC R9JNQ9; DT 24-JUL-2013, integrated into UniProtKB/TrEMBL. DT 24-JUL-2013, sequence version 1. DT 07-JUN-2017, entry version 29. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=C804_00838 {ECO:0000313|EMBL:EOS35636.1}; OS Lachnospiraceae bacterium A4. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Lachnospiraceae. OX NCBI_TaxID=397291 {ECO:0000313|EMBL:EOS35636.1, ECO:0000313|Proteomes:UP000014118}; RN [1] {ECO:0000313|EMBL:EOS35636.1, ECO:0000313|Proteomes:UP000014118} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=A4 {ECO:0000313|EMBL:EOS35636.1, RC ECO:0000313|Proteomes:UP000014118}; RG The Broad Institute Genomics Platform; RG The Broad Institute Genome Sequencing Center for Infectious Disease; RA Earl A., Xavier R., Elson C., Duck W., Walker B., Young S., Zeng Q., RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., RA Alvarado L., Arachchi H.M., Berlin A.M., Chapman S.B., RA Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M., RA Howarth C., Imamovic A., Ireland A., Larimer J., McCowan C., RA Murphy C., Pearson M., Poon T.W., Priest M., Roberts A., Saif S., RA Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C., Birren B.; RT "The Genome Sequence of Lachnospiraceae bacterium A4."; RL Submitted (APR-2013) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EOS35636.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ASSR01000021; EOS35636.1; -; Genomic_DNA. DR RefSeq; WP_016279548.1; NZ_KE159538.1. DR EnsemblBacteria; EOS35636; EOS35636; C804_00838. DR PATRIC; fig|397291.3.peg.876; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000014118; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000014118}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000014118}. FT DOMAIN 198 368 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 157 191 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 431 AA; 48523 MW; 151CA4DC91DE814A CRC64; MDKVLIVGVN FTTEHKSQHF DLAMEEMASL VKACDMEPVG RIEQNMESAN TATYIGAGKV QEVREMVRAL EADLVVFDNG LSPIQLRNLS RDLDCPVMDR TTLILEIFSA RAKTREAKLQ VEVARLQYML PRLVGLHDAL SRQGGASGAM SNKGAGEKKL ELDRRRLEQR LTTMRRELEK ISGERETQRK KRAASGIPRV ALVGYTNAGK STVMNAMLSA YDGEGEKMVY EEDMLFATLD TTVRRITPPD QNDFLLSDTV GFISNLPHNL VKAFRSTLEE VREADLLIQV IDYSDENYTE HIRVTEETLK DLGAERIPMI YAYNKADLCG MGAFATIQGD DRLYLSAKSQ SGIDALMTLI SGKLSKRYQD CAFIIPYQRG DVVSYLNDNA VIHCTEYRED GVYMETNVSR IDAARYEQFL VNCYERLPGC E // ID R9JQZ2_9FIRM Unreviewed; 415 AA. AC R9JQZ2; DT 24-JUL-2013, integrated into UniProtKB/TrEMBL. DT 24-JUL-2013, sequence version 1. DT 07-JUN-2017, entry version 29. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=C808_04240 {ECO:0000313|EMBL:EOS36356.1}; OS Lachnospiraceae bacterium M18-1. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Lachnospiraceae. OX NCBI_TaxID=1235792 {ECO:0000313|EMBL:EOS36356.1, ECO:0000313|Proteomes:UP000014090}; RN [1] {ECO:0000313|EMBL:EOS36356.1, ECO:0000313|Proteomes:UP000014090} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=M18-1 {ECO:0000313|EMBL:EOS36356.1, RC ECO:0000313|Proteomes:UP000014090}; RG The Broad Institute Genomics Platform; RG The Broad Institute Genome Sequencing Center for Infectious Disease; RA Earl A., Xavier R., Elson C., Duck W., Walker B., Young S., Zeng Q., RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., RA Alvarado L., Arachchi H.M., Berlin A.M., Chapman S.B., RA Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M., RA Howarth C., Imamovic A., Ireland A., Larimer J., McCowan C., RA Murphy C., Pearson M., Poon T.W., Priest M., Roberts A., Saif S., RA Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C., Birren B.; RT "The Genome Sequence of Lachnospiraceae bacterium M18-1."; RL Submitted (APR-2013) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EOS36356.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ASSV01000037; EOS36356.1; -; Genomic_DNA. DR RefSeq; WP_016297672.1; NZ_KE159611.1. DR EnsemblBacteria; EOS36356; EOS36356; C808_04240. DR PATRIC; fig|1235792.3.peg.4591; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000014090; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000014090}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000014090}. FT DOMAIN 201 365 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 160 197 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 415 AA; 46515 MW; 2001F277F351A1C8 CRC64; MELYELKQEE ERFILVGIQL GDNEPAEESL DELEALAKTA GAAAAGRLIQ NREAMHPQTY IGKGKIEELK DLIWEQDASG IICDDELSAV QLNNLQQELE CKVIDRTLLI LDIFAAHAVS GEGKIQVELA QLRYRSARLT GLGNSLSRLG GGIGTRGPGE KKLEMDRRLI RERISRLKRE LKEVEQHREL IRAQRKRSNM KVAALVGYTS AGKSSMENAL TDAGIPEDAM LFSTLDTTTR VLELEGKQKI LLTDTVGFIR KLPHHLIEAF KSTLEEVKYA DIMIHVVDAS NPQMDTQMHV VYETLRQLGA EGKPVITLFN KQDLLAEPGH FRDLQAEYTI PVSAKTGQGL EELKRGLSEI LRKDQVYIER LYPFEDAGKV QVIRGSGQLL EEEYVPEGIA VKAYVPKEIY LSGRI // ID R9KI21_9FIRM Unreviewed; 423 AA. AC R9KI21; DT 24-JUL-2013, integrated into UniProtKB/TrEMBL. DT 24-JUL-2013, sequence version 1. DT 07-JUN-2017, entry version 29. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=C810_02035 {ECO:0000313|EMBL:EOS45938.1}; OS Lachnospiraceae bacterium A2. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Lachnospiraceae. OX NCBI_TaxID=397290 {ECO:0000313|EMBL:EOS45938.1, ECO:0000313|Proteomes:UP000014150}; RN [1] {ECO:0000313|EMBL:EOS45938.1, ECO:0000313|Proteomes:UP000014150} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=A2 {ECO:0000313|EMBL:EOS45938.1, RC ECO:0000313|Proteomes:UP000014150}; RG The Broad Institute Genomics Platform; RG The Broad Institute Genome Sequencing Center for Infectious Disease; RA Earl A., Xavier R., Elson C., Duck W., Walker B., Young S., Zeng Q., RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., RA Alvarado L., Arachchi H.M., Berlin A.M., Chapman S.B., RA Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M., RA Howarth C., Imamovic A., Ireland A., Larimer J., McCowan C., RA Murphy C., Pearson M., Poon T.W., Priest M., Roberts A., Saif S., RA Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C., Birren B.; RT "The Genome Sequence of Lachnospiraceae bacterium A2."; RL Submitted (APR-2013) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EOS45938.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ASSX01000009; EOS45938.1; -; Genomic_DNA. DR RefSeq; WP_016305178.1; NZ_KE159636.1. DR EnsemblBacteria; EOS45938; EOS45938; C810_02035. DR PATRIC; fig|397290.3.peg.2236; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000014150; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000014150}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000014150}. FT DOMAIN 202 366 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 423 AA; 47078 MW; DD5F29AF5092E1C4 CRC64; MPEPLKIEEV TERVILVGVS LQENDDTEDS LAELGELAET AGALVVGSAI QNRESVHPGT YVGKGKLQEL RQLAAELDAT GIICDDELSP AQLRNMEDAL ECKVMDRTLV ILDIFAARAS TSEGKIQVEL AQLKYRLGRL AGLGTSLSRL GGGIGTRGPG EKKLEMDRRL IKNRISQLNR ELSQVKMHRE VTRSQRERSQ VKVAAIVGYT NAGKSTLLNH LTHASVLEED KLFATLDPTT RNLKLDSGQE LLLTDTVGFI RKLPHHLIEA FRSTLEEAKY ADIIIHVVDS SNPQREKQMY IVYETLRNLG VSGKKTITLF NKQDKLVENE ILKDAYADKT LKISARTGEG MPQLLEALEE FLREDKQLLE GIFPYGKGSQ VSQIRKYGEL LEEDYRENGI YVKAFVPTEL YHNLGKGMCS SGS // ID R9L7M4_9FIRM Unreviewed; 422 AA. AC R9L7M4; DT 24-JUL-2013, integrated into UniProtKB/TrEMBL. DT 24-JUL-2013, sequence version 1. DT 07-JUN-2017, entry version 29. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=C809_01203 {ECO:0000313|EMBL:EOS51742.1}; OS Lachnospiraceae bacterium COE1. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Lachnospiraceae. OX NCBI_TaxID=1235793 {ECO:0000313|EMBL:EOS51742.1, ECO:0000313|Proteomes:UP000014081}; RN [1] {ECO:0000313|EMBL:EOS51742.1, ECO:0000313|Proteomes:UP000014081} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=COE1 {ECO:0000313|EMBL:EOS51742.1, RC ECO:0000313|Proteomes:UP000014081}; RG The Broad Institute Genomics Platform; RG The Broad Institute Genome Sequencing Center for Infectious Disease; RA Earl A., Xavier R., Elson C., Duck W., Walker B., Young S., Zeng Q., RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., RA Alvarado L., Arachchi H.M., Berlin A.M., Chapman S.B., RA Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M., RA Howarth C., Imamovic A., Ireland A., Larimer J., McCowan C., RA Murphy C., Pearson M., Poon T.W., Priest M., Roberts A., Saif S., RA Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C., Birren B.; RT "The Genome Sequence of Lachnospiraceae bacterium COE1."; RL Submitted (APR-2013) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EOS51742.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ASSW01000016; EOS51742.1; -; Genomic_DNA. DR RefSeq; WP_016299917.1; NZ_KE159617.1. DR EnsemblBacteria; EOS51742; EOS51742; C809_01203. DR PATRIC; fig|1235793.3.peg.1246; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000014081; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000014081}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000014081}. FT DOMAIN 199 369 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 158 192 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 422 AA; 47056 MW; ED05E900B738C3EC CRC64; MERALIVGVN INGEKKSSAA FGLAMDEMIS LVKACDMQPV GRIEQNMEHA NTATYIGAGK VEEVRETAAQ LEADLVVFDN GLSPIQLRNL QRELNCPVID RTTLILEIFS SRAQTREAKL QVEVARLQYM LPRLVGLHAA LSRQGGASGA MSNKGAGEKK LELDRRRLEQ RLTSMKRELE EISGERRTQR KKRAESGLPR VTLVGYTNAG KSTVMNMLLS AYVDKEEKQV LEKDMLFATL DTTVRRIAPP DKNAFLLSDT VGFISNLPHS LVKAFRSTLE EVREADLLLQ IIDYSDENHR EHMRVTADTL RELGAGNVPM LYVFNKVDLC GMGTFASVQG DDKIYMSAKS QNGIDALLTL IAGKLSGGYR DCTFLLPYQR GDIVSYLKEN AVVFATEYRE EGVYMEANVT VRDAGKFQEY LL // ID R9LPZ7_9FIRM Unreviewed; 405 AA. AC R9LPZ7; DT 24-JUL-2013, integrated into UniProtKB/TrEMBL. DT 24-JUL-2013, sequence version 1. DT 07-JUN-2017, entry version 27. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=C815_01401 {ECO:0000313|EMBL:EOS60411.1}; OS Firmicutes bacterium M10-2. OC Bacteria; Firmicutes. OX NCBI_TaxID=1235796 {ECO:0000313|EMBL:EOS60411.1, ECO:0000313|Proteomes:UP000014154}; RN [1] {ECO:0000313|EMBL:EOS60411.1, ECO:0000313|Proteomes:UP000014154} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=M10-2 {ECO:0000313|EMBL:EOS60411.1, RC ECO:0000313|Proteomes:UP000014154}; RG The Broad Institute Genomics Platform; RG The Broad Institute Genome Sequencing Center for Infectious Disease; RA Earl A., Xavier R., Elson C., Duck W., Walker B., Young S., Zeng Q., RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., RA Alvarado L., Arachchi H.M., Berlin A.M., Chapman S.B., RA Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M., RA Howarth C., Imamovic A., Ireland A., Larimer J., McCowan C., RA Murphy C., Pearson M., Poon T.W., Priest M., Roberts A., Saif S., RA Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C., Birren B.; RT "The Genome Sequence of Firmicutes bacterium M10-2."; RL Submitted (APR-2013) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EOS60411.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ASTB01000028; EOS60411.1; -; Genomic_DNA. DR RefSeq; WP_016319463.1; NZ_KE159696.1. DR EnsemblBacteria; EOS60411; EOS60411; C815_01401. DR PATRIC; fig|1235796.3.peg.1410; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000014154; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000014154}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000014154}. FT DOMAIN 188 314 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 405 AA; 46656 MW; B49699C1572A90C1 CRC64; MNAILIFCKS ENEEQKSEMY DLLKTADITI LHTFFQNVRS ISKATYIGQG KCEEIACYLR DEPNIQSVIF SCELSVMQVR ELEKIFDLQV LDRTDLILQI FLTRARSAAA RLQIESALLK RQMNRLIGTN VHLTRQRAGV TNRGSGEKQL QLDRRLIKTR MIQIQKELKK LDKQRMTQRS SRLRSNLPIV ALAGYTNAGK STIMNGLLDF SKASNYKQVL QEDLLFATLD TSVRLIELPY GQSFLLVDTV GFLQNLPHEL VQAFHSTLED IKMAQLILQV IDASSSQYLE NIDTTNQTLE EIDAANIPRL LIYNQCDKTD IHHPTIHHEN MYISALCEND CAFLCEQICQ NLFGPWCEID LYIPFNDFSL QQKVRKYTCI QSQKNDENGT RIHGKVRKRF KLNLI // ID R9M401_9FIRM Unreviewed; 418 AA. AC R9M401; DT 24-JUL-2013, integrated into UniProtKB/TrEMBL. DT 24-JUL-2013, sequence version 1. DT 07-JUN-2017, entry version 29. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=C814_00042 {ECO:0000313|EMBL:EOS65563.1}; OS Anaerotruncus sp. G3(2012). OC Bacteria; Firmicutes; Clostridia; Clostridiales; Ruminococcaceae; OC Anaerotruncus. OX NCBI_TaxID=1235835 {ECO:0000313|EMBL:EOS65563.1, ECO:0000313|Proteomes:UP000014129}; RN [1] {ECO:0000313|EMBL:EOS65563.1, ECO:0000313|Proteomes:UP000014129} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=G3(2012) {ECO:0000313|Proteomes:UP000014129}; RG The Broad Institute Genomics Platform; RG The Broad Institute Genome Sequencing Center for Infectious Disease; RA Earl A., Xavier R., Elson C., Duck W., Walker B., Young S., Zeng Q., RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., RA Alvarado L., Arachchi H.M., Berlin A.M., Chapman S.B., RA Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M., RA Howarth C., Imamovic A., Ireland A., Larimer J., McCowan C., RA Murphy C., Pearson M., Poon T.W., Priest M., Roberts A., Saif S., RA Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C., Birren B.; RT "The Genome Sequence of Anaerotruncus bacterium G3."; RL Submitted (APR-2013) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EOS65563.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ASTA01000002; EOS65563.1; -; Genomic_DNA. DR RefSeq; WP_016314766.1; NZ_KE159657.1. DR EnsemblBacteria; EOS65563; EOS65563; C814_00042. DR PATRIC; fig|1235835.3.peg.50; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000014129; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000014129}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000014129}. FT DOMAIN 199 360 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 165 192 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 418 AA; 45449 MW; 5294C21976E7FE03 CRC64; MIETTENKPQ RVVLIAADTG EFDLEVSLAE LEELAATAGA EVVAKMTQKR AAFEAATVIG KGRLEEAAAF CKDHQIDLLI FDHELSPAQV RNIEQLCDVA VIDRTALILD IFAQRAVTAE GKLQVELAQL RYQLPRLAGL GSVLSRLGGG IGTRGPGESQ LETDRRHIRR GITALQEQLA ELEKRRGLLR SRRKKDGVTT VAIVGYTNVG KSTLLNALTD AGVLAENKLF ATLDPTSRAL TLPDGRTVML VDTVGLVRRL PHHLVEAFKS TLEEAAGADL LWNVCDISSG EADEQIAVTK KLMQELGAQE IPMLTVLNKC DLVSEAPLPI NDQTALISAR TGFGFDALLQ KTAKALAPTH KRLTLLIPYS KTGLINEIMQ EGKVFSQAYE ADGTLVDALV DCKLLHKVAE YAQHQQHT // ID R9M7M2_9FIRM Unreviewed; 423 AA. AC R9M7M2; DT 24-JUL-2013, integrated into UniProtKB/TrEMBL. DT 24-JUL-2013, sequence version 1. DT 07-JUN-2017, entry version 29. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=C816_00842 {ECO:0000313|EMBL:EOS66696.1}; OS Oscillibacter sp. 1-3. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Oscillospiraceae; OC Oscillibacter. OX NCBI_TaxID=1235797 {ECO:0000313|EMBL:EOS66696.1, ECO:0000313|Proteomes:UP000014108}; RN [1] {ECO:0000313|EMBL:EOS66696.1, ECO:0000313|Proteomes:UP000014108} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=1-3 {ECO:0000313|EMBL:EOS66696.1, RC ECO:0000313|Proteomes:UP000014108}; RG The Broad Institute Genomics Platform; RG The Broad Institute Genome Sequencing Center for Infectious Disease; RA Earl A., Xavier R., Elson C., Duck W., Walker B., Young S., Zeng Q., RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., RA Alvarado L., Arachchi H.M., Berlin A.M., Chapman S.B., RA Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M., RA Howarth C., Imamovic A., Ireland A., Larimer J., McCowan C., RA Murphy C., Pearson M., Poon T.W., Priest M., Roberts A., Saif S., RA Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C., Birren B.; RT "The Genome Sequence of Oscillibacter bacterium 1-3."; RL Submitted (APR-2013) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EOS66696.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ASTC01000006; EOS66696.1; -; Genomic_DNA. DR RefSeq; WP_016321166.1; NZ_KE159703.1. DR EnsemblBacteria; EOS66696; EOS66696; C816_00842. DR PATRIC; fig|1235797.3.peg.918; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000014108; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000014108}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000014108}. FT DOMAIN 208 370 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 167 201 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 423 AA; 47161 MW; 185E9035B8B19E35 CRC64; MRQTEEIRDK VVLVGLNSPV LKKEENASEE TMEELSALVE TAGGETVGIV LQNRPAPDPR TFIGEGKVAE VQLYCENVEA TMVIFDNDLS PSQQRVLTDL LGVQVLDRCG LILDIFAQRA QTKEGRLQVE LAQYRYLLPR LTGMWTHLER QAGTSGKGPI GSKGPGETQL ETDRRHIRRK IDKLREDLED VRRVRGTQRQ QRRKNEIPVA AIVGYTNAGK STLLNRLTGA GIPANNRLFD TLDTTSRLLA VNDTLDVVLS DTVGFIRKLP HQLVEAFKAT LEELEYADLL LHVIDVSNPE WQLQAQVVES LIAELGAGEL PRIDVFNKYD RLPVGEIMPH GEDICAISAK TGEGVDRLLE LIGRKLDKGV RRVVLRIPYD KGGLVDTLYR EAKVENVEYG ETIVVTAVCG PRTLGRMEPF IVE // ID R9MAX0_9FIRM Unreviewed; 434 AA. AC R9MAX0; DT 24-JUL-2013, integrated into UniProtKB/TrEMBL. DT 24-JUL-2013, sequence version 1. DT 07-JUN-2017, entry version 29. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=C818_03961 {ECO:0000313|EMBL:EOS67796.1}; OS Lachnospiraceae bacterium 3-2. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Lachnospiraceae. OX NCBI_TaxID=1235799 {ECO:0000313|EMBL:EOS67796.1, ECO:0000313|Proteomes:UP000014117}; RN [1] {ECO:0000313|EMBL:EOS67796.1, ECO:0000313|Proteomes:UP000014117} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=3-2 {ECO:0000313|EMBL:EOS67796.1, RC ECO:0000313|Proteomes:UP000014117}; RG The Broad Institute Genomics Platform; RG The Broad Institute Genome Sequencing Center for Infectious Disease; RA Earl A., Xavier R., Elson C., Duck W., Walker B., Young S., Zeng Q., RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., RA Alvarado L., Arachchi H.M., Berlin A.M., Chapman S.B., RA Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M., RA Howarth C., Imamovic A., Ireland A., Larimer J., McCowan C., RA Murphy C., Pearson M., Poon T.W., Priest M., Roberts A., Saif S., RA Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C., Birren B.; RT "The Genome Sequence of Lachnospiraceae bacterium 3-2."; RL Submitted (APR-2013) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EOS67796.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ASTE01000044; EOS67796.1; -; Genomic_DNA. DR RefSeq; WP_016226288.1; NZ_KE159798.1. DR EnsemblBacteria; EOS67796; EOS67796; C818_03961. DR PATRIC; fig|1235799.3.peg.4135; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000014117; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000014117}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000014117}. FT DOMAIN 199 363 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 434 AA; 48242 MW; 3931F677FFC54855 CRC64; MIEIGKETER VVVAGVCTFN MEDTGHLLDE LSELAQTAGA ETVGRIIQSR EQAHPATYLG KGKIEELKDL LWETSSTGVV CDDELSPVQM KNLQDMLDVK VMDRTLLILD IFAARAATSE GKIQVELAQL KYRQTRLTGF GTALSRLGGG IGTRGPGEKK LEMDRRLIKN RIAQLNRELK GIKCHREVAR GQRRKSRIPV VAIVGYTNAG KSTLHNKLTG AQILMEDKLF ATLDPTTRNL KLPGGQEVLL TDTVGFIRKL PHHLVEAFKS TLEEAKYADV ILHVVDASNP QMDEQMHTVY ETLRSLEVGR KPVVTVFNKQ DRISGEEILR DFQADCTVKA SAKTGEGLSE LLEALEAVLR EQKIAVECVY DYRDTAKIQL IRKYGELIEE DYREDGIFVR GYVPADVWGK AAPSGVPAHH GEDAAPGDSE NRRR // ID R9N5Q3_9FIRM Unreviewed; 430 AA. AC R9N5Q3; DT 24-JUL-2013, integrated into UniProtKB/TrEMBL. DT 24-JUL-2013, sequence version 1. DT 07-JUN-2017, entry version 29. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=C819_00244 {ECO:0000313|EMBL:EOS78644.1}; OS Lachnospiraceae bacterium 10-1. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Lachnospiraceae. OX NCBI_TaxID=1235800 {ECO:0000313|EMBL:EOS78644.1, ECO:0000313|Proteomes:UP000014134}; RN [1] {ECO:0000313|EMBL:EOS78644.1, ECO:0000313|Proteomes:UP000014134} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=10-1 {ECO:0000313|EMBL:EOS78644.1, RC ECO:0000313|Proteomes:UP000014134}; RG The Broad Institute Genomics Platform; RG The Broad Institute Genome Sequencing Center for Infectious Disease; RA Earl A., Xavier R., Elson C., Duck W., Walker B., Young S., Zeng Q., RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., RA Alvarado L., Arachchi H.M., Berlin A.M., Chapman S.B., RA Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M., RA Howarth C., Imamovic A., Ireland A., Larimer J., McCowan C., RA Murphy C., Pearson M., Poon T.W., Priest M., Roberts A., Saif S., RA Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C., Birren B.; RT "The Genome Sequence of Lachnospiraceae bacterium 10-01."; RL Submitted (APR-2013) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EOS78644.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ASTF01000001; EOS78644.1; -; Genomic_DNA. DR EnsemblBacteria; EOS78644; EOS78644; C819_00244. DR PATRIC; fig|1235800.3.peg.250; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000014134; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000014134}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000014134}. FT DOMAIN 206 377 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 165 199 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 430 AA; 48869 MW; C759FC272620E79E CRC64; MEKQEKNQMQ EMEKVLLVGA DDGSEKDFDR SMEELADLAR ACFMEPVGVI TQKLETINKG LYIGAGKVQE VKEAAELLMA DVVIFDDALT PSQIRNLQKE IGKPILDRTT LILDIFETRA RTREAKLQVE SARLKYLLPR LVGMHEALTR QGGTSGSMSS RGAGEKKLEL DRRRIEHRIS ELSGELKEIS KERQIQRKKR HESRIPLVAL VGYTNAGKST IMNGMIDKYK LDEEKKVLEE DMLFATLDTT VRRICTGNNR DFLLSDTVGF IHKLPHDLVE AFHSTLEEIE SADLLVHVVD YSDPFYLEQM HTTRQTLSEL HAGEIPVITV LNKADKCESE VSFPKAAGED KIYLSAREET SICMLADMIL DKVYADYRTE TFLIPYSQGS VVSYFMENTH IISKEYKEKG TCITVKCHRA DVEKYGEYLV // ID R9NDE8_9FIRM Unreviewed; 415 AA. AC R9NDE8; DT 24-JUL-2013, integrated into UniProtKB/TrEMBL. DT 24-JUL-2013, sequence version 1. DT 07-JUN-2017, entry version 30. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=C817_00810 {ECO:0000313|EMBL:EOS81153.1}; OS Dorea sp. 5-2. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Lachnospiraceae; OC Dorea. OX NCBI_TaxID=1235798 {ECO:0000313|EMBL:EOS81153.1, ECO:0000313|Proteomes:UP000014211}; RN [1] {ECO:0000313|EMBL:EOS81153.1, ECO:0000313|Proteomes:UP000014211} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=5-2 {ECO:0000313|EMBL:EOS81153.1, RC ECO:0000313|Proteomes:UP000014211}; RG The Broad Institute Genomics Platform; RG The Broad Institute Genome Sequencing Center for Infectious Disease; RA Earl A., Xavier R., Elson C., Duck W., Walker B., Young S., Zeng Q., RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., RA Alvarado L., Arachchi H.M., Berlin A.M., Chapman S.B., RA Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M., RA Howarth C., Imamovic A., Ireland A., Larimer J., McCowan C., RA Murphy C., Pearson M., Poon T.W., Priest M., Roberts A., Saif S., RA Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C., Birren B.; RT "The Genome Sequence of Dorea bacterium 5-2."; RL Submitted (APR-2013) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EOS81153.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ASTD01000018; EOS81153.1; -; Genomic_DNA. DR RefSeq; WP_016217580.1; NZ_KE159726.1. DR EnsemblBacteria; EOS81153; EOS81153; C817_00810. DR PATRIC; fig|1235798.3.peg.870; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000014211; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000014211}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000014211}. FT DOMAIN 198 362 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 157 191 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 415 AA; 46776 MW; E1816E348478B46D CRC64; MNLDQETERV ILVGVSTSDE DDTWRSLKEL KELAETAGAG TVGTLVQNRE QVHPGTYIGK GKIEELKDLL WELDATGIIC DDELTPAQMK NLQDELDTKV MDRTLVILDI FAARASTSEG KLQVELAQLK YRQTRLTGYG TAMSRLGGGI GTRGPGEKKL EVDRRLIKSR IARLNRELKD VKRHREVTRE LRSRNHVPVA AIVGYTNAGK STLMNALTGA GILAEDKLFA TLDPTTREVK LPSGQRVLLT DTVGFIRKLP HHLIEAFRST LEEARYADLI LHVADISNPQ MEEQMYVVYE TLRELGVTDK PVISVFNKQD KAKEERIIRD FHADYTVGIS AKTGGNIPEL LKTVEAALRE QKVYLEGIYP YREAGMLQMI RECGELEEEA YREDGIFVRA YVPVRIYEKL KKMST // ID R9PRQ5_AGAAL Unreviewed; 430 AA. AC R9PRQ5; DT 24-JUL-2013, integrated into UniProtKB/TrEMBL. DT 24-JUL-2013, sequence version 1. DT 30-AUG-2017, entry version 29. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=AALB_4060 {ECO:0000313|EMBL:GAD03980.1}; OS Agarivorans albus MKT 106. OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales; OC Alteromonadaceae; Agarivorans. OX NCBI_TaxID=1331007 {ECO:0000313|EMBL:GAD03980.1, ECO:0000313|Proteomes:UP000014461}; RN [1] {ECO:0000313|EMBL:GAD03980.1, ECO:0000313|Proteomes:UP000014461} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MKT 106 {ECO:0000313|Proteomes:UP000014461}; RA Yasuike M., Nakamura Y., Kai W., Fujiwara A., Fukui Y., Satomi M., RA Sano M.; RT "Draft Genome Sequence of Agarivorans albus Strain MKT 106T, an RT Agarolytic Marine Bacterium."; RL Genome Announc. 1:e00367-13(2013). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:GAD03980.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BARX01000039; GAD03980.1; -; Genomic_DNA. DR RefSeq; WP_016403747.1; NZ_BARX01000039.1. DR EnsemblBacteria; GAD03980; GAD03980; AALB_4060. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000014461; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000014461}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000014461}. FT DOMAIN 198 365 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 157 191 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 430 AA; 48471 MW; 7AA7DBF0137FEEE4 CRC64; MFDRYEAGEQ AILVHVNFSD EDEREDLEEL KMLVSSAGVN AVATITGSRV SPHPKYFVGA GKAEEIAELV KSAQADVIIF NHALSPAQER NLEMLCEARV LDRTTLILDI FAQRARTHEG KLQVELAQLR HMSTRLIRGW THLERQKGGI GLRGPGETQL ETDRRLLRAR IKQIQQRLEK VGKQREQGRR ARQRAELPTV SLAGYTNAGK STLFNRITES KVYAADQLFA TLDPTLRKID IEDVGKVILA DTVGFIRHLP HDLVAAFKAT LTETREAQLL LHVIDCSDER MAENVEQVEV VLDEIGAGDI PFLQVYNKVD QHPDMSPRIE RDDQGLPQKV WVSALTGEGL PLLFKAISER LVGDMVNHTL RLPPSEGRLR SRLYQLDCVA GERLDDEGNI VVDIRLDAIA WQRLDKQFDH SLESFIAQCE // ID S0EXN3_CHTCT Unreviewed; 426 AA. AC S0EXN3; DT 18-SEP-2013, integrated into UniProtKB/TrEMBL. DT 18-SEP-2013, sequence version 1. DT 07-JUN-2017, entry version 27. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=CCALI_00733 {ECO:0000313|EMBL:CCW34558.1}; OS Chthonomonas calidirosea (strain DSM 23976 / ICMP 18418 / T49). OC Bacteria; Armatimonadetes; Chthonomonadetes; Chthonomonadales; OC Chthonomonadaceae; Chthonomonas. OX NCBI_TaxID=1303518 {ECO:0000313|EMBL:CCW34558.1, ECO:0000313|Proteomes:UP000014227}; RN [1] {ECO:0000313|EMBL:CCW34558.1, ECO:0000313|Proteomes:UP000014227} RP NUCLEOTIDE SEQUENCE. RC STRAIN=T49 {ECO:0000313|EMBL:CCW34558.1}; RA Stott M.; RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; HF951689; CCW34558.1; -; Genomic_DNA. DR RefSeq; WP_016482120.1; NC_021487.1. DR EnsemblBacteria; CCW34558; CCW34558; CCALI_00733. DR KEGG; ccz:CCALI_00733; -. DR PATRIC; fig|1303518.3.peg.740; -. DR KO; K03665; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000014227; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000014227}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000014227}. FT DOMAIN 203 369 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 162 196 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 426 AA; 47542 MW; 2867CDBCB19F0643 CRC64; MPTRTLTSSS QLERAVLVSV EPDEVLRPYA LAELAALART AGAEVVGEFY QRRLRPDAAF FIGPGKVEEL LAGIHASQAN LVIVDSELSP VQARNLEEAL HCRVIDRTQL ILDIFAQRAR SREGKLQVEL AQLTYLLPRL SDLYTRFERQ QGGIGVRGGP GETKLETDRR RVRDTIRDLQ ARLAEIRKNR QNQRAHRRRL PFPTAALVGY TSAGKSTLLN VLSGSDVYAD PMLFATLDPT TRRMELPDGW GILLTDTVGF IRNLPAHLIA AFRATLEEVA EADFLIHVVD ASHPHRDIQI QAVLQTLEEL ELDEKPLLTV FNKADLVGDQ FALRKLVSQT PHAVYISAQK REGLEHLIAL IFKTIQSLLV PVHAKLPFDK GDLLAECYSF GRVTSVEYGT DGIYLNACVT KEMQGRLQPY ILSNPT // ID S0FLJ2_9FIRM Unreviewed; 615 AA. AC S0FLJ2; DT 18-SEP-2013, integrated into UniProtKB/TrEMBL. DT 18-SEP-2013, sequence version 1. DT 07-JUN-2017, entry version 29. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=CTER_4280 {ECO:0000313|EMBL:EMS70039.1}; OS [Clostridium] termitidis CT1112. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Ruminococcaceae; OC Ruminiclostridium. OX NCBI_TaxID=1195236 {ECO:0000313|EMBL:EMS70039.1, ECO:0000313|Proteomes:UP000014155}; RN [1] {ECO:0000313|EMBL:EMS70039.1, ECO:0000313|Proteomes:UP000014155} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CT1112 {ECO:0000313|EMBL:EMS70039.1, RC ECO:0000313|Proteomes:UP000014155}; RX PubMed=23704187; RA Lal S., Ramachandran U., Zhang X., Munir R., Sparling R., Levin D.B.; RT "Draft Genome Sequence of the Cellulolytic, Mesophilic, Anaerobic RT Bacterium Clostridium termitidis Strain CT1112 (DSM 5398)."; RL Genome Announc. 1:E00281-13(2013). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EMS70039.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AORV01000060; EMS70039.1; -; Genomic_DNA. DR EnsemblBacteria; EMS70039; EMS70039; CTER_4280. DR PATRIC; fig|1195236.3.peg.4458; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000014155; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000014155}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000014155}. FT DOMAIN 397 561 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 356 390 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 615 AA; 68119 MW; 88FABA8DA9D6CBEC CRC64; MQNWCASVPG RTWIIGGELI NINGNTQSIK ERLLNELEEL YDKKFESREL VPVELAETIA RISHEINREI SVLINRRGIV VDISIGDSGT VSLPQLDNRR GKSRLSAIRC IHTHPGGNGM LSQVDISTLQ KLRLDAMLAM GINEGQPGEI YAGCLSAEQD VDVYGPFTLG EPRLNYLYKI IEELDASAKN DIYENEGEAE KAILVGLETS QSRLESASLR DAEDSLSELE ELAGTAGAIV VDKVLQRKQA QDSAYYVGKG KIEELSLLCQ ARDVQLLIFD DELSGAQIRN IEDATGVRVV DRTTLILDIF AQRAISKEGK LQVELAQLKY QLPRLIGLGT QLSRLGGGIG TRGPGEKKLE VDRRHIRRRI SGLERELEQL EKRRDFMRST RSKNNVPVIA IVGYTNAGKS TLMNRLCGAD VFVEDKLFAT LDPSARKLIL ADGREAVLVD TVGFIRKLPH DLIEAFKSTL EEAVHADMLL HVVDASNENA AMQISVVEGL LDELGASSKN TILVLNKQDL VTSGGRINSI GYSSVCEISA VTGTGIDRLL EQITEGFKDR LREINLLIPY NEGWVLPYIY KYGQIINQEY LENGIQVKAL VKLDKIGKLE EFILV // ID S0FSE2_9FIRM Unreviewed; 420 AA. AC S0FSE2; DT 18-SEP-2013, integrated into UniProtKB/TrEMBL. DT 18-SEP-2013, sequence version 1. DT 07-JUN-2017, entry version 29. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=CTER_2698 {ECO:0000313|EMBL:EMS71398.1}; OS [Clostridium] termitidis CT1112. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Ruminococcaceae; OC Ruminiclostridium. OX NCBI_TaxID=1195236 {ECO:0000313|EMBL:EMS71398.1, ECO:0000313|Proteomes:UP000014155}; RN [1] {ECO:0000313|EMBL:EMS71398.1, ECO:0000313|Proteomes:UP000014155} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CT1112 {ECO:0000313|EMBL:EMS71398.1, RC ECO:0000313|Proteomes:UP000014155}; RX PubMed=23704187; RA Lal S., Ramachandran U., Zhang X., Munir R., Sparling R., Levin D.B.; RT "Draft Genome Sequence of the Cellulolytic, Mesophilic, Anaerobic RT Bacterium Clostridium termitidis Strain CT1112 (DSM 5398)."; RL Genome Announc. 1:E00281-13(2013). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EMS71398.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AORV01000038; EMS71398.1; -; Genomic_DNA. DR RefSeq; WP_004626488.1; NZ_AORV01000038.1. DR EnsemblBacteria; EMS71398; EMS71398; CTER_2698. DR PATRIC; fig|1195236.3.peg.3018; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000014155; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR Gene3D; 3.40.50.620; -; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR014729; Rossmann-like_a/b/a_fold. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000014155}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000014155}. FT DOMAIN 197 365 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 156 190 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 420 AA; 47188 MW; 410721638C211A30 CRC64; MIQKQRALLV GININNQTFF KDSMEELKNL AAACELEIAG VVEQNLKAVN TAYHIGSGKV KEVRLLIDEV KADVVVFSNE LTPSQLRNLE DSLEREVIDR TMLIIEIFAK RAKTREAKLQ VEVARLKFML PRLEGLNDNL SRQGGGSGLR NRGSGETKLE LDKRRIESKI AELSKELELL VNERNTQRSK RNKAGLPSVA LVGYTNAGKS TLMNALVEVY QKNADKKVFE KDMLFATLET SVRNITLPDK KAFLLSDTVG FISKLPHELV KAFRSTLEEV RTADLLLHVV DSSNPNFVQQ INVTNETLKQ IGADKIPTIL VFNKADLTDV TIPCIEDGKV YISAKKDSGI EELVGLIGKE VFTQYMEYKM LVPYDRGNIV AYFNENADVK AVSYEKDGTL LTVECRVSDY KRFEEFAFKG // ID S0G1J5_9DELT Unreviewed; 549 AA. AC S0G1J5; DT 18-SEP-2013, integrated into UniProtKB/TrEMBL. DT 18-SEP-2013, sequence version 1. DT 07-JUN-2017, entry version 27. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=Dpo_2c04960 {ECO:0000313|EMBL:EMS80795.1}; OS Desulfotignum phosphitoxidans DSM 13687. OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfobacterales; OC Desulfobacteraceae; Desulfotignum. OX NCBI_TaxID=1286635 {ECO:0000313|EMBL:EMS80795.1, ECO:0000313|Proteomes:UP000014216}; RN [1] {ECO:0000313|EMBL:EMS80795.1, ECO:0000313|Proteomes:UP000014216} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 13687 {ECO:0000313|EMBL:EMS80795.1, RC ECO:0000313|Proteomes:UP000014216}; RX PubMed=23704177; RA Poehlein A., Daniel R., Simeonova D.D.; RT "Draft Genome Sequence of Desulfotignum phosphitoxidans DSM 13687 RT Strain FiPS-3."; RL Genome Announc. 1:E00227-13(2013). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EMS80795.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; APJX01000002; EMS80795.1; -; Genomic_DNA. DR RefSeq; WP_006965074.1; NZ_APJX01000002.1. DR EnsemblBacteria; EMS80795; EMS80795; Dpo_2c04960. DR PATRIC; fig|1286635.3.peg.1473; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000014216; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000014216}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000014216}. FT DOMAIN 378 549 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 337 371 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 549 AA; 61710 MW; 18E8E6D6A989EA31 CRC64; MNKQVYGNLA GLRNTQLKRI ENLYAQKSSP EYIISPDIAV ELVEISHEIR RQMGLLVDRN GKIVCVIAGE PHRIVIPVTP DHMAIPGRLK GVRCVHTHLK DEPLTRDDLT DLALLRLDFI TAVCLTSDGR PGPVYSGHVL PDETKEPYQV QPPATLSDLN NDCLTQILAL EAELSRKNAL HKPASGLENA FLINAVIQDA DAAYASMDEL KELCKTSQIT VTGTAVQHRK RIDPKFVVGK GKLSALVIQA IQNHATLLIF DCELTPSQIR SITDFVEMKV IDRTQLILDI FAKQAKSREG KLQVELAQLE YLLPRLITKN TAMSRLTGGI GGRGPGETKL EINRRRVRDR ITRLKKEIKK IRKQRHQQKA RRRQRNIPVI SIVGYTNAGK STLLNTLTQS DIIAADRLFA TLDPSSRRLR FPADTEVIVT DTVGFIQHLP KELMEAFHAT LEELAEADII LHVIDISNPR YMQQKDSVEK ILTQLDLDDI PVLYVFNKMD RVDMADFDTP WLLNEGICIC ARQKQSLTGL IEKLESMVTL PASHLRVDQ // ID S0GGC0_9BACT Unreviewed; 403 AA. AC S0GGC0; DT 18-SEP-2013, integrated into UniProtKB/TrEMBL. DT 18-SEP-2013, sequence version 1. DT 30-AUG-2017, entry version 29. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=C803_04094 {ECO:0000313|EMBL:EOS15781.1}; OS Parabacteroides goldsteinii dnLKV18. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Tannerellaceae; OC Parabacteroides. OX NCBI_TaxID=1235789 {ECO:0000313|EMBL:EOS15781.1, ECO:0000313|Proteomes:UP000014140}; RN [1] {ECO:0000313|EMBL:EOS15781.1, ECO:0000313|Proteomes:UP000014140} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=dnLKV18 {ECO:0000313|Proteomes:UP000014140}; RG The Broad Institute Genomics Platform; RG The Broad Institute Genome Sequencing Center for Infectious Disease; RA Earl A., Xavier R., Kuhn K., Stappenbeck T., Walker B., Young S., RA Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., RA Allen A.W., Alvarado L., Arachchi H.M., Berlin A.M., Chapman S.B., RA Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M., RA Howarth C., Imamovic A., Ireland A., Larimer J., McCowan C., RA Murphy C., Pearson M., Poon T.W., Priest M., Roberts A., Saif S., RA Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C., Birren B.; RT "The Genome Sequence of Parabacteroides goldsteinii dnLKV18."; RL Submitted (APR-2013) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EOS15781.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ASSQ01000020; EOS15781.1; -; Genomic_DNA. DR RefSeq; WP_010800888.1; NZ_KE159520.1. DR EnsemblBacteria; EOS15781; EOS15781; C803_04094. DR PATRIC; fig|1235789.3.peg.4109; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000014140; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000014140}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000014140}. FT DOMAIN 202 386 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 403 AA; 46564 MW; FC53EE14F6D1499E CRC64; MKEFIISEAL TEKAVLVGLI TPEQNEQKVK EYLDELAFLA DTAGAEAVKK FYQKLDYPNP VTFVGTGKLQ EIKEYVIENE IGLVIFDDEL SPKQLRNIEK ELQVKILDRT SLILDIFASR AQTANAKTQV ELAQYKYMLP RLTRLWTHLE RQRGGVGMRG PGETQLETDK RIILDKIAKL KRDLVDIDKQ KSVQRKNRGK MVRVALVGYT NVGKSTLMNQ LSKSDVFAEN KLFATLDTTV RKVIVENLPF LLSDTVGFIR KLPTELVESF KSTLDEVREA DLLVHVVDIS HPTFEEQIEV VNKTLAEIDK TEKPMIMVFN KVDAFTFVPK DEDDLTPRKR ENIDLDELKR TWMNKLQDNC IFISAKERTN IDALKALLYE RVKQIHITRF PYNDFLFQQY DEE // ID S0IZ95_9FIRM Unreviewed; 431 AA. AC S0IZ95; DT 18-SEP-2013, integrated into UniProtKB/TrEMBL. DT 18-SEP-2013, sequence version 1. DT 07-JUN-2017, entry version 29. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=C805_03814 {ECO:0000313|EMBL:EOT21735.1}; OS Eubacterium sp. 14-2. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Eubacteriaceae; OC Eubacterium. OX NCBI_TaxID=1235790 {ECO:0000313|EMBL:EOT21735.1, ECO:0000313|Proteomes:UP000014176}; RN [1] {ECO:0000313|EMBL:EOT21735.1, ECO:0000313|Proteomes:UP000014176} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=14-2 {ECO:0000313|EMBL:EOT21735.1, RC ECO:0000313|Proteomes:UP000014176}; RG The Broad Institute Genomics Platform; RG The Broad Institute Genome Sequencing Center for Infectious Disease; RA Earl A., Xavier R., Elson C., Duck W., Walker B., Young S., Zeng Q., RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., RA Alvarado L., Arachchi H.M., Berlin A.M., Chapman S.B., RA Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M., RA Howarth C., Imamovic A., Ireland A., Larimer J., McCowan C., RA Murphy C., Pearson M., Poon T.W., Priest M., Roberts A., Saif S., RA Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C., Birren B.; RT "The Genome Sequence of Eubacterium bacterium 14-2."; RL Submitted (APR-2013) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EOT21735.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ASSS01000017; EOT21735.1; -; Genomic_DNA. DR RefSeq; WP_016216817.1; NZ_KE159569.1. DR EnsemblBacteria; EOT21735; EOT21735; C805_03814. DR PATRIC; fig|1235790.3.peg.4126; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000014176; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000014176}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000014176}. FT DOMAIN 202 366 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 161 188 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 431 AA; 48445 MW; 7AA2A4E9757AAB83 CRC64; MPEPFKTEEI TEKLILVGVS RQDDEDTEDS LTELAELVET AGGLVVGTAI QNRESVHPGT YVGKGKLEEL QQMISELEAD GIVCDDELSP AQLRNMEDVL ECRVMDRTLV ILDIFAARAS TSEGKIQVEL AQLKYRMSRL TGLGISLSRL GGGIGTRGPG EKKLEMDRRL IKNRIAQLNR ELVQVQKHRE ITRGQREHNQ TRVAAIVGYT NAGKSTLLNR LTHASVLEED MLFATLDPTT RNLKLDSGQE ILLTDTVGFI RKLPHHLIEA FRSTLEEARY ADIILHVVDA SSPQREKQME IVYETLQNLG VSGKKTITLF NKQDKVEEQE GQKDFQADKS LKISARSGQG LEELKEALEE ILREDKQLLE GIFPYDQGGQ LTVIRKYGEL LEEEYGEQGI YVKAFVPAEL YRNLEKNMKT QEAEIQAGEQ P // ID S0NPT7_9ENTE Unreviewed; 414 AA. AC S0NPT7; DT 18-SEP-2013, integrated into UniProtKB/TrEMBL. DT 18-SEP-2013, sequence version 1. DT 07-JUN-2017, entry version 28. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=I573_01218 {ECO:0000313|EMBL:EOT83497.1}; OS Enterococcus sulfureus ATCC 49903. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Enterococcaceae; OC Enterococcus. OX NCBI_TaxID=1140003 {ECO:0000313|EMBL:EOT83497.1, ECO:0000313|Proteomes:UP000015961}; RN [1] {ECO:0000313|EMBL:EOT83497.1, ECO:0000313|Proteomes:UP000015961} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 49903 {ECO:0000313|EMBL:EOT83497.1, RC ECO:0000313|Proteomes:UP000015961}; RG The Broad Institute Genomics Platform; RG The Broad Institute Genome Sequencing Center for Infectious Disease; RA Earl A., Russ C., Gilmore M., Surin D., Walker B., Young S., Zeng Q., RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., RA Alvarado L., Arachchi H.M., Berlin A.M., Chapman S.B., RA Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M., RA Howarth C., Imamovic A., Ireland A., Larimer J., McCowan C., RA Murphy C., Pearson M., Poon T.W., Priest M., Roberts A., Saif S., RA Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C., Birren B.; RT "The Genome Sequence of Enterococcus sulfureus ATCC_49903 RT (PacBio/Illumina hybrid assembly)."; RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EOT83497.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ASWO01000005; EOT83497.1; -; Genomic_DNA. DR RefSeq; WP_016185909.1; NZ_KE136394.1. DR EnsemblBacteria; EOT83497; EOT83497; I573_01218. DR PATRIC; fig|1140003.3.peg.1414; -. DR Proteomes; UP000015961; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000015961}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000015961}. FT DOMAIN 195 357 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 161 188 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 414 AA; 47048 MW; 7B8577FB0DEAA98F CRC64; MKEERVLIVG VETEENYRTF HSSLTEMRQL VQAAHGEVVA VMEQKRPVVN RQTIVGKGKL AEIALAVDAE EIDIVIFNHE LTPRQHQTLS DRLQVLVIDR VQLILDIFAL RARSKEGKLQ VELAQLNYLL PRLVGQGAAM SRLGAGIGTR GPGETKLETD RRHIRNRMTK VKRELKELAA HRERTREKRR QSQLIQVGLI GYTNAGKSTL LNRLTDAQTF EKDQLFATLD PLTKKWRLPE GLMLTLTDTV GFMQDLPTQL IDAFHSTLEE SRAMDILLHV VDASASDRQI QEKTVLALMK ELGLDHIPVL TVYNKADKLE EENFIPTVFP NILISAYDKE SIALVSKGIK QLIMEKFDPY VLSLPDQEAY RLANLERQTL VVAKEYDEEH GQYEVKGFVA PENRTDVSYS DMES // ID S0NVB8_9ENTE Unreviewed; 410 AA. AC S0NVB8; DT 18-SEP-2013, integrated into UniProtKB/TrEMBL. DT 18-SEP-2013, sequence version 1. DT 07-JUN-2017, entry version 30. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=OMQ_00582 {ECO:0000313|EMBL:EOT29891.1}; OS Enterococcus saccharolyticus subsp. saccharolyticus ATCC 43076. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Enterococcaceae; OC Enterococcus. OX NCBI_TaxID=1139996 {ECO:0000313|EMBL:EOT29891.1, ECO:0000313|Proteomes:UP000014136}; RN [1] {ECO:0000313|EMBL:EOT29891.1, ECO:0000313|Proteomes:UP000014136} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43076 {ECO:0000313|EMBL:EOT29891.1, RC ECO:0000313|Proteomes:UP000014136}; RG The Broad Institute Genomics Platform; RG The Broad Institute Genome Sequencing Center for Infectious Disease; RA Earl A., Russ C., Gilmore M., Surin D., Walker B., Young S., Zeng Q., RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., RA Alvarado L., Arachchi H.M., Berlin A.M., Chapman S.B., RA Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M., RA Howarth C., Imamovic A., Ireland A., Larimer J., McCowan C., RA Murphy C., Pearson M., Poon T.W., Priest M., Roberts A., Saif S., RA Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C., Birren B.; RT "The Genome Sequence of Enterococcus saccharolyticus ATCC_43076 RT (Illumina only assembly)."; RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EOT29891.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AHYT01000002; EOT29891.1; -; Genomic_DNA. DR RefSeq; WP_016174389.1; NZ_KE136523.1. DR EnsemblBacteria; EOT29891; EOT29891; OMQ_00582. DR PATRIC; fig|1139996.3.peg.575; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000014136; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000014136}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000014136}. FT DOMAIN 195 358 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 410 AA; 46434 MW; 10D089555D3DAD7D CRC64; METERVILVG VETEENYKNF EESMIELKSL TKTANGEVVF SLTQRRPQVD RQTLIGKGKL EELAQLADAH EADLIIFNHE LTPRQSQLIG DAVGIPVIDR VQLILDIFAM RARSKEGKLQ VELAQLDYLL PRLVGQGKNM SRLGGGIGTR GPGETKLETD RRHIRNKITI IKRELKEVAA HRERTRQKRK DNQTFQIGLI GYTNAGKSTI LNILTSAQTY EQDQLFATLD PLTKKWRLPE GFEVTVTDTV GFIQDLPTQL IDAFHSTLEE SQGMDLLLHV VDASAENRQQ HEETVLNLMN QLELGSLPML TIYNKADKTD VDQFVPTLFP NVLISAKSSK GKERLIQAIK LAIMESLEPY SFSLQQTEGK ILNRLKRETL LLSSDYEEET QSYLLKGFAQ PDSYAIRQMN // ID S0RXG5_ENTAV Unreviewed; 414 AA. AC S0RXG5; DT 18-SEP-2013, integrated into UniProtKB/TrEMBL. DT 18-SEP-2013, sequence version 1. DT 05-JUL-2017, entry version 30. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=OMU_04235 {ECO:0000313|EMBL:EOT39500.1}; OS Enterococcus avium ATCC 14025. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Enterococcaceae; OC Enterococcus. OX NCBI_TaxID=1140002 {ECO:0000313|EMBL:EOT39500.1, ECO:0000313|Proteomes:UP000014104}; RN [1] {ECO:0000313|EMBL:EOT39500.1, ECO:0000313|Proteomes:UP000014104} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 14025 {ECO:0000313|EMBL:EOT39500.1, RC ECO:0000313|Proteomes:UP000014104}; RG The Broad Institute Genomics Platform; RG The Broad Institute Genome Sequencing Center for Infectious Disease; RA Earl A., Russ C., Gilmore M., Surin D., Walker B., Young S., Zeng Q., RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., RA Alvarado L., Arachchi H.M., Berlin A.M., Chapman S.B., RA Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M., RA Howarth C., Imamovic A., Ireland A., Larimer J., McCowan C., RA Murphy C., Pearson M., Poon T.W., Priest M., Roberts A., Saif S., RA Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C., Birren B.; RT "The Genome Sequence of Enterococcus avium ATCC_14025 (Illumina only RT assembly)."; RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EOT39500.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AHYV01000044; EOT39500.1; -; Genomic_DNA. DR RefSeq; WP_016181979.1; NZ_KE136507.1. DR EnsemblBacteria; EOT39500; EOT39500; OMU_04235. DR GeneID; 31921034; -. DR PATRIC; fig|1140002.3.peg.4229; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000014104; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000014104}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000014104}. FT DOMAIN 194 356 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 160 190 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 414 AA; 47043 MW; 1BE95BE775CB6C41 CRC64; MSERVILVGV ETDESKYNYL ESMHELAGLT KTAHGEIVFS LTQKRPKVDR QTIIGKGKLE ELAQLVDAHE AELVIFNHSL SPRQSQTIEA QVGVPVIDRI QLILDIFAQR ARSKEGKLQV ELAQLDYLLP RLVGQGQSLS RLGGGIGTRG PGETKLETDR RHIRRRITAI KKELKEVEAH RERSRQKRQQ SSIFQMGLIG YTNAGKSTIL NLLTNADTYS EDKLFATLDP LTKRWHLPQG METTITDTVG FIQDLPTQLV DAFQSTLEES KGMDLLLHIV DASAEDRQQQ EKTVIDLLKE LEMDDIPMLT IYNKADRIDE FSFAPTLFPS VLISAKTNKG KELLAEAIKR EIMNLLEPYI LTLNADEGQA LSEMKRETLV LSENFDEENE QYIIRGFAKK KSLWIRRMED ELDD // ID S1NTA1_9ENTE Unreviewed; 415 AA. AC S1NTA1; DT 18-SEP-2013, integrated into UniProtKB/TrEMBL. DT 18-SEP-2013, sequence version 1. DT 07-JUN-2017, entry version 29. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=I568_00620 {ECO:0000313|EMBL:EOW84134.1}; OS Enterococcus columbae DSM 7374 = ATCC 51263. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Enterococcaceae; OC Enterococcus. OX NCBI_TaxID=1121865 {ECO:0000313|EMBL:EOW84134.1, ECO:0000313|Proteomes:UP000014113}; RN [1] {ECO:0000313|EMBL:EOW84134.1, ECO:0000313|Proteomes:UP000014113} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51263 {ECO:0000313|EMBL:EOW84134.1, RC ECO:0000313|Proteomes:UP000014113}; RG The Broad Institute Genomics Platform; RG The Broad Institute Genome Sequencing Center for Infectious Disease; RA Earl A., Russ C., Gilmore M., Surin D., Walker B., Young S., Zeng Q., RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., RA Alvarado L., Arachchi H.M., Berlin A.M., Chapman S.B., RA Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M., RA Howarth C., Imamovic A., Ireland A., Larimer J., McCowan C., RA Murphy C., Pearson M., Poon T.W., Priest M., Roberts A., Saif S., RA Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C., Birren B.; RT "The Genome Sequence of Enterococcus columbae ATCC_51263 RT (PacBio/Illumina hybrid assembly)."; RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EOW84134.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ASWJ01000004; EOW84134.1; -; Genomic_DNA. DR RefSeq; WP_016182198.1; NZ_KE136493.1. DR EnsemblBacteria; EOW84134; EOW84134; I568_00620. DR PATRIC; fig|1121865.3.peg.22; -. DR Proteomes; UP000014113; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000014113}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000014113}. SQ SEQUENCE 415 AA; 47283 MW; AF6E4EE8B4729610 CRC64; MNEKVILVGV ETESNFRYFE SSMDELRGLT KTAEGEIVFI LKQKRPQIDR QTILGKGKLE ELKQLVIAHE ANLVIFNHEL SPRQGQVLAE ILEVKVLDRV QLILDIFALR ARSKEGKLQV ELAQLEYLLP RLAGQGNQLS RLGGGIGTRG PGETKLETDR RHIRNKITQI KRELKEVAAH RLRARKQRQD KNIFQLGLIG YTNAGKSTIL NILTSAQTYE QDQLFATLDP LTKKWRMPEG FEVTVTDTVG FIQDLPTQLV DAFESTLEES KEVDMLLHVV DAHAQDRLQH EQTVAQLMQQ LAIVDIPILT VYNKSDLIGE EPFVPTLFPN VCISAKSNKG KEDLIRAIKQ QLMEQFEPYV TTINATDAKQ LYEIKRQTLV TSMEFDELKQ VYLISGFAPA YHQLVRIQID EEDLD // ID S1P3P9_9ENTE Unreviewed; 414 AA. AC S1P3P9; DT 18-SEP-2013, integrated into UniProtKB/TrEMBL. DT 18-SEP-2013, sequence version 1. DT 07-JUN-2017, entry version 30. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=OMK_01526 {ECO:0000313|EMBL:EOT41355.1}; OS Enterococcus dispar ATCC 51266. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Enterococcaceae; OC Enterococcus. OX NCBI_TaxID=1139219 {ECO:0000313|EMBL:EOT41355.1, ECO:0000313|Proteomes:UP000014127}; RN [1] {ECO:0000313|EMBL:EOT41355.1, ECO:0000313|Proteomes:UP000014127} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51266 {ECO:0000313|EMBL:EOT41355.1, RC ECO:0000313|Proteomes:UP000014127}; RG The Broad Institute Genomics Platform; RG The Broad Institute Genome Sequencing Center for Infectious Disease; RA Earl A., Russ C., Gilmore M., Surin D., Walker B., Young S., Zeng Q., RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., RA Alvarado L., Arachchi H.M., Berlin A.M., Chapman S.B., RA Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M., RA Howarth C., Imamovic A., Ireland A., Larimer J., McCowan C., RA Murphy C., Pearson M., Poon T.W., Priest M., Roberts A., Saif S., RA Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C., Birren B.; RT "The Genome Sequence of Enterococcus dispar ATCC_51266 (Illumina only RT assembly)."; RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EOT41355.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AHYR01000005; EOT41355.1; -; Genomic_DNA. DR RefSeq; WP_016172697.1; NZ_KE136354.1. DR EnsemblBacteria; EOT41355; EOT41355; OMK_01526. DR PATRIC; fig|1139219.3.peg.1488; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000014127; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000014127}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000014127}. FT DOMAIN 194 357 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 414 AA; 47176 MW; B4E3C3AFA4BFE2AE CRC64; MEQEKVILVG VETEETWKNF GESMQELKGL TKTAKGEVCF SLVQKRPQVD RQTIIGKGKL TELKNLVESY EADLVIFNHE LTPRQSQTIA DFIVVPVIDR VQLILDIFAL RARSKEGKLQ VELAQLEYLL PRLVGQGKYL SRLGGGIGTR GPGETKLETD RRHIRNKITA IKRELKEVAA HRERTRQRRK NNRFQIGLIG YTNAGKSTIM NVLTEAKTYE QDELFATLDP LTKRWKLPEG FEVTLTDTVG FIQDLPTQLI DAFHSTLEES RDMDLLLHVV DASSPDRSQQ EQTVLDLIKD LDFDKTPILT VYNKADKIDT AHFVPTLFPN VLISAKSSRS KEELTTAVRL QLMENLEPYT VYLAQNEGKL LAQLKSETLL VHEEFLPASE NYLVKGFSLP ETAIIRRMED ELDR // ID S1QV59_9ENTE Unreviewed; 404 AA. AC S1QV59; DT 18-SEP-2013, integrated into UniProtKB/TrEMBL. DT 18-SEP-2013, sequence version 1. DT 07-JUN-2017, entry version 30. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=OMO_00028 {ECO:0000313|EMBL:ESK62386.1}; OS Enterococcus cecorum DSM 20682 = ATCC 43198. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Enterococcaceae; OC Enterococcus. OX NCBI_TaxID=1121864 {ECO:0000313|EMBL:ESK62386.1, ECO:0000313|Proteomes:UP000017415}; RN [1] {ECO:0000313|EMBL:ESK62386.1, ECO:0000313|Proteomes:UP000017415} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43198 {ECO:0000313|EMBL:ESK62386.1, RC ECO:0000313|Proteomes:UP000017415}; RG The Broad Institute Genomics Platform; RG The Broad Institute Genome Sequencing Center for Infectious Disease; RA Earl A., Russ C., Gilmore M., Surin D., Walker B., Young S., Zeng Q., RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., RA Alvarado L., Arachchi H.M., Berlin A.M., Chapman S.B., RA Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M., RA Howarth C., Imamovic A., Ireland A., Larimer J., McCowan C., RA Murphy C., Pearson M., Poon T.W., Priest M., Roberts A., Saif S., RA Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C., Birren B.; RT "The Genome Sequence of Enterococcus cecorum DSM 20682 (= ATCC 43198) RT (Illumina assembly)."; RL Submitted (OCT-2013) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:ESK62386.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AHYS01000001; ESK62386.1; -; Genomic_DNA. DR RefSeq; WP_016251711.1; NZ_KI535313.1. DR EnsemblBacteria; ESK62386; ESK62386; OMO_00028. DR GeneID; 29475279; -. DR PATRIC; fig|1121864.4.peg.1566; -. DR Proteomes; UP000017415; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000017415}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000017415}. FT DOMAIN 198 360 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 164 194 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 404 AA; 46270 MW; B5D018A6D3B10ACC CRC64; MPEQEKDKVI LVGVETEENF AIFDTSMDEL RGLTKTADGE IVFILKQKRP QVDRQTILGK GKLAELKQLI DAYEANLVIF NHELTPRQGK ILTEELGVRV LDRVQLILDI FAIRARSKEG KLQVSLAQLE YLLPRLTGMG ASMSRLGGGI GTRGPGETKL EVDRRHIRNK ITQIRNELKE VEQHRERTRE QRKNKRVYQI GLIGYTNAGK STIMNILTTA NTYEQDQLFA TLDPLTKKWR LPEGFEMTIT DTVGFIQDLP TQLIDAFQST LEESKSMDFL LHVVDAHAKD RLLHEKTVFD LMQQLEIIDT PVLTVYNKAD LMKEEDFVPT LFPNVCISAK SSKGKEALIQ AIKQQLMEQF EPYMVELADN QASEIYKYKR ETIVTSQNYD ESKRKYIICG FSPK // ID S2E3E2_9BACT Unreviewed; 421 AA. AC S2E3E2; DT 18-SEP-2013, integrated into UniProtKB/TrEMBL. DT 18-SEP-2013, sequence version 1. DT 07-JUN-2017, entry version 29. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=A33Q_2443 {ECO:0000313|EMBL:EOZ96673.1}; OS Indibacter alkaliphilus LW1. OC Bacteria; Bacteroidetes; Cytophagia; Cytophagales; Cyclobacteriaceae. OX NCBI_TaxID=1189612 {ECO:0000313|EMBL:EOZ96673.1, ECO:0000313|Proteomes:UP000006073}; RN [1] {ECO:0000313|EMBL:EOZ96673.1, ECO:0000313|Proteomes:UP000006073} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=LW1 {ECO:0000313|EMBL:EOZ96673.1, RC ECO:0000313|Proteomes:UP000006073}; RX PubMed=23868132; RA Singh A., Kumar Jangir P., Sharma R., Singh A., Kumar Pinnaka A., RA Shivaji S.; RT "Draft Genome Sequence of Indibacter alkaliphilus Strain LW1T, RT Isolated from Lonar Lake, a Haloalkaline Lake in the Buldana District RT of Maharashtra, India."; RL Genome Announc. 1:E00513-13(2013). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EOZ96673.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ALWO02000033; EOZ96673.1; -; Genomic_DNA. DR RefSeq; WP_009034033.1; NZ_ALWO02000033.1. DR EnsemblBacteria; EOZ96673; EOZ96673; A33Q_2443. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000006073; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000006073}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000006073}. FT DOMAIN 210 399 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 171 198 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 421 AA; 48409 MW; 912565BAA9972551 CRC64; MSKYSRKLQK LYDTAPKKDT AVLVALIKQG QSDQQAAEYL DELAFLTETL GASTVYRFTQ RLEKPDVKTF VGTGKLEEIK SYIEHFEVDM VIFDDDLSPS QMRNLENELK IKVYDRSLLI LDIFLNRAQT AQAKTQVELA RFQYLLPRLT RMWTHLERQR GGTSTRGGAG EKEIETDKRD IRQKITLLKN KLKDIEKQGV TQRKGRKGIV RVALVGYTNV GKSTLMNLIT KSEILAENKL FATVDSTVRK VVLDNIPFLL SDTVGFIRKL PTHLIESFKS TLDEIREADL LVHVIDISHP GFEDHFTVVN NTLNEIGARD KPMLLVFNKI DLIQEKPSEE ELQHMTEIEV EENNYLDLEK LSEAYEKKTG ITPVFMAAQD GTHVEDFRKA LVKEVKKQHL KIYPHYLESE VFDLSQFEDL D // ID S2KLJ2_HALAF Unreviewed; 437 AA. AC S2KLJ2; DT 18-SEP-2013, integrated into UniProtKB/TrEMBL. DT 18-SEP-2013, sequence version 1. DT 30-AUG-2017, entry version 30. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=L861_12145 {ECO:0000313|EMBL:EPC01318.1}; OS Halomonas anticariensis (strain DSM 16096 / FP35). OC Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales; OC Halomonadaceae; Halomonas. OX NCBI_TaxID=1121939 {ECO:0000313|EMBL:EPC01318.1, ECO:0000313|Proteomes:UP000014463}; RN [1] {ECO:0000313|EMBL:EPC01318.1, ECO:0000313|Proteomes:UP000014463} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 16096 / FP35 {ECO:0000313|Proteomes:UP000014463}; RX PubMed=23868129; DOI=10.1128/genomeA.00497-13; RA Tahrioui A., Quesada E., Llamas I.; RT "Draft genome sequence of the moderately halophilic RT gammaproteobacterium Halomonas anticariensis FP35."; RL Genome Announc. 1:31-31(2013). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EPC01318.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ASTJ01000036; EPC01318.1; -; Genomic_DNA. DR RefSeq; WP_016418009.1; NZ_KE332392.1. DR EnsemblBacteria; EPC01318; EPC01318; L861_12145. DR PATRIC; fig|1121939.11.peg.3490; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000014463; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000014463}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000014463}. FT DOMAIN 199 365 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 437 AA; 49187 MW; EB594B63379A2B13 CRC64; MFFERPDAGE TAVLVHVDFQ DEQEREDPGE FLELVRSAGA EPATLLQGSR QRPDSRTFIG SGKLEELQEL LAIHHAELVI FNHALSPSQE RNLERALKCR VLDRTGLILD IFAQRARTHE GKLQVELAQL EYMSTRLVRG WTHLERQKGG IGLRGPGETQ LETDRRLLRA RIKSIHKRLD KVRRQRSQNR RARARAEIPS VSLVGYTNAG KSTLFNALTK SEVYAADQLF ATLDPTLRRL DIDDVGPVVL ADTVGFIRHL PHKLVEAFQA TLQEASEASL LVHVIDAADS DRDLNVAQVQ AVLEEIGAED VPTLRVMNKI DLLDSAPRIE RDGDGRPEVV WVSAQRGLGL ELLSQALSEC LAEDVVDTQV SLAPSQGRLR ASLHELGAVR EETFDERGRT LLDIRLPRRD FLQLMARLGE NANDYLPPEY QERPVWE // ID S2KYT2_9FIRM Unreviewed; 217 AA. AC S2KYT2; DT 18-SEP-2013, integrated into UniProtKB/TrEMBL. DT 18-SEP-2013, sequence version 1. DT 07-SEP-2016, entry version 14. DE SubName: Full=GTP-binding protein HflX {ECO:0000313|EMBL:EPC06876.1}; GN ORFNames=HMPREF9625_02181 {ECO:0000313|EMBL:EPC06876.1}; OS Oribacterium parvum ACB1. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Lachnospiraceae; OC Oribacterium. OX NCBI_TaxID=796943 {ECO:0000313|EMBL:EPC06876.1, ECO:0000313|Proteomes:UP000018461}; RN [1] {ECO:0000313|EMBL:EPC06876.1, ECO:0000313|Proteomes:UP000018461} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ACB1 {ECO:0000313|EMBL:EPC06876.1, RC ECO:0000313|Proteomes:UP000018461}; RG The Broad Institute Genome Sequencing Platform; RA Earl A., Ward D., Feldgarden M., Gevers D., Sizova M., Hazen A., RA Epstein S., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B., RA Abouelleil A., Alvarado L., Arachchi H.M., Berlin A., Brown A., RA Chapman S.B., Chen Z., Dunbar C., Freedman E., Gearin G., Gellesch M., RA Goldberg J., Griggs A., Gujja S., Heiman D., Howarth C., Larson L., RA Lui A., MacDonald P.J.P., Montmayeur A., Murphy C., Neiman D., RA Pearson M., Priest M., Roberts A., Saif S., Shea T., Shenoy N., RA Sisk P., Stolte C., Sykes S., Wortman J., Nusbaum C., Birren B.; RL Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:EPC06876.1, ECO:0000313|Proteomes:UP000018461} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ACB1 {ECO:0000313|EMBL:EPC06876.1, RC ECO:0000313|Proteomes:UP000018461}; RG The Broad Institute Genomics Platform; RG The Broad Institute Genome Sequencing Center for Infectious Disease; RA Earl A., Ward D., Feldgarden M., Gevers D., Sizova M., Hazen A., RA Epstein S., Walker B., Young S., Zeng Q., Gargeya S., Fitzgerald M., RA Haas B., Abouelleil A., Allen A.W., Alvarado L., Arachchi H.M., RA Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J., Griggs A., RA Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A., Larimer J., RA McCowan C., Murphy C., Pearson M., Poon T.W., Priest M., Roberts A., RA Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C., RA Birren B.; RT "The Genome Sequence of Oribacterium sp. ACB1."; RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EPC06876.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFZC02000001; EPC06876.1; -; Genomic_DNA. DR EnsemblBacteria; EPC06876; EPC06876; HMPREF9625_02181. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000018461; Unassembled WGS sequence. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. PE 4: Predicted; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000018461}; KW Reference proteome {ECO:0000313|Proteomes:UP000018461}. FT DOMAIN 27 112 GTP-bdg_N. {ECO:0000259|Pfam:PF13167}. FT DOMAIN 115 195 GTP-bdg_M. {ECO:0000259|Pfam:PF16360}. FT COILED 161 195 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 217 AA; 24665 MW; D4512A3652341EB5 CRC64; MEEYKIEERK AVLVGVQFPD NKDFSLDMEE LSGLCEALSI RPVTSLSQSL VREDSASFIG SGKVEEVREA ILFHEANLVI FQNPLSPSQL HNLTKALPCE VLDRTQLILQ IFSERAKTKE AKMQVKYATL QYMLPRLVGL RENLSRQGGA SGSLSNRGSG EKQIELDKRK IQEEMAILRR ELKKQEEVRK VKRQKGIGPP FQGWRWSAIP MQESPVL // ID S2X041_9ACTN Unreviewed; 476 AA. AC S2X041; DT 18-SEP-2013, integrated into UniProtKB/TrEMBL. DT 18-SEP-2013, sequence version 1. DT 07-JUN-2017, entry version 28. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=HMPREF9306_00863 {ECO:0000313|EMBL:EPD33324.1}; OS Propionimicrobium lymphophilum ACS-093-V-SCH5. OC Bacteria; Actinobacteria; Propionibacteriales; Propionibacteriaceae; OC Propionimicrobium. OX NCBI_TaxID=883161 {ECO:0000313|EMBL:EPD33324.1, ECO:0000313|Proteomes:UP000014417}; RN [1] {ECO:0000313|EMBL:EPD33324.1, ECO:0000313|Proteomes:UP000014417} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ACS-093-V-SCH5 {ECO:0000313|EMBL:EPD33324.1, RC ECO:0000313|Proteomes:UP000014417}; RG The Broad Institute Genomics Platform; RA Earl A., Ward D., Feldgarden M., Gevers D., Saerens B., RA Vaneechoutte M., Walker B., Young S., Zeng Q., Gargeya S., RA Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L., RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., RA Goldberg J., Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., RA Ireland A., Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., RA Priest M., Roberts A., Saif S., Shea T., Sisk P., Sykes S., RA Wortman J., Nusbaum C., Birren B.; RT "The Genome Sequence of Propionimicrobium lymphophilum ACS-093-V- RT SCH5."; RL Submitted (APR-2013) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EPD33324.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGZR01000005; EPD33324.1; -; Genomic_DNA. DR RefSeq; WP_016455699.1; NZ_KE150269.1. DR EnsemblBacteria; EPD33324; EPD33324; HMPREF9306_00863. DR PATRIC; fig|883161.3.peg.859; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000014417; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 2. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000014417}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000014417}. FT DOMAIN 257 422 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 223 250 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 476 AA; 52657 MW; 5C13986014C7788A CRC64; MTQEFEDISA DGEDPEAQLE LPEEDQLDLA ERLSLRRVPG LSTELEDVSD VEYRKLRLER VVLVSVWTTG SKADAQNALF ELKALAETAG SQVLDGLIQR RQRPDPATYI GRGKVGELRD SVITNGADTV ICDGELAPAQ LRNLEDRVGV KVVDRTALIL DIFAQHAKSA EGKTQVELAQ LNYLKQRLRG WGGNLSRQVG GRAAGGVGIG GRGPGETRIE TDRRRINSRI AILRKKLREL DSTREIKRAE RHRRQVPSVA IVGYTNAGKS SLLNKLTDAG VLVENALFAT LDPTTRRAQT ADGRVYTLTD TVGFVRHLPT DLVEAFRSTL EETNQADLLM HVVDGADPDP QGQITAVRQV LNDIGAGDIR EQLVINKCDL ADSDQMMILR RHYPDAIFCS ARTGQGVSEL RERIEQLLPR PEVEIHAIVP WNHGELVDKV HKQGELIFSE YLPEGTEIRA RVHGGLAAEL TDFLCD // ID S2XX97_9BACL Unreviewed; 423 AA. AC S2XX97; DT 18-SEP-2013, integrated into UniProtKB/TrEMBL. DT 18-SEP-2013, sequence version 1. DT 07-JUN-2017, entry version 28. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=HMPREF1210_03184 {ECO:0000313|EMBL:EPD49737.1}; OS Paenisporosarcina sp. HGH0030. OC Bacteria; Firmicutes; Bacilli; Bacillales; Planococcaceae; OC Paenisporosarcina. OX NCBI_TaxID=1078085 {ECO:0000313|EMBL:EPD49737.1, ECO:0000313|Proteomes:UP000014412}; RN [1] {ECO:0000313|EMBL:EPD49737.1, ECO:0000313|Proteomes:UP000014412} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=HGH0030 {ECO:0000313|EMBL:EPD49737.1, RC ECO:0000313|Proteomes:UP000014412}; RG The Broad Institute Genomics Platform; RA Earl A., Ward D., Feldgarden M., Gevers D., Schmidt T.M., Dai D., RA Dover J., Kim K., Walker B., Young S., Zeng Q., Gargeya S., RA Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L., RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., RA Goldberg J., Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., RA Ireland A., Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., RA Priest M., Roberts A., Saif S., Shea T., Sisk P., Sykes S., RA Wortman J., Nusbaum C., Birren B.; RT "The Genome Sequence of Paenisporosarcina sp. HGH0030."; RL Submitted (MAY-2013) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EPD49737.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGEQ01000018; EPD49737.1; -; Genomic_DNA. DR RefSeq; WP_016429657.1; NZ_KE150423.1. DR EnsemblBacteria; EPD49737; EPD49737; HMPREF1210_03184. DR PATRIC; fig|1078085.3.peg.3156; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000014412; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000014412}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000014412}. FT DOMAIN 200 368 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 159 193 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 423 AA; 48181 MW; 992F0C65067911A2 CRC64; MEELMERAIV VGVNLNKDEH FEYGLEELHN LAEALNVEVV GEVTQNLDRV NPAHYVGKGK IDEIKAFFEE ADANLVIFND ELSPSQIRNL EAALECKVID RTMLILDIFA RRAKSKEAQM QVELAQLQYM LPRLVGLRAS LGRQGGGTGG GFKNRGAGET KLELDRRKIE DQIAKLRRDL DHVKDQRETQ RKQRKKNEIP VVSIVGYTNA GKSTIMNRLL AKTGQIDDKQ VFEKDMLFAT LETSVRQIRL PDQKEFLLTD TVGFVSKLPT HLVKAFRSTL EEAREADLLL HVVDVSNDEY RYMMDVTNET LQAVGVENVQ TLEVYNKSDL AGVNYPHVSG NNIWISAKEE AGLDELIELI RTHIFADYKM CRMLIPYDRG DVVSYLNEQA SVQGSEYEEE GTLLKVELKQ ADYERYHDFV LDK // ID S2YMM6_9ACTN Unreviewed; 497 AA. AC S2YMM6; DT 18-SEP-2013, integrated into UniProtKB/TrEMBL. DT 18-SEP-2013, sequence version 1. DT 07-JUN-2017, entry version 29. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=HMPREF1211_02278 {ECO:0000313|EMBL:EPD65723.1}; OS Streptomyces sp. HGB0020. OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae; OC Streptomyces. OX NCBI_TaxID=1078086 {ECO:0000313|EMBL:EPD65723.1, ECO:0000313|Proteomes:UP000014410}; RN [1] {ECO:0000313|EMBL:EPD65723.1, ECO:0000313|Proteomes:UP000014410} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=HGB0020 {ECO:0000313|EMBL:EPD65723.1, RC ECO:0000313|Proteomes:UP000014410}; RG The Broad Institute Genomics Platform; RA Earl A., Ward D., Feldgarden M., Gevers D., Schmidt T.M., Dai D., RA Dover J., Kim K., Walker B., Young S., Zeng Q., Gargeya S., RA Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L., RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., RA Goldberg J., Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., RA Ireland A., Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., RA Priest M., Roberts A., Saif S., Shea T., Sisk P., Sykes S., RA Wortman J., Nusbaum C., Birren B.; RT "The Genome Sequence of Streptomyces sp. HGB0020."; RL Submitted (APR-2013) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EPD65723.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGER01000007; EPD65723.1; -; Genomic_DNA. DR RefSeq; WP_016432249.1; NZ_KE150426.1. DR EnsemblBacteria; EPD65723; EPD65723; HMPREF1211_02278. DR PATRIC; fig|1078086.3.peg.2322; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000014410; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000014410}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000014410}. FT DOMAIN 275 440 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 497 AA; 54513 MW; 7CE9EDE90DA1BD58 CRC64; MTSSSSPSQD TERFAHNYAE GLRADALMEE DVAWSHEIDG DRDGDQFDRS DRAALRRVVG LSTELEDVTE VEYRQLRLER VVLVGVWTTG TVRDAENSLA ELAALAETAG ALVLDGVIQR RDKPDAATYI GSGKATELRD MVLETGADTV ICDGELSPGQ LIHLEDVVKV KVIDRTALIL DIFAQHAKSR EGKAQVALAQ MQYMLPRLRG WGQSLSRQMG GGKGGGLATR GPGETKIETD RRRIREKMAK MRREIAEMKT GREIKRQERK RHKVPSVAIA GYTNAGKSSL LNRLTGAGVL VENALFATLD PTVRRAETPS GRLYTLADTV GFVRHLPHHL VEAFRSTMEE VGESDLILHV VDGSHPDPEE QLAAVREVIR DVGATDVPEI VVINKADAAD PLTLQRLLRI EKRAIAVSAR TGRGIAELLA LIDNELPRPS VEIEALVPYT HGKLVARAHD EGEVISEEHT PEGTLLKVRV HEELAAELQP YAPVPAL // ID S3NJ83_9GAMM Unreviewed; 446 AA. AC S3NJ83; DT 18-SEP-2013, integrated into UniProtKB/TrEMBL. DT 18-SEP-2013, sequence version 1. DT 30-AUG-2017, entry version 29. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=F945_00562 {ECO:0000313|EMBL:EPF80110.1}; OS Acinetobacter rudis CIP 110305. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Moraxellaceae; Acinetobacter. OX NCBI_TaxID=421052 {ECO:0000313|EMBL:EPF80110.1, ECO:0000313|Proteomes:UP000014568}; RN [1] {ECO:0000313|EMBL:EPF80110.1, ECO:0000313|Proteomes:UP000014568} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CIP 110305 {ECO:0000313|EMBL:EPF80110.1, RC ECO:0000313|Proteomes:UP000014568}; RG The Broad Institute Genome Sequencing Platform; RG The Broad Institute Genome Sequencing Center for Infectious Disease; RA Cerqueira G., Feldgarden M., Courvalin P., Perichon B., RA Grillot-Courvalin C., Clermont D., Rocha E., Yoon E.-J., Nemec A., RA Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Abouelleil A., RA Alvarado L., Berlin A.M., Chapman S.B., Dewar J., Goldberg J., RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Larimer J., RA McCowan C., Murphy C., Pearson M., Priest M., Roberts A., Saif S., RA Shea T., Sykes S., Wortman J., Nusbaum C., Birren B.; RT "The Genome Sequence of Acinetobacter rudis CIP 110305."; RL Submitted (JUN-2013) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EPF80110.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ATGI01000005; EPF80110.1; -; Genomic_DNA. DR RefSeq; WP_016654997.1; NZ_KE340348.1. DR EnsemblBacteria; EPF80110; EPF80110; F945_00562. DR PATRIC; fig|421052.3.peg.559; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000014568; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000014568}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000014568}. FT DOMAIN 199 364 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 446 AA; 50026 MW; 0B38DC0622937BA6 CRC64; MEYFDRYQGG ERAILVSVTV QMLEDLDTEE FRLLAKSAGA EVLEHVTAQR IKPDPKLFIG SGKAEEIAEL VQAHEAELVI FDHALSPAQE RNLEKIVQCR VIDRTGLILD IFAQRARTHE GKLQVELAQL EHLSTRLVRG WTHLERQKGG IGLRGPGESQ LETDRRLLRI RMGQLKDKLA KVKQTRTQGR AARQKADIPT VSLVGYTNAG KSTLFNLLAD SDVYAADQLF ATLDPTLRRL NWEGIGALVL ADTVGFVRNL PHSLVDSFKA TLEETLEATL LLHVIDSSSP DCMEQIDAVE SVLKEIGADV ATLRVYNKID QSGEEAKIIY AAPHQPDRVY VSAHAGLGID LLRQAVQECL LGQIQNFELK LKPIYGKLRT QLYSLNVIQS EQYDDEGNLL LTIRIAPHKL EQLLRQQHLP LRDILGQAAK MFERPLEAFE IKDEIS // ID S3X0P6_9ACTN Unreviewed; 462 AA. AC S3X0P6; DT 18-SEP-2013, integrated into UniProtKB/TrEMBL. DT 18-SEP-2013, sequence version 1. DT 07-JUN-2017, entry version 28. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=HMPREF1531_02233 {ECO:0000313|EMBL:EPH02917.1}; OS Propionibacterium sp. oral taxon 192 str. F0372. OC Bacteria; Actinobacteria; Propionibacteriales; Propionibacteriaceae; OC Propionibacterium. OX NCBI_TaxID=1203605 {ECO:0000313|EMBL:EPH02917.1, ECO:0000313|Proteomes:UP000014567}; RN [1] {ECO:0000313|EMBL:EPH02917.1, ECO:0000313|Proteomes:UP000014567} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=F0372 {ECO:0000313|EMBL:EPH02917.1, RC ECO:0000313|Proteomes:UP000014567}; RG The Broad Institute Genomics Platform; RA Earl A., Ward D., Feldgarden M., Gevers D., Kirega A., Socransky S.S., RA Dewhirst F.E., Izard J., Walker B., Young S., Zeng Q., Gargeya S., RA Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L., RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., RA Goldberg J., Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., RA Ireland A., Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., RA Priest M., Roberts A., Saif S., Shea T., Sisk P., Sykes S., RA Wortman J., Nusbaum C., Birren B.; RT "The Genome Sequence of Propionibacterium sp. oral taxon 192 str. RT F0372."; RL Submitted (MAY-2013) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EPH02917.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ATFL01000014; EPH02917.1; -; Genomic_DNA. DR RefSeq; WP_016670013.1; NZ_KE340297.1. DR EnsemblBacteria; EPH02917; EPH02917; HMPREF1531_02233. DR PATRIC; fig|1203605.3.peg.2292; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000014567; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000014567}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000014567}. FT DOMAIN 244 405 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 462 AA; 50575 MW; 89778EDBFA2B8135 CRC64; MSRKTDESAD IGELDLADRR SLRRVQGMST ELEDVSEVEY RRLRLERVVL VSVWTVGSQA DADNAMFELK ALAETAGSQV LAGLVQRRQY PDPATYVGSG KVAEIADEIR VHGADTVICD GELSPAQLRT LEDRLGVKVI DRTALILDIF AQHAKSVEGR TQVELAQLNY LKQRLRGWGG NLSRQVGGRA SGGVGIGGRG PGETKIEADR RRISHRISVL RSRLRDMDST RAIKRSDRLR RKMASVAIIG YTNAGKSSLL NRLTGAGVLV EDALFATLDP TTRRSTTATG RVFTLTDTVG FVRHLPTDLV EAFRSTLEET LDADLLVHVV DGSDPDPLGQ IEAVHRVLGE IGARNRPEQL VINKIDAANP DTLMILASHN PDAVFCSART GEGIDAVRRA VESGLPVPGV EVEFVIPWTH GELINRVHKE GELILVEHRE NGTYIHAWVY PDLASALENA SE // ID S3Y920_9MICO Unreviewed; 543 AA. AC S3Y920; DT 18-SEP-2013, integrated into UniProtKB/TrEMBL. DT 18-SEP-2013, sequence version 1. DT 05-JUL-2017, entry version 29. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=HMPREF1484_00059 {ECO:0000313|EMBL:EPH18202.1}; OS Dermabacter sp. HFH0086. OC Bacteria; Actinobacteria; Micrococcales; Dermabacteraceae; OC Dermabacter. OX NCBI_TaxID=1203568 {ECO:0000313|EMBL:EPH18202.1, ECO:0000313|Proteomes:UP000014577}; RN [1] {ECO:0000313|EMBL:EPH18202.1, ECO:0000313|Proteomes:UP000014577} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=HFH0086 {ECO:0000313|EMBL:EPH18202.1, RC ECO:0000313|Proteomes:UP000014577}; RG The Broad Institute Genomics Platform; RA Earl A., Ward D., Feldgarden M., Gevers D., Schmidt T.M., Dai D., RA Dover J., Walker B., Young S., Zeng Q., Gargeya S., Fitzgerald M., RA Haas B., Abouelleil A., Allen A.W., Alvarado L., Arachchi H.M., RA Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J., Griggs A., RA Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A., Larimer J., RA McCowan C., Murphy C., Pearson M., Poon T.W., Priest M., Roberts A., RA Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C., RA Birren B.; RT "The Genome Sequence of Dermabacter sp. HFH0086."; RL Submitted (MAY-2013) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EPH18202.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ATFO01000001; EPH18202.1; -; Genomic_DNA. DR EnsemblBacteria; EPH18202; EPH18202; HMPREF1484_00059. DR PATRIC; fig|1203568.3.peg.60; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000014577; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 2. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000014577}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000014577}. FT DOMAIN 325 490 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 543 AA; 59114 MW; FCC47609AE5BD89E CRC64; MAQNAKSSRI GFGRDTLIRR PHARPHLREP GVKAHLTPFV PDPEFETSHA APQAAEPENA GSDARESSIM QRVLSRGDAS ISATTYESDA DGDQLDLAER HSLRRVDQLR TDLEDVTEVE YRELRLENVV LAGLFTTGNV EDAENSMREL AALAETAGSR VLDGVMQRRA HPDPATFLGS GKAKELAEIV ADLRADTVIC DGQLAPSQRR ALEDIIKVKV IDRTALILDI FAQHAKSREG KAQVELAQLE YLLPRLRGWG ESMSRQAGGR VAGGAGIGSR GPGETKIELD RRRIRTRMAK LRRDIKAMAP SREAKRADRK RHNIPSVAIA GYTNAGKSSL LNRLTGAGVL VENALFATLD PTVRRSVTPD GREFTFADTV GFVRSLPTEL VEAFRSTLEE VSGADLLLHV VDASHPDPEG QIRAVRAVLA DIEGFDVPEI VALNKADLAS PETIARLRSQ VEHAAVVSAR TGEGIEELRA LIADMLPRPS VDIDVVVPYT RGDLVSRVHT QGELVSEEFL AEGTRLVARV DETLASELAA ARQ // ID S3ZLI2_9ACTN Unreviewed; 496 AA. AC S3ZLI2; DT 18-SEP-2013, integrated into UniProtKB/TrEMBL. DT 18-SEP-2013, sequence version 1. DT 07-JUN-2017, entry version 29. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=STRAU_2884 {ECO:0000313|EMBL:EPH44078.1}; OS Streptomyces aurantiacus JA 4570. OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae; OC Streptomyces. OX NCBI_TaxID=1286094 {ECO:0000313|EMBL:EPH44078.1, ECO:0000313|Proteomes:UP000014629}; RN [1] {ECO:0000313|EMBL:EPH44078.1, ECO:0000313|Proteomes:UP000014629} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=JA 4570 {ECO:0000313|EMBL:EPH44078.1, RC ECO:0000313|Proteomes:UP000014629}; RA Gruening B.A., Praeg A., Erxleben A., Guenther S., Mueller M.; RT "Draft Genome Sequence of Streptomyces aurantiacus, Which Produces RT Setomimycin."; RL Submitted (FEB-2013) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EPH44078.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AOPZ01000119; EPH44078.1; -; Genomic_DNA. DR RefSeq; WP_016641012.1; NZ_AOPZ01000119.1. DR EnsemblBacteria; EPH44078; EPH44078; STRAU_2884. DR PATRIC; fig|1286094.4.peg.2854; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000014629; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 2. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000014629}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000014629}. FT DOMAIN 275 440 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 496 AA; 53974 MW; F24AACB69D5E9A70 CRC64; MTSSSSPSQD AQSFAQNYPE GLRADALMEE DVAWSHEIDG ERDGEQLDRS ERAALRRVAG LSTELEDVTE VEYRQLRLER VVLVGVWTSG TVDDAENSLA ELAALAETAG AHVLDGVIQR RDKPDPATYI GSGKALELRD IVLETGADTV VCDGELSPGQ LIHLEDVVKV KVVDRTALIL DIFAQHAKSR EGKAQVALAQ MQYMLPRLRG WGQSLSRQMG GGGGGGMATR GPGETKIETD RRRIREKMAK MRREIAEMKT GREIKRQERK RNKVPSVAIA GYTNAGKSSL LNRLTGAGVL VENALFATLD PTVRRAETPS GRLYTLADTV GFVRHLPHHL VEAFRSTMEE VGESDLILHV VDGSHPAPEE QLAAVREVIR DVGATDVPEI VVINKADAAD PLVVQRLLRT QKHAIAVSAR TGLGIEELLA LIDAELPRPE VEIEALVPYT HGQLVSRAHA DGEVLSEEHT AEGTLLKARV HEELAAELAP FVPAAH // ID S4D7H3_ENTFL Unreviewed; 420 AA. AC S4D7H3; DT 18-SEP-2013, integrated into UniProtKB/TrEMBL. DT 18-SEP-2013, sequence version 1. DT 07-JUN-2017, entry version 26. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=D920_01442 {ECO:0000313|EMBL:EPH99074.1}; OS Enterococcus faecalis 13-SD-W-01. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Enterococcaceae; OC Enterococcus. OX NCBI_TaxID=1260356 {ECO:0000313|EMBL:EPH99074.1, ECO:0000313|Proteomes:UP000014594}; RN [1] {ECO:0000313|EMBL:EPH99074.1, ECO:0000313|Proteomes:UP000014594} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=13-SD-W-01 {ECO:0000313|EMBL:EPH99074.1, RC ECO:0000313|Proteomes:UP000014594}; RA Weinstock G., Sodergren E., Lobos E.A., Fulton L., Fulton R., RA Courtney L., Fronick C., O'Laughlin M., Godfrey J., Wilson R.M., RA Miner T., Farmer C., Delehaunty K., Cordes M., Minx P., Tomlinson C., RA Chen J., Wollam A., Pepin K.H., Bhonagiri V., Zhang X., Warren W., RA Mitreva M., Mardis E.R., Wilson R.K.; RL Submitted (JUN-2013) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EPH99074.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ATIO01000090; EPH99074.1; -; Genomic_DNA. DR EnsemblBacteria; EPH99074; EPH99074; D920_01442. DR PATRIC; fig|1260356.4.peg.1266; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000014594; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000014594}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000014594}. FT DOMAIN 203 366 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 420 AA; 47182 MW; 8E1BEC6224B23D23 CRC64; MDGGRKIMEK KEKAVLVGVE TENNYANFEE SMEELKNLTQ TASGEVVYTL TQKRPQVDRQ TLVGKGKLAE LAQQAEANEA DIVIFNHELS PRQSQLIGEA IGLPVIDRVQ LILDIFAMRA RSKEGKLQVE LAQLNYLLPR LAGQGKSLSR LGGGIGTRGP GETKLETDRR HIRNKILAVK KELKTIEAHR ERSRQKRKAS AVFQVGLIGY TNAGKSTILN LLTQADTYSE NQLFATLDPL TKKWRLDEGF EMTITDTVGF IQDLPTQLVN AFHSTLEESQ NMDLLLHVID ASSPDRIQQE KTVLDLMAEL SMENIPVLSV YNKADLIDPA SFTPTLFPNV LISAKSKTGK KDLLQAVKYQ LMEIMTPYTL EVPSSDGQKL SELKRKTLLL SQDFDEERES YIVKGFAQEE RLNNVEKEEH // ID S4N6R1_CHLPS Unreviewed; 451 AA. AC S4N6R1; DT 18-SEP-2013, integrated into UniProtKB/TrEMBL. DT 18-SEP-2013, sequence version 1. DT 10-MAY-2017, entry version 23. DE SubName: Full=GTP-binding protein HflX {ECO:0000313|EMBL:EPJ32159.1}; DE Flags: Fragment; GN Name=hflX {ECO:0000313|EMBL:EPJ32159.1}; GN ORFNames=CP061683_0434A {ECO:0000313|EMBL:EPJ32159.1}; OS Chlamydia psittaci 06-1683. OC Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae; OC Chlamydia/Chlamydophila group; Chlamydia. OX NCBI_TaxID=1112244 {ECO:0000313|EMBL:EPJ32159.1, ECO:0000313|Proteomes:UP000014600}; RN [1] {ECO:0000313|EMBL:EPJ32159.1, ECO:0000313|Proteomes:UP000014600} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=06-1683 {ECO:0000313|EMBL:EPJ32159.1, RC ECO:0000313|Proteomes:UP000014600}; RA Huot-Creasy H., McCracken C.L., Humphries M., Sachse K., Laroucau K., RA Bavoil P., Myers G.S.; RT "Genome sequence of Chlamydia psittaci 06-1683."; RL Submitted (APR-2013) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EPJ32159.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ATLF01000759; EPJ32159.1; -; Genomic_DNA. DR EnsemblBacteria; EPJ32159; EPJ32159; CP061683_0434A. DR Proteomes; UP000014600; Unassembled WGS sequence. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000014600}; KW Reference proteome {ECO:0000313|Proteomes:UP000014600}. FT DOMAIN 228 394 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT NON_TER 451 451 {ECO:0000313|EMBL:EPJ32159.1}. SQ SEQUENCE 451 AA; 51007 MW; A0A98CCE930F0091 CRC64; MKKKRKEEKK SRESALGWRF SLPREEQDPS QALAVACYSG KEEQQRVEEH SEELVSLAES CDITVLETRS WILRSSSSST YLNEGKLLEI EEILKVFPTI GTLIVDEEIT ASQQRNLEKR LGLVVLDRTE LILEIFANRA FTAEAGLQVE LARARYLLPR LKRMWGHLSR QKSGGGSGGG FVKGEGEKQI ELDRRMIRER IHKLTLDLKS VEKQRKERRK AKEKRGIPSF ALIGYTNSGK STLLNLLTSA ETYVEDKLFA TLDPKTRRCV LPSGQRVLVT DTVGFIRKLP HTLVAAFKST LEAALHEDVL LHVVDASHPL AFEHIETTKE ILKELGVDHP KIITVLNKID ALPHGKASTK LRLLSPRAVL ISAKTGEGIQ NLLEAMTDVI TEGFPEVTLK FSYKDYGKFT ELYDAGLVLS HRRKDDILIV EAYLPQELEK RYGPFIARKR S // ID S4XG15_SORCE Unreviewed; 621 AA. AC S4XG15; DT 16-OCT-2013, integrated into UniProtKB/TrEMBL. DT 16-OCT-2013, sequence version 1. DT 05-JUL-2017, entry version 31. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=SCE1572_02935 {ECO:0000313|EMBL:AGP32072.1}; OS Sorangium cellulosum So0157-2. OC Bacteria; Proteobacteria; Deltaproteobacteria; Myxococcales; OC Sorangiineae; Polyangiaceae; Sorangium. OX NCBI_TaxID=1254432 {ECO:0000313|EMBL:AGP32072.1, ECO:0000313|Proteomes:UP000014803}; RN [1] {ECO:0000313|EMBL:AGP32072.1, ECO:0000313|Proteomes:UP000014803} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=So0157-2 {ECO:0000313|EMBL:AGP32072.1, RC ECO:0000313|Proteomes:UP000014803}; RX PubMed=23812535; DOI=10.1038/srep02101; RA Han K., Li Z.F., Peng R., Zhu L.P., Zhou T., Wang L.G., Li S.G., RA Zhang X.B., Hu W., Wu Z.H., Qin N., Li Y.Z.; RT "Extraordinary expansion of a Sorangium cellulosum genome from an RT alkaline milieu."; RL Sci. Rep. 3:2101-2101(2013). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP003969; AGP32072.1; -; Genomic_DNA. DR RefSeq; WP_020732592.1; NC_021658.1. DR EnsemblBacteria; AGP32072; AGP32072; SCE1572_02935. DR KEGG; scu:SCE1572_02935; -. DR PATRIC; fig|1254432.3.peg.643; -. DR KO; K03665; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000014803; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000014803}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000014803}. FT DOMAIN 400 565 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 366 393 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 621 AA; 67927 MW; AEEC3B4AC319CD99 CRC64; MPTLYGNTTG LSPLATKTLE RIYRRKVPLG SIATPELIKA LAEASHETGR QVGALVHRSG EIDYVVVGDA TRLMLPDIGR LRAAQGRFRA LRLVHTHLFN EPLTRDDLVD LVRLRLDLVA AVQLSPQGEP RTLQYAYNVP VHGKEAVTVT VDDEGGDDRG KAELPYRTVG PVAVGRLDVD FGALIQALED EFAKRSRTRS VAAKDGRAIL VHVAEKAKAG ALARAEESLR ELTDLAGTAG VDVADRVLQL RDRIDPRLVL GKGKLDEVVL RASELDAETL VFDRDLTPSQ ASAIAKHTDL KVLDRTQLIL DIFAQRAESS DGKLQVELAQ LKYTLPRLGQ KDDSLSRLTG GIGGRGPGET KLEIGRRRAK ERVSFLEAQL KRLSRQREQR RRRRARLGVP VVSIVGYTNA GKSTLLNTLT GADVLAENKL FATLDTRSRR LRFPEEREVV ITDTVGFIRE LPKDLFAAFR ATFEEAADAD LLLHVVDASD PARDQHIETT EALLTELDLI GIPRVVVFNK ADLIAPEEGR RLLLGHPDAV LLSATDRETT RELLTKLADR LKSRWEEAAM VPAYEAETEG GELEEDGGLF DGEAESMTVL GPPSGAGAEA ISARARGTFG A // ID S4XIM3_SORCE Unreviewed; 474 AA. AC S4XIM3; DT 16-OCT-2013, integrated into UniProtKB/TrEMBL. DT 16-OCT-2013, sequence version 1. DT 05-JUL-2017, entry version 31. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=SCE1572_19160 {ECO:0000313|EMBL:AGP32394.1}; OS Sorangium cellulosum So0157-2. OC Bacteria; Proteobacteria; Deltaproteobacteria; Myxococcales; OC Sorangiineae; Polyangiaceae; Sorangium. OX NCBI_TaxID=1254432 {ECO:0000313|EMBL:AGP32394.1, ECO:0000313|Proteomes:UP000014803}; RN [1] {ECO:0000313|EMBL:AGP32394.1, ECO:0000313|Proteomes:UP000014803} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=So0157-2 {ECO:0000313|EMBL:AGP32394.1, RC ECO:0000313|Proteomes:UP000014803}; RX PubMed=23812535; DOI=10.1038/srep02101; RA Han K., Li Z.F., Peng R., Zhu L.P., Zhou T., Wang L.G., Li S.G., RA Zhang X.B., Hu W., Wu Z.H., Qin N., Li Y.Z.; RT "Extraordinary expansion of a Sorangium cellulosum genome from an RT alkaline milieu."; RL Sci. Rep. 3:2101-2101(2013). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP003969; AGP32394.1; -; Genomic_DNA. DR RefSeq; WP_020735771.1; NC_021658.1. DR EnsemblBacteria; AGP32394; AGP32394; SCE1572_19160. DR KEGG; scu:SCE1572_19160; -. DR PATRIC; fig|1254432.3.peg.4334; -. DR KO; K03665; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000014803; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 2. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000014803}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000014803}. FT DOMAIN 255 420 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 216 243 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 474 AA; 51016 MW; 9510038ED5B13F2E CRC64; MTTTQQERPL AVLVGVQLPG VDDVEHAADL AELGRLVHTL GFDVIATVSQ RRSALAAAAV LGEGKLKELA ELTGGSGVVP SGAPERKNKA RARRAAESGE GDDDGELGGD DVDDADEDGV GAAPDAGGRE ARRATVVAVD HDISPSQARN LERATGAQVL DRAGVIIEIF HRHARSREAK LEVEIARLNY VAPRLRETGG GGDRQRGGIG GKGAGESALE LDRRKIRDRI AELKQELSGV QREQSTRRAL RQGQRRVALV GYTNAGKSSL MRALTGSEVL VADKLFATLD TTVRALHPEV RPRILVSDTV GFIKKLPHDL VASFRSTLDE ALEASLLLYV ADASDPTFRD QLGVTRSVLS EIGASEVPSR LLLNKVDRLS EEEREALRLE FPEATLLSAK IPADVAGLRE AIIAFFEQSM VEAELLLPYA KQSLIGEIYE NARVLSEEYD DAGGRLSVRA HPAALDRLRS LLAR // ID S5QWH9_9STRE Unreviewed; 412 AA. AC S5QWH9; DT 16-OCT-2013, integrated into UniProtKB/TrEMBL. DT 16-OCT-2013, sequence version 1. DT 30-AUG-2017, entry version 30. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=KE3_0706 {ECO:0000313|EMBL:AGS05212.1}; OS Streptococcus lutetiensis 033. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=1076934 {ECO:0000313|EMBL:AGS05212.1, ECO:0000313|Proteomes:UP000015268}; RN [1] {ECO:0000313|EMBL:AGS05212.1, ECO:0000313|Proteomes:UP000015268} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=033 {ECO:0000313|EMBL:AGS05212.1, RC ECO:0000313|Proteomes:UP000015268}; RX PubMed=23782707; DOI=10.1186/1471-2180-13-141; RA Jin D., Chen C., Li L., Lu S., Li Z., Zhou Z., Jing H., Xu Y., Du P., RA Wang H., Xiong Y., Zheng H., Bai X., Sun H., Wang L., Ye C., RA Gottschalk M., Xu J.; RT "Dynamics of fecal microbial communities in children with diarrhea of RT unknown etiology and genomic analysis of associated Streptococcus RT lutetiensis."; RL BMC Microbiol. 13:141-141(2013). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP003025; AGS05212.1; -; Genomic_DNA. DR RefSeq; WP_020916507.1; NC_021900.1. DR EnsemblBacteria; AGS05212; AGS05212; KE3_0706. DR KEGG; slu:KE3_0706; -. DR PATRIC; fig|1076934.5.peg.646; -. DR KO; K03665; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000015268; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000015268}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000015268}. FT DOMAIN 199 359 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 158 192 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 412 AA; 46962 MW; AF9F6E7271B19608 CRC64; MIETSKHQER VILLGVELSD TENFEMSMEE LASLAETAGA EVVSSYRQKR EKYDSKSLIG SGKLAEIKAI VDADAIDTVI VNDRLTPRQN VNLEAELGVK VIDRMQLILD IFAMRARSHE GKLQVHLAQL KYMLPRLVGQ GVMLSRQAGG IGSRGPGESQ LELNRRSIRN QISDIERQLK IVEKNRETGR EKRTESQVFK IGLIGYTNAG KSTIMNVLTN DKQYEADELF ATLDATTKQI YLQNQFQVTL TDTVGFIQNL PTELVAAFKS TLEESRHVDL LLHVIDASDP NHAEHEKVVL NLLKNLDMLD IPRLAVYNKM DVAEHFAATA FPNVRISARD KDARSLLRRL IINEIREIFE PFSIRVHPNQ AYKLYDLNKI ALLDRYDFAE GYETITGYIN PKNRWRLEEF YD // ID S5SV18_9CORY Unreviewed; 524 AA. AC S5SV18; DT 16-OCT-2013, integrated into UniProtKB/TrEMBL. DT 16-OCT-2013, sequence version 1. DT 07-JUN-2017, entry version 29. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=B841_07730 {ECO:0000313|EMBL:AGS35019.1}; OS Corynebacterium maris DSM 45190. OC Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae; OC Corynebacterium. OX NCBI_TaxID=1224163 {ECO:0000313|EMBL:AGS35019.1, ECO:0000313|Proteomes:UP000015388}; RN [1] {ECO:0000313|EMBL:AGS35019.1, ECO:0000313|Proteomes:UP000015388} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Coryn-1 {ECO:0000313|Proteomes:UP000015388}; RA Schaffert L., Albersmeier A., Kalinowski J., Ruckert C.; RT "The complete genome sequence of Corynebacterium maris Coryn-1 (=DSM RT 45190)."; RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP003924; AGS35019.1; -; Genomic_DNA. DR RefSeq; WP_020934952.1; NC_021915.1. DR EnsemblBacteria; AGS35019; AGS35019; B841_07730. DR KEGG; cmd:B841_07730; -. DR PATRIC; fig|1224163.3.peg.1551; -. DR KO; K03665; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000015388; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000015388}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000015388}. FT DOMAIN 283 454 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 242 269 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 524 AA; 57375 MW; 096D07DB46746ED6 CRC64; MTKRDKNDEL LARAFRDNTP QPEEQEDPGV DLSDLTSPHQ PATPTTGELD LSERDSFRRA TRQTTIRTED AADVTEVEYR KLRLEQVVLV GVWSTGTTAE VDASMNELAA LAETAGAEVV EMLYQKRDKP DPGTYIGSGK VDQLRDVIDA TGADTVIADG ELSPGQLVAL EDRLNAKVID RTMLILDIFA QHAKSKEGKA QVSLAQMEYL YNRVRGWGGN LSRQAGGRAG SNGGVGLRGP GETKIESDRR RLRTEMAKLR KELTGMKTAR EIKRSQRRSS VVPQIAIAGY TNAGKSSLIN AITGAGVLVE DALFATLDPT TRRAQLADGR AVVFTDTVGF VRHLPTQLVE AFKSTLEEVL GADLILHVVD GSDPFPLKQI EAVNKVIYDI VRETGEEMPA EMIVINKIDQ ADPLVLAELR HVLGHEDVVF LSAKTGEGVD ELTSRIELFL NSRDAHVQLA LPFTRGDLVS YVHEVGTVLE EEYSGEGTLI DVRLPRRVAE ELAEFIVSGD DVEDEVGEPE AKRA // ID S5UY57_STRC3 Unreviewed; 469 AA. AC S5UY57; DT 16-OCT-2013, integrated into UniProtKB/TrEMBL. DT 16-OCT-2013, sequence version 1. DT 07-JUN-2017, entry version 31. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=B446_27125 {ECO:0000313|EMBL:AGS72233.1}; OS Streptomyces collinus (strain DSM 40733 / Tu 365). OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae; OC Streptomyces. OX NCBI_TaxID=1214242 {ECO:0000313|EMBL:AGS72233.1, ECO:0000313|Proteomes:UP000015423}; RN [1] {ECO:0000313|Proteomes:UP000015423} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 40733 / Tu 365 {ECO:0000313|Proteomes:UP000015423}; RA Ruckert C., Szczepanowski R., Goesmann A., Pross E.K., Musiol E.M., RA Blin K., Wohlleben W., Puhler A., Weber T., Kalinowski J.; RT "The complete genome sequence of Streptomyces collinus Tu 365."; RL Submitted (OCT-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP006259; AGS72233.1; -; Genomic_DNA. DR EnsemblBacteria; AGS72233; AGS72233; B446_27125. DR KEGG; sci:B446_27125; -. DR PATRIC; fig|1214242.5.peg.5555; -. DR KO; K03665; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000015423; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000015423}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000015423}. FT DOMAIN 247 412 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 469 AA; 51386 MW; 45E04DDC52C66087 CRC64; MEEDVAWSHE IDGERDGDQF DRSERAALRR VVGLSTELED VTEVEYRQLR LERVVLVGVW TTGTAQDADN SLAELAALAE TAGALVLDGV IQRRDKPDAA TYIGSGKALE LRDIVLESGA DTVICDGELS PGQLIQLEDV VKVKVIDRTA LILDIFAQHA KSREGKAQVA LAQMQYMLPR LRGWGQSLSR QMGGGRGGLA TRGPGETKIE TDRRRIREKM AKMRREIAEM KTGREIKRQE RRRNKVPSVA IAGYTNAGKS SLLNRLTGAG VLVENALFAT LDPTVRRAET PSGRLYTLAD TVGFVRHLPH HLVEAFRSTM EEVGDADLIL HVVDGSHPDP EEQLAAVREV IRDVGATDVP EIVVINKADA ADPLVLQRLL RVEKRSIAVS ARTGRGIEQL LTLIDDELPR PSVEVEALVP YTHGKLVARA HTEGEVISEE HTAEGTLLKV RVHEELAADL APYTPAPAA // ID S5XRI5_PARAH Unreviewed; 435 AA. AC S5XRI5; DT 16-OCT-2013, integrated into UniProtKB/TrEMBL. DT 16-OCT-2013, sequence version 1. DT 07-JUN-2017, entry version 30. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=JCM7686_0583 {ECO:0000313|EMBL:AGT07692.1}; OS Paracoccus aminophilus JCM 7686. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae; Paracoccus. OX NCBI_TaxID=1367847 {ECO:0000313|EMBL:AGT07692.1, ECO:0000313|Proteomes:UP000015480}; RN [1] {ECO:0000313|EMBL:AGT07692.1, ECO:0000313|Proteomes:UP000015480} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=JCM 7686 {ECO:0000313|EMBL:AGT07692.1}; RX PubMed=24517536; DOI=10.1186/1471-2164-15-124; RA Dziewit L., Czarnecki J., Wibberg D., Radlinska M., Mrozek P., RA Szymczak M., Schluter A., Puhler A., Bartosik D.; RT "Architecture and functions of a multipartite genome of the RT methylotrophic bacterium Paracoccus aminophilus JCM 7686, containing RT primary and secondary chromids."; RL BMC Genomics 15:124-124(2014). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP006650; AGT07692.1; -; Genomic_DNA. DR RefSeq; WP_020949331.1; NC_022041.1. DR EnsemblBacteria; AGT07692; AGT07692; JCM7686_0583. DR KEGG; pami:JCM7686_0583; -. DR PATRIC; fig|1367847.3.peg.534; -. DR KO; K03665; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000015480; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000015480}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000015480}. FT DOMAIN 211 380 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 435 AA; 48049 MW; E6A72E054A5674D7 CRC64; MSDNNETRAL PTRAYVLHPD LGNSRTRRSP ELALEEAVAL AHALPAITVE GAEVVRLRTP EAGMLFSKGK REEVAQHLKA VADGEGAELV LIDGPVTPVQ QRNLEKEWGV KILDRTGLIL EIFADRAQTR EGVLQVELAA LAYQRTRLVR AWTHLERQRG GLGFVGGPGE TQIEADRRAI DEQMTRLRRQ LEKVVRTREL HRRSRAKVPY PIVALVGYTN AGKSTLFNKL TGAEVVAKDQ LFATLDPTMR QMRLPSGRRV ILSDTVGFIS DLPHELVAAF RATLEEVLEA DLILHVRDIS HPETEEQAGD VGEILDGLGV DEDVALIEVW NKIDALGPET RAALLRTDAR TEGVQAVSAL SGEGIDALLQ TVDSVLTKAL DDPIHDSVVE LSHGDGRRRA WLHEQGVVTS ERPTASGVRL QVRWTERQEN TFNAL // ID S5ZT71_9SPIO Unreviewed; 385 AA. AC S5ZT71; DT 16-OCT-2013, integrated into UniProtKB/TrEMBL. DT 16-OCT-2013, sequence version 1. DT 07-JUN-2017, entry version 28. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=TPE_0824 {ECO:0000313|EMBL:AGT43320.1}; OS Treponema pedis str. T A4. OC Bacteria; Spirochaetes; Spirochaetales; Spirochaetaceae; Treponema. OX NCBI_TaxID=1291379 {ECO:0000313|EMBL:AGT43320.1, ECO:0000313|Proteomes:UP000015620}; RN [1] {ECO:0000313|EMBL:AGT43320.1, ECO:0000313|Proteomes:UP000015620} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=T A4 {ECO:0000313|EMBL:AGT43320.1}; RX PubMed=23977007; DOI=10.1371/journal.pone.0071281; RA Svartstrom O., Mushtaq M., Pringle M., Segerman B.; RT "Genome-Wide Relatedness of Treponema pedis, from Gingiva and Necrotic RT Skin Lesions of Pigs, with the Human Oral Pathogen Treponema RT denticola."; RL PLoS ONE 8:E71281-E71281(2013). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP004120; AGT43320.1; -; Genomic_DNA. DR EnsemblBacteria; AGT43320; AGT43320; TPE_0824. DR KEGG; tped:TPE_0824; -. DR PATRIC; fig|1291379.3.peg.820; -. DR KO; K03665; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000015620; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000015620}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000015620}. FT DOMAIN 216 385 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 175 202 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 385 AA; 42976 MW; 593732EEA84A8922 CRC64; MNLIKLKQEQ KKAVLVFTDI YSQVKNSLIH TNVKNLTALQ SVEESELKSL SETILVNPVF SLRFKIGSPN PATLVGSGQL EKILNVAEEK NADLIIFNCD LSPRIQRNLE EVSGLCVIDR REVIIQIFAD RAQTREAVLQ ARLAQLEYSM PRLTRKWTGL SQQRGGVKGS RGAGEKKLEL DKRRLRTEIS KLRKEVEKVR VQRNVQRKSR TEGNKKIGAI VGYTNAGKSS LLKKLSGTDI FAENKLFATL DSETRKIFFP NKTGGVQFLL TDTVGFVSNL PHQLIDAFHS TLEEAALADF LIILCDASHP AMCECLAVTQ SVLEELNCGK KNAIIVINKI DCVFDPASIL QLKTRYPEAV EISLKTGEGL DFLKIKLEEI VNTVL // ID S6AG93_9PROT Unreviewed; 451 AA. AC S6AG93; DT 16-OCT-2013, integrated into UniProtKB/TrEMBL. DT 16-OCT-2013, sequence version 1. DT 30-AUG-2017, entry version 34. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=SCD_n01181 {ECO:0000313|EMBL:BAN35011.1}; OS Sulfuricella denitrificans skB26. OC Bacteria; Proteobacteria; Betaproteobacteria; Nitrosomonadales; OC Gallionellaceae; Sulfuricella. OX NCBI_TaxID=1163617 {ECO:0000313|EMBL:BAN35011.1, ECO:0000313|Proteomes:UP000015559}; RN [1] {ECO:0000313|EMBL:BAN35011.1, ECO:0000313|Proteomes:UP000015559} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SkB26 {ECO:0000313|EMBL:BAN35011.1}; RX PubMed=22773644; DOI=10.1128/AEM.01349-12; RA Watanabe T., Kojima H., Fukui M.; RT "Draft genome sequence of a psychrotolerant sulfur-oxidizing RT bacterium, Sulfuricella denitrificans skB26, and proteomic insights RT into cold adaptation."; RL Appl. Environ. Microbiol. 78:6545-6549(2012). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AP013066; BAN35011.1; -; Genomic_DNA. DR RefSeq; WP_009206038.1; NC_022357.1. DR EnsemblBacteria; BAN35011; BAN35011; SCD_n01181. DR KEGG; sdr:SCD_n01181; -. DR KO; K03665; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000015559; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000015559}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000015559}. FT DOMAIN 225 395 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 451 AA; 49993 MW; 8D17C3F55171FE19 CRC64; MRKEVKEKPK YAVVASVQLP NVSDVEFESS LAELRDLAKT LGFEIAATFT QKRTSFDTTA YLGAGKRQEI RAFVDNEPEP VELERTPQAA ADPSAGKIDV VFVDHEISPS QARNLEIEVG CKVMDRTMVI LEIFHRHASS RAARAQVEIA RLGYMAPRLR EAAKLAGPQG RQRSGTGGRG AGESHTELDK RKIRDRIAEL QLEIAAMDVE RKTQRSRRQE RQGLANVALV GYTNAGKSTL MRALTGSEVL VENKLFATLD TTVRALQPES RPRVLVSDTV GFIKNLPHGL VASFKSTLEE ALDASLLLHV IDASDPGFER QLEVTDKVLA EIGAKDVPRI RVFNKIDHVG TTEAQAEREA ALRTQYPDCI VMSARRTGDV AKLREAIVTF FQQGLVEAEL FLPWSAQQLR GEIFASCEVR EERADSEGAF LRIRGDRETV KGLCERFGQA Q // ID S6AWY5_PSERE Unreviewed; 433 AA. AC S6AWY5; DT 16-OCT-2013, integrated into UniProtKB/TrEMBL. DT 16-OCT-2013, sequence version 1. DT 30-AUG-2017, entry version 29. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:BAN50913.1}; GN ORFNames=PCA10_51810 {ECO:0000313|EMBL:BAN50913.1}; OS Pseudomonas resinovorans NBRC 106553. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=1245471 {ECO:0000313|EMBL:BAN50913.1, ECO:0000313|Proteomes:UP000015503}; RN [1] {ECO:0000313|EMBL:BAN50913.1, ECO:0000313|Proteomes:UP000015503} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NBRC 106553 {ECO:0000313|EMBL:BAN50913.1}; RA Shintani M., Hosoyama A., Ohji S., Tsuchikane K., Takarada H., RA Yamazoe A., Fujita N., Nojiri H.; RT "Complete Genome Sequence of the Carbazole Degrader Pseudomonas RT resinovorans Strain CA10 (NBRC 106553)."; RL Genome Announc. 1:e00488-13(2013). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AP013068; BAN50913.1; -; Genomic_DNA. DR RefSeq; WP_016495040.1; NC_021499.1. DR EnsemblBacteria; BAN50913; BAN50913; PCA10_51810. DR KEGG; pre:PCA10_51810; -. DR PATRIC; fig|1245471.3.peg.5259; -. DR KO; K03665; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000015503; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000015503}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000015503}. FT DOMAIN 199 366 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 165 192 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 433 AA; 48769 MW; EE25F166DFD0A93A CRC64; MFFERPGGGE RAILVHLEGQ DPEAREDPQE FLELARSAGA ETVAFISVTR HQPTAKYLIG SGKVDELHDL VQAEKAELVI FNHTLTPSQE RNLERAFECR VLDRTGLILD IFAQRARTHE GKLQVELAQL EHMSTRLVRG WTHLERQKGG IGLRGPGETQ LETDRRLLRV RIRQIKQRLE KVRSQREQAR RGRKRADIPV VSLVGYTNAG KSTLFNSLTT SEVYAADQLF ATLDPTLRRL ELDDLGPVVL ADTVGFIRHL PHKLVEAFRA TLEESANADL LLHVIDAHEP ERMAQIEQVL AVLGEIGAEG LPMLEVYNKV DLLENVEPHI QRDADGKPER VWLSAREGSG VELLEQAVAE LLGDDLFVGT LCLPQRFGRL RAQFFALGAV QTEDHNEAGD ILLAVRLPRV ELNRLVSREG WQPSEFLEQH TLQ // ID S6B4W2_9PROT Unreviewed; 383 AA. AC S6B4W2; DT 16-OCT-2013, integrated into UniProtKB/TrEMBL. DT 16-OCT-2013, sequence version 1. DT 30-AUG-2017, entry version 28. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=SCD_n01801 {ECO:0000313|EMBL:BAN35612.1}; OS Sulfuricella denitrificans skB26. OC Bacteria; Proteobacteria; Betaproteobacteria; Nitrosomonadales; OC Gallionellaceae; Sulfuricella. OX NCBI_TaxID=1163617 {ECO:0000313|EMBL:BAN35612.1, ECO:0000313|Proteomes:UP000015559}; RN [1] {ECO:0000313|EMBL:BAN35612.1, ECO:0000313|Proteomes:UP000015559} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SkB26 {ECO:0000313|EMBL:BAN35612.1}; RX PubMed=22773644; DOI=10.1128/AEM.01349-12; RA Watanabe T., Kojima H., Fukui M.; RT "Draft genome sequence of a psychrotolerant sulfur-oxidizing RT bacterium, Sulfuricella denitrificans skB26, and proteomic insights RT into cold adaptation."; RL Appl. Environ. Microbiol. 78:6545-6549(2012). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AP013066; BAN35612.1; -; Genomic_DNA. DR RefSeq; WP_009204803.1; NC_022357.1. DR EnsemblBacteria; BAN35612; BAN35612; SCD_n01801. DR KEGG; sdr:SCD_n01801; -. DR KO; K03665; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000015559; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000015559}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000015559}. FT DOMAIN 198 364 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 383 AA; 42050 MW; 39149C68B4B05E80 CRC64; MIERPGSGDA AVLVSLDFGD TDYEESLEEL QRLTESAGVG ILGIVRGKRS RPDAALFAGS GKADEIGESV IANEANLVIF NHELSPAQQR NLEQRMNCRV IDRTSLILDI FAQRAQSHEG KLQVELAQLE HLATRLVRGW THLERQKGGI GLRGPGETQL ETDRRLLGKR VKLLKEKLAK LGRQRCVQRR ARVRANVLSV SIVGYTNAGK STLFNRLTHA KAYVADQLFA TLDTTSRKFF VADGGSVVLS DTVGFIKHLP HTLVAAFRAT LEEAVAADLL LHVVDASSPG RDQQIEEVNK VLAEIGADHI PQLMVLNKID VNGLAPGVER DEYGRISRIW VSARTGEGFD LLREALAEYS RQHQAEAVRA VVQASVDTGF NLN // ID S6BRZ8_9GAMM Unreviewed; 458 AA. AC S6BRZ8; DT 16-OCT-2013, integrated into UniProtKB/TrEMBL. DT 16-OCT-2013, sequence version 1. DT 05-JUL-2017, entry version 28. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:BAN68794.1}; GN ORFNames=EBS_0853 {ECO:0000313|EMBL:BAN68794.1}; OS endosymbiont of unidentified scaly snail isolate Monju. OC Bacteria; Proteobacteria; Gammaproteobacteria. OX NCBI_TaxID=1248727 {ECO:0000313|EMBL:BAN68794.1, ECO:0000313|Proteomes:UP000015562}; RN [1] {ECO:0000313|EMBL:BAN68794.1, ECO:0000313|Proteomes:UP000015562} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Monju {ECO:0000313|EMBL:BAN68794.1}; RX PubMed=23924784; DOI=10.1038/ismej.2013.131; RA Nakagawa S., Shimamura S., Takaki Y., Suzuki Y., Murakami S., RA Watanabe T., Fujiyoshi S., Mino S., Sawabe T., Maeda T., Makita H., RA Nemoto S., Nishimura S., Watanabe H., Watsuji T., Takai K.; RT "Allying with armored snails: the complete genome of RT gammaproteobacterial endosymbiont."; RL ISME J. 8:40-51(2014). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AP012978; BAN68794.1; -; Genomic_DNA. DR EnsemblBacteria; BAN68794; BAN68794; EBS_0853. DR KEGG; enm:EBS_0853; -. DR KO; K03665; -. DR Proteomes; UP000015562; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000015562}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000015562}. FT DOMAIN 198 365 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 458 AA; 51286 MW; 94D136B4B74CCEB5 CRC64; MFERPQRGER AILVHVAFHG APDPEALREF SELAISAGAE PQALVTAQRH APDRRLFVGS GKAEEIRAEV LAREAQLVIF DHELSPSQER NLERFFECRV LDRTGLILDI FAQRARSHEG KLQVELAQLR HLSTRLIRGW THLERQKGGI GLRGPGETQL ETDRRLLGQR IDQIRRRLAR VDSQRAQGRR ARQRAETPTV SLVGYTNAGK STLFNRLTDA HVYAQDQLFA TLDPTLRRLV LDGCPPVVLA DTVGFVSRLP HDLVAAFRST LQETAEADLL LHVIDAASPR RAENIAEVED VLAQIGALEV PRLNIYNKID CIEDAEPRID RDASGRAVAV WLSAADGRGC DLLLQVLAER FAEQAVRRRI CLPPEQGRLR ALLFARGCVP CCSRAAGCSP RKRPMMAVAA WRWNSRRRST SACASTRPGW PRIGRHWAKT ALPRRLRGQM NADSTARC // ID S6CET1_9ACTN Unreviewed; 440 AA. AC S6CET1; DT 16-OCT-2013, integrated into UniProtKB/TrEMBL. DT 16-OCT-2013, sequence version 1. DT 07-JUN-2017, entry version 31. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=AEQU_1053 {ECO:0000313|EMBL:BAN77022.1}; OS Adlercreutzia equolifaciens DSM 19450. OC Bacteria; Actinobacteria; Coriobacteriia; Eggerthellales; OC Eggerthellaceae; Adlercreutzia. OX NCBI_TaxID=1384484 {ECO:0000313|EMBL:BAN77022.1, ECO:0000313|Proteomes:UP000015924}; RN [1] {ECO:0000313|EMBL:BAN77022.1, ECO:0000313|Proteomes:UP000015924} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 19450 {ECO:0000313|EMBL:BAN77022.1}; RA Toh H., Oshima K., Suzuki T., Hattori M., Morita H.; RT "Complete Genome Sequence of the Equol-Producing Bacterium RT Adlercreutzia equolifaciens DSM 19450T."; RL Genome Announc. 1:e00742-13(2013). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AP013105; BAN77022.1; -; Genomic_DNA. DR RefSeq; WP_022739911.1; NC_022567.1. DR EnsemblBacteria; BAN77022; BAN77022; AEQU_1053. DR KEGG; aeq:AEQU_1053; -. DR PATRIC; fig|1384484.3.peg.1073; -. DR KO; K03665; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000015924; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000015924}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000015924}. FT DOMAIN 217 382 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 440 AA; 48020 MW; 1A48EDF8BE3B36A4 CRC64; MTEYESVIQK GPATKAEERR ERAVLVGVER PGLPWPLESS LAELERLADT AGADVVATTT QRLDAPNPRT FVGTGKADEI AELARSREAD LVIFDDELTP SQQANLEKVM DKSVKVIDRT ALILDIFALH ATSKEGRLQV RLAQNQYLYP RLRGMWAHLA SNRMGGGVGS RFGEGESQLE VDRRMVRKRI TSIRRELERL SDVRSLQRES RYGSGMFKVA LAGYTNAGKS SLINRLTGAD VLSYDKLFAT LDSTTRKFEL PEGREVTVTD TVGFIQKLPT TLVEAFKSTL DEITGADLVL HVIDASSPEF EGQIEAVCEV LDQIGAQSIP TIAAFNKCDL LDAETLAGLK RRYPSAQFVS ARTGEGIEGL VGAIAQAASA ADTKLDVLIP YQRGDLVSLA HERCHIISES HGEAGTRLQL LVAPAFVSTF SSYLVPEGDA // ID S6ES92_9CLOT Unreviewed; 598 AA. AC S6ES92; DT 16-OCT-2013, integrated into UniProtKB/TrEMBL. DT 16-OCT-2013, sequence version 1. DT 05-JUL-2017, entry version 27. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=CCH01_013530 {ECO:0000313|EMBL:CDG02065.1}, GN CCH01_16930 {ECO:0000313|EMBL:SLK19520.1}; OS Clostridium chauvoei JF4335. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=1351755 {ECO:0000313|EMBL:CDG02065.1, ECO:0000313|Proteomes:UP000018215}; RN [1] {ECO:0000313|EMBL:CDG02065.1, ECO:0000313|Proteomes:UP000018215} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=JF4335 {ECO:0000313|EMBL:CDG02065.1}; RA Falquet L., Calderon-Copete S.P., Frey J.; RT "Draft genome sequence and toxins identification of the virulent RT Clostridium chauvoei reference strain JF4335."; RL Submitted (JUN-2013) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:SLK19520.1, ECO:0000313|Proteomes:UP000190476} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=JF4335 {ECO:0000313|EMBL:SLK19520.1}; RA Afonso C.L., Miller P.J., Scott M.A., Spackman E., Goraichik I., RA Dimitrov K.M., Suarez D.L., Swayne D.E.; RL Submitted (MAR-2017) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CBML010000006; CDG02065.1; -; Genomic_DNA. DR EMBL; LT799839; SLK19520.1; -; Genomic_DNA. DR RefSeq; WP_021876008.1; NZ_LT799839.1. DR Proteomes; UP000018215; Unassembled WGS sequence. DR Proteomes; UP000190476; Chromosome i. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000018215}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000018215}. FT DOMAIN 364 541 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 598 AA; 67615 MW; 5399775FDEFDB633 CRC64; MIYGNIDGVK KCFLEELENL YKTKVLKDET FSMEILETIT RISTILEREV SVGVDRRGKV VSVAIGDSTS VEIGMIDIKE KRLSGVRIIH THPNGLCNFS ALDLTALLKL KLDAIVAVGI YGGKIIDCSL GMLTITDDML DYEEKNNLSV DEILSINILD KIKYIEGLIK EKEIIEEDEE KAILVGSDTK ESLEELKELT KACEIPVLDM IFQSRSKIDP AFYIGKGKVL EIAHLRQTER ANLIIFDDEL SGSQVRNLEA ALGAKVIDRT TLILEIFARR ARSKESKIQV ELAQLKYRLG RLQGLGTVLS RTGGGIGTRG PGEKKLETDR RHIRETIYDL NAELKKIKKI RETQREKRNK ESIPKVSLVG YTNAGKSTLR NKLCDIATQK EAKEKEKVFE ADMLFATLDI TTRAIVLGNK GVVTLTDTVG FVRKLPHDLV EAFKSTLEEV IYSDLLCHVV DTSSNYALEQ IKAVEDVLEE LGAKDKDTIL VLNKIDKATE EQIQVVKEAC KEYNTIEISA KEGLNLENLL KIIEEQLPYK MKKCEYLIPY DRSDMNSYLH RNGRVFEEDY RNEGTYMLVE LDDETFNKSS EFIINTII // ID S6EYB4_AVIPA Unreviewed; 452 AA. AC S6EYB4; DT 16-OCT-2013, integrated into UniProtKB/TrEMBL. DT 16-OCT-2013, sequence version 1. DT 30-AUG-2017, entry version 27. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=AJF4211_000740 {ECO:0000313|EMBL:CDF97763.1}; OS Avibacterium paragallinarum JF4211. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Avibacterium. OX NCBI_TaxID=1351754 {ECO:0000313|EMBL:CDF97763.1, ECO:0000313|Proteomes:UP000015362}; RN [1] {ECO:0000313|EMBL:CDF97763.1, ECO:0000313|Proteomes:UP000015362} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=JF4211 {ECO:0000313|EMBL:CDF97763.1, RC ECO:0000313|Proteomes:UP000015362}; RA Aguilar-Bultet L., Calderon-Copete S.P., Frey J., Falquet L.; RT "Draft genome sequence of the virulent Avibacterium paragallinarum RT serotype A strain JF4211 and identification of two toxins."; RL Submitted (JUN-2013) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:CDF97763.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CBMK010000002; CDF97763.1; -; Genomic_DNA. DR Proteomes; UP000015362; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000015362}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000015362}. FT DOMAIN 224 391 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 190 220 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 452 AA; 51108 MW; FF802F469AB13AFB CRC64; MDNQYPKSAV QNLDEISTAL FLSSETSSTA DPVRDRGIIV QAFFSAEKNL DDLNEFQLLA KSAQVEIAAT ITTSRATPQA KYFIGQGKAE EIAQAVQTYN ANVILVNHCL TPAQTRNLEA LCECRVVDRT GLILDIFAQR ARFHEGKLQV ELAQLKHLST RLVRRKTGLD QQKGAVGLRG LGETQLESDR RLIKVRIAQL QNRLNKVEKQ RNQNRQTRKK ADIPTLSLVG YTNAGKSTLF NVLTNAEVYA ADQLFATLDP TLRRLTIQDI GATILADTVG FIRELPHDLV SAFKSTLQET TEASLLLHVV DCTDARKLDN IQAVNEVLQE IQADSVPTLL VYNKIDQVEN LAPHIEYDEQ NRPIAVYISA HQQQGIELLT DAIRQRLSKN MLHLHLTLPP QEGQIRHWLY EMGCIRQEQI SEQGEFLLEI NLEQSEWKKL LKKRPHLIHY QT // ID S6GFS0_9GAMM Unreviewed; 432 AA. AC S6GFS0; DT 16-OCT-2013, integrated into UniProtKB/TrEMBL. DT 16-OCT-2013, sequence version 1. DT 07-JUN-2017, entry version 25. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=OFPII_25390 {ECO:0000313|EMBL:EPJ45891.1}; OS Osedax symbiont Rs1. OC Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales; OC unclassified Oceanospirillaceae. OX NCBI_TaxID=1330036 {ECO:0000313|EMBL:EPJ45891.1, ECO:0000313|Proteomes:UP000014822}; RN [1] {ECO:0000313|EMBL:EPJ45891.1, ECO:0000313|Proteomes:UP000014822} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Rs1 {ECO:0000313|Proteomes:UP000014822}; RA Yi H., Goffredi S.; RT "Comparative genomics of two novel heterotrophic symbionts of deep-sea RT Osedax worms: functional variation and environmental selection."; RL Submitted (MAY-2013) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EPJ45891.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ASZJ01000114; EPJ45891.1; -; Genomic_DNA. DR PATRIC; fig|1330036.3.peg.2432; -. DR Proteomes; UP000014822; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000014822}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000014822}. FT DOMAIN 199 366 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 432 AA; 48598 MW; DA63F6D64AE334D3 CRC64; MFFERPESGE RAILVHMEMA AEADQESPRE LEELALSAGA DPIEMLTGSR SKPSPKYYIG SGKLDELKQL VHKHEATLVI FNHAMSPAQE RNVETELECR VLDRTGLILD IFAQRARTHE GKLQVELAQL EHMSTRLVRG WTHLDREKGG IGLRGPGEKQ LETDRRLLRE RVKTIHKRLQ KVRTQREQGR KARARAEIPT LALVGYTNAG KSSIFNKITR AHVYAADQLF ATLDPTLRKI DLADVGAAIL VDTVGFIRHL PHKLVESFRA TLQETAEATL LLHVIDSQDE ERAKNMLEVD AVLAEIGASD VPILQLYNKI DMLDGQRSRI DYDSEGKPVR VWLSAVSGEG LDLMSQAITQ LLCEDLIVDV IKVAPQYGQL RSLLFEKGAV VSESIAENGD MLISVRVQRK YLLQMLTRVG MPTEPYRIVE VY // ID S6GKF2_9GAMM Unreviewed; 432 AA. AC S6GKF2; DT 16-OCT-2013, integrated into UniProtKB/TrEMBL. DT 16-OCT-2013, sequence version 1. DT 07-JUN-2017, entry version 28. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=OFPI_35370 {ECO:0000313|EMBL:EPJ46064.1}; OS Osedax symbiont Rs2. OC Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales; OC unclassified Oceanospirillaceae. OX NCBI_TaxID=1330035 {ECO:0000313|EMBL:EPJ46064.1, ECO:0000313|Proteomes:UP000014830}; RN [1] {ECO:0000313|EMBL:EPJ46064.1, ECO:0000313|Proteomes:UP000014830} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Rs2 {ECO:0000313|Proteomes:UP000014830}; RA Yi H., Goffredi S.; RT "Comparative genomics of two novel heterotrophic symbionts of deep-sea RT Osedax worms: functional variation and environmental selection."; RL Submitted (MAY-2013) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EPJ46064.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ASZI01000289; EPJ46064.1; -; Genomic_DNA. DR PATRIC; fig|1330035.3.peg.3414; -. DR Proteomes; UP000014830; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000014830}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000014830}. FT DOMAIN 199 366 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 158 185 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 432 AA; 48579 MW; 28CDAC326BAC68CE CRC64; MFFERPESGE RAILVHMDMA VEADQESPRE LEELALSAGA DPIEMLTGSR SKPSPKYFIG SGKLDELKQL VHQHEATLVI FNHAMSPAQE RNVETELECR VLDRTGLILD IFAQRARTHE GKLQVELAQL EHMSTRLVRG WTHLDREKGG IGLRGPGEKQ LETDRRLLRE RVKTINKRLQ KVRTQREQGR KSRARAEIAT LALVGYTNAG KSSIFNKITA ADVYAADQLF ATLDPTLRKI ELDDVGAAIL VDTVGFIRHL PHKLVESFRA TLQETVEATL LLHVIDCFDE ERAKHIIEVN TVLSDIGACD VPVLQIYNKI DMLEGQGPRI DYNSEGRPAR VWLSAVSGEG LDLMFKAITQ LLSEDLIIDV IKVAPQYGQL RSLLFAKGSV VSETIEENGD MLLSVRVQRK DLLQMLTRVG MPTEPYRIVE VY // ID S6HK82_9GAMM Unreviewed; 475 AA. AC S6HK82; DT 16-OCT-2013, integrated into UniProtKB/TrEMBL. DT 16-OCT-2013, sequence version 1. DT 07-JUN-2017, entry version 28. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=OFPII_28160 {ECO:0000313|EMBL:EPJ45452.1}; OS Osedax symbiont Rs1. OC Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales; OC unclassified Oceanospirillaceae. OX NCBI_TaxID=1330036 {ECO:0000313|EMBL:EPJ45452.1, ECO:0000313|Proteomes:UP000014822}; RN [1] {ECO:0000313|EMBL:EPJ45452.1, ECO:0000313|Proteomes:UP000014822} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Rs1 {ECO:0000313|Proteomes:UP000014822}; RA Yi H., Goffredi S.; RT "Comparative genomics of two novel heterotrophic symbionts of deep-sea RT Osedax worms: functional variation and environmental selection."; RL Submitted (MAY-2013) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EPJ45452.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ASZJ01000124; EPJ45452.1; -; Genomic_DNA. DR PATRIC; fig|1330036.3.peg.2695; -. DR Proteomes; UP000014822; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000014822}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000014822}. FT DOMAIN 255 420 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 475 AA; 52315 MW; 29F2BFC229FC29BA CRC64; MPDNSVELAV FRKQGLHCGA LTEKIMQLTE KATLTNALLI SICTPELNGD EAIESLAELA RLVTTLGFKV VGTQSQKLNS TKRANVLGLG KLADIAQLTG NQGEVEGREE PEEPPEEVDI ATIPEDISSQ NLTFGCADVV VFDCDLSPSQ LRNVENQLGV EVFDRTGIII EIFSRHARTK TAKLQVEIAR LNYVAPRLRE SSCGDKERQM GKGAGETTLE LNRRKVRDQL AALKHELVNV QDEMKGRRTQ RSEHFCVALV GYTNAGKSSL MRAITGSNVE GENKLFATLD TTVRALFPVT QPRILVSDTV GFIKKLPHDL VASFHSTLAE AHDASLLLYV VDASDPSFRA QLDVVHQVLE EVGVADSEKL LVLNKSDLLS PEQQQALLEE FPDAMLTSAR SATDVSKLHQ YIVGISLDGM IEEEIIVPYT AKGIIGEIRS VMSVTKEEYE YEHIKLTVRS SAINLARLKK RMLNL // ID S7IN56_CHLPS Unreviewed; 462 AA. AC S7IN56; DT 16-OCT-2013, integrated into UniProtKB/TrEMBL. DT 16-OCT-2013, sequence version 1. DT 30-AUG-2017, entry version 32. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:EPP29729.1}; GN ORFNames=CP082626L3_0468 {ECO:0000313|EMBL:EPP29729.1}; OS Chlamydia psittaci 08-2626_L3. OC Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae; OC Chlamydia/Chlamydophila group; Chlamydia. OX NCBI_TaxID=1112246 {ECO:0000313|EMBL:EPP29729.1, ECO:0000313|Proteomes:UP000014841}; RN [1] {ECO:0000313|EMBL:EPP29729.1, ECO:0000313|Proteomes:UP000014841} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=08-2626_L3 {ECO:0000313|EMBL:EPP29729.1, RC ECO:0000313|Proteomes:UP000014841}; RA Huot-Creasy H., McCracken C.L., Humphries M., Sachse K., Laroucau K., RA Bavoil P., Myers G.S.; RT "Genome sequence of Chlamydia psittaci 08-2626 L3."; RL Submitted (APR-2013) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EPP29729.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ATMX01000076; EPP29729.1; -; Genomic_DNA. DR RefSeq; WP_014943724.1; NZ_KE360748.1. DR EnsemblBacteria; EPP29729; EPP29729; CP082626L3_0468. DR PATRIC; fig|1112246.4.peg.246; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000014841; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000014841}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}. FT DOMAIN 228 394 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 462 AA; 52376 MW; 7CD96D6FF848EA67 CRC64; MKKKRKEEKK SRESALGWRF SLPREEQDPS QALAVACYSG KEEQQRVEEH SEELVSLAES CDITVLETRS WILRSSSSST YLNEGKLLEI EEILKVFPTI GTLIVDEEIT ASQQRNLEKR LGLVVLDRTE LILEIFANRA FTAEAGLQVE LARARYLLPR LKRMWGHLSR QKSGGGSGGG FVKGEGEKQI ELDRRMIRER IHKLTLDLKS VEKQRKERRK AKEKRGIPSF ALIGYTNSGK STLLNLLTSA ETYVEDKLFA TLDPKTRRCV LPSGQRVLVT DTVGFIRKLP HTLVAAFKST LEAALHEDVL LHVVDASHPL AFEHIETTKE ILKELGVDHP KIITVLNKID ALPHGKASTK LRLLSPRAVL ISAKTGEGIQ NLLEAMTDVI TEGFPEVTLK FSYKDYGKFT ELYDAGLVLS HRRKDDILIV EAYLPQELEK RYGPFIARKR SSQKQMEDEF FV // ID S7IWT9_CHLPS Unreviewed; 229 AA. AC S7IWT9; DT 16-OCT-2013, integrated into UniProtKB/TrEMBL. DT 16-OCT-2013, sequence version 1. DT 16-MAR-2016, entry version 11. DE SubName: Full=GTP-binding protein HflX {ECO:0000313|EMBL:EPP32493.1}; DE Flags: Fragment; GN Name=hflX {ECO:0000313|EMBL:EPP32493.1}; GN ORFNames=CP8484711_0559A {ECO:0000313|EMBL:EPP32493.1}; OS Chlamydia psittaci 84-8471/1. OC Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae; OC Chlamydia/Chlamydophila group; Chlamydia. OX NCBI_TaxID=1112230 {ECO:0000313|EMBL:EPP32493.1, ECO:0000313|Proteomes:UP000014827}; RN [1] {ECO:0000313|EMBL:EPP32493.1, ECO:0000313|Proteomes:UP000014827} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=84-8471/1 {ECO:0000313|EMBL:EPP32493.1, RC ECO:0000313|Proteomes:UP000014827}; RA Huot-Creasy H., McCracken C.L., Humphries M., Sachse K., Laroucau K., RA Bavoil P., Myers G.S.; RT "Genome sequence of Chlamydia psittaci 84-8471/1."; RL Submitted (APR-2013) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EPP32493.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ATMY01000944; EPP32493.1; -; Genomic_DNA. DR EnsemblBacteria; EPP32493; EPP32493; CP8484711_0559A. DR Proteomes; UP000014827; Unassembled WGS sequence. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000014827}; KW Reference proteome {ECO:0000313|Proteomes:UP000014827}. FT DOMAIN 45 134 GTP-bdg_N. {ECO:0000259|Pfam:PF13167}. FT DOMAIN 136 218 GTP-bdg_M. {ECO:0000259|Pfam:PF16360}. FT NON_TER 1 1 {ECO:0000313|EMBL:EPP32493.1}. FT NON_TER 229 229 {ECO:0000313|EMBL:EPP32493.1}. SQ SEQUENCE 229 AA; 26228 MW; 1C3104795860FB71 CRC64; KRKEEKKSRE SALGWRFSLP REEQDPSQAL AVACYSGKEE QQRVEEHSEE LVSLAESCDI TVLETRSWIL RSPSSSTYLN EGKLLEIEEI LKVFPTIGTL IVDEEITASQ QRNLEKRLGL VVLDRTELIL EIFANRAFTA EAGLQVELAR ARYLLPRLKR MWGHLSRQKS GGGSGGGFVK GEGEKQIELD RRMIRERIHK LTLDLKSVEK QRKERRKAKE KRGIPSFAL // ID S7T1P3_9DELT Unreviewed; 527 AA. AC S7T1P3; DT 16-OCT-2013, integrated into UniProtKB/TrEMBL. DT 16-OCT-2013, sequence version 1. DT 07-JUN-2017, entry version 27. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=dsat_1119 {ECO:0000313|EMBL:EPR30992.1}; OS Desulfovibrio alkalitolerans DSM 16529. OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfovibrionales; OC Desulfovibrionaceae; Desulfovibrio. OX NCBI_TaxID=1121439 {ECO:0000313|EMBL:EPR30992.1, ECO:0000313|Proteomes:UP000014975}; RN [1] {ECO:0000313|EMBL:EPR30992.1, ECO:0000313|Proteomes:UP000014975} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 16529 {ECO:0000313|EMBL:EPR30992.1, RC ECO:0000313|Proteomes:UP000014975}; RX PubMed=23950126; RA Brown S.D., Hurt R.A.Jr., Gilmour C.C., Elias D.A.; RT "Draft genome sequences for three mercury-methylating, sulfate- RT reducing bacteria."; RL Genome Announc. 1:e00618-13(2013). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EPR30992.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ATHI01000030; EPR30992.1; -; Genomic_DNA. DR EnsemblBacteria; EPR30992; EPR30992; dsat_1119. DR PATRIC; fig|1121439.3.peg.2496; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000014975; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000014975}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000014975}. FT DOMAIN 354 519 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 313 340 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 527 AA; 57790 MW; E1E7012DAEB65FEE CRC64; MGGLSPDQAR ELAVLSHGMG RQIGLLVDRQ GRPRMVIVGQ ASSIMIPELG RVRATGGRLR GLRLVHTHLG PDGLSEEDLM DMVFLRLDSV QVLTVSPDGA PLQVQHAHLL PGGGGKGYDV GPLVRFDRET TDFAAMAQAL EDELARGDAA RAAPGAARGV GREGRALLVH VSSDSRTQQE ASLRELTALS ETAGLTVAAT LTQRVHEVNP RTILGKGKLA ELEVLALQSG ADLIVFDCEL TPAQLRNIGE ATERKVVDRS QLILDIFAQH AKSSAGKLQV ELAQMQYRLP HLVGRGEALS RLMGGIGGRG PGETKLEIDR RRVRERITRL KRELAELRKR RGLRRTRRAK AEVPVVALVG YTNAGKSTLL NTLTKAAVLA EDKLFATLDP TSRRIRFPRE REIIMTDTVG FIRSLPKQLQ EAFRATLEEL ESADLLVHVA DTGHPEAFEQ IEAVESILHD MELDHLPRIL ALNKWDALDE DARRDMRLAF PQAVPISARD RESLEPLVRT ILDMLAMGQP IETVTIS // ID S7TQL8_DESML Unreviewed; 545 AA. AC S7TQL8; DT 16-OCT-2013, integrated into UniProtKB/TrEMBL. DT 16-OCT-2013, sequence version 1. DT 05-JUL-2017, entry version 29. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=dsmv_0370 {ECO:0000313|EMBL:EPR38960.1}; OS Desulfococcus multivorans DSM 2059. OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfobacterales; OC Desulfobacteraceae; Desulfococcus. OX NCBI_TaxID=1121405 {ECO:0000313|EMBL:EPR38960.1, ECO:0000313|Proteomes:UP000014977}; RN [1] {ECO:0000313|EMBL:EPR38960.1, ECO:0000313|Proteomes:UP000014977} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 2059 {ECO:0000313|EMBL:EPR38960.1, RC ECO:0000313|Proteomes:UP000014977}; RX PubMed=23950126; RA Brown S.D., Hurt R.A.Jr., Gilmour C.C., Elias D.A.; RT "Draft genome sequences for three mercury-methylating, sulfate- RT reducing bacteria."; RL Genome Announc. 1:e00618-13(2013). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EPR38960.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ATHJ01000094; EPR38960.1; -; Genomic_DNA. DR RefSeq; WP_020877032.1; NZ_FUWN01000005.1. DR EnsemblBacteria; EPR38960; EPR38960; dsmv_0370. DR PATRIC; fig|1121405.3.peg.2763; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000014977; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000014977}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000014977}. SQ SEQUENCE 545 AA; 61087 MW; 5407111291083D88 CRC64; MRTLYGNTED LKADHIRRLE NLCRRKVPDR FIITPELARD IARLSHEIHR QVGLLIERSG KIVAVIVGDA HKIVIPETGA YHTLPGRLKG LRCVHTHLKD EPLTADDLTD LALLRLDLMA AVTLTPEGGV RSVHAAHILP QGPPDAPYRI LDPLPPHRLD VGFAEIIRAL ESELAQIRSL YTAEKGEERA VLVSVSTAPR KIAEDSLAEL KELAISSGIE VVEVVLQQRK KADPRFLIGR GKLQDLNLLA LQKGISLIIF DQELNASQIR SIADQIELKV IDRTQLILDI FAQRAQTREG KLQVELAQLK YLLPRLVTKN TAMSRLTGGI GGRGPGETKL EINRRRVRQR INQLEKALQA VIRHRSRQKA RRTKKGLPVI SIIGYTNAGK STLLNTLTQS DVLAEDRLFA TLDPSSRRLR FPRDVEVIIT DTVGFIRELP KDLMVAFRAT LEELQSADLL LHVVDVSNPR CQEQIRSVER ILSDLDLQHI KVLRVLNKID LISAEDLDRR IRTLGGFPVS AVNRSTLVPL TEKMAEEIEK LSSIT // ID S7VII3_9DELT Unreviewed; 548 AA. AC S7VII3; DT 16-OCT-2013, integrated into UniProtKB/TrEMBL. DT 16-OCT-2013, sequence version 1. DT 07-JUN-2017, entry version 27. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=dsx2_1659 {ECO:0000313|EMBL:EPR44298.1}; OS Desulfovibrio sp. X2. OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfovibrionales; OC Desulfovibrionaceae; Desulfovibrio. OX NCBI_TaxID=941449 {ECO:0000313|EMBL:EPR44298.1, ECO:0000313|Proteomes:UP000014960}; RN [1] {ECO:0000313|EMBL:EPR44298.1, ECO:0000313|Proteomes:UP000014960} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=X2 {ECO:0000313|EMBL:EPR44298.1, RC ECO:0000313|Proteomes:UP000014960}; RX PubMed=23950126; RA Brown S.D., Hurt R.A.Jr., Gilmour C.C., Elias D.A.; RT "Draft genome sequences for three mercury-methylating, sulfate- RT reducing bacteria."; RL Genome Announc. 1:e00618-13(2013). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EPR44298.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ATHV01000004; EPR44298.1; -; Genomic_DNA. DR EnsemblBacteria; EPR44298; EPR44298; dsx2_1659. DR PATRIC; fig|941449.3.peg.413; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000014960; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000014960}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000014960}. FT DOMAIN 345 510 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 548 AA; 59954 MW; 22D865976859D4F1 CRC64; MSPEQARELA VLSSGLGRQI GLLLDRQGRP RLVVVGDAHS ILIPELGRVR ASGGRLRGLR LLHTHLSPDG LSEEDLMDMV FLRLDAVQVL TVGPDGLPGR VQSAHMLPPN PEGKAYDVGS MRPWDRDDTD FTVQAEALEE ELARAESARP VTAEGRAVLV HVSPMPRPAQ ESSLAELRAL ARTAGLDVAD TLTQRVPQVN PRTILGKGKL ADLEVAALQA GADVVVFDCE LTPAQLRNLG EATERKVIDR SQLILDIFAQ RATSRAGKLQ VELAQMQYRL PHLVGRGEAL SRLMGGIGGR GPGETKLEID RRRVRERITR VKRELSELRK RRGLRRARRA KAEVPVVALV GYTNAGKSTL LNTLTRSEVL AEDKLFATLD PTSRRIRFPE EREVILTDTV GFIRHLPKEL QEAFRATLEE LEAADALVLV ADAGHAQAAQ QIEAVERILE EMELSDIPRV LALNKWDTLD TQAREATAAA YPHGIPIRAR DRASLEPLVR AVLDLLSGHQ GGIQAGPPRA PRAAEPAVPS GPDDEAAWDD DIPTEYIP // ID S7VSX8_9FLAO Unreviewed; 403 AA. AC S7VSX8; DT 16-OCT-2013, integrated into UniProtKB/TrEMBL. DT 16-OCT-2013, sequence version 1. DT 07-JUN-2017, entry version 28. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=ADIWIN_2642 {ECO:0000313|EMBL:EPR72472.1}; OS Winogradskyella psychrotolerans RS-3. OC Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales; OC Flavobacteriaceae; Winogradskyella. OX NCBI_TaxID=641526 {ECO:0000313|EMBL:EPR72472.1, ECO:0000313|Proteomes:UP000014962}; RN [1] {ECO:0000313|EMBL:EPR72472.1, ECO:0000313|Proteomes:UP000014962} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=RS-3 {ECO:0000313|EMBL:EPR72472.1, RC ECO:0000313|Proteomes:UP000014962}; RX PubMed=23950132; RA Kumar Pinnaka A., Ara S., Singh A., Shivaji S.; RT "Draft Genome Sequence of Winogradskyella psychrotolerans RS-3T, RT Isolated from the Marine Transect of Kongsfjorden, Ny-Alesund, RT Svalbard, Arctic Ocean."; RL Genome Announc. 1:e00630-13(2013). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EPR72472.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ATMR01000124; EPR72472.1; -; Genomic_DNA. DR RefSeq; WP_020897547.1; NZ_ATMR01000124.1. DR EnsemblBacteria; EPR72472; EPR72472; ADIWIN_2642. DR PATRIC; fig|641526.4.peg.2623; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000014962; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000014962}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000014962}. FT DOMAIN 200 385 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 403 AA; 46473 MW; 70E2CAC9F2BF76B0 CRC64; MIEKKDIDLE KVVLIGVVTQ NQDEEKSQEY LDELEFLTYT AGGEVIKRYT QKMALPNPKT FIGTGKMEEV ANFVQENDIG TVIFDDELTP AQERNISKIL NCKILDRTNL ILDIFAQRAQ TSYARTQVEL AQCEYLLPRL KGMWTHLERQ KGGIGMRGPG ETEIETDRRI VRDKIALLKA KIKTIDKQQA VQRGNRGKMV RVALVGYTNV GKSTLMNVIS KSDVFAENKL FATLDTTVRK VVIGNLPFLV SDTVGFIRKL PTQLVESFKS TLDEVREADL LLHIVDISHA NFEEHIESVN QILDEIESKD KPTIMVFNKI DAYEAEPFDE EDLIEVRTEA NYTIEEWKKT WMNRVGDNAL FISALNKENM EEFRKRVYKE VREIHVTRFP YNHFLYPDVE DIE // ID S8CLW0_9LAMI Unreviewed; 543 AA. AC S8CLW0; DT 16-OCT-2013, integrated into UniProtKB/TrEMBL. DT 16-OCT-2013, sequence version 1. DT 07-JUN-2017, entry version 18. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EPS65761.1}; DE Flags: Fragment; GN ORFNames=M569_09013 {ECO:0000313|EMBL:EPS65761.1}; OS Genlisea aurea. OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae; OC Pentapetalae; asterids; lamiids; Lamiales; Lentibulariaceae; Genlisea. OX NCBI_TaxID=192259 {ECO:0000313|EMBL:EPS65761.1, ECO:0000313|Proteomes:UP000015453}; RN [1] {ECO:0000313|EMBL:EPS65761.1, ECO:0000313|Proteomes:UP000015453} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=23855885; RA Leushkin E.V., Sutormin R.A., Nabieva E.R., Penin A.A., RA Kondrashov A.S., Logacheva M.D.; RT "The miniature genome of a carnivorous plant Genlisea aurea contains a RT low number of genes and short non-coding sequences."; RL BMC Genomics 14:476-476(2013). CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EPS65761.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AUSU01004053; EPS65761.1; -; Genomic_DNA. DR Proteomes; UP000015453; Unassembled WGS sequence. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR CDD; cd01878; HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 2. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000015453}; KW Reference proteome {ECO:0000313|Proteomes:UP000015453}. FT DOMAIN 267 391 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT NON_TER 1 1 {ECO:0000313|EMBL:EPS65761.1}. FT NON_TER 543 543 {ECO:0000313|EMBL:EPS65761.1}. SQ SEQUENCE 543 AA; 59971 MW; 1D2643E21AF4DD35 CRC64; SSSSVLQRRY TDHHGGDESS QAPDRPPRLL VLQPRIRPSN LLRTKLEEAL NLANSLEQQR DGFYETDVEN PPHLVVQNPL ARSPRADTYF GAGTLETVKC LLNALESKGF VDAIFVNAAL SGAQQRNLEA SFHHSPILRG WGKPVLDRVG VIIEIFNAHA QTKEAKLQAE LAALMYKRSR LVRLRGPDGR HTFGGSADAE VVSAKGRGSG GRGFISGAGE TELQLQRRRI SDRKKKLLSE IQEVRRTRTI QRAARKREGC SSGEEMATVA VVGYTNAGKS TLVSALSNSY LYCDNRLFAT VDPKLSSVTL PSGRKVILSD TVGFISDLPV QLVEAFHATL EEVVEADLLV HVLDSSAQNL DEHRDTVMEV LAKIGVSDEK LRNMIEVHNK VPPFPKQCLL RPTLYESSLC CIVEQQIDLL EEQYHDVNEE DHGEEEDADE EHGIVAASGF EETTYYSDDF LESDDEQLVE CCGDASSSSD PPESSSSGSL CHVRTSAVSG VGLKELLEVI DEKFGEKKEG SKAVERSIFY TKWRPPREGE EEV // ID S8DKZ8_9LAMI Unreviewed; 197 AA. AC S8DKZ8; DT 16-OCT-2013, integrated into UniProtKB/TrEMBL. DT 16-OCT-2013, sequence version 1. DT 07-JUN-2017, entry version 11. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EPS60207.1}; DE Flags: Fragment; GN ORFNames=M569_14599 {ECO:0000313|EMBL:EPS60207.1}; OS Genlisea aurea. OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae; OC Pentapetalae; asterids; lamiids; Lamiales; Lentibulariaceae; Genlisea. OX NCBI_TaxID=192259 {ECO:0000313|EMBL:EPS60207.1, ECO:0000313|Proteomes:UP000015453}; RN [1] {ECO:0000313|EMBL:EPS60207.1, ECO:0000313|Proteomes:UP000015453} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=23855885; RA Leushkin E.V., Sutormin R.A., Nabieva E.R., Penin A.A., RA Kondrashov A.S., Logacheva M.D.; RT "The miniature genome of a carnivorous plant Genlisea aurea contains a RT low number of genes and short non-coding sequences."; RL BMC Genomics 14:476-476(2013). CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EPS60207.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AUSU01007739; EPS60207.1; -; Genomic_DNA. DR Proteomes; UP000015453; Unassembled WGS sequence. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF13167; GTP-bdg_N; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000015453}; KW Reference proteome {ECO:0000313|Proteomes:UP000015453}. FT DOMAIN 134 196 GTP-bdg_N. {ECO:0000259|Pfam:PF13167}. FT NON_TER 197 197 {ECO:0000313|EMBL:EPS60207.1}. SQ SEQUENCE 197 AA; 21586 MW; 0E42641198FDE84E CRC64; MSLCFCSLLK PLFVDSEYDF LFRCSPNSLR PRLGIGLLNL RTHAKDYGVK AFGAVSDRTA AFDSEQTRGG DVNGIQNDEF GDERSRIRLN RTAEVVVDRE SRFKLQNGRE VFQEKAYLVG VAKKSDCDAS FGIEYSLGEL AQLADTAGLL VVGSTYQKLA TPNPRTYIGS GKVAEIKSAI HAFGVETVIF DDELSAG // ID S8GY13_9BACT Unreviewed; 415 AA. AC S8GY13; DT 16-OCT-2013, integrated into UniProtKB/TrEMBL. DT 16-OCT-2013, sequence version 1. DT 07-JUN-2017, entry version 27. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:EPT33429.1}; GN ORFNames=HMPREF9012_0022 {ECO:0000313|EMBL:EPT33429.1}; OS Bacteroidetes bacterium oral taxon 272 str. F0290. OC Bacteria; Bacteroidetes. OX NCBI_TaxID=888054 {ECO:0000313|EMBL:EPT33429.1, ECO:0000313|Proteomes:UP000015345}; RN [1] {ECO:0000313|EMBL:EPT33429.1, ECO:0000313|Proteomes:UP000015345} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=F0290 {ECO:0000313|EMBL:EPT33429.1, RC ECO:0000313|Proteomes:UP000015345}; RA Durkin A.S., Haft D.R., McCorrison J., Torralba M., Gillis M., RA Haft D.H., Methe B., Sutton G., Nelson K.E.; RL Submitted (JUL-2013) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EPT33429.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AUTU01000020; EPT33429.1; -; Genomic_DNA. DR RefSeq; WP_021311838.1; NZ_AUTU01000020.1. DR EnsemblBacteria; EPT33429; EPT33429; HMPREF9012_0022. DR PATRIC; fig|888054.3.peg.1468; -. DR Proteomes; UP000015345; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000015345}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000015345}. FT DOMAIN 216 400 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 415 AA; 47097 MW; 1C9111D80E27FEB3 CRC64; MKEFVISETK AETAVLVGLI TPVQDEFKTK EYLDELEFLA HTAGAKVIKR FTQKVGGPNA VTYVGTGKLE EIRDYIQTEE EAERKVGMVI FDDELSAKQI RNIEKELKVK ILDRTSLILD IFAMRAQTAN AKTQVELAQY KYMLPRLQRL WTHLERQGGG SGAGGGKGTV GLRGPGETQL EMDRRIILNR MALLKGRLAE IDQQKATQRK NRGRLIRVAL VGYTNVGKST LMNLLAKSEV FAENKLFATL DTTVRKVVID NLPFLLSDTV GFIRKLPTDL VESFKSTLDE VREADLLIHI VDISHSDFEE QIKVVEKTIA EIGAGGKPTM IVFNKIDAYT YIQKEADDLT PKTKENVSLE ELMKTWMAKL DDNCLFISAK EKIHVNELKE KVYKKVCELH VQKYPYNDFL YPKYE // ID S9PNY3_9DELT Unreviewed; 550 AA. AC S9PNY3; DT 16-OCT-2013, integrated into UniProtKB/TrEMBL. DT 16-OCT-2013, sequence version 1. DT 07-JUN-2017, entry version 27. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=D187_000153 {ECO:0000313|EMBL:EPX64731.1}; OS Cystobacter fuscus DSM 2262. OC Bacteria; Proteobacteria; Deltaproteobacteria; Myxococcales; OC Cystobacterineae; Archangiaceae; Cystobacter. OX NCBI_TaxID=1242864 {ECO:0000313|EMBL:EPX64731.1, ECO:0000313|Proteomes:UP000011682}; RN [1] {ECO:0000313|EMBL:EPX64731.1, ECO:0000313|Proteomes:UP000011682} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 2262 {ECO:0000313|EMBL:EPX64731.1, RC ECO:0000313|Proteomes:UP000011682}; RA Sharma G., Khatri I., Kaur C., Mayilraj S., Subramanian S.; RT "Genome assembly of Cystobacter fuscus DSM 2262."; RL Submitted (MAY-2013) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EPX64731.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ANAH02000001; EPX64731.1; -; Genomic_DNA. DR RefSeq; WP_002629607.1; NZ_ANAH02000001.1. DR EnsemblBacteria; EPX64731; EPX64731; D187_000153. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000011682; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000011682}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000011682}. FT DOMAIN 378 542 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 337 371 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 550 AA; 60885 MW; BB143581E805AB51 CRC64; MKEIYGNTLG LKASEQSRLR NTYRRRVSPH EIVSPELARH LTELSRETNR QVGVLLNRKG EIEHVVVGNA HKLELPDIGR ARAGQVRLRG LRLVHTHLKS EPLTKDDLTD LALLRLDMVA AIGVGHDGLP GVLHYAHLVP ENGTGEFWSV STLPDVHDGQ PDVLDTLEAL EEELSRKAAA RAVSGRDKAL LVAVCLDGNR AAAEASLSEL KELARTAGVE VLDSVLQMRR EADPRYLIGR GKLEELNLRS MQAMADVLIF DKDLTPSQGR HISEATSLKV IDRSQLILDI FAQRAQSAEG KLQVELAQLK YRLPRLVQSD TSLSRLAGGI GGRGPGETKL EIDRRRARDR INHLEKRIDT LSREREVRRA QRNRRDLPII SIVGYTNAGK STLLNAITGS EVLAENKLFA TLDPTSRRLR FPQEREVIIT DTVGFIRDLP KDLVAAFRAT LEELYDADLL LHVVDANDPS RDEQVEAVEN ILDSLDLMQK PRLMVWNKAE LLGPDDVEAL LRSRGGVAIS AARREGLASL LAKADTTLFA EGASQSLGVM // ID S9Q8W3_9RHOB Unreviewed; 417 AA. AC S9Q8W3; DT 16-OCT-2013, integrated into UniProtKB/TrEMBL. DT 16-OCT-2013, sequence version 1. DT 12-APR-2017, entry version 24. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=Salmuc_00696 {ECO:0000313|EMBL:EPX76043.1}; OS Salipiger mucosus DSM 16094. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae; Salipiger. OX NCBI_TaxID=1123237 {ECO:0000313|EMBL:EPX76043.1, ECO:0000313|Proteomes:UP000015347}; RN [1] {ECO:0000313|EMBL:EPX76043.1, ECO:0000313|Proteomes:UP000015347} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 16094 {ECO:0000313|EMBL:EPX76043.1, RC ECO:0000313|Proteomes:UP000015347}; RA Riedel T., Spring S., Fiebig A., Petersen J., Goeker M., Klenk H.-P.; RT "Genome sequence of the exopolysaccharide-producing Salipiger RT mucosustype strain (A3T), a moderately halophilic member of the RT Roseobacterclade."; RL Stand. Genomic Sci. 0:0-0(2013). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EPX76043.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; APVH01000061; EPX76043.1; -; Genomic_DNA. DR EnsemblBacteria; EPX76043; EPX76043; Salmuc_00696. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000015347; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000015347}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000015347}. FT DOMAIN 197 366 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 417 AA; 46522 MW; A1C3702CFB5A06E1 CRC64; MTRAWVIHPD IRSDRDRRDA TMALEEAMAL AVALPDLVVA GGEVVQLREP HPGTLFGAGK IEELAERMKA EEVELVLVDG PVTPVQQRNL EKAWGVKLLD RTGLILEIFS DRAATREGVL QVEMAHLSYQ RTRLVRAWTH LERQRGGLGF VGGPGETQIE ADRRAIDEQL VRLRRQLDKV VKTRDLHRKA RAKVPYPIVA LVGYTNAGKS TLFNRLTGAE VMAKDMLFAT LDPTMRAVRL PTGLEVILSD TVGFISDLPT ELVAAFRATL EEVLAADIIL HVRDIAHPNT EEQAEDVSAI MASLGVNEAV PLVEVWNKID LLDPEARTAA LNRAERDEDV FAVSAWTGEG LDGLLEVVTE RLQGETVEEE IRLAFSDGKR RSWLFGKGLV QDEQQDEHGY LLRVRWTAKD RAQFDTL // ID S9QAV0_9DELT Unreviewed; 493 AA. AC S9QAV0; DT 16-OCT-2013, integrated into UniProtKB/TrEMBL. DT 16-OCT-2013, sequence version 1. DT 07-JUN-2017, entry version 29. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=D187_003931 {ECO:0000313|EMBL:EPX58459.1}; OS Cystobacter fuscus DSM 2262. OC Bacteria; Proteobacteria; Deltaproteobacteria; Myxococcales; OC Cystobacterineae; Archangiaceae; Cystobacter. OX NCBI_TaxID=1242864 {ECO:0000313|EMBL:EPX58459.1, ECO:0000313|Proteomes:UP000011682}; RN [1] {ECO:0000313|EMBL:EPX58459.1, ECO:0000313|Proteomes:UP000011682} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 2262 {ECO:0000313|EMBL:EPX58459.1, RC ECO:0000313|Proteomes:UP000011682}; RA Sharma G., Khatri I., Kaur C., Mayilraj S., Subramanian S.; RT "Genome assembly of Cystobacter fuscus DSM 2262."; RL Submitted (MAY-2013) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EPX58459.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ANAH02000024; EPX58459.1; -; Genomic_DNA. DR RefSeq; WP_002627941.1; NZ_ANAH02000024.1. DR EnsemblBacteria; EPX58459; EPX58459; D187_003931. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000011682; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 2. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000011682}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000011682}. FT DOMAIN 274 439 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 84 107 {ECO:0000256|SAM:Coils}. FT COILED 118 151 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 493 AA; 54026 MW; 3CA6585A5BF4F9BA CRC64; MSQSAPERPL AVLVGVQLPN VSDTEHAADL AELGRLVHTL GYEVVATVSQ RRDGIAAGTV LGTGKLEELA RLTGGHGTVP SGARARKSKA RERWEAETEE AEEAAAEAAP EAPPETGAEE AEEADEAEEA EEAEEADEAE EADEAEEADE ERAGARPTVV VVDHELTPSQ LSNLERATGA QVLDRTGVIV DIFHRHARSR EARMQVEIAR LNYLAPRMRE STGSRERQQG RGSGDSAMEL DRRRIRDRLA ELRAGLASIQ QDQDNRRYAR RDQLRVALVG YTNAGKSSLM RALTGSEVLV ADQLFATLDT TVRALKPETR PRILVSDTVG FIQKLPHDLV ASFRSTLDEA LEASLLLYVV DASDPTWQAQ LEVTRSVLRE IGAQSVPSLL LFNKADRLSA EAREALLQEH PEARVLSAHS PDDVAALRQG IVEFFERSMI EADLVIPYAR QGRLGEVYEH ARVLTESFDE NGRTLRIRAL PAAIARLTHA FGT // ID S9QL15_9RHOB Unreviewed; 429 AA. AC S9QL15; DT 16-OCT-2013, integrated into UniProtKB/TrEMBL. DT 16-OCT-2013, sequence version 1. DT 07-JUN-2017, entry version 27. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=thalar_01648 {ECO:0000313|EMBL:EPX80308.1}; OS Litoreibacter arenae DSM 19593. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae; Litoreibacter. OX NCBI_TaxID=1123360 {ECO:0000313|EMBL:EPX80308.1, ECO:0000313|Proteomes:UP000015351}; RN [1] {ECO:0000313|EMBL:EPX80308.1, ECO:0000313|Proteomes:UP000015351} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 19593 {ECO:0000313|EMBL:EPX80308.1, RC ECO:0000313|Proteomes:UP000015351}; RA Riedel J., Fiebig A., Petersen J., Gronow S., Goeker M., Klenk H.-P.; RT "Genome sequence of the Litoreibacter arenae type strain (DSM 19593T), RT a member of the Roseobacter clade isolated from sea sand."; RL Stand. Genomic Sci. 0:0-0(2013). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EPX80308.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AONI01000009; EPX80308.1; -; Genomic_DNA. DR RefSeq; WP_021100214.1; NZ_KE557306.1. DR PATRIC; fig|1123360.3.peg.1634; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000015351; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000015351}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000015351}. FT DOMAIN 209 378 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 429 AA; 47014 MW; 5AD092E3F9BF2D15 CRC64; MVKRILETED SGLTRAWVIH PDIKDVKARR LASFALSEAV SLAEALPGLE VAGSEIVPLP KVRAGTLFGT GKIVELKNRL KEAEVELVLI DGPVTPVQQR NLEKEWGVKI LDRTGLILEI FSDRAATREG VLQVELAALS YQRTRLVRAW THLERQRGGL GFVGGPGETQ IEADRRAIDD AIVRIRRQLE KTVKTRELHR AARAKVPYPV VALVGYTNAG KSTLFNRLTG AEVLVKDMLF ATLDPTMRSV ELSDGLEIIM SDTVGFISDL PTQLVAAFRA TLEEVLSADL ILHVRDISHP ESEGQARDVR SIMADLGVDK DVPVLEVWNK SDRLSPDALE AATNKADRDE HIFLTSATTG AGIDGLLDAV STLLRAGSTT EVIELGFADG KARAWLFGQE VVDSEEQTET GFNLTVTWSP AQKGQFEKL // ID S9S7K4_9RHOB Unreviewed; 436 AA. AC S9S7K4; DT 16-OCT-2013, integrated into UniProtKB/TrEMBL. DT 16-OCT-2013, sequence version 1. DT 07-JUN-2017, entry version 29. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=ruthe_00969 {ECO:0000313|EMBL:EPX86160.1}; OS Rubellimicrobium thermophilum DSM 16684. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae; Rubellimicrobium. OX NCBI_TaxID=1123069 {ECO:0000313|EMBL:EPX86160.1, ECO:0000313|Proteomes:UP000015346}; RN [1] {ECO:0000313|EMBL:EPX86160.1, ECO:0000313|Proteomes:UP000015346} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 16684 {ECO:0000313|EMBL:EPX86160.1, RC ECO:0000313|Proteomes:UP000015346}; RX PubMed=24501632; DOI=10.4056/sigs.4247911; RA Fiebig A., Riedel T., Gronow S., Petersen J., Klenk H.P., Goker M.; RT "Genome sequence of the reddish-pigmented Rubellimicrobium RT thermophilum type strain (DSM 16684(T)), a member of the Roseobacter RT clade."; RL Stand. Genomic Sci. 8:480-490(2013). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EPX86160.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AOLV01000010; EPX86160.1; -; Genomic_DNA. DR RefSeq; WP_021097068.1; NZ_KE557320.1. DR EnsemblBacteria; EPX86160; EPX86160; ruthe_00969. DR PATRIC; fig|1123069.3.peg.940; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000015346; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000015346}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Hydrolase {ECO:0000313|EMBL:EPX86160.1}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000015346}. FT DOMAIN 204 372 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 436 AA; 47896 MW; 8FFD2EA020975D05 CRC64; MRDTAAKRTP AWVLHPALRG GRDARPAGPA LEEAVALAAA LPGLDLRGAE VVPLARPHPG MLFGSGKVAE LKARFAEAGV ELVLVDGPVS PVQQRNLEKE WGTKLLDRTG LILEIFADRA RTREGVLQVE MAALSYQRTR LVRSWTHLER QRGGFGFVGG PGETQIEADR RAIDDQLVKL RRQLDRVSRT RTLHRAARAK VPFPVVALVG YTNAGKSTLF NRLTGSDVLA KDMLFATLDP TMRRVRLPAG LDVILSDTVG FISNLPTELV AAFRATLEEV LDADLILHVR DIAHPQSEAQ ARDVEAILAS LGVAESTPLI EVWNKIDLLP EEMRDRIAIR SGREPAVFPV SALTGEGIAP LLSAVAARLD DPRSEEDLFL PHAEGRLRAW LHDQGVVLGE EEAEGGTHLR IRWTARQRDR YRALQAATRR SRAEDG // ID S9ZD65_9RHOO Unreviewed; 389 AA. AC S9ZD65; DT 16-OCT-2013, integrated into UniProtKB/TrEMBL. DT 16-OCT-2013, sequence version 1. DT 30-AUG-2017, entry version 28. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=M622_03520 {ECO:0000313|EMBL:EPZ15205.1}; OS Thauera terpenica 58Eu. OC Bacteria; Proteobacteria; Betaproteobacteria; Rhodocyclales; OC Zoogloeaceae; Thauera. OX NCBI_TaxID=1348657 {ECO:0000313|EMBL:EPZ15205.1, ECO:0000313|Proteomes:UP000015455}; RN [1] {ECO:0000313|EMBL:EPZ15205.1, ECO:0000313|Proteomes:UP000015455} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=58Eu {ECO:0000313|EMBL:EPZ15205.1, RC ECO:0000313|Proteomes:UP000015455}; RA Liu B., Frostegard A.H., Shapleigh J.P.; RT "Draft genome sequence of Thauera terpenica."; RL Submitted (JUN-2013) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EPZ15205.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ATJV01000059; EPZ15205.1; -; Genomic_DNA. DR RefSeq; WP_021249599.1; NZ_ATJV01000059.1. DR EnsemblBacteria; EPZ15205; EPZ15205; M622_03520. DR PATRIC; fig|1348657.5.peg.2182; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000015455; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000015455}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000015455}. FT DOMAIN 198 363 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 389 AA; 42843 MW; 3861B0094DE5CCA2 CRC64; MFERPASGER AVLVQLDLGQ DLIDERLSEF KLLVLSAGAS VEAVVQGKRS APDAKLFAGS GKVQEIGEAL RAHEADIVIF NHALAPGQQR NLERVLECMV IDRTALILDI FAQRARSHEG KLQVELAQLE HLSTRLVRGW THLERQKGGI GLRGPGEKQL ETDRRLLGNR VKMLKQRLVQ MEKQRKVRRR ARERRDVLSV SLVGYTNAGK STLFNALTKA GAYAADQLFA TLDTTSRRLY VGGANVVLSD TVGFIRDLPH ALVAAFRATL EETVQADVVL HVVDSASADR DAQIEAVDKV LAEIGAAQVR QILVWNKIDL TPAEPAVERD DCGSIRRVFL SARTGEGLDL LREVLAELAQ EAFHEDADRD SGTAVELPFN PDYGHSNVT // ID T0C048_9DELT Unreviewed; 439 AA. AC T0C048; DT 16-OCT-2013, integrated into UniProtKB/TrEMBL. DT 16-OCT-2013, sequence version 1. DT 07-JUN-2017, entry version 29. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:EPZ49673.1}; GN ORFNames=M902_0455 {ECO:0000313|EMBL:EPZ49673.1}; OS Bacteriovorax sp. BAL6_X. OC Bacteria; Proteobacteria; Deltaproteobacteria; Bdellovibrionales; OC Bacteriovoracaceae; Bacteriovorax. OX NCBI_TaxID=1201290 {ECO:0000313|EMBL:EPZ49673.1, ECO:0000313|Proteomes:UP000015459}; RN [1] {ECO:0000313|EMBL:EPZ49673.1, ECO:0000313|Proteomes:UP000015459} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BAL6_X {ECO:0000313|EMBL:EPZ49673.1, RC ECO:0000313|Proteomes:UP000015459}; RA Chen H., Brinkac L.M., Mishra P., Dickerson T., Gordon-Bradley N., RA Lymperopoulou D.S., Williams H.N., Badger J.H.; RT "Draft genome sequences for the obligate bacterial predators RT Bacteriovorax spp. of four phylogenetic clusters."; RL Submitted (JUL-2013) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EPZ49673.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AUMC01000010; EPZ49673.1; -; Genomic_DNA. DR RefSeq; WP_021268220.1; NZ_AUMC01000010.1. DR EnsemblBacteria; EPZ49673; EPZ49673; M902_0455. DR PATRIC; fig|1201290.3.peg.2296; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000015459; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000015459}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000015459}. FT DOMAIN 208 374 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 175 202 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 439 AA; 50205 MW; D67D57B85BBA2E80 CRC64; MLDNEFFISR EAKASLVSLV CPKFKEHATE KDTLRSLGEL RELMRTLDIE TGEQYIQNKK TVDPGTILGT GKLEEIAMDA KAEGSTLLVF DCELTSSQIR NIKKLTGMSV VDRCHIILEI FSEHARTKEA RIQIEISRLQ YILPRLAGFW SHLGRQKGGI GVRGGEGEQQ IELDRRIIRE RIEFYKKELK EVEKSRIEQK KKRSKKAITT ALVGYTNAGK SSLMNRLCRV NVLEEDKLFA TLDSTFRMLN PDTKPPMILI DTVGFLSNLP NTLIDGFKTT LESALEADLL IIACDISDPN YEKHLEVTNN VLDELGLSDK ERFIVFNKKD KLNDKITETI IKRKHPNCFV ISSFNTEEID ELREYIVNFF LEKQNNYDLF IPYDAGAAHS IVVSKTNVIR TSNHEKGIYY QVRVPDFIYN PLGLQKFELG PHDPLLDEV // ID T0CEF2_ALIAG Unreviewed; 426 AA. AC T0CEF2; DT 16-OCT-2013, integrated into UniProtKB/TrEMBL. DT 16-OCT-2013, sequence version 1. DT 07-JUN-2017, entry version 28. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=N007_21025 {ECO:0000313|EMBL:EPZ50875.1}; OS Alicyclobacillus acidoterrestris (strain ATCC 49025 / DSM 3922 / CIP OS 106132 / NCIMB 13137 / GD3B). OC Bacteria; Firmicutes; Bacilli; Bacillales; Alicyclobacillaceae; OC Alicyclobacillus. OX NCBI_TaxID=1356854 {ECO:0000313|EMBL:EPZ50875.1, ECO:0000313|Proteomes:UP000015607}; RN [1] {ECO:0000313|EMBL:EPZ50875.1, ECO:0000313|Proteomes:UP000015607} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 49025 / DSM 3922 / CIP 106132 / NCIMB 13137 / GD3B RC {ECO:0000313|Proteomes:UP000015607}; RX PubMed=24009113; DOI=10.1128/genomeA.00638-13; RA Shemesh M., Pasvolsky R., Sela N., Green S.J., Zakin V.; RT "Draft genome sequence of Alicyclobacillus acidoterrestris strain ATCC RT 49025."; RL Genome Announc. 5:E00638-E00638(2013). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EPZ50875.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AURB01000074; EPZ50875.1; -; Genomic_DNA. DR EnsemblBacteria; EPZ50875; EPZ50875; N007_21025. DR PATRIC; fig|1356854.4.peg.910; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000015607; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000015607}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000015607}. FT DOMAIN 197 363 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 164 191 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 426 AA; 47983 MW; 28F9D5AFD7F38333 CRC64; MQEQAYRVIL AMCQVGQESD ERLAYREAEL TGLCEAAGGS VIGVMTQKRA QLDGRTFFGS GKLEELADLA TVNEADLVVA DRELSPAQIR NLERVLPCRI IDRTQLILDI FARRAQTREG RVQVEIAQLN YLMPRLTGRG VELSRLGGGI GTRGPGETQL ELDRRRIRTR MTHLRKELAA VERQRETMRG KRRRGVPVVA LVGYTNAGKT TVQSRWVRDK ANIEVPEGQN RLFDTLDPTA RQVRTKLGNE YVVVDTVGFV EDLPHHLVDA FKATLEETKY ADVVVVVVDA GHEPQSHLET TRRVLRDLGA LDKPVVTFFN KMDISPNQPG PDVHAVETLY GSAVNDSLEP LYQTVERLLS LDEVRVTLHT HPNDFIWDKL LRNGRIESAD PVSSDEWLVT AITSRRDAHL WQQQRQDGSA HEPQDH // ID T0CTW8_PAESO Unreviewed; 196 AA. AC T0CTW8; DT 16-OCT-2013, integrated into UniProtKB/TrEMBL. DT 16-OCT-2013, sequence version 1. DT 07-JUN-2017, entry version 20. DE SubName: Full=GTP-binding protein HflX {ECO:0000313|EMBL:EPZ61005.1}; GN Name=hflX {ECO:0000313|EMBL:EPZ61005.1}; GN ORFNames=H477_0542 {ECO:0000313|EMBL:EPZ61005.1}; OS Paeniclostridium sordellii ATCC 9714. OC Bacteria; Firmicutes; Clostridia; Clostridiales; OC Peptostreptococcaceae; Paeniclostridium. OX NCBI_TaxID=1292036 {ECO:0000313|EMBL:EPZ61005.1, ECO:0000313|Proteomes:UP000015748}; RN [1] {ECO:0000313|EMBL:EPZ61005.1, ECO:0000313|Proteomes:UP000015748} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 9714 {ECO:0000313|EMBL:EPZ61005.1, RC ECO:0000313|Proteomes:UP000015748}; RX PubMed=23873908; DOI=10.1128/JB.00711-13; RA Sirigi Reddy A.R., Girinathan B.P., Zapotocny R., Govind R.; RT "Identification and Characterization of Clostridium sordellii Toxin RT Gene Regulator."; RL J. Bacteriol. 195:4246-4254(2013). CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EPZ61005.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; APWR01000089; EPZ61005.1; -; Genomic_DNA. DR EnsemblBacteria; EPZ61005; EPZ61005; H477_0542. DR PATRIC; fig|1292036.3.peg.1287; -. DR Proteomes; UP000015748; Unassembled WGS sequence. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. PE 4: Predicted; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000015748}; KW Reference proteome {ECO:0000313|Proteomes:UP000015748}. FT DOMAIN 29 116 GTP-bdg_N. {ECO:0000259|Pfam:PF13167}. FT DOMAIN 118 195 GTP-bdg_M. {ECO:0000259|Pfam:PF16360}. FT COILED 175 196 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 196 AA; 21990 MW; 4C788A52F63E0D98 CRC64; MENIVERALL VGLNITTNVK KVDDIDINES MEELKELAKA AGAEVVGDLI QNRPARDAAF YIGKGKVEEI KAYCDSLDAT VVVFNDELSG AQIRNIEELV QRKVIDRTTL ILDIFAQRAL SKEGKLQVEL AQLKYRLPRL YGMGGEMSRT GAGIGTRGPG EQKLEVDKRH ILNKTADIRR ELREVKKNRE TQRAQD // ID T0HKE1_9SPHN Unreviewed; 440 AA. AC T0HKE1; DT 16-OCT-2013, integrated into UniProtKB/TrEMBL. DT 16-OCT-2013, sequence version 1. DT 07-JUN-2017, entry version 31. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=L485_20175 {ECO:0000313|EMBL:EQA98063.1}; OS Sphingobium baderi LL03. OC Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales; OC Sphingomonadaceae; Sphingobium. OX NCBI_TaxID=1114964 {ECO:0000313|EMBL:EQA98063.1, ECO:0000313|Proteomes:UP000015524}; RN [1] {ECO:0000313|EMBL:EQA98063.1, ECO:0000313|Proteomes:UP000015524} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=LL03 {ECO:0000313|EMBL:EQA98063.1, RC ECO:0000313|Proteomes:UP000015524}; RX PubMed=24051322; RA Kaur J., Verma H., Tripathi C., Khurana J.P., Lal R.; RT "Draft Genome Sequence of a Hexachlorocyclohexane-Degrading Bacterium, RT Sphingobium baderi Strain LL03T."; RL Genome Announc. 1:e00751-13(2013). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EQA98063.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ATIB01000085; EQA98063.1; -; Genomic_DNA. DR RefSeq; WP_021246578.1; NZ_KQ130471.1. DR PATRIC; fig|1114964.3.peg.3963; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000015524; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000015524}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}. FT DOMAIN 209 386 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 440 AA; 47628 MW; 9BAA8B6CD7ECFFE0 CRC64; MATFNRDSSD EVSRGARAVV VRAETQGAER RDSDARLEEA KGLALAIGID VCAAQAFRVR DRKPATLFGS GQVESIAALV EAEEAELVIV DNGLSPAQQS NLEKATSAKV IDRTGLILEI FGERAATNEG RLQVELAHLD YQAGRLVRSW THLERQRGGF GFLGGPGETQ IEADRRMIRD RMAKIRRELD QVTRTRGLHR ARRQRAPWPV IALVGYTNAG KSTLFNRLTG ADVMAQDLLF ATLDPTMRQI ALPGLDKAIL SDTVGFVSDL PTQLIAAFRA TLEEVLSADM IVHVRDIAHP DTEAQRDDVI DVLRELGVAG DGDEADSASP AIIEAWNKLD LLDPGAAALT HEVAARRDDV VILSALTGEG IDALQRTIGA RLTAGAIVHA LHVSLADGAA VAWLHEHGEV LSSRSEAGEM IVEVRLSDSA MARFLKRRAD // ID T0HQV4_9SPHN Unreviewed; 451 AA. AC T0HQV4; DT 16-OCT-2013, integrated into UniProtKB/TrEMBL. DT 16-OCT-2013, sequence version 1. DT 07-JUN-2017, entry version 28. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=L288_01490 {ECO:0000313|EMBL:EQB14543.1}; OS Sphingobium quisquiliarum P25. OC Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales; OC Sphingomonadaceae; Sphingobium. OX NCBI_TaxID=1329909 {ECO:0000313|EMBL:EQB14543.1, ECO:0000313|Proteomes:UP000015525}; RN [1] {ECO:0000313|EMBL:EQB14543.1, ECO:0000313|Proteomes:UP000015525} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=P25 {ECO:0000313|EMBL:EQB14543.1, RC ECO:0000313|Proteomes:UP000015525}; RX PubMed=24029763; RA Kumar Singh A., Sangwan N., Sharma A., Gupta V., Khurana J.P., Lal R.; RT "Draft Genome Sequence of Sphingobium quisquiliarum Strain P25T, a RT Novel Hexachlorocyclohexane (HCH)-Degrading Bacterium Isolated from an RT HCH Dumpsite."; RL Genome Announc. 1:e00717-13(2013). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EQB14543.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ATHO01000009; EQB14543.1; -; Genomic_DNA. DR RefSeq; WP_021236628.1; NZ_ATHO01000009.1. DR EnsemblBacteria; EQB14543; EQB14543; L288_01490. DR PATRIC; fig|1329909.3.peg.273; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000015525; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 2. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000015525}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000015525}. FT DOMAIN 209 389 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 451 AA; 49158 MW; 94979F3E962C57A7 CRC64; MAVFNRDSED EVTRGARAIV VRAETHGAER RDSDARLEEA RGLALAIGID VRAAQAFRVR DRKPATLFGS GQVEQIAALA EAEDAELVIV DNALSPVQQS NLEKATSTKV IDRTGLILEI FGERAATNEG RLQVELAHLD YQAGRLVRSW THLERQRGGF GFLGGPGETQ IEADRRMIRD RMAKIRRELD QVTRTRSLHR ARRQRAPWPV IALVGYTNAG KSTLFNRLTG ADVMAEDLLF ATLDPTMRQI ALPGLDKAIL SDTVGFVSDL PTQLIAAFRA TLEEVLSADL IIHVRDIAHP DSEAQRDDVM DVLSELGVAG EGALEGGEGD EPPPIIEAWN KLDLLDAEAA DHLRELAARR DDVVILSAIT GQGVDDLQRA ISKRLTAGAQ VHRLHVPLSD GAALAWLHEH GEVIGSTAEQ GEMLVDVRLS DSALARFLKR GGPKAEDGDE P // ID T0HRH2_9SPHN Unreviewed; 446 AA. AC T0HRH2; DT 16-OCT-2013, integrated into UniProtKB/TrEMBL. DT 16-OCT-2013, sequence version 1. DT 07-JUN-2017, entry version 28. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=L284_03570 {ECO:0000313|EMBL:EQB18951.1}; OS Novosphingobium lindaniclasticum LE124. OC Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales; OC Sphingomonadaceae; Novosphingobium. OX NCBI_TaxID=1096930 {ECO:0000313|EMBL:EQB18951.1, ECO:0000313|Proteomes:UP000015527}; RN [1] {ECO:0000313|EMBL:EQB18951.1, ECO:0000313|Proteomes:UP000015527} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=LE124 {ECO:0000313|EMBL:EQB18951.1, RC ECO:0000313|Proteomes:UP000015527}; RX PubMed=24029761; RA Saxena A., Nayyar N., Sangwan N., Kumari R., Khurana J.P., Lal R.; RT "Genome Sequence of Novosphingobium lindaniclasticum LE124T, Isolated RT from a Hexachlorocyclohexane Dumpsite."; RL Genome Announc. 1:e00715-13(2013). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EQB18951.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ATHL01000028; EQB18951.1; -; Genomic_DNA. DR RefSeq; WP_021232683.1; NZ_ATHL01000028.1. DR EnsemblBacteria; EQB18951; EQB18951; L284_03570. DR PATRIC; fig|1096930.3.peg.704; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000015527; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000015527}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000015527}. FT DOMAIN 206 390 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 446 AA; 49010 MW; E8639EB6777068AD CRC64; MNDELTGEVT RGARALVVYP QMRGRGDLDP EARLEEARGL AAAIGLVVAE AMAIPIREPR AGTLFGEGQI QNISVACELN EAELIIVDGS LSAIQQRNLE EKLKRKVIDR TGLILEIFGE RAATAEGRLQ VELAHLDYQA GRLVRSWTHL ERQRGGFGFL GGPGETQIEA DRRMIRDRMA KIRRELEQVR RTRGLHRDRR DKAPWPIVAL VGYTNAGKST LFNYLTGAEV MAEDLLFATL DPTMRAIRLP AVEKAILSDT VGFISDLPTQ LVAAFRATLE EVNAADVILH VRDIANPDTE SQKRQVLDVL ADLGVIDGEG GSEEEGETAL GIPIIEVWNK WDLLTPMQAD ELRDVMAQRP DEVIVPLSAR TGMGCEFLLE TIGATLTSDA KVYTFVIPAA DGQRIAFLHA RGEVLSEEDA GAGDQGPLLR LQVRLAEREL GRFSAL // ID T0KG09_9SPHN Unreviewed; 438 AA. AC T0KG09; DT 16-OCT-2013, integrated into UniProtKB/TrEMBL. DT 16-OCT-2013, sequence version 1. DT 07-JUN-2017, entry version 28. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=M529_09945 {ECO:0000313|EMBL:EQB32373.1}; OS Sphingobium ummariense RL-3. OC Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales; OC Sphingomonadaceae; Sphingobium. OX NCBI_TaxID=1346791 {ECO:0000313|EMBL:EQB32373.1, ECO:0000313|Proteomes:UP000015523}; RN [1] {ECO:0000313|EMBL:EQB32373.1, ECO:0000313|Proteomes:UP000015523} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=RL-3 {ECO:0000313|EMBL:EQB32373.1, RC ECO:0000313|Proteomes:UP000015523}; RX PubMed=24233594; RA Kohli P., Dua A., Sangwan N., Oldach P., Khurana J.P., Lal R.; RT "Draft Genome Sequence of Sphingobium ummariense Strain RL-3, a RT Hexachlorocyclohexane-Degrading Bacterium."; RL Genome Announc. 1:e00956-13(2013). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EQB32373.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AUWY01000072; EQB32373.1; -; Genomic_DNA. DR RefSeq; WP_021317813.1; NZ_AUWY01000072.1. DR EnsemblBacteria; EQB32373; EQB32373; M529_09945. DR PATRIC; fig|1346791.3.peg.1911; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000015523; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0016810; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds; IEA:InterPro. DR CDD; cd01878; HflX; 1. DR Gene3D; 2.30.40.10; -; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR011059; Metal-dep_hydrolase_composite. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000015523}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000015523}. FT DOMAIN 209 384 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 438 AA; 47805 MW; 17E5C01F56C5AF6B CRC64; MAVFNRDSAD EVSRGARAIV VRADVPGAER RDSDARIEEA KGLALAIGID VRAAQAFRVR DRKPATLFGS GQVDSIAALA QENEAELVIV DNALSPVQQS NLEKATGAKV IDRTGLILEI FGERAATNEG RLQVELAHLD YQAGRLVRSW THLERQRGGF GFLGGPGETQ IEADRRMIRD RMAKIRRELE QVTRTRGLHR ARRQRAPWPV IALVGYTNAG KSTLFNRLTG ADVMAEDLLF ATLDPTMRQI ALPGLDKAIL SDTVGFVSDL PTQLIAAFRA TLEEVLSADM IVHVRDIAHP DSEAQRDDVL DVLAELGIGG EQPQEDAPVI IEAWNKLDLL DAEAAAYVRE AAARRDDVVI LSALTGEGVD LLQRAIATRM TAGARVHKLR VPLADGAAIA WLHEHGEVLG SNPDGGDMAI EVRLSDSALA RFWKRERD // ID T0MW58_9CLOT Unreviewed; 595 AA. AC T0MW58; DT 16-OCT-2013, integrated into UniProtKB/TrEMBL. DT 16-OCT-2013, sequence version 1. DT 07-JUN-2017, entry version 29. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=M918_12015 {ECO:0000313|EMBL:EQB86879.1}; OS Clostridium sp. BL8. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=1354301 {ECO:0000313|EMBL:EQB86879.1, ECO:0000313|Proteomes:UP000015873}; RN [1] {ECO:0000313|EMBL:EQB86879.1, ECO:0000313|Proteomes:UP000015873} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BL8 {ECO:0000313|EMBL:EQB86879.1, RC ECO:0000313|Proteomes:UP000015873}; RX PubMed=25076986; DOI=10.1186/1757-4749-6-30; RA Marathe N.P., Shetty S.A., Lanjekar V.B., Rasane M.H., Ranade D.R., RA Shouche Y.S.; RT "Genome sequencing of multidrug resistant novel Clostridium sp. BL8 RT reveals its potential for pathogenicity."; RL Gut Pathog 6:30-30(2014). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EQB86879.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AUPA01000212; EQB86879.1; -; Genomic_DNA. DR RefSeq; WP_021284645.1; NZ_AUPA01000212.1. DR EnsemblBacteria; EQB86879; EQB86879; M918_12015. DR PATRIC; fig|1354301.3.peg.3533; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000015873; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000015873}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000015873}. FT DOMAIN 364 541 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 595 AA; 66228 MW; AB476A2705F8AC16 CRC64; MVNGNTEGVK KFILNKLDSI YDMKFGKVEI LSEELANLLK EVTLELEREV SVAIDRKGSV VSVAIGDSST VDMPEINIKE GKLSAVRVIH THPNGNPKLS ALDISALLKL KLDCIVAIGV SKDNPLYCNL GFCDVKDNIL IEEEIGPLSI SKVLDFNFLD KVKHIESLMK DNEIIEDNSE RAILVAVEDE ESLEELEELT KACNVEPVHS ILQKRNKIDP ALYIGSGKVE EIAMLRQALR ANVVIFDEEL SGSQVRNLEQ ALGVKVVDRT TLILDIFARR AKSKESKIQV ELSQLKYRLS RLSGLGTVLS RTGGGIGTRG PGEKKLETDR RHIKETIYDL NRELEKIKTT RATQREGRNK DNVSRISLVG YTNAGKSTLR NALCDFSPQK SSVTKEKVFE ADMLFATLDI TTRGIVLPDN REATVTDTVG FIRKLPHDLV EAFKSTLEEV VYSDVLLHVV DSSSSTAALQ VEVVEEVLKE LGAGEKPTIL VLNKVDKASE EQIKVLRDKF SKHNIIEISA KSGENLDGLL EECTKVLPYK LKSFKVLIPY SDSSTVAYLH RNAKVESEEY EEQGTLVKVQ GDEEVYNKCK AYIIE // ID T0NFR0_9CLOT Unreviewed; 419 AA. AC T0NFR0; DT 16-OCT-2013, integrated into UniProtKB/TrEMBL. DT 16-OCT-2013, sequence version 1. DT 07-JUN-2017, entry version 29. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=M918_22775 {ECO:0000313|EMBL:EQB88885.1}; OS Clostridium sp. BL8. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=1354301 {ECO:0000313|EMBL:EQB88885.1, ECO:0000313|Proteomes:UP000015873}; RN [1] {ECO:0000313|EMBL:EQB88885.1, ECO:0000313|Proteomes:UP000015873} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BL8 {ECO:0000313|EMBL:EQB88885.1, RC ECO:0000313|Proteomes:UP000015873}; RX PubMed=25076986; DOI=10.1186/1757-4749-6-30; RA Marathe N.P., Shetty S.A., Lanjekar V.B., Rasane M.H., Ranade D.R., RA Shouche Y.S.; RT "Genome sequencing of multidrug resistant novel Clostridium sp. BL8 RT reveals its potential for pathogenicity."; RL Gut Pathog 6:30-30(2014). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EQB88885.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AUPA01000071; EQB88885.1; -; Genomic_DNA. DR RefSeq; WP_021282638.1; NZ_AUPA01000071.1. DR EnsemblBacteria; EQB88885; EQB88885; M918_22775. DR PATRIC; fig|1354301.3.peg.1535; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000015873; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000015873}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000015873}. FT DOMAIN 197 365 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 419 AA; 47434 MW; 5C22E2A4689A9CC5 CRC64; METRQKALLV GVNLNNKIGF KESMEELKNL AFACDFQVEG EVAQNLRATT NAYYVGTGKV KEILHLMREK ECDVVIFNNE LSPSQLRNLE KILKCRILDR TALILEIFSE RAKTHEAKLQ VEVANLKYLL PRLIGAREAL GRQSGGVGTR NKGAGEKKLE LDRRKVEERI VALNKELEAV VFQRETQRKK RNKNSLPVVA LVGYTNAGKS TVMNTMIDAY KNTEEKKVFE KDMLFATLET AVRSIVLPDN KTFLLTDTVG FVSNLPHDLV KAFRSTLEEV CEADLLVHVV DLSNPNYNHE IEVTNDTLNQ IGAGDIPVIY AYNKIDLAQE PMDIQQEDSV QISAKNGIGI DKLTNLIREK IFVDYVQCKM LIPYDKGDIT SYLRANANVK LVKYENEGTL LNLECSKIDY EKLEEFVVK // ID T0PGW7_PHOTE Unreviewed; 426 AA. AC T0PGW7; DT 16-OCT-2013, integrated into UniProtKB/TrEMBL. DT 16-OCT-2013, sequence version 1. DT 30-AUG-2017, entry version 32. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=B738_01166 {ECO:0000313|EMBL:EQC02001.1}; OS Photorhabdus temperata subsp. temperata M1021. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; OC Morganellaceae; Photorhabdus. OX NCBI_TaxID=1221520 {ECO:0000313|EMBL:EQC02001.1, ECO:0000313|Proteomes:UP000015813}; RN [1] {ECO:0000313|EMBL:EQC02001.1, ECO:0000313|Proteomes:UP000015813} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=M1021 {ECO:0000313|EMBL:EQC02001.1, RC ECO:0000313|Proteomes:UP000015813}; RX PubMed=24029767; RA Park G.S., Khan A.R., Hong S.J., Jang E.K., Ullah I., Jung B.K., RA Choi J., Yoo N.K., Park K.J., Shin J.H.; RT "Draft Genome Sequence of Entomopathogenic Bacterium Photorhabdus RT temperata Strain M1021, Isolated from Nematodes."; RL Genome Announc. 1:e00747-13(2013). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EQC02001.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AUXQ01000003; EQC02001.1; -; Genomic_DNA. DR EnsemblBacteria; EQC02001; EQC02001; B738_01166. DR PATRIC; fig|1221520.3.peg.233; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000015813; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000015813}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}. FT DOMAIN 198 365 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 426 AA; 48165 MW; 9DF3E28DE8B18F68 CRC64; MFERYEGGER AVVVHIFFSQ DKDTDNLSEF ESLVTSAGVV PVQIVTGSRK APHPKYFVGE GKAEEVAEAV QASGADVVLF NHTLSPAQER NLERLCQCRV IDRTGVILDI FAQRARTHEG KLQVELAQLR HLSTRLVRGW THLERQKGGI GLRGPGETQL ETDRRLLRDK IRQILSRLSR VEKQREQGRQ ARNKADIPTI SLVGYTNAGK SSLFNRMTSA EVYTADQLFA TLDPTLRRIG VDDVGTAVLA DTVGFIRHLP HDLVAAFKAT LQETRQATLL LHVVDAADSR LDENITAVDS VLEEIEAHEI PVLLVMNKID MLEDFTPRID RNEDNLPVRV WLSAQTGEGI PLLLQALTER LSGEIAHYEL RLPPEAGRLR SRFYQLQAIE KEWIEEDGKV GIEVRMPIVD WRRLCKQEQD LFDYIV // ID T0RTN5_9DELT Unreviewed; 439 AA. AC T0RTN5; DT 16-OCT-2013, integrated into UniProtKB/TrEMBL. DT 16-OCT-2013, sequence version 1. DT 07-JUN-2017, entry version 27. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:EQC50191.1}; GN ORFNames=M899_2950 {ECO:0000313|EMBL:EQC50191.1}; OS Bacteriovorax sp. BSW11_IV. OC Bacteria; Proteobacteria; Deltaproteobacteria; Bdellovibrionales; OC Bacteriovoracaceae; Bacteriovorax. OX NCBI_TaxID=1353529 {ECO:0000313|EMBL:EQC50191.1, ECO:0000313|Proteomes:UP000015857}; RN [1] {ECO:0000313|EMBL:EQC50191.1, ECO:0000313|Proteomes:UP000015857} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BSW11_IV {ECO:0000313|EMBL:EQC50191.1, RC ECO:0000313|Proteomes:UP000015857}; RA Chen H., Brinkac L.M., Mishra P., Dickerson T., Gordon-Bradley N., RA Lymperopoulou D.S., Williams H.N., Badger J.H.; RT "Draft genome sequences for the obligate bacterial predators RT Bacteriovorax spp. of four phylogenetic clusters."; RL Submitted (JUL-2013) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EQC50191.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AUNE01000004; EQC50191.1; -; Genomic_DNA. DR RefSeq; WP_021269615.1; NZ_AUNE01000004.1. DR EnsemblBacteria; EQC50191; EQC50191; M899_2950. DR PATRIC; fig|1353529.3.peg.185; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000015857; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000015857}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000015857}. FT DOMAIN 208 334 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 439 AA; 50040 MW; 01D24FCE98BEC1F3 CRC64; MLDNEFFISR EAKASLVSLV CPSFKEHATI NETERSLTEL RELLRTLGIE AGESYIQNKK TVDPATILGS GKIEEIAEAA KEEGSTLLVF DCELTASQIR NIKKISGLSV VDRCHIILEI FSEHARTNEA RIQIEIARLQ YILPRLSGFW SHLGRQRGGI GVRGGEGEQQ IELDRRIIRE RIEFFKKELV EMQKSREQQR KRRQNKAVTA ALVGYTNAGK SSVMNRLCRV NVLEENKLFA TLDSTYRMLN PDTKPPMILI DTVGFISNLP NTLIDGFKTT LESALEADLL VIVCDISDPH FKKHLEVTNS VLDELNLGAK DRIIVFNKKD QLEDPLKGKI ISRSYENSFL VSSYEKDDMD NLRKYIINYF LDKQEHYDLF IPYDRGDAHA QIASKTNVMS TVNHETGIFY RIRVPAFIFN PLGLQNFILG PEDERPSEL // ID T0SQT7_9DELT Unreviewed; 442 AA. AC T0SQT7; DT 16-OCT-2013, integrated into UniProtKB/TrEMBL. DT 16-OCT-2013, sequence version 1. DT 07-JUN-2017, entry version 28. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:EQC47588.1}; GN ORFNames=M900_0710 {ECO:0000313|EMBL:EQC47588.1}; OS Bacteriovorax sp. Seq25_V. OC Bacteria; Proteobacteria; Deltaproteobacteria; Bdellovibrionales; OC Bacteriovoracaceae; Bacteriovorax. OX NCBI_TaxID=1201288 {ECO:0000313|EMBL:EQC47588.1, ECO:0000313|Proteomes:UP000015895}; RN [1] {ECO:0000313|EMBL:EQC47588.1, ECO:0000313|Proteomes:UP000015895} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SEQ25_V {ECO:0000313|Proteomes:UP000015895}; RA Chen H., Brinkac L.M., Mishra P., Dickerson T., Gordon-Bradley N., RA Lymperopoulou D.S., Williams H.N., Badger J.H.; RT "Draft Genome Sequences for the obligate bacterial predators RT Bacteriovorax spp. of four phylogenetic clusters."; RL Submitted (JUL-2013) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EQC47588.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AUNI01000009; EQC47588.1; -; Genomic_DNA. DR RefSeq; WP_021273534.1; NZ_AUNI01000009.1. DR EnsemblBacteria; EQC47588; EQC47588; M900_0710. DR PATRIC; fig|1201288.3.peg.484; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000015895; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000015895}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000015895}. FT DOMAIN 208 374 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 175 202 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 442 AA; 50263 MW; 84E80462D184DFBE CRC64; MLDNEFYISR EAKASLVSIV CPSFEEHATE KETLRSLGEL RELMRTLGIE TGDQYIQNKK AIDPASILGS GKILEIAEQA REEGSSLLVF DCELTSSQIR NIKKLTGLSV VDRCHIILEI FSEHAHTNEA KIQIEIARLQ YILPRLAGFW SHLGRQKGGI GVRGGEGEQQ IELDRRIIRE RIEFFKRELK EVEKSRVEQR KRRSKKAITA ALVGYTNAGK SSLMNRLCRV NVLEEDKLFA TLDSTFRMLN PDTKPPMILI DTVGFLSNLP NTLIDGFKTT LESALEADLL IIVCDISDEH YEKQLKVTMN VLNELGLEGK EKLIVFNKSD KLNDPIKASI IKRTYPESFV ISSFDPEQIK DLRSHIVNYF LEKQNRYDLF VPYDAGAAHS QVVSKTNVIK TANFERGIFY RVRAPDFIFE PLALHQFLIG PDDPLISEFN SL // ID T0T4V6_9DELT Unreviewed; 350 AA. AC T0T4V6; DT 16-OCT-2013, integrated into UniProtKB/TrEMBL. DT 16-OCT-2013, sequence version 1. DT 07-JUN-2017, entry version 20. DE SubName: Full=GTP-binding protein HflX {ECO:0000313|EMBL:EQC52388.1}; DE Flags: Fragment; GN Name=hflX {ECO:0000313|EMBL:EQC52388.1}; GN ORFNames=M901_0403 {ECO:0000313|EMBL:EQC52388.1}; OS Bacteriovorax sp. DB6_IX. OC Bacteria; Proteobacteria; Deltaproteobacteria; Bdellovibrionales; OC Bacteriovoracaceae; Bacteriovorax. OX NCBI_TaxID=1353530 {ECO:0000313|EMBL:EQC52388.1, ECO:0000313|Proteomes:UP000015812}; RN [1] {ECO:0000313|EMBL:EQC52388.1, ECO:0000313|Proteomes:UP000015812} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DB6_IX {ECO:0000313|EMBL:EQC52388.1, RC ECO:0000313|Proteomes:UP000015812}; RA Chen H., Brinkac L.M., Mishra P., Dickerson T., Gordon-Bradley N., RA Lymperopoulou D.S., Williams H.N., Badger J.H.; RT "Draft Genome Sequences for the obligate bacterial predators RT Bacteriovorax spp. of four phylogenetic clusters."; RL Submitted (JUL-2013) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EQC52388.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AUNJ01000065; EQC52388.1; -; Genomic_DNA. DR RefSeq; WP_021276523.1; NZ_AUNJ01000065.1. DR EnsemblBacteria; EQC52388; EQC52388; M901_0403. DR Proteomes; UP000015812; Unassembled WGS sequence. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000015812}; KW Reference proteome {ECO:0000313|Proteomes:UP000015812}. FT DOMAIN 208 350 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT NON_TER 350 350 {ECO:0000313|EMBL:EQC52388.1}. SQ SEQUENCE 350 AA; 39823 MW; 667E70C3E850E8E4 CRC64; MLDNEFYISR ESKASLVSLI CPKFAEHSTE KDTMRSLDEL RELMRTLGIE TGEEYIQNRK TIDPGTILGS GKIEEIANKA KAEGSTILVF DCELTSSQIR NIKKISGLSV VDRCHIILEI FSEHARTKEA KIQIEISRLQ YILPRLAGFW SHLGRQKGGI GVRGGEGEQQ IELDRRIIRD RIAFFKKELK EVEKSRIEQR KKRSKKAITA ALVGYTNAGK SSLMNRLCRV DVLEEDKLFA TLDSTFRMLN PDTKPPMILI DTVGFLSNLP NTLIDGFKTT LESAMEADLL IIVCDISDEN FEKHLEVTDN VLKELGVDDK ERLVIFNKKD KLNDPIKSRI IRRTHPDSFV // ID T0UDH7_9ENTE Unreviewed; 412 AA. AC T0UDH7; DT 16-OCT-2013, integrated into UniProtKB/TrEMBL. DT 16-OCT-2013, sequence version 1. DT 07-JUN-2017, entry version 29. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=HSIEG1_2974 {ECO:0000313|EMBL:EQC81432.1}; OS Enterococcus sp. HSIEG1. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Enterococcaceae; OC Enterococcus. OX NCBI_TaxID=1316414 {ECO:0000313|EMBL:EQC81432.1, ECO:0000313|Proteomes:UP000015939}; RN [1] {ECO:0000313|EMBL:EQC81432.1, ECO:0000313|Proteomes:UP000015939} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=HSIEG1 {ECO:0000313|EMBL:EQC81432.1}; RX PubMed=24336366; RA van den Bogert B., Boekhorst J., Smid E.J., Zoetendal E.G., RA Kleerebezem M.; RT "Draft Genome Sequence of Enterococcus sp. Strain HSIEG1, Isolated RT from the Human Small Intestine."; RL Genome Announc. 1:e01013-13(2013). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EQC81432.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ASKG01000017; EQC81432.1; -; Genomic_DNA. DR ProteinModelPortal; T0UDH7; -. DR EnsemblBacteria; EQC81432; EQC81432; HSIEG1_2974. DR PATRIC; fig|1316414.3.peg.1790; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000015939; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000015939}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000015939}. FT DOMAIN 195 357 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 412 AA; 46533 MW; 43418B8C4794C834 CRC64; MTQERVILVG VETERNYSTF ASSMNELKSL TKTANGEVIF SLIQKRPQVD RQTVIGKGKL AELQQLVDAH EADLVIFNHE LTPRQSQLIG EELGAPVIDR VQLILDIFAM RARSKEGKLQ VELAQLDYLL PRLIGQGKNM SRLGGGIGTR GPGETKLETD RRHIRNRITI IKRELKEVAA HRDRTRQKRR DSQVFQIGLI GYTNAGKSTI LNLLTSADTY EQDQLFATLD PLTKRWRLPE GLEVTVTDTV GFIQELPTQL IDAFHSTLEE SQNMDLLLHV VDAGSHDRQQ QEKTVLALME ELSLTQVPVL TIYNKADRID PEQFVPTLFP NVLISAKSSK GKEQLIQAIK MELMQIMQPY QTVLAANEGK RLSRLKRETL LLTNDFDEED QTYHLKGFAL PGSAGIYPTI EE // ID T0VCD2_9STRE Unreviewed; 202 AA. AC T0VCD2; DT 16-OCT-2013, integrated into UniProtKB/TrEMBL. DT 16-OCT-2013, sequence version 1. DT 07-JUN-2017, entry version 15. DE SubName: Full=GTP-binding protein Hfln {ECO:0000313|EMBL:EQC77163.1}; GN ORFNames=HSISM1_1660 {ECO:0000313|EMBL:EQC77163.1}; OS Streptococcus sp. HSISM1. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=1316408 {ECO:0000313|EMBL:EQC77163.1, ECO:0000313|Proteomes:UP000015933}; RN [1] {ECO:0000313|EMBL:EQC77163.1, ECO:0000313|Proteomes:UP000015933} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=HSISM1 {ECO:0000313|EMBL:EQC77163.1, RC ECO:0000313|Proteomes:UP000015933}; RA Van den Bogert B., Boekhorst J., Herrmann R., Smid E.J., RA Zoetendal E.G., Kleerebezem M.; RT "Comparative Genomics Analysis of Streptococcus Isolates from the RT Human Small Intestine Reveals their Adaptation to a Highly Dynamic RT Ecosystem."; RL PLoS ONE 8:E83418-E83418(2013). CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EQC77163.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ASKI01000055; EQC77163.1; -; Genomic_DNA. DR EnsemblBacteria; EQC77163; EQC77163; HSISM1_1660. DR PATRIC; fig|1316408.3.peg.1214; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000015933; Chromosome. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. PE 4: Predicted; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000015933}; KW Reference proteome {ECO:0000313|Proteomes:UP000015933}. FT DOMAIN 26 113 GTP-bdg_N. {ECO:0000259|Pfam:PF13167}. FT DOMAIN 115 185 GTP-bdg_M. {ECO:0000259|Pfam:PF16360}. FT COILED 158 185 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 202 AA; 22729 MW; E3DE09A70E1FB39E CRC64; MIETEKKQER ILLVGVELQG MDNFDMSMEE LASLAKTAGG DVRGSYTQKR EKYDTKTFVG SGKLEEIAQM VEADEITTVV VNNRLTPRQN VNLEEILGVK VIDRMQLILD IFAMRARSHE GKLQVHLAQL KYLLPRLVGQ GIMLSRQAGG IGSRGPGESQ LELNRRSVRN QITDIERQLK AVEKTGKPFV KNAWNHLSSR LV // ID T0Z926_9BACT Unreviewed; 616 AA. AC T0Z926; DT 16-OCT-2013, integrated into UniProtKB/TrEMBL. DT 16-OCT-2013, sequence version 1. DT 07-JUN-2017, entry version 18. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EQD25629.1}; DE Flags: Fragment; GN ORFNames=D084_Lepto4C00052G0002 {ECO:0000313|EMBL:EQD25629.1}; OS Leptospirillum sp. Group IV 'UBA BS'. OC Bacteria; Nitrospirae; Nitrospirales; Nitrospiraceae; Leptospirillum. OX NCBI_TaxID=1260983 {ECO:0000313|EMBL:EQD25629.1, ECO:0000313|Proteomes:UP000017751}; RN [1] {ECO:0000313|EMBL:EQD25629.1, ECO:0000313|Proteomes:UP000017751} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=23645189; DOI=10.1128/AEM.00202-13; RA Goltsman D.S., Dasari M., Thomas B.C., Shah M.B., VerBerkmoes N.C., RA Hettich R.L., Banfield J.F.; RT "New group in the Leptospirillum clade: cultivation-independent RT community genomics, proteomics, and transcriptomics of the new species RT "Leptospirillum group IV UBA BS"."; RL Appl. Environ. Microbiol. 79:5384-5393(2013). CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EQD25629.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AURA01000052; EQD25629.1; -; Genomic_DNA. DR PATRIC; fig|1260983.3.peg.123; -. DR Proteomes; UP000017751; Unassembled WGS sequence. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000017751}; KW Reference proteome {ECO:0000313|Proteomes:UP000017751}. FT DOMAIN 441 606 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 400 427 {ECO:0000256|SAM:Coils}. FT NON_TER 1 1 {ECO:0000313|EMBL:EQD25629.1}. SQ SEQUENCE 616 AA; 68922 MW; 204A56A58B1B3260 CRC64; DRSSLFDSLR PSSSLGRERV LKPFIPAIDR IRRSLRLRVW YNENNRVPAV SRVSPPAKGP PISGLTGNLT GLKASQIKSL SRLHGRRISP GLWISPEIAR QMALLSHETG RQIALLITRE GTVALVVVGT ARDIFLSELP PSRSGSRSLR GLRMVHTHLQ GEGLSQDDLN DLALLRFDAM VALQMNRDSG LLDRVSVATI NPDPVGDPPW IVEAPRPITP ESLSSGGRIE ALEEELSRSL SAAMKKTTGQ ERALLVSVSP DALSDQEDAL AELSELARSA DVDVLGVVRQ RIARYHPTTL MSVDRIKSLL IHALQVHATL IIFEQELSPN QVRKIAEMTE LKVIDRTQLI LDIFARRAHS RDGKLQVELA QLKYLLPRLF ERSTALSRLT GGIGGRGPGE TRLEEDRRRV RDRIASLSAR LRHLEVERSG RKSRRREAAL PVVSLVGYTN VGKSTLLNRL THSAVLVEDK MFATLDPTTR RLRFPREREI ILTDTVGFIR DLPADLRRAF MATFDELRDA DLIVHVTDAS HPQCELMIER VETILREMEL HRIPTLLLFN KCDRIPPETR RMLALRYPGA VFVSALDPES LRPLERILEG RLFEKPLESL VAGGSD // ID T1FNU6_HELRO Unreviewed; 499 AA. AC T1FNU6; DT 16-OCT-2013, integrated into UniProtKB/TrEMBL. DT 16-OCT-2013, sequence version 1. DT 07-JUN-2017, entry version 24. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:ESN90009.1, ECO:0000313|EnsemblMetazoa:HelroP186232}; GN ORFNames=HELRODRAFT_186232 {ECO:0000313|EMBL:ESN90009.1}; OS Helobdella robusta (Californian leech). OC Eukaryota; Metazoa; Lophotrochozoa; Annelida; Clitellata; Hirudinea; OC Rhynchobdellida; Glossiphoniidae; Helobdella. OX NCBI_TaxID=6412 {ECO:0000313|EnsemblMetazoa:HelroP186232, ECO:0000313|Proteomes:UP000015101}; RN [1] {ECO:0000313|EnsemblMetazoa:HelroP186232, ECO:0000313|Proteomes:UP000015101} RP NUCLEOTIDE SEQUENCE. RA Hellsten U., Grimwood J., Chapman J.A., Shapiro H., Aerts A., RA Otillar R.P., Terry A.Y., Boore J.L., Simakov O., Marletaz F., RA Cho S.-J., Edsinger-Gonzales E., Havlak P., Kuo D.-H., Larsson T., RA Lv J., Arendt D., Savage R., Osoegawa K., de Jong P., Lindberg D.R., RA Seaver E.C., Weisblat D.A., Putnam N.H., Grigoriev I.V., Rokhsar D.S.; RL Submitted (DEC-2012) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:ESN90009.1, ECO:0000313|EnsemblMetazoa:HelroP186232, ECO:0000313|Proteomes:UP000015101} RP NUCLEOTIDE SEQUENCE. RX PubMed=23254933; DOI=10.1038/nature11696; RA Simakov O., Marletaz F., Cho S.J., Edsinger-Gonzales E., Havlak P., RA Hellsten U., Kuo D.H., Larsson T., Lv J., Arendt D., Savage R., RA Osoegawa K., de Jong P., Grimwood J., Chapman J.A., Shapiro H., RA Aerts A., Otillar R.P., Terry A.Y., Boore J.L., Grigoriev I.V., RA Lindberg D.R., Seaver E.C., Weisblat D.A., Putnam N.H., Rokhsar D.S.; RT "Insights into bilaterian evolution from three spiralian genomes."; RL Nature 493:526-531(2013). RN [3] {ECO:0000313|EnsemblMetazoa:HelroP186232} RP IDENTIFICATION. RG EnsemblMetazoa; RL Submitted (JUN-2015) to UniProtKB. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AMQM01008464; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; KB097783; ESN90009.1; -; Genomic_DNA. DR RefSeq; XP_009031877.1; XM_009033629.1. DR EnsemblMetazoa; HelroT186232; HelroP186232; HelroG186232. DR GeneID; 20210493; -. DR KEGG; hro:HELRODRAFT_186232; -. DR CTD; 20210493; -. DR OMA; MDTVGFM; -. DR OrthoDB; EOG091G0852; -. DR Proteomes; UP000015101; Unassembled WGS sequence. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR CDD; cd01878; HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000015101}; KW Reference proteome {ECO:0000313|Proteomes:UP000015101}. FT DOMAIN 255 434 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 499 AA; 56916 MW; 06E995F935CA8A0B CRC64; MMKLVRKNIF KNYLSFCVCR SKILATSTRH FQDCADEDES LEELFPRLSK IRHSVFIIQP NMRDVPEKAK NTSANHQLSE LCSLVHSIPD WLVIDKAIHS LKFLDKQHVF GKGKLEELRQ HVKSSSLHIT AIVMGMPSLN TNQLSNLQHL FNLPVYDRYT LVLEIFRARA STNEAKLQVS MAEINYIRYH LHGLHRGTLD FQTDALELVG GTSEVPVQTR KMLLRDRESK IQKELVKLEK QRTLAMEKRR KMKIPSVAVV GYTNAGKTSL IKSLTKNENM APKNQLFATL DISNFQGFLP NRMKVLYVDT IGFISDLHPS LLNAFSSTLQ DIAYADLLVH VCDVSHPDRR LQDEVVRRTI TNLPLMPDEL LRSVVRVYNK VDLLGDSERA KLEEETLTSS SSSSSSPPVL ISVKNGWNRD EVMMTIQNAI IKATGRVTKK LKIPINSGLL QWLYKESEVE EVTSDPKNAE MYLIKTTMTA QSYAKFIKNF KLKDKNSLS // ID T1IAW0_RHOPR Unreviewed; 419 AA. AC T1IAW0; DT 16-OCT-2013, integrated into UniProtKB/TrEMBL. DT 16-OCT-2013, sequence version 1. DT 05-JUL-2017, entry version 26. DE SubName: Full=Uncharacterized protein {ECO:0000313|EnsemblMetazoa:RPRC013431-PA}; DE Flags: Fragment; OS Rhodnius prolixus (Triatomid bug). OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; OC Pterygota; Neoptera; Paraneoptera; Hemiptera; Heteroptera; OC Panheteroptera; Cimicomorpha; Reduviidae; Triatominae; Rhodnius. OX NCBI_TaxID=13249 {ECO:0000313|EnsemblMetazoa:RPRC013431-PA, ECO:0000313|Proteomes:UP000015103}; RN [1] {ECO:0000313|EnsemblMetazoa:RPRC013431-PA} RP NUCLEOTIDE SEQUENCE. RA Syromyatnikov M.Y., Popov V.N.; RL Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EnsemblMetazoa:RPRC013431-PA} RP IDENTIFICATION. RG EnsemblMetazoa; RL Submitted (MAY-2015) to UniProtKB. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACPB02016103; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EnsemblMetazoa; RPRC013431-RA; RPRC013431-PA; RPRC013431. DR VectorBase; RPRC013431-RA; RPRC013431-PA; RPRC013431. DR OMA; MDTVGFM; -. DR Proteomes; UP000015103; Unassembled WGS sequence. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR CDD; cd01878; HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR001611; Leu-rich_rpt. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR PROSITE; PS51705; G_HFLX; 1. DR PROSITE; PS51450; LRR; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000015103}; KW Reference proteome {ECO:0000313|Proteomes:UP000015103}. FT DOMAIN 202 365 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 419 AA; 48033 MW; 11F43E6EE552E022 CRC64; EETLKDLVPR SLRFAGTPHQ VGIIQPRIKW GQKKVRISTP QMQLDEGISL INSLPGWTVI DSKIISLLSY EKKTFFNTGQ LEIVKEWLQN EMFTSLFINI KSLKLEQVLF LEQYFHIPVF DRYSVIINIF KEHACTKEAK LQVALAEIPY ISSRIRISSC ETFIRKRFHI LNDQKRKIVK TIADLRKRRE LLRNKRRSQQ LPTVAVMGYT NAGKTSLIKC LTEETNLVPE DKLFATLDVT AHAVLLPYNI KALLIDTIGF ITDIPTNLME PFVATLEDAF MADAIIHVKD VSHPNHFAQE LHVIETLKTL NLSNNIIENI ITVGNKCDKA PMQKDAGSVH LVSCQTKYGI EDLKEIIART IIKAKDMMKI RIKVKSGGVE YKWLLKECAV SEISVDKNPQ YVLLDVFITK SKFNKFKHE // ID T1J1K0_STRMM Unreviewed; 471 AA. AC T1J1K0; DT 16-OCT-2013, integrated into UniProtKB/TrEMBL. DT 16-OCT-2013, sequence version 1. DT 10-MAY-2017, entry version 16. DE SubName: Full=Uncharacterized protein {ECO:0000313|EnsemblMetazoa:SMAR007419-PA}; OS Strigamia maritima (European centipede) (Geophilus maritimus). OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Myriapoda; Chilopoda; OC Pleurostigmophora; Geophilomorpha; Linotaeniidae; Strigamia. OX NCBI_TaxID=126957 {ECO:0000313|EnsemblMetazoa:SMAR007419-PA, ECO:0000313|Proteomes:UP000014500}; RN [1] {ECO:0000313|Proteomes:UP000014500} RP NUCLEOTIDE SEQUENCE. RA Richards S.R., Qu J., Jiang H., Jhangiani S.N., Agravi P., RA Goodspeed R., Gross S., Mandapat C., Jackson L., Mathew T., Pu L., RA Thornton R., Saada N., Wilczek-Boney K.B., Lee S., Kovar C., Wu Y., RA Scherer S.E., Worley K.C., Muzny D.M., Gibbs R.; RL Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EnsemblMetazoa:SMAR007419-PA} RP IDENTIFICATION. RG EnsemblMetazoa; RL Submitted (FEB-2015) to UniProtKB. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JH431789; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EnsemblMetazoa; SMAR007419-RA; SMAR007419-PA; SMAR007419. DR OMA; MDTVGFM; -. DR PhylomeDB; T1J1K0; -. DR Proteomes; UP000014500; Unassembled WGS sequence. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR CDD; cd01878; HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000014500}; KW Reference proteome {ECO:0000313|Proteomes:UP000014500}. FT DOMAIN 241 408 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 471 AA; 53215 MW; 2791C45B06815C17 CRC64; SDDRIITDFE DEENPTNEEI EFNTWRQQLY KVDGVGHRIF LVQPKLKYIP KKAKKSTSEL QLAEAVALIE TLPNWKVIEK KIVTVKEPNK KFIFSSGILD ELKYEIANSK RTNGVSAVFL GHDMLTGLQH SSLEAAFGIP VYDRYMIVLR IFRDHARTKE AKLQIALGEI PYLKSRIKGI LLHGYDKGGG NMTFSKGGGE TYLEARKRIL TERESKLKKG IEQLKSHRVL LRQNRVRKQF PVIAIVGYTN AGKTTLIKAM TGDKEIQPKD QLFATLDVTA HAGNLLNNIA VMYIDTVGFI SDIPTDLIHS FAATLEDVAL ADLIIHVCDL SHPDYVAQKA TVRSTLENLK IDQKLLDNMI EIDNKVDLMT EEERFSKNSA ALSVSLVTGE GVSDLKQLIQ DKILHPQSNL MSVQFRVPTG GQEFRWLYKE ANVTSTDADE SDTQFVYIRT VLTKASLSKF RHRFGNMEDS N // ID T1KLM4_TETUR Unreviewed; 493 AA. AC T1KLM4; DT 16-OCT-2013, integrated into UniProtKB/TrEMBL. DT 16-OCT-2013, sequence version 1. DT 07-JUN-2017, entry version 18. DE SubName: Full=Uncharacterized protein {ECO:0000313|EnsemblMetazoa:tetur14g02960.1}; OS Tetranychus urticae (Two-spotted spider mite). OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; OC Acari; Acariformes; Trombidiformes; Prostigmata; Eleutherengona; OC Raphignathae; Tetranychoidea; Tetranychidae; Tetranychus. OX NCBI_TaxID=32264 {ECO:0000313|EnsemblMetazoa:tetur14g02960.1, ECO:0000313|Proteomes:UP000015104}; RN [1] {ECO:0000313|EnsemblMetazoa:tetur14g02960.1, ECO:0000313|Proteomes:UP000015104} RP NUCLEOTIDE SEQUENCE. RC STRAIN=London {ECO:0000313|EnsemblMetazoa:tetur14g02960.1}; RA Rombauts S.; RL Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EnsemblMetazoa:tetur14g02960.1} RP IDENTIFICATION. RG EnsemblMetazoa; RL Submitted (JUN-2015) to UniProtKB. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CAEY01000211; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR RefSeq; XP_015788051.1; XM_015932565.1. DR EnsemblMetazoa; tetur14g02960.1; tetur14g02960.1; tetur14g02960. DR GeneID; 107365100; -. DR OMA; MDTVGFM; -. DR Proteomes; UP000015104; Unassembled WGS sequence. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR CDD; cd01878; HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 4: Predicted; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000015104}; KW Reference proteome {ECO:0000313|Proteomes:UP000015104}. FT DOMAIN 264 433 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 230 260 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 493 AA; 55892 MW; 338E0C5CCDC0FC4B CRC64; MMNFLKRLTF SSKFYKHSTV IRSLCNLNNF GENDYNFHEL LTPDPEYDAL RRNYIVDGRK AHSVLVCQPY IRFPTDIDDK PKSTPQLQLK ESISLIHSIP KWRVSDAGLF GVNDFHKPLF FSEKTVEEID GRIKGSSTTG LFIAADRLLG KQQYELENVL KVPVFDRYSI ILEIFKNHAT SAEAQIQLGL AEILYLKSRV NQYAPEVRGD KYSTGKTAGG SGMTARQRYR KLLESRTKVL KKASEKLEAN KERLRLRRKE LQYPIVSVIG YTNSGKTSLI KALSQDGKLS PEDRLFATLE VTAHPVKLPS LRKVLFLDSV GFIANIPKEL IDSFNVTFKE VANSDLLLHI YDASHPDLAN QKFTVLKTLD YLKFNPNLVS SMINVANKID LIDDSSSENS TAIEEGDIPV SVTEGQNLKS LIEKIDTKLT QVTGQQIVKV KVPNGGEELS WLHRETTIQS IEPDADANFL IVRATMNDVQ RKRFVAYFRR GKK // ID T1ZEM2_STRIT Unreviewed; 412 AA. AC T1ZEM2; DT 13-NOV-2013, integrated into UniProtKB/TrEMBL. DT 13-NOV-2013, sequence version 1. DT 07-JUN-2017, entry version 27. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:AGU75897.1}; GN ORFNames=SIR_0525 {ECO:0000313|EMBL:AGU75897.1}; OS Streptococcus intermedius B196. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus; Streptococcus anginosus group. OX NCBI_TaxID=862967 {ECO:0000313|EMBL:AGU75897.1, ECO:0000313|Proteomes:UP000016233}; RN [1] {ECO:0000313|EMBL:AGU75897.1, ECO:0000313|Proteomes:UP000016233} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=B196 {ECO:0000313|EMBL:AGU75897.1}; RX PubMed=24341328; DOI=10.1186/1471-2164-14-895; RA Olson A.B., Kent H., Sibley C.D., Grinwis M.E., Mabon P., RA Ouellette C., Tyson S., Graham M., Tyler S.D., Van Domselaar G., RA Surette M.G., Corbett C.R.; RT "Phylogenetic relationship and virulence inference of Streptococcus RT Anginosus Group: curated annotation and whole-genome comparative RT analysis support distinct species designation."; RL BMC Genomics 14:895-895(2013). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP003857; AGU75897.1; -; Genomic_DNA. DR RefSeq; WP_021002558.1; NC_022246.1. DR EnsemblBacteria; AGU75897; AGU75897; SIR_0525. DR GeneID; 16761073; -. DR KEGG; sib:SIR_0525; -. DR PATRIC; fig|862967.3.peg.514; -. DR KO; K03665; -. DR Proteomes; UP000016233; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000016233}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000016233}. FT DOMAIN 199 359 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 412 AA; 46542 MW; 5AC305BDAD7E41AA CRC64; MIETEKQQER VILIGVELQG IDNFSLSMEE LASLAGTAGA QVVSSYIQKR EKYDSKTFIG AGKLEEIKHM VEADEISTVI VNNRLTPRQN INLEEILGVK VIDRMQLILD IFAMRARSHE GKLQVHLAQL KYLLPRLVGQ GIMLSRQAGG IGSRGPGESQ LELNRRSVRN QIYDIERQLK IVEKNRATVR EKRLDSSVFK IGLIGYTNAG KSTIMNALTN KNQYEADELF ATLDATTKGA NLTGRLNVTL TDTVGFIQDL PTELISSFKS TLEESKNVDL LVHVIDASDP NHEEHEKTVL AIMKDLDMLD IPRLTLYNKA DKAENFLPTL TPYVLISAKM ENSRAVLQEA LLDKMRELFV PFCIKVGSSK AYKLYELESL AIIDKREYVE ESEVISGYIA EKNKWRLEEF YD // ID T2G743_DESGI Unreviewed; 610 AA. AC T2G743; DT 13-NOV-2013, integrated into UniProtKB/TrEMBL. DT 13-NOV-2013, sequence version 1. DT 07-JUN-2017, entry version 29. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=DGI_0511 {ECO:0000313|EMBL:AGW12420.1}; OS Desulfovibrio gigas DSM 1382 = ATCC 19364. OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfovibrionales; OC Desulfovibrionaceae; Desulfovibrio. OX NCBI_TaxID=1121448 {ECO:0000313|EMBL:AGW12420.1, ECO:0000313|Proteomes:UP000016587}; RN [1] {ECO:0000313|Proteomes:UP000016587} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 19364 / DSM 1382 / NCIB 9332 / VKM B-1759 RC {ECO:0000313|Proteomes:UP000016587}; RA Morais-Silva F.O., Rezende A.M., Pimentel C., Resende D.M., RA Santos C.I., Clemente C., de Oliveira L.M., da Silva S.M., Costa D.A., RA Varela-Raposo A., Horacio E.C.A., Matos M., Flores O., Ruiz J.C., RA Rodrigues-Pousada C.; RL Submitted (JUL-2013) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP006585; AGW12420.1; -; Genomic_DNA. DR EnsemblBacteria; AGW12420; AGW12420; DGI_0511. DR KEGG; dgg:DGI_0511; -. DR PATRIC; fig|1121448.10.peg.506; -. DR KO; K03665; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000016587; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000016587}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000016587}. FT DOMAIN 414 579 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 373 407 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 610 AA; 67528 MW; 12DF73FF1DEBDB13 CRC64; MAHHIPSGAS TIASKLQGNL QGLKPSQQKA LSRLYTRRYP NQSGYTTEQA RELAILSRGV GRQLGLLIDR QGRPQMVIVG EPGSIYIPEL PRARLGAGRL RGLRLLHTHL TPDLLSREDL MDMLFLRLDS LAVLTVDDQG EPRRLQYANL LPATPAPREE DDEPRAEQPA YQVHDVVPWD HVEVDFAELA QALEDEWARL APAPSESRRQ VTSPTPGAGT GEAARAVLVS ISTAPKSAQE RELDELEALA ETAGVVPAGR MIQRVHSLNS ATILSKEKLA ELETQALQAG AGLVLFAGDL SPSQLSNLAD ATERKVLDRT MLILDIFAQH ATSRAGKLQV ELAQLRYTLP RLVGKNKALS RLTGGIGGRG PGEQKLEMDR RKIRERETRL KKQLEELRRH RAAARRRRAR AGVPVAALVG YTNAGKSTLL NVLTQASVLA ENKLFATLDP TTRRLRVPEE RELILTDTVG FIRHLPEELK EAFRATLEEL ESADLLLHVA DASHPELDLH NQAVEDILRE MQLQDVPRLL ILNKWDLLDE ESQAALRFRF PDAVPIAARA GQGLEALSQE IVRRIDWERD VRLPPEPVAT AGDEAATEDM ADDESLFPKD // ID T2KQJ5_9FLAO Unreviewed; 408 AA. AC T2KQJ5; DT 13-NOV-2013, integrated into UniProtKB/TrEMBL. DT 13-NOV-2013, sequence version 1. DT 07-JUN-2017, entry version 28. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=BN863_32930 {ECO:0000313|EMBL:CDF81005.1}; OS Formosa agariphila KMM 3901. OC Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales; OC Flavobacteriaceae; Formosa. OX NCBI_TaxID=1347342 {ECO:0000313|EMBL:CDF81005.1, ECO:0000313|Proteomes:UP000016160}; RN [1] {ECO:0000313|EMBL:CDF81005.1, ECO:0000313|Proteomes:UP000016160} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Type strain: KMM 3901 {ECO:0000313|EMBL:CDF81005.1}; RX PubMed=23995932; DOI=10.1128/AEM.01937-13; RA Mann A.J., Hahnke R.L., Huang S., Werner J., Xing P., Barbeyron T., RA Huettel B., Stueber K., Reinhardt R., Harder J., Gloeckner F.O., RA Amann R.I., Teeling H.; RT "The genome of the alga-associated marine flavobacterium Formosa RT agariphila KMM 3901T reveals a broad potential for degradation of RT algal polysaccharides."; RL Appl. Environ. Microbiol. 79:6813-6822(2013). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; HG315671; CDF81005.1; -; Genomic_DNA. DR RefSeq; WP_038532439.1; NZ_HG315671.1. DR EnsemblBacteria; CDF81005; CDF81005; BN863_32930. DR PATRIC; fig|1347342.6.peg.3321; -. DR Proteomes; UP000016160; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000016160}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000016160}. FT DOMAIN 200 385 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 408 AA; 46989 MW; 2BC0146B2184C87A CRC64; MLEKKDINLE RAVLIGIITK DQNEEQSKEY LDELEFLTYT AGGEVLKRFT QKMEMPNPKT FIGTGKMADV QQFIEDNDVG TAIFDDELSA AQERNISKIL NCKVLDRTNL ILDIFAQRAQ TSYARTQVEL AQCEYLLPRL RGMWTHLERQ KGGIGMRGPG ETEIETDRRI VRERIALLKA KIKTIDKQMS VQRGNRGAMV RVALVGYTNV GKSTLMNVVS KSEVFAENKL FATLDTTVRK VVIHNLPFLL SDTVGFIRKL PTQLVDSFKS TLDEVREADL LLHVVDISHP NFEDHIASVE KILGEIQGAD KPTIMVFNKI DAYEAEPFDE TDLQEVRNSS HYSIEEWKRT WMNKLGENAL FISALNKENL EDFRKRVYDE VREIHVTRFP YNHFLYPDYE DLDLSEEE // ID U1GJQ2_9ACTN Unreviewed; 485 AA. AC U1GJQ2; DT 13-NOV-2013, integrated into UniProtKB/TrEMBL. DT 13-NOV-2013, sequence version 1. DT 07-JUN-2017, entry version 30. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=H641_01016 {ECO:0000313|EMBL:ERF58335.1}, GN L860_11560 {ECO:0000313|EMBL:OCT42240.1}; OS Cutibacterium granulosum DSM 20700. OC Bacteria; Actinobacteria; Propionibacteriales; Propionibacteriaceae; OC Cutibacterium. OX NCBI_TaxID=1160719 {ECO:0000313|EMBL:ERF58335.1, ECO:0000313|Proteomes:UP000016307}; RN [1] {ECO:0000313|EMBL:ERF58335.1, ECO:0000313|Proteomes:UP000016307} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 20700 {ECO:0000313|EMBL:ERF58335.1, RC ECO:0000313|Proteomes:UP000016307}; RX PubMed=24053623; DOI=10.1186/1471-2164-14-640; RA Mak T.N., Schmid M., Brzuszkiewicz E., Zeng G., Meyer R., Sfanos K.S., RA Brinkmann V., Meyer T.F., Bruggemann H.; RT "Comparative genomics reveals distinct host-interacting traits of RT three major human-associated propionibacteria."; RL BMC Genomics 14:640-640(2013). RN [2] {ECO:0000313|EMBL:OCT42240.1, ECO:0000313|Proteomes:UP000094467} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 20700 {ECO:0000313|EMBL:OCT42240.1, RC ECO:0000313|Proteomes:UP000094467}; RA Chronopoulou M.; RL Submitted (MAY-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:ERF58335.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AOSS01000031; ERF58335.1; -; Genomic_DNA. DR EMBL; JNBU01000034; OCT42240.1; -; Genomic_DNA. DR RefSeq; WP_021103224.1; NZ_AOSS01000031.1. DR EnsemblBacteria; ERF58335; ERF58335; H641_01016. DR EnsemblBacteria; OCT42240; OCT42240; L860_11560. DR PATRIC; fig|1160719.4.peg.184; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000016307; Unassembled WGS sequence. DR Proteomes; UP000094467; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000313|EMBL:OCT42240.1}; KW Complete proteome {ECO:0000313|Proteomes:UP000016307}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900, KW ECO:0000313|EMBL:OCT42240.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000016307}. FT DOMAIN 259 431 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 485 AA; 52953 MW; C19970FE6086D3B4 CRC64; MTTQHESPDS PLGDVTAPDD QRDPDGDQFD LAARLSLTRV PGMSTDLSDI SEVEYRQLRL ERVVLVSVWT TGTVQDAENA MIELKALAET AGSQVLEGIV QRRDVPDPAT YLGSGKVREL ADLVRATGAD TVICDGELTA AQLRNLEDRV GVKVVDRTAL ILDIFAQHAR STEGKTQVEL AQLTYLKQRL RGWGQSLSRQ AGGRAAGGAG IGGRGPGETR IETDRRRIGH RITVLRRRLR QMDSTRATTR ARRERDRIPS VAIVGYTNAG KSSLLNRLTG VGVLVEDALF ATLDPTTRRT TTQDGRVYTL TDTVGFVRHL PHDLVEAFKS TLEETAGADV LVHLVDASDP DPVGQIIAVR DVLRSLQDKP QSSEISQVPE ILVFNKIDLI DEVTLAGLRA SRPRARFIST RTGEGVDELI SQIEQALPTP QERVDVVIPY SRGDLVDRIH KHGTIHELEH GVQGTHVIAD LHPGLAAEVR AVGGR // ID U1GUI2_TRESO Unreviewed; 431 AA. AC U1GUI2; DT 13-NOV-2013, integrated into UniProtKB/TrEMBL. DT 13-NOV-2013, sequence version 1. DT 07-JUN-2017, entry version 27. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:ERF61600.1}; GN ORFNames=HMPREF1325_2387 {ECO:0000313|EMBL:ERF61600.1}; OS Treponema socranskii subsp. socranskii VPI DR56BR1116 = ATCC 35536. OC Bacteria; Spirochaetes; Spirochaetales; Spirochaetaceae; Treponema. OX NCBI_TaxID=1125725 {ECO:0000313|EMBL:ERF61600.1, ECO:0000313|Proteomes:UP000016412}; RN [1] {ECO:0000313|EMBL:ERF61600.1, ECO:0000313|Proteomes:UP000016412} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=VPI DR56BR1116 {ECO:0000313|EMBL:ERF61600.1, RC ECO:0000313|Proteomes:UP000016412}; RA Durkin A.S., Haft D.R., McCorrison J., Torralba M., Gillis M., RA Haft D.H., Methe B., Sutton G., Nelson K.E.; RL Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:ERF61600.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AUZJ01000009; ERF61600.1; -; Genomic_DNA. DR EnsemblBacteria; ERF61600; ERF61600; HMPREF1325_2387. DR PATRIC; fig|1125725.3.peg.457; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000016412; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000016412}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000016412}. FT DOMAIN 212 379 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 431 AA; 47705 MW; E0DC7CC13DBE3E6D CRC64; MIEILSKRSV YPYNSAMEEL QKEAERKTRC VLVGEPGNDL RELKSLIDTL GMETVSAITL SRLEVQPAYG MGKGKAEEIA SGAKECEADC IVFDFTLEPT KQRNWEKLSG LPSFDREEVI LRIFASRAQT HEAVLQVELA RLEYSLPRLA HMYGDLARQR GGNYGAKGSG ETQLELDQRQ VREKIFRVKR ELKSVAAGRD TQRKRRSKVS VPSCALVGYT NAGKSSLLNA LTGADVFVEN KLFATLDPTT RRMRIKDGGE VLLTDTVGFI SNLPHTLVNA FKSTLEEAVR ADLLLIVIDA SDANAEKQYE TVCRVLGEIG AVENERLILL NKIDALEKDG GRLAELRAQF PDSLSVSAKE KTGFDELSDK ITGAVFGKRC KCVLPQDKSP LLADIRKGGR ILSEQWLEDG VHVTVYARGK SLALIAPYLV E // ID U1JTR6_9GAMM Unreviewed; 428 AA. AC U1JTR6; DT 13-NOV-2013, integrated into UniProtKB/TrEMBL. DT 13-NOV-2013, sequence version 1. DT 30-AUG-2017, entry version 29. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=PCIT_02270 {ECO:0000313|EMBL:ERG20367.1}; OS Pseudoalteromonas citrea DSM 8771. OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales; OC Pseudoalteromonadaceae; Pseudoalteromonas. OX NCBI_TaxID=1117314 {ECO:0000313|EMBL:ERG20367.1, ECO:0000313|Proteomes:UP000016487}; RN [1] {ECO:0000313|EMBL:ERG20367.1, ECO:0000313|Proteomes:UP000016487} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 8771 {ECO:0000313|Proteomes:UP000016487}; RX PubMed=22535931; DOI=10.1128/JB.00265-12; RA Xie B.B., Shu Y.L., Qin Q.L., Rong J.C., Zhang X.Y., Chen X.L., RA Shi M., He H.L., Zhou B.C., Zhang Y.Z.; RT "Genome sequences of type strains of seven species of the marine RT bacterium Pseudoalteromonas."; RL J. Bacteriol. 194:2746-2747(2012). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:ERG20367.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AHBZ02000027; ERG20367.1; -; Genomic_DNA. DR RefSeq; WP_010362795.1; NZ_AHBZ02000027.1. DR EnsemblBacteria; ERG20367; ERG20367; PCIT_02270. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000016487; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000016487}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Hydrolase {ECO:0000313|EMBL:ERG20367.1}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Protease {ECO:0000313|EMBL:ERG20367.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000016487}. FT DOMAIN 198 365 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 428 AA; 48341 MW; 76D84C6C8686EB59 CRC64; MFDRYEAGEQ AVLVHIEFPN EGDREDLHEL EMLVSSAGVS SLAVVQGSRQ SPHAKLFVGT GKAEEIAETV KIHNADVIIF NHQLSPSQER NLERICQCRV LDRTTLILDI FAQRARTHEG KLQVELAQLR HVSTRLIRGW THLERQKGGI GLRGPGETQL ETDRRLLRER IKSIRKRLDK VALVREQGRR ARTRNEVPTV SLVGYTNAGK STLFNHITDA DVYAADQLFA TLDPTLRKLH IDDIGPVILA DTVGFIRHLP HDLVAAFKAT LTETREADLQ IHVIDAADSR RKENIEEVQS VLTEIEADDI PQLLVYNKID LLDEVRPRID RNDEGMPIRV WLSAHSGAGV ELLSDAISEL LAKKIFSESL CIPPSFGRLR GALFNLSAVQ QESYDEQGNW LIDVRVPHVD WEKLKKEQGS EIESFIIK // ID U1M4B4_ASCSU Unreviewed; 496 AA. AC U1M4B4; DT 13-NOV-2013, integrated into UniProtKB/TrEMBL. DT 13-NOV-2013, sequence version 1. DT 07-JUN-2017, entry version 13. DE SubName: Full=Gtp-binding protein 6 {ECO:0000313|EMBL:ERG84019.1}; GN ORFNames=ASU_06056 {ECO:0000313|EMBL:ERG84019.1}; OS Ascaris suum (Pig roundworm) (Ascaris lumbricoides). OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Ascaridida; OC Ascaridoidea; Ascarididae; Ascaris. OX NCBI_TaxID=6253 {ECO:0000313|EMBL:ERG84019.1, ECO:0000313|Proteomes:UP000017900}; RN [1] {ECO:0000313|EMBL:ERG84019.1, ECO:0000313|Proteomes:UP000017900} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC TISSUE=Sperm {ECO:0000313|EMBL:ERG84019.1}; RX PubMed=21685128; DOI=10.1101/gr.121426.111; RA Wang J., Czech B., Crunk A., Wallace A., Mitreva M., Hannon G.J., RA Davis R.E.; RT "Deep small RNA sequencing from the nematode Ascaris reveals RT conservation, functional diversification, and novel developmental RT profiles."; RL Genome Res. 21:1462-1477(2011). RN [2] {ECO:0000313|EMBL:ERG84019.1, ECO:0000313|Proteomes:UP000017900} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC TISSUE=Sperm {ECO:0000313|EMBL:ERG84019.1}; RX PubMed=23123092; DOI=10.1016/j.devcel.2012.09.020; RA Wang J., Mitreva M., Berriman M., Thorne A., Magrini V., RA Koutsovoulos G., Kumar S., Blaxter M.L., Davis R.E.; RT "Silencing of germline-expressed genes by DNA elimination in somatic RT cells."; RL Dev. Cell 23:1072-1080(2012). CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:ERG84019.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AEUI02000173; ERG84019.1; -; Genomic_DNA. DR Proteomes; UP000017900; Unassembled WGS sequence. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR CDD; cd01878; HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000017900}; KW Reference proteome {ECO:0000313|Proteomes:UP000017900}. FT DOMAIN 266 430 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 496 AA; 55658 MW; F47C45192EE2C7AF CRC64; MDNAGSTFMS TGRGSMLSRR FLVRSRFLGK FCSLNATARE EASRSEDDYR ILADAVGVRN ASLEGHSVLV VHPRIRWGRH SAPASTTAEL QLQEAVALTN TLPNFRVCSS VVVGTDYNTK KRRIWAQGRL DTLAELKEKE RATAIMINVD VLSPLQQAEL FSFFRVPIFD RYNIVLLIFK KFAKTKEARL QVELAEIPYI RHRLKCIDVE HIDPSILHVT FPISTKGDKW EVLRLREHTL RKRIKAAVDE KLNAVNGERI QRGIAATVAL VGYTNTGKSS LIRRLTQDES IFVEDRLFAT LDSSAHFCRL PSGTPILLTD TIGFISDLPM QLFASFHATL SHVVNADLLL VVEDVSHPNV MAQREVVIET LDALSVKRSL VDSLIYVGNK CDKIDPQLCH QPDVCYISCL NGSGIKQLIA EIDKRVMALR GSVVRHLKLH SGSPALPYLY RESLLISQPI PVDGDDFLLC KVVMDDAQFA KFRARFAFTK KKSDIS // ID U1MK30_9EURY Unreviewed; 172 AA. AC U1MK30; DT 13-NOV-2013, integrated into UniProtKB/TrEMBL. DT 13-NOV-2013, sequence version 1. DT 08-JUN-2016, entry version 6. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:ERG89874.1}; GN ORFNames=J07HX5_02046 {ECO:0000313|EMBL:ERG89874.1}; OS halophilic archaeon J07HX5. OC Archaea; Euryarchaeota; Halobacteria; Halobacteriales. OX NCBI_TaxID=1325472 {ECO:0000313|EMBL:ERG89874.1, ECO:0000313|Proteomes:UP000053694}; RN [1] {ECO:0000313|EMBL:ERG89874.1, ECO:0000313|Proteomes:UP000053694} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=23637883; RA Podell S., Ugalde J.A., Narasingarao P., Banfield J.F., RA Heidelberg K.B., Allen E.E.; RT "Assembly-driven community genomics of a hypersaline microbial RT ecosystem."; RL PLoS ONE 8:E61692-E61692(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; KE356559; ERG89874.1; -; Genomic_DNA. DR Proteomes; UP000053694; Unassembled WGS sequence. DR InterPro; IPR025121; GTPase_HflX_N. DR Pfam; PF13167; GTP-bdg_N; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000053694}; KW Reference proteome {ECO:0000313|Proteomes:UP000053694}. FT DOMAIN 22 93 GTP-bdg_N. {ECO:0000259|Pfam:PF13167}. SQ SEQUENCE 172 AA; 19155 MW; 0063AC5EE72BA0D4 CRC64; MSQRAVIACR QGEQTTRTPS FRAIVTALGH RIVDEREQQR QEHNRYNLGP GLVDELSQIV DERDCGYVAV DNQLHPGQLS DLTAALAPAT VRDCRGVVYE RLANGGNRAA ANRRDAQQLR GKRRRLLADN RERRQQPRIL SVNVSDSTRS STHSGSDSAS RLQTGKQRAR GS // ID U1MM73_9MICO Unreviewed; 499 AA. AC U1MM73; DT 13-NOV-2013, integrated into UniProtKB/TrEMBL. DT 13-NOV-2013, sequence version 1. DT 07-JUN-2017, entry version 27. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=L332_00690 {ECO:0000313|EMBL:ERG62981.1}; OS Agrococcus pavilionensis RW1. OC Bacteria; Actinobacteria; Micrococcales; Microbacteriaceae; OC Agrococcus. OX NCBI_TaxID=1330458 {ECO:0000313|EMBL:ERG62981.1, ECO:0000313|Proteomes:UP000016462}; RN [1] {ECO:0000313|EMBL:ERG62981.1, ECO:0000313|Proteomes:UP000016462} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=RW1 {ECO:0000313|EMBL:ERG62981.1, RC ECO:0000313|Proteomes:UP000016462}; RX PubMed=23814108; RA White R.A.III., Grassa C.J., Suttle C.A.; RT "First draft genome sequence from a member of the genus agrococcus, RT isolated from modern microbialites."; RL Genome Announc. 1:e00391-13(2013). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:ERG62981.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ASHR01000044; ERG62981.1; -; Genomic_DNA. DR EnsemblBacteria; ERG62981; ERG62981; L332_00690. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000016462; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 2. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000016462}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000016462}. FT DOMAIN 280 445 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 499 AA; 54231 MW; 2A02C9F42DD6A9E4 CRC64; MAEAQDGTDS GRAMERILAW AEPGEGELLA ARAQALQDDD APSDRDGDQL DREERAALRR VDGLRTELED VTEVEYRQLR LENVVLVGVY SGSAEDAENS LRELAALAET AGARVLDGVL QRRPNPDPAT YVGRGKAEEL AAMVKELGAD TVVADSELSP SQRRALEDRV KVKVIDRTAV ILDIFSQHAK SREGKAQVEL AQLEYLLPRL RGWGESMSRQ AGGQVGGQGA GMGSRGPGET KIELDRRRIH SRMARLRKQI KGFAPARQAK RANRDRHEVP GVAIAGYTNA GKSSLLNRIT GAGVLVENAL FATLDATVRR AQTPDGREFT IADTVGFVRD LPHQLVEAFR STLEEVAESD VIVHVVDASH PDPASQIATV RDVLGETGAR SIPEIVVFNK ADLVSDDERL VLRGLQPDAV FASARTGEGV DELLERIAEL LPRPEVAVSL LVPFDRGDII AMLHDRFEVL REDYEADGTR VEAKVTEAAA GQLAEFVVG // ID U1NL45_9EURY Unreviewed; 433 AA. AC U1NL45; DT 13-NOV-2013, integrated into UniProtKB/TrEMBL. DT 13-NOV-2013, sequence version 1. DT 10-MAY-2017, entry version 24. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=J07HR59_01451 {ECO:0000313|EMBL:ERH04320.1}; OS Halorubrum sp. J07HR59. OC Archaea; Euryarchaeota; Halobacteria; Haloferacales; Halorubraceae; OC Halorubrum. OX NCBI_TaxID=1238428 {ECO:0000313|EMBL:ERH04320.1, ECO:0000313|Proteomes:UP000054356}; RN [1] {ECO:0000313|EMBL:ERH04320.1, ECO:0000313|Proteomes:UP000054356} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=23637883; RA Podell S., Ugalde J.A., Narasingarao P., Banfield J.F., RA Heidelberg K.B., Allen E.E.; RT "Assembly-driven community genomics of a hypersaline microbial RT ecosystem."; RL PLoS ONE 8:E61692-E61692(2013). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; KE356576; ERH04320.1; -; Genomic_DNA. DR Proteomes; UP000054356; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000054356}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000054356}. FT DOMAIN 186 369 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 102 129 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 433 AA; 47940 MW; 5FE402C0CB55946D CRC64; MDAIIAKRAD STEADLTEIR QLAAAGGYDT VGHLAQKRVE DAAFHFGEGK VDQLARRVAR RDADCVIVDN DLGPYQTFNI GGKMPSGVEV INRFTLILQI FGQRAQTRKA QLQVELAQLR YELPRAEAKA SLATRDERPG FMGLGEYDES RELDIKRQIS EIRAELESIA TKEQDRRAQR RESGFNLVAM AGYTNAGKST LLRRLAAELD IDENAGRHPD LASTAESEDM LFTTLGTTTR RAELQKREVL LTDTVGFISD LPHWLVESFE STLDSVYRAD LVLLVVDASE PVPDMREKIV TCHDTLHQRV EAPIITVFNK IDRVDADELA DKQAALSALA PNPVAVSAKA GTDITALRTR VESELPDWMD ERLVLPMTDN TMSLVSWIHD HGHVETEDYG DDSVIVGFQA TPSVVSRARS KAAELRPSSI ESA // ID U1P2A0_9EURY Unreviewed; 439 AA. AC U1P2A0; DT 13-NOV-2013, integrated into UniProtKB/TrEMBL. DT 13-NOV-2013, sequence version 1. DT 12-APR-2017, entry version 13. DE SubName: Full=GTP-binding protein HflX {ECO:0000313|EMBL:ERH04316.1}; GN ORFNames=J07HR59_01447 {ECO:0000313|EMBL:ERH04316.1}; OS Halorubrum sp. J07HR59. OC Archaea; Euryarchaeota; Halobacteria; Haloferacales; Halorubraceae; OC Halorubrum. OX NCBI_TaxID=1238428 {ECO:0000313|EMBL:ERH04316.1, ECO:0000313|Proteomes:UP000054356}; RN [1] {ECO:0000313|EMBL:ERH04316.1, ECO:0000313|Proteomes:UP000054356} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=23637883; RA Podell S., Ugalde J.A., Narasingarao P., Banfield J.F., RA Heidelberg K.B., Allen E.E.; RT "Assembly-driven community genomics of a hypersaline microbial RT ecosystem."; RL PLoS ONE 8:E61692-E61692(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; KE356576; ERH04316.1; -; Genomic_DNA. DR Proteomes; UP000054356; Unassembled WGS sequence. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000054356}; KW Reference proteome {ECO:0000313|Proteomes:UP000054356}. FT DOMAIN 184 375 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 439 AA; 47193 MW; 9C9E6692C1DBD30D CRC64; MSQTAILAAR ASDEPPDTGE IRNLAKAADY QPIGEITQRG EDDPTYSLGR GKAEALMRLA ASEEADTVIF DGGLTPGQTA SLSELMPAGT DVLDRTRLVL ELFATRAGSA AATTQAELAR LRYLKPRLTE FSARGATTEN EYHSEGAGRV QDLERQITSL EQSLSEITAD RDRRREQRRS EGFDLVALTG YTNAGKSTLL QQLADDLDTT EPAGHDDLDS SAAAADALFG TVETTTHRAT IDGRRLLLTD TVGFVEGLPH EFVQSFESTI DAARDSDAVL LVTDASDAPE RFATKLGASL AAIDHTDGRL IPVLTKTDRV TESAVAQRMT TTHERLETWA GDATKITDPV AISSRDGSGI ETLRDQLRDV LPVATESIRL PNGGDAQSLL SWAYDHCDVS DVEYGDSSLG FTVTGNPEII AEIRRRANRI QPSGGDDSA // ID U1Q3F5_9ACTO Unreviewed; 501 AA. AC U1Q3F5; DT 13-NOV-2013, integrated into UniProtKB/TrEMBL. DT 13-NOV-2013, sequence version 1. DT 07-JUN-2017, entry version 19. DE SubName: Full=GTP-binding protein HflX {ECO:0000313|EMBL:ERH17091.1}; DE Flags: Fragment; GN ORFNames=HMPREF0043_01547 {ECO:0000313|EMBL:ERH17091.1}; OS Actinobaculum sp. oral taxon 183 str. F0552. OC Bacteria; Actinobacteria; Actinomycetales; Actinomycetaceae; OC Actinobaculum. OX NCBI_TaxID=1227261 {ECO:0000313|EMBL:ERH17091.1, ECO:0000313|Proteomes:UP000016495}; RN [1] {ECO:0000313|EMBL:ERH17091.1, ECO:0000313|Proteomes:UP000016495} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=F0552 {ECO:0000313|EMBL:ERH17091.1, RC ECO:0000313|Proteomes:UP000016495}; RA Weinstock G., Sodergren E., Lobos E.A., Fulton L., Fulton R., RA Courtney L., Fronick C., O'Laughlin M., Godfrey J., Wilson R.M., RA Miner T., Farmer C., Delehaunty K., Cordes M., Minx P., Tomlinson C., RA Chen J., Wollam A., Pepin K.H., Bhonagiri V., Zhang X., Warren W., RA Mitreva M., Mardis E.R., Wilson R.K.; RL Submitted (JUN-2013) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:ERH17091.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AWSB01000045; ERH17091.1; -; Genomic_DNA. DR RefSeq; WP_021601339.1; NZ_KE951413.1. DR EnsemblBacteria; ERH17091; ERH17091; HMPREF0043_01547. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000016495; Unassembled WGS sequence. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000016495}; KW Reference proteome {ECO:0000313|Proteomes:UP000016495}. FT DOMAIN 274 440 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT NON_TER 501 501 {ECO:0000313|EMBL:ERH17091.1}. SQ SEQUENCE 501 AA; 53970 MW; 33F34370D745936B CRC64; MSDSNQPGAR GRGARNLDVR SIRGTALQAE AVYGEDWSGD SLARETRSSL QRVAGLDAGI AREEGVDVEY RRVRLERVVL IGLSGRGALA EAEESLRELA ALAETAGAVV LDGLVQRRSL PDPATYLGSG KARELAGIVE RLEADTVIAD SELAPSQRRE LEDVVGVKVI DRTALILDIF ARHATSREGK AQVELAQLEY LLPRLRGWGE SMSRQAGGRV ASGAGIGSRG PGETQLELDR RRIRTRMARL RRDIRRMEPA RRQRRAERRR TSTPSAVVVG YTNAGKSSLL NRLTGAGVLV ENALFATVDP TVRRAETPSG RAFTLTDTVG FVRRLPTQLV EAFRSTLEEA GAADLLLHVV DSSHHDPAGQ VRAVRDVLAD VPGALDAPEI VVLSKCDLAD PIGVATLRSR FPGSVPVSCL TGEGLEDLRH AIDERLPRPQ AEVRLVVPYS RGDLVSRIHD DGELLAPVDY RDEGAFVHAL VPGDVEGALR EAGLLPGDAG A // ID U1RAB3_9BIFI Unreviewed; 500 AA. AC U1RAB3; DT 13-NOV-2013, integrated into UniProtKB/TrEMBL. DT 13-NOV-2013, sequence version 1. DT 07-JUN-2017, entry version 27. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=HMPREF9244_01010 {ECO:0000313|EMBL:ERH30519.1}; OS Alloscardovia omnicolens F0580. OC Bacteria; Actinobacteria; Bifidobacteriales; Bifidobacteriaceae; OC Alloscardovia. OX NCBI_TaxID=1321816 {ECO:0000313|EMBL:ERH30519.1, ECO:0000313|Proteomes:UP000016519}; RN [1] {ECO:0000313|EMBL:ERH30519.1, ECO:0000313|Proteomes:UP000016519} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=F0580 {ECO:0000313|EMBL:ERH30519.1, RC ECO:0000313|Proteomes:UP000016519}; RA Weinstock G., Sodergren E., Wylie T., Fulton L., Fulton R., RA Fronick C., O'Laughlin M., Godfrey J., Miner T., Herter B., RA Appelbaum E., Cordes M., Lek S., Wollam A., Pepin K.H., Palsikar V.B., RA Mitreva M., Wilson R.K.; RL Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:ERH30519.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AWSI01000032; ERH30519.1; -; Genomic_DNA. DR RefSeq; WP_021618138.1; NZ_KE952645.1. DR EnsemblBacteria; ERH30519; ERH30519; HMPREF9244_01010. DR PATRIC; fig|1321816.3.peg.891; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000016519; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000016519}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000016519}. FT DOMAIN 274 440 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 500 AA; 54707 MW; 168667CED20BA3F1 CRC64; MEDKVLEPTS FLGEHSEVLL DQHRGDEAAR EVQGLSGEQI WEEREGRNKL RHVTGLGELE DITEVEYRKV RLERVVLVGV WSNRETTLAQ AEESLRELAA LARTAGADVV DGVLQHRSRP DKATYIGSGK ANEVAGIVAA TQSDTIIVDA DLPPSQRRAL EDVTKVHVVD RTAVILDIFA QHATSREGKA QVELAQMEYM LPRLRGWGGS LSRQAGGQAA GQAGGIGSRG PGETKIEMDR RVIRTRMAKL RKQIEQMAPA REVKRGSRRR FGLPSVAVVG YTNAGKSSLI NRLTGSSELV ENALFATLDT AVRGAQTAQG RNFTYVDTVG FVRKLPTQLV EAFKSTLEEV AQSNVIVHVV DASHPDPFSQ IDAVNDVLED IDSIAGMPTV IVFNKIDLID DAALERLRQL APEAFFVSAA SSDGIEELNN YVESLLPTPS VRVEAVIPYN QGQLIFQARE NGIVHEIEYR NEGTYIVCEV DNVLAAALLA AHAQHDISEL // ID U1XXP1_9BURK Unreviewed; 353 AA. AC U1XXP1; DT 13-NOV-2013, integrated into UniProtKB/TrEMBL. DT 13-NOV-2013, sequence version 1. DT 07-JUN-2017, entry version 29. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=N879_00275 {ECO:0000313|EMBL:ERI33979.1}; OS Alcaligenes sp. EGD-AK7. OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Alcaligenaceae; Alcaligenes. OX NCBI_TaxID=1386079 {ECO:0000313|EMBL:ERI33979.1, ECO:0000313|Proteomes:UP000016497}; RN [1] {ECO:0000313|EMBL:ERI33979.1, ECO:0000313|Proteomes:UP000016497} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=EGD-AK7 {ECO:0000313|EMBL:ERI33979.1}; RX PubMed=24407646; RA Sagarkar S., Bhardwaj P., Yadav T.C., Qureshi A., Khardenavis A., RA Purohit H.J., Kapley A.; RT "Draft genome sequence of atrazine-utilizing bacteria isolated from RT Indian agricultural soil."; RL Genome Announc. 2:e01149-13(2014). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:ERI33979.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AVOG02000001; ERI33979.1; -; Genomic_DNA. DR EnsemblBacteria; ERI33979; ERI33979; N879_00275. DR PATRIC; fig|1386079.3.peg.55; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000016497; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000016497}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000016497}. FT DOMAIN 181 347 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 353 AA; 39361 MW; 67C883E79E4D014A CRC64; MGELDYKAHA EEFVMLAEGA GAQIMELMVV RRSRPDSAYY IGTGKLEEAV ALAKATGAEV VLFDHALSPA QQRNLERKLE LRVVDRVALI LDIFALRAQS HEGKLQVELA QLQHLTSRLT RMWTHLERQK GGIGMRGPGE SQLEMDRRMI GDKVRTLRER LAKVQRQRST QRRARSRSGT LSVSLVGYTN TGKSTLFNAL TRADAYAADQ LFATLDTTTR RIWIEGAGQV VISDTVGFIR ELPPTLIAAF RATLEETVHA DVLLHVVDAA NPQRDEQIAE VHKVLEDIGA HEIPRILVYN KIDQAGYEPR VERDEHGTIA RVFVSALERI GLDGLRTAIV ESGHFAENNA SEQ // ID U2A3E1_9PSED Unreviewed; 433 AA. AC U2A3E1; DT 13-NOV-2013, integrated into UniProtKB/TrEMBL. DT 13-NOV-2013, sequence version 1. DT 30-AUG-2017, entry version 28. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=N878_14180 {ECO:0000313|EMBL:ERI53768.1}; OS Pseudomonas sp. EGD-AK9. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=1386078 {ECO:0000313|EMBL:ERI53768.1, ECO:0000313|Proteomes:UP000016488}; RN [1] {ECO:0000313|EMBL:ERI53768.1, ECO:0000313|Proteomes:UP000016488} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=EGD-Ak9 {ECO:0000313|Proteomes:UP000016488}; RA Kapley A., Sagarkar S., Bhardwaj P., Qureshi A., Khardenavis A., RA Purohit H.J.; RT "Indian agricultural soil isolates capable of pesticide degradation."; RL Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:ERI53768.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AVOF01000071; ERI53768.1; -; Genomic_DNA. DR RefSeq; WP_021442388.1; NZ_AVOF01000071.1. DR EnsemblBacteria; ERI53768; ERI53768; N878_14180. DR PATRIC; fig|1386078.3.peg.755; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000016488; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000016488}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000016488}. FT DOMAIN 199 366 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 165 192 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 433 AA; 48792 MW; 0A4A48274E672ABB CRC64; MFFERHEGGE RAILVHLDGQ DSEASEDPQE FQELAMSAGA DMVAFFSVPS SRLTAKYLIG SGKVEELRDQ VKAEEADLVI FNHTLTPSQE RNLERAFECR VLDRTGLILD IFAQRARTHE GKLQVELAQL DHMSTRLVRG WTHLERQKGG IGLRGPGETQ LETDRRLLRV RIRQIKQKLE KVRSQREQAR RGRRRADIPS VSLVGYTNAG KSTLFNALTA SAVYAADQLF ATLDPTLRRL ELDDLGPIVL ADTVGFIRHL PHKLVEAFRA TLEESSNSDL LLHVIDAHEP ERMAQIEQVQ AVLKEIGADE LPMLEVYNKL DLLEGVEPQI QRDADGKPLR VWLSAREGRG LELLRQAVAE LLGEDLFVGT LQLPQRLGRL RAQFFALGAV QSEGHDEQGQ SLLSVRLPRV ELNRLVSREG LEPQAFIEQH TLQ // ID U2B2E2_9CLOT Unreviewed; 432 AA. AC U2B2E2; DT 13-NOV-2013, integrated into UniProtKB/TrEMBL. DT 13-NOV-2013, sequence version 1. DT 07-JUN-2017, entry version 26. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=HMPREF1548_00688 {ECO:0000313|EMBL:ERI72294.1}; OS Clostridium sp. KLE 1755. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=1226325 {ECO:0000313|EMBL:ERI72294.1, ECO:0000313|Proteomes:UP000016509}; RN [1] {ECO:0000313|EMBL:ERI72294.1, ECO:0000313|Proteomes:UP000016509} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=KLE 1755 {ECO:0000313|EMBL:ERI72294.1, RC ECO:0000313|Proteomes:UP000016509}; RA Weinstock G., Sodergren E., Lobos E.A., Fulton L., Fulton R., RA Courtney L., Fronick C., O'Laughlin M., Godfrey J., Wilson R.M., RA Miner T., Farmer C., Delehaunty K., Cordes M., Minx P., Tomlinson C., RA Chen J., Wollam A., Pepin K.H., Bhonagiri V., Zhang X., Warren W., RA Mitreva M., Mardis E.R., Wilson R.K.; RL Submitted (JUN-2013) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:ERI72294.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AWST01000017; ERI72294.1; -; Genomic_DNA. DR EnsemblBacteria; ERI72294; ERI72294; HMPREF1548_00688. DR PATRIC; fig|1226325.3.peg.643; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000016509; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000016509}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000016509}. FT DOMAIN 206 376 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 165 199 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 432 AA; 48990 MW; 4EC61FC746B8CFB7 CRC64; MNEINNMDQT EISRVLLVGV NIDDNPDFET AMGELESLAE ACGMEVAAII EQNLSTPNPA FYIGSGKVRE VQEAVDQMDL DYVIFDETLS PSQLKNLQKE VGVPIMDRTN LILEIFSRRA KTREARLQVE SANLQYMLPR LVGMREALGR QAGASGSLSN KGTGEKQIEL DRRKIEKRIS ELRRELEAIE HDRNTQRKRR NQSALPQVAL VGYTNAGKST LMNKMVETYV GKEEKMVMAK DMLFATLDTT VRKITQNDKK DFLLSDTVGF ISKLPHGLVK AFRSTLDEVR YADLLLEVVD ASDEHYREHM QVTAETLREL GAEKIPCIYV MNKADLVMQK DELPKVDGDK IFMSALDGCG LQELLRMIKE RVFSGNREGS FLIPYEKGEI VGYFNDHATV ISQEYLAEGV RLFVSCRESD YAKYKEYLIL ED // ID U2D1T7_9FIRM Unreviewed; 594 AA. AC U2D1T7; DT 13-NOV-2013, integrated into UniProtKB/TrEMBL. DT 13-NOV-2013, sequence version 1. DT 07-JUN-2017, entry version 26. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=HMPREF1982_03768 {ECO:0000313|EMBL:ERI90730.1}; OS Clostridiales bacterium oral taxon 876 str. F0540. OC Bacteria; Firmicutes; Clostridia; Clostridiales. OX NCBI_TaxID=1321778 {ECO:0000313|EMBL:ERI90730.1, ECO:0000313|Proteomes:UP000016490}; RN [1] {ECO:0000313|EMBL:ERI90730.1, ECO:0000313|Proteomes:UP000016490} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=F0540 {ECO:0000313|EMBL:ERI90730.1, RC ECO:0000313|Proteomes:UP000016490}; RA Weinstock G., Sodergren E., Wylie T., Fulton L., Fulton R., RA Fronick C., O'Laughlin M., Godfrey J., Miner T., Herter B., RA Appelbaum E., Cordes M., Lek S., Wollam A., Pepin K.H., Palsikar V.B., RA Mitreva M., Wilson R.K.; RL Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:ERI90730.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AWSZ01000069; ERI90730.1; -; Genomic_DNA. DR RefSeq; WP_021656844.1; NZ_KE993502.1. DR EnsemblBacteria; ERI90730; ERI90730; HMPREF1982_03768. DR PATRIC; fig|1321778.3.peg.3725; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000016490; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000016490}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000016490}. FT DOMAIN 362 539 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 594 AA; 66446 MW; 3BFF5F3EED94FD78 CRC64; MIFGNIEGIR NSILNKLESL YDLNIDKQTI FSLELSSVMC DVTNQIGREV SVAIDRKGRI TNIAIGDSTT VDVPMVDIRE KKLSGIKIIH THPNGISQLS ALDISALLKL KLDCIVAIAE ENGVCNEATV GFCSIENDVL VEENIGPLPV EEAVKIDYMD KVNYLEGQLK SNNIEEDNSE RAIIVGIESD ESLDELAELA RACEVNVVHK VLQKKSKMDT AFYVGKGKLE EISMLRQALK ANLIILDDEL TGSQVRNLEE VTGAKVIDRT TLILDIFAKR ARSREAKIQV ELAQLKYRLP RLLGLGSVLS RTGGGIGTRG PGEKKLEVDR RHIRERLYDL NSELVKIKRH RETQREKRND IPKVSLVGYT NAGKSTLRNK LCDIAMPKDA AAKEKVFEAD MLFATLDITT RAIVLPDNRL ITLTDTVGFV RKLPHDLVEA FKSTLEEVVY SDLLLHVVDT SSESSLEQIE AVNIVLKELG AIDKPTLIVL NKIDKAKEDD IRKLKEKLNG MNTIEISAKE SINLDVLLEE VSKTLPYTLK KAEYLIPYSD QSAAAFLHRN AKVLEEEFKE EGTYIVAQVD DEVFNKCEKY LFNK // ID U2EIV0_9FIRM Unreviewed; 442 AA. AC U2EIV0; DT 13-NOV-2013, integrated into UniProtKB/TrEMBL. DT 13-NOV-2013, sequence version 1. DT 07-JUN-2017, entry version 26. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=HMPREF1982_00859 {ECO:0000313|EMBL:ERI94552.1}; OS Clostridiales bacterium oral taxon 876 str. F0540. OC Bacteria; Firmicutes; Clostridia; Clostridiales. OX NCBI_TaxID=1321778 {ECO:0000313|EMBL:ERI94552.1, ECO:0000313|Proteomes:UP000016490}; RN [1] {ECO:0000313|EMBL:ERI94552.1, ECO:0000313|Proteomes:UP000016490} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=F0540 {ECO:0000313|EMBL:ERI94552.1, RC ECO:0000313|Proteomes:UP000016490}; RA Weinstock G., Sodergren E., Wylie T., Fulton L., Fulton R., RA Fronick C., O'Laughlin M., Godfrey J., Miner T., Herter B., RA Appelbaum E., Cordes M., Lek S., Wollam A., Pepin K.H., Palsikar V.B., RA Mitreva M., Wilson R.K.; RL Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:ERI94552.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AWSZ01000018; ERI94552.1; -; Genomic_DNA. DR EnsemblBacteria; ERI94552; ERI94552; HMPREF1982_00859. DR PATRIC; fig|1321778.3.peg.851; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000016490; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000016490}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000016490}. FT DOMAIN 219 387 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 442 AA; 50602 MW; 31D1784F68BF6431 CRC64; MLKGVDKLPL FSRNMVMNGG SCMEYRQRAV IVGCNINNDI GFLSMMEELS GLADACDIEV VGVITQKLER VYASHYIGKG KVKEVISLIH EKHSEMVIFN DELSPAQIRN LEKDLKCKVI DRTALILEIF AKRSKTKESQ LQVEIAKLQY ILPRLTDFQE SLEHQIDGGW LTNRDSRKTK FELDRRKIRS RISALNAELE TLFATRQNQR KQRKKAGIPV IALVGYTNAG KSSIMNTMID VYGSSIGKYV FEKDMLFATL ETYVRSIKLS DNRSFLLIDT VGFISKLPNQ LVKAFRSTLE EITDADMLIH VVDRSNPDYK QHIEVVKEIL GEMGAANIPT IYAYNKADLL RDEITKEEKD CIYVSAKYKT GIDNLINEIC KRAIEQQVCC QLLIPYEKGS ILSYFRDNAN IKSTEYKTNG VFISVECKEL DYRRYKQYES LI // ID U2F6U4_CLOS4 Unreviewed; 146 AA. AC U2F6U4; DT 13-NOV-2013, integrated into UniProtKB/TrEMBL. DT 13-NOV-2013, sequence version 1. DT 07-SEP-2016, entry version 13. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:ERJ00997.1}; DE Flags: Fragment; GN ORFNames=HMPREF0262_00226 {ECO:0000313|EMBL:ERJ00997.1}; OS Clostridium sp. (strain ATCC 29733 / VPI C48-50). OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=1507 {ECO:0000313|EMBL:ERJ00997.1, ECO:0000313|Proteomes:UP000016486}; RN [1] {ECO:0000313|EMBL:ERJ00997.1, ECO:0000313|Proteomes:UP000016486} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29733 {ECO:0000313|EMBL:ERJ00997.1, RC ECO:0000313|Proteomes:UP000016486}; RA Weinstock G., Sodergren E., Wylie T., Fulton L., Fulton R., RA Fronick C., O'Laughlin M., Godfrey J., Miner T., Herter B., RA Appelbaum E., Cordes M., Lek S., Wollam A., Pepin K.H., Palsikar V.B., RA Mitreva M., Wilson R.K.; RL Submitted (JUL-2013) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:ERJ00997.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AWTA01000006; ERJ00997.1; -; Genomic_DNA. DR EnsemblBacteria; ERJ00997; ERJ00997; HMPREF0262_00226. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000016486; Unassembled WGS sequence. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000016486}; KW Reference proteome {ECO:0000313|Proteomes:UP000016486}. FT DOMAIN 24 112 GTP-bdg_N. {ECO:0000259|Pfam:PF13167}. FT DOMAIN 115 146 GTP-bdg_M. {ECO:0000259|Pfam:PF16360}. FT NON_TER 146 146 {ECO:0000313|EMBL:ERJ00997.1}. SQ SEQUENCE 146 AA; 16039 MW; 2DA1B5B4FA17196F CRC64; MYETEETRPR ALAVALDTGA YDAEASLHEL AQLADTAGIE VICTAVQKKD TPDNATFVGP GKLREIAQLC QDEEIDVLLF DDELSPMQIR NIEQVAGLAP VDRTMLILDI FARNARTREG AVQVELAQQR YRLPRLAGAG VAMSRL // ID U2FMN0_9BACT Unreviewed; 417 AA. AC U2FMN0; DT 13-NOV-2013, integrated into UniProtKB/TrEMBL. DT 13-NOV-2013, sequence version 1. DT 07-JUN-2017, entry version 29. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=HLPCO_001395 {ECO:0000313|EMBL:ERJ12409.1}; OS Haloplasma contractile SSD-17B. OC Bacteria; Haloplasmatales; Haloplasmataceae; Haloplasma. OX NCBI_TaxID=1033810 {ECO:0000313|EMBL:ERJ12409.1, ECO:0000313|Proteomes:UP000005707}; RN [1] {ECO:0000313|EMBL:ERJ12409.1, ECO:0000313|Proteomes:UP000005707} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SSD-17B {ECO:0000313|EMBL:ERJ12409.1, RC ECO:0000313|Proteomes:UP000005707}; RX PubMed=21705599; DOI=10.1128/JB.05461-11; RA Antunes A., Alam I., El Dorry H., Siam R., Robertson A., Bajic V.B., RA Stingl U.; RT "Genome sequence of Haloplasma contractile, an unusual contractile RT bacterium from a deep-sea anoxic brine lake."; RL J. Bacteriol. 193:4551-4552(2011). RN [2] {ECO:0000313|EMBL:ERJ12409.1, ECO:0000313|Proteomes:UP000005707} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SSD-17B {ECO:0000313|EMBL:ERJ12409.1, RC ECO:0000313|Proteomes:UP000005707}; RX PubMed=24324765; RA Alam I., Antunes A., Kamau A.A., Ba Alawi W., Kalkatawi M., Stingl U., RA Bajic V.B.; RT "INDIGO - INtegrated Data Warehouse of MIcrobial GenOmes with Examples RT from the Red Sea Extremophiles."; RL PLoS ONE 8:E82210-E82210(2013). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:ERJ12409.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFNU02000004; ERJ12409.1; -; Genomic_DNA. DR RefSeq; WP_008825014.1; NZ_AFNU02000004.1. DR ProteinModelPortal; U2FMN0; -. DR STRING; 1033810.HLPCO_03210; -. DR EnsemblBacteria; ERJ12409; ERJ12409; HLPCO_001395. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000005707; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0016746; F:transferase activity, transferring acyl groups; IEA:UniProtKB-KW. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Acyltransferase {ECO:0000313|EMBL:ERJ12409.1}; KW Complete proteome {ECO:0000313|Proteomes:UP000005707}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000005707}; KW Transferase {ECO:0000313|EMBL:ERJ12409.1}. FT DOMAIN 198 364 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 417 AA; 47698 MW; D7F37E0A54E5A71B CRC64; MNELERVLLV GVNSNQYSSD QEFIYTMEEL ENLAVSCELE VKDVVTQNLS QIVAATYIGS GKLIEIKQYV LSDEIDTVVF NDELTPTQLR NIQEEIPCKV IDRTTLILDI FARRAKTKEA ILQVEIAQLR YLLPRLSSLH DDFSRQEGRI GSRGPGEKKI ELSRRRIESQ IDFLNKKLKE IAEKRKIQRS LRKRNKIPVV ALVGYTNAGK STVLNSLIGY SKNEEEKLVF SHNMLFATLE TTTRKIILEN NKRFLVTDTV GFVSKLPHHL IKAFRSTLEE VIEADLILHV IDSSNSNHTK QEQVTNQVLT ELGVKDTPVV KVYNKIDQAE NDIVSSEGIH ISAKKNINID SLISLLETHL FEHYRKINML IPYTEGQVFN VLKEQATLID YSYEDNGIKV YVEADEQLLG KYNDFVI // ID U2FQ25_9BACT Unreviewed; 421 AA. AC U2FQ25; DT 13-NOV-2013, integrated into UniProtKB/TrEMBL. DT 13-NOV-2013, sequence version 1. DT 07-JUN-2017, entry version 29. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:ERJ13149.1}; GN ORFNames=HLPCO_000768 {ECO:0000313|EMBL:ERJ13149.1}; OS Haloplasma contractile SSD-17B. OC Bacteria; Haloplasmatales; Haloplasmataceae; Haloplasma. OX NCBI_TaxID=1033810 {ECO:0000313|EMBL:ERJ13149.1, ECO:0000313|Proteomes:UP000005707}; RN [1] {ECO:0000313|EMBL:ERJ13149.1, ECO:0000313|Proteomes:UP000005707} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SSD-17B {ECO:0000313|EMBL:ERJ13149.1, RC ECO:0000313|Proteomes:UP000005707}; RX PubMed=21705599; DOI=10.1128/JB.05461-11; RA Antunes A., Alam I., El Dorry H., Siam R., Robertson A., Bajic V.B., RA Stingl U.; RT "Genome sequence of Haloplasma contractile, an unusual contractile RT bacterium from a deep-sea anoxic brine lake."; RL J. Bacteriol. 193:4551-4552(2011). RN [2] {ECO:0000313|EMBL:ERJ13149.1, ECO:0000313|Proteomes:UP000005707} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SSD-17B {ECO:0000313|EMBL:ERJ13149.1, RC ECO:0000313|Proteomes:UP000005707}; RX PubMed=24324765; RA Alam I., Antunes A., Kamau A.A., Ba Alawi W., Kalkatawi M., Stingl U., RA Bajic V.B.; RT "INDIGO - INtegrated Data Warehouse of MIcrobial GenOmes with Examples RT from the Red Sea Extremophiles."; RL PLoS ONE 8:E82210-E82210(2013). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:ERJ13149.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFNU02000002; ERJ13149.1; -; Genomic_DNA. DR RefSeq; WP_008826841.1; NZ_AFNU02000002.1. DR ProteinModelPortal; U2FQ25; -. DR STRING; 1033810.HLPCO_14394; -. DR EnsemblBacteria; ERJ13149; ERJ13149; HLPCO_000768. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000005707; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0016746; F:transferase activity, transferring acyl groups; IEA:UniProtKB-KW. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Acyltransferase {ECO:0000313|EMBL:ERJ13149.1}; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000005707}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000005707}; KW Transferase {ECO:0000313|EMBL:ERJ13149.1}. FT DOMAIN 198 366 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 164 191 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 421 AA; 48625 MW; C8C0C751B7D33FBD CRC64; MNNYDQNSRV VIVGVNTNQD DFDYQMEELK NLAVANDYHV VETMTQNLYK INNKYYMGKG KLEELANLVS HIQVPIVIFN DELSPSQVRI ISEYLSCKIM DRTKLILDIF NSRAKTKEAK IQTEIALLEY RLPRLVGEGD ALDRQRGGGV HNKGAGETKL ETDRRKISQR IKSLNIELSD IKTKRETTRK RRQKSDLPII SLIGYTNAGK STIMNALLEL YHHNDNKEVF EKNMLFATLN TSIRNIKLHD NKEFLLTDTV GFIKKLPHQV VNAFRSTLEE VLHSDLILHV VDCSDPNHKE HMETTQNVLN ELGYTDVPII MVYNKVDLLE ANNSSNSSNG VYISAKYKRG FDHLVELIEE HALKTYIRCE MLIPFQDGEL VHYFNEHANV LTTSYDYNGT MLYLECKQSD YEKYRDYVVE A // ID U2FSJ2_9GAMM Unreviewed; 447 AA. AC U2FSJ2; DT 13-NOV-2013, integrated into UniProtKB/TrEMBL. DT 13-NOV-2013, sequence version 1. DT 30-AUG-2017, entry version 30. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:ERJ18984.1}; GN ORFNames=SSPSH_002066 {ECO:0000313|EMBL:ERJ18984.1}; OS Salinisphaera shabanensis E1L3A. OC Bacteria; Proteobacteria; Gammaproteobacteria; Salinisphaerales; OC Salinisphaeraceae; Salinisphaera. OX NCBI_TaxID=1033802 {ECO:0000313|EMBL:ERJ18984.1, ECO:0000313|Proteomes:UP000006242}; RN [1] {ECO:0000313|EMBL:ERJ18984.1, ECO:0000313|Proteomes:UP000006242} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=E1L3A {ECO:0000313|EMBL:ERJ18984.1, RC ECO:0000313|Proteomes:UP000006242}; RX PubMed=21705588; DOI=10.1128/JB.05459-11; RA Antunes A., Alam I., Bajic V.B., Stingl U.; RT "Genome sequence of Salinisphaera shabanensis, a gammaproteobacterium RT from the harsh, variable environment of the brine-seawater interface RT of the Shaban Deep in the Red Sea."; RL J. Bacteriol. 193:4555-4556(2011). RN [2] {ECO:0000313|EMBL:ERJ18984.1, ECO:0000313|Proteomes:UP000006242} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=E1L3A {ECO:0000313|EMBL:ERJ18984.1, RC ECO:0000313|Proteomes:UP000006242}; RX PubMed=24324765; RA Alam I., Antunes A., Kamau A.A., Ba Alawi W., Kalkatawi M., Stingl U., RA Bajic V.B.; RT "INDIGO - INtegrated Data Warehouse of MIcrobial GenOmes with Examples RT from the Red Sea Extremophiles."; RL PLoS ONE 8:E82210-E82210(2013). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:ERJ18984.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AFNV02000013; ERJ18984.1; -; Genomic_DNA. DR RefSeq; WP_006914311.1; NZ_AFNV02000013.1. DR ProteinModelPortal; U2FSJ2; -. DR STRING; 1033802.SSPSH_13607; -. DR EnsemblBacteria; ERJ18984; ERJ18984; SSPSH_002066. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000006242; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0016746; F:transferase activity, transferring acyl groups; IEA:UniProtKB-KW. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Acyltransferase {ECO:0000313|EMBL:ERJ18984.1}; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000006242}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000006242}; KW Transferase {ECO:0000313|EMBL:ERJ18984.1}. FT DOMAIN 198 365 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 157 184 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 447 AA; 49097 MW; FD14282990E9BA23 CRC64; MFERPPTGQA AVIVHLAFGL DEYDEADREF HELVTSAGGE VLAHVGGSRR TPDPRYFVGG GKVDEIAELV VEHSAELVVF NHDLSPSQER NLEKRLNARV LDRAGLILDI FASRARSHEG KLQVELAQLQ HLATRLVRGW SHLERQKGGI GLRGPGETQL ETDRRLLNER IKMLRQRLEK VSARREQGRS ARRRARTPIV SLVGYTNAGK STLFNRLTGE DIYAADQLFA TLDPTLRRMD VPVGEPLIVA DTVGFIRDLP HELVAAFKAT LEETREADVL LHVIDAADVE RRAHAREVNN VLDEIGAGEV PQIEVFNKVD LIEDESARIE TDAHGRPLRV WLSAASGEGV DDLRAVLADF CNPDMIAGVL KVPAAAGRLR SALFELGVVD DESYDDDGAS RLTVTASQSD LERIVAQAGL VFEDVLVERR AARMASSGPA SSMPTSA // ID U2HYD9_9SPHI Unreviewed; 396 AA. AC U2HYD9; DT 13-NOV-2013, integrated into UniProtKB/TrEMBL. DT 13-NOV-2013, sequence version 1. DT 07-JUN-2017, entry version 26. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=M472_03550 {ECO:0000313|EMBL:ERJ57834.1}, GN M472_16120 {ECO:0000313|EMBL:ERJ60285.1}; OS Sphingobacterium paucimobilis HER1398. OC Bacteria; Bacteroidetes; Sphingobacteriia; Sphingobacteriales; OC Sphingobacteriaceae; Sphingobacterium. OX NCBI_TaxID=1346330 {ECO:0000313|EMBL:ERJ60285.1, ECO:0000313|Proteomes:UP000016584}; RN [1] {ECO:0000313|EMBL:ERJ60285.1, ECO:0000313|Proteomes:UP000016584} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=HER1398 {ECO:0000313|EMBL:ERJ60285.1, RC ECO:0000313|Proteomes:UP000016584}; RX PubMed=23929486; RA White R.A.III., Suttle C.A.; RT "The Draft Genome Sequence of Sphingomonas paucimobilis Strain HER1398 RT (Proteobacteria), Host to the Giant PAU Phage, Indicates That It Is a RT Member of the Genus Sphingobacterium (Bacteroidetes)."; RL Genome Announc. 1:e00598-13(2013). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:ERJ60285.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ATDL01000021; ERJ57834.1; -; Genomic_DNA. DR EMBL; ATDL01000007; ERJ60285.1; -; Genomic_DNA. DR RefSeq; WP_021069425.1; NZ_ATDL01000021.1. DR EnsemblBacteria; ERJ57834; ERJ57834; M472_03550. DR EnsemblBacteria; ERJ60285; ERJ60285; M472_16120. DR PATRIC; fig|1346330.5.peg.1248; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000016584; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000016584}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000016584}. FT DOMAIN 204 385 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 396 AA; 45336 MW; 866C165436606142 CRC64; MGKTKIYDTA IKQETAVLVS VITPDISEET AQEYLEELQF LVETAGGDTR GVFTQKLAKP EHATFVGTGK LQEIKEYVEA EDIDMIVFDD ELTPSQLRNI EKELKRKILD RSSLILDIFA KHAQTAQAKT QVELAQLQYL LPRLTRMWTH LERQRGGIGM RGPGESQIET DRRIILNKIS LLKERLKVID KQNETQRKNR GEMIRVALVG YTNVGKSTIL NMISKADVLI ENKLFATLDT TVRKVVIDNL PFLLSDTVGF IRKLPHHLVE SFKSTLDEVR EADVLIHVVD ISHPDFEHHI IAVNETLKDI NALDKPTITV FNKIDMFKPA VEFDENGEEI KVTLNDFKNS WMAKNSDPAI FLSATNKTNI EEFKEKLYEV ISDLHNKRYP YNNLLY // ID U2J930_9FIRM Unreviewed; 415 AA. AC U2J930; DT 13-NOV-2013, integrated into UniProtKB/TrEMBL. DT 13-NOV-2013, sequence version 1. DT 07-JUN-2017, entry version 27. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=HMPREF1987_01348 {ECO:0000313|EMBL:ERJ82751.1}; OS Peptostreptococcaceae bacterium oral taxon 113 str. W5053. OC Bacteria; Firmicutes; Clostridia; Clostridiales; OC Peptostreptococcaceae. OX NCBI_TaxID=1321784 {ECO:0000313|EMBL:ERJ82751.1, ECO:0000313|Proteomes:UP000016618}; RN [1] {ECO:0000313|EMBL:ERJ82751.1, ECO:0000313|Proteomes:UP000016618} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=W5053 {ECO:0000313|EMBL:ERJ82751.1, RC ECO:0000313|Proteomes:UP000016618}; RA Weinstock G., Sodergren E., Wylie T., Fulton L., Fulton R., RA Fronick C., O'Laughlin M., Godfrey J., Miner T., Herter B., RA Appelbaum E., Cordes M., Lek S., Wollam A., Pepin K.H., Palsikar V.B., RA Mitreva M., Wilson R.K.; RL Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:ERJ82751.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AWVB01000065; ERJ82751.1; -; Genomic_DNA. DR RefSeq; WP_021676545.1; NZ_KI259862.1. DR EnsemblBacteria; ERJ82751; ERJ82751; HMPREF1987_01348. DR PATRIC; fig|1321784.3.peg.1278; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000016618; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000016618}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000016618}. FT DOMAIN 190 359 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 156 183 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 415 AA; 47379 MW; 4226336CFAA2FD2F CRC64; MEKVILAGLR LDDEFEYKMD ELEALTKAAG AEVLGSVGQQ KRTVDPGTFL GKGKVQEIKE LAKNMEADSV IFLQELSGSQ IRNLEKIIEK KVLDRTMLIL DIFAGRATSR EGKLQVHLAQ LNYRLPRLIG FGNALSREGG GIGTRGPGEQ KMETDRRHIM REIDHVKAKL KEMERQRDLL RERRRKNVLP LISLFGYTNS GKSTLMNGIL RLSGNEKEVF AKDMLFATLE TRLRRCEFPK GGPFLLTDTV GLVSDLPTEF VEAFSSTLEE AKDADLILHV VDCAGANILL QIETTLDLMK KLNLNKTPIL TVFNKKDLIE EENFMWMRQE GEHILISAKD EEDIRRLLNK MQKMLGNYKL SRFLFPYTCS GEVSALMEMY AMDLVEHRED GIFLSFVADE RVREKYKIYL EEVHA // ID U2KGR3_9STRE Unreviewed; 412 AA. AC U2KGR3; DT 13-NOV-2013, integrated into UniProtKB/TrEMBL. DT 13-NOV-2013, sequence version 1. DT 07-JUN-2017, entry version 27. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=HMPREF1557_01048 {ECO:0000313|EMBL:ERJ76354.1}; OS Streptococcus sobrinus W1703. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=1227275 {ECO:0000313|EMBL:ERJ76354.1, ECO:0000313|Proteomes:UP000016617}; RN [1] {ECO:0000313|EMBL:ERJ76354.1, ECO:0000313|Proteomes:UP000016617} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=W1703 {ECO:0000313|EMBL:ERJ76354.1, RC ECO:0000313|Proteomes:UP000016617}; RA Weinstock G., Sodergren E., Lobos E.A., Fulton L., Fulton R., RA Courtney L., Fronick C., O'Laughlin M., Godfrey J., Wilson R.M., RA Miner T., Farmer C., Delehaunty K., Cordes M., Minx P., Tomlinson C., RA Chen J., Wollam A., Pepin K.H., Bhonagiri V., Zhang X., Warren W., RA Mitreva M., Mardis E.R., Wilson R.K.; RL Submitted (JUN-2013) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:ERJ76354.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AWVA01000066; ERJ76354.1; -; Genomic_DNA. DR RefSeq; WP_019795470.1; NZ_KI259679.1. DR EnsemblBacteria; ERJ76354; ERJ76354; HMPREF1557_01048. DR PATRIC; fig|1227275.3.peg.927; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000016617; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000016617}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000016617}. FT DOMAIN 199 359 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 412 AA; 46814 MW; 5A013FC082E808CA CRC64; MFETAESTER VILLGVELPS SQNFDMSMLE LASLAQTAGA EVVRSYRQKR DKYDSKTFVG SGKLQEIAAM IEADQIDMVI VNNRLTPRQN SNLEQAFGVK VIDRMQLILD IFAMRARSHE GKLQVHLAQL TYMLPRLAGQ GVMLSRQAGG IGSRGPGESQ LELNRRSIRH QISDIERQLK IVEKTRSTIR DKRLESTVFK IGLIGYTNAG KSTLMNRLTD NGQYEADELF ATLDATTKQI YLKDQFQATL TDTVGFIQDL PTELVAAFKS TLEESRHVDL LLHVIDASDS NHAEQEQVVL DILQDLDMLQ IPRLAIYNKM DQTDNLLATV FPNIRISLKN PDSRQSLRRQ ILDEIEQIFL PFSIKVGPDK LYKLHDLSKF ALLDPYDYNQ ASPEVSGFIA EKNKWRLEEF YD // ID U2LGA2_9BACT Unreviewed; 414 AA. AC U2LGA2; DT 13-NOV-2013, integrated into UniProtKB/TrEMBL. DT 13-NOV-2013, sequence version 1. DT 07-JUN-2017, entry version 26. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:ERK03331.1}; GN ORFNames=HMPREF1218_1819 {ECO:0000313|EMBL:ERK03331.1}; OS Prevotella pleuritidis F0068. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Prevotellaceae; OC Prevotella. OX NCBI_TaxID=1081904 {ECO:0000313|EMBL:ERK03331.1, ECO:0000313|Proteomes:UP000016600}; RN [1] {ECO:0000313|EMBL:ERK03331.1, ECO:0000313|Proteomes:UP000016600} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=F0068 {ECO:0000313|EMBL:ERK03331.1, RC ECO:0000313|Proteomes:UP000016600}; RA Durkin A.S., Haft D.R., McCorrison J., Torralba M., Gillis M., RA Haft D.H., Methe B., Sutton G., Nelson K.E.; RL Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:ERK03331.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AWET01000011; ERK03331.1; -; Genomic_DNA. DR RefSeq; WP_021583477.1; NZ_AWET01000011.1. DR EnsemblBacteria; ERK03331; ERK03331; HMPREF1218_1819. DR PATRIC; fig|1081904.3.peg.761; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000016600; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000016600}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000016600}. FT DOMAIN 216 400 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 414 AA; 47221 MW; 5E2C9593CA18F5AE CRC64; MKEFVISEVK AETAVLVGLI TQTQDEAKTK EYLDELEFLA DTAGAVTVKR FTQKVGGPNS VTYVGTGKLE EIKQYIRDEE DAERPVGMVI FDDELSAKQI RNIEASLGVK ILDRTSLILD IFAMRAQTAN AKTQVELAQY RYMLPRLQRL WTHLERQGGG SGSGGGKGSV GLRGPGETQL EMDRRIILNR MSLLKQRLTE IDKQKATQRK NRGRMIRVAL VGYTNVGKST IMNLMAKSEV FAENKLFATL DTTVRKVVIE NLPFLLADTV GFIRKLPTDL VDSFKSTLDE VREADLLLHV VDISHPDFEE QINVVENTLK DLGCADKPSM IVFNKIDQYH WVDKEADDLT PISRENIPLD ELRRTWMARL NENCLFISAR ERVNLIEFRD TLYNKVRELH VQKYPYNDFL YNIE // ID U2N3X7_9CLOT Unreviewed; 595 AA. AC U2N3X7; DT 13-NOV-2013, integrated into UniProtKB/TrEMBL. DT 13-NOV-2013, sequence version 1. DT 07-JUN-2017, entry version 27. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=CINTURNW_1250 {ECO:0000313|EMBL:ERK30202.1}; OS Clostridium intestinale URNW. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=1294142 {ECO:0000313|EMBL:ERK30202.1, ECO:0000313|Proteomes:UP000016721}; RN [1] {ECO:0000313|EMBL:ERK30202.1, ECO:0000313|Proteomes:UP000016721} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=URNW {ECO:0000313|EMBL:ERK30202.1, RC ECO:0000313|Proteomes:UP000016721}; RX PubMed=24136853; RA Lal S., Ramachandran U., Zhang X., Sparling R., Levin D.B.; RT "Draft Genome Sequence of the Hydrogen- and Ethanol-Producing RT Bacterium Clostridium intestinale Strain URNW."; RL Genome Announc. 1:e00871-13(2013). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:ERK30202.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; APJA01000012; ERK30202.1; -; Genomic_DNA. DR RefSeq; WP_021801273.1; NZ_KI273145.1. DR EnsemblBacteria; ERK30202; ERK30202; CINTURNW_1250. DR PATRIC; fig|1294142.3.peg.1259; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000016721; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000016721}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000016721}. FT DOMAIN 364 541 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 595 AA; 66358 MW; F2982F094F4F4D3F CRC64; MIYGNIEGIK NSYLKELEEI YKLKVLKYEY CSMEIIDTIS RLTSLVEREI SVGIDRRGNI VSVAVGDSNS VELPIIDISE KKLAGVRIVH THPNGNSHLS ALDVTALLKL KLDALVAVGV VDGTPKEVSI GFCAVENDIL IVETMLGLNL NESFDFNIGE KIQNLETALK RSNVEEDLAE RAILVGTDTE ESLDELGELA KACDITVLNK VFQNRAKIDA ALFIGSGKVS EIANLKQTLR ANLIIFDEEL SGSQVRNLEE AIGTKVIDRT TLILEIFARR AKTREARIQV ELAQLKYRAS RLSGLGTILS RTGGGIGTRG PGEKKLETDR RHIKERIYDL GDELKKIKKN REVQRERRGK QSIPQVSLVG YTNAGKSTLR NTLCDMVSIG EGNKKEKVFE ANMLFATLDT TTRAINLLDN RLITLTDTVG FVRKLPHELV EAFKSTLEEV IYSDMLLHVV DAASDTAREQ IKAVEEVLAE LGARDKDGFL VLNKIDLASE EALCELRTEF SNYEIIEISA KQKINLDKLL LKIGDKLPNK LKLAEFIIPY DQGGIVSYLH NNSNVLEEDY KEEGTYIKAE VDDEAYNKYS ELILK // ID U2QFL4_9BACT Unreviewed; 416 AA. AC U2QFL4; DT 13-NOV-2013, integrated into UniProtKB/TrEMBL. DT 13-NOV-2013, sequence version 1. DT 07-JUN-2017, entry version 28. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:ERK40108.1}; GN ORFNames=HMPREF9135_0065 {ECO:0000313|EMBL:ERK40108.1}; OS Prevotella baroniae F0067. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Prevotellaceae; OC Prevotella. OX NCBI_TaxID=1115809 {ECO:0000313|EMBL:ERK40108.1, ECO:0000313|Proteomes:UP000016648}; RN [1] {ECO:0000313|EMBL:ERK40108.1, ECO:0000313|Proteomes:UP000016648} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=F0067 {ECO:0000313|EMBL:ERK40108.1, RC ECO:0000313|Proteomes:UP000016648}; RA Durkin A.S., Haft D.R., McCorrison J., Torralba M., Gillis M., RA Haft D.H., Methe B., Sutton G., Nelson K.E.; RL Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:ERK40108.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AWEY01000008; ERK40108.1; -; Genomic_DNA. DR RefSeq; WP_021589237.1; NZ_AWEY01000008.1. DR EnsemblBacteria; ERK40108; ERK40108; HMPREF9135_0065. DR PATRIC; fig|1115809.3.peg.532; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000016648; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000016648}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000016648}. FT DOMAIN 216 400 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 416 AA; 47766 MW; A4870F056EFCB6D0 CRC64; MKEFVISEAK AETAILVGLV TPGQDEAKTK EYLDELEFLA DTAGAVTRKR FTQKVNGPSQ VTYVGKGKLQ EIKQYIDDCE EADEPVGMVI FDDELSAKQI RNIENELKVK ILDRTSLILD IFAMRAQTAN AKTQVELAQY RYMLPRLQRL WTHLERQGGG SGSGGGKGSV GLRGPGETQL EMDRRIILQR ITLLKQRLVE IDKQKTTQRK NRGRLIRVAL VGYTNVGKST IMNLMAKSEV FAENKLFATL DTTVRKVVIE NLPFLLADTV GFIRKLPTDL VDSFKSTLDE VREADLLLHV VDISHPDFEE QIRVVDQTLK DLECSDKPTM IVFNKIDNYK WVEKDEDDLT PETRENIDLE QLKRTWMARL NDNCLFISAK KKENIDDFRD ILYKKVRELH VQKYPYNDFL YPQVEE // ID U2QGL7_9ACTN Unreviewed; 473 AA. AC U2QGL7; DT 13-NOV-2013, integrated into UniProtKB/TrEMBL. DT 13-NOV-2013, sequence version 1. DT 07-JUN-2017, entry version 27. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:ERK55611.1}; GN ORFNames=HMPREF0682_0827 {ECO:0000313|EMBL:ERK55611.1}; OS Propionibacterium acidifaciens F0233. OC Bacteria; Actinobacteria; Propionibacteriales; Propionibacteriaceae; OC Propionibacterium. OX NCBI_TaxID=553198 {ECO:0000313|EMBL:ERK55611.1, ECO:0000313|Proteomes:UP000017052}; RN [1] {ECO:0000313|EMBL:ERK55611.1, ECO:0000313|Proteomes:UP000017052} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=F0233 {ECO:0000313|EMBL:ERK55611.1, RC ECO:0000313|Proteomes:UP000017052}; RA Durkin A.S., Haft D.R., McCorrison J., Torralba M., Gillis M., RA Haft D.H., Methe B., Sutton G., Nelson K.E.; RL Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:ERK55611.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACVN02000180; ERK55611.1; -; Genomic_DNA. DR RefSeq; WP_021797559.1; NZ_ACVN02000180.1. DR EnsemblBacteria; ERK55611; ERK55611; HMPREF0682_0827. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000017052; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000017052}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000017052}. FT DOMAIN 247 412 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 473 AA; 51148 MW; DB83FD6D8EF0273D CRC64; MADEHLPGPA DPDGDQQDLA DRMALTRVPG MSTELQDESE VEYRSLRLER VVLISVWTTG TADDARNAMI ELKALAEAAG SQVLEGLVQR RSRPDAATYL GAGKVDELRE VVVATGADTV IADGELSPAQ LRNLEDRVGV KVVDRTALIL DIFAQHARSV EGRTQVELAQ LTYLKQRLRG WGDSLSRQVG GRAASGVGIG GRGPGETRLE TDRRRINARI AVLRRRLRGM DATRALGREG RRRRRIPSVA VVGYTNAGKS SLLNRLTGAG LLVEDALFAT LDPTTRRCRA ADGRVYTMTD TVGFVRHLPT ELVEAFRSTL EESVQADLLV HVVDGSDPDP EGQITAVREV LDGIGAGGRP ELLAVNKTDL ADPDVLARLR AEHRDAVLVS ARTGEGVDAL REAVESALPA PHERVDVLIP WDRGDLVDRI HRFGEIESDE YLADGTRLVA RVHADLAAEL AGFAVAPGGG RPE // ID U2RXE2_9FIRM Unreviewed; 423 AA. AC U2RXE2; DT 13-NOV-2013, integrated into UniProtKB/TrEMBL. DT 13-NOV-2013, sequence version 1. DT 07-JUN-2017, entry version 26. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=HMPREF1546_03747 {ECO:0000313|EMBL:ERK58218.1}; OS Oscillibacter sp. KLE 1745. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Oscillospiraceae; OC Oscillibacter. OX NCBI_TaxID=1226323 {ECO:0000313|EMBL:ERK58218.1, ECO:0000313|Proteomes:UP000016601}; RN [1] {ECO:0000313|EMBL:ERK58218.1, ECO:0000313|Proteomes:UP000016601} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=KLE 1745 {ECO:0000313|EMBL:ERK58218.1, RC ECO:0000313|Proteomes:UP000016601}; RA Weinstock G., Sodergren E., Lobos E.A., Fulton L., Fulton R., RA Courtney L., Fronick C., O'Laughlin M., Godfrey J., Wilson R.M., RA Miner T., Farmer C., Delehaunty K., Cordes M., Minx P., Tomlinson C., RA Chen J., Wollam A., Pepin K.H., Bhonagiri V., Zhang X., Warren W., RA Mitreva M., Mardis E.R., Wilson R.K.; RL Submitted (JUN-2013) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:ERK58218.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AWVO01000233; ERK58218.1; -; Genomic_DNA. DR RefSeq; WP_021748735.1; NZ_KI271749.1. DR EnsemblBacteria; ERK58218; ERK58218; HMPREF1546_03747. DR PATRIC; fig|1226323.3.peg.3218; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000016601; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000016601}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000016601}. FT DOMAIN 208 370 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 167 201 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 423 AA; 46926 MW; EAF0500ABB6F2E5C CRC64; MAETQEVRDK VVLVGLNSPV LKKEENADED TMEELSALVE TAGGETVGIV LQNRPSPDPR TFIGEGKVAE VQLYCENTGA TMVIFDNDLS PSQMRVLTEL LGVQVLDRCG LILDIFAQRA KTKEGRLQVE LAQYQYLLPR LTGMWTHLER QAGTSGKGPI GSKGPGETQL ETDRRHIRRK IDKLREDLEE VRRVRSTQRQ RRQKNEIPVV AIVGYTNAGK STLLNHLTGA GIPANNRLFD TLDTTSRLLT VSDTLDVVIS DTVGFIRKLP HQLVEAFKAT LEELEYADLL LHVIDVSNPE WQQQAAVVEN LIRELGAGEL PRIDVFNKSD RLPAGEIMPH GQDICTLSAK TGEGVDKLLE MIGERLDSGS RRCVLHIPYD KGGLLDQLYR EAKVENVEYG ETIAVTAVCT PKVLGQMAPF LVE // ID U2T1N2_LEIAQ Unreviewed; 503 AA. AC U2T1N2; DT 13-NOV-2013, integrated into UniProtKB/TrEMBL. DT 13-NOV-2013, sequence version 1. DT 07-JUN-2017, entry version 27. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=N136_02256 {ECO:0000313|EMBL:ERK71393.1}; OS Leifsonia aquatica ATCC 14665. OC Bacteria; Actinobacteria; Micrococcales; Microbacteriaceae; Leifsonia. OX NCBI_TaxID=1358026 {ECO:0000313|EMBL:ERK71393.1, ECO:0000313|Proteomes:UP000016605}; RN [1] {ECO:0000313|EMBL:ERK71393.1, ECO:0000313|Proteomes:UP000016605} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 14665 {ECO:0000313|EMBL:ERK71393.1, RC ECO:0000313|Proteomes:UP000016605}; RA Weinstock G., Sodergren E., Wylie T., Fulton L., Fulton R., RA Fronick C., O'Laughlin M., Godfrey J., Miner T., Herter B., RA Appelbaum E., Cordes M., Lek S., Wollam A., Pepin K.H., Palsikar V.B., RA Mitreva M., Wilson R.K.; RL Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:ERK71393.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AWVQ01000288; ERK71393.1; -; Genomic_DNA. DR RefSeq; WP_021762551.1; NZ_KI272163.1. DR EnsemblBacteria; ERK71393; ERK71393; N136_02256. DR PATRIC; fig|1358026.3.peg.1928; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000016605; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 2. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000016605}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000016605}. FT DOMAIN 285 450 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 503 AA; 54577 MW; B430242F2C949801 CRC64; MTERTNIEEH EADDVVARVL ATEKNRASVT LFGTGAQALQ STETTDGSHD GEQFDREERA ALRRVSGLST ELEDVTEVEY RQLRLENVVL IGVYSQGSLQ DAENSMRELA ALAETAGAVV LDGLLQRRPH PDPSTYLGRG KAEELASVVA ALGADTVVAD TELASSQRRA LEDVVKVKVI DRTAVILDIF SQHAKSREGK AQVELAQLEY LLPRLRGWGE SMSRQAGGQV GGAGAGMGSR GPGETKIELD RRRIHTRMAK LRKQIAGFKP AREAKRANRN RNSVPSVAIA GYTNAGKSSL LNRVTKAGVL VENALFATLD ATVRRSVTAD GRLYTLADTV GFVRNLPHQL VEAFRSTLEE VADSDVILHV VDGSHPDPAS QLATVRDVIG EVGARDIPEI VVFNKSDLIG PDERLVLRGL EPVAIFASAR TGEGIDEVLA AISRLLPDLS VEVELMVPYD RGDLISALHE RGRVLATEYV EEGTRVHAKI MPEYTAVFEP FAV // ID U2TK06_9ACTN Unreviewed; 440 AA. AC U2TK06; DT 13-NOV-2013, integrated into UniProtKB/TrEMBL. DT 13-NOV-2013, sequence version 1. DT 07-JUN-2017, entry version 27. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:ERL06533.1}; GN ORFNames=HMPREF1316_1303 {ECO:0000313|EMBL:ERL06533.1}; OS Olsenella profusa F0195. OC Bacteria; Actinobacteria; Coriobacteriia; Coriobacteriales; OC Atopobiaceae; Olsenella. OX NCBI_TaxID=1125712 {ECO:0000313|EMBL:ERL06533.1, ECO:0000313|Proteomes:UP000016638}; RN [1] {ECO:0000313|EMBL:ERL06533.1, ECO:0000313|Proteomes:UP000016638} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=F0195 {ECO:0000313|EMBL:ERL06533.1, RC ECO:0000313|Proteomes:UP000016638}; RA Durkin A.S., Haft D.R., McCorrison J., Torralba M., Gillis M., RA Haft D.H., Methe B., Sutton G., Nelson K.E.; RL Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:ERL06533.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AWEZ01000064; ERL06533.1; -; Genomic_DNA. DR RefSeq; WP_021726987.1; NZ_AWEZ01000064.1. DR EnsemblBacteria; ERL06533; ERL06533; HMPREF1316_1303. DR PATRIC; fig|1125712.3.peg.2069; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000016638; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000016638}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000016638}. FT DOMAIN 210 375 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 440 AA; 48356 MW; 7D6F1DAE78700E5C CRC64; MARFKPRSTA PVPERALLVG VDLGTAAWPL RDSMAELGRL AVTDGAVVVG QLTQRLRKPV SRTFIGSGKT EELVRMVRAL DVDVVIFDDE LTPSQQTSLE RIVGDSVKVI DRTALILDIF GKHATTHEGR LQVQLAQLQY VLPRLRGMWS HLVGEQARGG IGSRFGQGES QLEIDRRLVR DRISHLCREL KELDKRRRMQ SRARWDSGIY RVALVGYTNA GKSTLLNRLT GADVYARDEL FATLDPTTRS LDLKAGRRIT LTDTVGFIQK LPTNLVESFK STLAEARAAE LVLKVADASD PNCERQIDAV DAILADIGAA DIASVVVYNK CDQLDREVVH GMEALHPDAE FVSALTGTGT DGLLYRIARE AARGDVTITS LIPHDKGLLV KLVHERGQIV RERYEQGGLL VTARVPRRMA DTLEPYGVSD AGEAQGRVGA // ID U2VHI2_9ACTN Unreviewed; 438 AA. AC U2VHI2; DT 13-NOV-2013, integrated into UniProtKB/TrEMBL. DT 13-NOV-2013, sequence version 1. DT 07-JUN-2017, entry version 28. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:ERL12016.1}; GN ORFNames=HMPREF1248_0634 {ECO:0000313|EMBL:ERL12016.1}; OS Coriobacteriaceae bacterium BV3Ac1. OC Bacteria; Actinobacteria; Coriobacteriia; Coriobacteriales; OC Coriobacteriaceae. OX NCBI_TaxID=1111135 {ECO:0000313|EMBL:ERL12016.1, ECO:0000313|Proteomes:UP000016652}; RN [1] {ECO:0000313|EMBL:ERL12016.1, ECO:0000313|Proteomes:UP000016652} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BV3AC1 {ECO:0000313|Proteomes:UP000016652}; RA Durkin A.S., Haft D.R., McCorrison J., Torralba M., Gillis M., RA Haft D.H., Methe B., Sutton G., Nelson K.E.; RL Submitted (SEP-2013) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:ERL12016.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AWUP01000011; ERL12016.1; -; Genomic_DNA. DR RefSeq; WP_021735237.1; NZ_AWUP01000011.1. DR EnsemblBacteria; ERL12016; ERL12016; HMPREF1248_0634. DR PATRIC; fig|1111135.3.peg.883; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000016652; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000016652}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000016652}. FT DOMAIN 210 375 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 438 AA; 48620 MW; 969A9F3341A91FC3 CRC64; MPRFNLRSTE FVPERAIIVG VDLGKSDWPL EESLDELERL AQTDGAEVIT RVTQKLDTPI SRTFIGSGKA LELKRLVAAL DIDIVIFDDE LSPSQQSNLE RLIGEPTKVI DRTALILDIF GRHAKTREGR LQVQLAQLQY LYPRLRGMWS HLAGDSTRGG IGSRFGMGES QLEVDRRLIR ARISTLRREL KNLDQRRSIQ SKARWSSGVW SVALVGYTNA GKSTILNRLT GSEVYAKDEL FATLDPTTRS LSLEEGRKIT LTDTVGFIQK LPTTLVEAFK STLAEVVSAD LILLVVDAAD PNAKRQIIAV RQVLEQIKAD HIPTVLVYNK CDLLADDAIH TIETTEAGSV AISAQQGWGL RGLLYRIAQE AATGQSTLTA CVPYDRGALL ARIHERCQMI SERYEQSGVL VTVKADKQMA AALQPYQIEE KATDKDLL // ID U2WDJ3_9FIRM Unreviewed; 604 AA. AC U2WDJ3; DT 13-NOV-2013, integrated into UniProtKB/TrEMBL. DT 13-NOV-2013, sequence version 1. DT 07-JUN-2017, entry version 28. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=HMPREF1985_00020 {ECO:0000313|EMBL:ERL25502.1}; OS Mitsuokella sp. oral taxon 131 str. W9106. OC Bacteria; Firmicutes; Negativicutes; Selenomonadales; OC Selenomonadaceae; Mitsuokella. OX NCBI_TaxID=1321781 {ECO:0000313|EMBL:ERL25502.1, ECO:0000313|Proteomes:UP000016614}; RN [1] {ECO:0000313|EMBL:ERL25502.1, ECO:0000313|Proteomes:UP000016614} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=W9106 {ECO:0000313|EMBL:ERL25502.1, RC ECO:0000313|Proteomes:UP000016614}; RA Weinstock G., Sodergren E., Wylie T., Fulton L., Fulton R., RA Fronick C., O'Laughlin M., Godfrey J., Miner T., Herter B., RA Appelbaum E., Cordes M., Lek S., Wollam A., Pepin K.H., Palsikar V.B., RA Mitreva M., Wilson R.K.; RL Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:ERL25502.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AWVT01000001; ERL25502.1; -; Genomic_DNA. DR RefSeq; WP_021770875.1; NZ_KI273055.1. DR EnsemblBacteria; ERL25502; ERL25502; HMPREF1985_00020. DR PATRIC; fig|1321781.3.peg.19; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000016614; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000016614}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000016614}. FT DOMAIN 378 543 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 604 AA; 66396 MW; 6DE8309BED0562BB CRC64; MKIHGDLANV KASVLEAIEA LYALSVPTDQ ISTRELNEAM LAVTDLLDRE VAVYVNRAGS IVQVSIGDVG TVDLPKVKAR SASSLSGIRC IHTHPSGDTR LSSPDLSSLR RLRFDCMAAI GRDGKDIVGS MGFLTGNSEE DGKLALGQMG PVCDDVLHGV NLTWLIAIVN RRLHASRAKG TEEEVERAIL AGVAWSGNGS WSHEASMEEL ARLADTAGTI VVGQCVQRKE KPDAMLFLGK GKVSEIAMEA QDQDATLLIV DDELTPSQQR NLERTLGLKV IDRTALILDI FAQRARSSEG KMQVELAQLR YHLPRLGGQG LALSRLGGGI GTRGPGETKL EMDRRRIRSR IHDIEQQIDR LKRNRTLRRK GRKEARIPLV ALVGYTNAGK STLLNKLTNA AVMAEDKLFA TLDPTTRKLV LPSGQEILLT DTVGFIQKLP HTLVTAFRAT LEEVQEADLL LHVVDASDEN VEQQIESVVH VLTELHAENK PTLYVWNKMD CLEERTRTET FLHNRDGVCI AAEKGENLDG LIAHIEAFFR ESYVNLTLLI PYADGAAIAA LHALHAVRDT AYCEQGTRVC AHIPLSAREQ FRAYECARNE RDKG // ID U2XK14_9MICO Unreviewed; 505 AA. AC U2XK14; DT 13-NOV-2013, integrated into UniProtKB/TrEMBL. DT 13-NOV-2013, sequence version 1. DT 07-JUN-2017, entry version 27. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:GAD33510.1}; GN ORFNames=MTS1_00860 {ECO:0000313|EMBL:GAD33510.1}; OS Microbacterium sp. TS-1. OC Bacteria; Actinobacteria; Micrococcales; Microbacteriaceae; OC Microbacterium. OX NCBI_TaxID=1344956 {ECO:0000313|EMBL:GAD33510.1, ECO:0000313|Proteomes:UP000018080}; RN [1] {ECO:0000313|EMBL:GAD33510.1, ECO:0000313|Proteomes:UP000018080} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=TS-1 {ECO:0000313|EMBL:GAD33510.1, RC ECO:0000313|Proteomes:UP000018080}; RA Fujinami S., Takeda K., Onodera T., Satoh K., Sano M., Narumi I., RA Ito M.; RT "Draft Genome Sequence of Sodium-Independent Alkaliphilic RT Microbacterium sp. Strain TS-1."; RL Genome Announc. 1:e01043-13(2013). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:GAD33510.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BASQ01000001; GAD33510.1; -; Genomic_DNA. DR RefSeq; WP_023951752.1; NZ_BASQ01000001.1. DR EnsemblBacteria; GAD33510; GAD33510; MTS1_00860. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000018080; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000018080}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000018080}. FT DOMAIN 287 452 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 505 AA; 54492 MW; 46690B3CB3C20CD5 CRC64; MTHITTPDGD DDIAVDPVER VLASAETRSS IRVFGGAQAL QDEATVAYGD TDGDQWDREE RAALRRVPGL STELEDVTEV EYRQLRLENV VLVGVYPQGS QEDAENSLRE LAALAETAGA VVLDGVLQRR PHPDPATYIG RGKAAELRDL VAAVGADTVI ADTELAPSQR RALEDVAKVK VIDRTTVILD IFSQHAKSRE GKAQVELAQL EYLLPRLRGW GESMSRQAGG QVGAGGAGMG SRGPGETKIE LDRRRIRTRM AQLRKQIREF APSREAKRAE RRRNTIPSVA IAGYTNAGKS SLLNRLTSAG VLVENALFAT LDATVRRAEA ADGRVFTLTD TVGFVRNLPH QLVEAFRSTL EEVSGADVIV HVVDGSHPDP AAQLATVRDV MGDVGARATR ELVVFNKADL VDDDARLLLR GLEPTAHFVS SRTGEGIDEL RAAIEDALPL PAVEVRALVP YDRGDLISAV HESGHIVATS HEQDGTAVHA HVSERLAAEL APYAV // ID U2YA50_STRCV Unreviewed; 412 AA. AC U2YA50; DT 13-NOV-2013, integrated into UniProtKB/TrEMBL. DT 13-NOV-2013, sequence version 1. DT 05-JUL-2017, entry version 28. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=ANG5_0135 {ECO:0000313|EMBL:GAD43607.1}; OS Streptococcus constellatus subsp. pharyngis SK1060 = CCUG 46377. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus; Streptococcus anginosus group. OX NCBI_TaxID=1035184 {ECO:0000313|EMBL:GAD43607.1, ECO:0000313|Proteomes:UP000016985}; RN [1] {ECO:0000313|EMBL:GAD43607.1, ECO:0000313|Proteomes:UP000016985} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CCUG46377 {ECO:0000313|Proteomes:UP000016985}; RA Maruyama F., Sakurai A., Ogura Y., Homma H., Takahashi N., Ohtsubo Y., RA Hoshino T., Okahashi N., Nakagawa I., Kimura S., Fujiwara T., RA Hayashi T., Shintani S.; RT "Genome Sequences of seven clinical isolates and type strains of RT anginosus group streptococci."; RL Submitted (SEP-2013) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:GAD43607.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BASX01000001; GAD43607.1; -; Genomic_DNA. DR RefSeq; WP_020997725.1; NZ_BASX01000001.1. DR EnsemblBacteria; GAD43607; GAD43607; ANG5_0135. DR eggNOG; COG2262; LUCA. DR Proteomes; UP000016985; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000016985}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}. FT DOMAIN 199 359 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 158 192 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 412 AA; 46514 MW; FD3398FF5245A851 CRC64; MIETEKQQER VILIGVELQG IDNFSLSMEE LASLARTAGA QVVSSYIQKR EKYDSKTFIG AGKLEEIKHM VEADEISTVI VNNRLTPRQN INLEEILGVK VIDRMQLILD IFAMRARSHE GKLQVHLAQL KYLLPRLVGQ GIMLSRQAGG IGSRGPGESQ LELNRRSVRN QIHDIERQLK IVEKNRAIVR EKRLDSSVFK IGLIGYTNAG KSTIMNALTN KNQYEADELF ATLDATTKGA NLTGRLNVTL TDTVGFIQDL PTELISSFKS TLEESKNVDL LVHVIDASDP NHEEHEKTVL AIMKDLGMLD ILRLTLYNKA DKAGNFLPTL TPYVLISAKM ENSRAVLQEA LLDKMRELFV PFCIKVGSSK AYKLYELESL AIIDKREYVE ESEVISGYIA EKNKWRLEEF YD // ID U2YU96_9CAUL Unreviewed; 434 AA. AC U2YU96; DT 13-NOV-2013, integrated into UniProtKB/TrEMBL. DT 13-NOV-2013, sequence version 1. DT 07-JUN-2017, entry version 26. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=MBEBAB_1306 {ECO:0000313|EMBL:GAD59056.1}; OS Brevundimonas abyssalis TAR-001. OC Bacteria; Proteobacteria; Alphaproteobacteria; Caulobacterales; OC Caulobacteraceae; Brevundimonas. OX NCBI_TaxID=1391729 {ECO:0000313|EMBL:GAD59056.1, ECO:0000313|Proteomes:UP000016569}; RN [1] {ECO:0000313|EMBL:GAD59056.1, ECO:0000313|Proteomes:UP000016569} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=TAR-001 {ECO:0000313|EMBL:GAD59056.1, RC ECO:0000313|Proteomes:UP000016569}; RA Tsubouchi T., Nishi S., Usui K., Shimane Y., Takaki Y., Maruyama T., RA Hatada Y.; RT "Draft Genome Sequence of the Dimorphic Prosthecate Bacterium RT Brevundimonas abyssalis TAR-001T."; RL Genome Announc. 1:e00826-13(2013). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:GAD59056.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BATC01000017; GAD59056.1; -; Genomic_DNA. DR RefSeq; WP_021697152.1; NZ_BATC01000017.1. DR EnsemblBacteria; GAD59056; GAD59056; MBEBAB_1306. DR Proteomes; UP000016569; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000016569}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000016569}. FT DOMAIN 206 380 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 172 199 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 434 AA; 48163 MW; F0D2532AAD418F8C CRC64; MTSKFIDHAP EVQRAIVIHP DGRGTSARLA EERLEEAVGL SAALDLDVRA AEVARLRRTV PATLFGMGKV DEIAALIRAA EADVVVIDDA LTPVQQRNLE KAWEVKVIDR SGLILEIFGR RARTAEGRLQ VELARLDYER SRLVRTWTHL ERQRGGTGST GGPGETQIEL DRRMIADRID KLKAELEDVR RTRALHRKAR KRVPFPAVAL VGYTNAGKST LFNRLTGSEV LAKDLLFATL DTTQRTIRLP QGRPAIIADT VGFISDLPHE LVAAFRATLE EVGEADLILH VRDIASTDTE AQRRDVEQVL EQIPVPEGRT RRVLEVWNKI DLLSDEDREA VLGQAARQLQ EGKAVAVSAW TGEGIETLRE AIAALVDDEP ETRLTLDPGQ GEALAWLYEH GRVTFRDTDA DGRVHLVIKL PAAALGRFEQ RFGL // ID U3A003_9SPHN Unreviewed; 434 AA. AC U3A003; DT 13-NOV-2013, integrated into UniProtKB/TrEMBL. DT 13-NOV-2013, sequence version 1. DT 12-APR-2017, entry version 26. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:GAD50969.1}; GN ORFNames=NT2_13_00560 {ECO:0000313|EMBL:GAD50969.1}; OS Novosphingobium tardaugens NBRC 16725. OC Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales; OC Sphingomonadaceae; Novosphingobium. OX NCBI_TaxID=1219035 {ECO:0000313|EMBL:GAD50969.1, ECO:0000313|Proteomes:UP000016568}; RN [1] {ECO:0000313|EMBL:GAD50969.1, ECO:0000313|Proteomes:UP000016568} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NBRC 16725 {ECO:0000313|EMBL:GAD50969.1, RC ECO:0000313|Proteomes:UP000016568}; RA Isaki S., Hosoyama A., Tsuchikane K., Katsumata H., Ando Y., RA Yamazaki S., Fujita N.; RT "Whole genome shotgun sequence of Novosphingobium tardaugens NBRC RT 16725."; RL Submitted (SEP-2013) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:GAD50969.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BASZ01000013; GAD50969.1; -; Genomic_DNA. DR EnsemblBacteria; GAD50969; GAD50969; NT2_13_00560. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000016568; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000016568}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000016568}. FT DOMAIN 203 378 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 434 AA; 47816 MW; 7987A83D4631962C CRC64; MTGEVTRGAR ALVVCPDIRG RPYSVDAEAR LEEGSNLALA IGIIVAEGFV VPVRDVRPGT LFGEGQIQRI ETACEQEQAE LVIIDGALSA IQQRNLEQRL KRKVIDRTGL ILEIFGERAA TAEGRLQVEL AHLDYQQSRL VRSWTHLERQ RGGFGFLGGP GETQIEADRR MIRARMGRLR KELDQVRRTR SLHRDRRGKA PWPVIALVGY TNAGKSTLFN RLTGSDVMAE DLLFATLDPT MRAIRLPGVE KAILSDTVGF ISDLPTQLVA AFRATLEEVT GADVIVHVRD IANPASSAQK KQVLRILEDL GVIDGEGGLS SIPIVEAWNK WDLLDDEHRV ELGELARDDD MIVPLSAVTG QGVDALLETL DALLTRGAIV HRFVLPAHDG QRIAWLYAHG DVIDVQDAGE GPDGPQRQID VRLTQRELGR FSAL // ID U3B7E3_9VIBR Unreviewed; 429 AA. AC U3B7E3; DT 13-NOV-2013, integrated into UniProtKB/TrEMBL. DT 13-NOV-2013, sequence version 1. DT 30-AUG-2017, entry version 28. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:GAD81322.1}; GN ORFNames=VEZ01S_56_00070 {ECO:0000313|EMBL:GAD81322.1}; OS Vibrio ezurae NBRC 102218. OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; OC Vibrionaceae; Vibrio. OX NCBI_TaxID=1219080 {ECO:0000313|EMBL:GAD81322.1, ECO:0000313|Proteomes:UP000016562}; RN [1] {ECO:0000313|EMBL:GAD81322.1, ECO:0000313|Proteomes:UP000016562} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NBRC 102218 {ECO:0000313|EMBL:GAD81322.1, RC ECO:0000313|Proteomes:UP000016562}; RA Yoshida I., Hosoyama A., Numata M., Hashimoto M., Hosoyama Y., RA Tsuchikane K., Noguchi M., Hirakata S., Ichikawa N., Ohji S., RA Yamazoe A., Fujita N.; RT "Whole genome shotgun sequence of Vibrio ezurae NBRC 102218."; RL Submitted (SEP-2013) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:GAD81322.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BATM01000056; GAD81322.1; -; Genomic_DNA. DR RefSeq; WP_021715019.1; NZ_BATM01000056.1. DR EnsemblBacteria; GAD81322; GAD81322; VEZ01S_56_00070. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000016562; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000016562}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000016562}. FT DOMAIN 198 365 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 429 AA; 48852 MW; A0072BFC48461800 CRC64; MFDRYESGEQ AILVHINFTQ EGEWEDLAEF EMLVSSAGVN NLQTVTGSRQ APHAKYYVGE GKAQEIADLV QLLDAEIIIF NHSLSPAQER NLEQLCKCRV LDRTGLILDI FAQRARTHEG KLQVELAQLR HLSTRLIRGW THLERQKGGI GLRGPGETQL ETDRRLLRDR IKAILRRLEK VAKQREQGRR ARKRAEIPTV SLVGYTNAGK STLFNRITEA SVYAADQLFA TLDPTLRKIE LEDVGLAILA DTVGFIRHLP HDLVAAFKAT LQETQEADIL LHVIDASDER FRENTQAVDI VLEEIDAHEI PVLLVMNKID NMEQQSPRIE YNEEGIPTTV WVSAMEGLGL DLLFQALTER LASQMVEYSL SIPPLYQGRL RSVFFNMKSI RQEAYDSEGN LLIDIRMQQA DWARLQKREE AQLDDFIVS // ID U3BA65_PSEA4 Unreviewed; 433 AA. AC U3BA65; DT 13-NOV-2013, integrated into UniProtKB/TrEMBL. DT 13-NOV-2013, sequence version 1. DT 30-AUG-2017, entry version 28. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:GAD63718.1}; GN ORFNames=PA6_028_00330 {ECO:0000313|EMBL:GAD63718.1}; OS Pseudomonas alcaligenes (strain ATCC 14909 / DSM 50342 / JCM 20561 / OS NBRC 14159 / NCIMB 9945 / NCTC 10367 / 1577). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=1215092 {ECO:0000313|EMBL:GAD63718.1, ECO:0000313|Proteomes:UP000016560}; RN [1] {ECO:0000313|EMBL:GAD63718.1, ECO:0000313|Proteomes:UP000016560} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 14909 / DSM 50342 / JCM 20561 / NBRC 14159 / NCIMB 9945 / RC NCTC 10367 / 1577 {ECO:0000313|Proteomes:UP000016560}; RA Yoshida I., Hosoyama A., Tsuchikane K., Noguchi M., Hirakata S., RA Ando Y., Ohji S., Yamazoe A., Yamazaki S., Fujita N.; RT "Whole genome shotgun sequence of Pseudomonas alcaligenes NBRC RT 14159."; RL Submitted (SEP-2013) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:GAD63718.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BATI01000028; GAD63718.1; -; Genomic_DNA. DR RefSeq; WP_021701803.1; NZ_BATI01000028.1. DR EnsemblBacteria; GAD63718; GAD63718; PA6_028_00330. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000016560; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000016560}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000016560}. FT DOMAIN 199 366 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 165 192 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 433 AA; 48814 MW; 9BF32F181DDFB32F CRC64; MFFERHGGGE RAILVHLEGS NPEAAEDPQE FQDLALSAGA DMVALVTVSR HMPTAKFLIG SGKVEELRDL VRESEAELVI FNHTLTPSQE RNLERVFECR VLDRTGLILD IFAQRARTHE GKLQVELAQL DHMSTRLVRG WTHLERQKGG IGLRGPGETQ LETDRRLLRV RIRQIKQKLE KVRSQREQAR RGRRRADIPS VSLVGYTNAG KSTLFNALTT SEVYAADQLF ATLDPTLRRL ELDDLGPVVL ADTVGFIRHL PHKLVEAFRA TLEESSNSDL LLHVIDSHEP ERDQQIEQVM AVLGEIGANE LPILEVYNKI DLVDGVEPQI QRDGDGKPER VWLSARDGKG LELLRQAVAE LLGEDLFVGT LRLPQRLGRL RAQFFELNAV QSESHDEAGD TLLAIRLPRA ELNRLVSREG LKPQDFLEQH TLQ // ID U3BIG2_VIBPR Unreviewed; 429 AA. AC U3BIG2; DT 13-NOV-2013, integrated into UniProtKB/TrEMBL. DT 13-NOV-2013, sequence version 1. DT 30-AUG-2017, entry version 29. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:GAD69424.1}; GN ORFNames=VPR01S_29_00280 {ECO:0000313|EMBL:GAD69424.1}; OS Vibrio proteolyticus NBRC 13287. OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; OC Vibrionaceae; Vibrio. OX NCBI_TaxID=1219065 {ECO:0000313|EMBL:GAD69424.1, ECO:0000313|Proteomes:UP000016570}; RN [1] {ECO:0000313|EMBL:GAD69424.1, ECO:0000313|Proteomes:UP000016570} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NBRC 13287 {ECO:0000313|EMBL:GAD69424.1, RC ECO:0000313|Proteomes:UP000016570}; RA Isaki S., Hosoyama A., Numata M., Hashimoto M., Hosoyama Y., RA Tsuchikane K., Noguchi M., Hirakata S., Ichikawa N., Ohji S., RA Yamazoe A., Fujita N.; RT "Whole genome shotgun sequence of Vibrio proteolyticus NBRC 13287."; RL Submitted (SEP-2013) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:GAD69424.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BATJ01000029; GAD69424.1; -; Genomic_DNA. DR RefSeq; WP_021707389.1; NZ_BATJ01000029.1. DR EnsemblBacteria; GAD69424; GAD69424; VPR01S_29_00280. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000016570; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000016570}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000016570}. FT DOMAIN 198 365 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 429 AA; 48866 MW; 4EF45C2A94E988AB CRC64; MFDRYEAGER AVLVHINFTQ EGEWEDLSEF EMLVSSAGVS TLQVITGSRQ APHPKYYVGE GKAQEIAQAV QLAGADIVIF NHALSPAQER NLEQLCKCRV LDRTGLILDI FAQRARTHEG KLQVELAQLR HISTRLIRGW THLERQKGGI GLRGPGETQL ETDRRLLRER IKAILRRLEK VAKQREQGRR ARHRAEIPTI SLVGYTNAGK STLFNRITEA GVYAADQLFA TLDPTLRKIE LDDVGTAILA DTVGFIRHLP HDLVAAFKAT LQETQEADIL LHVVDASDDR FRENIQAVHE VLEEIDAHEV PALVVMNKID NLDDQQPRIE RDEEGVPRTV WVSAMEGRGI ELLFDALTER LASQMVQYRL QIPPQYQGRL RSTFFQMNCI QNEEYDPDGN LLIDIRMQQV DWSRLEKREG AVLRDFIVT // ID U3CFU0_9VIBR Unreviewed; 429 AA. AC U3CFU0; DT 13-NOV-2013, integrated into UniProtKB/TrEMBL. DT 13-NOV-2013, sequence version 1. DT 30-AUG-2017, entry version 28. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:GAD77163.1}; GN ORFNames=VAZ01S_063_00390 {ECO:0000313|EMBL:GAD77163.1}; OS Vibrio azureus NBRC 104587. OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; OC Vibrionaceae; Vibrio. OX NCBI_TaxID=1219077 {ECO:0000313|EMBL:GAD77163.1, ECO:0000313|Proteomes:UP000016567}; RN [1] {ECO:0000313|EMBL:GAD77163.1, ECO:0000313|Proteomes:UP000016567} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NBRC 104587 {ECO:0000313|EMBL:GAD77163.1, RC ECO:0000313|Proteomes:UP000016567}; RA Isaki S., Hosoyama A., Numata M., Hashimoto M., Hosoyama Y., RA Tsuchikane K., Noguchi M., Hirakata S., Ichikawa N., Ohji S., RA Yamazoe A., Fujita N.; RT "Whole genome shotgun sequence of Vibrio azureus NBRC 104587."; RL Submitted (SEP-2013) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:GAD77163.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BATL01000063; GAD77163.1; -; Genomic_DNA. DR RefSeq; WP_021710903.1; NZ_BATL01000063.1. DR ProteinModelPortal; U3CFU0; -. DR EnsemblBacteria; GAD77163; GAD77163; VAZ01S_063_00390. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000016567; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000016567}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000016567}. FT DOMAIN 198 365 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 429 AA; 48745 MW; 117C7E7216442328 CRC64; MFDRYESGER AVLVHINFTQ EGEWEDLAEF EMLVSSAGVE ALQVVTGSRR SPHPKYYVGE GKAQEIATAV QLAGAEIVIF NHSLSPAQER NLEALCKCRV LDRTGLILDI FAQRARTHEG KLQVELAQLR HISTRLIRGW THLERQKGGI GLRGPGETQL ETDRRLLRER IKTILRRLEK VAKQREQGRR ARNRAEIPTI SLVGYTNAGK STLFNCITEA GVYAADQLFA TLDPTLRKIE LADVGPAILA DTVGFIRHLP HDLVAAFKAT LQETQEADIL LHVVDASDER FRENIQAVHD VLEEIDAHEV PSLVVMNKID NLEQPLPRIE RDEQGIPRTV WVSAMDGIGI ELLFEALTER LASKMVEYQL RVPPEYQGRI RSTFFQMKCI QREEYDQEGN LLIDVRMQQV DWSRLEKREG AVLVDFIVT // ID U3GVB7_9CORY Unreviewed; 504 AA. AC U3GVB7; DT 13-NOV-2013, integrated into UniProtKB/TrEMBL. DT 13-NOV-2013, sequence version 1. DT 07-JUN-2017, entry version 27. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=CARG_05705 {ECO:0000313|EMBL:AGU15269.1}; OS Corynebacterium argentoratense DSM 44202. OC Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae; OC Corynebacterium. OX NCBI_TaxID=1348662 {ECO:0000313|EMBL:AGU15269.1, ECO:0000313|Proteomes:UP000016943}; RN [1] {ECO:0000313|EMBL:AGU15269.1, ECO:0000313|Proteomes:UP000016943} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 44202 {ECO:0000313|EMBL:AGU15269.1}; RX PubMed=24092787; RA Bomholt C., Glaub A., Gravermann K., Albersmeier A., Brinkrolf K., RA Ruckert C., Tauch A.; RT "Whole-Genome Sequence of the Clinical Strain Corynebacterium RT argentoratense DSM 44202, Isolated from a Human Throat Specimen."; RL Genome Announc. 1:e00793-13(2013). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP006365; AGU15269.1; -; Genomic_DNA. DR EnsemblBacteria; AGU15269; AGU15269; CARG_05705. DR KEGG; caz:CARG_05705; -. DR PATRIC; fig|1348662.3.peg.1116; -. DR KO; K03665; -. DR Proteomes; UP000016943; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000016943}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000016943}. FT DOMAIN 275 444 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 234 261 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 504 AA; 54896 MW; E7BE55FCD81F7221 CRC64; MEKPAGTTCN KTVRQWQLML EEEKTLHTAA PTDATPTVGE LDLEARSSLR RLTRGSHIHD TEQQDGYDVE YRKLRLEKVI LVGVWTTGTI SEIEANMAEL AALAETAGAD VQDMLYQKRD KPDAGTYIGS GKVQELKEIV QATGVDTVVC DGELTPSQMI ALEKALDVKV IDRTMLILDI FAQHAKSKEG KAQVSLAQME YLITRVRGWG GALSRQAGGR AGSNGGVGLR GPGETKIEAD RRRLRQDMAR LRKELAGMKT ARDIKRSKRR SSTIPQIAIA GYTNAGKSSL INAMTGAGVL VEDALFATLD PTTRRAELAD GRAVVFTDTV GFVRHLPTQL VESFRSTLEE VIEADLVLHV VDGSDPFPLK QIAAVNDVIA DIVREQGAEA PPEIVVVNKI DAADPLTLAE LRHAVDDCVF VSAHTGEGID ELEARVELFL NSLDSHVRLS IPFTRGDIVA RIHEQGTVLA ETYDGSGTVL DVRLPPSLAA ELEEFRVEQN HGND // ID U3JNF0_FICAL Unreviewed; 476 AA. AC U3JNF0; DT 13-NOV-2013, integrated into UniProtKB/TrEMBL. DT 13-NOV-2013, sequence version 1. DT 30-AUG-2017, entry version 22. DE SubName: Full=GTP binding protein 6 (putative) {ECO:0000313|Ensembl:ENSFALP00000004304}; GN Name=GTPBP6 {ECO:0000313|Ensembl:ENSFALP00000004304}; OS Ficedula albicollis (Collared flycatcher) (Muscicapa albicollis). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda; OC Coelurosauria; Aves; Neognathae; Passeriformes; Muscicapidae; OC Ficedula. OX NCBI_TaxID=59894 {ECO:0000313|Ensembl:ENSFALP00000004304, ECO:0000313|Proteomes:UP000016665}; RN [1] {ECO:0000313|Ensembl:ENSFALP00000004304} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=23103876; DOI=10.1038/nature11584; RA Ellegren H., Smeds L., Burri R., Olason P.I., Backstrom N., RA Kawakami T., Kunstner A., Makinen H., Nadachowska-Brzyska K., RA Qvarnstrom A., Uebbing S., Wolf J.B.; RT "The genomic landscape of species divergence in Ficedula RT flycatchers."; RL Nature 491:756-760(2012). RN [2] {ECO:0000313|Ensembl:ENSFALP00000004304} RP IDENTIFICATION. RG Ensembl; RL Submitted (SEP-2013) to UniProtKB. CC -!- CAUTION: The sequence shown here is derived from an Ensembl CC automatic analysis pipeline and should be considered as CC preliminary data. {ECO:0000313|Ensembl:ENSFALP00000004304}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AGTO01020369; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR Ensembl; ENSFALT00000004325; ENSFALP00000004304; ENSFALG00000004133. DR GeneTree; ENSGT00390000001397; -. DR OMA; MDTVGFM; -. DR OrthoDB; EOG091G0852; -. DR Proteomes; UP000016665; Unplaced. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR CDD; cd01878; HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 4: Predicted; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000016665}; KW Reference proteome {ECO:0000313|Proteomes:UP000016665}. FT DOMAIN 249 413 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 218 245 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 476 AA; 51854 MW; 65FAA56DECEFF09A CRC64; GGGGGGGGGG GGGGGGGGAG GGEGGEEEDE AALEELLGPS PLAPGPGAQR VAIVHPAVKW GPRKTPHTTA ELQIAEAVAL VDTLQNWTVL DKIILPTRNP SKKFVFGKGN FQVLTEKIKK LPNVTAVFLN VERISSLTKK ELEGAWGVQV FDRYTVVLHI FRCNARTKEA KLQIALAEIP LLRSNLKNEA SQRDQQRGGS RYIMGSGETF LETQSRVLKE RELKIRNALE KLRRKRALLR TQRRKCEFPM VSVMGYTNCG KTTLIKALTG EAGIQPKDQL FATLDITAHA GYLPSHMAVI YVDTIGFLTD LPHNLVESFS ATLEEVAYSD LIVHVRDITH PETILQKATV LSVLRNLNLP SHLLDSMVEV HNKVDLVERY KPAEENALAV SALHGHGLEE LKQEIEKKIL AVTGKKILTV NINLEGPQLS WLYKEATVQE VEVMPEEGTA RVKVIIGSSA FGRYKNLFPS SKISMS // ID U3U0J6_9ENTR Unreviewed; 118 AA. AC U3U0J6; DT 11-DEC-2013, integrated into UniProtKB/TrEMBL. DT 11-DEC-2013, sequence version 1. DT 02-NOV-2016, entry version 12. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:BAN97746.1}; GN ORFNames=E05_29800 {ECO:0000313|EMBL:BAN97746.1}; OS Plautia stali symbiont. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; OC Enterobacteriaceae. OX NCBI_TaxID=891974 {ECO:0000313|EMBL:BAN97746.1, ECO:0000313|Proteomes:UP000016901}; RN [1] {ECO:0000313|EMBL:BAN97746.1, ECO:0000313|Proteomes:UP000016901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=21470838; DOI=10.1016/j.micres.2011.03.001; RA Kobayashi H., Kawasaki K., Takeishi K., Noda H.; RT "Symbiont of the stink bug Plautia stali synthesizes rough-type RT lipopolysaccharide."; RL Microbiol. Res. 167:48-54(2011). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AP012551; BAN97746.1; -; Genomic_DNA. DR EnsemblBacteria; BAN97746; BAN97746; E05_29800. DR KEGG; psts:E05_29800; -. DR KO; K03665; -. DR BioCyc; PSTA891974:G13B8-3034-MONOMER; -. DR Proteomes; UP000016901; Chromosome. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF13167; GTP-bdg_N; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000016901}; KW Reference proteome {ECO:0000313|Proteomes:UP000016901}. FT DOMAIN 25 98 GTP-bdg_N. {ECO:0000259|Pfam:PF13167}. SQ SEQUENCE 118 AA; 13196 MW; 71EC90B6C1E59E9A CRC64; MFDRYDAGEQ AVLVHIWFSQ DKELEDLQKF ETLVSSAGVD ALQVITGSRK APHPKYFVGE GKAVEIADAV KASGTSAVLF DHALSPAQER NLEQAVRMSR NRSHRLNSRY FCPARPHP // ID U3U7K6_9GAMM Unreviewed; 427 AA. AC U3U7K6; DT 11-DEC-2013, integrated into UniProtKB/TrEMBL. DT 11-DEC-2013, sequence version 1. DT 30-AUG-2017, entry version 31. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:BAO00249.1}; GN ORFNames=HHS_02790 {ECO:0000313|EMBL:BAO00249.1}; OS Candidatus Pantoea carbekii. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; OC Erwiniaceae; Pantoea. OX NCBI_TaxID=1235990 {ECO:0000313|EMBL:BAO00249.1, ECO:0000313|Proteomes:UP000016900}; RN [1] {ECO:0000313|EMBL:BAO00249.1, ECO:0000313|Proteomes:UP000016900} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Kobayashi H., Fujii-Muramatsu R., Takeishi K., Noda H.; RT "Genome sequence of the symbiont of the pentatomidae stink bug RT Halyomorpha halys."; RL Submitted (OCT-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AP012554; BAO00249.1; -; Genomic_DNA. DR RefSeq; WP_022564268.1; NZ_CP010907.1. DR EnsemblBacteria; BAO00249; BAO00249; HHS_02790. DR KEGG; hhs:HHS_02790; -. DR KEGG; pck:BMSBPS_0751; -. DR PATRIC; fig|1235990.3.peg.280; -. DR KO; K03665; -. DR Proteomes; UP000016900; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000016900}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000016900}. FT DOMAIN 199 366 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 427 AA; 48708 MW; D5465B8894B01489 CRC64; MFNHFNAGEQ TILVHIWFSQ SKTPEDLEEF KTLAASACLP SSLVITGRRK APHPKYFVGE GKALEIADAV KMQKVSVVLF NHALTATQER NLERLCSCRI MDRTGLILYI FAQRARSNEG KLQVELAQLT YFMSRLVRGW THLERQKGGI GLRGGPGETQ IEIDRRLLRN RMDHILRRLE RVEKQRTQSR QVRNKADVPT LSLVGYTNSG KSSLFNALTS DNVYTADQLF ATLDPMLHRL DVANVGKVVI ADTVGFIRDL PLELIVAFKA TLKEISQSML LLHIVDSVDP RLNDKIQQVN KILAEIKADK IPMLLIMNKI DLFKNCEARI DRDERNKPIC VWLSARTGIG LPLLFQALSE HLVSEKTKYN LCLPPQLGYL RSYFYALQAI DTEWVKEDGS MILQIRIPVV EWLRLCKQEP LLNSYLI // ID U4K988_9VIBR Unreviewed; 429 AA. AC U4K988; DT 11-DEC-2013, integrated into UniProtKB/TrEMBL. DT 11-DEC-2013, sequence version 1. DT 30-AUG-2017, entry version 28. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:CCO59230.1}; GN ORFNames=VIBNI_A3217 {ECO:0000313|EMBL:CCO59230.1}; OS Vibrio nigripulchritudo. OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; OC Vibrionaceae; Vibrio. OX NCBI_TaxID=28173 {ECO:0000313|EMBL:CCO59230.1, ECO:0000313|Proteomes:UP000016895}; RN [1] {ECO:0000313|EMBL:CCO59230.1, ECO:0000313|Proteomes:UP000016895} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SnF1 {ECO:0000313|Proteomes:UP000016895}; RX PubMed=23739050; DOI=10.1038/ismej.2013.90; RA Goudenege D., Labreuche Y., Krin E., Ansquer D., Mangenot S., RA Calteau A., Medigue C., Mazel D., Polz M.F., Le Roux F.; RT "Comparative genomics of pathogenic lineages of Vibrio RT nigripulchritudo identifies virulence-associated traits."; RL ISME J. 7:1985-1996(2013). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; FO203526; CCO59230.1; -; Genomic_DNA. DR RefSeq; WP_022551733.1; NC_022528.1. DR EnsemblBacteria; CCO59230; CCO59230; VIBNI_A3217. DR GeneID; 29464019; -. DR KEGG; vni:VIBNI_A3217; -. DR PATRIC; fig|1260221.3.peg.3060; -. DR KO; K03665; -. DR Proteomes; UP000016895; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000016895}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000016895}. FT DOMAIN 198 365 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 429 AA; 48737 MW; 5CCC5673CEBB7883 CRC64; MFDRYEAGEQ AVLVHINFTQ EGEWEDLAEC EMLVTSAGVE VLQVVTGSRQ SPHPKYYVGE GKAQEIAQAV KSSGAEIVIF NHSLSPAQER NLEHLFKCRV LDRTGLILDI FAQRARTHEG KLQVELAQLR HISTRLIRGW THLERQKGGI GLRGPGETQL ETDRRLLRDR IKAILRRLEK VAKQREQGRR ARNRAEIPTI SLVGYTNAGK STLFNRITEA GVYAADQLFA TLDPTLRKIE LSDVGTAILA DTVGFIRHLP HDLVAAFKAT LQETQEADIL LHVVDASDER FRENIQAVHD VLEEIDAHEV PTLVVMNKID NMEGQQPRIE YDDEGIPQRV WVSAMEGVGI ELLFEALTQR LASQMVQYQL RIPPQYQGRF RSTFFQLKSI QQEAYDEQGN LLIDVRMQQV DWSRLEKREG AVLGDFIVT // ID U4KQC3_9MOLU Unreviewed; 422 AA. AC U4KQC3; DT 11-DEC-2013, integrated into UniProtKB/TrEMBL. DT 11-DEC-2013, sequence version 1. DT 07-JUN-2017, entry version 27. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=BN85316240 {ECO:0000313|EMBL:CCV66645.1}; OS Acholeplasma brassicae. OC Bacteria; Tenericutes; Mollicutes; Acholeplasmatales; OC Acholeplasmataceae; Acholeplasma. OX NCBI_TaxID=61635 {ECO:0000313|EMBL:CCV66645.1, ECO:0000313|Proteomes:UP000032737}; RN [1] {ECO:0000313|EMBL:CCV66645.1, ECO:0000313|Proteomes:UP000032737} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=O502 {ECO:0000313|EMBL:CCV66645.1}; RX PubMed=24158107; DOI=10.1159/000354322; RA Kube M., Siewert C., Migdoll A.M., Duduk B., Holz S., Rabus R., RA Seemuller E., Mitrovic J., Muller I., Buttner C., Reinhardt R.; RT "Analysis of the Complete Genomes of Acholeplasma brassicae , A. RT palmae and A. laidlawii and Their Comparison to the Obligate Parasites RT from ' Candidatus Phytoplasma'."; RL J. Mol. Microbiol. Biotechnol. 24:19-36(2013). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; FO681348; CCV66645.1; -; Genomic_DNA. DR RefSeq; WP_030005497.1; NC_022549.1. DR EnsemblBacteria; CCV66645; CCV66645; BN85316240. DR KEGG; abra:BN85316240; -. DR KO; K03665; -. DR Proteomes; UP000032737; Chromosome Acholeplasma brassicae. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000032737}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000032737}. FT DOMAIN 192 360 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 151 178 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 422 AA; 48178 MW; 5EDB9DE4DE371F68 CRC64; MDNALLVFLD LGLYDLAESK KELENLAIAA ELNVLDSMTQ KLDKPTSNYY IGSGKVVELK KTVDVLKIDV CVFDTELSPA QIRNLEEALD TQVIDRGFLI LQIFAKRAKT KEARLEIDLA QQKYLLPRLI GLSSSLSRQG GGSFNSKGPG EKKLELDRRR IESNITKLED QLKKVHLEKK VNQKRRQSNQ IPIVALVGYT NAGKSSTMNS LLMKLMRNEE KKVFEKNMLF ATLQTQARQI NYYNEPSFIL TDTVGFVSRL PHDLVNSFKS TLEEVKQADL ILHIIDGSNP NYQHQMTTTN DVLDSIEASH IETINVLTKL DLMINQTPIT DFKYLSISNK TKTNLDFLID EIYTRLFGQK VEVDLSFTYE EKSLINALYQ SSKIIDISYL EDEIRVKSII RESQLVTYQN QLLQKELPSN EK // ID U4KQX4_ACHPJ Unreviewed; 420 AA. AC U4KQX4; DT 11-DEC-2013, integrated into UniProtKB/TrEMBL. DT 11-DEC-2013, sequence version 1. DT 05-JUL-2017, entry version 28. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=BN85401040 {ECO:0000313|EMBL:CCV63681.1}; OS Acholeplasma palmae (strain ATCC 49389 / J233). OC Bacteria; Tenericutes; Mollicutes; Acholeplasmatales; OC Acholeplasmataceae; Acholeplasma. OX NCBI_TaxID=1318466 {ECO:0000313|EMBL:CCV63681.1, ECO:0000313|Proteomes:UP000032740}; RN [1] {ECO:0000313|EMBL:CCV63681.1, ECO:0000313|Proteomes:UP000032740} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=J233 {ECO:0000313|EMBL:CCV63681.1, RC ECO:0000313|Proteomes:UP000032740}; RX PubMed=24158107; DOI=10.1159/000354322; RA Kube M., Siewert C., Migdoll A.M., Duduk B., Holz S., Rabus R., RA Seemuller E., Mitrovic J., Muller I., Buttner C., Reinhardt R.; RT "Analysis of the Complete Genomes of Acholeplasma brassicae , A. RT palmae and A. laidlawii and Their Comparison to the Obligate Parasites RT from ' Candidatus Phytoplasma'."; RL J. Mol. Microbiol. Biotechnol. 24:19-36(2013). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; FO681347; CCV63681.1; -; Genomic_DNA. DR EnsemblBacteria; CCV63681; CCV63681; BN85401040. DR KEGG; apal:BN85401040; -. DR KO; K03665; -. DR Proteomes; UP000032740; Chromosome Acholeplasma palmae. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000032740}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000032740}. FT DOMAIN 202 295 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 420 AA; 47276 MW; 54CB381200ABB3F6 CRC64; MSYRRLIVED RAILVGLDLS IPYINEEKSL QELEGLANAV GIKVVDKIIQ NSSKVYPKYY VGSGKVLEIK KAVEILNATM VIFDDPLSPA QIKNLEAELD VQIIDRSFLI LSIFAERAKT KEAVLEVDLA QKLYLLPRLS GMGSSLSRQG GGSYNAKGPG ETKLELDRRK LLGDISRIKT ELSKIQLEKE TSRKKRLKNR IPIVALVGYT NAGKSSLMNS LSKALNNDSD EVLEKDMLFA TLDTKTKKLQ KDNYPPFLLV DTVGFVSKLP HELVNSFEST LSDILNADLL IHVVDGLNPD SYHIQTTKDV ITRLGASNIP RMLVLTKGEY RIAPPFLSED YLLISNKTGF NIDLLINNIY GEIYNDFRSY TFKIPFNKGE IINHFKTNYQ VLSLDYLEDG ILVKALLPEN EKNKLIEYLL // ID U4TTF7_9LACO Unreviewed; 434 AA. AC U4TTF7; DT 11-DEC-2013, integrated into UniProtKB/TrEMBL. DT 11-DEC-2013, sequence version 1. DT 30-AUG-2017, entry version 27. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:ERL64737.1}; GN ORFNames=L248_0656 {ECO:0000313|EMBL:ERL64737.1}; OS Lactobacillus shenzhenensis LY-73. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; OC Lactobacillus. OX NCBI_TaxID=1231336 {ECO:0000313|EMBL:ERL64737.1, ECO:0000313|Proteomes:UP000030647}; RN [1] {ECO:0000313|Proteomes:UP000030647} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=LY-73 {ECO:0000313|Proteomes:UP000030647}; RX PubMed=24265500; RA Lin Z., Liu Z., Yang R., Zou Y., Wan D., Chen J., Guo M., Zhao J., RA Fang C., Yang R., Liu F.; RT "Whole-Genome Sequencing of Lactobacillus shenzhenensis Strain LY- RT 73T."; RL Genome Announc.1:e00972-13(2013). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; KI271593; ERL64737.1; -; Genomic_DNA. DR RefSeq; WP_022529988.1; NZ_KI271593.1. DR EnsemblBacteria; ERL64737; ERL64737; L248_0656. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000030647; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000030647}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000030647}. FT DOMAIN 206 374 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 434 AA; 47884 MW; 5204F0D2FDBD1840 CRC64; MQDTTIQPIP TIIAGLDRNQ DDFDYTMTEL GELVQAAGMT VAASVTQRAD HADPATYFGK GKVEEMAAQA RAADVPLIVV NSDLTPSQTR NLEKITKLSV MDRTELILRI FSSRARTREA KLQVAIAQEE YALPRVHPSA NPLDQQGGGR GASGGGATAN RGAGETQLEL DKRVIRKRIT HMRAELKEIM RAQATRRDRR IHQALPSVAL VGYTNAGKST MMNGMLAQYG VTDKQVEVKN QLFATLDTSV RQLQLPNHRH FLLSDTVGFV SHLPHHLVES FKATLAEARD ADLLIQVVDF ADPHYRQMMA TTEETLAAIG VKDVPMLTVY NKADLRAGVN FPEREGMTMT LSAQDPASIT LLGQTLDELL YKDYVRTSLL VPFTQGEIVN YLRDNAEVVS EHYTDDGTAI TAVLSPIDRG RFARFQQAQV PSTK // ID U4UWT5_DENPD Unreviewed; 444 AA. AC U4UWT5; DT 11-DEC-2013, integrated into UniProtKB/TrEMBL. DT 11-DEC-2013, sequence version 1. DT 12-APR-2017, entry version 14. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:ERL94771.1}; GN ORFNames=D910_12045 {ECO:0000313|EMBL:ERL94771.1}; OS Dendroctonus ponderosae (Mountain pine beetle). OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; OC Pterygota; Neoptera; Holometabola; Coleoptera; Polyphaga; OC Cucujiformia; Curculionidae; Scolytinae; Dendroctonus. OX NCBI_TaxID=77166 {ECO:0000313|EMBL:ERL94771.1, ECO:0000313|Proteomes:UP000030742}; RN [1] {ECO:0000313|EMBL:ERL94771.1, ECO:0000313|Proteomes:UP000030742} RP NUCLEOTIDE SEQUENCE. RX PubMed=23537049; DOI=10.1186/gb-2013-14-3-r27; RA Keeling C.I., Yuen M.M., Liao N.Y., Roderick Docking T., Chan S.K., RA Taylor G.A., Palmquist D.L., Jackman S.D., Nguyen A., Li M., RA Henderson H., Janes J.K., Zhao Y., Pandoh P., Moore R., Sperling F.A., RA W Huber D.P., Birol I., Jones S.J., Bohlmann J.; RT "Draft genome of the mountain pine beetle, Dendroctonus ponderosae RT Hopkins, a major forest pest."; RL Genome Biol. 14:R27-R27(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; KB632399; ERL94771.1; -; Genomic_DNA. DR Proteomes; UP000030742; Unassembled WGS sequence. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR CDD; cd01878; HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000030742}; KW Reference proteome {ECO:0000313|Proteomes:UP000030742}. FT DOMAIN 220 387 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 444 AA; 50102 MW; E941E1FD9E535BBF CRC64; MNPSNIMVLS SLVTTDSGRE YNHIAEHYFH LKEAHKCLII QPYVKWGPKK LTITPEEQLG EAIALINTLP AWNVKDTVTV PMDNLERKTL FKSGTMDRIK KLVQNNSDIT AIFVNSSSIN KSTTGILQGN FNRPILDRYK VVMQILKAHA TSKHAKLQVA LAELYYVQRK SEKDLMFKTY NTEALRLMFN EREKKIKNQI NILRNQRNLL RNNRKRMEFP VVAVVGYTNA GKTSLIKSLT GEQALTPKNQ LFATLDVTAH AGQLPSGLEV LFIDTVGFIS DIPTNLIECF VATLEDALLA DVILHIEDIS SESYEYKRQH VVKTLEQLEK QVGCKNIMTK VISVGNKCDL ADGRDIKDAN VLLISADKGI GLEKLRSQLE ESVLYRTDRQ KIAISIPNGG DEIRWLYKNA TILDEIPDPK DLQSISVKAI ITKANLAKFK HAFI // ID U4V6D6_9RHOB Unreviewed; 432 AA. AC U4V6D6; DT 11-DEC-2013, integrated into UniProtKB/TrEMBL. DT 11-DEC-2013, sequence version 1. DT 07-JUN-2017, entry version 26. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=HIMB11_01565 {ECO:0000313|EMBL:ERL98251.1}; OS Rhodobacteraceae bacterium HIMB11. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae. OX NCBI_TaxID=1366046 {ECO:0000313|EMBL:ERL98251.1, ECO:0000313|Proteomes:UP000016848}; RN [1] {ECO:0000313|EMBL:ERL98251.1, ECO:0000313|Proteomes:UP000016848} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=HIMB11 {ECO:0000313|EMBL:ERL98251.1, RC ECO:0000313|Proteomes:UP000016848}; RA Durham B.P., DeLong E.F., Rappe M.S.; RT "Draft genome sequence of marine alphaproteobacterial strain HIMB11, RT the first cultivated representative of a unique lineage within the RT Roseobacter clade possessing a remarkably small genome."; RL Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:ERL98251.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AVDB01000004; ERL98251.1; -; Genomic_DNA. DR RefSeq; WP_022572655.1; NZ_AVDB01000004.1. DR EnsemblBacteria; ERL98251; ERL98251; HIMB11_01565. DR PATRIC; fig|1366046.3.peg.1592; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000016848; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000016848}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Hydrolase {ECO:0000313|EMBL:ERL98251.1}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000016848}. FT DOMAIN 204 373 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 432 AA; 48313 MW; 740356BBDF1B3A3E CRC64; MKSHDVTPTR AWVLHPDIKS DHDRRPGEPA LEEAVSLAAA LPNLEVAGAT LVPLPKPQPG KLFGKGKLEE LKTLFHDHEV ELVLIDGPVT PVQQRNLEKE WKVKILDRTG LILEIFSDRA ATREGVLQVE MAHLTYQRTR LVRAWTHLER QRGGLGFVGG PGETQIEADR RAIDEQLVRL RRQLDKVVKT RSLHRAARAK VPFPIVALVG YTNAGKSTLF NRLTGAEVMA KDMLFATLDP TMRSIKLSSG VYIILSDTVG FISDLPTELV AAFRATLEEV LEADIILHVR DISHPATEEQ AEDVEKILES LGISEDTPQL EVWNKVDLID ADDRKALGKI AKRNDNILTI SAITGQGLDE LVNRVSTHLT RDIIEGEIHL PYADGRARAW LFEQGVVERE TQREDGSLFH LRWNAKQKAQ FEKSFGISHS AE // ID U5C3F8_9BACT Unreviewed; 421 AA. AC U5C3F8; DT 11-DEC-2013, integrated into UniProtKB/TrEMBL. DT 11-DEC-2013, sequence version 1. DT 07-JUN-2017, entry version 27. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=P872_03440 {ECO:0000313|EMBL:ERM83446.1}; OS Rhodonellum psychrophilum GCM71 = DSM 17998. OC Bacteria; Bacteroidetes; Cytophagia; Cytophagales; Cytophagaceae; OC Rhodonellum. OX NCBI_TaxID=1123057 {ECO:0000313|EMBL:ERM83446.1, ECO:0000313|Proteomes:UP000016843}; RN [1] {ECO:0000313|EMBL:ERM83446.1, ECO:0000313|Proteomes:UP000016843} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=GCM71 {ECO:0000313|EMBL:ERM83446.1, RC ECO:0000313|Proteomes:UP000016843}; RX PubMed=24309741; RA Hauptmann A.L., Glaring M.A., Hallin P.F., Prieme A., Stougaard P.; RT "Draft Genome Sequence of the Psychrophilic and Alkaliphilic RT Rhodonellum psychrophilum Strain GCM71T."; RL Genome Announc. 1:e01014-13(2013). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:ERM83446.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AWXR01000013; ERM83446.1; -; Genomic_DNA. DR RefSeq; WP_019595960.1; NZ_KB906673.1. DR EnsemblBacteria; ERM83446; ERM83446; P872_03440. DR PATRIC; fig|1123057.7.peg.1613; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000016843; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000016843}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000016843}. FT DOMAIN 210 399 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 421 AA; 48230 MW; 7D115B01A5058C5E CRC64; MTKYSKKLQK LHDTAPQPET AVLVALLRQG QSDQKAKEYL EELAFLTETL GAKSVYTFTQ RMERPDVKTF VGSGKLEEIK NYVTHFEVNM VVFDDDLSPS QMRNLENELK VKVYDRSLLI LDIFLNRAQS AQAKTQVELA RFQYLLPRLT NMWTHLERQR GGTGTRGGAG EKEIETDKRD IRSKITLLKA KLEEIEKQGA TQRKGRKGVV RVTLVGYTNV GKSTLMNLIT KSNILAENKL FATVDSTVRK VVLNNIPFLL SDTVGFIRKL PTHLIESFKS TLDEIREAEL LVHVVDISHP NFEDHITVVN QTLDEIGAGE KPMILVFNKV DLVKKMPTEV ERQNMSDFEF EEANFLDLEK LSEAYAKKTG IEPVFMAAHD GTNVELFREV LIKEVKKQHM KMYPHYLEDE VIDMSQFKDM E // ID U5DR36_9CHRO Unreviewed; 548 AA. AC U5DR36; DT 11-DEC-2013, integrated into UniProtKB/TrEMBL. DT 11-DEC-2013, sequence version 1. DT 07-JUN-2017, entry version 28. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=KR51_00012320 {ECO:0000313|EMBL:ERN42140.1}; OS Rubidibacter lacunae KORDI 51-2. OC Bacteria; Cyanobacteria; Oscillatoriophycideae; Chroococcales; OC Aphanothecaceae; Rubidibacter. OX NCBI_TaxID=582515 {ECO:0000313|EMBL:ERN42140.1, ECO:0000313|Proteomes:UP000016960}; RN [1] {ECO:0000313|EMBL:ERN42140.1, ECO:0000313|Proteomes:UP000016960} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=KORDI 51-2 {ECO:0000313|EMBL:ERN42140.1, RC ECO:0000313|Proteomes:UP000016960}; RA Choi D.H., Noh J.H., Kwon K.-K., Lee J.-H., Ryu J.-Y.; RT "Draft genome sequence of Rubidibacter lacunae KORDI 51-2."; RL Submitted (MAY-2013) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:ERN42140.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ASSJ01000031; ERN42140.1; -; Genomic_DNA. DR EnsemblBacteria; ERN42140; ERN42140; KR51_00012320. DR PATRIC; fig|582515.4.peg.1384; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000016960; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000016960}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000016960}. FT DOMAIN 375 545 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 334 371 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 548 AA; 59574 MW; E3D2C742D9C28D23 CRC64; MVTVEFAQRL GAIATEVGQA VCAYINRRGH PIRIGVGTPR QTQIPLLELP RYGAERLSGI RCITATPHAR PPQEASLTAL IVQRLDALAI LTLSGKGFQR RGGGATGYVA GAYLAHLLPD SAILASDAED AENGHTPASS HWSVSPLQSL DALTKQDFLA LVEGLEAEFR REFVARQVDA TRDRVLVVGL QTDNVDRQTF EDGLTEVTRL VDTAGGEVLA TLEQKRPRAH PQTAIGAGKV QELAVAVQTL GANLVVCDRD LTPAQARNLE TRVGVRAIDR TELILDIFAQ RAQSRAGKLQ VELAQLEYLL PRLTGRGRAM SRLGGGIGTR GPGETKLETE RRAIQRRMSR LQNEVDKLQA HRSRMRQQRQ RQDVPAVAIV GYTNAGKSTL LNTLTNANIY AADRLFATLD PTTRRLSVPA PETEDPDALL LTDTVGFIRQ LPPALMDAFR ATLEEVTESD AILHLVDLSH PAWESQIASV TSLLAEMPIS PGPMLVAFNK IDRADSAALA RAREQFPEAA FLSAQERLGL ESLRVKLGQL VRYAVAVA // ID U5EAN0_NOCAS Unreviewed; 516 AA. AC U5EAN0; DT 11-DEC-2013, integrated into UniProtKB/TrEMBL. DT 11-DEC-2013, sequence version 1. DT 07-JUN-2017, entry version 29. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:GAD84425.1}; GN ORFNames=NCAST_24_00310 {ECO:0000313|EMBL:GAD84425.1}; OS Nocardia asteroides NBRC 15531. OC Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae; Nocardia. OX NCBI_TaxID=1110697 {ECO:0000313|EMBL:GAD84425.1, ECO:0000313|Proteomes:UP000017048}; RN [1] {ECO:0000313|EMBL:GAD84425.1, ECO:0000313|Proteomes:UP000017048} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NBRC 15531 {ECO:0000313|EMBL:GAD84425.1, RC ECO:0000313|Proteomes:UP000017048}; RX PubMed=24884595; DOI=10.1186/1471-2164-15-323; RA Komaki H., Ichikawa N., Hosoyama A., Takahashi-Nakaguchi A., RA Matsuzawa T., Suzuki K., Fujita N., Gonoi T.; RT "Genome based analysis of type-I polyketide synthase and nonribosomal RT peptide synthetase gene clusters in seven strains of five RT representative Nocardia species."; RL BMC Genomics 15:323-323(2014). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:GAD84425.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BAFO02000024; GAD84425.1; -; Genomic_DNA. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000017048; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 2. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000017048}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000017048}. FT DOMAIN 285 454 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 244 278 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 516 AA; 55539 MW; 2546241AEE3B866D CRC64; MTKPENPTEP TSAEHTTAAE PDVAADRGDV DDALARHAAR MQRPGWSPEP TVGEMQLDER SSLRRVAGLS TELTDITEVE YRQLRLERVV LVGVWTTGSA AQAENSMVEL AALAETAGSE VLEGLIQRRD KPDPATYIGS GKAEELRTVV LETGADTVIC DGELTPAQLT ALEKVVKVKV IDRTALILDI FAQHATSREG KAQVALAQME YMLPRLRGWG ESMSRQAGGR AGSNGGVGLR GPGETKIETD RRRIRERMAK LRREIREMKT ARDTMRARRT GSGVPAVAIV GYTNAGKSSL MNALTGAGLL VQDALFATLD PTTRRAALDD GREMVFTDTV GFVRHLPTQL VEAFRSTLEE VTGADLLLHV VDGSDPLPLE QIKAVREVIT DVIKEQGTTA PPELLVVNKI DAADPNELTR LRGLLPDAAF VSAHTGAGVE ELRERLSEVL GGLDVDISVL LPYSRGDLLA RIHADGRIIS SDHEEGGTRV RARVPHALAA ALSEFAHAGP AEAVPS // ID U5L806_9BACI Unreviewed; 418 AA. AC U5L806; DT 22-JAN-2014, integrated into UniProtKB/TrEMBL. DT 22-JAN-2014, sequence version 1. DT 07-JUN-2017, entry version 27. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=N288_10265 {ECO:0000313|EMBL:AGX03969.1}; OS Bacillus infantis NRRL B-14911. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus. OX NCBI_TaxID=1367477 {ECO:0000313|EMBL:AGX03969.1, ECO:0000313|Proteomes:UP000017805}; RN [1] {ECO:0000313|EMBL:AGX03969.1, ECO:0000313|Proteomes:UP000017805} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NRRL B-14911 {ECO:0000313|EMBL:AGX03969.1, RC ECO:0000313|Proteomes:UP000017805}; RA Massilamany C., Smith T.P.L., Loy J.D., Barletta R., Reddy J.; RT "Complete genome sequence of Bacillus infantis NRRL B-14911 that has RT potential to induce cardiac disease by antigenic mimicry."; RL Submitted (JUL-2013) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP006643; AGX03969.1; -; Genomic_DNA. DR RefSeq; WP_022543743.1; NC_022524.1. DR EnsemblBacteria; AGX03969; AGX03969; N288_10265. DR KEGG; bif:N288_10265; -. DR PATRIC; fig|1367477.3.peg.1993; -. DR KO; K03665; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000017805; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000017805}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000017805}. FT DOMAIN 199 361 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 418 AA; 47521 MW; 9DE88D236EF2D4EC CRC64; MENKTKFERV ILVGCQTGED DRHFQYSMEE LASLTETANG KVLAELSQKR ERIHPSTYIG KGKVEELKML EEELGADLII FNDELSPSQV RNVSNEVNSR VIDRTQLILD IFAQRARSKE GKLQVELAQL QYLLPRLGGQ GIQLSRLGAG IGTRGPGETK LESDRRHIRR KIDDIKSQLS VIVQHRDRYR ERRKKNKAFQ IALVGYTNAG KSTLFNRLAE AESFEENQLF ATLDPMTRKL ILPSGYLALA TDTVGFIQDL PTTLVAAFRS TLEEVSEADL LLHVIDSSNP DYFQHEKTVN KLLEDLDIQH IPQLAVYNKS DQVHPDFVPS AKTESVVISA FADQDRSMLK RKIEELVLGM MKPYQVEIPS TEGRLLSQLK NETILRELSF QEETEVYLCK GYALEDHQIT GELNKYTV // ID U5MR40_CLOSA Unreviewed; 594 AA. AC U5MR40; DT 22-JAN-2014, integrated into UniProtKB/TrEMBL. DT 22-JAN-2014, sequence version 1. DT 07-JUN-2017, entry version 32. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:AGX42146.1}; GN ORFNames=CLSA_c11400 {ECO:0000313|EMBL:AGX42146.1}; OS Clostridium saccharobutylicum DSM 13864. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=1345695 {ECO:0000313|EMBL:AGX42146.1, ECO:0000313|Proteomes:UP000017118}; RN [1] {ECO:0000313|EMBL:AGX42146.1, ECO:0000313|Proteomes:UP000017118} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 13864 {ECO:0000313|EMBL:AGX42146.1}; RX PubMed=24285650; RA Poehlein A., Hartwich K., Krabben P., Ehrenreich A., Liebl W., RA Durre P., Gottschalk G., Daniel R.; RT "Complete Genome Sequence of the Solvent Producer Clostridium RT saccharobutylicum NCP262 (DSM 13864)."; RL Genome Announc. 1:e00997-13(2013). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP006721; AGX42146.1; -; Genomic_DNA. DR RefSeq; WP_022744428.1; NZ_AYXL01000301.1. DR EnsemblBacteria; AGX42146; AGX42146; CLSA_c11400. DR KEGG; csb:CLSA_c11400; -. DR PATRIC; fig|1345695.10.peg.3370; -. DR KO; K03665; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000017118; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000017118}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000017118}. FT DOMAIN 364 541 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 594 AA; 66992 MW; 971BF3E6F7AB1FAD CRC64; MIDGNVEGIR KSIIDELESI YSIRSSKDEI CNVEILDIIS RISSFIEREV SVAINRKGNV TSIAIGDSTS VEVPIIDIEE KRLSGVRVIH THPNGYCNLS ALDLTALLKL KLDAIVSVAI IEGKIVDFSL GMLTVYNDKL ESEERKNLSL EQMQSINILD KIKFIENLIK NNDVIEETEE KAILVGSDTK ESLEELRELT EACNIPVLKT IFQSRNKIDA AFFIGRGKVL EIASMRQIER ANVIIFDDEL SGSQVRNLES ALGAKVIDRT TLILEIFATR AKTKEAKIQV ELAQLKYRLS RLQGLGTILS RTGGGIGTRG PGEKKLETDR RHIMETIYDL KSELKKIKKT REVQREKRSK ENIPKVSLVG YTNAGKSTLR NALCDLAAKK ENKTKEKVFE ADMLFATLDT TTRAITLKNK GVITLTDTVG FVRKLPHDLV EAFKSTLEEV IYSDLLCHVI DTSSDYAVEQ YIAVNEVLTE LGAIDKETIL VFNKIDKATE EQIAKIKEAV NDNVIIEVSA KEGTNLEELL ELVEEKLPYN YRKAEYLIPY EKSDVQSFLH RNGRVIEEEY RDNGTFMMVE VDDEVYNKTQ DYVI // ID U5NCW1_9BURK Unreviewed; 376 AA. AC U5NCW1; DT 22-JAN-2014, integrated into UniProtKB/TrEMBL. DT 22-JAN-2014, sequence version 1. DT 05-JUL-2017, entry version 29. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:AGX88078.1}; GN ORFNames=Cenrod_2005 {ECO:0000313|EMBL:AGX88078.1}; OS Candidatus Symbiobacter mobilis CR. OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Comamonadaceae. OX NCBI_TaxID=946483 {ECO:0000313|EMBL:AGX88078.1, ECO:0000313|Proteomes:UP000017184}; RN [1] {ECO:0000313|EMBL:AGX88078.1, ECO:0000313|Proteomes:UP000017184} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CR {ECO:0000313|EMBL:AGX88078.1}; RX PubMed=24267588; DOI=10.1186/gb-2013-14-11-r127; RA Liu Z., Muller J., Li T., Alvey R.M., Vogl K., Frigaard N.U., RA Rockwell N.C., Boyd E.S., Tomsho L.P., Schuster S.C., Henke P., RA Rohde M., Overmann J., Bryant D.A.; RT "Genomic analysis reveals key aspects of prokaryotic symbiosis in the RT phototrophic consortium "Chlorochromatium aggregatum"."; RL Genome Biol. 14:R127-R127(2013). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP004885; AGX88078.1; -; Genomic_DNA. DR EnsemblBacteria; AGX88078; AGX88078; Cenrod_2005. DR KEGG; cbx:Cenrod_2005; -. DR PATRIC; fig|946483.4.peg.2020; -. DR KO; K03665; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000017184; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000017184}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000017184}. FT DOMAIN 194 369 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 376 AA; 41384 MW; B3FC47E0E1AA2FBA CRC64; MLVGVDLASS GSSGSLLFDP ALEELGLLAQ SAGMEPVARV ACRRKAPDPS LFIGSGKADE IRDLARDCGA LEVLFDQNLS PAQQRNLERH LGLPVNDRTF LILGIFAQRA RSHEGKLQVE LARLQYLSTR LVRRWSHLER QSGGIGMRGG PGESQIELDR RMIADGIRRI QSRLSRVKRQ RATQRRQRQR HGMLCVSLVG YTNAGKSTLF NALVKAGAFA ADQLFATLDT TTRKLYLGCA QPPQPILLSD TVGFIRDLPH GLVDAFEATL QEAVDADLLL HIVDYSDPHH IERIAQVQTV LEEIGAGDIP QVLVFNKVDA VGPERRPGVL RDTYEWGGSW VPRTFVSAHS GEGLPGLRQV LCEKLFPPPR ESDVPS // ID U5Q2M8_9BACT Unreviewed; 389 AA. AC U5Q2M8; DT 22-JAN-2014, integrated into UniProtKB/TrEMBL. DT 22-JAN-2014, sequence version 1. DT 07-JUN-2017, entry version 25. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:AGY52633.1}; GN ORFNames=BRDCF_p6 {ECO:0000313|EMBL:AGY52633.1}; OS Bacteroidales bacterium CF. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales. OX NCBI_TaxID=1400053 {ECO:0000313|EMBL:AGY52633.1, ECO:0000313|Proteomes:UP000017642}; RN [1] {ECO:0000313|EMBL:AGY52633.1, ECO:0000313|Proteomes:UP000017642} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CF {ECO:0000313|EMBL:AGY52633.1}; RX PubMed=24356833; RA Tang S., Edwards E.A.; RT "Complete Genome Sequence of Bacteroidales Strain CF from a RT Chloroform-Dechlorinating Enrichment Culture."; RL Genome Announc. 1:e01066-13(2013). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP006772; AGY52633.1; -; Genomic_DNA. DR RefSeq; WP_022544712.1; NZ_CP006772.1. DR KEGG; bacc:BRDCF_p6; -. DR KO; K03665; -. DR Proteomes; UP000017642; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000017642}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000017642}. FT DOMAIN 194 378 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 162 189 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 389 AA; 44898 MW; B9DE5B4DAC2487AB CRC64; MEIEKCVFVG VISQNDDESK VLEYLDELEF LAETAGAAGD KKFIQRLERP NNKTYVGSGK LDEIKSYITE NEIKLVIFDD ELTPSQLRNI EQELMCRVLD RTSLILDIFA QRAKTAYAKT QVELAQYQYL LPRLTRMWSH LERQRGGIGM RGPGESQIET DRRIILDKIS KLKEQLKKID RQMSSQRGNR GNLVRIALVG YTNVGKSTLM NLLAKSDVFA ENKLFATLDT TVRKVVIENV PFLLSDTVGF IRKLPHQLVE SFKSTLDEVR ESDILMHVVD ISHPGFEEQI KVVNETLADI GAKEKPLFLV FNKIDLYKYT PQDEYDFGPK KQENYSLDEL KNSWMGREHN PCIFISAKEK TQIDKLRNDI YKMVAEIHAG RYPFSNFLW // ID U5QJH1_9CYAN Unreviewed; 575 AA. AC U5QJH1; DT 22-JAN-2014, integrated into UniProtKB/TrEMBL. DT 22-JAN-2014, sequence version 1. DT 07-JUN-2017, entry version 26. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:AGY59066.1}; GN ORFNames=GKIL_2820 {ECO:0000313|EMBL:AGY59066.1}; OS Gloeobacter kilaueensis JS1. OC Bacteria; Cyanobacteria; Gloeobacteria; Gloeobacterales; OC Gloeobacteraceae; Gloeobacter. OX NCBI_TaxID=1183438 {ECO:0000313|EMBL:AGY59066.1, ECO:0000313|Proteomes:UP000017396}; RN [1] {ECO:0000313|EMBL:AGY59066.1, ECO:0000313|Proteomes:UP000017396} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=JS1 {ECO:0000313|EMBL:AGY59066.1}; RX PubMed=24194836; DOI=10.1371/journal.pone.0076376; RA Saw J.H., Schatz M., Brown M.V., Kunkel D.D., Foster J.S., Shick H., RA Christensen S., Hou S., Wan X., Donachie S.P.; RT "Cultivation and Complete Genome Sequencing of Gloeobacter kilaueensis RT sp. nov., from a Lava Cave in Kilauea Caldera, Hawai'i."; RL PLoS ONE 8:E76376-E76376(2013). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP003587; AGY59066.1; -; Genomic_DNA. DR EnsemblBacteria; AGY59066; AGY59066; GKIL_2820. DR KEGG; glj:GKIL_2820; -. DR PATRIC; fig|1183438.3.peg.2781; -. DR KO; K03665; -. DR Proteomes; UP000017396; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000017396}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000017396}. FT DOMAIN 397 562 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 363 390 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 575 AA; 63886 MW; 2091369031755F79 CRC64; MPFFQVQIID KIYGSHKGLK PAQLRQLSRL YSLPFPLNRF LSIEFGERLA ALSAELETPL CVYANRRGQV VRVGVGTPKE TQFSIDELPR QGTERLSGLR CIATQFDMQG PNRGALTALA LQRLDALVIL DVAVEGFRRR SAAPSGFVQR AQIANLVPDP LARWVVSTPQ SLSQVAAQDF DVFLEDLEDE FRRTATARAV ESDRERVLLV DFFSTRTSQR AMEEELSELV QLVTSAGGEV LKVFYQRRAQ PDPSTLIGQG KLEEVALSVQ DLGANLVVCG RELTPTQGRN LEQAVGVRVV DRNELILDIF ARRARSHEGK LQVELAQLQY LLPRLTGRGG ALSRLGGGIG TRGPGETKLE TDRRIIRRRI AKLQLEVNAL QAHRARLRAR RQRKEVPVFA LVGYTNAGKS TLLNTLTDAD ALVADQLFAT LDPTTRRLEL PTGDPVLLTD TVGFIHDLPP QLIDAFRATL EEVTEADALL HVVDLSNPAW MNHIQAVQRI LESLPIATGP QLLVFNKVDR VSPELRSFAE QEYPLALFIS AQKGWGFLSL RQALLRWVRS LTDLPLAESS IDGEP // ID U5RVF2_9CLOT Unreviewed; 595 AA. AC U5RVF2; DT 22-JAN-2014, integrated into UniProtKB/TrEMBL. DT 22-JAN-2014, sequence version 1. DT 07-JUN-2017, entry version 29. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=CAETHG_1289 {ECO:0000313|EMBL:AGY75514.1}; OS Clostridium autoethanogenum DSM 10061. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=1341692 {ECO:0000313|EMBL:AGY75514.1, ECO:0000313|Proteomes:UP000017590}; RN [1] {ECO:0000313|EMBL:AGY75514.1, ECO:0000313|Proteomes:UP000017590} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 10061 {ECO:0000313|EMBL:AGY75514.1}; RX PubMed=24655715; DOI=10.1186/1754-6834-7-40; RA Brown S.D., Nagaraju S., Utturkar S., De Tissera S., Segovia S., RA Mitchell W., Land M.L., Dassanayake A., Kopke M.; RT "Comparison of single-molecule sequencing and hybrid approaches for RT finishing the genome of Clostridium autoethanogenum and analysis of RT CRISPR systems in industrial relevant Clostridia."; RL Biotechnol. Biofuels 7:40-40(2014). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP006763; AGY75514.1; -; Genomic_DNA. DR RefSeq; WP_013240019.1; NZ_CP012395.1. DR ProteinModelPortal; U5RVF2; -. DR EnsemblBacteria; AGY75514; AGY75514; CAETHG_1289. DR KEGG; cah:CAETHG_1289; -. DR PATRIC; fig|1341692.11.peg.1286; -. DR KO; K03665; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000017590; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000017590}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000017590}. FT DOMAIN 362 539 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 595 AA; 66738 MW; 2A3980D90225C101 CRC64; MIYGNTEGIK NSTLDELEKI YDIRVSKESI CSREIVEVLS RITTYLNREL SLAIDKRGII VSISVGDSST VSITEIEGNQ NKLCGIRIVH THPNGDSRLS EIDISALVKL RLDCIAAIGV DKDGITGITI GFCKVKDGEV ISEVSEKLTL EDAVNFNIVQ KVNEIEKSMN DEYVLQEAGE RALLVGTDTE DSLDELKELA KACNVNVLEK ILQKRDTIDT AFYVGKGKVS EIALIAQLSG ANIVIFDDEL SGSQVRNLEE NLGIKVIDRT TLILHIFASR ARSKESKLQV ELAQLKYRLA RLSGLGIVLS RTGGGIGTRG PGEKKLETDR RHIREKIYEI SKELKKIKQV RKTQRKKRDE INKVSLVGYT NSGKSTLRNK LCEVAVTREN VNKEKVFEAD MLFATLDTTT RAVELEDGRT IAVTDTVGFI KKLPHDLVEA FKSTLEEVQY ADLLLHVVDA SSDYAEEQID AVNEVLSELD VNDKPVLIVL NKIDKLEDTK LSGIKDRYKN SNAIFISAKY GTNLDELLKR VLEMLPHNIK KAEYLIPYTE QSAVSFIHKY CKVKNEDYRE DGTYVNALVD EKTYNKFKKF IINPK // ID U5S9U0_9LACT Unreviewed; 423 AA. AC U5S9U0; DT 22-JAN-2014, integrated into UniProtKB/TrEMBL. DT 22-JAN-2014, sequence version 1. DT 07-JUN-2017, entry version 27. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=Q783_05970 {ECO:0000313|EMBL:AGY81821.1}; OS Carnobacterium inhibens subsp. gilichinskyi. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Carnobacteriaceae; OC Carnobacterium. OX NCBI_TaxID=1266845 {ECO:0000313|EMBL:AGY81821.1, ECO:0000313|Proteomes:UP000017469}; RN [1] {ECO:0000313|EMBL:AGY81821.1, ECO:0000313|Proteomes:UP000017469} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=WN1359 {ECO:0000313|EMBL:AGY81821.1, RC ECO:0000313|Proteomes:UP000017469}; RX PubMed=24285647; RA Leonard M.T., Panayotova N., Farmerie W.G., Triplett E.W., RA Nicholson W.L.; RT "Complete Genome Sequence of Carnobacterium gilichinskyi Strain RT WN1359T (DSM 27470T)."; RL Genome Announc. 1:e00985-13(2013). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP006812; AGY81821.1; -; Genomic_DNA. DR EnsemblBacteria; AGY81821; AGY81821; Q783_05970. DR KEGG; caw:Q783_05970; -. DR PATRIC; fig|1266845.5.peg.1130; -. DR KO; K03665; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000017469; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000017469}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000017469}. FT DOMAIN 207 368 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 423 AA; 47855 MW; 7AF241C954F5A69F CRC64; MNVMETKETA ETVERVILVG VQTNESNLDF EYSLRELEQL TETALGEVVG ELTQKRERVD SRTFLGKGKM EELVALVDEL EADTVIFNQG LTPGQTRNIQ KVLMDEVKVI DRIQLILDIF AMRAKSKEGK LQVELAQLQY LLPRLAGQGV NLSRLGGGIG TRGPGETKLE TDRRHIRDQI TDIKRDLTET EKHRSRTREQ RKESGTFQIG LMGYTNAGKS TLLNKLTQAD TYEENQLFAT LDPLTRQLLL PSGMTVTLTD TVGFIQDLPT QLIESFKSTL EETKGVDLLL HVVDASAENL SGHEQTVMQL LKELDMAKIP MLTVYNKKDL VEDAFYPSLF PNVVISANDP EDIDHLLSVI MDKMKELMVS YRLEINVDQG EKLVRLKRET LVISEEYDEE KNVYIVKGYA KAESKWNGEN QTS // ID U5VWG3_9ACTN Unreviewed; 399 AA. AC U5VWG3; DT 22-JAN-2014, integrated into UniProtKB/TrEMBL. DT 22-JAN-2014, sequence version 1. DT 07-JUN-2017, entry version 30. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=AFR_14175 {ECO:0000313|EMBL:AGZ41117.1}; OS Actinoplanes friuliensis DSM 7358. OC Bacteria; Actinobacteria; Micromonosporales; Micromonosporaceae; OC Actinoplanes. OX NCBI_TaxID=1246995 {ECO:0000313|EMBL:AGZ41117.1, ECO:0000313|Proteomes:UP000017746}; RN [1] {ECO:0000313|EMBL:AGZ41117.1, ECO:0000313|Proteomes:UP000017746} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 7358 {ECO:0000313|EMBL:AGZ41117.1, RC ECO:0000313|Proteomes:UP000017746}; RX PubMed=24637369; DOI=10.1016/j.jbiotec.2014.03.011; RA Ruckert C., Szczepanowski R., Albersmeier A., Goesmann A., Fischer N., RA Steinkamper A., Puhler A., Biener R., Schwartz D., Kalinowski J.; RT "Complete genome sequence of the actinobacterium Actinoplanes RT friuliensis HAG 010964, producer of the lipopeptide antibiotic RT friulimycin."; RL J. Biotechnol. 178:41-42(2014). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP006272; AGZ41117.1; -; Genomic_DNA. DR RefSeq; WP_023361176.1; NC_022657.1. DR EnsemblBacteria; AGZ41117; AGZ41117; AFR_14175. DR KEGG; afs:AFR_14175; -. DR PATRIC; fig|1246995.3.peg.2876; -. DR KO; K03665; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000017746; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000017746}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000017746}. FT DOMAIN 221 385 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 180 207 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 399 AA; 42773 MW; CBBB6E81648399C0 CRC64; MAGAWLLGAE TRATADERPR AVLMAVVQDD RTDEGAPGTP ASLRELERLA DTDGLTVAET LVQSRDRPDP ATYLGSGKAG ELAAAVERCA ADVVIADGEL SPGQARNLQD KVGVPVVDRT ALILDIFAGH ARTSEGRLQV ELAQIAYQLP RLQGAGRSMS RVGGGRVVGG AGMGVRGPGE MRLEIQRRRL RRRAAGLREQ VARLGRRRER MQWRRTRNRV PSVAITGYTN AGKSALLNRL SGADALTQDV LFATLDPTVR RVTAQELRFT LTDTVGFVRN LPHQLIEAFR STLEEVARAD LALHVVDASA ADALSQISTV HEVLREIGAG QVPEMLVLNK IDVASPETVS ALRRVYLDAL QVSALTGAGI NELRDALAGR LQEREAQRSA GTSGTPSPG // ID U5W820_9ACTN Unreviewed; 463 AA. AC U5W820; DT 22-JAN-2014, integrated into UniProtKB/TrEMBL. DT 22-JAN-2014, sequence version 1. DT 07-JUN-2017, entry version 29. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=AFR_35535 {ECO:0000313|EMBL:AGZ45363.1}; OS Actinoplanes friuliensis DSM 7358. OC Bacteria; Actinobacteria; Micromonosporales; Micromonosporaceae; OC Actinoplanes. OX NCBI_TaxID=1246995 {ECO:0000313|EMBL:AGZ45363.1, ECO:0000313|Proteomes:UP000017746}; RN [1] {ECO:0000313|EMBL:AGZ45363.1, ECO:0000313|Proteomes:UP000017746} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 7358 {ECO:0000313|EMBL:AGZ45363.1, RC ECO:0000313|Proteomes:UP000017746}; RX PubMed=24637369; DOI=10.1016/j.jbiotec.2014.03.011; RA Ruckert C., Szczepanowski R., Albersmeier A., Goesmann A., Fischer N., RA Steinkamper A., Puhler A., Biener R., Schwartz D., Kalinowski J.; RT "Complete genome sequence of the actinobacterium Actinoplanes RT friuliensis HAG 010964, producer of the lipopeptide antibiotic RT friulimycin."; RL J. Biotechnol. 178:41-42(2014). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP006272; AGZ45363.1; -; Genomic_DNA. DR EnsemblBacteria; AGZ45363; AGZ45363; AFR_35535. DR KEGG; afs:AFR_35535; -. DR PATRIC; fig|1246995.3.peg.7192; -. DR KO; K03665; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000017746; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 2. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000017746}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000017746}. FT DOMAIN 245 410 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 211 238 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 463 AA; 50454 MW; 593BC93E0D1F8162 CRC64; MRTEVSEPDV TTGELELEER HSLRRVAGLS TELTDVTEVE YRQLRLERVV LVGVWTEGSI SDAENSLTEL AALAETAGSE VLEGLIQRRG RPDAATFIGR GKVDELRDVV IATGADTVIC DGELSPSQLR KLEEQVKVKV VDRTALILDI FAQHAKSKEG KAQVELAQLQ YLLPRLRGWG ESLSRQGGGA GGSGGGVGTR GPGETKIETD RRRINTRISR LKREIKSLRT VRQTKRSKRT NSGVPAVAIA GYTNAGKSSL LNSLTSAGVL VEDALFATLD PTTRRTAAED GRVFTLSDTV GFVRHLPHHI VEAFRSTLEE VAYADLVVHV VDGAHPDPEG QVSAVREVLG EVGADRIPEL LVVNKMDAAD EETVLRLKRA WPDAVFVSAR SGLGIDELHA AIAQRLPRPA VDLRVLLPYD RGDLVARIHR TGQVLDTRHT EDGTELRVRV GEQLAADLEG FRV // ID U5WZD1_MYCKA Unreviewed; 480 AA. AC U5WZD1; DT 22-JAN-2014, integrated into UniProtKB/TrEMBL. DT 22-JAN-2014, sequence version 1. DT 07-JUN-2017, entry version 29. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=MKAN_25255 {ECO:0000313|EMBL:AGZ53246.1}; OS Mycobacterium kansasii ATCC 12478. OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae; OC Mycobacterium. OX NCBI_TaxID=557599 {ECO:0000313|EMBL:AGZ53246.1, ECO:0000313|Proteomes:UP000017786}; RN [1] {ECO:0000313|EMBL:AGZ53246.1, ECO:0000313|Proteomes:UP000017786} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 12478 {ECO:0000313|EMBL:AGZ53246.1, RC ECO:0000313|Proteomes:UP000017786}; RG McGill University Mycobacterium genome consortium; RA Veyrier F.J., Behr M.A.; RT "Genome sequence of Mycobacterium kansasii."; RL Submitted (OCT-2013) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP006835; AGZ53246.1; -; Genomic_DNA. DR RefSeq; WP_023372571.1; NC_022663.1. DR STRING; 557599.MkanA1_010100017936; -. DR EnsemblBacteria; AGZ53246; AGZ53246; MKAN_25255. DR GeneID; 29701658; -. DR KEGG; mkn:MKAN_25255; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR KO; K03665; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000017786; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000017786}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}. FT DOMAIN 250 426 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 209 243 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 480 AA; 51833 MW; 3CF80C7BA9B5505B CRC64; MTYPEFPHQD PLEPSTGELA LEDRSALRRV AGLSTELADI SEVEYRQLRL ERVVLVGVWT EGSAADTEAS MAELAALAET AGSQVLEGII QRRDRPDPST YIGSGKAAEL REIVVATGAD TVICDGELSP AQLTALEKAV KVKVIDRTAL ILDIFAQHAT SREGKAQVSL AQMEYMLPRL RGWGESMSRQ AGGRAGGSGG GVGLRGPGET KIETDRRRIR ERMAKLRREI KDMKQARDTR RSRRVHSDLP SIAIVGYTNA GKSSLLNALT GAGVLVQDAL FATLEPTTRR AEFDDGSGRP GRFLLTDTVG FVRHLPTQLV EAFRSTLEEV VDADLLVHVV DGADANPLAQ INAVRQVISE VIADRGADGG EAPQELLVVN KIDAASDLAL AKLRHALPGA VFVSARTGDG VDALRRRMAE LVAPTDAAVD VVIPYDRGDL VARLHSDGRV QHEEHSVHGT RIKARVPVTL AGRLQEFTVR // ID U6NQP0_HAECO Unreviewed; 510 AA. AC U6NQP0; DT 22-JAN-2014, integrated into UniProtKB/TrEMBL. DT 22-JAN-2014, sequence version 1. DT 10-MAY-2017, entry version 15. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:CDJ84045.1}; GN ORFNames=HCOI_00479600 {ECO:0000313|EMBL:CDJ84045.1}; OS Haemonchus contortus (Barber pole worm). OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida; OC Strongylida; Trichostrongyloidea; Haemonchidae; Haemonchinae; OC Haemonchus. OX NCBI_TaxID=6289 {ECO:0000313|EMBL:CDJ84045.1, ECO:0000313|Proteomes:UP000025227}; RN [1] {ECO:0000313|Proteomes:UP000025227} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ISE/inbred ISE {ECO:0000313|Proteomes:UP000025227}; RX PubMed=23985316; DOI=10.1186/gb-2013-14-8-r88; RA Laing R., Kikuchi T., Martinelli A., Tsai I.J., Beech R.N., Redman E., RA Holroyd N., Bartley D.J., Beasley H., Britton C., Curran D., RA Devaney E., Gilabert A., Hunt M., Jackson F., Johnston S.L., RA Kryukov I., Li K., Morrison A.A., Reid A.J., Sargison N., RA Saunders G.I., Wasmuth J.D., Wolstenholme A., Berriman M., RA Gilleard J.S., Cotton J.A.; RT "The genome and transcriptome of Haemonchus contortus, a key model RT parasite for drug and vaccine discovery."; RL Genome Biol. 14:R88.01-R88.16(2013). RN [2] {ECO:0000313|Proteomes:UP000025227} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ISE/inbred ISE {ECO:0000313|Proteomes:UP000025227}; RA Huang N.-L., Huang M.-D., Chen T.-L.L., Huang A.H.; RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases. RN [3] {ECO:0000313|EMBL:CDJ84045.1, ECO:0000313|Proteomes:UP000025227} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ISE/inbred ISE {ECO:0000313|EMBL:CDJ84045.1, RC ECO:0000313|Proteomes:UP000025227}; RA Laing R., Kikuchi T., Martinelli A., Tsai I.J., Beech R.N., Redman E., RA Holroyd N., Bartley D.J., Beasley H., Britton C., Curran D., RA Devaney E., Gilabert A., Jackson F., Hunt M., Johnston S., Kryukov I., RA Li K., Morrison A.A., Reid A.J., Sargison N., Saunders G., RA Wasmuth J.D., Wolstenholme A., Berriman M., Gilleard J.S., RA Cotton J.A.; RT "The genome and transcriptome of Haemonchus contortus: a key model RT parasite for drug and vaccine discovery."; RL Submitted (MAY-2013) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; HF959984; CDJ84045.1; -; Genomic_DNA. DR Proteomes; UP000025227; Unassembled WGS sequence. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR CDD; cd01878; HflX; 1. DR InterPro; IPR008584; DUF866_euk. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR Pfam; PF05907; DUF866; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000025227}; KW Reference proteome {ECO:0000313|Proteomes:UP000025227}. FT DOMAIN 196 360 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 510 AA; 57158 MW; 41352597E678804B CRC64; MVVHPKIRWG SSSASILKDP QRQLEEAVTL VNTLPGFRVV ESAVMGVDYN TKRKGVWGSG QLEALVNMKA KSRVTALMVN VDMLSPIQQR ELYNIFHVPI YDRYNIVLSI FKHYAKTPEA HLQIQLAEIP YIRNRLHYIN KYHSDPGMLH IERQPERASV DEFEVLRLRE QSLRKKLQAV IDKSTGKAVE ESRDAAMVAV VGYTNSGKTS LVKCLTGAAS LDPKDRLFAT LDTTRHLARL PSGRKVVFTD TIGFLSDLPM HLLAAFQATL SHVVLADVII HIRDISNPDW PAQSEDVDNT LKQIGLPSNR LNDVIVVDNK IDVNGAPSTS APSAMRISCK TSEGVENLIA KVDENVLRAT GCKLRRLSLK CSSPAIAYLY KEGLVSREPN PTGSHLVFDV FMNDAEFARF QKYTGLLRFA VSFVNMPVLA LEIKCNMVGV TGFTPSDPEN HRWFLKFRCM NCGESRDYWQ YVVINEVLEV PGSRGEANLV EKCKLCNRVN TVGEYNKKAL // ID U7D8F0_9BACT Unreviewed; 389 AA. AC U7D8F0; DT 22-JAN-2014, integrated into UniProtKB/TrEMBL. DT 22-JAN-2014, sequence version 1. DT 05-JUL-2017, entry version 28. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=CALK_0690 {ECO:0000313|EMBL:ERP38674.1}; OS Chitinivibrio alkaliphilus ACht1. OC Bacteria; Fibrobacteres; Chitinivibrionia; Chitinivibrionales; OC Chitinivibrionaceae; Chitinivibrio. OX NCBI_TaxID=1313304 {ECO:0000313|EMBL:ERP38674.1, ECO:0000313|Proteomes:UP000017148}; RN [1] {ECO:0000313|EMBL:ERP38674.1, ECO:0000313|Proteomes:UP000017148} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ACht1 {ECO:0000313|EMBL:ERP38674.1, RC ECO:0000313|Proteomes:UP000017148}; RX PubMed=24112708; RA Sorokin D.Y., Gumerov V.M., Rakitin A.L., Beletsky A.V., Damste J.S., RA Muyzer G., Mardanov A.V., Ravin N.V.; RT "Genome analysis of Chitinivibrio alkaliphilus gen. nov., sp. nov., a RT novel extremely haloalkaliphilic anaerobic chitinolytic bacterium from RT the candidate phylum Termite Group 3."; RL Environ. Microbiol. 0:0-0(2013). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:ERP38674.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ASJR01000005; ERP38674.1; -; Genomic_DNA. DR EnsemblBacteria; ERP38674; ERP38674; CALK_0690. DR PATRIC; fig|1313304.3.peg.662; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000017148; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000017148}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000017148}. FT DOMAIN 203 369 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 389 AA; 43726 MW; 3A7C988D5CD0D12E CRC64; MFDIEREQSL SESVILAALY MPRKMDEELF EEDLAEMETL IATAGAEVAD IFVQKRDKPR FSTWFGAGKL DEISRRMKET NSKCLVIDAE LKPSQIQNIE AIICGKVIDR SQLILDIFAL HARTNEAKIQ VELAQLNLMY PRLTRMWSHL SRQSGGIGTR GPGETQLETD KRLVQKKIAQ LKKSLKKIKK SREVQRRGRS DTFRISLVGY TNVGKSTLLN ALCGADVLVR DELFATLDTA SKKGYIPSVG EVVISDTVGF LRKLPHHLVA SFRSTLEVAQ ETDLLLIVMD ASSKWFSHQL DTVRDVLGDL SAGHKPAKII FNKIDRVDDP LQLRQIECEF PQASFVSALD KESVQQLKHD LGETIHEVRA DKKQAAAIEK RAGTYIHVG // ID U7GL94_9RHOB Unreviewed; 426 AA. AC U7GL94; DT 22-JAN-2014, integrated into UniProtKB/TrEMBL. DT 22-JAN-2014, sequence version 1. DT 07-JUN-2017, entry version 25. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=Q669_22640 {ECO:0000313|EMBL:ERP98003.1}; OS Labrenzia sp. C1B10. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae; Labrenzia. OX NCBI_TaxID=1397530 {ECO:0000313|EMBL:ERP98003.1, ECO:0000313|Proteomes:UP000017101}; RN [1] {ECO:0000313|EMBL:ERP98003.1, ECO:0000313|Proteomes:UP000017101} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C1B10 {ECO:0000313|EMBL:ERP98003.1}; RX PubMed=24356826; RA Overholt W.A., Green S.J., Marks K.P., Venkatraman R., Prakash O., RA Kostka J.E.; RT "Draft genome sequences for oil-degrading bacterial strains from beach RT sands impacted by the deepwater horizon oil spill."; RL Genome Announc. 1:e01015-13(2013). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:ERP98003.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AXBY01000005; ERP98003.1; -; Genomic_DNA. DR RefSeq; WP_022998589.1; NZ_AXBY01000005.1. DR EnsemblBacteria; ERP98003; ERP98003; Q669_22640. DR PATRIC; fig|1397530.3.peg.972; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000017101; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000017101}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000017101}. FT DOMAIN 200 370 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 166 193 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 426 AA; 47275 MW; 777FAC17CF6643B9 CRC64; MILEPVLQLR GESAQTELRG NRSPEARLEE ALGLSAAINL NIAHSGVVRV NNPKPATLFG DGKVAELAGI VASEDLDLVV IDHPLTPVQQ RNLERRLKTK VIDRTGLILE IFGDRARTKE GRLQVDLAHL TWQKSRLVRS WTHLERQRGG AGFMGGPGET QIEADRRQIQ DRIIALQKQL EQVRRTRDLH RKKRKKIPQP VVALVGYTNA GKSTLFNRMT ESDVFAKDLL FATLDPTLRK VALPHGKEVI LSDTVGFISD LPTHLVAAFR ATLEEVLEAD LILHVRDISH ADTEAQAEDV KKTLTDLGVD ALTGAPIIEV WNKIDCLDPA YRDKLLEDAG EEGPIALSAL TGEGIEQLYA RVDAFMAQHD DILTVKIPVA DGALLAKLYQ MAEVLERTDA EDFVTAEVRV SDKQRGPFRE LYAAYL // ID U7LFL3_9CORY Unreviewed; 502 AA. AC U7LFL3; DT 22-JAN-2014, integrated into UniProtKB/TrEMBL. DT 22-JAN-2014, sequence version 1. DT 07-JUN-2017, entry version 26. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=HMPREF1281_00513 {ECO:0000313|EMBL:ERS56731.1}; OS Corynebacterium sp. KPL1855. OC Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae; OC Corynebacterium. OX NCBI_TaxID=1203562 {ECO:0000313|EMBL:ERS56731.1, ECO:0000313|Proteomes:UP000017096}; RN [1] {ECO:0000313|EMBL:ERS56731.1, ECO:0000313|Proteomes:UP000017096} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=KPL1855 {ECO:0000313|EMBL:ERS56731.1, RC ECO:0000313|Proteomes:UP000017096}; RG The Broad Institute Genomics Platform; RA Earl A., Ward D., Feldgarden M., Gevers D., Jacobson B., Goguen K., RA Pagano E., Lemon K.P., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., RA Abouelleil A., Alvarado L., Berlin A.M., Chapman S.B., RA Gainer-Dewar J., Goldberg J., Gnerre S., Griggs A., Gujja S., RA Hansen M., Howarth C., Imamovic A., Ireland A., Larimer J., RA McCowan C., Murphy C., Pearson M., Poon T.W., Priest M., Roberts A., RA Saif S., Shea T., Sykes S., Wortman J., Nusbaum C., Birren B.; RT "The Genome Sequence of Corynebacterium sp. KPL1855."; RL Submitted (OCT-2013) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:ERS56731.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AXLX01000006; ERS56731.1; -; Genomic_DNA. DR RefSeq; WP_023022772.1; NZ_KI515741.1. DR EnsemblBacteria; ERS56731; ERS56731; HMPREF1281_00513. DR PATRIC; fig|1203562.3.peg.493; -. DR Proteomes; UP000017096; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000017096}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000017096}. FT DOMAIN 274 445 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 502 AA; 55124 MW; 1AC7E6B7071ACFA6 CRC64; MNKFSPQNSD SSASKDELLA QAFRDHADTP QETTPTSGDL DLAERNAFRR VTRETSIRAE DTTDGYEVEY RKLRLERVIL VGVWTEGTVA EVEATMDELA ALTETAGADV VEMIYQKRDK PDPGTFIGSG KVKELHDIVE ATGADTVVCD GELNPGQLTA LERALNTKVI DRTMLILDIF AQHAKSKEGK AQVSLAQLEY LYTHTRGWGG NLSRQAGGRA GSNGGVGLRG PGETKIETDR RRIRTEMARL RKELRGMKTA REVKRSRRQS STIAQIAIAG YTNAGKSSLI NAMTNAGVLV EDALFATLDP TTRRASLADG RQVVFTDTVG FVRHLPTQLV EAFKSTLEEV LAADIMLHVV DGSDPFPLKQ IEAVNKVIYD IVSETGEQAP PEIIVINKID QADPLVLAEL RHVLDHEDVV YVSARTGEGI DELSARVELF LNSRDSHVKL QVPFTRGDVV SRVHAEGTVR SEEYTENGTL VDVRLPATTA RELAEFIVDD DS // ID U7MNH7_9CORY Unreviewed; 550 AA. AC U7MNH7; DT 22-JAN-2014, integrated into UniProtKB/TrEMBL. DT 22-JAN-2014, sequence version 1. DT 07-JUN-2017, entry version 27. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=HMPREF1290_01518 {ECO:0000313|EMBL:ERS71684.1}; OS Corynebacterium sp. KPL1989. OC Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae; OC Corynebacterium. OX NCBI_TaxID=1203622 {ECO:0000313|EMBL:ERS71684.1, ECO:0000313|Proteomes:UP000017102}; RN [1] {ECO:0000313|EMBL:ERS71684.1, ECO:0000313|Proteomes:UP000017102} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=KPL1989 {ECO:0000313|EMBL:ERS71684.1, RC ECO:0000313|Proteomes:UP000017102}; RG The Broad Institute Genomics Platform; RA Earl A., Ward D., Feldgarden M., Gevers D., Jacobson B., Goguen K., RA Pagano E., Lemon K.P., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., RA Abouelleil A., Alvarado L., Berlin A.M., Chapman S.B., RA Gainer-Dewar J., Goldberg J., Gnerre S., Griggs A., Gujja S., RA Hansen M., Howarth C., Imamovic A., Ireland A., Larimer J., RA McCowan C., Murphy C., Pearson M., Poon T.W., Priest M., Roberts A., RA Saif S., Shea T., Sykes S., Wortman J., Nusbaum C., Birren B.; RT "The Genome Sequence of Corynebacterium sp. KPL1989."; RL Submitted (OCT-2013) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:ERS71684.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AXLR01000005; ERS71684.1; -; Genomic_DNA. DR EnsemblBacteria; ERS71684; ERS71684; HMPREF1290_01518. DR PATRIC; fig|1203622.3.peg.1501; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000017102; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000017102}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000017102}. FT DOMAIN 321 499 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 550 AA; 59833 MW; 1C22F7D4838ABE09 CRC64; MTKNFSHSFS AGSKNIDAKH NSSKSSKAAH DELLEAAFKD NEAQDSFAIT DAQDALSEIA AGKSEAIRSD LVSGDNSRDS APTTGDMDLA ERNAFRRVTR DTTIRTEDTT DGYEVEYRKL RLEQVILVGV WTEGTVAELE ATLEELAALA ETAGAEVLEI LYQKRDSPDS GTFIGSGKVQ QLKSLVQEYG ADTVICDGEL NPGQLTALER ELDTKVIDRT MLILDIFAQH AKSKEGKAQV SLAQLEYLYT HTRGWGGSLS RQAGGRAGSN GGVGLRGPGE TKIETDRRRI RAEMARLRKS LAGMKTAREV KRARRQGSLV PQIAIAGYTN AGKSSLINAM TDAGVLVEDA LFATLDPTTR KAQLGDGRSV VFTDTVGFVR HLPTQLVEAF KSTLEEVLAA DVMLHVVDAA DPFPLKQITA VNKVISDIVE ETGQQAPPEI IVMNKIDAAD PLVLAEMRHV LERDNVVYVS AKTGEGIAEL SGRVELFLNS LDTRMLLEIP YTRGDLVSRV HEYGTVHSES YNAEGTVIDV RLPAVMAKEL AEFESDYQTS // ID U7P475_9GAMM Unreviewed; 443 AA. AC U7P475; DT 22-JAN-2014, integrated into UniProtKB/TrEMBL. DT 22-JAN-2014, sequence version 1. DT 30-AUG-2017, entry version 26. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=Q671_01070 {ECO:0000313|EMBL:ERS89524.1}; OS Halomonas sp. PBN3. OC Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales; OC Halomonadaceae; Halomonas. OX NCBI_TaxID=1397528 {ECO:0000313|EMBL:ERS89524.1, ECO:0000313|Proteomes:UP000017115}; RN [1] {ECO:0000313|EMBL:ERS89524.1, ECO:0000313|Proteomes:UP000017115} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=PBN3 {ECO:0000313|EMBL:ERS89524.1, RC ECO:0000313|Proteomes:UP000017115}; RX PubMed=24356826; RA Overholt W.A., Green S.J., Marks K.P., Venkatraman R., Prakash O., RA Kostka J.E.; RT "Draft genome sequences for oil-degrading bacterial strains from beach RT sands impacted by the deepwater horizon oil spill."; RL Genome Announc. 1:e01015-13(2013). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:ERS89524.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AXCA01000152; ERS89524.1; -; Genomic_DNA. DR RefSeq; WP_023005612.1; NZ_AXCA01000152.1. DR EnsemblBacteria; ERS89524; ERS89524; Q671_01070. DR PATRIC; fig|1397528.3.peg.1410; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000017115; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000017115}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000017115}. FT DOMAIN 199 365 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 443 AA; 49700 MW; CABB759530FCCD41 CRC64; MFFERPDAGE TAVLVHVDFQ DEQEREDPGE FLELVRSAGA EPATLLTGSR HRPDPRTFVG SGKVEELREA LSVHGAELVI FNHALSPSQE RNLERTLKCR VLDRTGLILD IFAQRARTHE GKLQVELAQL EYMSTRLVRG WTHLERQKGG IGLRGPGETQ LETDRRLLRG RIKAIHRRLD KVRGQREQNR RSRARAEIPS VSLVGYTNAG KSTLFNALTA SRVYAADQLF ATLDPTLRRL EIEDVGPVVM ADTVGFIRHL PHKLVEAFQA TLQEAAEATL LVHVIDAADP DRDLNVEQVE TVLDEIGALE VPTLKVMNKI DLLDSAPRIE RDGEGRPEVV WLSAREGRGL ELLEQALAER LAEDVIGFPL TLAPEQGRLR AALHELGAVR EERFDDDGRT RLQVRLPRRD FLQLMARLGE RAEDYLPAAL QAREAWEEAS GPG // ID U7UJD9_9FIRM Unreviewed; 418 AA. AC U7UJD9; DT 22-JAN-2014, integrated into UniProtKB/TrEMBL. DT 22-JAN-2014, sequence version 1. DT 07-JUN-2017, entry version 26. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:ERT59009.1}; GN ORFNames=HMPREF1253_1915 {ECO:0000313|EMBL:ERT59009.1}; OS Peptoniphilus sp. BV3C26. OC Bacteria; Firmicutes; Tissierellia; Tissierellales; Peptoniphilaceae; OC Peptoniphilus. OX NCBI_TaxID=1111134 {ECO:0000313|EMBL:ERT59009.1, ECO:0000313|Proteomes:UP000017105}; RN [1] {ECO:0000313|EMBL:ERT59009.1, ECO:0000313|Proteomes:UP000017105} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BV3C26 {ECO:0000313|EMBL:ERT59009.1, RC ECO:0000313|Proteomes:UP000017105}; RA Durkin A.S., Haft D.R., McCorrison J., Torralba M., Gillis M., RA Haft D.H., Methe B., Sutton G., Nelson K.E.; RL Submitted (SEP-2013) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:ERT59009.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AWXB01000041; ERT59009.1; -; Genomic_DNA. DR RefSeq; WP_023055500.1; NZ_AWXB01000041.1. DR EnsemblBacteria; ERT59009; ERT59009; HMPREF1253_1915. DR PATRIC; fig|1111134.3.peg.859; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000017105; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000017105}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000017105}. FT DOMAIN 198 365 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 164 191 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 418 AA; 47280 MW; EDBBCCAB3E6AFFD8 CRC64; METTKKIEKV IIVATDLGSF PNTLSSSLEE LRELVKADEG QVVGVVTQNI EKFNPKYLIG TGKVKEIKEI AKNMEVETVI FNDELSGIQV RNLEEELKLK VVDRTNLILD IFAMRANTYE AKLQVQLAQR EYQLPRLLGI KGWSRTGGGI GTRGPGEQII ETDRRRLLRE INSIKKKLKK AELNRENAAK KRRESPLPNV ALVGYTNAGK STILNRIKEN TGRDVFVKNM LFATLDPGIR QAKLLNGRDF IISDTVGFVS KLPTKLVEAF KSTLEEVKNA DLIVHVIDSS NSDLEIQYKT TMDILKELEV LDRPILTVFN KMDRAEFEEM IVPQVPGDKI FISAKKDENM EVLLKAIEKN LGLSYTEEKL LFPFSQAGKL NEFLNNFKGE ILEYNEEGTL VKATLSEIEK KEFGDFIV // ID U7V5E7_9FUSO Unreviewed; 597 AA. AC U7V5E7; DT 22-JAN-2014, integrated into UniProtKB/TrEMBL. DT 22-JAN-2014, sequence version 1. DT 07-JUN-2017, entry version 26. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=HMPREF0202_02495 {ECO:0000313|EMBL:ERT66932.1}; OS Cetobacterium somerae ATCC BAA-474. OC Bacteria; Fusobacteria; Fusobacteriales; Fusobacteriaceae; OC Cetobacterium. OX NCBI_TaxID=1319815 {ECO:0000313|EMBL:ERT66932.1, ECO:0000313|Proteomes:UP000017081}; RN [1] {ECO:0000313|EMBL:ERT66932.1, ECO:0000313|Proteomes:UP000017081} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-474 {ECO:0000313|EMBL:ERT66932.1, RC ECO:0000313|Proteomes:UP000017081}; RA Weinstock G., Sodergren E., Wylie T., Fulton L., Fulton R., RA Fronick C., O'Laughlin M., Godfrey J., Miner T., Herter B., RA Appelbaum E., Cordes M., Lek S., Wollam A., Pepin K.H., Palsikar V.B., RA Mitreva M., Wilson R.K.; RL Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:ERT66932.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AXZF01000126; ERT66932.1; -; Genomic_DNA. DR RefSeq; WP_023052024.1; NZ_KI518104.1. DR EnsemblBacteria; ERT66932; ERT66932; HMPREF0202_02495. DR PATRIC; fig|1319815.3.peg.2395; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000017081; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000017081}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000017081}. FT DOMAIN 364 541 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 323 350 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 597 AA; 66697 MW; 6D4DFC7FAEE15314 CRC64; MIKGNVEGVR DSILAELDTI YSMSVEKGKL VSPEIVALIT DITRVINREI SVSIDRKGKI LEVAIGDSNS VELPILEISS KKLSGVKVIH THPNGYSKLS MIDISALLKL KLDAILAIGV GETEITGVNI GYCKIENQEL VYEEIENLSL DKVMSTDYLD KVLEIESELR KSDVIEDDSE YAIVVGVDSE ESLDELEELA RACDVNVAGR IFQKIKRIDN IFYIGSGKVR ELALLRQIKN ANLIIFDEEL SGVQIKNLEA VTGCKVIDRT ILILEIFARR ARTREAKIQV ELAQLKYRSQ RLIGLGSIMS RTGGGIGTKG PGEKKLEIDR RRIKDEIFAL RQELEKIKKI RALQRTKRES SGIPRVSLVG YTNVGKSTLR NLLVEMYPSD NTVKKEAVFA ENMLFATLDA TTRTMVLPDK RVTALTDTVG FVRKLPHDLI EAFKSTLEEV IFSDLLVHLV DASSDTVVQQ IKSVENVLTE LGAIDKPTIL ALNKCDVATD EQIEKLKELY NHMDIVEISA KNEINIDLLM DKITTSLPRT MKRVELLIPY SDSSINAYLH RNAIIESESY EADGTLIIAT VSDEVYNKCS NFIIKEI // ID U9VT70_9CYAN Unreviewed; 497 AA. AC U9VT70; DT 22-JAN-2014, integrated into UniProtKB/TrEMBL. DT 22-JAN-2014, sequence version 1. DT 07-JUN-2017, entry version 28. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=N836_09820 {ECO:0000313|EMBL:ESA35815.1}; OS Leptolyngbya sp. Heron Island J. OC Bacteria; Cyanobacteria; Synechococcales; Leptolyngbyaceae; OC Leptolyngbya. OX NCBI_TaxID=1385935 {ECO:0000313|EMBL:ESA35815.1, ECO:0000313|Proteomes:UP000017515}; RN [1] {ECO:0000313|EMBL:ESA35815.1, ECO:0000313|Proteomes:UP000017515} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Heron Island J {ECO:0000313|EMBL:ESA35815.1, RC ECO:0000313|Proteomes:UP000017515}; RX PubMed=24503993; RA Paul R., Jinkerson R.E., Buss K., Steel J., Mohr R., Hess W.R., RA Chen M., Fromme P.; RT "Draft Genome Sequence of the Filamentous Cyanobacterium Leptolyngbya RT sp. Strain Heron Island J, Exhibiting Chromatic Acclimation."; RL Genome Announc. 2:e01166-13(2014). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:ESA35815.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AWNH01000053; ESA35815.1; -; Genomic_DNA. DR EnsemblBacteria; ESA35815; ESA35815; N836_09820. DR PATRIC; fig|1385935.3.peg.3380; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000017515; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000017515}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000017515}. FT DOMAIN 325 495 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 284 318 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 497 AA; 54813 MW; FD66A5531D657B58 CRC64; MGVGSPRQTQ IPTLELPRYG AERLCGIRCI ATQLKQEKPG NAALTAMALQ RLDALVLITL TGSGFQRKGG GATGYIREAY LAHLIPDETQ RWSVSAAMDL ETLSQEDFTD LTEGLEEEFR RLFVAQQVDS SHDRVLLVGL QTDRMDPDQF KNGLEELSRL VETAGGEVLE TLKQKRAKPH PQTVLGAGKV DEIALEAQTL GVSLVVFNRD LSPAQVRSLE QRIGVRVVDR TEVILDIFAQ RARTGAGKLQ VELAQLEYQL PKLTGRGQAM SRLGGGIGTR GPGETKLETE RRAIQKRITR LQREVTQLQA HRSRMRQNRQ HHQVPSVAVV GYTNAGKSTL LNTLTNADIY AADQLFATLD PTTKRLSVVD NETHEKRAMV LTDTVGFIQD LPPSLMDAFR ATLEEVTEAD ALMHVVDLSH HAWQDHIRSV MGILGQMPTT PGPILLVFNK LDAVDSDTLA VAKDEYPQAL FISAAQKLGL ETLRQRLVQL IDYAVAG // ID V1CNC6_9FIRM Unreviewed; 452 AA. AC V1CNC6; DT 22-JAN-2014, integrated into UniProtKB/TrEMBL. DT 22-JAN-2014, sequence version 1. DT 07-JUN-2017, entry version 28. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=HMPREF9089_00052 {ECO:0000313|EMBL:ESE31587.1}; OS Eubacterium brachy ATCC 33089. OC Bacteria; Firmicutes; Clostridia; Clostridiales; OC Clostridiales Family XIII. Incertae Sedis. OX NCBI_TaxID=1321814 {ECO:0000313|EMBL:ESE31587.1, ECO:0000313|Proteomes:UP000017536}; RN [1] {ECO:0000313|EMBL:ESE31587.1, ECO:0000313|Proteomes:UP000017536} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33089 {ECO:0000313|EMBL:ESE31587.1, RC ECO:0000313|Proteomes:UP000017536}; RA Weinstock G., Sodergren E., Wylie T., Fulton L., Fulton R., RA Fronick C., O'Laughlin M., Godfrey J., Miner T., Herter B., RA Appelbaum E., Cordes M., Lek S., Wollam A., Pepin K.H., Palsikar V.B., RA Mitreva M., Wilson R.K.; RL Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:ESE31587.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AXUD01000001; ESE31587.1; -; Genomic_DNA. DR RefSeq; WP_023152232.1; NZ_KI535270.1. DR EnsemblBacteria; ESE31587; ESE31587; HMPREF9089_00052. DR PATRIC; fig|1321814.3.peg.36; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000017536; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000017536}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000017536}. FT DOMAIN 203 384 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 162 196 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 452 AA; 50742 MW; 58652E206A1980AC CRC64; MIKFDENNEI VTDDVKAILV GVEKRESISK SMLELEGLTE AAGGEVLGVL TQKLEKIDVG TYVGKGKVEE LKIIVERLGA NIAVFNDELS GIQIRNLEEI LKCRVIDRTI LILDIFASRA TSKEGKLQVE LAQLEYRMPR LLGFGKSLSR LGGGIGTRGP GEKKLEVDKR HIRKRIDDIK KELEEVRKNR KVQRARREKN EIPIVALVGY TNAGKSALMN KILEITSEKA DTENLKKVDS ENMLFSTLDV YRRKIRLDNK KDVILVDTVG FVSKLPHSLV DAFKSTLEEV KFADLILHVV DVSDDDHEFQ EEVTNQILNE IGIGSKECIM IYNKADAVGN ETGISIFGDV PVNKDKYNIV TSALSGKNVD KLIEIILDKI FGNSIRAKFK IPFDKGGVLS FIYDRAEILE EEYSEQGTIL TVNITKEDYG RISKYDFIQN GEERSCCGAN NR // ID V2K7G3_9BURK Unreviewed; 481 AA. AC V2K7G3; DT 22-JAN-2014, integrated into UniProtKB/TrEMBL. DT 22-JAN-2014, sequence version 1. DT 10-MAY-2017, entry version 25. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=B551_0207880 {ECO:0000313|EMBL:ESJ22353.1}; OS Cupriavidus sp. HPC(L). OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Cupriavidus. OX NCBI_TaxID=1217418 {ECO:0000313|EMBL:ESJ22353.1, ECO:0000313|Proteomes:UP000053474}; RN [1] {ECO:0000313|EMBL:ESJ22353.1, ECO:0000313|Proteomes:UP000053474} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=HPC(L) {ECO:0000313|Proteomes:UP000053474}; RA Purohit H.J., Agarwal L.; RT "Cupriavidus a Desert isolate."; RL Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:ESJ22353.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AMPR02000101; ESJ22353.1; -; Genomic_DNA. DR EnsemblBacteria; ESJ22353; ESJ22353; B551_0207880. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000053474; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000053474}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000053474}. FT DOMAIN 202 372 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 168 195 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 481 AA; 52156 MW; 51406156A11A028F CRC64; MQPRATSPSE PTRAILVGVD FGKHDFEESL SELALLTSTA GSTPVHTLTG KRSRPDPALF IGSGKAEELK EAADALDADV VVFNHALSPA QQRNLERFLN RHVIDRTGLI LDIFGQRAQS HVGKVQVELA QVQYRASRLV RAWSHLERQK GGIGMRGGPG ERQLELDRRM LDDRAKRLKT DLSRLQRQHS TQRRARARNE TLSISLVGYT NAGKSTLFNA LTKARAYAAN QLFATLDTTS RRLYLDGLGN VVLSDTVGFI RDLPTQLVAA FRATLEETVH ADLLLHVVDA ASPVRHEQIE QVNRVLAEID AADIPQIVVM NKIDAAPELL EHGPRIERNE DGVPVRVYIS ARDGIGLDGL RDAIVDVARW LAERPAAPDP ADPRLQDLHE RRQWEGDGAD GADGADGADG ADGADGADGA DGADGADGAE FADSGADARP DAQDANPHSE PDPDPDSDRS PDPGSDPQAR ANRRLPDRDA D // ID V2QC75_9BACT Unreviewed; 486 AA. AC V2QC75; DT 22-JAN-2014, integrated into UniProtKB/TrEMBL. DT 22-JAN-2014, sequence version 1. DT 07-JUN-2017, entry version 26. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=N508_00782 {ECO:0000313|EMBL:ESJ98566.1}; OS Mucispirillum schaedleri ASF457. OC Bacteria; Deferribacteres; Deferribacterales; Deferribacteraceae; OC Mucispirillum. OX NCBI_TaxID=1379858 {ECO:0000313|EMBL:ESJ98566.1, ECO:0000313|Proteomes:UP000017429}; RN [1] {ECO:0000313|EMBL:ESJ98566.1, ECO:0000313|Proteomes:UP000017429} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ASF457 {ECO:0000313|EMBL:ESJ98566.1, RC ECO:0000313|Proteomes:UP000017429}; RX PubMed=24723722; RA Wannemuehler M.J., Overstreet A.M., Ward D.V., Phillips G.J.; RT "Draft genome sequences of the altered schaedler flora, a defined RT bacterial community from gnotobiotic mice."; RL Genome Announc. 2:e00287-14(2014). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:ESJ98566.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AYGZ01000012; ESJ98566.1; -; Genomic_DNA. DR EnsemblBacteria; ESJ98566; ESJ98566; N508_00782. DR PATRIC; fig|1379858.3.peg.776; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000017429; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000017429}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000017429}. FT DOMAIN 315 480 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 281 308 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 486 AA; 55118 MW; AC83DC8330626702 CRC64; MLAGSYDSIM IPVLSRFKLV SGRLRGLRLI HTHPKGDKLD HDDMADLALL RLDSVTACTM NNKGYPLFLD TAYILPPEND ASQSEFGYLE DSDPYNQKTD YPLFIEALDD EIQRKTKQMH ISKDGEYAVL TGVFKSKEEC DINLDELEEL VRSAGVNIIA RVPQVKKEIH PKYVAGPGKL REAVIKALMT GAEYIIFDNS LSPSQSRAVS EFTELKILDR TQLILDIFAR RAKSNEGKIR VELAQLKYIL PRLGAKDDSL SRLTGGIGGR GPGETKLEID KRRINDRIAF LNDKLKKAEQ ARDIQRARRE KNSIPVVSII GYTNAGKSTL LNSLTKSDVY ADNLLFATLD TSSKRIRFPK ERDVIVTDTV GFIRDLPANL AGAFKSTLEE LHNADMFLHV VDISDKHFKK HIKSVEKVLE EMDLQEKERI IVFNKIDKLI DEKLDEIRKE YSDAVYISAF KRASFDDMLN KIGYYFFKEG IEGFND // ID V2TPT6_9GAMM Unreviewed; 444 AA. AC V2TPT6; DT 22-JAN-2014, integrated into UniProtKB/TrEMBL. DT 22-JAN-2014, sequence version 1. DT 07-JUN-2017, entry version 26. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=P256_01268 {ECO:0000313|EMBL:ESK39587.1}; OS Acinetobacter nectaris CIP 110549. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Moraxellaceae; Acinetobacter. OX NCBI_TaxID=1392540 {ECO:0000313|EMBL:ESK39587.1, ECO:0000313|Proteomes:UP000023785}; RN [1] {ECO:0000313|EMBL:ESK39587.1, ECO:0000313|Proteomes:UP000023785} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CIP 110549 {ECO:0000313|EMBL:ESK39587.1, RC ECO:0000313|Proteomes:UP000023785}; RG The Broad Institute Genomics Platform; RG The Broad Institute Genome Sequencing Center for Infectious Disease; RA Cerqueira G., Feldgarden M., Courvalin P., Grillot-Courvalin C., RA Clermont D., Rocha E., Yoon E.-J., Nemec A., Young S.K., Zeng Q., RA Gargeya S., Fitzgerald M., Abouelleil A., Alvarado L., Berlin A.M., RA Chapman S.B., Gainer-Dewar J., Goldberg J., Gnerre S., Griggs A., RA Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A., Larimer J., RA McCowan C., Murphy C., Pearson M., Poon T.W., Priest M., Roberts A., RA Saif S., Shea T., Sykes S., Wortman J., Nusbaum C., Birren B.; RT "The Genome Sequence of Acinetobacter nectaris CIP 110549."; RL Submitted (OCT-2013) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:ESK39587.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AYER01000004; ESK39587.1; -; Genomic_DNA. DR RefSeq; WP_023272900.1; NZ_KI530723.1. DR EnsemblBacteria; ESK39587; ESK39587; P256_01268. DR PATRIC; fig|1392540.3.peg.1229; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000023785; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000023785}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000023785}. FT DOMAIN 199 364 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 444 AA; 49826 MW; DE7CB36740951C13 CRC64; MEYFDRHQGG ERAILVHVTV QMLRDLDAEE FQLLAKSAGA DILENVTAQR QRPDPKLFIG SGKAEELAAL VEEREAELVI FDHSLSPGQE RNLEKILKCR VIDRTGLILD IFAQRARTHE GKLQVELAQL EHLSTRLVRG WTHLERQKGG IGLRGPGESQ LETDRRLLRV RMGQLKDKLE KVRQTRIQGR AARQKAAIPT VSLVGYTNAG KSTLFNILAN SEVYAADQLF ATLDPTLRRL NWDGIGSLVL ADTVGFVRDL PHSLVESFKA TLEETLEATL LLHVIDSSSP DMMEQIDAVE DVLKEIGADV PILRVYNKID QSGEEAKIIY ASPNIPERVY VSAHTQQGLD LLKQAVQESL LGQIQSFELI LKPAYGKLRT ALYNLNVIQS EDYNDSGDLL LKVIIAPNKL EQTIKQLHLP IDEILGQAAQ QFKRPLEAFE LEHH // ID V2UB14_9GAMM Unreviewed; 443 AA. AC V2UB14; DT 22-JAN-2014, integrated into UniProtKB/TrEMBL. DT 22-JAN-2014, sequence version 1. DT 30-AUG-2017, entry version 27. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=P255_02181 {ECO:0000313|EMBL:ESK51653.1}; OS Acinetobacter brisouii CIP 110357. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Moraxellaceae; Acinetobacter. OX NCBI_TaxID=1341683 {ECO:0000313|EMBL:ESK51653.1, ECO:0000313|Proteomes:UP000018418}; RN [1] {ECO:0000313|EMBL:ESK51653.1, ECO:0000313|Proteomes:UP000018418} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CIP 110357 {ECO:0000313|EMBL:ESK51653.1, RC ECO:0000313|Proteomes:UP000018418}; RG The Broad Institute Genomics Platform; RG The Broad Institute Genome Sequencing Center for Infectious Disease; RA Cerqueira G., Feldgarden M., Courvalin P., Grillot-Courvalin C., RA Clermont D., Rocha E., Yoon E.-J., Nemec A., Young S.K., Zeng Q., RA Gargeya S., Fitzgerald M., Abouelleil A., Alvarado L., Berlin A.M., RA Chapman S.B., Gainer-Dewar J., Goldberg J., Gnerre S., Griggs A., RA Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A., Larimer J., RA McCowan C., Murphy C., Pearson M., Poon T.W., Priest M., Roberts A., RA Saif S., Shea T., Sykes S., Wortman J., Nusbaum C., Birren B.; RT "The Genome Sequence of Acinetobacter brisouii CIP 110357."; RL Submitted (OCT-2013) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:ESK51653.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AYEU01000006; ESK51653.1; -; Genomic_DNA. DR RefSeq; WP_004902049.1; NZ_KI530762.1. DR EnsemblBacteria; ESK51653; ESK51653; P255_02181. DR PATRIC; fig|1341683.3.peg.2156; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000018418; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000018418}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000018418}. FT DOMAIN 199 364 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 443 AA; 49634 MW; 4AD30DEFAA13A1DE CRC64; MEYFERHQGG ERAILVSVSV NMLNDLDDEE FSLLAKSAGA EILHHMTAQR VKPDPKLFVG SGKAEEIAAL VAELEAELVI FDHSLSPAQE RNLERILKCR VIDRTGLILD IFAQRARTHE GKLQVELAQL EHLSSRLVRG WTHLERQKGG IGLRGPGESQ LETDRRLLRI RMGQLKEKLE KVRQTRSQGR AARQKAAIPT VSLVGYTNAG KSTLFNILAE SEVYAADQLF ATLDPTLRRL NWDGIGALVL ADTVGFVRDL PHSLVESFKA TLEETLEATL LLHVIDSSSP DMLEQIDAVE SVLKEIGADV PVLRVYNKID LSGDEAKIIY AKPHQPERVY VSAHSQQGLA LLRQAVQECL MGQIQNFQLS LKPAYGKLRT QLYALNVIQS EHYDDHGNLL LDVIIAPHKL EELIKKLHLP LHEILGERAV QFQAPLEEFE IKP // ID V2Y6Y0_9FIRM Unreviewed; 414 AA. AC V2Y6Y0; DT 22-JAN-2014, integrated into UniProtKB/TrEMBL. DT 22-JAN-2014, sequence version 1. DT 07-JUN-2017, entry version 27. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=GCWU0000282_001447 {ECO:0000313|EMBL:ESL03456.1}; OS Catonella morbi ATCC 51271. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Lachnospiraceae; OC Catonella. OX NCBI_TaxID=592026 {ECO:0000313|EMBL:ESL03456.1, ECO:0000313|Proteomes:UP000018227}; RN [1] {ECO:0000313|EMBL:ESL03456.1, ECO:0000313|Proteomes:UP000018227} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51271 {ECO:0000313|EMBL:ESL03456.1, RC ECO:0000313|Proteomes:UP000018227}; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Nelson J., Hou S., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Nash W.E., Warren W., Chinwalla A., Mardis E.R., RA Wilson R.K.; RL Submitted (JUN-2013) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:ESL03456.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACIL03000011; ESL03456.1; -; Genomic_DNA. DR RefSeq; WP_023354326.1; NZ_KI535367.1. DR ProteinModelPortal; V2Y6Y0; -. DR EnsemblBacteria; ESL03456; ESL03456; GCWU0000282_001447. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000018227; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000018227}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000018227}. FT DOMAIN 198 362 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 157 191 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 414 AA; 45390 MW; 25E8E6CD380D7F3B CRC64; MIQTSEKKEK FILVGVETGK DRMEESLSEL AELLDTAGGE TVGRVIQNLE SINKATYVGK GKVEEIKEIA EELGADGIVC DDELSPAQLS NLKDELDIKV LDRTLVILDI FASHAKSSEG KLQVEMAQLK YRSSRLMGLG KNLSRLGGGI GTRGPGESKL ETDRRAIRER VSQLRTEIEK VESSRDTLRK HRMSDGIPVI AIVGYTNAGK STFLNKITDA GILAEDKLFA TLDPTTRSLK IPDGEEVLFT DTVGFISKLP HNLVDAFKST LEEAKYADLI LHVADASNPE VDEQMKVVYR TLEELKVVGK PVITFLNKQD KIGEGRIIKD LKADALVKGS AKTGEGIDEL LNKISEILRE GKVLVDTLLT YADTAKISVI RKKGQLLSEE YEGDGIRVKA YVPKAVAGQL GLLR // ID V2ZH09_9FIRM Unreviewed; 429 AA. AC V2ZH09; DT 22-JAN-2014, integrated into UniProtKB/TrEMBL. DT 22-JAN-2014, sequence version 1. DT 07-JUN-2017, entry version 26. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=N510_02092 {ECO:0000313|EMBL:ESL13695.1}; OS Firmicutes bacterium ASF500. OC Bacteria; Firmicutes. OX NCBI_TaxID=1378168 {ECO:0000313|EMBL:ESL13695.1, ECO:0000313|Proteomes:UP000017395}; RN [1] {ECO:0000313|EMBL:ESL13695.1, ECO:0000313|Proteomes:UP000017395} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ASF500 {ECO:0000313|EMBL:ESL13695.1, RC ECO:0000313|Proteomes:UP000017395}; RX PubMed=24723722; RA Wannemuehler M.J., Overstreet A.M., Ward D.V., Phillips G.J.; RT "Draft genome sequences of the altered schaedler flora, a defined RT bacterial community from gnotobiotic mice."; RL Genome Announc. 2:e00287-14(2014). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:ESL13695.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AYJP01000008; ESL13695.1; -; Genomic_DNA. DR RefSeq; WP_023347793.1; NZ_KI535333.1. DR EnsemblBacteria; ESL13695; ESL13695; N510_02092. DR PATRIC; fig|1378168.3.peg.2183; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000017395; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000017395}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000017395}. FT DOMAIN 204 365 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 429 AA; 47845 MW; AED43276DFAE89C7 CRC64; MPDIEKTQFN RAVLVGLNAF SLSREENADE ESMEELAALL ETAGGQCVGV VTQSKDSPDP RTFIGEGKVV EVKQLVEAAN ADMVIFDNPL SPSQQRNLAE ELKVGVLDRS ALILDIFAQR ARTREGRLQV ELAQYKYLLP RLLGMWKHLE RQEGAIGTRG PGETQLESDR RILGRKIAKL EGELKDVRRV RATQRERRIK NEVPVVAIVG YTNAGKSTLL NHLTGAEIPA NNRLFDTLDT TTRTLEISDT CTVLLSDTVG FIRKLPHHLV EAFKATLEEL EYADLLLHVI DSSSPQWREQ AEVVDQLIHE LGADQTPRIE VFNKCDLWTG DIRPHGEDRV SISAKTGEGV PDLLAAIGRV LDNGARRVTI HLPYDKGGLL DKLYLEAKVE NVDYGETIDV VAVCTPKVIG QLGPLVEGWK PRREFWEEP // ID V3TIA6_SERS3 Unreviewed; 426 AA. AC V3TIA6; DT 22-JAN-2014, integrated into UniProtKB/TrEMBL. DT 22-JAN-2014, sequence version 1. DT 30-AUG-2017, entry version 27. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=Ser39006_03989 {ECO:0000313|EMBL:ESN61582.1}; OS Serratia sp. (strain ATCC 39006). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; OC Yersiniaceae; Serratia. OX NCBI_TaxID=104623 {ECO:0000313|EMBL:ESN61582.1, ECO:0000313|Proteomes:UP000017700}; RN [1] {ECO:0000313|EMBL:ESN61582.1, ECO:0000313|Proteomes:UP000017700} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 39006 {ECO:0000313|EMBL:ESN61582.1, RC ECO:0000313|Proteomes:UP000017700}; RX PubMed=24336377; RA Fineran P.C., Iglesias Cans M.C., Ramsay J.P., Wilf N.M., RA Cossyleon D., McNeil M.B., Williamson N.R., Monson R.E., Becher S.A., RA Stanton J.A., Brugger K., Brown S.D., Salmond G.P.; RT "Draft genome sequence of Serratia sp. strain ATCC 39006, a model RT bacterium for analysis of the biosynthesis and regulation of RT prodigiosin, a carbapenem, and gas vesicles."; RL Genome Announc. 1:E01039-E01039(2013). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:ESN61582.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AWXH01000004; ESN61582.1; -; Genomic_DNA. DR RefSeq; WP_021017249.1; NZ_AWXH01000004.1. DR EnsemblBacteria; ESN61582; ESN61582; Ser39006_03989. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000017700; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000017700}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000017700}. FT DOMAIN 198 365 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 426 AA; 48248 MW; 52E881C590E08633 CRC64; MFDRYEAGEQ AILVHIYFSQ EKDTEDLLEF ESLVSSAGIE SLQVITGSRK APHPKYFVGE GKAEEIAQAV KATNAFVVLF DHALTPAQER NLERLCECRV VDRIGLILDI FAQRARTHEG KLQVELAQLR HLATRLVRGW THLERQKGGI GLRGPGETQL ETDRRLLRNR ISLILSRLTR VEKQREQGRR ARVRADVPTV SLVGYTNAGK STLFNQMTSA GVYAADQLFA TLDPTLRRIE VEDVGDTVLA DTVGFIRQLP HDLVAAFKAT LQETRQASLL LHVVDAADPR MDENIEAVEI VLAEIEADDI PMLQVMNKID MLEGFEPRID RNEDNVPVRV WLSAQTGVGI SLLFRALTER LSGEIVHYSL HLPPQAGRLR SRFYQLQAIE KEWIEEDGSV GLTVRMPIVD WRRLCKQEQE LKDYIV // ID V4B023_LOTGI Unreviewed; 423 AA. AC V4B023; DT 22-JAN-2014, integrated into UniProtKB/TrEMBL. DT 22-JAN-2014, sequence version 1. DT 07-JUN-2017, entry version 22. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:ESO99351.1}; DE Flags: Fragment; GN ORFNames=LOTGIDRAFT_113712 {ECO:0000313|EMBL:ESO99351.1}; OS Lottia gigantea (Giant owl limpet). OC Eukaryota; Metazoa; Lophotrochozoa; Mollusca; Gastropoda; OC Patellogastropoda; Lottioidea; Lottiidae; Lottia. OX NCBI_TaxID=225164 {ECO:0000313|EMBL:ESO99351.1, ECO:0000313|Proteomes:UP000030746}; RN [1] {ECO:0000313|EMBL:ESO99351.1, ECO:0000313|Proteomes:UP000030746} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=23254933; DOI=10.1038/nature11696; RA Simakov O., Marletaz F., Cho S.J., Edsinger-Gonzales E., Havlak P., RA Hellsten U., Kuo D.H., Larsson T., Lv J., Arendt D., Savage R., RA Osoegawa K., de Jong P., Grimwood J., Chapman J.A., Shapiro H., RA Aerts A., Otillar R.P., Terry A.Y., Boore J.L., Grigoriev I.V., RA Lindberg D.R., Seaver E.C., Weisblat D.A., Putnam N.H., Rokhsar D.S.; RT "Insights into bilaterian evolution from three spiralian genomes."; RL Nature 493:526-531(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; KB201037; ESO99351.1; -; Genomic_DNA. DR RefSeq; XP_009049842.1; XM_009051594.1. DR EnsemblMetazoa; LotgiT113712; LotgiP113712; LotgiG113712. DR GeneID; 20231000; -. DR KEGG; lgi:LOTGIDRAFT_113712; -. DR CTD; 20231000; -. DR OMA; MDTVGFM; -. DR OrthoDB; EOG091G0852; -. DR Proteomes; UP000030746; Unassembled WGS sequence. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR CDD; cd01878; HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 4: Predicted; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000030746}; KW Reference proteome {ECO:0000313|Proteomes:UP000030746}. FT DOMAIN 199 365 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 168 192 {ECO:0000256|SAM:Coils}. FT NON_TER 1 1 {ECO:0000313|EMBL:ESO99351.1}. SQ SEQUENCE 423 AA; 48248 MW; 6DEA73CAA43FE340 CRC64; YFFYLDVKWG PHKNKLTSST LRLEETCTLV ETLPNWKVVE KKLVSVKFLK SDQIFQKEKF RQLKSEIRQN IRISGVLVGV DLLSSVQLAA LQKAWRVPVF DRYAIVLQIF KDHARTKESK LQIALAEIPF LRKRLGQVHQ GIFDKQIGDS RFIGGTGPVH ISRRKLMLQE RENKIRLALE KIERQRDLLR NNRLKKEFMS VAVVGYTNSG KTTLIKALTG DNKLEPKDML FATLDVTVHA GVLPNYMKTL YVDTVGFISD IPTNLIQAFS ATLEDALIAD VIIHIRDISH PDTSGQKHNV LDTLSSILPP DRLHSIIEVC NKTDLVPLEK LQEEKENDKL FVSAATGQGL QDLQLQIQQK LITVTGKLYK TFRIPNGGAE LSWLYKEATV QNIEADKDCN YLIVETIISP AVYQRFTSYF QQT // ID V4J2V9_9ACTN Unreviewed; 496 AA. AC V4J2V9; DT 22-JAN-2014, integrated into UniProtKB/TrEMBL. DT 22-JAN-2014, sequence version 1. DT 07-JUN-2017, entry version 23. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=B590_06049 {ECO:0000313|EMBL:ESQ06705.1}; OS Streptomyces sp. PVA 94-07. OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae; OC Streptomyces. OX NCBI_TaxID=1223307 {ECO:0000313|EMBL:ESQ06705.1, ECO:0000313|Proteomes:UP000017765}; RN [1] {ECO:0000313|EMBL:ESQ06705.1, ECO:0000313|Proteomes:UP000017765} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=PVA 94-07 {ECO:0000313|EMBL:ESQ06705.1, RC ECO:0000313|Proteomes:UP000017765}; RA Ian E., Sekurova O.N., Malko D.B., Ruckert C., Borisova M.E., RA Albersmeier A., Kalinowski J., Gelfand M.S., Zotchev S.B.; RT "Draft sequence of Streptomyces sp. PVA 94-07, a marine actinomycete RT isolated from the sponge Phakellia ventilabrum collected in the RT Trondheim fjord (Norway)."; RL Submitted (MAY-2013) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:ESQ06705.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ASHE01000006; ESQ06705.1; -; Genomic_DNA. DR EnsemblBacteria; ESQ06705; ESQ06705; B590_06049. DR PATRIC; fig|1223307.4.peg.1262; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000017765; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 2. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000017765}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000017765}. FT DOMAIN 275 440 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 496 AA; 53899 MW; 040E80F14B40BFB7 CRC64; MQHPHDATGP DAEPQAESLR ADALMEEDVA WSHTVDGERD GDQYDRSERA ALRRVAGLST ELEDVTEVEY RQLRLERVVL VGVWTSGTAE DADRSLAELA ALAETAGALV LDGVVQRRDK PDPATYIGSG KAQELYDIVR DSGADTVVCD GELSPGQLIH LEDVVKVKVV DRTALILDIF AQHAKSREGK AQVSLAQMQY MLPRLRGWGQ SLSRQMGGGG TSGGGGMATR GPGETKIETD RRRIREKMAK MRREIAAMKT GRELKRQERR RNKVPSVAIA GYTNAGKSSL LNRLTGAGVL VENALFATLD PTVRRAETPS GRLYTLADTV GFVRHLPHHL VEAFRSTMEE VGDSDLILHV VDGAHPAPEE QLAAVREVIR DVGAVNVPEI VVVNKADAAD PLVLQRLLRV EKHAIAVSAR TGAGIGELLG MIDEILPRPE VELEALIPYT QGQLVARAHA EGEVLSEEHT AEGTVLKVRV HRELAAELST FELATS // ID V4J5R1_9DELT Unreviewed; 329 AA. AC V4J5R1; DT 22-JAN-2014, integrated into UniProtKB/TrEMBL. DT 22-JAN-2014, sequence version 1. DT 07-JUN-2017, entry version 22. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=N839_05050 {ECO:0000313|EMBL:ESQ09769.1}; OS uncultured Desulfofustis sp. PB-SRB1. OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfobacterales; OC Desulfobulbaceae; Desulfofustis; environmental samples. OX NCBI_TaxID=1385624 {ECO:0000313|EMBL:ESQ09769.1, ECO:0000313|Proteomes:UP000017917}; RN [1] {ECO:0000313|EMBL:ESQ09769.1, ECO:0000313|Proteomes:UP000017917} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Wilbanks E.G., Jaekel U., Salman V., Humphrey P.T., Eisen J.A., RA Facciotti M.T., Buckley D.H., Zinder S.H., Druschel G.K., Fike D.A., RA Orphan V.J.; RT "A sulfurous symbiosis: microscale sulfur cycling in the pink berry RT consortia of the Sippewissett salt marsh."; RL Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:ESQ09769.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AVFQ01000266; ESQ09769.1; -; Genomic_DNA. DR PATRIC; fig|1385624.3.peg.2706; -. DR Proteomes; UP000017917; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000017917}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000017917}. FT DOMAIN 141 322 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 100 127 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 329 AA; 36822 MW; 050B4960AE9702A3 CRC64; MGRGKLSEII IRALRLDANL LIFSRELNPS QIRSITEFTD LRVIDRTQLI LDIFARRARS REGKLQVEMA QLKYMLPRLS TRDDALSRLT GGIGARGPGE TKLEIDRRRI NDRLARLTRE LASVGSERSR RRNRRRKRTV PVISLVGYTN AGKSTLLNTL TRSEVVAEDK LFATLDPTSR RLRFPEEMEV IISDTVGFID DLPADLLRAF QATLEELNEA DLLIHVIDAA NPAHTTHVEV VEKLLGELDL LAIPRIDVYN KIDLVDQSEP DSEGAVPSSA MISTSEPKSL SLDGSSIAIC AHDPDSLAPL LRRAYEMLRE IVPPELMAS // ID V4JET5_9DELT Unreviewed; 252 AA. AC V4JET5; DT 22-JAN-2014, integrated into UniProtKB/TrEMBL. DT 22-JAN-2014, sequence version 1. DT 07-JUN-2017, entry version 13. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:ESQ10815.1}; DE Flags: Fragment; GN ORFNames=N839_18050 {ECO:0000313|EMBL:ESQ10815.1}; OS uncultured Desulfofustis sp. PB-SRB1. OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfobacterales; OC Desulfobulbaceae; Desulfofustis; environmental samples. OX NCBI_TaxID=1385624 {ECO:0000313|EMBL:ESQ10815.1, ECO:0000313|Proteomes:UP000017917}; RN [1] {ECO:0000313|EMBL:ESQ10815.1, ECO:0000313|Proteomes:UP000017917} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Wilbanks E.G., Jaekel U., Salman V., Humphrey P.T., Eisen J.A., RA Facciotti M.T., Buckley D.H., Zinder S.H., Druschel G.K., Fike D.A., RA Orphan V.J.; RT "A sulfurous symbiosis: microscale sulfur cycling in the pink berry RT consortia of the Sippewissett salt marsh."; RL Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:ESQ10815.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AVFQ01000182; ESQ10815.1; -; Genomic_DNA. DR PATRIC; fig|1385624.3.peg.1893; -. DR Proteomes; UP000017917; Unassembled WGS sequence. DR InterPro; IPR025121; GTPase_HflX_N. DR Pfam; PF13167; GTP-bdg_N; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000017917}; KW Reference proteome {ECO:0000313|Proteomes:UP000017917}. FT DOMAIN 196 251 GTP-bdg_N. {ECO:0000259|Pfam:PF13167}. FT NON_TER 252 252 {ECO:0000313|EMBL:ESQ10815.1}. SQ SEQUENCE 252 AA; 28558 MW; 5C9A799CBAEC2322 CRC64; MKKSQLKALN RLGSRNISRD DIVSPEAART MAELSFEMNR QVGLLINRSG KIEQVIIGDY HGLFIPRESV RNNTGGRLCG LRLVHTHPGG ENISDDDLMD LLFLRLDLMA VLKLDQHGLP ERIYSAHLMP LSMDGANWQY LEPLHPANQK DSIYELIQAL ENEFSRIKQT GRAEAGRDRA LLISVGTESR SRAEPAMREL MELARSSEIV VLDSIYQRSR TINPRFIMGR GKLSEIIIRA LRLDANLLIF SR // ID V4JFI6_9GAMM Unreviewed; 442 AA. AC V4JFI6; DT 22-JAN-2014, integrated into UniProtKB/TrEMBL. DT 22-JAN-2014, sequence version 1. DT 07-JUN-2017, entry version 23. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=N838_11490 {ECO:0000313|EMBL:ESQ14471.1}; OS uncultured Thiohalocapsa sp. PB-PSB1. OC Bacteria; Proteobacteria; Gammaproteobacteria; Chromatiales; OC Chromatiaceae; Thiohalocapsa; environmental samples. OX NCBI_TaxID=1385625 {ECO:0000313|EMBL:ESQ14471.1, ECO:0000313|Proteomes:UP000017935}; RN [1] {ECO:0000313|EMBL:ESQ14471.1, ECO:0000313|Proteomes:UP000017935} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Wilbanks E.G., Jaekel U., Salman V., Humphrey P.T., Eisen J.A., RA Facciotti M.T., Buckley D.H., Zinder S.H., Druschel G.K., Fike D.A., RA Orphan V.J.; RT "A sulfurous symbiosis: microscale sulfur cycling in the pink berry RT consortia of the Sippewissett salt marsh."; RL Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:ESQ14471.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AVFR01000631; ESQ14471.1; -; Genomic_DNA. DR PATRIC; fig|1385625.5.peg.4130; -. DR Proteomes; UP000017935; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000017935}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000017935}. FT DOMAIN 197 364 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 442 AA; 48777 MW; 409547599DEF0A7D CRC64; MSVQVPVNGP FLVQLAIGHA ADDDAMLEFR LLAKAAGALE VGYLTGNRDR PDPRLFIGSG KADELRSLIE ATRAELAIFD HALSPAQERN LERLLQCRVV ERSGLILDIF AQRARSFEGK LQVELAQLRH LSTRLVRGWT HLERQKGGIG LRGPGETQLE TDRRLLGQRI TQLKARLSRI ETRQAQARRA RERADVSTVA LVGYTNAGKS TLFNQLTEAG VFQADQLFAT LDPTLRRLAL PNAPAIVLAD TVGFVNQLPH ELVAAFRSTL QETRSADLLL HVVDASNDQR DRRIADVDTV LEEIGARDIP VISVFNKIDM LPVSEPRIDR GEDGLVNRVW LSAATGAGVE LLPQVLADYF CGESLRQQLR LGPADGSLRA WLFDHAIVVS ESPTEQGGWD IEVQISRAQH DRYLLDPERW AGRLVSQCPA PAGANRDSEN SA // ID V4LRW4_EUTSA Unreviewed; 543 AA. AC V4LRW4; DT 22-JAN-2014, integrated into UniProtKB/TrEMBL. DT 22-JAN-2014, sequence version 1. DT 07-JUN-2017, entry version 19. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:ESQ42598.1}; GN ORFNames=EUTSA_v10013185mg {ECO:0000313|EMBL:ESQ42598.1}; OS Eutrema salsugineum (Saltwater cress) (Sisymbrium salsugineum). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae; OC Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Eutremeae; OC Eutrema. OX NCBI_TaxID=72664 {ECO:0000313|EMBL:ESQ42598.1, ECO:0000313|Proteomes:UP000030689}; RN [1] {ECO:0000313|EMBL:ESQ42598.1, ECO:0000313|Proteomes:UP000030689} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=23518688; DOI=10.3389/fpls.2013.00046; RA Yang R., Jarvis D.E., Chen H., Beilstein M.A., Grimwood J., RA Jenkins J., Shu S., Prochnik S., Xin M., Ma C., Schmutz J., Wing R.A., RA Mitchell-Olds T., Schumaker K.S., Wang X.; RT "The Reference Genome of the Halophytic Plant Eutrema salsugineum."; RL Front. Plant Sci. 4:46-46(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; KI517464; ESQ42598.1; -; Genomic_DNA. DR RefSeq; XP_006401145.1; XM_006401082.1. DR GeneID; 18016958; -. DR KEGG; eus:EUTSA_v10013185mg; -. DR KO; K03665; -. DR Proteomes; UP000030689; Unassembled WGS sequence. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000030689}; KW Reference proteome {ECO:0000313|Proteomes:UP000030689}. FT DOMAIN 313 479 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 543 AA; 61028 MW; 3A0F308508B103B8 CRC64; MSSFSFSSSS PVSKFQWRAN YNPQPNRPIV PFTLSLLRGN CYSWRLSCNL TQQHGLDFEE SVEQDEIPQF LDFSAAEEPD MEKATIDAPC TTLRKKKRGE ESLDDRFKLR NGKEVFEEKA YLVGVERKGD GECLFNIEES LEELEQLADT AGLMVVGSTY QKLASPNPRT YIGSGKVSEI KSAIHALDVE TVIFDDELSP GQLRNLEKAF GGDVRVCDRT ALILDIFNQR AATHEAALQV ALAQMEYQLP RLTRMWTHLE RQSGGQVKGM GEKQIEVDKR ILRTQIGVLK KELESVRKHR KQYRSRRVAI PVPVVSLVGY TNAGKSTLLN QLTGANVLAE NRLFATLDPT TRRVQMHNGK EFLLTDTVGF IQKLPTTLVA AFRATLEEIS ESCLLVHVVD ISHPLANQQI EAVEKVMSEL DVSSIPNLVV WNKVDRVDDP QKVKLEAEKS GDVICISALT GEGLDKFCNA VQEKLKDSMV WVEALLPFDK GDLLSTIHKV GMVKETEYTE NGTLIRAHVP LRFAQLLKPM RHLVKDTSLC KER // ID V4NHB6_EUTSA Unreviewed; 580 AA. AC V4NHB6; DT 22-JAN-2014, integrated into UniProtKB/TrEMBL. DT 22-JAN-2014, sequence version 1. DT 07-JUN-2017, entry version 17. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:ESQ45561.1}; GN ORFNames=EUTSA_v10010236mg {ECO:0000313|EMBL:ESQ45561.1}; OS Eutrema salsugineum (Saltwater cress) (Sisymbrium salsugineum). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae; OC Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Eutremeae; OC Eutrema. OX NCBI_TaxID=72664 {ECO:0000313|EMBL:ESQ45561.1, ECO:0000313|Proteomes:UP000030689}; RN [1] {ECO:0000313|EMBL:ESQ45561.1, ECO:0000313|Proteomes:UP000030689} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=23518688; DOI=10.3389/fpls.2013.00046; RA Yang R., Jarvis D.E., Chen H., Beilstein M.A., Grimwood J., RA Jenkins J., Shu S., Prochnik S., Xin M., Ma C., Schmutz J., Wing R.A., RA Mitchell-Olds T., Schumaker K.S., Wang X.; RT "The Reference Genome of the Halophytic Plant Eutrema salsugineum."; RL Front. Plant Sci. 4:46-46(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; KI517435; ESQ45561.1; -; Genomic_DNA. DR RefSeq; XP_006404108.1; XM_006404045.1. DR GeneID; 18021306; -. DR KEGG; eus:EUTSA_v10010236mg; -. DR Proteomes; UP000030689; Unassembled WGS sequence. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR CDD; cd01878; HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 2. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000030689}; KW Reference proteome {ECO:0000313|Proteomes:UP000030689}. FT DOMAIN 305 547 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 580 AA; 64918 MW; 36C48A1CB8AB5132 CRC64; MLKTLSLARD RLRSKAPLSS SPTSSSFTFR VLSSPFSSKR HAPKASKEEE PPLKESVLLY PKDPSSTPKL FLVQPRLSPP KFLQAKLNEA LCLANSLEEQ RHGYFESDFF DKELPSHVVV QNPVARSPKA HVDTYFGSGT VDNIKCHLNA EDSKEEVDAV FVNAILSAVQ QRNLERIWEK PVLDRVGLII EIFNAHAHTK EAKLQAELAA LMYKRSRLVR VRGTDGKQTF GQFGEAEVVS ARGRAASKGS GFVGGAGETE LQLQRRRISD RKLRLLSQIK DARRTRLLQR AARRRQGGLE GKSLATIAVV GYTNAGKSTL TSALTRTALY CNERLFATLD PTLKSAILPS RRKVLLSDTV GFISDLPIQL VEAFQSTLEE VVEADLLLHV VDSTAPNIEE HRSTVFHVLN QIGVPEEKLK NMIEVWNKID YEEEEEQVED MHYLDDGKGE EEEEEAAELI DGSIAEETLE ASEAAVEEDQ IENQEDDSDG WLLSDENVSD SELWKVPEDA KLVAAQKNGP DVRVSALTGV GLKELMYLID ERLKGEDDKL RSQTVVERSE LQSRKWRPPR KDDEELAVEQ // ID V4NMD7_9CAUL Unreviewed; 441 AA. AC V4NMD7; DT 22-JAN-2014, integrated into UniProtKB/TrEMBL. DT 22-JAN-2014, sequence version 1. DT 07-JUN-2017, entry version 26. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=AEAC466_15820 {ECO:0000313|EMBL:ESQ82972.1}; OS Asticcacaulis sp. AC466. OC Bacteria; Proteobacteria; Alphaproteobacteria; Caulobacterales; OC Caulobacteraceae; Asticcacaulis. OX NCBI_TaxID=1282362 {ECO:0000313|EMBL:ESQ82972.1, ECO:0000313|Proteomes:UP000017826}; RN [1] {ECO:0000313|EMBL:ESQ82972.1, ECO:0000313|Proteomes:UP000017826} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=AC466 {ECO:0000313|EMBL:ESQ82972.1, RC ECO:0000313|Proteomes:UP000017826}; RX PubMed=24463524; DOI=10.1038/nature12900; RA Jiang C., Brown P.J., Ducret A., Brun Y.V.; RT "Sequential evolution of bacterial morphology by co-option of a RT developmental regulator."; RL Nature 506:489-493(2014). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:ESQ82972.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AWGE01000015; ESQ82972.1; -; Genomic_DNA. DR RefSeq; WP_023459156.1; NZ_AWGE01000015.1. DR EnsemblBacteria; ESQ82972; ESQ82972; AEAC466_15820. DR PATRIC; fig|1282362.3.peg.3127; -. DR Proteomes; UP000017826; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000017826}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000017826}. FT DOMAIN 212 385 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 178 205 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 441 AA; 49411 MW; 8B4B0A07B5351509 CRC64; MSDKYIDHAP DIVRAIVVDP DIDTHARSEA SPARKYDYSR LEEAVGLALA LDLEIVGEMS VRVRKINPAT LFGQGKVADI KTACEDNDAS LCVVNGALTP IQQRNLEKDL GVKVVDRTGL ILEIFGRRAR TNEGKLQVEL ARLEYERSRL VRTWTHLERQ RATGTTGGPG ETQIELDRRM IADKIKQLKT ELEDVRRTRA LHRNQRKKVP YPIVALVGYT NAGKSTLFNN LTKSEVFAKD LLFATLDTTL RSLKLPNGRS AILSDTVGFI SDLPHELVAA FRATLEEVEQ ADLILHVRDV SNPETEAQKA DVEQVMAHIL PDLDRSRMIE VWNKIDLLDA ESKDILYSRA ITDRSKNKPL LVSAITGEGV PHLLREVALL VDADGEEIDI VIEPHQGELL AFLYAHGRVL GRHEDDDGRV HLCVKLSDQA YGRYEKMVEG R // ID V4Q3H1_9CAUL Unreviewed; 446 AA. AC V4Q3H1; DT 22-JAN-2014, integrated into UniProtKB/TrEMBL. DT 22-JAN-2014, sequence version 1. DT 07-JUN-2017, entry version 27. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=ABENE_01645 {ECO:0000313|EMBL:ESQ94239.1}; OS Asticcacaulis benevestitus DSM 16100 = ATCC BAA-896. OC Bacteria; Proteobacteria; Alphaproteobacteria; Caulobacterales; OC Caulobacteraceae; Asticcacaulis. OX NCBI_TaxID=1121022 {ECO:0000313|EMBL:ESQ94239.1, ECO:0000313|Proteomes:UP000017837}; RN [1] {ECO:0000313|EMBL:ESQ94239.1, ECO:0000313|Proteomes:UP000017837} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 16100 {ECO:0000313|EMBL:ESQ94239.1, RC ECO:0000313|Proteomes:UP000017837}; RX PubMed=24463524; DOI=10.1038/nature12900; RA Jiang C., Brown P.J., Ducret A., Brun Y.V.; RT "Sequential evolution of bacterial morphology by co-option of a RT developmental regulator."; RL Nature 506:489-493(2014). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:ESQ94239.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AWGB01000004; ESQ94239.1; -; Genomic_DNA. DR RefSeq; WP_018080168.1; NZ_AWGB01000004.1. DR EnsemblBacteria; ESQ94239; ESQ94239; ABENE_01645. DR PATRIC; fig|1121022.4.peg.328; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000017837; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000017837}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000017837}. FT DOMAIN 216 392 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 182 209 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 446 AA; 49773 MW; 465E7CDA7E3AD6A0 CRC64; MTDRFHDNAP EIVRAVVVDP DIDVHVSARH SGDTAVARKY DDSRLEEAVG LAMALDLEIT GTLSVRVRKL NPATLFGEGK VNEIKALCEE AEASLCVVNG SLSPIQQRNL EKALDVKVVD RTGLILEIFG RRARTGEGKL QVELARLEYE RSRLVRTWTH LERQRATGTT GGPGETQIEL DRRMIADKIK QLKSELEEVR RTRGLHRNQR KKVPYPIVAL VGYTNAGKST LFNNLTKSEV FAKDLLFATL DTTLRSLKLP NGRSAILSDT VGFISDLPHE LVAAFRATLE EVEQADLILH VRDVSNPETE AQKSDVEQVM AHILPDLDRS RMVEVWNKID LLDDESKDIL YSRAITDRAG NKPLLVSAIT GEGVANLLQQ IALLVDAAGE EMDITLEPHQ GDVVAFLYQH GRVLGRHEDE DGRTHLRVKL SDQAYGRYER MLTGKS // ID V4QV79_STRIN Unreviewed; 414 AA. AC V4QV79; DT 22-JAN-2014, integrated into UniProtKB/TrEMBL. DT 22-JAN-2014, sequence version 1. DT 07-JUN-2017, entry version 25. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=IUSA1_02285 {ECO:0000313|EMBL:ESR10317.1}; OS Streptococcus iniae IUSA1. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=1273539 {ECO:0000313|EMBL:ESR10317.1, ECO:0000313|Proteomes:UP000017720}; RN [1] {ECO:0000313|EMBL:ESR10317.1, ECO:0000313|Proteomes:UP000017720} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=IUSA1 {ECO:0000313|EMBL:ESR10317.1}; RX PubMed=23516181; RA El Aamri F., Acosta F., Real F., Padilla D.; RT "Whole-Genome Sequence of the Fish Virulent Strain Streptococcus iniae RT IUSA-1, Isolated from Gilthead Sea Bream (Sparus aurata) and Red Porgy RT (Pagrus pagrus)."; RL Genome Announc. 1:E0002513-E0002513(2013). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:ESR10317.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AOCT02000010; ESR10317.1; -; Genomic_DNA. DR RefSeq; WP_003099188.1; NZ_AOCT02000010.1. DR EnsemblBacteria; ESR10317; ESR10317; IUSA1_02285. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000017720; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000017720}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000017720}. FT DOMAIN 201 361 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 167 194 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 414 AA; 47210 MW; 089A8855832EAD08 CRC64; MVLTETKREK ERVIVLGVEL QNTENFAMSM EELASLAKTA GAEVISSYSQ KRDKYDSKTF IGSGKLAELK EIVDAEEIDT VIVNNRLTPR QNSNLEAEMG VKVIDRMQLI LDIFAMRAKS HEGKLQVHLA QLKYMLPRLV GQGVMLSRQA GGIGSRGPGE SQLELNRRSI RHQITDIERQ LAIVEKNRQT IRDKRLASDT FKIGLIGYTN AGKSTIMNVL TENSHYEANE LFATLDATTK QIYLQNQFQA TLTDTVGFIQ DLPTELVAAF KSTLEESKHV DLLLHVIDAS DPNHAEHEKV VTTILRDLDM LQIPRLAIYN KMDQVDYLRA TAFPNVRVSA KDPKSRDTLR RLLIDQIRDI FEPFSVKVSQ EKLYKLYELH KIALLDHYSF EDEIEEISGY IAAKNKWRLE ELYD // ID V4SFN0_9ROSI Unreviewed; 603 AA. AC V4SFN0; DT 22-JAN-2014, integrated into UniProtKB/TrEMBL. DT 22-JAN-2014, sequence version 1. DT 07-JUN-2017, entry version 16. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:ESR39387.1}; GN ORFNames=CICLE_v10025205mg {ECO:0000313|EMBL:ESR39387.1}; OS Citrus clementina. OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae; OC Pentapetalae; rosids; malvids; Sapindales; Rutaceae; Aurantioideae; OC Citrus. OX NCBI_TaxID=85681 {ECO:0000313|EMBL:ESR39387.1, ECO:0000313|Proteomes:UP000030687}; RN [1] {ECO:0000313|EMBL:ESR39387.1, ECO:0000313|Proteomes:UP000030687} RP NUCLEOTIDE SEQUENCE. RG International Citrus Genome Consortium; RA Jenkins J., Schmutz J., Prochnik S., Rokhsar D., Gmitter F., RA Ollitrault P., Machado M., Talon M., Wincker P., Jaillon O., RA Morgante M.; RL Submitted (OCT-2013) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; KI536925; ESR39387.1; -; Genomic_DNA. DR RefSeq; XP_006426147.1; XM_006426084.1. DR GeneID; 18037594; -. DR KEGG; cic:CICLE_v10025205mg; -. DR Proteomes; UP000030687; Unassembled WGS sequence. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR CDD; cd01878; HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 2. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000030687}; KW Reference proteome {ECO:0000313|Proteomes:UP000030687}. FT DOMAIN 304 429 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 603 AA; 67300 MW; 189F0C9A4B894ED6 CRC64; MGLKIYIARY LSPAPLNFVR LRPSVAFASD QPGPPLRPSQ RRQTKDNKDK DDLHDVVTLF NRDPDDPPRL FLVQPRLKPP TFLQAKLNEA LCLANSLEEQ RDGYFDTDFF DKELPPHVVV QNPSLKSGKA RADTFFGPGT VETIKCHING AESKGELDAI FVNAILSGIQ QRNLERAWGK PVLDRVGLII EIFNAHAHTK EAKLQAELAA LMYKKSRLVR VRGPDGRLTF GETGEAEVVS ARGRGSGGRG FISGAGETEL QLQRRRILER RSHLLSQIEE VRRTRAVQRA ARRRHGGSDG RGLATVAVVG YTNAGKSTLV GALSDSDLFS DARLFATLDP RLKSVVLPSG RKVLLSDTVG FISDLPLQLV DAFHATLEEV VEADLLVHVL DCTAPNLEEH RTTVLQVLQQ VGVSEEKLKN MIEVWNKIDY HDEEMGDVEY IDGDDISNFS RAEDEVMTSE PVDVECIDNY GGDDADNNDG FVSEDLGESI NKNHNDYSDG WLLSGDEQDN VEEEFWKAAE DQQPESTKDV CVMEKDSQSQ DQHAPDVKIS ARTGVGLREL LEIIDERLKT LDDKQKSPNV VERDFFNKKW RPPRTEDSSV AVQ // ID V4TN97_9RHIZ Unreviewed; 463 AA. AC V4TN97; DT 22-JAN-2014, integrated into UniProtKB/TrEMBL. DT 22-JAN-2014, sequence version 1. DT 07-JUN-2017, entry version 27. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=N177_0177 {ECO:0000313|EMBL:ESR27198.1}; OS Lutibaculum baratangense AMV1. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Rhodobiaceae; Lutibaculum. OX NCBI_TaxID=631454 {ECO:0000313|EMBL:ESR27198.1, ECO:0000313|Proteomes:UP000017819}; RN [1] {ECO:0000313|EMBL:ESR27198.1, ECO:0000313|Proteomes:UP000017819} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=AMV1 {ECO:0000313|EMBL:ESR27198.1, RC ECO:0000313|Proteomes:UP000017819}; RX PubMed=25059877; RA Singh A., Sreenivas A., Sathyanarayana Reddy G., Pinnaka A.K., RA Shivaji S.; RT "Draft Genome Sequence of Lutibaculum baratangense Strain AMV1T, RT Isolated from a Mud Volcano in Andamans, India."; RL Genome Announc. Announc.2:e00735-14(2014). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:ESR27198.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AWXZ01000007; ESR27198.1; -; Genomic_DNA. DR RefSeq; WP_023430334.1; NZ_AWXZ01000007.1. DR EnsemblBacteria; ESR27198; ESR27198; N177_0177. DR PATRIC; fig|631454.5.peg.175; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000017819; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000017819}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000017819}. FT DOMAIN 231 403 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 463 AA; 51644 MW; D7296FC9EB644E70 CRC64; MKPRDSDVHD PAEGEVEPRP VTEETKQKPT RTLVLVPVLE RGAAASGPAV NARSPDARLE EACGLAEAIA LEVVDRGTVR VTQVRPATLI GTGKVDEIAG SIKAQEIELV VVDHPLSPVQ QRNLERAWKA KVLDRTGLIL EIFGERARTK EGRLQVELAH LNWQKSRLVR SWTHLERQRG GFGFLGGPGE TQIEADRRII QDRIRRIEAD LKDVQRTRGL HRESRRRVPY PVLALVGYTN AGKSTLFNRL TKADVMAENL LFATLDPTLR EIKLPTGRPA ILSDTVGFIS DLPTHLVAAF RATLEEVIEA DVVVHVRDIS HPDSETQAKD VMNVLKALGV DVEDEKHIIE VYNKIDLLSP EAREALLARR ERESLEGIPV SAVTGEGIDQ LLATISERLG KEEILRRIRL AGTRGQDLNW LYERCEVVER VDDPETGETA VTIRVPPQRL PEFERRFGAL VEG // ID V4V858_9ROSI Unreviewed; 545 AA. AC V4V858; DT 22-JAN-2014, integrated into UniProtKB/TrEMBL. DT 22-JAN-2014, sequence version 1. DT 07-JUN-2017, entry version 17. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:ESR48304.1}; GN ORFNames=CICLE_v10000772mg {ECO:0000313|EMBL:ESR48304.1}; OS Citrus clementina. OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae; OC Pentapetalae; rosids; malvids; Sapindales; Rutaceae; Aurantioideae; OC Citrus. OX NCBI_TaxID=85681 {ECO:0000313|EMBL:ESR48304.1, ECO:0000313|Proteomes:UP000030687}; RN [1] {ECO:0000313|EMBL:ESR48304.1, ECO:0000313|Proteomes:UP000030687} RP NUCLEOTIDE SEQUENCE. RG International Citrus Genome Consortium; RA Jenkins J., Schmutz J., Prochnik S., Rokhsar D., Gmitter F., RA Ollitrault P., Machado M., Talon M., Wincker P., Jaillon O., RA Morgante M.; RL Submitted (OCT-2013) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; KI536799; ESR48304.1; -; Genomic_DNA. DR RefSeq; XP_006435064.1; XM_006435001.1. DR GeneID; 18042163; -. DR KEGG; cic:CICLE_v10000772mg; -. DR KO; K03665; -. DR Proteomes; UP000030687; Unassembled WGS sequence. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000030687}; KW Reference proteome {ECO:0000313|Proteomes:UP000030687}. FT DOMAIN 322 488 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 545 AA; 60796 MW; 7311229DDDA899F6 CRC64; MSFSLCSLTP VSPQIHERNS QWSQNAKRSI FRLSLTNNSS RCICRVVEQG LEVEVASADT APQKQGPVID TKEEEEQQQE VFNGVATTES DNKALNSSYT AKKKKRDDDD SYENRFKLQN GREVFQEKSY LVGVERKGGA EYLFVIEESL KELAQLADTA GLMVVGSTHQ KLNSPNPRTY IGSGKVAEIK SAIHALGVET VIFDDELSAG QLRNLEKAFG GDVRVCDRTA LILDIFNQRA ATHEAALQVA LAQMEYQLPR LTKMWTHLER QAGGQVKGMG EKQIEVDKRI LRTQIGVLKK ELESVRKHRK QYRNRRVSVP VPVVSLVGYT NAGKSTLLNR LTGATVLAED RLFATLDPTT RRVQMKNGGE FLLTDTVGFI QKLPTTLVAA FRATLEEISE SSLLVHVVDI SHPLAEQQIE AVDKVLSELD VSSIPKLMIW NKVDKVCDPQ KVKLEAQKRE DVVCISALSG NGLDEFCSAV QEKLKDSMVW VEALVPFDKG ELLSTIHQVG MVERTEYTEN GTLVKAHVPL RFARLLTPMR QMCIS // ID V4XB05_9ARCH Unreviewed; 460 AA. AC V4XB05; DT 22-JAN-2014, integrated into UniProtKB/TrEMBL. DT 22-JAN-2014, sequence version 1. DT 07-JUN-2017, entry version 16. DE SubName: Full=GTPase {ECO:0000313|EMBL:ESS05059.1}; GN ORFNames=A07HR67_00039 {ECO:0000313|EMBL:ESS05059.1}; OS uncultured archaeon A07HR67. OC Archaea; environmental samples. OX NCBI_TaxID=1412871 {ECO:0000313|EMBL:ESS05059.1, ECO:0000313|Proteomes:UP000030660}; RN [1] {ECO:0000313|Proteomes:UP000030660} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=24335829; RA Podell S., Emerson J.B., Jones C.M., Ugalde J.A., Welch S., RA Heidelberg K.B., Banfield J.F., Allen E.E.; RT "Seasonal fluctuations in ionic concentrations drive microbial RT succession in a hypersaline lake community."; RL ISME J. 0:0-0(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; KI543154; ESS05059.1; -; Genomic_DNA. DR PATRIC; fig|1412871.3.peg.37; -. DR OrthoDB; POG093Z07D6; -. DR Proteomes; UP000030660; Unassembled WGS sequence. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR SUPFAM; SSF52540; SSF52540; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000030660}; KW Reference proteome {ECO:0000313|Proteomes:UP000030660}. FT DOMAIN 37 120 GTP-bdg_N. {ECO:0000259|Pfam:PF13167}. FT DOMAIN 126 196 GTP-bdg_M. {ECO:0000259|Pfam:PF16360}. FT DOMAIN 204 342 G (guanine nucleotide-binding). FT {ECO:0000259|Pfam:PF01926}. SQ SEQUENCE 460 AA; 48523 MW; 000D93F7AFBB80AE CRC64; MTDDTHSSDP ETPDPTTDRS GTRALVAARD AEAEPDTTEI RELAAAAGYV VVGTVTQRRR EDPTYGLGRG RAEDLMRLAA ETDAEAVIYD GSLSPGQTFS LGELLPAGVA VIDRPRLVLD RLATAADSRS ADVQFELARL RYELPRLREV AARDRETVRL RPEGRGRVRD LERRIDALED TLETVTADRS QRRAERRAAG FDLVVAAGYT NAGKSRLCRR LAESDDGGGA DDDGGGVDGD IFNPDAPGSI ADRPFGTVAT STTEATLGGR RALITDTVGF VDGVAHGTMA SFRATLEAIR DADCVLLVID ASDDLDALRE KLRVVLGAVG STAGPVVPAL NKADRVDAPH LAACADAVAA TAAALQDEGV AVADALESPI PTSARDGTGC DDLVAAVVES LPTATTTLTV PYSDGVEAAL SWAYDREVVA DVAYRPEEVR VELAGRPSAV EAAARRFDQS // ID V4XFU5_9ARCH Unreviewed; 94 AA. AC V4XFU5; DT 22-JAN-2014, integrated into UniProtKB/TrEMBL. DT 22-JAN-2014, sequence version 1. DT 15-MAR-2017, entry version 11. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:ESS06994.1}; DE Flags: Fragment; GN ORFNames=A07HB70_00775 {ECO:0000313|EMBL:ESS06994.1}; OS uncultured archaeon A07HB70. OC Archaea; environmental samples. OX NCBI_TaxID=1412872 {ECO:0000313|EMBL:ESS06994.1, ECO:0000313|Proteomes:UP000030648}; RN [1] {ECO:0000313|Proteomes:UP000030648} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=24335829; RA Podell S., Emerson J.B., Jones C.M., Ugalde J.A., Welch S., RA Heidelberg K.B., Banfield J.F., Allen E.E.; RT "Seasonal fluctuations in ionic concentrations drive microbial RT succession in a hypersaline lake community."; RL ISME J. 0:0-0(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; KI543176; ESS06994.1; -; Genomic_DNA. DR OrthoDB; POG093Z04JY; -. DR Proteomes; UP000030648; Unassembled WGS sequence. DR InterPro; IPR025121; GTPase_HflX_N. DR Pfam; PF13167; GTP-bdg_N; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000030648}; KW Reference proteome {ECO:0000313|Proteomes:UP000030648}. FT DOMAIN 22 90 GTP-bdg_N. {ECO:0000259|Pfam:PF13167}. FT NON_TER 94 94 {ECO:0000313|EMBL:ESS06994.1}. SQ SEQUENCE 94 AA; 10065 MW; E1D08B5DE61327AC CRC64; MPDRAALARR DGADAPPPTP ALAALLDRLG VAVVARATQS RPEHSRYGVG PDLVERLRAP CRDRDVDTVV VDGHLHEGQV VDLVDALPVA TVWD // ID V4XQU1_9ARCH Unreviewed; 433 AA. AC V4XQU1; DT 22-JAN-2014, integrated into UniProtKB/TrEMBL. DT 22-JAN-2014, sequence version 1. DT 07-JUN-2017, entry version 27. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=A07HR60_02011 {ECO:0000313|EMBL:ESS10869.1}; OS uncultured archaeon A07HR60. OC Archaea; environmental samples. OX NCBI_TaxID=1412874 {ECO:0000313|EMBL:ESS10869.1, ECO:0000313|Proteomes:UP000030679}; RN [1] {ECO:0000313|Proteomes:UP000030679} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=24335829; RA Podell S., Emerson J.B., Jones C.M., Ugalde J.A., Welch S., RA Heidelberg K.B., Banfield J.F., Allen E.E.; RT "Seasonal fluctuations in ionic concentrations drive microbial RT succession in a hypersaline lake community."; RL ISME J. 0:0-0(2013). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; KI543233; ESS10869.1; -; Genomic_DNA. DR PATRIC; fig|1412874.3.peg.2310; -. DR OrthoDB; POG093Z07D6; -. DR Proteomes; UP000030679; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000030679}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000030679}. FT DOMAIN 186 369 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 102 129 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 433 AA; 47940 MW; 5FE402C0CB55946D CRC64; MDAIIAKRAD STEADLTEIR QLAAAGGYDT VGHLAQKRVE DAAFHFGEGK VDQLARRVAR RDADCVIVDN DLGPYQTFNI GGKMPSGVEV INRFTLILQI FGQRAQTRKA QLQVELAQLR YELPRAEAKA SLATRDERPG FMGLGEYDES RELDIKRQIS EIRAELESIA TKEQDRRAQR RESGFNLVAM AGYTNAGKST LLRRLAAELD IDENAGRHPD LASTAESEDM LFTTLGTTTR RAELQKREVL LTDTVGFISD LPHWLVESFE STLDSVYRAD LVLLVVDASE PVPDMREKIV TCHDTLHQRV EAPIITVFNK IDRVDADELA DKQAALSALA PNPVAVSAKA GTDITALRTR VESELPDWMD ERLVLPMTDN TMSLVSWIHD HGHVETEDYG DDSVIVGFQA TPSVVSRARS KAAELRPSSI ESA // ID V4XY96_9ARCH Unreviewed; 461 AA. AC V4XY96; DT 22-JAN-2014, integrated into UniProtKB/TrEMBL. DT 22-JAN-2014, sequence version 1. DT 07-JUN-2017, entry version 27. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=A07HR67_01985 {ECO:0000313|EMBL:ESS03587.1}; OS uncultured archaeon A07HR67. OC Archaea; environmental samples. OX NCBI_TaxID=1412871 {ECO:0000313|EMBL:ESS03587.1, ECO:0000313|Proteomes:UP000030660}; RN [1] {ECO:0000313|Proteomes:UP000030660} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=24335829; RA Podell S., Emerson J.B., Jones C.M., Ugalde J.A., Welch S., RA Heidelberg K.B., Banfield J.F., Allen E.E.; RT "Seasonal fluctuations in ionic concentrations drive microbial RT succession in a hypersaline lake community."; RL ISME J. 0:0-0(2013). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; KI543167; ESS03587.1; -; Genomic_DNA. DR PATRIC; fig|1412871.3.peg.2097; -. DR OrthoDB; POG093Z07D6; -. DR Proteomes; UP000030660; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000030660}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000030660}. FT DOMAIN 216 399 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 461 AA; 50779 MW; 99C972BE0EE3EDF0 CRC64; MTDGRDRPAN GPTQRSTGGI VPHRTDADAN RRAVVAKRVD AGDADLTEIT DLARAAGYEV VGRLTQTRTE DAAFMFGEGK VAELRELVRA READCVVIDN DVGPYQTFNI GGKLSAGVEV IDRFTLILEI FGQRANTRKA QLQVELAELR YELPRAEAKA SLAKRDERPG FMGLGEYDES VERDIKRQIS EIRDELESIA QKEQARRQQR RDSGFDLVAL AGYTNAGKST LMRQLAAELA VDENDDRHPD LATTAESQDM LFTTLGTTTR RAEMDKRDVL LTDTVGFIAD LPHWLVESFE STLDSVYRAD LVLLVVDASQ PVAEMREKLV TSHDTLYERN EAPIVTVFNK IDRLDPGELA DKRAALSGLA PNPVAVSART GAGVAELRDR VEAELPEWEE ERLMLPVSDD AMSLVSWIHD HAHVDGETYA DGSVTVTFEA RPSIVARARS KAAELAATSS T // ID V4Y1H4_9ARCH Unreviewed; 431 AA. AC V4Y1H4; DT 22-JAN-2014, integrated into UniProtKB/TrEMBL. DT 22-JAN-2014, sequence version 1. DT 07-JUN-2017, entry version 27. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=A07HN63_01743 {ECO:0000313|EMBL:ESS08513.1}; OS uncultured archaeon A07HN63. OC Archaea; environmental samples. OX NCBI_TaxID=1412873 {ECO:0000313|EMBL:ESS08513.1, ECO:0000313|Proteomes:UP000030667}; RN [1] {ECO:0000313|Proteomes:UP000030667} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=24335829; RA Podell S., Emerson J.B., Jones C.M., Ugalde J.A., Welch S., RA Heidelberg K.B., Banfield J.F., Allen E.E.; RT "Seasonal fluctuations in ionic concentrations drive microbial RT succession in a hypersaline lake community."; RL ISME J. 0:0-0(2013). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; KI543217; ESS08513.1; -; Genomic_DNA. DR PATRIC; fig|1412873.3.peg.1847; -. DR OrthoDB; POG093Z07D6; -. DR Proteomes; UP000030667; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000030667}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000030667}. FT DOMAIN 186 369 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 102 129 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 431 AA; 48080 MW; B63A11AAB9DB52EA CRC64; MKAVLAKRVD SGTADLDELR HLAASAGYDI AGELTQTRKE DTAHHFGEGK IAEIAELVVR TDADTVIIDN EVGPYQMFNI GRILPDETEV LDRFTLILTI FGQRAQTRKA QLQVELAELR YELPRASAKT SLAKRDERPG FMGLGEYDES REQDIKAQIA SIKRELDSIA DKAAQRRAER RDSGFDLVAL AGYTNAGKST LLRRLAAELD VDENAERHAD LDDVAQSQDR LFTTLGTTTR RAELDRRDVL LTDTVGFISD LPHWLVESFQ STLDSVYHAD LVLLVVDASE PIQEMREKLV TSHDTLRDRN EAPLLTVFNK TDLIDDAELD EKRAALSGIA PNPIAVSGKT GDSVDQLRER VEGELPDWET ERLVVPMADE TMSLVSWVHD HAYVDTESYE SEQVILEFEA RPAIIEQARA RAADLTPVES A // ID V4Y7K7_9ARCH Unreviewed; 439 AA. AC V4Y7K7; DT 22-JAN-2014, integrated into UniProtKB/TrEMBL. DT 22-JAN-2014, sequence version 1. DT 07-JUN-2017, entry version 16. DE SubName: Full=GTP-binding protein HflX {ECO:0000313|EMBL:ESS10858.1}; GN ORFNames=A07HR60_02000 {ECO:0000313|EMBL:ESS10858.1}; OS uncultured archaeon A07HR60. OC Archaea; environmental samples. OX NCBI_TaxID=1412874 {ECO:0000313|EMBL:ESS10858.1, ECO:0000313|Proteomes:UP000030679}; RN [1] {ECO:0000313|Proteomes:UP000030679} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=24335829; RA Podell S., Emerson J.B., Jones C.M., Ugalde J.A., Welch S., RA Heidelberg K.B., Banfield J.F., Allen E.E.; RT "Seasonal fluctuations in ionic concentrations drive microbial RT succession in a hypersaline lake community."; RL ISME J. 0:0-0(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; KI543233; ESS10858.1; -; Genomic_DNA. DR PATRIC; fig|1412874.3.peg.2299; -. DR OrthoDB; POG093Z07D6; -. DR Proteomes; UP000030679; Unassembled WGS sequence. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000030679}; KW Reference proteome {ECO:0000313|Proteomes:UP000030679}. FT DOMAIN 184 290 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 439 AA; 47206 MW; C95AC69AB63800F9 CRC64; MSQTAILAAR ASDEPPDTGE IRNLAKAADY QPIGEITQRG EDDPTYSLGR GKAEALMRLV ASEEADTVIF DGGLTPGQTA SLSELMPAGT DVLDRTRLVL ELFATRAGSA AATTQAELAR LRYLKPRLTE FSARGATTEN EYHSEGAGRV QDLERQITSL EQSLSEITAD RNRRREQRRS EGFDLVALTG YTNAGKSTLL QQLADDLDTT EPAGHDDLDS SAAAADALFG TVETTTHRAT IDGRRLLLTD TVGFVEGLPH EFVQSFKSTI DAARDSDAVL LVTDASDAPE RFATKLGASL AAIDHTDGRL IPVLTKTDRV TESAVAQRMT TTRERLETWA GDATRITDPV AISSRDGSGI ETLRDQLRDV LPVATEPIRL PNGGDAQSLL SWAYDHCDVS DVEYGGSSLG FTVTGNPETI AEIRRRANRI QPSGGDDSA // ID V4YQH9_9PROT Unreviewed; 403 AA. AC V4YQH9; DT 22-JAN-2014, integrated into UniProtKB/TrEMBL. DT 22-JAN-2014, sequence version 1. DT 07-JUN-2017, entry version 25. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:ESS13922.1}; GN ORFNames=MOLA814_01547 {ECO:0000313|EMBL:ESS13922.1}; OS Betaproteobacteria bacterium MOLA814. OC Bacteria; Proteobacteria; Betaproteobacteria. OX NCBI_TaxID=1408164 {ECO:0000313|EMBL:ESS13922.1, ECO:0000313|Proteomes:UP000017838}; RN [1] {ECO:0000313|EMBL:ESS13922.1, ECO:0000313|Proteomes:UP000017838} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MOLA814 {ECO:0000313|EMBL:ESS13922.1, RC ECO:0000313|Proteomes:UP000017838}; RX PubMed=24356832; RA Courties A., Riedel T., Jarek M., Intertaglia L., Lebaron P., RA Suzuki M.T.; RT "Genome Sequence of Strain MOLA814, a Proteorhodopsin-Containing RT Representative of the Betaproteobacteria Common in the Ocean."; RL Genome Announc. 1:e01062-13(2013). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:ESS13922.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AYMW01000002; ESS13922.1; -; Genomic_DNA. DR EnsemblBacteria; ESS13922; ESS13922; MOLA814_01547. DR PATRIC; fig|1408164.3.peg.1608; -. DR Proteomes; UP000017838; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000017838}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000017838}. FT DOMAIN 197 370 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 403 AA; 44619 MW; 4EFB634427F7A59F CRC64; MNDNSLPKVI LVSVDFGEPN FDAALLELGL LAESAGYAVV DRVTCKRKAP DAALFVGSGK AQEIKQLAEV NGATEILFDQ ALSPAQQRNL ERELGMAVND RTLLVLEIFA QRARSFEGKL QVELARLQYL STRLVRRWSH LERQRGGAGQ RGGPGERQIE LDKRMISDSV KRTRDKLTKV KRQRQTQRRQ RDRVGVFTMS LVGYTNAGKS SLFNALVKAQ TFVADQLFAT LDTTTRQMYL SGAGQSVSVS DTVGFIRDLP HGLVEAFSAT LQEAVEADVL LHVVDAANPA YIEQIIEVQR VLGDIGAGDI PQILLFNKLD LVEGGRGPRR MRDQMDVNGQ VFERLFVSAH TGEGLDGLRA LLVERLALFQ MQQGRPSEQH NSTPDEDAVY EHDPGDPRQL PTS // ID V4ZVT5_9ARCH Unreviewed; 394 AA. AC V4ZVT5; DT 22-JAN-2014, integrated into UniProtKB/TrEMBL. DT 22-JAN-2014, sequence version 1. DT 07-JUN-2017, entry version 26. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=A07HB70_00619 {ECO:0000313|EMBL:ESS07060.1}; OS uncultured archaeon A07HB70. OC Archaea; environmental samples. OX NCBI_TaxID=1412872 {ECO:0000313|EMBL:ESS07060.1, ECO:0000313|Proteomes:UP000030648}; RN [1] {ECO:0000313|Proteomes:UP000030648} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=24335829; RA Podell S., Emerson J.B., Jones C.M., Ugalde J.A., Welch S., RA Heidelberg K.B., Banfield J.F., Allen E.E.; RT "Seasonal fluctuations in ionic concentrations drive microbial RT succession in a hypersaline lake community."; RL ISME J. 0:0-0(2013). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; KI543174; ESS07060.1; -; Genomic_DNA. DR PATRIC; fig|1412872.3.peg.635; -. DR OrthoDB; POG093Z07D6; -. DR Proteomes; UP000030648; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000030648}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000030648}. FT DOMAIN 153 336 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 394 AA; 44040 MW; 1547CBADF9CE2A13 CRC64; MTQTRTEDAA YMFGEGKVDE IAAVVARTGA EAVVVDNQVG PYQTYNVGQK LPTGVGVVDR FTLILEIFGQ RANTRTAQLQ VELAELRYEL PRAEAKASLA KRDERPGFMG LGEYDESREQ DIKSQIADIR SELDQIVETE ERRRESRRES GFDLVALAGY TNAGKSTLLR RLAADHEVDE NADRHPDLDR TAESEDRLFT TLGTTTRRAE VGPREVLVTD TVGFVSDLPH WLVDSFRSTL DSVYHADLVL LVVDAGESVA EMREKLVTCH DTLARRNEAP IVTVLNKVDE VDDDELARKR GALAALAPDP VAVSGLTGER VGDLRRRVDR ELPDWEHERL YLPMTEDTMS LVSWVHDHGE VETESYEDDG VLLEFRARPS VVDRARARAG RLPA // ID V5AY35_ENTCL Unreviewed; 426 AA. AC V5AY35; DT 22-JAN-2014, integrated into UniProtKB/TrEMBL. DT 22-JAN-2014, sequence version 1. DT 30-AUG-2017, entry version 28. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:ESS60129.1}; GN ORFNames=EDP2_2065 {ECO:0000313|EMBL:ESS60129.1}; OS Enterobacter cloacae S611. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; OC Enterobacteriaceae; Enterobacter; Enterobacter cloacae complex. OX NCBI_TaxID=1399146 {ECO:0000313|EMBL:ESS60129.1, ECO:0000313|Proteomes:UP000017834}; RN [1] {ECO:0000313|EMBL:ESS60129.1, ECO:0000313|Proteomes:UP000017834} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=S611 {ECO:0000313|EMBL:ESS60129.1, RC ECO:0000313|Proteomes:UP000017834}; RX PubMed=25502660; RA Wang D., Han C.S., Dichosa A.E., Gleasner C.D., Johnson S.L., RA Daligault H.E., Davenport K.W., Li P.E., Pierson E.A., RA Pierson L.S.III.; RT "Draft Genome Sequence of Enterobacter cloacae Strain S611."; RL Genome Announc. Announc.2:0-0(2014). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:ESS60129.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AXOM01000010; ESS60129.1; -; Genomic_DNA. DR RefSeq; WP_023478522.1; NZ_AXOM01000010.1. DR EnsemblBacteria; ESS60129; ESS60129; EDP2_2065. DR PATRIC; fig|1399146.3.peg.179; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000017834; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000017834}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000017834}. FT DOMAIN 198 365 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 426 AA; 48125 MW; B38847E53DF4522E CRC64; MFDRYDAGEQ AVLVHIYFSQ DKDMEDLQEF EALVSSAGVE AMQVITGSRK APHPKYFVGE GKAVEIAEAV KATGASVVLF DHALSPAQER NLERLCECRV IDRTGLILDI FAQRARTHEG KLQVELAQLR HLATRLVRGW THLERQKGGI GLRGPGETQL ETDRRLLRNR ITQILSRLEK VEKQREQGRR SRTKADIPTV SLVGYTNAGK STLFNQITEA QVYAADQLFA TLDPTLRRID VADVGETVLA DTVGFIRHLP HDLVAAFKAT LQETRQATLL LHVIDGADVR VQENIDAVNT VLEEIDAHEI PTLLVMNKID MLEDFEPRID RDEENKPTRV WLSAQTGAGV PLLFQALTER LAGEVAQHTL RLPAEEGRLR SRFYQLQAIE KEWTEEDGSV GMQIRMPIVD WRRLCKQEPA LEEYIV // ID V5CAY3_9GAMM Unreviewed; 421 AA. AC V5CAY3; DT 22-JAN-2014, integrated into UniProtKB/TrEMBL. DT 22-JAN-2014, sequence version 1. DT 07-JUN-2017, entry version 25. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:ESS73973.1}; GN ORFNames=MGMO_8c01120 {ECO:0000313|EMBL:ESS73973.1}; OS Methyloglobulus morosus KoM1. OC Bacteria; Proteobacteria; Gammaproteobacteria; Methylococcales; OC Methylococcaceae; Methyloglobulus. OX NCBI_TaxID=1116472 {ECO:0000313|EMBL:ESS73973.1, ECO:0000313|Proteomes:UP000017842}; RN [1] {ECO:0000313|EMBL:ESS73973.1, ECO:0000313|Proteomes:UP000017842} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=KoM1 {ECO:0000313|EMBL:ESS73973.1, RC ECO:0000313|Proteomes:UP000017842}; RX PubMed=24356841; RA Poehlein A., Deutzmann J.S., Daniel R., Simeonova D.D.; RT "Draft Genome Sequence of the Methanotrophic Gammaproteobacterium RT Methyloglobulus morosus DSM 22980 Strain KoM1."; RL Genome Announc. 1:e01078-13(2013). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:ESS73973.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AYLO01000008; ESS73973.1; -; Genomic_DNA. DR RefSeq; WP_023493208.1; NZ_AYLO01000008.1. DR EnsemblBacteria; ESS73973; ESS73973; MGMO_8c01120. DR PATRIC; fig|1116472.3.peg.287; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000017842; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000017842}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000017842}. FT DOMAIN 196 363 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 421 AA; 47165 MW; DE4F7FD0AFE81601 CRC64; MFDRPDTGER AILVHLTLHS HHEDLLELKE LAKSAGTNPV HVITGSRKSP DAKYYVGTGK LDEIKLAVET HSADIVLFNH ALSPSQERNL EKFLGVRVVD RNGLILDIFA QRAQSFEGKL QVELAQLKHL STRLVRGWTH LERQKGGIGL RGPGETQLET DRRLLGLRIK QIQKRLDKVD KQRHQGRSKR KKAEIPSISF VGYTNAGKST LFNRLTGADS YAADQLFATL DPTLRSCRLP NNIEIVLADT VGFIRHLPHE LVASFKSTLQ EASEADLLLH VIDAHSENRD DNIAEVYQVL ADIGADKIRC IEVFNKIDLL ENGQPRIDRD DEGNPQRVWL SAETGQGIDL LLNVLAEQFA PVKNKRKCYL KPDQGQIRAK LFTCAKIIDE HINDSGGSDL IIEIDNKYLG LLNAVKTEEI A // ID V5SEA4_9RHIZ Unreviewed; 443 AA. AC V5SEA4; DT 19-FEB-2014, integrated into UniProtKB/TrEMBL. DT 19-FEB-2014, sequence version 1. DT 07-JUN-2017, entry version 25. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=W911_11030 {ECO:0000313|EMBL:AHB48812.1}; OS Hyphomicrobium nitrativorans NL23. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Hyphomicrobiaceae; Hyphomicrobium. OX NCBI_TaxID=1029756 {ECO:0000313|EMBL:AHB48812.1, ECO:0000313|Proteomes:UP000018542}; RN [1] {ECO:0000313|EMBL:AHB48812.1, ECO:0000313|Proteomes:UP000018542} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NL23 {ECO:0000313|EMBL:AHB48812.1}; RX PubMed=24435868; RA Martineau C., Villeneuve C., Mauffrey F., Villemur R.; RT "Complete Genome Sequence of Hyphomicrobium nitrativorans Strain NL23, RT a Denitrifying Bacterium Isolated from Biofilm of a Methanol-Fed RT Denitrification System Treating Seawater at the Montreal Biodome."; RL Genome Announc. 2:e01165-13(2014). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP006912; AHB48812.1; -; Genomic_DNA. DR EnsemblBacteria; AHB48812; AHB48812; W911_11030. DR KEGG; hni:W911_11030; -. DR PATRIC; fig|1029756.8.peg.2293; -. DR KO; K03665; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000018542; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000018542}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000018542}. FT DOMAIN 208 381 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 443 AA; 48727 MW; 0E6D1D63BE2F1EEB CRC64; MRALVLVPVL TRARAASEDA PRSAQRVSLH SPEDRLAEST GLAEAIDLDV AEARLVSVPQ PRPATLFGSG KVEEIADLVK DEDVGLVIVD HTISPVQQRN LERAWNAKVL DRTGLILEIF GRRARTREGR LQVELAHLSY QKGRLVRAWT HLERQRGGRG FLGGPGEAQI ELDRRMLDER IIAIRRELEG VVRTRELHRK GRRKVPYPVV AIVGYTNAGK STLFNRLTQA GVMAMDQVFA TLDPTMREVR LGSGRRIILS DTVGFISDLP TQLVAAFRAT LEEVIGADLV LHVRDIAHSE TDAQAVDVEH VLRDLGVETD AASGPILEVW NKVDLLSPVT REEAQAAARF RSHKPVLISA ASGDGLDRLL ARIDARLGAA DEIVSVRVPA SEGRLVAWLH ENAEVIARET QDDGTLDVRV RIASEKKQRL LNALGRAGLT PNV // ID V5UJV0_9BURK Unreviewed; 389 AA. AC V5UJV0; DT 19-FEB-2014, integrated into UniProtKB/TrEMBL. DT 19-FEB-2014, sequence version 1. DT 07-JUN-2017, entry version 27. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=X636_20325 {ECO:0000313|EMBL:AHB77532.1}; OS Pandoraea pnomenusa. OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Pandoraea. OX NCBI_TaxID=93220 {ECO:0000313|EMBL:AHB77532.1, ECO:0000313|Proteomes:UP000018548}; RN [1] {ECO:0000313|EMBL:AHB77532.1, ECO:0000313|Proteomes:UP000018548} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=RB-44 {ECO:0000313|EMBL:AHB77532.1, RC ECO:0000313|Proteomes:UP000018548}; RX PubMed=24699956; RA Ee R., Lim Y.L., Yin W.F., Chan K.G.; RT "De Novo Assembly of the Quorum-Sensing Pandoraea sp. Strain RB-44 RT Complete Genome Sequence Using PacBio Single-Molecule Real-Time RT Sequencing Technology."; RL Genome Announc. 2:e00245-14(2014). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP006938; AHB77532.1; -; Genomic_DNA. DR RefSeq; WP_023873940.1; NZ_AUZF01000001.1. DR EnsemblBacteria; AHB77532; AHB77532; X636_20325. DR KEGG; prb:X636_20325; -. DR PATRIC; fig|1380774.3.peg.4116; -. DR KO; K03665; -. DR Proteomes; UP000018548; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000018548}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000018548}. FT DOMAIN 192 362 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 158 185 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 389 AA; 43055 MW; 5BF518AD4E495CC8 CRC64; MTTNAALVGI DFGKLDFEAS LQELDLLTQS AGATPVVTIT GRRHSPDAKL FIGSGKAEEL RAAIAEYDVD LVIFNHALTP GQQRNLEHLL QRRVEDRTSL ILDIFAQRAK SHEGKLQVEL AQLQYLSTRL VRAWTHLERQ KGGIGLRGPG ETQLETDRRL LGERVKSLTA RLERLKRQHD TQRRARQRSG TMSISLVGYT NAGKSTLFNA MTKANAYAAD QLFATLDTTS RRVYLGEVGN IVLSDTVGFI RELPHQLVAA FRATLEETVH ADMLLHVVDA SSQVRQEQMA EVNAVLAEID AANIPQILVW NKIDAVPELA AQGPRIERDE AGRITRVFLS ARTGQGLDLL REAISEAVVA GTAGLQSQHE APDVRLIDRW EDAPRAEDR // ID V5WCX0_9SPIO Unreviewed; 436 AA. AC V5WCX0; DT 19-FEB-2014, integrated into UniProtKB/TrEMBL. DT 19-FEB-2014, sequence version 1. DT 07-JUN-2017, entry version 27. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=L21SP2_0221 {ECO:0000313|EMBL:AHC13663.1}; OS Salinispira pacifica. OC Bacteria; Spirochaetes; Spirochaetales; Spirochaetaceae; Salinispira. OX NCBI_TaxID=1307761 {ECO:0000313|EMBL:AHC13663.1, ECO:0000313|Proteomes:UP000018680}; RN [1] {ECO:0000313|EMBL:AHC13663.1, ECO:0000313|Proteomes:UP000018680} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=L21-RPul-D2 {ECO:0000313|EMBL:AHC13663.1, RC ECO:0000313|Proteomes:UP000018680}; RX PubMed=26203324; DOI=10.1186/1944-3277-10-7; RA Ben Hania W., Joseph M., Schumann P., Bunk B., Fiebig A., Sproer C., RA Klenk H.P., Fardeau M.L., Spring S.; RT "Complete genome sequence and description of Salinispira pacifica gen. RT nov., sp. nov., a novel spirochaete isolated form a hypersaline RT microbial mat."; RL Stand. Genomic Sci. 10:7-7(2015). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP006939; AHC13663.1; -; Genomic_DNA. DR RefSeq; WP_024266596.1; NC_023035.1. DR EnsemblBacteria; AHC13663; AHC13663; L21SP2_0221. DR KEGG; slr:L21SP2_0221; -. DR PATRIC; fig|1307761.3.peg.222; -. DR KO; K03665; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000018680; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000018680}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000018680}. FT DOMAIN 203 368 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 162 196 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 436 AA; 49449 MW; 8B6469737976A403 CRC64; MIEYEQQKEE SALLITLRNR ELSDREARDH LEELEGLCTT LGFTSAGEFI VPVREPQPKY LIGSGWAEEL AVQAEALEAD YVVFDDDLSP SQQRNLEKLC KKPVIDRHQV IIEIFAQRAN TREARLQVEL ARLIYSLPRL RRMWTHLSRQ RGGAKGTRGE GETQLEVDRR LVEARIARLK DELSQVQSQR STLRKQRESI PVPTAAIVGY TNAGKSSLHK ALTDSQILVE DKLFATLDPT TRRYHMPSGM EVLLTDTVGF IRKLPHDLVD AFKSTLEETV LAHFLLHIVD ITNPDLHQHI ATTRAVLEEI GVEDKPEILV FNKCDAARGD QKSFMRQRYP DALFISVKNG EGFDELAQAV EHQISKTLQK VRLTMTHNKG DIISLAHREG RVIETEYGDQ DVVVTAFLPP RLLSMIQSKE KEADSGIHLE LLDGEP // ID V5XBQ2_MYCNE Unreviewed; 470 AA. AC V5XBQ2; DT 19-FEB-2014, integrated into UniProtKB/TrEMBL. DT 19-FEB-2014, sequence version 1. DT 07-JUN-2017, entry version 28. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=D174_11915 {ECO:0000313|EMBL:AHC25253.1}; OS Mycobacterium neoaurum VKM Ac-1815D. OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae; OC Mycobacterium. OX NCBI_TaxID=700508 {ECO:0000313|EMBL:AHC25253.1, ECO:0000313|Proteomes:UP000018763}; RN [1] {ECO:0000313|EMBL:AHC25253.1, ECO:0000313|Proteomes:UP000018763} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=VKM Ac-1815D {ECO:0000313|EMBL:AHC25253.1}; RX PubMed=24435872; RA Shtratnikova V.Y., Bragin E.Y., Dovbnya D.V., Pekov Y.A., RA Schelkunov M.I., Strizhov N., Ivashina T.V., Ashapkin V.V., RA Donova M.V.; RT "Complete Genome Sequence of Sterol-Transforming Mycobacterium RT neoaurum Strain VKM Ac-1815D."; RL Genome Announc. 2:e01177-13(2014). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP006936; AHC25253.1; -; Genomic_DNA. DR RefSeq; WP_019513005.1; NC_023036.2. DR EnsemblBacteria; AHC25253; AHC25253; D174_11915. DR KEGG; mne:D174_11915; -. DR KO; K03665; -. DR Proteomes; UP000018763; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000018763}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000018763}. FT DOMAIN 247 416 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 206 233 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 470 AA; 50601 MW; 21A7435A3CDB9A37 CRC64; MTEFSPNNPV PSTGELALED RAALRRVAGL STELTDISEV EYRQLRLERV VLVGVWTEGS AADVDASMAE LAALAETAGS EVLEGLVQRR DKPDASTYIG SGKAIELREI VEATGADTVI CDGELSPAQL NALEKAVKVK VIDRTALILD IFAQHATSRE GKAQVSLAQM EYMLPRLRGW GESMSRQAGG RAGGAGGGVG TRGPGETKIE TDRRRIRERM SKLRREIKDM KKIRDTQRGS RRRSDAAALA IVGYTNAGKS SLLNALTGAG VLVENALFAT LEPTTRRGEF EDGRAFVLTD TVGFVRHLPT QLVEAFRSTL EEVADAELLI HVVDGSDVTP LAQIQAVRTV INDVVTEYGI APPPELLVVN KIDAAGDLAL AQLRRALPDA VFVSAHTGEG LAQLRTRMAE LVEPTDAFVD VTLPYERGDL VARVHAEGRI ESTEHTDKGT KIAARVPVPL AAALGEFSNW // ID V5XMB6_ENTMU Unreviewed; 414 AA. AC V5XMB6; DT 19-FEB-2014, integrated into UniProtKB/TrEMBL. DT 19-FEB-2014, sequence version 1. DT 07-JUN-2017, entry version 28. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:BAO06267.1}; GN ORFNames=EMQU_0710 {ECO:0000313|EMBL:BAO06267.1}; OS Enterococcus mundtii QU 25. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Enterococcaceae; OC Enterococcus. OX NCBI_TaxID=1300150 {ECO:0000313|EMBL:BAO06267.1, ECO:0000313|Proteomes:UP000018580}; RN [1] {ECO:0000313|Proteomes:UP000018580} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=QU25 {ECO:0000313|Proteomes:UP000018580}; RA Shimizu-Kadota M., Shiwa Y., Sonomoto K., Yoshikawa H.; RT "Complete genome sequencing of Enterococcus mundtii QU25."; RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AP013036; BAO06267.1; -; Genomic_DNA. DR RefSeq; WP_023519260.1; NC_022878.1. DR EnsemblBacteria; BAO06267; BAO06267; EMQU_0710. DR GeneID; 31546837; -. DR KEGG; emu:EMQU_0710; -. DR PATRIC; fig|1300150.4.peg.706; -. DR KO; K03665; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000018580; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000018580}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000018580}. FT DOMAIN 197 359 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 414 AA; 47059 MW; 24E73EADDC713387 CRC64; MREAKEKVII VGVETEENQR YFAESMKELE QLIDTAAGEV VYRLTQKRPQ VDRQTLIGKG KLQELTQLAD AYEADLVIFN HELTPRQSQL ITDAVGAPVI DRVQLILDIF AMRARSKEGK LQVELAQLQY LLPRLAGQGE SLSRLGGGIG TRGPGETKLE TDRRHIRNKI LGVKRELKAV EAHRERNRQK RQSSEVFQIG LIGYTNAGKS TILNLLTQAE SYAKDQLFAT LDPLTKKWRF AEGFELTVTD TVGFIQDLPT QLIDAFHSTL EESQGMDLLL HVVDASSSDR ILQEQTVLKL MDELDMKEMP VLTVYNKSDQ IDTAGFTPTL FPNVLISAQT QEGKERLIES VKRQLMELML PYTKIVPSDQ GQTLSELRRQ TLVLDEHFIE EQNSYEVRGF ANKNSKWLKK DELF // ID V6DG12_9DELT Unreviewed; 369 AA. AC V6DG12; DT 19-FEB-2014, integrated into UniProtKB/TrEMBL. DT 19-FEB-2014, sequence version 1. DT 07-JUN-2017, entry version 31. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:CDK30532.1}; GN ORFNames=BABL1_gene_487 {ECO:0000313|EMBL:CDK30532.1}; OS Candidatus Babela massiliensis. OC Bacteria; Proteobacteria; Deltaproteobacteria; Candidatus Babela. OX NCBI_TaxID=673862 {ECO:0000313|EMBL:CDK30532.1, ECO:0000313|Proteomes:UP000018769}; RN [1] {ECO:0000313|EMBL:CDK30532.1, ECO:0000313|Proteomes:UP000018769} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BABL1 {ECO:0000313|Proteomes:UP000018769}; RA Pagnier I., Yutin N., Croce O., Makarova K.S., Wolf Y.I., Benamar S., RA Raoult D., Koonin E.V., La Scola B.; RT "Babela massiliensis, a representative of a widespread bacterial RT phylum with unusual adaptations to parasitism in amoebae."; RL Biol. Direct 10:0-0(2015). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; HG793133; CDK30532.1; -; Genomic_DNA. DR RefSeq; WP_023791804.1; NC_023003.1. DR EnsemblBacteria; CDK30532; CDK30532; BABL1_gene_487. DR KEGG; dpb:BABL1_gene_487; -. DR PATRIC; fig|673862.3.peg.418; -. DR KO; K03665; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000018769; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000018769}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Hydrolase {ECO:0000313|EMBL:CDK30532.1}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Protease {ECO:0000313|EMBL:CDK30532.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000018769}. FT DOMAIN 204 369 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 170 197 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 369 AA; 42463 MW; 373C4C3338C62403 CRC64; MKNIQKPTII HPKTLLIGII APYNTTKNIE SYYEEFISLV ESNGIEYDNT YFTRLREIDS AYFVTKGKLE ELIKICQEED IEEVIFSESL NGQQERNLSK ALNCKVFDRT QLILEIFEKG AHSAEGKLQV ELAMLQHKKT RVAGRGIHMS QQSGRIGVRG PGETAKEKEL QHIDRRISKL RSELSDLEKH RQTQRQSRLE SKIPLICLVG YTNAGKSTIL NTLTKSNVLA ENKLFATLDT TTRELYIDHE KKGLISDTVG FIQQIPHKLI EAFKSTLTEL QYAHLLLLVV DVSDLNWESE IAVVLEVLKE IEIEKPILYV FNKIDKIENK EIFQFSVRNY QPHILISATS KEGIQPLIDF LRNWYPANY // ID V6EYY5_9PROT Unreviewed; 422 AA. AC V6EYY5; DT 19-FEB-2014, integrated into UniProtKB/TrEMBL. DT 19-FEB-2014, sequence version 1. DT 07-JUN-2017, entry version 27. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=MGMSRv2__1142 {ECO:0000313|EMBL:CDK98357.1}; OS Magnetospirillum gryphiswaldense MSR-1 v2. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales; OC Rhodospirillaceae; Magnetospirillum. OX NCBI_TaxID=1430440 {ECO:0000313|EMBL:CDK98357.1, ECO:0000313|Proteomes:UP000018922}; RN [1] {ECO:0000313|EMBL:CDK98357.1, ECO:0000313|Proteomes:UP000018922} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MSR-1 {ECO:0000313|EMBL:CDK98357.1}; RX PubMed=24625872; DOI=10.1128/genomeA.00171-14; RA Wang X., Wang Q., Zhang W., Wang Y., Li L., Wen T., Zhang T., RA Zhang Y., Xu J., Hu J., Li S., Liu L., Liu J., Jiang W., Tian J., RA Li Y., Schuler D., Wang L., Li J.; RT "Complete Genome Sequence of Magnetospirillum gryphiswaldense MSR-1."; RL Genome Announc. 2:e00171-e00114(2014). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; HG794546; CDK98357.1; -; Genomic_DNA. DR RefSeq; WP_024079386.1; NC_023065.1. DR EnsemblBacteria; CDK98357; CDK98357; MGMSRv2__1142. DR KEGG; mgy:MGMSRv2__1142; -. DR KO; K03665; -. DR Proteomes; UP000018922; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000018922}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000018922}. FT DOMAIN 193 364 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 159 189 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 422 AA; 46406 MW; F1BBCDF88A8D7C16 CRC64; MVVHPAIKVA DGGLRDPQSR LDEAVGLTQA IDLDVVAAEL VPVSKRRPAT LIGKGAVERL AIIVKDQDIQ VAIVDGHLSP VQQRNLEKEW ACKVIDRTGL ILEIFGARAR TREGSLQVEL AALSYQRSRL VRSWTHLERQ RGGFGFLGGP GETQIEADRR MIGDRIVKLK RELEEVKRTR ELHRSARRRV PYPIVALVGY TNAGKSTLFN RLTRSEVLAK DMLFATLDPT MRGLKLPSGR QIILSDTVGF ISDLPHELVA AFRATLEEVL EADVVVHVRD MAHPDTEAQA SDVELVLKEL GLGDMVDRGL VEALNKIDLL PEGGREGVVN QAARKPTALP ISALTGAGVD AFLACIDEKL SENRLIIDVS FDLGDGAAIA WMYRNGEVLE RSDDDTQTHL KVRLDPANIQ RYQQMLANGG IG // ID V6IXQ8_9BACL Unreviewed; 417 AA. AC V6IXQ8; DT 19-FEB-2014, integrated into UniProtKB/TrEMBL. DT 19-FEB-2014, sequence version 1. DT 07-JUN-2017, entry version 25. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=P343_08920 {ECO:0000313|EMBL:EST12173.1}; OS Sporolactobacillus laevolacticus DSM 442. OC Bacteria; Firmicutes; Bacilli; Bacillales; Sporolactobacillaceae; OC Sporolactobacillus. OX NCBI_TaxID=1395513 {ECO:0000313|EMBL:EST12173.1, ECO:0000313|Proteomes:UP000018296}; RN [1] {ECO:0000313|EMBL:EST12173.1, ECO:0000313|Proteomes:UP000018296} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 442 {ECO:0000313|EMBL:EST12173.1, RC ECO:0000313|Proteomes:UP000018296}; RX PubMed=24371202; RA Wang H., Wang L., Ju J., Yu B., Ma Y.; RT "Genome Sequence of Sporolactobacillus laevolacticus DSM442, an RT Efficient Polymer-Grade D-Lactate Producer from Agricultural Waste RT Cottonseed as a Nitrogen Source."; RL Genome Announc. 1:e01100-13(2013). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EST12173.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AWTC01000006; EST12173.1; -; Genomic_DNA. DR RefSeq; WP_023510043.1; NZ_AWTC01000006.1. DR EnsemblBacteria; EST12173; EST12173; P343_08920. DR PATRIC; fig|1395513.3.peg.1801; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000018296; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000018296}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000018296}. FT DOMAIN 194 354 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 417 AA; 46228 MW; F1F7900A54C69BFF CRC64; MESVILVACQ LPSQSDDHFE SSLQELEALT KTAGGQVVAV VTQKRQKIDS ATYIGSGKLQ ELDALEKQLG AGTVIFNGEL FPSQQGRLSE LLYAKVLDRT QLILDIFAMR ARSREGKLQV ELAQLQYLLP RLSGMGASLS RLGGGIGTRG PGETKLETDR RYIRSRMKDI SNQLKTVVQH RKRYRDRRLA NNQCQIVLVG YTNAGKSTLF NQLTSARTYA ENQLFATLDP LTRKMNLPSG FICLLSDTVG FIQDLPTQLV AAFRSTLEEV TGAQLIVHVL DASDPDLITH EKTVKALLSE LGADELPVLT IYNKKDLLQT AFIVPKGSLL VSARDVNDRE RILAEIKTQL VQQMVPFQAQ LPADEGKLLN EIKLHAVLNK QSYDEQAQAY VVEGFVYPET PIASKLIQDT VSTDEEI // ID V6KEH4_STRNV Unreviewed; 498 AA. AC V6KEH4; DT 19-FEB-2014, integrated into UniProtKB/TrEMBL. DT 19-FEB-2014, sequence version 1. DT 07-JUN-2017, entry version 26. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=M877_09645 {ECO:0000313|EMBL:EST30443.1}; OS Streptomyces niveus NCIMB 11891. OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae; OC Streptomyces. OX NCBI_TaxID=1352941 {ECO:0000313|EMBL:EST30443.1, ECO:0000313|Proteomes:UP000017971}; RN [1] {ECO:0000313|EMBL:EST30443.1, ECO:0000313|Proteomes:UP000017971} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NCIMB 11891 {ECO:0000313|EMBL:EST30443.1}; RX PubMed=24407644; RA Flinspach K., Ruckert C., Kalinowski J., Heide L., Apel A.K.; RT "Draft Genome Sequence of Streptomyces niveus NCIMB 11891, Producer of RT the Aminocoumarin Antibiotic Novobiocin."; RL Genome Announc. 2:e01146-13(2014). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EST30443.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AWQW01000067; EST30443.1; -; Genomic_DNA. DR RefSeq; WP_023538214.1; NZ_CM002280.1. DR EnsemblBacteria; EST30443; EST30443; M877_09645. DR PATRIC; fig|1352941.4.peg.1978; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000017971; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000313|EMBL:EST30443.1}; KW Complete proteome {ECO:0000313|Proteomes:UP000017971}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900, KW ECO:0000313|EMBL:EST30443.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000017971}. FT DOMAIN 275 440 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 498 AA; 54285 MW; 4E825E06825CAC50 CRC64; MTSSSSPSQD EQIAADPRTD SLRADALMEE DVAWSQEIDG QRDGDQFERS DRAALRRVVG LSTELEDVTE VEYRQLRLER VVLVGVWVTG TVQEAENSLA ELAALAETAG ALVLDGVIQR RDKPDPATYI GSGKARELYD LVLETGADTV VCDGELSPGQ LIHLEDVVKV KVVDRTALIL DIFAQHAKSR EGKAQVALAQ MQYMLPRLRG WGQSLSRQMG GGGGGGMATR GPGETKIETD RRRIREKMAK MRREIAEMKT GREIKRQERR RHRVPSVAIA GYTNAGKSSL LNRLTGAGVL VENSLFATLD PTVRRAETPS GRIYTLADTV GFVRHLPHHL VEAFRSTMEE VGDSDLILHV VDGAHPAPEE QLAAVREVIR DVGAVDVREI VVINKADAAD PEVLQRLLRM ERHAIAVSAR TGAGMTELLA LIDTELPRPE ITVEALVPYT DGGLVSRVHA EGEVLSEEHT PEGTMLKAQV HEELAAALAV YAPVPAIG // ID V6KQ92_STRRC Unreviewed; 497 AA. AC V6KQ92; DT 19-FEB-2014, integrated into UniProtKB/TrEMBL. DT 19-FEB-2014, sequence version 1. DT 07-JUN-2017, entry version 26. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=M878_10935 {ECO:0000313|EMBL:EST34262.1}; OS Streptomyces roseochromogenus subsp. oscitans DS 12.976. OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae; OC Streptomyces. OX NCBI_TaxID=1352936 {ECO:0000313|EMBL:EST34262.1, ECO:0000313|Proteomes:UP000017984}; RN [1] {ECO:0000313|EMBL:EST34262.1, ECO:0000313|Proteomes:UP000017984} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DS 12.976 {ECO:0000313|EMBL:EST34262.1}; RX PubMed=24407645; RA Ruckert C., Kalinowski J., Heide L., Apel A.K.; RT "Draft Genome Sequence of Streptomyces roseochromogenes subsp. RT oscitans DS 12.976, Producer of the Aminocoumarin Antibiotic RT Clorobiocin."; RL Genome Announc. 2:e01147-13(2014). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EST34262.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AWQX01000083; EST34262.1; -; Genomic_DNA. DR RefSeq; WP_023546163.1; NZ_CM002285.1. DR EnsemblBacteria; EST34262; EST34262; M878_10935. DR PATRIC; fig|1352936.5.peg.2317; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000017984; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 2. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000313|EMBL:EST34262.1}; KW Complete proteome {ECO:0000313|Proteomes:UP000017984}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900, KW ECO:0000313|EMBL:EST34262.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000017984}. FT DOMAIN 275 440 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 497 AA; 54432 MW; 4C77A27543158F3A CRC64; MTSSSSPSQD TKRLAHAYPE GLRADALMEE DVAWSYEIDG ERDGDQFDRS ERAALRRVAG LSTELEDVTE VEYRQLRLER VVLVGVWTTG TVQDADNSLA ELAALAETAG ALVLDGVIQR RDKPDPATYI GSGKAQELRD IVIETGADTV ICDGELSPGQ LIQLEDVVKV KVIDRTALIL DIFAQHAKSR EGKAQVALAQ MQYMLPRLRG WGQSLSRQMG GGKGGGLATR GPGETKIETD RRRIREKMAK MRREIAEMKT GREIKRQERR RHKVPSVAIA GYTNAGKSSL LNRLTGAGVL VENALFATLD PTVRRAETPS GRLYTLADTV GFVRHLPHHL VEAFRSTMEE VGDADLILHV VDGSHPVPEE QLAAVREVIR DVGATDVPEI VVINKADAAD PLVLQRLLRV EKRSIAVSAR TGRGIEELIG LIDNELPRPS VEIEALVPYT HGKLVARAHT EGEVISEEHT AEGTLLKVRV HEELAADLAP YVPVPTT // ID V6LBB5_9ACTN Unreviewed; 498 AA. AC V6LBB5; DT 19-FEB-2014, integrated into UniProtKB/TrEMBL. DT 19-FEB-2014, sequence version 1. DT 07-JUN-2017, entry version 27. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=N566_07320 {ECO:0000313|EMBL:EST38459.1}; OS Streptomycetaceae bacterium MP113-05. OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae. OX NCBI_TaxID=1380770 {ECO:0000313|EMBL:EST38459.1, ECO:0000313|Proteomes:UP000017915}; RN [1] {ECO:0000313|EMBL:EST38459.1, ECO:0000313|Proteomes:UP000017915} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MP113-05 {ECO:0000313|EMBL:EST38459.1, RC ECO:0000313|Proteomes:UP000017915}; RA Valde M., Degnes K.F., Sletta H., Ruckert C., Kalinowski J., RA Zotchev S.B.; RT "Streptomyces bacterium from a marine sponge: physiological RT characterization and genome-based analysis of secondary metabolite RT biosynthesis potential."; RL Submitted (SEP-2013) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EST38459.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AWQV01000211; EST38459.1; -; Genomic_DNA. DR RefSeq; WP_023528479.1; NZ_KI547039.1. DR EnsemblBacteria; EST38459; EST38459; N566_07320. DR PATRIC; fig|1380770.3.peg.1292; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000017915; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 2. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000313|EMBL:EST38459.1}; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000017915}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900, KW ECO:0000313|EMBL:EST38459.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000017915}. FT DOMAIN 276 441 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 235 269 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 498 AA; 53941 MW; 25886D99F59024CC CRC64; MTPSSSLPDP GQRLSEPNRR ADALMEEDVA WGGGTDAARD GEQLDRSERA ALRRIAGLST ELEDVTEVEY RQLRLERVVL VGVWTSGTSQ DADNSLAELA ALAETAGAMV LDGVVQRRDK PDPATYIGSG KAEELRDIVL ATGADTVVCD GELSPGQLIH LEDIVKVKVV DRTALILDIF AQHAKSREGK AQVALAQMQY MLPRLRGWGQ SLSRQMGGGG SGSAGGGMAT RGPGETKIET DRRRIREKMA KARREIAEMK TSRDVQRQDR RRHKVPSVAI AGYTNAGKSS LLNRLTGAGV LVQNSLFATL DPTVRRAETP SGRLYTLADT VGFVRHLPHH LIEAFRSTME EVADSDLVLH VVDGSHPAPE EQLASVREVI RDVGATDVPE IVVVNKADAA DPLVLQRLLR TERRALVVSA RTGQGVDELL ALIDEELPRP SVELEVVVPY TQGALVARAY AEGEVVSESH TEQGTLLKVR VHEELAAELR GFEPAGQA // ID V6M265_9BACL Unreviewed; 430 AA. AC V6M265; DT 19-FEB-2014, integrated into UniProtKB/TrEMBL. DT 19-FEB-2014, sequence version 1. DT 07-JUN-2017, entry version 25. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=T458_15845 {ECO:0000313|EMBL:EST52447.1}; OS Brevibacillus panacihumi W25. OC Bacteria; Firmicutes; Bacilli; Bacillales; Paenibacillaceae; OC Brevibacillus. OX NCBI_TaxID=1408254 {ECO:0000313|EMBL:EST52447.1, ECO:0000313|Proteomes:UP000017973}; RN [1] {ECO:0000313|EMBL:EST52447.1, ECO:0000313|Proteomes:UP000017973} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=W25 {ECO:0000313|EMBL:EST52447.1, RC ECO:0000313|Proteomes:UP000017973}; RX PubMed=24459276; RA Wang X., Jin D., Zhou L., Wu L., An W., Chen Y., Zhao L.; RT "Draft Genome Sequence of Brevibacillus panacihumi Strain W25, a RT Halotolerant Hydrocarbon-Degrading Bacterium."; RL Genome Announc. 2:e01215-13(2014). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EST52447.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AYJU01000017; EST52447.1; -; Genomic_DNA. DR RefSeq; WP_023557044.1; NZ_KI629785.1. DR EnsemblBacteria; EST52447; EST52447; T458_15845. DR PATRIC; fig|1408254.3.peg.3105; -. DR Proteomes; UP000017973; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000017973}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000017973}. FT DOMAIN 201 363 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 430 AA; 49047 MW; 6C4989357824C01F CRC64; MSEMIKTQET AILVGCLLDN RDVERMRLSM EELHELADTA GVEVLDVITQ NRDRVDSAWY LGSGKIEEIA HRAQELDVDV IIFNDELSPS QTRNLDRVFD CKVIDRTQLI LDIFAGRAQS REGKIQVELA QYNYLLPRLA GQGKQLSRLG GGIGTRGPGE TKLESDRRHI RKRISELKQQ LSDTVRTRQL HRERRKKNSV FQIALVGYTN AGKSTLLNQL TTAETLQEDK LFATLDPTTR QLQLPNGMEV LLTDTVGFIQ DLPTTLVAAF RSTLEGVKEA DLILHVVDSS HPDLEIHMEV VNRILKELKA EQIPELVVFN KADLVREGTY LPPAEESILV SALSKEDQRR LLERIESFVM ASFDQFTLKI PVERGDILSL LHREGVEMEQ QYEEEEESYR VKVRVNRDHP IYGRIAPFLL DPPETVEESW // ID V6Q4X6_9ENTE Unreviewed; 412 AA. AC V6Q4X6; DT 19-FEB-2014, integrated into UniProtKB/TrEMBL. DT 19-FEB-2014, sequence version 1. DT 07-JUN-2017, entry version 24. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=T233_01098 {ECO:0000313|EMBL:EST89705.1}; OS Vagococcus lutrae LBD1. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Enterococcaceae; OC Vagococcus. OX NCBI_TaxID=1408226 {ECO:0000313|EMBL:EST89705.1, ECO:0000313|Proteomes:UP000018126}; RN [1] {ECO:0000313|EMBL:EST89705.1, ECO:0000313|Proteomes:UP000018126} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=LBD1 {ECO:0000313|EMBL:EST89705.1, RC ECO:0000313|Proteomes:UP000018126}; RX PubMed=24371201; RA Lebreton F., Valentino M.D., Duncan L.B., Zeng Q., Manson McGuire A., RA Earl A.M., Gilmore M.S.; RT "High-Quality Draft Genome Sequence of Vagococcus lutrae Strain LBD1, RT Isolated from the Largemouth Bass Micropterus salmoides."; RL Genome Announc. 1:e01087-13(2013). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EST89705.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AYSH01000016; EST89705.1; -; Genomic_DNA. DR RefSeq; WP_023606425.1; NZ_AYSH01000016.1. DR EnsemblBacteria; EST89705; EST89705; T233_01098. DR PATRIC; fig|1408226.3.peg.1068; -. DR Proteomes; UP000018126; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000018126}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000018126}. FT DOMAIN 194 356 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 412 AA; 46541 MW; 5B6B733E15C4D180 CRC64; MSERVVIVGV ETQENYRYFE ASMSELVLLT ETAQGEVVAS LIQKRPAVDR QTLVGKGKLQ EIADVVDREE ADLVVFNHEL SPRQGSYIQE QLDVRVIDRV QLILDIFALR ARSKEGQLQV ELAQLNYLLP RLTGQGAAMS RLGGGIGTRG PGETKLEMDR RHIRDKITAI KRELKDVSAH RERNRQKRKN ANVFQIGLIG YTNAGKSTIL NGLTTADTYE KNELFATLDP LTKQWTIGEA MAVTLTDTVG FIQDLPTQLI EAFQSTLEES RNMDVLLHVV DASAKQRHLQ EETVMSLLNE LGMSEIPVLT VYNKMDCVDA DQFMPTLFPN VQISAKSEAS LEQLEEAIVT FLKKLFVPYH IELPAEKSYQ AQSLKQTTLL MSEEYNEDEN SYDYRGFAPQ TSPWIRKEAS EK // ID V6SDD8_9FLAO Unreviewed; 409 AA. AC V6SDD8; DT 19-FEB-2014, integrated into UniProtKB/TrEMBL. DT 19-FEB-2014, sequence version 1. DT 07-JUN-2017, entry version 25. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=Q767_12050 {ECO:0000313|EMBL:KGO95524.1}; OS Flavobacterium enshiense DK69. OC Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales; OC Flavobacteriaceae; Flavobacterium. OX NCBI_TaxID=1107311 {ECO:0000313|EMBL:KGO95524.1, ECO:0000313|Proteomes:UP000030149}; RN [1] {ECO:0000313|EMBL:KGO95524.1, ECO:0000313|Proteomes:UP000030149} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DK69 {ECO:0000313|EMBL:KGO95524.1, RC ECO:0000313|Proteomes:UP000030149}; RA Zeng Z., Chen C.; RL Submitted (SEP-2013) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KGO95524.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JRLZ01000010; KGO95524.1; -; Genomic_DNA. DR RefSeq; WP_023572574.1; NZ_JRLZ01000010.1. DR EnsemblBacteria; KGO95524; KGO95524; Q767_12050. DR PATRIC; fig|1107311.3.peg.513; -. DR Proteomes; UP000030149; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000030149}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000030149}. FT DOMAIN 200 386 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 409 AA; 47206 MW; 06491AE80A32E929 CRC64; MLEKVTHNFE KTVIVGIVTQ QQNEDKLNEY LDELEFLTFT AGGEVVKRFS QKMDKPNPKT FVGTGKIEDI NTYIKENEVS TVIFDDELTP AQQKNITKIL DCKVLDRTNL ILDIFAQRAE TSYARTQVEL AQCQYLLPRL SGMWTHLERQ RGGIGMRGPG ETEIETDRRI VRDRIALLKD KIKTIDKQMS IQRSNRGAMV RVALVGYTNV GKSTLMNAIG KSDVFVENKL FATLDTTVRK VVIKNLPFLL SDTVGFIRKL PTQLVESFKS TLDEVREADL LLHVVDISHA DFEDHIASVN QILQDIKSSD KPTIMVFNKI DSFKHLTIAE DDLITEKTTK HYTLEEWKNT WMSKVGEKHA LFISAKKKEN FEEFREKVYE AVREIHITRF PYNKFLYPDY KDAIEKEDE // ID V6Z1Y5_STRAG Unreviewed; 412 AA. AC V6Z1Y5; DT 19-FEB-2014, integrated into UniProtKB/TrEMBL. DT 19-FEB-2014, sequence version 1. DT 07-JUN-2017, entry version 26. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=SAG0136_03110 {ECO:0000313|EMBL:ESV54261.1}; OS Streptococcus agalactiae LMG 14747. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=1154860 {ECO:0000313|EMBL:ESV54261.1, ECO:0000313|Proteomes:UP000018482}; RN [1] {ECO:0000313|EMBL:ESV54261.1, ECO:0000313|Proteomes:UP000018482} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=LMG 14747 {ECO:0000313|EMBL:ESV54261.1, RC ECO:0000313|Proteomes:UP000018482}; RA Richards V.P., Durkin S.A.S., Kim M., Pavinski Bitar P.D., RA Stanhope M.J., Town C.D., Venter J.C.; RL Submitted (MAY-2013) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:ESV54261.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ANQC01000042; ESV54261.1; -; Genomic_DNA. DR RefSeq; WP_017769234.1; NZ_ANQC01000042.1. DR EnsemblBacteria; ESV54261; ESV54261; SAG0136_03110. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000018482; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000018482}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000018482}. FT DOMAIN 199 359 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 165 192 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 412 AA; 47047 MW; F55294C58D7667E8 CRC64; MYETQENQER VIIVGVELQD TQNFAMTMSE LASLARTAGA EVIDSYTQKR ERYDSKTFIG SGKLAEIRDM VEANEIDTVI VNNRLTPRQN SNLEAALAVK VIDRMQLILD IFAMRARSHE GKLQVHLAQL KYMLPRLVGQ GIMLSRQAGG IGSRGPGESQ LELNRRSIRH QITDIERQLK AVEKNRQIIR DKRLDSETFK VGLIGYTNAG KSTLMNTLTD NRQYEADQLF ATLDATTKQL YLKGQFQATL TDTVGFIQDL PTELVAAFKS TLEESRHVDL LLHVIDASDP NHSDQERVVL TLLKDLEMQD IPRLAIYNKI DKASNFTATA FPNIRISARD KASREQIRNL IVDEIRDLFA PFSLKVHQKD AYKLYQLEKL ALLDRYTFTE EVEEITGYIS PANKWKLEEF YD // ID V7B6E6_PHAVU Unreviewed; 542 AA. AC V7B6E6; DT 19-FEB-2014, integrated into UniProtKB/TrEMBL. DT 19-FEB-2014, sequence version 1. DT 07-JUN-2017, entry version 18. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:ESW13482.1}; GN ORFNames=PHAVU_008G200200g {ECO:0000313|EMBL:ESW13482.1}; OS Phaseolus vulgaris (Kidney bean) (French bean). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae; OC Pentapetalae; rosids; fabids; Fabales; Fabaceae; Papilionoideae; OC Phaseoleae; Phaseolus. OX NCBI_TaxID=3885 {ECO:0000313|EMBL:ESW13482.1, ECO:0000313|Proteomes:UP000000226}; RN [1] {ECO:0000313|EMBL:ESW13482.1, ECO:0000313|Proteomes:UP000000226} RP NUCLEOTIDE SEQUENCE. RA Schmutz J., McClean P., Shu S., Cregan P., Rokhsar D., Jackson S.; RL Submitted (APR-2013) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CM002295; ESW13482.1; -; Genomic_DNA. DR RefSeq; XP_007141488.1; XM_007141426.1. DR GeneID; 18623457; -. DR KEGG; pvu:PHAVU_008G200200g; -. DR PhylomeDB; V7B6E6; -. DR Proteomes; UP000000226; Chromosome 8. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR CDD; cd01878; HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 2. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 2. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000226}; KW Reference proteome {ECO:0000313|Proteomes:UP000000226}. FT DOMAIN 271 396 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 542 AA; 60476 MW; 0949774D8A15D14A CRC64; MLRSFSSTLR GCSRRFRTPL SCHQKLYTNG GEGARVRPPK LLVVQPRVRP DKLLQAKLNE ALCLANSLED QRDGYFLTDF FDKPLPPHVL VQNRVPRADS YFGHGTVDNI KCHVNAAEES KEEVDAVFVN ATLSGIQQRN LERAWGKPVL DRVGLIIEIF NAHAFTKEAK LQAELAALSY KKTRLVRARG PDGRYTFGAS GEAEVVSARG RGSGGQGFMS GAGETELQLQ RRRIIERRLY LLSQIEEVRR TRALQRAGRR RRGGSPGQGL PTVAVVGYTN AGKSTLVSRL SDSDLYSDCR LFATVDPRVR SAVLPSGKKV LFSDTVGFIS DLPVQLVEAF HATLEEVVEA DLLVHVVDSS APNLDEHRTT VLLVLRQIGV SEEKLQNMIE VWNKIDIEEE CDDGDEYLDD EDEDGFKVED DVKSELLAEN EGMKEVDCEA MEEKDYSDGW LYANDLVDEA DQLNESFEQH DGLEKDSSID QSGPHVKASA ITGVGLQELL ELIDNKLCVQ NKKGAQVVER SIYDRKWRPP HNQEESGIAV EQ // ID V7CRA0_PHAVU Unreviewed; 553 AA. AC V7CRA0; DT 19-FEB-2014, integrated into UniProtKB/TrEMBL. DT 19-FEB-2014, sequence version 1. DT 07-JUN-2017, entry version 17. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:ESW32712.1}; GN ORFNames=PHAVU_001G011200g {ECO:0000313|EMBL:ESW32712.1}; OS Phaseolus vulgaris (Kidney bean) (French bean). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae; OC Pentapetalae; rosids; fabids; Fabales; Fabaceae; Papilionoideae; OC Phaseoleae; Phaseolus. OX NCBI_TaxID=3885 {ECO:0000313|EMBL:ESW32712.1, ECO:0000313|Proteomes:UP000000226}; RN [1] {ECO:0000313|EMBL:ESW32712.1, ECO:0000313|Proteomes:UP000000226} RP NUCLEOTIDE SEQUENCE. RA Schmutz J., McClean P., Shu S., Cregan P., Rokhsar D., Jackson S.; RL Submitted (APR-2013) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CM002288; ESW32712.1; -; Genomic_DNA. DR RefSeq; XP_007160718.1; XM_007160656.1. DR GeneID; 18640023; -. DR KEGG; pvu:PHAVU_001G011200g; -. DR KO; K03665; -. DR PhylomeDB; V7CRA0; -. DR Proteomes; UP000000226; Chromosome 1. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000000226}; KW Reference proteome {ECO:0000313|Proteomes:UP000000226}. FT DOMAIN 328 494 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 553 AA; 61714 MW; 014CF9F681EC69B6 CRC64; MSGAAFLYGS LIHPPPPSPP SPPLIQQQRY HYLSPPIPIR PLCISPLTVA IVSTTSVLHR DSEVELASSS NDSSDAVSPQ NETVRLETER HTDETVQPPL SSEDKGTRLR KKKEDEVVSD NRFKLRNGRE VFEEKAYLVG VERKNDVQDF GNEESLSELA QLADTAGLLV VGSTYQKLTS PNPRTYIGSG KVSEIKSAIH ALDVETVIFD DELSAGQLRN LEKIFGGDVR VCDRTALILD IFNQRAATHE ASLQVSLAQM EYQLPRLTKM WTHLERQAGG KVKGMGEKQI EVDKRILRNQ IGILKKELES VRKHRKQYRS RRLSVPVPVV SLVGYTNAGK STLLNQLTGA DVLAEDKLFA TLDPTTRRVQ MKNGKEFLLT DTVGFIQKLP TTLVAAFRAT LEEISESSLM VHVVDISHPL AEQQINAVDK VLSELDVSSI PKLMVWNKVD KVSDPHKLRL EAEKRDDVVC ISAISGDGLQ EFCNAVQDRL KDSMVWVEAL VPFENGDLLS TIHQVGMVEK IEYTEQGTYI KAHVPLRFAR MLTPMRQLCV SRP // ID V7EPQ2_9RHOB Unreviewed; 412 AA. AC V7EPQ2; DT 19-FEB-2014, integrated into UniProtKB/TrEMBL. DT 19-FEB-2014, sequence version 1. DT 07-JUN-2017, entry version 24. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=Q27BPR15_02645 {ECO:0000313|EMBL:ESW62142.1}; OS Rhodobacter sp. CACIA14H1. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae; Rhodobacter. OX NCBI_TaxID=1408890 {ECO:0000313|EMBL:ESW62142.1, ECO:0000313|Proteomes:UP000018503}; RN [1] {ECO:0000313|EMBL:ESW62142.1, ECO:0000313|Proteomes:UP000018503} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=24435858; RA Lima A.R., Siqueira A.S., Dos Santos B.G., da Silva F.D., Inada D.T., RA Lima C.P., Cardoso J.F., Vianez-Junior J.L., Nunes M.R., RA Goncalves E.C.; RT "Draft Genome Sequence of Rhodobacter sp. Strain CACIA 14H1, a RT Heterotrophic Bacterium Obtained from a Nonaxenic Culture of a RT Cyanobium Species."; RL Genome Announc. 2:e01116-13(2014). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:ESW62142.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AYNO01000010; ESW62142.1; -; Genomic_DNA. DR PATRIC; fig|449393.3.peg.534; -. DR Proteomes; UP000018503; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000018503}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000018503}. FT DOMAIN 192 361 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 412 AA; 45696 MW; B2BAD3C5D6466AF5 CRC64; MLHPDIRNDR SRRLPEHGLA EAVSLAHALP ELDVVGGEVV RLPRVHPGML FGSGKVEELK ARFKADDIAL VLVDGPVSPV QQRNLEKEWG VKLLDRTGLI LEIFADRART REGVLQVELA ALSYQRTRLV RAWTHLERQR GGFGFVGGPG ETQIEADRRA IDDQVIRLKR QLDKVVKTRE LHRAARRKVP FPIVALVGYT NAGKSTLFNR ATGAEVLAKD MLFATLDPTM RGITLPSGRK IILSDTVGFI SDLPTQLVAA FRATLEEVLE ADLILHVRDI AHPETGEQAA DVADILQSLG VGPATPMFEI WNKLDLVAPA ERDALQAQAE TRDRVFPVSA LTGEGVPRLL DAISAAFDEE KTERTLAVPF TDGRRRAWLH AEGVVLAERA TDTGFAVDVR WTARQEKRYR EL // ID V7FPA1_9RHIZ Unreviewed; 463 AA. AC V7FPA1; DT 19-FEB-2014, integrated into UniProtKB/TrEMBL. DT 19-FEB-2014, sequence version 1. DT 07-JUN-2017, entry version 26. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=X759_06095 {ECO:0000313|EMBL:ESX82246.1}; OS Mesorhizobium sp. LSHC420B00. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Phyllobacteriaceae; Mesorhizobium. OX NCBI_TaxID=1287292 {ECO:0000313|EMBL:ESX82246.1, ECO:0000313|Proteomes:UP000018524}; RN [1] {ECO:0000313|EMBL:ESX82246.1, ECO:0000313|Proteomes:UP000018524} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=LSHC420B00 {ECO:0000313|EMBL:ESX82246.1, RC ECO:0000313|Proteomes:UP000018524}; RA Porter S.S., Chang P.L., Conow C.A., Dunham J.P., Friesen M.L.; RT "Adaptive variation in the core and flexible genome of wild RT Mesorhizobia."; RL Submitted (JUL-2013) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:ESX82246.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AYVY01000002; ESX82246.1; -; Genomic_DNA. DR RefSeq; WP_023717580.1; NZ_AYVY01000002.1. DR EnsemblBacteria; ESX82246; ESX82246; X759_06095. DR PATRIC; fig|381.35.peg.1239; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000018524; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000018524}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000018524}. FT DOMAIN 231 404 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 463 AA; 50934 MW; 0DFAAB9313711152 CRC64; MAREKDADRS VRGKPAHQTG TEANGPTRAV VIVPVLTRQP RGNDDTNRPR LTRSAEARRD EAVGLASAID LDLVHTAVVT VNDPRPATLL GSGKVAEFAE IVKEGHAEVV IVDHPLTPVQ QRNLEKELNA KVLDRTGLIL EIFGERARTK EGTLQVDLAH LNYQKGRLVR SWTHLERQRG GAGFLGGPGE TQIESDRRVL QDKITKLKHE LETVRRTRDL HRAKRKKVPF PVVAIVGYTN AGKSTLFNRL TGAGVLAEDM LFATLDPTLR RVRLRHGTPV ILSDTVGFIS DLPTHLVAAF RATLEEVVEA DLVIHLRDIS DPDTAAQAED VERILADLGV DARDSKRVIE VWNKIDRLDE GNRARLLADG ADGRKAPPIA ISAVTGEGID ALKAIIETMM SGELETFTVT LKADQLGVVD WLYRNGDIVS RDDNEDGSVT IALKATHSAR QEIESRLRRQ NNG // ID V7HUU5_9LACO Unreviewed; 421 AA. AC V7HUU5; DT 19-FEB-2014, integrated into UniProtKB/TrEMBL. DT 19-FEB-2014, sequence version 1. DT 07-JUN-2017, entry version 26. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=LEQ_1110c {ECO:0000313|EMBL:ETA73672.1}; OS Lactobacillus equi DPC 6820. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; OC Lactobacillus. OX NCBI_TaxID=1392007 {ECO:0000313|EMBL:ETA73672.1, ECO:0000313|Proteomes:UP000018559}; RN [1] {ECO:0000313|EMBL:ETA73672.1, ECO:0000313|Proteomes:UP000018559} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DPC 6820 {ECO:0000313|EMBL:ETA73672.1, RC ECO:0000313|Proteomes:UP000018559}; RX PubMed=24435863; RA O'Donnell M.M., Harris H.M., O'Toole P.W., Ross R.P.; RT "The Genome of the Predominant Equine Lactobacillus Species, RT Lactobacillus equi, Is Reflective of Its Lifestyle Adaptations to an RT Herbivorous Host."; RL Genome Announc. 2:e01155-13(2014). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:ETA73672.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AWWH01000164; ETA73672.1; -; Genomic_DNA. DR RefSeq; WP_023860101.1; NZ_AWWH01000164.1. DR EnsemblBacteria; ETA73672; ETA73672; LEQ_1110c. DR PATRIC; fig|1392007.3.peg.1503; -. DR Proteomes; UP000018559; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000018559}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000018559}. FT DOMAIN 198 366 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 421 AA; 46794 MW; 97CB698DC2AFD2C5 CRC64; MPQDITRVVI AGIDNEIENF SYTMQELKAL AQANYMKVVM EISQKLPKPV SGTYFGTGKA EEIKNAALAS EAETVIVNDE LTPTQIRNLE KLTDLTVIDR TALILQIFAS RARTKEAKLQ VQIAQLQYQL PRLHTSSATK LDQQSAGGGY SNRGAGETKL ELNRRVIEKR ISHLKAQLKD IDKDHQIQRK QRDSSGIKTV ALVGYTNAGK STTMNGLLRL TGQEDDKQVF EKDMLFATLD TSVRKIHFKD NKEILLSDTV GFVSKLPHQL VKSFRSTLAE AAQADLLIQV IDGSDENARD MIATTEETLK EIGVTEIPMI YAYNKADLAG QSYPLLAGDS FTYSARDQAS LEALIDLIKK EVFADYETHT YLIPFDQGRY VEALNQNAEI LATEYLPEGT QITANLAQDL AGKLQTFLVQ A // ID V7I5Q3_9CLOT Unreviewed; 596 AA. AC V7I5Q3; DT 19-FEB-2014, integrated into UniProtKB/TrEMBL. DT 19-FEB-2014, sequence version 1. DT 07-JUN-2017, entry version 26. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=T472_0212265 {ECO:0000313|EMBL:ETA80327.1}; OS Youngiibacter fragilis 232.1. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Youngiibacter. OX NCBI_TaxID=994573 {ECO:0000313|EMBL:ETA80327.1, ECO:0000313|Proteomes:UP000017747}; RN [1] {ECO:0000313|EMBL:ETA80327.1, ECO:0000313|Proteomes:UP000017747} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=232.1 {ECO:0000313|EMBL:ETA80327.1, RC ECO:0000313|Proteomes:UP000017747}; RX PubMed=24459265; RA Wawrik C.B., Callaghan A.V., Stamps B.W., Wawrik B.; RT "Genome Sequence of Youngiibacter fragilis, the Type Strain of the RT Genus Youngiibacter."; RL Genome Announc. 2:e01183-13(2014). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:ETA80327.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AXUN02000183; ETA80327.1; -; Genomic_DNA. DR RefSeq; WP_023387552.1; NZ_AXUN02000183.1. DR EnsemblBacteria; ETA80327; ETA80327; T472_0212265. DR PATRIC; fig|994573.3.peg.2283; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000017747; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000017747}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000017747}. FT DOMAIN 362 539 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 596 AA; 66669 MW; 82824A930DBB0CAA CRC64; MISGNIDGIR KRILDELETI FEIRTPKYQI ASQEITDLIS RLSGETEREI SVAIDRRGKV QEVTIGDSSS VSLPLLDVKE RKLSGTRIIH THPNGNPRLS ALDVSALLKM KLDCIAAIGL GEYPTMVIGF LTVDDGRLAA QATQPMDIQS ALSFDILDRI TFNESLMKQG ESISEPEERA VLAGIDTEDS LEELRELAKA CNLPVADMVI QNRERPDNAF YVGSGKVREI GERLQLTRSN VVIFDDELTG TQIRNLEEQL GVKVIDRTTL ILEIFARRAR SREAKLQVEL AQLKYRMNRL IGLGTVMSRT GGGIGTKGPG ETKLEIDRRR IREKVTDLTR ELSKITGVRE IQRENRETNE IQKVSLVGYT NAGKSTLRNA LYEISSKDSV VKEKVFEADM LFATLDTTTR AIALKDKRIV TLTDTVGFVR KLPHDIIEAF KSTLEEVVFS DLLVHVIDAS SDDAYKQAIT VDSVLEEIGC GDKDTIIALN KVDKGLSYVV EDIRELYEGK HKIIEISAKN GKNLEPLLDM IMEALPKTHS SIEVLVPYSE QKLLSSIRAR GIVIAEEYRE EGTYVKAEVP DRDLYMYEKF LVGGKK // ID V8CXK4_9ACTN Unreviewed; 478 AA. AC V8CXK4; DT 19-FEB-2014, integrated into UniProtKB/TrEMBL. DT 19-FEB-2014, sequence version 1. DT 07-JUN-2017, entry version 27. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=W823_16825 {ECO:0000313|EMBL:ETD32073.1}; OS Williamsia sp. D3. OC Bacteria; Actinobacteria; Corynebacteriales; Williamsiaceae; OC Williamsia. OX NCBI_TaxID=1313067 {ECO:0000313|EMBL:ETD32073.1, ECO:0000313|Proteomes:UP000018666}; RN [1] {ECO:0000313|EMBL:ETD32073.1, ECO:0000313|Proteomes:UP000018666} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=D3 {ECO:0000313|EMBL:ETD32073.1, RC ECO:0000313|Proteomes:UP000018666}; RX PubMed=24459282; RA Guerrero L.D., Makhalanyane T.P., Aislabie J.M., Cowan D.A.; RT "Draft Genome Sequence of Williamsia sp. Strain D3, Isolated From the RT Darwin Mountains, Antarctica."; RL Genome Announc. 2:e01230-13(2014). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:ETD32073.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AYTE01000026; ETD32073.1; -; Genomic_DNA. DR RefSeq; WP_023959666.1; NZ_AYTE01000026.1. DR EnsemblBacteria; ETD32073; ETD32073; W823_16825. DR PATRIC; fig|1313067.3.peg.3492; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000018666; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 2. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000018666}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000018666}. FT DOMAIN 251 420 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 478 AA; 51686 MW; ED43A789942CE1FD CRC64; MTEINKTGND QRDAPTIGEL QLDERSSLQR VAGLSTELTD VTEVEYRQLR LERVVLVGVW TQGSTTAQAN SSLAELKALA ETAGSEVLEG LIQRREKPDP ATYIGSGKAH ELREIVLATG ADTVICDGEL TPAQLTALEK VVKVKVVDRT ALILDIFAQH ATSREGKAQV ALAQMEYMLP RLRGWGESMS RQAGGRAGSN GGVGLRGPGE TKIETDRRRI RERTAKLRRE IREMKTSRTT KRAKRKQAAA SAVTIVGYTN AGKSSLINAL TGSGVLVQNA LFATLDPTTR QMSLEDGREL VITDTVGFVR HLPTQLVEAF RSTLEEVADA DLLLHIVDGS DPVPTDQIMA VRKVIESVLE EEKATAPPEL LVINKIDAAD PLVLAQLKGL FPTAVFISAA TGEGIDVLLD RIRESVARND VHVSVRVPYE RGDLVSRIHA EGDVLTERHE PDGTAITATV PAALSRQLAS LAIPEAAE // ID V8G7N0_9BURK Unreviewed; 367 AA. AC V8G7N0; DT 19-FEB-2014, integrated into UniProtKB/TrEMBL. DT 19-FEB-2014, sequence version 1. DT 07-JUN-2017, entry version 25. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=V757_06100 {ECO:0000313|EMBL:ETD72106.1}; OS Pelistega indica. OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Alcaligenaceae; Pelistega. OX NCBI_TaxID=1414851 {ECO:0000313|EMBL:ETD72106.1, ECO:0000313|Proteomes:UP000018766}; RN [1] {ECO:0000313|EMBL:ETD72106.1, ECO:0000313|Proteomes:UP000018766} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=HM-7 {ECO:0000313|EMBL:ETD72106.1, RC ECO:0000313|Proteomes:UP000018766}; RA Kumbhare S.V., Shetty S.A., Sharma O., Dhotre D.P.; RT "Genomic analysis of Pelistega sp. HM-7."; RL Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:ETD72106.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AYSV01000078; ETD72106.1; -; Genomic_DNA. DR RefSeq; WP_023950798.1; NZ_AYSV01000078.1. DR EnsemblBacteria; ETD72106; ETD72106; V757_06100. DR PATRIC; fig|1414851.3.peg.1238; -. DR Proteomes; UP000018766; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000018766}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000018766}. FT DOMAIN 190 356 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 156 183 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 367 AA; 40954 MW; D27899E50A3F46FA CRC64; MRAIIISVDF GNVDYPAHAQ EFAMLAKGAG AEIVATVVAK RDRPDAKFFI GSGKVDEIAL LIQSTNPDIV LFDQPLSPAQ QRNLERVFNL RVVDRVTLIL DIFALRAKSH EGKLQVELAQ LQHLVTRLTR MWTHLERQRG GIGMRGPGES QLEMDKRMIG DKVKSLKERL AKVEKQRATQ RRSRERSNTL SVSLVGYTNA GKSTLFNALT RAGAYAADQL FATLDTTTRR IWLENAGQVT ISDTVGFIRD LPTTLIAAFK ATLEETVHAD LLLHVIDAAS PQRDEQIIEV NKVLQEIGAQ DIPTILVYNK IDMLSYDPKV ERDEEGNIVR VFVSAQKREG LDGLRLAMAE AKTQLLGTTN IETDEHF // ID V8NKP0_OPHHA Unreviewed; 541 AA. AC V8NKP0; DT 19-FEB-2014, integrated into UniProtKB/TrEMBL. DT 19-FEB-2014, sequence version 1. DT 07-JUN-2017, entry version 16. DE SubName: Full=Putative GTP-binding protein 6 {ECO:0000313|EMBL:ETE62854.1}; DE Flags: Fragment; GN Name=GTPBP6 {ECO:0000313|EMBL:ETE62854.1}; GN ORFNames=L345_11389 {ECO:0000313|EMBL:ETE62854.1}; OS Ophiophagus hannah (King cobra) (Naja hannah). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; OC Toxicofera; Serpentes; Colubroidea; Elapidae; Elapinae; Ophiophagus. OX NCBI_TaxID=8665 {ECO:0000313|EMBL:ETE62854.1, ECO:0000313|Proteomes:UP000018936}; RN [1] {ECO:0000313|EMBL:ETE62854.1, ECO:0000313|Proteomes:UP000018936} RP NUCLEOTIDE SEQUENCE. RC TISSUE=Blood {ECO:0000313|EMBL:ETE62854.1}; RX PubMed=24297900; DOI=10.1073/pnas.1314702110; RA Vonk F.J., Casewell N.R., Henkel C.V., Heimberg A.M., Jansen H.J., RA McCleary R.J., Kerkkamp H.M., Vos R.A., Guerreiro I., Calvete J.J., RA Wuster W., Woods A.E., Logan J.M., Harrison R.A., Castoe T.A., RA de Koning A.P., Pollock D.D., Yandell M., Calderon D., Renjifo C., RA Currier R.B., Salgado D., Pla D., Sanz L., Hyder A.S., Ribeiro J.M., RA Arntzen J.W., van den Thillart G.E., Boetzer M., Pirovano W., RA Dirks R.P., Spaink H.P., Duboule D., McGlinn E., Kini R.M., RA Richardson M.K.; RT "The king cobra genome reveals dynamic gene evolution and adaptation RT in the snake venom system."; RL Proc. Natl. Acad. Sci. U.S.A. 110:20651-20656(2013). CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:ETE62854.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AZIM01003029; ETE62854.1; -; Genomic_DNA. DR Proteomes; UP000018936; Unassembled WGS sequence. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR CDD; cd01878; HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 4: Predicted; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000018936}; KW Reference proteome {ECO:0000313|Proteomes:UP000018936}. FT DOMAIN 315 479 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 281 311 {ECO:0000256|SAM:Coils}. FT NON_TER 1 1 {ECO:0000313|EMBL:ETE62854.1}. SQ SEQUENCE 541 AA; 61477 MW; 4D7F39FF0A7ABBA0 CRC64; MGSRWRQLQC LLQVLRPEVR LLPASCQWRN PVRFWHNSAV NYRQPPAGNG PARGKSGVGT LSSWGTEDNE DGDLVDNDDN EEEDDDDDDD EEEDLDVEDK LLEESRLPFV TLETQRVFIV HPAVKWGPDK PKLTTAELQL AEAVTLINTL QNWTVIDKII LPIQIPDKKF IFHKGNFQLL TEKIKRLPFL SSVFVNVEML SPVTKKELEK AWGVKVFDRY TIVLHIFRCN AQTKEAKLQI ALAELPLLRT NVRNEVAQLD QQRGGSRYIM GSGETFMEIQ LRLLKEKEIK IRKALRKLKK NRSLLRKQRN KCEFPIISVM GYTNCGKTTL IKALTGDAKL QPRDQLFATL DITAHAGYLP SRLTVLYVDT IGFLSQLPHN LVESFSATLE DVAFSDLIVH VRDVSHPETS LQKKTVLSVL KNLNIPNHLL ESIIEVHNKV DLVDRYQPTE QNAIVTSALL GHGLKELKEE IEARVLKGTG KKIMTIKINL SGPQLSWLYK EAVVQEVDVA PEDNTAKVKV IISDSALWKC KRLFPRSSYL S // ID V9G661_9BACL Unreviewed; 428 AA. AC V9G661; DT 19-FEB-2014, integrated into UniProtKB/TrEMBL. DT 19-FEB-2014, sequence version 1. DT 07-JUN-2017, entry version 25. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=JCM10914_1439 {ECO:0000313|EMBL:GAE05343.1}; OS Paenibacillus sp. JCM 10914. OC Bacteria; Firmicutes; Bacilli; Bacillales; Paenibacillaceae; OC Paenibacillus. OX NCBI_TaxID=1236974 {ECO:0000313|EMBL:GAE05343.1, ECO:0000313|Proteomes:UP000018028}; RN [1] {ECO:0000313|EMBL:GAE05343.1, ECO:0000313|Proteomes:UP000018028} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=JCM 10914 {ECO:0000313|EMBL:GAE05343.1, RC ECO:0000313|Proteomes:UP000018028}; RA Ohkuma M., Yuki M., Oshima K., Suda W., Oshida Y., Kitamura K., RA Iida T., Hattori M.; RT "Draft Genome Sequence of the Alkaliphilic and Xylanolytic RT Paenibacillus sp. Strain JCM 10914, Isolated from the Gut of a Soil- RT Feeding Termite."; RL Genome Announc. 2:e01144-13(2014). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:GAE05343.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BAUO01000003; GAE05343.1; -; Genomic_DNA. DR RefSeq; WP_023958597.1; NZ_BAZR01000003.1. DR EnsemblBacteria; GAE05343; GAE05343; JCM10914_1439. DR Proteomes; UP000018028; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000018028}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000018028}. FT DOMAIN 208 372 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 174 201 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 428 AA; 47728 MW; 83D9EF73D56EAD0C CRC64; MTNITHDTRT EIEDKAVLVS LVTDAVKRSG INPEHSLQEL VQLAETAGVE VLDVITQNKE TPDSRWFIGK GKVEELRMAI DGLGATTAIF DQELSGAQVR NLEETLDVKI IDRTQLILDI FAQRAKTREG IIQVELAQLT YLLPRLSGHG KNLSRLGAGI GTRGPGESKL EMDRRHIRDR ISDLKRQLDE VTRHRNLHRE RRKKSGAVQV ALVGYTNAGK STLLNRLTDA EVYIEDQLFA TLDPTSRVLE LPSGKEVVLT DTVGFIQNLP HDLVAAFRAT LEEANEADLI LHVVDSSSPM REEQMKVVEN ILGELGAADK PQLVLFNKKD ACSPEQLEML PSGDGYLKIS AYQDQDLAAV REAIQERLSG GNLTFRIPAD RGDLNSVVYR VGDVLEQSFD ETDILYEVSI NKADYDKLGY MLKDYVQQ // ID V9H633_9NEIS Unreviewed; 378 AA. AC V9H633; DT 19-FEB-2014, integrated into UniProtKB/TrEMBL. DT 19-FEB-2014, sequence version 1. DT 07-JUN-2017, entry version 26. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=HMPREF9021_00559 {ECO:0000313|EMBL:EFG31291.2}; OS Simonsiella muelleri ATCC 29453. OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Simonsiella. OX NCBI_TaxID=641147 {ECO:0000313|EMBL:EFG31291.2, ECO:0000313|Proteomes:UP000017813}; RN [1] {ECO:0000313|EMBL:EFG31291.2, ECO:0000313|Proteomes:UP000017813} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29453 {ECO:0000313|EMBL:EFG31291.2, RC ECO:0000313|Proteomes:UP000017813}; RG The Broad Institute Genome Sequencing Platform; RA Ward D., Earl A., Feldgarden M., Gevers D., Young S., Zeng Q., RA Koehrsen M., Alvarado L., Berlin A.M., Borenstein D., Chapman S.B., RA Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A., RA Gujja S., Heilman E.R., Heiman D.I., Hepburn T.A., Howarth C., Jen D., RA Larson L., Mehta T., Park D., Pearson M., Richards J., Roberts A., RA Saif S., Shea T.D., Shenoy N., Sisk P., Stolte C., Sykes S.N., RA Walk T., White J., Yandava C., Izard J., Baranova O.V., Blanton J.M., RA Tanner A.C., Dewhirst F., Haas B., Nusbaum C., Birren B.; RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:EFG31291.2, ECO:0000313|Proteomes:UP000017813} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29453 {ECO:0000313|EMBL:EFG31291.2, RC ECO:0000313|Proteomes:UP000017813}; RG The Broad Institute Genome Sequencing Platform; RG The Broad Institute Genome Sequencing Center for Infectious Disease; RA Earl A., Ward D., Feldgarden M., Gevers D., Izard J., Baranova O.V., RA Blanton J.M., Tanner A.C., Dewhirst F., Young S.K., Zeng Q., RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L., RA Arachchi H.M., Berlin A., Brown A., Chapman S.B., Chen Z., Dunbar C., RA Freedman E., Gearin G., Goldberg J., Griggs A., Gujja S., Heiman D., RA Howarth C., Larson L., Lui A., MacDonald P.J.P., Montmayeur A., RA Murphy C., Neiman D., Pearson M., Priest M., Roberts A., Saif S., RA Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., Wortman J., RA Nusbaum C., Birren B.; RT "The Genome Sequence of Simonsiella muelleri ATCC 29453."; RL Submitted (OCT-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EFG31291.2}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADCY02000009; EFG31291.2; -; Genomic_DNA. DR RefSeq; WP_002641345.1; NZ_JH815301.1. DR STRING; 641147.HMPREF9021_00559; -. DR EnsemblBacteria; EFG31291; EFG31291; HMPREF9021_00559. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000017813; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000017813}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000017813}. FT DOMAIN 213 378 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 179 206 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 378 AA; 42119 MW; 5F22A85BBA7C94A8 CRC64; MTRFRTDKSL EHAERIMLVS VMLPENYSGA NEIRERTFQA ACLEAAELVR ATGGELIAHE TAKREKAHTA LFVGTGKAEE LAKLVEQNQI ELVIFNHELS PTQERNLEKA LQCRVLDRVG LILAIFAQRA QSQEGKLQVE LAQLSHLSSR LVRGYKHLQS QKGGIGLKGP GETQLETDRR LIQNKINFLK KQLDNVKKQR ETRRKARLSG SLKTFAIVGY TNAGKSTLFN RLTKADVFAQ DQLFATLDTT ARRLYLNPET SIILTDTVGF VQNLPHKLVS AFAATLEETA LADVLLHVVD ASDPEYERKI QDVNHVLREI KADKIPQLVI YNKQDLLPAA EQSSGCLKNY VGKTVAVGVS AVSGMGLEDL RQALIEWA // ID V9HDH3_9CLOT Unreviewed; 598 AA. AC V9HDH3; DT 19-FEB-2014, integrated into UniProtKB/TrEMBL. DT 19-FEB-2014, sequence version 1. DT 07-JUN-2017, entry version 28. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=CSBG_01093 {ECO:0000313|EMBL:EEH97467.1}; OS Clostridium sp. 7_2_43FAA. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=457396 {ECO:0000313|EMBL:EEH97467.1, ECO:0000313|Proteomes:UP000017809}; RN [1] {ECO:0000313|EMBL:EEH97467.1, ECO:0000313|Proteomes:UP000017809} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=7_2_43FAA {ECO:0000313|EMBL:EEH97467.1, RC ECO:0000313|Proteomes:UP000017809}; RG The Broad Institute Genome Sequencing Platform; RA Earl A., Ward D., Feldgarden M., Gevers D., Allen-Vercoe E., RA Strauss J., Ambrose C., Young S.K., Zeng Q., Gargeya S., RA Fitzgerald M., Haas B., Abouelleil A., Alvarado L., Arachchi H.M., RA Berlin A., Chapman S.B., Gearin G., Goldberg J., Griggs A., Gujja S., RA Hansen M., Heiman D., Howarth C., Larimer J., Lui A., RA MacDonald P.J.P., McCowen C., Montmayeur A., Murphy C., Neiman D., RA Pearson M., Priest M., Roberts A., Saif S., Shea T., Sisk P., RA Stolte C., Sykes S., Wortman J., Nusbaum C., Birren B.; RT "The Genome Sequence of Clostridium sp. 7_2_43FAA."; RL Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EEH97467.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACDK02000032; EEH97467.1; -; Genomic_DNA. DR RefSeq; WP_008679475.1; NZ_JH815222.1. DR ProteinModelPortal; V9HDH3; -. DR STRING; 457396.CSBG_01093; -. DR EnsemblBacteria; EEH97467; EEH97467; CSBG_01093. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000017809; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000017809}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000017809}. FT DOMAIN 364 541 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 598 AA; 67253 MW; 2A3C5A18AF14B926 CRC64; MIFGNIDGIK KTYLDELERL YKVKVLKDEA CSVEIIEVIS RLTSILDREI SVAVDRRGKV VSVAIGDSTS VEVSMIDIRE KRLSGVRVIH THPNGFSNLS ALDISALLKL KLDAIMAIGV HEGNVTDCSL GMITISDDLL DYEEKLNLTI EEVLSIHILD KIQHIESMIK EKDIIEDEGE KAILVGSDTK ESLEELKELT KACDIPVLDS VYQSRSKIDP AFYIGKGKVL EIASLRQSKH ANLIIFDDEL SGSQVRNLEA ATGAKVIDRT TLILEIFARR ARSKESKIQV ELAQLKYRMS RLQGLGTVLS RTGGGIGTRG PGEKKLETDR RHIKETIYDL NDELKKIKKT REVQREKRTK ESIPRVSLVG YTNAGKSTLR NKLCDVAAQK EIQGKEKVFE ADMLFATLDI TTRSIILKNK GVVTITDTVG FVRKLPHDLV EAFKSTLEEV IYSDLLCHVV DTSSDSALDQ IKAVEEVLEE LGAKGKETIL VLNKIDRATE EQVEEVKKAC SEYKIIEISA KEGINLDNLL DLIEEKLPYK MKKCEYLIPY DRSDMNSYLH RNGRVLEEDY RDNGTFMIVE VDDEAYNKSS DFIINILT // ID V9VVM9_9RHOB Unreviewed; 423 AA. AC V9VVM9; DT 19-MAR-2014, integrated into UniProtKB/TrEMBL. DT 19-MAR-2014, sequence version 1. DT 07-JUN-2017, entry version 25. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=METH_09865 {ECO:0000313|EMBL:AHD00942.1}; OS Leisingera methylohalidivorans DSM 14336. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae; Leisingera. OX NCBI_TaxID=999552 {ECO:0000313|EMBL:AHD00942.1, ECO:0000313|Proteomes:UP000018780}; RN [1] {ECO:0000313|EMBL:AHD00942.1, ECO:0000313|Proteomes:UP000018780} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 14336 {ECO:0000313|EMBL:AHD00942.1, RC ECO:0000313|Proteomes:UP000018780}; RG DOE Joint Genome Institute; RA Klenk H.-P., Huntemann M., Han J., Chen A., Kyrpides N., RA Mavromatis K., Markowitz V., Palaniappan K., Ivanova N., RA Schaumberg A., Pati A., Liolios K., Nordberg H.P., Cantor M.N., RA Hua S.X., Woyke T.; RL Submitted (SEP-2013) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP006773; AHD00942.1; -; Genomic_DNA. DR RefSeq; WP_024090223.1; NC_023135.1. DR EnsemblBacteria; AHD00942; AHD00942; METH_09865. DR KEGG; lmd:METH_09865; -. DR PATRIC; fig|999552.6.peg.1968; -. DR KO; K03665; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000018780; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000018780}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000018780}. FT DOMAIN 203 372 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 423 AA; 47064 MW; 61B8EC2BF67A3458 CRC64; MEHERTRTRA WVLHPEIKSD SGRREAAPAL DEAIALAAAL PDLDVIGSNV VRLPKAHAGM LFGSGKIEEL AGILKANEVE LVLIDGSVSP VQQRNLEKAW KVKILDRTGL ILEIFSDRAA TREGVLQVEM AALSYQRTRL VRAWTHLERQ RGGLGFVGGP GETQIEADRR AIDDQLVRLR RQLDKVVKTR TLHRASRAKV PYPIVALVGY TNAGKSTLFN RLTGAEVMAK DMLFATLDPT MRRVQIPDGP EVILSDTVGF ISDLPTELVA AFRATLEEVL AADVILHVRD ISHDESKQQA ADVEAILASL GVDENRARIE VWNKLDQLPA EDAEARRQRA EREDGIHAIS ALTGEGLDGL LADIAEQLQG VRHEELLKLT FAEGKQRAWL FREDLVQSEE QTETGFDITV LWTDRQKAKF ERL // ID V9W9M3_9BACL Unreviewed; 437 AA. AC V9W9M3; DT 19-MAR-2014, integrated into UniProtKB/TrEMBL. DT 19-MAR-2014, sequence version 1. DT 07-JUN-2017, entry version 28. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:AHD06400.1}; GN ORFNames=ERIC2_c26130 {ECO:0000313|EMBL:AHD06400.1}; OS Paenibacillus larvae subsp. larvae DSM 25430. OC Bacteria; Firmicutes; Bacilli; Bacillales; Paenibacillaceae; OC Paenibacillus. OX NCBI_TaxID=697284 {ECO:0000313|EMBL:AHD06400.1, ECO:0000313|Proteomes:UP000029431}; RN [1] {ECO:0000313|EMBL:AHD06400.1, ECO:0000313|Proteomes:UP000029431} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 25430 {ECO:0000313|EMBL:AHD06400.1, RC ECO:0000313|Proteomes:UP000029431}; RX PubMed=24599066; RA Djukic M., Brzuszkiewicz E., Funfhaus A., Voss J., Gollnow K., RA Poppinga L., Liesegang H., Garcia-Gonzalez E., Genersch E., Daniel R.; RT "How to Kill the Honey Bee Larva: Genomic Potential and Virulence RT Mechanisms of Paenibacillus larvae."; RL PLoS ONE 9:E90914-E90914(2014). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP003355; AHD06400.1; -; Genomic_DNA. DR EnsemblBacteria; AHD06400; AHD06400; ERIC2_c26130. DR KEGG; plv:ERIC2_c26130; -. DR PATRIC; fig|697284.3.peg.2496; -. DR KO; K03665; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000029431; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000029431}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000029431}. FT DOMAIN 216 380 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 175 202 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 437 AA; 49729 MW; 89C447E05E029A19 CRC64; MNLRRRIELK PSMHETEMNK QDRAILVSLV TQTFKHYEAL AEYSLQELIQ LAETAGVEVL ETMTQSREVP DSRWFIGKGK AEELKNRIEE TGANTAIFDQ ELSGAQVRNL EALLDVKIID RTQLILDIFA QRAKTREGII QVELAQLSYL LPRLSGHGKN LSRLGGGIGT RGPGESKLET DRRHIRRRIN ELKSQLQEVV KHRNLHRARR KKSGVVQVAL VGYTNAGKST LLRELTQADV YVENQLFATL DPTSRTMKLP SGKDIVLTDT VGFIQNLPHD LIAAFRATLE EANEADLILH VVDSSSKMRQ EQMRVVDEVL EELGASGKPA ITVFNKIDLI PEKEQDMLTS PGKFLRLSAY QESDLERLKQ TIQDYVMGDS KEFLIPSTEG GIISLLYRIG DVEEEGMEAN SMKFRIHIQE EEYQKVRHRL EQYELKQ // ID V9XBR6_9NOCA Unreviewed; 488 AA. AC V9XBR6; DT 19-MAR-2014, integrated into UniProtKB/TrEMBL. DT 19-MAR-2014, sequence version 1. DT 07-JUN-2017, entry version 27. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=Y013_01575 {ECO:0000313|EMBL:AHD19484.1}; OS Rhodococcus pyridinivorans SB3094. OC Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae; OC Rhodococcus. OX NCBI_TaxID=1435356 {ECO:0000313|EMBL:AHD19484.1, ECO:0000313|Proteomes:UP000018781}; RN [1] {ECO:0000313|EMBL:AHD19484.1, ECO:0000313|Proteomes:UP000018781} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SB3094 {ECO:0000313|EMBL:AHD19484.1}; RX PubMed=24874690; RA Dueholm M.S., Albertsen M., D'Imperio S., Tale V.P., Lewis D., RA Nielsen P.H., Nielsen J.L.; RT "Complete Genome of Rhodococcus pyridinivorans SB3094, a Methyl-Ethyl- RT Ketone-Degrading Bacterium Used for Bioaugmentation."; RL Genome Announc. 2:e00525-14(2014). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP006996; AHD19484.1; -; Genomic_DNA. DR RefSeq; WP_006551306.1; NC_023150.1. DR EnsemblBacteria; AHD19484; AHD19484; Y013_01575. DR GeneID; 29940772; -. DR KEGG; rpy:Y013_01575; -. DR PATRIC; fig|1435356.3.peg.312; -. DR KO; K03665; -. DR Proteomes; UP000018781; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 2. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000018781}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000018781}. FT DOMAIN 266 435 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 225 259 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 488 AA; 52696 MW; F3E44AB3513B1B5A CRC64; MTNTQRMHRA TTDDSTPTAY DASGGWTAED PSVGEMQLED RSALRRVAGL STELEDITEV EYRQLRLERV VLVGVWTGGT AAQAEASLAE LAALAETAGS EVLEGLVQRR DRPDASTYIG SGKADELREI VLSTGADTVI CDGELTPAQL TALEKVVKVK VIDRTALILD IFAQHATSRE GKAQVSLAQM EYMLPRLRGW GESMSRQAGG RAGSNGGVGL RGPGETKIET DRRRIRERMA KLRREIKAMK AARDTKRTRR LRNKIPSVAI VGYTNAGKSS LLNKLTGSGV LVQNALFATL DPTTRRSALP DGREYVLTDT VGFVRHLPTQ LVEAFRSTLE EVADADVLLH VVDGSDPMPT EQIKAVREVV TEVLRESDAP PPPELIVVNK IDAADPVTLT QLRSAIPGAV FVSAHTGVGV EELQTQLAGL LEDPDVEVKL LLPYTRGDLL ARIHSDGQIL SSEHEVDGTR VHAKVPAALA SALVDFAA // ID W0A784_9SPHN Unreviewed; 432 AA. AC W0A784; DT 19-MAR-2014, integrated into UniProtKB/TrEMBL. DT 19-MAR-2014, sequence version 1. DT 07-JUN-2017, entry version 23. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=NX02_10410 {ECO:0000313|EMBL:AHE53799.1}; OS Sphingomonas sanxanigenens DSM 19645 = NX02. OC Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales; OC Sphingomonadaceae; Sphingomonas. OX NCBI_TaxID=1123269 {ECO:0000313|EMBL:AHE53799.1, ECO:0000313|Proteomes:UP000018851}; RN [1] {ECO:0000313|EMBL:AHE53799.1, ECO:0000313|Proteomes:UP000018851} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NX02 {ECO:0000313|EMBL:AHE53799.1, RC ECO:0000313|Proteomes:UP000018851}; RA Ma T., Huang H., Wu M., Li X., Li G.; RT "Completed genome of Sphingomonas sanxanigenens NX02."; RL Submitted (JUL-2013) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP006644; AHE53799.1; -; Genomic_DNA. DR RefSeq; WP_025292028.1; NZ_CP006644.1. DR EnsemblBacteria; AHE53799; AHE53799; NX02_10410. DR KEGG; ssan:NX02_10410; -. DR PATRIC; fig|1123269.5.peg.2017; -. DR KO; K03665; -. DR Proteomes; UP000018851; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000018851}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000018851}. FT DOMAIN 208 379 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 174 201 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 432 AA; 47228 MW; 53CC73F02682BF68 CRC64; MSGFRREEDE FRRGAKAVVA YPDMGKGGDR DVEARLDEAA GLAEAIGIDV VDRIAYRVRQ PRPATLFGAG QVEALATVAR AHEAELVVVD GAVTPVQQRN LEEELKTKVI DRTGLILEIF GERAATAEGR LQVELAHLDY QAGRLVRSWT HLERQRGGFG FLGGPGETQI EADRRMIRDR MAKLRRELEQ VSRTRGLHRE RRRRAPWPVV GLVGYTNAGK STLFNRLTGA GVMAEDLLFA TLDPTMRQIT LPGLDKAILS DTVGFVSDLP TQLVAAFRAT LEEVTSADLI VHVRDIAHPD SDAQATDVEQ VLAEIGVSGD GAAPRIEAWN KVDLLDPETQ AALAAEAARR DDVVLISAQT GEGVEALRRM MSTRLTATAR VRHIDLPIAD GAAAAWLHAH GEVLTQDADG ETIHLDVRLS ETDWARFQSR GA // ID W0BB03_9GAMM Unreviewed; 416 AA. AC W0BB03; DT 19-MAR-2014, integrated into UniProtKB/TrEMBL. DT 19-MAR-2014, sequence version 1. DT 07-JUN-2017, entry version 23. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:AHE65609.1}; GN ORFNames=Loa_00018 {ECO:0000313|EMBL:AHE65609.1}; OS Legionella oakridgensis ATCC 33761 = DSM 21215. OC Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales; OC Legionellaceae; Legionella. OX NCBI_TaxID=1268635 {ECO:0000313|EMBL:AHE65609.1, ECO:0000313|Proteomes:UP000018838}; RN [1] {ECO:0000313|EMBL:AHE65609.1, ECO:0000313|Proteomes:UP000018838} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33761 {ECO:0000313|EMBL:AHE65609.1}; RX PubMed=23932911; DOI=10.1016/j.ijmm.2013.07.003; RA Brzuszkiewicz E., Schulz T., Rydzewski K., Daniel R., Gillmaier N., RA Dittmann C., Holland G., Schunder E., Lautner M., Eisenreich W., RA Luck C., Heuner K.; RT "Legionella oakridgensis ATCC 33761 genome sequence and phenotypic RT characterization reveals its replication capacity in amoebae."; RL Int. J. Med. Microbiol. 303:514-528(2013). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP004006; AHE65609.1; -; Genomic_DNA. DR RefSeq; WP_025384620.1; NZ_CP004006.1. DR EnsemblBacteria; AHE65609; AHE65609; Loa_00018. DR KEGG; lok:Loa_00018; -. DR PATRIC; fig|1268635.3.peg.18; -. DR KO; K03665; -. DR Proteomes; UP000018838; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000018838}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000018838}. FT DOMAIN 198 363 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 164 191 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 416 AA; 46970 MW; 079E8724D1F0E0E9 CRC64; MFERPKSGER AVLVQLALPE IDTDTALAEF EELATSAQAD VVSHVRGARA TPEPKYYIGQ GKAEEVRQQI LAHEAELVLV NHELSPSQER NLERLLQCRV VDRTGLILDI FAQRARTFEG KLQVELAQLQ HLSTRLVRGW THLERQKGGI GLRGPGETQL ETDRRLLRER IKTIQKRLEK VRRNRDQSRQ ARRRAAMPTV SLVGYTNAGK SSLFNALTGA DLYSANQLFA TLDPTMRKLD IPGSASIILA DTVGFIRDLP HQLVDAFRAT LEEIKESDLL LHIIDVSDPS WREHVIAVEH VLKEINAEKI KIIQVFNKID RQEGWQPKSD CSEKSCKVWL SATTGAGLDL LLDTIAQQLH GTVIEEEIEL GAHEARLRAQ LYKLAAVVHE ELMPEGGWRL LIRISPTEKQ RLFQEG // ID W0DBI8_9AQUI Unreviewed; 370 AA. AC W0DBI8; DT 19-MAR-2014, integrated into UniProtKB/TrEMBL. DT 19-MAR-2014, sequence version 1. DT 07-JUN-2017, entry version 27. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=THERU_03335 {ECO:0000313|EMBL:AHE95874.1}; OS Thermocrinis ruber. OC Bacteria; Aquificae; Aquificales; Aquificaceae; Thermocrinis. OX NCBI_TaxID=75906 {ECO:0000313|Proteomes:UP000018914}; RN [1] {ECO:0000313|EMBL:AHE95874.1, ECO:0000313|Proteomes:UP000018914} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 23557 {ECO:0000313|EMBL:AHE95874.1, RC ECO:0000313|Proteomes:UP000018914}; RG DOE Joint Genome Institute; RA Eisen J., Huntemann M., Han J., Chen A., Kyrpides N., Mavromatis K., RA Markowitz V., Palaniappan K., Ivanova N., Schaumberg A., Pati A., RA Liolios K., Nordberg H.P., Cantor M.N., Hua S.X., Woyke T.; RL Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP007028; AHE95874.1; -; Genomic_DNA. DR RefSeq; WP_025305853.1; NZ_CP007028.1. DR EnsemblBacteria; AHE95874; AHE95874; THERU_03335. DR KEGG; trd:THERU_03335; -. DR PATRIC; fig|75906.3.peg.645; -. DR KO; K03665; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000018914; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000018914}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}. FT DOMAIN 196 366 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 151 185 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 370 AA; 41949 MW; 5A9CCC34A428386C CRC64; MKAILVFLLS SETKEEFREY LEELKELVRA VGGKVLGYIY QRRHSPDPRY YIGAGKAQEL KEIISGTGAD CVVFDSFLSP SQVANLEELL KVKVFDRADL VLEIFSRRVR SKTAKLQVEL ARLTHELPRL YGRGKELSRL GGKVGTRGPG EQEVEIKRRA IKRKIEQIKK ELEEVKRQRR EQRKRRERPL GDTKVVKVAL VGYTNVGKSS LMQALTGRET YIQDMPFATL DTKTSAKFLF PDIKILITDT VGFIRKLPPE LIESFKATLE EVQEADILLH VIDISDPKWL EKVKVVQGIL KELSADDKPT IYVFNKADKV VSKEEDIKLL TEPAFLEGRC VVVSSKLGWG LGELLKAIRE KVEELAGASL // ID W0DSX5_9GAMM Unreviewed; 436 AA. AC W0DSX5; DT 19-MAR-2014, integrated into UniProtKB/TrEMBL. DT 19-MAR-2014, sequence version 1. DT 07-JUN-2017, entry version 23. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=THIAE_07080 {ECO:0000313|EMBL:AHF01552.1}; OS Thioalkalimicrobium aerophilum AL3. OC Bacteria; Proteobacteria; Gammaproteobacteria; Thiotrichales; OC Piscirickettsiaceae; Thioalkalimicrobium. OX NCBI_TaxID=717772 {ECO:0000313|EMBL:AHF01552.1, ECO:0000313|Proteomes:UP000005380}; RN [1] {ECO:0000313|EMBL:AHF01552.1, ECO:0000313|Proteomes:UP000005380} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=AL2 {ECO:0000313|Proteomes:UP000005380}; RG DOE Joint Genome Institute; RA Kappler U., Huntemann M., Han J., Chen A., Kyrpides N., Mavromatis K., RA Markowitz V., Palaniappan K., Ivanova N., Schaumberg A., Pati A., RA Liolios K., Nordberg H.P., Cantor M.N., Hua S.X., Woyke T.; RL Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP007030; AHF01552.1; -; Genomic_DNA. DR RefSeq; WP_006461092.1; NZ_CP007030.1. DR EnsemblBacteria; AHF01552; AHF01552; THIAE_07080. DR KEGG; tao:THIAE_07080; -. DR KO; K03665; -. DR Proteomes; UP000005380; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000005380}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000005380}. FT DOMAIN 202 370 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 161 188 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 436 AA; 49004 MW; 5932F7E9C444233C CRC64; MELFGRLERK QLDVAILVHV DFEDETCREE LTEFLELVES AGAEQAELVK TKRDRPDAKL FIGSGKLDEV AAAVALHQAD VVIFNHALSP GQERNIERVV KARVIDRVGL ILDIFAQRAR SHEGKLQVEL AQLRHMSTRL VRGWTHLERQ KGGIGLRGPG ETQLESDKRL LQERIKHLLK RIEKVRKQRA LGRQSRQRSD HPTITLVGYT NAGKSTLFNQ LTAADVYAEN RLFATLDATL RSVHLPGGGQ AILADTVGFI RHIPHDLVTA FRSTLEETSE ADLLIHLIDA ADPLRDDKIA QVQQVITEVG ANDVPQLLVF NKIDLLKPAV EPHVDFDEEG QPARVWISAQ NNLGLDYLKD ALASFFKGQF VRIFIKLGAE AGHRRAQLYA LGKVEQEASD DDGTIGLQVY LTEQQYHQVS KWPECQYIEK LQEAVV // ID W0DZ75_MARPU Unreviewed; 428 AA. AC W0DZ75; DT 19-MAR-2014, integrated into UniProtKB/TrEMBL. DT 19-MAR-2014, sequence version 1. DT 07-JUN-2017, entry version 23. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=MARPU_07605 {ECO:0000313|EMBL:AHF03737.1}; OS Marichromatium purpuratum 984. OC Bacteria; Proteobacteria; Gammaproteobacteria; Chromatiales; OC Chromatiaceae; Marichromatium. OX NCBI_TaxID=765910 {ECO:0000313|EMBL:AHF03737.1, ECO:0000313|Proteomes:UP000005275}; RN [1] {ECO:0000313|EMBL:AHF03737.1, ECO:0000313|Proteomes:UP000005275} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=984 {ECO:0000313|EMBL:AHF03737.1, RC ECO:0000313|Proteomes:UP000005275}; RG DOE Joint Genome Institute; RA Bryant D.A., Huntemann M., Han J., Chen A., Kyrpides N., RA Mavromatis K., Markowitz V., Palaniappan K., Ivanova N., RA Schaumberg A., Pati A., Liolios K., Nordberg H.P., Cantor M.N., RA Hua S.X., Woyke T.; RL Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP007031; AHF03737.1; -; Genomic_DNA. DR RefSeq; WP_005223726.1; NZ_CP007031.1. DR STRING; 765910.MarpuDRAFT_1881; -. DR EnsemblBacteria; AHF03737; AHF03737; MARPU_07605. DR KEGG; mpur:MARPU_07605; -. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR KO; K03665; -. DR Proteomes; UP000005275; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000005275}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000005275}. FT DOMAIN 199 366 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 428 AA; 47148 MW; 2B30715D240E74E1 CRC64; MFERPDVGER AVLVQIDLGG ERVDAEQREE FALLAEAAGA EVLATLGGSR AAPDPRYFLG SGKAEELKDL VAACTADLVI VDHPLSPAQE RNLERLVQCR VLDRSGLILD IFAQRARSFE GKLQVELAQL RHLSTRLVRG WTHLERQKGG IGLRGPGETQ LETDRRLLGK RVAMLERRLG KIEGQRAQGR KARAKAELSV VSLVGYTNAG KSTLFNRLTE AGVFQADQLF ATLDPTLRRL ELPTGERALL ADTVGFVSDL PHELVAAFRS TLEEARNAAL LLHVIDAAAT QRSRLITDVE QVLEEIGCSE IPRLEVFNKI DRLEEGAPRL ERDAEGVPVR VWISAREGEG IELLLQAIAE RVGGQRVECR VRLEPADGRV RALLFAHAQI LADTPLESGG WEMAFSIARA DLERLRARDA RLAACVEP // ID W0E7W9_9FIRM Unreviewed; 534 AA. AC W0E7W9; DT 19-MAR-2014, integrated into UniProtKB/TrEMBL. DT 19-MAR-2014, sequence version 1. DT 07-JUN-2017, entry version 20. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=DESME_07650 {ECO:0000313|EMBL:AHF06960.1}; OS Desulfitobacterium metallireducens DSM 15288. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Peptococcaceae; OC Desulfitobacterium. OX NCBI_TaxID=871968 {ECO:0000313|EMBL:AHF06960.1, ECO:0000313|Proteomes:UP000010847}; RN [1] {ECO:0000313|EMBL:AHF06960.1, ECO:0000313|Proteomes:UP000010847} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 15288 {ECO:0000313|Proteomes:UP000010847}; RG DOE Joint Genome Institute; RA Smidt H., Huntemann M., Han J., Chen A., Kyrpides N., Mavromatis K., RA Markowitz V., Palaniappan K., Ivanova N., Schaumberg A., Pati A., RA Liolios K., Nordberg H.P., Cantor M.N., Hua S.X., Woyke T.; RL Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP007032; AHF06960.1; -; Genomic_DNA. DR RefSeq; WP_006715354.1; NZ_CP007032.1. DR EnsemblBacteria; AHF06960; AHF06960; DESME_07650. DR KEGG; dmt:DESME_07650; -. DR KO; K03665; -. DR Proteomes; UP000010847; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000010847}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000010847}. FT DOMAIN 363 534 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 534 AA; 59611 MW; 958D8C1773904415 CRC64; MDIFGDLSGI RLTQLEELKT LSSLRTERPE LIHVDLLDGL SILTDKWNKE IALYINRTGR VNGIAVGHHA SVKLPSVRVR EATHTRCIHT HPGGNFQLSS VDLSALESLS LESMTSIGIL NGKITGAELA CLTEDGTILT SNFSPQELER LDYDEFLSEN RTRQTPITRA LPEEERAYLV SVENEELAQE ILTELAELAR TAGVKVVGQL LQPKRYGSSV SYLGKGKLET LNQQLQNTHA NVLICDDELT PAQLRNLEEY TGIKVLDRTG LILDIFAQRA KSREGKLQVE LAQLQYLLPR LTGQGRSLSR LGGGIGTRGP GESKLEMDKR RVRQRIYILE QDLKEIRKHR LTQRQQRIRS GLQLVALVGY TNAGKTTFLQ KAMEQTRAKG ESLSGENKLF ATLDPTVRSL QIGTYRQILM SDTVGFIQKL PPKLLNAFLA TLEEVQNADL LVHVLDASHA RALEQADTVH EILKELDCAD KPTITVLNKT DQVEQISDLN RLAQQLPHPV SLSLKQGDSL VPVWKMIEEL LPEN // ID W0EVK2_9BACT Unreviewed; 413 AA. AC W0EVK2; DT 19-MAR-2014, integrated into UniProtKB/TrEMBL. DT 19-MAR-2014, sequence version 1. DT 30-AUG-2017, entry version 24. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=BARVI_11155 {ECO:0000313|EMBL:AHF13209.1}; OS Barnesiella viscericola DSM 18177. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Barnesiellaceae; OC Barnesiella. OX NCBI_TaxID=880074 {ECO:0000313|EMBL:AHF13209.1, ECO:0000313|Proteomes:UP000018901}; RN [1] {ECO:0000313|EMBL:AHF13209.1, ECO:0000313|Proteomes:UP000018901} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 18177 {ECO:0000313|Proteomes:UP000018901}; RG DOE Joint Genome Institute; RA Eisen J., Huntemann M., Han J., Chen A., Kyrpides N., Mavromatis K., RA Markowitz V., Palaniappan K., Ivanova N., Schaumberg A., Pati A., RA Liolios K., Nordberg H.P., Cantor M.N., Hua S.X., Woyke T.; RL Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP007034; AHF13209.1; -; Genomic_DNA. DR RefSeq; WP_025279268.1; NZ_CP007034.1. DR EnsemblBacteria; AHF13209; AHF13209; BARVI_11155. DR KEGG; bvs:BARVI_11155; -. DR PATRIC; fig|880074.11.peg.2306; -. DR KO; K03665; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000018901; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000018901}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000018901}. FT DOMAIN 202 387 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 413 AA; 47591 MW; 6ECC1021C2171638 CRC64; MKEFILTQEE TERTVLVGLI TNTQNEAKAN EYLDELAFLA ETAGAEPVKK FLQRLDMPNS RTFVGAGKLA EIKNYIDENE IGMVIFDDDL SAKQVQNIEK ELQVKILDRT SLILDIFAKR AQTANAKRQV ELAQYQYLLP RLTRLWTHLE RQRGGIGMRG PGETQIETDR RIILDKISHL KEELKSIDRQ KSIQRKNRGK LVRVALVGYT NVGKSTLMNL LAKSEVFAEN KLFATLDTTV RKVIVDNLPF LLSDTVGFIR KLPTHLVDSF KSTLDEVREA DLLLHVVDIS HPAFEEQIEV VNKTLQEVCD STNKPMILVF NKIDAFSYVE KAADDLTPRT RENISLDELK ETWMAKMHDN CIFISAREKK NIDELKALLY QRVKEIHTTR FPYNDFLFQH YDEIATDEEK EES // ID W0F3N4_9BACT Unreviewed; 395 AA. AC W0F3N4; DT 19-MAR-2014, integrated into UniProtKB/TrEMBL. DT 19-MAR-2014, sequence version 1. DT 07-JUN-2017, entry version 24. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=NIASO_13680 {ECO:0000313|EMBL:AHF15926.1}; OS Niabella soli DSM 19437. OC Bacteria; Bacteroidetes; Chitinophagia; Chitinophagales; OC Chitinophagaceae; Niabella. OX NCBI_TaxID=929713 {ECO:0000313|EMBL:AHF15926.1, ECO:0000313|Proteomes:UP000003586}; RN [1] {ECO:0000313|EMBL:AHF15926.1, ECO:0000313|Proteomes:UP000003586} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 19437 {ECO:0000313|Proteomes:UP000003586}; RG DOE Joint Genome Institute; RA Eisen J., Huntemann M., Han J., Chen A., Kyrpides N., Mavromatis K., RA Markowitz V., Palaniappan K., Ivanova N., Schaumberg A., Pati A., RA Liolios K., Nordberg H.P., Cantor M.N., Hua S.X., Woyke T.; RL Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP007035; AHF15926.1; -; Genomic_DNA. DR RefSeq; WP_025298943.1; NZ_CP007035.1. DR EnsemblBacteria; AHF15926; AHF15926; NIASO_13680. DR KEGG; nso:NIASO_13680; -. DR KO; K03665; -. DR Proteomes; UP000003586; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000003586}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000003586}. FT DOMAIN 202 384 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 395 AA; 45344 MW; 055970BA865D72A7 CRC64; MLDKKNVIQG TETAVIVGVV TKEQTEQQVN EYLDELAFLA ETAGAETKKR FIQKLAHPDT RTFVGKGKLE EINQYIISHG INLVIFDDEL TGAQLNNIEK VINTKTIDRS DLILDIFARR AKTAEAKAQV ELAQYQYILP RLRGMWKHLE RLGGGIGTRG PGETEIETDR RIVREKISLL RNRLKEIDKQ SATQRKNRGE FIRVALVGYT NVGKSTLMNL LSKREVFAEN KLFATLDTTT SKVVFENTPF LLSDTVGFIR KLPHHLIESF KSTLDEVRES DILIHVIDIS HPQYEDQMAV VNKTLQELKA GDKLVITVFN KMDLYEKNTF DEWLGADTKK EILQDLYDRW NNETDGNAVF VSATERRNVE GLRSTILNKV KELYQVRYPY KTLFY // ID W0H3D4_PSECI Unreviewed; 433 AA. AC W0H3D4; DT 19-MAR-2014, integrated into UniProtKB/TrEMBL. DT 19-MAR-2014, sequence version 1. DT 30-AUG-2017, entry version 25. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=PCH70_05610 {ECO:0000313|EMBL:AHF65714.1}; OS Pseudomonas cichorii JBC1. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=1441629 {ECO:0000313|EMBL:AHF65714.1, ECO:0000313|Proteomes:UP000019031}; RN [1] {ECO:0000313|EMBL:AHF65714.1, ECO:0000313|Proteomes:UP000019031} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=JBC1 {ECO:0000313|EMBL:AHF65714.1, RC ECO:0000313|Proteomes:UP000019031}; RA Kim B.-Y., Lee Y.H.; RT "Analysis of whole genome sequence of Pseudomonas cichorii JBC1."; RL Submitted (JAN-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP007039; AHF65714.1; -; Genomic_DNA. DR RefSeq; WP_025258297.1; NZ_CP007039.1. DR EnsemblBacteria; AHF65714; AHF65714; PCH70_05610. DR KEGG; pci:PCH70_05610; -. DR PATRIC; fig|1441629.3.peg.556; -. DR KO; K03665; -. DR Proteomes; UP000019031; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000019031}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000019031}. FT DOMAIN 199 366 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 165 192 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 433 AA; 48886 MW; CF27E034C9FF9E70 CRC64; MFFERHSGGE RAILVHLDGQ DPEAREDPQE FQELAISAGA DTVAFINVPR HRPSAKYLIG TGKVEELRDQ VRSEQADLVI FNHTLSPSQE RNLERAFECR VLDRTGLILD IFAQRARTHE GKLQVELAQL EHMSTRLVRG WTHLERQKGG IGLRGPGETQ LETDRRLLRV RLRQIKARLE KVRSQRDQAR RGRKRADIPS VSLVGYTNAG KSTLFNAVTD SEVFAADQLF ATLDPTLRRL QLDDLGPIVL ADTVGFIRHL PHKLVEAFRA TLEESSNSDL LLHVIDSHEP DRMSQIEQVM AVLGEIGAEG LPILEVYNKL DLLEGVDPQI QRDADGKPQR VWVSAHDGRG LDLLKQAVAE LLGDDLFVGT LRLPQRFARL RAQFFELGAV QSENHDEEGA SLLAVRLPRV EFNRLVSREG LQPLEFIEQH TLQ // ID W0HXD2_9GAMM Unreviewed; 426 AA. AC W0HXD2; DT 19-MAR-2014, integrated into UniProtKB/TrEMBL. DT 19-MAR-2014, sequence version 1. DT 30-AUG-2017, entry version 28. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:AHF78496.1}; GN ORFNames=Sant_3509 {ECO:0000313|EMBL:AHF78496.1}; OS Sodalis praecaptivus. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; OC Pectobacteriaceae; Sodalis. OX NCBI_TaxID=1239307 {ECO:0000313|EMBL:AHF78496.1, ECO:0000313|Proteomes:UP000019028}; RN [1] {ECO:0000313|EMBL:AHF78496.1, ECO:0000313|Proteomes:UP000019028} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=HS1 {ECO:0000313|EMBL:AHF78496.1, RC ECO:0000313|Proteomes:UP000019028}; RX PubMed=24407854; DOI=10.1093/gbe/evt210; RA Oakeson K.F., Gil R., Clayton A.L., Dunn D.M., von Niederhausern A.C., RA Hamil C., Aoyagi A., Duval B., Baca A., Silva F.J., Vallier A., RA Jackson D.G., Latorre A., Weiss R.B., Heddi A., Moya A., Dale C.; RT "Genome degeneration and adaptation in a nascent stage of symbiosis."; RL Genome Biol. Evol. 6:76-93(2014). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP006569; AHF78496.1; -; Genomic_DNA. DR RefSeq; WP_025423618.1; NZ_CP006569.1. DR EnsemblBacteria; AHF78496; AHF78496; Sant_3509. DR KEGG; sod:Sant_3509; -. DR PATRIC; fig|1239307.3.peg.3865; -. DR KO; K03665; -. DR Proteomes; UP000019028; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000019028}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000019028}. FT DOMAIN 198 365 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 426 AA; 47870 MW; 4D3C125766E76CBA CRC64; MFDRYDAGEQ AILVHIFFSQ DKDMEDLQEF ESLVSSAGVA ALHVVTGSRK APHPKYFVGE GKAEEIAEAV KTSSASVVLF DHALSPAQER NLERLCECRV IDRTGLILDI FAQRARTHEG KLQVELAQLR HLATRLVRGW THLERQKGGI GLRGPGETQL ETDRRLLRNR ISQILSRLER VEKQREQGRR ARARADVPTV SLVGYTNAGK STLFNLMTEA GVYAADQLFA TLDPTLRRIN VGDVGDTVLA DTVGFIRHLP HDLVAAFKAT LQETRQATLL LHIVDAADTR INENIDAVDQ VLAEIEANDI PTLLVMNKID LLDDFAPRID RDEENRPVRV WLSAHSGEGV ALLMQALTER LAGEIARHEL RLPPQAGRLR SRFYQLQAIE KEWVEEDGSV GLVVRLPIID WHRLCKQEMA LVDYLV // ID W0IW33_9BACT Unreviewed; 435 AA. AC W0IW33; DT 19-MAR-2014, integrated into UniProtKB/TrEMBL. DT 19-MAR-2014, sequence version 1. DT 07-JUN-2017, entry version 24. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=OPIT5_09395 {ECO:0000313|EMBL:AHF90382.1}; OS Opitutaceae bacterium TAV5. OC Bacteria; Verrucomicrobia; Opitutae; Opitutales; Opitutaceae. OX NCBI_TaxID=794903 {ECO:0000313|EMBL:AHF90382.1, ECO:0000313|Proteomes:UP000003813}; RN [1] {ECO:0000313|EMBL:AHF90382.1, ECO:0000313|Proteomes:UP000003813} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=TAV5 {ECO:0000313|EMBL:AHF90382.1}; RX PubMed=25744998; RA Kotak M., Isanapong J., Goodwin L., Bruce D., Chen A., Han C.S., RA Huntemann M., Ivanova N., Land M.L., Nolan M., Pati A., Woyke T., RA Rodrigues J.L.; RT "Complete Genome Sequence of the Opitutaceae Bacterium Strain TAV5, a RT Potential Facultative Methylotroph of the Wood-Feeding Termite RT Reticulitermes flavipes."; RL Genome Announc. 3:0-0(2015). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP007053; AHF90382.1; -; Genomic_DNA. DR RefSeq; WP_009509877.1; NZ_CP007053.1. DR EnsemblBacteria; AHF90382; AHF90382; OPIT5_09395. DR KEGG; obt:OPIT5_09395; -. DR KO; K03665; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000003813; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000003813}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000003813}. FT DOMAIN 209 374 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 168 195 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 435 AA; 48297 MW; 433786023DDB9518 CRC64; MADFLEETPA SRNQRCERAF LVGVQTPQMQ PGEGDELLNE LHELVENLHI GVVERALVNL RAPNPGTLLG SGKTEELIAR AKELDCDLIV IDDHLSPAQQ RNWEKLSEIA VIDREEVILD IFADRAQTRE AVLQVALARM EYSLPRLTRA WTHLSRQRGK GKMGGEGETQ LEQDRRLVRD RITRLKKELG EVRKQRGVQR HKRQRVPVPT AAIVGYTNAG KSSLINTLTG SSVLAEDKLF ATLDPTTRQL VLRGNQKLLV TDTVGFIRRL PHGLVEAFKA TLEEALVADF LIHVLDVTAP NVAAHHATTL AVLGELGADE KRILTVFNKV DAADEPHLAR ARQLDRDGIF LSARTGDGVP ALVDHCLDLI AGAFGSSKLF IPHSRHDVIS RLHAIGHVQV EEQRDDGVYI EGRFPPAQKG LFAEFEVSGA KRQNR // ID W0JJX9_DESAE Unreviewed; 357 AA. AC W0JJX9; DT 19-MAR-2014, integrated into UniProtKB/TrEMBL. DT 19-MAR-2014, sequence version 1. DT 07-JUN-2017, entry version 23. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=DESACE_09250 {ECO:0000313|EMBL:AHF97581.1}; OS Desulfurella acetivorans A63. OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfurellales; OC Desulfurellaceae; Desulfurella. OX NCBI_TaxID=694431 {ECO:0000313|EMBL:AHF97581.1, ECO:0000313|Proteomes:UP000019023}; RN [1] {ECO:0000313|EMBL:AHF97581.1, ECO:0000313|Proteomes:UP000019023} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=A63 {ECO:0000313|EMBL:AHF97581.1, RC ECO:0000313|Proteomes:UP000019023}; RG DOE Joint Genome Institute; RA Eisen J., Huntemann M., Han J., Chen A., Kyrpides N., Mavromatis K., RA Markowitz V., Palaniappan K., Ivanova N., Schaumberg A., Pati A., RA Liolios K., Nordberg H.P., Cantor M.N., Hua S.X., Woyke T.; RL Submitted (JAN-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP007051; AHF97581.1; -; Genomic_DNA. DR RefSeq; WP_051438171.1; NZ_CP007051.1. DR EnsemblBacteria; AHF97581; AHF97581; DESACE_09250. DR KEGG; dav:DESACE_09250; -. DR PATRIC; fig|694431.3.peg.1807; -. DR KO; K03665; -. DR Proteomes; UP000019023; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000019023}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000019023}. FT DOMAIN 194 354 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 357 AA; 40357 MW; 6F31C01F63B512A3 CRC64; MQDLQEKAIL VSVFLNVKDE KSLQELEELA KTAGAEVVGV LTQKRKNIDK TYYLGKGKIE ELKNLIEQKG ANIVIFNNEL SGSQVKNIED ILNTKVIDRT NLILDIFAKH AKTKEGMLQV KLAQLKYSLT RLRGIGVTLS RLGGGIGTRG PGETQLETDI RHIKRSILHI EKQIEEIKQH RSLYRKRRQK NQIPVVAIIG YTNAGKSTLI NALTNADAYV ENKLFATLDP LARKLRLPNN KIVLLIDTVG FIKNLPHQLI EAFKSTLEEI KFADLILNVV DISQNDYEEK IKVTEKILSD LECFNKPVIT VYNKSDLLEI LPKNTDKEVY ISAKYKTNLH DLVFCIQNAL ESGNKSL // ID W0JPW3_9EURY Unreviewed; 430 AA. AC W0JPW3; DT 19-MAR-2014, integrated into UniProtKB/TrEMBL. DT 19-MAR-2014, sequence version 1. DT 07-JUN-2017, entry version 25. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=HALLA_10930 {ECO:0000313|EMBL:AHF99296.1}; OS Halostagnicola larsenii XH-48. OC Archaea; Euryarchaeota; Halobacteria; Natrialbales; Natrialbaceae; OC Halostagnicola. OX NCBI_TaxID=797299 {ECO:0000313|EMBL:AHF99296.1, ECO:0000313|Proteomes:UP000019024}; RN [1] {ECO:0000313|EMBL:AHF99296.1, ECO:0000313|Proteomes:UP000019024} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=XH-48 {ECO:0000313|EMBL:AHF99296.1, RC ECO:0000313|Proteomes:UP000019024}; RG DOE Joint Genome Institute; RA Anderson I., Huntemann M., Han J., Chen A., Kyrpides N., RA Mavromatis K., Markowitz V., Palaniappan K., Ivanova N., RA Schaumberg A., Pati A., Liolios K., Nordberg H.P., Cantor M.N., RA Hua S.X., Woyke T.; RL Submitted (JAN-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP007055; AHF99296.1; -; Genomic_DNA. DR RefSeq; WP_049952503.1; NZ_CP007055.1. DR EnsemblBacteria; AHF99296; AHF99296; HALLA_10930. DR GeneID; 25144975; -. DR KEGG; hlr:HALLA_10930; -. DR PATRIC; fig|797299.3.peg.1218; -. DR KO; K03665; -. DR OrthoDB; POG093Z07D6; -. DR Proteomes; UP000019024; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000019024}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000019024}. FT DOMAIN 186 369 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 102 129 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 430 AA; 48120 MW; 7B35FCC37F2B58EF CRC64; MKALIAKRID SGTPDTSEIR ELAQAAGYEV VGEITQSRTA DAALQLGEGK ANELAERAGE TETETVIFDN RLGPYQMYNL GQLLPEGVEI IDRFTLILEI FGQRAQTRKA QLQVELAELR YELPRAEAKT SLAKRDEHPG FMGLGEYDES REQDIKAQIS RIRDELEQIE RTEQHRRERR RASGFDLVAL AGYTNAGKST LLRQLADDLD VDENEELHPD LDSTAESQDR LFTTLGTTTR RADIEPRDVL VTDTVGFISD LPHWLVESFK STLDSVYRAD LVLLVVDVSE PIDEIHEKLV TCHDTLYERN EAPIVTVLNK IDAVSEAELE EKAAALSALA PNPVTVSARE GTNVDELLER IDSELPDWER ERLVLPMTDD TMSLVSWIHD NANVEDVTYG DEDVLLSFEA RPMVISQARS RASDLEAASA // ID W0JZ02_9EURY Unreviewed; 435 AA. AC W0JZ02; DT 19-MAR-2014, integrated into UniProtKB/TrEMBL. DT 19-MAR-2014, sequence version 1. DT 07-JUN-2017, entry version 23. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=HALDL1_09820 {ECO:0000313|EMBL:AHG03864.1}; OS Halobacterium sp. DL1. OC Archaea; Euryarchaeota; Halobacteria; Halobacteriales; OC Halobacteriaceae; Halobacterium. OX NCBI_TaxID=751944 {ECO:0000313|EMBL:AHG03864.1, ECO:0000313|Proteomes:UP000004595}; RN [1] {ECO:0000313|EMBL:AHG03864.1, ECO:0000313|Proteomes:UP000004595} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DL1 {ECO:0000313|EMBL:AHG03864.1, RC ECO:0000313|Proteomes:UP000004595}; RG DOE Joint Genome Institute; RA Cavicchioli R., Huntemann M., Han J., Chen A., Kyrpides N., RA Mavromatis K., Markowitz V., Palaniappan K., Ivanova N., RA Schaumberg A., Pati A., Liolios K., Nordberg H.P., Cantor M.N., RA Hua S.X., Woyke T.; RL Submitted (JAN-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP007060; AHG03864.1; -; Genomic_DNA. DR RefSeq; WP_009761371.1; NZ_CP007060.1. DR EnsemblBacteria; AHG03864; AHG03864; HALDL1_09820. DR GeneID; 25141660; -. DR KEGG; hdl:HALDL1_09820; -. DR KO; K03665; -. DR OrthoDB; POG093Z07D6; -. DR Proteomes; UP000004595; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000004595}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000004595}. FT DOMAIN 192 375 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 158 188 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 435 AA; 48853 MW; 172BBAA0C6695DEF CRC64; MTGTDTNVAV VAKRVDDGTP DTAEIRDLVR AAGYDVAAEV TQERKADAAL QFGEGKVEEL AVVVDETDAD RVVFDNRLGP YQTYNLGQRL PEDTEVGDRF RLILDIFGQR AHTRKAQLQV ELAELRYELP RAEAKTSLAK RDERPGFMGL GEYDESREQD IKAQISRIRD ELEKIEKTES QRRDTRRESG FDLVALAGYT NAGKSTLLRQ LADDLDVDEN EDLHPDLDTT AESQDELFTT LGTTTRRLEM DRRNVLLTDT VGFISDLPHW LVESFKSTLE SVYQADLVLL VVDAGESIDE IREKLTTSHD TLYERNEAPI ITVFNKVDTV DEDELAEKME ALSALAPNPV AVSGLEATNL DTLRSRIDAE LPPREREKLV LPMTEDTMSV VSWVHDHAYV REVDYGDEQV VIDFEARPTV VEQSHAKASE LVAEA // ID W0LA90_9GAMM Unreviewed; 426 AA. AC W0LA90; DT 19-MAR-2014, integrated into UniProtKB/TrEMBL. DT 19-MAR-2014, sequence version 1. DT 30-AUG-2017, entry version 31. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=Z042_14930 {ECO:0000313|EMBL:AHG20753.1}; OS Chania multitudinisentens RB-25. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; OC Yersiniaceae; Chania. OX NCBI_TaxID=1441930 {ECO:0000313|EMBL:AHG20753.1, ECO:0000313|Proteomes:UP000019030}; RN [1] {ECO:0000313|EMBL:AHG20753.1, ECO:0000313|Proteomes:UP000019030} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=RB-25 {ECO:0000313|EMBL:AHG20753.1, RC ECO:0000313|Proteomes:UP000019030}; RA Robson E.H.J.; RT "Isolation of Serratia multitudinisentens RB-25 from Ex-Landfill RT site."; RL Submitted (JAN-2014) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:AHG20753.1, ECO:0000313|Proteomes:UP000019030} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=RB-25 {ECO:0000313|EMBL:AHG20753.1, RC ECO:0000313|Proteomes:UP000019030}; RA Chan K.-G.; RL Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP007044; AHG20753.1; -; Genomic_DNA. DR RefSeq; WP_024912406.1; NZ_JAJC01000015.1. DR EnsemblBacteria; AHG20753; AHG20753; Z042_14930. DR GeneID; 32579883; -. DR KEGG; sfo:Z042_14930; -. DR PATRIC; fig|1441930.4.peg.2943; -. DR KO; K03665; -. DR Proteomes; UP000019030; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000019030}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000019030}. FT DOMAIN 198 365 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 426 AA; 48054 MW; 3C039713EB28B2BF CRC64; MFDRYETGEQ AVLVHIYFSQ DKDTEDLSEF ESLVSSAGVE ALQVVTGSRK APHPKFFVGE GKAEEIADAV KASGASVVLF DHSLSPAQER NLERLCECRV IDRTGLILDI FAQRARTHEG KLQVELAQLR HIATRLVRGW THLERQKGGI GLRGPGETQL ETDRRLLRDR ISLILKRLER VEKQREQGRR ARTRADVPTV SLVGYTNAGK STLFNRMTSA EVYAADQLFA TLDPTLRRID VVDVGDTVLA DTVGFIRHLP HDLVAAFKAT LQETRQASLL LHVIDAADTR LNENIEAVNT VLAEIESDEI PTLLVMNKID MLDDFVPRID RNDENLPIRV WLSAASGEGI PLLLQALTER LSGEIAHHEL RLPPQAGRLR SRFYQIQAIE KEWIEEDGSI GVVVRMPIVE WRRLCKQEKE LINFIV // ID W0PAW9_9BURK Unreviewed; 362 AA. AC W0PAW9; DT 19-MAR-2014, integrated into UniProtKB/TrEMBL. DT 19-MAR-2014, sequence version 1. DT 07-JUN-2017, entry version 24. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:AHG63876.1}; GN ORFNames=MIM_c17950 {ECO:0000313|EMBL:AHG63876.1}; OS Advenella mimigardefordensis DPN7. OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Alcaligenaceae. OX NCBI_TaxID=1247726 {ECO:0000313|EMBL:AHG63876.1, ECO:0000313|Proteomes:UP000019095}; RN [1] {ECO:0000313|EMBL:AHG63876.1, ECO:0000313|Proteomes:UP000019095} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DPN7 {ECO:0000313|EMBL:AHG63876.1, RC ECO:0000313|Proteomes:UP000019095}; RX PubMed=24739217; DOI=10.1099/mic.0.078279-0; RA Wubbeler J.H., Hiessl S., Schuldes J., Thurmer A., Daniel R., RA Steinbuchel A.; RT "Unravelling the complete genome sequence of Advenella RT mimigardefordensis strain DPN7T and novel insights in the catabolism RT of the xenobiotic polythioester precursor 3,3'-dithiodipropionate."; RL Microbiology 160:1401-1416(2014). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP003915; AHG63876.1; -; Genomic_DNA. DR RefSeq; WP_025372511.1; NZ_CP003915.1. DR EnsemblBacteria; AHG63876; AHG63876; MIM_c17950. DR KEGG; amim:MIM_c17950; -. DR PATRIC; fig|1247726.3.peg.1977; -. DR KO; K03665; -. DR Proteomes; UP000019095; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000019095}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000019095}. FT DOMAIN 190 356 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 362 AA; 40071 MW; F5ABB7B00926C02E CRC64; MRVLIISVDS GDLDHPAHAE EFQMLAEGAG ADIAGTLTVK RDKPDAAHYI GKGKLEEAVA MADAEDVELI LFDQPLSPAQ QRNLERAFQR RVVDRVALIL DIFALRAKSH EGKLQVELAQ LQHLVTRLTR MWTHLERQRG GIGMRGPGES QLEMDRRMIG AKVKMLRERL ARVERQRKTQ RRSRARGNTL SVSLVGYTNA GKSTLFNALT KADAYAADQL FATLDTTTRK IWIEGAGNVV ISDTVGFIRD LPTTLIAAFK ATLEETVHAD LLLHVVDAAS PQRDEQIAEV DKVLEEIGAN EVPCILIYNK IDQAGYEPQV ERNERGEPAR VFVSALQRTG LDGLRGAIAE FRPSIGNEVA IL // ID W0RNL2_9BACT Unreviewed; 421 AA. AC W0RNL2; DT 19-MAR-2014, integrated into UniProtKB/TrEMBL. DT 19-MAR-2014, sequence version 1. DT 07-JUN-2017, entry version 22. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=J421_3506 {ECO:0000313|EMBL:AHG91043.1}; OS Gemmatirosa kalamazoonesis. OC Bacteria; Gemmatimonadetes; Gemmatimonadales; Gemmatimonadaceae; OC Gemmatirosa. OX NCBI_TaxID=861299 {ECO:0000313|EMBL:AHG91043.1, ECO:0000313|Proteomes:UP000019151}; RN [1] {ECO:0000313|EMBL:AHG91043.1, ECO:0000313|Proteomes:UP000019151} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=KBS708 {ECO:0000313|EMBL:AHG91043.1, RC ECO:0000313|Proteomes:UP000019151}; RX PubMed=24699952; RA Debruyn J.M., Radosevich M., Wommack K.E., Polson S.W., Hauser L.J., RA Fawaz M.N., Korlach J., Tsai Y.C.; RT "Genome Sequence and Methylome of Soil Bacterium Gemmatirosa RT kalamazoonensis KBS708T, a Member of the Rarely Cultivated RT Gemmatimonadetes Phylum."; RL Genome Announc. 2:e00226-14(2014). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP007128; AHG91043.1; -; Genomic_DNA. DR EnsemblBacteria; AHG91043; AHG91043; J421_3506. DR PATRIC; fig|861299.3.peg.3558; -. DR Proteomes; UP000019151; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000019151}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000019151}. FT DOMAIN 193 363 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 421 AA; 47296 MW; 27F8EB52136EC332 CRC64; MERALLVGAP LKRSNDRHQV GEHLEELARL ADTAGAEVVD TLTQQIDRPH PATYLGTGKL DELRQRAGDR GASLVIFDDE LSPAQGRNIE QTVGVRVMDR AELILDIFAT RARTNEAKMQ VELAQLEYML PRLTRMWTHL EKTRGGIGMR GPGETQLETD RRLINHRIKV LKERLQDVLR SREVQRASRR REFRAALVGY TNAGKSSILR ALSGARDVFV ENRLFATLDP LTREARVGEH TSVLVTDTVG FIRKLPHHLV ASFRATLEET READLLLHVI DVSHPAWEEQ RQVVEEVLAD IGVQDTPVLY VFNKIDAVDP AMLDALRERA RNEKLPAVFV SAVTSDGLEP LARALADRAR RERPIVELRI PASDGKMLAT IHRDGEVLEQ RVDGDALVVR ARVTDALARR LTRDSETVPP D // ID W0SCW3_9PROT Unreviewed; 371 AA. AC W0SCW3; DT 19-MAR-2014, integrated into UniProtKB/TrEMBL. DT 19-MAR-2014, sequence version 1. DT 30-AUG-2017, entry version 24. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=SUTH_01065 {ECO:0000313|EMBL:BAO28866.1}; OS Sulfuritalea hydrogenivorans sk43H. OC Bacteria; Proteobacteria; Betaproteobacteria; Nitrosomonadales; OC Sterolibacteriaceae; Sulfuritalea. OX NCBI_TaxID=1223802 {ECO:0000313|EMBL:BAO28866.1, ECO:0000313|Proteomes:UP000031637}; RN [1] {ECO:0000313|EMBL:BAO28866.1, ECO:0000313|Proteomes:UP000031637} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM22779 {ECO:0000313|EMBL:BAO28866.1}; RX PubMed=25017294; DOI=10.1016/j.syapm.2014.05.010; RA Watanabe T., Kojima H., Fukui M.; RT "Complete genomes of freshwater sulfur oxidizers Sulfuricella RT denitrificans skB26 and Sulfuritalea hydrogenivorans sk43H: genetic RT insights into the sulfur oxidation pathway of betaproteobacteria."; RL Syst. Appl. Microbiol. 37:387-395(2014). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AP012547; BAO28866.1; -; Genomic_DNA. DR RefSeq; WP_041097625.1; NZ_AP012547.1. DR EnsemblBacteria; BAO28866; BAO28866; SUTH_01065. DR KEGG; shd:SUTH_01065; -. DR KO; K03665; -. DR Proteomes; UP000031637; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000031637}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000031637}. FT DOMAIN 198 364 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 164 191 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 371 AA; 40093 MW; 5CC9FEE735DDDFCF CRC64; MFERPASGEN AVLVQLDFGE GDFAERLSEF NLLVGSAGAR SLAVISGKRA RPDPALFAGK GKVAEIGDAV GLHQADVVIF NHELSPGQQR NLERTLECRV VDRSSLILDI FALRAKSHEG KLQVELAQLQ HLATRLVRGW THLERQKGGI GLRGPGEKQL ETDRRLLGKR VSLLKDRLKQ LERQREVRRR ARTRGEVLAI SLVGYTNAGK STLFNALTRA GAYAADQLFA TLDTTSRRLF IEGAGPIVLS DTVGFIRDLP HALVAAFQAT LEETAQADLL LHVVDSASAD RDQQMAAVGA VLEEIGALDV PQILVWNKVD LTAASPGIER DDCGNISCVR LSARTGAGVS LLREALAEVA SRHDEIPAAA A // ID W0SFR5_9PROT Unreviewed; 450 AA. AC W0SFR5; DT 19-MAR-2014, integrated into UniProtKB/TrEMBL. DT 19-MAR-2014, sequence version 1. DT 30-AUG-2017, entry version 24. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX2 {ECO:0000313|EMBL:BAO29856.1}; GN Synonyms=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=SUTH_02065 {ECO:0000313|EMBL:BAO29856.1}; OS Sulfuritalea hydrogenivorans sk43H. OC Bacteria; Proteobacteria; Betaproteobacteria; Nitrosomonadales; OC Sterolibacteriaceae; Sulfuritalea. OX NCBI_TaxID=1223802 {ECO:0000313|EMBL:BAO29856.1, ECO:0000313|Proteomes:UP000031637}; RN [1] {ECO:0000313|EMBL:BAO29856.1, ECO:0000313|Proteomes:UP000031637} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM22779 {ECO:0000313|EMBL:BAO29856.1}; RX PubMed=25017294; DOI=10.1016/j.syapm.2014.05.010; RA Watanabe T., Kojima H., Fukui M.; RT "Complete genomes of freshwater sulfur oxidizers Sulfuricella RT denitrificans skB26 and Sulfuritalea hydrogenivorans sk43H: genetic RT insights into the sulfur oxidation pathway of betaproteobacteria."; RL Syst. Appl. Microbiol. 37:387-395(2014). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AP012547; BAO29856.1; -; Genomic_DNA. DR RefSeq; WP_041099033.1; NZ_AP012547.1. DR EnsemblBacteria; BAO29856; BAO29856; SUTH_02065. DR KEGG; shd:SUTH_02065; -. DR KO; K03665; -. DR Proteomes; UP000031637; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000031637}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000031637}. FT DOMAIN 225 395 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 190 217 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 450 AA; 49858 MW; 9C0ADF30149CD0F3 CRC64; MRKEVKEKPK YAIVAAVQLP NVSDIEFEAS LAELRDLAKT LGYQITATFT QKRSSFDATA YLGKGKREEM RAFVDSEPAP GTFEHPLHAA ADPEAGKIEA IFVDHEISPS QARDLEKEVG AEVLDRTMVI LEIFHRHATS RAARAQVEIA RLGYMAPRLR EAAKLAGPQG RQRSGTGGRG AGESHTELDK RKIRDHIAEL QKEIDAMDVE RKTQRSRRQG RQGLATVALV GYTNAGKSTL MRALTGSDVL VENKLFATLD TTVRALHPES RPRVLVSDTV GFIKNLPHGL VASFKSTLEE ALDAALLLHV IDASDPGFER QLAVTDKVLA EIGAQEVPRI RVFNKIDHVG DAAAQAEREA ALRAAWPDCI VMSARRADDV TLLREAIIDF FRQDQVEAEL FLPWSAQQQR SQIFASCEVL DERADEEGAL LRVRGEREAV ERLKEQFGKT // ID W0TN10_9GAMM Unreviewed; 428 AA. AC W0TN10; DT 19-MAR-2014, integrated into UniProtKB/TrEMBL. DT 19-MAR-2014, sequence version 1. DT 07-JUN-2017, entry version 25. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=TBH_C2095 {ECO:0000313|EMBL:BAO45007.1}; OS Thiolapillus brandeum. OC Bacteria; Proteobacteria; Gammaproteobacteria; Thiolapillus. OX NCBI_TaxID=1076588 {ECO:0000313|EMBL:BAO45007.1, ECO:0000313|Proteomes:UP000031631}; RN [1] {ECO:0000313|EMBL:BAO45007.1, ECO:0000313|Proteomes:UP000031631} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Hiromi1 {ECO:0000313|EMBL:BAO45007.1}; RX PubMed=25133584; DOI=10.1371/journal.pone.0104959; RA Nunoura T., Takaki Y., Kazama H., Kakuta J., Shimamura S., Makita H., RA Hirai M., Miyazaki M., Takai K.; RT "Physiological and genomic features of a novel sulfur-oxidizing RT gammaproteobacterium belonging to a previously uncultivated symbiotic RT lineage isolated from a hydrothermal vent."; RL PLoS ONE 9:e104959-e104959(2014). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AP012273; BAO45007.1; -; Genomic_DNA. DR RefSeq; WP_041070981.1; NZ_AP012273.1. DR EnsemblBacteria; BAO45007; BAO45007; TBH_C2095. DR KEGG; tbn:TBH_C2095; -. DR KO; K03665; -. DR Proteomes; UP000031631; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000031631}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000031631}. FT DOMAIN 198 365 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 157 184 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 428 AA; 48192 MW; D832BC3109C04820 CRC64; MFERPRAGET AILVHVSQQG AADPDELQEF RELAESAGAQ VAEMVTGVRR SPDPRYFVGR GKAEEVHSLV ESLEAELVIF DHALSPSQER NLEALFQCRV LDRSGLILDI FAQRARSFEG KLQVELAQLR HLSTRLVRGW THLERQKGGI GLRGPGETQL ETDRRLLNQR IDQIRRRLSK VDSQRDQGRK ARRRAEVPTV SLVGYTNAGK STLFNRLTHA HVYARDQLFA TLDPTLRRLK LPEGENLVLA DTVGFISKLP HELVAAFKST LQETVEASLL LHVIDAASHC RADNMAEVTD VLQQIGAHEV PCIDVYNKID LLDDVQAHVD RDEEGQVIRV WCSAVTGEGM DLLVDALQER FHQAHVRRHV HLEAADGRLR ALLHEKAHVL QHQSLDDGSC EMEIELTVAD FNRLLKKEPG LADRLLKE // ID W0V908_9BURK Unreviewed; 405 AA. AC W0V908; DT 19-MAR-2014, integrated into UniProtKB/TrEMBL. DT 19-MAR-2014, sequence version 1. DT 07-JUN-2017, entry version 25. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:CDG84070.1}; GN ORFNames=GJA_3454 {ECO:0000313|EMBL:CDG84070.1}; OS Janthinobacterium agaricidamnosum NBRC 102515 = DSM 9628. OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Oxalobacteraceae; Janthinobacterium. OX NCBI_TaxID=1349767 {ECO:0000313|EMBL:CDG84070.1, ECO:0000313|Proteomes:UP000027604}; RN [1] {ECO:0000313|EMBL:CDG84070.1, ECO:0000313|Proteomes:UP000027604} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NBRC 102515 / DSM 9628 {ECO:0000313|Proteomes:UP000027604}; RX PubMed=25883287; DOI=10.1128/genomeA.00277-15; RA Graupner K., Lackner G., Hertweck C.; RT "Genome Sequence of Mushroom Soft-Rot Pathogen Janthinobacterium RT agaricidamnosum."; RL Genome Announc. 3:e00277-e00277(2015). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; HG322949; CDG84070.1; -; Genomic_DNA. DR RefSeq; WP_038494026.1; NZ_HG322949.1. DR EnsemblBacteria; CDG84070; CDG84070; GJA_3454. DR GeneID; 29912796; -. DR KEGG; jag:GJA_3454; -. DR PATRIC; fig|1349767.4.peg.55; -. DR KO; K03665; -. DR Proteomes; UP000027604; Chromosome I. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000027604}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000027604}. FT DOMAIN 190 357 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 405 AA; 44434 MW; 71F9E9F1CE2C6218 CRC64; MRAALVGVDF GQGDFAASVE ELTLLSRSAG AEPIMTITAK RSSPDSAYFV GSGKADEIGD AVLNDGLEIV IFNHALSPAQ QRNLEKRLNT RVLDRTSLIL DIFAQRAKSH EGKLQVELAQ LQHLATRLIR GWTHLERQKG GIGLRGPGET QLETDRRLIG DRVKALRARL EKLHKQRETQ RRSRGRSHTF SVSLVGYTNA GKSTLFNAVT KAGVYVADQL FATLDTTSRR VYLGQEVGNV VISDTVGFVR ELPHQLVAAF RATLEETIHA DLLLHVVDAA SPVRMEQIEQ VNLVLKEIGA DHIPQILVWN KIDAADLEPS VERDENDKLH RVFISARTGS GLDLLREAIV EAARDAPAAA HLYHHGDAAM QDDQADDLQD DAGQDQAVEA DQADSIPTHS QVGTR // ID W0Z6I9_9MICO Unreviewed; 505 AA. AC W0Z6I9; DT 19-MAR-2014, integrated into UniProtKB/TrEMBL. DT 19-MAR-2014, sequence version 1. DT 07-JUN-2017, entry version 23. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:CDJ98936.1}; GN ORFNames=MIC448_110012 {ECO:0000313|EMBL:CDJ98936.1}; OS Microbacterium sp. C448. OC Bacteria; Actinobacteria; Micrococcales; Microbacteriaceae; OC Microbacterium. OX NCBI_TaxID=1177594 {ECO:0000313|EMBL:CDJ98936.1, ECO:0000313|Proteomes:UP000028883}; RN [1] {ECO:0000313|EMBL:CDJ98936.1, ECO:0000313|Proteomes:UP000028883} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C448 {ECO:0000313|EMBL:CDJ98936.1, RC ECO:0000313|Proteomes:UP000028883}; RX PubMed=24526651; DOI=10.1128/genomeA.01113-13; RA Martin-Laurent F., Marti R., Waglechner N., Wright G.D., Topp E.; RT "Draft Genome Sequence of the Sulfonamide Antibiotic-Degrading RT Microbacterium sp. Strain C448."; RL Genome Announc. Announc.2:e01113-e01113(2014). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:CDJ98936.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CBVQ010000013; CDJ98936.1; -; Genomic_DNA. DR RefSeq; WP_036294646.1; NZ_HG779591.1. DR EnsemblBacteria; CDJ98936; CDJ98936; MIC448_110012. DR Proteomes; UP000028883; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000028883}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000028883}. FT DOMAIN 287 452 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 505 AA; 54308 MW; 21C66C794243B5E2 CRC64; MTDTIPTSHE NGEADDVVAR VLARAETRSG VRTFGAAQAL QDASTTAGAD SDGDQWDRED RQALRRVPGL STELEDVTEV EYRQLRLENV VLVGVYPQGE QEDAENSLRE LAALAETAGA IVLDAVLQRR PHPDPATYLG SGKAQELRDL VAAVGADTVI ADTELAPSQR RALEDVVKVK VIDRTTVILD IFSQHAKSRE GKAQVELAQL EYLLPRLRGW GDSMSRQAGG QVGAGGAGMG SRGPGETKIE LDRRRIRTKM ALLRRQIRDF APAREAKRAE RTRNTIPSVA IAGYTNAGKS SLLNRLTSAG VLVENALFAT LDATVRRSET VDGRVFTLTD TVGFVRNLPH QLVEAFRSTL EEVAGADVVL HVVDAAHPDP ASQLATVRDV MAEAGARDAH EIVVFNKADL IDADDRMVLR GLVPNAMFVS SRTGEGIDEL RTAVEAALPL PAVEVHALVP YDRGDLVSAA HDSGLIISEG HEEGGTALHA HVSARLAAEL APFLR // ID W1DDF2_KLEPN Unreviewed; 426 AA. AC W1DDF2; DT 19-MAR-2014, integrated into UniProtKB/TrEMBL. DT 19-MAR-2014, sequence version 1. DT 30-AUG-2017, entry version 25. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; OS Klebsiella pneumoniae IS43. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; OC Enterobacteriaceae; Klebsiella. OX NCBI_TaxID=1432552 {ECO:0000313|EMBL:CDL07566.1, ECO:0000313|Proteomes:UP000019183}; RN [1] {ECO:0000313|EMBL:CDL07566.1, ECO:0000313|Proteomes:UP000019183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=IS43 {ECO:0000313|EMBL:CDL07566.1, RC ECO:0000313|Proteomes:UP000019183}; RA Barisic I., Mitteregger D., Hirschl A.M., Noehammer C., RA Wiesinger-Mayr H.; RT "Antibiotic resistance diversity of beta-lactamase producers in the RT General Hospital Vienna."; RL Submitted (OCT-2013) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:CDL07566.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CBWK010000068; CDL07566.1; -; Genomic_DNA. DR EnsemblBacteria; CDL07566; CDL07566; CDL07566. DR Proteomes; UP000019183; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000019183}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000019183}. FT DOMAIN 198 365 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 426 AA; 48088 MW; 4F4E7D38BEE54660 CRC64; MFDRYDAGEQ AVLVHIYFSQ DKDMEDLQEF ETLASSAGVE AMQVITGSRK APHPKYFVGE GKAVEIAEAV KATGASVVLF DHALSPAQER NMERLCECRV IDRTGLILDI FAQRARTHEG KLQVELAQLR HMATRLVRGW THLERQKGGI GLRGPGETQL ETDRRLLRNR IMQILSRLEK VEKQREQGRR SRAKADIPTV SLVGYTNAGK STLFNQITAA EVYAANQLFA TLDPTLRRID VPDVGETVLA DTVGFIRHLP HDLVAAFKAT LQETRQATLL LHVIDAADVR VQENIDAVNT VLAEIEADEI PALLVMNKID MLDDFEPRID RDDENKPIRV WLSAQTGVGV PLLFQALTER LSGEVAQHTL RLPPKEGRLR SRFYQLQAIE KEWMEDDGSV SLQVRMPIVD WRRLCKQEPT LVDYVV // ID W1DYK9_KLEPN Unreviewed; 426 AA. AC W1DYK9; DT 19-MAR-2014, integrated into UniProtKB/TrEMBL. DT 19-MAR-2014, sequence version 1. DT 30-AUG-2017, entry version 24. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; OS Klebsiella pneumoniae IS46. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; OC Enterobacteriaceae; Klebsiella. OX NCBI_TaxID=1432553 {ECO:0000313|EMBL:CDL14529.1, ECO:0000313|Proteomes:UP000019191}; RN [1] {ECO:0000313|EMBL:CDL14529.1, ECO:0000313|Proteomes:UP000019191} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=IS46 {ECO:0000313|EMBL:CDL14529.1, RC ECO:0000313|Proteomes:UP000019191}; RA Barisic I., Mitteregger D., Hirschl A.M., Noehammer C., RA Wiesinger-Mayr H.; RT "Antibiotic resistance diversity of beta-lactamase producers in the RT General Hospital Vienna."; RL Submitted (OCT-2013) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:CDL14529.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CBWL010000265; CDL14529.1; -; Genomic_DNA. DR ProteinModelPortal; W1DYK9; -. DR EnsemblBacteria; CDL14529; CDL14529; CDL14529. DR Proteomes; UP000019191; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000019191}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000019191}. FT DOMAIN 198 365 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 426 AA; 48070 MW; 7E24BDE9CE348D9F CRC64; MFDRYDAGEQ AVLVHIYFSQ DKDMEDLQEF ETLASSAGVE AMQVITGSRK APHPKYFVGE GKAVEIAEAV KATGASVVLF DHALSPAQER NLERLCECRV IDRTGLILDI FAQRARTHEG KLQVELAQLR HMATRLVRGW THLERQKGGI GLRGPGETQL ETDRRLLRNR IMQILSRLEK VEKQREQGRR SRAKADIPTV SLVGYTNAGK STLFNQITAA EVYAANQLFA TLDPTLRRID VPDVGETVLA DTVGFIRHLP HDLVAAFKAT LQETRQATLL LHVIDAADVR VQENIDAVNT VLAEIEADEI PALLVMNKID MLDDFEPRID RDDENKPIRV WLSAQTGVGV PLLFQALTER LSGEVAQHTL RLPPKEGRLR SRFYQLQAIE KEWMEDDGSV SLQVRMPIVD WRRLCKQEPT LVDYVV // ID W1G158_ECOLX Unreviewed; 181 AA. AC W1G158; DT 19-MAR-2014, integrated into UniProtKB/TrEMBL. DT 19-MAR-2014, sequence version 1. DT 02-NOV-2016, entry version 11. DE SubName: Full=GTP-binding protein HflX {ECO:0000313|EMBL:CDL39636.1}; OS Escherichia coli ISC11. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=1432557 {ECO:0000313|EMBL:CDL39636.1, ECO:0000313|Proteomes:UP000019194}; RN [1] {ECO:0000313|EMBL:CDL39636.1, ECO:0000313|Proteomes:UP000019194} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ISC11 {ECO:0000313|EMBL:CDL39636.1, RC ECO:0000313|Proteomes:UP000019194}; RA Barisic I., Mitteregger D., Hirschl A.M., Noehammer C., RA Wiesinger-Mayr H.; RT "Antibiotic resistance diversity of beta-lactamase producers in the RT General Hospital Vienna."; RL Submitted (OCT-2013) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:CDL39636.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CBWP010000061; CDL39636.1; -; Genomic_DNA. DR EnsemblBacteria; CDL39636; CDL39636; CDL39636. DR Proteomes; UP000019194; Unassembled WGS sequence. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000019194}; KW Reference proteome {ECO:0000313|Proteomes:UP000019194}. FT DOMAIN 25 112 GTP-bdg_N. {ECO:0000259|Pfam:PF13167}. FT DOMAIN 114 180 GTP-bdg_M. {ECO:0000259|Pfam:PF16360}. SQ SEQUENCE 181 AA; 20377 MW; F6445C942677681E CRC64; MFDRYDAGEQ AVLVHIYFSQ DKDMEDLQEF ESLVSSAGVE AMQVITGSRK APHPKYFVGE GKAIEIAEAV KATGAAVVIF DHALSPAQER NLEQLCQCLV IDRTGLILDI FAQRARTHEG KLQVELAQLR HMATRLVRGW THLERQKGGI GLRGPGETQL ETDRRLLRNR ILQIQSRLEK S // ID W1H4E5_KLEPN Unreviewed; 426 AA. AC W1H4E5; DT 19-MAR-2014, integrated into UniProtKB/TrEMBL. DT 19-MAR-2014, sequence version 1. DT 30-AUG-2017, entry version 24. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; OS Klebsiella pneumoniae ISC21. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; OC Enterobacteriaceae; Klebsiella. OX NCBI_TaxID=1432558 {ECO:0000313|EMBL:CDL52490.1, ECO:0000313|Proteomes:UP000019189}; RN [1] {ECO:0000313|EMBL:CDL52490.1, ECO:0000313|Proteomes:UP000019189} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ISC21 {ECO:0000313|EMBL:CDL52490.1, RC ECO:0000313|Proteomes:UP000019189}; RA Barisic I., Mitteregger D., Hirschl A.M., Noehammer C., RA Wiesinger-Mayr H.; RT "Antibiotic resistance diversity of beta-lactamase producers in the RT General Hospital Vienna."; RL Submitted (OCT-2013) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:CDL52490.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CBWQ010000748; CDL52490.1; -; Genomic_DNA. DR ProteinModelPortal; W1H4E5; -. DR EnsemblBacteria; CDL52490; CDL52490; CDL52490. DR Proteomes; UP000019189; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000019189}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000019189}. FT DOMAIN 198 365 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 426 AA; 48070 MW; 7E24BDE9CE348D9F CRC64; MFDRYDAGEQ AVLVHIYFSQ DKDMEDLQEF ETLASSAGVE AMQVITGSRK APHPKYFVGE GKAVEIAEAV KATGASVVLF DHALSPAQER NLERLCECRV IDRTGLILDI FAQRARTHEG KLQVELAQLR HMATRLVRGW THLERQKGGI GLRGPGETQL ETDRRLLRNR IMQILSRLEK VEKQREQGRR SRAKADIPTV SLVGYTNAGK STLFNQITAA EVYAANQLFA TLDPTLRRID VPDVGETVLA DTVGFIRHLP HDLVAAFKAT LQETRQATLL LHVIDAADVR VQENIDAVNT VLAEIEADEI PALLVMNKID MLDDFEPRID RDDENKPIRV WLSAQTGVGV PLLFQALTER LSGEVAQHTL RLPPKEGRLR SRFYQLQAIE KEWMEDDGSV SLQVRMPIVD WRRLCKQEPT LVDYVV // ID W1HYP8_KLEPN Unreviewed; 263 AA. AC W1HYP8; DT 19-MAR-2014, integrated into UniProtKB/TrEMBL. DT 19-MAR-2014, sequence version 1. DT 02-NOV-2016, entry version 12. DE SubName: Full=GTP-binding protein HflX {ECO:0000313|EMBL:CDL63474.1}; OS Klebsiella pneumoniae IS39. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; OC Enterobacteriaceae; Klebsiella. OX NCBI_TaxID=1432561 {ECO:0000313|EMBL:CDL63474.1, ECO:0000313|Proteomes:UP000019190}; RN [1] {ECO:0000313|EMBL:CDL63474.1, ECO:0000313|Proteomes:UP000019190} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=IS39 {ECO:0000313|EMBL:CDL63474.1, RC ECO:0000313|Proteomes:UP000019190}; RA Barisic I., Mitteregger D., Hirschl A.M., Noehammer C., RA Wiesinger-Mayr H.; RT "Antibiotic resistance diversity of beta-lactamase producers in the RT General Hospital Vienna."; RL Submitted (OCT-2013) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:CDL63474.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CBWU010000697; CDL63474.1; -; Genomic_DNA. DR EnsemblBacteria; CDL63474; CDL63474; CDL63474. DR Proteomes; UP000019190; Unassembled WGS sequence. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000019190}; KW Reference proteome {ECO:0000313|Proteomes:UP000019190}. FT DOMAIN 25 112 GTP-bdg_N. {ECO:0000259|Pfam:PF13167}. FT DOMAIN 114 192 GTP-bdg_M. {ECO:0000259|Pfam:PF16360}. SQ SEQUENCE 263 AA; 29669 MW; 4E31868942E5F32B CRC64; MFDRYDAGEQ AVLVHIYFSQ DKDMEDLQEF ETLASSAGVE AMQVITGSRK APHPKYFVGE GKAVEIAEAV KATGASVVLF DHALSPAQER NLERLCECRV IDRTGLILDI FAQRARTHEG KLQVELAQLR HMATRLVRGW THLERQKGGI GLRGPGETQL ETDRRLLRNR IMQILSRLEK VEKQREQGRR SRAKADIPTV SLVAIPTPEN QRSLTRSLPP RSMPRTSCSP PWTRRCAALT SLTSAKRCWP IPSALFATCR TIW // ID W1IP78_9GAMM Unreviewed; 426 AA. AC W1IP78; DT 19-MAR-2014, integrated into UniProtKB/TrEMBL. DT 19-MAR-2014, sequence version 1. DT 30-AUG-2017, entry version 27. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:CDL80249.1}; GN ORFNames=XCR1_1430011 {ECO:0000313|EMBL:CDL80249.1}; OS Xenorhabdus cabanillasii JM26. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; OC Morganellaceae; Xenorhabdus. OX NCBI_TaxID=1427517 {ECO:0000313|EMBL:CDL80249.1, ECO:0000313|Proteomes:UP000019197}; RN [1] {ECO:0000313|EMBL:CDL80249.1, ECO:0000313|Proteomes:UP000019197} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=JM26 {ECO:0000313|EMBL:CDL80249.1, RC ECO:0000313|Proteomes:UP000019197}; RA Gualtieri M., Ogier J.C., Pages S., Givaudan A., Gaudriault S.; RT "Draft genome sequence and annotation of the entomopathogenic RT bacterium, Xenorhabdus cabanillasi strain JM26."; RL Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:CDL80249.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CBXE010000050; CDL80249.1; -; Genomic_DNA. DR RefSeq; WP_038261376.1; NZ_CBXE010000050.1. DR EnsemblBacteria; CDL80249; CDL80249; XCR1_1430011. DR Proteomes; UP000019197; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000019197}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000019197}. FT DOMAIN 198 365 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 426 AA; 48217 MW; 6788D442CEA18E1B CRC64; MFDRYEGGEL AVLVHVFFSQ EKDTENLSEF ESLVTSAGVS PVQIVTGSRK APHPKYFVGE GKAEEIAEAV KNSDADVVLF NHALSPAQER NLERLCQCRV VDRTGVILDI FAQRARTHEG KLQVELAQLR HLSTRLVRGW THLERQKGGI GLRGPGETQL ESDRRMLRDK IKQILGRLNK VEKQREQGRQ ARNKADIPTV SLVGYTNAGK SSLFNRITSA EVYAADQLFA TLDPTLRRIN VNDVGPVVLA DTVGFIRHLP HDLVAAFKAT LQETRQARLL LHVVDASDNR LDENILAVDS VLEEIEAHEI PSLLVMNKID MLADFVPRID RDEENRPVRV WLSAQTGEGI PLLLQALTER LSGEIAHYEL HLPPEAGRLR SRFYQLQAIE REWMEEDGQL GLEVRMPMVD WRRLCKQEPN LPDYVV // ID W1J4S7_9GAMM Unreviewed; 429 AA. AC W1J4S7; DT 19-MAR-2014, integrated into UniProtKB/TrEMBL. DT 19-MAR-2014, sequence version 1. DT 30-AUG-2017, entry version 26. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:CDL85739.1}; GN ORFNames=XSR1_90078 {ECO:0000313|EMBL:CDL85739.1}; OS Xenorhabdus szentirmaii DSM 16338. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; OC Morganellaceae; Xenorhabdus. OX NCBI_TaxID=1427518 {ECO:0000313|EMBL:CDL85739.1, ECO:0000313|Proteomes:UP000019202}; RN [1] {ECO:0000313|EMBL:CDL85739.1, ECO:0000313|Proteomes:UP000019202} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 16338 {ECO:0000313|EMBL:CDL85739.1, RC ECO:0000313|Proteomes:UP000019202}; RA Gualtieri M., Ogier J.C., Pages S., Givaudan A., Gaudriault S.; RT "Draft genome sequence and annotation of the entomopathogenic RT bacteria, Xenorhabdus cabanillasi strain JM26 and Xenorhabdus RT szentirmai strain DSM 16338."; RL Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:CDL85739.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CBXF010000154; CDL85739.1; -; Genomic_DNA. DR RefSeq; WP_038242343.1; NZ_CBXF010000154.1. DR EnsemblBacteria; CDL85739; CDL85739; XSR1_90078. DR Proteomes; UP000019202; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000019202}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000019202}. FT DOMAIN 198 365 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 429 AA; 48337 MW; 57706856AD903A32 CRC64; MFDRYEGGEL AVLVHVFFSQ EKDTENLNEF ESLVTSAGVS PVQIVTGSRK APHPKYFVGE GKAEEIAEAV KNSGADVVLF NHALSPAQER NLERLCQCRV VDRTGVILDI FAQRARTHEG KLQVELAQLR HLSTRLVRGW THLERQKGGI GLRGPGETQL ESDRRMLRDK IKQILGRLGK VEKQREQGRQ ARTKADIPTV SLVGYTNAGK SSLFNQITSA EVYAADQLFA TLDPTLRRIE VNDVGAVVLA DTVGFIRHLP HDLVAAFKAT LQETRQAKLL LHVVDAADAR LDENILAVDS VLEEIEAHEI PSMLVMNKID MLEDFVPRID RDEENRPVRV WVSAQTGDGI PLLLQALTER LSGEIAHYEL HLPPEAGRLR SRFYQLQAIE REWMEESGLM GVEIRMPIAD WCRLCKQEPN LPDYIYLTM // ID W1N420_9GAMM Unreviewed; 438 AA. AC W1N420; DT 19-MAR-2014, integrated into UniProtKB/TrEMBL. DT 19-MAR-2014, sequence version 1. DT 30-AUG-2017, entry version 27. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=BJB45_03750 {ECO:0000313|EMBL:ERL50254.1}; OS Halomonas huangheensis. OC Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales; OC Halomonadaceae; Halomonas. OX NCBI_TaxID=1178482 {ECO:0000313|EMBL:ERL50254.1, ECO:0000313|Proteomes:UP000019113}; RN [1] {ECO:0000313|EMBL:ERL50254.1, ECO:0000313|Proteomes:UP000019113} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BJGMM-B45 {ECO:0000313|EMBL:ERL50254.1, RC ECO:0000313|Proteomes:UP000019113}; RA Miao C., Wan Y., Jin W.; RT "draft genome of Halomonas huanghegensis, strain BJGMM-B45T."; RL Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:ERL50254.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AVBC01000039; ERL50254.1; -; Genomic_DNA. DR RefSeq; WP_021820305.1; NZ_CP013106.1. DR EnsemblBacteria; ERL50254; ERL50254; BJB45_03750. DR KEGG; hhu:AR456_05215; -. DR PATRIC; fig|1178482.3.peg.3352; -. DR KO; K03665; -. DR Proteomes; UP000019113; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000019113}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000019113}. SQ SEQUENCE 438 AA; 49499 MW; A0135A9779DEA29F CRC64; MFFERPNAGE TAVLVHIDFQ DEQEREDPGE FLELVRSAGA EPATLITGSR QRPDSRTYVG SGKLEELREA LSVHHAELVI FNHALSPSQE RNVEQSLKCR VLDRTGLILD IFAQRARTHE GKLQVELAQL EYMSTRLVRG WTHLERQKGG IGLRGPGETQ LETDRRLLRA RIKSIHKRLD KVRSQRSQNR RARSRAEIPS VSLVGYTNAG KSTLFNSLTQ AEVYAADQLF ATLDPTLRRL EVADVGPVVM ADTVGFIRHL PHKLVEAFRA TLQEAAEASL LVHVIDAADP DRELNVTQVN NVLEEIGASE VPSLKVMNKI DLFDSSPRIE RDEHGVHQTV WLSAREGRGL DLLAEALAER LAEDILDFPL TLTPEQGRLR AALHESGAVR GEDFDEQGRS RLALRLPRRD FYQLMSRLDE RAEDYLPRSL QQREAWEA // ID W1NFG2_AMBTC Unreviewed; 649 AA. AC W1NFG2; DT 19-MAR-2014, integrated into UniProtKB/TrEMBL. DT 19-MAR-2014, sequence version 1. DT 12-APR-2017, entry version 18. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:ERM93915.1}; GN ORFNames=AMTR_s00137p00063430 {ECO:0000313|EMBL:ERM93915.1}; OS Amborella trichopoda. OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; basal Magnoliophyta; Amborellales; OC Amborellaceae; Amborella. OX NCBI_TaxID=13333 {ECO:0000313|EMBL:ERM93915.1, ECO:0000313|Proteomes:UP000017836}; RN [1] {ECO:0000313|Proteomes:UP000017836} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=24357323; RG Amborella Genome Project; RT "The Amborella genome and the evolution of flowering plants."; RL Science 342:1241089-1241089(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; KI397541; ERM93915.1; -; Genomic_DNA. DR EnsemblPlants; ERM93915; ERM93915; AMTR_s00137p00063430. DR Gramene; ERM93915; ERM93915; AMTR_s00137p00063430. DR OrthoDB; EOG09360975; -. DR Proteomes; UP000017836; Unassembled WGS sequence. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR CDD; cd01878; HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000017836}; KW Reference proteome {ECO:0000313|Proteomes:UP000017836}. FT DOMAIN 372 546 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 649 AA; 71811 MW; E6DEAD96A1B4CDE8 CRC64; MFRCRSALRP TLSSMLHCKI SSSKTLILQN PTSQSINSHF FIKPRTPSFK SSSLPETLVS SPEFPFCKAL ILPNPYLQSR STHFIRSSGI PPFCAFSLSS TLTSHRGSHY GQSSPEIDDD DANERFIIHR DLTKAPRLFV VQPRIRPDSL LQSKLSEALN LANSLEEQRE GVLYNEPSSK EMPPHLVVQN PVARSLKTHA DTYFGAGTVD NIKCHLNALD SKEEVDAIFV NAILSGIQQR NLERDWGKPV LDRVGLIIEI FNAHAQTKEA KLQSELASLM YKKSRLVRVR GSDGRLTFGA SGEAEVVSAR GRGSGGQGFM SGAGETELQL QRRRILERRN RLLSRIEDVR RTRALQRAAR KRRGGLQGQG LPTVAVVGYT NAGKSTLVSA LSNTDLYSDD RLFATVDPRL RSVILPSGKK VLLSDTVGFI SDLPVQLVEA FHATLEEVVE ADLLVHVLDS SAMNLEEQRA AVLQVLQQIG VPEVKLQNMI EVWNKIDLLH EKSGSNDCED QGEDEGDGEV VEEQEEQHDE VSELMDCHYA KLQEDEGEQP DNEASELASH ATTDSDEAKS EEDDKVGSFS EEAQVEPKNI QHIEASAVMG LGLQELLKLI DQKLNMQSST ASSSSCSFTE GCVDRKWRPP FNREVSVGG // ID W1NZV8_AMBTC Unreviewed; 543 AA. AC W1NZV8; DT 19-MAR-2014, integrated into UniProtKB/TrEMBL. DT 19-MAR-2014, sequence version 1. DT 07-JUN-2017, entry version 24. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:ERN01193.1}; GN ORFNames=AMTR_s00002p00233660 {ECO:0000313|EMBL:ERN01193.1}; OS Amborella trichopoda. OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; basal Magnoliophyta; Amborellales; OC Amborellaceae; Amborella. OX NCBI_TaxID=13333 {ECO:0000313|EMBL:ERN01193.1, ECO:0000313|Proteomes:UP000017836}; RN [1] {ECO:0000313|Proteomes:UP000017836} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=24357323; RG Amborella Genome Project; RT "The Amborella genome and the evolution of flowering plants."; RL Science 342:1241089-1241089(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; KI394767; ERN01193.1; -; Genomic_DNA. DR RefSeq; XP_006838624.1; XM_006838561.2. DR RefSeq; XP_011621533.1; XM_011623231.1. DR EnsemblPlants; ERN01193; ERN01193; AMTR_s00002p00233660. DR GeneID; 18429275; -. DR Gramene; ERN01193; ERN01193; AMTR_s00002p00233660. DR KEGG; atr:18429275; -. DR KO; K03665; -. DR OMA; VILEIFH; -. DR OrthoDB; EOG093609UJ; -. DR Proteomes; UP000017836; Unassembled WGS sequence. DR GO; GO:0009507; C:chloroplast; IEA:EnsemblPlants. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000017836}; KW Reference proteome {ECO:0000313|Proteomes:UP000017836}. FT DOMAIN 320 486 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 286 313 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 543 AA; 60577 MW; 8F224D09DB7B81A0 CRC64; MSVAVVPLSC RAPLGARILH TRPWKNYPTC WLPLWTRPLK VSSAIGDLQP TQIIEVDAIA AGEAMVAKSE LEVNGDSPEV VEESIKEDKG NGFPKKSSNK DRKPGDGTFD YERFTLRNGR EVYLEKAYLV GVEHKRGEDD FLGIEESLEE LAQLADTAGL LVVGSTYQKL AHPNSRTYIG SGKVSEIKNA IHALDVETVI FDDELSAGQL RNLEKAFGGD VRVCDRTALI LDIFNQRAAT HEAALQVSLA QMEYQLPRLT KMWSHLERQA GGRVKGMGEK QIEVDKRILR TQITALRKEL ESVREHRRQY RNRRVSVPVP VVSLVGYTNA GKSTILNRLT GADVLAEDRL FATLDPTTRR VQLNNGKEFL LTDTVGFIQK LPTTLVAAFR ATLEEISESS LLVHVVDISH PLAQQQTWAV DKILSELDVA SIPKLVVWNK VDKTMDPTKI KMEALERDHV ICISALSGDG LKELCDAIQG KLKDSMVWIE ALVPYDKGDL LNTIYQIGMV EWTEYKEQGT LIKGHVPLPL ARQLTPMRQL CIS // ID W1Q4I1_ABIDE Unreviewed; 417 AA. AC W1Q4I1; DT 19-MAR-2014, integrated into UniProtKB/TrEMBL. DT 19-MAR-2014, sequence version 1. DT 07-JUN-2017, entry version 25. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=GCWU000182_000498 {ECO:0000313|EMBL:ESK66155.1}; OS Abiotrophia defectiva ATCC 49176. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Aerococcaceae; OC Abiotrophia. OX NCBI_TaxID=592010 {ECO:0000313|EMBL:ESK66155.1, ECO:0000313|Proteomes:UP000019050}; RN [1] {ECO:0000313|EMBL:ESK66155.1, ECO:0000313|Proteomes:UP000019050} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 49176 {ECO:0000313|EMBL:ESK66155.1, RC ECO:0000313|Proteomes:UP000019050}; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Nelson J., Hou S., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Nash W.E., Warren W., Chinwalla A., Mardis E.R., RA Wilson R.K.; RL Submitted (JUN-2013) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:ESK66155.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ACIN03000003; ESK66155.1; -; Genomic_DNA. DR RefSeq; WP_023391149.1; NZ_KI535340.1. DR ProteinModelPortal; W1Q4I1; -. DR EnsemblBacteria; ESK66155; ESK66155; GCWU000182_000498. DR Proteomes; UP000019050; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000019050}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000019050}. FT DOMAIN 201 364 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 417 AA; 46974 MW; 3BF7E1F71E03CE89 CRC64; MIDLQVGPER VLVMAVQTDQ YSPEQFQVIL DEMTSLTETA GGQVIEVVTQ KLPKLDGRTA VGSGKLEEIA ALVEAREIDL VISLNALTPS MNRQLEASLK VQVIDRVQLI LDIFAMRARS REGKLQVALA QYNYLLPRLY GQGKHLSRQG GGIGTRGPGE TKLESDRRHI RSVIHHVKEE LADIAAHRER TRSRRAQGGH WQVGLVGYTN AGKSTLLTQL TQSETYVQDQ LFATLDPLTR RMPLKGEDRF TLTDTVGFIE ELPTELIHAF KSTLEEIGGM DLLLHVVDAS DPAQTLHEQT VLRIIKELGY GHLPVLTVYN KIDCLAPDQS VQATAFPSIA ISAYEPSHID RLKQEIWKLL MADADWVDQR IPAHEAYKVA GMRQELLVTK FDYDENTGDY HLQGYRRRQQ DREEETH // ID W1SB52_9SPHN Unreviewed; 444 AA. AC W1SB52; DT 19-MAR-2014, integrated into UniProtKB/TrEMBL. DT 19-MAR-2014, sequence version 1. DT 07-JUN-2017, entry version 25. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=C100_02960 {ECO:0000313|EMBL:ETI65254.1}; OS Sphingobium sp. C100. OC Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales; OC Sphingomonadaceae; Sphingobium. OX NCBI_TaxID=1207055 {ECO:0000313|EMBL:ETI65254.1, ECO:0000313|Proteomes:UP000018867}; RN [1] {ECO:0000313|EMBL:ETI65254.1, ECO:0000313|Proteomes:UP000018867} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C100 {ECO:0000313|EMBL:ETI65254.1, RC ECO:0000313|Proteomes:UP000018867}; RX PubMed=24482512; RA Dong C., Bai X., Lai Q., Xie Y., Chen X., Shao Z.; RT "Draft Genome Sequence of Sphingobium sp. Strain C100, a Polycyclic RT Aromatic Hydrocarbon-Degrading Bacterium from the Deep-Sea Sediment of RT the Arctic Ocean."; RL Genome Announc. 2:0-0(2014). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:ETI65254.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AYOY01000026; ETI65254.1; -; Genomic_DNA. DR RefSeq; WP_024018391.1; NZ_AYOY01000026.1. DR EnsemblBacteria; ETI65254; ETI65254; C100_02960. DR PATRIC; fig|1207055.3.peg.578; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000018867; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 2. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000018867}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000018867}. FT DOMAIN 209 390 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 444 AA; 49085 MW; A343AF4F65EFBC40 CRC64; MAIFNRDSDD EVARGARAVV VHAETHNADR RDSDARLEEA RGLALAIGID VRAAQAFRVR DRKPATLFGS GQVDQIATLI KQEEAELVIV DNSLSPVQQS NLEKACEAKV IDRTGLILEI FGERAATNEG RLQVELAHLD YQAGRLVRSW THLERQRGGF GFLGGPGETQ IEADRRMIRD RMAKIRRELD QVTRTRGLHR ARRQRAPWPV IALVGYTNAG KSTLFNRMTG ATVMAEDLLF ATLDPTMRQI ALPGLDKAIL SDTVGFVSDL PTQLIAAFRA TLEEVLSADL IVHVRDIAHP DSEAQRDDVL DVLGELGVAG EPALERGEGE PAPPPIIEAW NKLDLLSADD EVLAREQAAR RDDVVILSAL TGEGVDMLQR AISDRMTRGA KVYGLRLPVS DGATLAWLHE HGEVLSTRIE EEETRVDVRL SDAAFARFNK RERE // ID W1SI30_9BACI Unreviewed; 419 AA. AC W1SI30; DT 19-MAR-2014, integrated into UniProtKB/TrEMBL. DT 19-MAR-2014, sequence version 1. DT 07-JUN-2017, entry version 26. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=BAVI_10802 {ECO:0000313|EMBL:ETI68862.1}; OS Bacillus vireti LMG 21834. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus. OX NCBI_TaxID=1131730 {ECO:0000313|EMBL:ETI68862.1, ECO:0000313|Proteomes:UP000018877}; RN [1] {ECO:0000313|EMBL:ETI68862.1, ECO:0000313|Proteomes:UP000018877} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=LMG 21834 {ECO:0000313|EMBL:ETI68862.1, RC ECO:0000313|Proteomes:UP000018877}; RX PubMed=24708037; DOI=10.1111/1462-2920.12478; RA Mania D., Heylen K., van Spanning R.J., Frostegard A.; RT "The nitrate-ammonifying and nosZ-carrying bacterium Bacillus vireti RT is a potent source and sink for nitric and nitrous oxide under high RT nitrate conditions."; RL Environ. Microbiol. 16:3196-3210(2014). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:ETI68862.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ALAN01000060; ETI68862.1; -; Genomic_DNA. DR RefSeq; WP_024028348.1; NZ_ALAN01000060.1. DR EnsemblBacteria; ETI68862; ETI68862; BAVI_10802. DR PATRIC; fig|1131730.3.peg.2248; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000018877; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000018877}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000018877}. FT DOMAIN 200 362 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 419 AA; 47832 MW; A4C257CF57ED800B CRC64; MEQKETKEKA ILVGCQTSGD DDLRFHYSME ELEALTETAQ GEVLVSVVQK RERRHPATYI GKGKVEELNT LVEELEADIV IFNDELSPSQ KRNLASEVNA RIIDRTQLIL DIFAQRARSK EGKLQVELAQ LQYILPRLAG QGVALSRLGA GIGTRGPGET KLESDRRHIR RRIDDIKTQL SVIVQHRDRY RERRKKNKAF QVAIVGYTNA GKSTLFNRLS EADSYEENQL FATLDPMTRK LILPSGFLSL ITDTVGFIQD LPTTLIAAFR STLEEVKEAD LLLHVVDMSN PDYFHHEKTV NKLLEDLDIK EIPQLTVYNK KDIQHPDFVP TAGTPTAFIS AFNQEDRQAL KEKMEKLVME MMDPYDVQVP STEGKLLSQL KNETILRELS FDEEAQVYRC KGYTLQDHQI TGQLLQFKK // ID W1SN78_9BACI Unreviewed; 418 AA. AC W1SN78; DT 19-MAR-2014, integrated into UniProtKB/TrEMBL. DT 19-MAR-2014, sequence version 1. DT 07-JUN-2017, entry version 26. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=BAVI_11619 {ECO:0000313|EMBL:ETI68603.1}; OS Bacillus vireti LMG 21834. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus. OX NCBI_TaxID=1131730 {ECO:0000313|EMBL:ETI68603.1, ECO:0000313|Proteomes:UP000018877}; RN [1] {ECO:0000313|EMBL:ETI68603.1, ECO:0000313|Proteomes:UP000018877} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=LMG 21834 {ECO:0000313|EMBL:ETI68603.1, RC ECO:0000313|Proteomes:UP000018877}; RX PubMed=24708037; DOI=10.1111/1462-2920.12478; RA Mania D., Heylen K., van Spanning R.J., Frostegard A.; RT "The nitrate-ammonifying and nosZ-carrying bacterium Bacillus vireti RT is a potent source and sink for nitric and nitrous oxide under high RT nitrate conditions."; RL Environ. Microbiol. 16:3196-3210(2014). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:ETI68603.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ALAN01000064; ETI68603.1; -; Genomic_DNA. DR RefSeq; WP_024028511.1; NZ_ALAN01000064.1. DR EnsemblBacteria; ETI68603; ETI68603; BAVI_11619. DR PATRIC; fig|1131730.3.peg.2420; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000018877; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000018877}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000018877}. FT DOMAIN 197 365 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 163 190 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 418 AA; 46992 MW; 2D4BAA2EE3712ADE CRC64; MKGNRKALLV GVNIKQQADF SYSMKELANL AAACHIDSVA EVTQNLNRIN KTHYIGTGKI EETLRFLEEL DAELVIFNDE LSATQIRNLE QELGKTVIDR TMLILDIFAS RAKTREAQLQ VEVAHLKYML PRITGQRESL GRQGGGVGLK NRGAGETKLE LDRRKIEAKI VVLNKELEAL VAQRETQRNQ RKKSGVPLVS LVGYTNAGKS TILNALLRRS HQSFNKQVFE KDMLFATLDT SVRKIKLANH QPFLLSDTVG FVDKLPHHLV KAFRSTLEEA ATADLLIVVV DFSSPNYQKL VDVTNKTLKD IGIENVPMIY AYNKADLVDI EIPQLKGESL YLSAKQEVGI EELAELIGER VFKNKIHCDM LIPFDGGRLV SYLNENANVL ATSYDDNGTK LTVECNQNDF EKYQQYVI // ID W1TPN7_9ACTO Unreviewed; 533 AA. AC W1TPN7; DT 19-MAR-2014, integrated into UniProtKB/TrEMBL. DT 19-MAR-2014, sequence version 1. DT 07-JUN-2017, entry version 24. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=Q618_VCMC00001G1062 {ECO:0000313|EMBL:ETI83481.1}; OS Varibaculum cambriense DORA_20. OC Bacteria; Actinobacteria; Actinomycetales; Actinomycetaceae; OC Varibaculum. OX NCBI_TaxID=1403948 {ECO:0000313|EMBL:ETI83481.1, ECO:0000313|Proteomes:UP000018843}; RN [1] {ECO:0000313|EMBL:ETI83481.1, ECO:0000313|Proteomes:UP000018843} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DORA_20 {ECO:0000313|Proteomes:UP000018843}; RA Brown C.T., Sharon I., Thomas B.C., Castelle C.J., Morowitz M.J., RA Banfield J.F.; RT "A Varibaculum cambriense genome reconstructed from a premature infant RT gut community with otherwise low bacterial novelty that shifts toward RT anaerobic metabolism during the third week of life."; RL Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:ETI83481.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AZMI01000001; ETI83481.1; -; Genomic_DNA. DR PATRIC; fig|1403948.3.peg.80; -. DR Proteomes; UP000018843; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000018843}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000018843}. FT DOMAIN 314 480 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 273 307 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 533 AA; 58158 MW; 2CBD630CCA862C11 CRC64; MREAAQIPAE TEVSKQELDR AYDLVRRVRS RSLNRSETDS DLGSALKDSP ENPHYSNYAD ANIPQGGLEL LDWASTALTK QSSHGGDFSR KLREEFQRNQ ASDLDISEVE YRRVQLEKVF LVGIYDSDRR KAQHSLSELA ALAQTAGAEL VGAALQRRSS PDAATFVGRG KAKELAEQVA ALEADTVIVN AQLQPSQRRG LEDQVKVKVI DRTAVILDIF AQHASSREGK AQVELAQLQY LLPRLRGWGQ SMSRQAGGRV SGGAGIGARG PGETKLETDR RRITKRIAKL RREIKQMKKS RDTKREGRLS SSLASVVIVG YTNAGKSSLL NVLVDADVMV QDALFATLDP TVRQAETPDG RAYTLSDTVG FIDELPHELV EAFRSTLEEV EYADLIVHVV DASHHNPVQQ VETVHEVLAD LPQVSQIPEI IVLNKADLVD ALHLRALQSA IGGGIPLSTR TGQGIAQLRE AIANALPSPA KPIDYVIPYD QSALVARLHE EGIVDKVEYL ENGTHVVGRA GPALAQAILE AAN // ID W2BXP0_9FIRM Unreviewed; 425 AA. AC W2BXP0; DT 19-MAR-2014, integrated into UniProtKB/TrEMBL. DT 19-MAR-2014, sequence version 1. DT 07-JUN-2017, entry version 24. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:ETJ98981.1}; GN ORFNames=HMPREF0378_0395 {ECO:0000313|EMBL:ETJ98981.1}; OS Eubacterium nodatum ATCC 33099. OC Bacteria; Firmicutes; Clostridia; Clostridiales; OC Clostridiales Family XIII. Incertae Sedis. OX NCBI_TaxID=1161902 {ECO:0000313|EMBL:ETJ98981.1, ECO:0000313|Proteomes:UP000018868}; RN [1] {ECO:0000313|EMBL:ETJ98981.1, ECO:0000313|Proteomes:UP000018868} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33099 {ECO:0000313|EMBL:ETJ98981.1, RC ECO:0000313|Proteomes:UP000018868}; RA Durkin A.S., Haft D.R., McCorrison J., Torralba M., Gillis M., RA Haft D.H., Methe B., Sutton G., Nelson K.E.; RL Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:ETJ98981.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AZKM01000028; ETJ98981.1; -; Genomic_DNA. DR EnsemblBacteria; ETJ98981; ETJ98981; HMPREF0378_0395. DR PATRIC; fig|1161902.3.peg.1554; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000018868; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000018868}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000018868}. FT DOMAIN 204 372 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 163 190 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 425 AA; 48276 MW; C0F7D322F3307E12 CRC64; MLRFTEDNQV IEEEKHRAIL VGFTRSEDIE YSMAELSGLA EADNIQVIGE MIQILPKPNS ATLIGSGKVL ELAEMVKRME ADMVVFNNEL TGMQLRNLEE TLDVKVIDRT ILILDIFASR ADSAEGKLQV ELAQLRYRMP RLLGFGRSLS RLGAGIGTRG PGEKKLETDR RHIEKRIEDI KADLRKVQST RMIQRAKREK SDIPVVALVG YTNSGKSAIM NNILSLAEKE DKAVREKDML FATLDAQQRN IKLGSNQEFI LVDTVGFISK LPHGLVEAFK ATLEEVKFAD LLLHVVDSSY EDNQFQIDVT NQVLEEIGVA DKNKLLVFNK IDIVREYDSS PSEYKKIFIS AKTGEGVEEL LEEVRRRIFD DTTVKFLIPY DRGDISSYLC EKTNVISMDY KDNGTEIVVE ISRSDYQRLR EFEVI // ID W2CQW2_9BACT Unreviewed; 306 AA. AC W2CQW2; DT 19-MAR-2014, integrated into UniProtKB/TrEMBL. DT 19-MAR-2014, sequence version 1. DT 30-AUG-2017, entry version 15. DE SubName: Full=GTPase HflX {ECO:0000313|EMBL:ETK09433.1}; DE Flags: Fragment; GN ORFNames=T230_04910 {ECO:0000313|EMBL:ETK09433.1}; OS Tannerella sp. oral taxon BU063 isolate Cell 1/3. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Tannerellaceae; OC Tannerella. OX NCBI_TaxID=1411022 {ECO:0000313|EMBL:ETK09433.1, ECO:0000313|Proteomes:UP000034982}; RN [1] {ECO:0000313|EMBL:ETK09433.1, ECO:0000313|Proteomes:UP000034982} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Cell 1/3 {ECO:0000313|EMBL:ETK09433.1}; RA Beall C.J., Campbell A.G., Griffen A.L., Podar M., Leys E.J.; RT "Single cell genomics of uncultured Tannerella BU063 (oral taxon RT 286)."; RL Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:ETK09433.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AYYE01000824; ETK09433.1; -; Genomic_DNA. DR EnsemblBacteria; ETK09433; ETK09433; T230_04910. DR Proteomes; UP000034982; Unassembled WGS sequence. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000034982}; KW Reference proteome {ECO:0000313|Proteomes:UP000034982}. FT DOMAIN 202 306 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 170 197 {ECO:0000256|SAM:Coils}. FT NON_TER 306 306 {ECO:0000313|EMBL:ETK09433.1}. SQ SEQUENCE 306 AA; 34914 MW; AF355D0729685DB3 CRC64; MKEFIITQEQ TERAVLVGLV TPEQSEAQVK EYLDELAFLA ETAGIEPVRR FTQKADKPHA VTFVGSGKLQ QIGEYVAENE IGIVVFDDEL SAKQLRNIEK ELKVRILDRT NLILDIFAKR AQTAHAKTQV ELAQYRYMLP CLTRLWTHLE RQRGGVGMRG PGETQLETDR RIILDRISKL KRELEEIDRQ KATQRRNRGK MVRVALVGYT NVGKSTLMNL LGKSDVFAEN KLFATLDTTV RKVIIDNLPF LLSDTVGFIR KLPTELVESF KSTLDEVREA DLLVHVVDIS HPTFEEQIEV VERTLA // ID W2EY20_9ACTN Unreviewed; 420 AA. AC W2EY20; DT 19-MAR-2014, integrated into UniProtKB/TrEMBL. DT 19-MAR-2014, sequence version 1. DT 07-JUN-2017, entry version 24. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=MPTA5024_11880 {ECO:0000313|EMBL:ETK35876.1}; OS Microbispora sp. ATCC PTA-5024. OC Bacteria; Actinobacteria; Streptosporangiales; Streptosporangiaceae; OC Microbispora. OX NCBI_TaxID=316330 {ECO:0000313|EMBL:ETK35876.1, ECO:0000313|Proteomes:UP000018869}; RN [1] {ECO:0000313|EMBL:ETK35876.1, ECO:0000313|Proteomes:UP000018869} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC PTA-5024 {ECO:0000313|EMBL:ETK35876.1, RC ECO:0000313|Proteomes:UP000018869}; RX PubMed=24459268; RA Sosio M., Gallo G., Pozzi R., Serina S., Monciardini P., Bera A., RA Stegmann E., Weber T.; RT "Draft Genome Sequence of the Microbispora sp. Strain ATCC-PTA-5024, RT Producing the Lantibiotic NAI-107."; RL Genome Announc. 2:e01198-13(2014). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:ETK35876.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AWEV01000089; ETK35876.1; -; Genomic_DNA. DR EnsemblBacteria; ETK35876; ETK35876; MPTA5024_11880. DR PATRIC; fig|316330.3.peg.2308; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000018869; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000313|EMBL:ETK35876.1}; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000018869}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900, KW ECO:0000313|EMBL:ETK35876.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000018869}. FT DOMAIN 196 362 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 155 182 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 420 AA; 45692 MW; F57AE12410078DA1 CRC64; MLVGVWTDGT IVDAENSLQE LKLLAETAGS QVLEGLIQRR DRPDPATYIG SGKAIELRDI VAAGGADTVI CDGELTPGQL RQLEEVVKVK VIDRTALILD IFAQHAKSRE GKAQVELAQL QYLLPRLRGW GGNLSRQVGG RAAGGVGIGG RGPGETKIEL DRRRIRERMA KLRRQIKEMS TARVTKRHRR QSREVPAVAI AGYTNAGKSS LLNRLTGAGV LVEDALFATL DPTVRRARTP EGRVFTLADT VGFVRHLPHQ LVEAFRSTLE EVGDADLILH VVDGSHPDPE SQIAAVREVL AEIEGARHIP EIVVVNKADA ADPVVLSRLT MKERHSVVVS ARTGSGMGEL MAAIERELPR LDHEIRMLVP YDRGDLVARA HSEGEVLSLE HTGDGTILHA RVLSGLFAEL DRVAKPVETV // ID W2ULG5_9FLAO Unreviewed; 406 AA. AC W2ULG5; DT 19-MAR-2014, integrated into UniProtKB/TrEMBL. DT 19-MAR-2014, sequence version 1. DT 07-JUN-2017, entry version 26. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=P278_29760 {ECO:0000313|EMBL:ETN94172.1}; OS Zhouia amylolytica AD3. OC Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales; OC Flavobacteriaceae; Zhouia. OX NCBI_TaxID=1286632 {ECO:0000313|EMBL:ETN94172.1, ECO:0000313|Proteomes:UP000018850}; RN [1] {ECO:0000313|Proteomes:UP000018850} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=AD3 {ECO:0000313|Proteomes:UP000018850}; RA Jin H., Jeon C.O.; RT "Draft genome sequence from a member of Zhouia, isolated tidal flat."; RL Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:ETN94172.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AYXY01000026; ETN94172.1; -; Genomic_DNA. DR RefSeq; WP_038268472.1; NZ_AYXY01000026.1. DR EnsemblBacteria; ETN94172; ETN94172; P278_29760. DR PATRIC; fig|1286632.3.peg.2972; -. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000018850; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000018850}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000018850}. FT DOMAIN 200 385 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 168 195 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 406 AA; 47015 MW; 21F63760D7E5B9FE CRC64; MLEKKTLDYE KVVLIGVVNQ EQDEEKCKEY LDELEFLAYT AGGEVIERFW QKIDTPNPKT FIGTGKMEDV RAFVKTHDIG TVIFDDELSP AQQKNIEKIL RCKILDRTSL ILDIFAQRAQ TSYARTQVEL AQYQYLLPRL AGLWTHLERQ RGGIGMRGPG ETEIETDRRI VRDRIALLKK KLEKIDKQMA TQRGNRGSLV RVALVGYTNV GKSTLMNVLS KSEVFAENKL FATLDTTVRK VVIGNLPFLL SDTVGFIRKL PTQLVESFKS TLDEVREADL LLHVVDISHP NFEEHVASVN KVLDEIESAD KPTIMVFNKI DAYEHESIDE DDLVTEKTAK HFTLKEWKNT WMGKIGDYAL FISALNKENM EEFRKRVYQE VRKIHITRFP YNHFLYPEYD EMEKDL // ID W3AML8_9FIRM Unreviewed; 148 AA. AC W3AML8; DT 19-MAR-2014, integrated into UniProtKB/TrEMBL. DT 19-MAR-2014, sequence version 1. DT 07-SEP-2016, entry version 13. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:ETP72053.1}; DE Flags: Fragment; GN ORFNames=UYO_2020 {ECO:0000313|EMBL:ETP72053.1}; OS Lachnospiraceae bacterium JC7. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Lachnospiraceae. OX NCBI_TaxID=1165092 {ECO:0000313|EMBL:ETP72053.1, ECO:0000313|Proteomes:UP000018967}; RN [1] {ECO:0000313|EMBL:ETP72053.1, ECO:0000313|Proteomes:UP000018967} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=JC7 {ECO:0000313|EMBL:ETP72053.1, RC ECO:0000313|Proteomes:UP000018967}; RA Rosewarne C.P., Cheung J.L., Evans P.N., Tomkins N.W., Denman S.E., RA O Cuiv P., Morrison M.; RT "Isolation and genomic characterisation of Lachnospiraceae sp. JC7, a RT newly identified member of the bovine rumen core microbiota."; RL Submitted (JUL-2012) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:ETP72053.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ALYD01000023; ETP72053.1; -; Genomic_DNA. DR EnsemblBacteria; ETP72053; ETP72053; UYO_2020. DR OrthoDB; POG091H0464; -. DR Proteomes; UP000018967; Unassembled WGS sequence. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000018967}; KW Reference proteome {ECO:0000313|Proteomes:UP000018967}. FT DOMAIN 29 115 GTP-bdg_N. {ECO:0000259|Pfam:PF13167}. FT DOMAIN 117 148 GTP-bdg_M. {ECO:0000259|Pfam:PF16360}. FT NON_TER 148 148 {ECO:0000313|EMBL:ETP72053.1}. SQ SEQUENCE 148 AA; 16710 MW; 7FDAF94E091E9178 CRC64; MFENETNDKR RKAVLVGACL NNDPDFTVSM RELEGLAEAE NLLVVADITQ NLDSQDSAYY IGSGKVQELK AAIWEMDADI VIVNNQLSPS QLANLAHDLE VEVIDRTNLI LNIFADRARS REAKMQVDYA KLQYMLPRLV GLRQNLSR // ID W3REH7_9BRAD Unreviewed; 462 AA. AC W3REH7; DT 19-MAR-2014, integrated into UniProtKB/TrEMBL. DT 19-MAR-2014, sequence version 1. DT 07-JUN-2017, entry version 22. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=X566_20565 {ECO:0000313|EMBL:ETR75132.1}; OS Afipia sp. P52-10. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Bradyrhizobiaceae; Afipia. OX NCBI_TaxID=1429916 {ECO:0000313|EMBL:ETR75132.1, ECO:0000313|Proteomes:UP000018975}; RN [1] {ECO:0000313|Proteomes:UP000018975} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=P52-10 {ECO:0000313|Proteomes:UP000018975}; RX PubMed=25874801; RA Pickering B.S., Tyler S., Smith G., Burton L., Li M., Dallaire A., RA Weingartl H.; RT "Identification of a novel afipia species isolated from an Indian RT flying fox."; RL PLoS ONE 10:E0121274-E0121274(2015). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:ETR75132.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AZSJ01000007; ETR75132.1; -; Genomic_DNA. DR RefSeq; WP_034470838.1; NZ_AZSJ01000007.1. DR EnsemblBacteria; ETR75132; ETR75132; X566_20565. DR PATRIC; fig|1429916.3.peg.4164; -. DR Proteomes; UP000018975; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000018975}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000018975}. FT DOMAIN 227 401 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 462 AA; 50877 MW; 0C072FCF7599869B CRC64; MEPRQRHERE ADRPGSAGGK AAGRVLVIGP YLRQRPGEGG SAGDAVSSRS ASARLDEATG LARAIDLDVC EALIAPISQI RPATYLGKGK VEEIVGLVTT HKADLVVMDC ALSPVQQRNL EKAWNTKVLD RTGLILEIFG RRARTREGTL QVELAHLTYQ RSRLVRSWTH LERQRGGFGF LGGPGETQIE ADRRMIGERI VRIENELKKV QAARRLHRAG RQRVPYRIAA LVGYTNAGKS TLFNRLTRAN VQSADMLFAT LDPTLRALTL PHGGKAMLSD TVGFISDLPT MLVAAFRATL EEVLEADVIV HVRDISQGDS EAQKRDVETV LRQLGIEEDG GGRIIEVWNK IDRLDEAGRE RLANIAARQP TGRACYLVSA ETGEGLDALL AAIEERLAAA KVTLQLDVDA ADGAGMSWLH RHTEVLEKHL DEGRYRVTVR VDGDRSEGVL RKFADDPQSR RH // ID W4E2B9_9BACL Unreviewed; 429 AA. AC W4E2B9; DT 19-MAR-2014, integrated into UniProtKB/TrEMBL. DT 19-MAR-2014, sequence version 1. DT 07-JUN-2017, entry version 24. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=C173_10500 {ECO:0000313|EMBL:ETT74006.1}; OS Paenibacillus sp. FSL R7-277. OC Bacteria; Firmicutes; Bacilli; Bacillales; Paenibacillaceae; OC Paenibacillus. OX NCBI_TaxID=1227352 {ECO:0000313|EMBL:ETT74006.1, ECO:0000313|Proteomes:UP000019051}; RN [1] {ECO:0000313|EMBL:ETT74006.1, ECO:0000313|Proteomes:UP000019051} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=FSL R7-277 {ECO:0000313|EMBL:ETT74006.1, RC ECO:0000313|Proteomes:UP000019051}; RX PubMed=24422886; DOI=10.1186/1471-2164-15-26; RA Moreno Switt A.I., Andrus A.D., Ranieri M.L., Orsi R.H., Ivy R., RA den Bakker H.C., Martin N.H., Wiedmann M., Boor K.J.; RT "Genomic comparison of sporeforming bacilli isolated from milk."; RL BMC Genomics 15:26-26(2014). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:ETT74006.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ASPX01000027; ETT74006.1; -; Genomic_DNA. DR RefSeq; WP_036724631.1; NZ_ASPX01000027.1. DR EnsemblBacteria; ETT74006; ETT74006; C173_10500. DR PATRIC; fig|1227352.4.peg.2102; -. DR Proteomes; UP000019051; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000019051}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}. FT DOMAIN 208 372 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 167 194 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 429 AA; 47925 MW; C54B23F493726EFE CRC64; MATTTHDTET EVQDRAILVS LVTDKIKRTG IDPELSLQEL VQLAETAGVE VLDVLRQNKE TPDSRWFIGK GKVEELRMAA DGLGANTAIF DQELSGAQVR NLEEALDLKI IDRTQLILDI FAGRAKTREG IIQVELAQLS YLLPRLSGQG KNLSRQGGGI GTRGPGESKL ETDRRHIRER ITELKRQLDE VVKTRELHRE HRRKSGAVQV ALVGYTNAGK STLLKQLTDA DVYIENQLFA TLDPTSRVLQ LPGGKEVVLT DTVGFIQNLP HDLVASFRAT LEEVNEANLV LHVVDSSSPM REEQMEVVQT ILQDLGAAGK PQIVLFNKID LCQPEQLEML PTGEGFLKIS AFNEEDLSRI TEIINDQLAG DTLIFRIPGD RGDLSSLLYR VGEVLEQDYD GSDVLYNVRL NKEDYDKWSY KLAEFVEPQ // ID W4E7N9_9BACL Unreviewed; 423 AA. AC W4E7N9; DT 19-MAR-2014, integrated into UniProtKB/TrEMBL. DT 19-MAR-2014, sequence version 1. DT 07-JUN-2017, entry version 24. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=C173_07482 {ECO:0000313|EMBL:ETT75886.1}; OS Paenibacillus sp. FSL R7-277. OC Bacteria; Firmicutes; Bacilli; Bacillales; Paenibacillaceae; OC Paenibacillus. OX NCBI_TaxID=1227352 {ECO:0000313|EMBL:ETT75886.1, ECO:0000313|Proteomes:UP000019051}; RN [1] {ECO:0000313|EMBL:ETT75886.1, ECO:0000313|Proteomes:UP000019051} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=FSL R7-277 {ECO:0000313|EMBL:ETT75886.1, RC ECO:0000313|Proteomes:UP000019051}; RX PubMed=24422886; DOI=10.1186/1471-2164-15-26; RA Moreno Switt A.I., Andrus A.D., Ranieri M.L., Orsi R.H., Ivy R., RA den Bakker H.C., Martin N.H., Wiedmann M., Boor K.J.; RT "Genomic comparison of sporeforming bacilli isolated from milk."; RL BMC Genomics 15:26-26(2014). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:ETT75886.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ASPX01000015; ETT75886.1; -; Genomic_DNA. DR RefSeq; WP_036723729.1; NZ_ASPX01000015.1. DR EnsemblBacteria; ETT75886; ETT75886; C173_07482. DR PATRIC; fig|1227352.4.peg.1499; -. DR Proteomes; UP000019051; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000019051}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}. FT DOMAIN 198 366 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 157 184 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 423 AA; 47593 MW; 28556112868C806D CRC64; MEPILQKAVI VGMQLQNDTN FAYSMEELRN LAAACEIEVV AELSQKSSRV NPSHYIGTGK IQELALLMEQ HEAPIVIFND ELSPSQIRNL ESALDRQVID RTILILNIFA SRAKTKEAQL QVEVAQLQYM LPRLSGLRES LGRQGGGAGL KNRGAGETKL ELDRRRIEER ISALQLELQT QVARRQIQRK QRHKNEVPVV CLVGYTNTGK SSLMNTLVET YHPGSGKGVL AKDMLFATLE TSVRSIVLPD HKTFLLTDTV GFVSQLPHHL VKAFRSTLEE VTEADLLIHV VDIADPQHEQ HMAVTNETLK ALGADGIPTL YAYNKADLRE DPYPEVEENS VTLSAKKNRG IAELVTLIRS RIFTDYVQCE ILVPFDRGSI VSYFNEHADV QSVSYEEQGT RLKLECRAAD YERFRDDFVE LPQ // ID W4ESZ2_9BACL Unreviewed; 422 AA. AC W4ESZ2; DT 19-MAR-2014, integrated into UniProtKB/TrEMBL. DT 19-MAR-2014, sequence version 1. DT 07-JUN-2017, entry version 24. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=C176_13467 {ECO:0000313|EMBL:ETT82921.1}; OS Viridibacillus arenosi FSL R5-213. OC Bacteria; Firmicutes; Bacilli; Bacillales; Planococcaceae; OC Viridibacillus. OX NCBI_TaxID=1227360 {ECO:0000313|EMBL:ETT82921.1, ECO:0000313|Proteomes:UP000019062}; RN [1] {ECO:0000313|EMBL:ETT82921.1, ECO:0000313|Proteomes:UP000019062} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=FSL R5-213 {ECO:0000313|EMBL:ETT82921.1, RC ECO:0000313|Proteomes:UP000019062}; RX PubMed=24422886; DOI=10.1186/1471-2164-15-26; RA Moreno Switt A.I., Andrus A.D., Ranieri M.L., Orsi R.H., Ivy R., RA den Bakker H.C., Martin N.H., Wiedmann M., Boor K.J.; RT "Genomic comparison of sporeforming bacilli isolated from milk."; RL BMC Genomics 15:26-26(2014). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:ETT82921.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ASQA01000033; ETT82921.1; -; Genomic_DNA. DR RefSeq; WP_038186213.1; NZ_ASQA01000033.1. DR EnsemblBacteria; ETT82921; ETT82921; C176_13467. DR PATRIC; fig|1227360.4.peg.2747; -. DR Proteomes; UP000019062; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000019062}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000019062}. FT DOMAIN 200 368 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 159 193 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 422 AA; 48159 MW; 36EAEFED0D038F05 CRC64; MDELIEKAVI VGVNLRGDVH FEYSLEELKN LAEALNVEVV GTVTQNLERV NPSHYVGTGK IEEIKNFYDE SEANLVIFDD ELSPSQIRNL EADLECKVID RTMLILDIFA RRAKSKEAQM QVELAQLQYM LPRLVGLHAS LSRQGGGTGG GFKNRGAGET KLELDRRKIE DQIAKLRRDL EVVKEQRETQ RKQRRKNEIP VVSIVGYTNA GKSTIMNQLL RKTEHDEHKQ VFEKDMLFAT LETSVRQIEL PDHKSFLLTD TVGFVSKLPH HLVKAFRSTL EEARDADLLL HVVDSSNEEY QYMMEVTNDT LHSVGVEDVP TVYVYNKADL ANVEYPRVSG DTVWMAAKDG VGLDELLQVV RRHIFSDYVT CRICIPYDRG DIVSYLNEYS NIQETAYEEE GTVLKVEMKE ADANRFAEFI LK // ID W4HR01_9RHOB Unreviewed; 424 AA. AC W4HR01; DT 19-MAR-2014, integrated into UniProtKB/TrEMBL. DT 19-MAR-2014, sequence version 1. DT 07-JUN-2017, entry version 25. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=ATO8_00810 {ECO:0000313|EMBL:ETW14405.1}; OS Roseivivax atlanticus. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae; Roseivivax. OX NCBI_TaxID=1317118 {ECO:0000313|EMBL:ETW14405.1, ECO:0000313|Proteomes:UP000019063}; RN [1] {ECO:0000313|EMBL:ETW14405.1, ECO:0000313|Proteomes:UP000019063} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=22II-s10s {ECO:0000313|EMBL:ETW14405.1, RC ECO:0000313|Proteomes:UP000019063}; RX PubMed=24567080; DOI=10.1007/s10482-014-0140-5; RA Li G., Lai Q., Liu X., Sun F., Shao Z.; RT "Roseivivax atlanticus sp. nov., isolated from surface seawater of the RT Atlantic Ocean."; RL Antonie Van Leeuwenhoek 105:863-869(2014). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:ETW14405.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AQQW01000001; ETW14405.1; -; Genomic_DNA. DR RefSeq; WP_043841277.1; NZ_AQQW01000001.1. DR EnsemblBacteria; ETW14405; ETW14405; ATO8_00810. DR PATRIC; fig|1317118.6.peg.166; -. DR Proteomes; UP000019063; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000019063}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000019063}. FT DOMAIN 204 373 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 424 AA; 47062 MW; ACD3E0421372206D CRC64; MNETEEVPTR AWVLHPDIKS DRDRRDPAVA LDEAVALAAA LPGIEVVGSE IVPLPQPHPN ALFGSGKIEE LGARLKAEEV ELVLVDGPVT PVQQRNLERD WKVKLLDRTG LILEIFSDRA ATREGVLQVE MAHLSYQRTR LVRAWTHLER QRGGLGFVGG PGETQIEADR RAIDEQLVRL RRQLEKVVKT RALHRKARAK VPYPIVALVG YTNAGKSTLF NRLTGAEVMA KDMLFATLDP TMRGVKLENG PEVILSDTVG FISDLPTELV AAFRATLEEV LEADLIVHVR DISHPNAQEQ ADDVHAILAS LGVAESTPQI EVWNKIDQLP PDAHEAALTR AERVDSIYAL SAWTGEGMEP LLNGIARAIE GEKMHTDLHL GFDEGRKRAW LFERGLIVDE SQTEEGYDLS VRWTAKEAAQ FDKV // ID W4ITW1_PLAFP Unreviewed; 698 AA. AC W4ITW1; DT 19-MAR-2014, integrated into UniProtKB/TrEMBL. DT 19-MAR-2014, sequence version 1. DT 10-MAY-2017, entry version 17. DE SubName: Full=GTP-binding protein HflX {ECO:0000313|EMBL:ETW52761.1}; GN ORFNames=PFUGPA_05068 {ECO:0000313|EMBL:ETW52761.1}; OS Plasmodium falciparum (isolate Palo Alto / Uganda). OC Eukaryota; Alveolata; Apicomplexa; Aconoidasida; Haemosporida; OC Plasmodiidae; Plasmodium; Plasmodium (Laverania). OX NCBI_TaxID=57270 {ECO:0000313|EMBL:ETW52761.1, ECO:0000313|Proteomes:UP000019103}; RN [1] {ECO:0000313|EMBL:ETW52761.1, ECO:0000313|Proteomes:UP000019103} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Palo Alto/Uganda {ECO:0000313|EMBL:ETW52761.1, RC ECO:0000313|Proteomes:UP000019103}; RG The Broad Institute Genome Sequencing Platform; RG The Broad Institute Genome Sequencing Center for Infectious Disease; RA Neafsey D., Hoffman S., Volkman S., Rosenthal P., Walker B., RA Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B., RA Abouelleil A., Allen A.W., Alvarado L., Arachchi H.M., Berlin A.M., RA Chapman S.B., Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., RA Hansen M., Howarth C., Imamovic A., Ireland A., Larimer J., RA McCowan C., Murphy C., Pearson M., Poon T.W., Priest M., Roberts A., RA Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C., RA Birren B.; RT "The Genome Annotation of Plasmodium falciparum Palo Alto/Uganda."; RL Submitted (FEB-2013) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:ETW52761.1, ECO:0000313|Proteomes:UP000019103} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Palo Alto/Uganda {ECO:0000313|EMBL:ETW52761.1, RC ECO:0000313|Proteomes:UP000019103}; RG The Broad Institute Genome Sequencing Platform; RG The Broad Institute Genome Sequencing Center for Infectious Disease; RA Neafsey D., Cheeseman I., Volkman S., Adams J., Walker B., Young S.K., RA Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., RA Alvarado L., Arachchi H.M., Berlin A.M., Chapman S.B., Dewar J., RA Goldberg J., Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., RA Larimer J., McCowan C., Murphy C., Neiman D., Pearson M., Priest M., RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., RA Nusbaum C., Birren B.; RT "The Genome Sequence of Plasmodium falciparum Palo Alto/Uganda."; RL Submitted (FEB-2013) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; KI927387; ETW52761.1; -; Genomic_DNA. DR ProteinModelPortal; W4ITW1; -. DR SMR; W4ITW1; -. DR EnsemblProtists; ETW52761; ETW52761; PFUGPA_05068. DR Proteomes; UP000019103; Unassembled WGS sequence. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000019103}; KW Reference proteome {ECO:0000313|Proteomes:UP000019103}. FT DOMAIN 459 629 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 698 AA; 81678 MW; FD385C7811AB7D0C CRC64; MGRILFLLKN VNKIEKRYFT NKSNIYYHNE SQKKEIIVLH PILKRSKNNS NKLFQEIIYD AQEALGLAKS ANFQIAKGIS MPLGGWYLKN EKQKKKNDPK NDKIDEGQVP NKELSQNNEH HHVFEKSEKE IPNEMSFTTD KSSSKYINYD EIERKVAESI LIKVNHIDNK FYFSKGKLNE LSKYYLKNPT PCIFINTLLS PEQFRNLEFL FNSLLKSYQD ELILNNKRER DNSEMYERVS DVKFDNCDSD DIIIDNSSYC LDAYNNFLDK EDEQCDDVDL EQNMNVLNEH IGDTSCEQAN DIPYEQISDT QECSKNIPMY VELFDRYSMI LYILKSRAKN NLSKLQLELA RANFVLNTYS EDSKSRMKYI KYIENNVLGG SCIDYEEKYT KLNFFTVGKQ NKKSNVNFSG YTSNYIKSNE TYKEYEKRII NNLYSKLKNE LIKCKNNMIL QNNSRKHKAI IAIVGYTNVG KTKLINYLTK SNLKARNLLF QTLDNAYKNL NISTCYSTIF VDSIGFIQNI PYSLYESFKI SLEAIKTADV IIHVIDVSHP YKDKHKKCVL ETLNKIGISD EFIKNNVIEV WNKIDKLTDN ELYTLCKNKP KNALPISAKY GTNCNYLIQI IEHLINQIKD VHILNLQFPT SEAKERINFL MKNYKVVPHS ISYSDDGNTT FIKLVENKSN LKKYYEKFEI KETYKSDN // ID W4LGN8_9BACT Unreviewed; 540 AA. AC W4LGN8; DT 19-MAR-2014, integrated into UniProtKB/TrEMBL. DT 19-MAR-2014, sequence version 1. DT 07-JUN-2017, entry version 25. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=ETSY1_26375 {ECO:0000313|EMBL:ETW96501.1}; OS Candidatus Entotheonella sp. TSY1. OC Bacteria; Nitrospinae/Tectomicrobia group; Candidatus Tectomicrobia; OC Candidatus Entotheonella. OX NCBI_TaxID=1429438 {ECO:0000313|EMBL:ETW96501.1, ECO:0000313|Proteomes:UP000019141}; RN [1] {ECO:0000313|EMBL:ETW96501.1, ECO:0000313|Proteomes:UP000019141} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=TSY1 {ECO:0000313|Proteomes:UP000019141}; RX PubMed=24476823; DOI=10.1038/nature12959; RA Wilson M.C., Mori T., Ruckert C., Uria A.R., Helf M.J., Takada K., RA Gernert C., Steffens U.A., Heycke N., Schmitt S., Rinke C., RA Helfrich E.J., Brachmann A.O., Gurgui C., Wakimoto T., Kracht M., RA Crusemann M., Hentschel U., Abe I., Matsunaga S., Kalinowski J., RA Takeyama H., Piel J.; RT "An environmental bacterial taxon with a large and distinct metabolic RT repertoire."; RL Nature 506:58-62(2014). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:ETW96501.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AZHW01000777; ETW96501.1; -; Genomic_DNA. DR EnsemblBacteria; ETW96501; ETW96501; ETSY1_26375. DR PATRIC; fig|1429438.4.peg.5036; -. DR Proteomes; UP000019141; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000019141}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000019141}. FT DOMAIN 363 527 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 322 349 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 540 AA; 60278 MW; 55E15A62254AC236 CRC64; MRRLQHIYRR KLPAKQIVTQ ELARYLCELS AEIGRQVGVL IDRKGAIAYV IVGDAKGLFL PDLGRFRAAA NRLRGLRYIH THLRGEPLSA DDMADLAHLR FDVMVAIGVG ADGLPDGSHV ASLLPDNPEG LQWDIQENLP IGQLDQDFMR FIQSLEEEFE RTQRAYAVGG NRERAILMSV TSGNKAAAEE SLDELAELAE SGGVVPADRI IQQRHRIDPN YLIGRGKLDE VTVRSLQVGA DLLIFDQSLT PSQSRAIAER TELKVIDRTM LILDIFAQRA LSREGKIQVE LAQLKYLMPY LANKGTALSR LAGGIGGRGP GETKLEIDRR RVQDRINQLE KQLRSVSQGR HLRRQQRQRR QLPVISIVGY TNAGKSTLLN TLTNSQVLAQ DRLFATLDPS SRRLRFPRDI EVLITDTVGF IRDLPPDLLA AFQATLDELH DADLLLHVVD VSSPYLDDHI QAVETILGDL NLDGIPRLMV FNKMDLVSSD TAVNVARMHD GVALSAHDRQ TLQPLIDRLQ DILIDHQLGR VEEVPVMAGQ // ID W4M628_9BACT Unreviewed; 358 AA. AC W4M628; DT 19-MAR-2014, integrated into UniProtKB/TrEMBL. DT 19-MAR-2014, sequence version 1. DT 07-JUN-2017, entry version 14. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:ETX05371.1}; DE Flags: Fragment; GN ORFNames=ETSY2_23345 {ECO:0000313|EMBL:ETX05371.1}; OS Candidatus Entotheonella sp. TSY2. OC Bacteria; Nitrospinae/Tectomicrobia group; Candidatus Tectomicrobia; OC Candidatus Entotheonella. OX NCBI_TaxID=1429439 {ECO:0000313|EMBL:ETX05371.1, ECO:0000313|Proteomes:UP000019140}; RN [1] {ECO:0000313|EMBL:ETX05371.1, ECO:0000313|Proteomes:UP000019140} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=TSY2 {ECO:0000313|Proteomes:UP000019140}; RX PubMed=24476823; DOI=10.1038/nature12959; RA Wilson M.C., Mori T., Ruckert C., Uria A.R., Helf M.J., Takada K., RA Gernert C., Steffens U.A., Heycke N., Schmitt S., Rinke C., RA Helfrich E.J., Brachmann A.O., Gurgui C., Wakimoto T., Kracht M., RA Crusemann M., Hentschel U., Abe I., Matsunaga S., Kalinowski J., RA Takeyama H., Piel J.; RT "An environmental bacterial taxon with a large and distinct metabolic RT repertoire."; RL Nature 506:58-62(2014). CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:ETX05371.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AZHX01000966; ETX05371.1; -; Genomic_DNA. DR EnsemblBacteria; ETX05371; ETX05371; ETSY2_23345. DR Proteomes; UP000019140; Unassembled WGS sequence. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. PE 4: Predicted; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000019140}; KW Reference proteome {ECO:0000313|Proteomes:UP000019140}. FT DOMAIN 194 282 GTP-bdg_N. {ECO:0000259|Pfam:PF13167}. FT DOMAIN 284 357 GTP-bdg_M. {ECO:0000259|Pfam:PF16360}. FT COILED 327 354 {ECO:0000256|SAM:Coils}. FT NON_TER 358 358 {ECO:0000313|EMBL:ETX05371.1}. SQ SEQUENCE 358 AA; 39994 MW; 6793A786CF855FEC CRC64; MKANQIRRLQ HIYRRKVPAK QIVTQELARY LCELSSEIAR QVGVLIDRKG AIAYVIVGDA KGLFLPDLGR FRAAPNRLRG LRYIHTHLRG EPLSADDMAD LAHLRFDVMV AIGVGADGLP DGSHVASLLP DNPEGRQWDI REHLPIGQLD QDFMRFIQSL EEEFERTQRA YAVGGNRERA ILMSVTPGNK AAAEESLDEL AELAESGGVV PAGRMIQQRH RIDPNYLIGR GKLDEVIVRG LQVGADLLIF DQSLTPSQSR AIAERTELKV IDRTMLILDI FAQRALSREG KIQVELAQLK YLMPYLANKG TALSRLAGGI GGRGPGETKL ESDRRRVQDR INQLEKQLRG VSQGRHLR // ID W4P867_9BACE Unreviewed; 384 AA. AC W4P867; DT 19-MAR-2014, integrated into UniProtKB/TrEMBL. DT 19-MAR-2014, sequence version 1. DT 12-APR-2017, entry version 22. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=JCM6292_2336 {ECO:0000313|EMBL:GAE15976.1}; OS Bacteroides pyogenes JCM 6292. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae; OC Bacteroides. OX NCBI_TaxID=1235809 {ECO:0000313|EMBL:GAE15976.1, ECO:0000313|Proteomes:UP000018861}; RN [1] {ECO:0000313|EMBL:GAE15976.1, ECO:0000313|Proteomes:UP000018861} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=JCM 6292 {ECO:0000313|EMBL:GAE15976.1, RC ECO:0000313|Proteomes:UP000018861}; RA Sakamoto M., Oshima K., Suda W., Kitamura K., Iida T., Hattori M., RA Ohkuma M.; RT "Draft Genome Sequences of Three Strains of Bacteroides pyogenes RT Isolated from a Cat and Swine."; RL Genome Announc. 2:e01242-13(2014). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:GAE15976.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BAIQ01000025; GAE15976.1; -; Genomic_DNA. DR EnsemblBacteria; GAE15976; GAE15976; JCM6292_2336. DR Proteomes; UP000018861; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000018861}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000018861}. FT DOMAIN 182 366 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 384 AA; 43745 MW; E34D96D6EA961A2D CRC64; MAFLAETAGA EVVKRFTQRL PTANSVTYVG KGKLDEIKQY ILNEEEEERE VGMVIFDDEL SAKQIRNIEA ELKVKILDRT SLILDIFAMR AQTANAKTQV ELAQYKYMLP RLQRLWTHLE RQSGGSGSGS GKGGSVGLRG PGETQLEMDR RIILNRMSLL KERLVEIDKQ KATQRKNRGR MIRVALVGYT NVGKSTMMNL LSKSEVFAEN KLFATLDTTV RKVIIDNLPF LLSDTVGFIR KLPTDLVDSF KSTLDEVREA DLLVHVVDIS HPGFEEQIEI VNKTLADIGG GGKPMILVFN KIDAYTYIEK APDDLTPPTK ENLTLEDLMK TWMAKMEDSC LFISARDRIH IDELKSVVYK RVKELHVQKY PYNDFLYQIY DEEE // ID W4PS08_9BACE Unreviewed; 419 AA. AC W4PS08; DT 19-MAR-2014, integrated into UniProtKB/TrEMBL. DT 19-MAR-2014, sequence version 1. DT 07-JUN-2017, entry version 24. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=JCM10003_2037 {ECO:0000313|EMBL:GAE22440.1}; OS Bacteroides pyogenes JCM 10003. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae; OC Bacteroides. OX NCBI_TaxID=1235813 {ECO:0000313|EMBL:GAE22440.1, ECO:0000313|Proteomes:UP000018823}; RN [1] {ECO:0000313|EMBL:GAE22440.1, ECO:0000313|Proteomes:UP000018823} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=JCM 10003 {ECO:0000313|EMBL:GAE22440.1, RC ECO:0000313|Proteomes:UP000018823}; RA Sakamoto M., Oshima K., Suda W., Kitamura K., Iida T., Hattori M., RA Ohkuma M.; RT "Draft Genome Sequences of Three Strains of Bacteroides pyogenes RT Isolated from a Cat and Swine."; RL Genome Announc. 2:e01242-13(2014). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:GAE22440.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BAIU01000013; GAE22440.1; -; Genomic_DNA. DR RefSeq; WP_034543194.1; NZ_BAIU01000013.1. DR EnsemblBacteria; GAE22440; GAE22440; JCM10003_2037. DR Proteomes; UP000018823; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000018823}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000018823}. FT DOMAIN 217 401 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 419 AA; 47738 MW; CE7FA3696E2D3689 CRC64; MKEFVISEAK VETAVLVGLI TQTQDERKTN EYLDELAFLA ETAGAEVVKR FTQRLPTANS VTYVGKGKLD EIKQYILNEE EEEREVGMVI FDDELSAKQI RNIEAELKVK ILDRTSLILD IFAMRAQTAN AKTQVELAQY KYMLPRLQRL WTHLERQSGG SGSGSGKGGS VGLRGPGETQ LEMDRRIILN RMSLLKERLV EIDKQKATQR KNRGRMIRVA LVGYTNVGKS TMMNLLSKSE VFAENKLFAT LDTTVRKVII DNLPFLLSDT VGFIRKLPTD LVDSFKSTLD EVREADLLVH VVDISHPGFE EQIEIVNKTL ADIGGGGKPM ILVFNKIDAY TYIEKAPDDL TPPTKENLTL EDLMKTWMAK MEDSCLFISA RDRIHIDELK SVVYKRVKEL HVQKYPYNDF LYQIYDEEE // ID W4PWX3_9BACI Unreviewed; 430 AA. AC W4PWX3; DT 19-MAR-2014, integrated into UniProtKB/TrEMBL. DT 19-MAR-2014, sequence version 1. DT 12-APR-2017, entry version 21. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=JCM9140_267 {ECO:0000313|EMBL:GAE24351.1}; OS Bacillus wakoensis JCM 9140. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus. OX NCBI_TaxID=1236970 {ECO:0000313|EMBL:GAE24351.1, ECO:0000313|Proteomes:UP000018890}; RN [1] {ECO:0000313|EMBL:GAE24351.1, ECO:0000313|Proteomes:UP000018890} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=JCM 9140 {ECO:0000313|EMBL:GAE24351.1, RC ECO:0000313|Proteomes:UP000018890}; RA Yuki M., Oshima K., Suda W., Oshida Y., Kitamura K., Iida T., RA Hattori M., Ohkuma M.; RT "Draft Genome Sequences of Three Alkaliphilic Bacillus Strains, RT Bacillus wakoensis JCM 9140T, Bacillus akibai JCM 9157T, and Bacillus RT hemicellulosilyticus JCM 9152T."; RL Genome Announc. 2:e01258-13(2014). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:GAE24351.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BAUT01000001; GAE24351.1; -; Genomic_DNA. DR EnsemblBacteria; GAE24351; GAE24351; JCM9140_267. DR Proteomes; UP000018890; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000018890}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000018890}. FT DOMAIN 202 364 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 430 AA; 48836 MW; 344415D2685AB469 CRC64; MLLEINHNET ETVVLVGCQF EQDDLAFDHS MEELKSLVET AKGQVVGSIT QKRQKPEPST YIGKGKVDEL QALLDEKDVD TIIFNDELSP SQIRNVHTRT KKTVIDRTQL ILDIFAARAR SREGKLQVEL AQLSYLLPRL AGQGLALSRQ GGGIGSKGPG ETQLESDRRH IRRRMDEIKH QLEAVVSHRQ RYRERRKQND AFQVAIVGYT NAGKSTILNR LAEVETLEEN QLFATLDPTT RQFNLPSGMN ILLSDTVGFI QDLPTTLVAA FRSTLEELQG ANVLLHVVDS SNPDYEQHER TVKELIQELD AENIPRLVVY NKSEIKTEQF IPSHDEDSIE ISAYDEEDLK SLKEAIEDKL MEQMTEYHVL LKAEEGSLLS RCRESTVIKK QEWNEETEHY EILGYVLPDT ALGHELAIRS IIEPKIAVEE // ID W4QFZ0_9BACI Unreviewed; 424 AA. AC W4QFZ0; DT 19-MAR-2014, integrated into UniProtKB/TrEMBL. DT 19-MAR-2014, sequence version 1. DT 07-JUN-2017, entry version 26. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=JCM9152_2269 {ECO:0000313|EMBL:GAE30847.1}; OS Bacillus hemicellulosilyticus JCM 9152. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus. OX NCBI_TaxID=1236971 {ECO:0000313|EMBL:GAE30847.1, ECO:0000313|Proteomes:UP000018895}; RN [1] {ECO:0000313|EMBL:GAE30847.1, ECO:0000313|Proteomes:UP000018895} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=JCM 9152 {ECO:0000313|EMBL:GAE30847.1, RC ECO:0000313|Proteomes:UP000018895}; RA Yuki M., Oshima K., Suda W., Oshida Y., Kitamura K., Iida T., RA Hattori M., Ohkuma M.; RT "Draft Genome Sequences of Three Alkaliphilic Bacillus Strains, RT Bacillus wakoensis JCM 9140T, Bacillus akibai JCM 9157T, and Bacillus RT hemicellulosilyticus JCM 9152T."; RL Genome Announc. 2:e01258-13(2014). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:GAE30847.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BAUU01000014; GAE30847.1; -; Genomic_DNA. DR RefSeq; WP_035343872.1; NZ_BAZO01000014.1. DR EnsemblBacteria; GAE30847; GAE30847; JCM9152_2269. DR Proteomes; UP000018895; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000018895}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000018895}. FT DOMAIN 201 363 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 424 AA; 47997 MW; 31DECDEF05C3E328 CRC64; MEEVIKREQE QVVLIGCQLD SDDERFDYSM GELKSLVETA QGTVVMTIIQ KRQKVEPSTY IGRGKVEELV SFIEDTDVDL IVFNDELTPS QIRNVYTRTK VTVIDRTQLI LDIFAARAKS REGKLQVELA QLSYLLPRLA GQGIALSRQG GGIGAKGPGE TKLESDRRHI RRRMDEIKQQ LETIVGHRKR YRAQRKRNET LQVALVGYTN AGKSTLLNRL ANAETLEENQ LFATLDPTTR KCSLTNGLTI LLSDTVGFIQ DLPTTLVAAF RSTLEELVEA DLLLHVVDCS NADYVQHEET VKQLVAELGA QHVPQLLIYN KSDQKIIPFV PSYHDDSIEI SALEADDIDA LKEAIEEKLL EQMVAYHVQL FATEGKFLAK CKQTTILKQA EWNEEGEYYD VCGFVHQHTT IGQELMKRMK DEEE // ID W4QRG6_BACA3 Unreviewed; 427 AA. AC W4QRG6; DT 19-MAR-2014, integrated into UniProtKB/TrEMBL. DT 19-MAR-2014, sequence version 1. DT 07-JUN-2017, entry version 26. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=JCM9157_1774 {ECO:0000313|EMBL:GAE34700.1}; OS Bacillus akibai (strain ATCC 43226 / DSM 21942 / JCM 9157 / 1139). OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus. OX NCBI_TaxID=1236973 {ECO:0000313|EMBL:GAE34700.1, ECO:0000313|Proteomes:UP000018896}; RN [1] {ECO:0000313|EMBL:GAE34700.1, ECO:0000313|Proteomes:UP000018896} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=JCM 9157 {ECO:0000313|EMBL:GAE34700.1, RC ECO:0000313|Proteomes:UP000018896}; RA Yuki M., Oshima K., Suda W., Oshida Y., Kitamura K., Iida T., RA Hattori M., Ohkuma M.; RT "Draft Genome Sequences of Three Alkaliphilic Bacillus Strains, RT Bacillus wakoensis JCM 9140T, Bacillus akibai JCM 9157T, and Bacillus RT hemicellulosilyticus JCM 9152T."; RL Genome Announc. 2:e01258-13(2014). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:GAE34700.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BAUV01000010; GAE34700.1; -; Genomic_DNA. DR RefSeq; WP_035663723.1; NZ_BAZQ01000010.1. DR EnsemblBacteria; GAE34700; GAE34700; JCM9157_1774. DR Proteomes; UP000018896; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000018896}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000018896}. FT DOMAIN 201 363 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 427 AA; 48721 MW; 10BD7ED1627DD934 CRC64; MQEINHRETE KVVLVGCDFE GDDVAFQHSM DELKSLVETA KGTVVGMLTQ KRQKVEPSTY IGRGKVEELQ ALIDEKGVDT IVFNDELSPS QIRNVHTRTK TTVIDRTQLI LDIFAQRARS REGKLQVELA QLSYLLPRLA GQGLALSRQG GGIGSKGPGE TQLESDRRHI RRRMDEIKHQ LEAVVGHRQR YRERRKQNEV FQVAIVGYTN AGKSTILNRL ADVATLEENQ LFATLDPTTR QFILPSGMKV LLSDTVGFIQ DLPTTLVAAF RSTLEELQEA SMLLHVVDSS NPDYVQHERT VKELITDLEA EKIPQLVVYN KSDQKHSDFF PSHEEDSIEI SAFEQEDLES LKHAIEEKLM EQMTEYHVVL RAEEGNLLSR CRETTLIQKQ EWNEETEHYE LRGFVLPDTA LGHELAIRSI VERKERN // ID W4TEY0_CUTAC Unreviewed; 483 AA. AC W4TEY0; DT 19-MAR-2014, integrated into UniProtKB/TrEMBL. DT 19-MAR-2014, sequence version 1. DT 12-APR-2017, entry version 23. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=JCM18909_117 {ECO:0000313|EMBL:GAE67082.1}; OS Propionibacterium acnes JCM 18909. OC Bacteria; Actinobacteria; Propionibacteriales; Propionibacteriaceae; OC Cutibacterium. OX NCBI_TaxID=1302241 {ECO:0000313|EMBL:GAE67082.1, ECO:0000313|Proteomes:UP000019082}; RN [1] {ECO:0000313|EMBL:GAE67082.1, ECO:0000313|Proteomes:UP000019082} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=JCM 18909 {ECO:0000313|EMBL:GAE67082.1, RC ECO:0000313|Proteomes:UP000019082}; RA Hattori M., Oshima K., Inaba H., Suda W., Sakamoto M., Iino T., RA Kitahara M., Iida T., Kudo T., Itoh T., Ohkuma M.; RT "NBRP : Genome information of microbial organism related human and RT environment."; RL Submitted (JAN-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:GAE67082.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BAVM01000001; GAE67082.1; -; Genomic_DNA. DR EnsemblBacteria; GAE67082; GAE67082; JCM18909_117. DR Proteomes; UP000019082; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000019082}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000019082}. FT DOMAIN 263 428 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 483 AA; 52325 MW; BD8EC1319AB670C5 CRC64; MSEIEQIDNE REDALKSNNG FSEDQSDYDG DQFDLDARLS LTRVPGMSTD LSDISEVEYR QLRLERVVLC SVWTQGTAAD AENAMAELKA LAETAGSQVL EAVMQRRTTP DPATYIGSGK VAELAEVVWA TGADTVICDG ELDAAQLRNL EDRVKVKVVD RTALILDIFA QHARSVEGRT QVELAQLNYL KQRLRGWGGN LSRQTGGRAA GGAGIGGRGP GETRIETDRR RISHRIAVLR RRLTHIESTR ASKRADRIRN KVPSVAIVGY TNAGKSSLLN RLTRAGVLVE NALFATLDPT TRRATTSDGR VYTLTDTVGF VRHLPHDLVE AFASTLEETA MADVLLHVVD ADDPDPLGQV DAVRGVLSGI GASNIPEILV LNKIDRLSDE TILTLRSTFP GAYLVSAHTG EGIDKLVEAI EAGLPIPSQR VDVVIPYARG DLMDKIHHNG TIGFIDHTAD GTHVVAHLHP ALAAEVEEAC DGV // ID W4TR55_CUTAC Unreviewed; 483 AA. AC W4TR55; DT 19-MAR-2014, integrated into UniProtKB/TrEMBL. DT 19-MAR-2014, sequence version 1. DT 12-APR-2017, entry version 23. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=JCM18916_187 {ECO:0000313|EMBL:GAE70898.1}; OS Propionibacterium acnes JCM 18916. OC Bacteria; Actinobacteria; Propionibacteriales; Propionibacteriaceae; OC Cutibacterium. OX NCBI_TaxID=1302242 {ECO:0000313|EMBL:GAE70898.1, ECO:0000313|Proteomes:UP000019080}; RN [1] {ECO:0000313|EMBL:GAE70898.1, ECO:0000313|Proteomes:UP000019080} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=JCM 18916 {ECO:0000313|EMBL:GAE70898.1, RC ECO:0000313|Proteomes:UP000019080}; RA Hattori M., Oshima K., Inaba H., Suda W., Sakamoto M., Iino T., RA Kitahara M., Oshida Y., Iida T., Kudo T., Itoh T., Ohkuma M.; RT "NBRP : Genome information of microbial organism related human and RT environment."; RL Submitted (JAN-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:GAE70898.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BAVN01000001; GAE70898.1; -; Genomic_DNA. DR ProteinModelPortal; W4TR55; -. DR EnsemblBacteria; GAE70898; GAE70898; JCM18916_187. DR Proteomes; UP000019080; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000019080}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000019080}. FT DOMAIN 263 428 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 483 AA; 52345 MW; DF3C7DAF6DE802E4 CRC64; MSEIEQIDNE REDALKNNNG FSEDQSDYDG DQFDLDARLS LTRVPGMSTD LSDISEVEYR QLRLERVVLC SVWTQGTAAD AENTMAELKA LAETAGSQVL EAVMQHRTTP DPATYIGSGK VAELAEVVRA TGADTVICDG ELDAAQLRNL EDRVKVKVVD RTALILDIFA QHARSVEGRT QVELAQLNYL KQRLRGWGGN LSRQTGGRAA GGAGIGGRGP GETRIETDRR RISHRIAVLR RRLTHIESTR ASKRADRIRN KVPSVAIVGY TNAGKSSLLN RLTRAGVLVE NALFATLDPT TRRATTSDGR VYTLTDTVGF VRHLPHDLVE AFASTLEETA MADVLLHVVD ADDPDPLGQV DAVRGVLSGI GASNIPEILV LNKIDRLSDE TILTLRSTFP GAYLVSAHTG EGIDKLVEAI EAGLPIPSQR VDVVIPYARG DLMDKIHHNG TIGFIDHTAD GIHVVAHLHP ALAAEVEEAC DGV // ID W4U5Q5_CUTAC Unreviewed; 392 AA. AC W4U5Q5; DT 19-MAR-2014, integrated into UniProtKB/TrEMBL. DT 19-MAR-2014, sequence version 1. DT 10-MAY-2017, entry version 17. DE SubName: Full=GTP-binding protein HflX {ECO:0000313|EMBL:GAE75908.1}; GN ORFNames=JCM18918_1651 {ECO:0000313|EMBL:GAE75908.1}; OS Propionibacterium acnes JCM 18918. OC Bacteria; Actinobacteria; Propionibacteriales; Propionibacteriaceae; OC Cutibacterium. OX NCBI_TaxID=1302243 {ECO:0000313|EMBL:GAE75908.1, ECO:0000313|Proteomes:UP000019081}; RN [1] {ECO:0000313|EMBL:GAE75908.1, ECO:0000313|Proteomes:UP000019081} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=JCM 18918 {ECO:0000313|EMBL:GAE75908.1, RC ECO:0000313|Proteomes:UP000019081}; RA Hattori M., Oshima K., Inaba H., Suda W., Sakamoto M., Iino T., RA Kitahara M., Oshida Y., Iida T., Kudo T., Itoh T., Ohkuma M.; RT "NBRP : Genome information of microbial organism related human and RT environment."; RL Submitted (JAN-2014) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:GAE75908.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BAVO01000005; GAE75908.1; -; Genomic_DNA. DR EnsemblBacteria; GAE75908; GAE75908; JCM18918_1651. DR Proteomes; UP000019081; Unassembled WGS sequence. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000019081}; KW Reference proteome {ECO:0000313|Proteomes:UP000019081}. FT DOMAIN 263 299 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 392 AA; 43407 MW; 86D8204E4A22E0B4 CRC64; MSEIEQIDNE REDALKNNNG FSEDQSDYDG DQFDLDARLS LTRVPGMSTD LSDISEVEYR QLRLERVVLC SVWTQGTAAD AENAMAELKA LAETAGSQVL EAVMQHRTTP DPATYIGSGK VAELAEVVWA TGADTVICDG ELDAAQLRNL EDRVKVKVVD RTALILDIFA QHARSVEGRT QVELAQLNYL KQRLRGWGGN LSRQTGGRAA GGAGIGGRGP GETRIETDRR RISHRIAVLR RRLTHIESTR ASKRADRIRN KVPSVAIVGY TNAGKSSLLN RLTRAGVLVE NALFATLDPR LDAPPPPTVG STPSLTRWDL FDTCRTTSSR PLHLLWRRRR WPMCSSTLWM QMIQIHSARS TQYAGCCRGL GPVIFLRFSS LTRLIVLAMK PS // ID W4UDB1_CUTAC Unreviewed; 37 AA. AC W4UDB1; DT 19-MAR-2014, integrated into UniProtKB/TrEMBL. DT 19-MAR-2014, sequence version 1. DT 15-FEB-2017, entry version 10. DE SubName: Full=GTP-binding protein HflX {ECO:0000313|EMBL:GAE79135.1}; GN ORFNames=JCM18920_682 {ECO:0000313|EMBL:GAE79135.1}; OS Propionibacterium acnes JCM 18920. OC Bacteria; Actinobacteria; Propionibacteriales; Propionibacteriaceae; OC Cutibacterium. OX NCBI_TaxID=1302244 {ECO:0000313|EMBL:GAE79135.1, ECO:0000313|Proteomes:UP000019083}; RN [1] {ECO:0000313|EMBL:GAE79135.1, ECO:0000313|Proteomes:UP000019083} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=JCM 18920 {ECO:0000313|EMBL:GAE79135.1, RC ECO:0000313|Proteomes:UP000019083}; RA Hattori M., Oshima K., Inaba H., Suda W., Sakamoto M., Iino T., RA Kitahara M., Oshida Y., Iida T., Kudo T., Itoh T., Ohkuma M.; RT "NBRP : Genome information of microbial organism related human and RT environment."; RL Submitted (JAN-2014) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:GAE79135.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BAVP01000002; GAE79135.1; -; Genomic_DNA. DR EnsemblBacteria; GAE79135; GAE79135; JCM18920_682. DR Proteomes; UP000019083; Unassembled WGS sequence. DR InterPro; IPR025121; GTPase_HflX_N. DR Pfam; PF13167; GTP-bdg_N; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000019083}; KW Reference proteome {ECO:0000313|Proteomes:UP000019083}. FT DOMAIN 2 37 GTP-bdg_N. {ECO:0000259|Pfam:PF13167}. SQ SEQUENCE 37 AA; 4030 MW; 3F19E45237B18569 CRC64; MVRATGADTV ICDGELDAAQ LRNLEDRVKV KVVDRTA // ID W4UYF2_9BACE Unreviewed; 416 AA. AC W4UYF2; DT 19-MAR-2014, integrated into UniProtKB/TrEMBL. DT 19-MAR-2014, sequence version 1. DT 07-JUN-2017, entry version 25. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=JCM10512_4333 {ECO:0000313|EMBL:GAE85867.1}; OS Bacteroides reticulotermitis JCM 10512. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae; OC Bacteroides. OX NCBI_TaxID=1445607 {ECO:0000313|EMBL:GAE85867.1, ECO:0000313|Proteomes:UP000019131}; RN [1] {ECO:0000313|EMBL:GAE85867.1, ECO:0000313|Proteomes:UP000019131} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=JCM 10512 {ECO:0000313|EMBL:GAE85867.1, RC ECO:0000313|Proteomes:UP000019131}; RA Yuki M., Oshima K., Suda W., Sakamoto M., Iida T., Hattori M., RA Ohkuma M.; RT "Draft Genome Sequence of Bacteroides reticulotermitis Strain JCM RT 10512T, Isolated from the Gut of a Termite."; RL Genome Announc. 2:e00072-14(2014). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:GAE85867.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BAIV01000032; GAE85867.1; -; Genomic_DNA. DR RefSeq; WP_044164909.1; NZ_BAIV01000032.1. DR EnsemblBacteria; GAE85867; GAE85867; JCM10512_4333. DR Proteomes; UP000019131; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000019131}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000019131}. FT DOMAIN 215 399 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 416 AA; 47530 MW; B4E04FABB3BAFB6D CRC64; MKEFVISEAK AETAVLVGLI TQTQDERKTK EYLDELAFLA ETAGAEVVKE FTQKLPIANS VTYVGKGKLE EIKTYIATEA EEEREVGMVI FDDELSPKQL RNIEAELNVK ILDRTSLILD IFAMRAQTAN AKTQVELAQY KYMLPRLQRL WTHLERQGGG SGSGKGGSVG LRGPGETQLE MDRRIILNRM SLLKERLREI DKQKATQRKN RGRMIRVALV GYTNVGKSTI MNLLAKSEVF AENKLFATLD TTVRKVIIEN LPFLLSDTVG FIRKLPTDLV ESFKSTLDEV READLLIHVV DISHVGFEEQ IDVVNKTLAE IEGSGKPMIL IFNKIDAYTY IEKASDDLTP RTKENLTLEE LMKTWMAKME DNCLFISARE RINIDELKDV VYQRVKELHV QKYPYNDFLY QTYDEE // ID W4VCL7_9FIRM Unreviewed; 292 AA. AC W4VCL7; DT 19-MAR-2014, integrated into UniProtKB/TrEMBL. DT 19-MAR-2014, sequence version 1. DT 12-APR-2017, entry version 20. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=JCM21531_4605 {ECO:0000313|EMBL:GAE90942.1}; OS [Clostridium] straminisolvens JCM 21531. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Ruminococcaceae; OC Ruminiclostridium. OX NCBI_TaxID=1294263 {ECO:0000313|EMBL:GAE90942.1, ECO:0000313|Proteomes:UP000019109}; RN [1] {ECO:0000313|EMBL:GAE90942.1, ECO:0000313|Proteomes:UP000019109} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=JCM 21531 {ECO:0000313|EMBL:GAE90942.1, RC ECO:0000313|Proteomes:UP000019109}; RA Yuki M., Oshima K., Suda W., Sakamoto M., Kitamura K., Iida T., RA Hattori M., Ohkuma M.; RT "Draft Genome Sequence of Clostridium straminisolvens Strain JCM RT 21531T, Isolated from a Cellulose-Degrading Bacterial Community."; RL Genome Announc. 2:e00110-14(2014). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:GAE90942.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BAVR01000113; GAE90942.1; -; Genomic_DNA. DR EnsemblBacteria; GAE90942; GAE90942; JCM21531_4605. DR Proteomes; UP000019109; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000019109}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000019109}. FT DOMAIN 220 292 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 186 213 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 292 AA; 32540 MW; F9D277EC23800F7F CRC64; MWNIILETDK LKSSAVYLNE SDDERAILVG LETSSKVLVG GKSEGERSLD ELEELAHTAG AVVLEKIIQR RPVKDPAFFI GRGKVEELSL MCQALDADLI IFDDELSGAQ VRNIEEVTGV KVIDRTTLIL DIFAKRARSR EGKLQVELAQ LKYRVSRLVG LGTQLSRLGG GIGTRGPGEK KLEVDRRHIK KRISFLESQL KDVEKRRNSL RESRTRNAIP TIALVGYTNA GKSTLMNRLC ESDVLAENKL FATLDPTTRS FSLPDGREVL LIDTVGFIRK LPHELVEAFK ST // ID W4VFD7_9BACI Unreviewed; 443 AA. AC W4VFD7; DT 19-MAR-2014, integrated into UniProtKB/TrEMBL. DT 19-MAR-2014, sequence version 1. DT 12-APR-2017, entry version 22. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=JCM21714_479 {ECO:0000313|EMBL:GAE91528.1}; OS Gracilibacillus boraciitolerans JCM 21714. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; OC Gracilibacillus. OX NCBI_TaxID=1298598 {ECO:0000313|EMBL:GAE91528.1, ECO:0000313|Proteomes:UP000019102}; RN [1] {ECO:0000313|EMBL:GAE91528.1, ECO:0000313|Proteomes:UP000019102} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=JCM 21714 {ECO:0000313|EMBL:GAE91528.1, RC ECO:0000313|Proteomes:UP000019102}; RA Ahmed I., Oshima K., Suda W., Kitamura K., Iida T., Ohmori Y., RA Fujiwara T., Hattori M., Ohkuma M.; RT "Draft Genome Sequence of the Boron-Tolerant and Moderately RT Halotolerant Bacterium Gracilibacillus boraciitolerans JCM 21714T."; RL Genome Announc. 2:e00097-14(2014). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:GAE91528.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BAVS01000001; GAE91528.1; -; Genomic_DNA. DR EnsemblBacteria; GAE91528; GAE91528; JCM21714_479. DR Proteomes; UP000019102; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000019102}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000019102}. FT DOMAIN 223 385 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 189 216 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 443 AA; 51539 MW; 297D89081FF25494 CRC64; MIVRRRYNKV ASFLCIKIKI IRKGKKVIII EKVLLAAVMH ERTNEQQFYY SLNELEALVK TAEGEVIKTI IQKRPRPHRA YYVGEGKLKE IKELINEFEI EIVITNEELS GGQIRNLQEQ LEVRVIDRSQ LILDIFAARA RTKEGKLQVE LAQYTYMLPR LHGQGADLSR LGAGIGTRGP GETKLETDRR HIRRRMDDIK KRLEQVVNQR EQYRGNRKRH QLFQVAVVGY TNAGKSTLFN SLTKSDTLYE DKLFATLDPL TRRMKLPSNL EVLLTDTVGF IQDLPTALVA AFRSTLEEVK EADLIIHVID AAAPNRDNHE QTVYQLLSEL EADKIPILTI YNKEDLIDKT DFVPTTHPYL LISALDDNHI KHVKNKTERL IKEQWSHFAL HVPESESTKL SKIRQYTILE KEEYQEKHFS YYLEGYVDPN HAIMREIKEF NHE // ID W4XPQ7_STRPU Unreviewed; 591 AA. AC W4XPQ7; DT 19-MAR-2014, integrated into UniProtKB/TrEMBL. DT 19-MAR-2014, sequence version 1. DT 07-JUN-2017, entry version 21. DE SubName: Full=Uncharacterized protein {ECO:0000313|EnsemblMetazoa:SPU_005393-tr}; OS Strongylocentrotus purpuratus (Purple sea urchin). OC Eukaryota; Metazoa; Echinodermata; Eleutherozoa; Echinozoa; OC Echinoidea; Euechinoidea; Echinacea; Echinoida; Strongylocentrotidae; OC Strongylocentrotus. OX NCBI_TaxID=7668 {ECO:0000313|EnsemblMetazoa:SPU_005393-tr, ECO:0000313|Proteomes:UP000007110}; RN [1] {ECO:0000313|EnsemblMetazoa:SPU_005393-tr} RP NUCLEOTIDE SEQUENCE. RA Murali S., Liu Y., Vee V., English A., Wang M., Skinner E., Han Y., RA Muzny D.M., Worley K.C., Gibbs R.A.; RT "Genome sequencing for Strongylocentrotus purpuratus."; RL Submitted (FEB-2015) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EnsemblMetazoa:SPU_005393-tr} RP IDENTIFICATION. RG EnsemblMetazoa; RL Submitted (JUN-2015) to UniProtKB. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AAGJ04118803; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR RefSeq; XP_011678181.1; XM_011679879.1. DR RefSeq; XP_011678182.1; XM_011679880.1. DR RefSeq; XP_011678183.1; XM_011679881.1. DR RefSeq; XP_011678184.1; XM_011679882.1. DR UniGene; Spu.34566; -. DR STRING; 7668.SPU_005393tr; -. DR EnsemblMetazoa; SPU_005393-tr; SPU_005393-tr; SPU_005393. DR GeneID; 593681; -. DR KEGG; spu:593681; -. DR eggNOG; KOG0410; Eukaryota. DR eggNOG; COG2262; LUCA. DR OMA; MDTVGFM; -. DR OrthoDB; EOG091G0852; -. DR Proteomes; UP000007110; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR GO; GO:0043022; F:ribosome binding; IBA:GO_Central. DR CDD; cd01878; HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000007110}; KW Reference proteome {ECO:0000313|Proteomes:UP000007110}. FT DOMAIN 363 529 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 591 AA; 67291 MW; 9BE766E3AF177B19 CRC64; MNIERLRIPA RLLYAVLRVP SSMCRNTNRH RHAMCIPFRA FCIQRNITEI SNSMRMSAIS LTLMNARRSS CFVSSRDYFR YPQIFSSLLS LDDTVQELHC SPTKRCLHQS PVFHRKRKSR TPDENERRFD ETTGDGIDED QEYGEEAIEY ANELVNRGHQ GLQGHRVLVI QPVIKTERRH KSDSELKMIE AQSLVTTLQT WSLFDSRLMT VKSLSKKYMF GQGTFEELTA QIRSQPDITS VFLNVDRLSG VQKKTMEEEW GLPVYDRYEV VLQIFKEHAS SKEAKLQIAL AELHFRRSHL HQETFDLDQQ SGAQQYIGGG GETLLEKKQR QLRDKEGALR KALEKLKGKR ALLRKGRERK HFPHVAVVGY TNAGKTSLIK AMTGDTRLEP RNQLFATLDV TSHAGYLSNR MPVIYIDTVG FISQLPHQLI ASFAATLEDV LCADLLVHVR DVSHPESENQ KIQVISVLHD LGVNQHLLDN MIEVNNKIDL LHNKSEFAAL DECYPVSATH GTGLNQLKEV IEVKLVEVTK SVMCDVRIPQ AGTHLGWLYK EATVQDVSTI EGDTEHLLVS AVFSCTAYSK FTAKYGNLRP S // ID W5DLV6_WHEAT Unreviewed; 589 AA. AC W5DLV6; DT 19-MAR-2014, integrated into UniProtKB/TrEMBL. DT 19-MAR-2014, sequence version 1. DT 07-JUN-2017, entry version 25. DE SubName: Full=Uncharacterized protein {ECO:0000313|EnsemblPlants:TRIAE_CS42_4AL_TGACv1_288523_AA0950970.1}; OS Triticum aestivum (Wheat). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; BOP clade; OC Pooideae; Triticodae; Triticeae; Triticinae; Triticum. OX NCBI_TaxID=4565 {ECO:0000313|EnsemblPlants:TRIAE_CS42_4AL_TGACv1_288523_AA0950970.1, ECO:0000313|Proteomes:UP000019116}; RN [1] {ECO:0000313|EnsemblPlants:TRIAE_CS42_4AL_TGACv1_288523_AA0950970.1, ECO:0000313|Proteomes:UP000019116} RP NUCLEOTIDE SEQUENCE. RC STRAIN=cv. Chinese Spring RC {ECO:0000313|EnsemblPlants:TRIAE_CS42_4AL_TGACv1_288523_AA0950970.1, RC ECO:0000313|Proteomes:UP000019116}; RX PubMed=23192148; DOI=10.1038/nature11650; RA Brenchley R., Spannagl M., Pfeifer M., Barker G.L., D'Amore R., RA Allen A.M., McKenzie N., Kramer M., Kerhornou A., Bolser D., Kay S., RA Waite D., Trick M., Bancroft I., Gu Y., Huo N., Luo M.C., Sehgal S., RA Gill B., Kianian S., Anderson O., Kersey P., Dvorak J., McCombie W.R., RA Hall A., Mayer K.F., Edwards K.J., Bevan M.W., Hall N.; RT "Analysis of the bread wheat genome using whole-genome shotgun RT sequencing."; RL Nature 491:705-710(2012). RN [2] {ECO:0000313|EnsemblPlants:TRIAE_CS42_4AL_TGACv1_288523_AA0950970.1} RP IDENTIFICATION. RG EnsemblPlants; RL Submitted (OCT-2016) to UniProtKB. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EnsemblPlants; TRIAE_CS42_4AL_TGACv1_288523_AA0950970.1; TRIAE_CS42_4AL_TGACv1_288523_AA0950970.1; TRIAE_CS42_4AL_TGACv1_288523_AA0950970. DR EnsemblPlants; TRIAE_CS42_4AL_TGACv1_288523_AA0950970.2; TRIAE_CS42_4AL_TGACv1_288523_AA0950970.2; TRIAE_CS42_4AL_TGACv1_288523_AA0950970. DR Gramene; TRIAE_CS42_4AL_TGACv1_288523_AA0950970.1; TRIAE_CS42_4AL_TGACv1_288523_AA0950970.1; TRIAE_CS42_4AL_TGACv1_288523_AA0950970. DR Gramene; TRIAE_CS42_4AL_TGACv1_288523_AA0950970.2; TRIAE_CS42_4AL_TGACv1_288523_AA0950970.2; TRIAE_CS42_4AL_TGACv1_288523_AA0950970. DR OMA; NGPEAIS; -. DR OrthoDB; EOG09360975; -. DR Proteomes; UP000019116; Unplaced. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR CDD; cd01878; HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000019116}; KW Reference proteome {ECO:0000313|Proteomes:UP000019116}. FT DOMAIN 299 562 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 589 AA; 64315 MW; 3A0725117FFB64A4 CRC64; MLRAAISRLG AHLHRQPSPA TPPLRALSTG RGKRSSPTAP PPEPEDEGLM RGLFVLSRDP AHPPRLLVVQ PRLRRGALLD SKLSEALNLA SSLEESRDGF EHAESAAKGA PPHLVVQNPA SRGRNHADTY FGPGTVDNIK CYLRALDEKE ELDAVFVNTL LSGVQQRNLE VAWGKPVLDR VGLIIEIFNA HAETKEAKLQ SELAALMYMK TRLVRVRGPG GKLAFGASGE AEVVSARGRG SGGRGFMSGA GETELQLQRR RIQERRLSLL AQIEDVRRTR AIQRSSRKRH GGSFGQDLVT VAVVGYTNAG KSTLVSALSG AGLYSDDRLF ATVDPRLRSV ILPSGRKILL SDTVGFISDL PVQLVEAFHA TLEEVAEADM LVHVLDSSAP DLEEHRSTVL QVLQQIGVSQ DKINNMIEVW NKIDLVDNIA LTDGIEDEIF LTEGEEEEDL FSEDDVSSEQ SSFDSLDDTV DSESLSEKSC ENDDDKMASE ESIAEPVEMK AMNSELLPED RFRESNGPEA ISTSACTLTE PVSTCHVKTS AVAGTGLQEL LQLIDTKLNG QQTVVQRSYG PFDRKWRPSS MDDEKAAEQ // ID W5IHN1_SCAIO Unreviewed; 540 AA. AC W5IHN1; DT 19-MAR-2014, integrated into UniProtKB/TrEMBL. DT 19-MAR-2014, sequence version 1. DT 07-JUN-2017, entry version 26. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=HMPREF9020_01413 {ECO:0000313|EMBL:EFG26328.1}; OS Scardovia inopinata F0304. OC Bacteria; Actinobacteria; Bifidobacteriales; Bifidobacteriaceae; OC Scardovia. OX NCBI_TaxID=641146 {ECO:0000313|EMBL:EFG26328.1, ECO:0000313|Proteomes:UP000005777}; RN [1] {ECO:0000313|EMBL:EFG26328.1, ECO:0000313|Proteomes:UP000005777} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=F0304 {ECO:0000313|EMBL:EFG26328.1, RC ECO:0000313|Proteomes:UP000005777}; RG The Broad Institute Genome Sequencing Platform; RA Earl A., Ward D., Feldgarden M., Gevers D., Izard J., Baranova O.V., RA Blanton J.M., Tanner A.C., Dewhirst F.E., Young S.K., Zeng Q., RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L., RA Arachchi H.M., Berlin A., Chapman S.B., Gearin G., Goldberg J., RA Griggs A., Gujja S., Hansen M., Heiman D., Howarth C., Larimer J., RA Lui A., MacDonald P.J., McCowen C., Montmayeur A., Murphy C., RA Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T., RA Sisk P., Stolte C., Sykes S., Wortman J., Nusbaum C., Birren B.; RT "The Genome Sequence of Scardovia inopinata F0304."; RL Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EFG26328.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ADCX01000013; EFG26328.1; -; Genomic_DNA. DR RefSeq; WP_006293803.1; NZ_GG770226.1. DR ProteinModelPortal; W5IHN1; -. DR STRING; 641146.HMPREF9020_01413; -. DR EnsemblBacteria; EFG26328; EFG26328; HMPREF9020_01413. DR eggNOG; ENOG4105C1N; Bacteria. DR eggNOG; COG2262; LUCA. DR Proteomes; UP000005777; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000005777}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000005777}. FT DOMAIN 303 469 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 540 AA; 59139 MW; 4F6226A9D2BD4E4F CRC64; MVQEHSHKSQ ASYKSVRKEG RRNTRLGSIL ENKSQVLLQD SDPGVSGRDM AADDQNQQGA GSREWEQEDW QERESRNQLK KVSGLGELQD VTEVEYRRVR LEKVVLVGIW SSRDSSQSQA EESLRELAAL AQTAGAQVME GVLQHRFKPD PATYIGKGKA GELAAIVAAT QADTIIVDAD LPPSQRRALE DVTKVKVVDR TAVILDIFAQ HATSREGKAQ VELAQLEYML PRLRGWGAAL SRQAGGQAAG VNGGIGSRGP GETQLELDRR VIRTRMARLR KQIARMAPAR DIKRGSRRRN SLPTVAVVGY TNAGKSSLIN RLTNSHELVE NALFATLDTA VRQSKTADSR KFMYVDTVGF VRRLPTQLIE AFKSTLEEVA QASLIVHVVD ISYPDPFSQI DAVNKVLADV PGVEGIPTLM VFNKVDRVDN TTRQRIENLA PDAFFVSAAT GEGIDRLRHA VQAGLPRPNV HVDAVIPYSQ GSLISQIRQF GSLDSADYMD RGVHLVADVD DRLAARIISC AENSGQEENP GGSGQTEAVQ // ID W5KZ42_ASTMX Unreviewed; 552 AA. AC W5KZ42; DT 16-APR-2014, integrated into UniProtKB/TrEMBL. DT 16-APR-2014, sequence version 1. DT 30-AUG-2017, entry version 22. DE SubName: Full=GTP binding protein 6 (putative) {ECO:0000313|Ensembl:ENSAMXP00000012854}; OS Astyanax mexicanus (Blind cave fish) (Astyanax fasciatus mexicanus). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Characiformes; OC Characoidei; Characidae; Characidae incertae sedis; Astyanax clade; OC Astyanax. OX NCBI_TaxID=7994 {ECO:0000313|Ensembl:ENSAMXP00000012854, ECO:0000313|Proteomes:UP000018467}; RN [1] {ECO:0000313|Ensembl:ENSAMXP00000012854, ECO:0000313|Proteomes:UP000018467} RP NUCLEOTIDE SEQUENCE. RC STRAIN=female {ECO:0000313|Ensembl:ENSAMXP00000012854}; RA Jeffery W., Warren W., Wilson R.K.; RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Ensembl:ENSAMXP00000012854} RP IDENTIFICATION. RG Ensembl; RL Submitted (FEB-2014) to UniProtKB. CC -!- CAUTION: The sequence shown here is derived from an Ensembl CC automatic analysis pipeline and should be considered as CC preliminary data. {ECO:0000313|Ensembl:ENSAMXP00000012854}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; APWO01087335; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR RefSeq; XP_007249149.1; XM_007249087.2. DR Ensembl; ENSAMXT00000012854; ENSAMXP00000012854; ENSAMXG00000012493. DR GeneID; 103035228; -. DR CTD; 8225; -. DR GeneTree; ENSGT00390000001397; -. DR OMA; MDTVGFM; -. DR OrthoDB; EOG091G0852; -. DR Proteomes; UP000018467; Unassembled WGS sequence. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR CDD; cd01878; HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000018467}; KW Reference proteome {ECO:0000313|Proteomes:UP000018467}. FT DOMAIN 330 494 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 552 AA; 62550 MW; 0EB5307D966FD5FF CRC64; MDPRRSSLMF RHVLVVCRLA GRRCSLWTNH NEQRFISIQT KHPFTLLNPL LPCPAQSLKT AYRNLHSLQS YLQSRAFSLT LSQFKSKNHS SGDEYVDEVE GANEEDFSGD TEVEELFQQQ VPTGIGEEDH RVFIVHPDVK WGQKKQYLTT AKLQMDEAIG LVNTLQNWSV VDKIILSTKT PEKKRIFGKG NFQLLTEKIR KTAGVTAVFM NVEQLSPLSE KDMQEAWGVK VFDRYSLVLH IFRRNARTKE AKLQISLAEI PLLKSRLKNE VANLDQQGGG SRYIMGSGET LYEVQQRLLK EREMKIRSAL QRLRKKRHLL RSHRKHKDFP VVSVMGYTNC GKTTLIKALT GDSGLQPKDQ LFATLDVTVH GGQLPSHMTV LYVDTIGFLS QLPHQLIDSF SATLEDVAHS DLIVHVRDIS HPETVNQKVN VLNVLKNLQI PEKLMNSIIE VHNKIDLVES YESSEPEAVP ISALKEMGLE ALKQRVEEAV VKSTGKQTIT LKVQLNSPQL GWLYKEATVQ EVCDVGDDCT ANVKVIISAA AYGRYRKLFQ VT // ID W5KZ45_ASTMX Unreviewed; 549 AA. AC W5KZ45; DT 16-APR-2014, integrated into UniProtKB/TrEMBL. DT 16-APR-2014, sequence version 1. DT 30-AUG-2017, entry version 14. DE SubName: Full=GTP binding protein 6 (putative) {ECO:0000313|Ensembl:ENSAMXP00000012857}; OS Astyanax mexicanus (Blind cave fish) (Astyanax fasciatus mexicanus). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Characiformes; OC Characoidei; Characidae; Characidae incertae sedis; Astyanax clade; OC Astyanax. OX NCBI_TaxID=7994 {ECO:0000313|Ensembl:ENSAMXP00000012857, ECO:0000313|Proteomes:UP000018467}; RN [1] {ECO:0000313|Ensembl:ENSAMXP00000012857, ECO:0000313|Proteomes:UP000018467} RP NUCLEOTIDE SEQUENCE. RC STRAIN=female {ECO:0000313|Ensembl:ENSAMXP00000012857}; RA Jeffery W., Warren W., Wilson R.K.; RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Ensembl:ENSAMXP00000012857} RP IDENTIFICATION. RG Ensembl; RL Submitted (FEB-2014) to UniProtKB. CC -!- CAUTION: The sequence shown here is derived from an Ensembl CC automatic analysis pipeline and should be considered as CC preliminary data. {ECO:0000313|Ensembl:ENSAMXP00000012857}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; APWO01087335; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR Ensembl; ENSAMXT00000012857; ENSAMXP00000012857; ENSAMXG00000012493. DR GeneTree; ENSGT00390000001397; -. DR Proteomes; UP000018467; Unassembled WGS sequence. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR CDD; cd01878; HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000018467}; KW Reference proteome {ECO:0000313|Proteomes:UP000018467}. FT DOMAIN 324 488 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 549 AA; 62175 MW; 240763F254E1AE9D CRC64; MFRHVLVVCR LAGRRCSLWT NHNEQRFISI QTKHPFTLLN PLLPCPAQSL KTAYRNLHSL QSYLQSRAFS LTLSQFKSKN HSSGDEYVDE VEGANEEDFS GDTEVEELFQ QQVPTGIGEE DHRVFIVHPD VKWGQKKQYL TTAKLQMDEA IGLVNTLQNW SVVDKIILST KTPEKKRIFG KGNFQLLTEK IRKTAGVTAV FMNVEQLSPL SEKDMQEAWG VKVFDRYSLV LHIFRRNART KEAKLQISLA EIPLLKSRSR LKNEVANLDQ QGGGSRYIMG SGETLYEVQQ RLLKEREMKI RSALQRLRKK RHLLRSHRKH KDFPVVSVMG YTNCGKTTLI KALTGDSGLQ PKDQLFATLD VTVHGGQLPS HMTVLYVDTI GFLSQLPHQL IDSFSATLED VAHSDLIVHV RDISHPETVN QKVNVLNVLK NLQIPEKLMN SIIEVHNKID LVESYESSEP EAVPISALKE MGLEALKQRV EEAVVKSTGK QTITLKVQLN SPQLGWLYKE ATVQEVCDVG DDCTANVKVI ISAAAYGRYR KLFQINALN // ID W5MMX2_LEPOC Unreviewed; 481 AA. AC W5MMX2; DT 16-APR-2014, integrated into UniProtKB/TrEMBL. DT 16-APR-2014, sequence version 1. DT 30-AUG-2017, entry version 20. DE SubName: Full=GTP binding protein 6 (putative) {ECO:0000313|Ensembl:ENSLOCP00000009731}; OS Lepisosteus oculatus (Spotted gar). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Holostei; Semionotiformes; Lepisosteidae; OC Lepisosteus. OX NCBI_TaxID=7918 {ECO:0000313|Ensembl:ENSLOCP00000009731, ECO:0000313|Proteomes:UP000018468}; RN [1] {ECO:0000313|Ensembl:ENSLOCP00000009731, ECO:0000313|Proteomes:UP000018468} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D., RA MacCallum I., Young S., Walker B.J., Lander E.S., Lindblad-Toh K.; RT "The Draft Genome of Lepisosteus oculatus."; RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Ensembl:ENSLOCP00000009731} RP IDENTIFICATION. RG Ensembl; RL Submitted (FEB-2014) to UniProtKB. CC -!- CAUTION: The sequence shown here is derived from an Ensembl CC automatic analysis pipeline and should be considered as CC preliminary data. {ECO:0000313|Ensembl:ENSLOCP00000009731}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AHAT01003385; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AHAT01003386; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR Ensembl; ENSLOCT00000009742; ENSLOCP00000009731; ENSLOCG00000008009. DR GeneTree; ENSGT00390000001397; -. DR OMA; MDTVGFM; -. DR OrthoDB; EOG091G0852; -. DR Proteomes; UP000018468; Unassembled WGS sequence. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR CDD; cd01878; HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000018468}; KW Reference proteome {ECO:0000313|Proteomes:UP000018468}. FT DOMAIN 256 420 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 481 AA; 54056 MW; FC9210CF9FEDA173 CRC64; ISSRSFSVNT CRSKNSNSDL GGESQDPEDD LLEDGDIDQL IQQQITTGVG DQDHRVFIVH PEIKWGQRKQ RLTTAALQME EAVGLVSTLQ NWTVVDKIIV STKTPEKRRI FGKGNFQALT ERIRGLPQIT AVFVNVERLA PVTERELQEA WGLKVFDRYT VVLHIFRCNA RTKEAKLQIS LAEIPLLRSQ LKNDLANLDQ QGGGSRYIMF IHAGETFMEV QQRLLKEREL KLRAALEKLK RKRCLLRSQR QDRDFPIISV VGYTNCGKTT LIKALTGDAG LQPRDQLFAT LDVTVHAGQL PSHMTVLFVD TIGFLSQLPH QLIDSFSATL QDVVHSDLII HVRDISHPES LNQKVNVLNV LKNLQVPSRL MDNIIEVHNK IDLVDGYQPT EPNIQPISAL KGQGLEVLKK RVEDVVLKTT GKHILTIKVD LSSSQLSWLY REATVQEVGV VPEEGTANVK VIISSAAYGR YRKLFQASVL S // ID W5NS42_SHEEP Unreviewed; 414 AA. AC W5NS42; DT 16-APR-2014, integrated into UniProtKB/TrEMBL. DT 16-APR-2014, sequence version 1. DT 30-AUG-2017, entry version 20. DE SubName: Full=GTP binding protein 6 (putative) {ECO:0000313|Ensembl:ENSOARP00000000982}; GN Name=GTPBP6 {ECO:0000313|Ensembl:ENSOARP00000000982}; OS Ovis aries (Sheep). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia; OC Pecora; Bovidae; Caprinae; Ovis. OX NCBI_TaxID=9940 {ECO:0000313|Ensembl:ENSOARP00000000982, ECO:0000313|Proteomes:UP000002356}; RN [1] {ECO:0000313|Ensembl:ENSOARP00000000982, ECO:0000313|Proteomes:UP000002356} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Texel {ECO:0000313|Ensembl:ENSOARP00000000982, RC ECO:0000313|Proteomes:UP000002356}; RX PubMed=20809919; DOI=10.1111/j.1365-2052.2010.02100.x; RA Archibald A.L., Cockett N.E., Dalrymple B.P., Faraut T., Kijas J.W., RA Maddox J.F., McEwan J.C., Hutton Oddy V., Raadsma H.W., Wade C., RA Wang J., Wang W., Xun X.; RT "The sheep genome reference sequence: a work in progress."; RL Anim. Genet. 41:449-453(2010). RN [2] {ECO:0000313|Ensembl:ENSOARP00000000982} RP IDENTIFICATION. RG Ensembl; RL Submitted (FEB-2014) to UniProtKB. CC -!- CAUTION: The sequence shown here is derived from an Ensembl CC automatic analysis pipeline and should be considered as CC preliminary data. {ECO:0000313|Ensembl:ENSOARP00000000982}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR Ensembl; ENSOART00000001015; ENSOARP00000000982; ENSOARG00000000946. DR GeneTree; ENSGT00390000001397; -. DR OMA; MDTVGFM; -. DR OrthoDB; EOG091G0852; -. DR Proteomes; UP000002356; Unplaced. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR CDD; cd01878; HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000002356}; KW Reference proteome {ECO:0000313|Proteomes:UP000002356}. FT DOMAIN 186 350 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 414 AA; 45107 MW; 6156D86B16994875 CRC64; AEWQVAEARA LVCTLDGWSV VATMVVPTKT PDKKLIFGRG TLEQLTERIR GSPEITAVFL NVERLATPTK KDLEAAWCVP VFDRFTLVLH IFRCNACAQV RAGPGLGQTD PPLPPPPPPR SHVKSNAAHL GGRGRSSRYT MGSGESFLQV QQRLLRDRET KIQKALERLR RKRRLLGQQR RRREFPVVSV VGYTNCGKTT LIKALTGDAA IQPRDQLFAT LDVTAHAGRL PSALTVLYMD TIGFLSQLPH SLVESFSATL QDVAHSDLIV HVRDVSHPET ELQKASVLSA LGGLGLPDAL LESMVEVHNK VDLVPGYTPV EPDVLAVSAL LGLGLDELMA RVEDAILRAT GRRTLTLRVR LAGPQLSWLH QEATVQAVDV IPEAGAADVK VIISDSAYGR FQKLFPGSAP AGLH // ID W5TME4_9NOCA Unreviewed; 532 AA. AC W5TME4; DT 16-APR-2014, integrated into UniProtKB/TrEMBL. DT 16-APR-2014, sequence version 1. DT 07-JUN-2017, entry version 24. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:AHH20168.1}; GN ORFNames=NONO_c53880 {ECO:0000313|EMBL:AHH20168.1}; OS Nocardia nova SH22a. OC Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae; Nocardia. OX NCBI_TaxID=1415166 {ECO:0000313|EMBL:AHH20168.1, ECO:0000313|Proteomes:UP000019150}; RN [1] {ECO:0000313|EMBL:AHH20168.1, ECO:0000313|Proteomes:UP000019150} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SH22a {ECO:0000313|EMBL:AHH20168.1}; RX PubMed=24747905; RA Luo Q., Hiessl S., Poehlein A., Daniel R., Steinbuchel A.; RT "Insights into the Microbial Degradation of Rubber and Gutta-Percha by RT Analysis of the Complete Genome of Nocardia nova SH22a."; RL Appl. Environ. Microbiol. 80:3895-3907(2014). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP006850; AHH20168.1; -; Genomic_DNA. DR EnsemblBacteria; AHH20168; AHH20168; NONO_c53880. DR KEGG; nno:NONO_c53880; -. DR PATRIC; fig|1415166.3.peg.5557; -. DR KO; K03665; -. DR Proteomes; UP000019150; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 2. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000019150}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000019150}. FT DOMAIN 294 463 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 253 287 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 532 AA; 57131 MW; 210BB7C3BE1C202D CRC64; MRKSETYEFT PIEQLDSDGD GYVDQDYSIG DDDIDIGVSD YDDDVEYGDA RAGWSAAPTV GELQLDERSA LRRVAGLSTE LTDVTEVEYR QLRLERVVLV GVWTEGSAAQ ADASMAELAA LAETAGSQVL DALIQRRDKP DPATYIGSGK ADELRTVVLG TGADTVICDG ELTPAQLTAL EKVVKVKVID RTALILDIFA QHATSREGKA QVSLAQMEYM LPRLRGWGES MSRQAGGRAG GAGGGVGTRG PGETKIETDR RRIRERMSKL RREIKEMKTA RDTKRSRRTS SGIPSVAIVG YTNAGKSSLM NALTGAGILV QDALFATLDP TTRRAALDDG REVVFTDTVG FVRHLPTQLV EAFRSTLEEV TGADLLLHVV DGSDALPDQQ IKAVREVVTD VLREQGATAP PELLVVNKID ALDPTALAQL RAQLPGAIFV SARTGRGIDK LRARLAEILG GLDVEVSVLL PYTRGDLLAR IHSDGRIISS SHEEGGTRVR ARVPRALAPT LSQYAHASTV SGAEAAGPSH QL // ID W5WFN6_9PSEU Unreviewed; 480 AA. AC W5WFN6; DT 16-APR-2014, integrated into UniProtKB/TrEMBL. DT 16-APR-2014, sequence version 1. DT 07-JUN-2017, entry version 22. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=KALB_6659 {ECO:0000313|EMBL:AHI00019.1}; OS Kutzneria albida DSM 43870. OC Bacteria; Actinobacteria; Pseudonocardiales; Pseudonocardiaceae; OC Kutzneria. OX NCBI_TaxID=1449976 {ECO:0000313|EMBL:AHI00019.1, ECO:0000313|Proteomes:UP000019225}; RN [1] {ECO:0000313|EMBL:AHI00019.1, ECO:0000313|Proteomes:UP000019225} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 43870 {ECO:0000313|EMBL:AHI00019.1}; RX PubMed=25301375; DOI=10.1186/1471-2164-15-885; RA Rebets Y., Tokovenko B., Lushchyk I., Ruckert C., Zaburannyi N., RA Bechthold A., Kalinowski J., Luzhetskyy A.; RT "Complete genome sequence of producer of the glycopeptide antibiotic RT Aculeximycin Kutzneria albida DSM 43870T, a representative of minor RT genus of Pseudonocardiaceae."; RL BMC Genomics 15:885-885(2014). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP007155; AHI00019.1; -; Genomic_DNA. DR RefSeq; WP_025359895.1; NZ_CP007155.1. DR EnsemblBacteria; AHI00019; AHI00019; KALB_6659. DR KEGG; kal:KALB_6659; -. DR PATRIC; fig|1449976.3.peg.6685; -. DR KO; K03665; -. DR Proteomes; UP000019225; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 2. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000019225}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000019225}. FT DOMAIN 253 422 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 480 AA; 51870 MW; 3564D7191E2B10E0 CRC64; MTETYAFEPG DDGDELLSTG DLELADRAAL RRIAGLSTEL DDITEVEYRQ LRLERVVLVG VWTEGSAADS EASLAELARL AETAGSQVLE GLVQRRDRPD PATYVGSGKV REVRDVVVAT GADTVICDGE LSSGQLRQLE ERLKVKVVDR TALILDIFAQ HAQSKEGKAQ VELAQLQYLL PRLRGWGSAM SRQAGGRAGG ASGGVGLRGP GETKLETDRR RIHKRIAKLR KEIQAMSVVR ETKRGRRVAN EVPSVAIVGY TNAGKSSLLN AVTEAGVLVQ DALFATLDPT TRRSTTPEGL PYTLTDTVGF VRHLPHQIVE AFRSTLEEAA DADLLLHVVD GSDPRPEWQV QAVREVLGEI GGELNRPMPR ELVVVNKTDA ADEVALARLR NLLPGAAFVS AHTGSGVAAL REQVAELLPR PTLVVEVLVP YTQGALVARV HAEGEVLEER HTEEGTELRA RVRGDLAGAL ERFAVNSTPA // ID W5WR55_9CORY Unreviewed; 501 AA. AC W5WR55; DT 16-APR-2014, integrated into UniProtKB/TrEMBL. DT 16-APR-2014, sequence version 1. DT 07-JUN-2017, entry version 24. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=CFAL_06180 {ECO:0000313|EMBL:AHI03251.1}; OS Corynebacterium falsenii DSM 44353. OC Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae; OC Corynebacterium. OX NCBI_TaxID=1451189 {ECO:0000313|EMBL:AHI03251.1, ECO:0000313|Proteomes:UP000019232}; RN [1] {ECO:0000313|EMBL:AHI03251.1, ECO:0000313|Proteomes:UP000019232} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BL 8171 {ECO:0000313|EMBL:AHI03251.1}; RX PubMed=24604654; RA Glaub A., Bomholt C., Gravermann K., Brinkrolf K., Albersmeier A., RA Ruckert C., Tauch A.; RT "Complete Genome Sequence of Corynebacterium falsenii DSM 44353 To RT Study the Evolution of Corynebacterium Cluster 3 Species."; RL Genome Announc. 2:e00158-14(2014). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP007156; AHI03251.1; -; Genomic_DNA. DR EnsemblBacteria; AHI03251; AHI03251; CFAL_06180. DR KEGG; cfn:CFAL_06180; -. DR PATRIC; fig|1451189.3.peg.1203; -. DR KO; K03665; -. DR Proteomes; UP000019232; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000019232}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000019232}. FT DOMAIN 279 448 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 238 265 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 501 AA; 54860 MW; 28C68EBAA5795D4A CRC64; MTDFSQHNFT ERDAANSDDY YSDDYYDAVH GANQNPRHDP TVGELDLEAR SSLRRLTRGV SSYTDEQSDG YDVEYRKLRL EKVVLVGVWT EGTVAQIEAR LEELAALAET AGSDIVDMLY QRRDKPDAGT YIGRGKVEEL KSIVAETGAD TVICDGELSP GQMIALEKAL NVKVIDRTML ILDIFAQHAK SKEGKAQVAL AQMEYLITRV RGWGGALSRQ AGGRAGSNGG VGLRGPGETK IEADRRRLRS EMAKLRKEIA GMKTSRDIKR ERRDRAAIPQ VAIAGYTNAG KSSLINALTG AGVLVEDALF ATLDPTTRRA SLADGRTVVF SDTVGFVRHL PTQLVEAFRS TLEEVLAADV VLHVVDGSDP FPLEQIQAVN KVINEIVEET GRPAPPEIMV VNKIDKADPL VLAELRAAID DVVFVSAHTG EGIKELEARL EVFLNTLDKQ VTLHVPFDRG DVVARLHELG TVLDEQYDEQ GTRVEVRVPA AVANELASFE V // ID W5WY82_BDEBC Unreviewed; 421 AA. AC W5WY82; DT 16-APR-2014, integrated into UniProtKB/TrEMBL. DT 16-APR-2014, sequence version 1. DT 07-JUN-2017, entry version 21. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=BDW_06785 {ECO:0000313|EMBL:AHI05863.1}; OS Bdellovibrio bacteriovorus W. OC Bacteria; Proteobacteria; Deltaproteobacteria; Bdellovibrionales; OC Bdellovibrionaceae; Bdellovibrio. OX NCBI_TaxID=765869 {ECO:0000313|EMBL:AHI05863.1, ECO:0000313|Proteomes:UP000019233}; RN [1] {ECO:0000313|EMBL:AHI05863.1, ECO:0000313|Proteomes:UP000019233} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=W {ECO:0000313|EMBL:AHI05863.1, RC ECO:0000313|Proteomes:UP000019233}; RA Mussa H.J., Iandolo J.J.; RL Submitted (SEP-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002190; AHI05863.1; -; Genomic_DNA. DR RefSeq; WP_025308089.1; NZ_CP002190.1. DR EnsemblBacteria; AHI05863; AHI05863; BDW_06785. DR KEGG; bbw:BDW_06785; -. DR PATRIC; fig|765869.4.peg.1349; -. DR KO; K03665; -. DR Proteomes; UP000019233; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000019233}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000019233}. FT DOMAIN 204 367 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 421 AA; 47210 MW; DCB2963D614E6F1D CRC64; MSQDTKLTAQ DKAIVIGVGL KTEPLSEIKE NLLELEELVG AAGGEVVGSL TQVLDKWNPS TLIGSGKVEE VAEMVRDSEA NLVVVDHQLS GVQQRNLAQI VKVRVLDRNQ LILDIFAQRA QTFEGKLQVE LAQLLDQMPR MVGAWLESLS RQGGGIGTRG PGETALENDR RRIRERVAII RKKLDGVRKN RAQHRQSRRR SEIPSFALIG YTNSGKSSIL NRLTGAQVMA KNQVFATLDP TTRKIFLPDG PPAVVTDTVG FIRKLPTQLI EAFKATLEES SEADVLIHVI DLSSPNMDRQ IEVVEALIEE FKWDQKKIIH VYNKCDIAPL ERQFRVKHHP RVFVSALTGQ GLEQLKKMMA QTVAEMQTNV ELFFPKSEEF KIFDLSREAP ILRRESASEG TVCYTQLSPQ LLAKWKSYIV K // ID W5X4T5_BDEBC Unreviewed; 478 AA. AC W5X4T5; DT 16-APR-2014, integrated into UniProtKB/TrEMBL. DT 16-APR-2014, sequence version 1. DT 07-JUN-2017, entry version 22. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=BDW_04760 {ECO:0000313|EMBL:AHI05460.1}; OS Bdellovibrio bacteriovorus W. OC Bacteria; Proteobacteria; Deltaproteobacteria; Bdellovibrionales; OC Bdellovibrionaceae; Bdellovibrio. OX NCBI_TaxID=765869 {ECO:0000313|EMBL:AHI05460.1, ECO:0000313|Proteomes:UP000019233}; RN [1] {ECO:0000313|EMBL:AHI05460.1, ECO:0000313|Proteomes:UP000019233} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=W {ECO:0000313|EMBL:AHI05460.1, RC ECO:0000313|Proteomes:UP000019233}; RA Mussa H.J., Iandolo J.J.; RL Submitted (SEP-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP002190; AHI05460.1; -; Genomic_DNA. DR RefSeq; WP_025307709.1; NZ_CP002190.1. DR EnsemblBacteria; AHI05460; AHI05460; BDW_04760. DR KEGG; bbw:BDW_04760; -. DR PATRIC; fig|765869.4.peg.951; -. DR KO; K03665; -. DR Proteomes; UP000019233; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 2. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000019233}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000019233}. FT DOMAIN 259 424 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 220 247 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 478 AA; 53272 MW; A0339626E12A62F5 CRC64; MNVIINEKPQ KAFLVAVQLP RVSDAEIQSS LKELSRLVTT LGYEVIGQTS QRRSSERGGT VLGDGKLKEV ASWTGGTGVV GPLVVKKKHK AALKFKKNQE DEEDELLEAD DLDADLDYSV QEEDPEEIGV TAPKKELAEV LVVDCELSPS QIRNLESATG AKVLDRTGVI IEIFSRHART KAAKLQVEIA RLKYIAPRLR ETLGGEDRQG GGTGSKGLGE TSIELDRRKI RDRIKELRDE LRSIANEHTV RRSRREQEIT VALVGYTNAG KSSLMRSLTG SDVYIADKLF ATLDTTIRIM QPESKPKILI SDTVGFIKKL PHDLVASFKS TLDEALNASL LLYIVDCADP TFRSQLQVTK KVLAEVGAQD IESKLILNKI DKLSEEERQL LSDEFPDAIQ MCSLKKEDVI DLREKLIKHF ESSMTDQEIF IPYDVQGAIG DIRGKLKVLS EEYTDRGLML KVRGDDDDIL KIKKKFGL // ID W5XSH5_9CORY Unreviewed; 525 AA. AC W5XSH5; DT 16-APR-2014, integrated into UniProtKB/TrEMBL. DT 16-APR-2014, sequence version 1. DT 07-JUN-2017, entry version 23. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=CCASEI_06405 {ECO:0000313|EMBL:AHI19857.1}; OS Corynebacterium casei LMG S-19264. OC Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae; OC Corynebacterium. OX NCBI_TaxID=1285583 {ECO:0000313|EMBL:AHI19857.1, ECO:0000313|Proteomes:UP000019226}; RN [1] {ECO:0000313|EMBL:AHI19857.1, ECO:0000313|Proteomes:UP000019226} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=LMG S-19264 {ECO:0000313|EMBL:AHI19857.1, RC ECO:0000313|Proteomes:UP000019226}; RA Ruckert C., Albersmeier A., Kalinowski J.; RT "The complete genome sequence of Corynebacterium casei LMG S-19264 RT (=DSM 44701)."; RL Submitted (FEB-2013) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP004350; AHI19857.1; -; Genomic_DNA. DR RefSeq; WP_006821782.1; NZ_CP004350.1. DR EnsemblBacteria; AHI19857; AHI19857; CCASEI_06405. DR KEGG; ccg:CCASEI_06405; -. DR PATRIC; fig|1285583.3.peg.1266; -. DR KO; K03665; -. DR Proteomes; UP000019226; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000019226}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000019226}. FT DOMAIN 278 449 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 525 AA; 57829 MW; 953FB09A97AF79EA CRC64; MTDFSNRFNS EKERDELLAR AFSENTPQPR SGERDDEDLT LGELELAERN AFRRVTRDTE IRAEDTTDGY EVEYRKLRLE QVVLVGVWTE GTAAEVEATM SELAALTETA GAEIVQMLYQ KRDRPDPGTF IGSGKVKELK QIIESTGADT VVCDGELNPG QLSALERELN TKVIDRTMLI LDIFAQHAKS KEGKAQVSLA QLEYLYTHTR GWGGNLSRQG GGRAGSNGGV GLRGPGETKI ESDRRRIRTE MSRLRKELKG MQTARDVKRA NRQRSTVPQI AIAGYTNAGK SSLINALTGA GVLVEDALFA TLDPTTRKAE LGDGRHVVLT DTVGFVRHLP TQLVEAFKST LEEVFNADLM LHVVDGADPF PLKQIDAVNK VIYDIAKETG ETPPPEIIVI NKIDAADELA LAEIRHVLDR DNVVYVSAFT GEGISELTTR IELFLNSLDS HVQLLVPFTR GDVIARVHDL GTVLDESYVE EGTFVDVRLP AQLAGELEEF IIGEEEATKL MNKDSSATDS DRSAS // ID W5Y251_9CORY Unreviewed; 516 AA. AC W5Y251; DT 16-APR-2014, integrated into UniProtKB/TrEMBL. DT 16-APR-2014, sequence version 1. DT 07-JUN-2017, entry version 22. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=B843_08045 {ECO:0000313|EMBL:AHI22994.1}; OS Corynebacterium vitaeruminis DSM 20294. OC Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae; OC Corynebacterium. OX NCBI_TaxID=1224164 {ECO:0000313|EMBL:AHI22994.1, ECO:0000313|Proteomes:UP000019222}; RN [1] {ECO:0000313|EMBL:AHI22994.1, ECO:0000313|Proteomes:UP000019222} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 10234 {ECO:0000313|Proteomes:UP000019222}; RA Ruckert C., Albersmeier A., Kalinowski J.; RT "The complete genome sequence of Corynebacterium vitaeruminis DSM RT 20294."; RL Submitted (FEB-2013) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP004353; AHI22994.1; -; Genomic_DNA. DR RefSeq; WP_025253012.1; NZ_CP004353.1. DR EnsemblBacteria; AHI22994; AHI22994; B843_08045. DR KEGG; cvt:B843_08045; -. DR PATRIC; fig|1224164.3.peg.1620; -. DR KO; K03665; -. DR Proteomes; UP000019222; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000019222}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000019222}. FT DOMAIN 288 464 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 247 274 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 516 AA; 56289 MW; C9FDB14A2BCC5791 CRC64; MDHTHSPSRH NDLLAEAFKD HYDTVAEPKG VDLTGLEAVT EHPEGAHTPT TGELDLEARS SLRRLTRGSD IHATDQDDGY DVEYRKLRLE RVILVGVWTT GTTAEIEATM QELAALAETA GSEVVEMLYQ KRDKPDPGTY IGSGKVAELK DIVMSTGVDT VICDGELSPG QMIALEKALD VKVIDRTMLI LDIFAQHAKS KEGKAQVSLA QMEYLITRVR GWGGALSRQA GGRAGSNGGV GLRGPGETKI EADRRRLRSD MAKLRREIAG MKTAREVKRS RRRASTIPQI AIAGYTNAGK SSLINAMTGA GVLVEDALFA TLDPTTRRAE LADGRAVVFT DTVGFVRHLP TQLVEAFRST LEEVVEADLV LHVVDGSDPF PLKQIEAVNS VIGDIVRELD VPAPPEIIVV NKIDAADPLV LAELRHALDD VVFVSAHTHE GIPELEARVE LFLNSLDAHV SLLIPFTRGD VVSRLHEFGT VLRESYTETG TLIDVRLPQE LAAELREFQV EATQEV // ID W5Y597_KOMXY Unreviewed; 436 AA. AC W5Y597; DT 16-APR-2014, integrated into UniProtKB/TrEMBL. DT 16-APR-2014, sequence version 1. DT 07-JUN-2017, entry version 20. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=H845_436 {ECO:0000313|EMBL:AHI24397.1}; OS Komagataeibacter xylinus E25. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales; OC Acetobacteraceae; Komagataeibacter. OX NCBI_TaxID=1296990 {ECO:0000313|EMBL:AHI24397.1, ECO:0000313|Proteomes:UP000019231}; RN [1] {ECO:0000313|EMBL:AHI24397.1, ECO:0000313|Proteomes:UP000019231} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=E25 {ECO:0000313|EMBL:AHI24397.1, RC ECO:0000313|Proteomes:UP000019231}; RA Kubiak K., Kurzawa M., Jedrzejczak-Krzepkowska M., Krystynowicz A., RA Krawczyk M., Migdalski A., Kacprzak M., Loska D., Bielecki S.; RL Submitted (FEB-2013) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP004360; AHI24397.1; -; Genomic_DNA. DR RefSeq; WP_025437488.1; NZ_CP004360.1. DR EnsemblBacteria; AHI24397; AHI24397; H845_436. DR GeneID; 25559699; -. DR KEGG; gxl:H845_436; -. DR PATRIC; fig|1296990.3.peg.474; -. DR KO; K03665; -. DR Proteomes; UP000019231; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000019231}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000019231}. FT DOMAIN 206 375 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 436 AA; 47935 MW; ADCFD3ECCD364BD0 CRC64; MTVAQPPSAT RAAVILPWER PDRHDDARAA EARLEEAVGL AASIGLVVVC QAVLLLRARR PATLLGGGQV DSLKETVKAD NITVVIIDSR LTPVQQRNLE RALGCKVIDR TALILDIFGE RAATREGTLQ VELAHLEYQR SRLVRTWTHL ERQRGGFGFL GGPGETQIEA DRRMIGDRIV RLKRELEQVR RTRGLHRQAR RRVPFPIVAL VGYTNAGKST LFNALTGASV YAQDQLFATL DPTMRGIQLP SGRRVILSDT VGFISDLPTE LIAAFRATLE EVAEADIILH VRDVSHPDSA SQRSDVIEVL EGMARNGTIE QDWQSRVIEV LNKADLVGGR DAVGARPGNV VISAITGDGL PDLLAAIDER MTRAMEVVAY RVPLVEGAAM AWLYEHGEVT QRTDGEDGAE MTVRLSPANR ARFEMQFGRI VTCLLE // ID W6JCI2_9ENTR Unreviewed; 426 AA. AC W6JCI2; DT 16-APR-2014, integrated into UniProtKB/TrEMBL. DT 16-APR-2014, sequence version 1. DT 30-AUG-2017, entry version 29. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=C813_12940 {ECO:0000313|EMBL:AHJ75539.1}; OS Kosakonia sacchari SP1. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; OC Enterobacteriaceae; Kosakonia. OX NCBI_TaxID=1235834 {ECO:0000313|EMBL:AHJ75539.1, ECO:0000313|Proteomes:UP000019435}; RN [1] {ECO:0000313|EMBL:AHJ75539.1, ECO:0000313|Proteomes:UP000019435} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SP1 {ECO:0000313|EMBL:AHJ75539.1, RC ECO:0000313|Proteomes:UP000019435}; RX PubMed=23209221; DOI=10.1128/JB.01933-12; RA Zhu B., Chen M., Lin L., Yang L., Li Y., An Q.; RT "Genome sequence of Enterobacter sp. strain SP1, an endophytic RT nitrogen-fixing bacterium isolated from sugarcane."; RL J. Bacteriol. 194:6963-6964(2012). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP007215; AHJ75539.1; -; Genomic_DNA. DR RefSeq; WP_017459170.1; NZ_CP007215.2. DR EnsemblBacteria; AHJ75539; AHJ75539; C813_12940. DR GeneID; 23845827; -. DR KEGG; ksa:C813_12940; -. DR KO; K03665; -. DR Proteomes; UP000019435; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000019435}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}. FT DOMAIN 198 365 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 426 AA; 48193 MW; A371D34A0D1A159C CRC64; MFDRYDAGEQ AVLVHIYFSQ DKDMEDLQEF ESLVSSAGVE AMQVITGSRK APHPKYFVGE GKAVEIADAV KSAGASVVLF DHALTPAQER NLERLCECRV IDRTGLILDI FAQRARTHEG KLQVELAQLR HLATRLVRGW THLERQKGGI GLRGPGETQL ETDRRLLRNR ITQILSRLEK VEKQREQGRR SRTKADIPTV SLVGYTNAGK STLFNHITEA QVYAADQLFA TLDPTLRRID VADVGETVLA DTVGFIRHLP HDLVAAFKAT LQETRQATLL LHVIDAADVR VQENIDAVNT VLEEIEAHEI STLLVMNKID MLDDFEPRID RDEENKPIRV WLSAQTGVGV PLLFQALTER LAGEVAQHTL RLPPQEGRLR SRFYQLQAIE KEWMEDDGSV GMQVRMPIVD WRRLCKQEPA LEEYVV // ID W6JVH7_9MICO Unreviewed; 487 AA. AC W6JVH7; DT 16-APR-2014, integrated into UniProtKB/TrEMBL. DT 16-APR-2014, sequence version 1. DT 07-JUN-2017, entry version 23. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:CCH72590.1}; GN ORFNames=BN11_180008 {ECO:0000313|EMBL:CCH72590.1}; OS Tetrasphaera australiensis Ben110. OC Bacteria; Actinobacteria; Micrococcales; Intrasporangiaceae; OC Tetrasphaera. OX NCBI_TaxID=1193182 {ECO:0000313|EMBL:CCH72590.1, ECO:0000313|Proteomes:UP000035763}; RN [1] {ECO:0000313|EMBL:CCH72590.1, ECO:0000313|Proteomes:UP000035763} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Ben110 {ECO:0000313|EMBL:CCH72590.1, RC ECO:0000313|Proteomes:UP000035763}; RX PubMed=23178666; DOI=10.1038/ismej.2012.136; RA Kristiansen R., Nguyen H.T.T., Saunders A.M., Nielsen J.L., Wimmer R., RA Le V.Q., McIlroy S.J., Petrovski S., Seviour R.J., Calteau A., RA Nielsen K.L., Nielsen P.H.; RT "A metabolic model for members of the genus Tetrasphaera involved in RT enhanced biological phosphorus removal."; RL ISME J. 7:543-554(2013). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:CCH72590.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CAJA01000090; CCH72590.1; -; Genomic_DNA. DR RefSeq; WP_048693859.1; NZ_HG764815.1. DR EnsemblBacteria; CCH72590; CCH72590; BN11_180008. DR Proteomes; UP000035763; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000035763}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000035763}. FT DOMAIN 269 434 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 487 AA; 53013 MW; 19213CA0ADC57639 CRC64; MTEPLDDLRG DDADDILARP AEALAGTTYD HDDRDGDQFD REERAALQRV EGLSTELEDI TEVEYRQLRL ERVVLAGVWT EGAAEDAENS LRELAALAET AGSTVLAGLM QRRQRPDPGT WLGSGKAQEL RDVVIAEGAD TVVCDSELAP SQRRALEDIV KVKVIDRTAL ILDIFAQHAK SREGKAQVEL AQLQYLLPRL RGWGESMSRQ AGGRVAGGEG IGSRGPGETK IELDRRRINS RIAKLRRDIR DMKTHRDTKR HSRKAHGTPS VAIAGYTNAG KSSILNRLTG AGVLVENQLF ATLDTTVRRA ETPDGREFTL TDTVGFVRQL PHELIDAFRS TLEEVADADL LLHVVDGSHP DPEGQISAVR AVLADVDAAD VKEVIVVNKA DIADPEVVDR ILRHEKHAIA VSAHTGAGIA ELIELIADEL PRPSVRVVAT VPYARGDLMS RIHESGEIAE TEHREDGTYV VALVGPDLAA DLAAFAS // ID W6K775_9PROT Unreviewed; 425 AA. AC W6K775; DT 16-APR-2014, integrated into UniProtKB/TrEMBL. DT 16-APR-2014, sequence version 1. DT 07-JUN-2017, entry version 23. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=MGMAQ_1900 {ECO:0000313|EMBL:CCQ73796.1}; OS Magnetospira sp. QH-2. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales; OC Rhodospirillaceae; Magnetospira. OX NCBI_TaxID=1288970 {ECO:0000313|EMBL:CCQ73796.1, ECO:0000313|Proteomes:UP000032733}; RN [1] {ECO:0000313|EMBL:CCQ73796.1, ECO:0000313|Proteomes:UP000032733} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=QH-2 {ECO:0000313|EMBL:CCQ73796.1}; RX PubMed=23841906; DOI=10.1111/1462-2920.12180; RA Ji B., Zhang S.D., Arnoux P., Rouy Z., Alberto F., Philippe N., RA Murat D., Zhang W.J., Rioux J.B., Ginet N., Sabaty M., Mangenot S., RA Pradel N., Tian J., Yang J., Zhang L., Zhang W., Pan H., Henrissat B., RA Coutinho P.M., Li Y., Xiao T., Medigue C., Barbe V., Pignol D., RA Talla E., Wu L.F.; RT "Comparative genomic analysis provides insights into the evolution and RT niche adaptation of marine Magnetospira sp. QH-2 strain."; RL Environ. Microbiol. 16:525-544(2014). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; FO538765; CCQ73796.1; -; Genomic_DNA. DR RefSeq; WP_046021288.1; NZ_FO538765.1. DR EnsemblBacteria; CCQ73796; CCQ73796; MGMAQ_1900. DR KEGG; magq:MGMAQ_1900; -. DR KO; K03665; -. DR Proteomes; UP000032733; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000032733}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000032733}. FT DOMAIN 197 370 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 425 AA; 47260 MW; 5EC952332014D4A1 CRC64; MSDNCLVIHP VLHRRDAARD PQGRLQEARG LAEAIRLNIV HGEAVTVSRI KPATLLGGGS VERFARIIEE NKVDVVVMDA ALTPVQQRNL EKAWDCKVID RTGLILEIFG DRARTKEGVL QVELAALTYA RSRLVRSWTH LERQRGGLGF VGGPGETQIE ADRRMIDEKI VRLKRDLEDV RRTRLLHRQA RQRVPYPIVA LVGYTNAGKS TLFNRLTAAH VEAKDQLFAT LDPTMRGLDL PSGRRVILSD TVGFVSDLPH ELVNAFHATL EEVREADLLI HVRDIAHGDT EAQKQDVLSV LKDEMSLEDM AEQGTIEALN KTDLLDEESL EALINRTTRP DSLAVALSAH SGEGCASILA MIDARLSVAW ETVELALRPT EGKMLAWLYN HGEVLAREDT EDHTAVTVRL SPENLGRLKI LQKSA // ID W6LSW8_9GAMM Unreviewed; 426 AA. AC W6LSW8; DT 16-APR-2014, integrated into UniProtKB/TrEMBL. DT 16-APR-2014, sequence version 1. DT 12-APR-2017, entry version 20. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:CDH43699.1}; GN ORFNames=BN874_130024 {ECO:0000313|EMBL:CDH43699.1}; OS Candidatus Contendobacter odensis Run_B_J11. OC Bacteria; Proteobacteria; Gammaproteobacteria; Competibacteraceae; OC Candidatus Contendobacter. OX NCBI_TaxID=1400861 {ECO:0000313|EMBL:CDH43699.1, ECO:0000313|Proteomes:UP000019184}; RN [1] {ECO:0000313|EMBL:CDH43699.1, ECO:0000313|Proteomes:UP000019184} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Run_B_J11 {ECO:0000313|EMBL:CDH43699.1, RC ECO:0000313|Proteomes:UP000019184}; RX DOI=10.1038/ismej.2013.162; RA McIlroy S.J., Albertsen M., Andresen E.K., Saunders A.M., RA Kristiansen R., Stokholm-Bjerregaard M., Nielsen K.L., Nielsen P.H.; RT "Candidatus Competibacter-lineage genomes retrieved from metagenomes RT reveal functional metabolic diversity."; RL ISME J. 0:0-0(2014). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:CDH43699.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CBTK010000035; CDH43699.1; -; Genomic_DNA. DR Proteomes; UP000019184; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000019184}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Hydrolase {ECO:0000313|EMBL:CDH43699.1}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Protease {ECO:0000313|EMBL:CDH43699.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000019184}. FT DOMAIN 186 352 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 152 179 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 426 AA; 47142 MW; 0F3CBDD50A182B29 CRC64; MHLLLDRAGD EDQDRAEFRD LAISAGAECV ALISGHRKAP DPRLFVGSGK AEEIRTTIQE TGAELVLFDH ALSPGQERNL EALLQCRVVD RTGLILDIFA QRARSFEGKL QVELAQLRHL STRLVRGWTH LERQRGGIGL RGPGETQLET DRRLLADRIR QLRLRLDRVD RQREQGRRAR RKADLPTVSL VGYTNAGKST LFNALTQAGV YAADQLFATL DPTLRRLDLP GAEPVVLADT VGFINRLPHE LVAAFRSTLR ETCEARLLLH VIDASHPDRD AVIEHVEAVL AEIGATAVPQ LQIFNKIDLS SESPRLERDA DGQVRAVWVS AVTGAGIDVL MTALAERLQG DTVHGWLCLP PAAARLRAKL FDLGAVVAEQ MEPTGEWLIE VHTSRGNVDW LCRREGLRAE WVRSGFDIPA ASTISI // ID W6M2G8_9GAMM Unreviewed; 441 AA. AC W6M2G8; DT 16-APR-2014, integrated into UniProtKB/TrEMBL. DT 16-APR-2014, sequence version 1. DT 12-APR-2017, entry version 19. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:CDI01701.1}; GN ORFNames=BN873_20025 {ECO:0000313|EMBL:CDI01701.1}; OS Candidatus Competibacter denitrificans Run_A_D11. OC Bacteria; Proteobacteria; Gammaproteobacteria; Competibacteraceae; OC Candidatus Competibacter. OX NCBI_TaxID=1400863 {ECO:0000313|EMBL:CDI01701.1, ECO:0000313|Proteomes:UP000035760}; RN [1] {ECO:0000313|EMBL:CDI01701.1, ECO:0000313|Proteomes:UP000035760} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Run_A_D11 {ECO:0000313|EMBL:CDI01701.1, RC ECO:0000313|Proteomes:UP000035760}; RA McIlroy S.; RL Submitted (JUL-2013) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:CDI01701.1, ECO:0000313|Proteomes:UP000035760} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Run_A_D11 {ECO:0000313|EMBL:CDI01701.1, RC ECO:0000313|Proteomes:UP000035760}; RA McIlroy S.J., Albertsen M., Andresen E.K., Saunders A.M., RA Kristiansen R., Stokholm-Bjerregaard M., Nielsen K.L., Nielsen P.H.; RT "Candidatus Competibacter-lineage genomes retrieved from metagenomes RT reveal functional metabolic diversity."; RL Submitted (FEB-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:CDI01701.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CBTJ020000025; CDI01701.1; -; Genomic_DNA. DR Proteomes; UP000035760; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000035760}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Hydrolase {ECO:0000313|EMBL:CDI01701.1}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Protease {ECO:0000313|EMBL:CDI01701.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000035760}. FT DOMAIN 206 372 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 441 AA; 49102 MW; B89D83E196D19296 CRC64; MTQFAEDGLF ERPRGGERAV LVHVQLEAFA GEQDFSEFRE LAMSAGAECM ALITGRRQAP DPRLFVGSGK AEEIREAVRQ NAADLAIFDH TLTPGQERNL EAFLQCRVVD RTRLILDIFA QRARSFEGKL QVELAQLRHL STRLVRGWTH LERQRGGIGL RGPGETQLET DRRLLADRIR QIRLRLEHVD RQREQGRRAR RKADLATVSV VGYTNAGKST LFNALTQAGV YAADQLFATL DPTLRRLDLP GMEPAILADT VGFISDLPHE LVAAFRATLR ETCEANLLLH VIDASHHDRE AVIAQVEGVL TEIGADAVPC LQVFNKIDLT GEPPRLERDA QGQVRAVWLS AIRGAGMDLL AVAIAERLRG EGVYGWLCLP VTAARLRARL FGLGAVLGEH TDADGQWLIE VRMSRGNVEL LRRRYGLRPE WVRSGFDVPA V // ID W6N7C4_CLOTY Unreviewed; 419 AA. AC W6N7C4; DT 16-APR-2014, integrated into UniProtKB/TrEMBL. DT 16-APR-2014, sequence version 1. DT 07-JUN-2017, entry version 25. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=CTDIVETGP_2451 {ECO:0000313|EMBL:CDL92381.1}; OS Clostridium tyrobutyricum DIVETGP. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=1408889 {ECO:0000313|EMBL:CDL92381.1, ECO:0000313|Proteomes:UP000019482}; RN [1] {ECO:0000313|EMBL:CDL92381.1, ECO:0000313|Proteomes:UP000019482} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DIVETGP {ECO:0000313|EMBL:CDL92381.1, RC ECO:0000313|Proteomes:UP000019482}; RA Soggiu A., Piras C., Gaiarsa S., Sassera D., Roncada P., Bendixen E., RA Brasca M., Bonizzi L.; RT "Draft Genome Sequence of Clostridium tyrobutyricum Strain DIVETGP, RT Isolated from Cow's Milk for Grana Padano Production."; RL Genome Announc. 3:213-215(2015). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:CDL92381.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CBXI010000043; CDL92381.1; -; Genomic_DNA. DR RefSeq; WP_017895437.1; NZ_CBXI010000043.1. DR EnsemblBacteria; CDL92381; CDL92381; CTDIVETGP_2451. DR Proteomes; UP000019482; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000019482}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000019482}. FT DOMAIN 197 365 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 156 190 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 419 AA; 48092 MW; 87581F826F91C125 CRC64; MEDREKAIIA GVELSNQDDF ENLMEELYNL ADACNIEVID RITQRLDKIN SSQYFGKGKV EELQKLVDEK NVDMVIFDDE LTPSQIRNLE KAIDCKIIDR TSVILDIFAK RARTREAQLQ VEIAKLQYML PRLIGFGESM DRQGGGSGLY NRGSGETKLE LDRRKIEDRI SKLDKELETL VTQRQNQRKR RKKEGIPVIS LVGYTNAGKS TIMNLFIDLF NPSMEKKVFE KNMLFATLET SVRRIDLPDN KAFLLTDTVG FISKLPHYLI KAFRSTLEEV SEADMLVHVV DYSNVNYEKQ IAVTKNTLKE LGAENIPVIY CYNKIDLKDS EIPEQSEGKK YISARKKQGM DKLIDAIIKK VFGEYVNCNM LIPYDRGDIV SYLNDNANIK STDYKNEGIS IAVECSKVDY EKYKKYATQ // ID W6SHK6_9CLOT Unreviewed; 595 AA. AC W6SHK6; DT 16-APR-2014, integrated into UniProtKB/TrEMBL. DT 16-APR-2014, sequence version 1. DT 07-JUN-2017, entry version 23. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=CM240_2027 {ECO:0000313|EMBL:CDM69185.1}; OS Clostridium bornimense. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=1216932 {ECO:0000313|EMBL:CDM69185.1, ECO:0000313|Proteomes:UP000019426}; RN [1] {ECO:0000313|EMBL:CDM69185.1, ECO:0000313|Proteomes:UP000019426} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=M2/40 {ECO:0000313|Proteomes:UP000019426}; RA Wibberg D., Puehler A., Schlueter A.; RT "Complete genome sequence of Clostridum sp. M2/40."; RL Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; HG917868; CDM69185.1; -; Genomic_DNA. DR RefSeq; WP_044038925.1; NZ_HG917868.1. DR EnsemblBacteria; CDM69185; CDM69185; CM240_2027. DR KEGG; clt:CM240_2027; -. DR PATRIC; fig|1216932.3.peg.2027; -. DR KO; K03665; -. DR Proteomes; UP000019426; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000019426}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000019426}. FT DOMAIN 364 541 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 323 357 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 595 AA; 67030 MW; AF215CF444D07B5A CRC64; MIYGNLEGIK NSYINELEEL YNIKVPKKEF ITEEIISVMC KITELINREV SISINRKGDI LGISVGNAES VELPVIDIKE KSLSGVRVVH THPSGNSHLS VIDISALLKL KLDVMAAIGV KDGKAKDISL GFCGVYENNL VVEKKYNNTI EEILRFDYLD KVHYIEETLK SSEIKEVEEE KAILVSTDSE EMLDELEELA FACNVTVVYK VLQKKSKIEA ATFIGSGKAE EISLLRQVYD ANVIIFDDEL SGAQVKNLES IIGAKVIDRT TLILDIFARR AKTREAKIQV ELAQLKYRSA RLLGLGVVMS RTGAGIGTRG PGEKKLEIDK RKIRENIHDL NKELEKIRKN RSVQREKRNK ANMPKISLVG YTNAGKSTLR NLLAIKYAKD STLNKENVFA ENMLFATLDV TTRAIELKDR RIAALTDTVG FVRKLPHDLV AAFKSTLEEV TYSDLLLHVV DGSSDAVFEQ IKAVEEVLVE LNANDKPQIL VINKIDIIDE DQVSKLEEKF NYLPIVKISA KNEINIENLM EKITEVIPST MRKVEYLIPY TDSSAVSYIH RTSIVEEEEY LEDGTRIVAT VDEEVFNKTT NYIKK // ID W6TAQ5_9LACO Unreviewed; 428 AA. AC W6TAQ5; DT 16-APR-2014, integrated into UniProtKB/TrEMBL. DT 16-APR-2014, sequence version 1. DT 07-JUN-2017, entry version 23. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=LFAB_03935 {ECO:0000313|EMBL:ETY75053.1}; OS Lactobacillus fabifermentans T30PCM01. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; OC Lactobacillus. OX NCBI_TaxID=1400520 {ECO:0000313|EMBL:ETY75053.1, ECO:0000313|Proteomes:UP000019247}; RN [1] {ECO:0000313|EMBL:ETY75053.1, ECO:0000313|Proteomes:UP000019247} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=T30PCM01 {ECO:0000313|EMBL:ETY75053.1, RC ECO:0000313|Proteomes:UP000019247}; RX PubMed=24558238; RA Treu L., Vendramin V., Bovo B., Giacomini A., Corich V., Campanaro S.; RT "Genome Sequence of Lactobacillus fabifermentans Strain T30PCM01, RT Isolated from Fermenting Grape Marc."; RL Genome Announc. 2:e00060-14(2014). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:ETY75053.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AWWK01000020; ETY75053.1; -; Genomic_DNA. DR RefSeq; WP_024624860.1; NZ_KK036473.1. DR EnsemblBacteria; ETY75053; ETY75053; LFAB_03935. DR PATRIC; fig|1400520.3.peg.772; -. DR Proteomes; UP000019247; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000019247}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000019247}. FT DOMAIN 204 372 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 428 AA; 47615 MW; CA46D012BACBA4EA CRC64; MSEPIVQEVI IAGMSKTVAN YDYAMSELES LVEANNMHAA LRIDQGLEKP NPATYFGKGK VVEIKEMAEA NELNIMVINA DLTPSQVRNL ETETGLQIID RTGLILEIFG NRARSKEAKL QVKIAQLQYQ LPRLRTSISN RLDQQAGAAA GGGGGFTNRG AGETQLELNR RTIQDRISHA KHELKELNKD EEVRRAQRDK AGLPNVALVG YTNAGKSTTM NGLVKLFGKG EDKQVFEKDM LFATLDTSIR QLTFPDNKQL LLSDTVGFVS DLPHNLINAF RSTLSEAASA DLLIQVIDYA DPHYKEMMDT TEKTLKEIGV TDVPMLYAYN KADLTEASYP SQQDDQLIYA ARDEKSLQVL TKMIKDKVFK DYVKTTLLIP FSDGDVVAYL NDHANILKTD YLADGTQLEV ELNAVDAQRY EKYVVTPA // ID W6TJS5_9SPHI Unreviewed; 396 AA. AC W6TJS5; DT 16-APR-2014, integrated into UniProtKB/TrEMBL. DT 16-APR-2014, sequence version 1. DT 07-JUN-2017, entry version 22. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=N824_12200 {ECO:0000313|EMBL:ETZ19497.1}; OS Pedobacter sp. V48. OC Bacteria; Bacteroidetes; Sphingobacteriia; Sphingobacteriales; OC Sphingobacteriaceae; Pedobacter. OX NCBI_TaxID=509635 {ECO:0000313|EMBL:ETZ19497.1, ECO:0000313|Proteomes:UP000019145}; RN [1] {ECO:0000313|EMBL:ETZ19497.1, ECO:0000313|Proteomes:UP000019145} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=V48 {ECO:0000313|EMBL:ETZ19497.1, RC ECO:0000313|Proteomes:UP000019145}; RX PubMed=24578271; RA Bitzer A.S., Garbeva P., Silby M.W.; RT "Draft Genome Sequence of Pedobacter sp. Strain V48, Isolated from a RT Coastal Sand Dune in the Netherlands."; RL Genome Announc. 2:e00094-14(2014). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:ETZ19497.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AWRU01000034; ETZ19497.1; -; Genomic_DNA. DR RefSeq; WP_048908268.1; NZ_AWRU01000034.1. DR EnsemblBacteria; ETZ19497; ETZ19497; N824_12200. DR PATRIC; fig|509635.5.peg.5425; -. DR Proteomes; UP000019145; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000019145}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000019145}. FT DOMAIN 204 385 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 396 AA; 45529 MW; 49BDA2DC16860E16 CRC64; MGKQKYYDTA LKPERAVLVG VIRPGEKPEE TREYLDELAF LVDTAGGVVE HEFTQKMLKP DRGTFVGTGK LEEIQAYVKS EEIDMVVFDD ELSPSQLRNI ERELQVKILD RSNLILDIFA SRAQTAQAKT QVELAQLQYL LPRLTRLWTH LERQKGGIGM RGPGETQIES DRRMILEKIA LLKSRLSQID RQNETQRKNR GQLIRVALVG YTNVGKSTIM NMLSKSEVFA ENKLFATLDT TVRKVVIENL PFLLSDTVGF IRKLPHHLVE CFKSTLDEVR EADVLIHVVD VSHANFEDQI NVVNETLKDL GARDKETIMV FNKMDAYVSP EPDHEDEERA VLTLDDFKRS WMANHNAPSI FISALHKENL EEFKQLLYDK VVALHTERYP YDKLLY // ID W6VVY0_9RHIZ Unreviewed; 446 AA. AC W6VVY0; DT 16-APR-2014, integrated into UniProtKB/TrEMBL. DT 16-APR-2014, sequence version 1. DT 07-JUN-2017, entry version 21. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=PMI07_002278 {ECO:0000313|EMBL:EUB95790.1}; OS Rhizobium sp. CF080. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium. OX NCBI_TaxID=1144310 {ECO:0000313|EMBL:EUB95790.1, ECO:0000313|Proteomes:UP000007505}; RN [1] {ECO:0000313|EMBL:EUB95790.1, ECO:0000313|Proteomes:UP000007505} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CF080 {ECO:0000313|EMBL:EUB95790.1, RC ECO:0000313|Proteomes:UP000007505}; RA Brown S.D., Utturkar S.M., Klingeman D.M., Johnson C.M., Martin S.L., RA Land M.L., Lu T.-Y., Schadt C.W., Pelletier D.A., Doktycz M.J.; RT "Sequencing of Twenty One Pseudomonas Genomes and Twenty Two Genomes RT from Diverse Bacteria Isolated from Populus deltoides Endosphere RT Communities."; RL Submitted (JUL-2013) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EUB95790.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AKKC02000015; EUB95790.1; -; Genomic_DNA. DR RefSeq; WP_007757454.1; NZ_AKKC02000015.1. DR EnsemblBacteria; EUB95790; EUB95790; PMI07_002278. DR Proteomes; UP000007505; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000007505}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000007505}. FT DOMAIN 208 380 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 167 201 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 446 AA; 49147 MW; E6287F4E6B0A7243 CRC64; MRALVIVPVL KQGRSKAGQG DSSPAPAPQR SNEARLEEAI GLAKAIDLEI VQGLIVPISQ PRPGTLMGTG KIEEIKALLD EHDAGLVIVD HPLTPVQQRN LEKEWNAKVI DRTGLILEIF GRRASTKEGT LQVDLAHLNY QKGRLVRSWT HLERQRGGAG FMGGPGETQI EADRRLLQER IVKLERELEQ VVRTRQLHRA KRRKVPHPIV ALVGYTNAGK STLFNRITGA GVLAEDMLFA TLDPTLRRMK LPHGRTVILS DTVGFISNLP THLVAAFRAT LEEVLEADLV LHVRDMSDPD NAAQAGDVMR ILSDLGIDEK EAAKRIIEVW NKIDRLDPDA HEAIAERAVG RENVMAVSAI SGEGVDALMD EISRRLSGVL TETSIIIPAD QLSILSWVYS NAVVDGREDN EDGSVTLDVR MSEAEAAEFE RKLGNGPKAT KEDWER // ID W6ZXT2_9APIC Unreviewed; 699 AA. AC W6ZXT2; DT 16-APR-2014, integrated into UniProtKB/TrEMBL. DT 16-APR-2014, sequence version 1. DT 07-JUN-2017, entry version 16. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EUD65592.1}; GN ORFNames=C922_04098 {ECO:0000313|EMBL:EUD65592.1}; OS Plasmodium inui San Antonio 1. OC Eukaryota; Alveolata; Apicomplexa; Aconoidasida; Haemosporida; OC Plasmodiidae; Plasmodium; Plasmodium (Plasmodium). OX NCBI_TaxID=1237626 {ECO:0000313|EMBL:EUD65592.1, ECO:0000313|Proteomes:UP000030640}; RN [1] {ECO:0000313|EMBL:EUD65592.1, ECO:0000313|Proteomes:UP000030640} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=San Antonio 1 {ECO:0000313|EMBL:EUD65592.1, RC ECO:0000313|Proteomes:UP000030640}; RG The Broad Institute Genome Sequencing Platform; RG The Broad Institute Genome Sequencing Center for Infectious Disease; RA Neafsey D., Cheeseman I., Volkman S., Adams J., Walker B., Young S.K., RA Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., RA Alvarado L., Arachchi H.M., Berlin A.M., Chapman S.B., Dewar J., RA Goldberg J., Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., RA Larimer J., McCowan C., Murphy C., Neiman D., Pearson M., Priest M., RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., RA Nusbaum C., Birren B.; RT "The Genome Sequence of Plasmodium inui San Antonio 1."; RL Submitted (FEB-2013) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; KI965478; EUD65592.1; -; Genomic_DNA. DR RefSeq; XP_008817905.1; XM_008819683.1. DR EnsemblProtists; EUD65592; EUD65592; C922_04098. DR GeneID; 20039372; -. DR EuPathDB; PlasmoDB:C922_04098; -. DR Proteomes; UP000030640; Unassembled WGS sequence. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR CDD; cd01878; HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 4: Predicted; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000030640}; KW Reference proteome {ECO:0000313|Proteomes:UP000030640}. FT DOMAIN 457 627 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 425 452 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 699 AA; 80046 MW; E2F4012B78A1A370 CRC64; MLRWSTTLRT FPRTQKRSFT NGRKKEIIVL HPTLKKTKNG SKSFNEIIYE AQEALGLARS AGFKVANGIS MPLGGWTFFK HPSGSKEEGE GEDLANRYRE EDTFRGTRHS NGETPCGGDT NEAEKCHTNE YAGEDEGAEA ETDAPSEEVP PQGDDLEKKI AESIIMKTNR IDNKFYFGKG KLNELSTYFL KHPTPYVFIN TLLSPEQFRN LDMLFNSLLR SHHDELKLSR EKERGEDCLS VRASEFSAED YGGAEHARGE ELAYVEMYNQ WMERQAEQED QEDGSVSEGE EHAALGEAEE ERVVSRDDAE NSNVPLYVEL FDRYSIILQI LKSRAKSNLS KLQLELARAN FIFNTYAEDN KSRMKYIKYI ENNVLGKSNF DYEEKHSRQN TFHVDRQMGK NKNYDHLGYT SSYIKSSETY KEYEKRIIQN LYAKLKKELA KCKNNNALQR SARKHKALIA VVGYTNVGKT KLINYLTKSN LKARNLLFQT LDNAFKSVKI SDGHSSIFID SIGFIQNIPF SLYESFKVTL EAIKNADILI HVIDVCHPYR EQHKKCVIDT LQKIGIPSDF LKCNMIEVWN KVDKLADEEL LHLYKTKPKN VLPISAKVGT NCDVLIKIIQ TMINRIRDVQ VLTLQFPTME AQERMPYLVK NFKVVPNSIS YSSDGNTTFI KLVENPRNLS KYYHRFNKGE KGPSAGGSK // ID W7BAA9_9LIST Unreviewed; 419 AA. AC W7BAA9; DT 16-APR-2014, integrated into UniProtKB/TrEMBL. DT 16-APR-2014, sequence version 1. DT 07-JUN-2017, entry version 25. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=MAQA_02822 {ECO:0000313|EMBL:EUJ21610.1}; OS Listeria aquatica FSL S10-1188. OC Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria. OX NCBI_TaxID=1265818 {ECO:0000313|EMBL:EUJ21610.1, ECO:0000313|Proteomes:UP000019246}; RN [1] {ECO:0000313|EMBL:EUJ21610.1, ECO:0000313|Proteomes:UP000019246} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=FSL S10-1188 {ECO:0000313|EMBL:EUJ21610.1, RC ECO:0000313|Proteomes:UP000019246}; RX PubMed=24599893; DOI=10.1099/ijs.0.052720-0; RA den Bakker H.C., Warchocki S., Wright E.M., Allred A.F., Ahlstrom C., RA Manuel C.S., Stasiewicz M.J., Burrell A., Roof S., Strawn L., RA Fortes E.D., Nightingale K.K., Kephart D., Wiedmann M.; RT "Listeria floridensis sp. nov., Listeria aquatica sp. nov., Listeria RT cornellensis sp. nov., Listeria riparia sp. nov. and Listeria RT grandensis sp. nov., from agricultural and natural environments."; RL Int. J. Syst. Evol. Microbiol. 64:1882-1889(2014). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EUJ21610.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AOCG01000002; EUJ21610.1; -; Genomic_DNA. DR RefSeq; WP_036070903.1; NZ_AOCG01000002.1. DR EnsemblBacteria; EUJ21610; EUJ21610; MAQA_02822. DR PATRIC; fig|1265818.5.peg.574; -. DR Proteomes; UP000019246; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000019246}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000019246}. FT DOMAIN 194 363 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 419 AA; 47418 MW; 99207FEA5BF47D11 CRC64; MSKKVILVGV SGSEKDFDYT MLELRNLAEA NHYQVVDEVR QNLDSAHKAT YVGKGKLEEL KQLGEMQEAK AFVLNDELTG SQIRNLEDAT GFQIIDRTAL ILSIFAERAK TREAQLQVEI ARLKYELPRM IGEGESLDQQ GGGSGLRNRG SGEKKLEQDR RIIKDRISKL TKELDAIVAE RETRRRKRKK NEIPVVSLVG YTNAGKSTTM NGLVADFSTS EHKQVFEKDM LFATLETSVR EIVLPDHKRF LLTDTVGFVS KLPTHLVKAF RSTLEEARDA DLLIHVVDYS DPNYQTMIET TECTLKEVGV EGIPVLFAYN KADKIAEENY PVLAGDTLVY SARDEASLFE LAETVKKRIF TGYKKVTLLI PFEEGQVVAY LNDKANVLSE EYLNEGTKVE VELSPVDQER LKKFRWRVS // ID W7BHU4_9LIST Unreviewed; 423 AA. AC W7BHU4; DT 16-APR-2014, integrated into UniProtKB/TrEMBL. DT 16-APR-2014, sequence version 1. DT 07-JUN-2017, entry version 27. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=PCORN_14279 {ECO:0000313|EMBL:EUJ26689.1}; OS Listeria cornellensis FSL F6-0969. OC Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria. OX NCBI_TaxID=1265820 {ECO:0000313|EMBL:EUJ26689.1, ECO:0000313|Proteomes:UP000019254}; RN [1] {ECO:0000313|EMBL:EUJ26689.1, ECO:0000313|Proteomes:UP000019254} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=FSL F6-969 {ECO:0000313|Proteomes:UP000019254}; RX PubMed=24599893; DOI=10.1099/ijs.0.052720-0; RA den Bakker H.C., Warchocki S., Wright E.M., Allred A.F., Ahlstrom C., RA Manuel C.S., Stasiewicz M.J., Burrell A., Roof S., Strawn L., RA Fortes E.D., Nightingale K.K., Kephart D., Wiedmann M.; RT "Listeria floridensis sp. nov., Listeria aquatica sp. nov., Listeria RT cornellensis sp. nov., Listeria riparia sp. nov. and Listeria RT grandensis sp. nov., from agricultural and natural environments."; RL Int. J. Syst. Evol. Microbiol. 64:1882-1889(2014). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EUJ26689.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AODE01000029; EUJ26689.1; -; Genomic_DNA. DR RefSeq; WP_036081047.1; NZ_AODE01000029.1. DR EnsemblBacteria; EUJ26689; EUJ26689; PCORN_14279. DR PATRIC; fig|1265820.5.peg.2820; -. DR Proteomes; UP000019254; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000019254}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000019254}. FT DOMAIN 194 363 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 153 187 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 423 AA; 47901 MW; E7C383CEB815A6D9 CRC64; MTRTAILVGI TMQQADFEYS MAELANLAEA NAIEPVGEIT QKLDRKNKAT YVGKGKVDEI KSLADYEDVD LVIFNDELAP SQIRNLEELL EIEVMDRTRL ILDIFAERAK TREAQLQVQV ARLKYELPRV VGQGEGMDQQ SGKGGLKNRG AGETKLEMDR RRIKNQISQL NKELDGLVAE RQVQRRQRQK NEIPVVSLVG YTNAGKSTIM NAMVTAHSQT ANKQVFEKDM LFATLETSVR EIVLPDKKQF LLTDTVGFVS KLPHNLVKAF RSTLEEAAEA DVLIHVVDVS HEHFEAMIKT TEETLAELDI TDRPLIFAYN KADLATNVMF PRREGDSLYL SAREDTGLEL LIDMIKEQVF NDYKTVTFVI PFDRGDVVSY LNEHADVLET AYENEGTVLR VNAQESDRMK YAEFISEDTQ KES // ID W7C121_9LIST Unreviewed; 403 AA. AC W7C121; DT 16-APR-2014, integrated into UniProtKB/TrEMBL. DT 16-APR-2014, sequence version 1. DT 07-JUN-2017, entry version 24. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=PCORN_07880 {ECO:0000313|EMBL:EUJ30917.1}; OS Listeria cornellensis FSL F6-0969. OC Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria. OX NCBI_TaxID=1265820 {ECO:0000313|EMBL:EUJ30917.1, ECO:0000313|Proteomes:UP000019254}; RN [1] {ECO:0000313|EMBL:EUJ30917.1, ECO:0000313|Proteomes:UP000019254} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=FSL F6-969 {ECO:0000313|Proteomes:UP000019254}; RX PubMed=24599893; DOI=10.1099/ijs.0.052720-0; RA den Bakker H.C., Warchocki S., Wright E.M., Allred A.F., Ahlstrom C., RA Manuel C.S., Stasiewicz M.J., Burrell A., Roof S., Strawn L., RA Fortes E.D., Nightingale K.K., Kephart D., Wiedmann M.; RT "Listeria floridensis sp. nov., Listeria aquatica sp. nov., Listeria RT cornellensis sp. nov., Listeria riparia sp. nov. and Listeria RT grandensis sp. nov., from agricultural and natural environments."; RL Int. J. Syst. Evol. Microbiol. 64:1882-1889(2014). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EUJ30917.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AODE01000014; EUJ30917.1; -; Genomic_DNA. DR EnsemblBacteria; EUJ30917; EUJ30917; PCORN_07880. DR PATRIC; fig|1265820.5.peg.1543; -. DR Proteomes; UP000019254; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000019254}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000019254}. FT DOMAIN 195 356 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 403 AA; 45964 MW; 1A29F3E08861417E CRC64; MVERAILVGC ELPKQTEEHF YYSMLELGSL AKTAQAEVVG EVTQKRERIH PATFVGSGKI EEIAAFVAEM EVDVVLFNSE LSATQVRNIS NIVDARILDR TQLILDIFAM RAKTREGKLQ VALAQYQYLL PRLSGQGVSL SRLGGGIGTR GPGETKLEMD RRHIRQKMVD IKKQLDIVVK HRERMTARRN DQAIFRFGLI GYTNAGKSTL FNRLSDAKTL EEDQLFATLD PTTRKLAFSQ GYTALLTDTV GFIQDLPTTV VAAFRSTLEE TANVDVLLHV VDCSNPDYIQ HEKTVLTLLE ELEMQHIPIL TVYNKKDQQL PYFIPTQPNY VEVSALEESS QYFLMEKMLW EIKQLWQPYV ACVPASDGRM LHRYKQETVI IEETFDEETE SYQLKGYQAR KDK // ID W7C3V6_9LIST Unreviewed; 156 AA. AC W7C3V6; DT 16-APR-2014, integrated into UniProtKB/TrEMBL. DT 16-APR-2014, sequence version 1. DT 07-JUN-2017, entry version 13. DE SubName: Full=Putative GTP-binding protein HflX {ECO:0000313|EMBL:EUJ30316.1}; GN ORFNames=MFLO_10853 {ECO:0000313|EMBL:EUJ30316.1}; OS Listeria floridensis FSL S10-1187. OC Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria. OX NCBI_TaxID=1265817 {ECO:0000313|EMBL:EUJ30316.1, ECO:0000313|Proteomes:UP000019249}; RN [1] {ECO:0000313|EMBL:EUJ30316.1, ECO:0000313|Proteomes:UP000019249} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=FSL S10-1187 {ECO:0000313|EMBL:EUJ30316.1, RC ECO:0000313|Proteomes:UP000019249}; RX PubMed=24599893; DOI=10.1099/ijs.0.052720-0; RA den Bakker H.C., Warchocki S., Wright E.M., Allred A.F., Ahlstrom C., RA Manuel C.S., Stasiewicz M.J., Burrell A., Roof S., Strawn L., RA Fortes E.D., Nightingale K.K., Kephart D., Wiedmann M.; RT "Listeria floridensis sp. nov., Listeria aquatica sp. nov., Listeria RT cornellensis sp. nov., Listeria riparia sp. nov. and Listeria RT grandensis sp. nov., from agricultural and natural environments."; RL Int. J. Syst. Evol. Microbiol. 64:1882-1889(2014). CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EUJ30316.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AODF01000024; EUJ30316.1; -; Genomic_DNA. DR EnsemblBacteria; EUJ30316; EUJ30316; MFLO_10853. DR PATRIC; fig|1265817.5.peg.2186; -. DR Proteomes; UP000019249; Unassembled WGS sequence. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000019249}; KW Reference proteome {ECO:0000313|Proteomes:UP000019249}. FT DOMAIN 19 106 GTP-bdg_N. {ECO:0000259|Pfam:PF13167}. FT DOMAIN 108 155 GTP-bdg_M. {ECO:0000259|Pfam:PF16360}. SQ SEQUENCE 156 AA; 17441 MW; B96CE37ECE487695 CRC64; MERKVILVGV SGSDKDFDYS MIELFNLAKA NNYDVVDEVR QNLETAHKAT YVGKGKVEEL KQLAEMQDAE AFVINDELTA SQIRNLEEAT ERMVIDRTAL ILSIFADRAK TREAQLQVQI AMLQYELPRM IGEGESLDQQ GGGSGLRNRG SGEKKT // ID W7CKK0_9LIST Unreviewed; 418 AA. AC W7CKK0; DT 16-APR-2014, integrated into UniProtKB/TrEMBL. DT 16-APR-2014, sequence version 1. DT 07-JUN-2017, entry version 23. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=BCAMP_05955 {ECO:0000313|EMBL:EUJ39969.1}; OS Brochothrix campestris FSL F6-1037. OC Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Brochothrix. OX NCBI_TaxID=1265861 {ECO:0000313|EMBL:EUJ39969.1, ECO:0000313|Proteomes:UP000019243}; RN [1] {ECO:0000313|EMBL:EUJ39969.1, ECO:0000313|Proteomes:UP000019243} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=FSL F6-1037 {ECO:0000313|EMBL:EUJ39969.1, RC ECO:0000313|Proteomes:UP000019243}; RA den Bakker H.C., Allred A., Warchocki S., Wright E.M., Burrell A., RA Nightingale K.K., Kephart D., Wiedmann M.; RT "Novel taxa of Listeriaceae from agricultural environments in the RT United States."; RL Submitted (DEC-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EUJ39969.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AODH01000022; EUJ39969.1; -; Genomic_DNA. DR RefSeq; WP_051456909.1; NZ_AODH01000022.1. DR EnsemblBacteria; EUJ39969; EUJ39969; BCAMP_05955. DR PATRIC; fig|1265861.3.peg.1178; -. DR Proteomes; UP000019243; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000019243}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000019243}. FT DOMAIN 195 364 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 161 188 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 418 AA; 46599 MW; BE637F588F795135 CRC64; MTNVILVGVE LPRVNDFAES MVELEGLAEA AGLTVGHVLT QKRERVHAGT YIGKGKLAEL EGYLAAAQSE TLVFNDELTP SQIKNLEAAL EVEIIDRTML ILAIFADRAQ TREAKLQVEV ARLQYLMPRL AGMGISMSRQ GGGSSGLANR GAGETKLELD RRTISDKINQ YQRELKIVAN ERDNQRRSRQ KKGLRVAALV GYTNAGKSSI LNTLVSAYHP QTDEKHVLEK DMLFATLETS VRRIHPKYHQ PFLLTDTVGF VDKLPTQLVK AFRSTLEEVI QADVLIHVID AASPDADKRQ RVTEETLKAI GVEDKPMIHV WNKADLVPEV SQIMPPNHVW VSTRTGLGLP ALMAAIEAEL FADEEEHSWL IPYDRGDVVA QMNEEARIIK LEYVEDGTQI TAITPQHFIR THGEFITE // ID W7CND4_BROTH Unreviewed; 418 AA. AC W7CND4; DT 16-APR-2014, integrated into UniProtKB/TrEMBL. DT 16-APR-2014, sequence version 1. DT 07-JUN-2017, entry version 25. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=BFR34_00695 {ECO:0000313|EMBL:ODJ51512.1}, GN BTHER_11563 {ECO:0000313|EMBL:EUJ34633.1}; OS Brochothrix thermosphacta DSM 20171 = FSL F6-1036. OC Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Brochothrix. OX NCBI_TaxID=1121126 {ECO:0000313|EMBL:EUJ34633.1, ECO:0000313|Proteomes:UP000019242}; RN [1] {ECO:0000313|EMBL:EUJ34633.1, ECO:0000313|Proteomes:UP000019242} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=FSL F6-1036 {ECO:0000313|EMBL:EUJ34633.1, RC ECO:0000313|Proteomes:UP000019242}; RA den Bakker H.C., Allred A., Warchocki S., Wright E.M., Burrell A., RA Nightingale K.K., Kephart D., Wiedmann M.; RT "Novel taxa of Listeriaceae from agricultural environments in the RT United States."; RL Submitted (DEC-2012) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:ODJ51512.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 20171 {ECO:0000313|EMBL:ODJ51512.1}; RA Seilhamer J.J.; RL Submitted (AUG-2016) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EUJ34633.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AODI01000031; EUJ34633.1; -; Genomic_DNA. DR EMBL; MDLK01000018; ODJ51512.1; -; Genomic_DNA. DR RefSeq; WP_036027485.1; NZ_MDLK01000018.1. DR EnsemblBacteria; EUJ34633; EUJ34633; BTHER_11563. DR GeneID; 29820326; -. DR PATRIC; fig|1121126.4.peg.2279; -. DR Proteomes; UP000019242; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000019242}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000019242}. FT DOMAIN 195 364 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 161 188 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 418 AA; 46960 MW; FA0083597C16C9CA CRC64; MTNVVLVGVE LPRVNDFAES MIELHGLAEA ADLNVTHVLT QKRERVHAGT YLGKGKLAEL QGYLEGTESE AIIVNDELTP SQIKNLEAVL ECEIMDRTML ILAIFAERAQ TREAKLQVEV ARLQYLMPRL AGMGISMSRQ GGGSSGLANR GAGETKLELD RRTISDKINQ YQRELKVVAN ERDNQRRSRQ KKGLRVAALV GYTNAGKSSI MNTLVSSYHP QTTEKQVLEK DMLFATLDTS VRRIHPKYHQ PFLLTDTVGF VDKLPTQLVK AFRSTLEEVV QADVLIHVID ASSPDSEKRQ RVTEETLKAI GAEDKPMIYV WNKADLVPEV SQIMPKNHLW VSTYTGKGIS ELMSAVEAEL FADEEQHVWL VPYDRGDVVA LMNEEARIIE LEYVEEGTQI TAITPQHFIR NYGEFIVK // ID W7DL71_9LIST Unreviewed; 423 AA. AC W7DL71; DT 16-APR-2014, integrated into UniProtKB/TrEMBL. DT 16-APR-2014, sequence version 1. DT 07-JUN-2017, entry version 24. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=PROCOU_06363 {ECO:0000313|EMBL:EUJ48102.1}; OS Listeria rocourtiae FSL F6-920. OC Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria. OX NCBI_TaxID=1265846 {ECO:0000313|EMBL:EUJ48102.1, ECO:0000313|Proteomes:UP000019244}; RN [1] {ECO:0000313|EMBL:EUJ48102.1, ECO:0000313|Proteomes:UP000019244} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=FSL F6-920 {ECO:0000313|EMBL:EUJ48102.1, RC ECO:0000313|Proteomes:UP000019244}; RA den Bakker H.C., Allred A., Warchocki S., Wright E.M., Burrell A., RA Nightingale K.K., Kephart D., Wiedmann M.; RT "Novel taxa of Listeriaceae from agricultural environments in the RT United States."; RL Submitted (DEC-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EUJ48102.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AODK01000013; EUJ48102.1; -; Genomic_DNA. DR RefSeq; WP_036070262.1; NZ_AODK01000013.1. DR EnsemblBacteria; EUJ48102; EUJ48102; PROCOU_06363. DR PATRIC; fig|1265846.4.peg.1258; -. DR Proteomes; UP000019244; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000019244}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000019244}. FT DOMAIN 194 363 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 153 187 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 423 AA; 47728 MW; 5D4F9D5F3C6CFE4A CRC64; MIRTAILVGI TMQQADFEYS MAELGNLAEA NAIKPVGEIT QKLDRKNKAT YVGKGKVDEI KGLAEHEDVD VVIFNDELAP SQIRNLEELL EIEVMDRTRL ILDIFAERAK TREAQLQVQV ARLKYELPRI VGQGEGMDQQ SGKGGLKNRG AGETKLEMDR RRIKSQISQL NKELDGLVAE RQVQRRQRQK NEIPVVSLVG YTNAGKSTIM NAMVTAHSQT ANKQVFEKDM LFATLETSVR EIVLPDKKQF LLTDTVGFVS KLPHNLVKAF RSTLEEAAEA DLLIHVVDVS HEHFEAMIKT TEETLAELDI TDRPLIFVYN KADLATNVVF PRREGDSIYL SAKEDAGLEL LIEIIKEQVF NDYKTVTFVI PFNRGDIVSY LNEHADVLET AYENEGTVLQ VNAQESDRMK FAEFITDDIQ KEG // ID W7DNL1_9LIST Unreviewed; 403 AA. AC W7DNL1; DT 16-APR-2014, integrated into UniProtKB/TrEMBL. DT 16-APR-2014, sequence version 1. DT 07-JUN-2017, entry version 20. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=PROCOU_03339 {ECO:0000313|EMBL:EUJ51100.1}; OS Listeria rocourtiae FSL F6-920. OC Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria. OX NCBI_TaxID=1265846 {ECO:0000313|EMBL:EUJ51100.1, ECO:0000313|Proteomes:UP000019244}; RN [1] {ECO:0000313|EMBL:EUJ51100.1, ECO:0000313|Proteomes:UP000019244} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=FSL F6-920 {ECO:0000313|EMBL:EUJ51100.1, RC ECO:0000313|Proteomes:UP000019244}; RA den Bakker H.C., Allred A., Warchocki S., Wright E.M., Burrell A., RA Nightingale K.K., Kephart D., Wiedmann M.; RT "Novel taxa of Listeriaceae from agricultural environments in the RT United States."; RL Submitted (DEC-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EUJ51100.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AODK01000006; EUJ51100.1; -; Genomic_DNA. DR EnsemblBacteria; EUJ51100; EUJ51100; PROCOU_03339. DR PATRIC; fig|1265846.4.peg.666; -. DR Proteomes; UP000019244; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000019244}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000019244}. FT DOMAIN 195 317 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 403 AA; 46053 MW; 21EC21D7D7957296 CRC64; MVERAILVGC ELPKQTEEHF YYSMLELGSL AKTAQAEVVG EVTQKRERVH PATFVGSGKI EEIAAFVAEM EVDIVLFNSE LSATQVRNIS KIVDARILDR TQLILDIFAM RAKTREGKLQ VAFAQYQYLL PRLSGQGASL SRLGGGIGTR GPGETKLEMD RRHIRQKMVD IKEQLDTVVK HRERMTARRN DQAIFRFGLI GYTNAGKSTL FNRLSDAKTL EENQLFATLD PTTRKLVFSE GYTALLTDTV GFIQDLPTTV IAAFRSTLEE TANVDVLLHV VDSSNPDYVQ HEKTVLKLLE ELDMQHIPIL TVYNKKDQQL PYFIPTQPNY VEVSALEEYS QYFLMEKMLW EIKQLWQPYV ASIPASDGRM LHKYKRETVV IEEIFDEKAE SYQLKGYQAR KEK // ID W7INE2_9PSEU Unreviewed; 483 AA. AC W7INE2; DT 16-APR-2014, integrated into UniProtKB/TrEMBL. DT 16-APR-2014, sequence version 1. DT 07-JUN-2017, entry version 22. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=UO65_6419 {ECO:0000313|EMBL:EWC58277.1}; OS Actinokineospora spheciospongiae. OC Bacteria; Actinobacteria; Pseudonocardiales; Pseudonocardiaceae; OC Actinokineospora. OX NCBI_TaxID=909613 {ECO:0000313|EMBL:EWC58277.1, ECO:0000313|Proteomes:UP000019277}; RN [1] {ECO:0000313|EMBL:EWC58277.1, ECO:0000313|Proteomes:UP000019277} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=EG49 {ECO:0000313|EMBL:EWC58277.1, RC ECO:0000313|Proteomes:UP000019277}; RX PubMed=24604655; RA Harjes J., Ryu T., Abdelmohsen U.R., Moitinho-Silva L., Horn H., RA Ravasi T., Hentschel U.; RT "Draft Genome Sequence of the Antitrypanosomally Active Sponge- RT Associated Bacterium Actinokineospora sp. Strain EG49."; RL Genome Announc. 2:e00160-14(2014). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EWC58277.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AYXG01000244; EWC58277.1; -; Genomic_DNA. DR EnsemblBacteria; EWC58277; EWC58277; UO65_6419. DR PATRIC; fig|909613.9.peg.6414; -. DR Proteomes; UP000019277; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 2. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000019277}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000019277}. FT DOMAIN 256 425 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 483 AA; 52573 MW; D2A2F2549EE43379 CRC64; MTEESIQRDI HGDGTGPAEL SLGELELEER SSLRRVVGLS TELEDITEVE YRQLRLERVV LVGVWTEGTA LESESSLAEL ARLAETAGSE VLDGLVQRRD RPDPATYIGS GKVTELADVV RATGADTVIC DGELSPSQLQ QLEARLKVKV VDRTALILDI FAQHARSREG KAQVELAQLQ YLLPRLRGWG ATLSRQAGGR AGGGNGGVGL RGPGETKIET DRRRIRNKIS KLRKDIKEMS AFRDTKRSRR VANDVPSVAI AGYTNAGKSS LLNALTGAGV LVEDALFATL DATTRRTETT EGNVYTLTDT VGFVRHLPHQ LVEAFRSTLD EVADADLVVH VVDGADPMPE WQVTAVREVL NDIGDRRDTR MPPELVVVNK VDASTEIALA RLRHLLPGAV FVSARTGQGI DELRERIAEL IPRPDVEVDV LVPYDRGEVV ARVHREGEVL GERHTETGTA LHAKVKPDLA GALERFAVNG SSA // ID W7JM15_PLAFA Unreviewed; 698 AA. AC W7JM15; DT 16-APR-2014, integrated into UniProtKB/TrEMBL. DT 16-APR-2014, sequence version 1. DT 10-MAY-2017, entry version 17. DE SubName: Full=GTP-binding protein HflX {ECO:0000313|EMBL:EWC76038.1}; GN ORFNames=C923_03322 {ECO:0000313|EMBL:EWC76038.1}; OS Plasmodium falciparum UGT5.1. OC Eukaryota; Alveolata; Apicomplexa; Aconoidasida; Haemosporida; OC Plasmodiidae; Plasmodium; Plasmodium (Laverania). OX NCBI_TaxID=1237627 {ECO:0000313|EMBL:EWC76038.1, ECO:0000313|Proteomes:UP000030697}; RN [1] {ECO:0000313|EMBL:EWC76038.1, ECO:0000313|Proteomes:UP000030697} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=UGT5.1 {ECO:0000313|EMBL:EWC76038.1, RC ECO:0000313|Proteomes:UP000030697}; RG The Broad Institute Genome Sequencing Platform; RG The Broad Institute Genome Sequencing Center for Infectious Disease; RA Neafsey D., Cheeseman I., Volkman S., Adams J., Walker B., Young S.K., RA Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., RA Alvarado L., Arachchi H.M., Berlin A.M., Chapman S.B., Dewar J., RA Goldberg J., Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., RA Larimer J., McCowan C., Murphy C., Neiman D., Pearson M., Priest M., RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., RA Nusbaum C., Birren B.; RT "The Genome Sequence of Plasmodium falciparum UGT5.1."; RL Submitted (FEB-2013) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; KE124610; EWC76038.1; -; Genomic_DNA. DR ProteinModelPortal; W7JM15; -. DR SMR; W7JM15; -. DR EnsemblProtists; EWC76038; EWC76038; C923_03322. DR Proteomes; UP000030697; Unassembled WGS sequence. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000030697}; KW Reference proteome {ECO:0000313|Proteomes:UP000030697}. FT DOMAIN 459 629 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 698 AA; 81678 MW; FD385C7811AB7D0C CRC64; MGRILFLLKN VNKIEKRYFT NKSNIYYHNE SQKKEIIVLH PILKRSKNNS NKLFQEIIYD AQEALGLAKS ANFQIAKGIS MPLGGWYLKN EKQKKKNDPK NDKIDEGQVP NKELSQNNEH HHVFEKSEKE IPNEMSFTTD KSSSKYINYD EIERKVAESI LIKVNHIDNK FYFSKGKLNE LSKYYLKNPT PCIFINTLLS PEQFRNLEFL FNSLLKSYQD ELILNNKRER DNSEMYERVS DVKFDNCDSD DIIIDNSSYC LDAYNNFLDK EDEQCDDVDL EQNMNVLNEH IGDTSCEQAN DIPYEQISDT QECSKNIPMY VELFDRYSMI LYILKSRAKN NLSKLQLELA RANFVLNTYS EDSKSRMKYI KYIENNVLGG SCIDYEEKYT KLNFFTVGKQ NKKSNVNFSG YTSNYIKSNE TYKEYEKRII NNLYSKLKNE LIKCKNNMIL QNNSRKHKAI IAIVGYTNVG KTKLINYLTK SNLKARNLLF QTLDNAYKNL NISTCYSTIF VDSIGFIQNI PYSLYESFKI SLEAIKTADV IIHVIDVSHP YKDKHKKCVL ETLNKIGISD EFIKNNVIEV WNKIDKLTDN ELYTLCKNKP KNALPISAKY GTNCNYLIQI IEHLINQIKD VHILNLQFPT SEAKERINFL MKNYKVVPHS ISYSDDGNTT FIKLVENKSN LKKYYEKFEI KETYKSDN // ID W7K5M0_PLAFO Unreviewed; 698 AA. AC W7K5M0; DT 16-APR-2014, integrated into UniProtKB/TrEMBL. DT 16-APR-2014, sequence version 1. DT 10-MAY-2017, entry version 19. DE SubName: Full=GTP-binding protein HflX {ECO:0000313|EMBL:EWC88180.1}; GN ORFNames=PFNF54_03099 {ECO:0000313|EMBL:EWC88180.1}; OS Plasmodium falciparum (isolate NF54). OC Eukaryota; Alveolata; Apicomplexa; Aconoidasida; Haemosporida; OC Plasmodiidae; Plasmodium; Plasmodium (Laverania). OX NCBI_TaxID=5843 {ECO:0000313|EMBL:EWC88180.1, ECO:0000313|Proteomes:UP000030673}; RN [1] {ECO:0000313|EMBL:EWC88180.1, ECO:0000313|Proteomes:UP000030673} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NF54 {ECO:0000313|EMBL:EWC88180.1, RC ECO:0000313|Proteomes:UP000030673}; RG The Broad Institute Genome Sequencing Platform; RG The Broad Institute Genome Sequencing Center for Infectious Disease; RA Neafsey D., Cheeseman I., Volkman S., Adams J., Walker B., Young S.K., RA Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., RA Alvarado L., Arachchi H.M., Berlin A.M., Chapman S.B., Dewar J., RA Goldberg J., Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., RA Larimer J., McCowan C., Murphy C., Neiman D., Pearson M., Priest M., RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., RA Nusbaum C., Birren B.; RT "The Genome Sequence of Plasmodium falciparum NF54."; RL Submitted (FEB-2013) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; KE123833; EWC88180.1; -; Genomic_DNA. DR ProteinModelPortal; W7K5M0; -. DR SMR; W7K5M0; -. DR EnsemblProtists; EWC88180; EWC88180; PFNF54_03099. DR Proteomes; UP000030673; Unassembled WGS sequence. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000030673}; KW Reference proteome {ECO:0000313|Proteomes:UP000030673}. FT DOMAIN 459 629 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 698 AA; 81678 MW; FD385C7811AB7D0C CRC64; MGRILFLLKN VNKIEKRYFT NKSNIYYHNE SQKKEIIVLH PILKRSKNNS NKLFQEIIYD AQEALGLAKS ANFQIAKGIS MPLGGWYLKN EKQKKKNDPK NDKIDEGQVP NKELSQNNEH HHVFEKSEKE IPNEMSFTTD KSSSKYINYD EIERKVAESI LIKVNHIDNK FYFSKGKLNE LSKYYLKNPT PCIFINTLLS PEQFRNLEFL FNSLLKSYQD ELILNNKRER DNSEMYERVS DVKFDNCDSD DIIIDNSSYC LDAYNNFLDK EDEQCDDVDL EQNMNVLNEH IGDTSCEQAN DIPYEQISDT QECSKNIPMY VELFDRYSMI LYILKSRAKN NLSKLQLELA RANFVLNTYS EDSKSRMKYI KYIENNVLGG SCIDYEEKYT KLNFFTVGKQ NKKSNVNFSG YTSNYIKSNE TYKEYEKRII NNLYSKLKNE LIKCKNNMIL QNNSRKHKAI IAIVGYTNVG KTKLINYLTK SNLKARNLLF QTLDNAYKNL NISTCYSTIF VDSIGFIQNI PYSLYESFKI SLEAIKTADV IIHVIDVSHP YKDKHKKCVL ETLNKIGISD EFIKNNVIEV WNKIDKLTDN ELYTLCKNKP KNALPISAKY GTNCNYLIQI IEHLINQIKD VHILNLQFPT SEAKERINFL MKNYKVVPHS ISYSDDGNTT FIKLVENKSN LKKYYEKFEI KETYKSDN // ID W7KVI1_9CREN Unreviewed; 354 AA. AC W7KVI1; DT 16-APR-2014, integrated into UniProtKB/TrEMBL. DT 16-APR-2014, sequence version 1. DT 07-JUN-2017, entry version 18. DE SubName: Full=GTP-binding protein HflX {ECO:0000313|EMBL:EWG07266.1}; DE SubName: Full=GTPase HflX {ECO:0000313|EMBL:KJR79757.1}; GN ORFNames=ASUL_04716 {ECO:0000313|EMBL:EWG07266.1}, GN TQ35_00375 {ECO:0000313|EMBL:KJR79757.1}; OS Sulfolobales archaeon AZ1. OC Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; OC unclassified Sulfolobales. OX NCBI_TaxID=1326980 {ECO:0000313|EMBL:EWG07266.1, ECO:0000313|Proteomes:UP000054284}; RN [1] {ECO:0000313|EMBL:EWG07266.1, ECO:0000313|Proteomes:UP000054284} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=AZ1-illumnia {ECO:0000313|EMBL:EWG07266.1}; RX PubMed=24604657; RA Servin-Garciduenas L.E., Martinez-Romero E.; RT "Draft Genome Sequence of the Sulfolobales Archaeon AZ1, Obtained RT through Metagenomic Analysis of a Mexican Hot Spring."; RL Genome Announc. 2:e00164-14(2014). RN [2] {ECO:0000313|EMBL:KJR79757.1, ECO:0000313|Proteomes:UP000053480} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=AZ1-454 {ECO:0000313|EMBL:KJR79757.1}; RA Servin-Garciduenas L.E., Martinez-Romero E.; RT "Metagenome Sequencing of an Archaeal-Dominated Microbial Community RT from a Hot Spring at the Los Azufres Geothermal Field, Mexico."; RL Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EWG07266.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ASRH01000004; EWG07266.1; -; Genomic_DNA. DR EMBL; JZWS01000001; KJR79757.1; -; Genomic_DNA. DR PATRIC; fig|1326980.6.peg.936; -. DR OrthoDB; POG093Z07D6; -. DR Proteomes; UP000053480; Unassembled WGS sequence. DR Proteomes; UP000054284; Unassembled WGS sequence. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR CDD; cd01878; HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 4: Predicted; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000054284}; KW Reference proteome {ECO:0000313|Proteomes:UP000054284}. FT DOMAIN 179 354 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 145 172 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 354 AA; 39931 MW; 04EA63C9725340CE CRC64; MRAVLFVSDE YKEEALTLAE NAGYDVVEVF KLPKDPNSLF YIPQDKVEKL AESEDVETII VFTLLKPRHF INLGKKLPNK KVIDKLLLLL EIFALHAGSK EAKLQIELAK LRYELPIVKD LYRKTKITEQ QGPLGAGVYG VEAELRLYRR KIARITRELE HLKKVRETQL QDVKRIGLPT VTIVGYTNAG KTSIFNALTG LRQKVDNSMF TTTSPKRYSI NVDGKKVLLV DTVGFIRGIP PQIIEAFFVT LSEIKYANGI LLVVDVSLSD TLLVDMIRSS FAILREIGVS GKPIVVVANK VDKVTSSKEV EEKLELISKL SEELYNPIVN VIVTSATKFY NIDKLREEIL RLVS // ID W7Q1A3_9GAMM Unreviewed; 440 AA. AC W7Q1A3; DT 16-APR-2014, integrated into UniProtKB/TrEMBL. DT 16-APR-2014, sequence version 1. DT 07-JUN-2017, entry version 22. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=Q427_28545 {ECO:0000313|EMBL:EWG98792.1}; OS Halomonas sp. BC04. OC Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales; OC Halomonadaceae; Halomonas. OX NCBI_TaxID=1403540 {ECO:0000313|EMBL:EWG98792.1, ECO:0000313|Proteomes:UP000019279}; RN [1] {ECO:0000313|EMBL:EWG98792.1, ECO:0000313|Proteomes:UP000019279} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BC04 {ECO:0000313|EMBL:EWG98792.1, RC ECO:0000313|Proteomes:UP000019279}; RA Farooqui S., Greene A.C., Patel B.K.; RT "Draft Genome Sequence of Halomonas Strain BC04, an Aromatic-degrading RT moderate Halophilic Bacterium."; RL Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EWG98792.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AZQX01000350; EWG98792.1; -; Genomic_DNA. DR RefSeq; WP_043517693.1; NZ_AZQX01000350.1. DR EnsemblBacteria; EWG98792; EWG98792; Q427_28545. DR PATRIC; fig|1403540.3.peg.5344; -. DR Proteomes; UP000019279; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000019279}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000019279}. FT DOMAIN 199 365 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 440 AA; 49632 MW; 8BA6BE20C183E4F7 CRC64; MFFERPDAGE TAVLVHVDFQ DEREREDPGE FLELVRSAGA EPATLLSGSR HRPDSRTFIG SGKVEELRET LRVHGAELVI FNHALSPSQE RNLEQVLKCR VLDRTGLILD IFAQRARTHE GKLQVELAQL EYMSTRLVRG WTHLERQKGG IGLRGPGETQ LETDRRLLRA RIKAIHKRLD KVRSQRAQNR RARARAEIPS VSLVGYTNAG KSTLFNALTE SKVYTADQLF ATLDPTLRRL EIGDVGPVVL ADTVGFIRHL PHKLVEAFQA TLQEAAEAAL LVHVIDAADP DRERNIGEVE GVLNEIGALD VPMLKVMNKI DLLDSAPRIE RDGQGRPEVV WLSAQEGRGL ELLEEALSEC LAVDVIDFSL TLSPEQGRLR AGLHELDAVR EEHFEEPDGR VELKVRLPRR DFLQLMSRLD ERAEDYLPPE LCERPVWEGR // ID W7QMG2_9GAMM Unreviewed; 440 AA. AC W7QMG2; DT 16-APR-2014, integrated into UniProtKB/TrEMBL. DT 16-APR-2014, sequence version 1. DT 07-JUN-2017, entry version 22. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=Q427_07855 {ECO:0000313|EMBL:EWH02606.1}; OS Halomonas sp. BC04. OC Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales; OC Halomonadaceae; Halomonas. OX NCBI_TaxID=1403540 {ECO:0000313|EMBL:EWH02606.1, ECO:0000313|Proteomes:UP000019279}; RN [1] {ECO:0000313|EMBL:EWH02606.1, ECO:0000313|Proteomes:UP000019279} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BC04 {ECO:0000313|EMBL:EWH02606.1, RC ECO:0000313|Proteomes:UP000019279}; RA Farooqui S., Greene A.C., Patel B.K.; RT "Draft Genome Sequence of Halomonas Strain BC04, an Aromatic-degrading RT moderate Halophilic Bacterium."; RL Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EWH02606.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AZQX01000086; EWH02606.1; -; Genomic_DNA. DR RefSeq; WP_043512122.1; NZ_AZQX01000086.1. DR EnsemblBacteria; EWH02606; EWH02606; Q427_07855. DR PATRIC; fig|1403540.3.peg.1482; -. DR Proteomes; UP000019279; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000019279}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000019279}. FT DOMAIN 199 365 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 440 AA; 49478 MW; 067A353FD88B14CE CRC64; MFFERPDAGE TAVLVHVDFQ DEREREDPGE FLELVRSAGA EPATLLSGSR HRPDSRTFIG SGKVEELREA LRVHGAELVI FNHALSPSQE RNLEQVLKCR VLDRTGLILD IFAQRARTHE GKLQVELAQL EYMSTRLVRG WTHLERQKGG IGLRGPGETQ LETDRRLLRA RIKAIHKRLD KVRSQRAQNR RARARAEIPS VSLVGYTNAG KSTLFNALTE SKVYTADQLF ATLDPTLRRL EVGDVGPVVL ADTVGFIRHL PHKLVEAFQA TLQEAAEAAL LVHVIDAADP DRERNIAEVE GVLNEIGALD VPMLKVMNKI DLLDSAPRIE RDGQGRPEVV WLSAQEGRGL ELLEEALSEC LADDVIDFSL TLSPEQGRLR AGLHELGAVR EEHFEEPDGR VGLKVRLPRR DFLQLMSRLD ERAEDYLPSE LCERPVWEGR // ID W7QSR9_9ALTE Unreviewed; 428 AA. AC W7QSR9; DT 16-APR-2014, integrated into UniProtKB/TrEMBL. DT 16-APR-2014, sequence version 1. DT 30-AUG-2017, entry version 24. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=DS2_17247 {ECO:0000313|EMBL:EWH08435.1}; OS Catenovulum agarivorans DS-2. OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales; OC Alteromonadaceae; Catenovulum. OX NCBI_TaxID=1328313 {ECO:0000313|EMBL:EWH08435.1, ECO:0000313|Proteomes:UP000019276}; RN [1] {ECO:0000313|EMBL:EWH08435.1, ECO:0000313|Proteomes:UP000019276} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DS-2 {ECO:0000313|EMBL:EWH08435.1, RC ECO:0000313|Proteomes:UP000019276}; RX PubMed=24604650; RA Shan D., Li X., Gu Z., Wei G., Gao Z., Shao Z.; RT "Draft Genome Sequence of the Agar-Degrading Bacterium Catenovulum sp. RT Strain DS-2, Isolated from Intestines of Haliotis diversicolor."; RL Genome Announc. 2:e00144-14(2014). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EWH08435.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ARZY01000046; EWH08435.1; -; Genomic_DNA. DR RefSeq; WP_035016203.1; NZ_ARZY01000046.1. DR EnsemblBacteria; EWH08435; EWH08435; DS2_17247. DR PATRIC; fig|1328313.3.peg.3525; -. DR Proteomes; UP000019276; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000019276}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000019276}. FT DOMAIN 198 365 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 164 191 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 428 AA; 48397 MW; D4C6475950C756F8 CRC64; MFDRYKAGDQ AILVHVDLDD EVAREDLEEL KLLASSAGVN TLAVVTAARS KPDPKFFVGS GKAEEIQQAV VALEANVVIF NHALSPSQEK SLEALVKCRV LDRTTLILDI FAQRARTHEG NLQVELAQLK HISTRLVRGW THLERQKGGI GLRGPGETQL ETDRRLIRGR IKNIEKRLEK VAKQRDQGRR ARKRSALPTI SLVGYTNAGK STLFNRLTES DVYAADQLFA TLDPTLRKIT LEEVGDSILA DTVGFIRHLP HDLVAAFKAT LQETRDADIQ LHVIDAADER RAENIGAVNK VLEEIEADDI SQILVYNKID QLEEVRPHID RDDEGRVVRV WLSARTGEGC ELLLQALTEQ LARSMVEYKL AIPPAEQQWR GVFYQLDCIV EESYSELGDW LVDVKMSSED WNRLNKTHQR QLEHFIIH // ID W7T8D3_9PSEU Unreviewed; 285 AA. AC W7T8D3; DT 16-APR-2014, integrated into UniProtKB/TrEMBL. DT 16-APR-2014, sequence version 1. DT 07-JUN-2017, entry version 17. DE SubName: Full=GTP-binding protein HflX {ECO:0000313|EMBL:EWM16984.1}; DE Flags: Fragment; GN ORFNames=KUTG_07288 {ECO:0000313|EMBL:EWM16984.1}; OS Kutzneria sp. 744. OC Bacteria; Actinobacteria; Pseudonocardiales; Pseudonocardiaceae; OC Kutzneria. OX NCBI_TaxID=345341 {ECO:0000313|EMBL:EWM16984.1, ECO:0000313|Proteomes:UP000030658}; RN [1] {ECO:0000313|EMBL:EWM16984.1, ECO:0000313|Proteomes:UP000030658} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=744 {ECO:0000313|EMBL:EWM16984.1, RC ECO:0000313|Proteomes:UP000030658}; RG The Broad Institute Genome Sequencing Platform; RG Broad Institute Microbial Sequencing Center; RA Fischbach M., Godfrey P., Ward D., Young S., Zeng Q., Koehrsen M., RA Alvarado L., Berlin A.M., Bochicchio J., Borenstein D., Chapman S.B., RA Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A., RA Gujja S., Heilman E.R., Heiman D.I., Hepburn T.A., Howarth C., Jen D., RA Larson L., Lewis B., Mehta T., Park D., Pearson M., Richards J., RA Roberts A., Saif S., Shea T.D., Shenoy N., Sisk P., Stolte C., RA Sykes S.N., Thomson T., Walk T., White J., Yandava C., Straight P., RA Clardy J., Hung D., Kolter R., Mekalanos J., Walker S., Walsh C.T., RA Wieland-Brown L.C., Haas B., Nusbaum C., Birren B.; RT "The genome sequence of Kutzneria sp. strain 744."; RL Submitted (OCT-2009) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; KK037166; EWM16984.1; -; Genomic_DNA. DR RefSeq; WP_043723701.1; NZ_KK037166.1. DR EnsemblBacteria; EWM16984; EWM16984; KUTG_07288. DR Proteomes; UP000030658; Unassembled WGS sequence. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000030658}; KW Reference proteome {ECO:0000313|Proteomes:UP000030658}. FT DOMAIN 254 285 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT NON_TER 285 285 {ECO:0000313|EMBL:EWM16984.1}. SQ SEQUENCE 285 AA; 30855 MW; 0ECF0D473EC84C69 CRC64; MTETYAFDPD DTADDELVST GELELADRAA LRRIVGLSTE LEDITEVEYR RLRLERVVLV GVWTEGNAAD AEASLAELAR LAETAGSHVL EGLVQRRDRP DPATYVGSGK VIEVRDVVVA TGADTVICDG ELSSGQLRNL EDRLKVKVVD RTALILDIFA QHAQSKEGKA QVELAQLQYL LPRLRGWGSA MSRQAGGRAG GATGGVGLRG PGETKLETDR RRIHKRISKL RNEIKAMSVV RDTKRGRRVA NDVPNVAIVG YTNAGKSSLL NAITSAGVLV EDALF // ID W7TED9_9STRA Unreviewed; 499 AA. AC W7TED9; DT 16-APR-2014, integrated into UniProtKB/TrEMBL. DT 16-APR-2014, sequence version 1. DT 07-JUN-2017, entry version 14. DE SubName: Full=Gtp-binding protein {ECO:0000313|EMBL:EWM25385.1}; GN ORFNames=Naga_100005g135 {ECO:0000313|EMBL:EWM25385.1}; OS Nannochloropsis gaditana. OC Eukaryota; Stramenopiles; Eustigmatophyceae; Eustigmatales; OC Monodopsidaceae; Nannochloropsis. OX NCBI_TaxID=72520 {ECO:0000313|EMBL:EWM25385.1, ECO:0000313|Proteomes:UP000019335}; RN [1] {ECO:0000313|EMBL:EWM25385.1, ECO:0000313|Proteomes:UP000019335} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=B-31 {ECO:0000313|EMBL:EWM25385.1, RC ECO:0000313|Proteomes:UP000019335}; RX PubMed=23966634; DOI=10.1093/mp/sst120; RA Corteggiani Carpinelli E., Telatin A., Vitulo N., Forcato C., RA D'Angelo M., Schiavon R., Vezzi A., Giacometti G.M., Morosinotto T., RA Valle G.; RT "Chromosome Scale Genome Assembly and Transcriptome Profiling of RT Nannochloropsis gaditana in Nitrogen Depletion."; RL Mol. Plant 7:323-335(2014). CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EWM25385.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AZIL01000936; EWM25385.1; -; Genomic_DNA. DR EnsemblProtists; EWM25385; EWM25385; Naga_100005g135. DR Proteomes; UP000019335; Chromosome 11. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000019335}; KW Reference proteome {ECO:0000313|Proteomes:UP000019335}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1 27 {ECO:0000256|SAM:SignalP}. FT CHAIN 28 499 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5004900804. FT DOMAIN 263 445 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 225 252 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 499 AA; 55601 MW; 0DC1EC31ABE52899 CRC64; MWTLCGKCRM IKLPASLLPS TFMFAAASIE PAQLWSWQRA TKPILGDNFH RNYSIRPQKV PSAPVPNCIV LHITPPRSTL EDRLQEEDFL DEACALAQTL GYAVPVREIL RLRAIHPKTF IGKGKVVELR GLLRATDAIL FINTPRLTAL QQRNLKELCQ TEGVKDRISV ILDIFGQRAR TMEAKLQVEL AQCKYALSHL VRGASAGYEQ QRGASGTGFM AGGGEKALEL RRRQLREQSK VLQHKLKTVE KRRMEQRKHR RQPTVSLLGY TNVGKSSLLN ALTHSHAVSV EDRPFETLDT TTRALFLPSV GASALLTDTV GFIRQLPLEL VAAFRATLEE AVSADLLLHV RDASTLGTPL FAEQYASVDK ILRDVGTPEH LKHSVVEVWN KVDLLTNKQR DQMARVLAGA KREASSPDVV LVSAQTKEGM RELVRMIGDR LVEGGFLQPA ETRGADKKSS CEKDGKKHMC YSDEEGKQEV LSSRTENMSN KKAVNEVDV // ID W7UUQ4_RUMFL Unreviewed; 415 AA. AC W7UUQ4; DT 16-APR-2014, integrated into UniProtKB/TrEMBL. DT 16-APR-2014, sequence version 1. DT 07-JUN-2017, entry version 24. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=RF007C_11235 {ECO:0000313|EMBL:EWM54904.1}; OS Ruminococcus flavefaciens 007c. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Ruminococcaceae; OC Ruminococcus. OX NCBI_TaxID=1341157 {ECO:0000313|EMBL:EWM54904.1, ECO:0000313|Proteomes:UP000019365}; RN [1] {ECO:0000313|EMBL:EWM54904.1, ECO:0000313|Proteomes:UP000019365} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=007c {ECO:0000313|EMBL:EWM54904.1, RC ECO:0000313|Proteomes:UP000019365}; RX PubMed=24992679; RA Dassa B., Borovok I., Ruimy-Israeli V., Lamed R., Flint H.J., RA Duncan S.H., Henrissat B., Coutinho P., Morrison M., Mosoni P., RA Yeoman C.J., White B.A., Bayer E.A.; RT "Rumen cellulosomics: divergent fiber-degrading strategies revealed by RT comparative genome-wide analysis of six ruminococcal strains."; RL PLoS ONE 9:E99221-E99221(2014). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EWM54904.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ATAX01000008; EWM54904.1; -; Genomic_DNA. DR RefSeq; WP_037296949.1; NZ_ATAX01000008.1. DR EnsemblBacteria; EWM54904; EWM54904; RF007C_11235. DR PATRIC; fig|1341157.4.peg.522; -. DR Proteomes; UP000019365; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000019365}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000019365}. FT DOMAIN 200 362 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 415 AA; 46164 MW; CE47F0DACCF094E0 CRC64; MYENKTEERP VKAVLACVDT GEFDAEVSIK ELEELASTAQ AEVVGTVIQK RPSYDPATCM GTGRLEELKE QLEAIEAELV IFDHELTGIQ VRNIEQILDV RVIDRTTLIL DIFAQRARTK EGKLQVELAQ QKYRLPRLTG MGTALSRLGG GIGTRGPGET KLETDKRHIR KRISYLEAEL EELKKHRNFS RSRRKKDGIL CAAIVGYTNV GKSTLLNALT DAGVLAENKL FATLDITSRS IELPDGRSVM LIDTVGLIRR LPHNLVEAFK STLEEAAAAD IILNVQDLSS PEIREQAEVT ASLLSELGCE GIPQIFVMNK ADAAPFTDTV FEDESTVMIS AKEHTGFDKL LECIMRNLPE TAKRMKLLIP YDKGAFLGRI RQDGKIFSEE YAENGTLIDA LVDVKLIKEA ESYRV // ID W7WR06_9BURK Unreviewed; 340 AA. AC W7WR06; DT 16-APR-2014, integrated into UniProtKB/TrEMBL. DT 16-APR-2014, sequence version 1. DT 07-JUN-2017, entry version 19. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:EWS65256.1}; GN ORFNames=Y695_01492 {ECO:0000313|EMBL:EWS65256.1}; OS Hydrogenophaga sp. T4. OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Comamonadaceae; Hydrogenophaga. OX NCBI_TaxID=1437444 {ECO:0000313|EMBL:EWS65256.1, ECO:0000313|Proteomes:UP000019362}; RN [1] {ECO:0000313|EMBL:EWS65256.1, ECO:0000313|Proteomes:UP000019362} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=T4 {ECO:0000313|EMBL:EWS65256.1, RC ECO:0000313|Proteomes:UP000019362}; RA Szabo Z., Gyula P., Robotka H., Bihari Z.; RT "Genome sequencing of the TBA-degrading Hydrogenophaga sp. T4."; RL Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EWS65256.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AZSO01000147; EWS65256.1; -; Genomic_DNA. DR EnsemblBacteria; EWS65256; EWS65256; Y695_01492. DR PATRIC; fig|1437444.3.peg.1426; -. DR Proteomes; UP000019362; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000019362}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000019362}. FT DOMAIN 204 295 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 340 AA; 37818 MW; 1A3D3F68D2DC6E33 CRC64; MDLNPSASQN PSIPSVILVG VDFGLPHFDA ELEELGLLAQ TAGFAVADRV SCKRRAPDPA LFVGSGKAEE IKMLAQSKGA SEILFDQALS PAQQRNLERT LGLPVNDRTL LILQIFAQRA RSHEGKLQVE LARLQYLSTR LVRRWSHLER QSGGIGMRGG PGETQIELDR RMIGDSIKRT KERLEKVKKQ RATQRRQRER RDSFAISLVG YTNAGKSSIF NALVKARAYA ADQLFATLDT TTRQLYLGEA GRSVSLSDTV GFIRDLPHGL VDAFAATLQE AADADLLLHV VDASNLRTWS RSLRCWVCSR TLAPIACRRS WCSTSSTPWT RQRCPVCWKM // ID W7YLA2_9BACL Unreviewed; 428 AA. AC W7YLA2; DT 16-APR-2014, integrated into UniProtKB/TrEMBL. DT 16-APR-2014, sequence version 1. DT 07-JUN-2017, entry version 25. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=JCM16418_2610 {ECO:0000313|EMBL:GAF08528.1}; OS Paenibacillus pini JCM 16418. OC Bacteria; Firmicutes; Bacilli; Bacillales; Paenibacillaceae; OC Paenibacillus. OX NCBI_TaxID=1236976 {ECO:0000313|EMBL:GAF08528.1, ECO:0000313|Proteomes:UP000019364}; RN [1] {ECO:0000313|EMBL:GAF08528.1, ECO:0000313|Proteomes:UP000019364} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=JCM 16418 {ECO:0000313|EMBL:GAF08528.1, RC ECO:0000313|Proteomes:UP000019364}; RA Yuki M., Oshima K., Suda W., Oshida Y., Kitamura K., Iida Y., RA Hattori M., Ohkuma M.; RT "Draft Genome Sequence of Paenibacillus pini JCM 16418T, Isolated from RT the Rhizosphere of Pine Tree."; RL Genome Announc. 2:e00210-14(2014). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:GAF08528.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BAVZ01000007; GAF08528.1; -; Genomic_DNA. DR RefSeq; WP_036649043.1; NZ_BAZT01000007.1. DR EnsemblBacteria; GAF08528; GAF08528; JCM16418_2610. DR Proteomes; UP000019364; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000019364}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000019364}. FT DOMAIN 200 371 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 428 AA; 48824 MW; 8C358A3E1AC4249C CRC64; MEEEQQKAII VGVNLKQKHQ DDFEYSMEEL GNLAHACHVE VVGKMTQNME KVNKSHYIGT GKVEELAGLY RGLEANLIIF NDELSPSQLR NLEADLECKV IDRTILILDI FEKRAKTREA QLQVEIAQLQ YMLPRLSGLR ESLGRQSGGV GTKNKGAGET RLELDRRRIE DKINALHKEL ETLVFQRQTQ RKQRKKNQVP VVSLVGYTNA GKSTIMNAMV ELYSPSGGTE EKKVFEKDML FATLETSVRN IHLADNKDFL LTDTVGFVSK LPHHLVKAFR STLEEVAEAD LLVHVIDYSN ANYEQLIRIT ENTLKDIGIT DIPTIFAYNK CDMAGRDIPE VEGNNIYLAA KPRLGITELV DMIRGFIFTD YVQCEMLIPY EQGQIVSYLN EQANIKSTEY ENEGTRLSLE CKAMDYEKYR QFVIEETE // ID W7YLE5_9BACT Unreviewed; 412 AA. AC W7YLE5; DT 16-APR-2014, integrated into UniProtKB/TrEMBL. DT 16-APR-2014, sequence version 1. DT 07-JUN-2017, entry version 25. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=JCM21142_104123 {ECO:0000313|EMBL:GAF05391.1}; OS Saccharicrinis fermentans DSM 9555 = JCM 21142. OC Bacteria; Bacteroidetes; Bacteroidia; Marinilabiliales; OC Marinilabiliaceae; Saccharicrinis. OX NCBI_TaxID=869213 {ECO:0000313|EMBL:GAF05391.1, ECO:0000313|Proteomes:UP000019402}; RN [1] {ECO:0000313|EMBL:GAF05391.1, ECO:0000313|Proteomes:UP000019402} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=JCM 21142 {ECO:0000313|EMBL:GAF05391.1, RC ECO:0000313|Proteomes:UP000019402}; RA Starns D., Oshima K., Suda W., Iino T., Yuki M., Inoue J., RA Kitamura K., Iida T., Darby A., Hattori M., Ohkuma M.; RT "Draft Genome Sequence of Cytophaga fermentans JCM 21142T, a RT Facultative Anaerobe Isolated from Marine Mud."; RL Genome Announc. 2:e00206-14(2014). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:GAF05391.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BAMD01000083; GAF05391.1; -; Genomic_DNA. DR RefSeq; WP_027473267.1; NZ_KI912107.1. DR EnsemblBacteria; GAF05391; GAF05391; JCM21142_104123. DR Proteomes; UP000019402; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000019402}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000019402}. FT DOMAIN 202 385 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 412 AA; 46934 MW; C26A3E905754F06C CRC64; MGEQISTHQE LEKVILVGLR TPGITEALLT EYLDELAFLA ETAGGIPVKR YTQSLPMPDN KTFVGRGKLE EVLEGVKVYE ADCVIFDDEL SPSQLRNLES ILKIRILDRT NLILDIFAKN AKTAAAKTQV ELAQYQYLLP RLTRMWTHLQ RQRGGMGMRG PGEKEIETDR RIIRDKIAKL KLDLVKIDKQ KSTQRKNRGK MVRVALVGYT NVGKSTLMNT ISKSTVLAEN KLFATLDTTV RKVVVGNLPF LVADTVGFIR KLPHHLVDSF KSTLDEVREA DILVHVVDIS HAGFEQQVDI VNQTLQELDK TEKKMIMVFN KMDAFTYTPK DDDDLTPMAQ ENYSLEDLKK SWMAKGLDTV FISAKNKENL NEFKELIYNE VRKIHTARFP YNDFLYPNIS FDDLEMEDGG ES // ID W7YTW5_9BACL Unreviewed; 429 AA. AC W7YTW5; DT 16-APR-2014, integrated into UniProtKB/TrEMBL. DT 16-APR-2014, sequence version 1. DT 07-JUN-2017, entry version 23. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=JCM16418_4839 {ECO:0000313|EMBL:GAF10623.1}; OS Paenibacillus pini JCM 16418. OC Bacteria; Firmicutes; Bacilli; Bacillales; Paenibacillaceae; OC Paenibacillus. OX NCBI_TaxID=1236976 {ECO:0000313|EMBL:GAF10623.1, ECO:0000313|Proteomes:UP000019364}; RN [1] {ECO:0000313|EMBL:GAF10623.1, ECO:0000313|Proteomes:UP000019364} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=JCM 16418 {ECO:0000313|EMBL:GAF10623.1, RC ECO:0000313|Proteomes:UP000019364}; RA Yuki M., Oshima K., Suda W., Oshida Y., Kitamura K., Iida Y., RA Hattori M., Ohkuma M.; RT "Draft Genome Sequence of Paenibacillus pini JCM 16418T, Isolated from RT the Rhizosphere of Pine Tree."; RL Genome Announc. 2:e00210-14(2014). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:GAF10623.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BAVZ01000029; GAF10623.1; -; Genomic_DNA. DR RefSeq; WP_036653189.1; NZ_BAZT01000029.1. DR EnsemblBacteria; GAF10623; GAF10623; JCM16418_4839. DR Proteomes; UP000019364; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000019364}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000019364}. FT DOMAIN 208 372 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 429 AA; 48337 MW; F009EBEB2AFD20A8 CRC64; MANSTYDTHT QIRDKAILVS LVTDEIKRSG MDSEHSLHEL VQLAETAGVE VLEVLTQNKS VPDSRWFIGK GKVEELRMLL EMHGGNTVIF DHELSGAQVR NLEQSLDAKI IDRTQLILDI FAQRAKTREG IIQVELAQLM YLLPRLSGQG KNLSRLGGGI GTRGPGESKL ETDRRHIRGR ILELKNHLAE VTRHRKLYRA RRQKSGIIQL ALVGYTNAGK STLLKQLTQA DVYIENQLFA TLDPTTREME LPSGNNVVIT DTVGFIQNLP HDLIAAFRAT LEEVNEADLV LHVVDASSEM REDQMAVVDS ILQELGSSDT PQIVLFNKKD LCTPQQLEML PTGDGYLKLS AYDESDLLKL RQIIQQKLTG DTLKFRIPSD RGEVVSVLYR VGDVINQKLV DDDMLYTVQL HQSDYEKYGH TLKDFIERD // ID W7YWZ1_9BACI Unreviewed; 419 AA. AC W7YWZ1; DT 16-APR-2014, integrated into UniProtKB/TrEMBL. DT 16-APR-2014, sequence version 1. DT 07-JUN-2017, entry version 23. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=JCM19045_971 {ECO:0000313|EMBL:GAF11833.1}; OS Bacillus sp. JCM 19045. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus. OX NCBI_TaxID=1460639 {ECO:0000313|EMBL:GAF11833.1, ECO:0000313|Proteomes:UP000019372}; RN [1] {ECO:0000313|EMBL:GAF11833.1, ECO:0000313|Proteomes:UP000019372} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=JCM 19045 {ECO:0000313|EMBL:GAF11833.1, RC ECO:0000313|Proteomes:UP000019372}; RA Kudo T., Sakamoto K., Akinaga M., Kawauchi A., Nakahara T., Zhang X., RA Yamada A., Oshima K., Suda W., Kuwahara H., Nakamura N., Nogi Y., RA Kitamura K., Yuki M., Iida T., Moriya S., Inoue T., Hongoh Y., RA Hattori M., Ohkuma M.; RT "Draft Genome Sequences of Cyclodextrin-Producing Alkaliphilic RT Bacillus Strains JCM 19045, JCM 19046, and JCM 19047."; RL Genome Announc. 2:e00211-14(2014). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:GAF11833.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BAWA01000004; GAF11833.1; -; Genomic_DNA. DR RefSeq; WP_051990968.1; NZ_BAWA01000004.1. DR EnsemblBacteria; GAF11833; GAF11833; JCM19045_971. DR Proteomes; UP000019372; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000019372}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000019372}. FT DOMAIN 203 367 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 162 196 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 419 AA; 48232 MW; 94FB70689AF5959C CRC64; MHEQQTRKTV DTIIIGVEKQ QDVDFSYSMK ELTNLTEALD LRTVAQVSQK LTVPNQATYI GSGKVSEIKM MCEEMDVSLV IFNDELTPSQ IRNLEKLLEV TVYDRTMLIL DIFGERAKTK EAQMQVEVAR LKYLLPRLVG MRASLSRQGG SGTGLANRGA GETKLELDRR KIESRINMLE KELESIVNRR DIQRSQRKKQ QMPVVALIGY TNAGKSSLLN AMLTDDQEKH VFEKDMLFAT LDTSVRRVEW KKNLPFLMAD TVGFVSKLPT HLVKAFRSTL EEAREADLLL HVVDYSHEYY KEMIETTTET LKSMDIEQPM VFVYNKIDLT DENEPRTQAN ELFVSASKKL GLNLLADAIQ ASIFKEYRVQ NLLIPYDEGA VQARINEQTH VIKQEEREEG WFIKAFFNEQ DRLAFERFL // ID W8F355_9BACT Unreviewed; 446 AA. AC W8F355; DT 14-MAY-2014, integrated into UniProtKB/TrEMBL. DT 14-MAY-2014, sequence version 1. DT 07-JUN-2017, entry version 20. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=Hsw_3788 {ECO:0000313|EMBL:AHJ99383.1}; OS Hymenobacter swuensis DY53. OC Bacteria; Bacteroidetes; Cytophagia; Cytophagales; Hymenobacteraceae; OC Hymenobacter. OX NCBI_TaxID=1227739 {ECO:0000313|EMBL:AHJ99383.1, ECO:0000313|Proteomes:UP000019423}; RN [1] {ECO:0000313|EMBL:AHJ99383.1, ECO:0000313|Proteomes:UP000019423} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DY53 {ECO:0000313|EMBL:AHJ99383.1, RC ECO:0000313|Proteomes:UP000019423}; RA Jung J.-H., Jeong S.-W., Joe M.-H., Cho y.-j., Kim M.-K., Lim S.-Y.; RT "Complete genome sequence of ionizing-radiation resistance bacterium RT Hymenobacter swuensis DY53."; RL Submitted (JAN-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP007145; AHJ99383.1; -; Genomic_DNA. DR EnsemblBacteria; AHJ99383; AHJ99383; Hsw_3788. DR KEGG; hsw:Hsw_3788; -. DR PATRIC; fig|1227739.3.peg.3945; -. DR KO; K03665; -. DR Proteomes; UP000019423; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000019423}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000019423}. FT DOMAIN 236 427 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 204 231 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 446 AA; 50352 MW; F54273C17F167C42 CRC64; MAKESKRREN STRHPGATDN VKGRAGRILA KASKHDTYET APEAETAILV AVPDKRQADA RTQEYLDELA FLAETAGAIV TKRFVQRLEK PDIRTFVGEG KLAEIKAYVD HSGASMVIFD DDLSPSQLRN LEAELQVKIV DRSLLIIDIF ASRAKSATAR TQVELAQYQY LLPRLTGLWT HLDKQRGGGV SQRGPGETEI ETDRRVVRER IDFLKERLKE LDKQSQTQRK SRTGMVRVAL VGYTNVGKST IMNLLSRADV FAENKLFATV DSTVRKVVLE TVPFLLSDTV GFIRKLPTRL IESFKSTLDE IREADLLLHV VDISHPSFEE HIAVVNDTLK DINAADKPML LIFNKIDLYN PEVTAEHHGG FEGMNEEEEE TPRPTLEQLK ATYMAKLHDP VIFISAQERE NVDELRAMLT RRVAAIHAER YPSVQPISPD NEEWQS // ID W8KGY7_HALHR Unreviewed; 427 AA. AC W8KGY7; DT 14-MAY-2014, integrated into UniProtKB/TrEMBL. DT 14-MAY-2014, sequence version 1. DT 30-AUG-2017, entry version 22. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=M911_03730 {ECO:0000313|EMBL:AHK78438.1}; OS Halorhodospira halochloris str. A. OC Bacteria; Proteobacteria; Gammaproteobacteria; Chromatiales; OC Ectothiorhodospiraceae; Halorhodospira. OX NCBI_TaxID=1354791 {ECO:0000313|EMBL:AHK78438.1, ECO:0000313|Proteomes:UP000019442}; RN [1] {ECO:0000313|EMBL:AHK78438.1, ECO:0000313|Proteomes:UP000019442} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=A {ECO:0000313|EMBL:AHK78438.1, RC ECO:0000313|Proteomes:UP000019442}; RA Singh K.S.; RT "Draft Genome Sequence of extremely halophilic bacteria Halorhodospira RT halochloris."; RL Submitted (FEB-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP007268; AHK78438.1; -; Genomic_DNA. DR EnsemblBacteria; AHK78438; AHK78438; M911_03730. DR KEGG; hhc:M911_03730; -. DR PATRIC; fig|1354791.3.peg.1140; -. DR KO; K03665; -. DR Proteomes; UP000019442; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000019442}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000019442}. FT DOMAIN 198 365 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 164 191 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 427 AA; 47967 MW; B8F74CA78EAB4E15 CRC64; MFERPRSGER AVLVHLNLPT QDDDEDCQEF MELVRSAGAE PVGLITGSRK SPDPRYFVGS GKAEEVRDLV KSEEAEVAIF DHPLSPSQER NLEKLLQCRV LDRAGLILDI FAQRARSHEG KLQVELAQLR HMSTRLVRGW THLERQKGGI GLRGPGETQL ETDRRLLGVR IKQITRRLEK VEQQREQGRR SRLRAEVPTI SLVGYTNAGK STLFNRLTQA GVYAADQLFA TLDPTLRRVE LPSQQAMILA DTVGFVRQLP HDLVAAFRAT LTETREASLL LHVVDAHDAQ RDVYMEQVNQ VLEEIGAREV PQILVFNKID LIPGATPRIE PADHGEPARV WLSAQTGAGV DALLEMLADH YAESIVGGWL ELPPTAGRER AGLFEMDAVE QEEVTESGGW RLRIRLPQRR LDELFRDAGF TPKLSQD // ID W8RV87_9RHOB Unreviewed; 434 AA. AC W8RV87; DT 14-MAY-2014, integrated into UniProtKB/TrEMBL. DT 14-MAY-2014, sequence version 1. DT 07-JUN-2017, entry version 19. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=roselon_02898 {ECO:0000313|EMBL:AHM05188.1}; OS Roseibacterium elongatum DSM 19469. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae; Roseibacterium. OX NCBI_TaxID=1294273 {ECO:0000313|EMBL:AHM05188.1, ECO:0000313|Proteomes:UP000019593}; RN [1] {ECO:0000313|EMBL:AHM05188.1, ECO:0000313|Proteomes:UP000019593} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 19469 {ECO:0000313|Proteomes:UP000019593}; RA Fiebig A., Goeker M., Klenk H.-P.P.; RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP004372; AHM05188.1; -; Genomic_DNA. DR EnsemblBacteria; AHM05188; AHM05188; roselon_02898. DR KEGG; red:roselon_02898; -. DR PATRIC; fig|1294273.3.peg.2861; -. DR KO; K03665; -. DR Proteomes; UP000019593; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000019593}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000019593}. FT DOMAIN 214 383 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 434 AA; 47624 MW; 5BA188084D07B398 CRC64; MTASDRHLPE DDMNARGPTR AMVLHPDIQT ERERRDPGPA LDEAVALAAA LPDLEVVAAE VVRLPKAHPG LLFGSGKIEE LKAKVKAQEI ELVLIDGPVT PVQQRNLEKE WGVKLLDRTG LILEIFADRA ATREGVLQVD LAALSYQRTR LVRAWTHLER QRGGLGFVGG PGETQIEADR RAIDEAVTRI RRQLAKVVKT RTLHRAARKK VPYPIVALVG YTNAGKSTLF NRLTGAEVMT KDMLFATLDP TMRAIELPDG TEVILSDTVG FISDLPTQLV AAFRATLEEV LDADLIVHVR DISHPETGEQ AADVTQILTD LGVTGETPLI EVWNKIDQLP GPERATRLTE AARRAHVYAA SALTGEGMGP LLKAVAEAVS PPRTRTVVTL THADGRRRAW LFEQGIVEGE DAGEEETRLT VNWTDRQRAA FQAL // ID W8RXP5_PSEST Unreviewed; 433 AA. AC W8RXP5; DT 14-MAY-2014, integrated into UniProtKB/TrEMBL. DT 14-MAY-2014, sequence version 1. DT 30-AUG-2017, entry version 27. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=CH92_18025 {ECO:0000313|EMBL:AHL76876.1}; OS Pseudomonas stutzeri (Pseudomonas perfectomarina). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=316 {ECO:0000313|EMBL:AHL76876.1, ECO:0000313|Proteomes:UP000019522}; RN [1] {ECO:0000313|EMBL:AHL76876.1, ECO:0000313|Proteomes:UP000019522} RP NUCLEOTIDE SEQUENCE. RC STRAIN=28a24 {ECO:0000313|EMBL:AHL76876.1, RC ECO:0000313|Proteomes:UP000019522}; RA Baltrus D., Dougherty K.; RL Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP007441; AHL76876.1; -; Genomic_DNA. DR RefSeq; WP_025243087.1; NZ_CP007441.1. DR EnsemblBacteria; AHL76876; AHL76876; CH92_18025. DR GeneID; 31554434; -. DR KEGG; pstt:CH92_18025; -. DR PATRIC; fig|316.77.peg.3597; -. DR KO; K03665; -. DR Proteomes; UP000019522; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000019522}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000019522}. FT DOMAIN 199 366 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 165 192 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 433 AA; 48695 MW; 3FAB1C422D448403 CRC64; MFFERPGGGE RAILVHLDGQ DPAAREDPQE FRELARSAGA ETVGFVNVAK HQPSARFLIG SGKVEELHDL VKDGEVELVI FNHTLTPSQE RNLERALECR VLDRTGLILD IFAQRARTHE GKLQVELAQL EHMSTRLVRG WTHLERQKGG IGLRGPGETQ LETDRRLLRV RIRQIKQRLE KVRGQREQAR RGRRRADIPL ISLVGYTNAG KSTLFNALTE SDVYAANQLF ATLDPTLRRL ELGDLGPVVL ADTVGFIRHL PHKLVESFRA TLEESSNADL LLHVIDAHEP ERDQQIEQVL AVLTEIGAHE LPILEVYNKI DLLEGIEPQI QRNADGVPQR VWVSAQQGLG LDLVKQAVAE LLGNDLFVGT LRLPQRLGRL RAQLFDLGAV QSESHDEEGG SLLDVRLQRV ELHRLISRAG LEAEQFFEQH TLQ // ID W8T600_PEPAC Unreviewed; 426 AA. AC W8T600; DT 14-MAY-2014, integrated into UniProtKB/TrEMBL. DT 14-MAY-2014, sequence version 1. DT 07-JUN-2017, entry version 22. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=ynbA {ECO:0000313|EMBL:AHM56290.1}; GN Synonyms=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=EAL2_c09910 {ECO:0000313|EMBL:AHM56290.1}; OS Peptoclostridium acidaminophilum DSM 3953. OC Bacteria; Firmicutes; Clostridia; Clostridiales; OC Peptostreptococcaceae; Peptoclostridium. OX NCBI_TaxID=1286171 {ECO:0000313|EMBL:AHM56290.1, ECO:0000313|Proteomes:UP000019591}; RN [1] {ECO:0000313|EMBL:AHM56290.1, ECO:0000313|Proteomes:UP000019591} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 3953 {ECO:0000313|EMBL:AHM56290.1, RC ECO:0000313|Proteomes:UP000019591}; RX PubMed=24926057; RA Poehlein A., Andreesen J.R., Daniel R.; RT "Complete Genome Sequence of Amino Acid-Utilizing Eubacterium RT acidaminophilum al-2 (DSM 3953)."; RL Genome Announc. 2:e00573-14(2014). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP007452; AHM56290.1; -; Genomic_DNA. DR RefSeq; WP_025435301.1; NZ_CP007452.1. DR EnsemblBacteria; AHM56290; AHM56290; EAL2_c09910. DR KEGG; eac:EAL2_c09910; -. DR PATRIC; fig|1286171.3.peg.941; -. DR KO; K03665; -. DR Proteomes; UP000019591; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000019591}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000019591}. FT DOMAIN 201 371 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 160 194 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 426 AA; 48372 MW; C7EB42A934F8E63B CRC64; MEEKKEKILI VGLNITDIKK KSQFEMEASM DELEELVEAA GGEVVARLTQ NRPSRDAAYY IGTGKAEEVR DYVEKLEADM VVFNDELSGV QIRNLEDAVG VTVLDRTALI LDIFAQRALS REGKMQVELA QLKYRRSRLI GLGKQLSRTG GGIGTRGPGE KKLETDRRHI EGRINDIKKE LADVRRNREV QRGQRMKANV PIVALVGYTN AGKSSLLNSL IKTHREYSAE KEVFSKDMLF ATLDVTLRKA VLPSGKEFLV TDTVGFVSNL PHDLVEAFKA TLEEVKYADL IVHVVDASNE NYDMQMDTTL DILKQLDSLD KDIITVFNKM DKMGFEADYP KQEDMVFISC KTGYNMDLLV DMIEKKLLKS FTKAKLLIPF ERGDIFNSIQ KKSQVEHFEY VENGISVTAL LSDEDYNRYR EFVLEQ // ID W8VBA3_YEREN Unreviewed; 433 AA. AC W8VBA3; DT 14-MAY-2014, integrated into UniProtKB/TrEMBL. DT 14-MAY-2014, sequence version 1. DT 30-AUG-2017, entry version 22. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:AHM76055.1}; GN ORFNames=LC20_04802 {ECO:0000313|EMBL:AHM76055.1}; OS Yersinia enterocolitica LC20. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; OC Yersiniaceae; Yersinia. OX NCBI_TaxID=1443113 {ECO:0000313|EMBL:AHM76055.1, ECO:0000313|Proteomes:UP000019587}; RN [1] {ECO:0000313|EMBL:AHM76055.1, ECO:0000313|Proteomes:UP000019587} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=LC20 {ECO:0000313|EMBL:AHM76055.1, RC ECO:0000313|Proteomes:UP000019587}; RA Shi G., Su M., Liang J., Gu W., Xiao Y., Zhang Z., Qiu H., Duan R., RA Zhang Z., Li Y., Zhang X., Ling Y., Song L., Chen M., Zhao Y., Wu J., RA Jing H., Xiao J., Wang X.; RT "The complete genome sequence and comparative genome analysis of RT Yersinia enterocolitica strain LC20."; RL Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP007448; AHM76055.1; -; Genomic_DNA. DR EnsemblBacteria; AHM76055; AHM76055; LC20_04802. DR KEGG; yel:LC20_04802; -. DR PATRIC; fig|1443113.3.peg.4721; -. DR KO; K03665; -. DR Proteomes; UP000019587; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000019587}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}. FT DOMAIN 198 365 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 433 AA; 48386 MW; 3B9A8281BE311CA2 CRC64; MFDRYEAGEQ AVLVHIYFSQ DKNSEDLREF EALVSSAGVE ALQIVTGSRK APHPKFFVGE GKAEEIADAV KASGASVVLF DHALSAAQER NLERLCECRV IDRTGLILDI FAQRARTHEG KLQVELAQLR HIATRLVRGW THLERQKGGI GLRGPGETQL ETDRRLLRDR ISLILSRLDR VAKQREQGRR ARTRADIPTV SLVGYTNAGK SSLFNKITAA DVYAADQLFA TLDPTLRRIN VADVGDTVLA DTVGFIRHLP HDLVAAFKAT LQETRQASLL LHIIDAADPR VAENMAAVDA VLAEIEADEI PTLLVMNKID LLDDFVPRID RNEENLPVRV WLSAQTGAGI PLLFQALTER LSGEIAHFEL RLPPQAGRLR SRFYQLQAIE KEWIDEDGNV GMVVRMPIVD WRRLCKQEQD LVSYIVSEPN SGN // ID W8VZP5_9FLAO Unreviewed; 404 AA. AC W8VZP5; DT 14-MAY-2014, integrated into UniProtKB/TrEMBL. DT 14-MAY-2014, sequence version 1. DT 07-JUN-2017, entry version 21. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=NMS_0927 {ECO:0000313|EMBL:BAO54936.1}; OS Nonlabens marinus S1-08. OC Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales; OC Flavobacteriaceae; Nonlabens. OX NCBI_TaxID=1454201 {ECO:0000313|EMBL:BAO54936.1, ECO:0000313|Proteomes:UP000031760}; RN [1] {ECO:0000313|EMBL:BAO54936.1, ECO:0000313|Proteomes:UP000031760} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=S1-08 {ECO:0000313|EMBL:BAO54936.1}; RX PubMed=24706784; DOI=10.1073/pnas.1403051111; RA Yoshizawa S., Kumagai Y., Kim H., Ogura Y., Hayashi T., Iwasaki W., RA DeLong E.F., Kogure K.; RT "Functional characterization of flavobacteria rhodopsins reveals a RT unique class of light-driven chloride pump in bacteria."; RL Proc. Natl. Acad. Sci. U.S.A. 111:6732-6737(2014). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AP014548; BAO54936.1; -; Genomic_DNA. DR RefSeq; WP_041495627.1; NZ_AP014548.1. DR EnsemblBacteria; BAO54936; BAO54936; NMS_0927. DR Proteomes; UP000031760; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000031760}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000031760}. FT DOMAIN 200 385 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 404 AA; 46644 MW; 81A4D8C9B98E377A CRC64; MLETDNHEYE KAILIGVITQ SQDEEKLNEY MDELEFLAFT AGATVHKRFS QKMAKPNPKT FIGTGKMEEI HAYVKAHDID TIIFDDELSP AQQRNIEKVL EAKIIDRTYL ILDIFAQRAQ TSYARTQVEL AQYEYLLPRL VGLWTHLERQ KGGIGMRGPG ETEIETDRRI VRDRITLLKA KLIKIDKQMA TQRGNRGQLV RVALVGYTNV GKSTLMNVVS KSDVFAENKL FATLDTTVRK VVVGNLPFLL TDTVGFIRKL PTQLVESFKS TLDEVRESDL LLHVVDISHE SFEDHIASVN KILDEIDAID KPTIMVFNKI DQYKAEEYDE SDLMTDRSSV HYSLEEWKKT WMSRMGDDVI FISAIEKENM DEFRKKVYDK VREIHVSRFP YNAFLYPDVM GEEE // ID W8X444_CASDE Unreviewed; 368 AA. AC W8X444; DT 14-MAY-2014, integrated into UniProtKB/TrEMBL. DT 14-MAY-2014, sequence version 1. DT 07-JUN-2017, entry version 23. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=BN940_08391 {ECO:0000313|EMBL:CDM24141.1}; OS Castellaniella defragrans 65Phen. OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Alcaligenaceae; Castellaniella. OX NCBI_TaxID=1437824 {ECO:0000313|EMBL:CDM24141.1, ECO:0000313|Proteomes:UP000019805}; RN [1] {ECO:0000313|EMBL:CDM24141.1, ECO:0000313|Proteomes:UP000019805} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=65Phen {ECO:0000313|EMBL:CDM24141.1}; RX PubMed=24952578; DOI=10.1186/1471-2180-14-164; RA Petasch J., Disch E.M., Markert S., Becher D., Schweder T., Huttel B., RA Reinhardt R., Harder J.; RT "The oxygen-independent metabolism of cyclic monoterpenes in RT Castellaniella defragrans 65Phen."; RL BMC Microbiol. 14:164-164(2014). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; HG916765; CDM24141.1; -; Genomic_DNA. DR RefSeq; WP_043681928.1; NZ_HG916765.1. DR EnsemblBacteria; CDM24141; CDM24141; BN940_08391. DR KEGG; cdn:BN940_08391; -. DR PATRIC; fig|1437824.5.peg.1657; -. DR KO; K03665; -. DR Proteomes; UP000019805; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000019805}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000019805}. FT DOMAIN 190 356 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 368 AA; 40659 MW; 553F6D47E510D2E9 CRC64; MKSLVISVDL GEPDYAAHAE EFLMLASGAG ADIVEVLTAR RSRPDAAGFI GSGKIEEATA LVKATRAEVV LFDQALTPAQ QRNLERHFEV RVVDRVALIL DIFALRAKSH EGKLQVELAQ LQHLSTRLTR MWTHLERQRG GIGVRGPGES QLETDRRLIG VRVRALKERL ERVQRQRLTQ RRARVRGKTL SVSLVGYTNA GKSTLFNALT RADAYAADQL FATLDTTTRR VWIEGAGQVV VSDTVGFIRS LPPMLIAAFR ATLEETVHAD LLLHVIDAAS PQRDEQAAAV NQVLRDIDAH EIPQILVYNK IDVAGYEPRV ERNEHGTIAR VFVSALQRSG LDGLRQSIVE FGGEPTGNNA FDETVQPE // ID W9A8S4_9BACI Unreviewed; 411 AA. AC W9A8S4; DT 14-MAY-2014, integrated into UniProtKB/TrEMBL. DT 14-MAY-2014, sequence version 1. DT 07-JUN-2017, entry version 22. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:CDO02149.1}; GN ORFNames=BN988_00606 {ECO:0000313|EMBL:CDO02149.1}, GN OPHB3_1263 {ECO:0000313|EMBL:GAQ17338.1}; OS Oceanobacillus picturae. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; OC Oceanobacillus. OX NCBI_TaxID=171693 {ECO:0000313|EMBL:CDO02149.1, ECO:0000313|Proteomes:UP000028863}; RN [1] {ECO:0000313|EMBL:CDO02149.1, ECO:0000313|Proteomes:UP000028863} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=S1 {ECO:0000313|EMBL:CDO02149.1, RC ECO:0000313|Proteomes:UP000028863}; RA Croce O., Lagier J.C., Raoult D.; RT "Draft genome sequencing of Oceanobacillus picturae strain S1 isolated RT from human gut."; RL Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:CDO02149.1, ECO:0000313|Proteomes:UP000028863} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=S1 {ECO:0000313|EMBL:CDO02149.1, RC ECO:0000313|Proteomes:UP000028863}; RA Urmite Genomes U.; RL Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases. RN [3] {ECO:0000313|Proteomes:UP000052946} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Heshi-B3 {ECO:0000313|Proteomes:UP000052946}; RA Akuzawa S., Nakagawa J., Kanekatsu T., Kanesaki Y., Suzuki T.; RT "Draft Genome Sequence of Oceanobacillus picturae Heshi-B3 that Was RT Isolated from Fermented Rice Bran with Aging Salted Mackerel, Which RT Was Named Heshiko as Traditional Fermented Seafood in Japan."; RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases. RN [4] {ECO:0000313|EMBL:GAQ17338.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=Heshi-B3 {ECO:0000313|EMBL:GAQ17338.1}; RA Akuzawa S., Nagaoka J., Kanekatsu M., Kanesaki Y., Suzuki T.; RT "Draft Genome Sequence of Oceanobacillus picturae Heshi-B3, Isolated RT from Fermented Rice Bran in a Traditional Japanese Seafood Dish."; RL Genome Announc. 4:e01621-15(2016). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:CDO02149.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CCAX010000001; CDO02149.1; -; Genomic_DNA. DR EMBL; BBXV01000014; GAQ17338.1; -; Genomic_DNA. DR RefSeq; WP_036572967.1; NZ_CCAX010000001.1. DR EnsemblBacteria; CDO02149; CDO02149; BN988_00606. DR EnsemblBacteria; GAQ17338; GAQ17338; OPHB3_1263. DR Proteomes; UP000028863; Unassembled WGS sequence. DR Proteomes; UP000052946; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000028863}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000028863}. FT DOMAIN 195 323 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 411 AA; 47041 MW; 3A6A360E694883CF CRC64; MSEKILIIAV NKKQQNEAKF QSSLDELISL SETAGGNVES IMTQNRDRID PAHYIGTGKV QEIKEAITEL GIDLVISNDE LSAGQLRNLG AEFGVRIIDR SQLILDIFAQ RARTKEGKLQ VELAQHEYTL PRLRGQGIEM SRLGAGIGTR GPGETKLESD QRHIRRRIYD IKRRLETIVR QREQYRKRRK SNEAFQIAIV GYTNAGKSTL FNRLTNSSSL EENQLFATLD PLTRQIQLPS GFQALITDTV GFMQDLPTAL IAAFRSTLEE VKEADFLLHV VDVSHPDQEQ QQDTVIKLLD ELDAGSIPML TIYNKEDRLN GEEVIPMQHP YFFMSAYQQK DIDNMLSKVE TILQEIWKPY NVQLGPEEGK QLNRLEQETL IIRKEFEETT NRYVLQGYIK QDHPLRGFLE E // ID W9AZ73_9MYCO Unreviewed; 468 AA. AC W9AZ73; DT 14-MAY-2014, integrated into UniProtKB/TrEMBL. DT 14-MAY-2014, sequence version 1. DT 07-JUN-2017, entry version 23. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=BN977_05690 {ECO:0000313|EMBL:CDO10853.1}; OS Mycobacterium cosmeticum. OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae; OC Mycobacterium. OX NCBI_TaxID=258533 {ECO:0000313|EMBL:CDO10853.1, ECO:0000313|Proteomes:UP000028870}; RN [1] {ECO:0000313|EMBL:CDO10853.1, ECO:0000313|Proteomes:UP000028870} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 44829 {ECO:0000313|EMBL:CDO10853.1, RC ECO:0000313|Proteomes:UP000028870}; RA Croce O., Robert C., Raoult D., Drancourt M.; RT "Draft Genome Sequence of Mycobacterium cosmeticum DSM 44829."; RL Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:CDO10853.1, ECO:0000313|Proteomes:UP000028870} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 44829 {ECO:0000313|EMBL:CDO10853.1, RC ECO:0000313|Proteomes:UP000028870}; RA Urmite Genomes U.; RL Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:CDO10853.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CCBB010000003; CDO10853.1; -; Genomic_DNA. DR RefSeq; WP_024449741.1; NZ_CCBB010000003.1. DR EnsemblBacteria; CDO10853; CDO10853; BN977_05690. DR Proteomes; UP000028870; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000028870}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000028870}. FT DOMAIN 245 414 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 204 238 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 468 AA; 50344 MW; 67E80E8E7BC041F6 CRC64; MTRPENSVPS TGDLALEDRT ALRRVAGLST ELADITEVEY RQLRLERVVL VGVWTEGSAA DAEASLAELA ALAETAGSEV LEGLIQRRDK PDPSTYIGSG KAQELRETVL ATGADTVICD GELSPAQLNA LEKAVKVKVI DRTALILDIF AQHATSREGK AQVSLAQMEY MLPRLRGWGE SMSRQAGGRA GGAGGGVGTR GPGETKIETD RRRIRERMSK LRREIREMKK VRDTQRGKRR AADMPSVAIV GYTNAGKSSL LNALTGAGVL VENALFATLE PTTRRGQLDD GRPFVLTDTV GFVRHLPTQL VEAFRSTLEE VVDADLLVHV VDGSDANPMA QISAVREVIR DVYADHGGAP ATELLVINKI DAAGDLALAQ LRRALPDAVF VSAHTGEGLD QLRRRMAALV EPTDTAIDVT IPYDRGDLVA RVHADGRIES TEHTADGTRI IGRVPVSLAA TLRDYPSG // ID W9E722_RHILI Unreviewed; 463 AA. AC W9E722; DT 14-MAY-2014, integrated into UniProtKB/TrEMBL. DT 14-MAY-2014, sequence version 1. DT 07-JUN-2017, entry version 21. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=MesloDRAFT_1914 {ECO:0000313|EMBL:ETA73016.1}; OS Mesorhizobium loti R7A. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Phyllobacteriaceae; Mesorhizobium. OX NCBI_TaxID=935547 {ECO:0000313|EMBL:ETA73016.1, ECO:0000313|Proteomes:UP000053249}; RN [1] {ECO:0000313|EMBL:ETA73016.1, ECO:0000313|Proteomes:UP000053249} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=R7A {ECO:0000313|EMBL:ETA73016.1, RC ECO:0000313|Proteomes:UP000053249}; RG DOE Joint Genome Institute; RA Kyrpides N., Huntemann M., Han J., Chen A., Mavromatis K., RA Markowitz V., Palaniappan K., Ivanova N., Schaumberg A., Pati A., RA Liolios K., Nordberg H.P., Cantor M.N., Hua S.X., Woyke T.; RL Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:ETA73016.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AZAM01000001; ETA73016.1; -; Genomic_DNA. DR RefSeq; WP_032930226.1; NZ_KI632510.1. DR EnsemblBacteria; ETA73016; ETA73016; MesloDRAFT_1914. DR PATRIC; fig|935547.3.peg.1924; -. DR Proteomes; UP000053249; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000053249}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000053249}. FT DOMAIN 231 404 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 190 217 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 463 AA; 50829 MW; 0CBA2968177BD0EC CRC64; MAREKDADAT VRGKPAHHPG TEAKGPTRAV VIVPVLTRQP RGDDDTNRPR LTRSADARHD EAVGLARAIN LDPVHTAVVT VNDPRPATLL GSGKVEEFAQ IVKDNDAELV IVDHPLTPVQ QRNLEKELHA KVLDRTGLIL EIFGERARTK EGTLQVELAH LNYQKGRLVR SWTHLERQRG GAGFLGGPGE TQIESDRRQL QEKIIKLKHE LETVRRTRDL HRAKRKKVPF PVVAIVGYTN AGKSTLFNRL TGADVLAQDM LFATLDPTLR RVRLPHGTPI ILSDTVGFIS DLPTHLIAAF RATLEEVVEA DLVIHLRDIS DPDTAAQAED VERILADLGV DAGDTKRVIE VWNKVDLLDE GNRSRLLADA VGGSKGPPIA ISAVTGEGID ALKAVIETRM AGELEDLTVT IEPAQFGLVD WLYRNGDIVS RADNEDGSAT ISLKATQSAR EEIESRLRRK NNG // ID W9EHT3_9LACO Unreviewed; 420 AA. AC W9EHT3; DT 14-MAY-2014, integrated into UniProtKB/TrEMBL. DT 14-MAY-2014, sequence version 1. DT 07-JUN-2017, entry version 20. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=B808_275 {ECO:0000313|EMBL:ETO40816.1}; OS Lactobacillus florum 8D. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; OC Lactobacillus. OX NCBI_TaxID=1221538 {ECO:0000313|EMBL:ETO40816.1, ECO:0000313|Proteomes:UP000019474}; RN [1] {ECO:0000313|EMBL:ETO40816.1, ECO:0000313|Proteomes:UP000019474} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=8D {ECO:0000313|EMBL:ETO40816.1, RC ECO:0000313|Proteomes:UP000019474}; RA Kim E.B., Marco M.L.; RT "Genome sequencing of Lactobacillus florum 8D."; RL Submitted (AUG-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:ETO40816.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ALXG01000013; ETO40816.1; -; Genomic_DNA. DR RefSeq; WP_009166871.1; NZ_ALXG01000013.1. DR EnsemblBacteria; ETO40816; ETO40816; B808_275. DR PATRIC; fig|1221538.3.peg.283; -. DR Proteomes; UP000019474; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000019474}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000019474}. FT DOMAIN 197 365 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 420 AA; 46501 MW; 02A42DDEB5780619 CRC64; MEQNINTIII GLNLDQADFN YSMEELEQLT TANHLKTVGK VTQKLPHPEA ATYFGKGKVE EVAQLVVTTN ASTIIANDEL SPSQIRNLEK ATNATVMDRT GLILEIFATR AHTREAKLQV ELAKLKYQLP RLRTGASQHL DQQSAGGGLA NRGTGETKLE LNRRTIEHQI NHVRHELKES EQSHATQRKR RAESHLKTVA LVGYTNAGKS TIMNQLVQRF GENEDKQVFV KNMLFATLDT SVRKLELPGH RSCLLSDTVG FVSKLPHQLV AAFQSTLSEA AQADLLLQVV DYSDPNQALM METTNATLQE IGVPELPMIT VFNKADLAGT AYPIRTGHEI IISAKDEHSI DLLVETITTQ LFADEVVKSF TIPFADGAVV ESLNRQFAVQ QTDYTEAGTV LTVRLPQAAV GRYQKYLTSN // ID W9GF54_9MICO Unreviewed; 489 AA. AC W9GF54; DT 14-MAY-2014, integrated into UniProtKB/TrEMBL. DT 14-MAY-2014, sequence version 1. DT 07-JUN-2017, entry version 24. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=N865_17185 {ECO:0000313|EMBL:EWT03458.1}; OS Intrasporangium oryzae NRRL B-24470. OC Bacteria; Actinobacteria; Micrococcales; Intrasporangiaceae; OC Intrasporangium. OX NCBI_TaxID=1386089 {ECO:0000313|EMBL:EWT03458.1, ECO:0000313|Proteomes:UP000019489}; RN [1] {ECO:0000313|EMBL:EWT03458.1, ECO:0000313|Proteomes:UP000019489} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NRRL B-24470 {ECO:0000313|EMBL:EWT03458.1, RC ECO:0000313|Proteomes:UP000019489}; RA Liu H., Wang G.; RT "Intrasporangium oryzae NRRL B-24470."; RL Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EWT03458.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AWSA01000002; EWT03458.1; -; Genomic_DNA. DR RefSeq; WP_034800645.1; NZ_AWSA01000002.1. DR ProteinModelPortal; W9GF54; -. DR EnsemblBacteria; EWT03458; EWT03458; N865_17185. DR PATRIC; fig|1386089.3.peg.264; -. DR Proteomes; UP000019489; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000019489}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000019489}. FT DOMAIN 268 433 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 489 AA; 53431 MW; AF9A2938ABF0AE2D CRC64; MTRKNTTNTD LFATRAEALA DDIHEADESA LLYDGDQLDR EERAALRRVG GLSTELEDIT EVEYRQLRLE RVVLAAVWTE GSAEDAENSI RELAALAETA GSTVLEGVIQ RRQRPDPATY LGKGKALELR DIVVAEGADT VICDGELAPS QRRALEDVVK VKVIDRTALI LDIFAQHAKS REGKAQVELA QLQYLLPRLR GWGESMSRQA GGRVAGGEGI GSRGPGETKI ELDRRRINTK IAKLRRDIKD MKTSRDTKRH GRRAGGIPSV AIAGYTNAGK SSLLNRLTGA GVLVQNQLFA TLDPTVRRAE TEDGRVYTLA DTVGFVRSLP HQLVEAFRST LEEVGDADLL LHVVDGSHPD PEGQISAVRE VLAEVGGDRI KEVIVVNKAD IADPDVLDRL RRHEKHCITV SARTGAGIDE LLALVARELP KPDIEVEVLV PYHRGDLISR IHEDGEILES EHVAEGTRVR AKVTPAIEAD LTAYAVVAS // ID W9GL11_9MICO Unreviewed; 487 AA. AC W9GL11; DT 14-MAY-2014, integrated into UniProtKB/TrEMBL. DT 14-MAY-2014, sequence version 1. DT 07-JUN-2017, entry version 22. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=N864_04485 {ECO:0000313|EMBL:EWT05488.1}; OS Intrasporangium chromatireducens Q5-1. OC Bacteria; Actinobacteria; Micrococcales; Intrasporangiaceae; OC Intrasporangium. OX NCBI_TaxID=584657 {ECO:0000313|EMBL:EWT05488.1, ECO:0000313|Proteomes:UP000019494}; RN [1] {ECO:0000313|Proteomes:UP000019494} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Q5-1 {ECO:0000313|Proteomes:UP000019494}; RA Liu H., Wang G.; RT "Intrasporangium oryzae NRRL B-24470."; RL Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EWT05488.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AWQS01000109; EWT05488.1; -; Genomic_DNA. DR RefSeq; WP_034717475.1; NZ_AWQS01000109.1. DR EnsemblBacteria; EWT05488; EWT05488; N864_04485. DR PATRIC; fig|584657.3.peg.2630; -. DR Proteomes; UP000019494; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 2. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000019494}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000019494}. FT DOMAIN 268 433 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 487 AA; 53099 MW; 29FEEA319F067ACF CRC64; MTNQHLTSSD LFATRAEALA EDALEASTAT YDYDGEQLER EERAALRRVG GLSTELEDIT EVEYRQLRLE RVVLAGVWSE GTLEDAENSL RELAALAETA GSTVLEGVVQ RRQRPDPATY LGKGKAQELR DIVLAGGADT VICDGELAPS QRRALEDVVK VKVIDRTALI LDIFAQHAKS REGKAQVELA QLQYLLPRLR GWGDSMSRQA GGRVAGGEGI GSRGPGETKI ELDRRRINTK IAKLRRDIKA MKTVRDTKRH GRRAVGVPSV AIAGYTNAGK SSLLNRLTGA GVLVQNQLFA TLDPTVRRAE TPDGRLYTLS DTVGFVRSLP HQLVEAFRST LEEVGDADLL LHVVDGSHPD PEGQISAVRE VLADVGGDSI KEVIVVNKAD IADPEVLDRI RRHEKHSIAV SARTGAGIEE LRELIAAELP KPDIEVDVLV PYDRGDLVSR LHEEAEILES EHVADGTRVR AKVTPAIEAD LSEYVVA // ID W9H7Q4_9PROT Unreviewed; 440 AA. AC W9H7Q4; DT 14-MAY-2014, integrated into UniProtKB/TrEMBL. DT 14-MAY-2014, sequence version 1. DT 07-JUN-2017, entry version 21. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=N825_20425 {ECO:0000313|EMBL:EWY42260.1}; OS Skermanella stibiiresistens SB22. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales; OC Rhodospirillaceae; Skermanella. OX NCBI_TaxID=1385369 {ECO:0000313|EMBL:EWY42260.1, ECO:0000313|Proteomes:UP000019486}; RN [1] {ECO:0000313|EMBL:EWY42260.1, ECO:0000313|Proteomes:UP000019486} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SB22 {ECO:0000313|EMBL:EWY42260.1, RC ECO:0000313|Proteomes:UP000019486}; RA Zhu W., Wang G.; RT "The genome sequence of Skermanella stibiiresistens."; RL Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EWY42260.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AVFL01000002; EWY42260.1; -; Genomic_DNA. DR EnsemblBacteria; EWY42260; EWY42260; N825_20425. DR PATRIC; fig|1385369.3.peg.1006; -. DR Proteomes; UP000019486; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000019486}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000019486}. FT DOMAIN 211 382 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 184 207 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 440 AA; 48927 MW; 84BF47BE7F89F7B6 CRC64; MGTGRALVIH PILRETRRSE ASSEGGARSP EARLDEAVGL ASAIDLTVVH AEAIKVNKPQ PATLLGSGVV EHFAELIREA EENEQPIDLV VMDHALSPVQ QRNLERGLKA KVIDRTGLIL EIFGARARTK EGQLQVELAA LTYQRSRLVR SWTHLERQRG GFGFLGGPGE SQLEIDRRLI GDRIIKLKRE LEEVRRTRDL HRKARERVPY PVVALVGYTN AGKSSLFNRM AGSDVFAKDL LFATLDPTMR GIELPTGRRV ILSDTVGFIS DLPTHLVASF RATLEEVQAA DIILHVRDIA HPDTEAQKAD VESVLRDLGI DREQDGRVVE VLNKIDLLDP ETRNGLLAQA ARNDNMQAVS ALTGEGLPEL FGLLDRHMTA DRQTVDLSVR IEDGAALAWL HQKGDVLERR DDESFAHLRI ALDPADLARF ESRYDYHPAR // ID W9S403_9ROSA Unreviewed; 507 AA. AC W9S403; DT 14-MAY-2014, integrated into UniProtKB/TrEMBL. DT 14-MAY-2014, sequence version 1. DT 07-JUN-2017, entry version 15. DE SubName: Full=GTPase HflX {ECO:0000313|EMBL:EXC25037.1}; GN ORFNames=L484_021908 {ECO:0000313|EMBL:EXC25037.1}; OS Morus notabilis. OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae; OC Pentapetalae; rosids; fabids; Rosales; Moraceae; Morus. OX NCBI_TaxID=981085 {ECO:0000313|EMBL:EXC25037.1, ECO:0000313|Proteomes:UP000030645}; RN [1] {ECO:0000313|Proteomes:UP000030645} RP NUCLEOTIDE SEQUENCE. RA He N., Zhao S.; RT "Draft Genome Sequence of a Mulberry Tree, Morus notabilis C.K. RT Schneid."; RL Submitted (JAN-2013) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; KE346040; EXC25037.1; -; Genomic_DNA. DR RefSeq; XP_010110019.1; XM_010111717.1. DR GeneID; 21404746; -. DR Proteomes; UP000030645; Unassembled WGS sequence. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 2. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000030645}; KW Reference proteome {ECO:0000313|Proteomes:UP000030645}. FT DOMAIN 284 450 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 507 AA; 56770 MW; F1348139A5313404 CRC64; MTACFSSFLL RPSITTTELC FPWHPPNPNR KIYPIILRKD SNFSPRIFAR VLQQGTGVVS PDEFSLQTPP VETKGDEKKD AHRVFDEFVV ADSESEDKAL SSSTRAKKKR ESEDGFKNRF KLRNGREVFE ERAYLVGVER KGDTENSFGI EESLKELTQL ASPNPRTYIG SGKVAEIKSA IYALGVETVI FDDELSAGQL RNLEKTFGGD VALAQMEYQL PRLTKMWAHL ERQAGGKVKG MGEKQIEVDK RILRTQIGVL KKELESVRKH RKQYRNRRTS VPVPVVSLVG YTNAGKSTLL NQLTGAGVLA EDKLFATLDP TTRRVQIKNG KEFLLTDTVG FIQKLPTTLV AAFRATLEEI SESSLLVHVV DISHPLAQQQ IDAVNKVLSE LDVSSIPRLM VWNKVDKVAS PETVKLEANK RDDVACISAL NGDGLLDFCN AVQEKLKDSM VWVEALIPFE KGELLSTIHQ VGMVERTEYM ENGTLVKAHV PLRFARLLTP MRQVCIT // ID W9TP67_9PSED Unreviewed; 433 AA. AC W9TP67; DT 14-MAY-2014, integrated into UniProtKB/TrEMBL. DT 14-MAY-2014, sequence version 1. DT 30-AUG-2017, entry version 24. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:EXF44639.1}; GN ORFNames=BAY1663_02961 {ECO:0000313|EMBL:EXF44639.1}; OS Pseudomonas sp. BAY1663. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=1439940 {ECO:0000313|EMBL:EXF44639.1, ECO:0000313|Proteomes:UP000019475}; RN [1] {ECO:0000313|EMBL:EXF44639.1, ECO:0000313|Proteomes:UP000019475} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BAY1663 {ECO:0000313|EMBL:EXF44639.1, RC ECO:0000313|Proteomes:UP000019475}; RA Gyula P., Szabo Z., Robotka H., Bihari Z.; RT "Genome sequencing of Pseudomonas sp. BAY1663."; RL Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EXF44639.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AZSV01000041; EXF44639.1; -; Genomic_DNA. DR EnsemblBacteria; EXF44639; EXF44639; BAY1663_02961. DR PATRIC; fig|1439940.3.peg.2923; -. DR Proteomes; UP000019475; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000019475}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000019475}. FT DOMAIN 199 366 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 165 192 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 433 AA; 48587 MW; BDBD046DDF24AF87 CRC64; MFFERPGGGE RAILVHLDGQ DPAAREDPQE FQELARSAGA EAVGFVNVAR HQPSAKFLIG SGKVEELHDL VKEGEVELVI FNHTLTPSQE RNLERALECR VLDRTGLILD IFAQRARTHE GKLQVELAQL EHMSTRLVRG WTHLERQKGG IGLRGPGETQ LETDRRLLRV RIRQIKQRLE KVRGQREQAR RGRRRADIPS VSLVGYTNAG KSTLFNALTE SEVFAANQLF ATLDPTLRRL ELEDVGAVVL ADTVGFIRHL PHKLVESFRA TLEESSNADL LLHVIDAHEP ERDQQIEQVL AVLGEIGAQE LPLLEVYNKV DLMDGIEPQI QRDADGRPQR VWVSAREGLG LDLLRQAIAE LLGDDLFVGT LCLPQRLGRL RAQLFELGAV QRESHDEEGG SLLEIRLPRI ELNRLISRAG LPLGAFLEQH TLQ // ID W9UY31_9GAMM Unreviewed; 434 AA. AC W9UY31; DT 14-MAY-2014, integrated into UniProtKB/TrEMBL. DT 14-MAY-2014, sequence version 1. DT 07-JUN-2017, entry version 21. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:EXJ12153.1}; GN ORFNames=D791_01042 {ECO:0000313|EMBL:EXJ12153.1}; OS Nitrincola nitratireducens. OC Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales; OC Nitrincola. OX NCBI_TaxID=1229521 {ECO:0000313|EMBL:EXJ12153.1, ECO:0000313|Proteomes:UP000019464}; RN [1] {ECO:0000313|EMBL:EXJ12153.1, ECO:0000313|Proteomes:UP000019464} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=AK23 {ECO:0000313|EMBL:EXJ12153.1, RC ECO:0000313|Proteomes:UP000019464}; RA Singh A., Pinnaka A.K., Vaidya B.; RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EXJ12153.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AONB01000003; EXJ12153.1; -; Genomic_DNA. DR RefSeq; WP_036508470.1; NZ_AONB01000003.1. DR EnsemblBacteria; EXJ12153; EXJ12153; D791_01042. DR PATRIC; fig|1229521.3.peg.1045; -. DR Proteomes; UP000019464; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000019464}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000019464}. FT DOMAIN 199 366 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 434 AA; 49147 MW; 8F6C9562C77E73B5 CRC64; MFFERPESGE RAILVHIDFY SESEPESPRE LEELALSAGA DPVAFLTGSR SDPSPKFFLG KGKVAELAEM VRLYEAELVI FNHSLSPAQE RNLEREIQCR VLDRTGLILD IFAQRARTHE GKLQVELAQL EHMSTRLVRG WTHLERQKGG IGLRGPGETQ LETDRRLLRV RLKSILKRLD KVRKQRDQGR RARVRASVPT VSLVGYTNAG KSTLFNSLTA SDVYAADQLF ATLDPTLRKI QLDDAGAAIL ADTVGFIRHL PHKLVEAFRA TLQETCEATL LLHVIDSYDE ERQLHIEQVN DVLTEIGADD VPTLLVYNKV DLLEQVEPRI DRDDEGVPIR VWLSAQTGAG TDLLLQAINE RLSDDVFESE LKLTPSEGQF RAQLYAANAI LSESVDDEGQ MHLKVRIQRK DFRQLLSRLQ IPFERYLSET VDYV // ID X0PLW9_9LACO Unreviewed; 376 AA. AC X0PLW9; DT 14-MAY-2014, integrated into UniProtKB/TrEMBL. DT 14-MAY-2014, sequence version 1. DT 12-APR-2017, entry version 21. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=JCM14108_2863 {ECO:0000313|EMBL:GAF37801.1}; OS Lactobacillus farraginis DSM 18382 = JCM 14108. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; OC Lactobacillus. OX NCBI_TaxID=1423743 {ECO:0000313|EMBL:GAF37801.1, ECO:0000313|Proteomes:UP000019488}; RN [1] {ECO:0000313|EMBL:GAF37801.1, ECO:0000313|Proteomes:UP000019488} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=JCM 14108 {ECO:0000313|EMBL:GAF37801.1, RC ECO:0000313|Proteomes:UP000019488}; RA Yuki M., Oshima K., Suda W., Kitahara M., Kitamura K., Iida T., RA Hattori M., Ohkuma M.; RT "Draft Genome Sequences of Two Lactobacillus Strains, L. farraginis RT JCM 14108T and L. composti JCM 14202T, Isolated from Compost of RT Distilled Shochu Residue."; RL Genome Announc. 2:e00257-14(2014). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:GAF37801.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BAKI01000047; GAF37801.1; -; Genomic_DNA. DR EnsemblBacteria; GAF37801; GAF37801; JCM14108_2863. DR Proteomes; UP000019488; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000019488}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000019488}. FT DOMAIN 203 371 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 376 AA; 41900 MW; 3A986DD2F8B2BC61 CRC64; MDLTQTLTPV VTIGLSQHPN SFDYAMTELN NLVQANNMDV VETLVQKLDK PDPATYFGKG KIEELTQVVI DDGVKTIVAN DELSPSQIRN IEKATKARII DRTGLILEIF ANRAQSREAK LQVELAKLKY QLPRLHTSAS QRLDQQTGTS SGGGFTNRGA GESQYELDRR TLEKRITHVN RELKEAGKAD QIKRKQRDKS DIPTVALVGY TNAGKSTIMN GMINLYGEND DKQVMVKNML FATLDTSVRK LSLPDQKKFL LSDTVGFVSQ LPHQLVQAFK STLAEAANAD LLVQVVDYAD PHRDMMIKTT EETLKEIGVD NVPMIVAFNK ADKLDVTFPT REGDNLIMAA NDTSSLKELA AIIKEKVFKT TRRCRC // ID X0PVY8_9LACO Unreviewed; 424 AA. AC X0PVY8; DT 14-MAY-2014, integrated into UniProtKB/TrEMBL. DT 14-MAY-2014, sequence version 1. DT 07-JUN-2017, entry version 27. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=FC83_GL002165 {ECO:0000313|EMBL:KRM34390.1}; OS Lactobacillus composti DSM 18527 = JCM 14202. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; OC Lactobacillus. OX NCBI_TaxID=1423734 {ECO:0000313|EMBL:KRM34390.1, ECO:0000313|Proteomes:UP000051236}; RN [1] {ECO:0000313|EMBL:KRM34390.1, ECO:0000313|Proteomes:UP000051236} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 18527 {ECO:0000313|EMBL:KRM34390.1, RC ECO:0000313|Proteomes:UP000051236}; RX PubMed=26415554; DOI=10.1038/ncomms9322; RA Sun Z., Harris H.M., McCann A., Guo C., Argimon S., Zhang W., Yang X., RA Jeffery I.B., Cooney J.C., Kagawa T.F., Liu W., Song Y., Salvetti E., RA Wrobel A., Rasinkangas P., Parkhill J., Rea M.C., O'Sullivan O., RA Ritari J., Douillard F.P., Paul Ross R., Yang R., Briner A.E., RA Felis G.E., de Vos W.M., Barrangou R., Klaenhammer T.R., RA Caufield P.W., Cui Y., Zhang H., O'Toole P.W.; RT "Expanding the biotechnology potential of lactobacilli through RT comparative genomics of 213 strains and associated genera."; RL Nat. Commun. 6:8322-8322(2015). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KRM34390.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AZGA01000026; KRM34390.1; -; Genomic_DNA. DR RefSeq; WP_035455679.1; NZ_BAMK01000043.1. DR EnsemblBacteria; KRM34390; KRM34390; FC83_GL002165. DR PATRIC; fig|1423734.3.peg.2186; -. DR Proteomes; UP000051236; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000051236}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000051236}. FT COILED 159 193 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 424 AA; 47196 MW; DED1677FA36BEF88 CRC64; MQKIADEKLK VILGGVNLGT ENFDYTMSEL AQLAAANNLD VVDTIVQNSD KIIAGTYFGT GKVTDIKETA QDTDAKLLVL NDELTPSQIR NLENLTKLYV IDRTGLILRI FADRAQTKLA KTQVEIARLQ YELPRIHPSS NPLDQQSASG GLANRGAGET QLELDRRVLR KRISRLQNEL KQLMQSQDVQ SKERQKSLIP KVALVGYTNA GKSTIMNALL AHYDQDAAEK QVMVKDMLFA TLDTSVRQIN LPNQLSFLLS DTVGFVSKLP HNLVESFKAT LAEASNADLL LHVVDYANPN YQEMMDVTDK VLHQLGITDI PVIEVYNKAD KTDMTYPTVT GNEIYLSAKD DASIERLSDM IQQRLFANNP VVTLLIPFTK GNVTEYVTSH ARIIDRDYTN DGTQLKVQLA PEVLGKVKAY VVTE // ID X0R682_9BACI Unreviewed; 430 AA. AC X0R682; DT 14-MAY-2014, integrated into UniProtKB/TrEMBL. DT 14-MAY-2014, sequence version 1. DT 07-JUN-2017, entry version 24. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=BTS2_1477 {ECO:0000313|EMBL:GAF64584.1}; OS Bacillus sp. TS-2. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus. OX NCBI_TaxID=1450694 {ECO:0000313|EMBL:GAF64584.1, ECO:0000313|Proteomes:UP000019504}; RN [1] {ECO:0000313|EMBL:GAF64584.1, ECO:0000313|Proteomes:UP000019504} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=TS-2 {ECO:0000313|EMBL:GAF64584.1, RC ECO:0000313|Proteomes:UP000019504}; RA Fujinami S., Takeda K., Onodera T., Satoh K., Sano M., Narumi I., RA Ito M.; RT "Draft Genome Sequence of Potassium-Dependent Alkaliphilic Bacillus RT sp. Strain TS-2, Isolated from a Jumping Spider."; RL Genome Announc. 2:e00458-14(2014). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:GAF64584.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BAWL01000008; GAF64584.1; -; Genomic_DNA. DR RefSeq; WP_045481893.1; NZ_BAWL01000008.1. DR EnsemblBacteria; GAF64584; GAF64584; BTS2_1477. DR Proteomes; UP000019504; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000019504}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000019504}. FT DOMAIN 200 332 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 159 186 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 430 AA; 49627 MW; 5B5A483159DA2B13 CRC64; MQELEQVIIV GVEEASTEQY QHERSMNELK QLAEACQLQV VAELSQKLEQ IHPTTYIGSG KLNELKLLME EKNVETVIFN DELSSSQIRN IESVLSCRVI DRTILILDIF AIRAKTKEAK LQVEIAEWQY MLPRLIGLRK SLGRQGGGGV GTFNRGAGEK KLELDRRHIE SKINSLQNDL KQLVKHRKVQ RGRRNKQGIR TVALVGYTNA GKSTLMNRFL EMDTNQTQTS KYVYEENMLF ATLETSVRKI ALPEFFPFLL TDTVGFVERL PHHLVKAFRS TLEEVKEADL LIHVVDYSNP FFEEQIEVTN HTLKEIGVKD IPMIYAYNKI DLMNEVPDYG RENTVYISTK NKKGLDSLTT IIQEQLYGEQ VVCDFLIPYE KSAIIDEMKE HALIKKWEHL ENGTFLQAQC SRHVKDKYSD WLQNESMEIQ // ID X1WE07_DANRE Unreviewed; 543 AA. AC X1WE07; DT 14-MAY-2014, integrated into UniProtKB/TrEMBL. DT 14-MAY-2014, sequence version 1. DT 30-AUG-2017, entry version 24. DE SubName: Full=GTP-binding protein 6 (putative) {ECO:0000313|Ensembl:ENSDARP00000128458}; GN Name=gtpbp6 {ECO:0000313|Ensembl:ENSDARP00000128458, GN ECO:0000313|ZFIN:ZDB-GENE-031118-62}; OS Danio rerio (Zebrafish) (Brachydanio rerio). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes; OC Cyprinidae; Danio. OX NCBI_TaxID=7955 {ECO:0000313|Ensembl:ENSDARP00000128458, ECO:0000313|Proteomes:UP000000437}; RN [1] {ECO:0000313|Ensembl:ENSDARP00000128458, ECO:0000313|Proteomes:UP000000437} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Tuebingen {ECO:0000313|Ensembl:ENSDARP00000128458, RC ECO:0000313|Proteomes:UP000000437}; RX PubMed=23594743; DOI=10.1038/nature12111; RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., RA Muffato M., Collins J.E., Humphray S., McLaren K., Matthews L., RA McLaren S., Sealy I., Caccamo M., Churcher C., Scott C., Barrett J.C., RA Koch R., Rauch G.J., White S., Chow W., Kilian B., Quintais L.T., RA Guerra-Assuncao J.A., Zhou Y., Gu Y., Yen J., Vogel J.H., Eyre T., RA Redmond S., Banerjee R., Chi J., Fu B., Langley E., Maguire S.F., RA Laird G.K., Lloyd D., Kenyon E., Donaldson S., Sehra H., RA Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M., RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J., RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G., RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P., RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., RA Clark S., Pelan S., Griffiths G., Smith M., Glithero R., Howden P., RA Barker N., Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., RA Lovell J., Beasley H., Henderson C., Gordon D., Auger K., Wright D., RA Collins J., Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., RA Leongamornlert D., McGuire S., Gilderthorp R., Griffiths C., RA Manthravadi D., Nichol S., Barker G., Whitehead S., Kay M., Brown J., RA Murnane C., Gray E., Humphries M., Sycamore N., Barker D., RA Saunders D., Wallis J., Babbage A., Hammond S., RA Mashreghi-Mohammadi M., Barr L., Martin S., Wray P., Ellington A., RA Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J., RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E., RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., RA Bird C., Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., RA Eser C., Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., RA Konantz M., Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., RA Raddatz G., Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., RA Yang F., Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., RA Searle S.M., Enright A., Geisler R., Plasterk R.H., Lee C., RA Westerfield M., de Jong P.J., Zon L.I., Postlethwait J.H., RA Nusslein-Volhard C., Hubbard T.J., Roest Crollius H., Rogers J., RA Stemple D.L.; RT "The zebrafish reference genome sequence and its relationship to the RT human genome."; RL Nature 496:498-503(2013). RN [2] {ECO:0000313|Ensembl:ENSDARP00000128458} RP IDENTIFICATION. RC STRAIN=Tuebingen {ECO:0000313|Ensembl:ENSDARP00000128458}; RG Ensembl; RL Submitted (MAR-2014) to UniProtKB. CC -!- CAUTION: The sequence shown here is derived from an Ensembl CC automatic analysis pipeline and should be considered as CC preliminary data. {ECO:0000313|Ensembl:ENSDARP00000128458}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BX323016; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BX324166; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR STRING; 7955.ENSDARP00000081167; -. DR PaxDb; X1WE07; -. DR Ensembl; ENSDART00000157317; ENSDARP00000128458; ENSDARG00000061091. DR ZFIN; ZDB-GENE-031118-62; gtpbp6. DR eggNOG; KOG0410; Eukaryota. DR eggNOG; COG2262; LUCA. DR GeneTree; ENSGT00390000001397; -. DR OMA; MDTVGFM; -. DR OrthoDB; EOG091G0852; -. DR Proteomes; UP000000437; Chromosome 6. DR Bgee; ENSDARG00000061091; -. DR ExpressionAtlas; X1WE07; baseline. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR GO; GO:0043022; F:ribosome binding; IBA:GO_Central. DR CDD; cd01878; HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 1: Evidence at protein level; KW Complete proteome {ECO:0000313|Proteomes:UP000000437}; KW Proteomics identification {ECO:0000213|PeptideAtlas:X1WE07}; KW Reference proteome {ECO:0000313|Proteomes:UP000000437}. FT DOMAIN 310 474 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 543 AA; 61449 MW; 5BEAF738C8185840 CRC64; MNLNKISVLT RHVFLCKHVL SRSYVRFAKC EVVRFPQCAS KLIVNTLPSQ SLKPGLVVPV LPARTLSLTA RMFKYDNTDD NNVEEDEIDD AEIEKLFQEQ IPSGIGKEDH RVFIVHPDVK WGSRKQYLTT AALQMEEAVG LVKTLHKWSV VDKLILSTKT PEKKRIFGKG NFQMLTEKIR ATPGVTAVFV NVERLSPSSE KDLEEAWGVK VLDRYSLVLH IFRCNAKTKE AKLQISLAEI PLFRSRLRNE VANLDQQGGG PRYIMGSGET LYEMQQRLLK ERELKIRSAL ERLRRKRNLL RSQRKHKDFP IISVMGYTNC GKTTLIKALT GDDGLQPKDQ LFATLDVTVH AGQLPCHMTV LYVDTIGFLS QLPHQLIDSF SATLEDVIHS DLIIHVRDIS HPETVSQKVN VLNVLNNLQI PERLLTSIIE VHNKIDLIEG YESSDPEVIP ISALKQCGLE ALKEKIEEAV LKCTGKQMMT LKVQLNTSQL SWLYKEATVQ AVDNVGDDCT ANVKVIISQA AYGRYRKLFQ GTAWSEKCSS VHR // ID X1WIH0_ACYPI Unreviewed; 482 AA. AC X1WIH0; DT 14-MAY-2014, integrated into UniProtKB/TrEMBL. DT 14-MAY-2014, sequence version 1. DT 07-JUN-2017, entry version 21. DE SubName: Full=Uncharacterized protein {ECO:0000313|EnsemblMetazoa:ACYPI002236-PA}; OS Acyrthosiphon pisum (Pea aphid). OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; OC Pterygota; Neoptera; Paraneoptera; Hemiptera; Sternorrhyncha; OC Aphidomorpha; Aphidoidea; Aphididae; Macrosiphini; Acyrthosiphon. OX NCBI_TaxID=7029 {ECO:0000313|EnsemblMetazoa:ACYPI002236-PA, ECO:0000313|Proteomes:UP000007819}; RN [1] {ECO:0000313|EnsemblMetazoa:ACYPI002236-PA} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=LSR1 {ECO:0000313|EnsemblMetazoa:ACYPI002236-PA}; RA Jiang H., Abraham K., Ali S., Alsbrooks S.L., Anim B.N., Anosike U.S., RA Attaway T., Bandaranaike D.P., Battles P.K., Bell S.N., Bell A.V., RA Beltran B., Bickham C., Bustamante Y., Caleb T., Canada A., RA Cardenas V., Carter K., Chacko J., Chandrabose M.N., Chavez D., RA Chavez A., Chen L., Chu H.-S., Claassen K.J., Cockrell R., Collins M., RA Cooper J.A., Cree A., Curry S.M., Da Y., Dao M.D., Das B., RA Davila M.-L., Davy-Carroll L., Denson S., Dinh H., Ebong V.E., RA Edwards J.R., Egan A., El-Daye J., Escobedo L., Fernandez S., RA Fernando P.R., Flagg N., Forbes L.D., Fowler R.G., Fu Q., Gabisi R.A., RA Ganer J., Garbino Pronczuk A., Garcia R.M., Garner T., Garrett T.E., RA Gonzalez D.A., Hamid H., Hawkins E.S., Hirani K., Hogues M.E., RA Hollins B., Hsiao C.-H., Jabil R., James M.L., Jhangiani S.N., RA Johnson B., Johnson Q., Joshi V., Kalu J.B., Kam C., Kashfia A., RA Keebler J., Kisamo H., Kovar C.L., Lago L.A., Lai C.-Y., Laidlaw J., RA Lara F., Le T.-K., Lee S.L., Legall F.H., Lemon S.J., Lewis L.R., RA Li B., Liu Y., Liu Y.-S., Lopez J., Lozado R.J., Lu J., Madu R.C., RA Maheshwari M., Maheshwari R., Malloy K., Martinez E., Mathew T., RA Mercado I.C., Mercado C., Meyer B., Montgomery K., Morgan M.B., RA Munidasa M., Nazareth L.V., Nelson J., Ng B.M., Nguyen N.B., RA Nguyen P.Q., Nguyen T., Obregon M., Okwuonu G.O., Onwere C.G., RA Orozco G., Parra A., Patel S., Patil S., Perez A., Perez Y., Pham C., RA Primus E.L., Pu L.-L., Puazo M., Qin X., Quiroz J.B., Reese J., RA Richards S., Rives C.M., Robberts R., Ruiz S.J., Ruiz M.J., RA Santibanez J., Schneider B.W., Sisson I., Smith M., Sodergren E., RA Song X.-Z., Song B.B., Summersgill H., Thelus R., Thornton R.D., RA Trejos Z.Y., Usmani K., Vattathil S., Villasana D., Walker D.L., RA Wang S., Wang K., White C.S., Williams A.C., Williamson J., Wilson K., RA Woghiren I.O., Woodworth J.R., Worley K.C., Wright R.A., Wu W., RA Young L., Zhang L., Zhang J., Zhu Y., Muzny D.M., Weinstock G., RA Gibbs R.A.; RL Submitted (JUN-2010) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EnsemblMetazoa:ACYPI002236-PA} RP IDENTIFICATION. RG EnsemblMetazoa; RL Submitted (JUN-2015) to UniProtKB. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; ABLF02023704; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR RefSeq; XP_008182077.1; XM_008183855.2. DR UniGene; Aps.50616; -. DR EnsemblMetazoa; ACYPI002236-RA; ACYPI002236-PA; ACYPI002236. DR GeneID; 103309145; -. DR KEGG; api:103309145; -. DR PhylomeDB; X1WIH0; -. DR Proteomes; UP000007819; Unassembled WGS sequence. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR CDD; cd01878; HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 4: Predicted; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000007819}; KW Reference proteome {ECO:0000313|Proteomes:UP000007819}. FT DOMAIN 259 422 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 221 248 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 482 AA; 53967 MW; 0D99480D77A6DC6C CRC64; MPGLMGRLAR TVMAGRRGRF VRWYGGGGDD DGGGGSAEDA QARELIDRQL KLAPAGGHQV LIVQPYIKWG ANKDRSTRPE VKADESRSLV RTLAEWSVTD TLLVGLTSYR KHTFFGPGNV DAIALRVARD RRITAVFVSV NVLKPIQHQH LEHRFGVPVY DRYLMVVQIF RRHAVTREAK LQVALAELPY IWSRIRGAQD GYAERLGTEA GQIALSGKLM YDDKKDLLKA YEKKLKKLVE KLRSHRQHLR HNRTNKDLPV VAVVGYTNAG KTSLVRALTG DVGLVPKDCL FATLDVTVHG GVLPSNMTVL YVDTIGFISD IPTRLIEPFV ATLEDAMFAD VIVHIRDMSH PNVIVQKSHV EETLKNLSIN PELLNSVIDV GNKVDRLDNV ERDGSSVFIS CTTGEGLDEL KKKIESQIMK ATGRRTIKIR VRTGQDEYEW LRTHTAIVNI NTDGDYSVME VIVTQSDLDV FKSLFIRKKI NN // ID X2GWD5_9GAMM Unreviewed; 431 AA. AC X2GWD5; DT 11-JUN-2014, integrated into UniProtKB/TrEMBL. DT 11-JUN-2014, sequence version 1. DT 30-AUG-2017, entry version 23. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=GAPWK_0021 {ECO:0000313|EMBL:AHN24600.1}; OS Gilliamella apicola. OC Bacteria; Proteobacteria; Gammaproteobacteria; Orbales; Orbaceae; OC Gilliamella. OX NCBI_TaxID=1196095 {ECO:0000313|EMBL:AHN24600.1, ECO:0000313|Proteomes:UP000019656}; RN [1] {ECO:0000313|EMBL:AHN24600.1, ECO:0000313|Proteomes:UP000019656} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=wkB1 {ECO:0000313|Proteomes:UP000019656}; RX PubMed=25053814; RA Kwong W.K., Engel P., Koch H., Moran N.A.; RT "Genomics and host specialization of honey bee and bumble bee gut RT symbionts."; RL Proc. Natl. Acad. Sci. U.S.A. 111:11509-11514(2014). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP007445; AHN24600.1; -; Genomic_DNA. DR RefSeq; WP_025314277.1; NZ_CP007445.1. DR EnsemblBacteria; AHN24600; AHN24600; GAPWK_0021. DR GeneID; 29848753; -. DR KEGG; gap:GAPWK_0021; -. DR PATRIC; fig|1196095.8.peg.21; -. DR KO; K03665; -. DR Proteomes; UP000019656; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000019656}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000019656}. FT DOMAIN 198 365 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 431 AA; 48866 MW; 99B175CF2B4821A5 CRC64; MFERYKGGES ALLVHVFLPQ ESDIEDLKEF EVLVTSARIE ILDIVTTSRK TPQAKYFIGE GKALEIAEKV KELQASVILV NHTLTPTQER NLEKLCECRV VDRTGLILDI FAQRARTHEG KLQVELAQLQ YLSTRLVRGW THLERQKGGI GLRGPGETQL ETDRRLIRHR IQLILSRLAK VEKQRNQNRQ SRNKADLSTA SLVGYTNAGK STLFNVLTNA DVYAADQLFA TLDPTLRRII VDDVGEVVLA DTVGFIRHLP HDLIAAFKAT LLETQEAALL LHVIDAADPN MLDNIHAVEE VLFEIDAHDI PTLLVMNKID LIEGRQPSID RDEEGVPIRV WISAQNGLGL DLLFIALKER LAKQIQVCQL SLPAHLAKLR SRFYQLNAVE REFINDDGSF QLDVRMPSIE WNRLCKQEPD LLYLINTQNN N // ID X2GXG8_9BACI Unreviewed; 428 AA. AC X2GXG8; DT 11-JUN-2014, integrated into UniProtKB/TrEMBL. DT 11-JUN-2014, sequence version 1. DT 07-JUN-2017, entry version 24. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=T479_21780 {ECO:0000313|EMBL:AHN23561.1}; OS Lysinibacillus varians. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; OC Lysinibacillus. OX NCBI_TaxID=1145276 {ECO:0000313|EMBL:AHN23561.1, ECO:0000313|Proteomes:UP000019675}; RN [1] {ECO:0000313|EMBL:AHN23561.1, ECO:0000313|Proteomes:UP000019675} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=GY32 {ECO:0000313|EMBL:AHN23561.1, RC ECO:0000313|Proteomes:UP000019675}; RX PubMed=25070216; RA Zhu C., Sun G., Chen X., Guo J., Xu M.; RT "Lysinibacillus varians sp. nov., an endospore-forming bacterium with RT a filament-to-rod cell cycle."; RL Int. J. Syst. Evol. Microbiol. 0:0-0(2014). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP006837; AHN23561.1; -; Genomic_DNA. DR RefSeq; WP_025220734.1; NZ_CP006837.1. DR EnsemblBacteria; AHN23561; AHN23561; T479_21780. DR KEGG; lgy:T479_21780; -. DR PATRIC; fig|1145276.3.peg.4224; -. DR KO; K03665; -. DR Proteomes; UP000019675; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000019675}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}. FT DOMAIN 206 374 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 165 203 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 428 AA; 48559 MW; 25FBC428CF36D963 CRC64; MDKLKEVDVL LEKAILVGVN LRNDKHFDYS MEELTNLAEA LNVEVVGIVT QNLERVTPSH YVGTGKIEEI KSFYEEAQAN LVIFNDELSP SQIRNLERDL ETKVIDRTML ILDIFGRRAK TREAQMQVEL AQLQYMLPRL VGLHASLSRQ GGGTGGGFKN RGAGETKLEL DRRKIEDQIS KIKKELEQVK EQRETQRKQR RKNAVPVVSI VGYTNAGKST IMNQLLAKIG QEDHKQVFEK DMLFATLETS VRYIELHDKK SFLLTDTVGF VSKLPHHLVK AFRSTLEEAR DADLLLHVVD VSNAEHGFMM DVTNETLKAV GVEGIPTIYV YNKADLANVP YPVISGDNIW ISAKQGNGLD ELLQIIRQHI FSDYVTCKML IPYEQGNIVS YLNENATIYE TAYEEAGTLL KLEVKEADYA KYQHFVVK // ID X2H9M7_9NEIS Unreviewed; 391 AA. AC X2H9M7; DT 11-JUN-2014, integrated into UniProtKB/TrEMBL. DT 11-JUN-2014, sequence version 1. DT 05-JUL-2017, entry version 23. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=SALWKB2_1688 {ECO:0000313|EMBL:AHN29070.1}; OS Snodgrassella alvi wkB2. OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Snodgrassella. OX NCBI_TaxID=1196094 {ECO:0000313|EMBL:AHN29070.1, ECO:0000313|Proteomes:UP000019668}; RN [1] {ECO:0000313|EMBL:AHN29070.1, ECO:0000313|Proteomes:UP000019668} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=WkB2 {ECO:0000313|EMBL:AHN29070.1}; RX PubMed=25053814; RA Kwong W.K., Engel P., Koch H., Moran N.A.; RT "Genomics and host specialization of honey bee and bumble bee gut RT symbionts."; RL Proc. Natl. Acad. Sci. U.S.A. 111:11509-11514(2014). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP007446; AHN29070.1; -; Genomic_DNA. DR RefSeq; WP_025331252.1; NZ_CP007446.1. DR EnsemblBacteria; AHN29070; AHN29070; SALWKB2_1688. DR GeneID; 32537136; -. DR KEGG; salv:SALWKB2_1688; -. DR PATRIC; fig|1196094.4.peg.1689; -. DR KO; K03665; -. DR Proteomes; UP000019668; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR Gene3D; 3.60.21.10; -; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR029052; Metallo-depent_PP-like. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000019668}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000019668}. FT DOMAIN 214 383 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 180 207 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 391 AA; 43866 MW; 0335748E3B3BB643 CRC64; MSRFDKTNLS EQQPERVLLV GVLLDKDFPV AAGRRTILFE SALAEAEELV RATGADLVEV VPCKRQQPDS ALFVGKGKAE ELAQKVAEAG IDLVVFNHAL TPTQERNLER LLQCRVLDRV GLILAIFARR AQSQEGRLQV ELAQLVHLSS RLVRGYGHLQ SQRGGIGLRG PGETRLETDR RLIRQKITRL RQQLQQVRRQ RATQRKSRYQ GTLPAFALVG YTNVGKSSLF NRLTKAQVMA EDQLFATLDN TVRRLYLNDQ TSVLLSDTVG FIRDLPHGLV AAFAATLEET ALADVLLHVV DITHPEFERQ IDAVNTVLQE IDAENIPQLI IYNKIDKLSA EQRMQGIVRD IHGRPQAVYI SVQDGSGLDD LRTAMIEMAG MKYAQYNKQD E // ID X4QWR9_9ACTO Unreviewed; 438 AA. AC X4QWR9; DT 11-JUN-2014, integrated into UniProtKB/TrEMBL. DT 11-JUN-2014, sequence version 1. DT 30-AUG-2017, entry version 24. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=CQ11_01725 {ECO:0000313|EMBL:AHU88926.1}; OS Trueperella pyogenes. OC Bacteria; Actinobacteria; Actinomycetales; Actinomycetaceae; OC Trueperella. OX NCBI_TaxID=1661 {ECO:0000313|EMBL:AHU88926.1, ECO:0000313|Proteomes:UP000019771}; RN [1] {ECO:0000313|EMBL:AHU88926.1, ECO:0000313|Proteomes:UP000019771} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=TP6375 {ECO:0000313|EMBL:AHU88926.1, RC ECO:0000313|Proteomes:UP000019771}; RX PubMed=24786956; RA Machado V.S., Bicalho R.C.; RT "Complete Genome Sequence of Trueperella pyogenes, an Important RT Opportunistic Pathogen of Livestock."; RL Genome Announc. 2:e00400-14(2014). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP007519; AHU88926.1; -; Genomic_DNA. DR EnsemblBacteria; AHU88926; AHU88926; CQ11_01725. DR KEGG; tpy:CQ11_01725; -. DR PATRIC; fig|1661.13.peg.335; -. DR KO; K03665; -. DR Proteomes; UP000019771; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000019771}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000019771}. FT DOMAIN 213 378 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 438 AA; 47385 MW; ED3B3804F8397555 CRC64; MEDVTEVEYR KLRLERVILV GVVTDGDLKA GEESLRELAA LAETAGSQVL DGVLQRRQHP DPATYLGSGK AKELADLVAA SGADTVIADC ELSPSQRRAL EDIAKVKVID RTALILDIFA QHAKSREGKA QVELAQLEYL LPRLRGWGES MSRQAGGRVA GGEGIGSRGP GETKIELDRR RIRQRMAKLR RDIAHMKNSR ETKRATRRKN RTPSVVVVGY TNAGKSSLMN ILTDAGVLVE NALFATLDPT VRRAETGDGR EFTLTDTVGF VRNLPTQLVE AFRSTLEEAA DADVLLHVVD ASHDDPIGQI AAVHEVLADV DGALDVPELI VLSKEDIADP VTVATLRSRY PDAVVVSAVT GAGIGELRSR IEKMLPHPQF PVDVVIPYGR GDLVSRIHND GEILHESHEE GGTHVIARVT PEIYGSLVEA GLTGAIGE // ID X4ZM41_9BACL Unreviewed; 432 AA. AC X4ZM41; DT 11-JUN-2014, integrated into UniProtKB/TrEMBL. DT 11-JUN-2014, sequence version 1. DT 07-JUN-2017, entry version 21. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=PSAB_14095 {ECO:0000313|EMBL:AHV97730.1}; OS Paenibacillus sabinae T27. OC Bacteria; Firmicutes; Bacilli; Bacillales; Paenibacillaceae; OC Paenibacillus. OX NCBI_TaxID=1268072 {ECO:0000313|EMBL:AHV97730.1, ECO:0000313|Proteomes:UP000019772}; RN [1] {ECO:0000313|EMBL:AHV97730.1, ECO:0000313|Proteomes:UP000019772} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=T27 {ECO:0000313|EMBL:AHV97730.1, RC ECO:0000313|Proteomes:UP000019772}; RX PubMed=24651173; RA Xie J.B., Du Z., Bai L., Tian C., Zhang Y., Xie J.Y., Wang T., Liu X., RA Chen X., Cheng Q., Chen S., Li J.; RT "Comparative Genomic Analysis of N2-Fixing and Non-N2-Fixing RT Paenibacillus spp.: Organization, Evolution and Expression of the RT Nitrogen Fixation Genes."; RL PLoS Genet. 10:E1004231-E1004231(2014). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP004078; AHV97730.1; -; Genomic_DNA. DR RefSeq; WP_025335238.1; NZ_CP004078.1. DR EnsemblBacteria; AHV97730; AHV97730; PSAB_14095. DR KEGG; psab:PSAB_14095; -. DR PATRIC; fig|1268072.3.peg.2913; -. DR KO; K03665; -. DR Proteomes; UP000019772; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000019772}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000019772}. FT DOMAIN 208 372 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 432 AA; 48058 MW; C0E58178B267C326 CRC64; MATTTHDTNL EIQDRAILVS LVTDEVKRSG IDPEYSLQEL VQLAETAGVE VLEVLRQNKE TPDSKWFIGK GKVEELRMAA DGLGANTAIF DQELSGAQVR NLEEALDLKI IDRTQLILDI FAGRAKTREG IIQVELAQLS YLLPRLSGHG KNLSRLGGGI GTRGPGESKL ETDRRHIRDR IGELKRQLDE VVKTRNLHRE RRRKSGVVQV ALVGYTNAGK STLLKQLTDA DVYIENQLFA TLDPTSRLLE LPGGKSVVLT DTVGFIQNLP HDLVASFRAT LEEVNEANLV LHVVDASSPM QEEQMDVVQT ILEDLGASGK PQIVLFNKSD LCRPEQLEML PGGSGYLKVS AFNAEDLDRI KDTIQNELSG DTLSFRIPSS RGDLSSLLYR VGDVLDQSFE EDDTLYSVRV NKDDYEKWGY MLADFVNHTD QD // ID X5DFX6_9BACT Unreviewed; 404 AA. AC X5DFX6; DT 11-JUN-2014, integrated into UniProtKB/TrEMBL. DT 11-JUN-2014, sequence version 1. DT 07-JUN-2017, entry version 22. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=FH5T_11290 {ECO:0000313|EMBL:AHW59989.1}, GN SAMN05444285_1129 {ECO:0000313|EMBL:SET39082.1}; OS Draconibacterium orientale. OC Bacteria; Bacteroidetes; Bacteroidia; Marinilabiliales; OC Prolixibacteraceae; Draconibacterium. OX NCBI_TaxID=1168034 {ECO:0000313|EMBL:AHW59989.1, ECO:0000313|Proteomes:UP000023772}; RN [1] {ECO:0000313|EMBL:AHW59989.1, ECO:0000313|Proteomes:UP000023772} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=FH5 {ECO:0000313|EMBL:AHW59989.1, RC ECO:0000313|Proteomes:UP000023772}; RA Li X., Wang X., Xie Z., Du Z., Chen G.; RT "Complete genome sequence of a deeply braunched marine Bacteroidia RT bacterium Draconibacterium orientale type strain FH5T."; RL Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:SET39082.1, ECO:0000313|Proteomes:UP000181981} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 25947 {ECO:0000313|EMBL:SET39082.1, RC ECO:0000313|Proteomes:UP000181981}; RA de Groot N.N.; RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP007451; AHW59989.1; -; Genomic_DNA. DR EMBL; FOHT01000012; SET39082.1; -; Genomic_DNA. DR RefSeq; WP_038558347.1; NZ_FOHT01000012.1. DR EnsemblBacteria; AHW59989; AHW59989; FH5T_11290. DR KEGG; doi:FH5T_11290; -. DR KO; K03665; -. DR Proteomes; UP000023772; Chromosome. DR Proteomes; UP000181981; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000023772}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000023772}. FT DOMAIN 199 383 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 404 AA; 46376 MW; 106738A9686FDB1D CRC64; MIETAPITEK AVIVGLINQD QDERQAKEYL DELEFLADTA GAQVLKKFTQ KLDIPNKATF VGPGKLDEIN QYIKVVEADT VIFDDELTPT QLRNIERELE CKILDRTNLI LDIFAKRAKT AHAKTQVELA QYQYLLPRLT RMWTHLERQR GGIGMRGPGE TQIETDRRII LDKISRLKTQ LVKIDKQKAT QRKNRGKMVR VALVGYTNVG KSTIMNMMAK SEVFAENKLF ATLDTTVRKV VIGNLPFFLA DTVGFIRKLP HGLVESFKST LDEVREADIL LHIVDISHPG FEEQIETVDS TLEEIGAGDK PAFYIFNKID AFTYEEKEED DLSPRTKDNF TLEEWKGSWM AKSNTPALFI SAKEKTNIEE FKIELYEKVK GIHSQRFPYN DYLYDSDWTQ GIQE // ID X5DTM3_9CORY Unreviewed; 483 AA. AC X5DTM3; DT 11-JUN-2014, integrated into UniProtKB/TrEMBL. DT 11-JUN-2014, sequence version 1. DT 07-JUN-2017, entry version 25. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=CGLY_07885 {ECO:0000313|EMBL:AHW64022.1}; OS Corynebacterium glyciniphilum AJ 3170. OC Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae; OC Corynebacterium. OX NCBI_TaxID=1404245 {ECO:0000313|EMBL:AHW64022.1, ECO:0000313|Proteomes:UP000023703}; RN [1] {ECO:0000313|EMBL:AHW64022.1, ECO:0000313|Proteomes:UP000023703} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=AJ 3170 {ECO:0000313|EMBL:AHW64022.1}; RX PubMed=25323597; DOI=10.1099/ijs.0.065102-0; RA Al-Dilaimi A., Bednarz H., Lomker A., Niehaus K., Kalinowski J., RA Ruckert C.; RT "Revisiting Corynebacterium glyciniphilum (ex Kubota et al., 1972) sp. RT nov., nom. rev., isolated from putrefied banana."; RL Int. J. Syst. Evol. Microbiol. 65:177-182(2015). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP006842; AHW64022.1; -; Genomic_DNA. DR RefSeq; WP_038548305.1; NZ_CP006842.1. DR EnsemblBacteria; AHW64022; AHW64022; CGLY_07885. DR KEGG; cgy:CGLY_07885; -. DR KO; K03665; -. DR Proteomes; UP000023703; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000023703}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000023703}. FT DOMAIN 254 430 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 213 240 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 483 AA; 52574 MW; 4CB309CFA4D8CF7E CRC64; MTSMNQNPEE IHAETTVGEL DLEQRSSLRR LSRGTNVHST EQDDGYDVEY RKLRLEKVVL VGVWTEGSLE QIEARLAELA ALAETAGSEI ADMLYQRRDK PDAGTYIGSG KVEELRQIVL ETNADTVVAD GELSPGQMIA LEKALDVKVI DRTMLILDIF AQHAKSKEGK AQVALAQLEY LITRVRGWGG ALSRQAGGRA GSNGGVGLRG PGETKIEADR RRLRSEMARL RREIQGMKKS RDIKRGRRDA SAIAKVAIAG YTNAGKSSLL NSLTGAGVLV EDALFATLDP TTRRAELADG RAVVFSDTVG FIRFLPTQLV EAFRSTLEEV MAADVVLHVV DGSDPFPMEQ IAAVNKVIGE IAEETGEPAP PEILVINKVD AADPLVLAEL RSRLDDVLFV SAATGEGIPV LESRLELFLN SLDDHVVLQV PFDRGDVVSR LHEYGTVLSQ EYTEDGTRVE VRLPGIIAAE LSDLRIAVDE GTE // ID X5JXS0_9NOST Unreviewed; 530 AA. AC X5JXS0; DT 11-JUN-2014, integrated into UniProtKB/TrEMBL. DT 11-JUN-2014, sequence version 1. DT 07-JUN-2017, entry version 21. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=RintRC_3454 {ECO:0000313|EMBL:CDN16630.1}; OS Richelia intracellularis. OC Bacteria; Cyanobacteria; Nostocales; Nostocaceae; Richelia. OX NCBI_TaxID=1164990 {ECO:0000313|EMBL:CDN16630.1, ECO:0000313|Proteomes:UP000019767}; RN [1] {ECO:0000313|EMBL:CDN16630.1, ECO:0000313|Proteomes:UP000019767} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=RC01 {ECO:0000313|EMBL:CDN16630.1, RC ECO:0000313|Proteomes:UP000019767}; RA Hilton J.; RL Submitted (JAN-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:CDN16630.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CBZS010000768; CDN16630.1; -; Genomic_DNA. DR EnsemblBacteria; CDN16630; CDN16630; RintRC_3454. DR Proteomes; UP000019767; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000019767}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000019767}. FT DOMAIN 357 527 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 316 350 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 530 AA; 58766 MW; CAB0CF7D89EF5D94 CRC64; MCAYLNRRGQ VIRVGVGCPR QTQIPLLELP RYGAERLSGI RCIATHMKSE PPNDGVMTTM ALQRLDALVV LNITKSGFTR RAGGATGYVK EAYLAHLTPQ DTRALLASSY FLEAGTSPVP RPSWTLSPAM SLDVLGKQDF LDLVEGLEAE FRREFTAQEV DSDHERVVLV GVMTERISTH SFQDTLAELA RLVDTAGGDV LQTLWQKRSR IHPQTVVGEG KVQEIALTAQ ILGANLIVFD RDLSPAQVRN LEARIGLRVV DRTEVILDIF AQRAQSGAGK LQVELAQLEY MLPRLAGRGE AMSRLGGGIG TRGPGETKLE TERRAIQRRI YRLQREVNQL QAHRARLRQR RQHHEVPSIA LVGYTNAGKS TLLNTITNAE VYTADQLFAT LDPTTRRLSV PHPDKIQNQE ILVTDTVGFI HELPPSLMDA FRATLEEVTE ADALLHLVDL SHPAWLTHIR AVRDILAQML ITPGPALVAF NKIDQVDSDT LTQAQEEFPL AVFISSSARL GLETLRQRLG QLVDYAVTSR // ID X5LGH9_9MYCO Unreviewed; 466 AA. AC X5LGH9; DT 11-JUN-2014, integrated into UniProtKB/TrEMBL. DT 11-JUN-2014, sequence version 1. DT 07-JUN-2017, entry version 25. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=BN978_05043 {ECO:0000313|EMBL:CDO24547.1}; OS Mycobacterium mageritense DSM 44476 = CIP 104973. OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae; OC Mycobacterium. OX NCBI_TaxID=1209984 {ECO:0000313|EMBL:CDO24547.1, ECO:0000313|Proteomes:UP000028867}; RN [1] {ECO:0000313|EMBL:CDO24547.1, ECO:0000313|Proteomes:UP000028867} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CIP 104973 {ECO:0000313|EMBL:CDO24547.1, RC ECO:0000313|Proteomes:UP000028867}; RA Croce O., Robert C., Raoult D., Drancourt M.; RT "Draft genome sequence of Mycobacterium margeritense."; RL Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:CDO24547.1, ECO:0000313|Proteomes:UP000028867} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CIP 104973 {ECO:0000313|EMBL:CDO24547.1, RC ECO:0000313|Proteomes:UP000028867}; RA Urmite Genomes U.; RL Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:CDO24547.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CCBF010000002; CDO24547.1; -; Genomic_DNA. DR RefSeq; WP_036437131.1; NZ_CCBF010000002.1. DR EnsemblBacteria; CDO24547; CDO24547; BN978_05043. DR Proteomes; UP000028867; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000028867}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000028867}. FT DOMAIN 243 412 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 202 236 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 466 AA; 50173 MW; 31863817BB3DB5AA CRC64; MTYPETPSTG ELALEDRASL RRVAGLSTEL ADVTEVEYRQ LRLERVVLVG VWTDGSAADA DASLAELAAL AETAGSEVLE GLIQRRDKPD PSTYIGSGKA AELREVVLAT GADTVICDGE LSPAQLNALE KAVKVKVIDR TALILDIFAQ HATSREGKAQ VSLAQMEYML PRLRGWGESM SRQAGGRAGG AGGGVGTRGP GETKIETDRR RIRERMAKLR REIRDMKKIR DTQRSRRLSA DVASVAIVGY TNAGKSSLLN ALTGAGVLVE NALFATLEPT TRRGEFDDGR PFVLTDTVGF VRHLPTQLVE AFRSTLEEVV DADLLVHVVD GSDANPLAQI SAVRQVISDV IAEHDGRRAP ELLVVNKIDA TGDLALAQLR RALPDAVFVS AHTGDGLERL RQRMGELVEP TDTMVDVTIP YDRGDLVAKV HADGRVDATE HTADGTRIKA RVPVALAASL GEYTTF // ID X5MAT7_9RHIZ Unreviewed; 450 AA. AC X5MAT7; DT 11-JUN-2014, integrated into UniProtKB/TrEMBL. DT 11-JUN-2014, sequence version 1. DT 07-JUN-2017, entry version 25. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=BN1012_Phect2866 {ECO:0000313|EMBL:CDO61078.1}; OS Candidatus Phaeomarinobacter ectocarpi. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Rhodobiaceae; Candidatus Phaeomarinobacter. OX NCBI_TaxID=1458461 {ECO:0000313|EMBL:CDO61078.1, ECO:0000313|Proteomes:UP000032160}; RN [1] {ECO:0000313|EMBL:CDO61078.1, ECO:0000313|Proteomes:UP000032160} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Ec32 {ECO:0000313|EMBL:CDO61078.1}; RX PubMed=25120558; DOI=10.3389/fgene.2014.00241; RA Dittami S.M., Barbeyron T., Boyen C., Cambefort J., Collet G., RA Delage L., Gobet A., Groisillier A., Leblanc C., Michel G., RA Scornet D., Siegel A., Tapia J.E., Tonon T.; RT "Genome and metabolic network of "Candidatus Phaeomarinobacter RT ectocarpi" Ec32, a new candidate genus of Alphaproteobacteria RT frequently associated with brown algae."; RL Front. Genet. 5:241-241(2014). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; HG966617; CDO61078.1; -; Genomic_DNA. DR RefSeq; WP_043948970.1; NZ_HG966617.1. DR EnsemblBacteria; CDO61078; CDO61078; BN1012_Phect2866. DR PATRIC; fig|1458461.3.peg.2872; -. DR Proteomes; UP000032160; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000032160}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000032160}. FT DOMAIN 215 386 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 174 208 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 450 AA; 49142 MW; 4EBC423BDA50AFC0 CRC64; MTPVDDRVAA TESGRAIVLH PWIKSGPVAA AARHTQRAPE DRLEEAVGLA AAIHLDISQA IVVPVADPKP GTLFGQGKVD EIKHMVELEE AGLVIIDGQV TPIQQRNLER AWKAKVLDRT GLILEIFGER AATREGSLQV ELAHLMYQKS RLVRSWTHLE RQRGGLGFVG GPGETQIEAD RRHIQDRITK LENQLERVTR TRELHRKTRR RVPYPVVALV GYTNAGKSTL FNRLTASGVL AEDMLFATLD PTMRALDMPG GQRVILSDTV GFISDLPTSL VAAFRATLEE VLEAELILHV RDISHPDTAA QRQDVHEVLR ELGVDPQDTE RVIEVANKID QLDGPGRAVL ADTIEGDPNQ IAVSAITGEG IDPLNALIEA RVTAHLTEID VLLGPGDAAA RAWLHENCTV TGEDDPDDQG NVRILIKVSS ADTGRINKRF PGLLPEALGL // ID X6DCY0_9RHIZ Unreviewed; 463 AA. AC X6DCY0; DT 11-JUN-2014, integrated into UniProtKB/TrEMBL. DT 11-JUN-2014, sequence version 1. DT 07-JUN-2017, entry version 23. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=X743_06730 {ECO:0000313|EMBL:ESY74946.1}; OS Mesorhizobium sp. LNHC252B00. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Phyllobacteriaceae; Mesorhizobium. OX NCBI_TaxID=1287252 {ECO:0000313|EMBL:ESY74946.1, ECO:0000313|Proteomes:UP000020180}; RN [1] {ECO:0000313|EMBL:ESY74946.1, ECO:0000313|Proteomes:UP000020180} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=LNHC252B00 {ECO:0000313|EMBL:ESY74946.1, RC ECO:0000313|Proteomes:UP000020180}; RA Porter S.S., Chang P.L., Conow C.A., Dunham J.P., Friesen M.L.; RT "Adaptive variation in the core and flexible genome of wild RT Mesorhizobia."; RL Submitted (JUL-2013) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:ESY74946.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AYWO01000003; ESY74946.1; -; Genomic_DNA. DR RefSeq; WP_023757914.1; NZ_AYWO01000003.1. DR EnsemblBacteria; ESY74946; ESY74946; X743_06730. DR PATRIC; fig|381.20.peg.1365; -. DR Proteomes; UP000020180; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000020180}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000020180}. FT DOMAIN 231 404 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 190 224 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 463 AA; 51010 MW; 2EA4D19DCB215142 CRC64; MAREKDADDT VRGKPAHHPG TEAEGPTRAV VIVPVLTRHQ RNEDETNRPR LMRSADARHD EAVGLARAID LDLIHTAVVT VNDPRPATLL GSGKVAEFAE IVKEGHAEVV VVDHPLTPVQ QRNLEKELNA KVLDRTGLIL EIFGERARTK EGTLQVELAH LNYQKGRLVR SWTHLERQRG GAGFLGGPGE TQIESDRRQL QEKIIKLKQE LETVRRTRDL HRAKRKKVPF PVVAIVGYTN AGKSTLFNRL TGADVLAQDM LFATLDPTLR RVRLPHGTPI ILSDTVGFIS DLPTHLIAAF RATLEEVVEA DLVIHLRDIS DPDTAAQAED VERILADLGV DAGDAKRIIE VWNKIDLLDE GNRSRLLADS ADASKAPPIA ISAVTGEGID ALKAIIETRM AGELEDLTVT IEPAQFGLVD WIYRNGDIVS RSDNDDGSAT ISLRATQSAR EEIESKLRRK NNG // ID X6GGT5_9RHIZ Unreviewed; 463 AA. AC X6GGT5; DT 11-JUN-2014, integrated into UniProtKB/TrEMBL. DT 11-JUN-2014, sequence version 1. DT 07-JUN-2017, entry version 22. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=X737_13395 {ECO:0000313|EMBL:ESZ19821.1}; OS Mesorhizobium sp. L48C026A00. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Phyllobacteriaceae; Mesorhizobium. OX NCBI_TaxID=1287182 {ECO:0000313|EMBL:ESZ19821.1, ECO:0000313|Proteomes:UP000019863}; RN [1] {ECO:0000313|EMBL:ESZ19821.1, ECO:0000313|Proteomes:UP000019863} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=L48C026A00 {ECO:0000313|EMBL:ESZ19821.1, RC ECO:0000313|Proteomes:UP000019863}; RA Porter S.S., Chang P.L., Conow C.A., Dunham J.P., Friesen M.L.; RT "Adaptive variation in the core and flexible genome of wild RT Mesorhizobia."; RL Submitted (JUL-2013) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:ESZ19821.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AYWU01000007; ESZ19821.1; -; Genomic_DNA. DR RefSeq; WP_023799220.1; NZ_AYWU01000007.1. DR EnsemblBacteria; ESZ19821; ESZ19821; X737_13395. DR PATRIC; fig|381.14.peg.2746; -. DR Proteomes; UP000019863; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000019863}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000019863}. FT DOMAIN 231 404 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 190 224 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 463 AA; 50965 MW; 3303DBD370E0D958 CRC64; MARKKDADRS VREKPAYQPG AEAEGPTRAV VIVPVLTRQP RGDEDTNRPR LTRSAEARHD EAVGLAQAIN LDPIHTAVVT VNDPRPATLL GSGKVAEFAE IVKEGRAELV IVDHPLTPVQ QRNLEKELNA KVLDRTGLIL EIFGERARTK EGTLQVDLAH LNYQKGRLVR SWTHLERQRG GAGFLGGPGE TQIESDRRVL QDKINKLKHE LETVRRTRDL HRAKRKKVPF PVVAIVGYTN AGKSTLFNRL TGAGVLAEDM LFATLDPTLR RVRLPHGTPV ILSDTVGFIS DLPTHLIAAF RATLEEVVEA DLVIHLRDIS DPDTAAQAED VERILADLGV DAGDGRRVIE VWNKIDRLDE GNRERLLADG IDGSKAPPIA ISAATGEGID VLKAIIETRV SGELETQTVT LKPDQLGFVD WLYRNGDVVS RTDNEDGGIT VSLKATRSAH EDIETRLHRK NNG // ID X6L3B1_9RHOB Unreviewed; 425 AA. AC X6L3B1; DT 11-JUN-2014, integrated into UniProtKB/TrEMBL. DT 11-JUN-2014, sequence version 1. DT 05-JUL-2017, entry version 25. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=P279_05055 {ECO:0000313|EMBL:ETA53105.1}; OS Rhodobacteraceae bacterium PD-2. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae. OX NCBI_TaxID=1169855 {ECO:0000313|EMBL:ETA53105.1, ECO:0000313|Proteomes:UP000023196}; RN [1] {ECO:0000313|EMBL:ETA53105.1, ECO:0000313|Proteomes:UP000023196} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=PD-2 {ECO:0000313|EMBL:ETA53105.1, RC ECO:0000313|Proteomes:UP000023196}; RX PubMed=25700405; RA Zheng L., Cui Z., Xu L., Sun C., Powell R.J., Hill R.T.; RT "Draft Genome Sequence of Rhodobacteraceae Strain PD-2, an Algicidal RT Bacterium with a Quorum-Sensing System, Isolated from the Marine RT Microalga Prorocentrum donghaiense."; RL Genome Announc. Announc.3:e01549-14(2015). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:ETA53105.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AWRV02000006; ETA53105.1; -; Genomic_DNA. DR EnsemblBacteria; ETA53105; ETA53105; P279_05055. DR PATRIC; fig|1169855.3.peg.890; -. DR Proteomes; UP000023196; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000023196}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000023196}. FT DOMAIN 204 373 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 425 AA; 47087 MW; 22B78FD056E65CF1 CRC64; MKEHAPHVTR AWVVHPDIKS DPNRRDARMA LEEAVSLAHA LPGLEVAGSE VVPLPRPHAG ALFGTGKIAE LKDRFHDAEV ELVLVDGPVS PVQQRNLEKE WKVKLLDRTG LILEIFSDRA ATREGVLQVE MAALSYQRTR LVRAWTHLER QRGGLGFVGG PGETQIEADR RAIDEQMVRL RRQLDKVVRT RELHRKARAK VPYPIVALVG YTNAGKSTLF NRLTGAEVMA KDMLFATLDP TMRAVRLPTG ADVILSDTVG FISDLPTQLV AAFRATLEEV LAADVIVHVR DISHPESEAQ AEDVNAILSE LGLDEETPRL ELWNKLDRLD PEAAEAVALR AERDEAVFAV SALTGAGLDG FLEAVTSALG EETRQDRLRL GFDAGRRRAW LFEKGLVEAE TQDEDGYVLT VNWSAADRAR FDSME // ID X7E3B0_9GAMM Unreviewed; 429 AA. AC X7E3B0; DT 11-JUN-2014, integrated into UniProtKB/TrEMBL. DT 11-JUN-2014, sequence version 1. DT 07-JUN-2017, entry version 23. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=MUS1_15680 {ECO:0000313|EMBL:ETX10355.1}; OS Marinomonas ushuaiensis DSM 15871. OC Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales; OC Marinomonas. OX NCBI_TaxID=1122207 {ECO:0000313|EMBL:ETX10355.1, ECO:0000313|Proteomes:UP000054058}; RN [1] {ECO:0000313|EMBL:ETX10355.1, ECO:0000313|Proteomes:UP000054058} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 15871 {ECO:0000313|EMBL:ETX10355.1, RC ECO:0000313|Proteomes:UP000054058}; RA Lai Q., Shao Z.S.; RT "Marinomonas ushuaiensis DSM 15871 Genome Sequencing."; RL Submitted (JAN-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:ETX10355.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JAMB01000009; ETX10355.1; -; Genomic_DNA. DR RefSeq; WP_036162471.1; NZ_JAMB01000009.1. DR EnsemblBacteria; ETX10355; ETX10355; MUS1_15680. DR PATRIC; fig|1122207.3.peg.2286; -. DR Proteomes; UP000054058; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000054058}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}. FT DOMAIN 199 366 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 429 AA; 48110 MW; 2960F98866991205 CRC64; MFFERPDSGD VAVLVHIDFH DKNESYGPEE FVELAISAGA DPVAVVTGSR QRPDARYFIG TGKLAEIKDI VDREEAEVVL FDHALSPSQE RNLESILQCR VLDRTGLILD IFAQRARTHE GKLQVELAQL QHMSTRLIRG WTHLERQKGG IGMRGPGETQ LETDRRLLRE RIKAIQKRLS KVGSQRDQNR RSRSRSEVPT VSLVGYTNAG KSTLFNRATG AEVYAADQLF ATLDPTLRRL DVEQIGSIVL ADTVGFIRQL PHRLIKAFQA TLKESSEADL LLHIVDAADI SRDENMAHVD SVLEEIGASE VPTLKVFNKI DALETAEPRI DRDVDGNPYR VWLSARDGQG IDLLKQAIAE LLSEDVFNET LSLSNESGRL RAMLFEHGAV RSERFDETGR SVLEVRLPKK DYLQILARAE LSENQIQTA // ID X7E6X3_9GAMM Unreviewed; 446 AA. AC X7E6X3; DT 11-JUN-2014, integrated into UniProtKB/TrEMBL. DT 11-JUN-2014, sequence version 1. DT 07-JUN-2017, entry version 23. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=MUS1_07730 {ECO:0000313|EMBL:ETX11824.1}; OS Marinomonas ushuaiensis DSM 15871. OC Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales; OC Marinomonas. OX NCBI_TaxID=1122207 {ECO:0000313|EMBL:ETX11824.1, ECO:0000313|Proteomes:UP000054058}; RN [1] {ECO:0000313|EMBL:ETX11824.1, ECO:0000313|Proteomes:UP000054058} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 15871 {ECO:0000313|EMBL:ETX11824.1, RC ECO:0000313|Proteomes:UP000054058}; RA Lai Q., Shao Z.S.; RT "Marinomonas ushuaiensis DSM 15871 Genome Sequencing."; RL Submitted (JAN-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:ETX11824.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JAMB01000002; ETX11824.1; -; Genomic_DNA. DR RefSeq; WP_036159723.1; NZ_JAMB01000002.1. DR EnsemblBacteria; ETX11824; ETX11824; MUS1_07730. DR PATRIC; fig|1122207.3.peg.855; -. DR Proteomes; UP000054058; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000054058}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}. FT DOMAIN 226 391 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 187 221 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 446 AA; 49518 MW; 15272C125047F10D CRC64; MQLTAKPSLN NALLISVCTP EFRGEEAVES LAELARLVTT LGFKVVGTQS QNQSSTNRVN VLGLGKLAEI AQLTGNKGVI EAQEDEDELD YDLDITSVPS DNLPLACADI VVFDCDLSPS QLRNVENQLG VEVYDRTGVI IEIFSRHART KTAKLQVEIA RLNYVAPRLR ETSTGDREHQ MGKGAGETTL ELNRRNVRDQ LAELRRQLVS VQEEMRGRRT QRSENFCVAL VGYTNAGKSS MMRAITGSDV EGENKLFATL DTTVRALFPI THPRILVSDT VGFIKKLPHD LVASFHSTLA EAHDASLLLY VVDASDPSFR KQLDVVHEVL EEVGVEDSKK LLILNKSDQL SAEQQAELMI EFPEAMLTSA RDPKDIAKLH KYIVGISEEG MLQEEIVIPY TANGIVGEIR NSMSVTKEEY EFDHIKLTVR TSEIGLARLK KKMLDL // ID X7ED83_9RHOB Unreviewed; 426 AA. AC X7ED83; DT 11-JUN-2014, integrated into UniProtKB/TrEMBL. DT 11-JUN-2014, sequence version 1. DT 05-JUL-2017, entry version 23. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=OCH239_13540 {ECO:0000313|EMBL:ETX13083.1}; OS Roseivivax halodurans JCM 10272. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae; Roseivivax. OX NCBI_TaxID=1449350 {ECO:0000313|EMBL:ETX13083.1, ECO:0000313|Proteomes:UP000022447}; RN [1] {ECO:0000313|EMBL:ETX13083.1, ECO:0000313|Proteomes:UP000022447} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=JCM 10272 {ECO:0000313|EMBL:ETX13083.1, RC ECO:0000313|Proteomes:UP000022447}; RA Lai Q., Li G., Shao Z.; RT "Roseivivax halodurans JCM 10272 Genome Sequencing."; RL Submitted (JAN-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:ETX13083.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JALZ01000038; ETX13083.1; -; Genomic_DNA. DR EnsemblBacteria; ETX13083; ETX13083; OCH239_13540. DR PATRIC; fig|1449350.3.peg.3754; -. DR Proteomes; UP000022447; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000022447}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000022447}. FT DOMAIN 206 375 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 426 AA; 47661 MW; 0E0426CB5201FF8D CRC64; MTETDHEVRP TRAWVLHPDI KSDRQRRDPD MALEEAVALA EALPGMEVVA SAVVPLPQPH PNALFGSGKI EELRERIQGD DIELVLVDGP LSPVQQRNLE KEWKVKILDR TGLILEIFSD RAATREGVLQ VEMAHLSYQR TRLVRAWTHL ERQRGGLGFV GGPGETQIEA DRRAIDEQLV RLRRQLDKVV KTRSLHRKAR AKVPYPIVAL VGYTNAGKST LFNRLTGAEV MAKDMLFATL DPTMRGVKLE NGPDVILSDT VGFISDLPTE LVAAFRATLE EVLEADLIVH VRDISHPNTQ EQADDVHAIL ASLGVAEDTP HIEVWNKIDQ LAPEAREAAQ TRAERVDSIY ALSAWTGEGM DALLSGITRI IEGDKRRASV HLDFADGRKR AWLFERNLVE AETQTEDGYD LDVRWTAKEA AQFDKV // ID X7F3E2_9RHOB Unreviewed; 417 AA. AC X7F3E2; DT 11-JUN-2014, integrated into UniProtKB/TrEMBL. DT 11-JUN-2014, sequence version 1. DT 07-JUN-2017, entry version 22. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=RISW2_14810 {ECO:0000313|EMBL:ETX27268.1}; OS Roseivivax isoporae LMG 25204. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae; Roseivivax. OX NCBI_TaxID=1449351 {ECO:0000313|EMBL:ETX27268.1, ECO:0000313|Proteomes:UP000023430}; RN [1] {ECO:0000313|EMBL:ETX27268.1, ECO:0000313|Proteomes:UP000023430} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=LMG 25204 {ECO:0000313|EMBL:ETX27268.1, RC ECO:0000313|Proteomes:UP000023430}; RA Lai Q., Li G., Shao Z.; RT "Roseivivax isoporae LMG 25204 Genome Sequencing."; RL Submitted (JAN-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:ETX27268.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JAME01000036; ETX27268.1; -; Genomic_DNA. DR RefSeq; WP_043774042.1; NZ_JAME01000036.1. DR EnsemblBacteria; ETX27268; ETX27268; RISW2_14810. DR PATRIC; fig|1449351.3.peg.3831; -. DR Proteomes; UP000023430; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000023430}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000023430}. FT DOMAIN 197 366 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 417 AA; 46397 MW; 4585E80E2E385F66 CRC64; MTRAWVLHPD IKSDRERRDA HMALDEAVAL AVALPDLEVV GSEIVPLPQP HANALFGTGK IAELGERLKE AEVELVLVDG PVTPVQQRNL EKAWKVKLLD RTGLILEIFS DRAATREGVL QVEMAHLSYQ RTRLVRAWTH LERQRGGLGF VGGPGETQIE ADRRAIDEQL VRLRRQLDKV VKTRALHRKA RAKVPYPIVA LVGYTNAGKS TLFNRLTGAE VMAKDMLFAT LDPTMRAVRL ENGVDVILSD TVGFISDLPT ELVAAFRATL EEVLEADLIV HVRDISHPNA QEQADDVHAI LASLGVAQST PQIEVWNKID RLPPESREAA LTRAERTRGI LALSAWTGEG MAPLLDAIAE SVEGDKREEA LHLDFSDGRK RAWLFDRGLV EEEVQTDDGY DLTVRWTARE AAQFEKV // ID X7Y064_MYCKA Unreviewed; 480 AA. AC X7Y064; DT 11-JUN-2014, integrated into UniProtKB/TrEMBL. DT 11-JUN-2014, sequence version 1. DT 30-AUG-2017, entry version 28. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:EUA00236.1}; GN ORFNames=I547_5373 {ECO:0000313|EMBL:EUA00236.1}; OS Mycobacterium kansasii 824. OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae; OC Mycobacterium. OX NCBI_TaxID=1299328 {ECO:0000313|EMBL:EUA00236.1, ECO:0000313|Proteomes:UP000022044}; RN [1] {ECO:0000313|EMBL:EUA00236.1, ECO:0000313|Proteomes:UP000022044} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=824 {ECO:0000313|EMBL:EUA00236.1, RC ECO:0000313|Proteomes:UP000022044}; RA Brown-Elliot B., Wallace R., Lenaerts A., Ordway D., DeGroote M.A., RA Parker T., Sizemore C., Tallon L.J., Sadzewicz L.K., Sengamalay N., RA Fraser C.M., Hine E., Shefchek K.A., Das S.P., Tettelin H.; RL Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EUA00236.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JANY01000004; EUA00236.1; -; Genomic_DNA. DR RefSeq; WP_023372571.1; NZ_JANY01000004.1. DR EnsemblBacteria; EUA00236; EUA00236; I547_5373. DR GeneID; 29701658; -. DR KEGG; mki:LH54_25140; -. DR PATRIC; fig|1299328.3.peg.5171; -. DR KO; K03665; -. DR Proteomes; UP000022044; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000022044}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000022044}. FT DOMAIN 250 426 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 209 243 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 480 AA; 51833 MW; 3CF80C7BA9B5505B CRC64; MTYPEFPHQD PLEPSTGELA LEDRSALRRV AGLSTELADI SEVEYRQLRL ERVVLVGVWT EGSAADTEAS MAELAALAET AGSQVLEGII QRRDRPDPST YIGSGKAAEL REIVVATGAD TVICDGELSP AQLTALEKAV KVKVIDRTAL ILDIFAQHAT SREGKAQVSL AQMEYMLPRL RGWGESMSRQ AGGRAGGSGG GVGLRGPGET KIETDRRRIR ERMAKLRREI KDMKQARDTR RSRRVHSDLP SIAIVGYTNA GKSSLLNALT GAGVLVQDAL FATLEPTTRR AEFDDGSGRP GRFLLTDTVG FVRHLPTQLV EAFRSTLEEV VDADLLVHVV DGADANPLAQ INAVRQVISE VIADRGADGG EAPQELLVVN KIDAASDLAL AKLRHALPGA VFVSARTGDG VDALRRRMAE LVAPTDAAVD VVIPYDRGDL VARLHSDGRV QHEEHSVHGT RIKARVPVTL AGRLQEFTVR // ID X8ATW7_MYCXE Unreviewed; 232 AA. AC X8ATW7; DT 11-JUN-2014, integrated into UniProtKB/TrEMBL. DT 11-JUN-2014, sequence version 1. DT 07-JUN-2017, entry version 11. DE SubName: Full=GTP-binding GTPase family protein {ECO:0000313|EMBL:EUA34463.1}; GN ORFNames=I552_5246 {ECO:0000313|EMBL:EUA34463.1}; OS Mycobacterium xenopi 3993. OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae; OC Mycobacterium. OX NCBI_TaxID=1299333 {ECO:0000313|EMBL:EUA34463.1, ECO:0000313|Proteomes:UP000023198}; RN [1] {ECO:0000313|EMBL:EUA34463.1, ECO:0000313|Proteomes:UP000023198} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=3993 {ECO:0000313|EMBL:EUA34463.1, RC ECO:0000313|Proteomes:UP000023198}; RA Brown-Elliot B., Wallace R., Lenaerts A., Ordway D., DeGroote M.A., RA Parker T., Sizemore C., Tallon L.J., Sadzewicz L.K., Sengamalay N., RA Fraser C.M., Hine E., Shefchek K.A., Das S.P., Tettelin H.; RL Submitted (JAN-2014) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EUA34463.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JAOC01000010; EUA34463.1; -; Genomic_DNA. DR EnsemblBacteria; EUA34463; EUA34463; I552_5246. DR PATRIC; fig|1299333.3.peg.5053; -. DR Proteomes; UP000023198; Unassembled WGS sequence. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF13167; GTP-bdg_N; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000023198}; KW Reference proteome {ECO:0000313|Proteomes:UP000023198}. FT DOMAIN 68 156 GTP-bdg_N. {ECO:0000259|Pfam:PF13167}. SQ SEQUENCE 232 AA; 24540 MW; 3BDE1C82D74DBE32 CRC64; MTYPESPDQV LPEPSAGELA LDDRSALRRV AGLSTELADI SEVEYRQLRL ERVVLVGVWT EGSAADAEAS LAELAALAET AGSLVLEGLI QRRSKPDPST YIGSGKAQEL REVVLATGAD TVICDGELSP AQLTALEKAV KVKVIDRTAL ILDIFAQHAT SRKARRKCRW HKWNTCCRGC AAGVSRCRGR PVAAPAAAPA AWACVVPVRP RSRPTGAASA SGWPGCAATS RA // ID X8DNX1_9MYCO Unreviewed; 464 AA. AC X8DNX1; DT 11-JUN-2014, integrated into UniProtKB/TrEMBL. DT 11-JUN-2014, sequence version 1. DT 07-JUN-2017, entry version 22. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:EUA69756.1}; GN ORFNames=I540_3526 {ECO:0000313|EMBL:EUA69756.1}; OS Mycobacterium abscessus subsp. bolletii 1513. OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae; OC Mycobacterium; Mycobacterium abscessus. OX NCBI_TaxID=1299321 {ECO:0000313|EMBL:EUA69756.1, ECO:0000313|Proteomes:UP000023351}; RN [1] {ECO:0000313|EMBL:EUA69756.1, ECO:0000313|Proteomes:UP000023351} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=1513 {ECO:0000313|EMBL:EUA69756.1, RC ECO:0000313|Proteomes:UP000023351}; RA Zelazny A., Olivier K., Holland S., Lenaerts A., Ordway D., RA DeGroote M.A., Parker T., Sizemore C., Tallon L.J., Sadzewicz L.K., RA Sengamalay N., Fraser C.M., Hine E., Shefchek K.A., Das S.P., RA Tettelin H.; RL Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EUA69756.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JAOJ01000002; EUA69756.1; -; Genomic_DNA. DR EnsemblBacteria; EUA69756; EUA69756; I540_3526. DR PATRIC; fig|1299321.3.peg.3386; -. DR Proteomes; UP000023351; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000023351}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000023351}. FT DOMAIN 244 413 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 203 237 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 464 AA; 49795 MW; D0A1BC305C021A83 CRC64; MRATYETPTD GELALEDRAA LKRVAGLSTE LADVTEVEYR QLRLERVVLV GVWTEGTSQE AEASMAELAA LAETAGSEVL EGLIQRRQKP DPATYIGSGK AIELREIVLA TGADTVICDG ELSPAQLVAL EKAVKVKVID RTALILDIFA QHATSREGKA QVSLAQMEYM LPRLRGWGES MSRQAGGRAG GAGGGVGTRG PGETKIETDR RRIRERMSKL RREIRDMKKV RDTKRSRRLE SDVPSVAIVG YTNAGKSSLL NAITGAGVLV QDALFATLEP TTRRGTFDDG REFVITDTVG FVRHLPTQLV EAFRSTLEEV ADADLLVHVV DGSDMAPLAQ IEAVRTVIGE VVADHDASAA PELLVINKVD AAGDLALAQL RRALPKALFV SAHTGEGIAT LREAIAEAVP RGDVPVDVVI PYERGDLVAR MHAEGQVQST EHLADGTRVV GRVPRALAAV LTAL // ID X8F5N4_MYCUL Unreviewed; 375 AA. AC X8F5N4; DT 11-JUN-2014, integrated into UniProtKB/TrEMBL. DT 11-JUN-2014, sequence version 1. DT 07-JUN-2017, entry version 15. DE SubName: Full=GTP-binding protein HflX {ECO:0000313|EMBL:EUA88154.1}; GN Name=hflX {ECO:0000313|EMBL:EUA88154.1}; GN ORFNames=I551_5356 {ECO:0000313|EMBL:EUA88154.1}; OS Mycobacterium ulcerans str. Harvey. OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae; OC Mycobacterium. OX NCBI_TaxID=1299332 {ECO:0000313|EMBL:EUA88154.1, ECO:0000313|Proteomes:UP000020681}; RN [1] {ECO:0000313|EMBL:EUA88154.1, ECO:0000313|Proteomes:UP000020681} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Harvey {ECO:0000313|EMBL:EUA88154.1, RC ECO:0000313|Proteomes:UP000020681}; RA Dobos K., Lenaerts A., Ordway D., DeGroote M.A., Parker T., RA Sizemore C., Tallon L.J., Sadzewicz L.K., Sengamalay N., Fraser C.M., RA Hine E., Shefchek K.A., Das S.P., Tettelin H.; RL Submitted (JAN-2014) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EUA88154.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JAOL01000147; EUA88154.1; -; Genomic_DNA. DR EnsemblBacteria; EUA88154; EUA88154; I551_5356. DR PATRIC; fig|1299332.3.peg.6108; -. DR Proteomes; UP000020681; Unassembled WGS sequence. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. PE 4: Predicted; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000020681}; KW Reference proteome {ECO:0000313|Proteomes:UP000020681}. FT DOMAIN 75 162 GTP-bdg_N. {ECO:0000259|Pfam:PF13167}. FT DOMAIN 164 250 GTP-bdg_M. {ECO:0000259|Pfam:PF16360}. FT DOMAIN 258 278 G (guanine nucleotide-binding). FT {ECO:0000259|Pfam:PF01926}. FT COILED 215 249 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 375 AA; 40437 MW; 27EA965EC5CF200A CRC64; MTYSEFPDSV RRASEPAAEP SIGELALEDR SALRRVAGLS TELADVSEVE YRQLRLERVV LVGVWTEGTA ADNQASLAEL AALAETTGSQ VLEGLIQRRD RPDPSTYIGS GKAAELREVV VATGADTVIC DGELSPAQLT ALEKAVKVKV IDRTALILDI FAQHATSREG KAQVALAQME YMLPRLRGWG ESMSRQAGGR AGGSGGGVGL RGPGETKIET DRRRIRERMA KLRREIKAMK QARDTQRSRR LHSDVPSIAI VGYTNAGKSS LLNALTGAGS WCRTRCSRHS IQPPGARSST PIPMVRGPFC SPTPSVSCAI CPPAGRGVSV HAGGGHRRGS AVTRRRRLRP EPVGPDQRGA PGDLRGHRRR GHRRR // ID Y0KG57_9PROT Unreviewed; 375 AA. AC Y0KG57; DT 11-JUN-2014, integrated into UniProtKB/TrEMBL. DT 11-JUN-2014, sequence version 1. DT 30-AUG-2017, entry version 23. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=Meth11DRAFT_0995 {ECO:0000313|EMBL:EUJ10182.1}; OS Methylophilaceae bacterium 11. OC Bacteria; Proteobacteria; Betaproteobacteria; Nitrosomonadales; OC Methylophilaceae. OX NCBI_TaxID=1101195 {ECO:0000313|EMBL:EUJ10182.1, ECO:0000313|Proteomes:UP000022668}; RN [1] {ECO:0000313|EMBL:EUJ10182.1, ECO:0000313|Proteomes:UP000022668} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=11 {ECO:0000313|EMBL:EUJ10182.1, RC ECO:0000313|Proteomes:UP000022668}; RG DOE Joint Genome Institute; RA Chistoserdova L., Huntemann M., Han J., Chen A., Kyrpides N., RA Mavromatis K., Markowitz V., Palaniappan K., Ivanova N., RA Schaumberg A., Pati A., Liolios K., Nordberg H.P., Cantor M.N., RA Hua S.X., Woyke T.; RL Submitted (JUL-2013) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EUJ10182.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JCKJ01000001; EUJ10182.1; -; Genomic_DNA. DR RefSeq; WP_025224055.1; NZ_JCKJ01000001.1. DR EnsemblBacteria; EUJ10182; EUJ10182; Meth11DRAFT_0995. DR PATRIC; fig|1101195.3.peg.965; -. DR Proteomes; UP000022668; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000022668}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000022668}. FT DOMAIN 199 365 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 158 192 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 375 AA; 41715 MW; 96ECBBCD6D328A3A CRC64; MFERPSGGDA VVLVSADFGD ADYAESLQEL RHLVTTAGMQ IRATVEGKRQ SPDAKYFIGS GKAEELKLML ESSESKVAAF NHDLSPSQQR NLERFLQARV VDRTGLILDI FAQRAQTHEG KLQVELAQLE HLSTRLVRGW THLERQKGGI GVRGGPGETQ LELDRRMLRV RVKQLREKLE KLKQQRGMQR RARKRSNLMT VSIVGYTNAG KSTLFNRLTR SGVYAADQLF ATLDTTSRKM HLADANPVVL SDTVGFIKHL PTTLIEAFGA TLEEAAQADL LLHVVDVAST NRDAQIEQVN FVLNEIGASQ VHQILVLNQI DRLGMPAGIE RDEYGKISKV RISAIDGTGL DDLRLALTEY QQLLKQLSTE ESAYA // ID Y3725_ARATH Reviewed; 620 AA. AC Q0WTB4; Q9M2Y5; DT 16-DEC-2008, integrated into UniProtKB/Swiss-Prot. DT 16-DEC-2008, sequence version 2. DT 07-JUN-2017, entry version 71. DE RecName: Full=GTP-binding protein At3g49725, chloroplastic; DE Flags: Precursor; GN OrderedLocusNames=At3g49725; ORFNames=T16K5.80; OS Arabidopsis thaliana (Mouse-ear cress). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae; OC Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae; OC Arabidopsis. OX NCBI_TaxID=3702; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Columbia; RX PubMed=11130713; DOI=10.1038/35048706; RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., RA Fartmann B., Valle G., Bloecker H., Perez-Alonso M., Obermaier B., RA Delseny M., Boutry M., Grivell L.A., Mache R., Puigdomenech P., RA De Simone V., Choisne N., Artiguenave F., Robert C., Brottier P., RA Wincker P., Cattolico L., Weissenbach J., Saurin W., Quetier F., RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Benes V., RA Wurmbach E., Drzonek H., Erfle H., Jordan N., Bangert S., RA Wiedelmann R., Kranz H., Voss H., Holland R., Brandt P., Nyakatura G., RA Vezzi A., D'Angelo M., Pallavicini A., Toppo S., Simionati B., RA Conrad A., Hornischer K., Kauer G., Loehnert T.-H., Nordsiek G., RA Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J., Climent J., RA Navarro P., Collado C., Perez-Perez A., Ottenwaelder B., Duchemin D., RA Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D., RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E., RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., RA Mannhaupt G., Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., RA Mayer K.F.X., Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., RA Rooney T., Rizzo M., Walts A., Utterback T., Fujii C.Y., Shea T.P., RA Creasy T.H., Haas B., Maiti R., Wu D., Peterson J., Van Aken S., RA Pai G., Militscher J., Sellers P., Gill J.E., Feldblyum T.V., RA Preuss D., Lin X., Nierman W.C., Salzberg S.L., White O., Venter J.C., RA Fraser C.M., Kaneko T., Nakamura Y., Sato S., Kato T., Asamizu E., RA Sasamoto S., Kimura T., Idesawa K., Kawashima K., Kishida Y., RA Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Muraki A., RA Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T., RA Watanabe A., Yamada M., Yasuda M., Tabata S.; RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis RT thaliana."; RL Nature 408:820-822(2000). RN [2] RP GENOME REANNOTATION. RC STRAIN=cv. Columbia; RG The Arabidopsis Information Portal (Araport); RL Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=cv. Columbia; RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A., RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y., RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K., RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., RA Hayashizaki Y., Shinozaki K.; RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs."; RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000255|PROSITE-ProRule:PRU01042}; CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000305}. CC -!- DOMAIN: In contrast to other GTP-binding proteins, this family is CC characterized by a circular permutation of the GTPase motifs CC described by a G4-G1-G3 pattern. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000255|PROSITE- CC ProRule:PRU01042}. CC -!- SEQUENCE CAUTION: CC Sequence=CAB66911.1; Type=Erroneous gene model prediction; Note=The predicted gene has been split into 2 genes: At3g49725 and At3g49730.; Evidence={ECO:0000305}; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AL132965; CAB66911.1; ALT_SEQ; Genomic_DNA. DR EMBL; CP002686; AEE78582.1; -; Genomic_DNA. DR EMBL; AK227647; BAE99634.1; -; mRNA. DR PIR; T46039; T46039. DR RefSeq; NP_001154669.1; NM_001161197.2. DR UniGene; At.74537; -. DR ProteinModelPortal; Q0WTB4; -. DR STRING; 3702.AT3G49725.1; -. DR PaxDb; Q0WTB4; -. DR PRIDE; Q0WTB4; -. DR EnsemblPlants; AT3G49725.1; AT3G49725.1; AT3G49725. DR GeneID; 7922380; -. DR Gramene; AT3G49725.1; AT3G49725.1; AT3G49725. DR KEGG; ath:AT3G49725; -. DR Araport; AT3G49725; -. DR TAIR; locus:5019474783; AT3G49725. DR eggNOG; KOG0410; Eukaryota. DR eggNOG; KOG4197; Eukaryota. DR eggNOG; COG2262; LUCA. DR HOGENOM; HOG000083465; -. DR OMA; NGPEAIS; -. DR OrthoDB; EOG09360975; -. DR PhylomeDB; Q0WTB4; -. DR PRO; PR:Q0WTB4; -. DR Proteomes; UP000006548; Chromosome 3. DR Genevisible; Q0WTB4; AT. DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0043022; F:ribosome binding; IBA:GO_Central. DR CDD; cd01878; HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 2. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 2: Evidence at transcript level; KW Chloroplast; Complete proteome; GTP-binding; Magnesium; Metal-binding; KW Nucleotide-binding; Plastid; Reference proteome; Transit peptide. FT TRANSIT 1 65 Chloroplast. {ECO:0000255}. FT CHAIN 66 620 GTP-binding protein At3g49725, FT chloroplastic. FT /FTId=PRO_0000355994. FT DOMAIN 346 585 Hflx-type G. {ECO:0000255|PROSITE- FT ProRule:PRU01042}. FT NP_BIND 352 359 GTP. {ECO:0000255|PROSITE- FT ProRule:PRU01042}. FT NP_BIND 377 381 GTP. {ECO:0000255|PROSITE- FT ProRule:PRU01042}. FT NP_BIND 399 402 GTP. {ECO:0000255|PROSITE- FT ProRule:PRU01042}. FT NP_BIND 468 471 GTP. {ECO:0000255|PROSITE- FT ProRule:PRU01042}. FT NP_BIND 563 565 GTP. {ECO:0000255|PROSITE- FT ProRule:PRU01042}. FT METAL 359 359 Magnesium. {ECO:0000255|PROSITE- FT ProRule:PRU01042}. FT METAL 379 379 Magnesium. {ECO:0000255|PROSITE- FT ProRule:PRU01042}. FT CONFLICT 368 368 T -> A (in Ref. 3; BAE99634). FT {ECO:0000305}. FT CONFLICT 540 540 E -> G (in Ref. 3; BAE99634). FT {ECO:0000305}. SQ SEQUENCE 620 AA; 69579 MW; 94F0F6ECD532C929 CRC64; MSVTTSFGIW LNHINLDNQA SFLYNNPHFC NRRFNRISML RTVSLARNRL RSETPSSFLA RDRLRSKTPS SSPFSSKRHT PKTSEIEEES TPKDSVLLNP KDPSSAPKLF LVQPRLAPPK YLQAKLNEAL CLANSLEEQR YGYFESDFFD KELPSHVVVQ NPVRRSSKPR VDTYFGSGTV DNIKCHLNAE DSKEEVDAVF VNAILTAIQQ RNLERIWAKP VLDRVGLIIE IFNAHAHTKE AKLQAELAAL MYNKSRLVRV RGTDGRHTFG QFGEAEVVSA RGRAGSKGTG GGFVGGAGET ELQLQRRRIS DRRIRLLSQI KEAQRTRLLQ RAGRKKRVGL EGESSGTIAV VGYTNAGKST LISALTKTAL YCNERLFATL DPTLKSAHLP SGNFVLLSDT VGFISDLPIQ LVKAFQSTLE EVVEADLLLH VVDSTAPNIE EHRSTVLHVL NQIGVPEEKL QNMIEVWNKI DYEEDEVEEE KYLDDGEGVG EEDEDEADLK AEETVDASEA TVDEDQIQNG DGDDADGWLL SEDENADDPE FWKVPEVAKV DAANKKGPDV RVSALTGVGL KELLYLIDDK MKEKKLKSPT IVERSELHKR KWRPPRNDDE EERLIPLDQR // ID Z4WSI0_9PORP Unreviewed; 410 AA. AC Z4WSI0; DT 11-JUN-2014, integrated into UniProtKB/TrEMBL. DT 11-JUN-2014, sequence version 1. DT 07-JUN-2017, entry version 24. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900, GN ECO:0000313|EMBL:EWC91782.1}; GN ORFNames=HMPREF0636_1510 {ECO:0000313|EMBL:EWC91782.1}; OS Porphyromonas catoniae ATCC 51270. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; OC Porphyromonadaceae; Porphyromonas. OX NCBI_TaxID=887901 {ECO:0000313|EMBL:EWC91782.1, ECO:0000313|Proteomes:UP000023482}; RN [1] {ECO:0000313|EMBL:EWC91782.1, ECO:0000313|Proteomes:UP000023482} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51270 {ECO:0000313|EMBL:EWC91782.1, RC ECO:0000313|Proteomes:UP000023482}; RA Durkin A.S., McCorrison J., Torralba M., Gillis M., Haft D.H., RA Methe B., Sutton G., Nelson K.E.; RL Submitted (JAN-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EWC91782.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JDFF01000022; EWC91782.1; -; Genomic_DNA. DR RefSeq; WP_044169157.1; NZ_JDFF01000022.1. DR EnsemblBacteria; EWC91782; EWC91782; HMPREF0636_1510. DR PATRIC; fig|887901.3.peg.1266; -. DR Proteomes; UP000023482; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000023482}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000023482}. FT DOMAIN 202 388 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. FT COILED 163 197 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 410 AA; 47375 MW; D97BEF2BFE14B8C5 CRC64; MREFIITETK SDEAVLVGLI TRNQTEDQAK EYLDELDFLS RTAGVEPVVR FLQRLEQPHP VTFVGKGKLE EIRLYVEERE IGLVIFDDEL TPKQLRNIEA VLKVRILDRT SLILDIFAAR ATTAYAKTQV ELAQYRYMLP RLTRLWTHLE RQRGGVGMRG PGETQLETDK RLIQDRIAHL KEELKGIDRQ MAMQRKNRGK LVRVALVGYT NVGKSTLMNV LSKSDVFAEN KLFATLDTTV RKVIVHNLPF LLSDTVGFIR KLPTELIESF KSTLDEVREA DLLVHVVDIS HPNFEEHIEV VSSTLREITA GDEKSVLLVF NKIDAFTYDE KPLDDLSERT RRNLSREDLE RTWMARLGES GCTFISARTG EGIDELKTLL YDRVKELHIQ RFPYNDFLFQ DYTLETNDDE // ID Z5XKN0_9GAMM Unreviewed; 429 AA. AC Z5XKN0; DT 11-JUN-2014, integrated into UniProtKB/TrEMBL. DT 11-JUN-2014, sequence version 1. DT 30-AUG-2017, entry version 23. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=AT00_17705 {ECO:0000313|EMBL:EWH04684.1}; OS Pseudoalteromonas lipolytica SCSIO 04301. OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales; OC Pseudoalteromonadaceae; Pseudoalteromonas. OX NCBI_TaxID=1452721 {ECO:0000313|EMBL:EWH04684.1, ECO:0000313|Proteomes:UP000021443}; RN [1] {ECO:0000313|EMBL:EWH04684.1, ECO:0000313|Proteomes:UP000021443} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SCSIO 04301 {ECO:0000313|EMBL:EWH04684.1, RC ECO:0000313|Proteomes:UP000021443}; RA Wang X., Tian X.; RT "Pseudoalteromonas lipolytica SCSIO 04301 Genome sequencing."; RL Submitted (FEB-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EWH04684.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JDVB01000010; EWH04684.1; -; Genomic_DNA. DR RefSeq; WP_036973351.1; NZ_KK070036.1. DR EnsemblBacteria; EWH04684; EWH04684; AT00_17705. DR PATRIC; fig|1452721.3.peg.3411; -. DR Proteomes; UP000021443; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000021443}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000021443}. FT DOMAIN 198 365 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 429 AA; 48373 MW; 5E635F3AC8EA5EC9 CRC64; MFDRYEAGEQ AVLVHIDLPK EGDREDLHEL ELLVSSAGVS SLAIVQGSRQ APHPKLFVGT GKAEEIAETV KIHNADVIIF NHQLSPSQER NLERVCQCRV LDRTSLILDI FAQRARTHEG KLQVELAQLR HISTRLIRGW THLERQKGGI GLRGPGETQL ETDRRLLRAR IKNIRARLDK VAVQREQGRR ARTRNEIPTV SLVGYTNAGK STLFNRITNS DVYAADQLFA TLDPTLRKLD IGDIGPVILA DTVGFIRHLP HDLVAAFKAT LTETREADLQ LHVIDVADPR RKENIEQVQS VLKEIEADDV PQLLVYNKID ALDDVAPRID RNDEGQPIRV WLSARTGVGC ELLSEAINEL LAKKMFADEL KLPPQHGRIR AALFNLNAVH EEQFDEQGNW LLSVRLPMAE WNRLKKEMGH DLDSFVAAN // ID Z9JTW5_9MICO Unreviewed; 516 AA. AC Z9JTW5; DT 11-JUN-2014, integrated into UniProtKB/TrEMBL. DT 11-JUN-2014, sequence version 1. DT 07-JUN-2017, entry version 23. DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900}; GN ORFNames=BF93_18890 {ECO:0000313|EMBL:EWS81236.1}; OS Brachybacterium phenoliresistens. OC Bacteria; Actinobacteria; Micrococcales; Dermabacteraceae; OC Brachybacterium. OX NCBI_TaxID=396014 {ECO:0000313|EMBL:EWS81236.1, ECO:0000313|Proteomes:UP000023067}; RN [1] {ECO:0000313|EMBL:EWS81236.1, ECO:0000313|Proteomes:UP000023067} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=W13A50 {ECO:0000313|EMBL:EWS81236.1, RC ECO:0000313|Proteomes:UP000023067}; RA Wang X.; RT "Genome sequence of Brachybacterium phenoliresistens strain W13A50."; RL Submitted (FEB-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000256|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00900}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EWS81236.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; JDYK01000009; EWS81236.1; -; Genomic_DNA. DR RefSeq; WP_038372496.1; NZ_KK069994.1. DR EnsemblBacteria; EWS81236; EWS81236; BF93_18890. DR PATRIC; fig|396014.3.peg.2113; -. DR Proteomes; UP000023067; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR CDD; cd01878; HflX; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000023067}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00900}; KW Reference proteome {ECO:0000313|Proteomes:UP000023067}. FT DOMAIN 295 460 Hflx-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51705}. SQ SEQUENCE 516 AA; 56142 MW; DB250BEFAF318EF3 CRC64; MPIAFHPDPD RTEDVTADAP AEQTGGGSRS TERSRDPLTE RILARGDASV SSVTYSSTSD GDQFDLADRQ ALRRVAGLRT DIEDVTEVEY RQLRLERVVL AGLFTTGNVE DAENSLRELA ALAETAGSEV LDGVMQRRAH PDPATFLGKG KAQELAEVVA ETGADTVIAD GELAPSQRRA LEDIVKVKVV DRTALILDIF AQHAKSREGK AQVELAQLEY LLPRLRGWGD SMSRQAGGRV AAGGAGMGSR GPGETKIELD RRRIRTRMSK LRREIKEMAP GREAKRADRK RREVPAVAIA GYTNAGKSSL LNRLTGAGVL VENALFATLD PTVRRSQTPD GREFTFADTV GFVRHLPTEL VEAFRSTLEE VGDADLLLHV VDASHPDPEG QIRAVRDVLA DIDGFDVPEV IVLNKADIAE PETIARLRSQ VEDCIVVSAR SGEGIEELRQ LIADRLPRPE VEVDLLVPYT RGDLISRAHS SGEVLDEEHR SEGTRLHARV DAALAAELQA QAVHVA //